data_8QS4
# 
_entry.id   8QS4 
# 
_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   8QS4         pdb_00008qs4 10.2210/pdb8qs4/pdb 
WWPDB D_1292132192 ?            ?                   
# 
_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                        8QS4 
_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    2   ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                                                 24.305    4   ? ? ? ? 
5 non-polymer syn '~{N}-[[1-(4-bromophenyl)sulfonylpiperidin-4-yl]methyl]-2-chloranyl-ethanamide' 409.726   1   ? ? ? ? 
6 water       nat water                                                                           18.015    117 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Epithelial cell marker protein 1,Stratifin' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
A ? 
2 'polypeptide(L)' no yes 'QRST(SEP)TPNVH' QRSTSTPNVH P ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CHLORIDE ION'                                                                  CL  
4 'MAGNESIUM ION'                                                                 MG  
5 '~{N}-[[1-(4-bromophenyl)sulfonylpiperidin-4-yl]methyl]-2-chloranyl-ethanamide' WPN 
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 
WPN non-polymer         . '~{N}-[[1-(4-bromophenyl)sulfonylpiperidin-4-yl]methyl]-2-chloranyl-ethanamide' ?               
'C14 H18 Br Cl N2 O3 S' 409.726 
# 
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  ?   ?   ?   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        WPN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WPN 
_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   301 233 CL  CL  A . 
D 3 CL  1   302 234 CL  CL  A . 
E 4 MG  1   303 236 MG  MG  A . 
F 4 MG  1   304 237 MG  MG  A . 
G 4 MG  1   305 238 MG  MG  A . 
H 5 WPN 1   306 239 WPN 853 A . 
I 4 MG  1   307 1   MG  MG  A . 
J 6 HOH 1   401 115 HOH HOH A . 
J 6 HOH 2   402 61  HOH HOH A . 
J 6 HOH 3   403 9   HOH HOH A . 
J 6 HOH 4   404 116 HOH HOH A . 
J 6 HOH 5   405 119 HOH HOH A . 
J 6 HOH 6   406 121 HOH HOH A . 
J 6 HOH 7   407 83  HOH HOH A . 
J 6 HOH 8   408 96  HOH HOH A . 
J 6 HOH 9   409 88  HOH HOH A . 
J 6 HOH 10  410 26  HOH HOH A . 
J 6 HOH 11  411 95  HOH HOH A . 
J 6 HOH 12  412 11  HOH HOH A . 
J 6 HOH 13  413 31  HOH HOH A . 
J 6 HOH 14  414 42  HOH HOH A . 
J 6 HOH 15  415 28  HOH HOH A . 
J 6 HOH 16  416 39  HOH HOH A . 
J 6 HOH 17  417 127 HOH HOH A . 
J 6 HOH 18  418 52  HOH HOH A . 
J 6 HOH 19  419 54  HOH HOH A . 
J 6 HOH 20  420 24  HOH HOH A . 
J 6 HOH 21  421 55  HOH HOH A . 
J 6 HOH 22  422 92  HOH HOH A . 
J 6 HOH 23  423 4   HOH HOH A . 
J 6 HOH 24  424 36  HOH HOH A . 
J 6 HOH 25  425 44  HOH HOH A . 
J 6 HOH 26  426 120 HOH HOH A . 
J 6 HOH 27  427 41  HOH HOH A . 
J 6 HOH 28  428 108 HOH HOH A . 
J 6 HOH 29  429 85  HOH HOH A . 
J 6 HOH 30  430 12  HOH HOH A . 
J 6 HOH 31  431 109 HOH HOH A . 
J 6 HOH 32  432 63  HOH HOH A . 
J 6 HOH 33  433 69  HOH HOH A . 
J 6 HOH 34  434 20  HOH HOH A . 
J 6 HOH 35  435 30  HOH HOH A . 
J 6 HOH 36  436 7   HOH HOH A . 
J 6 HOH 37  437 117 HOH HOH A . 
J 6 HOH 38  438 58  HOH HOH A . 
J 6 HOH 39  439 40  HOH HOH A . 
J 6 HOH 40  440 32  HOH HOH A . 
J 6 HOH 41  441 49  HOH HOH A . 
J 6 HOH 42  442 57  HOH HOH A . 
J 6 HOH 43  443 73  HOH HOH A . 
J 6 HOH 44  444 3   HOH HOH A . 
J 6 HOH 45  445 70  HOH HOH A . 
J 6 HOH 46  446 23  HOH HOH A . 
J 6 HOH 47  447 34  HOH HOH A . 
J 6 HOH 48  448 10  HOH HOH A . 
J 6 HOH 49  449 8   HOH HOH A . 
J 6 HOH 50  450 93  HOH HOH A . 
J 6 HOH 51  451 5   HOH HOH A . 
J 6 HOH 52  452 104 HOH HOH A . 
J 6 HOH 53  453 114 HOH HOH A . 
J 6 HOH 54  454 72  HOH HOH A . 
J 6 HOH 55  455 37  HOH HOH A . 
J 6 HOH 56  456 38  HOH HOH A . 
J 6 HOH 57  457 98  HOH HOH A . 
J 6 HOH 58  458 33  HOH HOH A . 
J 6 HOH 59  459 19  HOH HOH A . 
J 6 HOH 60  460 2   HOH HOH A . 
J 6 HOH 61  461 53  HOH HOH A . 
J 6 HOH 62  462 86  HOH HOH A . 
J 6 HOH 63  463 84  HOH HOH A . 
J 6 HOH 64  464 14  HOH HOH A . 
J 6 HOH 65  465 6   HOH HOH A . 
J 6 HOH 66  466 13  HOH HOH A . 
J 6 HOH 67  467 76  HOH HOH A . 
J 6 HOH 68  468 18  HOH HOH A . 
J 6 HOH 69  469 80  HOH HOH A . 
J 6 HOH 70  470 43  HOH HOH A . 
J 6 HOH 71  471 71  HOH HOH A . 
J 6 HOH 72  472 21  HOH HOH A . 
J 6 HOH 73  473 29  HOH HOH A . 
J 6 HOH 74  474 16  HOH HOH A . 
J 6 HOH 75  475 90  HOH HOH A . 
J 6 HOH 76  476 45  HOH HOH A . 
J 6 HOH 77  477 1   HOH HOH A . 
J 6 HOH 78  478 81  HOH HOH A . 
J 6 HOH 79  479 97  HOH HOH A . 
J 6 HOH 80  480 62  HOH HOH A . 
J 6 HOH 81  481 46  HOH HOH A . 
J 6 HOH 82  482 118 HOH HOH A . 
J 6 HOH 83  483 89  HOH HOH A . 
J 6 HOH 84  484 124 HOH HOH A . 
J 6 HOH 85  485 107 HOH HOH A . 
J 6 HOH 86  486 128 HOH HOH A . 
J 6 HOH 87  487 22  HOH HOH A . 
J 6 HOH 88  488 59  HOH HOH A . 
J 6 HOH 89  489 113 HOH HOH A . 
J 6 HOH 90  490 50  HOH HOH A . 
J 6 HOH 91  491 106 HOH HOH A . 
J 6 HOH 92  492 91  HOH HOH A . 
J 6 HOH 93  493 68  HOH HOH A . 
J 6 HOH 94  494 87  HOH HOH A . 
J 6 HOH 95  495 74  HOH HOH A . 
J 6 HOH 96  496 75  HOH HOH A . 
J 6 HOH 97  497 47  HOH HOH A . 
J 6 HOH 98  498 82  HOH HOH A . 
J 6 HOH 99  499 99  HOH HOH A . 
J 6 HOH 100 500 51  HOH HOH A . 
J 6 HOH 101 501 64  HOH HOH A . 
J 6 HOH 102 502 65  HOH HOH A . 
J 6 HOH 103 503 17  HOH HOH A . 
J 6 HOH 104 504 77  HOH HOH A . 
J 6 HOH 105 505 25  HOH HOH A . 
J 6 HOH 106 506 111 HOH HOH A . 
J 6 HOH 107 507 101 HOH HOH A . 
J 6 HOH 108 508 105 HOH HOH A . 
J 6 HOH 109 509 35  HOH HOH A . 
J 6 HOH 110 510 103 HOH HOH A . 
K 6 HOH 1   301 27  HOH HOH P . 
K 6 HOH 2   302 112 HOH HOH P . 
K 6 HOH 3   303 15  HOH HOH P . 
K 6 HOH 4   304 94  HOH HOH P . 
K 6 HOH 5   305 60  HOH HOH P . 
K 6 HOH 6   306 66  HOH HOH P . 
K 6 HOH 7   307 123 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                     8QS4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.300 
_cell.length_a_esd                 ? 
_cell.length_b                     149.224 
_cell.length_b_esd                 ? 
_cell.length_c                     76.442 
_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                         8QS4 
_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                   8QS4 
_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             3.20 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.57 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.095 M HEPES pH=7.1-7.7
0.19 M CaCl2 
5% glycerol
24-29% PEG400
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-30 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.885603 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.885603 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QS4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               76.44 
_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                                     24193 
_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                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.9 
_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                                    2.00 
_reflns_shell.d_res_low                                     2.05 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1791 
_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                                  0.916 
_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                                 8QS4 
_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                            2.00 
_refine.ls_d_res_low                             34.02 
_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                     24170 
_refine.ls_number_reflns_R_free                  1209 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.52 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2135 
_refine.ls_R_factor_R_free                       0.2435 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2119 
_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                          1.34 
_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                 29.74 
_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                            0.26 
_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                       2.00 
_refine_hist.d_res_low                        34.02 
_refine_hist.number_atoms_solvent             117 
_refine_hist.number_atoms_total               2029 
_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        1885 
_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' ? 0.007 ? 428 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.889 ? 454 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.432 ? 276 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045 ? 288 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007 ? 336 ? 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' 2.00 2.08  . . 147 2546 100.00 . . . . 0.2938 . . . . . . . . . . . 0.3062 
'X-RAY DIFFRACTION' 2.08 2.17  . . 139 2534 100.00 . . . . 0.2511 . . . . . . . . . . . 0.3034 
'X-RAY DIFFRACTION' 2.17 2.29  . . 118 2226 87.00  . . . . 0.2415 . . . . . . . . . . . 0.2993 
'X-RAY DIFFRACTION' 2.29 2.43  . . 132 2556 100.00 . . . . 0.2307 . . . . . . . . . . . 0.3057 
'X-RAY DIFFRACTION' 2.43 2.62  . . 142 2572 100.00 . . . . 0.2520 . . . . . . . . . . . 0.2715 
'X-RAY DIFFRACTION' 2.62 2.88  . . 116 2580 100.00 . . . . 0.2419 . . . . . . . . . . . 0.3114 
'X-RAY DIFFRACTION' 2.88 3.30  . . 125 2611 100.00 . . . . 0.2359 . . . . . . . . . . . 0.2365 
'X-RAY DIFFRACTION' 3.30 4.16  . . 140 2609 100.00 . . . . 0.1944 . . . . . . . . . . . 0.2409 
'X-RAY DIFFRACTION' 4.16 34.02 . . 150 2727 100.00 . . . . 0.1833 . . . . . . . . . . . 0.2009 
# 
_struct.entry_id                     8QS4 
_struct.title                        'Ternary structure of 14-3-3s, C-RAF phosphopeptide (pS259) and compound 22 (1083853)' 
_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        8QS4 
_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 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
I N N 4 ? 
J N N 6 ? 
K 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 8QS4        8QS4   ? 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 8QS4 A 6 ? 236 ? P31947 1   ? 231 ? 1   231 
2 2 8QS4 P 1 ? 10  ? 8QS4   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 8QS4 GLY A 1 ? UNP P31947 ? ? 'expression tag' -4 1 
1 8QS4 ALA A 2 ? UNP P31947 ? ? 'expression tag' -3 2 
1 8QS4 MET A 3 ? UNP P31947 ? ? 'expression tag' -2 3 
1 8QS4 GLY A 4 ? UNP P31947 ? ? 'expression tag' -1 4 
1 8QS4 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)' 6070  ? 
1 MORE         -95   ? 
1 'SSA (A^2)'  22540 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_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 62.3000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 76.4420000000 
# 
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 H WPN . C2 ? ? A CYS 38  A WPN 306 1_555 ? ? ? ? ? ? ? 1.773 ? ? 
covale2 covale both ? B THR 4  C   ? ? ? 1_555 B SEP 5 N  ? ? P THR 258 P SEP 259 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale3 covale both ? B SEP 5  C   ? ? ? 1_555 B THR 6 N  ? ? P SEP 259 P THR 260 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
metalc1 metalc ?    ? A GLY 4  O   ? ? ? 1_555 I MG  . MG ? ? A GLY -1  A MG  307 1_555 ? ? ? ? ? ? ? 2.845 ? ? 
metalc2 metalc ?    ? A GLU 7  OE2 ? ? ? 1_555 E MG  . MG ? ? A GLU 2   A MG  303 6_655 ? ? ? ? ? ? ? 2.874 ? ? 
metalc3 metalc ?    ? E MG  .  MG  ? ? ? 1_555 J HOH . O  ? ? A MG  303 A HOH 502 1_555 ? ? ? ? ? ? ? 2.735 ? ? 
metalc4 metalc ?    ? G MG  .  MG  ? ? ? 1_555 J HOH . O  ? ? A MG  305 A HOH 510 1_555 ? ? ? ? ? ? ? 2.370 ? ? 
metalc5 metalc ?    ? I MG  .  MG  ? ? ? 1_555 J HOH . O  ? ? A MG  307 A HOH 422 8_556 ? ? ? ? ? ? ? 2.881 ? ? 
metalc6 metalc ?    ? I MG  .  MG  ? ? ? 1_555 J HOH . O  ? ? A MG  307 A HOH 496 1_555 ? ? ? ? ? ? ? 2.967 ? ? 
# 
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 O   ? A GLY 4 ? A GLY -1  ? 1_555 MG ? I MG . ? A MG 307 ? 1_555 O ? J HOH . ? A HOH 422 ? 8_556 73.0  ? 
2 O   ? A GLY 4 ? A GLY -1  ? 1_555 MG ? I MG . ? A MG 307 ? 1_555 O ? J HOH . ? A HOH 496 ? 1_555 97.5  ? 
3 O   ? J HOH . ? A HOH 422 ? 8_556 MG ? I MG . ? A MG 307 ? 1_555 O ? J HOH . ? A HOH 496 ? 1_555 156.3 ? 
4 OE2 ? A GLU 7 ? A GLU 2   ? 1_555 MG ? E MG . ? A MG 303 ? 6_655 O ? J HOH . ? A HOH 502 ? 1_555 71.1  ? 
# 
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 WPN H . ? CYS A 43 ? WPN A 306 ? 1_555 CYS A 38 ? 1_555 C2 SG CYS 1 WPN None            'Covalent chemical modification' 
# 
_pdbx_entry_details.entry_id                   8QS4 
_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 ? ? -134.37 -39.26 
2 1 THR A 136 ? ? -130.21 -62.60 
3 1 SER A 212 ? ? -140.21 13.90  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     441 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   J 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 71 ? A GLU 76 
2 1 Y 1 A GLU 72 ? A GLU 77 
3 1 Y 1 A GLY 73 ? A GLY 78 
4 1 Y 1 A SER 74 ? A SER 79 
5 1 Y 1 A GLU 75 ? A GLU 80 
6 1 Y 1 A GLU 76 ? A GLU 81 
7 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 
WPN C1   C  N N 412 
WPN C2   C  N N 413 
WPN C3   C  N N 414 
WPN C4   C  N N 415 
WPN C5   C  N N 416 
WPN C6   C  N N 417 
WPN C10  C  Y N 418 
WPN C11  C  Y N 419 
WPN C14  C  N N 420 
WPN C12  C  Y N 421 
WPN C13  C  N N 422 
WPN C7   C  Y N 423 
WPN C8   C  Y N 424 
WPN C9   C  Y N 425 
WPN N1   N  N N 426 
WPN N2   N  N N 427 
WPN O1   O  N N 428 
WPN O2   O  N N 429 
WPN O3   O  N N 430 
WPN S1   S  N N 431 
WPN BR1  BR N N 432 
WPN H1   H  N N 433 
WPN H2   H  N N 434 
WPN H4   H  N N 435 
WPN H5   H  N N 436 
WPN H6   H  N N 437 
WPN H7   H  N N 438 
WPN H8   H  N N 439 
WPN H9   H  N N 440 
WPN H10  H  N N 441 
WPN H11  H  N N 442 
WPN H12  H  N N 443 
WPN H13  H  N N 444 
WPN H14  H  N N 445 
WPN H15  H  N N 446 
WPN H16  H  N N 447 
WPN H17  H  N N 448 
WPN H18  H  N N 449 
WPN H19  H  N N 450 
WPN CL1  CL N N 451 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SEP N   CA   sing N N 277 
SEP N   H    sing N N 278 
SEP N   H2   sing N N 279 
SEP CA  CB   sing N N 280 
SEP CA  C    sing N N 281 
SEP CA  HA   sing N N 282 
SEP CB  OG   sing N N 283 
SEP CB  HB2  sing N N 284 
SEP CB  HB3  sing N N 285 
SEP OG  P    sing N N 286 
SEP C   O    doub N N 287 
SEP C   OXT  sing N N 288 
SEP OXT HXT  sing N N 289 
SEP P   O1P  doub N N 290 
SEP P   O2P  sing N N 291 
SEP P   O3P  sing N N 292 
SEP O2P HOP2 sing N N 293 
SEP O3P HOP3 sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
THR N   CA   sing N N 308 
THR N   H    sing N N 309 
THR N   H2   sing N N 310 
THR CA  C    sing N N 311 
THR CA  CB   sing N N 312 
THR CA  HA   sing N N 313 
THR C   O    doub N N 314 
THR C   OXT  sing N N 315 
THR CB  OG1  sing N N 316 
THR CB  CG2  sing N N 317 
THR CB  HB   sing N N 318 
THR OG1 HG1  sing N N 319 
THR CG2 HG21 sing N N 320 
THR CG2 HG22 sing N N 321 
THR CG2 HG23 sing N N 322 
THR OXT HXT  sing N N 323 
TRP N   CA   sing N N 324 
TRP N   H    sing N N 325 
TRP N   H2   sing N N 326 
TRP CA  C    sing N N 327 
TRP CA  CB   sing N N 328 
TRP CA  HA   sing N N 329 
TRP C   O    doub N N 330 
TRP C   OXT  sing N N 331 
TRP CB  CG   sing N N 332 
TRP CB  HB2  sing N N 333 
TRP CB  HB3  sing N N 334 
TRP CG  CD1  doub Y N 335 
