data_8QS7
# 
_entry.id   8QS7 
# 
_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   8QS7         pdb_00008qs7 10.2210/pdb8qs7/pdb 
WWPDB D_1292132195 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8QS7 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              michelle.arkin@ucsf.edu 
_pdbx_contact_author.name_first         Michelle 
_pdbx_contact_author.name_last          Arkin 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9366-6770 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Konstantinidou, M.' 1  ? 
'Vickery, H.'        2  ? 
'Pennings, M.A.M.'   3  ? 
'Virta, J.'          4  ? 
'Visser, E.J.'       5  ? 
'Oetelaar, M.C.M.'   6  ? 
'Overmans, M.'       7  ? 
'Neitz, J.'          8  ? 
'Ottmann, C.'        9  ? 
'Brunsveld, L.'      10 ? 
'Arkin, M.R.'        11 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Small molecule stabilization of the 14-3-3sigma/CRAF complex inhibits the MAPK pathway' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Konstantinidou, M.' 1  ? 
primary 'Vickery, H.'        2  ? 
primary 'Pennings, M.A.M.'   3  ? 
primary 'Virta, J.'          4  ? 
primary 'Visser, E.J.'       5  ? 
primary 'Oetelaar, M.C.M.'   6  ? 
primary 'Overmans, M.'       7  ? 
primary 'Neitz, J.'          8  ? 
primary 'Ottmann, C.'        9  ? 
primary 'Brunsveld, L.'      10 ? 
primary 'Arkin, M.R.'        11 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '14-3-3 protein sigma'                                                                                   
26542.914 1   ? ? ? ? 
2 polymer     syn 'C-RAF peptide pS259'                                                                                    
1208.175  1   ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                                                           35.453 
1   ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                                                                          24.305 
3   ? ? ? ? 
5 non-polymer syn '1-[8-(4-bromanyl-3-fluoranyl-phenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone' 441.700 
1   ? ? ? ? 
6 water       nat water                                                                                                    18.015 
193 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Epithelial cell marker protein 1,Stratifin' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
A ? 
2 'polypeptide(L)' no yes 'QRST(SEP)TPNVH' QRSTSTPNVH P ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CHLORIDE ION'                                                                                           CL  
4 'MAGNESIUM ION'                                                                                          MG  
5 '1-[8-(4-bromanyl-3-fluoranyl-phenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone' WQX 
6 water                                                                                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   GLY n 
1 5   SER n 
1 6   MET n 
1 7   GLU n 
1 8   ARG n 
1 9   ALA n 
1 10  SER n 
1 11  LEU n 
1 12  ILE n 
1 13  GLN n 
1 14  LYS n 
1 15  ALA n 
1 16  LYS n 
1 17  LEU n 
1 18  ALA n 
1 19  GLU n 
1 20  GLN n 
1 21  ALA n 
1 22  GLU n 
1 23  ARG n 
1 24  TYR n 
1 25  GLU n 
1 26  ASP n 
1 27  MET n 
1 28  ALA n 
1 29  ALA n 
1 30  PHE n 
1 31  MET n 
1 32  LYS n 
1 33  GLY n 
1 34  ALA n 
1 35  VAL n 
1 36  GLU n 
1 37  LYS n 
1 38  GLY n 
1 39  GLU n 
1 40  GLU n 
1 41  LEU n 
1 42  SER n 
1 43  CYS n 
1 44  GLU n 
1 45  GLU n 
1 46  ARG n 
1 47  ASN n 
1 48  LEU n 
1 49  LEU n 
1 50  SER n 
1 51  VAL n 
1 52  ALA n 
1 53  TYR n 
1 54  LYS n 
1 55  ASN n 
1 56  VAL n 
1 57  VAL n 
1 58  GLY n 
1 59  GLY n 
1 60  GLN n 
1 61  ARG n 
1 62  ALA n 
1 63  ALA n 
1 64  TRP n 
1 65  ARG n 
1 66  VAL n 
1 67  LEU n 
1 68  SER n 
1 69  SER n 
1 70  ILE n 
1 71  GLU n 
1 72  GLN n 
1 73  LYS n 
1 74  SER n 
1 75  ASN n 
1 76  GLU n 
1 77  GLU n 
1 78  GLY n 
1 79  SER n 
1 80  GLU n 
1 81  GLU n 
1 82  LYS n 
1 83  GLY n 
1 84  PRO n 
1 85  GLU n 
1 86  VAL n 
1 87  ARG n 
1 88  GLU n 
1 89  TYR n 
1 90  ARG n 
1 91  GLU n 
1 92  LYS n 
1 93  VAL n 
1 94  GLU n 
1 95  THR n 
1 96  GLU n 
1 97  LEU n 
1 98  GLN n 
1 99  GLY n 
1 100 VAL n 
1 101 CYS n 
1 102 ASP n 
1 103 THR n 
1 104 VAL n 
1 105 LEU n 
1 106 GLY n 
1 107 LEU n 
1 108 LEU n 
1 109 ASP n 
1 110 SER n 
1 111 HIS n 
1 112 LEU n 
1 113 ILE n 
1 114 LYS n 
1 115 GLU n 
1 116 ALA n 
1 117 GLY n 
1 118 ASP n 
1 119 ALA n 
1 120 GLU n 
1 121 SER n 
1 122 ARG n 
1 123 VAL n 
1 124 PHE n 
1 125 TYR n 
1 126 LEU n 
1 127 LYS n 
1 128 MET n 
1 129 LYS n 
1 130 GLY n 
1 131 ASP n 
1 132 TYR n 
1 133 TYR n 
1 134 ARG n 
1 135 TYR n 
1 136 LEU n 
1 137 ALA n 
1 138 GLU n 
1 139 VAL n 
1 140 ALA n 
1 141 THR n 
1 142 GLY n 
1 143 ASP n 
1 144 ASP n 
1 145 LYS n 
1 146 LYS n 
1 147 ARG n 
1 148 ILE n 
1 149 ILE n 
1 150 ASP n 
1 151 SER n 
1 152 ALA n 
1 153 ARG n 
1 154 SER n 
1 155 ALA n 
1 156 TYR n 
1 157 GLN n 
1 158 GLU n 
1 159 ALA n 
1 160 MET n 
1 161 ASP n 
1 162 ILE n 
1 163 SER n 
1 164 LYS n 
1 165 LYS n 
1 166 GLU n 
1 167 MET n 
1 168 PRO n 
1 169 PRO n 
1 170 THR n 
1 171 ASN n 
1 172 PRO n 
1 173 ILE n 
1 174 ARG n 
1 175 LEU n 
1 176 GLY n 
1 177 LEU n 
1 178 ALA n 
1 179 LEU n 
1 180 ASN n 
1 181 PHE n 
1 182 SER n 
1 183 VAL n 
1 184 PHE n 
1 185 HIS n 
1 186 TYR n 
1 187 GLU n 
1 188 ILE n 
1 189 ALA n 
1 190 ASN n 
1 191 SER n 
1 192 PRO n 
1 193 GLU n 
1 194 GLU n 
1 195 ALA n 
1 196 ILE n 
1 197 SER n 
1 198 LEU n 
1 199 ALA n 
1 200 LYS n 
1 201 THR n 
1 202 THR n 
1 203 PHE n 
1 204 ASP n 
1 205 GLU n 
1 206 ALA n 
1 207 MET n 
1 208 ALA n 
1 209 ASP n 
1 210 LEU n 
1 211 HIS n 
1 212 THR n 
1 213 LEU n 
1 214 SER n 
1 215 GLU n 
1 216 ASP n 
1 217 SER n 
1 218 TYR n 
1 219 LYS n 
1 220 ASP n 
1 221 SER n 
1 222 THR n 
1 223 LEU n 
1 224 ILE n 
1 225 MET n 
1 226 GLN n 
1 227 LEU n 
1 228 LEU n 
1 229 ARG n 
1 230 ASP n 
1 231 ASN n 
1 232 LEU n 
1 233 THR n 
1 234 LEU n 
1 235 TRP n 
1 236 THR n 
2 1   GLN n 
2 2   ARG n 
2 3   SER n 
2 4   THR n 
2 5   SEP n 
2 6   THR n 
2 7   PRO n 
2 8   ASN n 
2 9   VAL n 
2 10  HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   236 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SFN, HME1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       10 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                                  
?               'C3 H7 N O2'              89.093  
ARG 'L-peptide linking' y ARGININE                                                                                                 
?               'C6 H15 N4 O2 1'          175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                               
?               'C4 H8 N2 O3'             132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                                          
?               'C4 H7 N O4'              133.103 
CL  non-polymer         . 'CHLORIDE ION'                                                                                           
?               'Cl -1'                   35.453  
CYS 'L-peptide linking' y CYSTEINE                                                                                                 
?               'C3 H7 N O2 S'            121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                                
?               'C5 H10 N2 O3'            146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                          
?               'C5 H9 N O4'              147.129 
GLY 'peptide linking'   y GLYCINE                                                                                                  
?               'C2 H5 N O2'              75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                                
?               'C6 H10 N3 O2 1'          156.162 
HOH non-polymer         . WATER                                                                                                    
?               'H2 O'                    18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                               
?               'C6 H13 N O2'             131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                                  
?               'C6 H13 N O2'             131.173 
LYS 'L-peptide linking' y LYSINE                                                                                                   
?               'C6 H15 N2 O2 1'          147.195 
MET 'L-peptide linking' y METHIONINE                                                                                               
?               'C5 H11 N O2 S'           149.211 
MG  non-polymer         . 'MAGNESIUM ION'                                                                                          
?               'Mg 2'                    24.305  
PHE 'L-peptide linking' y PHENYLALANINE                                                                                            
?               'C9 H11 N O2'             165.189 
PRO 'L-peptide linking' y PROLINE                                                                                                  
?               'C5 H9 N O2'              115.130 
SEP 'L-peptide linking' n PHOSPHOSERINE                                                                                            
PHOSPHONOSERINE 'C3 H8 N O6 P'            185.072 
SER 'L-peptide linking' y SERINE                                                                                                   
?               'C3 H7 N O3'              105.093 
THR 'L-peptide linking' y THREONINE                                                                                                
?               'C4 H9 N O3'              119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                               
?               'C11 H12 N2 O2'           204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                                 
?               'C9 H11 N O3'             181.189 
VAL 'L-peptide linking' y VALINE                                                                                                   
?               'C5 H11 N O2'             117.146 
WQX non-polymer         . '1-[8-(4-bromanyl-3-fluoranyl-phenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone' 
?               'C14 H15 Br Cl F N2 O4 S' 441.700 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -4  -4  GLY GLY A . n 
A 1 2   ALA 2   -3  -3  ALA ALA A . n 
A 1 3   MET 3   -2  -2  MET MET A . n 
A 1 4   GLY 4   -1  -1  GLY GLY A . n 
A 1 5   SER 5   0   0   SER SER A . n 
A 1 6   MET 6   1   1   MET MET A . n 
A 1 7   GLU 7   2   2   GLU GLU A . n 
A 1 8   ARG 8   3   3   ARG ARG A . n 
A 1 9   ALA 9   4   4   ALA ALA A . n 
A 1 10  SER 10  5   5   SER SER A . n 
A 1 11  LEU 11  6   6   LEU LEU A . n 
A 1 12  ILE 12  7   7   ILE ILE A . n 
A 1 13  GLN 13  8   8   GLN GLN A . n 
A 1 14  LYS 14  9   9   LYS LYS A . n 
A 1 15  ALA 15  10  10  ALA ALA A . n 
A 1 16  LYS 16  11  11  LYS LYS A . n 
A 1 17  LEU 17  12  12  LEU LEU A . n 
A 1 18  ALA 18  13  13  ALA ALA A . n 
A 1 19  GLU 19  14  14  GLU GLU A . n 
A 1 20  GLN 20  15  15  GLN GLN A . n 
A 1 21  ALA 21  16  16  ALA ALA A . n 
A 1 22  GLU 22  17  17  GLU GLU A . n 
A 1 23  ARG 23  18  18  ARG ARG A . n 
A 1 24  TYR 24  19  19  TYR TYR A . n 
A 1 25  GLU 25  20  20  GLU GLU A . n 
A 1 26  ASP 26  21  21  ASP ASP A . n 
A 1 27  MET 27  22  22  MET MET A . n 
A 1 28  ALA 28  23  23  ALA ALA A . n 
A 1 29  ALA 29  24  24  ALA ALA A . n 
A 1 30  PHE 30  25  25  PHE PHE A . n 
A 1 31  MET 31  26  26  MET MET A . n 
A 1 32  LYS 32  27  27  LYS LYS A . n 
A 1 33  GLY 33  28  28  GLY GLY A . n 
A 1 34  ALA 34  29  29  ALA ALA A . n 
A 1 35  VAL 35  30  30  VAL VAL A . n 
A 1 36  GLU 36  31  31  GLU GLU A . n 
A 1 37  LYS 37  32  32  LYS LYS A . n 
A 1 38  GLY 38  33  33  GLY GLY A . n 
A 1 39  GLU 39  34  34  GLU GLU A . n 
A 1 40  GLU 40  35  35  GLU GLU A . n 
A 1 41  LEU 41  36  36  LEU LEU A . n 
A 1 42  SER 42  37  37  SER SER A . n 
A 1 43  CYS 43  38  38  CYS CYS A . n 
A 1 44  GLU 44  39  39  GLU GLU A . n 
A 1 45  GLU 45  40  40  GLU GLU A . n 
A 1 46  ARG 46  41  41  ARG ARG A . n 
A 1 47  ASN 47  42  42  ASN ASN A . n 
A 1 48  LEU 48  43  43  LEU LEU A . n 
A 1 49  LEU 49  44  44  LEU LEU A . n 
A 1 50  SER 50  45  45  SER SER A . n 
A 1 51  VAL 51  46  46  VAL VAL A . n 
A 1 52  ALA 52  47  47  ALA ALA A . n 
A 1 53  TYR 53  48  48  TYR TYR A . n 
A 1 54  LYS 54  49  49  LYS LYS A . n 
A 1 55  ASN 55  50  50  ASN ASN A . n 
A 1 56  VAL 56  51  51  VAL VAL A . n 
A 1 57  VAL 57  52  52  VAL VAL A . n 
A 1 58  GLY 58  53  53  GLY GLY A . n 
A 1 59  GLY 59  54  54  GLY GLY A . n 
A 1 60  GLN 60  55  55  GLN GLN A . n 
A 1 61  ARG 61  56  56  ARG ARG A . n 
A 1 62  ALA 62  57  57  ALA ALA A . n 
A 1 63  ALA 63  58  58  ALA ALA A . n 
A 1 64  TRP 64  59  59  TRP TRP A . n 
A 1 65  ARG 65  60  60  ARG ARG A . n 
A 1 66  VAL 66  61  61  VAL VAL A . n 
A 1 67  LEU 67  62  62  LEU LEU A . n 
A 1 68  SER 68  63  63  SER SER A . n 
A 1 69  SER 69  64  64  SER SER A . n 
A 1 70  ILE 70  65  65  ILE ILE A . n 
A 1 71  GLU 71  66  66  GLU GLU A . n 
A 1 72  GLN 72  67  67  GLN GLN A . n 
A 1 73  LYS 73  68  68  LYS LYS A . n 
A 1 74  SER 74  69  69  SER SER A . n 
A 1 75  ASN 75  70  70  ASN ASN A . n 
A 1 76  GLU 76  71  71  GLU GLU A . n 
A 1 77  GLU 77  72  ?   ?   ?   A . n 
A 1 78  GLY 78  73  ?   ?   ?   A . n 
A 1 79  SER 79  74  ?   ?   ?   A . n 
A 1 80  GLU 80  75  ?   ?   ?   A . n 
A 1 81  GLU 81  76  ?   ?   ?   A . n 
A 1 82  LYS 82  77  ?   ?   ?   A . n 
A 1 83  GLY 83  78  78  GLY GLY A . n 
A 1 84  PRO 84  79  79  PRO PRO A . n 
A 1 85  GLU 85  80  80  GLU GLU A . n 
A 1 86  VAL 86  81  81  VAL VAL A . n 
A 1 87  ARG 87  82  82  ARG ARG A . n 
A 1 88  GLU 88  83  83  GLU GLU A . n 
A 1 89  TYR 89  84  84  TYR TYR A . n 
A 1 90  ARG 90  85  85  ARG ARG A . n 
A 1 91  GLU 91  86  86  GLU GLU A . n 
A 1 92  LYS 92  87  87  LYS LYS A . n 
A 1 93  VAL 93  88  88  VAL VAL A . n 
A 1 94  GLU 94  89  89  GLU GLU A . n 
A 1 95  THR 95  90  90  THR THR A . n 
A 1 96  GLU 96  91  91  GLU GLU A . n 
A 1 97  LEU 97  92  92  LEU LEU A . n 
A 1 98  GLN 98  93  93  GLN GLN A . n 
A 1 99  GLY 99  94  94  GLY GLY A . n 
A 1 100 VAL 100 95  95  VAL VAL A . n 
A 1 101 CYS 101 96  96  CYS CYS A . n 
A 1 102 ASP 102 97  97  ASP ASP A . n 
A 1 103 THR 103 98  98  THR THR A . n 
A 1 104 VAL 104 99  99  VAL VAL A . n 
A 1 105 LEU 105 100 100 LEU LEU A . n 
A 1 106 GLY 106 101 101 GLY GLY A . n 
A 1 107 LEU 107 102 102 LEU LEU A . n 
A 1 108 LEU 108 103 103 LEU LEU A . n 
A 1 109 ASP 109 104 104 ASP ASP A . n 
A 1 110 SER 110 105 105 SER SER A . n 
A 1 111 HIS 111 106 106 HIS HIS A . n 
A 1 112 LEU 112 107 107 LEU LEU A . n 
A 1 113 ILE 113 108 108 ILE ILE A . n 
A 1 114 LYS 114 109 109 LYS LYS A . n 
A 1 115 GLU 115 110 110 GLU GLU A . n 
A 1 116 ALA 116 111 111 ALA ALA A . n 
A 1 117 GLY 117 112 112 GLY GLY A . n 
A 1 118 ASP 118 113 113 ASP ASP A . n 
A 1 119 ALA 119 114 114 ALA ALA A . n 
A 1 120 GLU 120 115 115 GLU GLU A . n 
A 1 121 SER 121 116 116 SER SER A . n 
A 1 122 ARG 122 117 117 ARG ARG A . n 
A 1 123 VAL 123 118 118 VAL VAL A . n 
A 1 124 PHE 124 119 119 PHE PHE A . n 
A 1 125 TYR 125 120 120 TYR TYR A . n 
A 1 126 LEU 126 121 121 LEU LEU A . n 
A 1 127 LYS 127 122 122 LYS LYS A . n 
A 1 128 MET 128 123 123 MET MET A . n 
A 1 129 LYS 129 124 124 LYS LYS A . n 
A 1 130 GLY 130 125 125 GLY GLY A . n 
A 1 131 ASP 131 126 126 ASP ASP A . n 
A 1 132 TYR 132 127 127 TYR TYR A . n 
A 1 133 TYR 133 128 128 TYR TYR A . n 
A 1 134 ARG 134 129 129 ARG ARG A . n 
A 1 135 TYR 135 130 130 TYR TYR A . n 
A 1 136 LEU 136 131 131 LEU LEU A . n 
A 1 137 ALA 137 132 132 ALA ALA A . n 
A 1 138 GLU 138 133 133 GLU GLU A . n 
A 1 139 VAL 139 134 134 VAL VAL A . n 
A 1 140 ALA 140 135 135 ALA ALA A . n 
A 1 141 THR 141 136 136 THR THR A . n 
A 1 142 GLY 142 137 137 GLY GLY A . n 
A 1 143 ASP 143 138 138 ASP ASP A . n 
A 1 144 ASP 144 139 139 ASP ASP A . n 
A 1 145 LYS 145 140 140 LYS LYS A . n 
A 1 146 LYS 146 141 141 LYS LYS A . n 
A 1 147 ARG 147 142 142 ARG ARG A . n 
A 1 148 ILE 148 143 143 ILE ILE A . n 
A 1 149 ILE 149 144 144 ILE ILE A . n 
A 1 150 ASP 150 145 145 ASP ASP A . n 
A 1 151 SER 151 146 146 SER SER A . n 
A 1 152 ALA 152 147 147 ALA ALA A . n 
A 1 153 ARG 153 148 148 ARG ARG A . n 
A 1 154 SER 154 149 149 SER SER A . n 
A 1 155 ALA 155 150 150 ALA ALA A . n 
A 1 156 TYR 156 151 151 TYR TYR A . n 
A 1 157 GLN 157 152 152 GLN GLN A . n 
A 1 158 GLU 158 153 153 GLU GLU A . n 
A 1 159 ALA 159 154 154 ALA ALA A . n 
A 1 160 MET 160 155 155 MET MET A . n 
A 1 161 ASP 161 156 156 ASP ASP A . n 
A 1 162 ILE 162 157 157 ILE ILE A . n 
A 1 163 SER 163 158 158 SER SER A . n 
A 1 164 LYS 164 159 159 LYS LYS A . n 
A 1 165 LYS 165 160 160 LYS LYS A . n 
A 1 166 GLU 166 161 161 GLU GLU A . n 
A 1 167 MET 167 162 162 MET MET A . n 
A 1 168 PRO 168 163 163 PRO PRO A . n 
A 1 169 PRO 169 164 164 PRO PRO A . n 
A 1 170 THR 170 165 165 THR THR A . n 
A 1 171 ASN 171 166 166 ASN ASN A . n 
A 1 172 PRO 172 167 167 PRO PRO A . n 
A 1 173 ILE 173 168 168 ILE ILE A . n 
A 1 174 ARG 174 169 169 ARG ARG A . n 
A 1 175 LEU 175 170 170 LEU LEU A . n 
A 1 176 GLY 176 171 171 GLY GLY A . n 
A 1 177 LEU 177 172 172 LEU LEU A . n 
A 1 178 ALA 178 173 173 ALA ALA A . n 
A 1 179 LEU 179 174 174 LEU LEU A . n 
A 1 180 ASN 180 175 175 ASN ASN A . n 
A 1 181 PHE 181 176 176 PHE PHE A . n 
A 1 182 SER 182 177 177 SER SER A . n 
A 1 183 VAL 183 178 178 VAL VAL A . n 
A 1 184 PHE 184 179 179 PHE PHE A . n 
A 1 185 HIS 185 180 180 HIS HIS A . n 
A 1 186 TYR 186 181 181 TYR TYR A . n 
A 1 187 GLU 187 182 182 GLU GLU A . n 
A 1 188 ILE 188 183 183 ILE ILE A . n 
A 1 189 ALA 189 184 184 ALA ALA A . n 
A 1 190 ASN 190 185 185 ASN ASN A . n 
A 1 191 SER 191 186 186 SER SER A . n 
A 1 192 PRO 192 187 187 PRO PRO A . n 
A 1 193 GLU 193 188 188 GLU GLU A . n 
A 1 194 GLU 194 189 189 GLU GLU A . n 
A 1 195 ALA 195 190 190 ALA ALA A . n 
A 1 196 ILE 196 191 191 ILE ILE A . n 
A 1 197 SER 197 192 192 SER SER A . n 
A 1 198 LEU 198 193 193 LEU LEU A . n 
A 1 199 ALA 199 194 194 ALA ALA A . n 
A 1 200 LYS 200 195 195 LYS LYS A . n 
A 1 201 THR 201 196 196 THR THR A . n 
A 1 202 THR 202 197 197 THR THR A . n 
A 1 203 PHE 203 198 198 PHE PHE A . n 
A 1 204 ASP 204 199 199 ASP ASP A . n 
A 1 205 GLU 205 200 200 GLU GLU A . n 
A 1 206 ALA 206 201 201 ALA ALA A . n 
A 1 207 MET 207 202 202 MET MET A . n 
A 1 208 ALA 208 203 203 ALA ALA A . n 
A 1 209 ASP 209 204 204 ASP ASP A . n 
A 1 210 LEU 210 205 205 LEU LEU A . n 
A 1 211 HIS 211 206 206 HIS HIS A . n 
A 1 212 THR 212 207 207 THR THR A . n 
A 1 213 LEU 213 208 208 LEU LEU A . n 
A 1 214 SER 214 209 209 SER SER A . n 
A 1 215 GLU 215 210 210 GLU GLU A . n 
A 1 216 ASP 216 211 211 ASP ASP A . n 
A 1 217 SER 217 212 212 SER SER A . n 
A 1 218 TYR 218 213 213 TYR TYR A . n 
A 1 219 LYS 219 214 214 LYS LYS A . n 
A 1 220 ASP 220 215 215 ASP ASP A . n 
A 1 221 SER 221 216 216 SER SER A . n 
A 1 222 THR 222 217 217 THR THR A . n 
A 1 223 LEU 223 218 218 LEU LEU A . n 
A 1 224 ILE 224 219 219 ILE ILE A . n 
A 1 225 MET 225 220 220 MET MET A . n 
A 1 226 GLN 226 221 221 GLN GLN A . n 
A 1 227 LEU 227 222 222 LEU LEU A . n 
A 1 228 LEU 228 223 223 LEU LEU A . n 
A 1 229 ARG 229 224 224 ARG ARG A . n 
A 1 230 ASP 230 225 225 ASP ASP A . n 
A 1 231 ASN 231 226 226 ASN ASN A . n 
A 1 232 LEU 232 227 227 LEU LEU A . n 
A 1 233 THR 233 228 228 THR THR A . n 
A 1 234 LEU 234 229 229 LEU LEU A . n 
A 1 235 TRP 235 230 230 TRP TRP A . n 
A 1 236 THR 236 231 231 THR THR A . n 
B 2 1   GLN 1   255 255 GLN GLN P . n 
B 2 2   ARG 2   256 256 ARG ARG P . n 
B 2 3   SER 3   257 257 SER SER P . n 
B 2 4   THR 4   258 258 THR THR P . n 
B 2 5   SEP 5   259 259 SEP SEP P . n 
B 2 6   THR 6   260 260 THR THR P . n 
B 2 7   PRO 7   261 261 PRO PRO P . n 
B 2 8   ASN 8   262 262 ASN ASN P . n 
B 2 9   VAL 9   263 263 VAL VAL P . n 
B 2 10  HIS 10  264 264 HIS HIS P . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WQX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WQX 
_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 WQX 1   305 236 WQX 352 A . 
H 6 HOH 1   401 154 HOH HOH A . 
H 6 HOH 2   402 181 HOH HOH A . 
H 6 HOH 3   403 165 HOH HOH A . 
H 6 HOH 4   404 98  HOH HOH A . 
H 6 HOH 5   405 190 HOH HOH A . 
H 6 HOH 6   406 86  HOH HOH A . 
H 6 HOH 7   407 183 HOH HOH A . 
H 6 HOH 8   408 163 HOH HOH A . 
H 6 HOH 9   409 199 HOH HOH A . 
H 6 HOH 10  410 2   HOH HOH A . 
H 6 HOH 11  411 187 HOH HOH A . 
H 6 HOH 12  412 196 HOH HOH A . 
H 6 HOH 13  413 58  HOH HOH A . 
H 6 HOH 14  414 186 HOH HOH A . 
H 6 HOH 15  415 155 HOH HOH A . 
H 6 HOH 16  416 14  HOH HOH A . 
H 6 HOH 17  417 102 HOH HOH A . 
H 6 HOH 18  418 83  HOH HOH A . 
H 6 HOH 19  419 28  HOH HOH A . 
H 6 HOH 20  420 127 HOH HOH A . 
H 6 HOH 21  421 107 HOH HOH A . 
H 6 HOH 22  422 118 HOH HOH A . 
H 6 HOH 23  423 53  HOH HOH A . 
H 6 HOH 24  424 65  HOH HOH A . 
H 6 HOH 25  425 50  HOH HOH A . 
H 6 HOH 26  426 189 HOH HOH A . 
H 6 HOH 27  427 80  HOH HOH A . 
H 6 HOH 28  428 133 HOH HOH A . 
H 6 HOH 29  429 175 HOH HOH A . 
H 6 HOH 30  430 138 HOH HOH A . 
H 6 HOH 31  431 96  HOH HOH A . 
H 6 HOH 32  432 78  HOH HOH A . 
H 6 HOH 33  433 39  HOH HOH A . 
H 6 HOH 34  434 51  HOH HOH A . 
H 6 HOH 35  435 142 HOH HOH A . 
H 6 HOH 36  436 38  HOH HOH A . 
H 6 HOH 37  437 160 HOH HOH A . 
H 6 HOH 38  438 129 HOH HOH A . 
H 6 HOH 39  439 147 HOH HOH A . 
H 6 HOH 40  440 116 HOH HOH A . 
H 6 HOH 41  441 117 HOH HOH A . 
H 6 HOH 42  442 25  HOH HOH A . 
H 6 HOH 43  443 46  HOH HOH A . 
H 6 HOH 44  444 9   HOH HOH A . 
H 6 HOH 45  445 132 HOH HOH A . 
H 6 HOH 46  446 33  HOH HOH A . 
H 6 HOH 47  447 113 HOH HOH A . 
H 6 HOH 48  448 112 HOH HOH A . 
H 6 HOH 49  449 109 HOH HOH A . 
H 6 HOH 50  450 32  HOH HOH A . 
H 6 HOH 51  451 123 HOH HOH A . 
H 6 HOH 52  452 79  HOH HOH A . 
H 6 HOH 53  453 171 HOH HOH A . 
H 6 HOH 54  454 16  HOH HOH A . 
H 6 HOH 55  455 29  HOH HOH A . 
H 6 HOH 56  456 7   HOH HOH A . 
H 6 HOH 57  457 73  HOH HOH A . 
H 6 HOH 58  458 180 HOH HOH A . 
H 6 HOH 59  459 49  HOH HOH A . 
H 6 HOH 60  460 85  HOH HOH A . 
H 6 HOH 61  461 191 HOH HOH A . 
H 6 HOH 62  462 21  HOH HOH A . 
H 6 HOH 63  463 71  HOH HOH A . 
H 6 HOH 64  464 11  HOH HOH A . 
H 6 HOH 65  465 56  HOH HOH A . 
H 6 HOH 66  466 45  HOH HOH A . 
H 6 HOH 67  467 82  HOH HOH A . 
H 6 HOH 68  468 5   HOH HOH A . 
H 6 HOH 69  469 144 HOH HOH A . 
H 6 HOH 70  470 34  HOH HOH A . 
H 6 HOH 71  471 4   HOH HOH A . 
H 6 HOH 72  472 12  HOH HOH A . 
H 6 HOH 73  473 176 HOH HOH A . 
H 6 HOH 74  474 20  HOH HOH A . 
H 6 HOH 75  475 27  HOH HOH A . 
H 6 HOH 76  476 99  HOH HOH A . 
H 6 HOH 77  477 68  HOH HOH A . 
H 6 HOH 78  478 184 HOH HOH A . 
H 6 HOH 79  479 8   HOH HOH A . 
H 6 HOH 80  480 18  HOH HOH A . 
H 6 HOH 81  481 59  HOH HOH A . 
H 6 HOH 82  482 19  HOH HOH A . 
H 6 HOH 83  483 37  HOH HOH A . 
H 6 HOH 84  484 141 HOH HOH A . 
H 6 HOH 85  485 75  HOH HOH A . 
H 6 HOH 86  486 26  HOH HOH A . 
H 6 HOH 87  487 81  HOH HOH A . 
H 6 HOH 88  488 15  HOH HOH A . 
H 6 HOH 89  489 148 HOH HOH A . 
H 6 HOH 90  490 22  HOH HOH A . 
H 6 HOH 91  491 74  HOH HOH A . 
H 6 HOH 92  492 30  HOH HOH A . 
H 6 HOH 93  493 105 HOH HOH A . 
H 6 HOH 94  494 57  HOH HOH A . 
H 6 HOH 95  495 70  HOH HOH A . 
H 6 HOH 96  496 101 HOH HOH A . 
H 6 HOH 97  497 10  HOH HOH A . 
H 6 HOH 98  498 90  HOH HOH A . 
H 6 HOH 99  499 111 HOH HOH A . 
H 6 HOH 100 500 161 HOH HOH A . 
H 6 HOH 101 501 63  HOH HOH A . 
H 6 HOH 102 502 92  HOH HOH A . 
H 6 HOH 103 503 201 HOH HOH A . 
H 6 HOH 104 504 130 HOH HOH A . 
H 6 HOH 105 505 188 HOH HOH A . 
H 6 HOH 106 506 77  HOH HOH A . 
H 6 HOH 107 507 55  HOH HOH A . 
H 6 HOH 108 508 100 HOH HOH A . 
H 6 HOH 109 509 54  HOH HOH A . 
H 6 HOH 110 510 76  HOH HOH A . 
H 6 HOH 111 511 40  HOH HOH A . 
H 6 HOH 112 512 13  HOH HOH A . 
H 6 HOH 113 513 93  HOH HOH A . 
H 6 HOH 114 514 23  HOH HOH A . 
H 6 HOH 115 515 178 HOH HOH A . 
H 6 HOH 116 516 139 HOH HOH A . 
H 6 HOH 117 517 104 HOH HOH A . 
H 6 HOH 118 518 36  HOH HOH A . 
H 6 HOH 119 519 106 HOH HOH A . 
H 6 HOH 120 520 149 HOH HOH A . 
H 6 HOH 121 521 3   HOH HOH A . 
H 6 HOH 122 522 125 HOH HOH A . 
H 6 HOH 123 523 192 HOH HOH A . 
H 6 HOH 124 524 128 HOH HOH A . 
H 6 HOH 125 525 17  HOH HOH A . 
H 6 HOH 126 526 162 HOH HOH A . 
H 6 HOH 127 527 167 HOH HOH A . 
H 6 HOH 128 528 172 HOH HOH A . 
H 6 HOH 129 529 119 HOH HOH A . 
H 6 HOH 130 530 60  HOH HOH A . 
H 6 HOH 131 531 1   HOH HOH A . 
H 6 HOH 132 532 153 HOH HOH A . 
H 6 HOH 133 533 48  HOH HOH A . 
H 6 HOH 134 534 103 HOH HOH A . 
H 6 HOH 135 535 182 HOH HOH A . 
H 6 HOH 136 536 124 HOH HOH A . 
H 6 HOH 137 537 110 HOH HOH A . 
H 6 HOH 138 538 198 HOH HOH A . 
H 6 HOH 139 539 157 HOH HOH A . 
H 6 HOH 140 540 42  HOH HOH A . 
H 6 HOH 141 541 134 HOH HOH A . 
H 6 HOH 142 542 137 HOH HOH A . 
H 6 HOH 143 543 143 HOH HOH A . 
H 6 HOH 144 544 169 HOH HOH A . 
H 6 HOH 145 545 173 HOH HOH A . 
H 6 HOH 146 546 179 HOH HOH A . 
H 6 HOH 147 547 94  HOH HOH A . 
H 6 HOH 148 548 166 HOH HOH A . 
H 6 HOH 149 549 62  HOH HOH A . 
H 6 HOH 150 550 91  HOH HOH A . 
H 6 HOH 151 551 122 HOH HOH A . 
H 6 HOH 152 552 200 HOH HOH A . 
H 6 HOH 153 553 131 HOH HOH A . 
H 6 HOH 154 554 108 HOH HOH A . 
H 6 HOH 155 555 140 HOH HOH A . 
H 6 HOH 156 556 150 HOH HOH A . 
H 6 HOH 157 557 84  HOH HOH A . 
H 6 HOH 158 558 115 HOH HOH A . 
H 6 HOH 159 559 69  HOH HOH A . 
H 6 HOH 160 560 177 HOH HOH A . 
H 6 HOH 161 561 35  HOH HOH A . 
H 6 HOH 162 562 47  HOH HOH A . 
H 6 HOH 163 563 89  HOH HOH A . 
H 6 HOH 164 564 66  HOH HOH A . 
H 6 HOH 165 565 151 HOH HOH A . 
H 6 HOH 166 566 61  HOH HOH A . 
H 6 HOH 167 567 88  HOH HOH A . 
H 6 HOH 168 568 136 HOH HOH A . 
H 6 HOH 169 569 52  HOH HOH A . 
H 6 HOH 170 570 174 HOH HOH A . 
H 6 HOH 171 571 202 HOH HOH A . 
H 6 HOH 172 572 126 HOH HOH A . 
H 6 HOH 173 573 87  HOH HOH A . 
H 6 HOH 174 574 194 HOH HOH A . 
H 6 HOH 175 575 72  HOH HOH A . 
H 6 HOH 176 576 135 HOH HOH A . 
H 6 HOH 177 577 145 HOH HOH A . 
H 6 HOH 178 578 114 HOH HOH A . 
H 6 HOH 179 579 185 HOH HOH A . 
I 6 HOH 1   301 31  HOH HOH P . 
I 6 HOH 2   302 67  HOH HOH P . 
I 6 HOH 3   303 120 HOH HOH P . 
I 6 HOH 4   304 6   HOH HOH P . 
I 6 HOH 5   305 43  HOH HOH P . 
I 6 HOH 6   306 44  HOH HOH P . 
I 6 HOH 7   307 41  HOH HOH P . 
I 6 HOH 8   308 64  HOH HOH P . 
I 6 HOH 9   309 24  HOH HOH P . 
I 6 HOH 10  310 197 HOH HOH P . 
I 6 HOH 11  311 146 HOH HOH P . 
I 6 HOH 12  312 164 HOH HOH P . 
I 6 HOH 13  313 158 HOH HOH P . 
I 6 HOH 14  314 156 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       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 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                     8QS7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.377 
_cell.length_a_esd                 ? 
_cell.length_b                     149.389 
_cell.length_b_esd                 ? 
_cell.length_c                     76.700 
_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                         8QS7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                21 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8QS7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.22 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.79 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-30 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.885603 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.885603 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QS7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               76.7 
_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                                     33622 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.80 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1964 
_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                                  0.890 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8QS7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             34.12 
_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                     33602 
_refine.ls_number_reflns_R_free                  1676 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.90 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2041 
_refine.ls_R_factor_R_free                       0.2358 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2024 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.38 
_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       ML 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.57 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.22 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        34.12 
_refine_hist.number_atoms_solvent             193 
_refine_hist.number_atoms_total               2114 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1894 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         27 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.010 ? 534 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.148 ? 600 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.430 ? 279 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.134 ? 289 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 339 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.80 1.85  . . 140 2602 100.00 . . . . 0.3071 . . . . . . . . . . . 0.3368 
'X-RAY DIFFRACTION' 1.85 1.91  . . 127 2614 100.00 . . . . 0.2851 . . . . . . . . . . . 0.2831 
'X-RAY DIFFRACTION' 1.91 1.98  . . 129 2655 100.00 . . . . 0.2646 . . . . . . . . . . . 0.2899 
'X-RAY DIFFRACTION' 1.98 2.06  . . 141 2640 100.00 . . . . 0.2423 . . . . . . . . . . . 0.2863 
'X-RAY DIFFRACTION' 2.06 2.15  . . 143 2613 100.00 . . . . 0.2273 . . . . . . . . . . . 0.2561 
'X-RAY DIFFRACTION' 2.15 2.27  . . 132 2649 100.00 . . . . 0.2193 . . . . . . . . . . . 0.2543 
'X-RAY DIFFRACTION' 2.27 2.41  . . 147 2648 100.00 . . . . 0.2276 . . . . . . . . . . . 0.2343 
'X-RAY DIFFRACTION' 2.41 2.60  . . 118 2681 100.00 . . . . 0.2204 . . . . . . . . . . . 0.2808 
'X-RAY DIFFRACTION' 2.60 2.86  . . 168 2628 100.00 . . . . 0.2220 . . . . . . . . . . . 0.2684 
'X-RAY DIFFRACTION' 2.86 3.27  . . 145 2670 100.00 . . . . 0.2156 . . . . . . . . . . . 0.2327 
'X-RAY DIFFRACTION' 3.27 4.12  . . 141 2715 100.00 . . . . 0.1805 . . . . . . . . . . . 0.2277 
'X-RAY DIFFRACTION' 4.12 34.12 . . 145 2811 100.00 . . . . 0.1757 . . . . . . . . . . . 0.2017 
# 
_struct.entry_id                     8QS7 
_struct.title                        'Ternary structure of 14-3-3s, C-RAF phosphopeptide (pS259) and compound 70 (1084352)' 
_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        8QS7 
_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 6 ? 
I N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP 1433S_HUMAN P31947 ? 1 
;MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPE
VREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKK
EMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
1 
2 PDB 8QS7        8QS7   ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8QS7 A 6 ? 236 ? P31947 1   ? 231 ? 1   231 
2 2 8QS7 P 1 ? 10  ? 8QS7   255 ? 264 ? 255 264 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8QS7 GLY A 1 ? UNP P31947 ? ? 'expression tag' -4 1 
1 8QS7 ALA A 2 ? UNP P31947 ? ? 'expression tag' -3 2 
1 8QS7 MET A 3 ? UNP P31947 ? ? 'expression tag' -2 3 
1 8QS7 GLY A 4 ? UNP P31947 ? ? 'expression tag' -1 4 
1 8QS7 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)' 5850  ? 
1 MORE         -75   ? 
1 'SSA (A^2)'  22570 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 3_656 -x+1,y,-z+1 -1.0000000000 0.0000000000 0.0000000000 62.3770000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 76.7000000000 
# 
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  ? SER A 74  ? SER A 37  SER A 69  1 ? 33 
HELX_P HELX_P4  AA4 PRO A 84  ? HIS A 111 ? PRO A 79  HIS A 106 1 ? 28 
HELX_P HELX_P5  AA5 ASP A 118 ? VAL A 139 ? ASP A 113 VAL A 134 1 ? 22 
HELX_P HELX_P6  AA6 GLY A 142 ? MET A 167 ? GLY A 137 MET A 162 1 ? 26 
HELX_P HELX_P7  AA7 ASN A 171 ? ILE A 188 ? ASN A 166 ILE A 183 1 ? 18 
HELX_P HELX_P8  AA8 SER A 191 ? ASP A 209 ? SER A 186 ASP A 204 1 ? 19 
HELX_P HELX_P9  AA9 LEU A 210 ? LEU A 213 ? LEU A 205 LEU A 208 5 ? 4  
HELX_P HELX_P10 AB1 SER A 217 ? THR A 236 ? SER A 212 THR A 231 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one  ? A CYS 43  SG  ? ? ? 1_555 G WQX . C2 ? ? A CYS 38  A WQX 305 1_555 ? ? ? ? ? ? ? 1.770 ? ? 
covale2 covale both ? B THR 4   C   ? ? ? 1_555 B SEP 5 N  ? ? P THR 258 P SEP 259 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
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   OE2 ? ? ? 1_555 F MG  . MG ? ? A GLU 2   A MG  304 1_555 ? ? ? ? ? ? ? 2.960 ? ? 
metalc2 metalc ?    ? A GLU 94  OE2 ? ? ? 1_555 D MG  . MG ? ? A GLU 89  A MG  302 1_555 ? ? ? ? ? ? ? 2.616 ? ? 
metalc3 metalc ?    ? A ASN 190 O   ? ? ? 1_555 E MG  . MG ? ? A ASN 185 A MG  303 3_556 ? ? ? ? ? ? ? 2.947 ? ? 
metalc4 metalc ?    ? F MG  .   MG  ? ? ? 1_555 H HOH . O  ? ? A MG  304 A HOH 411 6_655 ? ? ? ? ? ? ? 2.614 ? ? 
metalc5 metalc ?    ? F MG  .   MG  ? ? ? 1_555 H HOH . O  ? ? A MG  304 A HOH 554 6_655 ? ? ? ? ? ? ? 2.808 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OE2 ? A GLU 7 ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O ? H HOH . ? A HOH 411 ? 6_655 84.0  ? 
2 OE2 ? A GLU 7 ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O ? H HOH . ? A HOH 554 ? 6_655 121.0 ? 
3 O   ? H HOH . ? A HOH 411 ? 6_655 MG ? F MG . ? A MG 304 ? 1_555 O ? H HOH . ? A HOH 554 ? 6_655 95.0  ? 
# 
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 WQX G . ? CYS A 43 ? WQX A 305 ? 1_555 CYS A 38 ? 1_555 C2 SG CYS 1 WQX None            'Covalent chemical modification' 
# 
_pdbx_entry_details.entry_id                   8QS7 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 106 ? ? -131.46 -36.51 
2 1 THR A 136 ? ? -130.29 -54.02 
3 1 SER A 212 ? ? -145.25 11.45  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 426 ? H HOH . 