TRP CG  CD2  sing Y N 336 
TRP CD1 NE1  sing Y N 337 
TRP CD1 HD1  sing N N 338 
TRP CD2 CE2  doub Y N 339 
TRP CD2 CE3  sing Y N 340 
TRP NE1 CE2  sing Y N 341 
TRP NE1 HE1  sing N N 342 
TRP CE2 CZ2  sing Y N 343 
TRP CE3 CZ3  doub Y N 344 
TRP CE3 HE3  sing N N 345 
TRP CZ2 CH2  doub Y N 346 
TRP CZ2 HZ2  sing N N 347 
TRP CZ3 CH2  sing Y N 348 
TRP CZ3 HZ3  sing N N 349 
TRP CH2 HH2  sing N N 350 
TRP OXT HXT  sing N N 351 
TYR N   CA   sing N N 352 
TYR N   H    sing N N 353 
TYR N   H2   sing N N 354 
TYR CA  C    sing N N 355 
TYR CA  CB   sing N N 356 
TYR CA  HA   sing N N 357 
TYR C   O    doub N N 358 
TYR C   OXT  sing N N 359 
TYR CB  CG   sing N N 360 
TYR CB  HB2  sing N N 361 
TYR CB  HB3  sing N N 362 
TYR CG  CD1  doub Y N 363 
TYR CG  CD2  sing Y N 364 
TYR CD1 CE1  sing Y N 365 
TYR CD1 HD1  sing N N 366 
TYR CD2 CE2  doub Y N 367 
TYR CD2 HD2  sing N N 368 
TYR CE1 CZ   doub Y N 369 
TYR CE1 HE1  sing N N 370 
TYR CE2 CZ   sing Y N 371 
TYR CE2 HE2  sing N N 372 
TYR CZ  OH   sing N N 373 
TYR OH  HH   sing N N 374 
TYR OXT HXT  sing N N 375 
VAL N   CA   sing N N 376 
VAL N   H    sing N N 377 
VAL N   H2   sing N N 378 
VAL CA  C    sing N N 379 
VAL CA  CB   sing N N 380 
VAL CA  HA   sing N N 381 
VAL C   O    doub N N 382 
VAL C   OXT  sing N N 383 
VAL CB  CG1  sing N N 384 
VAL CB  CG2  sing N N 385 
VAL CB  HB   sing N N 386 
VAL CG1 HG11 sing N N 387 
VAL CG1 HG12 sing N N 388 
VAL CG1 HG13 sing N N 389 
VAL CG2 HG21 sing N N 390 
VAL CG2 HG22 sing N N 391 
VAL CG2 HG23 sing N N 392 
VAL OXT HXT  sing N N 393 
WPN O1  C1   doub N N 394 
WPN C2  C1   sing N N 395 
WPN C1  N1   sing N N 396 
WPN N1  C3   sing N N 397 
WPN C5  C6   sing N N 398 
WPN C5  C4   sing N N 399 
WPN C3  C4   sing N N 400 
WPN C6  N2   sing N N 401 
WPN C4  C14  sing N N 402 
WPN O3  S1   doub N N 403 
WPN N2  S1   sing N N 404 
WPN N2  C13  sing N N 405 
WPN C8  C9   doub Y N 406 
WPN C8  C7   sing Y N 407 
WPN S1  C7   sing N N 408 
WPN S1  O2   doub N N 409 
WPN C14 C13  sing N N 410 
WPN C9  C10  sing Y N 411 
WPN C7  C12  doub Y N 412 
WPN C10 BR1  sing N N 413 
WPN C10 C11  doub Y N 414 
WPN C12 C11  sing Y N 415 
WPN C2  H1   sing N N 416 
WPN C2  H2   sing N N 417 
WPN C3  H4   sing N N 418 
WPN C3  H5   sing N N 419 
WPN C4  H6   sing N N 420 
WPN C5  H7   sing N N 421 
WPN C5  H8   sing N N 422 
WPN C6  H9   sing N N 423 
WPN C6  H10  sing N N 424 
WPN C11 H11  sing N N 425 
WPN C14 H12  sing N N 426 
WPN C14 H13  sing N N 427 
WPN C12 H14  sing N N 428 
WPN C13 H15  sing N N 429 
WPN C13 H16  sing N N 430 
WPN C8  H17  sing N N 431 
WPN C9  H18  sing N N 432 
WPN N1  H19  sing N N 433 
WPN 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   3IQV 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8QS4 
_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]   0.016051 
_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]   0.006701 
_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]   0.013082 
_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 
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   ? 35.349 41.458 24.704 1.00 61.58 ? -4  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1   ? 35.212 40.391 25.679 1.00 59.64 ? -4  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1   ? 36.464 40.183 26.506 1.00 56.78 ? -4  GLY A C   1 
ATOM   4    O  O   . GLY A 1 1   ? 37.505 40.786 26.232 1.00 57.27 ? -4  GLY A O   1 
ATOM   5    N  N   . ALA A 1 2   ? 36.359 39.315 27.517 1.00 57.38 ? -3  ALA A N   1 
ATOM   6    C  CA  . ALA A 1 2   ? 37.479 39.042 28.411 1.00 54.43 ? -3  ALA A CA  1 
ATOM   7    C  C   . ALA A 1 2   ? 38.623 38.321 27.712 1.00 50.55 ? -3  ALA A C   1 
ATOM   8    O  O   . ALA A 1 2   ? 39.756 38.363 28.204 1.00 52.38 ? -3  ALA A O   1 
ATOM   9    C  CB  . ALA A 1 2   ? 37.003 38.218 29.606 1.00 49.80 ? -3  ALA A CB  1 
ATOM   10   N  N   . MET A 1 3   ? 38.355 37.657 26.591 1.00 48.80 ? -2  MET A N   1 
ATOM   11   C  CA  . MET A 1 3   ? 39.374 36.947 25.825 1.00 47.28 ? -2  MET A CA  1 
ATOM   12   C  C   . MET A 1 3   ? 39.936 37.779 24.680 1.00 47.48 ? -2  MET A C   1 
ATOM   13   O  O   . MET A 1 3   ? 40.723 37.265 23.876 1.00 45.45 ? -2  MET A O   1 
ATOM   14   C  CB  . MET A 1 3   ? 38.796 35.647 25.275 1.00 46.91 ? -2  MET A CB  1 
ATOM   15   C  CG  . MET A 1 3   ? 38.301 34.701 26.352 1.00 43.69 ? -2  MET A CG  1 
ATOM   16   S  SD  . MET A 1 3   ? 39.575 34.325 27.566 1.00 46.55 ? -2  MET A SD  1 
ATOM   17   C  CE  . MET A 1 3   ? 38.598 33.447 28.766 1.00 42.74 ? -2  MET A CE  1 
ATOM   18   N  N   . GLY A 1 4   ? 39.562 39.058 24.598 1.00 51.52 ? -1  GLY A N   1 
ATOM   19   C  CA  . GLY A 1 4   ? 39.873 39.846 23.414 1.00 45.79 ? -1  GLY A CA  1 
ATOM   20   C  C   . GLY A 1 4   ? 41.355 40.013 23.147 1.00 45.14 ? -1  GLY A C   1 
ATOM   21   O  O   . GLY A 1 4   ? 41.768 40.115 21.988 1.00 42.10 ? -1  GLY A O   1 
ATOM   22   N  N   . SER A 1 5   ? 42.180 40.030 24.200 1.00 39.19 ? 0   SER A N   1 
ATOM   23   C  CA  . SER A 1 5   ? 43.608 40.277 24.024 1.00 38.67 ? 0   SER A CA  1 
ATOM   24   C  C   . SER A 1 5   ? 44.418 39.013 23.757 1.00 41.67 ? 0   SER A C   1 
ATOM   25   O  O   . SER A 1 5   ? 45.618 39.113 23.472 1.00 40.41 ? 0   SER A O   1 
ATOM   26   C  CB  . SER A 1 5   ? 44.182 41.003 25.249 1.00 39.80 ? 0   SER A CB  1 
ATOM   27   O  OG  . SER A 1 5   ? 44.206 40.160 26.393 1.00 45.02 ? 0   SER A OG  1 
ATOM   28   N  N   . MET A 1 6   ? 43.802 37.835 23.824 1.00 42.09 ? 1   MET A N   1 
ATOM   29   C  CA  . MET A 1 6   ? 44.537 36.586 23.688 1.00 41.80 ? 1   MET A CA  1 
ATOM   30   C  C   . MET A 1 6   ? 44.505 36.085 22.250 1.00 39.13 ? 1   MET A C   1 
ATOM   31   O  O   . MET A 1 6   ? 43.493 36.186 21.551 1.00 36.44 ? 1   MET A O   1 
ATOM   32   C  CB  . MET A 1 6   ? 43.985 35.509 24.634 1.00 41.73 ? 1   MET A CB  1 
ATOM   33   C  CG  . MET A 1 6   ? 45.051 34.542 25.105 1.00 40.53 ? 1   MET A CG  1 
ATOM   34   S  SD  . MET A 1 6   ? 44.395 33.123 26.011 1.00 44.20 ? 1   MET A SD  1 
ATOM   35   C  CE  . MET A 1 6   ? 43.391 33.951 27.229 1.00 41.55 ? 1   MET A CE  1 
ATOM   36   N  N   . GLU A 1 7   ? 45.636 35.565 21.811 1.00 40.55 ? 2   GLU A N   1 
ATOM   37   C  CA  . GLU A 1 7   ? 45.741 35.031 20.464 1.00 40.93 ? 2   GLU A CA  1 
ATOM   38   C  C   . GLU A 1 7   ? 44.836 33.818 20.276 1.00 41.97 ? 2   GLU A C   1 
ATOM   39   O  O   . GLU A 1 7   ? 44.735 32.956 21.152 1.00 35.70 ? 2   GLU A O   1 
ATOM   40   C  CB  . GLU A 1 7   ? 47.191 34.674 20.195 1.00 41.47 ? 2   GLU A CB  1 
ATOM   41   C  CG  . GLU A 1 7   ? 47.945 35.806 19.523 1.00 46.31 ? 2   GLU A CG  1 
ATOM   42   C  CD  . GLU A 1 7   ? 49.383 35.448 19.302 1.00 50.61 ? 2   GLU A CD  1 
ATOM   43   O  OE1 . GLU A 1 7   ? 49.794 34.354 19.801 1.00 55.91 ? 2   GLU A OE1 1 
ATOM   44   O  OE2 . GLU A 1 7   ? 50.092 36.229 18.650 1.00 45.80 ? 2   GLU A OE2 1 
ATOM   45   N  N   . ARG A 1 8   ? 44.174 33.767 19.119 1.00 38.36 ? 3   ARG A N   1 
ATOM   46   C  CA  . ARG A 1 8   ? 43.291 32.646 18.784 1.00 41.39 ? 3   ARG A CA  1 
ATOM   47   C  C   . ARG A 1 8   ? 43.930 31.287 19.062 1.00 38.06 ? 3   ARG A C   1 
ATOM   48   O  O   . ARG A 1 8   ? 43.281 30.398 19.622 1.00 40.14 ? 3   ARG A O   1 
ATOM   49   C  CB  . ARG A 1 8   ? 42.860 32.725 17.313 1.00 41.04 ? 3   ARG A CB  1 
ATOM   50   C  CG  . ARG A 1 8   ? 41.716 31.758 16.968 1.00 41.38 ? 3   ARG A CG  1 
ATOM   51   C  CD  . ARG A 1 8   ? 41.563 31.592 15.457 1.00 42.02 ? 3   ARG A CD  1 
ATOM   52   N  NE  . ARG A 1 8   ? 40.364 30.846 15.086 1.00 40.45 ? 3   ARG A NE  1 
ATOM   53   C  CZ  . ARG A 1 8   ? 40.278 29.522 15.086 1.00 45.59 ? 3   ARG A CZ  1 
ATOM   54   N  NH1 . ARG A 1 8   ? 41.285 28.762 15.496 1.00 42.54 ? 3   ARG A NH1 1 
ATOM   55   N  NH2 . ARG A 1 8   ? 39.155 28.945 14.664 1.00 44.17 ? 3   ARG A NH2 1 
ATOM   56   N  N   . ALA A 1 9   ? 45.191 31.096 18.681 1.00 37.89 ? 4   ALA A N   1 
ATOM   57   C  CA  . ALA A 1 9   ? 45.794 29.779 18.876 1.00 42.42 ? 4   ALA A CA  1 
ATOM   58   C  C   . ALA A 1 9   ? 45.981 29.459 20.355 1.00 42.98 ? 4   ALA A C   1 
ATOM   59   O  O   . ALA A 1 9   ? 45.898 28.291 20.754 1.00 40.08 ? 4   ALA A O   1 
ATOM   60   C  CB  . ALA A 1 9   ? 47.130 29.685 18.141 1.00 40.44 ? 4   ALA A CB  1 
ATOM   61   N  N   . SER A 1 10  ? 46.248 30.478 21.172 1.00 40.52 ? 5   SER A N   1 
ATOM   62   C  CA  . SER A 1 10  ? 46.346 30.289 22.610 1.00 37.63 ? 5   SER A CA  1 
ATOM   63   C  C   . SER A 1 10  ? 44.986 29.986 23.213 1.00 40.05 ? 5   SER A C   1 
ATOM   64   O  O   . SER A 1 10  ? 44.877 29.182 24.150 1.00 38.26 ? 5   SER A O   1 
ATOM   65   C  CB  . SER A 1 10  ? 46.949 31.537 23.261 1.00 40.27 ? 5   SER A CB  1 
ATOM   66   O  OG  . SER A 1 10  ? 48.277 31.731 22.822 1.00 41.36 ? 5   SER A OG  1 
ATOM   67   N  N   . LEU A 1 11  ? 43.937 30.620 22.692 1.00 34.91 ? 6   LEU A N   1 
ATOM   68   C  CA  . LEU A 1 11  ? 42.592 30.295 23.144 1.00 34.58 ? 6   LEU A CA  1 
ATOM   69   C  C   . LEU A 1 11  ? 42.271 28.820 22.886 1.00 40.83 ? 6   LEU A C   1 
ATOM   70   O  O   . LEU A 1 11  ? 41.804 28.108 23.789 1.00 38.00 ? 6   LEU A O   1 
ATOM   71   C  CB  . LEU A 1 11  ? 41.584 31.220 22.470 1.00 35.72 ? 6   LEU A CB  1 
ATOM   72   C  CG  . LEU A 1 11  ? 41.597 32.627 23.105 1.00 37.64 ? 6   LEU A CG  1 
ATOM   73   C  CD1 . LEU A 1 11  ? 40.922 33.636 22.200 1.00 37.07 ? 6   LEU A CD1 1 
ATOM   74   C  CD2 . LEU A 1 11  ? 40.935 32.599 24.475 1.00 34.84 ? 6   LEU A CD2 1 
ATOM   75   N  N   . ILE A 1 12  ? 42.573 28.328 21.679 1.00 39.47 ? 7   ILE A N   1 
ATOM   76   C  CA  . ILE A 1 12  ? 42.309 26.920 21.363 1.00 38.41 ? 7   ILE A CA  1 
ATOM   77   C  C   . ILE A 1 12  ? 43.123 26.013 22.269 1.00 39.67 ? 7   ILE A C   1 
ATOM   78   O  O   . ILE A 1 12  ? 42.613 25.019 22.805 1.00 36.49 ? 7   ILE A O   1 
ATOM   79   C  CB  . ILE A 1 12  ? 42.615 26.612 19.893 1.00 38.09 ? 7   ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 12  ? 41.764 27.466 18.943 1.00 38.35 ? 7   ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 12  ? 42.397 25.118 19.646 1.00 38.01 ? 7   ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 12  ? 40.288 27.260 19.104 1.00 36.68 ? 7   ILE A CD1 1 
ATOM   83   N  N   . GLN A 1 13  ? 44.411 26.333 22.425 1.00 39.49 ? 8   GLN A N   1 
ATOM   84   C  CA  . GLN A 1 13  ? 45.296 25.566 23.289 1.00 40.25 ? 8   GLN A CA  1 
ATOM   85   C  C   . GLN A 1 13  ? 44.764 25.493 24.712 1.00 43.45 ? 8   GLN A C   1 
ATOM   86   O  O   . GLN A 1 13  ? 44.825 24.433 25.357 1.00 39.18 ? 8   GLN A O   1 
ATOM   87   C  CB  . GLN A 1 13  ? 46.692 26.184 23.266 1.00 44.07 ? 8   GLN A CB  1 
ATOM   88   C  CG  . GLN A 1 13  ? 47.773 25.353 23.944 1.00 51.42 ? 8   GLN A CG  1 
ATOM   89   C  CD  . GLN A 1 13  ? 49.149 26.032 23.923 1.00 58.93 ? 8   GLN A CD  1 
ATOM   90   O  OE1 . GLN A 1 13  ? 49.430 26.876 23.052 1.00 58.94 ? 8   GLN A OE1 1 
ATOM   91   N  NE2 . GLN A 1 13  ? 50.014 25.669 24.896 1.00 51.21 ? 8   GLN A NE2 1 
ATOM   92   N  N   . LYS A 1 14  ? 44.229 26.605 25.221 1.00 38.99 ? 9   LYS A N   1 
ATOM   93   C  CA  . LYS A 1 14  ? 43.734 26.609 26.595 1.00 38.49 ? 9   LYS A CA  1 
ATOM   94   C  C   . LYS A 1 14  ? 42.381 25.916 26.712 1.00 35.06 ? 9   LYS A C   1 
ATOM   95   O  O   . LYS A 1 14  ? 42.110 25.271 27.727 1.00 35.52 ? 9   LYS A O   1 
ATOM   96   C  CB  . LYS A 1 14  ? 43.682 28.051 27.121 1.00 35.98 ? 9   LYS A CB  1 
ATOM   97   C  CG  . LYS A 1 14  ? 45.037 28.566 27.535 1.00 36.10 ? 9   LYS A CG  1 
ATOM   98   C  CD  . LYS A 1 14  ? 44.985 30.062 27.918 1.00 44.63 ? 9   LYS A CD  1 
ATOM   99   C  CE  . LYS A 1 14  ? 46.356 30.612 28.268 1.00 42.84 ? 9   LYS A CE  1 
ATOM   100  N  NZ  . LYS A 1 14  ? 46.318 32.056 28.700 1.00 42.13 ? 9   LYS A NZ  1 
ATOM   101  N  N   . ALA A 1 15  ? 41.538 25.983 25.678 1.00 38.78 ? 10  ALA A N   1 
ATOM   102  C  CA  . ALA A 1 15  ? 40.318 25.175 25.697 1.00 36.91 ? 10  ALA A CA  1 
ATOM   103  C  C   . ALA A 1 15  ? 40.644 23.697 25.864 1.00 37.20 ? 10  ALA A C   1 
ATOM   104  O  O   . ALA A 1 15  ? 39.935 22.974 26.576 1.00 35.12 ? 10  ALA A O   1 
ATOM   105  C  CB  . ALA A 1 15  ? 39.509 25.392 24.424 1.00 33.57 ? 10  ALA A CB  1 
ATOM   106  N  N   . LYS A 1 16  ? 41.720 23.234 25.223 1.00 37.41 ? 11  LYS A N   1 
ATOM   107  C  CA  . LYS A 1 16  ? 42.095 21.824 25.315 1.00 41.77 ? 11  LYS A CA  1 
ATOM   108  C  C   . LYS A 1 16  ? 42.679 21.491 26.676 1.00 41.92 ? 11  LYS A C   1 
ATOM   109  O  O   . LYS A 1 16  ? 42.454 20.396 27.197 1.00 43.80 ? 11  LYS A O   1 
ATOM   110  C  CB  . LYS A 1 16  ? 43.098 21.470 24.225 1.00 38.77 ? 11  LYS A CB  1 
ATOM   111  C  CG  . LYS A 1 16  ? 42.544 21.514 22.828 1.00 39.06 ? 11  LYS A CG  1 
ATOM   112  C  CD  . LYS A 1 16  ? 43.686 21.373 21.855 1.00 39.81 ? 11  LYS A CD  1 
ATOM   113  C  CE  . LYS A 1 16  ? 43.195 21.295 20.419 1.00 44.98 ? 11  LYS A CE  1 
ATOM   114  N  NZ  . LYS A 1 16  ? 44.316 21.545 19.472 1.00 45.82 ? 11  LYS A NZ  1 
ATOM   115  N  N   . LEU A 1 17  ? 43.442 22.417 27.267 1.00 41.75 ? 12  LEU A N   1 
ATOM   116  C  CA  . LEU A 1 17  ? 43.865 22.230 28.655 1.00 42.63 ? 12  LEU A CA  1 
ATOM   117  C  C   . LEU A 1 17  ? 42.667 22.199 29.597 1.00 41.81 ? 12  LEU A C   1 
ATOM   118  O  O   . LEU A 1 17  ? 42.599 21.363 30.515 1.00 40.68 ? 12  LEU A O   1 
ATOM   119  C  CB  . LEU A 1 17  ? 44.830 23.346 29.067 1.00 43.63 ? 12  LEU A CB  1 
ATOM   120  C  CG  . LEU A 1 17  ? 46.152 23.429 28.311 1.00 42.80 ? 12  LEU A CG  1 
ATOM   121  C  CD1 . LEU A 1 17  ? 46.849 24.744 28.690 1.00 44.01 ? 12  LEU A CD1 1 
ATOM   122  C  CD2 . LEU A 1 17  ? 47.019 22.221 28.628 1.00 42.65 ? 12  LEU A CD2 1 
ATOM   123  N  N   . ALA A 1 18  ? 41.714 23.109 29.394 1.00 39.74 ? 13  ALA A N   1 
ATOM   124  C  CA  . ALA A 1 18  ? 40.541 23.153 30.260 1.00 39.29 ? 13  ALA A CA  1 
ATOM   125  C  C   . ALA A 1 18  ? 39.716 21.877 30.136 1.00 41.05 ? 13  ALA A C   1 
ATOM   126  O  O   . ALA A 1 18  ? 39.145 21.400 31.123 1.00 40.78 ? 13  ALA A O   1 
ATOM   127  C  CB  . ALA A 1 18  ? 39.695 24.377 29.923 1.00 40.99 ? 13  ALA A CB  1 
ATOM   128  N  N   . GLU A 1 19  ? 39.634 21.309 28.925 1.00 40.45 ? 14  GLU A N   1 
ATOM   129  C  CA  . GLU A 1 19  ? 38.945 20.032 28.771 1.00 40.11 ? 14  GLU A CA  1 
ATOM   130  C  C   . GLU A 1 19  ? 39.647 18.942 29.571 1.00 41.58 ? 14  GLU A C   1 
ATOM   131  O  O   . GLU A 1 19  ? 39.007 18.188 30.313 1.00 43.28 ? 14  GLU A O   1 
ATOM   132  C  CB  . GLU A 1 19  ? 38.862 19.646 27.297 1.00 40.03 ? 14  GLU A CB  1 
ATOM   133  C  CG  . GLU A 1 19  ? 38.108 18.346 27.044 1.00 41.50 ? 14  GLU A CG  1 
ATOM   134  C  CD  . GLU A 1 19  ? 38.127 17.944 25.570 1.00 41.36 ? 14  GLU A CD  1 
ATOM   135  O  OE1 . GLU A 1 19  ? 39.145 18.211 24.888 1.00 42.04 ? 14  GLU A OE1 1 
ATOM   136  O  OE2 . GLU A 1 19  ? 37.123 17.373 25.093 1.00 45.55 ? 14  GLU A OE2 1 
ATOM   137  N  N   . GLN A 1 20  ? 40.971 18.852 29.434 1.00 41.47 ? 15  GLN A N   1 
ATOM   138  C  CA  . GLN A 1 20  ? 41.735 17.882 30.208 1.00 42.47 ? 15  GLN A CA  1 
ATOM   139  C  C   . GLN A 1 20  ? 41.550 18.089 31.704 1.00 42.40 ? 15  GLN A C   1 
ATOM   140  O  O   . GLN A 1 20  ? 41.520 17.114 32.469 1.00 40.28 ? 15  GLN A O   1 
ATOM   141  C  CB  . GLN A 1 20  ? 43.215 17.978 29.845 1.00 44.43 ? 15  GLN A CB  1 
ATOM   142  C  CG  . GLN A 1 20  ? 43.553 17.458 28.463 1.00 46.57 ? 15  GLN A CG  1 
ATOM   143  C  CD  . GLN A 1 20  ? 45.042 17.467 28.203 1.00 53.53 ? 15  GLN A CD  1 
ATOM   144  O  OE1 . GLN A 1 20  ? 45.731 16.473 28.440 1.00 62.93 ? 15  GLN A OE1 1 
ATOM   145  N  NE2 . GLN A 1 20  ? 45.559 18.610 27.753 1.00 51.42 ? 15  GLN A NE2 1 
ATOM   146  N  N   . ALA A 1 21  ? 41.389 19.336 32.138 1.00 40.06 ? 16  ALA A N   1 
ATOM   147  C  CA  . ALA A 1 21  ? 41.203 19.645 33.545 1.00 40.62 ? 16  ALA A CA  1 
ATOM   148  C  C   . ALA A 1 21  ? 39.758 19.499 34.007 1.00 43.66 ? 16  ALA A C   1 
ATOM   149  O  O   . ALA A 1 21  ? 39.493 19.682 35.206 1.00 43.11 ? 16  ALA A O   1 
ATOM   150  C  CB  . ALA A 1 21  ? 41.685 21.068 33.837 1.00 42.20 ? 16  ALA A CB  1 
ATOM   151  N  N   . GLU A 1 22  ? 38.834 19.185 33.090 1.00 41.09 ? 17  GLU A N   1 
ATOM   152  C  CA  . GLU A 1 22  ? 37.390 19.166 33.363 1.00 40.20 ? 17  GLU A CA  1 
ATOM   153  C  C   . GLU A 1 22  ? 36.903 20.512 33.904 1.00 38.93 ? 17  GLU A C   1 
ATOM   154  O  O   . GLU A 1 22  ? 36.027 20.576 34.763 1.00 37.41 ? 17  GLU A O   1 
ATOM   155  C  CB  . GLU A 1 22  ? 37.010 18.020 34.314 1.00 40.88 ? 17  GLU A CB  1 
ATOM   156  C  CG  . GLU A 1 22  ? 37.403 16.677 33.783 1.00 37.53 ? 17  GLU A CG  1 
ATOM   157  C  CD  . GLU A 1 22  ? 36.994 15.543 34.705 1.00 52.41 ? 17  GLU A CD  1 
ATOM   158  O  OE1 . GLU A 1 22  ? 35.788 15.237 34.791 1.00 54.30 ? 17  GLU A OE1 1 
ATOM   159  O  OE2 . GLU A 1 22  ? 37.883 14.969 35.354 1.00 57.91 ? 17  GLU A OE2 1 
ATOM   160  N  N   . ARG A 1 23  ? 37.465 21.601 33.376 1.00 40.16 ? 18  ARG A N   1 
ATOM   161  C  CA  . ARG A 1 23  ? 37.030 22.961 33.700 1.00 38.80 ? 18  ARG A CA  1 
ATOM   162  C  C   . ARG A 1 23  ? 36.199 23.472 32.527 1.00 40.48 ? 18  ARG A C   1 
ATOM   163  O  O   . ARG A 1 23  ? 36.686 24.179 31.653 1.00 38.73 ? 18  ARG A O   1 
ATOM   164  C  CB  . ARG A 1 23  ? 38.242 23.848 33.964 1.00 37.16 ? 18  ARG A CB  1 
ATOM   165  C  CG  . ARG A 1 23  ? 39.033 23.409 35.207 1.00 42.31 ? 18  ARG A CG  1 
ATOM   166  C  CD  . ARG A 1 23  ? 38.494 24.127 36.410 1.00 39.62 ? 18  ARG A CD  1 
ATOM   167  N  NE  . ARG A 1 23  ? 38.687 25.561 36.262 1.00 41.71 ? 18  ARG A NE  1 
ATOM   168  C  CZ  . ARG A 1 23  ? 38.586 26.438 37.253 1.00 41.51 ? 18  ARG A CZ  1 
ATOM   169  N  NH1 . ARG A 1 23  ? 38.295 26.057 38.485 1.00 39.62 ? 18  ARG A NH1 1 
ATOM   170  N  NH2 . ARG A 1 23  ? 38.765 27.729 36.994 1.00 36.00 ? 18  ARG A NH2 1 
ATOM   171  N  N   . TYR A 1 24  ? 34.922 23.087 32.502 1.00 39.88 ? 19  TYR A N   1 
ATOM   172  C  CA  . TYR A 1 24  ? 34.165 23.245 31.264 1.00 40.70 ? 19  TYR A CA  1 
ATOM   173  C  C   . TYR A 1 24  ? 33.615 24.653 31.087 1.00 37.93 ? 19  TYR A C   1 
ATOM   174  O  O   . TYR A 1 24  ? 33.389 25.076 29.950 1.00 36.91 ? 19  TYR A O   1 
ATOM   175  C  CB  . TYR A 1 24  ? 33.035 22.219 31.192 1.00 39.92 ? 19  TYR A CB  1 
ATOM   176  C  CG  . TYR A 1 24  ? 33.528 20.783 31.180 1.00 41.67 ? 19  TYR A CG  1 
ATOM   177  C  CD1 . TYR A 1 24  ? 34.098 20.224 30.031 1.00 43.57 ? 19  TYR A CD1 1 
ATOM   178  C  CD2 . TYR A 1 24  ? 33.436 19.989 32.327 1.00 43.20 ? 19  TYR A CD2 1 
ATOM   179  C  CE1 . TYR A 1 24  ? 34.551 18.910 30.025 1.00 44.40 ? 19  TYR A CE1 1 
ATOM   180  C  CE2 . TYR A 1 24  ? 33.882 18.672 32.335 1.00 43.08 ? 19  TYR A CE2 1 
ATOM   181  C  CZ  . TYR A 1 24  ? 34.436 18.142 31.194 1.00 45.36 ? 19  TYR A CZ  1 
ATOM   182  O  OH  . TYR A 1 24  ? 34.869 16.845 31.221 1.00 51.69 ? 19  TYR A OH  1 
ATOM   183  N  N   . GLU A 1 25  ? 33.379 25.393 32.177 1.00 39.79 ? 20  GLU A N   1 
ATOM   184  C  CA  . GLU A 1 25  ? 33.072 26.809 32.010 1.00 37.47 ? 20  GLU A CA  1 
ATOM   185  C  C   . GLU A 1 25  ? 34.245 27.551 31.389 1.00 35.62 ? 20  GLU A C   1 
ATOM   186  O  O   . GLU A 1 25  ? 34.067 28.317 30.436 1.00 38.64 ? 20  GLU A O   1 
ATOM   187  C  CB  . GLU A 1 25  ? 32.684 27.456 33.344 1.00 40.11 ? 20  GLU A CB  1 
ATOM   188  C  CG  . GLU A 1 25  ? 31.384 26.967 33.914 1.00 46.37 ? 20  GLU A CG  1 
ATOM   189  C  CD  . GLU A 1 25  ? 31.060 27.617 35.259 1.00 61.08 ? 20  GLU A CD  1 
ATOM   190  O  OE1 . GLU A 1 25  ? 31.360 28.828 35.428 1.00 62.79 ? 20  GLU A OE1 1 
ATOM   191  O  OE2 . GLU A 1 25  ? 30.539 26.903 36.151 1.00 66.63 ? 20  GLU A OE2 1 
ATOM   192  N  N   . ASP A 1 26  ? 35.446 27.390 31.958 1.00 36.73 ? 21  ASP A N   1 
ATOM   193  C  CA  . ASP A 1 26  ? 36.635 27.972 31.346 1.00 37.51 ? 21  ASP A CA  1 
ATOM   194  C  C   . ASP A 1 26  ? 36.709 27.570 29.881 1.00 38.03 ? 21  ASP A C   1 
ATOM   195  O  O   . ASP A 1 26  ? 36.866 28.416 28.993 1.00 34.43 ? 21  ASP A O   1 
ATOM   196  C  CB  . ASP A 1 26  ? 37.908 27.499 32.049 1.00 37.12 ? 21  ASP A CB  1 
ATOM   197  C  CG  . ASP A 1 26  ? 38.082 28.071 33.453 1.00 42.40 ? 21  ASP A CG  1 
ATOM   198  O  OD1 . ASP A 1 26  ? 37.315 28.959 33.838 1.00 39.61 ? 21  ASP A OD1 1 
ATOM   199  O  OD2 . ASP A 1 26  ? 38.993 27.603 34.169 1.00 41.41 ? 21  ASP A OD2 1 
ATOM   200  N  N   . MET A 1 27  ? 36.609 26.260 29.621 1.00 36.19 ? 22  MET A N   1 
ATOM   201  C  CA  . MET A 1 27  ? 36.708 25.758 28.254 1.00 35.44 ? 22  MET A CA  1 
ATOM   202  C  C   . MET A 1 27  ? 35.702 26.451 27.348 1.00 34.32 ? 22  MET A C   1 
ATOM   203  O  O   . MET A 1 27  ? 36.040 26.859 26.233 1.00 37.68 ? 22  MET A O   1 
ATOM   204  C  CB  . MET A 1 27  ? 36.517 24.235 28.253 1.00 34.94 ? 22  MET A CB  1 
ATOM   205  C  CG  . MET A 1 27  ? 36.479 23.617 26.880 1.00 37.79 ? 22  MET A CG  1 
ATOM   206  S  SD  . MET A 1 27  ? 36.057 21.858 26.950 1.00 38.05 ? 22  MET A SD  1 
ATOM   207  C  CE  . MET A 1 27  ? 36.505 21.350 25.275 1.00 34.84 ? 22  MET A CE  1 
ATOM   208  N  N   . ALA A 1 28  ? 34.473 26.637 27.829 1.00 35.55 ? 23  ALA A N   1 
ATOM   209  C  CA  . ALA A 1 28  ? 33.486 27.353 27.030 1.00 34.95 ? 23  ALA A CA  1 
ATOM   210  C  C   . ALA A 1 28  ? 33.890 28.812 26.818 1.00 38.55 ? 23  ALA A C   1 
ATOM   211  O  O   . ALA A 1 28  ? 33.719 29.345 25.718 1.00 38.41 ? 23  ALA A O   1 
ATOM   212  C  CB  . ALA A 1 28  ? 32.116 27.273 27.692 1.00 35.89 ? 23  ALA A CB  1 
ATOM   213  N  N   . ALA A 1 29  ? 34.424 29.474 27.857 1.00 37.08 ? 24  ALA A N   1 
ATOM   214  C  CA  . ALA A 1 29  ? 34.850 30.864 27.700 1.00 37.91 ? 24  ALA A CA  1 
ATOM   215  C  C   . ALA A 1 29  ? 35.957 30.990 26.662 1.00 37.54 ? 24  ALA A C   1 
ATOM   216  O  O   . ALA A 1 29  ? 35.947 31.915 25.839 1.00 35.77 ? 24  ALA A O   1 
ATOM   217  C  CB  . ALA A 1 29  ? 35.319 31.432 29.045 1.00 37.49 ? 24  ALA A CB  1 
ATOM   218  N  N   . PHE A 1 30  ? 36.930 30.076 26.702 1.00 36.42 ? 25  PHE A N   1 
ATOM   219  C  CA  . PHE A 1 30  ? 38.036 30.093 25.751 1.00 36.33 ? 25  PHE A CA  1 
ATOM   220  C  C   . PHE A 1 30  ? 37.534 29.906 24.325 1.00 38.97 ? 25  PHE A C   1 
ATOM   221  O  O   . PHE A 1 30  ? 37.992 30.592 23.393 1.00 36.35 ? 25  PHE A O   1 
ATOM   222  C  CB  . PHE A 1 30  ? 39.046 28.997 26.118 1.00 35.63 ? 25  PHE A CB  1 
ATOM   223  C  CG  . PHE A 1 30  ? 39.840 29.281 27.371 1.00 39.92 ? 25  PHE A CG  1 
ATOM   224  C  CD1 . PHE A 1 30  ? 40.356 30.552 27.618 1.00 35.38 ? 25  PHE A CD1 1 
ATOM   225  C  CD2 . PHE A 1 30  ? 40.077 28.271 28.313 1.00 37.11 ? 25  PHE A CD2 1 
ATOM   226  C  CE1 . PHE A 1 30  ? 41.089 30.804 28.783 1.00 39.80 ? 25  PHE A CE1 1 
ATOM   227  C  CE2 . PHE A 1 30  ? 40.816 28.519 29.448 1.00 39.42 ? 25  PHE A CE2 1 
ATOM   228  C  CZ  . PHE A 1 30  ? 41.319 29.783 29.695 1.00 39.70 ? 25  PHE A CZ  1 
ATOM   229  N  N   . MET A 1 31  ? 36.574 28.995 24.140 1.00 38.39 ? 26  MET A N   1 
ATOM   230  C  CA  . MET A 1 31  ? 36.058 28.705 22.803 1.00 35.30 ? 26  MET A CA  1 
ATOM   231  C  C   . MET A 1 31  ? 35.212 29.872 22.282 1.00 39.56 ? 26  MET A C   1 
ATOM   232  O  O   . MET A 1 31  ? 35.272 30.203 21.093 1.00 38.83 ? 26  MET A O   1 
ATOM   233  C  CB  . MET A 1 31  ? 35.246 27.406 22.845 1.00 37.55 ? 26  MET A CB  1 
ATOM   234  C  CG  . MET A 1 31  ? 36.030 26.121 22.609 1.00 33.28 ? 26  MET A CG  1 
ATOM   235  S  SD  . MET A 1 31  ? 37.558 26.193 21.645 1.00 38.65 ? 26  MET A SD  1 
ATOM   236  C  CE  . MET A 1 31  ? 36.848 26.237 20.009 1.00 41.84 ? 26  MET A CE  1 
ATOM   237  N  N   . LYS A 1 32  ? 34.415 30.500 23.155 1.00 39.47 ? 27  LYS A N   1 
ATOM   238  C  CA  . LYS A 1 32  ? 33.730 31.745 22.797 1.00 37.16 ? 27  LYS A CA  1 
ATOM   239  C  C   . LYS A 1 32  ? 34.718 32.796 22.299 1.00 38.34 ? 27  LYS A C   1 
ATOM   240  O  O   . LYS A 1 32  ? 34.493 33.432 21.259 1.00 39.17 ? 27  LYS A O   1 
ATOM   241  C  CB  . LYS A 1 32  ? 32.938 32.264 24.005 1.00 40.66 ? 27  LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 32  ? 32.154 33.571 23.753 1.00 46.35 ? 27  LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 32  ? 31.197 33.875 24.897 1.00 43.75 ? 27  LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 32  ? 30.336 35.102 24.584 1.00 53.86 ? 27  LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 32  ? 31.117 36.369 24.573 1.00 51.68 ? 27  LYS A NZ  1 
ATOM   246  N  N   . GLY A 1 33  ? 35.819 33.001 23.031 1.00 38.45 ? 28  GLY A N   1 
ATOM   247  C  CA  . GLY A 1 33  ? 36.845 33.927 22.570 1.00 40.66 ? 28  GLY A CA  1 
ATOM   248  C  C   . GLY A 1 33  ? 37.403 33.544 21.211 1.00 40.73 ? 28  GLY A C   1 
ATOM   249  O  O   . GLY A 1 33  ? 37.601 34.398 20.338 1.00 39.23 ? 28  GLY A O   1 
ATOM   250  N  N   . ALA A 1 34  ? 37.679 32.257 21.017 1.00 35.69 ? 29  ALA A N   1 
ATOM   251  C  CA  . ALA A 1 34  ? 38.125 31.793 19.714 1.00 39.19 ? 29  ALA A CA  1 
ATOM   252  C  C   . ALA A 1 34  ? 37.108 32.147 18.641 1.00 36.81 ? 29  ALA A C   1 
ATOM   253  O  O   . ALA A 1 34  ? 37.470 32.678 17.584 1.00 40.52 ? 29  ALA A O   1 
ATOM   254  C  CB  . ALA A 1 34  ? 38.377 30.287 19.749 1.00 38.26 ? 29  ALA A CB  1 
ATOM   255  N  N   . VAL A 1 35  ? 35.824 31.866 18.893 1.00 35.83 ? 30  VAL A N   1 
ATOM   256  C  CA  . VAL A 1 35  ? 34.811 32.121 17.866 1.00 38.06 ? 30  VAL A CA  1 
ATOM   257  C  C   . VAL A 1 35  ? 34.775 33.600 17.531 1.00 43.10 ? 30  VAL A C   1 
ATOM   258  O  O   . VAL A 1 35  ? 34.592 33.994 16.372 1.00 41.19 ? 30  VAL A O   1 
ATOM   259  C  CB  . VAL A 1 35  ? 33.429 31.632 18.334 1.00 40.70 ? 30  VAL A CB  1 
ATOM   260  C  CG1 . VAL A 1 35  ? 32.337 32.143 17.420 1.00 37.67 ? 30  VAL A CG1 1 
ATOM   261  C  CG2 . VAL A 1 35  ? 33.382 30.112 18.390 1.00 36.53 ? 30  VAL A CG2 1 
ATOM   262  N  N   . GLU A 1 36  ? 34.948 34.445 18.544 1.00 38.63 ? 31  GLU A N   1 
ATOM   263  C  CA  . GLU A 1 36  ? 34.822 35.878 18.347 1.00 41.31 ? 31  GLU A CA  1 
ATOM   264  C  C   . GLU A 1 36  ? 35.976 36.461 17.551 1.00 38.86 ? 31  GLU A C   1 
ATOM   265  O  O   . GLU A 1 36  ? 35.909 37.630 17.157 1.00 40.56 ? 31  GLU A O   1 
ATOM   266  C  CB  . GLU A 1 36  ? 34.683 36.564 19.713 1.00 40.39 ? 31  GLU A CB  1 
ATOM   267  C  CG  . GLU A 1 36  ? 33.270 36.432 20.232 1.00 45.50 ? 31  GLU A CG  1 
ATOM   268  C  CD  . GLU A 1 36  ? 33.104 36.865 21.667 1.00 46.02 ? 31  GLU A CD  1 
ATOM   269  O  OE1 . GLU A 1 36  ? 34.123 37.086 22.354 1.00 51.79 ? 31  GLU A OE1 1 
ATOM   270  O  OE2 . GLU A 1 36  ? 31.944 36.978 22.114 1.00 51.70 ? 31  GLU A OE2 1 
ATOM   271  N  N   . LYS A 1 37  ? 37.029 35.691 17.293 1.00 38.58 ? 32  LYS A N   1 
ATOM   272  C  CA  . LYS A 1 37  ? 38.036 36.176 16.367 1.00 40.15 ? 32  LYS A CA  1 
ATOM   273  C  C   . LYS A 1 37  ? 37.515 36.274 14.934 1.00 47.79 ? 32  LYS A C   1 
ATOM   274  O  O   . LYS A 1 37  ? 38.195 36.860 14.090 1.00 45.17 ? 32  LYS A O   1 
ATOM   275  C  CB  . LYS A 1 37  ? 39.267 35.277 16.417 1.00 39.12 ? 32  LYS A CB  1 
ATOM   276  C  CG  . LYS A 1 37  ? 39.873 35.113 17.810 1.00 38.67 ? 32  LYS A CG  1 
ATOM   277  C  CD  . LYS A 1 37  ? 40.362 36.463 18.419 1.00 41.39 ? 32  LYS A CD  1 
ATOM   278  C  CE  . LYS A 1 37  ? 41.116 36.201 19.719 1.00 40.35 ? 32  LYS A CE  1 
ATOM   279  N  NZ  . LYS A 1 37  ? 41.256 37.419 20.599 1.00 43.56 ? 32  LYS A NZ  1 
ATOM   280  N  N   . GLY A 1 38  ? 36.353 35.694 14.630 1.00 46.34 ? 33  GLY A N   1 
ATOM   281  C  CA  . GLY A 1 38  ? 35.743 35.873 13.331 1.00 43.39 ? 33  GLY A CA  1 
ATOM   282  C  C   . GLY A 1 38  ? 36.154 34.891 12.255 1.00 48.08 ? 33  GLY A C   1 
ATOM   283  O  O   . GLY A 1 38  ? 35.697 35.030 11.117 1.00 49.20 ? 33  GLY A O   1 
ATOM   284  N  N   . GLU A 1 39  ? 36.984 33.898 12.563 1.00 45.80 ? 34  GLU A N   1 
ATOM   285  C  CA  . GLU A 1 39  ? 37.370 32.902 11.571 1.00 45.49 ? 34  GLU A CA  1 
ATOM   286  C  C   . GLU A 1 39  ? 36.559 31.627 11.748 1.00 44.96 ? 34  GLU A C   1 
ATOM   287  O  O   . GLU A 1 39  ? 36.054 31.336 12.835 1.00 43.06 ? 34  GLU A O   1 
ATOM   288  C  CB  . GLU A 1 39  ? 38.861 32.592 11.673 1.00 44.60 ? 34  GLU A CB  1 
ATOM   289  C  CG  . GLU A 1 39  ? 39.688 33.843 11.607 1.00 54.64 ? 34  GLU A CG  1 
ATOM   290  C  CD  . GLU A 1 39  ? 41.156 33.560 11.640 1.00 62.40 ? 34  GLU A CD  1 
ATOM   291  O  OE1 . GLU A 1 39  ? 41.544 32.509 12.200 1.00 62.58 ? 34  GLU A OE1 1 
ATOM   292  O  OE2 . GLU A 1 39  ? 41.916 34.384 11.083 1.00 73.84 ? 34  GLU A OE2 1 
ATOM   293  N  N   . GLU A 1 40  ? 36.437 30.862 10.663 1.00 43.84 ? 35  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 40  ? 35.693 29.618 10.747 1.00 41.70 ? 35  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 40  ? 36.413 28.622 11.655 1.00 45.34 ? 35  GLU A C   1 
ATOM   296  O  O   . GLU A 1 40  ? 37.627 28.686 11.868 1.00 46.80 ? 35  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 40  ? 35.456 28.996 9.362  1.00 48.72 ? 35  GLU A CB  1 
ATOM   298  C  CG  . GLU A 1 40  ? 34.895 29.965 8.338  1.00 59.31 ? 35  GLU A CG  1 
ATOM   299  C  CD  . GLU A 1 40  ? 34.611 29.309 6.996  1.00 65.61 ? 35  GLU A CD  1 
ATOM   300  O  OE1 . GLU A 1 40  ? 35.282 28.309 6.662  1.00 60.79 ? 35  GLU A OE1 1 
ATOM   301  O  OE2 . GLU A 1 40  ? 33.712 29.805 6.278  1.00 73.03 ? 35  GLU A OE2 1 
ATOM   302  N  N   . LEU A 1 41  ? 35.637 27.697 12.200 1.00 42.84 ? 36  LEU A N   1 
ATOM   303  C  CA  . LEU A 1 41  ? 36.145 26.667 13.090 1.00 40.43 ? 36  LEU A CA  1 
ATOM   304  C  C   . LEU A 1 41  ? 36.355 25.369 12.315 1.00 43.93 ? 36  LEU A C   1 
ATOM   305  O  O   . LEU A 1 41  ? 35.530 24.997 11.476 1.00 42.37 ? 36  LEU A O   1 
ATOM   306  C  CB  . LEU A 1 41  ? 35.172 26.438 14.247 1.00 41.71 ? 36  LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 41  ? 35.276 27.369 15.468 1.00 42.35 ? 36  LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 41  ? 34.998 28.801 15.098 1.00 46.08 ? 36  LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 41  ? 34.328 26.914 16.583 1.00 39.19 ? 36  LEU A CD2 1 
ATOM   310  N  N   . SER A 1 42  ? 37.474 24.704 12.584 1.00 40.09 ? 37  SER A N   1 
ATOM   311  C  CA  . SER A 1 42  ? 37.730 23.362 12.084 1.00 42.75 ? 37  SER A CA  1 
ATOM   312  C  C   . SER A 1 42  ? 36.839 22.348 12.798 1.00 44.46 ? 37  SER A C   1 
ATOM   313  O  O   . SER A 1 42  ? 36.198 22.651 13.812 1.00 40.78 ? 37  SER A O   1 
ATOM   314  C  CB  . SER A 1 42  ? 39.187 22.991 12.309 1.00 43.78 ? 37  SER A CB  1 
ATOM   315  O  OG  . SER A 1 42  ? 39.435 22.843 13.702 1.00 42.30 ? 37  SER A OG  1 
ATOM   316  N  N   . CYS A 1 43  ? 36.828 21.113 12.272 1.00 40.70 ? 38  CYS A N   1 
ATOM   317  C  CA  . CYS A 1 43  ? 36.069 20.033 12.911 1.00 41.21 ? 38  CYS A CA  1 
ATOM   318  C  C   . CYS A 1 43  ? 36.508 19.813 14.359 1.00 40.78 ? 38  CYS A C   1 
ATOM   319  O  O   . CYS A 1 43  ? 35.671 19.632 15.253 1.00 37.56 ? 38  CYS A O   1 