2 1 A HOH 448 ? H HOH . 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       579 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.75 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 72 ? A GLU 77 
2 1 Y 1 A GLY 73 ? A GLY 78 
3 1 Y 1 A SER 74 ? A SER 79 
4 1 Y 1 A GLU 75 ? A GLU 80 
5 1 Y 1 A GLU 76 ? A GLU 81 
6 1 Y 1 A LYS 77 ? A LYS 82 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
MG  MG   MG N N 251 
PHE N    N  N N 252 
PHE CA   C  N S 253 
PHE C    C  N N 254 
PHE O    O  N N 255 
PHE CB   C  N N 256 
PHE CG   C  Y N 257 
PHE CD1  C  Y N 258 
PHE CD2  C  Y N 259 
PHE CE1  C  Y N 260 
PHE CE2  C  Y N 261 
PHE CZ   C  Y N 262 
PHE OXT  O  N N 263 
PHE H    H  N N 264 
PHE H2   H  N N 265 
PHE HA   H  N N 266 
PHE HB2  H  N N 267 
PHE HB3  H  N N 268 
PHE HD1  H  N N 269 
PHE HD2  H  N N 270 
PHE HE1  H  N N 271 
PHE HE2  H  N N 272 
PHE HZ   H  N N 273 
PHE HXT  H  N N 274 
PRO N    N  N N 275 
PRO CA   C  N S 276 
PRO C    C  N N 277 
PRO O    O  N N 278 
PRO CB   C  N N 279 
PRO CG   C  N N 280 
PRO CD   C  N N 281 
PRO OXT  O  N N 282 
PRO H    H  N N 283 
PRO HA   H  N N 284 
PRO HB2  H  N N 285 
PRO HB3  H  N N 286 
PRO HG2  H  N N 287 
PRO HG3  H  N N 288 
PRO HD2  H  N N 289 
PRO HD3  H  N N 290 
PRO HXT  H  N N 291 
SEP N    N  N N 292 
SEP CA   C  N S 293 
SEP CB   C  N N 294 
SEP OG   O  N N 295 
SEP C    C  N N 296 
SEP O    O  N N 297 
SEP OXT  O  N N 298 
SEP P    P  N N 299 
SEP O1P  O  N N 300 
SEP O2P  O  N N 301 
SEP O3P  O  N N 302 
SEP H    H  N N 303 
SEP H2   H  N N 304 
SEP HA   H  N N 305 
SEP HB2  H  N N 306 
SEP HB3  H  N N 307 
SEP HXT  H  N N 308 
SEP HOP2 H  N N 309 
SEP HOP3 H  N N 310 
SER N    N  N N 311 
SER CA   C  N S 312 
SER C    C  N N 313 
SER O    O  N N 314 
SER CB   C  N N 315 
SER OG   O  N N 316 
SER OXT  O  N N 317 
SER H    H  N N 318 
SER H2   H  N N 319 
SER HA   H  N N 320 
SER HB2  H  N N 321 
SER HB3  H  N N 322 
SER HG   H  N N 323 
SER HXT  H  N N 324 
THR N    N  N N 325 
THR CA   C  N S 326 
THR C    C  N N 327 
THR O    O  N N 328 
THR CB   C  N R 329 
THR OG1  O  N N 330 
THR CG2  C  N N 331 
THR OXT  O  N N 332 
THR H    H  N N 333 
THR H2   H  N N 334 
THR HA   H  N N 335 
THR HB   H  N N 336 
THR HG1  H  N N 337 
THR HG21 H  N N 338 
THR HG22 H  N N 339 
THR HG23 H  N N 340 
THR HXT  H  N N 341 
TRP N    N  N N 342 
TRP CA   C  N S 343 
TRP C    C  N N 344 
TRP O    O  N N 345 
TRP CB   C  N N 346 
TRP CG   C  Y N 347 
TRP CD1  C  Y N 348 
TRP CD2  C  Y N 349 
TRP NE1  N  Y N 350 
TRP CE2  C  Y N 351 
TRP CE3  C  Y N 352 
TRP CZ2  C  Y N 353 
TRP CZ3  C  Y N 354 
TRP CH2  C  Y N 355 
TRP OXT  O  N N 356 
TRP H    H  N N 357 
TRP H2   H  N N 358 
TRP HA   H  N N 359 
TRP HB2  H  N N 360 
TRP HB3  H  N N 361 
TRP HD1  H  N N 362 
TRP HE1  H  N N 363 
TRP HE3  H  N N 364 
TRP HZ2  H  N N 365 
TRP HZ3  H  N N 366 
TRP HH2  H  N N 367 
TRP HXT  H  N N 368 
TYR N    N  N N 369 
TYR CA   C  N S 370 
TYR C    C  N N 371 
TYR O    O  N N 372 
TYR CB   C  N N 373 
TYR CG   C  Y N 374 
TYR CD1  C  Y N 375 
TYR CD2  C  Y N 376 
TYR CE1  C  Y N 377 
TYR CE2  C  Y N 378 
TYR CZ   C  Y N 379 
TYR OH   O  N N 380 
TYR OXT  O  N N 381 
TYR H    H  N N 382 
TYR H2   H  N N 383 
TYR HA   H  N N 384 
TYR HB2  H  N N 385 
TYR HB3  H  N N 386 
TYR HD1  H  N N 387 
TYR HD2  H  N N 388 
TYR HE1  H  N N 389 
TYR HE2  H  N N 390 
TYR HH   H  N N 391 
TYR HXT  H  N N 392 
VAL N    N  N N 393 
VAL CA   C  N S 394 
VAL C    C  N N 395 
VAL O    O  N N 396 
VAL CB   C  N N 397 
VAL CG1  C  N N 398 
VAL CG2  C  N N 399 
VAL OXT  O  N N 400 
VAL H    H  N N 401 
VAL H2   H  N N 402 
VAL HA   H  N N 403 
VAL HB   H  N N 404 
VAL HG11 H  N N 405 
VAL HG12 H  N N 406 
VAL HG13 H  N N 407 
VAL HG21 H  N N 408 
VAL HG22 H  N N 409 
VAL HG23 H  N N 410 
VAL HXT  H  N N 411 
WQX C1   C  N N 412 
WQX C2   C  N N 413 
WQX C3   C  N N 414 
WQX C4   C  N N 415 
WQX C5   C  N N 416 
WQX C6   C  N N 417 
WQX C7   C  Y N 418 
WQX C8   C  Y N 419 
WQX C10  C  Y N 420 
WQX C11  C  Y N 421 
WQX C13  C  N N 422 
WQX C14  C  N N 423 
WQX C12  C  Y N 424 
WQX C9   C  Y N 425 
WQX F1   F  N N 426 
WQX N1   N  N N 427 
WQX N2   N  N N 428 
WQX O1   O  N N 429 
WQX O2   O  N N 430 
WQX O3   O  N N 431 
WQX O4   O  N N 432 
WQX S1   S  N N 433 
WQX BR1  BR N N 434 
WQX H1   H  N N 435 
WQX H2   H  N N 436 
WQX H4   H  N N 437 
WQX H5   H  N N 438 
WQX H6   H  N N 439 
WQX H7   H  N N 440 
WQX H8   H  N N 441 
WQX H9   H  N N 442 
WQX H10  H  N N 443 
WQX H11  H  N N 444 
WQX H12  H  N N 445 
WQX H13  H  N N 446 
WQX H14  H  N N 447 
WQX H15  H  N N 448 
WQX H16  H  N N 449 
WQX CL1  CL N N 450 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SEP N   CA   sing N N 277 
SEP N   H    sing N N 278 
SEP N   H2   sing N N 279 
SEP CA  CB   sing N N 280 
SEP CA  C    sing N N 281 
SEP CA  HA   sing N N 282 
SEP CB  OG   sing N N 283 
SEP CB  HB2  sing N N 284 
SEP CB  HB3  sing N N 285 
SEP OG  P    sing N N 286 
SEP C   O    doub N N 287 
SEP C   OXT  sing N N 288 
SEP OXT HXT  sing N N 289 
SEP P   O1P  doub N N 290 
SEP P   O2P  sing N N 291 
SEP P   O3P  sing N N 292 
SEP O2P HOP2 sing N N 293 
SEP O3P HOP3 sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
THR N   CA   sing N N 308 
THR N   H    sing N N 309 
THR N   H2   sing N N 310 
THR CA  C    sing N N 311 
THR CA  CB   sing N N 312 
THR CA  HA   sing N N 313 
THR C   O    doub N N 314 
THR C   OXT  sing N N 315 
THR CB  OG1  sing N N 316 
THR CB  CG2  sing N N 317 
THR CB  HB   sing N N 318 
THR OG1 HG1  sing N N 319 
THR CG2 HG21 sing N N 320 
THR CG2 HG22 sing N N 321 
THR CG2 HG23 sing N N 322 
THR OXT HXT  sing N N 323 
TRP N   CA   sing N N 324 
TRP N   H    sing N N 325 
TRP N   H2   sing N N 326 
TRP CA  C    sing N N 327 
TRP CA  CB   sing N N 328 
TRP CA  HA   sing N N 329 
TRP C   O    doub N N 330 
TRP C   OXT  sing N N 331 
TRP CB  CG   sing N N 332 
TRP CB  HB2  sing N N 333 
TRP CB  HB3  sing N N 334 
TRP CG  CD1  doub Y N 335 
TRP CG  CD2  sing Y N 336 
TRP CD1 NE1  sing Y N 337 
TRP CD1 HD1  sing N N 338 
TRP CD2 CE2  doub Y N 339 
TRP CD2 CE3  sing Y N 340 
TRP NE1 CE2  sing Y N 341 
TRP NE1 HE1  sing N N 342 
TRP CE2 CZ2  sing Y N 343 
TRP CE3 CZ3  doub Y N 344 
TRP CE3 HE3  sing N N 345 
TRP CZ2 CH2  doub Y N 346 
TRP CZ2 HZ2  sing N N 347 
TRP CZ3 CH2  sing Y N 348 
TRP CZ3 HZ3  sing N N 349 
TRP CH2 HH2  sing N N 350 
TRP OXT HXT  sing N N 351 
TYR N   CA   sing N N 352 
TYR N   H    sing N N 353 
TYR N   H2   sing N N 354 
TYR CA  C    sing N N 355 
TYR CA  CB   sing N N 356 
TYR CA  HA   sing N N 357 
TYR C   O    doub N N 358 
TYR C   OXT  sing N N 359 
TYR CB  CG   sing N N 360 
TYR CB  HB2  sing N N 361 
TYR CB  HB3  sing N N 362 
TYR CG  CD1  doub Y N 363 
TYR CG  CD2  sing Y N 364 
TYR CD1 CE1  sing Y N 365 
TYR CD1 HD1  sing N N 366 
TYR CD2 CE2  doub Y N 367 
TYR CD2 HD2  sing N N 368 
TYR CE1 CZ   doub Y N 369 
TYR CE1 HE1  sing N N 370 
TYR CE2 CZ   sing Y N 371 
TYR CE2 HE2  sing N N 372 
TYR CZ  OH   sing N N 373 
TYR OH  HH   sing N N 374 
TYR OXT HXT  sing N N 375 
VAL N   CA   sing N N 376 
VAL N   H    sing N N 377 
VAL N   H2   sing N N 378 
VAL CA  C    sing N N 379 
VAL CA  CB   sing N N 380 
VAL CA  HA   sing N N 381 
VAL C   O    doub N N 382 
VAL C   OXT  sing N N 383 
VAL CB  CG1  sing N N 384 
VAL CB  CG2  sing N N 385 
VAL CB  HB   sing N N 386 
VAL CG1 HG11 sing N N 387 
VAL CG1 HG12 sing N N 388 
VAL CG1 HG13 sing N N 389 
VAL CG2 HG21 sing N N 390 
VAL CG2 HG22 sing N N 391 
VAL CG2 HG23 sing N N 392 
VAL OXT HXT  sing N N 393 
WQX C2  C1   sing N N 394 
WQX O1  C1   doub N N 395 
WQX C1  N1   sing N N 396 
WQX N1  C3   sing N N 397 
WQX N1  C5   sing N N 398 
WQX C3  C4   sing N N 399 
WQX C5  C4   sing N N 400 
WQX O2  S1   doub N N 401 
WQX C6  C4   sing N N 402 
WQX C6  N2   sing N N 403 
WQX C4  O4   sing N N 404 
WQX F1  C11  sing N N 405 
WQX C12 C11  doub Y N 406 
WQX C12 C7   sing Y N 407 
WQX S1  N2   sing N N 408 
WQX S1  C7   sing N N 409 
WQX S1  O3   doub N N 410 
WQX N2  C13  sing N N 411 
WQX C11 C10  sing Y N 412 
WQX O4  C14  sing N N 413 
WQX C7  C8   doub Y N 414 
WQX C14 C13  sing N N 415 
WQX C10 BR1  sing N N 416 
WQX C10 C9   doub Y N 417 
WQX C8  C9   sing Y N 418 
WQX C2  H1   sing N N 419 
WQX C2  H2   sing N N 420 
WQX C3  H4   sing N N 421 
WQX C3  H5   sing N N 422 
WQX C5  H6   sing N N 423 
WQX C5  H7   sing N N 424 
WQX C6  H8   sing N N 425 
WQX C6  H9   sing N N 426 
WQX C8  H10  sing N N 427 
WQX C13 H11  sing N N 428 
WQX C13 H12  sing N N 429 
WQX C14 H13  sing N N 430 
WQX C14 H14  sing N N 431 
WQX C12 H15  sing N N 432 
WQX C9  H16  sing N N 433 
WQX C2  CL1  sing N N 434 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM147696 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3IQU 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8QS7 
_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]   0.016032 
_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]   0.006694 
_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]   0.013038 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
BR 
C  
CL 
F  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLY A 1 1   ? 35.597 41.605 24.790 1.00 62.23 ? -4  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1   ? 35.385 40.599 25.821 1.00 58.08 ? -4  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1   ? 36.615 40.322 26.672 1.00 54.29 ? -4  GLY A C   1 
ATOM   4    O  O   . GLY A 1 1   ? 37.703 40.845 26.388 1.00 55.76 ? -4  GLY A O   1 
ATOM   5    N  N   . ALA A 1 2   ? 36.450 39.490 27.709 1.00 53.20 ? -3  ALA A N   1 
ATOM   6    C  CA  . ALA A 1 2   ? 37.558 39.157 28.602 1.00 52.07 ? -3  ALA A CA  1 
ATOM   7    C  C   . ALA A 1 2   ? 38.697 38.459 27.877 1.00 48.07 ? -3  ALA A C   1 
ATOM   8    O  O   . ALA A 1 2   ? 39.818 38.439 28.393 1.00 49.33 ? -3  ALA A O   1 
ATOM   9    C  CB  . ALA A 1 2   ? 37.079 38.267 29.753 1.00 53.18 ? -3  ALA A CB  1 
ATOM   10   N  N   . MET A 1 3   ? 38.429 37.879 26.703 1.00 45.78 ? -2  MET A N   1 
ATOM   11   C  CA  . MET A 1 3   ? 39.390 37.081 25.955 1.00 41.67 ? -2  MET A CA  1 
ATOM   12   C  C   . MET A 1 3   ? 40.003 37.863 24.798 1.00 42.65 ? -2  MET A C   1 
ATOM   13   O  O   . MET A 1 3   ? 40.806 37.306 24.028 1.00 43.48 ? -2  MET A O   1 
ATOM   14   C  CB  . MET A 1 3   ? 38.679 35.843 25.398 1.00 42.80 ? -2  MET A CB  1 
ATOM   15   C  CG  . MET A 1 3   ? 38.451 34.661 26.347 1.00 41.51 ? -2  MET A CG  1 
ATOM   16   S  SD  . MET A 1 3   ? 39.552 34.400 27.747 1.00 44.35 ? -2  MET A SD  1 
ATOM   17   C  CE  . MET A 1 3   ? 38.486 33.610 28.946 1.00 43.28 ? -2  MET A CE  1 
ATOM   18   N  N   . GLY A 1 4   ? 39.602 39.131 24.632 1.00 45.77 ? -1  GLY A N   1 
ATOM   19   C  CA  . GLY A 1 4   ? 39.964 39.891 23.442 1.00 42.39 ? -1  GLY A CA  1 
ATOM   20   C  C   . GLY A 1 4   ? 41.457 40.098 23.283 1.00 43.69 ? -1  GLY A C   1 
ATOM   21   O  O   . GLY A 1 4   ? 41.947 40.217 22.155 1.00 39.19 ? -1  GLY A O   1 
ATOM   22   N  N   . SER A 1 5   ? 42.213 40.085 24.395 1.00 36.53 ? 0   SER A N   1 
ATOM   23   C  CA  . SER A 1 5   ? 43.652 40.293 24.289 1.00 34.09 ? 0   SER A CA  1 
ATOM   24   C  C   . SER A 1 5   ? 44.437 39.019 24.021 1.00 37.49 ? 0   SER A C   1 
ATOM   25   O  O   . SER A 1 5   ? 45.643 39.098 23.782 1.00 34.77 ? 0   SER A O   1 
ATOM   26   C  CB  . SER A 1 5   ? 44.199 40.972 25.553 1.00 36.58 ? 0   SER A CB  1 
ATOM   27   O  OG  . SER A 1 5   ? 44.093 40.124 26.692 1.00 43.79 ? 0   SER A OG  1 
ATOM   28   N  N   . MET A 1 6   ? 43.812 37.841 24.076 1.00 35.58 ? 1   MET A N   1 
ATOM   29   C  CA  . MET A 1 6   ? 44.563 36.605 23.852 1.00 35.59 ? 1   MET A CA  1 
ATOM   30   C  C   . MET A 1 6   ? 44.558 36.154 22.401 1.00 34.43 ? 1   MET A C   1 
ATOM   31   O  O   . MET A 1 6   ? 43.562 36.288 21.694 1.00 34.25 ? 1   MET A O   1 
ATOM   32   C  CB  . MET A 1 6   ? 44.029 35.457 24.721 1.00 33.54 ? 1   MET A CB  1 
ATOM   33   C  CG  . MET A 1 6   ? 45.125 34.516 25.166 1.00 38.37 ? 1   MET A CG  1 
ATOM   34   S  SD  . MET A 1 6   ? 44.481 33.153 26.175 1.00 41.27 ? 1   MET A SD  1 
ATOM   35   C  CE  . MET A 1 6   ? 43.410 34.024 27.277 1.00 38.03 ? 1   MET A CE  1 
ATOM   36   N  N   . GLU A 1 7   ? 45.691 35.621 21.956 1.00 33.74 ? 2   GLU A N   1 
ATOM   37   C  CA  . GLU A 1 7   ? 45.759 35.099 20.602 1.00 36.57 ? 2   GLU A CA  1 
ATOM   38   C  C   . GLU A 1 7   ? 44.833 33.913 20.431 1.00 37.83 ? 2   GLU A C   1 
ATOM   39   O  O   . GLU A 1 7   ? 44.695 33.088 21.338 1.00 33.81 ? 2   GLU A O   1 
ATOM   40   C  CB  . GLU A 1 7   ? 47.183 34.695 20.247 1.00 42.16 ? 2   GLU A CB  1 
ATOM   41   C  CG  . GLU A 1 7   ? 48.158 35.865 20.335 1.00 45.61 ? 2   GLU A CG  1 
ATOM   42   C  CD  . GLU A 1 7   ? 48.868 36.051 19.032 1.00 50.27 ? 2   GLU A CD  1 
ATOM   43   O  OE1 . GLU A 1 7   ? 50.124 36.114 18.979 1.00 48.22 ? 2   GLU A OE1 1 
ATOM   44   O  OE2 . GLU A 1 7   ? 48.134 36.056 18.016 1.00 57.01 ? 2   GLU A OE2 1 
ATOM   45   N  N   . ARG A 1 8   ? 44.213 33.838 19.247 1.00 37.42 ? 3   ARG A N   1 
ATOM   46   C  CA  . ARG A 1 8   ? 43.344 32.702 18.920 1.00 38.14 ? 3   ARG A CA  1 
ATOM   47   C  C   . ARG A 1 8   ? 43.985 31.352 19.234 1.00 36.20 ? 3   ARG A C   1 
ATOM   48   O  O   . ARG A 1 8   ? 43.333 30.478 19.815 1.00 36.22 ? 3   ARG A O   1 
ATOM   49   C  CB  . ARG A 1 8   ? 42.941 32.754 17.451 1.00 37.50 ? 3   ARG A CB  1 
ATOM   50   C  CG  . ARG A 1 8   ? 41.738 31.817 17.125 1.00 35.15 ? 3   ARG A CG  1 
ATOM   51   C  CD  . ARG A 1 8   ? 41.606 31.672 15.614 1.00 39.00 ? 3   ARG A CD  1 
ATOM   52   N  NE  . ARG A 1 8   ? 40.422 30.904 15.257 1.00 38.14 ? 3   ARG A NE  1 
ATOM   53   C  CZ  . ARG A 1 8   ? 40.361 29.579 15.275 1.00 39.13 ? 3   ARG A CZ  1 
ATOM   54   N  NH1 . ARG A 1 8   ? 41.412 28.841 15.606 1.00 38.87 ? 3   ARG A NH1 1 
ATOM   55   N  NH2 . ARG A 1 8   ? 39.216 28.980 14.961 1.00 39.72 ? 3   ARG A NH2 1 
ATOM   56   N  N   . ALA A 1 9   ? 45.240 31.137 18.827 1.00 34.97 ? 4   ALA A N   1 
ATOM   57   C  CA  . ALA A 1 9   ? 45.837 29.822 19.052 1.00 36.65 ? 4   ALA A CA  1 
ATOM   58   C  C   . ALA A 1 9   ? 45.998 29.528 20.538 1.00 38.57 ? 4   ALA A C   1 
ATOM   59   O  O   . ALA A 1 9   ? 45.864 28.370 20.960 1.00 36.44 ? 4   ALA A O   1 
ATOM   60   C  CB  . ALA A 1 9   ? 47.177 29.695 18.341 1.00 37.97 ? 4   ALA A CB  1 
ATOM   61   N  N   . SER A 1 10  ? 46.271 30.560 21.348 1.00 36.31 ? 5   SER A N   1 
ATOM   62   C  CA  . SER A 1 10  ? 46.386 30.368 22.784 1.00 35.69 ? 5   SER A CA  1 
ATOM   63   C  C   . SER A 1 10  ? 45.038 30.040 23.395 1.00 34.73 ? 5   SER A C   1 
ATOM   64   O  O   . SER A 1 10  ? 44.953 29.251 24.351 1.00 32.69 ? 5   SER A O   1 
ATOM   65   C  CB  . SER A 1 10  ? 46.962 31.634 23.445 1.00 35.02 ? 5   SER A CB  1 
ATOM   66   O  OG  . SER A 1 10  ? 48.256 31.905 22.935 1.00 38.43 ? 5   SER A OG  1 
ATOM   67   N  N   . LEU A 1 11  ? 43.975 30.643 22.862 1.00 32.32 ? 6   LEU A N   1 
ATOM   68   C  CA  . LEU A 1 11  ? 42.647 30.331 23.363 1.00 30.61 ? 6   LEU A CA  1 
ATOM   69   C  C   . LEU A 1 11  ? 42.293 28.872 23.076 1.00 34.50 ? 6   LEU A C   1 
ATOM   70   O  O   . LEU A 1 11  ? 41.798 28.174 23.966 1.00 32.59 ? 6   LEU A O   1 
ATOM   71   C  CB  . LEU A 1 11  ? 41.613 31.267 22.761 1.00 32.48 ? 6   LEU A CB  1 
ATOM   72   C  CG  . LEU A 1 11  ? 41.685 32.709 23.296 1.00 34.12 ? 6   LEU A CG  1 
ATOM   73   C  CD1 . LEU A 1 11  ? 40.879 33.609 22.328 1.00 34.76 ? 6   LEU A CD1 1 
ATOM   74   C  CD2 . LEU A 1 11  ? 41.163 32.750 24.729 1.00 31.17 ? 6   LEU A CD2 1 
ATOM   75   N  N   . ILE A 1 12  ? 42.583 28.393 21.855 1.00 33.89 ? 7   ILE A N   1 
ATOM   76   C  CA  . ILE A 1 12  ? 42.343 26.978 21.539 1.00 34.20 ? 7   ILE A CA  1 
ATOM   77   C  C   . ILE A 1 12  ? 43.142 26.084 22.471 1.00 36.09 ? 7   ILE A C   1 
ATOM   78   O  O   . ILE A 1 12  ? 42.638 25.072 22.979 1.00 34.34 ? 7   ILE A O   1 
ATOM   79   C  CB  . ILE A 1 12  ? 42.698 26.667 20.079 1.00 32.71 ? 7   ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 12  ? 41.845 27.482 19.087 1.00 36.05 ? 7   ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 12  ? 42.619 25.139 19.840 1.00 32.04 ? 7   ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 12  ? 40.372 27.340 19.285 1.00 33.10 ? 7   ILE A CD1 1 
ATOM   83   N  N   . GLN A 1 13  ? 44.422 26.412 22.656 1.00 33.65 ? 8   GLN A N   1 
ATOM   84   C  CA  . GLN A 1 13  ? 45.291 25.611 23.504 1.00 36.61 ? 8   GLN A CA  1 
ATOM   85   C  C   . GLN A 1 13  ? 44.764 25.562 24.931 1.00 39.28 ? 8   GLN A C   1 
ATOM   86   O  O   . GLN A 1 13  ? 44.767 24.496 25.575 1.00 33.44 ? 8   GLN A O   1 
ATOM   87   C  CB  . GLN A 1 13  ? 46.708 26.178 23.452 1.00 39.99 ? 8   GLN A CB  1 
ATOM   88   C  CG  . GLN A 1 13  ? 47.732 25.427 24.272 1.00 46.41 ? 8   GLN A CG  1 
ATOM   89   C  CD  . GLN A 1 13  ? 49.098 26.119 24.242 1.00 51.51 ? 8   GLN A CD  1 
ATOM   90   O  OE1 . GLN A 1 13  ? 49.348 26.987 23.381 1.00 53.08 ? 8   GLN A OE1 1 
ATOM   91   N  NE2 . GLN A 1 13  ? 50.030 25.647 25.096 1.00 51.12 ? 8   GLN A NE2 1 
ATOM   92   N  N   . LYS A 1 14  ? 44.275 26.702 25.437 1.00 33.48 ? 9   LYS A N   1 
ATOM   93   C  CA  . LYS A 1 14  ? 43.765 26.726 26.802 1.00 33.77 ? 9   LYS A CA  1 
ATOM   94   C  C   . LYS A 1 14  ? 42.422 26.019 26.906 1.00 31.53 ? 9   LYS A C   1 
ATOM   95   O  O   . LYS A 1 14  ? 42.130 25.409 27.940 1.00 32.70 ? 9   LYS A O   1 
ATOM   96   C  CB  . LYS A 1 14  ? 43.690 28.178 27.309 1.00 35.10 ? 9   LYS A CB  1 
ATOM   97   C  CG  . LYS A 1 14  ? 45.078 28.705 27.604 1.00 36.37 ? 9   LYS A CG  1 
ATOM   98   C  CD  . LYS A 1 14  ? 45.032 30.168 28.120 1.00 35.91 ? 9   LYS A CD  1 
ATOM   99   C  CE  . LYS A 1 14  ? 46.430 30.726 28.248 1.00 40.69 ? 9   LYS A CE  1 
ATOM   100  N  NZ  . LYS A 1 14  ? 46.351 32.120 28.834 1.00 36.98 ? 9   LYS A NZ  1 
ATOM   101  N  N   . ALA A 1 15  ? 41.615 26.035 25.844 1.00 34.03 ? 10  ALA A N   1 
ATOM   102  C  CA  . ALA A 1 15  ? 40.383 25.248 25.885 1.00 32.29 ? 10  ALA A CA  1 
ATOM   103  C  C   . ALA A 1 15  ? 40.707 23.770 26.017 1.00 32.10 ? 10  ALA A C   1 
ATOM   104  O  O   . ALA A 1 15  ? 40.012 23.039 26.734 1.00 34.77 ? 10  ALA A O   1 
ATOM   105  C  CB  . ALA A 1 15  ? 39.536 25.492 24.642 1.00 31.09 ? 10  ALA A CB  1 
ATOM   106  N  N   . LYS A 1 16  ? 41.756 23.314 25.331 1.00 29.86 ? 11  LYS A N   1 
ATOM   107  C  CA  . LYS A 1 16  ? 42.150 21.907 25.440 1.00 34.53 ? 11  LYS A CA  1 
ATOM   108  C  C   . LYS A 1 16  ? 42.660 21.569 26.844 1.00 39.15 ? 11  LYS A C   1 
ATOM   109  O  O   . LYS A 1 16  ? 42.369 20.488 27.372 1.00 33.76 ? 11  LYS A O   1 
ATOM   110  C  CB  . LYS A 1 16  ? 43.199 21.582 24.394 1.00 34.03 ? 11  LYS A CB  1 
ATOM   111  C  CG  . LYS A 1 16  ? 42.651 21.572 22.967 1.00 36.23 ? 11  LYS A CG  1 
ATOM   112  C  CD  . LYS A 1 16  ? 43.761 21.260 21.975 1.00 40.01 ? 11  LYS A CD  1 
ATOM   113  C  CE  . LYS A 1 16  ? 43.264 21.357 20.529 1.00 44.93 ? 11  LYS A CE  1 
ATOM   114  N  NZ  . LYS A 1 16  ? 44.396 21.458 19.547 1.00 39.74 ? 11  LYS A NZ  1 
ATOM   115  N  N   . LEU A 1 17  ? 43.439 22.470 27.453 1.00 32.18 ? 12  LEU A N   1 
ATOM   116  C  CA  . LEU A 1 17  ? 43.857 22.289 28.847 1.00 34.41 ? 12  LEU A CA  1 
ATOM   117  C  C   . LEU A 1 17  ? 42.660 22.269 29.783 1.00 36.15 ? 12  LEU A C   1 
ATOM   118  O  O   . LEU A 1 17  ? 42.600 21.451 30.716 1.00 36.67 ? 12  LEU A O   1 
ATOM   119  C  CB  . LEU A 1 17  ? 44.818 23.413 29.265 1.00 35.45 ? 12  LEU A CB  1 
ATOM   120  C  CG  . LEU A 1 17  ? 46.135 23.463 28.488 1.00 37.02 ? 12  LEU A CG  1 
ATOM   121  C  CD1 . LEU A 1 17  ? 46.855 24.825 28.823 1.00 39.17 ? 12  LEU A CD1 1 
ATOM   122  C  CD2 . LEU A 1 17  ? 47.018 22.248 28.810 1.00 36.40 ? 12  LEU A CD2 1 
ATOM   123  N  N   . ALA A 1 18  ? 41.719 23.206 29.591 1.00 32.10 ? 13  ALA A N   1 
ATOM   124  C  CA  . ALA A 1 18  ? 40.538 23.231 30.448 1.00 35.08 ? 13  ALA A CA  1 
ATOM   125  C  C   . ALA A 1 18  ? 39.726 21.937 30.332 1.00 34.09 ? 13  ALA A C   1 
ATOM   126  O  O   . ALA A 1 18  ? 39.170 21.458 31.326 1.00 33.78 ? 13  ALA A O   1 
ATOM   127  C  CB  . ALA A 1 18  ? 39.678 24.445 30.105 1.00 34.73 ? 13  ALA A CB  1 
ATOM   128  N  N   . GLU A 1 19  ? 39.619 21.383 29.121 1.00 36.09 ? 14  GLU A N   1 
ATOM   129  C  CA  . GLU A 1 19  ? 38.956 20.089 28.965 1.00 37.29 ? 14  GLU A CA  1 
ATOM   130  C  C   . GLU A 1 19  ? 39.674 19.009 29.774 1.00 38.13 ? 14  GLU A C   1 
ATOM   131  O  O   . GLU A 1 19  ? 39.040 18.221 30.497 1.00 36.82 ? 14  GLU A O   1 
ATOM   132  C  CB  . GLU A 1 19  ? 38.894 19.709 27.489 1.00 35.80 ? 14  GLU A CB  1 
ATOM   133  C  CG  . GLU A 1 19  ? 38.123 18.390 27.252 1.00 38.62 ? 14  GLU A CG  1 
ATOM   134  C  CD  . GLU A 1 19  ? 38.076 17.964 25.792 1.00 42.61 ? 14  GLU A CD  1 
ATOM   135  O  OE1 . GLU A 1 19  ? 38.976 18.331 24.994 1.00 42.74 ? 14  GLU A OE1 1 
ATOM   136  O  OE2 . GLU A 1 19  ? 37.102 17.272 25.431 1.00 43.85 ? 14  GLU A OE2 1 
ATOM   137  N  N   . GLN A 1 20  ? 41.008 18.989 29.696 1.00 35.35 ? 15  GLN A N   1 
ATOM   138  C  CA  . GLN A 1 20  ? 41.788 18.008 30.451 1.00 36.73 ? 15  GLN A CA  1 
ATOM   139  C  C   . GLN A 1 20  ? 41.580 18.151 31.949 1.00 39.57 ? 15  GLN A C   1 
ATOM   140  O  O   . GLN A 1 20  ? 41.538 17.146 32.677 1.00 34.82 ? 15  GLN A O   1 
ATOM   141  C  CB  . GLN A 1 20  ? 43.265 18.142 30.115 1.00 37.20 ? 15  GLN A CB  1 
ATOM   142  C  CG  . GLN A 1 20  ? 43.655 17.467 28.825 1.00 41.68 ? 15  GLN A CG  1 
ATOM   143  C  CD  . GLN A 1 20  ? 45.106 17.721 28.477 1.00 51.73 ? 15  GLN A CD  1 
ATOM   144  O  OE1 . GLN A 1 20  ? 45.480 18.834 28.088 1.00 54.76 ? 15  GLN A OE1 1 
ATOM   145  N  NE2 . GLN A 1 20  ? 45.949 16.717 28.684 1.00 54.11 ? 15  GLN A NE2 1 
ATOM   146  N  N   . ALA A 1 21  ? 41.435 19.373 32.433 1.00 34.21 ? 16  ALA A N   1 
ATOM   147  C  CA  . ALA A 1 21  ? 41.239 19.656 33.847 1.00 35.70 ? 16  ALA A CA  1 
ATOM   148  C  C   . ALA A 1 21  ? 39.771 19.601 34.276 1.00 36.08 ? 16  ALA A C   1 
ATOM   149  O  O   . ALA A 1 21  ? 39.478 19.848 35.454 1.00 34.93 ? 16  ALA A O   1 
ATOM   150  C  CB  . ALA A 1 21  ? 41.827 21.037 34.183 1.00 36.57 ? 16  ALA A CB  1 
ATOM   151  N  N   . GLU A 1 22  ? 38.857 19.272 33.353 1.00 32.27 ? 17  GLU A N   1 
ATOM   152  C  CA  . GLU A 1 22  ? 37.412 19.245 33.603 1.00 35.77 ? 17  GLU A CA  1 
ATOM   153  C  C   . GLU A 1 22  ? 36.924 20.603 34.103 1.00 36.41 ? 17  GLU A C   1 
ATOM   154  O  O   . GLU A 1 22  ? 36.055 20.709 34.961 1.00 36.54 ? 17  GLU A O   1 
ATOM   155  C  CB  . GLU A 1 22  ? 37.017 18.104 34.567 1.00 40.17 ? 17  GLU A CB  1 
ATOM   156  C  CG  . GLU A 1 22  ? 37.492 16.774 34.023 1.00 38.92 ? 17  GLU A CG  1 
ATOM   157  C  CD  . GLU A 1 22  ? 37.079 15.589 34.879 1.00 51.83 ? 17  GLU A CD  1 
ATOM   158  O  OE1 . GLU A 1 22  ? 35.866 15.345 35.043 1.00 54.40 ? 17  GLU A OE1 1 
ATOM   159  O  OE2 . GLU A 1 22  ? 37.977 14.930 35.423 1.00 55.43 ? 17  GLU A OE2 1 
ATOM   160  N  N   . ARG A 1 23  ? 37.494 21.667 33.549 1.00 36.48 ? 18  ARG A N   1 
ATOM   161  C  CA  . ARG A 1 23  ? 37.067 23.030 33.865 1.00 34.70 ? 18  ARG A CA  1 
ATOM   162  C  C   . ARG A 1 23  ? 36.219 23.529 32.702 1.00 36.68 ? 18  ARG A C   1 
ATOM   163  O  O   . ARG A 1 23  ? 36.696 24.243 31.824 1.00 33.17 ? 18  ARG A O   1 
ATOM   164  C  CB  . ARG A 1 23  ? 38.294 23.915 34.087 1.00 35.49 ? 18  ARG A CB  1 
ATOM   165  C  CG  . ARG A 1 23  ? 39.117 23.516 35.312 1.00 37.67 ? 18  ARG A CG  1 
ATOM   166  C  CD  . ARG A 1 23  ? 38.562 24.187 36.532 1.00 38.67 ? 18  ARG A CD  1 
ATOM   167  N  NE  . ARG A 1 23  ? 38.752 25.625 36.412 1.00 39.27 ? 18  ARG A NE  1 
ATOM   168  C  CZ  . ARG A 1 23  ? 38.717 26.478 37.425 1.00 41.36 ? 18  ARG A CZ  1 
ATOM   169  N  NH1 . ARG A 1 23  ? 38.550 26.065 38.674 1.00 39.01 ? 18  ARG A NH1 1 
ATOM   170  N  NH2 . ARG A 1 23  ? 38.859 27.778 37.180 1.00 33.71 ? 18  ARG A NH2 1 
ATOM   171  N  N   . TYR A 1 24  ? 34.939 23.131 32.677 1.00 35.36 ? 19  TYR A N   1 
ATOM   172  C  CA  . TYR A 1 24  ? 34.198 23.316 31.431 1.00 33.69 ? 19  TYR A CA  1 
ATOM   173  C  C   . TYR A 1 24  ? 33.693 24.740 31.259 1.00 33.32 ? 19  TYR A C   1 
ATOM   174  O  O   . TYR A 1 24  ? 33.524 25.184 30.115 1.00 32.64 ? 19  TYR A O   1 
ATOM   175  C  CB  . TYR A 1 24  ? 33.026 22.341 31.331 1.00 34.26 ? 19  TYR A CB  1 
ATOM   176  C  CG  . TYR A 1 24  ? 33.525 20.917 31.249 1.00 35.91 ? 19  TYR A CG  1 
ATOM   177  C  CD1 . TYR A 1 24  ? 34.118 20.449 30.088 1.00 38.30 ? 19  TYR A CD1 1 
ATOM   178  C  CD2 . TYR A 1 24  ? 33.458 20.066 32.362 1.00 39.39 ? 19  TYR A CD2 1 
ATOM   179  C  CE1 . TYR A 1 24  ? 34.609 19.156 29.998 1.00 38.46 ? 19  TYR A CE1 1 
ATOM   180  C  CE2 . TYR A 1 24  ? 33.958 18.760 32.291 1.00 41.16 ? 19  TYR A CE2 1 
ATOM   181  C  CZ  . TYR A 1 24  ? 34.526 18.326 31.109 1.00 43.67 ? 19  TYR A CZ  1 
ATOM   182  O  OH  . TYR A 1 24  ? 35.020 17.041 31.009 1.00 47.52 ? 19  TYR A OH  1 
ATOM   183  N  N   . GLU A 1 25  ? 33.442 25.452 32.359 1.00 34.05 ? 20  GLU A N   1 
ATOM   184  C  CA  . GLU A 1 25  ? 33.112 26.866 32.226 1.00 36.64 ? 20  GLU A CA  1 
ATOM   185  C  C   . GLU A 1 25  ? 34.284 27.644 31.629 1.00 35.31 ? 20  GLU A C   1 
ATOM   186  O  O   . GLU A 1 25  ? 34.093 28.463 30.724 1.00 34.06 ? 20  GLU A O   1 
ATOM   187  C  CB  . GLU A 1 25  ? 32.691 27.436 33.586 1.00 38.14 ? 20  GLU A CB  1 
ATOM   188  C  CG  . GLU A 1 25  ? 31.270 27.019 33.951 1.00 46.09 ? 20  GLU A CG  1 
ATOM   189  C  CD  . GLU A 1 25  ? 30.662 27.799 35.122 1.00 63.74 ? 20  GLU A CD  1 
ATOM   190  O  OE1 . GLU A 1 25  ? 31.409 28.554 35.810 1.00 57.52 ? 20  GLU A OE1 1 
ATOM   191  O  OE2 . GLU A 1 25  ? 29.421 27.647 35.333 1.00 62.56 ? 20  GLU A OE2 1 
ATOM   192  N  N   . ASP A 1 26  ? 35.498 27.433 32.154 1.00 33.41 ? 21  ASP A N   1 
ATOM   193  C  CA  . ASP A 1 26  ? 36.688 28.010 31.531 1.00 31.48 ? 21  ASP A CA  1 
ATOM   194  C  C   . ASP A 1 26  ? 36.757 27.615 30.056 1.00 33.64 ? 21  ASP A C   1 
ATOM   195  O  O   . ASP A 1 26  ? 37.085 28.427 29.177 1.00 31.56 ? 21  ASP A O   1 
ATOM   196  C  CB  . ASP A 1 26  ? 37.965 27.517 32.223 1.00 32.48 ? 21  ASP A CB  1 
ATOM   197  C  CG  . ASP A 1 26  ? 38.174 28.080 33.619 1.00 37.94 ? 21  ASP A CG  1 
ATOM   198  O  OD1 . ASP A 1 26  ? 37.449 29.005 34.040 1.00 36.77 ? 21  ASP A OD1 1 
ATOM   199  O  OD2 . ASP A 1 26  ? 39.103 27.591 34.285 1.00 40.16 ? 21  ASP A OD2 1 
ATOM   200  N  N   . MET A 1 27  ? 36.516 26.329 29.763 1.00 32.12 ? 22  MET A N   1 
ATOM   201  C  CA  . MET A 1 27  ? 36.757 25.937 28.389 1.00 29.92 ? 22  MET A CA  1 
ATOM   202  C  C   . MET A 1 27  ? 35.691 26.555 27.486 1.00 32.15 ? 22  MET A C   1 
ATOM   203  O  O   . MET A 1 27  ? 35.998 26.932 26.357 1.00 34.10 ? 22  MET A O   1 
ATOM   204  C  CB  . MET A 1 27  ? 36.928 24.393 28.287 1.00 35.74 ? 22  MET A CB  1 
ATOM   205  C  CG  . MET A 1 27  ? 36.678 23.735 26.970 1.00 28.94 ? 22  MET A CG  1 
ATOM   206  S  SD  . MET A 1 27  ? 36.106 21.968 27.111 1.00 33.19 ? 22  MET A SD  1 
ATOM   207  C  CE  . MET A 1 27  ? 36.443 21.438 25.435 1.00 34.10 ? 22  MET A CE  1 
ATOM   208  N  N   . ALA A 1 28  ? 34.473 26.782 28.001 1.00 31.10 ? 23  ALA A N   1 
ATOM   209  C  CA  . ALA A 1 28  ? 33.488 27.487 27.199 1.00 31.39 ? 23  ALA A CA  1 
ATOM   210  C  C   . ALA A 1 28  ? 33.913 28.937 26.988 1.00 32.42 ? 23  ALA A C   1 
ATOM   211  O  O   . ALA A 1 28  ? 33.800 29.460 25.873 1.00 32.60 ? 23  ALA A O   1 
ATOM   212  C  CB  . ALA A 1 28  ? 32.103 27.434 27.838 1.00 28.82 ? 23  ALA A CB  1 