ATOM   320  C  CB  . CYS A 1 43  ? 36.208 18.732 12.108 1.00 46.83 ? 38  CYS A CB  1 
ATOM   321  S  SG  . CYS A 1 43  ? 34.774 18.348 11.007 1.00 56.75 ? 38  CYS A SG  1 
ATOM   322  N  N   . GLU A 1 44  ? 37.818 19.779 14.608 1.00 39.17 ? 39  GLU A N   1 
ATOM   323  C  CA  . GLU A 1 44  ? 38.284 19.615 15.985 1.00 43.42 ? 39  GLU A CA  1 
ATOM   324  C  C   . GLU A 1 44  ? 37.804 20.754 16.880 1.00 41.33 ? 39  GLU A C   1 
ATOM   325  O  O   . GLU A 1 44  ? 37.426 20.527 18.037 1.00 41.01 ? 39  GLU A O   1 
ATOM   326  C  CB  . GLU A 1 44  ? 39.807 19.528 16.030 1.00 45.49 ? 39  GLU A CB  1 
ATOM   327  C  CG  . GLU A 1 44  ? 40.326 18.916 17.318 1.00 50.59 ? 39  GLU A CG  1 
ATOM   328  C  CD  . GLU A 1 44  ? 41.832 19.034 17.459 1.00 55.37 ? 39  GLU A CD  1 
ATOM   329  O  OE1 . GLU A 1 44  ? 42.355 18.788 18.569 1.00 60.97 ? 39  GLU A OE1 1 
ATOM   330  O  OE2 . GLU A 1 44  ? 42.494 19.369 16.455 1.00 60.25 ? 39  GLU A OE2 1 
ATOM   331  N  N   . GLU A 1 45  ? 37.823 21.986 16.367 1.00 40.27 ? 40  GLU A N   1 
ATOM   332  C  CA  . GLU A 1 45  ? 37.417 23.136 17.179 1.00 37.71 ? 40  GLU A CA  1 
ATOM   333  C  C   . GLU A 1 45  ? 35.913 23.134 17.415 1.00 39.66 ? 40  GLU A C   1 
ATOM   334  O  O   . GLU A 1 45  ? 35.444 23.510 18.498 1.00 38.33 ? 40  GLU A O   1 
ATOM   335  C  CB  . GLU A 1 45  ? 37.863 24.443 16.499 1.00 38.69 ? 40  GLU A CB  1 
ATOM   336  C  CG  . GLU A 1 45  ? 39.382 24.569 16.443 1.00 40.46 ? 40  GLU A CG  1 
ATOM   337  C  CD  . GLU A 1 45  ? 39.907 25.631 15.481 1.00 44.05 ? 40  GLU A CD  1 
ATOM   338  O  OE1 . GLU A 1 45  ? 39.144 26.139 14.630 1.00 40.63 ? 40  GLU A OE1 1 
ATOM   339  O  OE2 . GLU A 1 45  ? 41.114 25.943 15.582 1.00 44.20 ? 40  GLU A OE2 1 
ATOM   340  N  N   . ARG A 1 46  ? 35.138 22.702 16.415 1.00 38.02 ? 41  ARG A N   1 
ATOM   341  C  CA  . ARG A 1 46  ? 33.698 22.582 16.613 1.00 39.20 ? 41  ARG A CA  1 
ATOM   342  C  C   . ARG A 1 46  ? 33.384 21.573 17.703 1.00 40.83 ? 41  ARG A C   1 
ATOM   343  O  O   . ARG A 1 46  ? 32.445 21.766 18.490 1.00 42.07 ? 41  ARG A O   1 
ATOM   344  C  CB  . ARG A 1 46  ? 33.010 22.194 15.308 1.00 38.99 ? 41  ARG A CB  1 
ATOM   345  C  CG  . ARG A 1 46  ? 32.759 23.371 14.414 1.00 41.24 ? 41  ARG A CG  1 
ATOM   346  C  CD  . ARG A 1 46  ? 31.893 22.998 13.221 1.00 43.65 ? 41  ARG A CD  1 
ATOM   347  N  NE  . ARG A 1 46  ? 32.487 21.941 12.418 1.00 44.40 ? 41  ARG A NE  1 
ATOM   348  C  CZ  . ARG A 1 46  ? 33.242 22.129 11.344 1.00 50.31 ? 41  ARG A CZ  1 
ATOM   349  N  NH1 . ARG A 1 46  ? 33.633 23.336 10.978 1.00 50.19 ? 41  ARG A NH1 1 
ATOM   350  N  NH2 . ARG A 1 46  ? 33.594 21.078 10.607 1.00 49.32 ? 41  ARG A NH2 1 
ATOM   351  N  N   . ASN A 1 47  ? 34.182 20.506 17.790 1.00 39.09 ? 42  ASN A N   1 
ATOM   352  C  CA  . ASN A 1 47  ? 34.012 19.555 18.884 1.00 40.55 ? 42  ASN A CA  1 
ATOM   353  C  C   . ASN A 1 47  ? 34.283 20.189 20.238 1.00 38.07 ? 42  ASN A C   1 
ATOM   354  O  O   . ASN A 1 47  ? 33.549 19.942 21.200 1.00 36.68 ? 42  ASN A O   1 
ATOM   355  C  CB  . ASN A 1 47  ? 34.932 18.368 18.705 1.00 41.60 ? 42  ASN A CB  1 
ATOM   356  C  CG  . ASN A 1 47  ? 34.457 17.197 19.473 1.00 45.81 ? 42  ASN A CG  1 
ATOM   357  O  OD1 . ASN A 1 47  ? 33.387 16.660 19.188 1.00 48.61 ? 42  ASN A OD1 1 
ATOM   358  N  ND2 . ASN A 1 47  ? 35.220 16.801 20.483 1.00 47.10 ? 42  ASN A ND2 1 
ATOM   359  N  N   . LEU A 1 48  ? 35.362 20.968 20.346 1.00 38.40 ? 43  LEU A N   1 
ATOM   360  C  CA  . LEU A 1 48  ? 35.647 21.655 21.604 1.00 39.32 ? 43  LEU A CA  1 
ATOM   361  C  C   . LEU A 1 48  ? 34.486 22.557 21.994 1.00 38.08 ? 43  LEU A C   1 
ATOM   362  O  O   . LEU A 1 48  ? 34.021 22.538 23.146 1.00 35.47 ? 43  LEU A O   1 
ATOM   363  C  CB  . LEU A 1 48  ? 36.949 22.455 21.484 1.00 37.89 ? 43  LEU A CB  1 
ATOM   364  C  CG  . LEU A 1 48  ? 38.220 21.645 21.220 1.00 40.07 ? 43  LEU A CG  1 
ATOM   365  C  CD1 . LEU A 1 48  ? 39.361 22.517 20.689 1.00 38.90 ? 43  LEU A CD1 1 
ATOM   366  C  CD2 . LEU A 1 48  ? 38.649 20.848 22.476 1.00 36.22 ? 43  LEU A CD2 1 
ATOM   367  N  N   . LEU A 1 49  ? 34.002 23.361 21.039 1.00 38.37 ? 44  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 49  ? 32.886 24.260 21.326 1.00 39.78 ? 44  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 49  ? 31.678 23.477 21.807 1.00 39.73 ? 44  LEU A C   1 
ATOM   370  O  O   . LEU A 1 49  ? 31.038 23.841 22.802 1.00 35.16 ? 44  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 49  ? 32.525 25.069 20.079 1.00 35.75 ? 44  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 49  ? 31.374 26.074 20.210 1.00 35.59 ? 44  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 49  ? 31.832 27.292 20.984 1.00 34.57 ? 44  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 49  ? 30.858 26.509 18.791 1.00 32.16 ? 44  LEU A CD2 1 
ATOM   375  N  N   . SER A 1 50  ? 31.343 22.402 21.085 1.00 38.99 ? 45  SER A N   1 
ATOM   376  C  CA  . SER A 1 50  ? 30.202 21.565 21.435 1.00 37.28 ? 45  SER A CA  1 
ATOM   377  C  C   . SER A 1 50  ? 30.381 20.928 22.803 1.00 36.71 ? 45  SER A C   1 
ATOM   378  O  O   . SER A 1 50  ? 29.474 20.971 23.643 1.00 38.00 ? 45  SER A O   1 
ATOM   379  C  CB  . SER A 1 50  ? 30.018 20.483 20.371 1.00 37.20 ? 45  SER A CB  1 
ATOM   380  O  OG  . SER A 1 50  ? 28.906 19.668 20.677 1.00 39.14 ? 45  SER A OG  1 
ATOM   381  N  N   . VAL A 1 51  ? 31.555 20.345 23.056 1.00 34.24 ? 46  VAL A N   1 
ATOM   382  C  CA  . VAL A 1 51  ? 31.758 19.621 24.314 1.00 34.88 ? 46  VAL A CA  1 
ATOM   383  C  C   . VAL A 1 51  ? 31.674 20.580 25.498 1.00 39.58 ? 46  VAL A C   1 
ATOM   384  O  O   . VAL A 1 51  ? 31.065 20.268 26.528 1.00 36.59 ? 46  VAL A O   1 
ATOM   385  C  CB  . VAL A 1 51  ? 33.101 18.868 24.285 1.00 35.21 ? 46  VAL A CB  1 
ATOM   386  C  CG1 . VAL A 1 51  ? 33.499 18.406 25.688 1.00 42.28 ? 46  VAL A CG1 1 
ATOM   387  C  CG2 . VAL A 1 51  ? 33.039 17.667 23.302 1.00 36.88 ? 46  VAL A CG2 1 
ATOM   388  N  N   . ALA A 1 52  ? 32.245 21.778 25.350 1.00 39.63 ? 47  ALA A N   1 
ATOM   389  C  CA  . ALA A 1 52  ? 32.286 22.736 26.454 1.00 36.33 ? 47  ALA A CA  1 
ATOM   390  C  C   . ALA A 1 52  ? 30.887 23.181 26.844 1.00 39.67 ? 47  ALA A C   1 
ATOM   391  O  O   . ALA A 1 52  ? 30.483 23.063 28.005 1.00 40.68 ? 47  ALA A O   1 
ATOM   392  C  CB  . ALA A 1 52  ? 33.140 23.944 26.061 1.00 37.43 ? 47  ALA A CB  1 
ATOM   393  N  N   . TYR A 1 53  ? 30.126 23.714 25.878 1.00 35.95 ? 48  TYR A N   1 
ATOM   394  C  CA  . TYR A 1 53  ? 28.813 24.254 26.214 1.00 36.52 ? 48  TYR A CA  1 
ATOM   395  C  C   . TYR A 1 53  ? 27.819 23.162 26.601 1.00 38.84 ? 48  TYR A C   1 
ATOM   396  O  O   . TYR A 1 53  ? 26.988 23.367 27.494 1.00 34.53 ? 48  TYR A O   1 
ATOM   397  C  CB  . TYR A 1 53  ? 28.290 25.094 25.061 1.00 37.69 ? 48  TYR A CB  1 
ATOM   398  C  CG  . TYR A 1 53  ? 28.834 26.505 25.129 1.00 37.15 ? 48  TYR A CG  1 
ATOM   399  C  CD1 . TYR A 1 53  ? 28.456 27.358 26.165 1.00 36.19 ? 48  TYR A CD1 1 
ATOM   400  C  CD2 . TYR A 1 53  ? 29.765 26.963 24.204 1.00 37.76 ? 48  TYR A CD2 1 
ATOM   401  C  CE1 . TYR A 1 53  ? 28.958 28.650 26.262 1.00 40.87 ? 48  TYR A CE1 1 
ATOM   402  C  CE2 . TYR A 1 53  ? 30.277 28.259 24.291 1.00 39.21 ? 48  TYR A CE2 1 
ATOM   403  C  CZ  . TYR A 1 53  ? 29.864 29.092 25.325 1.00 40.99 ? 48  TYR A CZ  1 
ATOM   404  O  OH  . TYR A 1 53  ? 30.364 30.368 25.434 1.00 38.75 ? 48  TYR A OH  1 
ATOM   405  N  N   . LYS A 1 54  ? 27.858 22.005 25.933 1.00 37.31 ? 49  LYS A N   1 
ATOM   406  C  CA  . LYS A 1 54  ? 26.977 20.910 26.351 1.00 38.26 ? 49  LYS A CA  1 
ATOM   407  C  C   . LYS A 1 54  ? 27.227 20.503 27.804 1.00 38.22 ? 49  LYS A C   1 
ATOM   408  O  O   . LYS A 1 54  ? 26.284 20.186 28.539 1.00 38.56 ? 49  LYS A O   1 
ATOM   409  C  CB  . LYS A 1 54  ? 27.153 19.713 25.416 1.00 44.81 ? 49  LYS A CB  1 
ATOM   410  C  CG  . LYS A 1 54  ? 25.898 18.873 25.259 1.00 50.14 ? 49  LYS A CG  1 
ATOM   411  C  CD  . LYS A 1 54  ? 26.026 17.869 24.107 1.00 50.61 ? 49  LYS A CD  1 
ATOM   412  C  CE  . LYS A 1 54  ? 25.345 16.576 24.470 1.00 48.33 ? 49  LYS A CE  1 
ATOM   413  N  NZ  . LYS A 1 54  ? 24.160 16.803 25.380 1.00 52.86 ? 49  LYS A NZ  1 
ATOM   414  N  N   . ASN A 1 55  ? 28.490 20.460 28.228 1.00 39.84 ? 50  ASN A N   1 
ATOM   415  C  CA  . ASN A 1 55  ? 28.791 20.129 29.618 1.00 37.42 ? 50  ASN A CA  1 
ATOM   416  C  C   . ASN A 1 55  ? 28.227 21.186 30.565 1.00 41.29 ? 50  ASN A C   1 
ATOM   417  O  O   . ASN A 1 55  ? 27.619 20.851 31.584 1.00 37.42 ? 50  ASN A O   1 
ATOM   418  C  CB  . ASN A 1 55  ? 30.302 20.001 29.817 1.00 39.63 ? 50  ASN A CB  1 
ATOM   419  C  CG  . ASN A 1 55  ? 30.794 18.576 29.742 1.00 48.24 ? 50  ASN A CG  1 
ATOM   420  O  OD1 . ASN A 1 55  ? 31.432 18.163 28.763 1.00 48.13 ? 50  ASN A OD1 1 
ATOM   421  N  ND2 . ASN A 1 55  ? 30.573 17.834 30.818 1.00 45.35 ? 50  ASN A ND2 1 
ATOM   422  N  N   . VAL A 1 56  ? 28.378 22.466 30.217 1.00 37.53 ? 51  VAL A N   1 
ATOM   423  C  CA  . VAL A 1 56  ? 27.868 23.530 31.076 1.00 38.79 ? 51  VAL A CA  1 
ATOM   424  C  C   . VAL A 1 56  ? 26.357 23.424 31.194 1.00 41.36 ? 51  VAL A C   1 
ATOM   425  O  O   . VAL A 1 56  ? 25.805 23.310 32.294 1.00 38.41 ? 51  VAL A O   1 
ATOM   426  C  CB  . VAL A 1 56  ? 28.286 24.909 30.538 1.00 39.70 ? 51  VAL A CB  1 
ATOM   427  C  CG1 . VAL A 1 56  ? 27.611 26.030 31.353 1.00 38.74 ? 51  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A 1 56  ? 29.793 25.046 30.565 1.00 38.40 ? 51  VAL A CG2 1 
ATOM   429  N  N   . VAL A 1 57  ? 25.668 23.436 30.047 1.00 39.25 ? 52  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 57  ? 24.211 23.429 30.061 1.00 34.46 ? 52  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 57  ? 23.679 22.096 30.586 1.00 37.32 ? 52  VAL A C   1 
ATOM   432  O  O   . VAL A 1 57  ? 22.606 22.049 31.203 1.00 38.80 ? 52  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 57  ? 23.674 23.782 28.659 1.00 37.92 ? 52  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 57  ? 23.682 22.544 27.723 1.00 37.89 ? 52  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 57  ? 22.292 24.372 28.755 1.00 40.69 ? 52  VAL A CG2 1 
ATOM   436  N  N   . GLY A 1 58  ? 24.423 21.001 30.394 1.00 37.39 ? 53  GLY A N   1 
ATOM   437  C  CA  . GLY A 1 58  ? 23.983 19.718 30.939 1.00 37.20 ? 53  GLY A CA  1 
ATOM   438  C  C   . GLY A 1 58  ? 23.871 19.734 32.454 1.00 39.93 ? 53  GLY A C   1 
ATOM   439  O  O   . GLY A 1 58  ? 22.891 19.242 33.023 1.00 39.00 ? 53  GLY A O   1 
ATOM   440  N  N   . GLY A 1 59  ? 24.874 20.300 33.131 1.00 41.09 ? 54  GLY A N   1 
ATOM   441  C  CA  . GLY A 1 59  ? 24.801 20.396 34.575 1.00 43.53 ? 54  GLY A CA  1 
ATOM   442  C  C   . GLY A 1 59  ? 23.648 21.273 35.018 1.00 43.21 ? 54  GLY A C   1 
ATOM   443  O  O   . GLY A 1 59  ? 22.995 20.994 36.027 1.00 41.54 ? 54  GLY A O   1 
ATOM   444  N  N   . GLN A 1 60  ? 23.359 22.331 34.245 1.00 39.84 ? 55  GLN A N   1 
ATOM   445  C  CA  . GLN A 1 60  ? 22.260 23.220 34.604 1.00 39.45 ? 55  GLN A CA  1 
ATOM   446  C  C   . GLN A 1 60  ? 20.911 22.545 34.400 1.00 41.70 ? 55  GLN A C   1 
ATOM   447  O  O   . GLN A 1 60  ? 20.005 22.706 35.230 1.00 39.14 ? 55  GLN A O   1 
ATOM   448  C  CB  . GLN A 1 60  ? 22.342 24.506 33.796 1.00 42.30 ? 55  GLN A CB  1 
ATOM   449  C  CG  . GLN A 1 60  ? 23.525 25.365 34.132 1.00 39.90 ? 55  GLN A CG  1 
ATOM   450  C  CD  . GLN A 1 60  ? 23.678 26.503 33.138 1.00 42.42 ? 55  GLN A CD  1 
ATOM   451  O  OE1 . GLN A 1 60  ? 23.509 26.314 31.918 1.00 41.98 ? 55  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A 1 60  ? 23.984 27.692 33.644 1.00 36.83 ? 55  GLN A NE2 1 
ATOM   453  N  N   . ARG A 1 61  ? 20.762 21.778 33.306 1.00 38.31 ? 56  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 61  ? 19.530 21.025 33.068 1.00 37.86 ? 56  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 61  ? 19.278 20.005 34.169 1.00 39.78 ? 56  ARG A C   1 
ATOM   456  O  O   . ARG A 1 61  ? 18.147 19.855 34.642 1.00 40.35 ? 56  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 61  ? 19.594 20.315 31.704 1.00 37.42 ? 56  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 61  ? 19.492 21.255 30.512 1.00 38.27 ? 56  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 61  ? 19.902 20.548 29.213 1.00 44.84 ? 56  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 61  ? 18.868 19.633 28.728 1.00 45.96 ? 56  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 61  ? 19.100 18.559 27.978 1.00 48.94 ? 56  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 61  ? 20.328 18.190 27.653 1.00 42.23 ? 56  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 61  ? 18.072 17.838 27.538 1.00 44.96 ? 56  ARG A NH2 1 
ATOM   464  N  N   . ALA A 1 62  ? 20.313 19.245 34.538 1.00 40.61 ? 57  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 62  ? 20.168 18.259 35.604 1.00 42.76 ? 57  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 62  ? 19.769 18.922 36.918 1.00 38.83 ? 57  ALA A C   1 
ATOM   467  O  O   . ALA A 1 62  ? 18.896 18.419 37.633 1.00 38.04 ? 57  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 62  ? 21.467 17.473 35.776 1.00 41.88 ? 57  ALA A CB  1 
ATOM   469  N  N   . ALA A 1 63  ? 20.398 20.055 37.246 1.00 37.85 ? 58  ALA A N   1 
ATOM   470  C  CA  . ALA A 1 63  ? 20.016 20.804 38.442 1.00 40.79 ? 58  ALA A CA  1 
ATOM   471  C  C   . ALA A 1 63  ? 18.571 21.275 38.359 1.00 38.86 ? 58  ALA A C   1 
ATOM   472  O  O   . ALA A 1 63  ? 17.796 21.109 39.310 1.00 40.37 ? 58  ALA A O   1 
ATOM   473  C  CB  . ALA A 1 63  ? 20.958 21.998 38.640 1.00 38.12 ? 58  ALA A CB  1 
ATOM   474  N  N   . TRP A 1 64  ? 18.194 21.888 37.229 1.00 38.89 ? 59  TRP A N   1 
ATOM   475  C  CA  . TRP A 1 64  ? 16.829 22.377 37.071 1.00 36.72 ? 59  TRP A CA  1 
ATOM   476  C  C   . TRP A 1 64  ? 15.813 21.263 37.262 1.00 40.81 ? 59  TRP A C   1 
ATOM   477  O  O   . TRP A 1 64  ? 14.771 21.466 37.897 1.00 41.52 ? 59  TRP A O   1 
ATOM   478  C  CB  . TRP A 1 64  ? 16.670 23.017 35.697 1.00 39.69 ? 59  TRP A CB  1 
ATOM   479  C  CG  . TRP A 1 64  ? 15.361 23.676 35.447 1.00 44.36 ? 59  TRP A CG  1 
ATOM   480  C  CD1 . TRP A 1 64  ? 15.073 25.013 35.591 1.00 41.59 ? 59  TRP A CD1 1 
ATOM   481  C  CD2 . TRP A 1 64  ? 14.161 23.057 34.958 1.00 45.35 ? 59  TRP A CD2 1 
ATOM   482  N  NE1 . TRP A 1 64  ? 13.769 25.250 35.242 1.00 42.98 ? 59  TRP A NE1 1 
ATOM   483  C  CE2 . TRP A 1 64  ? 13.185 24.073 34.848 1.00 45.73 ? 59  TRP A CE2 1 
ATOM   484  C  CE3 . TRP A 1 64  ? 13.816 21.743 34.608 1.00 44.06 ? 59  TRP A CE3 1 
ATOM   485  C  CZ2 . TRP A 1 64  ? 11.886 23.818 34.411 1.00 46.99 ? 59  TRP A CZ2 1 
ATOM   486  C  CZ3 . TRP A 1 64  ? 12.530 21.490 34.168 1.00 47.52 ? 59  TRP A CZ3 1 
ATOM   487  C  CH2 . TRP A 1 64  ? 11.579 22.525 34.069 1.00 53.50 ? 59  TRP A CH2 1 
ATOM   488  N  N   . ARG A 1 65  ? 16.092 20.074 36.713 1.00 42.38 ? 60  ARG A N   1 
ATOM   489  C  CA  . ARG A 1 65  ? 15.139 18.976 36.818 1.00 41.53 ? 60  ARG A CA  1 
ATOM   490  C  C   . ARG A 1 65  ? 14.999 18.500 38.258 1.00 42.88 ? 60  ARG A C   1 
ATOM   491  O  O   . ARG A 1 65  ? 13.895 18.165 38.695 1.00 47.25 ? 60  ARG A O   1 
ATOM   492  C  CB  . ARG A 1 65  ? 15.568 17.818 35.916 1.00 44.75 ? 60  ARG A CB  1 
ATOM   493  C  CG  . ARG A 1 65  ? 15.440 18.115 34.434 1.00 44.10 ? 60  ARG A CG  1 
ATOM   494  C  CD  . ARG A 1 65  ? 15.526 16.831 33.626 1.00 53.52 ? 60  ARG A CD  1 
ATOM   495  N  NE  . ARG A 1 65  ? 16.908 16.459 33.346 1.00 57.62 ? 60  ARG A NE  1 
ATOM   496  C  CZ  . ARG A 1 65  ? 17.497 16.579 32.160 1.00 61.04 ? 60  ARG A CZ  1 
ATOM   497  N  NH1 . ARG A 1 65  ? 16.860 17.090 31.115 1.00 57.20 ? 60  ARG A NH1 1 
ATOM   498  N  NH2 . ARG A 1 65  ? 18.755 16.169 32.017 1.00 61.96 ? 60  ARG A NH2 1 
ATOM   499  N  N   . VAL A 1 66  ? 16.107 18.445 39.005 1.00 42.81 ? 61  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 66  ? 16.039 18.073 40.422 1.00 44.14 ? 61  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 66  ? 15.149 19.049 41.179 1.00 44.67 ? 61  VAL A C   1 
ATOM   502  O  O   . VAL A 1 66  ? 14.294 18.654 41.983 1.00 44.68 ? 61  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 66  ? 17.451 18.025 41.034 1.00 42.20 ? 61  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 66  ? 17.389 18.110 42.553 1.00 42.74 ? 61  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 66  ? 18.183 16.770 40.595 1.00 45.25 ? 61  VAL A CG2 1 
ATOM   506  N  N   . LEU A 1 67  ? 15.349 20.346 40.938 1.00 41.85 ? 62  LEU A N   1 
ATOM   507  C  CA  . LEU A 1 67  ? 14.618 21.362 41.689 1.00 42.35 ? 62  LEU A CA  1 
ATOM   508  C  C   . LEU A 1 67  ? 13.166 21.408 41.254 1.00 48.06 ? 62  LEU A C   1 
ATOM   509  O  O   . LEU A 1 67  ? 12.268 21.610 42.082 1.00 44.09 ? 62  LEU A O   1 
ATOM   510  C  CB  . LEU A 1 67  ? 15.270 22.732 41.490 1.00 41.80 ? 62  LEU A CB  1 
ATOM   511  C  CG  . LEU A 1 67  ? 16.727 22.770 41.921 1.00 40.68 ? 62  LEU A CG  1 
ATOM   512  C  CD1 . LEU A 1 67  ? 17.366 24.058 41.451 1.00 40.24 ? 62  LEU A CD1 1 
ATOM   513  C  CD2 . LEU A 1 67  ? 16.830 22.613 43.436 1.00 37.75 ? 62  LEU A CD2 1 
ATOM   514  N  N   . SER A 1 68  ? 12.927 21.248 39.947 1.00 45.03 ? 63  SER A N   1 
ATOM   515  C  CA  . SER A 1 68  ? 11.566 21.191 39.433 1.00 48.69 ? 63  SER A CA  1 
ATOM   516  C  C   . SER A 1 68  ? 10.802 20.026 40.039 1.00 47.72 ? 63  SER A C   1 
ATOM   517  O  O   . SER A 1 68  ? 9.619  20.155 40.374 1.00 51.67 ? 63  SER A O   1 
ATOM   518  C  CB  . SER A 1 68  ? 11.593 21.076 37.905 1.00 48.38 ? 63  SER A CB  1 
ATOM   519  O  OG  . SER A 1 68  ? 10.382 21.525 37.325 1.00 53.45 ? 63  SER A OG  1 
ATOM   520  N  N   . SER A 1 69  ? 11.457 18.877 40.185 1.00 45.73 ? 64  SER A N   1 
ATOM   521  C  CA  . SER A 1 69  ? 10.782 17.731 40.787 1.00 50.30 ? 64  SER A CA  1 
ATOM   522  C  C   . SER A 1 69  ? 10.414 18.016 42.237 1.00 56.85 ? 64  SER A C   1 
ATOM   523  O  O   . SER A 1 69  ? 9.292  17.732 42.675 1.00 59.20 ? 64  SER A O   1 
ATOM   524  C  CB  . SER A 1 69  ? 11.658 16.489 40.694 1.00 48.26 ? 64  SER A CB  1 
ATOM   525  O  OG  . SER A 1 69  ? 11.206 15.509 41.607 1.00 61.94 ? 64  SER A OG  1 
ATOM   526  N  N   . ILE A 1 70  ? 11.354 18.575 43.002 1.00 52.86 ? 65  ILE A N   1 
ATOM   527  C  CA  . ILE A 1 70  ? 11.052 18.973 44.373 1.00 53.01 ? 65  ILE A CA  1 
ATOM   528  C  C   . ILE A 1 70  ? 9.912  19.979 44.386 1.00 56.01 ? 65  ILE A C   1 
ATOM   529  O  O   . ILE A 1 70  ? 8.983  19.876 45.195 1.00 57.98 ? 65  ILE A O   1 
ATOM   530  C  CB  . ILE A 1 70  ? 12.318 19.528 45.048 1.00 45.79 ? 65  ILE A CB  1 
ATOM   531  C  CG1 . ILE A 1 70  ? 13.375 18.426 45.108 1.00 43.70 ? 65  ILE A CG1 1 
ATOM   532  C  CG2 . ILE A 1 70  ? 11.989 20.110 46.446 1.00 47.27 ? 65  ILE A CG2 1 
ATOM   533  C  CD1 . ILE A 1 70  ? 14.750 18.907 45.414 1.00 41.91 ? 65  ILE A CD1 1 
ATOM   534  N  N   . GLU A 1 71  ? 9.945  20.943 43.458 1.00 56.53 ? 66  GLU A N   1 
ATOM   535  C  CA  . GLU A 1 71  ? 8.927  21.989 43.420 1.00 57.36 ? 66  GLU A CA  1 
ATOM   536  C  C   . GLU A 1 71  ? 7.535  21.402 43.226 1.00 63.89 ? 66  GLU A C   1 
ATOM   537  O  O   . GLU A 1 71  ? 6.587  21.788 43.919 1.00 65.98 ? 66  GLU A O   1 
ATOM   538  C  CB  . GLU A 1 71  ? 9.247  22.984 42.308 1.00 53.72 ? 66  GLU A CB  1 
ATOM   539  C  CG  . GLU A 1 71  ? 8.532  24.318 42.431 1.00 55.74 ? 66  GLU A CG  1 
ATOM   540  C  CD  . GLU A 1 71  ? 8.760  25.217 41.231 1.00 53.12 ? 66  GLU A CD  1 
ATOM   541  O  OE1 . GLU A 1 71  ? 9.564  24.852 40.347 1.00 56.89 ? 66  GLU A OE1 1 
ATOM   542  O  OE2 . GLU A 1 71  ? 8.135  26.292 41.156 1.00 55.66 ? 66  GLU A OE2 1 
ATOM   543  N  N   . GLN A 1 72  ? 7.396  20.448 42.307 1.00 63.88 ? 67  GLN A N   1 
ATOM   544  C  CA  . GLN A 1 72  ? 6.077  19.902 42.017 1.00 67.05 ? 67  GLN A CA  1 
ATOM   545  C  C   . GLN A 1 72  ? 5.636  18.872 43.051 1.00 69.07 ? 67  GLN A C   1 
ATOM   546  O  O   . GLN A 1 72  ? 4.436  18.746 43.318 1.00 73.47 ? 67  GLN A O   1 
ATOM   547  C  CB  . GLN A 1 72  ? 6.068  19.294 40.617 1.00 65.97 ? 67  GLN A CB  1 
ATOM   548  C  CG  . GLN A 1 72  ? 6.527  20.282 39.561 1.00 71.19 ? 67  GLN A CG  1 
ATOM   549  C  CD  . GLN A 1 72  ? 5.403  20.746 38.664 1.00 77.43 ? 67  GLN A CD  1 
ATOM   550  O  OE1 . GLN A 1 72  ? 4.502  21.466 39.106 1.00 78.79 ? 67  GLN A OE1 1 
ATOM   551  N  NE2 . GLN A 1 72  ? 5.447  20.342 37.393 1.00 78.02 ? 67  GLN A NE2 1 
ATOM   552  N  N   . LYS A 1 73  ? 6.577  18.131 43.639 1.00 67.23 ? 68  LYS A N   1 
ATOM   553  C  CA  . LYS A 1 73  ? 6.210  17.163 44.666 1.00 68.54 ? 68  LYS A CA  1 
ATOM   554  C  C   . LYS A 1 73  ? 5.704  17.861 45.925 1.00 73.56 ? 68  LYS A C   1 
ATOM   555  O  O   . LYS A 1 73  ? 4.885  17.300 46.664 1.00 76.03 ? 68  LYS A O   1 
ATOM   556  C  CB  . LYS A 1 73  ? 7.403  16.255 44.976 1.00 69.79 ? 68  LYS A CB  1 
ATOM   557  C  CG  . LYS A 1 73  ? 7.313  15.495 46.297 1.00 70.67 ? 68  LYS A CG  1 
ATOM   558  C  CD  . LYS A 1 73  ? 8.040  14.161 46.220 1.00 75.92 ? 68  LYS A CD  1 
ATOM   559  C  CE  . LYS A 1 73  ? 7.693  13.395 44.948 1.00 76.74 ? 68  LYS A CE  1 
ATOM   560  N  NZ  . LYS A 1 73  ? 6.228  13.123 44.833 1.00 78.25 ? 68  LYS A NZ  1 
ATOM   561  N  N   . SER A 1 74  ? 6.155  19.085 46.177 1.00 71.85 ? 69  SER A N   1 
ATOM   562  C  CA  . SER A 1 74  ? 5.594  19.881 47.258 1.00 75.61 ? 69  SER A CA  1 
ATOM   563  C  C   . SER A 1 74  ? 4.304  20.596 46.851 1.00 78.57 ? 69  SER A C   1 
ATOM   564  O  O   . SER A 1 74  ? 3.976  21.635 47.439 1.00 77.25 ? 69  SER A O   1 
ATOM   565  C  CB  . SER A 1 74  ? 6.625  20.893 47.759 1.00 69.87 ? 69  SER A CB  1 
ATOM   566  O  OG  . SER A 1 74  ? 6.794  21.940 46.819 1.00 73.66 ? 69  SER A OG  1 
ATOM   567  N  N   . ASN A 1 75  ? 3.582  20.066 45.863 1.00 79.71 ? 70  ASN A N   1 
ATOM   568  C  CA  . ASN A 1 75  ? 2.282  20.602 45.452 1.00 79.46 ? 70  ASN A CA  1 
ATOM   569  C  C   . ASN A 1 75  ? 1.220  19.499 45.438 1.00 80.18 ? 70  ASN A C   1 
ATOM   570  O  O   . ASN A 1 75  ? 1.481  18.370 45.010 1.00 79.09 ? 70  ASN A O   1 
ATOM   571  C  CB  . ASN A 1 75  ? 2.370  21.258 44.070 1.00 77.19 ? 70  ASN A CB  1 
ATOM   572  C  CG  . ASN A 1 75  ? 3.125  22.579 44.090 1.00 78.89 ? 70  ASN A CG  1 
ATOM   573  O  OD1 . ASN A 1 75  ? 3.480  23.093 45.153 1.00 82.03 ? 70  ASN A OD1 1 
ATOM   574  N  ND2 . ASN A 1 75  ? 3.362  23.141 42.912 1.00 78.98 ? 70  ASN A ND2 1 
ATOM   575  N  N   . GLY A 1 83  ? 6.358  27.644 51.415 1.00 53.35 ? 78  GLY A N   1 
ATOM   576  C  CA  . GLY A 1 83  ? 7.453  28.604 51.356 1.00 54.11 ? 78  GLY A CA  1 
ATOM   577  C  C   . GLY A 1 83  ? 7.997  28.805 49.951 1.00 50.65 ? 78  GLY A C   1 
ATOM   578  O  O   . GLY A 1 83  ? 7.925  27.899 49.110 1.00 52.34 ? 78  GLY A O   1 
ATOM   579  N  N   . PRO A 1 84  ? 8.557  29.988 49.684 1.00 51.32 ? 79  PRO A N   1 
ATOM   580  C  CA  . PRO A 1 84  ? 8.947  30.337 48.312 1.00 44.87 ? 79  PRO A CA  1 
ATOM   581  C  C   . PRO A 1 84  ? 10.320 29.836 47.886 1.00 47.36 ? 79  PRO A C   1 
ATOM   582  O  O   . PRO A 1 84  ? 10.665 30.000 46.706 1.00 43.85 ? 79  PRO A O   1 
ATOM   583  C  CB  . PRO A 1 84  ? 8.924  31.866 48.347 1.00 47.78 ? 79  PRO A CB  1 
ATOM   584  C  CG  . PRO A 1 84  ? 9.375  32.173 49.748 1.00 47.99 ? 79  PRO A CG  1 
ATOM   585  C  CD  . PRO A 1 84  ? 8.728  31.122 50.609 1.00 46.93 ? 79  PRO A CD  1 
ATOM   586  N  N   . GLU A 1 85  ? 11.082 29.207 48.796 1.00 44.03 ? 80  GLU A N   1 
ATOM   587  C  CA  . GLU A 1 85  ? 12.510 28.965 48.579 1.00 40.20 ? 80  GLU A CA  1 
ATOM   588  C  C   . GLU A 1 85  ? 12.775 28.061 47.362 1.00 40.73 ? 80  GLU A C   1 
ATOM   589  O  O   . GLU A 1 85  ? 13.671 28.337 46.555 1.00 39.29 ? 80  GLU A O   1 
ATOM   590  C  CB  . GLU A 1 85  ? 13.123 28.367 49.850 1.00 43.73 ? 80  GLU A CB  1 
ATOM   591  C  CG  . GLU A 1 85  ? 13.307 29.368 51.006 1.00 43.42 ? 80  GLU A CG  1 
ATOM   592  C  CD  . GLU A 1 85  ? 12.047 29.568 51.860 1.00 46.80 ? 80  GLU A CD  1 
ATOM   593  O  OE1 . GLU A 1 85  ? 10.990 28.971 51.557 1.00 45.80 ? 80  GLU A OE1 1 
ATOM   594  O  OE2 . GLU A 1 85  ? 12.108 30.345 52.843 1.00 48.72 ? 80  GLU A OE2 1 
ATOM   595  N  N   . VAL A 1 86  ? 12.028 26.963 47.219 1.00 44.68 ? 81  VAL A N   1 
ATOM   596  C  CA  . VAL A 1 86  ? 12.290 26.051 46.098 1.00 42.61 ? 81  VAL A CA  1 
ATOM   597  C  C   . VAL A 1 86  ? 12.004 26.743 44.767 1.00 41.34 ? 81  VAL A C   1 
ATOM   598  O  O   . VAL A 1 86  ? 12.810 26.683 43.826 1.00 42.23 ? 81  VAL A O   1 
ATOM   599  C  CB  . VAL A 1 86  ? 11.485 24.749 46.244 1.00 40.58 ? 81  VAL A CB  1 
ATOM   600  C  CG1 . VAL A 1 86  ? 11.757 23.831 45.050 1.00 50.47 ? 81  VAL A CG1 1 
ATOM   601  C  CG2 . VAL A 1 86  ? 11.866 24.027 47.508 1.00 49.17 ? 81  VAL A CG2 1 
ATOM   602  N  N   . ARG A 1 87  ? 10.861 27.423 44.664 1.00 43.63 ? 82  ARG A N   1 
ATOM   603  C  CA  . ARG A 1 87  ? 10.566 28.151 43.431 1.00 44.53 ? 82  ARG A CA  1 
ATOM   604  C  C   . ARG A 1 87  ? 11.630 29.208 43.135 1.00 46.47 ? 82  ARG A C   1 
ATOM   605  O  O   . ARG A 1 87  ? 12.068 29.359 41.986 1.00 44.91 ? 82  ARG A O   1 
ATOM   606  C  CB  . ARG A 1 87  ? 9.181  28.793 43.512 1.00 50.19 ? 82  ARG A CB  1 
ATOM   607  C  CG  . ARG A 1 87  ? 8.852  29.656 42.298 1.00 52.63 ? 82  ARG A CG  1 
ATOM   608  C  CD  . ARG A 1 87  ? 7.526  30.384 42.452 1.00 57.53 ? 82  ARG A CD  1 
ATOM   609  N  NE  . ARG A 1 87  ? 7.460  31.178 43.676 1.00 54.97 ? 82  ARG A NE  1 
ATOM   610  C  CZ  . ARG A 1 87  ? 8.112  32.316 43.880 1.00 55.12 ? 82  ARG A CZ  1 
ATOM   611  N  NH1 . ARG A 1 87  ? 8.918  32.831 42.963 1.00 54.28 ? 82  ARG A NH1 1 
ATOM   612  N  NH2 . ARG A 1 87  ? 7.955  32.953 45.036 1.00 54.79 ? 82  ARG A NH2 1 
ATOM   613  N  N   . GLU A 1 88  ? 12.058 29.950 44.161 1.00 43.42 ? 83  GLU A N   1 
ATOM   614  C  CA  . GLU A 1 88  ? 13.073 30.987 43.974 1.00 42.56 ? 83  GLU A CA  1 
ATOM   615  C  C   . GLU A 1 88  ? 14.376 30.386 43.472 1.00 39.88 ? 83  GLU A C   1 
ATOM   616  O  O   . GLU A 1 88  ? 15.004 30.912 42.551 1.00 42.07 ? 83  GLU A O   1 
ATOM   617  C  CB  . GLU A 1 88  ? 13.316 31.727 45.297 1.00 41.22 ? 83  GLU A CB  1 
ATOM   618  C  CG  . GLU A 1 88  ? 12.119 32.451 45.858 1.00 42.11 ? 83  GLU A CG  1 
ATOM   619  C  CD  . GLU A 1 88  ? 12.428 33.170 47.176 1.00 44.61 ? 83  GLU A CD  1 
ATOM   620  O  OE1 . GLU A 1 88  ? 13.307 32.686 47.949 1.00 42.10 ? 83  GLU A OE1 1 
ATOM   621  O  OE2 . GLU A 1 88  ? 11.772 34.198 47.452 1.00 41.69 ? 83  GLU A OE2 1 
ATOM   622  N  N   . TYR A 1 89  ? 14.822 29.297 44.099 1.00 41.41 ? 84  TYR A N   1 
ATOM   623  C  CA  . TYR A 1 89  ? 16.086 28.700 43.696 1.00 42.14 ? 84  TYR A CA  1 
ATOM   624  C  C   . TYR A 1 89  ? 15.961 28.051 42.323 1.00 38.16 ? 84  TYR A C   1 
ATOM   625  O  O   . TYR A 1 89  ? 16.895 28.113 41.514 1.00 37.84 ? 84  TYR A O   1 
ATOM   626  C  CB  . TYR A 1 89  ? 16.559 27.686 44.745 1.00 40.96 ? 84  TYR A CB  1 
ATOM   627  C  CG  . TYR A 1 89  ? 17.926 27.136 44.425 1.00 40.90 ? 84  TYR A CG  1 
ATOM   628  C  CD1 . TYR A 1 89  ? 18.927 27.971 43.946 1.00 40.99 ? 84  TYR A CD1 1 
ATOM   629  C  CD2 . TYR A 1 89  ? 18.221 25.782 44.593 1.00 44.36 ? 84  TYR A CD2 1 
ATOM   630  C  CE1 . TYR A 1 89  ? 20.176 27.483 43.632 1.00 42.22 ? 84  TYR A CE1 1 
ATOM   631  C  CE2 . TYR A 1 89  ? 19.478 25.282 44.272 1.00 39.93 ? 84  TYR A CE2 1 
ATOM   632  C  CZ  . TYR A 1 89  ? 20.445 26.140 43.790 1.00 41.41 ? 84  TYR A CZ  1 
ATOM   633  O  OH  . TYR A 1 89  ? 21.693 25.665 43.470 1.00 42.32 ? 84  TYR A OH  1 
ATOM   634  N  N   . ARG A 1 90  ? 14.808 27.445 42.035 1.00 39.33 ? 85  ARG A N   1 
ATOM   635  C  CA  . ARG A 1 90  ? 14.585 26.893 40.697 1.00 41.57 ? 85  ARG A CA  1 
ATOM   636  C  C   . ARG A 1 90  ? 14.620 27.990 39.636 1.00 42.15 ? 85  ARG A C   1 
ATOM   637  O  O   . ARG A 1 90  ? 15.210 27.805 38.567 1.00 41.47 ? 85  ARG A O   1 
ATOM   638  C  CB  . ARG A 1 90  ? 13.256 26.132 40.636 1.00 41.54 ? 85  ARG A CB  1 
ATOM   639  C  CG  . ARG A 1 90  ? 13.042 25.342 39.288 1.00 42.13 ? 85  ARG A CG  1 
ATOM   640  C  CD  . ARG A 1 90  ? 12.190 26.113 38.286 1.00 46.63 ? 85  ARG A CD  1 
ATOM   641  N  NE  . ARG A 1 90  ? 10.932 26.563 38.868 1.00 46.00 ? 85  ARG A NE  1 
ATOM   642  C  CZ  . ARG A 1 90  ? 10.271 27.646 38.482 1.00 49.69 ? 85  ARG A CZ  1 
ATOM   643  N  NH1 . ARG A 1 90  ? 10.695 28.396 37.473 1.00 48.69 ? 85  ARG A NH1 1 
ATOM   644  N  NH2 . ARG A 1 90  ? 9.163  27.993 39.133 1.00 52.93 ? 85  ARG A NH2 1 
ATOM   645  N  N   . GLU A 1 91  ? 14.015 29.149 39.925 1.00 41.18 ? 86  GLU A N   1 
ATOM   646  C  CA  . GLU A 1 91  ? 14.065 30.271 38.988 1.00 42.42 ? 86  GLU A CA  1 
ATOM   647  C  C   . GLU A 1 91  ? 15.486 30.773 38.784 1.00 42.07 ? 86  GLU A C   1 
ATOM   648  O  O   . GLU A 1 91  ? 15.831 31.226 37.684 1.00 44.46 ? 86  GLU A O   1 
ATOM   649  C  CB  . GLU A 1 91  ? 13.167 31.419 39.472 1.00 46.28 ? 86  GLU A CB  1 
ATOM   650  C  CG  . GLU A 1 91  ? 11.672 31.195 39.219 1.00 51.39 ? 86  GLU A CG  1 
ATOM   651  C  CD  . GLU A 1 91  ? 10.777 32.178 39.969 1.00 57.13 ? 86  GLU A CD  1 
ATOM   652  O  OE1 . GLU A 1 91  ? 11.299 33.157 40.555 1.00 61.79 ? 86  GLU A OE1 1 
ATOM   653  O  OE2 . GLU A 1 91  ? 9.544  31.971 39.974 1.00 58.06 ? 86  GLU A OE2 1 
ATOM   654  N  N   . LYS A 1 92  ? 16.319 30.712 39.826 1.00 39.88 ? 87  LYS A N   1 
ATOM   655  C  CA  . LYS A 1 92  ? 17.697 31.186 39.720 1.00 38.03 ? 87  LYS A CA  1 
ATOM   656  C  C   . LYS A 1 92  ? 18.507 30.308 38.776 1.00 39.48 ? 87  LYS A C   1 
ATOM   657  O  O   . LYS A 1 92  ? 19.255 30.808 37.926 1.00 41.31 ? 87  LYS A O   1 
ATOM   658  C  CB  . LYS A 1 92  ? 18.347 31.206 41.110 1.00 41.06 ? 87  LYS A CB  1 
ATOM   659  C  CG  . LYS A 1 92  ? 19.846 31.511 41.072 1.00 45.75 ? 87  LYS A CG  1 
ATOM   660  C  CD  . LYS A 1 92  ? 20.490 31.387 42.454 1.00 50.81 ? 87  LYS A CD  1 
ATOM   661  C  CE  . LYS A 1 92  ? 21.959 31.804 42.436 1.00 52.60 ? 87  LYS A CE  1 
ATOM   662  N  NZ  . LYS A 1 92  ? 22.387 32.168 43.831 1.00 55.16 ? 87  LYS A NZ  1 
ATOM   663  N  N   . VAL A 1 93  ? 18.400 28.990 38.941 1.00 38.30 ? 88  VAL A N   1 
ATOM   664  C  CA  . VAL A 1 93  ? 19.059 28.067 38.017 1.00 42.24 ? 88  VAL A CA  1 
ATOM   665  C  C   . VAL A 1 93  ? 18.495 28.236 36.609 1.00 40.22 ? 88  VAL A C   1 
ATOM   666  O  O   . VAL A 1 93  ? 19.238 28.283 35.626 1.00 41.07 ? 88  VAL A O   1 
ATOM   667  C  CB  . VAL A 1 93  ? 18.909 26.619 38.519 1.00 41.18 ? 88  VAL A CB  1 
ATOM   668  C  CG1 . VAL A 1 93  ? 19.521 25.633 37.532 1.00 37.96 ? 88  VAL A CG1 1 
ATOM   669  C  CG2 . VAL A 1 93  ? 19.547 26.472 39.882 1.00 37.46 ? 88  VAL A CG2 1 
ATOM   670  N  N   . GLU A 1 94  ? 17.173 28.358 36.501 1.00 42.34 ? 89  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 94  ? 16.518 28.533 35.209 1.00 39.84 ? 89  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 94  ? 17.057 29.749 34.464 1.00 43.85 ? 89  GLU A C   1 