ATOM   213  N  N   . ALA A 1 29  ? 34.459 29.561 28.032 1.00 34.33 ? 24  ALA A N   1 
ATOM   214  C  CA  . ALA A 1 29  ? 34.914 30.950 27.923 1.00 33.99 ? 24  ALA A CA  1 
ATOM   215  C  C   . ALA A 1 29  ? 36.029 31.091 26.891 1.00 35.12 ? 24  ALA A C   1 
ATOM   216  O  O   . ALA A 1 29  ? 36.020 32.021 26.082 1.00 31.67 ? 24  ALA A O   1 
ATOM   217  C  CB  . ALA A 1 29  ? 35.370 31.441 29.299 1.00 32.83 ? 24  ALA A CB  1 
ATOM   218  N  N   . PHE A 1 30  ? 37.005 30.171 26.907 1.00 32.73 ? 25  PHE A N   1 
ATOM   219  C  CA  . PHE A 1 30  ? 38.078 30.176 25.923 1.00 34.05 ? 25  PHE A CA  1 
ATOM   220  C  C   . PHE A 1 30  ? 37.553 30.001 24.496 1.00 33.94 ? 25  PHE A C   1 
ATOM   221  O  O   . PHE A 1 30  ? 38.001 30.695 23.563 1.00 32.81 ? 25  PHE A O   1 
ATOM   222  C  CB  . PHE A 1 30  ? 39.094 29.073 26.251 1.00 29.64 ? 25  PHE A CB  1 
ATOM   223  C  CG  . PHE A 1 30  ? 39.887 29.326 27.491 1.00 35.90 ? 25  PHE A CG  1 
ATOM   224  C  CD1 . PHE A 1 30  ? 40.451 30.601 27.743 1.00 33.20 ? 25  PHE A CD1 1 
ATOM   225  C  CD2 . PHE A 1 30  ? 40.109 28.296 28.405 1.00 33.86 ? 25  PHE A CD2 1 
ATOM   226  C  CE1 . PHE A 1 30  ? 41.178 30.822 28.904 1.00 34.82 ? 25  PHE A CE1 1 
ATOM   227  C  CE2 . PHE A 1 30  ? 40.842 28.505 29.550 1.00 35.36 ? 25  PHE A CE2 1 
ATOM   228  C  CZ  . PHE A 1 30  ? 41.394 29.765 29.805 1.00 34.57 ? 25  PHE A CZ  1 
ATOM   229  N  N   . MET A 1 31  ? 36.611 29.071 24.304 1.00 31.14 ? 26  MET A N   1 
ATOM   230  C  CA  . MET A 1 31  ? 36.095 28.806 22.963 1.00 30.74 ? 26  MET A CA  1 
ATOM   231  C  C   . MET A 1 31  ? 35.262 29.984 22.459 1.00 35.87 ? 26  MET A C   1 
ATOM   232  O  O   . MET A 1 31  ? 35.281 30.282 21.258 1.00 33.56 ? 26  MET A O   1 
ATOM   233  C  CB  . MET A 1 31  ? 35.259 27.523 23.001 1.00 31.99 ? 26  MET A CB  1 
ATOM   234  C  CG  . MET A 1 31  ? 36.091 26.260 22.747 1.00 34.95 ? 26  MET A CG  1 
ATOM   235  S  SD  . MET A 1 31  ? 37.634 26.359 21.827 1.00 32.60 ? 26  MET A SD  1 
ATOM   236  C  CE  . MET A 1 31  ? 36.926 26.499 20.200 1.00 33.61 ? 26  MET A CE  1 
ATOM   237  N  N   . LYS A 1 32  ? 34.493 30.622 23.348 1.00 34.01 ? 27  LYS A N   1 
ATOM   238  C  CA  . LYS A 1 32  ? 33.742 31.818 22.958 1.00 38.15 ? 27  LYS A CA  1 
ATOM   239  C  C   . LYS A 1 32  ? 34.700 32.909 22.494 1.00 36.30 ? 27  LYS A C   1 
ATOM   240  O  O   . LYS A 1 32  ? 34.488 33.541 21.442 1.00 36.27 ? 27  LYS A O   1 
ATOM   241  C  CB  . LYS A 1 32  ? 32.886 32.310 24.137 1.00 36.53 ? 27  LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 32  ? 32.169 33.691 23.910 1.00 42.21 ? 27  LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 32  ? 31.157 33.978 25.048 1.00 42.47 ? 27  LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 32  ? 30.287 35.225 24.785 1.00 50.92 ? 27  LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 32  ? 31.114 36.452 24.786 1.00 45.20 ? 27  LYS A NZ  1 
ATOM   246  N  N   . GLY A 1 33  ? 35.790 33.098 23.243 1.00 35.34 ? 28  GLY A N   1 
ATOM   247  C  CA  . GLY A 1 33  ? 36.822 34.040 22.814 1.00 38.46 ? 28  GLY A CA  1 
ATOM   248  C  C   . GLY A 1 33  ? 37.422 33.667 21.474 1.00 39.47 ? 28  GLY A C   1 
ATOM   249  O  O   . GLY A 1 33  ? 37.687 34.527 20.634 1.00 35.36 ? 28  GLY A O   1 
ATOM   250  N  N   . ALA A 1 34  ? 37.647 32.375 21.248 1.00 34.49 ? 29  ALA A N   1 
ATOM   251  C  CA  . ALA A 1 34  ? 38.135 31.951 19.945 1.00 34.52 ? 29  ALA A CA  1 
ATOM   252  C  C   . ALA A 1 34  ? 37.117 32.265 18.861 1.00 37.19 ? 29  ALA A C   1 
ATOM   253  O  O   . ALA A 1 34  ? 37.479 32.748 17.785 1.00 35.17 ? 29  ALA A O   1 
ATOM   254  C  CB  . ALA A 1 34  ? 38.459 30.449 19.957 1.00 33.04 ? 29  ALA A CB  1 
ATOM   255  N  N   . VAL A 1 35  ? 35.837 31.966 19.112 1.00 32.66 ? 30  VAL A N   1 
ATOM   256  C  CA  . VAL A 1 35  ? 34.823 32.228 18.094 1.00 35.65 ? 30  VAL A CA  1 
ATOM   257  C  C   . VAL A 1 35  ? 34.812 33.712 17.749 1.00 37.80 ? 30  VAL A C   1 
ATOM   258  O  O   . VAL A 1 35  ? 34.652 34.097 16.582 1.00 38.97 ? 30  VAL A O   1 
ATOM   259  C  CB  . VAL A 1 35  ? 33.436 31.774 18.573 1.00 36.60 ? 30  VAL A CB  1 
ATOM   260  C  CG1 . VAL A 1 35  ? 32.345 32.301 17.647 1.00 36.79 ? 30  VAL A CG1 1 
ATOM   261  C  CG2 . VAL A 1 35  ? 33.375 30.195 18.659 1.00 35.66 ? 30  VAL A CG2 1 
ATOM   262  N  N   . GLU A 1 36  ? 34.972 34.554 18.764 1.00 36.66 ? 31  GLU A N   1 
ATOM   263  C  CA  . GLU A 1 36  ? 34.906 36.001 18.602 1.00 37.91 ? 31  GLU A CA  1 
ATOM   264  C  C   . GLU A 1 36  ? 36.059 36.563 17.779 1.00 41.46 ? 31  GLU A C   1 
ATOM   265  O  O   . GLU A 1 36  ? 35.962 37.711 17.314 1.00 40.55 ? 31  GLU A O   1 
ATOM   266  C  CB  . GLU A 1 36  ? 34.814 36.636 19.988 1.00 38.41 ? 31  GLU A CB  1 
ATOM   267  C  CG  . GLU A 1 36  ? 33.374 36.582 20.465 1.00 43.33 ? 31  GLU A CG  1 
ATOM   268  C  CD  . GLU A 1 36  ? 33.169 36.939 21.910 1.00 45.69 ? 31  GLU A CD  1 
ATOM   269  O  OE1 . GLU A 1 36  ? 34.163 37.102 22.660 1.00 47.70 ? 31  GLU A OE1 1 
ATOM   270  O  OE2 . GLU A 1 36  ? 31.985 37.032 22.300 1.00 50.78 ? 31  GLU A OE2 1 
ATOM   271  N  N   . LYS A 1 37  ? 37.118 35.789 17.534 1.00 36.67 ? 32  LYS A N   1 
ATOM   272  C  CA  . LYS A 1 37  ? 38.134 36.239 16.587 1.00 38.93 ? 32  LYS A CA  1 
ATOM   273  C  C   . LYS A 1 37  ? 37.590 36.364 15.166 1.00 43.18 ? 32  LYS A C   1 
ATOM   274  O  O   . LYS A 1 37  ? 38.221 37.015 14.327 1.00 41.30 ? 32  LYS A O   1 
ATOM   275  C  CB  . LYS A 1 37  ? 39.346 35.308 16.604 1.00 36.72 ? 32  LYS A CB  1 
ATOM   276  C  CG  . LYS A 1 37  ? 40.018 35.153 17.986 1.00 36.34 ? 32  LYS A CG  1 
ATOM   277  C  CD  . LYS A 1 37  ? 40.545 36.497 18.566 1.00 38.22 ? 32  LYS A CD  1 
ATOM   278  C  CE  . LYS A 1 37  ? 41.112 36.260 19.946 1.00 41.13 ? 32  LYS A CE  1 
ATOM   279  N  NZ  . LYS A 1 37  ? 41.271 37.533 20.771 1.00 40.12 ? 32  LYS A NZ  1 
ATOM   280  N  N   . GLY A 1 38  ? 36.441 35.753 14.878 1.00 41.21 ? 33  GLY A N   1 
ATOM   281  C  CA  . GLY A 1 38  ? 35.787 35.900 13.600 1.00 41.44 ? 33  GLY A CA  1 
ATOM   282  C  C   . GLY A 1 38  ? 36.293 35.005 12.498 1.00 44.09 ? 33  GLY A C   1 
ATOM   283  O  O   . GLY A 1 38  ? 35.927 35.229 11.342 1.00 43.63 ? 33  GLY A O   1 
ATOM   284  N  N   . GLU A 1 39  ? 37.124 34.004 12.794 1.00 41.65 ? 34  GLU A N   1 
ATOM   285  C  CA  . GLU A 1 39  ? 37.509 33.037 11.774 1.00 39.96 ? 34  GLU A CA  1 
ATOM   286  C  C   . GLU A 1 39  ? 36.701 31.749 11.935 1.00 39.04 ? 34  GLU A C   1 
ATOM   287  O  O   . GLU A 1 39  ? 36.138 31.488 13.000 1.00 39.72 ? 34  GLU A O   1 
ATOM   288  C  CB  . GLU A 1 39  ? 39.003 32.719 11.831 1.00 41.93 ? 34  GLU A CB  1 
ATOM   289  C  CG  . GLU A 1 39  ? 39.862 33.951 11.921 1.00 51.47 ? 34  GLU A CG  1 
ATOM   290  C  CD  . GLU A 1 39  ? 41.339 33.617 11.932 1.00 59.26 ? 34  GLU A CD  1 
ATOM   291  O  OE1 . GLU A 1 39  ? 41.697 32.480 12.322 1.00 60.50 ? 34  GLU A OE1 1 
ATOM   292  O  OE2 . GLU A 1 39  ? 42.140 34.497 11.531 1.00 70.14 ? 34  GLU A OE2 1 
ATOM   293  N  N   . GLU A 1 40  ? 36.632 30.963 10.861 1.00 41.16 ? 35  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 40  ? 35.874 29.713 10.929 1.00 39.01 ? 35  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 40  ? 36.486 28.777 11.959 1.00 38.24 ? 35  GLU A C   1 
ATOM   296  O  O   . GLU A 1 40  ? 37.662 28.872 12.301 1.00 38.59 ? 35  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 40  ? 35.845 28.986 9.583  1.00 43.44 ? 35  GLU A CB  1 
ATOM   298  C  CG  . GLU A 1 40  ? 35.076 29.670 8.518  1.00 49.94 ? 35  GLU A CG  1 
ATOM   299  C  CD  . GLU A 1 40  ? 35.351 29.065 7.147  1.00 57.13 ? 35  GLU A CD  1 
ATOM   300  O  OE1 . GLU A 1 40  ? 36.254 28.190 7.035  1.00 56.78 ? 35  GLU A OE1 1 
ATOM   301  O  OE2 . GLU A 1 40  ? 34.667 29.477 6.187  1.00 64.93 ? 35  GLU A OE2 1 
ATOM   302  N  N   . LEU A 1 41  ? 35.679 27.840 12.444 1.00 39.31 ? 36  LEU A N   1 
ATOM   303  C  CA  . LEU A 1 41  ? 36.176 26.814 13.348 1.00 35.62 ? 36  LEU A CA  1 
ATOM   304  C  C   . LEU A 1 41  ? 36.283 25.508 12.581 1.00 37.19 ? 36  LEU A C   1 
ATOM   305  O  O   . LEU A 1 41  ? 35.362 25.152 11.836 1.00 39.16 ? 36  LEU A O   1 
ATOM   306  C  CB  . LEU A 1 41  ? 35.258 26.629 14.561 1.00 34.80 ? 36  LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 41  ? 35.454 27.541 15.757 1.00 39.31 ? 36  LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 41  ? 35.214 28.966 15.364 1.00 42.38 ? 36  LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 41  ? 34.518 27.110 16.883 1.00 37.30 ? 36  LEU A CD2 1 
ATOM   310  N  N   . SER A 1 42  ? 37.420 24.831 12.724 1.00 37.88 ? 37  SER A N   1 
ATOM   311  C  CA  . SER A 1 42  ? 37.587 23.489 12.177 1.00 40.75 ? 37  SER A CA  1 
ATOM   312  C  C   . SER A 1 42  ? 36.666 22.497 12.893 1.00 39.30 ? 37  SER A C   1 
ATOM   313  O  O   . SER A 1 42  ? 36.062 22.797 13.924 1.00 35.43 ? 37  SER A O   1 
ATOM   314  C  CB  . SER A 1 42  ? 39.031 23.027 12.341 1.00 38.15 ? 37  SER A CB  1 
ATOM   315  O  OG  . SER A 1 42  ? 39.343 22.882 13.732 1.00 37.49 ? 37  SER A OG  1 
ATOM   316  N  N   . CYS A 1 43  ? 36.590 21.277 12.345 1.00 35.80 ? 38  CYS A N   1 
ATOM   317  C  CA  . CYS A 1 43  ? 35.847 20.201 13.014 1.00 36.96 ? 38  CYS A CA  1 
ATOM   318  C  C   . CYS A 1 43  ? 36.316 19.991 14.449 1.00 36.66 ? 38  CYS A C   1 
ATOM   319  O  O   . CYS A 1 43  ? 35.496 19.886 15.369 1.00 34.74 ? 38  CYS A O   1 
ATOM   320  C  CB  . CYS A 1 43  ? 35.982 18.901 12.219 1.00 34.64 ? 38  CYS A CB  1 
ATOM   321  S  SG  . CYS A 1 43  ? 35.209 17.444 12.997 1.00 39.94 ? 38  CYS A SG  1 
ATOM   322  N  N   . GLU A 1 44  ? 37.638 19.910 14.659 1.00 35.91 ? 39  GLU A N   1 
ATOM   323  C  CA  . GLU A 1 44  ? 38.176 19.727 16.010 1.00 37.01 ? 39  GLU A CA  1 
ATOM   324  C  C   . GLU A 1 44  ? 37.755 20.867 16.928 1.00 35.60 ? 39  GLU A C   1 
ATOM   325  O  O   . GLU A 1 44  ? 37.463 20.655 18.114 1.00 31.40 ? 39  GLU A O   1 
ATOM   326  C  CB  . GLU A 1 44  ? 39.701 19.666 15.950 1.00 41.42 ? 39  GLU A CB  1 
ATOM   327  C  CG  . GLU A 1 44  ? 40.354 19.106 17.208 1.00 48.41 ? 39  GLU A CG  1 
ATOM   328  C  CD  . GLU A 1 44  ? 41.875 19.244 17.173 1.00 53.41 ? 39  GLU A CD  1 
ATOM   329  O  OE1 . GLU A 1 44  ? 42.523 19.112 18.241 1.00 59.67 ? 39  GLU A OE1 1 
ATOM   330  O  OE2 . GLU A 1 44  ? 42.413 19.522 16.073 1.00 56.92 ? 39  GLU A OE2 1 
ATOM   331  N  N   . GLU A 1 45  ? 37.753 22.099 16.403 1.00 37.80 ? 40  GLU A N   1 
ATOM   332  C  CA  . GLU A 1 45  ? 37.392 23.235 17.250 1.00 34.38 ? 40  GLU A CA  1 
ATOM   333  C  C   . GLU A 1 45  ? 35.891 23.282 17.504 1.00 33.49 ? 40  GLU A C   1 
ATOM   334  O  O   . GLU A 1 45  ? 35.459 23.639 18.608 1.00 34.97 ? 40  GLU A O   1 
ATOM   335  C  CB  . GLU A 1 45  ? 37.885 24.535 16.599 1.00 34.15 ? 40  GLU A CB  1 
ATOM   336  C  CG  . GLU A 1 45  ? 39.414 24.510 16.439 1.00 38.63 ? 40  GLU A CG  1 
ATOM   337  C  CD  . GLU A 1 45  ? 39.973 25.632 15.555 1.00 38.44 ? 40  GLU A CD  1 
ATOM   338  O  OE1 . GLU A 1 45  ? 39.226 26.158 14.692 1.00 38.38 ? 40  GLU A OE1 1 
ATOM   339  O  OE2 . GLU A 1 45  ? 41.169 25.970 15.737 1.00 38.04 ? 40  GLU A OE2 1 
ATOM   340  N  N   . ARG A 1 46  ? 35.081 22.898 16.519 1.00 31.73 ? 41  ARG A N   1 
ATOM   341  C  CA  . ARG A 1 46  ? 33.652 22.797 16.780 1.00 33.78 ? 41  ARG A CA  1 
ATOM   342  C  C   . ARG A 1 46  ? 33.390 21.801 17.902 1.00 31.84 ? 41  ARG A C   1 
ATOM   343  O  O   . ARG A 1 46  ? 32.512 22.025 18.745 1.00 31.27 ? 41  ARG A O   1 
ATOM   344  C  CB  . ARG A 1 46  ? 32.896 22.387 15.513 1.00 35.04 ? 41  ARG A CB  1 
ATOM   345  C  CG  . ARG A 1 46  ? 32.902 23.482 14.504 1.00 37.20 ? 41  ARG A CG  1 
ATOM   346  C  CD  . ARG A 1 46  ? 32.044 23.157 13.313 1.00 39.07 ? 41  ARG A CD  1 
ATOM   347  N  NE  . ARG A 1 46  ? 32.528 22.021 12.545 1.00 39.94 ? 41  ARG A NE  1 
ATOM   348  C  CZ  . ARG A 1 46  ? 33.177 22.111 11.386 1.00 42.14 ? 41  ARG A CZ  1 
ATOM   349  N  NH1 . ARG A 1 46  ? 33.625 23.268 10.931 1.00 42.35 ? 41  ARG A NH1 1 
ATOM   350  N  NH2 . ARG A 1 46  ? 33.382 21.009 10.669 1.00 39.15 ? 41  ARG A NH2 1 
ATOM   351  N  N   . ASN A 1 47  ? 34.169 20.714 17.944 1.00 32.85 ? 42  ASN A N   1 
ATOM   352  C  CA  . ASN A 1 47  ? 33.992 19.734 19.012 1.00 33.91 ? 42  ASN A CA  1 
ATOM   353  C  C   . ASN A 1 47  ? 34.324 20.338 20.369 1.00 33.84 ? 42  ASN A C   1 
ATOM   354  O  O   . ASN A 1 47  ? 33.632 20.071 21.354 1.00 32.61 ? 42  ASN A O   1 
ATOM   355  C  CB  . ASN A 1 47  ? 34.851 18.495 18.766 1.00 35.58 ? 42  ASN A CB  1 
ATOM   356  C  CG  . ASN A 1 47  ? 34.628 17.443 19.822 1.00 38.70 ? 42  ASN A CG  1 
ATOM   357  O  OD1 . ASN A 1 47  ? 33.524 16.920 19.961 1.00 40.44 ? 42  ASN A OD1 1 
ATOM   358  N  ND2 . ASN A 1 47  ? 35.648 17.185 20.621 1.00 39.72 ? 42  ASN A ND2 1 
ATOM   359  N  N   . LEU A 1 48  ? 35.373 21.174 20.432 1.00 31.93 ? 43  LEU A N   1 
ATOM   360  C  CA  . LEU A 1 48  ? 35.732 21.818 21.693 1.00 36.34 ? 43  LEU A CA  1 
ATOM   361  C  C   . LEU A 1 48  ? 34.607 22.732 22.159 1.00 32.21 ? 43  LEU A C   1 
ATOM   362  O  O   . LEU A 1 48  ? 34.204 22.702 23.330 1.00 32.90 ? 43  LEU A O   1 
ATOM   363  C  CB  . LEU A 1 48  ? 37.041 22.614 21.532 1.00 30.54 ? 43  LEU A CB  1 
ATOM   364  C  CG  . LEU A 1 48  ? 38.364 21.868 21.300 1.00 33.26 ? 43  LEU A CG  1 
ATOM   365  C  CD1 . LEU A 1 48  ? 39.530 22.829 20.883 1.00 37.35 ? 43  LEU A CD1 1 
ATOM   366  C  CD2 . LEU A 1 48  ? 38.736 21.036 22.543 1.00 36.26 ? 43  LEU A CD2 1 
ATOM   367  N  N   . LEU A 1 49  ? 34.081 23.551 21.239 1.00 31.02 ? 44  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 49  ? 32.967 24.438 21.563 1.00 30.72 ? 44  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 49  ? 31.773 23.649 22.083 1.00 31.73 ? 44  LEU A C   1 
ATOM   370  O  O   . LEU A 1 49  ? 31.179 23.982 23.118 1.00 32.25 ? 44  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 49  ? 32.582 25.229 20.304 1.00 32.32 ? 44  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 49  ? 31.401 26.192 20.385 1.00 31.22 ? 44  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 49  ? 31.788 27.450 21.235 1.00 32.73 ? 44  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 49  ? 30.966 26.575 18.953 1.00 30.30 ? 44  LEU A CD2 1 
ATOM   375  N  N   . SER A 1 50  ? 31.417 22.592 21.351 1.00 31.21 ? 45  SER A N   1 
ATOM   376  C  CA  . SER A 1 50  ? 30.305 21.723 21.711 1.00 31.48 ? 45  SER A CA  1 
ATOM   377  C  C   . SER A 1 50  ? 30.502 21.100 23.081 1.00 31.53 ? 45  SER A C   1 
ATOM   378  O  O   . SER A 1 50  ? 29.606 21.159 23.931 1.00 32.25 ? 45  SER A O   1 
ATOM   379  C  CB  . SER A 1 50  ? 30.180 20.618 20.646 1.00 34.06 ? 45  SER A CB  1 
ATOM   380  O  OG  . SER A 1 50  ? 29.073 19.778 20.937 1.00 33.69 ? 45  SER A OG  1 
ATOM   381  N  N   . VAL A 1 51  ? 31.653 20.451 23.298 1.00 31.73 ? 46  VAL A N   1 
ATOM   382  C  CA  . VAL A 1 51  ? 31.886 19.771 24.576 1.00 32.04 ? 46  VAL A CA  1 
ATOM   383  C  C   . VAL A 1 51  ? 31.796 20.754 25.733 1.00 35.58 ? 46  VAL A C   1 
ATOM   384  O  O   . VAL A 1 51  ? 31.210 20.459 26.785 1.00 33.18 ? 46  VAL A O   1 
ATOM   385  C  CB  . VAL A 1 51  ? 33.248 19.043 24.564 1.00 35.76 ? 46  VAL A CB  1 
ATOM   386  C  CG1 . VAL A 1 51  ? 33.654 18.589 25.978 1.00 36.82 ? 46  VAL A CG1 1 
ATOM   387  C  CG2 . VAL A 1 51  ? 33.212 17.844 23.597 1.00 34.40 ? 46  VAL A CG2 1 
ATOM   388  N  N   . ALA A 1 52  ? 32.373 21.947 25.562 1.00 30.79 ? 47  ALA A N   1 
ATOM   389  C  CA  . ALA A 1 52  ? 32.395 22.895 26.664 1.00 33.66 ? 47  ALA A CA  1 
ATOM   390  C  C   . ALA A 1 52  ? 30.988 23.309 27.045 1.00 32.51 ? 47  ALA A C   1 
ATOM   391  O  O   . ALA A 1 52  ? 30.584 23.195 28.206 1.00 33.22 ? 47  ALA A O   1 
ATOM   392  C  CB  . ALA A 1 52  ? 33.221 24.118 26.271 1.00 33.30 ? 47  ALA A CB  1 
ATOM   393  N  N   . TYR A 1 53  ? 30.245 23.850 26.082 1.00 32.87 ? 48  TYR A N   1 
ATOM   394  C  CA  . TYR A 1 53  ? 28.927 24.361 26.409 1.00 33.81 ? 48  TYR A CA  1 
ATOM   395  C  C   . TYR A 1 53  ? 27.960 23.255 26.783 1.00 33.28 ? 48  TYR A C   1 
ATOM   396  O  O   . TYR A 1 53  ? 27.100 23.477 27.633 1.00 33.26 ? 48  TYR A O   1 
ATOM   397  C  CB  . TYR A 1 53  ? 28.369 25.190 25.261 1.00 30.77 ? 48  TYR A CB  1 
ATOM   398  C  CG  . TYR A 1 53  ? 28.874 26.615 25.333 1.00 32.42 ? 48  TYR A CG  1 
ATOM   399  C  CD1 . TYR A 1 53  ? 28.475 27.438 26.372 1.00 34.31 ? 48  TYR A CD1 1 
ATOM   400  C  CD2 . TYR A 1 53  ? 29.795 27.107 24.392 1.00 34.00 ? 48  TYR A CD2 1 
ATOM   401  C  CE1 . TYR A 1 53  ? 28.944 28.738 26.462 1.00 35.59 ? 48  TYR A CE1 1 
ATOM   402  C  CE2 . TYR A 1 53  ? 30.287 28.408 24.494 1.00 34.29 ? 48  TYR A CE2 1 
ATOM   403  C  CZ  . TYR A 1 53  ? 29.841 29.205 25.524 1.00 37.84 ? 48  TYR A CZ  1 
ATOM   404  O  OH  . TYR A 1 53  ? 30.313 30.497 25.646 1.00 36.19 ? 48  TYR A OH  1 
ATOM   405  N  N   . LYS A 1 54  ? 28.086 22.063 26.186 1.00 36.12 ? 49  LYS A N   1 
ATOM   406  C  CA  . LYS A 1 54  ? 27.164 20.993 26.562 1.00 34.29 ? 49  LYS A CA  1 
ATOM   407  C  C   . LYS A 1 54  ? 27.351 20.584 28.010 1.00 34.75 ? 49  LYS A C   1 
ATOM   408  O  O   . LYS A 1 54  ? 26.379 20.249 28.691 1.00 34.91 ? 49  LYS A O   1 
ATOM   409  C  CB  . LYS A 1 54  ? 27.330 19.773 25.662 1.00 35.53 ? 49  LYS A CB  1 
ATOM   410  C  CG  . LYS A 1 54  ? 26.185 18.771 25.835 1.00 44.79 ? 49  LYS A CG  1 
ATOM   411  C  CD  . LYS A 1 54  ? 25.918 17.980 24.541 1.00 42.84 ? 49  LYS A CD  1 
ATOM   412  C  CE  . LYS A 1 54  ? 25.068 16.737 24.854 1.00 47.90 ? 49  LYS A CE  1 
ATOM   413  N  NZ  . LYS A 1 54  ? 23.873 17.106 25.739 1.00 47.05 ? 49  LYS A NZ  1 
ATOM   414  N  N   . ASN A 1 55  ? 28.600 20.571 28.479 1.00 33.24 ? 50  ASN A N   1 
ATOM   415  C  CA  . ASN A 1 55  ? 28.898 20.247 29.872 1.00 34.69 ? 50  ASN A CA  1 
ATOM   416  C  C   . ASN A 1 55  ? 28.302 21.291 30.803 1.00 36.02 ? 50  ASN A C   1 
ATOM   417  O  O   . ASN A 1 55  ? 27.715 20.970 31.843 1.00 32.24 ? 50  ASN A O   1 
ATOM   418  C  CB  . ASN A 1 55  ? 30.416 20.188 30.039 1.00 36.84 ? 50  ASN A CB  1 
ATOM   419  C  CG  . ASN A 1 55  ? 30.957 18.779 30.013 1.00 42.99 ? 50  ASN A CG  1 
ATOM   420  O  OD1 . ASN A 1 55  ? 30.767 18.007 30.956 1.00 42.33 ? 50  ASN A OD1 1 
ATOM   421  N  ND2 . ASN A 1 55  ? 31.615 18.426 28.917 1.00 40.89 ? 50  ASN A ND2 1 
ATOM   422  N  N   . VAL A 1 56  ? 28.476 22.561 30.457 1.00 31.56 ? 51  VAL A N   1 
ATOM   423  C  CA  . VAL A 1 56  ? 27.947 23.633 31.278 1.00 35.00 ? 51  VAL A CA  1 
ATOM   424  C  C   . VAL A 1 56  ? 26.431 23.535 31.362 1.00 34.79 ? 51  VAL A C   1 
ATOM   425  O  O   . VAL A 1 56  ? 25.855 23.464 32.455 1.00 34.47 ? 51  VAL A O   1 
ATOM   426  C  CB  . VAL A 1 56  ? 28.394 24.993 30.714 1.00 35.03 ? 51  VAL A CB  1 
ATOM   427  C  CG1 . VAL A 1 56  ? 27.673 26.112 31.453 1.00 35.13 ? 51  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A 1 56  ? 29.923 25.101 30.822 1.00 34.07 ? 51  VAL A CG2 1 
ATOM   429  N  N   . VAL A 1 57  ? 25.768 23.536 30.202 1.00 34.09 ? 52  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 57  ? 24.313 23.564 30.197 1.00 32.93 ? 52  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 57  ? 23.766 22.237 30.713 1.00 36.21 ? 52  VAL A C   1 
ATOM   432  O  O   . VAL A 1 57  ? 22.704 22.211 31.338 1.00 35.85 ? 52  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 57  ? 23.779 23.938 28.788 1.00 33.43 ? 52  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 57  ? 23.884 22.797 27.817 1.00 38.39 ? 52  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 57  ? 22.341 24.400 28.874 1.00 40.26 ? 52  VAL A CG2 1 
ATOM   436  N  N   . GLY A 1 58  ? 24.494 21.132 30.494 1.00 33.29 ? 53  GLY A N   1 
ATOM   437  C  CA  . GLY A 1 58  ? 24.058 19.845 31.034 1.00 36.61 ? 53  GLY A CA  1 
ATOM   438  C  C   . GLY A 1 58  ? 23.966 19.840 32.548 1.00 36.87 ? 53  GLY A C   1 
ATOM   439  O  O   . GLY A 1 58  ? 23.006 19.314 33.126 1.00 36.81 ? 53  GLY A O   1 
ATOM   440  N  N   . GLY A 1 59  ? 24.960 20.431 33.216 1.00 36.83 ? 54  GLY A N   1 
ATOM   441  C  CA  . GLY A 1 59  ? 24.902 20.519 34.661 1.00 37.17 ? 54  GLY A CA  1 
ATOM   442  C  C   . GLY A 1 59  ? 23.756 21.395 35.137 1.00 38.56 ? 54  GLY A C   1 
ATOM   443  O  O   . GLY A 1 59  ? 23.129 21.113 36.156 1.00 36.46 ? 54  GLY A O   1 
ATOM   444  N  N   . GLN A 1 60  ? 23.464 22.468 34.401 1.00 37.59 ? 55  GLN A N   1 
ATOM   445  C  CA  . GLN A 1 60  ? 22.329 23.318 34.772 1.00 35.51 ? 55  GLN A CA  1 
ATOM   446  C  C   . GLN A 1 60  ? 21.004 22.617 34.530 1.00 37.28 ? 55  GLN A C   1 
ATOM   447  O  O   . GLN A 1 60  ? 20.091 22.722 35.352 1.00 35.13 ? 55  GLN A O   1 
ATOM   448  C  CB  . GLN A 1 60  ? 22.385 24.623 33.994 1.00 36.12 ? 55  GLN A CB  1 
ATOM   449  C  CG  . GLN A 1 60  ? 23.682 25.368 34.162 1.00 34.87 ? 55  GLN A CG  1 
ATOM   450  C  CD  . GLN A 1 60  ? 23.727 26.558 33.220 1.00 36.84 ? 55  GLN A CD  1 
ATOM   451  O  OE1 . GLN A 1 60  ? 23.491 26.396 32.000 1.00 37.49 ? 55  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A 1 60  ? 24.022 27.742 33.749 1.00 39.49 ? 55  GLN A NE2 1 
ATOM   453  N  N   . ARG A 1 61  ? 20.878 21.885 33.407 1.00 34.18 ? 56  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 61  ? 19.643 21.143 33.168 1.00 35.87 ? 56  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 61  ? 19.420 20.088 34.247 1.00 37.42 ? 56  ARG A C   1 
ATOM   456  O  O   . ARG A 1 61  ? 18.297 19.912 34.740 1.00 35.22 ? 56  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 61  ? 19.677 20.480 31.777 1.00 38.70 ? 56  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 61  ? 19.740 21.448 30.610 1.00 36.88 ? 56  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 61  ? 20.147 20.709 29.296 1.00 39.96 ? 56  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 61  ? 19.129 19.755 28.848 1.00 40.00 ? 56  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 61  ? 19.382 18.679 28.101 1.00 44.79 ? 56  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 61  ? 20.618 18.330 27.775 1.00 40.20 ? 56  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 61  ? 18.370 17.936 27.664 1.00 38.70 ? 56  ARG A NH2 1 
ATOM   464  N  N   . ALA A 1 62  ? 20.477 19.346 34.604 1.00 38.07 ? 57  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 62  ? 20.355 18.358 35.667 1.00 39.41 ? 57  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 62  ? 19.924 19.006 36.979 1.00 37.15 ? 57  ALA A C   1 
ATOM   467  O  O   . ALA A 1 62  ? 19.050 18.479 37.678 1.00 35.15 ? 57  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 62  ? 21.674 17.603 35.850 1.00 38.85 ? 57  ALA A CB  1 
ATOM   469  N  N   . ALA A 1 63  ? 20.510 20.159 37.317 1.00 34.74 ? 58  ALA A N   1 
ATOM   470  C  CA  . ALA A 1 63  ? 20.123 20.857 38.541 1.00 36.76 ? 58  ALA A CA  1 
ATOM   471  C  C   . ALA A 1 63  ? 18.673 21.310 38.468 1.00 35.42 ? 58  ALA A C   1 
ATOM   472  O  O   . ALA A 1 63  ? 17.901 21.138 39.417 1.00 33.23 ? 58  ALA A O   1 
ATOM   473  C  CB  . ALA A 1 63  ? 21.053 22.054 38.784 1.00 34.18 ? 58  ALA A CB  1 
ATOM   474  N  N   . TRP A 1 64  ? 18.293 21.917 37.342 1.00 36.01 ? 59  TRP A N   1 
ATOM   475  C  CA  . TRP A 1 64  ? 16.927 22.390 37.165 1.00 34.33 ? 59  TRP A CA  1 
ATOM   476  C  C   . TRP A 1 64  ? 15.926 21.251 37.312 1.00 38.21 ? 59  TRP A C   1 
ATOM   477  O  O   . TRP A 1 64  ? 14.859 21.435 37.897 1.00 35.84 ? 59  TRP A O   1 
ATOM   478  C  CB  . TRP A 1 64  ? 16.796 23.042 35.788 1.00 35.07 ? 59  TRP A CB  1 
ATOM   479  C  CG  . TRP A 1 64  ? 15.491 23.709 35.542 1.00 40.31 ? 59  TRP A CG  1 
ATOM   480  C  CD1 . TRP A 1 64  ? 15.198 25.044 35.725 1.00 39.88 ? 59  TRP A CD1 1 
ATOM   481  C  CD2 . TRP A 1 64  ? 14.287 23.096 35.064 1.00 39.02 ? 59  TRP A CD2 1 
ATOM   482  N  NE1 . TRP A 1 64  ? 13.878 25.288 35.400 1.00 39.16 ? 59  TRP A NE1 1 
ATOM   483  C  CE2 . TRP A 1 64  ? 13.296 24.112 34.999 1.00 42.69 ? 59  TRP A CE2 1 
ATOM   484  C  CE3 . TRP A 1 64  ? 13.941 21.785 34.702 1.00 39.60 ? 59  TRP A CE3 1 
ATOM   485  C  CZ2 . TRP A 1 64  ? 11.991 23.858 34.577 1.00 44.15 ? 59  TRP A CZ2 1 
ATOM   486  C  CZ3 . TRP A 1 64  ? 12.643 21.536 34.283 1.00 45.40 ? 59  TRP A CZ3 1 
ATOM   487  C  CH2 . TRP A 1 64  ? 11.684 22.571 34.213 1.00 44.93 ? 59  TRP A CH2 1 
ATOM   488  N  N   . ARG A 1 65  ? 16.241 20.067 36.757 1.00 38.03 ? 60  ARG A N   1 
ATOM   489  C  CA  . ARG A 1 65  ? 15.312 18.946 36.870 1.00 39.01 ? 60  ARG A CA  1 
ATOM   490  C  C   . ARG A 1 65  ? 15.152 18.493 38.312 1.00 38.39 ? 60  ARG A C   1 
ATOM   491  O  O   . ARG A 1 65  ? 14.037 18.156 38.728 1.00 40.85 ? 60  ARG A O   1 
ATOM   492  C  CB  . ARG A 1 65  ? 15.760 17.785 35.983 1.00 39.79 ? 60  ARG A CB  1 
ATOM   493  C  CG  . ARG A 1 65  ? 15.626 18.150 34.516 1.00 39.07 ? 60  ARG A CG  1 
ATOM   494  C  CD  . ARG A 1 65  ? 15.731 16.940 33.630 1.00 48.53 ? 60  ARG A CD  1 
ATOM   495  N  NE  . ARG A 1 65  ? 17.091 16.425 33.703 1.00 54.11 ? 60  ARG A NE  1 
ATOM   496  C  CZ  . ARG A 1 65  ? 17.918 16.354 32.666 1.00 58.17 ? 60  ARG A CZ  1 
ATOM   497  N  NH1 . ARG A 1 65  ? 17.526 16.690 31.441 1.00 55.08 ? 60  ARG A NH1 1 
ATOM   498  N  NH2 . ARG A 1 65  ? 19.170 15.936 32.867 1.00 58.90 ? 60  ARG A NH2 1 
ATOM   499  N  N   . VAL A 1 66  ? 16.246 18.474 39.090 1.00 37.66 ? 61  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 66  ? 16.146 18.136 40.516 1.00 37.77 ? 61  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 66  ? 15.240 19.125 41.229 1.00 39.59 ? 61  VAL A C   1 
ATOM   502  O  O   . VAL A 1 66  ? 14.339 18.740 41.991 1.00 39.16 ? 61  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 66  ? 17.541 18.096 41.172 1.00 34.68 ? 61  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 66  ? 17.444 18.115 42.695 1.00 37.30 ? 61  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 66  ? 18.329 16.877 40.700 1.00 38.19 ? 61  VAL A CG2 1 
ATOM   506  N  N   . LEU A 1 67  ? 15.493 20.422 41.021 1.00 36.99 ? 62  LEU A N   1 
ATOM   507  C  CA  . LEU A 1 67  ? 14.749 21.441 41.742 1.00 35.45 ? 62  LEU A CA  1 
ATOM   508  C  C   . LEU A 1 67  ? 13.296 21.454 41.307 1.00 39.61 ? 62  LEU A C   1 
ATOM   509  O  O   . LEU A 1 67  ? 12.394 21.624 42.138 1.00 42.10 ? 62  LEU A O   1 
ATOM   510  C  CB  . LEU A 1 67  ? 15.394 22.811 41.525 1.00 37.60 ? 62  LEU A CB  1 
ATOM   511  C  CG  . LEU A 1 67  ? 16.834 22.879 42.037 1.00 36.32 ? 62  LEU A CG  1 
ATOM   512  C  CD1 . LEU A 1 67  ? 17.474 24.225 41.674 1.00 35.79 ? 62  LEU A CD1 1 
ATOM   513  C  CD2 . LEU A 1 67  ? 16.854 22.725 43.555 1.00 34.94 ? 62  LEU A CD2 1 
ATOM   514  N  N   . SER A 1 68  ? 13.053 21.238 40.009 1.00 41.69 ? 63  SER A N   1 
ATOM   515  C  CA  . SER A 1 68  ? 11.690 21.236 39.495 1.00 45.08 ? 63  SER A CA  1 
ATOM   516  C  C   . SER A 1 68  ? 10.896 20.069 40.065 1.00 46.84 ? 63  SER A C   1 
ATOM   517  O  O   . SER A 1 68  ? 9.705  20.205 40.374 1.00 49.39 ? 63  SER A O   1 
ATOM   518  C  CB  . SER A 1 68  ? 11.717 21.188 37.966 1.00 43.51 ? 63  SER A CB  1 
ATOM   519  O  OG  . SER A 1 68  ? 10.428 21.381 37.444 1.00 52.46 ? 63  SER A OG  1 
ATOM   520  N  N   . SER A 1 69  ? 11.543 18.923 40.231 1.00 41.36 ? 64  SER A N   1 
ATOM   521  C  CA  . SER A 1 69  ? 10.862 17.782 40.815 1.00 47.35 ? 64  SER A CA  1 
ATOM   522  C  C   . SER A 1 69  ? 10.555 18.019 42.291 1.00 52.13 ? 64  SER A C   1 
ATOM   523  O  O   . SER A 1 69  ? 9.475  17.649 42.774 1.00 54.40 ? 64  SER A O   1 
ATOM   524  C  CB  . SER A 1 69  ? 11.709 16.525 40.633 1.00 46.82 ? 64  SER A CB  1 