ATOM   673  O  O   . GLU A 1 94  ? 17.352 29.683 33.263 1.00 41.89 ? 89  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 94  ? 15.011 28.653 35.430 1.00 43.61 ? 89  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 94  ? 14.175 28.876 34.178 1.00 43.22 ? 89  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 94  ? 12.698 28.649 34.439 1.00 46.19 ? 89  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 94  ? 12.361 27.623 35.078 1.00 45.16 ? 89  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 94  ? 11.877 29.498 34.025 1.00 49.14 ? 89  GLU A OE2 1 
ATOM   679  N  N   . THR A 1 95  ? 17.188 30.876 35.162 1.00 42.80 ? 90  THR A N   1 
ATOM   680  C  CA  . THR A 1 95  ? 17.698 32.087 34.532 1.00 40.70 ? 90  THR A CA  1 
ATOM   681  C  C   . THR A 1 95  ? 19.131 31.910 34.051 1.00 41.30 ? 90  THR A C   1 
ATOM   682  O  O   . THR A 1 95  ? 19.514 32.440 33.000 1.00 37.97 ? 90  THR A O   1 
ATOM   683  C  CB  . THR A 1 95  ? 17.608 33.243 35.532 1.00 44.57 ? 90  THR A CB  1 
ATOM   684  O  OG1 . THR A 1 95  ? 16.245 33.400 35.936 1.00 46.07 ? 90  THR A OG1 1 
ATOM   685  C  CG2 . THR A 1 95  ? 18.116 34.524 34.927 1.00 42.86 ? 90  THR A CG2 1 
ATOM   686  N  N   . GLU A 1 96  ? 19.956 31.210 34.836 1.00 39.54 ? 91  GLU A N   1 
ATOM   687  C  CA  . GLU A 1 96  ? 21.331 30.953 34.426 1.00 41.86 ? 91  GLU A CA  1 
ATOM   688  C  C   . GLU A 1 96  ? 21.378 30.075 33.181 1.00 39.37 ? 91  GLU A C   1 
ATOM   689  O  O   . GLU A 1 96  ? 22.227 30.275 32.309 1.00 38.03 ? 91  GLU A O   1 
ATOM   690  C  CB  . GLU A 1 96  ? 22.105 30.285 35.565 1.00 41.96 ? 91  GLU A CB  1 
ATOM   691  C  CG  . GLU A 1 96  ? 23.057 31.237 36.299 1.00 51.30 ? 91  GLU A CG  1 
ATOM   692  C  CD  . GLU A 1 96  ? 23.467 30.745 37.681 1.00 50.38 ? 91  GLU A CD  1 
ATOM   693  O  OE1 . GLU A 1 96  ? 24.140 29.699 37.758 1.00 43.59 ? 91  GLU A OE1 1 
ATOM   694  O  OE2 . GLU A 1 96  ? 23.169 31.447 38.686 1.00 56.82 ? 91  GLU A OE2 1 
ATOM   695  N  N   . LEU A 1 97  ? 20.507 29.069 33.117 1.00 41.30 ? 92  LEU A N   1 
ATOM   696  C  CA  . LEU A 1 97  ? 20.463 28.173 31.963 1.00 43.04 ? 92  LEU A CA  1 
ATOM   697  C  C   . LEU A 1 97  ? 20.065 28.938 30.714 1.00 43.39 ? 92  LEU A C   1 
ATOM   698  O  O   . LEU A 1 97  ? 20.688 28.802 29.654 1.00 42.68 ? 92  LEU A O   1 
ATOM   699  C  CB  . LEU A 1 97  ? 19.477 27.037 32.230 1.00 39.11 ? 92  LEU A CB  1 
ATOM   700  C  CG  . LEU A 1 97  ? 19.346 25.889 31.217 1.00 40.89 ? 92  LEU A CG  1 
ATOM   701  C  CD1 . LEU A 1 97  ? 18.964 24.597 31.954 1.00 38.89 ? 92  LEU A CD1 1 
ATOM   702  C  CD2 . LEU A 1 97  ? 18.321 26.204 30.156 1.00 45.02 ? 92  LEU A CD2 1 
ATOM   703  N  N   . GLN A 1 98  ? 19.009 29.743 30.823 1.00 45.53 ? 93  GLN A N   1 
ATOM   704  C  CA  . GLN A 1 98  ? 18.593 30.560 29.695 1.00 42.40 ? 93  GLN A CA  1 
ATOM   705  C  C   . GLN A 1 98  ? 19.713 31.484 29.258 1.00 44.81 ? 93  GLN A C   1 
ATOM   706  O  O   . GLN A 1 98  ? 19.867 31.750 28.058 1.00 44.86 ? 93  GLN A O   1 
ATOM   707  C  CB  . GLN A 1 98  ? 17.342 31.354 30.068 1.00 45.27 ? 93  GLN A CB  1 
ATOM   708  C  CG  . GLN A 1 98  ? 16.094 30.487 30.248 1.00 41.75 ? 93  GLN A CG  1 
ATOM   709  C  CD  . GLN A 1 98  ? 14.986 31.217 30.983 1.00 48.22 ? 93  GLN A CD  1 
ATOM   710  O  OE1 . GLN A 1 98  ? 15.252 32.060 31.848 1.00 46.34 ? 93  GLN A OE1 1 
ATOM   711  N  NE2 . GLN A 1 98  ? 13.737 30.893 30.655 1.00 43.92 ? 93  GLN A NE2 1 
ATOM   712  N  N   . GLY A 1 99  ? 20.514 31.968 30.213 1.00 44.22 ? 94  GLY A N   1 
ATOM   713  C  CA  . GLY A 1 99  ? 21.603 32.867 29.868 1.00 42.54 ? 94  GLY A CA  1 
ATOM   714  C  C   . GLY A 1 99  ? 22.685 32.172 29.065 1.00 45.54 ? 94  GLY A C   1 
ATOM   715  O  O   . GLY A 1 99  ? 23.292 32.769 28.166 1.00 43.50 ? 94  GLY A O   1 
ATOM   716  N  N   . VAL A 1 100 ? 22.940 30.897 29.373 1.00 43.34 ? 95  VAL A N   1 
ATOM   717  C  CA  . VAL A 1 100 ? 23.932 30.163 28.604 1.00 43.36 ? 95  VAL A CA  1 
ATOM   718  C  C   . VAL A 1 100 ? 23.389 29.840 27.219 1.00 39.46 ? 95  VAL A C   1 
ATOM   719  O  O   . VAL A 1 100 ? 24.101 29.975 26.219 1.00 40.63 ? 95  VAL A O   1 
ATOM   720  C  CB  . VAL A 1 100 ? 24.375 28.901 29.367 1.00 43.72 ? 95  VAL A CB  1 
ATOM   721  C  CG1 . VAL A 1 100 ? 25.136 27.955 28.427 1.00 45.25 ? 95  VAL A CG1 1 
ATOM   722  C  CG2 . VAL A 1 100 ? 25.244 29.304 30.532 1.00 40.05 ? 95  VAL A CG2 1 
ATOM   723  N  N   . CYS A 1 101 ? 22.115 29.451 27.129 1.00 39.71 ? 96  CYS A N   1 
ATOM   724  C  CA  . CYS A 1 101 ? 21.526 29.176 25.818 1.00 41.80 ? 96  CYS A CA  1 
ATOM   725  C  C   . CYS A 1 101 ? 21.503 30.432 24.954 1.00 46.89 ? 96  CYS A C   1 
ATOM   726  O  O   . CYS A 1 101 ? 21.740 30.365 23.737 1.00 43.29 ? 96  CYS A O   1 
ATOM   727  C  CB  . CYS A 1 101 ? 20.113 28.619 25.966 1.00 40.12 ? 96  CYS A CB  1 
ATOM   728  S  SG  . CYS A 1 101 ? 19.971 27.014 26.826 1.00 41.13 ? 96  CYS A SG  1 
ATOM   729  N  N   . ASP A 1 102 ? 21.222 31.591 25.563 1.00 42.02 ? 97  ASP A N   1 
ATOM   730  C  CA  . ASP A 1 102 ? 21.268 32.840 24.807 1.00 45.15 ? 97  ASP A CA  1 
ATOM   731  C  C   . ASP A 1 102 ? 22.670 33.116 24.295 1.00 41.96 ? 97  ASP A C   1 
ATOM   732  O  O   . ASP A 1 102 ? 22.845 33.601 23.171 1.00 47.13 ? 97  ASP A O   1 
ATOM   733  C  CB  . ASP A 1 102 ? 20.766 33.995 25.668 1.00 46.78 ? 97  ASP A CB  1 
ATOM   734  C  CG  . ASP A 1 102 ? 19.272 33.943 25.875 1.00 50.49 ? 97  ASP A CG  1 
ATOM   735  O  OD1 . ASP A 1 102 ? 18.620 33.116 25.199 1.00 51.79 ? 97  ASP A OD1 1 
ATOM   736  O  OD2 . ASP A 1 102 ? 18.748 34.711 26.711 1.00 54.05 ? 97  ASP A OD2 1 
ATOM   737  N  N   . THR A 1 103 ? 23.682 32.772 25.085 1.00 40.98 ? 98  THR A N   1 
ATOM   738  C  CA  . THR A 1 103 ? 25.057 32.989 24.657 1.00 39.67 ? 98  THR A CA  1 
ATOM   739  C  C   . THR A 1 103 ? 25.412 32.105 23.468 1.00 42.33 ? 98  THR A C   1 
ATOM   740  O  O   . THR A 1 103 ? 25.996 32.578 22.487 1.00 41.47 ? 98  THR A O   1 
ATOM   741  C  CB  . THR A 1 103 ? 25.989 32.749 25.844 1.00 42.58 ? 98  THR A CB  1 
ATOM   742  O  OG1 . THR A 1 103 ? 25.645 33.683 26.870 1.00 45.20 ? 98  THR A OG1 1 
ATOM   743  C  CG2 . THR A 1 103 ? 27.449 32.944 25.467 1.00 40.15 ? 98  THR A CG2 1 
ATOM   744  N  N   . VAL A 1 104 ? 25.055 30.823 23.528 1.00 41.11 ? 99  VAL A N   1 
ATOM   745  C  CA  . VAL A 1 104 ? 25.323 29.933 22.404 1.00 38.23 ? 99  VAL A CA  1 
ATOM   746  C  C   . VAL A 1 104 ? 24.593 30.426 21.162 1.00 39.06 ? 99  VAL A C   1 
ATOM   747  O  O   . VAL A 1 104 ? 25.184 30.557 20.085 1.00 38.45 ? 99  VAL A O   1 
ATOM   748  C  CB  . VAL A 1 104 ? 24.936 28.485 22.756 1.00 36.84 ? 99  VAL A CB  1 
ATOM   749  C  CG1 . VAL A 1 104 ? 25.130 27.571 21.538 1.00 41.60 ? 99  VAL A CG1 1 
ATOM   750  C  CG2 . VAL A 1 104 ? 25.775 27.986 23.932 1.00 35.43 ? 99  VAL A CG2 1 
ATOM   751  N  N   . LEU A 1 105 ? 23.298 30.726 21.303 1.00 41.09 ? 100 LEU A N   1 
ATOM   752  C  CA  . LEU A 1 105 ? 22.502 31.143 20.152 1.00 45.02 ? 100 LEU A CA  1 
ATOM   753  C  C   . LEU A 1 105 ? 23.016 32.446 19.564 1.00 46.26 ? 100 LEU A C   1 
ATOM   754  O  O   . LEU A 1 105 ? 22.922 32.658 18.349 1.00 47.22 ? 100 LEU A O   1 
ATOM   755  C  CB  . LEU A 1 105 ? 21.032 31.276 20.554 1.00 44.37 ? 100 LEU A CB  1 
ATOM   756  C  CG  . LEU A 1 105 ? 20.339 29.952 20.894 1.00 44.30 ? 100 LEU A CG  1 
ATOM   757  C  CD1 . LEU A 1 105 ? 18.991 30.189 21.536 1.00 44.35 ? 100 LEU A CD1 1 
ATOM   758  C  CD2 . LEU A 1 105 ? 20.200 29.102 19.634 1.00 44.82 ? 100 LEU A CD2 1 
ATOM   759  N  N   . GLY A 1 106 ? 23.561 33.328 20.407 1.00 42.45 ? 101 GLY A N   1 
ATOM   760  C  CA  . GLY A 1 106 ? 24.138 34.557 19.898 1.00 46.13 ? 101 GLY A CA  1 
ATOM   761  C  C   . GLY A 1 106 ? 25.414 34.321 19.119 1.00 47.22 ? 101 GLY A C   1 
ATOM   762  O  O   . GLY A 1 106 ? 25.644 34.957 18.087 1.00 49.17 ? 101 GLY A O   1 
ATOM   763  N  N   . LEU A 1 107 ? 26.264 33.408 19.598 1.00 44.62 ? 102 LEU A N   1 
ATOM   764  C  CA  . LEU A 1 107 ? 27.452 33.046 18.829 1.00 44.31 ? 102 LEU A CA  1 
ATOM   765  C  C   . LEU A 1 107 ? 27.066 32.423 17.501 1.00 44.28 ? 102 LEU A C   1 
ATOM   766  O  O   . LEU A 1 107 ? 27.686 32.705 16.467 1.00 44.40 ? 102 LEU A O   1 
ATOM   767  C  CB  . LEU A 1 107 ? 28.335 32.074 19.617 1.00 42.58 ? 102 LEU A CB  1 
ATOM   768  C  CG  . LEU A 1 107 ? 29.140 32.610 20.802 1.00 46.52 ? 102 LEU A CG  1 
ATOM   769  C  CD1 . LEU A 1 107 ? 29.694 31.450 21.657 1.00 39.79 ? 102 LEU A CD1 1 
ATOM   770  C  CD2 . LEU A 1 107 ? 30.265 33.557 20.347 1.00 42.97 ? 102 LEU A CD2 1 
ATOM   771  N  N   . LEU A 1 108 ? 26.034 31.578 17.506 1.00 41.33 ? 103 LEU A N   1 
ATOM   772  C  CA  . LEU A 1 108 ? 25.610 30.928 16.272 1.00 41.17 ? 103 LEU A CA  1 
ATOM   773  C  C   . LEU A 1 108 ? 25.136 31.953 15.247 1.00 43.81 ? 103 LEU A C   1 
ATOM   774  O  O   . LEU A 1 108 ? 25.521 31.897 14.071 1.00 47.47 ? 103 LEU A O   1 
ATOM   775  C  CB  . LEU A 1 108 ? 24.514 29.913 16.577 1.00 40.96 ? 103 LEU A CB  1 
ATOM   776  C  CG  . LEU A 1 108 ? 25.010 28.618 17.244 1.00 39.84 ? 103 LEU A CG  1 
ATOM   777  C  CD1 . LEU A 1 108 ? 23.855 27.903 17.874 1.00 36.52 ? 103 LEU A CD1 1 
ATOM   778  C  CD2 . LEU A 1 108 ? 25.712 27.735 16.216 1.00 39.95 ? 103 LEU A CD2 1 
ATOM   779  N  N   . ASP A 1 109 ? 24.314 32.911 15.674 1.00 45.12 ? 104 ASP A N   1 
ATOM   780  C  CA  . ASP A 1 109 ? 23.778 33.883 14.720 1.00 48.42 ? 104 ASP A CA  1 
ATOM   781  C  C   . ASP A 1 109 ? 24.797 34.956 14.362 1.00 49.88 ? 104 ASP A C   1 
ATOM   782  O  O   . ASP A 1 109 ? 24.886 35.368 13.197 1.00 50.30 ? 104 ASP A O   1 
ATOM   783  C  CB  . ASP A 1 109 ? 22.504 34.519 15.269 1.00 51.54 ? 104 ASP A CB  1 
ATOM   784  C  CG  . ASP A 1 109 ? 21.316 33.565 15.241 1.00 57.93 ? 104 ASP A CG  1 
ATOM   785  O  OD1 . ASP A 1 109 ? 20.456 33.705 16.137 1.00 61.77 ? 104 ASP A OD1 1 
ATOM   786  O  OD2 . ASP A 1 109 ? 21.240 32.672 14.342 1.00 50.79 ? 104 ASP A OD2 1 
ATOM   787  N  N   . SER A 1 110 ? 25.574 35.422 15.337 1.00 48.14 ? 105 SER A N   1 
ATOM   788  C  CA  . SER A 1 110 ? 26.534 36.482 15.069 1.00 47.35 ? 105 SER A CA  1 
ATOM   789  C  C   . SER A 1 110 ? 27.753 35.984 14.313 1.00 49.28 ? 105 SER A C   1 
ATOM   790  O  O   . SER A 1 110 ? 28.381 36.756 13.580 1.00 48.09 ? 105 SER A O   1 
ATOM   791  C  CB  . SER A 1 110 ? 26.972 37.131 16.382 1.00 48.16 ? 105 SER A CB  1 
ATOM   792  O  OG  . SER A 1 110 ? 25.846 37.666 17.062 1.00 49.61 ? 105 SER A OG  1 
ATOM   793  N  N   . HIS A 1 111 ? 28.110 34.728 14.469 1.00 46.55 ? 106 HIS A N   1 
ATOM   794  C  CA  . HIS A 1 111 ? 29.426 34.365 13.958 1.00 46.67 ? 106 HIS A CA  1 
ATOM   795  C  C   . HIS A 1 111 ? 29.452 33.079 13.160 1.00 46.04 ? 106 HIS A C   1 
ATOM   796  O  O   . HIS A 1 111 ? 30.176 33.007 12.166 1.00 49.69 ? 106 HIS A O   1 
ATOM   797  C  CB  . HIS A 1 111 ? 30.422 34.242 15.116 1.00 47.58 ? 106 HIS A CB  1 
ATOM   798  C  CG  . HIS A 1 111 ? 30.853 35.558 15.675 1.00 51.07 ? 106 HIS A CG  1 
ATOM   799  N  ND1 . HIS A 1 111 ? 31.863 36.309 15.108 1.00 49.39 ? 106 HIS A ND1 1 
ATOM   800  C  CD2 . HIS A 1 111 ? 30.403 36.268 16.735 1.00 52.10 ? 106 HIS A CD2 1 
ATOM   801  C  CE1 . HIS A 1 111 ? 32.023 37.421 15.804 1.00 48.73 ? 106 HIS A CE1 1 
ATOM   802  N  NE2 . HIS A 1 111 ? 31.147 37.423 16.794 1.00 52.23 ? 106 HIS A NE2 1 
ATOM   803  N  N   . LEU A 1 112 ? 28.710 32.058 13.575 1.00 43.09 ? 107 LEU A N   1 
ATOM   804  C  CA  . LEU A 1 112 ? 28.975 30.713 13.077 1.00 44.31 ? 107 LEU A CA  1 
ATOM   805  C  C   . LEU A 1 112 ? 28.109 30.301 11.892 1.00 44.17 ? 107 LEU A C   1 
ATOM   806  O  O   . LEU A 1 112 ? 28.631 29.722 10.933 1.00 44.40 ? 107 LEU A O   1 
ATOM   807  C  CB  . LEU A 1 112 ? 28.814 29.704 14.217 1.00 40.80 ? 107 LEU A CB  1 
ATOM   808  C  CG  . LEU A 1 112 ? 29.817 29.931 15.355 1.00 41.33 ? 107 LEU A CG  1 
ATOM   809  C  CD1 . LEU A 1 112 ? 29.383 29.178 16.615 1.00 35.90 ? 107 LEU A CD1 1 
ATOM   810  C  CD2 . LEU A 1 112 ? 31.206 29.490 14.897 1.00 41.10 ? 107 LEU A CD2 1 
ATOM   811  N  N   . ILE A 1 113 ? 26.797 30.531 11.948 1.00 44.55 ? 108 ILE A N   1 
ATOM   812  C  CA  . ILE A 1 113 ? 25.940 30.108 10.847 1.00 45.99 ? 108 ILE A CA  1 
ATOM   813  C  C   . ILE A 1 113 ? 26.152 31.034 9.656  1.00 51.49 ? 108 ILE A C   1 
ATOM   814  O  O   . ILE A 1 113 ? 26.023 32.260 9.761  1.00 52.84 ? 108 ILE A O   1 
ATOM   815  C  CB  . ILE A 1 113 ? 24.458 30.066 11.255 1.00 45.17 ? 108 ILE A CB  1 
ATOM   816  C  CG1 . ILE A 1 113 ? 24.212 29.060 12.381 1.00 47.03 ? 108 ILE A CG1 1 
ATOM   817  C  CG2 . ILE A 1 113 ? 23.598 29.692 10.046 1.00 52.21 ? 108 ILE A CG2 1 
ATOM   818  C  CD1 . ILE A 1 113 ? 22.884 29.241 13.085 1.00 45.42 ? 108 ILE A CD1 1 
ATOM   819  N  N   . LYS A 1 114 ? 26.498 30.454 8.516  1.00 51.40 ? 109 LYS A N   1 
ATOM   820  C  CA  . LYS A 1 114 ? 26.643 31.234 7.298  1.00 60.84 ? 109 LYS A CA  1 
ATOM   821  C  C   . LYS A 1 114 ? 26.024 30.456 6.146  1.00 64.74 ? 109 LYS A C   1 
ATOM   822  O  O   . LYS A 1 114 ? 25.764 29.253 6.251  1.00 61.47 ? 109 LYS A O   1 
ATOM   823  C  CB  . LYS A 1 114 ? 28.117 31.560 7.008  1.00 59.28 ? 109 LYS A CB  1 
ATOM   824  C  CG  . LYS A 1 114 ? 28.751 32.528 7.974  1.00 59.11 ? 109 LYS A CG  1 
ATOM   825  C  CD  . LYS A 1 114 ? 30.257 32.461 7.874  1.00 61.98 ? 109 LYS A CD  1 
ATOM   826  C  CE  . LYS A 1 114 ? 30.905 33.293 8.963  1.00 64.51 ? 109 LYS A CE  1 
ATOM   827  N  NZ  . LYS A 1 114 ? 32.393 33.190 8.916  1.00 69.09 ? 109 LYS A NZ  1 
ATOM   828  N  N   . GLU A 1 115 ? 25.761 31.170 5.047  1.00 69.63 ? 110 GLU A N   1 
ATOM   829  C  CA  . GLU A 1 115 ? 25.376 30.500 3.812  1.00 71.20 ? 110 GLU A CA  1 
ATOM   830  C  C   . GLU A 1 115 ? 26.553 29.765 3.179  1.00 66.45 ? 110 GLU A C   1 
ATOM   831  O  O   . GLU A 1 115 ? 26.338 28.807 2.429  1.00 71.85 ? 110 GLU A O   1 
ATOM   832  C  CB  . GLU A 1 115 ? 24.794 31.510 2.821  1.00 76.32 ? 110 GLU A CB  1 
ATOM   833  C  CG  . GLU A 1 115 ? 23.418 32.080 3.191  1.00 79.29 ? 110 GLU A CG  1 
ATOM   834  C  CD  . GLU A 1 115 ? 22.250 31.189 2.768  1.00 86.24 ? 110 GLU A CD  1 
ATOM   835  O  OE1 . GLU A 1 115 ? 22.465 29.979 2.516  1.00 85.13 ? 110 GLU A OE1 1 
ATOM   836  O  OE2 . GLU A 1 115 ? 21.117 31.714 2.659  1.00 89.90 ? 110 GLU A OE2 1 
ATOM   837  N  N   . ALA A 1 116 ? 27.785 30.185 3.479  1.00 68.57 ? 111 ALA A N   1 
ATOM   838  C  CA  . ALA A 1 116 ? 28.992 29.578 2.930  1.00 70.44 ? 111 ALA A CA  1 
ATOM   839  C  C   . ALA A 1 116 ? 29.456 28.423 3.826  1.00 73.28 ? 111 ALA A C   1 
ATOM   840  O  O   . ALA A 1 116 ? 28.696 27.917 4.662  1.00 65.38 ? 111 ALA A O   1 
ATOM   841  C  CB  . ALA A 1 116 ? 30.071 30.654 2.750  1.00 74.97 ? 111 ALA A CB  1 
ATOM   842  N  N   . GLY A 1 117 ? 30.706 27.993 3.669  1.00 72.17 ? 112 GLY A N   1 
ATOM   843  C  CA  . GLY A 1 117 ? 31.210 26.839 4.381  1.00 70.40 ? 112 GLY A CA  1 
ATOM   844  C  C   . GLY A 1 117 ? 30.644 25.543 3.825  1.00 66.68 ? 112 GLY A C   1 
ATOM   845  O  O   . GLY A 1 117 ? 29.657 25.519 3.086  1.00 68.78 ? 112 GLY A O   1 
ATOM   846  N  N   . ASP A 1 118 ? 31.282 24.437 4.185  1.00 64.85 ? 113 ASP A N   1 
ATOM   847  C  CA  . ASP A 1 118 ? 30.786 23.170 3.673  1.00 60.91 ? 113 ASP A CA  1 
ATOM   848  C  C   . ASP A 1 118 ? 29.478 22.798 4.377  1.00 59.91 ? 113 ASP A C   1 
ATOM   849  O  O   . ASP A 1 118 ? 28.999 23.487 5.289  1.00 57.32 ? 113 ASP A O   1 
ATOM   850  C  CB  . ASP A 1 118 ? 31.847 22.075 3.802  1.00 63.49 ? 113 ASP A CB  1 
ATOM   851  C  CG  . ASP A 1 118 ? 32.383 21.912 5.216  1.00 60.72 ? 113 ASP A CG  1 
ATOM   852  O  OD1 . ASP A 1 118 ? 31.755 22.401 6.176  1.00 58.18 ? 113 ASP A OD1 1 
ATOM   853  O  OD2 . ASP A 1 118 ? 33.438 21.257 5.356  1.00 62.17 ? 113 ASP A OD2 1 
ATOM   854  N  N   . ALA A 1 119 ? 28.880 21.699 3.919  1.00 59.06 ? 114 ALA A N   1 
ATOM   855  C  CA  . ALA A 1 119 ? 27.599 21.271 4.461  1.00 56.49 ? 114 ALA A CA  1 
ATOM   856  C  C   . ALA A 1 119 ? 27.738 20.706 5.863  1.00 53.30 ? 114 ALA A C   1 
ATOM   857  O  O   . ALA A 1 119 ? 26.828 20.883 6.680  1.00 54.44 ? 114 ALA A O   1 
ATOM   858  C  CB  . ALA A 1 119 ? 26.959 20.227 3.546  1.00 61.29 ? 114 ALA A CB  1 
ATOM   859  N  N   . GLU A 1 120 ? 28.838 19.998 6.146  1.00 50.23 ? 115 GLU A N   1 
ATOM   860  C  CA  . GLU A 1 120 ? 29.116 19.534 7.503  1.00 53.06 ? 115 GLU A CA  1 
ATOM   861  C  C   . GLU A 1 120 ? 28.965 20.661 8.518  1.00 48.74 ? 115 GLU A C   1 
ATOM   862  O  O   . GLU A 1 120 ? 28.208 20.548 9.494  1.00 45.82 ? 115 GLU A O   1 
ATOM   863  C  CB  . GLU A 1 120 ? 30.529 18.952 7.583  1.00 52.34 ? 115 GLU A CB  1 
ATOM   864  C  CG  . GLU A 1 120 ? 30.702 17.573 6.986  1.00 56.97 ? 115 GLU A CG  1 
ATOM   865  C  CD  . GLU A 1 120 ? 31.540 16.681 7.876  1.00 58.29 ? 115 GLU A CD  1 
ATOM   866  O  OE1 . GLU A 1 120 ? 32.730 17.016 8.080  1.00 61.10 ? 115 GLU A OE1 1 
ATOM   867  O  OE2 . GLU A 1 120 ? 31.029 15.646 8.356  1.00 54.64 ? 115 GLU A OE2 1 
ATOM   868  N  N   . SER A 1 121 ? 29.699 21.757 8.312  1.00 49.31 ? 116 SER A N   1 
ATOM   869  C  CA  . SER A 1 121 ? 29.645 22.850 9.279  1.00 48.86 ? 116 SER A CA  1 
ATOM   870  C  C   . SER A 1 121 ? 28.253 23.466 9.337  1.00 46.10 ? 116 SER A C   1 
ATOM   871  O  O   . SER A 1 121 ? 27.733 23.730 10.428 1.00 44.52 ? 116 SER A O   1 
ATOM   872  C  CB  . SER A 1 121 ? 30.692 23.911 8.948  1.00 52.20 ? 116 SER A CB  1 
ATOM   873  O  OG  . SER A 1 121 ? 30.608 24.304 7.597  1.00 56.04 ? 116 SER A OG  1 
ATOM   874  N  N   . ARG A 1 122 ? 27.623 23.688 8.176  1.00 46.52 ? 117 ARG A N   1 
ATOM   875  C  CA  . ARG A 1 122 ? 26.305 24.317 8.176  1.00 46.87 ? 117 ARG A CA  1 
ATOM   876  C  C   . ARG A 1 122 ? 25.279 23.454 8.898  1.00 45.48 ? 117 ARG A C   1 
ATOM   877  O  O   . ARG A 1 122 ? 24.446 23.970 9.654  1.00 43.51 ? 117 ARG A O   1 
ATOM   878  C  CB  . ARG A 1 122 ? 25.849 24.609 6.745  1.00 54.68 ? 117 ARG A CB  1 
ATOM   879  C  CG  . ARG A 1 122 ? 26.379 25.919 6.170  1.00 57.50 ? 117 ARG A CG  1 
ATOM   880  C  CD  . ARG A 1 122 ? 25.937 26.128 4.716  1.00 63.12 ? 117 ARG A CD  1 
ATOM   881  N  NE  . ARG A 1 122 ? 26.439 25.086 3.824  1.00 64.85 ? 117 ARG A NE  1 
ATOM   882  C  CZ  . ARG A 1 122 ? 25.671 24.277 3.101  1.00 64.43 ? 117 ARG A CZ  1 
ATOM   883  N  NH1 . ARG A 1 122 ? 24.349 24.371 3.126  1.00 64.92 ? 117 ARG A NH1 1 
ATOM   884  N  NH2 . ARG A 1 122 ? 26.245 23.353 2.334  1.00 62.38 ? 117 ARG A NH2 1 
ATOM   885  N  N   . VAL A 1 123 ? 25.320 22.137 8.684  1.00 43.01 ? 118 VAL A N   1 
ATOM   886  C  CA  . VAL A 1 123 ? 24.379 21.261 9.372  1.00 41.17 ? 118 VAL A CA  1 
ATOM   887  C  C   . VAL A 1 123 ? 24.664 21.251 10.869 1.00 43.10 ? 118 VAL A C   1 
ATOM   888  O  O   . VAL A 1 123 ? 23.740 21.226 11.693 1.00 40.99 ? 118 VAL A O   1 
ATOM   889  C  CB  . VAL A 1 123 ? 24.435 19.836 8.793  1.00 40.97 ? 118 VAL A CB  1 
ATOM   890  C  CG1 . VAL A 1 123 ? 23.545 18.914 9.584  1.00 40.53 ? 118 VAL A CG1 1 
ATOM   891  C  CG2 . VAL A 1 123 ? 24.028 19.834 7.296  1.00 44.48 ? 118 VAL A CG2 1 
ATOM   892  N  N   . PHE A 1 124 ? 25.941 21.229 11.246 1.00 41.55 ? 119 PHE A N   1 
ATOM   893  C  CA  . PHE A 1 124 ? 26.247 21.102 12.667 1.00 41.44 ? 119 PHE A CA  1 
ATOM   894  C  C   . PHE A 1 124 ? 25.768 22.326 13.447 1.00 39.75 ? 119 PHE A C   1 
ATOM   895  O  O   . PHE A 1 124 ? 25.252 22.195 14.566 1.00 42.58 ? 119 PHE A O   1 
ATOM   896  C  CB  . PHE A 1 124 ? 27.741 20.895 12.896 1.00 38.36 ? 119 PHE A CB  1 
ATOM   897  C  CG  . PHE A 1 124 ? 28.125 21.106 14.336 1.00 44.14 ? 119 PHE A CG  1 
ATOM   898  C  CD1 . PHE A 1 124 ? 27.904 20.100 15.267 1.00 42.00 ? 119 PHE A CD1 1 
ATOM   899  C  CD2 . PHE A 1 124 ? 28.613 22.342 14.774 1.00 41.50 ? 119 PHE A CD2 1 
ATOM   900  C  CE1 . PHE A 1 124 ? 28.203 20.294 16.603 1.00 45.03 ? 119 PHE A CE1 1 
ATOM   901  C  CE2 . PHE A 1 124 ? 28.924 22.545 16.124 1.00 40.98 ? 119 PHE A CE2 1 
ATOM   902  C  CZ  . PHE A 1 124 ? 28.712 21.510 17.037 1.00 41.61 ? 119 PHE A CZ  1 
ATOM   903  N  N   . TYR A 1 125 ? 25.931 23.526 12.874 1.00 39.14 ? 120 TYR A N   1 
ATOM   904  C  CA  . TYR A 1 125 ? 25.515 24.734 13.588 1.00 39.51 ? 120 TYR A CA  1 
ATOM   905  C  C   . TYR A 1 125 ? 24.000 24.838 13.661 1.00 41.20 ? 120 TYR A C   1 
ATOM   906  O  O   . TYR A 1 125 ? 23.454 25.279 14.676 1.00 39.19 ? 120 TYR A O   1 
ATOM   907  C  CB  . TYR A 1 125 ? 26.110 25.974 12.936 1.00 39.67 ? 120 TYR A CB  1 
ATOM   908  C  CG  . TYR A 1 125 ? 27.608 26.051 13.067 1.00 41.83 ? 120 TYR A CG  1 
ATOM   909  C  CD1 . TYR A 1 125 ? 28.240 25.879 14.307 1.00 40.04 ? 120 TYR A CD1 1 
ATOM   910  C  CD2 . TYR A 1 125 ? 28.395 26.293 11.960 1.00 44.12 ? 120 TYR A CD2 1 
ATOM   911  C  CE1 . TYR A 1 125 ? 29.610 25.951 14.416 1.00 36.86 ? 120 TYR A CE1 1 
ATOM   912  C  CE2 . TYR A 1 125 ? 29.764 26.374 12.066 1.00 43.88 ? 120 TYR A CE2 1 
ATOM   913  C  CZ  . TYR A 1 125 ? 30.367 26.198 13.289 1.00 39.52 ? 120 TYR A CZ  1 
ATOM   914  O  OH  . TYR A 1 125 ? 31.744 26.270 13.356 1.00 39.76 ? 120 TYR A OH  1 
ATOM   915  N  N   . LEU A 1 126 ? 23.299 24.428 12.599 1.00 40.55 ? 121 LEU A N   1 
ATOM   916  C  CA  . LEU A 1 126 ? 21.839 24.435 12.650 1.00 40.41 ? 121 LEU A CA  1 
ATOM   917  C  C   . LEU A 1 126 ? 21.302 23.388 13.625 1.00 40.38 ? 121 LEU A C   1 
ATOM   918  O  O   . LEU A 1 126 ? 20.268 23.605 14.273 1.00 39.74 ? 121 LEU A O   1 
ATOM   919  C  CB  . LEU A 1 126 ? 21.273 24.211 11.247 1.00 43.07 ? 121 LEU A CB  1 
ATOM   920  C  CG  . LEU A 1 126 ? 21.431 25.376 10.258 1.00 42.28 ? 121 LEU A CG  1 
ATOM   921  C  CD1 . LEU A 1 126 ? 21.244 24.889 8.798  1.00 43.76 ? 121 LEU A CD1 1 
ATOM   922  C  CD2 . LEU A 1 126 ? 20.436 26.449 10.589 1.00 44.33 ? 121 LEU A CD2 1 
ATOM   923  N  N   . LYS A 1 127 ? 21.949 22.220 13.696 1.00 41.13 ? 122 LYS A N   1 
ATOM   924  C  CA  . LYS A 1 127 ? 21.618 21.263 14.751 1.00 42.57 ? 122 LYS A CA  1 
ATOM   925  C  C   . LYS A 1 127 ? 21.880 21.864 16.130 1.00 40.81 ? 122 LYS A C   1 
ATOM   926  O  O   . LYS A 1 127 ? 21.060 21.723 17.044 1.00 37.75 ? 122 LYS A O   1 
ATOM   927  C  CB  . LYS A 1 127 ? 22.417 19.969 14.564 1.00 37.40 ? 122 LYS A CB  1 
ATOM   928  C  CG  . LYS A 1 127 ? 22.494 19.111 15.826 1.00 39.90 ? 122 LYS A CG  1 
ATOM   929  C  CD  . LYS A 1 127 ? 23.589 18.070 15.741 1.00 35.47 ? 122 LYS A CD  1 
ATOM   930  C  CE  . LYS A 1 127 ? 23.555 17.171 16.964 1.00 40.76 ? 122 LYS A CE  1 
ATOM   931  N  NZ  . LYS A 1 127 ? 23.901 17.976 18.203 1.00 38.63 ? 122 LYS A NZ  1 
ATOM   932  N  N   . MET A 1 128 ? 23.016 22.547 16.294 1.00 40.37 ? 123 MET A N   1 
ATOM   933  C  CA  . MET A 1 128 ? 23.309 23.180 17.580 1.00 38.56 ? 123 MET A CA  1 
ATOM   934  C  C   . MET A 1 128 ? 22.269 24.244 17.909 1.00 40.18 ? 123 MET A C   1 
ATOM   935  O  O   . MET A 1 128 ? 21.772 24.310 19.037 1.00 41.07 ? 123 MET A O   1 
ATOM   936  C  CB  . MET A 1 128 ? 24.712 23.783 17.556 1.00 39.64 ? 123 MET A CB  1 
ATOM   937  C  CG  . MET A 1 128 ? 25.187 24.366 18.908 1.00 42.11 ? 123 MET A CG  1 
ATOM   938  S  SD  . MET A 1 128 ? 26.905 24.924 18.829 1.00 44.99 ? 123 MET A SD  1 
ATOM   939  C  CE  . MET A 1 128 ? 27.489 24.527 20.490 1.00 42.80 ? 123 MET A CE  1 
ATOM   940  N  N   . LYS A 1 129 ? 21.887 25.057 16.917 1.00 42.46 ? 124 LYS A N   1 
ATOM   941  C  CA  . LYS A 1 129 ? 20.818 26.025 17.133 1.00 38.95 ? 124 LYS A CA  1 
ATOM   942  C  C   . LYS A 1 129 ? 19.522 25.341 17.554 1.00 41.63 ? 124 LYS A C   1 
ATOM   943  O  O   . LYS A 1 129 ? 18.824 25.815 18.460 1.00 39.59 ? 124 LYS A O   1 
ATOM   944  C  CB  . LYS A 1 129 ? 20.591 26.851 15.867 1.00 38.70 ? 124 LYS A CB  1 
ATOM   945  C  CG  . LYS A 1 129 ? 19.483 27.883 16.031 1.00 44.15 ? 124 LYS A CG  1 
ATOM   946  C  CD  . LYS A 1 129 ? 19.568 28.950 14.922 1.00 45.39 ? 124 LYS A CD  1 
ATOM   947  C  CE  . LYS A 1 129 ? 18.321 29.813 14.874 1.00 46.75 ? 124 LYS A CE  1 
ATOM   948  N  NZ  . LYS A 1 129 ? 18.426 30.813 13.753 1.00 52.99 ? 124 LYS A NZ  1 
ATOM   949  N  N   . GLY A 1 130 ? 19.158 24.246 16.875 1.00 39.13 ? 125 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 130 ? 17.980 23.489 17.287 1.00 41.53 ? 125 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 130 ? 18.077 22.968 18.713 1.00 41.00 ? 125 GLY A C   1 
ATOM   952  O  O   . GLY A 1 130 ? 17.107 23.031 19.472 1.00 42.04 ? 125 GLY A O   1 
ATOM   953  N  N   . ASP A 1 131 ? 19.246 22.440 19.091 1.00 38.49 ? 126 ASP A N   1 
ATOM   954  C  CA  . ASP A 1 131 ? 19.437 21.905 20.443 1.00 40.97 ? 126 ASP A CA  1 
ATOM   955  C  C   . ASP A 1 131 ? 19.207 22.977 21.513 1.00 41.95 ? 126 ASP A C   1 
ATOM   956  O  O   . ASP A 1 131 ? 18.437 22.774 22.455 1.00 42.12 ? 126 ASP A O   1 
ATOM   957  C  CB  . ASP A 1 131 ? 20.841 21.317 20.573 1.00 41.17 ? 126 ASP A CB  1 
ATOM   958  C  CG  . ASP A 1 131 ? 21.008 19.999 19.816 1.00 43.92 ? 126 ASP A CG  1 
ATOM   959  O  OD1 . ASP A 1 131 ? 19.977 19.353 19.509 1.00 39.77 ? 126 ASP A OD1 1 
ATOM   960  O  OD2 . ASP A 1 131 ? 22.172 19.619 19.534 1.00 42.84 ? 126 ASP A OD2 1 
ATOM   961  N  N   . TYR A 1 132 ? 19.848 24.136 21.371 1.00 41.08 ? 127 TYR A N   1 
ATOM   962  C  CA  . TYR A 1 132 ? 19.783 25.121 22.446 1.00 44.16 ? 127 TYR A CA  1 
ATOM   963  C  C   . TYR A 1 132 ? 18.446 25.854 22.492 1.00 43.71 ? 127 TYR A C   1 
ATOM   964  O  O   . TYR A 1 132 ? 18.034 26.280 23.570 1.00 46.89 ? 127 TYR A O   1 
ATOM   965  C  CB  . TYR A 1 132 ? 20.980 26.076 22.344 1.00 40.25 ? 127 TYR A CB  1 
ATOM   966  C  CG  . TYR A 1 132 ? 22.228 25.398 22.885 1.00 40.29 ? 127 TYR A CG  1 
ATOM   967  C  CD1 . TYR A 1 132 ? 23.012 24.591 22.064 1.00 45.63 ? 127 TYR A CD1 1 
ATOM   968  C  CD2 . TYR A 1 132 ? 22.567 25.487 24.236 1.00 40.09 ? 127 TYR A CD2 1 
ATOM   969  C  CE1 . TYR A 1 132 ? 24.122 23.936 22.551 1.00 39.48 ? 127 TYR A CE1 1 
ATOM   970  C  CE2 . TYR A 1 132 ? 23.685 24.840 24.736 1.00 38.91 ? 127 TYR A CE2 1 
ATOM   971  C  CZ  . TYR A 1 132 ? 24.457 24.059 23.886 1.00 40.12 ? 127 TYR A CZ  1 
ATOM   972  O  OH  . TYR A 1 132 ? 25.564 23.403 24.378 1.00 36.74 ? 127 TYR A OH  1 
ATOM   973  N  N   . TYR A 1 133 ? 17.717 25.950 21.377 1.00 41.94 ? 128 TYR A N   1 
ATOM   974  C  CA  . TYR A 1 133 ? 16.310 26.322 21.488 1.00 39.98 ? 128 TYR A CA  1 
ATOM   975  C  C   . TYR A 1 133 ? 15.511 25.231 22.198 1.00 42.56 ? 128 TYR A C   1 
ATOM   976  O  O   . TYR A 1 133 ? 14.608 25.534 22.986 1.00 44.92 ? 128 TYR A O   1 
ATOM   977  C  CB  . TYR A 1 133 ? 15.719 26.620 20.109 1.00 45.25 ? 128 TYR A CB  1 
ATOM   978  C  CG  . TYR A 1 133 ? 15.898 28.060 19.664 1.00 48.37 ? 128 TYR A CG  1 
ATOM   979  C  CD1 . TYR A 1 133 ? 15.325 29.098 20.384 1.00 47.40 ? 128 TYR A CD1 1 
ATOM   980  C  CD2 . TYR A 1 133 ? 16.632 28.377 18.522 1.00 47.97 ? 128 TYR A CD2 1 
ATOM   981  C  CE1 . TYR A 1 133 ? 15.479 30.411 19.991 1.00 52.18 ? 128 TYR A CE1 1 
ATOM   982  C  CE2 . TYR A 1 133 ? 16.800 29.691 18.119 1.00 47.69 ? 128 TYR A CE2 1 
ATOM   983  C  CZ  . TYR A 1 133 ? 16.212 30.709 18.863 1.00 53.04 ? 128 TYR A CZ  1 
ATOM   984  O  OH  . TYR A 1 133 ? 16.360 32.025 18.493 1.00 51.36 ? 128 TYR A OH  1 
ATOM   985  N  N   . ARG A 1 134 ? 15.829 23.952 21.942 1.00 42.93 ? 129 ARG A N   1 
ATOM   986  C  CA  . ARG A 1 134 ? 15.155 22.870 22.660 1.00 43.05 ? 129 ARG A CA  1 
ATOM   987  C  C   . ARG A 1 134 ? 15.424 22.948 24.163 1.00 42.89 ? 129 ARG A C   1 
ATOM   988  O  O   . ARG A 1 134 ? 14.541 22.653 24.978 1.00 44.11 ? 129 ARG A O   1 
ATOM   989  C  CB  . ARG A 1 134 ? 15.592 21.506 22.118 1.00 40.08 ? 129 ARG A CB  1 
ATOM   990  C  CG  . ARG A 1 134 ? 15.150 20.334 23.000 1.00 40.74 ? 129 ARG A CG  1 
ATOM   991  C  CD  . ARG A 1 134 ? 15.079 18.982 22.229 1.00 47.59 ? 129 ARG A CD  1 
ATOM   992  N  NE  . ARG A 1 134 ? 16.377 18.595 21.685 1.00 46.30 ? 129 ARG A NE  1 
ATOM   993  C  CZ  . ARG A 1 134 ? 17.313 17.953 22.373 1.00 45.20 ? 129 ARG A CZ  1 
ATOM   994  N  NH1 . ARG A 1 134 ? 17.090 17.525 23.603 1.00 44.47 ? 129 ARG A NH1 1 
ATOM   995  N  NH2 . ARG A 1 134 ? 18.504 17.741 21.814 1.00 41.84 ? 129 ARG A NH2 1 
ATOM   996  N  N   . TYR A 1 135 ? 16.645 23.312 24.555 1.00 43.50 ? 130 TYR A N   1 
ATOM   997  C  CA  . TYR A 1 135 ? 16.926 23.434 25.986 1.00 43.90 ? 130 TYR A CA  1 
ATOM   998  C  C   . TYR A 1 135 ? 16.135 24.583 26.586 1.00 43.97 ? 130 TYR A C   1 
ATOM   999  O  O   . TYR A 1 135 ? 15.635 24.471 27.709 1.00 47.12 ? 130 TYR A O   1 
ATOM   1000 C  CB  . TYR A 1 135 ? 18.428 23.601 26.237 1.00 40.28 ? 130 TYR A CB  1 
ATOM   1001 C  CG  . TYR A 1 135 ? 19.261 22.455 25.676 1.00 40.07 ? 130 TYR A CG  1 
ATOM   1002 C  CD1 . TYR A 1 135 ? 18.747 21.163 25.615 1.00 39.54 ? 130 TYR A CD1 1 
ATOM   1003 C  CD2 . TYR A 1 135 ? 20.545 22.676 25.185 1.00 36.13 ? 130 TYR A CD2 1 
ATOM   1004 C  CE1 . TYR A 1 135 ? 19.497 20.108 25.066 1.00 41.74 ? 130 TYR A CE1 1 
ATOM   1005 C  CE2 . TYR A 1 135 ? 21.302 21.633 24.649 1.00 40.77 ? 130 TYR A CE2 1 
ATOM   1006 C  CZ  . TYR A 1 135 ? 20.771 20.354 24.594 1.00 43.03 ? 130 TYR A CZ  1 
ATOM   1007 O  OH  . TYR A 1 135 ? 21.536 19.331 24.066 1.00 43.70 ? 130 TYR A OH  1 
ATOM   1008 N  N   . LEU A 1 136 ? 15.980 25.683 25.841 1.00 43.62 ? 131 LEU A N   1 
ATOM   1009 C  CA  . LEU A 1 136 ? 15.122 26.774 26.309 1.00 44.98 ? 131 LEU A CA  1 
ATOM   1010 C  C   . LEU A 1 136 ? 13.673 26.323 26.422 1.00 47.37 ? 131 LEU A C   1 
ATOM   1011 O  O   . LEU A 1 136 ? 12.957 26.737 27.339 1.00 50.19 ? 131 LEU A O   1 
ATOM   1012 C  CB  . LEU A 1 136 ? 15.215 27.977 25.370 1.00 43.81 ? 131 LEU A CB  1 
ATOM   1013 C  CG  . LEU A 1 136 ? 16.495 28.801 25.389 1.00 45.59 ? 131 LEU A CG  1 
ATOM   1014 C  CD1 . LEU A 1 136 ? 16.430 29.885 24.357 1.00 39.77 ? 131 LEU A CD1 1 
ATOM   1015 C  CD2 . LEU A 1 136 ? 16.704 29.394 26.785 1.00 43.28 ? 131 LEU A CD2 1 
ATOM   1016 N  N   . ALA A 1 137 ? 13.226 25.471 25.493 1.00 48.07 ? 132 ALA A N   1 
ATOM   1017 C  CA  . ALA A 1 137 ? 11.843 25.011 25.484 1.00 47.41 ? 132 ALA A CA  1 
ATOM   1018 C  C   . ALA A 1 137 ? 11.542 24.082 26.649 1.00 47.72 ? 132 ALA A C   1 
ATOM   1019 O  O   . ALA A 1 137 ? 10.393 24.006 27.099 1.00 53.03 ? 132 ALA A O   1 
ATOM   1020 C  CB  . ALA A 1 137 ? 11.540 24.299 24.160 1.00 49.20 ? 132 ALA A CB  1 
ATOM   1021 N  N   . GLU A 1 138 ? 12.545 23.353 27.142 1.00 44.38 ? 133 GLU A N   1 
ATOM   1022 C  CA  . GLU A 1 138 ? 12.319 22.517 28.315 1.00 47.76 ? 133 GLU A CA  1 
ATOM   1023 C  C   . GLU A 1 138 ? 11.886 23.340 29.533 1.00 48.89 ? 133 GLU A C   1 
ATOM   1024 O  O   . GLU A 1 138 ? 11.219 22.803 30.424 1.00 52.13 ? 133 GLU A O   1 
ATOM   1025 C  CB  . GLU A 1 138 ? 13.577 21.693 28.634 1.00 45.69 ? 133 GLU A CB  1 
ATOM   1026 C  CG  . GLU A 1 138 ? 14.004 20.719 27.508 1.00 46.08 ? 133 GLU A CG  1 
ATOM   1027 C  CD  . GLU A 1 138 ? 15.280 19.956 27.836 1.00 48.64 ? 133 GLU A CD  1 