ATOM   525  O  OG  . SER A 1 69  ? 11.109 15.432 41.281 1.00 56.49 ? 64  SER A OG  1 
ATOM   526  N  N   . ILE A 1 70  ? 11.494 18.620 43.029 1.00 46.19 ? 65  ILE A N   1 
ATOM   527  C  CA  . ILE A 1 70  ? 11.217 18.990 44.419 1.00 49.18 ? 65  ILE A CA  1 
ATOM   528  C  C   . ILE A 1 70  ? 10.062 19.978 44.475 1.00 53.29 ? 65  ILE A C   1 
ATOM   529  O  O   . ILE A 1 70  ? 9.193  19.902 45.355 1.00 55.22 ? 65  ILE A O   1 
ATOM   530  C  CB  . ILE A 1 70  ? 12.484 19.560 45.083 1.00 42.69 ? 65  ILE A CB  1 
ATOM   531  C  CG1 . ILE A 1 70  ? 13.564 18.479 45.143 1.00 44.56 ? 65  ILE A CG1 1 
ATOM   532  C  CG2 . ILE A 1 70  ? 12.166 20.146 46.491 1.00 44.93 ? 65  ILE A CG2 1 
ATOM   533  C  CD1 . ILE A 1 70  ? 14.937 18.976 45.552 1.00 43.78 ? 65  ILE A CD1 1 
ATOM   534  N  N   . GLU A 1 71  ? 10.036 20.912 43.522 1.00 47.89 ? 66  GLU A N   1 
ATOM   535  C  CA  . GLU A 1 71  ? 9.002  21.934 43.460 1.00 51.39 ? 66  GLU A CA  1 
ATOM   536  C  C   . GLU A 1 71  ? 7.629  21.332 43.193 1.00 59.70 ? 66  GLU A C   1 
ATOM   537  O  O   . GLU A 1 71  ? 6.655  21.647 43.888 1.00 61.34 ? 66  GLU A O   1 
ATOM   538  C  CB  . GLU A 1 71  ? 9.353  22.942 42.377 1.00 50.09 ? 66  GLU A CB  1 
ATOM   539  C  CG  . GLU A 1 71  ? 8.599  24.219 42.515 1.00 51.20 ? 66  GLU A CG  1 
ATOM   540  C  CD  . GLU A 1 71  ? 8.820  25.151 41.363 1.00 50.65 ? 66  GLU A CD  1 
ATOM   541  O  OE1 . GLU A 1 71  ? 9.672  24.863 40.494 1.00 49.71 ? 66  GLU A OE1 1 
ATOM   542  O  OE2 . GLU A 1 71  ? 8.156  26.199 41.327 1.00 50.94 ? 66  GLU A OE2 1 
ATOM   543  N  N   . GLN A 1 72  ? 7.527  20.477 42.173 1.00 57.76 ? 67  GLN A N   1 
ATOM   544  C  CA  . GLN A 1 72  ? 6.233  19.894 41.841 1.00 63.24 ? 67  GLN A CA  1 
ATOM   545  C  C   . GLN A 1 72  ? 5.723  19.019 42.979 1.00 64.48 ? 67  GLN A C   1 
ATOM   546  O  O   . GLN A 1 72  ? 4.520  18.995 43.266 1.00 68.47 ? 67  GLN A O   1 
ATOM   547  C  CB  . GLN A 1 72  ? 6.331  19.087 40.546 1.00 60.93 ? 67  GLN A CB  1 
ATOM   548  C  CG  . GLN A 1 72  ? 6.564  19.946 39.301 1.00 65.15 ? 67  GLN A CG  1 
ATOM   549  C  CD  . GLN A 1 72  ? 5.678  21.188 39.236 1.00 71.89 ? 67  GLN A CD  1 
ATOM   550  O  OE1 . GLN A 1 72  ? 6.136  22.263 38.826 1.00 68.09 ? 67  GLN A OE1 1 
ATOM   551  N  NE2 . GLN A 1 72  ? 4.399  21.043 39.609 1.00 73.34 ? 67  GLN A NE2 1 
ATOM   552  N  N   . LYS A 1 73  ? 6.629  18.314 43.656 1.00 61.31 ? 68  LYS A N   1 
ATOM   553  C  CA  . LYS A 1 73  ? 6.226  17.414 44.724 1.00 65.36 ? 68  LYS A CA  1 
ATOM   554  C  C   . LYS A 1 73  ? 5.811  18.173 45.982 1.00 70.05 ? 68  LYS A C   1 
ATOM   555  O  O   . LYS A 1 73  ? 5.058  17.634 46.802 1.00 71.55 ? 68  LYS A O   1 
ATOM   556  C  CB  . LYS A 1 73  ? 7.367  16.431 45.000 1.00 66.64 ? 68  LYS A CB  1 
ATOM   557  C  CG  . LYS A 1 73  ? 7.007  15.204 45.825 1.00 71.98 ? 68  LYS A CG  1 
ATOM   558  C  CD  . LYS A 1 73  ? 8.130  14.852 46.793 1.00 73.21 ? 68  LYS A CD  1 
ATOM   559  C  CE  . LYS A 1 73  ? 8.053  13.395 47.245 1.00 77.41 ? 68  LYS A CE  1 
ATOM   560  N  NZ  . LYS A 1 73  ? 8.082  13.270 48.733 1.00 79.32 ? 68  LYS A NZ  1 
ATOM   561  N  N   . SER A 1 74  ? 6.259  19.416 46.145 1.00 67.81 ? 69  SER A N   1 
ATOM   562  C  CA  . SER A 1 74  ? 5.745  20.269 47.210 1.00 70.78 ? 69  SER A CA  1 
ATOM   563  C  C   . SER A 1 74  ? 4.506  21.055 46.784 1.00 71.77 ? 69  SER A C   1 
ATOM   564  O  O   . SER A 1 74  ? 3.938  21.785 47.605 1.00 70.50 ? 69  SER A O   1 
ATOM   565  C  CB  . SER A 1 74  ? 6.836  21.228 47.713 1.00 65.47 ? 69  SER A CB  1 
ATOM   566  O  OG  . SER A 1 74  ? 7.168  22.210 46.743 1.00 67.08 ? 69  SER A OG  1 
ATOM   567  N  N   . ASN A 1 75  ? 4.075  20.923 45.525 1.00 73.05 ? 70  ASN A N   1 
ATOM   568  C  CA  . ASN A 1 75  ? 2.767  21.390 45.077 1.00 76.08 ? 70  ASN A CA  1 
ATOM   569  C  C   . ASN A 1 75  ? 1.686  20.315 45.209 1.00 77.19 ? 70  ASN A C   1 
ATOM   570  O  O   . ASN A 1 75  ? 0.676  20.367 44.493 1.00 77.69 ? 70  ASN A O   1 
ATOM   571  C  CB  . ASN A 1 75  ? 2.836  21.881 43.627 1.00 73.49 ? 70  ASN A CB  1 
ATOM   572  C  CG  . ASN A 1 75  ? 3.606  23.175 43.484 1.00 73.02 ? 70  ASN A CG  1 
ATOM   573  O  OD1 . ASN A 1 75  ? 3.833  23.892 44.462 1.00 73.10 ? 70  ASN A OD1 1 
ATOM   574  N  ND2 . ASN A 1 75  ? 4.004  23.489 42.253 1.00 77.20 ? 70  ASN A ND2 1 
ATOM   575  N  N   . GLU A 1 76  ? 1.881  19.350 46.106 1.00 77.85 ? 71  GLU A N   1 
ATOM   576  C  CA  . GLU A 1 76  ? 0.949  18.243 46.299 1.00 80.68 ? 71  GLU A CA  1 
ATOM   577  C  C   . GLU A 1 76  ? 0.342  18.236 47.710 1.00 80.71 ? 71  GLU A C   1 
ATOM   578  O  O   . GLU A 1 76  ? 1.009  18.559 48.697 1.00 77.31 ? 71  GLU A O   1 
ATOM   579  C  CB  . GLU A 1 76  ? 1.665  16.920 46.015 1.00 77.19 ? 71  GLU A CB  1 
ATOM   580  C  CG  . GLU A 1 76  ? 2.062  16.751 44.555 1.00 76.52 ? 71  GLU A CG  1 
ATOM   581  C  CD  . GLU A 1 76  ? 2.884  15.486 44.297 1.00 79.60 ? 71  GLU A CD  1 
ATOM   582  O  OE1 . GLU A 1 76  ? 3.242  14.783 45.278 1.00 75.09 ? 71  GLU A OE1 1 
ATOM   583  O  OE2 . GLU A 1 76  ? 3.151  15.190 43.102 1.00 78.86 ? 71  GLU A OE2 1 
ATOM   584  N  N   . GLY A 1 83  ? 7.127  27.393 51.842 1.00 55.12 ? 78  GLY A N   1 
ATOM   585  C  CA  . GLY A 1 83  ? 7.793  28.665 51.589 1.00 52.05 ? 78  GLY A CA  1 
ATOM   586  C  C   . GLY A 1 83  ? 8.140  28.878 50.124 1.00 46.27 ? 78  GLY A C   1 
ATOM   587  O  O   . GLY A 1 83  ? 7.965  27.986 49.290 1.00 49.59 ? 78  GLY A O   1 
ATOM   588  N  N   . PRO A 1 84  ? 8.633  30.070 49.785 1.00 47.42 ? 79  PRO A N   1 
ATOM   589  C  CA  . PRO A 1 84  ? 8.985  30.349 48.392 1.00 41.93 ? 79  PRO A CA  1 
ATOM   590  C  C   . PRO A 1 84  ? 10.355 29.826 47.970 1.00 42.15 ? 79  PRO A C   1 
ATOM   591  O  O   . PRO A 1 84  ? 10.695 29.953 46.792 1.00 39.94 ? 79  PRO A O   1 
ATOM   592  C  CB  . PRO A 1 84  ? 8.944  31.882 48.343 1.00 43.99 ? 79  PRO A CB  1 
ATOM   593  C  CG  . PRO A 1 84  ? 9.426  32.274 49.724 1.00 44.26 ? 79  PRO A CG  1 
ATOM   594  C  CD  . PRO A 1 84  ? 8.861  31.233 50.661 1.00 46.38 ? 79  PRO A CD  1 
ATOM   595  N  N   . GLU A 1 85  ? 11.123 29.196 48.873 1.00 39.26 ? 80  GLU A N   1 
ATOM   596  C  CA  . GLU A 1 85  ? 12.549 28.971 48.633 1.00 39.27 ? 80  GLU A CA  1 
ATOM   597  C  C   . GLU A 1 85  ? 12.800 28.027 47.451 1.00 38.92 ? 80  GLU A C   1 
ATOM   598  O  O   . GLU A 1 85  ? 13.700 28.278 46.639 1.00 36.80 ? 80  GLU A O   1 
ATOM   599  C  CB  . GLU A 1 85  ? 13.222 28.444 49.901 1.00 39.70 ? 80  GLU A CB  1 
ATOM   600  C  CG  . GLU A 1 85  ? 13.392 29.494 51.036 1.00 41.59 ? 80  GLU A CG  1 
ATOM   601  C  CD  . GLU A 1 85  ? 12.152 29.653 51.925 1.00 44.97 ? 80  GLU A CD  1 
ATOM   602  O  OE1 . GLU A 1 85  ? 11.127 28.988 51.661 1.00 45.23 ? 80  GLU A OE1 1 
ATOM   603  O  OE2 . GLU A 1 85  ? 12.202 30.441 52.905 1.00 47.30 ? 80  GLU A OE2 1 
ATOM   604  N  N   . VAL A 1 86  ? 12.047 26.923 47.340 1.00 42.33 ? 81  VAL A N   1 
ATOM   605  C  CA  . VAL A 1 86  ? 12.282 26.014 46.210 1.00 37.55 ? 81  VAL A CA  1 
ATOM   606  C  C   . VAL A 1 86  ? 12.056 26.734 44.884 1.00 40.56 ? 81  VAL A C   1 
ATOM   607  O  O   . VAL A 1 86  ? 12.887 26.656 43.966 1.00 36.96 ? 81  VAL A O   1 
ATOM   608  C  CB  . VAL A 1 86  ? 11.412 24.747 46.307 1.00 39.88 ? 81  VAL A CB  1 
ATOM   609  C  CG1 . VAL A 1 86  ? 11.698 23.853 45.089 1.00 42.27 ? 81  VAL A CG1 1 
ATOM   610  C  CG2 . VAL A 1 86  ? 11.728 23.968 47.552 1.00 47.02 ? 81  VAL A CG2 1 
ATOM   611  N  N   . ARG A 1 87  ? 10.920 27.439 44.752 1.00 39.53 ? 82  ARG A N   1 
ATOM   612  C  CA  . ARG A 1 87  ? 10.645 28.140 43.502 1.00 39.46 ? 82  ARG A CA  1 
ATOM   613  C  C   . ARG A 1 87  ? 11.715 29.194 43.217 1.00 39.99 ? 82  ARG A C   1 
ATOM   614  O  O   . ARG A 1 87  ? 12.199 29.302 42.086 1.00 40.67 ? 82  ARG A O   1 
ATOM   615  C  CB  . ARG A 1 87  ? 9.257  28.791 43.540 1.00 42.18 ? 82  ARG A CB  1 
ATOM   616  C  CG  . ARG A 1 87  ? 8.995  29.679 42.321 1.00 46.56 ? 82  ARG A CG  1 
ATOM   617  C  CD  . ARG A 1 87  ? 7.680  30.473 42.415 1.00 52.10 ? 82  ARG A CD  1 
ATOM   618  N  NE  . ARG A 1 87  ? 7.568  31.259 43.645 1.00 47.97 ? 82  ARG A NE  1 
ATOM   619  C  CZ  . ARG A 1 87  ? 8.213  32.395 43.893 1.00 50.05 ? 82  ARG A CZ  1 
ATOM   620  N  NH1 . ARG A 1 87  ? 9.035  32.937 43.009 1.00 50.63 ? 82  ARG A NH1 1 
ATOM   621  N  NH2 . ARG A 1 87  ? 8.028  33.002 45.063 1.00 49.80 ? 82  ARG A NH2 1 
ATOM   622  N  N   . GLU A 1 88  ? 12.099 29.979 44.234 1.00 39.80 ? 83  GLU A N   1 
ATOM   623  C  CA  . GLU A 1 88  ? 13.119 31.016 44.030 1.00 40.56 ? 83  GLU A CA  1 
ATOM   624  C  C   . GLU A 1 88  ? 14.425 30.426 43.529 1.00 35.43 ? 83  GLU A C   1 
ATOM   625  O  O   . GLU A 1 88  ? 15.043 30.965 42.611 1.00 36.77 ? 83  GLU A O   1 
ATOM   626  C  CB  . GLU A 1 88  ? 13.369 31.785 45.325 1.00 40.21 ? 83  GLU A CB  1 
ATOM   627  C  CG  . GLU A 1 88  ? 12.163 32.540 45.852 1.00 41.39 ? 83  GLU A CG  1 
ATOM   628  C  CD  . GLU A 1 88  ? 12.423 33.186 47.205 1.00 46.09 ? 83  GLU A CD  1 
ATOM   629  O  OE1 . GLU A 1 88  ? 13.375 32.769 47.929 1.00 39.22 ? 83  GLU A OE1 1 
ATOM   630  O  OE2 . GLU A 1 88  ? 11.685 34.147 47.525 1.00 44.38 ? 83  GLU A OE2 1 
ATOM   631  N  N   . TYR A 1 89  ? 14.866 29.323 44.125 1.00 35.84 ? 84  TYR A N   1 
ATOM   632  C  CA  . TYR A 1 89  ? 16.139 28.749 43.713 1.00 36.74 ? 84  TYR A CA  1 
ATOM   633  C  C   . TYR A 1 89  ? 16.018 28.090 42.335 1.00 33.08 ? 84  TYR A C   1 
ATOM   634  O  O   . TYR A 1 89  ? 16.921 28.209 41.500 1.00 36.02 ? 84  TYR A O   1 
ATOM   635  C  CB  . TYR A 1 89  ? 16.629 27.775 44.800 1.00 35.94 ? 84  TYR A CB  1 
ATOM   636  C  CG  . TYR A 1 89  ? 18.001 27.237 44.509 1.00 35.76 ? 84  TYR A CG  1 
ATOM   637  C  CD1 . TYR A 1 89  ? 18.990 28.066 44.015 1.00 35.14 ? 84  TYR A CD1 1 
ATOM   638  C  CD2 . TYR A 1 89  ? 18.304 25.887 44.707 1.00 38.97 ? 84  TYR A CD2 1 
ATOM   639  C  CE1 . TYR A 1 89  ? 20.238 27.585 43.701 1.00 37.24 ? 84  TYR A CE1 1 
ATOM   640  C  CE2 . TYR A 1 89  ? 19.565 25.396 44.403 1.00 37.51 ? 84  TYR A CE2 1 
ATOM   641  C  CZ  . TYR A 1 89  ? 20.527 26.262 43.916 1.00 36.80 ? 84  TYR A CZ  1 
ATOM   642  O  OH  . TYR A 1 89  ? 21.773 25.773 43.598 1.00 40.10 ? 84  TYR A OH  1 
ATOM   643  N  N   . ARG A 1 90  ? 14.886 27.437 42.050 1.00 35.12 ? 85  ARG A N   1 
ATOM   644  C  CA  . ARG A 1 90  ? 14.687 26.894 40.704 1.00 37.18 ? 85  ARG A CA  1 
ATOM   645  C  C   . ARG A 1 90  ? 14.692 28.008 39.665 1.00 36.53 ? 85  ARG A C   1 
ATOM   646  O  O   . ARG A 1 90  ? 15.277 27.860 38.581 1.00 37.28 ? 85  ARG A O   1 
ATOM   647  C  CB  . ARG A 1 90  ? 13.383 26.084 40.644 1.00 37.97 ? 85  ARG A CB  1 
ATOM   648  C  CG  . ARG A 1 90  ? 13.128 25.341 39.310 1.00 40.46 ? 85  ARG A CG  1 
ATOM   649  C  CD  . ARG A 1 90  ? 12.330 26.180 38.312 1.00 43.44 ? 85  ARG A CD  1 
ATOM   650  N  NE  . ARG A 1 90  ? 11.011 26.521 38.831 1.00 43.43 ? 85  ARG A NE  1 
ATOM   651  C  CZ  . ARG A 1 90  ? 10.311 27.587 38.460 1.00 47.26 ? 85  ARG A CZ  1 
ATOM   652  N  NH1 . ARG A 1 90  ? 10.706 28.365 37.461 1.00 45.43 ? 85  ARG A NH1 1 
ATOM   653  N  NH2 . ARG A 1 90  ? 9.187  27.878 39.107 1.00 47.67 ? 85  ARG A NH2 1 
ATOM   654  N  N   . GLU A 1 91  ? 14.084 29.156 39.998 1.00 37.06 ? 86  GLU A N   1 
ATOM   655  C  CA  . GLU A 1 91  ? 14.086 30.297 39.087 1.00 40.13 ? 86  GLU A CA  1 
ATOM   656  C  C   . GLU A 1 91  ? 15.500 30.829 38.888 1.00 37.74 ? 86  GLU A C   1 
ATOM   657  O  O   . GLU A 1 91  ? 15.870 31.223 37.782 1.00 37.34 ? 86  GLU A O   1 
ATOM   658  C  CB  . GLU A 1 91  ? 13.165 31.406 39.620 1.00 41.31 ? 86  GLU A CB  1 
ATOM   659  C  CG  . GLU A 1 91  ? 11.696 31.302 39.184 1.00 47.97 ? 86  GLU A CG  1 
ATOM   660  C  CD  . GLU A 1 91  ? 10.765 32.230 39.992 1.00 53.91 ? 86  GLU A CD  1 
ATOM   661  O  OE1 . GLU A 1 91  ? 9.541  31.970 40.068 1.00 52.40 ? 86  GLU A OE1 1 
ATOM   662  O  OE2 . GLU A 1 91  ? 11.268 33.233 40.549 1.00 57.55 ? 86  GLU A OE2 1 
ATOM   663  N  N   . LYS A 1 92  ? 16.312 30.827 39.950 1.00 36.02 ? 87  LYS A N   1 
ATOM   664  C  CA  . LYS A 1 92  ? 17.701 31.265 39.837 1.00 36.20 ? 87  LYS A CA  1 
ATOM   665  C  C   . LYS A 1 92  ? 18.490 30.394 38.860 1.00 38.04 ? 87  LYS A C   1 
ATOM   666  O  O   . LYS A 1 92  ? 19.226 30.896 37.997 1.00 35.37 ? 87  LYS A O   1 
ATOM   667  C  CB  . LYS A 1 92  ? 18.361 31.210 41.209 1.00 38.21 ? 87  LYS A CB  1 
ATOM   668  C  CG  . LYS A 1 92  ? 19.847 31.565 41.173 1.00 43.18 ? 87  LYS A CG  1 
ATOM   669  C  CD  . LYS A 1 92  ? 20.509 31.239 42.521 1.00 46.63 ? 87  LYS A CD  1 
ATOM   670  C  CE  . LYS A 1 92  ? 22.035 31.401 42.458 1.00 49.21 ? 87  LYS A CE  1 
ATOM   671  N  NZ  . LYS A 1 92  ? 22.522 31.966 43.759 1.00 56.50 ? 87  LYS A NZ  1 
ATOM   672  N  N   . VAL A 1 93  ? 18.405 29.078 39.037 1.00 36.24 ? 88  VAL A N   1 
ATOM   673  C  CA  . VAL A 1 93  ? 19.098 28.155 38.135 1.00 36.20 ? 88  VAL A CA  1 
ATOM   674  C  C   . VAL A 1 93  ? 18.531 28.278 36.724 1.00 36.00 ? 88  VAL A C   1 
ATOM   675  O  O   . VAL A 1 93  ? 19.268 28.269 35.733 1.00 34.07 ? 88  VAL A O   1 
ATOM   676  C  CB  . VAL A 1 93  ? 18.990 26.716 38.674 1.00 35.97 ? 88  VAL A CB  1 
ATOM   677  C  CG1 . VAL A 1 93  ? 19.602 25.706 37.685 1.00 34.91 ? 88  VAL A CG1 1 
ATOM   678  C  CG2 . VAL A 1 93  ? 19.668 26.611 40.015 1.00 35.05 ? 88  VAL A CG2 1 
ATOM   679  N  N   . GLU A 1 94  ? 17.215 28.448 36.623 1.00 37.86 ? 89  GLU A N   1 
ATOM   680  C  CA  . GLU A 1 94  ? 16.568 28.634 35.330 1.00 38.11 ? 89  GLU A CA  1 
ATOM   681  C  C   . GLU A 1 94  ? 17.134 29.839 34.591 1.00 38.78 ? 89  GLU A C   1 
ATOM   682  O  O   . GLU A 1 94  ? 17.480 29.759 33.405 1.00 37.44 ? 89  GLU A O   1 
ATOM   683  C  CB  . GLU A 1 94  ? 15.066 28.788 35.542 1.00 40.97 ? 89  GLU A CB  1 
ATOM   684  C  CG  . GLU A 1 94  ? 14.257 28.956 34.260 1.00 40.41 ? 89  GLU A CG  1 
ATOM   685  C  CD  . GLU A 1 94  ? 12.783 28.707 34.506 1.00 46.16 ? 89  GLU A CD  1 
ATOM   686  O  OE1 . GLU A 1 94  ? 12.442 27.633 35.072 1.00 42.22 ? 89  GLU A OE1 1 
ATOM   687  O  OE2 . GLU A 1 94  ? 11.975 29.610 34.173 1.00 46.96 ? 89  GLU A OE2 1 
ATOM   688  N  N   . THR A 1 95  ? 17.200 30.979 35.271 1.00 37.64 ? 90  THR A N   1 
ATOM   689  C  CA  . THR A 1 95  ? 17.724 32.181 34.645 1.00 39.87 ? 90  THR A CA  1 
ATOM   690  C  C   . THR A 1 95  ? 19.152 31.985 34.153 1.00 41.80 ? 90  THR A C   1 
ATOM   691  O  O   . THR A 1 95  ? 19.531 32.497 33.088 1.00 39.86 ? 90  THR A O   1 
ATOM   692  C  CB  . THR A 1 95  ? 17.623 33.316 35.658 1.00 42.34 ? 90  THR A CB  1 
ATOM   693  O  OG1 . THR A 1 95  ? 16.234 33.488 35.952 1.00 43.39 ? 90  THR A OG1 1 
ATOM   694  C  CG2 . THR A 1 95  ? 18.211 34.573 35.116 1.00 40.98 ? 90  THR A CG2 1 
ATOM   695  N  N   . GLU A 1 96  ? 19.960 31.234 34.911 1.00 37.91 ? 91  GLU A N   1 
ATOM   696  C  CA  . GLU A 1 96  ? 21.352 31.034 34.526 1.00 38.32 ? 91  GLU A CA  1 
ATOM   697  C  C   . GLU A 1 96  ? 21.424 30.137 33.298 1.00 35.72 ? 91  GLU A C   1 
ATOM   698  O  O   . GLU A 1 96  ? 22.238 30.361 32.398 1.00 35.15 ? 91  GLU A O   1 
ATOM   699  C  CB  . GLU A 1 96  ? 22.100 30.395 35.697 1.00 36.93 ? 91  GLU A CB  1 
ATOM   700  C  CG  . GLU A 1 96  ? 23.020 31.369 36.434 1.00 49.09 ? 91  GLU A CG  1 
ATOM   701  C  CD  . GLU A 1 96  ? 23.548 30.811 37.763 1.00 50.85 ? 91  GLU A CD  1 
ATOM   702  O  OE1 . GLU A 1 96  ? 23.302 31.447 38.842 1.00 53.13 ? 91  GLU A OE1 1 
ATOM   703  O  OE2 . GLU A 1 96  ? 24.202 29.753 37.729 1.00 41.11 ? 91  GLU A OE2 1 
ATOM   704  N  N   . LEU A 1 97  ? 20.598 29.089 33.283 1.00 36.35 ? 92  LEU A N   1 
ATOM   705  C  CA  . LEU A 1 97  ? 20.538 28.188 32.132 1.00 37.62 ? 92  LEU A CA  1 
ATOM   706  C  C   . LEU A 1 97  ? 20.122 28.950 30.892 1.00 38.89 ? 92  LEU A C   1 
ATOM   707  O  O   . LEU A 1 97  ? 20.730 28.814 29.820 1.00 36.55 ? 92  LEU A O   1 
ATOM   708  C  CB  . LEU A 1 97  ? 19.547 27.053 32.420 1.00 35.90 ? 92  LEU A CB  1 
ATOM   709  C  CG  . LEU A 1 97  ? 19.306 25.974 31.359 1.00 38.49 ? 92  LEU A CG  1 
ATOM   710  C  CD1 . LEU A 1 97  ? 18.802 24.707 32.086 1.00 39.39 ? 92  LEU A CD1 1 
ATOM   711  C  CD2 . LEU A 1 97  ? 18.278 26.388 30.345 1.00 39.85 ? 92  LEU A CD2 1 
ATOM   712  N  N   . GLN A 1 98  ? 19.089 29.788 31.031 1.00 39.68 ? 93  GLN A N   1 
ATOM   713  C  CA  . GLN A 1 98  ? 18.650 30.588 29.891 1.00 42.36 ? 93  GLN A CA  1 
ATOM   714  C  C   . GLN A 1 98  ? 19.769 31.499 29.402 1.00 40.83 ? 93  GLN A C   1 
ATOM   715  O  O   . GLN A 1 98  ? 19.970 31.664 28.186 1.00 39.25 ? 93  GLN A O   1 
ATOM   716  C  CB  . GLN A 1 98  ? 17.413 31.390 30.287 1.00 41.22 ? 93  GLN A CB  1 
ATOM   717  C  CG  . GLN A 1 98  ? 16.130 30.560 30.348 1.00 39.78 ? 93  GLN A CG  1 
ATOM   718  C  CD  . GLN A 1 98  ? 15.024 31.259 31.139 1.00 44.03 ? 93  GLN A CD  1 
ATOM   719  O  OE1 . GLN A 1 98  ? 15.298 32.129 31.980 1.00 42.75 ? 93  GLN A OE1 1 
ATOM   720  N  NE2 . GLN A 1 98  ? 13.776 30.915 30.847 1.00 43.60 ? 93  GLN A NE2 1 
ATOM   721  N  N   . GLY A 1 99  ? 20.532 32.070 30.338 1.00 42.76 ? 94  GLY A N   1 
ATOM   722  C  CA  . GLY A 1 99  ? 21.616 32.965 29.961 1.00 42.60 ? 94  GLY A CA  1 
ATOM   723  C  C   . GLY A 1 99  ? 22.689 32.266 29.148 1.00 40.01 ? 94  GLY A C   1 
ATOM   724  O  O   . GLY A 1 99  ? 23.267 32.852 28.220 1.00 38.87 ? 94  GLY A O   1 
ATOM   725  N  N   . VAL A 1 100 ? 22.966 30.998 29.485 1.00 36.36 ? 95  VAL A N   1 
ATOM   726  C  CA  . VAL A 1 100 ? 23.960 30.238 28.743 1.00 36.29 ? 95  VAL A CA  1 
ATOM   727  C  C   . VAL A 1 100 ? 23.428 29.902 27.356 1.00 33.88 ? 95  VAL A C   1 
ATOM   728  O  O   . VAL A 1 100 ? 24.139 30.034 26.357 1.00 36.77 ? 95  VAL A O   1 
ATOM   729  C  CB  . VAL A 1 100 ? 24.363 28.980 29.538 1.00 34.84 ? 95  VAL A CB  1 
ATOM   730  C  CG1 . VAL A 1 100 ? 25.165 28.019 28.652 1.00 37.62 ? 95  VAL A CG1 1 
ATOM   731  C  CG2 . VAL A 1 100 ? 25.181 29.407 30.726 1.00 35.70 ? 95  VAL A CG2 1 
ATOM   732  N  N   . CYS A 1 101 ? 22.153 29.511 27.267 1.00 35.64 ? 96  CYS A N   1 
ATOM   733  C  CA  . CYS A 1 101 ? 21.581 29.217 25.959 1.00 38.27 ? 96  CYS A CA  1 
ATOM   734  C  C   . CYS A 1 101 ? 21.543 30.476 25.100 1.00 39.79 ? 96  CYS A C   1 
ATOM   735  O  O   . CYS A 1 101 ? 21.773 30.416 23.888 1.00 37.34 ? 96  CYS A O   1 
ATOM   736  C  CB  . CYS A 1 101 ? 20.177 28.625 26.094 1.00 38.22 ? 96  CYS A CB  1 
ATOM   737  S  SG  . CYS A 1 101 ? 20.044 26.987 26.903 1.00 37.03 ? 96  CYS A SG  1 
ATOM   738  N  N   . ASP A 1 102 ? 21.277 31.632 25.719 1.00 40.49 ? 97  ASP A N   1 
ATOM   739  C  CA  . ASP A 1 102 ? 21.283 32.878 24.960 1.00 42.93 ? 97  ASP A CA  1 
ATOM   740  C  C   . ASP A 1 102 ? 22.679 33.187 24.450 1.00 40.04 ? 97  ASP A C   1 
ATOM   741  O  O   . ASP A 1 102 ? 22.847 33.666 23.317 1.00 41.28 ? 97  ASP A O   1 
ATOM   742  C  CB  . ASP A 1 102 ? 20.759 34.033 25.820 1.00 44.78 ? 97  ASP A CB  1 
ATOM   743  C  CG  . ASP A 1 102 ? 19.251 33.977 26.015 1.00 47.96 ? 97  ASP A CG  1 
ATOM   744  O  OD1 . ASP A 1 102 ? 18.744 34.551 27.000 1.00 51.76 ? 97  ASP A OD1 1 
ATOM   745  O  OD2 . ASP A 1 102 ? 18.576 33.295 25.211 1.00 53.09 ? 97  ASP A OD2 1 
ATOM   746  N  N   . THR A 1 103 ? 23.693 32.917 25.271 1.00 36.98 ? 98  THR A N   1 
ATOM   747  C  CA  . THR A 1 103 ? 25.073 33.117 24.842 1.00 40.50 ? 98  THR A CA  1 
ATOM   748  C  C   . THR A 1 103 ? 25.409 32.244 23.640 1.00 39.02 ? 98  THR A C   1 
ATOM   749  O  O   . THR A 1 103 ? 26.008 32.719 22.660 1.00 37.17 ? 98  THR A O   1 
ATOM   750  C  CB  . THR A 1 103 ? 26.034 32.834 25.994 1.00 39.48 ? 98  THR A CB  1 
ATOM   751  O  OG1 . THR A 1 103 ? 25.786 33.767 27.058 1.00 43.46 ? 98  THR A OG1 1 
ATOM   752  C  CG2 . THR A 1 103 ? 27.480 32.963 25.522 1.00 40.62 ? 98  THR A CG2 1 
ATOM   753  N  N   . VAL A 1 104 ? 25.048 30.951 23.701 1.00 36.04 ? 99  VAL A N   1 
ATOM   754  C  CA  . VAL A 1 104 ? 25.333 30.051 22.588 1.00 33.59 ? 99  VAL A CA  1 
ATOM   755  C  C   . VAL A 1 104 ? 24.562 30.493 21.342 1.00 37.38 ? 99  VAL A C   1 
ATOM   756  O  O   . VAL A 1 104 ? 25.118 30.587 20.235 1.00 34.66 ? 99  VAL A O   1 
ATOM   757  C  CB  . VAL A 1 104 ? 25.013 28.588 22.976 1.00 32.69 ? 99  VAL A CB  1 
ATOM   758  C  CG1 . VAL A 1 104 ? 25.101 27.664 21.767 1.00 35.10 ? 99  VAL A CG1 1 
ATOM   759  C  CG2 . VAL A 1 104 ? 25.979 28.126 24.058 1.00 35.59 ? 99  VAL A CG2 1 
ATOM   760  N  N   . LEU A 1 105 ? 23.270 30.782 21.505 1.00 37.34 ? 100 LEU A N   1 
ATOM   761  C  CA  . LEU A 1 105 ? 22.465 31.130 20.336 1.00 40.17 ? 100 LEU A CA  1 
ATOM   762  C  C   . LEU A 1 105 ? 22.932 32.443 19.727 1.00 40.89 ? 100 LEU A C   1 
ATOM   763  O  O   . LEU A 1 105 ? 22.876 32.606 18.498 1.00 41.52 ? 100 LEU A O   1 
ATOM   764  C  CB  . LEU A 1 105 ? 20.985 31.190 20.719 1.00 42.33 ? 100 LEU A CB  1 
ATOM   765  C  CG  . LEU A 1 105 ? 20.330 29.828 20.986 1.00 42.04 ? 100 LEU A CG  1 
ATOM   766  C  CD1 . LEU A 1 105 ? 19.015 30.012 21.716 1.00 42.01 ? 100 LEU A CD1 1 
ATOM   767  C  CD2 . LEU A 1 105 ? 20.121 29.076 19.669 1.00 44.67 ? 100 LEU A CD2 1 
ATOM   768  N  N   . GLY A 1 106 ? 23.443 33.357 20.563 1.00 41.13 ? 101 GLY A N   1 
ATOM   769  C  CA  . GLY A 1 106 ? 24.017 34.585 20.049 1.00 42.47 ? 101 GLY A CA  1 
ATOM   770  C  C   . GLY A 1 106 ? 25.299 34.355 19.277 1.00 42.44 ? 101 GLY A C   1 
ATOM   771  O  O   . GLY A 1 106 ? 25.527 34.980 18.239 1.00 43.89 ? 101 GLY A O   1 
ATOM   772  N  N   . LEU A 1 107 ? 26.145 33.438 19.753 1.00 38.60 ? 102 LEU A N   1 
ATOM   773  C  CA  . LEU A 1 107 ? 27.373 33.141 19.021 1.00 41.52 ? 102 LEU A CA  1 
ATOM   774  C  C   . LEU A 1 107 ? 27.057 32.489 17.683 1.00 38.66 ? 102 LEU A C   1 
ATOM   775  O  O   . LEU A 1 107 ? 27.735 32.747 16.680 1.00 41.58 ? 102 LEU A O   1 
ATOM   776  C  CB  . LEU A 1 107 ? 28.280 32.217 19.841 1.00 41.67 ? 102 LEU A CB  1 
ATOM   777  C  CG  . LEU A 1 107 ? 29.146 32.733 20.991 1.00 43.68 ? 102 LEU A CG  1 
ATOM   778  C  CD1 . LEU A 1 107 ? 29.810 31.531 21.784 1.00 36.62 ? 102 LEU A CD1 1 
ATOM   779  C  CD2 . LEU A 1 107 ? 30.182 33.785 20.517 1.00 41.06 ? 102 LEU A CD2 1 
ATOM   780  N  N   . LEU A 1 108 ? 26.057 31.600 17.660 1.00 38.50 ? 103 LEU A N   1 
ATOM   781  C  CA  . LEU A 1 108 ? 25.666 30.970 16.411 1.00 36.98 ? 103 LEU A CA  1 
ATOM   782  C  C   . LEU A 1 108 ? 25.209 32.016 15.418 1.00 40.89 ? 103 LEU A C   1 
ATOM   783  O  O   . LEU A 1 108 ? 25.607 31.997 14.245 1.00 41.02 ? 103 LEU A O   1 
ATOM   784  C  CB  . LEU A 1 108 ? 24.550 29.955 16.649 1.00 38.05 ? 103 LEU A CB  1 
ATOM   785  C  CG  . LEU A 1 108 ? 25.046 28.677 17.364 1.00 35.41 ? 103 LEU A CG  1 
ATOM   786  C  CD1 . LEU A 1 108 ? 23.849 27.896 17.936 1.00 36.46 ? 103 LEU A CD1 1 
ATOM   787  C  CD2 . LEU A 1 108 ? 25.875 27.828 16.418 1.00 36.91 ? 103 LEU A CD2 1 
ATOM   788  N  N   . ASP A 1 109 ? 24.375 32.943 15.873 1.00 39.95 ? 104 ASP A N   1 
ATOM   789  C  CA  . ASP A 1 109 ? 23.827 33.913 14.927 1.00 42.39 ? 104 ASP A CA  1 
ATOM   790  C  C   . ASP A 1 109 ? 24.849 34.975 14.547 1.00 45.91 ? 104 ASP A C   1 
ATOM   791  O  O   . ASP A 1 109 ? 24.949 35.357 13.371 1.00 46.42 ? 104 ASP A O   1 
ATOM   792  C  CB  . ASP A 1 109 ? 22.558 34.542 15.481 1.00 47.42 ? 104 ASP A CB  1 
ATOM   793  C  CG  . ASP A 1 109 ? 21.291 33.955 14.831 1.00 60.61 ? 104 ASP A CG  1 
ATOM   794  O  OD1 . ASP A 1 109 ? 21.250 32.717 14.497 1.00 53.10 ? 104 ASP A OD1 1 
ATOM   795  O  OD2 . ASP A 1 109 ? 20.392 34.780 14.524 1.00 66.34 ? 104 ASP A OD2 1 
ATOM   796  N  N   . SER A 1 110 ? 25.635 35.447 15.514 1.00 44.40 ? 105 SER A N   1 
ATOM   797  C  CA  . SER A 1 110 ? 26.584 36.512 15.234 1.00 43.15 ? 105 SER A CA  1 
ATOM   798  C  C   . SER A 1 110 ? 27.780 36.033 14.437 1.00 46.32 ? 105 SER A C   1 
ATOM   799  O  O   . SER A 1 110 ? 28.341 36.805 13.653 1.00 43.22 ? 105 SER A O   1 
ATOM   800  C  CB  . SER A 1 110 ? 27.069 37.136 16.534 1.00 46.07 ? 105 SER A CB  1 
ATOM   801  O  OG  . SER A 1 110 ? 26.002 37.814 17.177 1.00 51.45 ? 105 SER A OG  1 
ATOM   802  N  N   . HIS A 1 111 ? 28.194 34.789 14.616 1.00 40.66 ? 106 HIS A N   1 
ATOM   803  C  CA  . HIS A 1 111 ? 29.525 34.431 14.136 1.00 40.84 ? 106 HIS A CA  1 
ATOM   804  C  C   . HIS A 1 111 ? 29.591 33.156 13.311 1.00 43.46 ? 106 HIS A C   1 
ATOM   805  O  O   . HIS A 1 111 ? 30.385 33.095 12.367 1.00 45.39 ? 106 HIS A O   1 
ATOM   806  C  CB  . HIS A 1 111 ? 30.454 34.289 15.342 1.00 43.52 ? 106 HIS A CB  1 
ATOM   807  C  CG  . HIS A 1 111 ? 30.848 35.598 15.938 1.00 44.77 ? 106 HIS A CG  1 
ATOM   808  N  ND1 . HIS A 1 111 ? 31.817 36.402 15.377 1.00 48.65 ? 106 HIS A ND1 1 
ATOM   809  C  CD2 . HIS A 1 111 ? 30.402 36.251 17.037 1.00 49.95 ? 106 HIS A CD2 1 
ATOM   810  C  CE1 . HIS A 1 111 ? 31.965 37.488 16.115 1.00 43.56 ? 106 HIS A CE1 1 
ATOM   811  N  NE2 . HIS A 1 111 ? 31.118 37.421 17.127 1.00 51.92 ? 106 HIS A NE2 1 
ATOM   812  N  N   . LEU A 1 112 ? 28.800 32.134 13.646 1.00 40.05 ? 107 LEU A N   1 
ATOM   813  C  CA  . LEU A 1 112 ? 29.057 30.773 13.164 1.00 39.93 ? 107 LEU A CA  1 
ATOM   814  C  C   . LEU A 1 112 ? 28.156 30.309 12.025 1.00 39.94 ? 107 LEU A C   1 
ATOM   815  O  O   . LEU A 1 112 ? 28.636 29.613 11.121 1.00 41.38 ? 107 LEU A O   1 
ATOM   816  C  CB  . LEU A 1 112 ? 28.916 29.792 14.327 1.00 38.32 ? 107 LEU A CB  1 
ATOM   817  C  CG  . LEU A 1 112 ? 29.926 30.062 15.437 1.00 39.12 ? 107 LEU A CG  1 
ATOM   818  C  CD1 . LEU A 1 112 ? 29.550 29.211 16.658 1.00 35.93 ? 107 LEU A CD1 1 
ATOM   819  C  CD2 . LEU A 1 112 ? 31.350 29.768 14.947 1.00 39.59 ? 107 LEU A CD2 1 
ATOM   820  N  N   . ILE A 1 113 ? 26.862 30.621 12.070 1.00 40.75 ? 108 ILE A N   1 
ATOM   821  C  CA  . ILE A 1 113 ? 25.923 30.180 11.046 1.00 40.08 ? 108 ILE A CA  1 
ATOM   822  C  C   . ILE A 1 113 ? 26.061 31.080 9.821  1.00 45.48 ? 108 ILE A C   1 
ATOM   823  O  O   . ILE A 1 113 ? 25.970 32.312 9.915  1.00 43.56 ? 108 ILE A O   1 
ATOM   824  C  CB  . ILE A 1 113 ? 24.476 30.178 11.571 1.00 43.46 ? 108 ILE A CB  1 
ATOM   825  C  CG1 . ILE A 1 113 ? 24.248 29.048 12.590 1.00 42.56 ? 108 ILE A CG1 1 
ATOM   826  C  CG2 . ILE A 1 113 ? 23.505 29.993 10.412 1.00 43.73 ? 108 ILE A CG2 1 
ATOM   827  C  CD1 . ILE A 1 113 ? 22.863 29.103 13.308 1.00 41.92 ? 108 ILE A CD1 1 
ATOM   828  N  N   . LYS A 1 114 ? 26.308 30.473 8.671  1.00 47.50 ? 109 LYS A N   1 
ATOM   829  C  CA  . LYS A 1 114 ? 26.373 31.262 7.446  1.00 50.91 ? 109 LYS A CA  1 
ATOM   830  C  C   . LYS A 1 114 ? 26.069 30.366 6.259  1.00 51.04 ? 109 LYS A C   1 
ATOM   831  O  O   . LYS A 1 114 ? 25.869 29.157 6.399  1.00 48.28 ? 109 LYS A O   1 
ATOM   832  C  CB  . LYS A 1 114 ? 27.725 31.963 7.312  1.00 54.68 ? 109 LYS A CB  1 
ATOM   833  C  CG  . LYS A 1 114 ? 28.888 31.206 7.880  1.00 53.46 ? 109 LYS A CG  1 
ATOM   834  C  CD  . LYS A 1 114 ? 30.064 32.141 8.095  1.00 54.59 ? 109 LYS A CD  1 
ATOM   835  C  CE  . LYS A 1 114 ? 29.610 33.426 8.767  1.00 55.10 ? 109 LYS A CE  1 
ATOM   836  N  NZ  . LYS A 1 114 ? 30.749 34.153 9.400  1.00 58.26 ? 109 LYS A NZ  1 
ATOM   837  N  N   . GLU A 1 115 ? 26.013 30.995 5.073  1.00 53.96 ? 110 GLU A N   1 
ATOM   838  C  CA  . GLU A 1 115 ? 25.683 30.294 3.834  1.00 55.47 ? 110 GLU A CA  1 
ATOM   839  C  C   . GLU A 1 115 ? 26.882 29.538 3.281  1.00 53.79 ? 110 GLU A C   1 
ATOM   840  O  O   . GLU A 1 115 ? 26.717 28.462 2.700  1.00 60.97 ? 110 GLU A O   1 
ATOM   841  C  CB  . GLU A 1 115 ? 25.164 31.304 2.798  1.00 62.16 ? 110 GLU A CB  1 
ATOM   842  C  CG  . GLU A 1 115 ? 23.876 32.034 3.218  1.00 65.67 ? 110 GLU A CG  1 
ATOM   843  C  CD  . GLU A 1 115 ? 22.599 31.221 2.975  1.00 72.91 ? 110 GLU A CD  1 
ATOM   844  O  OE1 . GLU A 1 115 ? 22.540 30.029 3.368  1.00 69.65 ? 110 GLU A OE1 1 
ATOM   845  O  OE2 . GLU A 1 115 ? 21.643 31.792 2.391  1.00 80.01 ? 110 GLU A OE2 1 
ATOM   846  N  N   . ALA A 1 116 ? 28.091 30.059 3.475  1.00 56.93 ? 111 ALA A N   1 
ATOM   847  C  CA  . ALA A 1 116 ? 29.294 29.379 3.018  1.00 56.06 ? 111 ALA A CA  1 
ATOM   848  C  C   . ALA A 1 116 ? 29.702 28.279 4.002  1.00 57.78 ? 111 ALA A C   1 
ATOM   849  O  O   . ALA A 1 116 ? 29.068 28.060 5.044  1.00 51.74 ? 111 ALA A O   1 
ATOM   850  C  CB  . ALA A 1 116 ? 30.429 30.385 2.831  1.00 60.28 ? 111 ALA A CB  1 
ATOM   851  N  N   . GLY A 1 117 ? 30.788 27.587 3.672  1.00 57.34 ? 112 GLY A N   1 
ATOM   852  C  CA  . GLY A 1 117 ? 31.324 26.536 4.511  1.00 56.36 ? 112 GLY A CA  1 
ATOM   853  C  C   . GLY A 1 117 ? 30.864 25.170 4.046  1.00 52.36 ? 112 GLY A C   1 
ATOM   854  O  O   . GLY A 1 117 ? 29.936 25.024 3.244  1.00 48.46 ? 112 GLY A O   1 
ATOM   855  N  N   . ASP A 1 118 ? 31.535 24.143 4.562  1.00 50.71 ? 113 ASP A N   1 
ATOM   856  C  CA  . ASP A 1 118 ? 31.177 22.809 4.114  1.00 49.00 ? 113 ASP A CA  1 
ATOM   857  C  C   . ASP A 1 118 ? 29.871 22.342 4.774  1.00 47.10 ? 113 ASP A C   1 
ATOM   858  O  O   . ASP A 1 118 ? 29.293 23.009 5.647  1.00 44.34 ? 113 ASP A O   1 
ATOM   859  C  CB  . ASP A 1 118 ? 32.338 21.833 4.344  1.00 50.28 ? 113 ASP A CB  1 
ATOM   860  C  CG  . ASP A 1 118 ? 32.825 21.787 5.798  1.00 51.49 ? 113 ASP A CG  1 
ATOM   861  O  OD1 . ASP A 1 118 ? 32.119 22.260 6.718  1.00 49.77 ? 113 ASP A OD1 1 
ATOM   862  O  OD2 . ASP A 1 118 ? 33.941 21.263 6.011  1.00 51.98 ? 113 ASP A OD2 1 
ATOM   863  N  N   . ALA A 1 119 ? 29.379 21.196 4.300  1.00 47.95 ? 114 ALA A N   1 
ATOM   864  C  CA  . ALA A 1 119 ? 28.111 20.677 4.803  1.00 49.36 ? 114 ALA A CA  1 
ATOM   865  C  C   . ALA A 1 119 ? 28.197 20.353 6.288  1.00 44.97 ? 114 ALA A C   1 
ATOM   866  O  O   . ALA A 1 119 ? 27.257 20.640 7.038  1.00 44.50 ? 114 ALA A O   1 
ATOM   867  C  CB  . ALA A 1 119 ? 27.688 19.437 4.008  1.00 47.52 ? 114 ALA A CB  1 
ATOM   868  N  N   . GLU A 1 120 ? 29.313 19.764 6.732  1.00 42.62 ? 115 GLU A N   1 
ATOM   869  C  CA  . GLU A 1 120 ? 29.456 19.458 8.157  1.00 45.34 ? 115 GLU A CA  1 
ATOM   870  C  C   . GLU A 1 120 ? 29.258 20.684 9.030  1.00 43.31 ? 115 GLU A C   1 
ATOM   871  O  O   . GLU A 1 120 ? 28.502 20.640 10.012 1.00 41.75 ? 115 GLU A O   1 
ATOM   872  C  CB  . GLU A 1 120 ? 30.810 18.819 8.476  1.00 46.81 ? 115 GLU A CB  1 
ATOM   873  C  CG  . GLU A 1 120 ? 30.878 17.359 8.122  1.00 52.19 ? 115 GLU A CG  1 
ATOM   874  C  CD  . GLU A 1 120 ? 32.172 16.700 8.557  1.00 49.82 ? 115 GLU A CD  1 
ATOM   875  O  OE1 . GLU A 1 120 ? 32.199 15.450 8.581  1.00 54.23 ? 115 GLU A OE1 1 
ATOM   876  O  OE2 . GLU A 1 120 ? 33.151 17.411 8.873  1.00 52.18 ? 115 GLU A OE2 1 
ATOM   877  N  N   . SER A 1 121 ? 29.966 21.777 8.719  1.00 40.24 ? 116 SER A N   1 
ATOM   878  C  CA  . SER A 1 121 ? 29.855 22.963 9.559  1.00 42.77 ? 116 SER A CA  1 
ATOM   879  C  C   . SER A 1 121 ? 28.430 23.488 9.549  1.00 41.15 ? 116 SER A C   1 
ATOM   880  O  O   . SER A 1 121 ? 27.864 23.795 10.606 1.00 37.54 ? 116 SER A O   1 
ATOM   881  C  CB  . SER A 1 121 ? 30.839 24.043 9.103  1.00 44.45 ? 116 SER A CB  1 
ATOM   882  O  OG  . SER A 1 121 ? 30.450 24.552 7.837  1.00 49.43 ? 116 SER A OG  1 
ATOM   883  N  N   . ARG A 1 122 ? 27.813 23.562 8.368  1.00 39.26 ? 117 ARG A N   1 
ATOM   884  C  CA  . ARG A 1 122 ? 26.486 24.165 8.297  1.00 41.66 ? 117 ARG A CA  1 
ATOM   885  C  C   . ARG A 1 122 ? 25.458 23.327 9.034  1.00 38.48 ? 117 ARG A C   1 
ATOM   886  O  O   . ARG A 1 122 ? 24.611 23.871 9.758  1.00 40.29 ? 117 ARG A O   1 
ATOM   887  C  CB  . ARG A 1 122 ? 26.075 24.362 6.838  1.00 41.61 ? 117 ARG A CB  1 
ATOM   888  C  CG  . ARG A 1 122 ? 26.706 25.601 6.208  1.00 44.15 ? 117 ARG A CG  1 
ATOM   889  C  CD  . ARG A 1 122 ? 26.217 25.769 4.762  1.00 43.04 ? 117 ARG A CD  1 
ATOM   890  N  NE  . ARG A 1 122 ? 26.942 24.884 3.859  1.00 46.63 ? 117 ARG A NE  1 
ATOM   891  C  CZ  . ARG A 1 122 ? 26.392 23.901 3.153  1.00 47.23 ? 117 ARG A CZ  1 
ATOM   892  N  NH1 . ARG A 1 122 ? 25.086 23.672 3.177  1.00 49.18 ? 117 ARG A NH1 1 
ATOM   893  N  NH2 . ARG A 1 122 ? 27.169 23.139 2.390  1.00 49.32 ? 117 ARG A NH2 1 
ATOM   894  N  N   . VAL A 1 123 ? 25.540 22.001 8.896  1.00 37.05 ? 118 VAL A N   1 
ATOM   895  C  CA  . VAL A 1 123 ? 24.595 21.132 9.583  1.00 37.71 ? 118 VAL A CA  1 
ATOM   896  C  C   . VAL A 1 123 ? 24.872 21.169 11.077 1.00 36.96 ? 118 VAL A C   1 
ATOM   897  O  O   . VAL A 1 123 ? 23.943 21.221 11.900 1.00 35.69 ? 118 VAL A O   1 
ATOM   898  C  CB  . VAL A 1 123 ? 24.669 19.689 9.048  1.00 36.91 ? 118 VAL A CB  1 
ATOM   899  C  CG1 . VAL A 1 123 ? 23.728 18.788 9.824  1.00 40.12 ? 118 VAL A CG1 1 
ATOM   900  C  CG2 . VAL A 1 123 ? 24.311 19.600 7.542  1.00 40.84 ? 118 VAL A CG2 1 
ATOM   901  N  N   . PHE A 1 124 ? 26.153 21.151 11.447 1.00 37.26 ? 119 PHE A N   1 
ATOM   902  C  CA  . PHE A 1 124 ? 26.479 21.110 12.866 1.00 37.56 ? 119 PHE A CA  1 
ATOM   903  C  C   . PHE A 1 124 ? 25.954 22.345 13.588 1.00 39.33 ? 119 PHE A C   1 
ATOM   904  O  O   . PHE A 1 124 ? 25.363 22.232 14.670 1.00 35.96 ? 119 PHE A O   1 
ATOM   905  C  CB  . PHE A 1 124 ? 27.978 20.978 13.107 1.00 35.94 ? 119 PHE A CB  1 
ATOM   906  C  CG  . PHE A 1 124 ? 28.330 21.235 14.550 1.00 37.57 ? 119 PHE A CG  1 
ATOM   907  C  CD1 . PHE A 1 124 ? 28.077 20.269 15.516 1.00 36.53 ? 119 PHE A CD1 1 
ATOM   908  C  CD2 . PHE A 1 124 ? 28.817 22.469 14.937 1.00 39.57 ? 119 PHE A CD2 1 
ATOM   909  C  CE1 . PHE A 1 124 ? 28.356 20.509 16.831 1.00 39.60 ? 119 PHE A CE1 1 
ATOM   910  C  CE2 . PHE A 1 124 ? 29.096 22.735 16.262 1.00 37.98 ? 119 PHE A CE2 1 
ATOM   911  C  CZ  . PHE A 1 124 ? 28.877 21.757 17.210 1.00 36.04 ? 119 PHE A CZ  1 
ATOM   912  N  N   . TYR A 1 125 ? 26.174 23.545 13.020 1.00 35.81 ? 120 TYR A N   1 
ATOM   913  C  CA  . TYR A 1 125 ? 25.734 24.746 13.725 1.00 38.01 ? 120 TYR A CA  1 
ATOM   914  C  C   . TYR A 1 125 ? 24.218 24.836 13.774 1.00 36.46 ? 120 TYR A C   1 
ATOM   915  O  O   . TYR A 1 125 ? 23.652 25.309 14.761 1.00 36.16 ? 120 TYR A O   1 
ATOM   916  C  CB  . TYR A 1 125 ? 26.328 26.006 13.090 1.00 36.02 ? 120 TYR A CB  1 
ATOM   917  C  CG  . TYR A 1 125 ? 27.828 26.105 13.244 1.00 36.62 ? 120 TYR A CG  1 
ATOM   918  C  CD1 . TYR A 1 125 ? 28.436 25.963 14.504 1.00 35.65 ? 120 TYR A CD1 1 
ATOM   919  C  CD2 . TYR A 1 125 ? 28.641 26.347 12.152 1.00 39.78 ? 120 TYR A CD2 1 
ATOM   920  C  CE1 . TYR A 1 125 ? 29.816 26.071 14.643 1.00 34.56 ? 120 TYR A CE1 1 
ATOM   921  C  CE2 . TYR A 1 125 ? 30.013 26.467 12.299 1.00 37.87 ? 120 TYR A CE2 1 
ATOM   922  C  CZ  . TYR A 1 125 ? 30.588 26.322 13.542 1.00 36.25 ? 120 TYR A CZ  1 
ATOM   923  O  OH  . TYR A 1 125 ? 31.964 26.406 13.634 1.00 39.42 ? 120 TYR A OH  1 
ATOM   924  N  N   . LEU A 1 126 ? 23.535 24.395 12.717 1.00 37.80 ? 121 LEU A N   1 
ATOM   925  C  CA  . LEU A 1 126 ? 22.078 24.448 12.750 1.00 36.77 ? 121 LEU A CA  1 
ATOM   926  C  C   . LEU A 1 126 ? 21.521 23.425 13.731 1.00 38.49 ? 121 LEU A C   1 
ATOM   927  O  O   . LEU A 1 126 ? 20.540 23.705 14.430 1.00 39.09 ? 121 LEU A O   1 
ATOM   928  C  CB  . LEU A 1 126 ? 21.511 24.239 11.339 1.00 37.85 ? 121 LEU A CB  1 
ATOM   929  C  CG  . LEU A 1 126 ? 21.655 25.468 10.412 1.00 37.96 ? 121 LEU A CG  1 
ATOM   930  C  CD1 . LEU A 1 126 ? 21.432 25.063 8.939  1.00 39.30 ? 121 LEU A CD1 1 
ATOM   931  C  CD2 . LEU A 1 126 ? 20.687 26.555 10.817 1.00 41.97 ? 121 LEU A CD2 1 
ATOM   932  N  N   . LYS A 1 127 ? 22.117 22.224 13.775 1.00 35.57 ? 122 LYS A N   1 
ATOM   933  C  CA  . LYS A 1 127 ? 21.834 21.283 14.859 1.00 37.54 ? 122 LYS A CA  1 
ATOM   934  C  C   . LYS A 1 127 ? 22.048 21.932 16.230 1.00 37.78 ? 122 LYS A C   1 
ATOM   935  O  O   . LYS A 1 127 ? 21.213 21.784 17.128 1.00 36.49 ? 122 LYS A O   1 
ATOM   936  C  CB  . LYS A 1 127 ? 22.710 20.039 14.734 1.00 33.17 ? 122 LYS A CB  1 
ATOM   937  C  CG  . LYS A 1 127 ? 22.614 19.096 15.968 1.00 34.51 ? 122 LYS A CG  1 
ATOM   938  C  CD  . LYS A 1 127 ? 23.672 18.018 15.886 1.00 35.89 ? 122 LYS A CD  1 
ATOM   939  C  CE  . LYS A 1 127 ? 23.774 17.219 17.205 1.00 37.11 ? 122 LYS A CE  1 
ATOM   940  N  NZ  . LYS A 1 127 ? 24.046 18.070 18.457 1.00 34.35 ? 122 LYS A NZ  1 
ATOM   941  N  N   . MET A 1 128 ? 23.186 22.619 16.422 1.00 36.16 ? 123 MET A N   1 
ATOM   942  C  CA  . MET A 1 128 ? 23.414 23.308 17.696 1.00 33.41 ? 123 MET A CA  1 
ATOM   943  C  C   . MET A 1 128 ? 22.279 24.266 18.012 1.00 36.80 ? 123 MET A C   1 
ATOM   944  O  O   . MET A 1 128 ? 21.808 24.354 19.151 1.00 35.02 ? 123 MET A O   1 
ATOM   945  C  CB  . MET A 1 128 ? 24.680 24.152 17.682 1.00 36.44 ? 123 MET A CB  1 
ATOM   946  C  CG  . MET A 1 128 ? 25.297 24.326 19.096 1.00 37.88 ? 123 MET A CG  1 
ATOM   947  S  SD  . MET A 1 128 ? 26.963 24.990 19.016 1.00 38.48 ? 123 MET A SD  1 
ATOM   948  C  CE  . MET A 1 128 ? 27.425 24.959 20.763 1.00 37.83 ? 123 MET A CE  1 
ATOM   949  N  N   . LYS A 1 129 ? 21.875 25.058 17.013 1.00 37.04 ? 124 LYS A N   1 
ATOM   950  C  CA  . LYS A 1 129 ? 20.818 26.033 17.257 1.00 36.60 ? 124 LYS A CA  1 
ATOM   951  C  C   . LYS A 1 129 ? 19.535 25.338 17.674 1.00 36.72 ? 124 LYS A C   1 
ATOM   952  O  O   . LYS A 1 129 ? 18.849 25.789 18.598 1.00 37.82 ? 124 LYS A O   1 
ATOM   953  C  CB  . LYS A 1 129 ? 20.570 26.874 16.011 1.00 37.38 ? 124 LYS A CB  1 
ATOM   954  C  CG  . LYS A 1 129 ? 19.488 27.934 16.197 1.00 38.88 ? 124 LYS A CG  1 
ATOM   955  C  CD  . LYS A 1 129 ? 19.446 28.828 14.946 1.00 44.11 ? 124 LYS A CD  1 
ATOM   956  C  CE  . LYS A 1 129 ? 18.172 29.654 14.869 1.00 44.65 ? 124 LYS A CE  1 
ATOM   957  N  NZ  . LYS A 1 129 ? 18.278 30.540 13.672 1.00 51.53 ? 124 LYS A NZ  1 
ATOM   958  N  N   . GLY A 1 130 ? 19.187 24.242 16.998 1.00 35.64 ? 125 GLY A N   1 
ATOM   959  C  CA  . GLY A 1 130 ? 18.017 23.483 17.410 1.00 40.20 ? 125 GLY A CA  1 
ATOM   960  C  C   . GLY A 1 130 ? 18.126 22.972 18.839 1.00 39.02 ? 125 GLY A C   1 
ATOM   961  O  O   . GLY A 1 130 ? 17.153 23.008 19.596 1.00 37.43 ? 125 GLY A O   1 
ATOM   962  N  N   . ASP A 1 131 ? 19.310 22.469 19.219 1.00 38.00 ? 126 ASP A N   1 
ATOM   963  C  CA  . ASP A 1 131 ? 19.503 21.938 20.572 1.00 36.21 ? 126 ASP A CA  1 
ATOM   964  C  C   . ASP A 1 131 ? 19.299 23.013 21.631 1.00 37.65 ? 126 ASP A C   1 
ATOM   965  O  O   . ASP A 1 131 ? 18.646 22.776 22.652 1.00 37.71 ? 126 ASP A O   1 
ATOM   966  C  CB  . ASP A 1 131 ? 20.898 21.353 20.737 1.00 35.36 ? 126 ASP A CB  1 
ATOM   967  C  CG  . ASP A 1 131 ? 21.098 20.045 19.998 1.00 37.33 ? 126 ASP A CG  1 
ATOM   968  O  OD1 . ASP A 1 131 ? 20.108 19.365 19.618 1.00 37.97 ? 126 ASP A OD1 1 
ATOM   969  O  OD2 . ASP A 1 131 ? 22.287 19.717 19.780 1.00 38.90 ? 126 ASP A OD2 1 
ATOM   970  N  N   . TYR A 1 132 ? 19.908 24.182 21.440 1.00 35.93 ? 127 TYR A N   1 
ATOM   971  C  CA  . TYR A 1 132 ? 19.856 25.162 22.521 1.00 39.04 ? 127 TYR A CA  1 
ATOM   972  C  C   . TYR A 1 132 ? 18.491 25.846 22.589 1.00 39.77 ? 127 TYR A C   1 
ATOM   973  O  O   . TYR A 1 132 ? 18.056 26.228 23.678 1.00 38.49 ? 127 TYR A O   1 
ATOM   974  C  CB  . TYR A 1 132 ? 21.030 26.142 22.395 1.00 36.60 ? 127 TYR A CB  1 
ATOM   975  C  CG  . TYR A 1 132 ? 22.271 25.485 22.951 1.00 36.78 ? 127 TYR A CG  1 
ATOM   976  C  CD1 . TYR A 1 132 ? 23.049 24.642 22.159 1.00 36.62 ? 127 TYR A CD1 1 
ATOM   977  C  CD2 . TYR A 1 132 ? 22.624 25.641 24.298 1.00 37.35 ? 127 TYR A CD2 1 
ATOM   978  C  CE1 . TYR A 1 132 ? 24.159 23.989 22.679 1.00 37.53 ? 127 TYR A CE1 1 
ATOM   979  C  CE2 . TYR A 1 132 ? 23.731 24.996 24.829 1.00 36.85 ? 127 TYR A CE2 1 
ATOM   980  C  CZ  . TYR A 1 132 ? 24.502 24.182 24.019 1.00 35.44 ? 127 TYR A CZ  1 
ATOM   981  O  OH  . TYR A 1 132 ? 25.596 23.538 24.565 1.00 35.47 ? 127 TYR A OH  1 
ATOM   982  N  N   . TYR A 1 133 ? 17.756 25.917 21.474 1.00 39.11 ? 128 TYR A N   1 
ATOM   983  C  CA  . TYR A 1 133 ? 16.339 26.272 21.568 1.00 38.27 ? 128 TYR A CA  1 
ATOM   984  C  C   . TYR A 1 133 ? 15.547 25.187 22.288 1.00 40.85 ? 128 TYR A C   1 
ATOM   985  O  O   . TYR A 1 133 ? 14.652 25.491 23.092 1.00 45.17 ? 128 TYR A O   1 
ATOM   986  C  CB  . TYR A 1 133 ? 15.764 26.531 20.165 1.00 41.91 ? 128 TYR A CB  1 
ATOM   987  C  CG  . TYR A 1 133 ? 15.920 27.971 19.746 1.00 45.58 ? 128 TYR A CG  1 
ATOM   988  C  CD1 . TYR A 1 133 ? 15.326 28.983 20.478 1.00 46.86 ? 128 TYR A CD1 1 
ATOM   989  C  CD2 . TYR A 1 133 ? 16.694 28.324 18.632 1.00 45.76 ? 128 TYR A CD2 1 
ATOM   990  C  CE1 . TYR A 1 133 ? 15.477 30.298 20.119 1.00 48.15 ? 128 TYR A CE1 1 
ATOM   991  C  CE2 . TYR A 1 133 ? 16.861 29.638 18.269 1.00 47.96 ? 128 TYR A CE2 1 
ATOM   992  C  CZ  . TYR A 1 133 ? 16.239 30.626 19.015 1.00 51.72 ? 128 TYR A CZ  1 
ATOM   993  O  OH  . TYR A 1 133 ? 16.390 31.948 18.671 1.00 51.59 ? 128 TYR A OH  1 
ATOM   994  N  N   . ARG A 1 134 ? 15.868 23.919 22.025 1.00 38.89 ? 129 ARG A N   1 
ATOM   995  C  CA  . ARG A 1 134 ? 15.211 22.838 22.734 1.00 39.83 ? 129 ARG A CA  1 
ATOM   996  C  C   . ARG A 1 134 ? 15.465 22.950 24.236 1.00 40.17 ? 129 ARG A C   1 
ATOM   997  O  O   . ARG A 1 134 ? 14.559 22.714 25.037 1.00 40.17 ? 129 ARG A O   1 
ATOM   998  C  CB  . ARG A 1 134 ? 15.692 21.491 22.203 1.00 39.08 ? 129 ARG A CB  1 
ATOM   999  C  CG  . ARG A 1 134 ? 15.230 20.298 23.052 1.00 37.92 ? 129 ARG A CG  1 
ATOM   1000 C  CD  . ARG A 1 134 ? 15.316 18.982 22.261 1.00 41.00 ? 129 ARG A CD  1 
ATOM   1001 N  NE  . ARG A 1 134 ? 16.682 18.696 21.827 1.00 40.05 ? 129 ARG A NE  1 
ATOM   1002 C  CZ  . ARG A 1 134 ? 17.557 17.982 22.530 1.00 39.18 ? 129 ARG A CZ  1 
ATOM   1003 N  NH1 . ARG A 1 134 ? 17.239 17.473 23.714 1.00 35.90 ? 129 ARG A NH1 1 
ATOM   1004 N  NH2 . ARG A 1 134 ? 18.776 17.761 22.027 1.00 37.14 ? 129 ARG A NH2 1 
ATOM   1005 N  N   . TYR A 1 135 ? 16.687 23.325 24.635 1.00 37.53 ? 130 TYR A N   1 
ATOM   1006 C  CA  . TYR A 1 135 ? 16.965 23.460 26.072 1.00 40.62 ? 130 TYR A CA  1 
ATOM   1007 C  C   . TYR A 1 135 ? 16.160 24.604 26.667 1.00 39.60 ? 130 TYR A C   1 
ATOM   1008 O  O   . TYR A 1 135 ? 15.607 24.466 27.764 1.00 39.43 ? 130 TYR A O   1 
ATOM   1009 C  CB  . TYR A 1 135 ? 18.466 23.648 26.328 1.00 38.56 ? 130 TYR A CB  1 
ATOM   1010 C  CG  . TYR A 1 135 ? 19.306 22.508 25.749 1.00 35.18 ? 130 TYR A CG  1 
ATOM   1011 C  CD1 . TYR A 1 135 ? 18.782 21.216 25.646 1.00 37.90 ? 130 TYR A CD1 1 
ATOM   1012 C  CD2 . TYR A 1 135 ? 20.595 22.735 25.271 1.00 36.39 ? 130 TYR A CD2 1 
ATOM   1013 C  CE1 . TYR A 1 135 ? 19.537 20.167 25.109 1.00 36.04 ? 130 TYR A CE1 1 
ATOM   1014 C  CE2 . TYR A 1 135 ? 21.358 21.681 24.717 1.00 37.10 ? 130 TYR A CE2 1 
ATOM   1015 C  CZ  . TYR A 1 135 ? 20.812 20.401 24.649 1.00 39.60 ? 130 TYR A CZ  1 
ATOM   1016 O  OH  . TYR A 1 135 ? 21.560 19.353 24.119 1.00 38.43 ? 130 TYR A OH  1 
ATOM   1017 N  N   . LEU A 1 136 ? 16.046 25.719 25.937 1.00 38.57 ? 131 LEU A N   1 
ATOM   1018 C  CA  . LEU A 1 136 ? 15.171 26.813 26.368 1.00 41.53 ? 131 LEU A CA  1 
ATOM   1019 C  C   . LEU A 1 136 ? 13.723 26.349 26.456 1.00 43.79 ? 131 LEU A C   1 
ATOM   1020 O  O   . LEU A 1 136 ? 12.993 26.736 27.375 1.00 44.74 ? 131 LEU A O   1 
ATOM   1021 C  CB  . LEU A 1 136 ? 15.281 28.006 25.415 1.00 40.08 ? 131 LEU A CB  1 
ATOM   1022 C  CG  . LEU A 1 136 ? 16.535 28.885 25.476 1.00 40.37 ? 131 LEU A CG  1 
ATOM   1023 C  CD1 . LEU A 1 136 ? 16.462 29.980 24.441 1.00 42.49 ? 131 LEU A CD1 1 
ATOM   1024 C  CD2 . LEU A 1 136 ? 16.740 29.472 26.880 1.00 39.08 ? 131 LEU A CD2 1 
ATOM   1025 N  N   . ALA A 1 137 ? 13.296 25.504 25.514 1.00 42.47 ? 132 ALA A N   1 
ATOM   1026 C  CA  . ALA A 1 137 ? 11.928 24.999 25.521 1.00 45.57 ? 132 ALA A CA  1 
ATOM   1027 C  C   . ALA A 1 137 ? 11.653 24.102 26.722 1.00 46.22 ? 132 ALA A C   1 
ATOM   1028 O  O   . ALA A 1 137 ? 10.522 24.074 27.223 1.00 47.73 ? 132 ALA A O   1 
ATOM   1029 C  CB  . ALA A 1 137 ? 11.646 24.239 24.217 1.00 46.69 ? 132 ALA A CB  1 
ATOM   1030 N  N   . GLU A 1 138 ? 12.665 23.373 27.209 1.00 43.30 ? 133 GLU A N   1 
ATOM   1031 C  CA  . GLU A 1 138 ? 12.467 22.524 28.382 1.00 43.73 ? 133 GLU A CA  1 
ATOM   1032 C  C   . GLU A 1 138 ? 12.021 23.314 29.618 1.00 44.78 ? 133 GLU A C   1 
ATOM   1033 O  O   . GLU A 1 138 ? 11.345 22.754 30.484 1.00 47.76 ? 133 GLU A O   1 
ATOM   1034 C  CB  . GLU A 1 138 ? 13.747 21.744 28.693 1.00 42.40 ? 133 GLU A CB  1 
ATOM   1035 C  CG  . GLU A 1 138 ? 14.101 20.680 27.649 1.00 45.92 ? 133 GLU A CG  1 
ATOM   1036 C  CD  . GLU A 1 138 ? 15.398 19.944 27.953 1.00 45.19 ? 133 GLU A CD  1 
ATOM   1037 O  OE1 . GLU A 1 138 ? 16.180 20.434 28.790 1.00 44.64 ? 133 GLU A OE1 1 
ATOM   1038 O  OE2 . GLU A 1 138 ? 15.641 18.865 27.365 1.00 44.08 ? 133 GLU A OE2 1 
ATOM   1039 N  N   . VAL A 1 139 ? 12.378 24.594 29.729 1.00 44.47 ? 134 VAL A N   1 
ATOM   1040 C  CA  . VAL A 1 139 ? 12.016 25.390 30.906 1.00 47.07 ? 134 VAL A CA  1 
ATOM   1041 C  C   . VAL A 1 139 ? 11.066 26.546 30.568 1.00 50.65 ? 134 VAL A C   1 
ATOM   1042 O  O   . VAL A 1 139 ? 10.785 27.381 31.435 1.00 45.73 ? 134 VAL A O   1 
ATOM   1043 C  CB  . VAL A 1 139 ? 13.262 25.916 31.648 1.00 46.07 ? 134 VAL A CB  1 
ATOM   1044 C  CG1 . VAL A 1 139 ? 14.279 24.802 31.893 1.00 42.66 ? 134 VAL A CG1 1 
ATOM   1045 C  CG2 . VAL A 1 139 ? 13.898 27.103 30.930 1.00 43.15 ? 134 VAL A CG2 1 
ATOM   1046 N  N   . ALA A 1 140 ? 10.544 26.615 29.341 1.00 48.57 ? 135 ALA A N   1 
ATOM   1047 C  CA  . ALA A 1 140 ? 9.701  27.751 28.967 1.00 52.91 ? 135 ALA A CA  1 
ATOM   1048 C  C   . ALA A 1 140 ? 8.223  27.498 29.301 1.00 54.87 ? 135 ALA A C   1 
ATOM   1049 O  O   . ALA A 1 140 ? 7.788  26.357 29.488 1.00 58.55 ? 135 ALA A O   1 
ATOM   1050 C  CB  . ALA A 1 140 ? 9.853  28.066 27.470 1.00 51.64 ? 135 ALA A CB  1 
ATOM   1051 N  N   . THR A 1 141 ? 7.444  28.591 29.340 1.00 62.41 ? 136 THR A N   1 
ATOM   1052 C  CA  . THR A 1 141 ? 6.006  28.508 29.614 1.00 66.64 ? 136 THR A CA  1 
ATOM   1053 C  C   . THR A 1 141 ? 5.078  29.258 28.637 1.00 69.44 ? 136 THR A C   1 
ATOM   1054 O  O   . THR A 1 141 ? 4.149  28.646 28.093 1.00 71.16 ? 136 THR A O   1 
ATOM   1055 C  CB  . THR A 1 141 ? 5.724  28.998 31.036 1.00 67.81 ? 136 THR A CB  1 
ATOM   1056 O  OG1 . THR A 1 141 ? 6.438  30.223 31.264 1.00 69.55 ? 136 THR A OG1 1 
ATOM   1057 C  CG2 . THR A 1 141 ? 6.119  27.936 32.067 1.00 62.63 ? 136 THR A CG2 1 
ATOM   1058 N  N   . GLY A 1 142 ? 5.284  30.553 28.401 1.00 66.90 ? 137 GLY A N   1 
ATOM   1059 C  CA  . GLY A 1 142 ? 4.211  31.403 27.837 1.00 67.77 ? 137 GLY A CA  1 
ATOM   1060 C  C   . GLY A 1 142 ? 4.324  31.677 26.346 1.00 68.55 ? 137 GLY A C   1 
ATOM   1061 O  O   . GLY A 1 142 ? 4.589  30.780 25.538 1.00 65.37 ? 137 GLY A O   1 
ATOM   1062 N  N   . ASP A 1 143 ? 4.054  32.934 25.963 1.00 70.15 ? 138 ASP A N   1 
ATOM   1063 C  CA  . ASP A 1 143 ? 4.297  33.362 24.585 1.00 71.36 ? 138 ASP A CA  1 
ATOM   1064 C  C   . ASP A 1 143 ? 5.766  33.219 24.205 1.00 71.31 ? 138 ASP A C   1 
ATOM   1065 O  O   . ASP A 1 143 ? 6.091  33.142 23.008 1.00 70.91 ? 138 ASP A O   1 
ATOM   1066 C  CB  . ASP A 1 143 ? 3.863  34.825 24.363 1.00 68.76 ? 138 ASP A CB  1 
ATOM   1067 C  CG  . ASP A 1 143 ? 2.347  34.989 24.204 1.00 70.19 ? 138 ASP A CG  1 
ATOM   1068 O  OD1 . ASP A 1 143 ? 1.651  34.002 23.835 1.00 70.16 ? 138 ASP A OD1 1 
ATOM   1069 O  OD2 . ASP A 1 143 ? 1.865  36.132 24.417 1.00 66.26 ? 138 ASP A OD2 1 
ATOM   1070 N  N   . ASP A 1 144 ? 6.660  33.221 25.200 1.00 68.69 ? 139 ASP A N   1 
ATOM   1071 C  CA  . ASP A 1 144 ? 8.044  32.828 24.962 1.00 69.58 ? 139 ASP A CA  1 
ATOM   1072 C  C   . ASP A 1 144 ? 8.120  31.402 24.409 1.00 66.11 ? 139 ASP A C   1 
ATOM   1073 O  O   . ASP A 1 144 ? 8.916  31.125 23.503 1.00 63.54 ? 139 ASP A O   1 
ATOM   1074 C  CB  . ASP A 1 144 ? 8.842  32.965 26.268 1.00 66.92 ? 139 ASP A CB  1 
ATOM   1075 C  CG  . ASP A 1 144 ? 10.347 33.184 26.041 1.00 70.38 ? 139 ASP A CG  1 
ATOM   1076 O  OD1 . ASP A 1 144 ? 10.730 33.716 24.971 1.00 72.59 ? 139 ASP A OD1 1 
ATOM   1077 O  OD2 . ASP A 1 144 ? 11.146 32.822 26.948 1.00 69.69 ? 139 ASP A OD2 1 
ATOM   1078 N  N   . LYS A 1 145 ? 7.260  30.497 24.909 1.00 64.01 ? 140 LYS A N   1 
ATOM   1079 C  CA  . LYS A 1 145 ? 7.437  29.065 24.667 1.00 61.05 ? 140 LYS A CA  1 
ATOM   1080 C  C   . LYS A 1 145 ? 7.077  28.666 23.240 1.00 65.39 ? 140 LYS A C   1 
ATOM   1081 O  O   . LYS A 1 145 ? 7.688  27.747 22.670 1.00 61.21 ? 140 LYS A O   1 
ATOM   1082 C  CB  . LYS A 1 145 ? 6.595  28.254 25.649 1.00 61.40 ? 140 LYS A CB  1 
ATOM   1083 C  CG  . LYS A 1 145 ? 6.604  26.774 25.329 1.00 58.18 ? 140 LYS A CG  1 
ATOM   1084 C  CD  . LYS A 1 145 ? 6.645  25.891 26.560 1.00 61.29 ? 140 LYS A CD  1 
ATOM   1085 C  CE  . LYS A 1 145 ? 6.561  24.415 26.178 1.00 60.56 ? 140 LYS A CE  1 
ATOM   1086 N  NZ  . LYS A 1 145 ? 5.687  23.629 27.092 1.00 62.44 ? 140 LYS A NZ  1 
ATOM   1087 N  N   . LYS A 1 146 ? 6.048  29.294 22.668 1.00 66.70 ? 141 LYS A N   1 
ATOM   1088 C  CA  . LYS A 1 146 ? 5.702  29.002 21.281 1.00 64.88 ? 141 LYS A CA  1 
ATOM   1089 C  C   . LYS A 1 146 ? 6.798  29.484 20.344 1.00 59.47 ? 141 LYS A C   1 
ATOM   1090 O  O   . LYS A 1 146 ? 7.267  28.729 19.487 1.00 64.02 ? 141 LYS A O   1 
ATOM   1091 C  CB  . LYS A 1 146 ? 4.354  29.637 20.915 1.00 69.73 ? 141 LYS A CB  1 
ATOM   1092 C  CG  . LYS A 1 146 ? 3.222  29.385 21.912 1.00 74.29 ? 141 LYS A CG  1 
ATOM   1093 C  CD  . LYS A 1 146 ? 2.094  30.403 21.741 1.00 75.82 ? 141 LYS A CD  1 
ATOM   1094 C  CE  . LYS A 1 146 ? 0.870  30.020 22.561 1.00 75.97 ? 141 LYS A CE  1 
ATOM   1095 N  NZ  . LYS A 1 146 ? 0.255  28.750 22.083 1.00 77.88 ? 141 LYS A NZ  1 
ATOM   1096 N  N   . ARG A 1 147 ? 7.220  30.742 20.500 1.00 60.69 ? 142 ARG A N   1 
ATOM   1097 C  CA  . ARG A 1 147 ? 8.352  31.267 19.739 1.00 60.94 ? 142 ARG A CA  1 
ATOM   1098 C  C   . ARG A 1 147 ? 9.534  30.292 19.769 1.00 62.45 ? 142 ARG A C   1 
ATOM   1099 O  O   . ARG A 1 147 ? 10.087 29.931 18.719 1.00 55.34 ? 142 ARG A O   1 
ATOM   1100 C  CB  . ARG A 1 147 ? 8.736  32.631 20.315 1.00 65.35 ? 142 ARG A CB  1 
ATOM   1101 C  CG  . ARG A 1 147 ? 7.760  33.747 19.937 1.00 64.69 ? 142 ARG A CG  1 
ATOM   1102 C  CD  . ARG A 1 147 ? 8.388  35.135 19.985 1.00 67.15 ? 142 ARG A CD  1 
ATOM   1103 N  NE  . ARG A 1 147 ? 8.230  35.730 21.312 1.00 68.92 ? 142 ARG A NE  1 
ATOM   1104 C  CZ  . ARG A 1 147 ? 7.192  36.476 21.679 1.00 63.30 ? 142 ARG A CZ  1 
ATOM   1105 N  NH1 . ARG A 1 147 ? 6.201  36.742 20.840 1.00 65.54 ? 142 ARG A NH1 1 
ATOM   1106 N  NH2 . ARG A 1 147 ? 7.149  36.967 22.917 1.00 62.28 ? 142 ARG A NH2 1 
ATOM   1107 N  N   . ILE A 1 148 ? 9.877  29.798 20.968 1.00 58.45 ? 143 ILE A N   1 
ATOM   1108 C  CA  . ILE A 1 148 ? 11.044 28.929 21.154 1.00 57.51 ? 143 ILE A CA  1 
ATOM   1109 C  C   . ILE A 1 148 ? 10.878 27.590 20.441 1.00 53.71 ? 143 ILE A C   1 
ATOM   1110 O  O   . ILE A 1 148 ? 11.783 27.154 19.719 1.00 53.86 ? 143 ILE A O   1 
ATOM   1111 C  CB  . ILE A 1 148 ? 11.338 28.732 22.655 1.00 51.18 ? 143 ILE A CB  1 
ATOM   1112 C  CG1 . ILE A 1 148 ? 11.740 30.061 23.293 1.00 54.59 ? 143 ILE A CG1 1 
ATOM   1113 C  CG2 . ILE A 1 148 ? 12.375 27.630 22.875 1.00 47.45 ? 143 ILE A CG2 1 
ATOM   1114 C  CD1 . ILE A 1 148 ? 11.727 30.029 24.794 1.00 53.18 ? 143 ILE A CD1 1 
ATOM   1115 N  N   . ILE A 1 149 ? 9.742  26.904 20.641 1.00 53.87 ? 144 ILE A N   1 
ATOM   1116 C  CA  . ILE A 1 149 ? 9.568  25.576 20.049 1.00 54.76 ? 144 ILE A CA  1 
ATOM   1117 C  C   . ILE A 1 149 ? 9.623  25.635 18.521 1.00 56.41 ? 144 ILE A C   1 
ATOM   1118 O  O   . ILE A 1 149 ? 10.199 24.751 17.871 1.00 54.55 ? 144 ILE A O   1 
ATOM   1119 C  CB  . ILE A 1 149 ? 8.266  24.921 20.543 1.00 55.47 ? 144 ILE A CB  1 
ATOM   1120 C  CG1 . ILE A 1 149 ? 8.434  24.509 22.009 1.00 54.28 ? 144 ILE A CG1 1 
ATOM   1121 C  CG2 . ILE A 1 149 ? 7.946  23.697 19.709 1.00 55.25 ? 144 ILE A CG2 1 
ATOM   1122 C  CD1 . ILE A 1 149 ? 7.261  23.782 22.597 1.00 53.15 ? 144 ILE A CD1 1 
ATOM   1123 N  N   . ASP A 1 150 ? 9.033  26.665 17.921 1.00 57.90 ? 145 ASP A N   1 
ATOM   1124 C  CA  . ASP A 1 150 ? 9.077  26.756 16.465 1.00 58.52 ? 145 ASP A CA  1 
ATOM   1125 C  C   . ASP A 1 150 ? 10.488 27.058 15.987 1.00 56.79 ? 145 ASP A C   1 
ATOM   1126 O  O   . ASP A 1 150 ? 10.928 26.525 14.959 1.00 55.02 ? 145 ASP A O   1 
ATOM   1127 C  CB  . ASP A 1 150 ? 8.101  27.821 15.952 1.00 60.22 ? 145 ASP A CB  1 
ATOM   1128 C  CG  . ASP A 1 150 ? 6.640  27.442 16.188 1.00 62.99 ? 145 ASP A CG  1 
ATOM   1129 O  OD1 . ASP A 1 150 ? 6.279  26.263 15.941 1.00 66.00 ? 145 ASP A OD1 1 
ATOM   1130 O  OD2 . ASP A 1 150 ? 5.848  28.338 16.574 1.00 65.69 ? 145 ASP A OD2 1 
ATOM   1131 N  N   . SER A 1 151 ? 11.212 27.904 16.731 1.00 55.29 ? 146 SER A N   1 
ATOM   1132 C  CA  . SER A 1 151 ? 12.590 28.223 16.370 1.00 53.96 ? 146 SER A CA  1 
ATOM   1133 C  C   . SER A 1 151 ? 13.461 26.975 16.400 1.00 50.93 ? 146 SER A C   1 
ATOM   1134 O  O   . SER A 1 151 ? 14.356 26.818 15.560 1.00 49.38 ? 146 SER A O   1 
ATOM   1135 C  CB  . SER A 1 151 ? 13.165 29.287 17.308 1.00 48.09 ? 146 SER A CB  1 
ATOM   1136 O  OG  . SER A 1 151 ? 12.568 30.548 17.126 1.00 53.25 ? 146 SER A OG  1 
ATOM   1137 N  N   . ALA A 1 152 ? 13.219 26.084 17.371 1.00 51.32 ? 147 ALA A N   1 
ATOM   1138 C  CA  . ALA A 1 152 ? 13.942 24.816 17.425 1.00 48.52 ? 147 ALA A CA  1 
ATOM   1139 C  C   . ALA A 1 152 ? 13.612 23.941 16.222 1.00 50.30 ? 147 ALA A C   1 
ATOM   1140 O  O   . ALA A 1 152 ? 14.514 23.436 15.539 1.00 46.60 ? 147 ALA A O   1 
ATOM   1141 C  CB  . ALA A 1 152 ? 13.618 24.069 18.718 1.00 43.98 ? 147 ALA A CB  1 
ATOM   1142 N  N   . ARG A 1 153 ? 12.317 23.718 15.970 1.00 52.19 ? 148 ARG A N   1 
ATOM   1143 C  CA  . ARG A 1 153 ? 11.923 22.861 14.854 1.00 52.71 ? 148 ARG A CA  1 
ATOM   1144 C  C   . ARG A 1 153 ? 12.458 23.414 13.539 1.00 48.28 ? 148 ARG A C   1 
ATOM   1145 O  O   . ARG A 1 153 ? 12.965 22.662 12.700 1.00 51.33 ? 148 ARG A O   1 
ATOM   1146 C  CB  . ARG A 1 153 ? 10.399 22.712 14.811 1.00 54.44 ? 148 ARG A CB  1 
ATOM   1147 C  CG  . ARG A 1 153 ? 9.870  22.029 13.547 1.00 57.20 ? 148 ARG A CG  1 
ATOM   1148 C  CD  . ARG A 1 153 ? 8.339  22.030 13.463 1.00 57.94 ? 148 ARG A CD  1 
ATOM   1149 N  NE  . ARG A 1 153 ? 7.690  21.381 14.601 1.00 57.27 ? 148 ARG A NE  1 
ATOM   1150 C  CZ  . ARG A 1 153 ? 7.026  22.029 15.551 1.00 55.48 ? 148 ARG A CZ  1 
ATOM   1151 N  NH1 . ARG A 1 153 ? 6.911  23.347 15.540 1.00 60.40 ? 148 ARG A NH1 1 
ATOM   1152 N  NH2 . ARG A 1 153 ? 6.452  21.338 16.527 1.00 59.50 ? 148 ARG A NH2 1 
ATOM   1153 N  N   . SER A 1 154 ? 12.387 24.732 13.374 1.00 48.48 ? 149 SER A N   1 
ATOM   1154 C  CA  . SER A 1 154 ? 12.857 25.389 12.161 1.00 54.64 ? 149 SER A CA  1 
ATOM   1155 C  C   . SER A 1 154 ? 14.349 25.141 11.930 1.00 53.82 ? 149 SER A C   1 
ATOM   1156 O  O   . SER A 1 154 ? 14.774 24.801 10.815 1.00 47.54 ? 149 SER A O   1 
ATOM   1157 C  CB  . SER A 1 154 ? 12.549 26.882 12.266 1.00 53.27 ? 149 SER A CB  1 
ATOM   1158 O  OG  . SER A 1 154 ? 12.938 27.583 11.112 1.00 60.77 ? 149 SER A OG  1 
ATOM   1159 N  N   . ALA A 1 155 ? 15.163 25.315 12.977 1.00 50.33 ? 150 ALA A N   1 
ATOM   1160 C  CA  . ALA A 1 155 ? 16.601 25.088 12.852 1.00 47.47 ? 150 ALA A CA  1 
ATOM   1161 C  C   . ALA A 1 155 ? 16.900 23.622 12.568 1.00 44.28 ? 150 ALA A C   1 
ATOM   1162 O  O   . ALA A 1 155 ? 17.766 23.306 11.736 1.00 42.21 ? 150 ALA A O   1 
ATOM   1163 C  CB  . ALA A 1 155 ? 17.324 25.565 14.128 1.00 43.23 ? 150 ALA A CB  1 
ATOM   1164 N  N   . TYR A 1 156 ? 16.207 22.708 13.257 1.00 43.41 ? 151 TYR A N   1 
ATOM   1165 C  CA  . TYR A 1 156 ? 16.417 21.287 13.008 1.00 42.46 ? 151 TYR A CA  1 
ATOM   1166 C  C   . TYR A 1 156 ? 16.042 20.931 11.571 1.00 46.26 ? 151 TYR A C   1 
ATOM   1167 O  O   . TYR A 1 156 ? 16.688 20.089 10.940 1.00 41.69 ? 151 TYR A O   1 
ATOM   1168 C  CB  . TYR A 1 156 ? 15.585 20.445 13.969 1.00 42.15 ? 151 TYR A CB  1 
ATOM   1169 C  CG  . TYR A 1 156 ? 16.158 20.263 15.373 1.00 42.25 ? 151 TYR A CG  1 
ATOM   1170 C  CD1 . TYR A 1 156 ? 17.472 19.844 15.568 1.00 42.49 ? 151 TYR A CD1 1 
ATOM   1171 C  CD2 . TYR A 1 156 ? 15.359 20.445 16.493 1.00 45.98 ? 151 TYR A CD2 1 
ATOM   1172 C  CE1 . TYR A 1 156 ? 17.998 19.632 16.872 1.00 37.78 ? 151 TYR A CE1 1 
ATOM   1173 C  CE2 . TYR A 1 156 ? 15.871 20.240 17.795 1.00 43.85 ? 151 TYR A CE2 1 
ATOM   1174 C  CZ  . TYR A 1 156 ? 17.195 19.839 17.970 1.00 40.43 ? 151 TYR A CZ  1 
ATOM   1175 O  OH  . TYR A 1 156 ? 17.693 19.625 19.263 1.00 38.68 ? 151 TYR A OH  1 
ATOM   1176 N  N   . GLN A 1 157 ? 14.982 21.552 11.051 1.00 47.82 ? 152 GLN A N   1 
ATOM   1177 C  CA  . GLN A 1 157 ? 14.512 21.183 9.718  1.00 51.16 ? 152 GLN A CA  1 
ATOM   1178 C  C   . GLN A 1 157 ? 15.502 21.629 8.652  1.00 46.98 ? 152 GLN A C   1 
ATOM   1179 O  O   . GLN A 1 157 ? 15.820 20.863 7.733  1.00 50.26 ? 152 GLN A O   1 
ATOM   1180 C  CB  . GLN A 1 157 ? 13.125 21.772 9.453  1.00 52.14 ? 152 GLN A CB  1 
ATOM   1181 C  CG  . GLN A 1 157 ? 12.436 21.111 8.245  1.00 55.72 ? 152 GLN A CG  1 
ATOM   1182 C  CD  . GLN A 1 157 ? 12.171 19.627 8.462  1.00 57.49 ? 152 GLN A CD  1 
ATOM   1183 O  OE1 . GLN A 1 157 ? 11.327 19.251 9.284  1.00 64.67 ? 152 GLN A OE1 1 
ATOM   1184 N  NE2 . GLN A 1 157 ? 12.893 18.777 7.731  1.00 57.93 ? 152 GLN A NE2 1 
ATOM   1185 N  N   . GLU A 1 158 ? 16.014 22.856 8.772  1.00 44.85 ? 153 GLU A N   1 
ATOM   1186 C  CA  . GLU A 1 158 ? 17.076 23.311 7.876  1.00 49.14 ? 153 GLU A CA  1 
ATOM   1187 C  C   . GLU A 1 158 ? 18.251 22.350 7.886  1.00 47.60 ? 153 GLU A C   1 
ATOM   1188 O  O   . GLU A 1 158 ? 18.801 21.992 6.840  1.00 44.77 ? 153 GLU A O   1 
ATOM   1189 C  CB  . GLU A 1 158 ? 17.568 24.679 8.303  1.00 50.41 ? 153 GLU A CB  1 
ATOM   1190 C  CG  . GLU A 1 158 ? 16.934 25.862 7.692  1.00 54.66 ? 153 GLU A CG  1 
ATOM   1191 C  CD  . GLU A 1 158 ? 18.009 26.898 7.379  1.00 60.24 ? 153 GLU A CD  1 
ATOM   1192 O  OE1 . GLU A 1 158 ? 18.812 26.658 6.439  1.00 59.75 ? 153 GLU A OE1 1 
ATOM   1193 O  OE2 . GLU A 1 158 ? 18.080 27.918 8.102  1.00 61.60 ? 153 GLU A OE2 1 
ATOM   1194 N  N   . ALA A 1 159 ? 18.680 21.965 9.089  1.00 41.07 ? 154 ALA A N   1 
ATOM   1195 C  CA  . ALA A 1 159 ? 19.796 21.046 9.209  1.00 42.09 ? 154 ALA A CA  1 
ATOM   1196 C  C   . ALA A 1 159 ? 19.487 19.722 8.525  1.00 41.77 ? 154 ALA A C   1 
ATOM   1197 O  O   . ALA A 1 159 ? 20.341 19.174 7.824  1.00 39.48 ? 154 ALA A O   1 
ATOM   1198 C  CB  . ALA A 1 159 ? 20.135 20.849 10.693 1.00 37.99 ? 154 ALA A CB  1 
ATOM   1199 N  N   . MET A 1 160 ? 18.268 19.197 8.712  1.00 41.14 ? 155 MET A N   1 
ATOM   1200 C  CA  . MET A 1 160 ? 17.894 17.914 8.121  1.00 41.89 ? 155 MET A CA  1 
ATOM   1201 C  C   . MET A 1 160 ? 17.928 17.980 6.598  1.00 44.05 ? 155 MET A C   1 
ATOM   1202 O  O   . MET A 1 160 ? 18.446 17.072 5.933  1.00 43.59 ? 155 MET A O   1 
ATOM   1203 C  CB  . MET A 1 160 ? 16.496 17.529 8.598  1.00 41.55 ? 155 MET A CB  1 
ATOM   1204 C  CG  . MET A 1 160 ? 16.424 17.059 10.059 1.00 44.89 ? 155 MET A CG  1 
ATOM   1205 S  SD  . MET A 1 160 ? 17.054 15.414 10.427 1.00 50.33 ? 155 MET A SD  1 
ATOM   1206 C  CE  . MET A 1 160 ? 16.398 14.456 9.051  1.00 51.60 ? 155 MET A CE  1 
ATOM   1207 N  N   . ASP A 1 161 ? 17.384 19.063 6.038  1.00 45.84 ? 156 ASP A N   1 
ATOM   1208 C  CA  . ASP A 1 161 ? 17.317 19.227 4.589  1.00 45.19 ? 156 ASP A CA  1 
ATOM   1209 C  C   . ASP A 1 161 ? 18.713 19.194 3.994  1.00 46.52 ? 156 ASP A C   1 
ATOM   1210 O  O   . ASP A 1 161 ? 18.991 18.409 3.079  1.00 46.03 ? 156 ASP A O   1 
ATOM   1211 C  CB  . ASP A 1 161 ? 16.609 20.543 4.275  1.00 49.44 ? 156 ASP A CB  1 
ATOM   1212 C  CG  . ASP A 1 161 ? 15.121 20.460 4.562  1.00 52.69 ? 156 ASP A CG  1 
ATOM   1213 O  OD1 . ASP A 1 161 ? 14.453 21.512 4.666  1.00 59.55 ? 156 ASP A OD1 1 
ATOM   1214 O  OD2 . ASP A 1 161 ? 14.633 19.322 4.748  1.00 60.07 ? 156 ASP A OD2 1 
ATOM   1215 N  N   . ILE A 1 162 ? 19.629 19.981 4.575  1.00 44.68 ? 157 ILE A N   1 
ATOM   1216 C  CA  . ILE A 1 162 ? 21.021 19.997 4.130  1.00 43.85 ? 157 ILE A CA  1 
ATOM   1217 C  C   . ILE A 1 162 ? 21.676 18.626 4.301  1.00 44.07 ? 157 ILE A C   1 
ATOM   1218 O  O   . ILE A 1 162 ? 22.378 18.144 3.403  1.00 43.10 ? 157 ILE A O   1 
ATOM   1219 C  CB  . ILE A 1 162 ? 21.801 21.095 4.879  1.00 40.95 ? 157 ILE A CB  1 
ATOM   1220 C  CG1 . ILE A 1 162 ? 21.210 22.475 4.584  1.00 48.98 ? 157 ILE A CG1 1 
ATOM   1221 C  CG2 . ILE A 1 162 ? 23.285 21.033 4.512  1.00 45.63 ? 157 ILE A CG2 1 
ATOM   1222 C  CD1 . ILE A 1 162 ? 21.660 23.551 5.555  1.00 46.61 ? 157 ILE A CD1 1 
ATOM   1223 N  N   . SER A 1 163 ? 21.483 17.976 5.461  1.00 40.07 ? 158 SER A N   1 
ATOM   1224 C  CA  . SER A 1 163 ? 22.208 16.733 5.697  1.00 37.70 ? 158 SER A CA  1 
ATOM   1225 C  C   . SER A 1 163 ? 21.752 15.611 4.767  1.00 41.05 ? 158 SER A C   1 
ATOM   1226 O  O   . SER A 1 163 ? 22.559 14.757 4.402  1.00 39.11 ? 158 SER A O   1 
ATOM   1227 C  CB  . SER A 1 163 ? 22.042 16.277 7.151  1.00 41.52 ? 158 SER A CB  1 
ATOM   1228 O  OG  . SER A 1 163 ? 20.761 15.697 7.351  1.00 44.67 ? 158 SER A OG  1 
ATOM   1229 N  N   . LYS A 1 164 ? 20.461 15.567 4.427  1.00 41.64 ? 159 LYS A N   1 
ATOM   1230 C  CA  . LYS A 1 164 ? 19.952 14.543 3.521  1.00 41.99 ? 159 LYS A CA  1 
ATOM   1231 C  C   . LYS A 1 164 ? 20.453 14.762 2.094  1.00 45.90 ? 159 LYS A C   1 
ATOM   1232 O  O   . LYS A 1 164 ? 20.566 13.805 1.328  1.00 45.81 ? 159 LYS A O   1 
ATOM   1233 C  CB  . LYS A 1 164 ? 18.423 14.533 3.559  1.00 45.00 ? 159 LYS A CB  1 
ATOM   1234 C  CG  . LYS A 1 164 ? 17.818 13.985 4.856  1.00 48.98 ? 159 LYS A CG  1 
ATOM   1235 C  CD  . LYS A 1 164 ? 16.369 13.476 4.654  1.00 56.25 ? 159 LYS A CD  1 
ATOM   1236 C  CE  . LYS A 1 164 ? 15.356 14.178 5.574  1.00 57.44 ? 159 LYS A CE  1 
ATOM   1237 N  NZ  . LYS A 1 164 ? 15.093 15.601 5.181  1.00 59.09 ? 159 LYS A NZ  1 
ATOM   1238 N  N   . LYS A 1 165 ? 20.774 16.000 1.733  1.00 45.52 ? 160 LYS A N   1 
ATOM   1239 C  CA  . LYS A 1 165 ? 21.216 16.326 0.382  1.00 46.59 ? 160 LYS A CA  1 
ATOM   1240 C  C   . LYS A 1 165 ? 22.723 16.165 0.217  1.00 50.13 ? 160 LYS A C   1 
ATOM   1241 O  O   . LYS A 1 165 ? 23.191 15.755 -0.855 1.00 47.42 ? 160 LYS A O   1 
ATOM   1242 C  CB  . LYS A 1 165 ? 20.797 17.762 0.078  1.00 48.60 ? 160 LYS A CB  1 
ATOM   1243 C  CG  . LYS A 1 165 ? 19.345 17.844 -0.333 1.00 57.07 ? 160 LYS A CG  1 
ATOM   1244 C  CD  . LYS A 1 165 ? 18.930 19.250 -0.709 1.00 61.85 ? 160 LYS A CD  1 
ATOM   1245 C  CE  . LYS A 1 165 ? 17.409 19.389 -0.615 1.00 64.31 ? 160 LYS A CE  1 
ATOM   1246 N  NZ  . LYS A 1 165 ? 17.023 20.759 -0.163 1.00 66.19 ? 160 LYS A NZ  1 
ATOM   1247 N  N   . GLU A 1 166 ? 23.489 16.410 1.280  1.00 41.24 ? 161 GLU A N   1 
ATOM   1248 C  CA  . GLU A 1 166 ? 24.930 16.591 1.208  1.00 40.87 ? 161 GLU A CA  1 
ATOM   1249 C  C   . GLU A 1 166 ? 25.739 15.538 1.958  1.00 45.78 ? 161 GLU A C   1 
ATOM   1250 O  O   . GLU A 1 166 ? 26.954 15.468 1.753  1.00 46.04 ? 161 GLU A O   1 
ATOM   1251 C  CB  . GLU A 1 166 ? 25.282 17.963 1.786  1.00 46.91 ? 161 GLU A CB  1 
ATOM   1252 C  CG  . GLU A 1 166 ? 24.363 19.098 1.338  1.00 49.37 ? 161 GLU A CG  1 
ATOM   1253 C  CD  . GLU A 1 166 ? 25.072 20.393 1.002  1.00 53.18 ? 161 GLU A CD  1 
ATOM   1254 O  OE1 . GLU A 1 166 ? 26.323 20.426 0.958  1.00 55.66 ? 161 GLU A OE1 1 
ATOM   1255 O  OE2 . GLU A 1 166 ? 24.354 21.420 0.922  1.00 50.36 ? 161 GLU A OE2 1 
ATOM   1256 N  N   . MET A 1 167 ? 25.127 14.746 2.846  1.00 41.06 ? 162 MET A N   1 
ATOM   1257 C  CA  . MET A 1 167 ? 25.924 13.845 3.662  1.00 40.27 ? 162 MET A CA  1 
ATOM   1258 C  C   . MET A 1 167 ? 25.459 12.412 3.473  1.00 37.45 ? 162 MET A C   1 
ATOM   1259 O  O   . MET A 1 167 ? 24.259 12.175 3.275  1.00 40.23 ? 162 MET A O   1 
ATOM   1260 C  CB  . MET A 1 167 ? 25.791 14.194 5.155  1.00 41.08 ? 162 MET A CB  1 
ATOM   1261 C  CG  . MET A 1 167 ? 26.435 15.521 5.559  1.00 42.59 ? 162 MET A CG  1 
ATOM   1262 S  SD  . MET A 1 167 ? 25.894 15.967 7.240  1.00 45.66 ? 162 MET A SD  1 
ATOM   1263 C  CE  . MET A 1 167 ? 27.411 16.642 7.887  1.00 44.97 ? 162 MET A CE  1 
ATOM   1264 N  N   . PRO A 1 168 ? 26.347 11.436 3.608  1.00 36.19 ? 163 PRO A N   1 
ATOM   1265 C  CA  . PRO A 1 168 ? 25.898 10.041 3.617  1.00 42.69 ? 163 PRO A CA  1 
ATOM   1266 C  C   . PRO A 1 168 ? 25.045 9.772  4.841  1.00 40.04 ? 163 PRO A C   1 
ATOM   1267 O  O   . PRO A 1 168 ? 25.145 10.480 5.863  1.00 37.52 ? 163 PRO A O   1 
ATOM   1268 C  CB  . PRO A 1 168 ? 27.205 9.229  3.650  1.00 40.66 ? 163 PRO A CB  1 
ATOM   1269 C  CG  . PRO A 1 168 ? 28.192 10.144 4.235  1.00 40.05 ? 163 PRO A CG  1 
ATOM   1270 C  CD  . PRO A 1 168 ? 27.793 11.547 3.849  1.00 40.36 ? 163 PRO A CD  1 
ATOM   1271 N  N   . PRO A 1 169 ? 24.165 8.774  4.768  1.00 37.33 ? 164 PRO A N   1 
ATOM   1272 C  CA  . PRO A 1 169 ? 23.251 8.515  5.887  1.00 40.03 ? 164 PRO A CA  1 
ATOM   1273 C  C   . PRO A 1 169 ? 23.944 7.939  7.126  1.00 38.58 ? 164 PRO A C   1 
ATOM   1274 O  O   . PRO A 1 169 ? 23.284 7.829  8.162  1.00 40.93 ? 164 PRO A O   1 
ATOM   1275 C  CB  . PRO A 1 169 ? 22.246 7.520  5.296  1.00 44.35 ? 164 PRO A CB  1 
ATOM   1276 C  CG  . PRO A 1 169 ? 22.976 6.879  4.157  1.00 43.12 ? 164 PRO A CG  1 
ATOM   1277 C  CD  . PRO A 1 169 ? 23.980 7.837  3.638  1.00 43.11 ? 164 PRO A CD  1 
ATOM   1278 N  N   . THR A 1 170 ? 25.230 7.575  7.067  1.00 35.97 ? 165 THR A N   1 
ATOM   1279 C  CA  . THR A 1 170 ? 25.953 7.212  8.285  1.00 37.48 ? 165 THR A CA  1 
ATOM   1280 C  C   . THR A 1 170 ? 26.753 8.365  8.886  1.00 36.97 ? 165 THR A C   1 
ATOM   1281 O  O   . THR A 1 170 ? 27.431 8.147  9.906  1.00 34.36 ? 165 THR A O   1 
ATOM   1282 C  CB  . THR A 1 170 ? 26.944 6.091  8.044  1.00 35.57 ? 165 THR A CB  1 
ATOM   1283 O  OG1 . THR A 1 170 ? 27.833 6.511  7.011  1.00 35.60 ? 165 THR A OG1 1 
ATOM   1284 C  CG2 . THR A 1 170 ? 26.249 4.744  7.685  1.00 34.88 ? 165 THR A CG2 1 
ATOM   1285 N  N   . ASN A 1 171 ? 26.765 9.539  8.250  1.00 34.84 ? 166 ASN A N   1 
ATOM   1286 C  CA  . ASN A 1 171 ? 27.588 10.635 8.760  1.00 35.01 ? 166 ASN A CA  1 
ATOM   1287 C  C   . ASN A 1 171 ? 27.189 10.945 10.201 1.00 35.00 ? 166 ASN A C   1 
ATOM   1288 O  O   . ASN A 1 171 ? 25.996 11.142 10.481 1.00 34.72 ? 166 ASN A O   1 
ATOM   1289 C  CB  . ASN A 1 171 ? 27.438 11.882 7.892  1.00 35.85 ? 166 ASN A CB  1 
ATOM   1290 C  CG  . ASN A 1 171 ? 28.171 13.088 8.480  1.00 37.05 ? 166 ASN A CG  1 
ATOM   1291 O  OD1 . ASN A 1 171 ? 27.677 13.749 9.404  1.00 38.02 ? 166 ASN A OD1 1 
ATOM   1292 N  ND2 . ASN A 1 171 ? 29.366 13.354 7.970  1.00 38.26 ? 166 ASN A ND2 1 
ATOM   1293 N  N   . PRO A 1 172 ? 28.147 11.019 11.135 1.00 35.81 ? 167 PRO A N   1 
ATOM   1294 C  CA  . PRO A 1 172 ? 27.770 11.143 12.557 1.00 33.65 ? 167 PRO A CA  1 
ATOM   1295 C  C   . PRO A 1 172 ? 27.068 12.453 12.899 1.00 34.01 ? 167 PRO A C   1 
ATOM   1296 O  O   . PRO A 1 172 ? 26.219 12.464 13.799 1.00 34.68 ? 167 PRO A O   1 
ATOM   1297 C  CB  . PRO A 1 172 ? 29.108 10.990 13.302 1.00 36.74 ? 167 PRO A CB  1 
ATOM   1298 C  CG  . PRO A 1 172 ? 30.186 11.272 12.304 1.00 40.51 ? 167 PRO A CG  1 
ATOM   1299 C  CD  . PRO A 1 172 ? 29.608 10.946 10.921 1.00 34.64 ? 167 PRO A CD  1 
ATOM   1300 N  N   . ILE A 1 173 ? 27.372 13.554 12.201 1.00 33.19 ? 168 ILE A N   1 
ATOM   1301 C  CA  . ILE A 1 173 ? 26.621 14.786 12.415 1.00 33.94 ? 168 ILE A CA  1 
ATOM   1302 C  C   . ILE A 1 173 ? 25.177 14.616 11.948 1.00 34.15 ? 168 ILE A C   1 
ATOM   1303 O  O   . ILE A 1 173 ? 24.227 15.010 12.636 1.00 35.21 ? 168 ILE A O   1 
ATOM   1304 C  CB  . ILE A 1 173 ? 27.343 15.960 11.715 1.00 33.51 ? 168 ILE A CB  1 
ATOM   1305 C  CG1 . ILE A 1 173 ? 28.777 16.057 12.265 1.00 34.32 ? 168 ILE A CG1 1 
ATOM   1306 C  CG2 . ILE A 1 173 ? 26.549 17.294 11.815 1.00 38.37 ? 168 ILE A CG2 1 
ATOM   1307 C  CD1 . ILE A 1 173 ? 29.588 17.166 11.667 1.00 40.54 ? 168 ILE A CD1 1 
ATOM   1308 N  N   . ARG A 1 174 ? 24.984 13.999 10.787 1.00 36.11 ? 169 ARG A N   1 
ATOM   1309 C  CA  . ARG A 1 174 ? 23.626 13.752 10.315 1.00 35.99 ? 169 ARG A CA  1 
ATOM   1310 C  C   . ARG A 1 174 ? 22.871 12.826 11.263 1.00 33.08 ? 169 ARG A C   1 
ATOM   1311 O  O   . ARG A 1 174 ? 21.707 13.072 11.581 1.00 35.41 ? 169 ARG A O   1 
ATOM   1312 C  CB  . ARG A 1 174 ? 23.685 13.174 8.895  1.00 35.11 ? 169 ARG A CB  1 
ATOM   1313 C  CG  . ARG A 1 174 ? 22.399 12.566 8.405  1.00 35.02 ? 169 ARG A CG  1 
ATOM   1314 C  CD  . ARG A 1 174 ? 22.453 12.299 6.871  1.00 38.20 ? 169 ARG A CD  1 
ATOM   1315 N  NE  . ARG A 1 174 ? 21.214 11.655 6.446  1.00 40.68 ? 169 ARG A NE  1 
ATOM   1316 C  CZ  . ARG A 1 174 ? 20.963 11.243 5.208  1.00 45.91 ? 169 ARG A CZ  1 
ATOM   1317 N  NH1 . ARG A 1 174 ? 21.877 11.333 4.252  1.00 39.10 ? 169 ARG A NH1 1 
ATOM   1318 N  NH2 . ARG A 1 174 ? 19.772 10.718 4.928  1.00 44.41 ? 169 ARG A NH2 1 
ATOM   1319 N  N   . LEU A 1 175 ? 23.537 11.780 11.756 1.00 31.68 ? 170 LEU A N   1 
ATOM   1320 C  CA  . LEU A 1 175 ? 22.918 10.860 12.700 1.00 35.40 ? 170 LEU A CA  1 
ATOM   1321 C  C   . LEU A 1 175 ? 22.594 11.570 14.018 1.00 35.93 ? 170 LEU A C   1 
ATOM   1322 O  O   . LEU A 1 175 ? 21.479 11.459 14.553 1.00 34.37 ? 170 LEU A O   1 
ATOM   1323 C  CB  . LEU A 1 175 ? 23.877 9.698  12.936 1.00 33.52 ? 170 LEU A CB  1 
ATOM   1324 C  CG  . LEU A 1 175 ? 24.070 8.699  11.785 1.00 33.91 ? 170 LEU A CG  1 
ATOM   1325 C  CD1 . LEU A 1 175 ? 25.119 7.647  12.185 1.00 33.66 ? 170 LEU A CD1 1 
ATOM   1326 C  CD2 . LEU A 1 175 ? 22.716 8.082  11.527 1.00 34.05 ? 170 LEU A CD2 1 
ATOM   1327 N  N   . GLY A 1 176 ? 23.564 12.307 14.557 1.00 35.07 ? 171 GLY A N   1 
ATOM   1328 C  CA  . GLY A 1 176 ? 23.322 12.978 15.828 1.00 35.20 ? 171 GLY A CA  1 
ATOM   1329 C  C   . GLY A 1 176 ? 22.227 14.021 15.721 1.00 35.18 ? 171 GLY A C   1 
ATOM   1330 O  O   . GLY A 1 176 ? 21.419 14.184 16.639 1.00 36.43 ? 171 GLY A O   1 
ATOM   1331 N  N   . LEU A 1 177 ? 22.195 14.753 14.604 1.00 34.24 ? 172 LEU A N   1 
ATOM   1332 C  CA  . LEU A 1 177 ? 21.094 15.670 14.335 1.00 36.85 ? 172 LEU A CA  1 
ATOM   1333 C  C   . LEU A 1 177 ? 19.745 14.945 14.345 1.00 37.84 ? 172 LEU A C   1 
ATOM   1334 O  O   . LEU A 1 177 ? 18.787 15.408 14.977 1.00 37.57 ? 172 LEU A O   1 
ATOM   1335 C  CB  . LEU A 1 177 ? 21.324 16.372 12.995 1.00 34.08 ? 172 LEU A CB  1 
ATOM   1336 C  CG  . LEU A 1 177 ? 20.084 16.921 12.311 1.00 38.41 ? 172 LEU A CG  1 
ATOM   1337 C  CD1 . LEU A 1 177 ? 19.512 18.106 13.094 1.00 38.82 ? 172 LEU A CD1 1 
ATOM   1338 C  CD2 . LEU A 1 177 ? 20.423 17.348 10.867 1.00 42.64 ? 172 LEU A CD2 1 
ATOM   1339 N  N   . ALA A 1 178 ? 19.644 13.818 13.626 1.00 40.04 ? 173 ALA A N   1 
ATOM   1340 C  CA  . ALA A 1 178 ? 18.367 13.105 13.559 1.00 40.52 ? 173 ALA A CA  1 
ATOM   1341 C  C   . ALA A 1 178 ? 17.983 12.544 14.919 1.00 39.35 ? 173 ALA A C   1 
ATOM   1342 O  O   . ALA A 1 178 ? 16.812 12.595 15.309 1.00 41.28 ? 173 ALA A O   1 
ATOM   1343 C  CB  . ALA A 1 178 ? 18.434 11.981 12.523 1.00 37.52 ? 173 ALA A CB  1 
ATOM   1344 N  N   . LEU A 1 179 ? 18.948 11.969 15.631 1.00 36.98 ? 174 LEU A N   1 
ATOM   1345 C  CA  . LEU A 1 179 ? 18.703 11.582 17.015 1.00 37.49 ? 174 LEU A CA  1 
ATOM   1346 C  C   . LEU A 1 179 ? 18.116 12.749 17.794 1.00 39.45 ? 174 LEU A C   1 
ATOM   1347 O  O   . LEU A 1 179 ? 17.080 12.605 18.449 1.00 39.71 ? 174 LEU A O   1 
ATOM   1348 C  CB  . LEU A 1 179 ? 19.990 11.080 17.673 1.00 35.52 ? 174 LEU A CB  1 
ATOM   1349 C  CG  . LEU A 1 179 ? 19.887 10.718 19.182 1.00 38.38 ? 174 LEU A CG  1 
ATOM   1350 C  CD1 . LEU A 1 179 ? 18.887 9.586  19.438 1.00 40.06 ? 174 LEU A CD1 1 
ATOM   1351 C  CD2 . LEU A 1 179 ? 21.258 10.329 19.716 1.00 37.03 ? 174 LEU A CD2 1 
ATOM   1352 N  N   . ASN A 1 180 ? 18.732 13.939 17.700 1.00 37.76 ? 175 ASN A N   1 
ATOM   1353 C  CA  . ASN A 1 180 ? 18.275 15.024 18.572 1.00 39.91 ? 175 ASN A CA  1 
ATOM   1354 C  C   . ASN A 1 180 ? 16.942 15.591 18.106 1.00 42.94 ? 175 ASN A C   1 
ATOM   1355 O  O   . ASN A 1 180 ? 16.120 16.004 18.933 1.00 39.05 ? 175 ASN A O   1 
ATOM   1356 C  CB  . ASN A 1 180 ? 19.314 16.154 18.659 1.00 36.24 ? 175 ASN A CB  1 
ATOM   1357 C  CG  . ASN A 1 180 ? 20.467 15.801 19.567 1.00 39.95 ? 175 ASN A CG  1 
ATOM   1358 O  OD1 . ASN A 1 180 ? 20.603 14.655 19.982 1.00 36.49 ? 175 ASN A OD1 1 
ATOM   1359 N  ND2 . ASN A 1 180 ? 21.318 16.779 19.866 1.00 35.75 ? 175 ASN A ND2 1 
ATOM   1360 N  N   . PHE A 1 181 ? 16.699 15.603 16.791 1.00 41.27 ? 176 PHE A N   1 
ATOM   1361 C  CA  . PHE A 1 181 ? 15.391 16.014 16.300 1.00 43.15 ? 176 PHE A CA  1 
ATOM   1362 C  C   . PHE A 1 181 ? 14.299 15.054 16.776 1.00 39.25 ? 176 PHE A C   1 
ATOM   1363 O  O   . PHE A 1 181 ? 13.200 15.488 17.139 1.00 42.45 ? 176 PHE A O   1 
ATOM   1364 C  CB  . PHE A 1 181 ? 15.432 16.114 14.767 1.00 42.36 ? 176 PHE A CB  1 
ATOM   1365 C  CG  . PHE A 1 181 ? 14.346 16.966 14.175 1.00 43.42 ? 176 PHE A CG  1 
ATOM   1366 C  CD1 . PHE A 1 181 ? 14.033 16.859 12.821 1.00 47.18 ? 176 PHE A CD1 1 
ATOM   1367 C  CD2 . PHE A 1 181 ? 13.621 17.858 14.956 1.00 46.31 ? 176 PHE A CD2 1 
ATOM   1368 C  CE1 . PHE A 1 181 ? 13.036 17.649 12.252 1.00 49.00 ? 176 PHE A CE1 1 
ATOM   1369 C  CE2 . PHE A 1 181 ? 12.612 18.653 14.398 1.00 47.78 ? 176 PHE A CE2 1 
ATOM   1370 C  CZ  . PHE A 1 181 ? 12.319 18.542 13.039 1.00 49.15 ? 176 PHE A CZ  1 
ATOM   1371 N  N   . SER A 1 182 ? 14.574 13.752 16.776 1.00 43.80 ? 177 SER A N   1 
ATOM   1372 C  CA  . SER A 1 182 ? 13.554 12.809 17.227 1.00 48.99 ? 177 SER A CA  1 
ATOM   1373 C  C   . SER A 1 182 ? 13.261 12.981 18.720 1.00 47.60 ? 177 SER A C   1 
ATOM   1374 O  O   . SER A 1 182 ? 12.121 12.778 19.155 1.00 45.81 ? 177 SER A O   1 
ATOM   1375 C  CB  . SER A 1 182 ? 13.964 11.368 16.891 1.00 48.88 ? 177 SER A CB  1 
ATOM   1376 O  OG  . SER A 1 182 ? 15.014 10.852 17.700 1.00 49.36 ? 177 SER A OG  1 
ATOM   1377 N  N   . VAL A 1 183 ? 14.266 13.373 19.506 1.00 45.27 ? 178 VAL A N   1 
ATOM   1378 C  CA  . VAL A 1 183 ? 14.044 13.665 20.923 1.00 42.41 ? 178 VAL A CA  1 
ATOM   1379 C  C   . VAL A 1 183 ? 13.168 14.900 21.080 1.00 44.09 ? 178 VAL A C   1 
ATOM   1380 O  O   . VAL A 1 183 ? 12.245 14.922 21.904 1.00 47.85 ? 178 VAL A O   1 
ATOM   1381 C  CB  . VAL A 1 183 ? 15.398 13.821 21.639 1.00 44.68 ? 178 VAL A CB  1 
ATOM   1382 C  CG1 . VAL A 1 183 ? 15.188 14.336 23.089 1.00 45.62 ? 178 VAL A CG1 1 
ATOM   1383 C  CG2 . VAL A 1 183 ? 16.130 12.505 21.660 1.00 42.96 ? 178 VAL A CG2 1 
ATOM   1384 N  N   . PHE A 1 184 ? 13.453 15.953 20.303 1.00 44.26 ? 179 PHE A N   1 
ATOM   1385 C  CA  . PHE A 1 184 ? 12.555 17.098 20.182 1.00 48.08 ? 179 PHE A CA  1 
ATOM   1386 C  C   . PHE A 1 184 ? 11.118 16.651 19.931 1.00 50.70 ? 179 PHE A C   1 
ATOM   1387 O  O   . PHE A 1 184 ? 10.201 17.034 20.665 1.00 51.65 ? 179 PHE A O   1 
ATOM   1388 C  CB  . PHE A 1 184 ? 13.031 18.033 19.062 1.00 41.09 ? 179 PHE A CB  1 
ATOM   1389 C  CG  . PHE A 1 184 ? 12.089 19.164 18.768 1.00 45.34 ? 179 PHE A CG  1 
ATOM   1390 C  CD1 . PHE A 1 184 ? 12.133 20.334 19.503 1.00 45.93 ? 179 PHE A CD1 1 
ATOM   1391 C  CD2 . PHE A 1 184 ? 11.152 19.061 17.737 1.00 51.05 ? 179 PHE A CD2 1 
ATOM   1392 C  CE1 . PHE A 1 184 ? 11.268 21.401 19.225 1.00 49.16 ? 179 PHE A CE1 1 
ATOM   1393 C  CE2 . PHE A 1 184 ? 10.281 20.117 17.456 1.00 52.10 ? 179 PHE A CE2 1 
ATOM   1394 C  CZ  . PHE A 1 184 ? 10.339 21.288 18.208 1.00 50.95 ? 179 PHE A CZ  1 
ATOM   1395 N  N   . HIS A 1 185 ? 10.899 15.840 18.888 1.00 50.66 ? 180 HIS A N   1 
ATOM   1396 C  CA  . HIS A 1 185 ? 9.541  15.388 18.586 1.00 51.31 ? 180 HIS A CA  1 
ATOM   1397 C  C   . HIS A 1 185 ? 8.900  14.721 19.797 1.00 51.71 ? 180 HIS A C   1 
ATOM   1398 O  O   . HIS A 1 185 ? 7.759  15.020 20.162 1.00 53.88 ? 180 HIS A O   1 
ATOM   1399 C  CB  . HIS A 1 185 ? 9.545  14.421 17.399 1.00 50.74 ? 180 HIS A CB  1 
ATOM   1400 C  CG  . HIS A 1 185 ? 9.815  15.074 16.078 1.00 50.60 ? 180 HIS A CG  1 
ATOM   1401 N  ND1 . HIS A 1 185 ? 9.270  16.287 15.716 1.00 49.39 ? 180 HIS A ND1 1 
ATOM   1402 C  CD2 . HIS A 1 185 ? 10.552 14.660 15.017 1.00 49.38 ? 180 HIS A CD2 1 
ATOM   1403 C  CE1 . HIS A 1 185 ? 9.670  16.599 14.496 1.00 49.76 ? 180 HIS A CE1 1 
ATOM   1404 N  NE2 . HIS A 1 185 ? 10.453 15.632 14.052 1.00 48.28 ? 180 HIS A NE2 1 
ATOM   1405 N  N   . TYR A 1 186 ? 9.627  13.816 20.436 1.00 48.52 ? 181 TYR A N   1 
ATOM   1406 C  CA  . TYR A 1 186 ? 9.032  13.023 21.500 1.00 53.35 ? 181 TYR A CA  1 
ATOM   1407 C  C   . TYR A 1 186 ? 8.834  13.861 22.758 1.00 56.85 ? 181 TYR A C   1 
ATOM   1408 O  O   . TYR A 1 186 ? 7.720  13.941 23.296 1.00 56.39 ? 181 TYR A O   1 
ATOM   1409 C  CB  . TYR A 1 186 ? 9.910  11.806 21.781 1.00 52.18 ? 181 TYR A CB  1 
ATOM   1410 C  CG  . TYR A 1 186 ? 9.261  10.763 22.660 1.00 55.92 ? 181 TYR A CG  1 
ATOM   1411 C  CD1 . TYR A 1 186 ? 9.299  10.873 24.038 1.00 54.86 ? 181 TYR A CD1 1 
ATOM   1412 C  CD2 . TYR A 1 186 ? 8.606  9.669  22.104 1.00 57.25 ? 181 TYR A CD2 1 
ATOM   1413 C  CE1 . TYR A 1 186 ? 8.708  9.924  24.844 1.00 58.53 ? 181 TYR A CE1 1 
ATOM   1414 C  CE2 . TYR A 1 186 ? 8.008  8.716  22.899 1.00 60.79 ? 181 TYR A CE2 1 
ATOM   1415 C  CZ  . TYR A 1 186 ? 8.066  8.848  24.267 1.00 58.68 ? 181 TYR A CZ  1 
ATOM   1416 O  OH  . TYR A 1 186 ? 7.485  7.899  25.062 1.00 65.38 ? 181 TYR A OH  1 
ATOM   1417 N  N   . GLU A 1 187 ? 9.899  14.529 23.213 1.00 52.58 ? 182 GLU A N   1 
ATOM   1418 C  CA  . GLU A 1 187 ? 9.911  15.150 24.536 1.00 54.38 ? 182 GLU A CA  1 
ATOM   1419 C  C   . GLU A 1 187 ? 9.373  16.571 24.532 1.00 52.81 ? 182 GLU A C   1 
ATOM   1420 O  O   . GLU A 1 187 ? 8.837  17.015 25.550 1.00 58.91 ? 182 GLU A O   1 
ATOM   1421 C  CB  . GLU A 1 187 ? 11.335 15.146 25.107 1.00 49.01 ? 182 GLU A CB  1 
ATOM   1422 C  CG  . GLU A 1 187 ? 11.964 13.764 25.281 1.00 48.66 ? 182 GLU A CG  1 
ATOM   1423 C  CD  . GLU A 1 187 ? 11.373 12.946 26.426 1.00 56.31 ? 182 GLU A CD  1 
ATOM   1424 O  OE1 . GLU A 1 187 ? 10.615 13.520 27.237 1.00 60.61 ? 182 GLU A OE1 1 
ATOM   1425 O  OE2 . GLU A 1 187 ? 11.675 11.730 26.526 1.00 55.21 ? 182 GLU A OE2 1 
ATOM   1426 N  N   . ILE A 1 188 ? 9.492  17.297 23.423 1.00 50.96 ? 183 ILE A N   1 
ATOM   1427 C  CA  . ILE A 1 188 ? 9.169  18.712 23.373 1.00 53.55 ? 183 ILE A CA  1 
ATOM   1428 C  C   . ILE A 1 188 ? 7.889  18.973 22.584 1.00 58.46 ? 183 ILE A C   1 
ATOM   1429 O  O   . ILE A 1 188 ? 7.083  19.827 22.964 1.00 55.26 ? 183 ILE A O   1 
ATOM   1430 C  CB  . ILE A 1 188 ? 10.348 19.514 22.769 1.00 54.01 ? 183 ILE A CB  1 
ATOM   1431 C  CG1 . ILE A 1 188 ? 11.647 19.264 23.552 1.00 53.14 ? 183 ILE A CG1 1 
ATOM   1432 C  CG2 . ILE A 1 188 ? 10.012 20.989 22.691 1.00 49.26 ? 183 ILE A CG2 1 
ATOM   1433 C  CD1 . ILE A 1 188 ? 11.686 19.917 24.899 1.00 49.54 ? 183 ILE A CD1 1 
ATOM   1434 N  N   . ALA A 1 189 ? 7.707  18.283 21.462 1.00 55.72 ? 184 ALA A N   1 
ATOM   1435 C  CA  . ALA A 1 189 ? 6.621  18.582 20.539 1.00 59.77 ? 184 ALA A CA  1 
ATOM   1436 C  C   . ALA A 1 189 ? 5.427  17.653 20.696 1.00 61.72 ? 184 ALA A C   1 
ATOM   1437 O  O   . ALA A 1 189 ? 4.455  17.790 19.946 1.00 67.31 ? 184 ALA A O   1 
ATOM   1438 C  CB  . ALA A 1 189 ? 7.124  18.529 19.092 1.00 53.55 ? 184 ALA A CB  1 
ATOM   1439 N  N   . ASN A 1 190 ? 5.481  16.707 21.633 1.00 61.32 ? 185 ASN A N   1 
ATOM   1440 C  CA  . ASN A 1 190 ? 4.373  15.786 21.878 1.00 66.12 ? 185 ASN A CA  1 
ATOM   1441 C  C   . ASN A 1 190 ? 3.961  15.027 20.619 1.00 68.50 ? 185 ASN A C   1 
ATOM   1442 O  O   . ASN A 1 190 ? 2.773  14.780 20.388 1.00 70.30 ? 185 ASN A O   1 
ATOM   1443 C  CB  . ASN A 1 190 ? 3.174  16.525 22.465 1.00 71.20 ? 185 ASN A CB  1 
ATOM   1444 C  CG  . ASN A 1 190 ? 2.689  15.898 23.730 1.00 76.29 ? 185 ASN A CG  1 
ATOM   1445 O  OD1 . ASN A 1 190 ? 3.095  14.780 24.070 1.00 76.80 ? 185 ASN A OD1 1 
ATOM   1446 N  ND2 . ASN A 1 190 ? 1.806  16.599 24.444 1.00 79.76 ? 185 ASN A ND2 1 
ATOM   1447 N  N   . SER A 1 191 ? 4.944  14.651 19.797 1.00 65.22 ? 186 SER A N   1 
ATOM   1448 C  CA  . SER A 1 191 ? 4.711  13.966 18.526 1.00 60.59 ? 186 SER A CA  1 
ATOM   1449 C  C   . SER A 1 191 ? 5.435  12.628 18.534 1.00 60.82 ? 186 SER A C   1 
ATOM   1450 O  O   . SER A 1 191 ? 6.381  12.424 17.764 1.00 62.26 ? 186 SER A O   1 
ATOM   1451 C  CB  . SER A 1 191 ? 5.181  14.806 17.341 1.00 60.81 ? 186 SER A CB  1 
ATOM   1452 O  OG  . SER A 1 191 ? 4.543  16.064 17.337 1.00 65.85 ? 186 SER A OG  1 
ATOM   1453 N  N   . PRO A 1 192 ? 5.003  11.689 19.378 1.00 60.87 ? 187 PRO A N   1 
ATOM   1454 C  CA  . PRO A 1 192 ? 5.731  10.411 19.471 1.00 62.42 ? 187 PRO A CA  1 
ATOM   1455 C  C   . PRO A 1 192 ? 5.861  9.710  18.132 1.00 61.81 ? 187 PRO A C   1 
ATOM   1456 O  O   . PRO A 1 192 ? 6.915  9.147  17.821 1.00 59.52 ? 187 PRO A O   1 
ATOM   1457 C  CB  . PRO A 1 192 ? 4.894  9.582  20.461 1.00 62.73 ? 187 PRO A CB  1 
ATOM   1458 C  CG  . PRO A 1 192 ? 3.867  10.507 21.028 1.00 64.22 ? 187 PRO A CG  1 
ATOM   1459 C  CD  . PRO A 1 192 ? 3.743  11.692 20.141 1.00 63.27 ? 187 PRO A CD  1 
ATOM   1460 N  N   . GLU A 1 193 ? 4.810  9.749  17.319 1.00 63.65 ? 188 GLU A N   1 
ATOM   1461 C  CA  . GLU A 1 193 ? 4.844  9.074  16.028 1.00 64.25 ? 188 GLU A CA  1 
ATOM   1462 C  C   . GLU A 1 193 ? 5.871  9.702  15.085 1.00 59.51 ? 188 GLU A C   1 
ATOM   1463 O  O   . GLU A 1 193 ? 6.608  8.975  14.409 1.00 58.69 ? 188 GLU A O   1 
ATOM   1464 C  CB  . GLU A 1 193 ? 3.427  9.040  15.435 1.00 64.81 ? 188 GLU A CB  1 
ATOM   1465 C  CG  . GLU A 1 193 ? 2.808  10.387 15.034 1.00 66.85 ? 188 GLU A CG  1 
ATOM   1466 C  CD  . GLU A 1 193 ? 2.568  11.330 16.223 1.00 70.09 ? 188 GLU A CD  1 
ATOM   1467 O  OE1 . GLU A 1 193 ? 1.786  10.961 17.140 1.00 69.60 ? 188 GLU A OE1 1 
ATOM   1468 O  OE2 . GLU A 1 193 ? 3.149  12.445 16.229 1.00 68.10 ? 188 GLU A OE2 1 
ATOM   1469 N  N   . GLU A 1 194 ? 5.962  11.039 15.039 1.00 61.56 ? 189 GLU A N   1 
ATOM   1470 C  CA  . GLU A 1 194 ? 7.039  11.678 14.278 1.00 58.70 ? 189 GLU A CA  1 
ATOM   1471 C  C   . GLU A 1 194 ? 8.410  11.250 14.782 1.00 58.35 ? 189 GLU A C   1 
ATOM   1472 O  O   . GLU A 1 194 ? 9.351  11.103 13.992 1.00 55.03 ? 189 GLU A O   1 
ATOM   1473 C  CB  . GLU A 1 194 ? 6.942  13.199 14.354 1.00 58.08 ? 189 GLU A CB  1 
ATOM   1474 C  CG  . GLU A 1 194 ? 5.627  13.835 13.977 1.00 64.75 ? 189 GLU A CG  1 
ATOM   1475 C  CD  . GLU A 1 194 ? 5.841  15.071 13.103 1.00 69.92 ? 189 GLU A CD  1 
ATOM   1476 O  OE1 . GLU A 1 194 ? 4.854  15.769 12.777 1.00 75.07 ? 189 GLU A OE1 1 
ATOM   1477 O  OE2 . GLU A 1 194 ? 7.009  15.352 12.748 1.00 70.15 ? 189 GLU A OE2 1 
ATOM   1478 N  N   . ALA A 1 195 ? 8.550  11.094 16.103 1.00 56.89 ? 190 ALA A N   1 
ATOM   1479 C  CA  . ALA A 1 195 ? 9.827  10.718 16.701 1.00 55.01 ? 190 ALA A CA  1 
ATOM   1480 C  C   . ALA A 1 195 ? 10.207 9.290  16.343 1.00 54.13 ? 190 ALA A C   1 
ATOM   1481 O  O   . ALA A 1 195 ? 11.336 9.032  15.911 1.00 52.23 ? 190 ALA A O   1 
ATOM   1482 C  CB  . ALA A 1 195 ? 9.760  10.884 18.226 1.00 52.35 ? 190 ALA A CB  1 
ATOM   1483 N  N   . ILE A 1 196 ? 9.292  8.336  16.560 1.00 53.19 ? 191 ILE A N   1 
ATOM   1484 C  CA  . ILE A 1 196 ? 9.550  6.954  16.155 1.00 55.70 ? 191 ILE A CA  1 
ATOM   1485 C  C   . ILE A 1 196 ? 9.799  6.866  14.659 1.00 51.29 ? 191 ILE A C   1 
ATOM   1486 O  O   . ILE A 1 196 ? 10.701 6.150  14.213 1.00 50.54 ? 191 ILE A O   1 
ATOM   1487 C  CB  . ILE A 1 196 ? 8.406  6.021  16.612 1.00 56.21 ? 191 ILE A CB  1 
ATOM   1488 C  CG1 . ILE A 1 196 ? 7.918  6.414  18.019 1.00 58.54 ? 191 ILE A CG1 1 
ATOM   1489 C  CG2 . ILE A 1 196 ? 8.789  4.547  16.460 1.00 57.53 ? 191 ILE A CG2 1 
ATOM   1490 C  CD1 . ILE A 1 196 ? 6.602  5.796  18.450 1.00 59.14 ? 191 ILE A CD1 1 
ATOM   1491 N  N   . SER A 1 197 ? 9.028  7.611  13.868 1.00 52.28 ? 192 SER A N   1 
ATOM   1492 C  CA  . SER A 1 197 ? 9.213  7.593  12.420 1.00 54.24 ? 192 SER A CA  1 
ATOM   1493 C  C   . SER A 1 197 ? 10.606 8.078  12.046 1.00 53.04 ? 192 SER A C   1 
ATOM   1494 O  O   . SER A 1 197 ? 11.337 7.398  11.315 1.00 54.19 ? 192 SER A O   1 
ATOM   1495 C  CB  . SER A 1 197 ? 8.142  8.451  11.743 1.00 53.67 ? 192 SER A CB  1 
ATOM   1496 O  OG  . SER A 1 197 ? 8.606  8.989  10.515 1.00 65.66 ? 192 SER A OG  1 
ATOM   1497 N  N   . LEU A 1 198 ? 10.999 9.254  12.547 1.00 51.25 ? 193 LEU A N   1 
ATOM   1498 C  CA  . LEU A 1 198 ? 12.305 9.788  12.186 1.00 47.79 ? 193 LEU A CA  1 
ATOM   1499 C  C   . LEU A 1 198 ? 13.420 8.865  12.657 1.00 46.72 ? 193 LEU A C   1 
ATOM   1500 O  O   . LEU A 1 198 ? 14.365 8.588  11.903 1.00 46.39 ? 193 LEU A O   1 
ATOM   1501 C  CB  . LEU A 1 198 ? 12.486 11.195 12.752 1.00 47.43 ? 193 LEU A CB  1 
ATOM   1502 C  CG  . LEU A 1 198 ? 13.845 11.876 12.529 1.00 44.48 ? 193 LEU A CG  1 
ATOM   1503 C  CD1 . LEU A 1 198 ? 14.214 12.030 11.068 1.00 45.89 ? 193 LEU A CD1 1 
ATOM   1504 C  CD2 . LEU A 1 198 ? 13.787 13.241 13.185 1.00 44.39 ? 193 LEU A CD2 1 
ATOM   1505 N  N   . ALA A 1 199 ? 13.325 8.364  13.894 1.00 47.44 ? 194 ALA A N   1 
ATOM   1506 C  CA  . ALA A 1 199 ? 14.386 7.517  14.416 1.00 42.15 ? 194 ALA A CA  1 
ATOM   1507 C  C   . ALA A 1 199 ? 14.472 6.210  13.638 1.00 47.86 ? 194 ALA A C   1 
ATOM   1508 O  O   . ALA A 1 199 ? 15.569 5.692  13.395 1.00 45.77 ? 194 ALA A O   1 
ATOM   1509 C  CB  . ALA A 1 199 ? 14.161 7.247  15.901 1.00 48.72 ? 194 ALA A CB  1 
ATOM   1510 N  N   . LYS A 1 200 ? 13.320 5.649  13.270 1.00 49.61 ? 195 LYS A N   1 
ATOM   1511 C  CA  . LYS A 1 200 ? 13.295 4.405  12.501 1.00 51.46 ? 195 LYS A CA  1 
ATOM   1512 C  C   . LYS A 1 200 ? 13.888 4.606  11.107 1.00 45.83 ? 195 LYS A C   1 
ATOM   1513 O  O   . LYS A 1 200 ? 14.785 3.859  10.693 1.00 50.06 ? 195 LYS A O   1 
ATOM   1514 C  CB  . LYS A 1 200 ? 11.856 3.882  12.429 1.00 52.38 ? 195 LYS A CB  1 
ATOM   1515 C  CG  . LYS A 1 200 ? 11.575 2.846  11.366 1.00 52.23 ? 195 LYS A CG  1 
ATOM   1516 C  CD  . LYS A 1 200 ? 11.472 1.469  11.985 1.00 57.17 ? 195 LYS A CD  1 
ATOM   1517 C  CE  . LYS A 1 200 ? 11.134 0.410  10.952 1.00 56.76 ? 195 LYS A CE  1 
ATOM   1518 N  NZ  . LYS A 1 200 ? 11.893 -0.825 11.290 1.00 59.54 ? 195 LYS A NZ  1 
ATOM   1519 N  N   . THR A 1 201 ? 13.404 5.611  10.372 1.00 48.17 ? 196 THR A N   1 
ATOM   1520 C  CA  . THR A 1 201 ? 13.987 5.936  9.069  1.00 48.01 ? 196 THR A CA  1 
ATOM   1521 C  C   . THR A 1 201 ? 15.497 6.132  9.163  1.00 49.13 ? 196 THR A C   1 
ATOM   1522 O  O   . THR A 1 201 ? 16.257 5.617  8.336  1.00 46.53 ? 196 THR A O   1 
ATOM   1523 C  CB  . THR A 1 201 ? 13.342 7.194  8.472  1.00 50.29 ? 196 THR A CB  1 
ATOM   1524 O  OG1 . THR A 1 201 ? 11.916 7.072  8.455  1.00 54.69 ? 196 THR A OG1 1 
ATOM   1525 C  CG2 . THR A 1 201 ? 13.887 7.484  7.068  1.00 54.10 ? 196 THR A CG2 1 
ATOM   1526 N  N   . THR A 1 202 ? 15.948 6.893  10.167 1.00 47.35 ? 197 THR A N   1 
ATOM   1527 C  CA  . THR A 1 202 ? 17.370 7.202  10.269 1.00 43.41 ? 197 THR A CA  1 
ATOM   1528 C  C   . THR A 1 202 ? 18.195 5.953  10.506 1.00 38.54 ? 197 THR A C   1 
ATOM   1529 O  O   . THR A 1 202 ? 19.248 5.759  9.884  1.00 38.30 ? 197 THR A O   1 
ATOM   1530 C  CB  . THR A 1 202 ? 17.608 8.206  11.398 1.00 38.97 ? 197 THR A CB  1 
ATOM   1531 O  OG1 . THR A 1 202 ? 16.790 9.355  11.172 1.00 40.43 ? 197 THR A OG1 1 
ATOM   1532 C  CG2 . THR A 1 202 ? 19.063 8.594  11.400 1.00 38.07 ? 197 THR A CG2 1 
ATOM   1533 N  N   . PHE A 1 203 ? 17.762 5.108  11.439 1.00 39.25 ? 198 PHE A N   1 
ATOM   1534 C  CA  . PHE A 1 203 ? 18.496 3.882  11.692 1.00 38.70 ? 198 PHE A CA  1 
ATOM   1535 C  C   . PHE A 1 203 ? 18.484 2.986  10.450 1.00 42.33 ? 198 PHE A C   1 
ATOM   1536 O  O   . PHE A 1 203 ? 19.524 2.479  10.012 1.00 39.53 ? 198 PHE A O   1 
ATOM   1537 C  CB  . PHE A 1 203 ? 17.899 3.149  12.898 1.00 42.09 ? 198 PHE A CB  1 
ATOM   1538 C  CG  . PHE A 1 203 ? 18.586 1.866  13.216 1.00 39.86 ? 198 PHE A CG  1 
ATOM   1539 C  CD1 . PHE A 1 203 ? 19.665 1.839  14.080 1.00 41.86 ? 198 PHE A CD1 1 
ATOM   1540 C  CD2 . PHE A 1 203 ? 18.160 0.673  12.650 1.00 41.83 ? 198 PHE A CD2 1 
ATOM   1541 C  CE1 . PHE A 1 203 ? 20.314 0.645  14.371 1.00 45.08 ? 198 PHE A CE1 1 
ATOM   1542 C  CE2 . PHE A 1 203 ? 18.806 -0.524 12.939 1.00 47.95 ? 198 PHE A CE2 1 
ATOM   1543 C  CZ  . PHE A 1 203 ? 19.885 -0.540 13.797 1.00 49.23 ? 198 PHE A CZ  1 
ATOM   1544 N  N   . ASP A 1 204 ? 17.310 2.796  9.861  1.00 44.00 ? 199 ASP A N   1 
ATOM   1545 C  CA  . ASP A 1 204 ? 17.223 1.864  8.739  1.00 44.30 ? 199 ASP A CA  1 
ATOM   1546 C  C   . ASP A 1 204 ? 18.039 2.352  7.549  1.00 41.68 ? 199 ASP A C   1 
ATOM   1547 O  O   . ASP A 1 204 ? 18.689 1.552  6.873  1.00 45.51 ? 199 ASP A O   1 
ATOM   1548 C  CB  . ASP A 1 204 ? 15.763 1.659  8.354  1.00 45.04 ? 199 ASP A CB  1 
ATOM   1549 C  CG  . ASP A 1 204 ? 15.019 0.801  9.363  1.00 47.43 ? 199 ASP A CG  1 
ATOM   1550 O  OD1 . ASP A 1 204 ? 15.661 0.081  10.171 1.00 45.83 ? 199 ASP A OD1 1 
ATOM   1551 O  OD2 . ASP A 1 204 ? 13.781 0.881  9.358  1.00 51.12 ? 199 ASP A OD2 1 
ATOM   1552 N  N   . GLU A 1 205 ? 18.035 3.655  7.294  1.00 44.03 ? 200 GLU A N   1 
ATOM   1553 C  CA  . GLU A 1 205 ? 18.794 4.172  6.159  1.00 45.51 ? 200 GLU A CA  1 
ATOM   1554 C  C   . GLU A 1 205 ? 20.298 4.090  6.403  1.00 44.94 ? 200 GLU A C   1 
ATOM   1555 O  O   . GLU A 1 205 ? 21.062 3.782  5.481  1.00 40.43 ? 200 GLU A O   1 
ATOM   1556 C  CB  . GLU A 1 205 ? 18.334 5.586  5.833  1.00 45.79 ? 200 GLU A CB  1 
ATOM   1557 C  CG  . GLU A 1 205 ? 16.932 5.558  5.209  1.00 51.57 ? 200 GLU A CG  1 
ATOM   1558 C  CD  . GLU A 1 205 ? 16.461 6.883  4.671  1.00 56.37 ? 200 GLU A CD  1 
ATOM   1559 O  OE1 . GLU A 1 205 ? 17.176 7.899  4.862  1.00 56.88 ? 200 GLU A OE1 1 
ATOM   1560 O  OE2 . GLU A 1 205 ? 15.381 6.909  4.019  1.00 55.98 ? 200 GLU A OE2 1 
ATOM   1561 N  N   . ALA A 1 206 ? 20.753 4.335  7.641  1.00 38.06 ? 201 ALA A N   1 
ATOM   1562 C  CA  . ALA A 1 206 ? 22.165 4.116  7.943  1.00 38.21 ? 201 ALA A CA  1 
ATOM   1563 C  C   . ALA A 1 206 ? 22.540 2.662  7.731  1.00 37.88 ? 201 ALA A C   1 
ATOM   1564 O  O   . ALA A 1 206 ? 23.653 2.352  7.277  1.00 39.36 ? 201 ALA A O   1 
ATOM   1565 C  CB  . ALA A 1 206 ? 22.476 4.525  9.408  1.00 35.96 ? 201 ALA A CB  1 
ATOM   1566 N  N   . MET A 1 207 ? 21.643 1.745  8.114  1.00 36.50 ? 202 MET A N   1 
ATOM   1567 C  CA  . MET A 1 207 ? 21.959 0.330  8.038  1.00 35.75 ? 202 MET A CA  1 
ATOM   1568 C  C   . MET A 1 207 ? 21.982 -0.077 6.557  1.00 39.81 ? 202 MET A C   1 
ATOM   1569 O  O   . MET A 1 207 ? 22.856 -0.819 6.104  1.00 37.68 ? 202 MET A O   1 
ATOM   1570 C  CB  . MET A 1 207 ? 20.867 -0.446 8.792  1.00 38.40 ? 202 MET A CB  1 
ATOM   1571 C  CG  . MET A 1 207 ? 21.221 -0.816 10.271 1.00 40.22 ? 202 MET A CG  1 
ATOM   1572 S  SD  . MET A 1 207 ? 22.755 -1.540 10.796 1.00 48.93 ? 202 MET A SD  1 
ATOM   1573 C  CE  . MET A 1 207 ? 22.318 -3.274 10.846 1.00 51.44 ? 202 MET A CE  1 
ATOM   1574 N  N   . ALA A 1 208 ? 21.038 0.467  5.799  1.00 37.56 ? 203 ALA A N   1 
ATOM   1575 C  CA  . ALA A 1 208 ? 20.949 0.170  4.368  1.00 45.32 ? 203 ALA A CA  1 
ATOM   1576 C  C   . ALA A 1 208 ? 22.190 0.644  3.616  1.00 43.65 ? 203 ALA A C   1 
ATOM   1577 O  O   . ALA A 1 208 ? 22.587 0.029  2.631  1.00 41.33 ? 203 ALA A O   1 
ATOM   1578 C  CB  . ALA A 1 208 ? 19.695 0.814  3.789  1.00 39.71 ? 203 ALA A CB  1 
ATOM   1579 N  N   . ASP A 1 209 ? 22.830 1.717  4.075  1.00 38.17 ? 204 ASP A N   1 
ATOM   1580 C  CA  . ASP A 1 209 ? 24.035 2.210  3.417  1.00 39.76 ? 204 ASP A CA  1 
ATOM   1581 C  C   . ASP A 1 209 ? 25.209 2.175  4.400  1.00 37.99 ? 204 ASP A C   1 
ATOM   1582 O  O   . ASP A 1 209 ? 26.004 3.126  4.474  1.00 38.01 ? 204 ASP A O   1 
ATOM   1583 C  CB  . ASP A 1 209 ? 23.798 3.617  2.847  1.00 34.24 ? 204 ASP A CB  1 
ATOM   1584 C  CG  . ASP A 1 209 ? 23.019 3.610  1.534  1.00 41.49 ? 204 ASP A CG  1 
ATOM   1585 O  OD1 . ASP A 1 209 ? 23.187 2.677  0.739  1.00 41.63 ? 204 ASP A OD1 1 
ATOM   1586 O  OD2 . ASP A 1 209 ? 22.212 4.523  1.294  1.00 42.93 ? 204 ASP A OD2 1 
ATOM   1587 N  N   . LEU A 1 210 ? 25.345 1.042  5.101  1.00 38.93 ? 205 LEU A N   1 
ATOM   1588 C  CA  . LEU A 1 210 ? 26.387 0.859  6.114  1.00 37.57 ? 205 LEU A CA  1 
ATOM   1589 C  C   . LEU A 1 210 ? 27.784 1.010  5.539  1.00 38.62 ? 205 LEU A C   1 
ATOM   1590 O  O   . LEU A 1 210 ? 28.690 1.475  6.229  1.00 35.19 ? 205 LEU A O   1 
ATOM   1591 C  CB  . LEU A 1 210 ? 26.245 -0.518 6.769  1.00 39.24 ? 205 LEU A CB  1 
ATOM   1592 C  CG  . LEU A 1 210 ? 27.097 -0.725 8.016  1.00 40.69 ? 205 LEU A CG  1 
ATOM   1593 C  CD1 . LEU A 1 210 ? 26.621 0.231  9.122  1.00 37.38 ? 205 LEU A CD1 1 
ATOM   1594 C  CD2 . LEU A 1 210 ? 27.121 -2.217 8.462  1.00 43.13 ? 205 LEU A CD2 1 
ATOM   1595 N  N   . HIS A 1 211 ? 27.978 0.651  4.261  1.00 37.19 ? 206 HIS A N   1 
ATOM   1596 C  CA  . HIS A 1 211 ? 29.278 0.778  3.609  1.00 35.72 ? 206 HIS A CA  1 
ATOM   1597 C  C   . HIS A 1 211 ? 29.780 2.232  3.532  1.00 33.21 ? 206 HIS A C   1 
ATOM   1598 O  O   . HIS A 1 211 ? 30.939 2.428  3.156  1.00 35.03 ? 206 HIS A O   1 
ATOM   1599 C  CB  . HIS A 1 211 ? 29.172 0.245  2.161  1.00 34.57 ? 206 HIS A CB  1 
ATOM   1600 C  CG  . HIS A 1 211 ? 28.262 1.080  1.315  1.00 38.06 ? 206 HIS A CG  1 
ATOM   1601 N  ND1 . HIS A 1 211 ? 26.887 0.958  1.354  1.00 39.25 ? 206 HIS A ND1 1 
ATOM   1602 C  CD2 . HIS A 1 211 ? 28.526 2.080  0.438  1.00 39.16 ? 206 HIS A CD2 1 
ATOM   1603 C  CE1 . HIS A 1 211 ? 26.347 1.836  0.525  1.00 35.70 ? 206 HIS A CE1 1 
ATOM   1604 N  NE2 . HIS A 1 211 ? 27.319 2.534  -0.034 1.00 38.25 ? 206 HIS A NE2 1 
ATOM   1605 N  N   . THR A 1 212 ? 28.941 3.232  3.822  1.00 33.00 ? 207 THR A N   1 
ATOM   1606 C  CA  . THR A 1 212 ? 29.369 4.638  3.793  1.00 34.40 ? 207 THR A CA  1 
ATOM   1607 C  C   . THR A 1 212 ? 30.023 5.098  5.100  1.00 39.83 ? 207 THR A C   1 
ATOM   1608 O  O   . THR A 1 212 ? 30.437 6.266  5.192  1.00 35.64 ? 207 THR A O   1 
ATOM   1609 C  CB  . THR A 1 212 ? 28.193 5.575  3.457  1.00 37.43 ? 207 THR A CB  1 
ATOM   1610 O  OG1 . THR A 1 212 ? 27.215 5.586  4.517  1.00 34.73 ? 207 THR A OG1 1 
ATOM   1611 C  CG2 . THR A 1 212 ? 27.506 5.150  2.124  1.00 37.88 ? 207 THR A CG2 1 
ATOM   1612 N  N   . LEU A 1 213 ? 30.109 4.228  6.104  1.00 34.93 ? 208 LEU A N   1 
ATOM   1613 C  CA  . LEU A 1 213 ? 30.872 4.541  7.313  1.00 36.86 ? 208 LEU A CA  1 
ATOM   1614 C  C   . LEU A 1 213 ? 32.278 5.018  6.960  1.00 39.26 ? 208 LEU A C   1 
ATOM   1615 O  O   . LEU A 1 213 ? 32.949 4.465  6.077  1.00 37.21 ? 208 LEU A O   1 
ATOM   1616 C  CB  . LEU A 1 213 ? 30.983 3.306  8.228  1.00 37.04 ? 208 LEU A CB  1 
ATOM   1617 C  CG  . LEU A 1 213 ? 29.774 2.842  9.022  1.00 37.32 ? 208 LEU A CG  1 
ATOM   1618 C  CD1 . LEU A 1 213 ? 30.093 1.498  9.718  1.00 33.60 ? 208 LEU A CD1 1 
ATOM   1619 C  CD2 . LEU A 1 213 ? 29.374 3.887  10.059 1.00 33.56 ? 208 LEU A CD2 1 
ATOM   1620 N  N   . SER A 1 214 ? 32.741 6.033  7.686  1.00 37.21 ? 209 SER A N   1 
ATOM   1621 C  CA  . SER A 1 214 ? 34.050 6.611  7.432  1.00 39.12 ? 209 SER A CA  1 
ATOM   1622 C  C   . SER A 1 214 ? 35.086 6.059  8.402  1.00 39.41 ? 209 SER A C   1 
ATOM   1623 O  O   . SER A 1 214 ? 34.812 5.924  9.596  1.00 37.62 ? 209 SER A O   1 
ATOM   1624 C  CB  . SER A 1 214 ? 33.994 8.143  7.551  1.00 43.24 ? 209 SER A CB  1 
ATOM   1625 O  OG  . SER A 1 214 ? 35.308 8.639  7.572  1.00 46.04 ? 209 SER A OG  1 
ATOM   1626 N  N   . GLU A 1 215 ? 36.289 5.779  7.881  1.00 37.75 ? 210 GLU A N   1 
ATOM   1627 C  CA  . GLU A 1 215 ? 37.404 5.329  8.714  1.00 43.90 ? 210 GLU A CA  1 
ATOM   1628 C  C   . GLU A 1 215 ? 37.629 6.209  9.939  1.00 44.06 ? 210 GLU A C   1 
ATOM   1629 O  O   . GLU A 1 215 ? 37.992 5.704  11.012 1.00 43.74 ? 210 GLU A O   1 
ATOM   1630 C  CB  . GLU A 1 215 ? 38.698 5.317  7.919  1.00 46.64 ? 210 GLU A CB  1 
ATOM   1631 C  CG  . GLU A 1 215 ? 39.034 4.030  7.263  1.00 52.39 ? 210 GLU A CG  1 
ATOM   1632 C  CD  . GLU A 1 215 ? 40.003 4.227  6.137  1.00 55.87 ? 210 GLU A CD  1 
ATOM   1633 O  OE1 . GLU A 1 215 ? 41.226 4.096  6.413  1.00 59.69 ? 210 GLU A OE1 1 
ATOM   1634 O  OE2 . GLU A 1 215 ? 39.549 4.456  4.985  1.00 59.56 ? 210 GLU A OE2 1 
ATOM   1635 N  N   . ASP A 1 216 ? 37.480 7.526  9.798  1.00 38.94 ? 211 ASP A N   1 
ATOM   1636 C  CA  . ASP A 1 216 ? 37.854 8.402  10.910 1.00 42.92 ? 211 ASP A CA  1 
ATOM   1637 C  C   . ASP A 1 216 ? 36.699 8.695  11.872 1.00 43.08 ? 211 ASP A C   1 
ATOM   1638 O  O   . ASP A 1 216 ? 36.926 9.361  12.888 1.00 42.20 ? 211 ASP A O   1 
ATOM   1639 C  CB  . ASP A 1 216 ? 38.441 9.732  10.390 1.00 51.04 ? 211 ASP A CB  1 
ATOM   1640 C  CG  . ASP A 1 216 ? 37.630 10.333 9.271  1.00 56.60 ? 211 ASP A CG  1 
ATOM   1641 O  OD1 . ASP A 1 216 ? 36.385 10.384 9.445  1.00 55.15 ? 211 ASP A OD1 1 
ATOM   1642 O  OD2 . ASP A 1 216 ? 38.218 10.769 8.241  1.00 61.35 ? 211 ASP A OD2 1 
ATOM   1643 N  N   . SER A 1 217 ? 35.475 8.172  11.624 1.00 38.40 ? 212 SER A N   1 
ATOM   1644 C  CA  . SER A 1 217 ? 34.349 8.476  12.504 1.00 36.90 ? 212 SER A CA  1 
ATOM   1645 C  C   . SER A 1 217 ? 33.354 7.325  12.688 1.00 36.00 ? 212 SER A C   1 
ATOM   1646 O  O   . SER A 1 217 ? 32.272 7.557  13.246 1.00 33.61 ? 212 SER A O   1 
ATOM   1647 C  CB  . SER A 1 217 ? 33.585 9.691  11.968 1.00 36.80 ? 212 SER A CB  1 
ATOM   1648 O  OG  . SER A 1 217 ? 33.075 9.401  10.674 1.00 37.09 ? 212 SER A OG  1 
ATOM   1649 N  N   . TYR A 1 218 ? 33.668 6.106  12.260 1.00 38.59 ? 213 TYR A N   1 
ATOM   1650 C  CA  . TYR A 1 218 ? 32.671 5.037  12.323 1.00 35.28 ? 213 TYR A CA  1 
ATOM   1651 C  C   . TYR A 1 218 ? 32.272 4.703  13.751 1.00 35.76 ? 213 TYR A C   1 
ATOM   1652 O  O   . TYR A 1 218 ? 31.120 4.322  13.987 1.00 37.73 ? 213 TYR A O   1 
ATOM   1653 C  CB  . TYR A 1 218 ? 33.190 3.785  11.622 1.00 32.87 ? 213 TYR A CB  1 
ATOM   1654 C  CG  . TYR A 1 218 ? 34.318 3.068  12.323 1.00 36.38 ? 213 TYR A CG  1 
ATOM   1655 C  CD1 . TYR A 1 218 ? 35.644 3.406  12.078 1.00 36.86 ? 213 TYR A CD1 1 
ATOM   1656 C  CD2 . TYR A 1 218 ? 34.057 2.026  13.224 1.00 38.08 ? 213 TYR A CD2 1 
ATOM   1657 C  CE1 . TYR A 1 218 ? 36.685 2.746  12.714 1.00 39.44 ? 213 TYR A CE1 1 
ATOM   1658 C  CE2 . TYR A 1 218 ? 35.088 1.361  13.868 1.00 36.15 ? 213 TYR A CE2 1 
ATOM   1659 C  CZ  . TYR A 1 218 ? 36.397 1.717  13.609 1.00 41.84 ? 213 TYR A CZ  1 
ATOM   1660 O  OH  . TYR A 1 218 ? 37.427 1.054  14.241 1.00 41.02 ? 213 TYR A OH  1 
ATOM   1661 N  N   . LYS A 1 219 ? 33.195 4.834  14.718 1.00 34.95 ? 214 LYS A N   1 
ATOM   1662 C  CA  . LYS A 1 219 ? 32.815 4.569  16.104 1.00 37.45 ? 214 LYS A CA  1 
ATOM   1663 C  C   . LYS A 1 219 ? 31.729 5.526  16.560 1.00 38.65 ? 214 LYS A C   1 
ATOM   1664 O  O   . LYS A 1 219 ? 30.800 5.124  17.274 1.00 34.64 ? 214 LYS A O   1 
ATOM   1665 C  CB  . LYS A 1 219 ? 34.044 4.643  17.012 1.00 40.24 ? 214 LYS A CB  1 
ATOM   1666 C  CG  . LYS A 1 219 ? 35.118 3.663  16.577 1.00 42.69 ? 214 LYS A CG  1 
ATOM   1667 C  CD  . LYS A 1 219 ? 36.083 3.303  17.688 1.00 53.12 ? 214 LYS A CD  1 
ATOM   1668 C  CE  . LYS A 1 219 ? 37.259 4.252  17.680 1.00 54.37 ? 214 LYS A CE  1 
ATOM   1669 N  NZ  . LYS A 1 219 ? 38.468 3.566  17.138 1.00 57.66 ? 214 LYS A NZ  1 
ATOM   1670 N  N   . ASP A 1 220 ? 31.815 6.808  16.146 1.00 35.72 ? 215 ASP A N   1 
ATOM   1671 C  CA  . ASP A 1 220 ? 30.761 7.758  16.471 1.00 36.24 ? 215 ASP A CA  1 
ATOM   1672 C  C   . ASP A 1 220 ? 29.458 7.394  15.783 1.00 32.98 ? 215 ASP A C   1 
ATOM   1673 O  O   . ASP A 1 220 ? 28.383 7.464  16.391 1.00 35.09 ? 215 ASP A O   1 
ATOM   1674 C  CB  . ASP A 1 220 ? 31.192 9.175  16.061 1.00 39.05 ? 215 ASP A CB  1 
ATOM   1675 C  CG  . ASP A 1 220 ? 32.308 9.732  16.948 1.00 45.64 ? 215 ASP A CG  1 
ATOM   1676 O  OD1 . ASP A 1 220 ? 32.505 9.189  18.059 1.00 45.19 ? 215 ASP A OD1 1 
ATOM   1677 O  OD2 . ASP A 1 220 ? 32.987 10.708 16.537 1.00 47.56 ? 215 ASP A OD2 1 
ATOM   1678 N  N   . SER A 1 221 ? 29.525 7.029  14.502 1.00 34.24 ? 216 SER A N   1 
ATOM   1679 C  CA  . SER A 1 221 ? 28.302 6.669  13.795 1.00 31.48 ? 216 SER A CA  1 
ATOM   1680 C  C   . SER A 1 221 ? 27.601 5.515  14.496 1.00 31.21 ? 216 SER A C   1 
ATOM   1681 O  O   . SER A 1 221 ? 26.397 5.562  14.736 1.00 34.02 ? 216 SER A O   1 
ATOM   1682 C  CB  . SER A 1 221 ? 28.630 6.298  12.346 1.00 31.15 ? 216 SER A CB  1 
ATOM   1683 O  OG  . SER A 1 221 ? 29.232 7.396  11.693 1.00 35.42 ? 216 SER A OG  1 
ATOM   1684 N  N   . THR A 1 222 ? 28.349 4.466  14.816 1.00 36.15 ? 217 THR A N   1 
ATOM   1685 C  CA  . THR A 1 222 ? 27.701 3.256  15.324 1.00 37.66 ? 217 THR A CA  1 
ATOM   1686 C  C   . THR A 1 222 ? 27.191 3.475  16.736 1.00 36.88 ? 217 THR A C   1 
ATOM   1687 O  O   . THR A 1 222 ? 26.160 2.902  17.121 1.00 33.94 ? 217 THR A O   1 
ATOM   1688 C  CB  . THR A 1 222 ? 28.654 2.065  15.207 1.00 35.42 ? 217 THR A CB  1 
ATOM   1689 O  OG1 . THR A 1 222 ? 29.854 2.275  15.959 1.00 38.90 ? 217 THR A OG1 1 
ATOM   1690 C  CG2 . THR A 1 222 ? 29.016 1.835  13.735 1.00 38.34 ? 217 THR A CG2 1 
ATOM   1691 N  N   . LEU A 1 223 ? 27.819 4.399  17.474 1.00 33.39 ? 218 LEU A N   1 
ATOM   1692 C  CA  . LEU A 1 223 ? 27.270 4.801  18.762 1.00 36.49 ? 218 LEU A CA  1 
ATOM   1693 C  C   . LEU A 1 223 ? 25.892 5.441  18.603 1.00 35.69 ? 218 LEU A C   1 
ATOM   1694 O  O   . LEU A 1 223 ? 24.951 5.099  19.330 1.00 34.14 ? 218 LEU A O   1 
ATOM   1695 C  CB  . LEU A 1 223 ? 28.236 5.772  19.467 1.00 36.98 ? 218 LEU A CB  1 
ATOM   1696 C  CG  . LEU A 1 223 ? 27.684 6.354  20.773 1.00 37.55 ? 218 LEU A CG  1 
ATOM   1697 C  CD1 . LEU A 1 223 ? 27.217 5.226  21.677 1.00 42.52 ? 218 LEU A CD1 1 
ATOM   1698 C  CD2 . LEU A 1 223 ? 28.755 7.191  21.424 1.00 42.31 ? 218 LEU A CD2 1 
ATOM   1699 N  N   . ILE A 1 224 ? 25.762 6.418  17.698 1.00 34.11 ? 219 ILE A N   1 
ATOM   1700 C  CA  . ILE A 1 224 ? 24.467 7.073  17.513 1.00 31.71 ? 219 ILE A CA  1 
ATOM   1701 C  C   . ILE A 1 224 ? 23.421 6.080  16.997 1.00 37.51 ? 219 ILE A C   1 
ATOM   1702 O  O   . ILE A 1 224 ? 22.240 6.161  17.364 1.00 35.85 ? 219 ILE A O   1 
ATOM   1703 C  CB  . ILE A 1 224 ? 24.589 8.282  16.569 1.00 33.71 ? 219 ILE A CB  1 
ATOM   1704 C  CG1 . ILE A 1 224 ? 25.615 9.303  17.109 1.00 39.30 ? 219 ILE A CG1 1 
ATOM   1705 C  CG2 . ILE A 1 224 ? 23.208 8.947  16.345 1.00 36.00 ? 219 ILE A CG2 1 
ATOM   1706 C  CD1 . ILE A 1 224 ? 25.271 9.858  18.473 1.00 38.71 ? 219 ILE A CD1 1 
ATOM   1707 N  N   . MET A 1 225 ? 23.794 5.193  16.068 1.00 35.10 ? 220 MET A N   1 
ATOM   1708 C  CA  . MET A 1 225 ? 22.746 4.244  15.680 1.00 38.20 ? 220 MET A CA  1 
ATOM   1709 C  C   . MET A 1 225 ? 22.294 3.368  16.842 1.00 37.59 ? 220 MET A C   1 
ATOM   1710 O  O   . MET A 1 225 ? 21.091 3.117  16.961 1.00 41.69 ? 220 MET A O   1 
ATOM   1711 C  CB  . MET A 1 225 ? 23.047 3.420  14.414 1.00 43.52 ? 220 MET A CB  1 
ATOM   1712 C  CG  . MET A 1 225 ? 23.802 4.059  13.211 1.00 40.98 ? 220 MET A CG  1 
ATOM   1713 S  SD  . MET A 1 225 ? 24.938 3.048  12.231 1.00 39.49 ? 220 MET A SD  1 
ATOM   1714 C  CE  . MET A 1 225 ? 23.759 1.775  11.676 1.00 39.08 ? 220 MET A CE  1 
ATOM   1715 N  N   . GLN A 1 226 ? 23.191 2.988  17.753 1.00 34.44 ? 221 GLN A N   1 
ATOM   1716 C  CA  . GLN A 1 226 ? 22.737 2.266  18.945 1.00 40.15 ? 221 GLN A CA  1 
ATOM   1717 C  C   . GLN A 1 226 ? 21.806 3.127  19.802 1.00 44.52 ? 221 GLN A C   1 
ATOM   1718 O  O   . GLN A 1 226 ? 20.825 2.621  20.367 1.00 40.68 ? 221 GLN A O   1 
ATOM   1719 C  CB  . GLN A 1 226 ? 23.933 1.784  19.755 1.00 42.40 ? 221 GLN A CB  1 
ATOM   1720 C  CG  . GLN A 1 226 ? 23.560 0.929  20.972 1.00 46.35 ? 221 GLN A CG  1 
ATOM   1721 C  CD  . GLN A 1 226 ? 22.892 -0.357 20.555 1.00 49.78 ? 221 GLN A CD  1 
ATOM   1722 O  OE1 . GLN A 1 226 ? 23.451 -1.130 19.757 1.00 52.06 ? 221 GLN A OE1 1 
ATOM   1723 N  NE2 . GLN A 1 226 ? 21.691 -0.599 21.075 1.00 53.29 ? 221 GLN A NE2 1 
ATOM   1724 N  N   . LEU A 1 227 ? 22.086 4.438  19.911 1.00 39.78 ? 222 LEU A N   1 
ATOM   1725 C  CA  . LEU A 1 227 ? 21.196 5.295  20.692 1.00 41.03 ? 222 LEU A CA  1 
ATOM   1726 C  C   . LEU A 1 227 ? 19.847 5.477  20.009 1.00 43.72 ? 222 LEU A C   1 
ATOM   1727 O  O   . LEU A 1 227 ? 18.816 5.585  20.686 1.00 39.20 ? 222 LEU A O   1 
ATOM   1728 C  CB  . LEU A 1 227 ? 21.843 6.668  20.948 1.00 37.37 ? 222 LEU A CB  1 
ATOM   1729 C  CG  . LEU A 1 227 ? 23.166 6.636  21.727 1.00 39.53 ? 222 LEU A CG  1 
ATOM   1730 C  CD1 . LEU A 1 227 ? 23.707 8.074  21.987 1.00 36.93 ? 222 LEU A CD1 1 
ATOM   1731 C  CD2 . LEU A 1 227 ? 22.995 5.907  23.044 1.00 42.91 ? 222 LEU A CD2 1 
ATOM   1732 N  N   . LEU A 1 228 ? 19.823 5.528  18.673 1.00 40.62 ? 223 LEU A N   1 
ATOM   1733 C  CA  . LEU A 1 228 ? 18.543 5.511  17.972 1.00 43.96 ? 223 LEU A CA  1 
ATOM   1734 C  C   . LEU A 1 228 ? 17.754 4.255  18.329 1.00 43.81 ? 223 LEU A C   1 
ATOM   1735 O  O   . LEU A 1 228 ? 16.551 4.319  18.602 1.00 44.66 ? 223 LEU A O   1 
ATOM   1736 C  CB  . LEU A 1 228 ? 18.764 5.586  16.452 1.00 40.92 ? 223 LEU A CB  1 
ATOM   1737 C  CG  . LEU A 1 228 ? 19.297 6.942  15.983 1.00 41.67 ? 223 LEU A CG  1 
ATOM   1738 C  CD1 . LEU A 1 228 ? 19.897 6.857  14.569 1.00 38.17 ? 223 LEU A CD1 1 
ATOM   1739 C  CD2 . LEU A 1 228 ? 18.196 7.981  16.034 1.00 41.31 ? 223 LEU A CD2 1 
ATOM   1740 N  N   . ARG A 1 229 ? 18.432 3.109  18.344 1.00 42.59 ? 224 ARG A N   1 
ATOM   1741 C  CA  . ARG A 1 229 ? 17.778 1.842  18.672 1.00 48.03 ? 224 ARG A CA  1 
ATOM   1742 C  C   . ARG A 1 229 ? 17.280 1.833  20.113 1.00 51.26 ? 224 ARG A C   1 
ATOM   1743 O  O   . ARG A 1 229 ? 16.201 1.298  20.401 1.00 54.92 ? 224 ARG A O   1 
ATOM   1744 C  CB  . ARG A 1 229 ? 18.761 0.696  18.445 1.00 48.73 ? 224 ARG A CB  1 
ATOM   1745 C  CG  . ARG A 1 229 ? 18.551 -0.107 17.175 1.00 56.94 ? 224 ARG A CG  1 
ATOM   1746 C  CD  . ARG A 1 229 ? 17.297 -0.995 17.229 1.00 57.39 ? 224 ARG A CD  1 
ATOM   1747 N  NE  . ARG A 1 229 ? 17.247 -1.902 16.088 1.00 62.24 ? 224 ARG A NE  1 
ATOM   1748 C  CZ  . ARG A 1 229 ? 18.062 -2.943 15.918 1.00 67.14 ? 224 ARG A CZ  1 
ATOM   1749 N  NH1 . ARG A 1 229 ? 19.022 -3.228 16.791 1.00 61.25 ? 224 ARG A NH1 1 
ATOM   1750 N  NH2 . ARG A 1 229 ? 17.915 -3.717 14.839 1.00 64.68 ? 224 ARG A NH2 1 
ATOM   1751 N  N   . ASP A 1 230 ? 18.063 2.403  21.040 1.00 49.69 ? 225 ASP A N   1 
ATOM   1752 C  CA  . ASP A 1 230 ? 17.631 2.453  22.438 1.00 51.06 ? 225 ASP A CA  1 
ATOM   1753 C  C   . ASP A 1 230 ? 16.361 3.278  22.589 1.00 52.43 ? 225 ASP A C   1 
ATOM   1754 O  O   . ASP A 1 230 ? 15.430 2.872  23.294 1.00 55.08 ? 225 ASP A O   1 
ATOM   1755 C  CB  . ASP A 1 230 ? 18.740 3.022  23.326 1.00 46.16 ? 225 ASP A CB  1 
ATOM   1756 C  CG  . ASP A 1 230 ? 19.985 2.162  23.330 1.00 50.02 ? 225 ASP A CG  1 
ATOM   1757 O  OD1 . ASP A 1 230 ? 19.900 0.995  22.887 1.00 56.44 ? 225 ASP A OD1 1 
ATOM   1758 O  OD2 . ASP A 1 230 ? 21.047 2.638  23.790 1.00 52.82 ? 225 ASP A OD2 1 
ATOM   1759 N  N   . ASN A 1 231 ? 16.306 4.446  21.942 1.00 47.35 ? 226 ASN A N   1 
ATOM   1760 C  CA  . ASN A 1 231 ? 15.101 5.265  21.995 1.00 50.20 ? 226 ASN A CA  1 
ATOM   1761 C  C   . ASN A 1 231 ? 13.917 4.546  21.367 1.00 54.72 ? 226 ASN A C   1 
ATOM   1762 O  O   . ASN A 1 231 ? 12.796 4.623  21.880 1.00 54.94 ? 226 ASN A O   1 
ATOM   1763 C  CB  . ASN A 1 231 ? 15.323 6.611  21.302 1.00 48.09 ? 226 ASN A CB  1 
ATOM   1764 C  CG  . ASN A 1 231 ? 16.098 7.586  22.172 1.00 48.19 ? 226 ASN A CG  1 
ATOM   1765 O  OD1 . ASN A 1 231 ? 16.268 7.357  23.369 1.00 47.44 ? 226 ASN A OD1 1 
ATOM   1766 N  ND2 . ASN A 1 231 ? 16.540 8.694  21.581 1.00 45.69 ? 226 ASN A ND2 1 
ATOM   1767 N  N   . LEU A 1 232 ? 14.138 3.873  20.235 1.00 49.64 ? 227 LEU A N   1 
ATOM   1768 C  CA  . LEU A 1 232 ? 13.073 3.078  19.636 1.00 54.61 ? 227 LEU A CA  1 
ATOM   1769 C  C   . LEU A 1 232 ? 12.559 2.021  20.614 1.00 55.59 ? 227 LEU A C   1 
ATOM   1770 O  O   . LEU A 1 232 ? 11.345 1.838  20.754 1.00 59.34 ? 227 LEU A O   1 
ATOM   1771 C  CB  . LEU A 1 232 ? 13.575 2.437  18.342 1.00 48.21 ? 227 LEU A CB  1 
ATOM   1772 C  CG  . LEU A 1 232 ? 13.759 3.500  17.259 1.00 48.47 ? 227 LEU A CG  1 
ATOM   1773 C  CD1 . LEU A 1 232 ? 14.584 2.998  16.076 1.00 51.08 ? 227 LEU A CD1 1 
ATOM   1774 C  CD2 . LEU A 1 232 ? 12.402 4.037  16.815 1.00 49.01 ? 227 LEU A CD2 1 
ATOM   1775 N  N   . THR A 1 233 ? 13.470 1.329  21.307 1.00 54.23 ? 228 THR A N   1 
ATOM   1776 C  CA  . THR A 1 233 ? 13.069 0.329  22.298 1.00 58.64 ? 228 THR A CA  1 
ATOM   1777 C  C   . THR A 1 233 ? 12.268 0.972  23.423 1.00 63.33 ? 228 THR A C   1 
ATOM   1778 O  O   . THR A 1 233 ? 11.206 0.470  23.819 1.00 66.41 ? 228 THR A O   1 
ATOM   1779 C  CB  . THR A 1 233 ? 14.309 -0.370 22.871 1.00 61.85 ? 228 THR A CB  1 
ATOM   1780 O  OG1 . THR A 1 233 ? 14.927 -1.183 21.868 1.00 61.20 ? 228 THR A OG1 1 
ATOM   1781 C  CG2 . THR A 1 233 ? 13.947 -1.239 24.079 1.00 60.42 ? 228 THR A CG2 1 
ATOM   1782 N  N   . LEU A 1 234 ? 12.782 2.079  23.964 1.00 61.20 ? 229 LEU A N   1 
ATOM   1783 C  CA  . LEU A 1 234 ? 12.076 2.826  24.998 1.00 60.79 ? 229 LEU A CA  1 
ATOM   1784 C  C   . LEU A 1 234 ? 10.715 3.307  24.502 1.00 63.43 ? 229 LEU A C   1 
ATOM   1785 O  O   . LEU A 1 234 ? 9.724  3.268  25.240 1.00 65.80 ? 229 LEU A O   1 
ATOM   1786 C  CB  . LEU A 1 234 ? 12.937 4.013  25.445 1.00 60.09 ? 229 LEU A CB  1 
ATOM   1787 C  CG  . LEU A 1 234 ? 12.323 5.012  26.430 1.00 64.81 ? 229 LEU A CG  1 
ATOM   1788 C  CD1 . LEU A 1 234 ? 12.084 4.348  27.776 1.00 65.41 ? 229 LEU A CD1 1 
ATOM   1789 C  CD2 . LEU A 1 234 ? 13.151 6.302  26.569 1.00 62.14 ? 229 LEU A CD2 1 
ATOM   1790 N  N   . TRP A 1 235 ? 10.640 3.755  23.254 1.00 60.62 ? 230 TRP A N   1 
ATOM   1791 C  CA  . TRP A 1 235 ? 9.411  4.340  22.735 1.00 61.20 ? 230 TRP A CA  1 
ATOM   1792 C  C   . TRP A 1 235 ? 8.400  3.301  22.245 1.00 65.72 ? 230 TRP A C   1 
ATOM   1793 O  O   . TRP A 1 235 ? 7.312  3.692  21.807 1.00 65.52 ? 230 TRP A O   1 
ATOM   1794 C  CB  . TRP A 1 235 ? 9.744  5.310  21.596 1.00 59.91 ? 230 TRP A CB  1 
ATOM   1795 C  CG  . TRP A 1 235 ? 10.581 6.474  22.030 1.00 58.95 ? 230 TRP A CG  1 
ATOM   1796 C  CD1 . TRP A 1 235 ? 10.833 6.873  23.316 1.00 58.07 ? 230 TRP A CD1 1 
ATOM   1797 C  CD2 . TRP A 1 235 ? 11.295 7.383  21.178 1.00 56.26 ? 230 TRP A CD2 1 
ATOM   1798 N  NE1 . TRP A 1 235 ? 11.652 7.983  23.310 1.00 58.69 ? 230 TRP A NE1 1 
ATOM   1799 C  CE2 . TRP A 1 235 ? 11.946 8.316  22.012 1.00 53.50 ? 230 TRP A CE2 1 
ATOM   1800 C  CE3 . TRP A 1 235 ? 11.445 7.498  19.789 1.00 54.66 ? 230 TRP A CE3 1 
ATOM   1801 C  CZ2 . TRP A 1 235 ? 12.731 9.357  21.503 1.00 53.46 ? 230 TRP A CZ2 1 
ATOM   1802 C  CZ3 . TRP A 1 235 ? 12.229 8.531  19.286 1.00 54.80 ? 230 TRP A CZ3 1 
ATOM   1803 C  CH2 . TRP A 1 235 ? 12.860 9.445  20.141 1.00 52.50 ? 230 TRP A CH2 1 
ATOM   1804 N  N   . THR A 1 236 ? 8.735  2.008  22.289 1.00 64.40 ? 231 THR A N   1 
ATOM   1805 C  CA  . THR A 1 236 ? 7.838  0.941  21.841 1.00 65.97 ? 231 THR A CA  1 
ATOM   1806 C  C   . THR A 1 236 ? 7.820  -0.260 22.809 1.00 68.78 ? 231 THR A C   1 
ATOM   1807 O  O   . THR A 1 236 ? 6.847  -1.007 22.813 1.00 75.25 ? 231 THR A O   1 
ATOM   1808 C  CB  . THR A 1 236 ? 8.218  0.417  20.427 1.00 67.51 ? 231 THR A CB  1 
ATOM   1809 O  OG1 . THR A 1 236 ? 9.488  -0.244 20.481 1.00 68.16 ? 231 THR A OG1 1 
ATOM   1810 C  CG2 . THR A 1 236 ? 8.267  1.546  19.398 1.00 60.30 ? 231 THR A CG2 1 
ATOM   1811 O  OXT . THR A 1 236 ? 8.727  -0.543 23.610 1.00 67.99 ? 231 THR A OXT 1 
ATOM   1812 N  N   . GLN B 2 1   ? 11.501 6.735  32.064 1.00 75.66 ? 255 GLN P N   1 
ATOM   1813 C  CA  . GLN B 2 1   ? 12.870 7.033  31.655 1.00 73.44 ? 255 GLN P CA  1 
ATOM   1814 C  C   . GLN B 2 1   ? 12.907 8.123  30.580 1.00 72.22 ? 255 GLN P C   1 
ATOM   1815 O  O   . GLN B 2 1   ? 11.967 8.282  29.789 1.00 72.32 ? 255 GLN P O   1 
ATOM   1816 C  CB  . GLN B 2 1   ? 13.560 5.771  31.148 1.00 72.18 ? 255 GLN P CB  1 
ATOM   1817 C  CG  . GLN B 2 1   ? 15.001 5.980  30.737 1.00 76.36 ? 255 GLN P CG  1 
ATOM   1818 C  CD  . GLN B 2 1   ? 15.690 4.689  30.358 1.00 81.62 ? 255 GLN P CD  1 
ATOM   1819 O  OE1 . GLN B 2 1   ? 15.175 3.594  30.615 1.00 85.65 ? 255 GLN P OE1 1 
ATOM   1820 N  NE2 . GLN B 2 1   ? 16.857 4.807  29.730 1.00 82.23 ? 255 GLN P NE2 1 
ATOM   1821 N  N   . ARG B 2 2   ? 14.002 8.873  30.551 1.00 69.27 ? 256 ARG P N   1 
ATOM   1822 C  CA  . ARG B 2 2   ? 14.130 10.001 29.647 1.00 67.30 ? 256 ARG P CA  1 
ATOM   1823 C  C   . ARG B 2 2   ? 14.769 9.548  28.328 1.00 62.26 ? 256 ARG P C   1 
ATOM   1824 O  O   . ARG B 2 2   ? 15.570 8.607  28.288 1.00 62.06 ? 256 ARG P O   1 
ATOM   1825 C  CB  . ARG B 2 2   ? 14.959 11.096 30.326 1.00 65.78 ? 256 ARG P CB  1 
ATOM   1826 C  CG  . ARG B 2 2   ? 14.659 12.493 29.859 1.00 63.54 ? 256 ARG P CG  1 
ATOM   1827 C  CD  . ARG B 2 2   ? 15.660 12.980 28.849 1.00 62.75 ? 256 ARG P CD  1 
ATOM   1828 N  NE  . ARG B 2 2   ? 15.025 13.962 27.984 1.00 65.00 ? 256 ARG P NE  1 
ATOM   1829 C  CZ  . ARG B 2 2   ? 15.570 14.500 26.901 1.00 58.96 ? 256 ARG P CZ  1 
ATOM   1830 N  NH1 . ARG B 2 2   ? 16.798 14.161 26.489 1.00 50.88 ? 256 ARG P NH1 1 
ATOM   1831 N  NH2 . ARG B 2 2   ? 14.871 15.404 26.219 1.00 52.68 ? 256 ARG P NH2 1 
ATOM   1832 N  N   . SER B 2 3   ? 14.378 10.200 27.237 1.00 60.15 ? 257 SER P N   1 
ATOM   1833 C  CA  . SER B 2 3   ? 14.975 9.861  25.949 1.00 55.82 ? 257 SER P CA  1 
ATOM   1834 C  C   . SER B 2 3   ? 16.454 10.245 25.941 1.00 55.35 ? 257 SER P C   1 
ATOM   1835 O  O   . SER B 2 3   ? 16.876 11.189 26.620 1.00 49.82 ? 257 SER P O   1 
ATOM   1836 C  CB  . SER B 2 3   ? 14.237 10.566 24.808 1.00 54.54 ? 257 SER P CB  1 
ATOM   1837 O  OG  . SER B 2 3   ? 12.868 10.190 24.752 1.00 54.42 ? 257 SER P OG  1 
ATOM   1838 N  N   . THR B 2 4   ? 17.253 9.495  25.177 1.00 48.42 ? 258 THR P N   1 
ATOM   1839 C  CA  . THR B 2 4   ? 18.676 9.809  25.089 1.00 42.30 ? 258 THR P CA  1 
ATOM   1840 C  C   . THR B 2 4   ? 18.996 10.650 23.866 1.00 42.15 ? 258 THR P C   1 
ATOM   1841 O  O   . THR B 2 4   ? 18.607 10.302 22.744 1.00 43.80 ? 258 THR P O   1 
ATOM   1842 C  CB  . THR B 2 4   ? 19.521 8.556  25.034 1.00 45.68 ? 258 THR P CB  1 
ATOM   1843 O  OG1 . THR B 2 4   ? 19.175 7.718  26.133 1.00 46.18 ? 258 THR P OG1 1 
ATOM   1844 C  CG2 . THR B 2 4   ? 21.008 8.903  25.128 1.00 45.63 ? 258 THR P CG2 1 
HETATM 1845 N  N   . SEP B 2 5   ? 19.740 11.728 24.080 1.00 40.00 ? 259 SEP P N   1 
HETATM 1846 C  CA  . SEP B 2 5   ? 20.169 12.587 22.981 1.00 34.16 ? 259 SEP P CA  1 
HETATM 1847 C  CB  . SEP B 2 5   ? 19.908 14.081 23.287 1.00 38.52 ? 259 SEP P CB  1 
HETATM 1848 O  OG  . SEP B 2 5   ? 20.660 14.471 24.415 1.00 37.72 ? 259 SEP P OG  1 
HETATM 1849 C  C   . SEP B 2 5   ? 21.642 12.332 22.729 1.00 37.27 ? 259 SEP P C   1 
HETATM 1850 O  O   . SEP B 2 5   ? 22.268 11.493 23.391 1.00 35.71 ? 259 SEP P O   1 
HETATM 1851 P  P   . SEP B 2 5   ? 20.375 15.979 24.944 1.00 37.16 ? 259 SEP P P   1 
HETATM 1852 O  O1P . SEP B 2 5   ? 20.744 17.055 23.810 1.00 36.90 ? 259 SEP P O1P 1 
HETATM 1853 O  O2P . SEP B 2 5   ? 18.846 16.107 25.391 1.00 39.23 ? 259 SEP P O2P 1 
HETATM 1854 O  O3P . SEP B 2 5   ? 21.332 16.098 26.229 1.00 39.63 ? 259 SEP P O3P 1 
ATOM   1855 N  N   . THR B 2 6   ? 22.192 13.033 21.743 1.00 34.65 ? 260 THR P N   1 
ATOM   1856 C  CA  . THR B 2 6   ? 23.584 12.862 21.379 1.00 35.10 ? 260 THR P CA  1 
ATOM   1857 C  C   . THR B 2 6   ? 24.482 13.174 22.575 1.00 40.06 ? 260 THR P C   1 
ATOM   1858 O  O   . THR B 2 6   ? 24.283 14.188 23.245 1.00 38.23 ? 260 THR P O   1 
ATOM   1859 C  CB  . THR B 2 6   ? 23.915 13.762 20.187 1.00 40.59 ? 260 THR P CB  1 
ATOM   1860 O  OG1 . THR B 2 6   ? 23.013 13.456 19.103 1.00 41.17 ? 260 THR P OG1 1 
ATOM   1861 C  CG2 . THR B 2 6   ? 25.320 13.523 19.723 1.00 41.36 ? 260 THR P CG2 1 
ATOM   1862 N  N   . PRO B 2 7   ? 25.438 12.302 22.876 1.00 38.52 ? 261 PRO P N   1 
ATOM   1863 C  CA  . PRO B 2 7   ? 26.283 12.500 24.056 1.00 40.46 ? 261 PRO P CA  1 
ATOM   1864 C  C   . PRO B 2 7   ? 27.496 13.371 23.743 1.00 40.40 ? 261 PRO P C   1 
ATOM   1865 O  O   . PRO B 2 7   ? 27.798 13.659 22.584 1.00 39.21 ? 261 PRO P O   1 
ATOM   1866 C  CB  . PRO B 2 7   ? 26.726 11.070 24.406 1.00 38.77 ? 261 PRO P CB  1 
ATOM   1867 C  CG  . PRO B 2 7   ? 26.855 10.427 23.036 1.00 39.66 ? 261 PRO P CG  1 
ATOM   1868 C  CD  . PRO B 2 7   ? 25.719 11.012 22.213 1.00 38.76 ? 261 PRO P CD  1 
ATOM   1869 N  N   . ASN B 2 8   ? 28.200 13.777 24.815 1.00 40.13 ? 262 ASN P N   1 
ATOM   1870 C  CA  . ASN B 2 8   ? 29.538 14.348 24.642 1.00 40.58 ? 262 ASN P CA  1 
ATOM   1871 C  C   . ASN B 2 8   ? 30.563 13.268 24.293 1.00 54.17 ? 262 ASN P C   1 
ATOM   1872 O  O   . ASN B 2 8   ? 30.536 12.162 24.839 1.00 59.91 ? 262 ASN P O   1 
ATOM   1873 C  CB  . ASN B 2 8   ? 29.979 15.070 25.909 1.00 50.91 ? 262 ASN P CB  1 
ATOM   1874 C  CG  . ASN B 2 8   ? 29.510 16.506 25.941 1.00 45.26 ? 262 ASN P CG  1 
ATOM   1875 O  OD1 . ASN B 2 8   ? 29.446 17.173 24.901 1.00 42.51 ? 262 ASN P OD1 1 
ATOM   1876 N  ND2 . ASN B 2 8   ? 29.226 17.015 27.141 1.00 51.19 ? 262 ASN P ND2 1 
ATOM   1877 N  N   . VAL B 2 9   ? 31.502 13.602 23.411 1.00 49.41 ? 263 VAL P N   1 
ATOM   1878 C  CA  . VAL B 2 9   ? 32.530 12.661 22.977 1.00 54.89 ? 263 VAL P CA  1 
ATOM   1879 C  C   . VAL B 2 9   ? 33.776 13.439 22.568 1.00 58.84 ? 263 VAL P C   1 
ATOM   1880 O  O   . VAL B 2 9   ? 33.689 14.562 22.054 1.00 56.65 ? 263 VAL P O   1 
ATOM   1881 C  CB  . VAL B 2 9   ? 32.015 11.760 21.823 1.00 55.90 ? 263 VAL P CB  1 
ATOM   1882 C  CG1 . VAL B 2 9   ? 32.172 12.459 20.451 1.00 54.06 ? 263 VAL P CG1 1 
ATOM   1883 C  CG2 . VAL B 2 9   ? 32.732 10.415 21.830 1.00 60.72 ? 263 VAL P CG2 1 
ATOM   1884 N  N   . HIS B 2 10  ? 34.945 12.839 22.820 1.00 59.35 ? 264 HIS P N   1 
ATOM   1885 C  CA  . HIS B 2 10  ? 36.252 13.342 22.342 1.00 60.55 ? 264 HIS P CA  1 
ATOM   1886 C  C   . HIS B 2 10  ? 36.689 14.739 22.850 1.00 57.08 ? 264 HIS P C   1 
ATOM   1887 O  O   . HIS B 2 10  ? 36.089 15.405 23.703 1.00 56.50 ? 264 HIS P O   1 
ATOM   1888 C  CB  . HIS B 2 10  ? 36.287 13.386 20.808 1.00 58.90 ? 264 HIS P CB  1 
ATOM   1889 C  CG  . HIS B 2 10  ? 36.124 12.048 20.152 1.00 63.49 ? 264 HIS P CG  1 
ATOM   1890 N  ND1 . HIS B 2 10  ? 35.056 11.750 19.329 1.00 62.69 ? 264 HIS P ND1 1 
ATOM   1891 C  CD2 . HIS B 2 10  ? 36.873 10.922 20.221 1.00 64.57 ? 264 HIS P CD2 1 
ATOM   1892 C  CE1 . HIS B 2 10  ? 35.163 10.503 18.904 1.00 60.54 ? 264 HIS P CE1 1 
ATOM   1893 N  NE2 . HIS B 2 10  ? 36.254 9.976  19.434 1.00 68.39 ? 264 HIS P NE2 1 
ATOM   1894 O  OXT . HIS B 2 10  ? 37.720 15.247 22.386 1.00 54.93 ? 264 HIS P OXT 1 
HETATM 1895 CL CL  . CL  C 3 .   ? 17.719 31.859 45.280 1.00 41.31 ? 301 CL  A CL  1 
HETATM 1896 MG MG  . MG  D 4 .   ? 12.298 32.165 34.632 1.00 62.86 ? 302 MG  A MG  1 
HETATM 1897 MG MG  . MG  E 4 .   ? 0.132  15.066 56.714 1.00 78.00 ? 303 MG  A MG  1 
HETATM 1898 MG MG  . MG  F 4 .   ? 49.383 38.672 17.420 1.00 51.25 ? 304 MG  A MG  1 
HETATM 1899 C  C1  . WQX G 5 .   ? 32.526 18.373 13.099 1.00 39.79 ? 305 WQX A C1  1 
HETATM 1900 C  C2  . WQX G 5 .   ? 33.558 17.534 12.366 1.00 40.83 ? 305 WQX A C2  1 
HETATM 1901 C  C3  . WQX G 5 .   ? 32.585 16.875 15.199 1.00 36.83 ? 305 WQX A C3  1 
HETATM 1902 C  C4  . WQX G 5 .   ? 31.447 17.305 16.129 1.00 37.98 ? 305 WQX A C4  1 
HETATM 1903 C  C5  . WQX G 5 .   ? 31.296 18.602 15.320 1.00 36.76 ? 305 WQX A C5  1 
HETATM 1904 C  C6  . WQX G 5 .   ? 30.169 16.503 16.048 1.00 38.40 ? 305 WQX A C6  1 
HETATM 1905 C  C7  . WQX G 5 .   ? 27.990 14.551 17.577 1.00 39.61 ? 305 WQX A C7  1 
HETATM 1906 C  C8  . WQX G 5 .   ? 28.346 14.380 18.908 1.00 38.66 ? 305 WQX A C8  1 
HETATM 1907 C  C10 . WQX G 5 .   ? 28.625 12.027 18.546 1.00 42.15 ? 305 WQX A C10 1 
HETATM 1908 C  C11 . WQX G 5 .   ? 28.328 12.241 17.212 1.00 38.82 ? 305 WQX A C11 1 
HETATM 1909 C  C13 . WQX G 5 .   ? 29.585 17.521 18.357 1.00 40.30 ? 305 WQX A C13 1 
HETATM 1910 C  C14 . WQX G 5 .   ? 30.912 18.234 18.187 1.00 36.15 ? 305 WQX A C14 1 
HETATM 1911 C  C12 . WQX G 5 .   ? 28.032 13.483 16.702 1.00 36.11 ? 305 WQX A C12 1 
HETATM 1912 C  C9  . WQX G 5 .   ? 28.639 13.116 19.397 1.00 40.81 ? 305 WQX A C9  1 
HETATM 1913 F  F1  . WQX G 5 .   ? 28.312 11.193 16.376 1.00 42.17 ? 305 WQX A F1  1 
HETATM 1914 N  N1  . WQX G 5 .   ? 32.179 17.997 14.322 1.00 36.93 ? 305 WQX A N1  1 
HETATM 1915 N  N2  . WQX G 5 .   ? 29.219 16.772 17.133 1.00 40.27 ? 305 WQX A N2  1 
HETATM 1916 O  O1  . WQX G 5 .   ? 32.046 19.381 12.583 1.00 39.67 ? 305 WQX A O1  1 
HETATM 1917 O  O2  . WQX G 5 .   ? 27.397 16.124 15.564 1.00 37.74 ? 305 WQX A O2  1 
HETATM 1918 O  O3  . WQX G 5 .   ? 26.847 16.867 17.869 1.00 38.38 ? 305 WQX A O3  1 
HETATM 1919 O  O4  . WQX G 5 .   ? 31.867 17.450 17.471 1.00 39.82 ? 305 WQX A O4  1 
HETATM 1920 S  S1  . WQX G 5 .   ? 27.707 16.173 16.969 1.00 39.69 ? 305 WQX A S1  1 
HETATM 1921 BR BR1 . WQX G 5 .   ? 29.041 10.276 19.181 1.00 66.29 ? 305 WQX A BR1 1 
HETATM 1922 O  O   . HOH H 6 .   ? 36.754 16.153 29.878 1.00 46.60 ? 401 HOH A O   1 
HETATM 1923 O  O   . HOH H 6 .   ? 2.058  18.584 50.704 1.00 72.58 ? 402 HOH A O   1 
HETATM 1924 O  O   . HOH H 6 .   ? 22.146 21.867 0.654  1.00 55.17 ? 403 HOH A O   1 
HETATM 1925 O  O   . HOH H 6 .   ? 39.701 2.504  3.709  1.00 48.56 ? 404 HOH A O   1 
HETATM 1926 O  O   . HOH H 6 .   ? 6.420  5.421  23.103 1.00 68.02 ? 405 HOH A O   1 
HETATM 1927 O  O   . HOH H 6 .   ? 12.418 2.157  7.927  1.00 55.31 ? 406 HOH A O   1 
HETATM 1928 O  O   . HOH H 6 .   ? 17.200 -1.578 9.468  1.00 57.35 ? 407 HOH A O   1 
HETATM 1929 O  O   . HOH H 6 .   ? 19.611 -4.719 13.472 1.00 66.45 ? 408 HOH A O   1 
HETATM 1930 O  O   . HOH H 6 .   ? 19.268 14.634 34.881 1.00 68.09 ? 409 HOH A O   1 
HETATM 1931 O  O   . HOH H 6 .   ? 41.724 41.867 20.393 1.00 36.01 ? 410 HOH A O   1 
HETATM 1932 O  O   . HOH H 6 .   ? 46.492 35.479 16.324 1.00 58.90 ? 411 HOH A O   1 
HETATM 1933 O  O   . HOH H 6 .   ? 24.477 27.648 2.149  1.00 67.91 ? 412 HOH A O   1 
HETATM 1934 O  O   . HOH H 6 .   ? 32.253 7.610  19.914 1.00 51.60 ? 413 HOH A O   1 
HETATM 1935 O  O   . HOH H 6 .   ? 32.543 34.249 12.094 1.00 56.28 ? 414 HOH A O   1 
HETATM 1936 O  O   . HOH H 6 .   ? 32.950 2.232  5.023  1.00 38.68 ? 415 HOH A O   1 
HETATM 1937 O  O   . HOH H 6 .   ? 43.335 24.818 16.018 1.00 42.07 ? 416 HOH A O   1 
HETATM 1938 O  O   . HOH H 6 .   ? 31.788 13.729 10.406 1.00 44.76 ? 417 HOH A O   1 
HETATM 1939 O  O   . HOH H 6 .   ? 15.185 33.465 42.136 1.00 45.47 ? 418 HOH A O   1 
HETATM 1940 O  O   . HOH H 6 .   ? 31.554 8.036  3.734  1.00 42.84 ? 419 HOH A O   1 
HETATM 1941 O  O   . HOH H 6 .   ? 19.145 30.085 11.313 1.00 56.79 ? 420 HOH A O   1 
HETATM 1942 O  O   . HOH H 6 .   ? 39.179 17.340 22.642 1.00 49.19 ? 421 HOH A O   1 
HETATM 1943 O  O   . HOH H 6 .   ? 40.787 39.551 30.489 1.00 48.47 ? 422 HOH A O   1 
HETATM 1944 O  O   . HOH H 6 .   ? 25.014 17.198 20.680 1.00 42.88 ? 423 HOH A O   1 
HETATM 1945 O  O   . HOH H 6 .   ? 31.176 29.572 10.602 1.00 45.21 ? 424 HOH A O   1 
HETATM 1946 O  O   . HOH H 6 .   ? 9.278  23.643 37.986 1.00 53.96 ? 425 HOH A O   1 
HETATM 1947 O  O   . HOH H 6 .   ? 31.189 29.046 38.350 0.50 56.21 ? 426 HOH A O   1 
HETATM 1948 O  O   . HOH H 6 .   ? 30.081 37.915 20.743 1.00 55.12 ? 427 HOH A O   1 
HETATM 1949 O  O   . HOH H 6 .   ? 23.144 25.418 3.348  1.00 54.32 ? 428 HOH A O   1 
HETATM 1950 O  O   . HOH H 6 .   ? 23.591 2.273  24.292 1.00 57.68 ? 429 HOH A O   1 
HETATM 1951 O  O   . HOH H 6 .   ? 46.387 19.744 25.798 1.00 55.70 ? 430 HOH A O   1 
HETATM 1952 O  O   . HOH H 6 .   ? 38.120 5.995  13.620 1.00 47.68 ? 431 HOH A O   1 
HETATM 1953 O  O   . HOH H 6 .   ? 26.830 23.524 34.896 1.00 41.35 ? 432 HOH A O   1 
HETATM 1954 O  O   . HOH H 6 .   ? 30.695 31.519 28.040 1.00 38.80 ? 433 HOH A O   1 
HETATM 1955 O  O   . HOH H 6 .   ? 27.001 22.141 22.834 1.00 39.72 ? 434 HOH A O   1 
HETATM 1956 O  O   . HOH H 6 .   ? 20.770 4.580  25.548 1.00 53.15 ? 435 HOH A O   1 
HETATM 1957 O  O   . HOH H 6 .   ? 25.514 0.399  16.614 1.00 39.60 ? 436 HOH A O   1 
HETATM 1958 O  O   . HOH H 6 .   ? 21.062 31.445 16.819 1.00 47.07 ? 437 HOH A O   1 
HETATM 1959 O  O   . HOH H 6 .   ? 17.104 5.736  25.303 1.00 52.36 ? 438 HOH A O   1 
HETATM 1960 O  O   . HOH H 6 .   ? 13.660 31.966 27.071 1.00 59.46 ? 439 HOH A O   1 
HETATM 1961 O  O   . HOH H 6 .   ? 11.135 20.165 31.056 1.00 45.78 ? 440 HOH A O   1 
HETATM 1962 O  O   . HOH H 6 .   ? 34.355 19.931 8.440  1.00 49.97 ? 441 HOH A O   1 
HETATM 1963 O  O   . HOH H 6 .   ? 36.570 38.163 23.062 1.00 47.10 ? 442 HOH A O   1 
HETATM 1964 O  O   . HOH H 6 .   ? 33.024 27.651 11.525 1.00 41.85 ? 443 HOH A O   1 
HETATM 1965 O  O   . HOH H 6 .   ? 31.172 7.450  9.850  1.00 36.70 ? 444 HOH A O   1 
HETATM 1966 O  O   . HOH H 6 .   ? 26.917 34.410 11.286 1.00 57.06 ? 445 HOH A O   1 
HETATM 1967 O  O   . HOH H 6 .   ? 32.649 11.471 9.020  1.00 40.75 ? 446 HOH A O   1 
HETATM 1968 O  O   . HOH H 6 .   ? 40.129 17.961 37.248 1.00 44.40 ? 447 HOH A O   1 
HETATM 1969 O  O   . HOH H 6 .   ? 23.124 0.000  0.000  0.50 36.44 ? 448 HOH A O   1 
HETATM 1970 O  O   . HOH H 6 .   ? 10.146 31.302 54.404 1.00 46.63 ? 449 HOH A O   1 
HETATM 1971 O  O   . HOH H 6 .   ? 41.930 22.171 13.901 1.00 48.20 ? 450 HOH A O   1 
HETATM 1972 O  O   . HOH H 6 .   ? 15.281 28.848 14.043 1.00 53.21 ? 451 HOH A O   1 
HETATM 1973 O  O   . HOH H 6 .   ? 31.140 3.081  19.004 1.00 44.16 ? 452 HOH A O   1 
HETATM 1974 O  O   . HOH H 6 .   ? 32.390 30.914 6.380  1.00 60.50 ? 453 HOH A O   1 
HETATM 1975 O  O   . HOH H 6 .   ? 16.832 22.905 29.698 1.00 38.43 ? 454 HOH A O   1 
HETATM 1976 O  O   . HOH H 6 .   ? 38.282 37.116 21.215 1.00 41.39 ? 455 HOH A O   1 
HETATM 1977 O  O   . HOH H 6 .   ? 37.851 32.180 15.146 1.00 38.51 ? 456 HOH A O   1 
HETATM 1978 O  O   . HOH H 6 .   ? 36.929 5.225  5.039  1.00 50.73 ? 457 HOH A O   1 
HETATM 1979 O  O   . HOH H 6 .   ? 8.151  30.418 38.300 1.00 61.20 ? 458 HOH A O   1 
HETATM 1980 O  O   . HOH H 6 .   ? 34.866 34.402 26.786 1.00 38.64 ? 459 HOH A O   1 
HETATM 1981 O  O   . HOH H 6 .   ? 15.703 19.612 31.363 1.00 44.14 ? 460 HOH A O   1 
HETATM 1982 O  O   . HOH H 6 .   ? 18.725 32.867 17.542 1.00 57.47 ? 461 HOH A O   1 
HETATM 1983 O  O   . HOH H 6 .   ? 46.360 26.207 19.328 1.00 37.47 ? 462 HOH A O   1 
HETATM 1984 O  O   . HOH H 6 .   ? 9.921  26.893 34.243 1.00 47.99 ? 463 HOH A O   1 
HETATM 1985 O  O   . HOH H 6 .   ? 18.404 8.992  7.074  1.00 45.99 ? 464 HOH A O   1 
HETATM 1986 O  O   . HOH H 6 .   ? 34.038 32.817 14.211 1.00 42.46 ? 465 HOH A O   1 
HETATM 1987 O  O   . HOH H 6 .   ? 37.496 20.870 9.755  1.00 43.17 ? 466 HOH A O   1 
HETATM 1988 O  O   . HOH H 6 .   ? 20.462 33.378 38.079 1.00 53.63 ? 467 HOH A O   1 
HETATM 1989 O  O   . HOH H 6 .   ? 24.150 19.452 38.131 1.00 52.03 ? 468 HOH A O   1 
HETATM 1990 O  O   . HOH H 6 .   ? 19.071 34.824 31.644 1.00 47.49 ? 469 HOH A O   1 
HETATM 1991 O  O   . HOH H 6 .   ? 40.793 26.597 12.437 1.00 45.99 ? 470 HOH A O   1 
HETATM 1992 O  O   . HOH H 6 .   ? 26.721 21.016 20.114 1.00 34.89 ? 471 HOH A O   1 
HETATM 1993 O  O   . HOH H 6 .   ? 24.187 32.327 32.685 1.00 40.58 ? 472 HOH A O   1 
HETATM 1994 O  O   . HOH H 6 .   ? 30.507 20.077 2.011  1.00 49.43 ? 473 HOH A O   1 
HETATM 1995 O  O   . HOH H 6 .   ? 18.637 15.731 37.387 1.00 44.53 ? 474 HOH A O   1 
HETATM 1996 O  O   . HOH H 6 .   ? 17.637 -1.038 6.576  1.00 43.69 ? 475 HOH A O   1 
HETATM 1997 O  O   . HOH H 6 .   ? 16.920 10.712 8.713  1.00 45.73 ? 476 HOH A O   1 
HETATM 1998 O  O   . HOH H 6 .   ? 49.634 31.508 20.514 1.00 45.94 ? 477 HOH A O   1 
HETATM 1999 O  O   . HOH H 6 .   ? 12.053 17.157 36.996 1.00 49.68 ? 478 HOH A O   1 
HETATM 2000 O  O   . HOH H 6 .   ? 41.719 18.326 25.654 1.00 40.94 ? 479 HOH A O   1 
HETATM 2001 O  O   . HOH H 6 .   ? 31.834 30.140 30.505 1.00 41.79 ? 480 HOH A O   1 
HETATM 2002 O  O   . HOH H 6 .   ? 29.439 27.187 7.797  1.00 47.38 ? 481 HOH A O   1 
HETATM 2003 O  O   . HOH H 6 .   ? 25.490 -1.157 2.600  1.00 43.16 ? 482 HOH A O   1 
HETATM 2004 O  O   . HOH H 6 .   ? 13.169 29.402 28.306 1.00 46.95 ? 483 HOH A O   1 
HETATM 2005 O  O   . HOH H 6 .   ? 44.053 33.538 13.487 1.00 61.07 ? 484 HOH A O   1 
HETATM 2006 O  O   . HOH H 6 .   ? 8.643  27.236 46.641 1.00 45.62 ? 485 HOH A O   1 
HETATM 2007 O  O   . HOH H 6 .   ? 26.878 35.418 22.602 1.00 46.59 ? 486 HOH A O   1 
HETATM 2008 O  O   . HOH H 6 .   ? 42.946 22.118 17.108 1.00 48.78 ? 487 HOH A O   1 
HETATM 2009 O  O   . HOH H 6 .   ? 20.437 7.714  8.192  1.00 43.08 ? 488 HOH A O   1 
HETATM 2010 O  O   . HOH H 6 .   ? 38.044 31.887 8.555  1.00 51.33 ? 489 HOH A O   1 
HETATM 2011 O  O   . HOH H 6 .   ? 29.924 8.383  7.583  1.00 35.71 ? 490 HOH A O   1 
HETATM 2012 O  O   . HOH H 6 .   ? 21.343 9.960  1.785  1.00 53.45 ? 491 HOH A O   1 
HETATM 2013 O  O   . HOH H 6 .   ? 23.438 35.713 27.959 1.00 45.85 ? 492 HOH A O   1 
HETATM 2014 O  O   . HOH H 6 .   ? 46.647 22.370 25.079 1.00 44.75 ? 493 HOH A O   1 
HETATM 2015 O  O   . HOH H 6 .   ? 35.558 16.020 27.521 1.00 44.15 ? 494 HOH A O   1 
HETATM 2016 O  O   . HOH H 6 .   ? 24.928 26.737 9.572  1.00 40.66 ? 495 HOH A O   1 
HETATM 2017 O  O   . HOH H 6 .   ? 36.770 21.187 37.723 1.00 44.81 ? 496 HOH A O   1 
HETATM 2018 O  O   . HOH H 6 .   ? 38.306 18.480 19.826 1.00 39.12 ? 497 HOH A O   1 
HETATM 2019 O  O   . HOH H 6 .   ? 37.270 23.581 39.429 1.00 38.99 ? 498 HOH A O   1 
HETATM 2020 O  O   . HOH H 6 .   ? 23.517 19.084 27.827 1.00 43.60 ? 499 HOH A O   1 
HETATM 2021 O  O   . HOH H 6 .   ? 10.189 27.786 54.127 1.00 55.76 ? 500 HOH A O   1 
HETATM 2022 O  O   . HOH H 6 .   ? 10.218 26.178 49.537 1.00 46.93 ? 501 HOH A O   1 
HETATM 2023 O  O   . HOH H 6 .   ? 19.716 14.309 9.673  1.00 41.72 ? 502 HOH A O   1 
HETATM 2024 O  O   . HOH H 6 .   ? 45.509 18.826 20.076 1.00 69.01 ? 503 HOH A O   1 
HETATM 2025 O  O   . HOH H 6 .   ? 14.398 -1.045 12.750 1.00 63.00 ? 504 HOH A O   1 
HETATM 2026 O  O   . HOH H 6 .   ? 42.507 5.308  8.732  1.00 56.99 ? 505 HOH A O   1 
HETATM 2027 O  O   . HOH H 6 .   ? 18.880 12.359 8.043  1.00 46.51 ? 506 HOH A O   1 
HETATM 2028 O  O   . HOH H 6 .   ? 31.668 13.193 15.764 1.00 44.16 ? 507 HOH A O   1 
HETATM 2029 O  O   . HOH H 6 .   ? 19.928 5.035  3.099  1.00 45.96 ? 508 HOH A O   1 
HETATM 2030 O  O   . HOH H 6 .   ? 27.679 27.751 9.082  1.00 41.93 ? 509 HOH A O   1 
HETATM 2031 O  O   . HOH H 6 .   ? 4.139  37.905 24.918 1.00 56.10 ? 510 HOH A O   1 
HETATM 2032 O  O   . HOH H 6 .   ? 32.858 15.845 28.316 1.00 45.46 ? 511 HOH A O   1 
HETATM 2033 O  O   . HOH H 6 .   ? 46.695 32.951 17.019 1.00 43.06 ? 512 HOH A O   1 
HETATM 2034 O  O   . HOH H 6 .   ? 25.316 20.472 17.318 1.00 42.10 ? 513 HOH A O   1 
HETATM 2035 O  O   . HOH H 6 .   ? 46.101 23.711 20.383 1.00 40.65 ? 514 HOH A O   1 
HETATM 2036 O  O   . HOH H 6 .   ? 28.358 32.968 3.866  1.00 59.04 ? 515 HOH A O   1 
HETATM 2037 O  O   . HOH H 6 .   ? 40.429 29.119 11.292 1.00 48.74 ? 516 HOH A O   1 
HETATM 2038 O  O   . HOH H 6 .   ? 26.392 32.994 29.847 1.00 50.57 ? 517 HOH A O   1 
HETATM 2039 O  O   . HOH H 6 .   ? 39.559 19.327 12.474 1.00 43.19 ? 518 HOH A O   1 
HETATM 2040 O  O   . HOH H 6 .   ? 49.324 22.938 26.082 1.00 51.14 ? 519 HOH A O   1 
HETATM 2041 O  O   . HOH H 6 .   ? 15.793 6.321  1.139  1.00 58.27 ? 520 HOH A O   1 
HETATM 2042 O  O   . HOH H 6 .   ? 35.730 6.388  14.736 1.00 41.75 ? 521 HOH A O   1 
HETATM 2043 O  O   . HOH H 6 .   ? 41.125 18.566 20.810 1.00 57.56 ? 522 HOH A O   1 
HETATM 2044 O  O   . HOH H 6 .   ? 35.722 11.203 14.901 1.00 60.94 ? 523 HOH A O   1 
HETATM 2045 O  O   . HOH H 6 .   ? 11.031 14.970 11.198 1.00 49.93 ? 524 HOH A O   1 
HETATM 2046 O  O   . HOH H 6 .   ? 44.296 29.420 16.133 1.00 38.87 ? 525 HOH A O   1 
HETATM 2047 O  O   . HOH H 6 .   ? -1.158 34.985 24.187 1.00 67.68 ? 526 HOH A O   1 
HETATM 2048 O  O   . HOH H 6 .   ? 9.508  21.529 10.045 1.00 60.91 ? 527 HOH A O   1 
HETATM 2049 O  O   . HOH H 6 .   ? 6.905  21.215 25.722 1.00 61.17 ? 528 HOH A O   1 
HETATM 2050 O  O   . HOH H 6 .   ? 28.408 29.486 33.110 1.00 49.13 ? 529 HOH A O   1 
HETATM 2051 O  O   . HOH H 6 .   ? 3.479  38.042 20.330 1.00 48.79 ? 530 HOH A O   1 
HETATM 2052 O  O   . HOH H 6 .   ? 35.652 26.024 34.886 1.00 37.20 ? 531 HOH A O   1 
HETATM 2053 O  O   . HOH H 6 .   ? 34.030 25.056 6.157  1.00 56.64 ? 532 HOH A O   1 
HETATM 2054 O  O   . HOH H 6 .   ? 12.295 14.842 44.089 1.00 59.15 ? 533 HOH A O   1 
HETATM 2055 O  O   . HOH H 6 .   ? 18.516 14.589 29.377 1.00 52.44 ? 534 HOH A O   1 
HETATM 2056 O  O   . HOH H 6 .   ? 13.717 34.593 25.089 1.00 68.24 ? 535 HOH A O   1 
HETATM 2057 O  O   . HOH H 6 .   ? 14.556 15.767 42.973 1.00 56.60 ? 536 HOH A O   1 
HETATM 2058 O  O   . HOH H 6 .   ? 20.279 33.448 45.427 1.00 49.53 ? 537 HOH A O   1 
HETATM 2059 O  O   . HOH H 6 .   ? 24.311 6.676  0.253  1.00 63.32 ? 538 HOH A O   1 
HETATM 2060 O  O   . HOH H 6 .   ? 20.405 1.609  -0.380 1.00 42.19 ? 539 HOH A O   1 
HETATM 2061 O  O   . HOH H 6 .   ? 30.860 10.801 6.742  1.00 39.96 ? 540 HOH A O   1 
HETATM 2062 O  O   . HOH H 6 .   ? 35.268 28.389 36.335 1.00 55.42 ? 541 HOH A O   1 
HETATM 2063 O  O   . HOH H 6 .   ? 2.916  26.917 16.378 1.00 69.89 ? 542 HOH A O   1 
HETATM 2064 O  O   . HOH H 6 .   ? 2.737  29.438 16.872 1.00 72.56 ? 543 HOH A O   1 
HETATM 2065 O  O   . HOH H 6 .   ? 26.321 34.290 5.296  1.00 56.46 ? 544 HOH A O   1 
HETATM 2066 O  O   . HOH H 6 .   ? 6.031  29.050 45.601 1.00 59.03 ? 545 HOH A O   1 
HETATM 2067 O  O   . HOH H 6 .   ? 36.268 43.682 27.465 1.00 56.88 ? 546 HOH A O   1 
HETATM 2068 O  O   . HOH H 6 .   ? 33.705 23.798 35.810 1.00 51.20 ? 547 HOH A O   1 
HETATM 2069 O  O   . HOH H 6 .   ? 5.604  31.726 47.155 1.00 51.42 ? 548 HOH A O   1 
HETATM 2070 O  O   . HOH H 6 .   ? 33.386 26.267 9.201  1.00 48.85 ? 549 HOH A O   1 
HETATM 2071 O  O   . HOH H 6 .   ? 19.461 7.494  2.164  1.00 57.01 ? 550 HOH A O   1 
HETATM 2072 O  O   . HOH H 6 .   ? 31.553 28.523 7.924  1.00 53.29 ? 551 HOH A O   1 
HETATM 2073 O  O   . HOH H 6 .   ? 21.768 13.889 34.570 1.00 67.44 ? 552 HOH A O   1 
HETATM 2074 O  O   . HOH H 6 .   ? 38.265 39.503 19.722 1.00 47.71 ? 553 HOH A O   1 
HETATM 2075 O  O   . HOH H 6 .   ? 42.696 35.629 15.070 1.00 48.87 ? 554 HOH A O   1 
HETATM 2076 O  O   . HOH H 6 .   ? 38.899 16.584 13.364 1.00 57.82 ? 555 HOH A O   1 
HETATM 2077 O  O   . HOH H 6 .   ? 21.609 34.506 35.862 1.00 52.33 ? 556 HOH A O   1 
HETATM 2078 O  O   . HOH H 6 .   ? 16.166 14.765 38.327 1.00 53.27 ? 557 HOH A O   1 
HETATM 2079 O  O   . HOH H 6 .   ? 16.592 34.177 43.889 1.00 50.26 ? 558 HOH A O   1 
HETATM 2080 O  O   . HOH H 6 .   ? 16.374 22.130 32.336 1.00 40.23 ? 559 HOH A O   1 
HETATM 2081 O  O   . HOH H 6 .   ? 38.269 43.327 22.672 1.00 53.98 ? 560 HOH A O   1 
HETATM 2082 O  O   . HOH H 6 .   ? 45.803 31.353 15.051 1.00 45.44 ? 561 HOH A O   1 
HETATM 2083 O  O   . HOH H 6 .   ? 49.508 32.419 17.762 1.00 46.51 ? 562 HOH A O   1 
HETATM 2084 O  O   . HOH H 6 .   ? 28.001 31.326 29.221 1.00 46.02 ? 563 HOH A O   1 
HETATM 2085 O  O   . HOH H 6 .   ? 49.331 26.450 19.449 1.00 50.12 ? 564 HOH A O   1 
HETATM 2086 O  O   . HOH H 6 .   ? 35.155 40.719 20.132 1.00 58.24 ? 565 HOH A O   1 
HETATM 2087 O  O   . HOH H 6 .   ? 47.501 22.202 22.278 1.00 49.46 ? 566 HOH A O   1 
HETATM 2088 O  O   . HOH H 6 .   ? 32.538 13.998 13.050 1.00 37.73 ? 567 HOH A O   1 
HETATM 2089 O  O   . HOH H 6 .   ? 8.749  24.892 35.661 1.00 56.41 ? 568 HOH A O   1 
HETATM 2090 O  O   . HOH H 6 .   ? 45.171 26.836 16.784 1.00 43.01 ? 569 HOH A O   1 
HETATM 2091 O  O   . HOH H 6 .   ? 9.759  24.024 10.030 1.00 65.83 ? 570 HOH A O   1 
HETATM 2092 O  O   . HOH H 6 .   ? 46.127 18.368 23.763 1.00 65.83 ? 571 HOH A O   1 
HETATM 2093 O  O   . HOH H 6 .   ? 29.880 7.948  1.120  1.00 47.36 ? 572 HOH A O   1 
HETATM 2094 O  O   . HOH H 6 .   ? 15.473 14.355 40.625 1.00 56.33 ? 573 HOH A O   1 
HETATM 2095 O  O   . HOH H 6 .   ? 7.772  22.623 33.864 1.00 63.08 ? 574 HOH A O   1 
HETATM 2096 O  O   . HOH H 6 .   ? 29.144 29.465 30.962 1.00 48.80 ? 575 HOH A O   1 
HETATM 2097 O  O   . HOH H 6 .   ? 14.337 11.441 7.492  1.00 55.62 ? 576 HOH A O   1 
HETATM 2098 O  O   . HOH H 6 .   ? 32.143 10.780 4.521  1.00 53.10 ? 577 HOH A O   1 
HETATM 2099 O  O   . HOH H 6 .   ? 27.516 8.530  -0.136 1.00 61.39 ? 578 HOH A O   1 
HETATM 2100 O  O   . HOH H 6 .   ? 42.830 44.536 17.039 1.00 60.65 ? 579 HOH A O   1 
HETATM 2101 O  O   . HOH I 6 .   ? 14.806 17.477 25.170 1.00 44.51 ? 301 HOH P O   1 
HETATM 2102 O  O   . HOH I 6 .   ? 23.290 11.244 25.702 1.00 43.37 ? 302 HOH P O   1 
HETATM 2103 O  O   . HOH I 6 .   ? 21.096 14.520 28.254 1.00 44.35 ? 303 HOH P O   1 
HETATM 2104 O  O   . HOH I 6 .   ? 29.453 17.584 22.326 1.00 38.40 ? 304 HOH P O   1 
HETATM 2105 O  O   . HOH I 6 .   ? 22.861 16.416 22.360 1.00 39.72 ? 305 HOH P O   1 
HETATM 2106 O  O   . HOH I 6 .   ? 27.598 12.797 27.335 1.00 45.77 ? 306 HOH P O   1 
HETATM 2107 O  O   . HOH I 6 .   ? 27.230 16.204 21.580 1.00 40.23 ? 307 HOH P O   1 
HETATM 2108 O  O   . HOH I 6 .   ? 31.194 15.652 21.279 1.00 45.99 ? 308 HOH P O   1 
HETATM 2109 O  O   . HOH I 6 .   ? 20.777 12.046 26.903 1.00 42.53 ? 309 HOH P O   1 
HETATM 2110 O  O   . HOH I 6 .   ? 27.220 16.814 29.476 1.00 58.13 ? 310 HOH P O   1 
HETATM 2111 O  O   . HOH I 6 .   ? 25.504 13.754 27.534 1.00 53.29 ? 311 HOH P O   1 
HETATM 2112 O  O   . HOH I 6 .   ? 22.558 6.084  27.106 1.00 55.55 ? 312 HOH P O   1 
HETATM 2113 O  O   . HOH I 6 .   ? 24.637 8.222  26.144 1.00 56.62 ? 313 HOH P O   1 
HETATM 2114 O  O   . HOH I 6 .   ? 26.350 7.309  24.861 1.00 47.62 ? 314 HOH P O   1 
# 