ATOM   1028 O  OE1 . GLU A 1 138 ? 16.035 20.406 28.727 1.00 47.91 ? 133 GLU A OE1 1 
ATOM   1029 O  OE2 . GLU A 1 138 ? 15.533 18.899 27.215 1.00 45.28 ? 133 GLU A OE2 1 
ATOM   1030 N  N   . VAL A 1 139 ? 12.233 24.630 29.596 1.00 46.44 ? 134 VAL A N   1 
ATOM   1031 C  CA  . VAL A 1 139 ? 11.897 25.443 30.761 1.00 50.83 ? 134 VAL A CA  1 
ATOM   1032 C  C   . VAL A 1 139 ? 10.952 26.599 30.429 1.00 54.28 ? 134 VAL A C   1 
ATOM   1033 O  O   . VAL A 1 139 ? 10.740 27.480 31.271 1.00 49.06 ? 134 VAL A O   1 
ATOM   1034 C  CB  . VAL A 1 139 ? 13.163 25.973 31.467 1.00 49.03 ? 134 VAL A CB  1 
ATOM   1035 C  CG1 . VAL A 1 139 ? 14.151 24.846 31.742 1.00 43.20 ? 134 VAL A CG1 1 
ATOM   1036 C  CG2 . VAL A 1 139 ? 13.814 27.102 30.659 1.00 46.46 ? 134 VAL A CG2 1 
ATOM   1037 N  N   . ALA A 1 140 ? 10.359 26.616 29.236 1.00 54.17 ? 135 ALA A N   1 
ATOM   1038 C  CA  . ALA A 1 140 ? 9.476  27.717 28.872 1.00 55.76 ? 135 ALA A CA  1 
ATOM   1039 C  C   . ALA A 1 140 ? 8.018  27.373 29.175 1.00 61.11 ? 135 ALA A C   1 
ATOM   1040 O  O   . ALA A 1 140 ? 7.666  26.212 29.409 1.00 65.18 ? 135 ALA A O   1 
ATOM   1041 C  CB  . ALA A 1 140 ? 9.642  28.081 27.395 1.00 57.21 ? 135 ALA A CB  1 
ATOM   1042 N  N   . THR A 1 141 ? 7.165  28.409 29.160 1.00 69.24 ? 136 THR A N   1 
ATOM   1043 C  CA  . THR A 1 141 ? 5.756  28.267 29.535 1.00 70.41 ? 136 THR A CA  1 
ATOM   1044 C  C   . THR A 1 141 ? 4.758  28.862 28.532 1.00 75.17 ? 136 THR A C   1 
ATOM   1045 O  O   . THR A 1 141 ? 3.936  28.128 27.971 1.00 77.47 ? 136 THR A O   1 
ATOM   1046 C  CB  . THR A 1 141 ? 5.518  28.902 30.903 1.00 68.28 ? 136 THR A CB  1 
ATOM   1047 O  OG1 . THR A 1 141 ? 6.347  30.065 31.028 1.00 68.40 ? 136 THR A OG1 1 
ATOM   1048 C  CG2 . THR A 1 141 ? 5.837  27.904 32.014 1.00 61.69 ? 136 THR A CG2 1 
ATOM   1049 N  N   . GLY A 1 142 ? 4.798  30.177 28.303 1.00 70.05 ? 137 GLY A N   1 
ATOM   1050 C  CA  . GLY A 1 142 ? 3.717  30.835 27.579 1.00 74.49 ? 137 GLY A CA  1 
ATOM   1051 C  C   . GLY A 1 142 ? 4.022  31.333 26.177 1.00 74.36 ? 137 GLY A C   1 
ATOM   1052 O  O   . GLY A 1 142 ? 4.479  30.568 25.323 1.00 73.24 ? 137 GLY A O   1 
ATOM   1053 N  N   . ASP A 1 143 ? 3.753  32.620 25.919 1.00 76.22 ? 138 ASP A N   1 
ATOM   1054 C  CA  . ASP A 1 143 ? 4.003  33.186 24.595 1.00 76.06 ? 138 ASP A CA  1 
ATOM   1055 C  C   . ASP A 1 143 ? 5.456  33.028 24.167 1.00 78.42 ? 138 ASP A C   1 
ATOM   1056 O  O   . ASP A 1 143 ? 5.760  33.153 22.973 1.00 78.73 ? 138 ASP A O   1 
ATOM   1057 C  CB  . ASP A 1 143 ? 3.625  34.674 24.547 1.00 79.35 ? 138 ASP A CB  1 
ATOM   1058 C  CG  . ASP A 1 143 ? 2.128  34.903 24.352 1.00 77.72 ? 138 ASP A CG  1 
ATOM   1059 O  OD1 . ASP A 1 143 ? 1.453  34.034 23.748 1.00 73.32 ? 138 ASP A OD1 1 
ATOM   1060 O  OD2 . ASP A 1 143 ? 1.637  35.975 24.785 1.00 76.02 ? 138 ASP A OD2 1 
ATOM   1061 N  N   . ASP A 1 144 ? 6.362  32.776 25.116 1.00 74.85 ? 139 ASP A N   1 
ATOM   1062 C  CA  . ASP A 1 144 ? 7.719  32.389 24.752 1.00 76.02 ? 139 ASP A CA  1 
ATOM   1063 C  C   . ASP A 1 144 ? 7.765  30.939 24.263 1.00 73.30 ? 139 ASP A C   1 
ATOM   1064 O  O   . ASP A 1 144 ? 8.435  30.633 23.269 1.00 73.78 ? 139 ASP A O   1 
ATOM   1065 C  CB  . ASP A 1 144 ? 8.656  32.604 25.947 1.00 74.94 ? 139 ASP A CB  1 
ATOM   1066 C  CG  . ASP A 1 144 ? 9.955  33.290 25.561 1.00 79.32 ? 139 ASP A CG  1 
ATOM   1067 O  OD1 . ASP A 1 144 ? 10.066 33.739 24.392 1.00 79.40 ? 139 ASP A OD1 1 
ATOM   1068 O  OD2 . ASP A 1 144 ? 10.862 33.369 26.426 1.00 74.61 ? 139 ASP A OD2 1 
ATOM   1069 N  N   . LYS A 1 145 ? 7.014  30.048 24.914 1.00 70.90 ? 140 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 145 ? 7.169  28.615 24.686 1.00 67.93 ? 140 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 145 ? 6.744  28.211 23.279 1.00 72.62 ? 140 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 145 ? 7.416  27.400 22.626 1.00 64.96 ? 140 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 145 ? 6.363  27.845 25.723 1.00 69.55 ? 140 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 145 ? 6.379  26.353 25.542 1.00 67.64 ? 140 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 145 ? 5.870  25.665 26.796 1.00 69.41 ? 140 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 145 ? 5.628  24.191 26.557 1.00 66.49 ? 140 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 145 ? 6.830  23.571 25.953 1.00 69.93 ? 140 LYS A NZ  1 
ATOM   1078 N  N   . LYS A 1 146 ? 5.607  28.738 22.811 1.00 75.65 ? 141 LYS A N   1 
ATOM   1079 C  CA  . LYS A 1 146 ? 5.145  28.422 21.462 1.00 73.39 ? 141 LYS A CA  1 
ATOM   1080 C  C   . LYS A 1 146 ? 6.194  28.818 20.433 1.00 69.35 ? 141 LYS A C   1 
ATOM   1081 O  O   . LYS A 1 146 ? 6.533  28.033 19.538 1.00 70.33 ? 141 LYS A O   1 
ATOM   1082 C  CB  . LYS A 1 146 ? 3.816  29.129 21.173 1.00 75.59 ? 141 LYS A CB  1 
ATOM   1083 C  CG  . LYS A 1 146 ? 2.628  28.635 21.993 1.00 81.40 ? 141 LYS A CG  1 
ATOM   1084 C  CD  . LYS A 1 146 ? 1.372  29.461 21.705 1.00 79.77 ? 141 LYS A CD  1 
ATOM   1085 C  CE  . LYS A 1 146 ? 0.163  28.922 22.462 1.00 80.57 ? 141 LYS A CE  1 
ATOM   1086 N  NZ  . LYS A 1 146 ? -0.204 27.536 22.057 1.00 80.09 ? 141 LYS A NZ  1 
ATOM   1087 N  N   . ARG A 1 147 ? 6.743  30.029 20.568 1.00 66.60 ? 142 ARG A N   1 
ATOM   1088 C  CA  . ARG A 1 147 ? 7.676  30.543 19.574 1.00 68.23 ? 142 ARG A CA  1 
ATOM   1089 C  C   . ARG A 1 147 ? 9.055  29.897 19.687 1.00 68.57 ? 142 ARG A C   1 
ATOM   1090 O  O   . ARG A 1 147 ? 9.767  29.787 18.678 1.00 62.80 ? 142 ARG A O   1 
ATOM   1091 C  CB  . ARG A 1 147 ? 7.768  32.065 19.694 1.00 69.93 ? 142 ARG A CB  1 
ATOM   1092 C  CG  . ARG A 1 147 ? 8.902  32.581 20.556 1.00 75.34 ? 142 ARG A CG  1 
ATOM   1093 C  CD  . ARG A 1 147 ? 9.331  33.986 20.125 1.00 77.73 ? 142 ARG A CD  1 
ATOM   1094 N  NE  . ARG A 1 147 ? 8.384  35.042 20.493 1.00 81.14 ? 142 ARG A NE  1 
ATOM   1095 C  CZ  . ARG A 1 147 ? 8.044  35.374 21.736 1.00 80.61 ? 142 ARG A CZ  1 
ATOM   1096 N  NH1 . ARG A 1 147 ? 8.549  34.743 22.786 1.00 79.04 ? 142 ARG A NH1 1 
ATOM   1097 N  NH2 . ARG A 1 147 ? 7.186  36.376 21.931 1.00 70.98 ? 142 ARG A NH2 1 
ATOM   1098 N  N   . ILE A 1 148 ? 9.449  29.461 20.891 1.00 66.80 ? 143 ILE A N   1 
ATOM   1099 C  CA  . ILE A 1 148 ? 10.720 28.756 21.040 1.00 62.67 ? 143 ILE A CA  1 
ATOM   1100 C  C   . ILE A 1 148 ? 10.668 27.411 20.329 1.00 55.63 ? 143 ILE A C   1 
ATOM   1101 O  O   . ILE A 1 148 ? 11.618 27.026 19.643 1.00 55.53 ? 143 ILE A O   1 
ATOM   1102 C  CB  . ILE A 1 148 ? 11.104 28.591 22.527 1.00 57.35 ? 143 ILE A CB  1 
ATOM   1103 C  CG1 . ILE A 1 148 ? 11.671 29.889 23.100 1.00 59.87 ? 143 ILE A CG1 1 
ATOM   1104 C  CG2 . ILE A 1 148 ? 12.120 27.483 22.720 1.00 49.12 ? 143 ILE A CG2 1 
ATOM   1105 C  CD1 . ILE A 1 148 ? 11.148 30.214 24.494 1.00 61.63 ? 143 ILE A CD1 1 
ATOM   1106 N  N   . ILE A 1 149 ? 9.557  26.684 20.472 1.00 56.31 ? 144 ILE A N   1 
ATOM   1107 C  CA  . ILE A 1 149 ? 9.421  25.375 19.838 1.00 58.81 ? 144 ILE A CA  1 
ATOM   1108 C  C   . ILE A 1 149 ? 9.479  25.492 18.318 1.00 60.03 ? 144 ILE A C   1 
ATOM   1109 O  O   . ILE A 1 149 ? 10.059 24.638 17.638 1.00 60.19 ? 144 ILE A O   1 
ATOM   1110 C  CB  . ILE A 1 149 ? 8.127  24.692 20.307 1.00 59.49 ? 144 ILE A CB  1 
ATOM   1111 C  CG1 . ILE A 1 149 ? 8.237  24.373 21.799 1.00 59.38 ? 144 ILE A CG1 1 
ATOM   1112 C  CG2 . ILE A 1 149 ? 7.857  23.445 19.477 1.00 62.33 ? 144 ILE A CG2 1 
ATOM   1113 C  CD1 . ILE A 1 149 ? 6.987  23.835 22.404 1.00 62.37 ? 144 ILE A CD1 1 
ATOM   1114 N  N   . ASP A 1 150 ? 8.893  26.550 17.762 1.00 58.40 ? 145 ASP A N   1 
ATOM   1115 C  CA  . ASP A 1 150 ? 8.951  26.739 16.317 1.00 62.83 ? 145 ASP A CA  1 
ATOM   1116 C  C   . ASP A 1 150 ? 10.371 27.050 15.869 1.00 60.48 ? 145 ASP A C   1 
ATOM   1117 O  O   . ASP A 1 150 ? 10.838 26.519 14.854 1.00 57.57 ? 145 ASP A O   1 
ATOM   1118 C  CB  . ASP A 1 150 ? 7.994  27.853 15.894 1.00 63.60 ? 145 ASP A CB  1 
ATOM   1119 C  CG  . ASP A 1 150 ? 6.542  27.530 16.214 1.00 64.93 ? 145 ASP A CG  1 
ATOM   1120 O  OD1 . ASP A 1 150 ? 5.727  28.476 16.270 1.00 69.47 ? 145 ASP A OD1 1 
ATOM   1121 O  OD2 . ASP A 1 150 ? 6.218  26.338 16.413 1.00 63.99 ? 145 ASP A OD2 1 
ATOM   1122 N  N   . SER A 1 151 ? 11.079 27.897 16.622 1.00 58.40 ? 146 SER A N   1 
ATOM   1123 C  CA  . SER A 1 151 ? 12.469 28.188 16.291 1.00 55.83 ? 146 SER A CA  1 
ATOM   1124 C  C   . SER A 1 151 ? 13.321 26.925 16.332 1.00 55.09 ? 146 SER A C   1 
ATOM   1125 O  O   . SER A 1 151 ? 14.189 26.729 15.471 1.00 58.63 ? 146 SER A O   1 
ATOM   1126 C  CB  . SER A 1 151 ? 13.025 29.248 17.234 1.00 52.92 ? 146 SER A CB  1 
ATOM   1127 O  OG  . SER A 1 151 ? 12.571 30.527 16.859 1.00 57.64 ? 146 SER A OG  1 
ATOM   1128 N  N   . ALA A 1 152 ? 13.077 26.043 17.307 1.00 54.99 ? 147 ALA A N   1 
ATOM   1129 C  CA  . ALA A 1 152 ? 13.795 24.771 17.339 1.00 50.25 ? 147 ALA A CA  1 
ATOM   1130 C  C   . ALA A 1 152 ? 13.453 23.916 16.122 1.00 54.38 ? 147 ALA A C   1 
ATOM   1131 O  O   . ALA A 1 152 ? 14.349 23.447 15.408 1.00 49.69 ? 147 ALA A O   1 
ATOM   1132 C  CB  . ALA A 1 152 ? 13.479 24.007 18.624 1.00 51.45 ? 147 ALA A CB  1 
ATOM   1133 N  N   . ARG A 1 153 ? 12.157 23.677 15.890 1.00 54.94 ? 148 ARG A N   1 
ATOM   1134 C  CA  . ARG A 1 153 ? 11.746 22.851 14.755 1.00 55.04 ? 148 ARG A CA  1 
ATOM   1135 C  C   . ARG A 1 153 ? 12.268 23.421 13.442 1.00 54.28 ? 148 ARG A C   1 
ATOM   1136 O  O   . ARG A 1 153 ? 12.758 22.677 12.586 1.00 54.73 ? 148 ARG A O   1 
ATOM   1137 C  CB  . ARG A 1 153 ? 10.224 22.723 14.722 1.00 54.41 ? 148 ARG A CB  1 
ATOM   1138 C  CG  . ARG A 1 153 ? 9.672  22.163 13.420 1.00 58.50 ? 148 ARG A CG  1 
ATOM   1139 C  CD  . ARG A 1 153 ? 8.155  22.189 13.413 1.00 56.95 ? 148 ARG A CD  1 
ATOM   1140 N  NE  . ARG A 1 153 ? 7.578  21.258 14.378 1.00 52.78 ? 148 ARG A NE  1 
ATOM   1141 C  CZ  . ARG A 1 153 ? 6.826  21.628 15.407 1.00 58.99 ? 148 ARG A CZ  1 
ATOM   1142 N  NH1 . ARG A 1 153 ? 6.584  22.903 15.664 1.00 56.75 ? 148 ARG A NH1 1 
ATOM   1143 N  NH2 . ARG A 1 153 ? 6.305  20.696 16.198 1.00 63.09 ? 148 ARG A NH2 1 
ATOM   1144 N  N   . SER A 1 154 ? 12.202 24.744 13.282 1.00 51.66 ? 149 SER A N   1 
ATOM   1145 C  CA  . SER A 1 154 ? 12.687 25.380 12.062 1.00 54.49 ? 149 SER A CA  1 
ATOM   1146 C  C   . SER A 1 154 ? 14.169 25.090 11.830 1.00 56.57 ? 149 SER A C   1 
ATOM   1147 O  O   . SER A 1 154 ? 14.574 24.700 10.725 1.00 52.48 ? 149 SER A O   1 
ATOM   1148 C  CB  . SER A 1 154 ? 12.427 26.888 12.129 1.00 56.78 ? 149 SER A CB  1 
ATOM   1149 O  OG  . SER A 1 154 ? 13.086 27.570 11.079 1.00 63.99 ? 149 SER A OG  1 
ATOM   1150 N  N   . ALA A 1 155 ? 14.994 25.254 12.873 1.00 54.44 ? 150 ALA A N   1 
ATOM   1151 C  CA  . ALA A 1 155 ? 16.437 25.056 12.728 1.00 49.94 ? 150 ALA A CA  1 
ATOM   1152 C  C   . ALA A 1 155 ? 16.773 23.599 12.438 1.00 46.67 ? 150 ALA A C   1 
ATOM   1153 O  O   . ALA A 1 155 ? 17.648 23.311 11.609 1.00 43.84 ? 150 ALA A O   1 
ATOM   1154 C  CB  . ALA A 1 155 ? 17.162 25.526 13.993 1.00 45.82 ? 150 ALA A CB  1 
ATOM   1155 N  N   . TYR A 1 156 ? 16.111 22.670 13.140 1.00 46.16 ? 151 TYR A N   1 
ATOM   1156 C  CA  . TYR A 1 156 ? 16.302 21.247 12.882 1.00 46.54 ? 151 TYR A CA  1 
ATOM   1157 C  C   . TYR A 1 156 ? 15.914 20.886 11.452 1.00 49.23 ? 151 TYR A C   1 
ATOM   1158 O  O   . TYR A 1 156 ? 16.612 20.112 10.782 1.00 46.25 ? 151 TYR A O   1 
ATOM   1159 C  CB  . TYR A 1 156 ? 15.464 20.427 13.861 1.00 47.00 ? 151 TYR A CB  1 
ATOM   1160 C  CG  . TYR A 1 156 ? 16.047 20.254 15.265 1.00 46.36 ? 151 TYR A CG  1 
ATOM   1161 C  CD1 . TYR A 1 156 ? 17.386 19.938 15.455 1.00 45.44 ? 151 TYR A CD1 1 
ATOM   1162 C  CD2 . TYR A 1 156 ? 15.238 20.368 16.390 1.00 45.89 ? 151 TYR A CD2 1 
ATOM   1163 C  CE1 . TYR A 1 156 ? 17.911 19.738 16.748 1.00 45.15 ? 151 TYR A CE1 1 
ATOM   1164 C  CE2 . TYR A 1 156 ? 15.759 20.192 17.679 1.00 47.17 ? 151 TYR A CE2 1 
ATOM   1165 C  CZ  . TYR A 1 156 ? 17.095 19.881 17.847 1.00 43.77 ? 151 TYR A CZ  1 
ATOM   1166 O  OH  . TYR A 1 156 ? 17.610 19.687 19.119 1.00 47.02 ? 151 TYR A OH  1 
ATOM   1167 N  N   . GLN A 1 157 ? 14.777 21.405 10.983 1.00 49.34 ? 152 GLN A N   1 
ATOM   1168 C  CA  . GLN A 1 157 ? 14.298 21.033 9.653  1.00 52.39 ? 152 GLN A CA  1 
ATOM   1169 C  C   . GLN A 1 157 ? 15.251 21.510 8.566  1.00 48.54 ? 152 GLN A C   1 
ATOM   1170 O  O   . GLN A 1 157 ? 15.556 20.759 7.628  1.00 52.63 ? 152 GLN A O   1 
ATOM   1171 C  CB  . GLN A 1 157 ? 12.892 21.582 9.423  1.00 55.04 ? 152 GLN A CB  1 
ATOM   1172 C  CG  . GLN A 1 157 ? 12.130 20.929 8.238  1.00 56.80 ? 152 GLN A CG  1 
ATOM   1173 C  CD  . GLN A 1 157 ? 11.936 19.428 8.387  1.00 56.33 ? 152 GLN A CD  1 
ATOM   1174 O  OE1 . GLN A 1 157 ? 10.969 18.975 9.003  1.00 59.03 ? 152 GLN A OE1 1 
ATOM   1175 N  NE2 . GLN A 1 157 ? 12.823 18.649 7.770  1.00 56.86 ? 152 GLN A NE2 1 
ATOM   1176 N  N   . GLU A 1 158 ? 15.750 22.742 8.670  1.00 44.73 ? 153 GLU A N   1 
ATOM   1177 C  CA  . GLU A 1 158 ? 16.713 23.184 7.666  1.00 51.24 ? 153 GLU A CA  1 
ATOM   1178 C  C   . GLU A 1 158 ? 17.962 22.314 7.704  1.00 51.69 ? 153 GLU A C   1 
ATOM   1179 O  O   . GLU A 1 158 ? 18.517 21.964 6.654  1.00 46.32 ? 153 GLU A O   1 
ATOM   1180 C  CB  . GLU A 1 158 ? 17.084 24.655 7.846  1.00 47.40 ? 153 GLU A CB  1 
ATOM   1181 C  CG  . GLU A 1 158 ? 17.911 25.150 6.657  1.00 53.85 ? 153 GLU A CG  1 
ATOM   1182 C  CD  . GLU A 1 158 ? 18.446 26.548 6.832  1.00 54.14 ? 153 GLU A CD  1 
ATOM   1183 O  OE1 . GLU A 1 158 ? 17.950 27.257 7.727  1.00 59.27 ? 153 GLU A OE1 1 
ATOM   1184 O  OE2 . GLU A 1 158 ? 19.362 26.935 6.067  1.00 56.59 ? 153 GLU A OE2 1 
ATOM   1185 N  N   . ALA A 1 159 ? 18.400 21.933 8.911  1.00 46.41 ? 154 ALA A N   1 
ATOM   1186 C  CA  . ALA A 1 159 ? 19.546 21.041 9.035  1.00 45.83 ? 154 ALA A CA  1 
ATOM   1187 C  C   . ALA A 1 159 ? 19.257 19.689 8.395  1.00 40.66 ? 154 ALA A C   1 
ATOM   1188 O  O   . ALA A 1 159 ? 20.125 19.110 7.740  1.00 43.04 ? 154 ALA A O   1 
ATOM   1189 C  CB  . ALA A 1 159 ? 19.927 20.878 10.511 1.00 41.73 ? 154 ALA A CB  1 
ATOM   1190 N  N   . MET A 1 160 ? 18.037 19.176 8.572  1.00 41.95 ? 155 MET A N   1 
ATOM   1191 C  CA  . MET A 1 160 ? 17.678 17.878 8.001  1.00 42.41 ? 155 MET A CA  1 
ATOM   1192 C  C   . MET A 1 160 ? 17.703 17.923 6.476  1.00 46.03 ? 155 MET A C   1 
ATOM   1193 O  O   . MET A 1 160 ? 18.250 17.023 5.825  1.00 45.87 ? 155 MET A O   1 
ATOM   1194 C  CB  . MET A 1 160 ? 16.291 17.463 8.484  1.00 42.44 ? 155 MET A CB  1 
ATOM   1195 C  CG  . MET A 1 160 ? 16.197 17.027 9.942  1.00 48.56 ? 155 MET A CG  1 
ATOM   1196 S  SD  . MET A 1 160 ? 16.968 15.432 10.280 1.00 52.10 ? 155 MET A SD  1 
ATOM   1197 C  CE  . MET A 1 160 ? 15.607 14.350 9.897  1.00 52.83 ? 155 MET A CE  1 
ATOM   1198 N  N   . ASP A 1 161 ? 17.133 18.982 5.894  1.00 48.26 ? 156 ASP A N   1 
ATOM   1199 C  CA  . ASP A 1 161 ? 17.084 19.102 4.437  1.00 48.42 ? 156 ASP A CA  1 
ATOM   1200 C  C   . ASP A 1 161 ? 18.486 19.075 3.840  1.00 48.35 ? 156 ASP A C   1 
ATOM   1201 O  O   . ASP A 1 161 ? 18.761 18.315 2.902  1.00 51.38 ? 156 ASP A O   1 
ATOM   1202 C  CB  . ASP A 1 161 ? 16.349 20.388 4.057  1.00 52.03 ? 156 ASP A CB  1 
ATOM   1203 C  CG  . ASP A 1 161 ? 14.873 20.348 4.426  1.00 52.20 ? 156 ASP A CG  1 
ATOM   1204 O  OD1 . ASP A 1 161 ? 14.229 21.418 4.435  1.00 54.36 ? 156 ASP A OD1 1 
ATOM   1205 O  OD2 . ASP A 1 161 ? 14.356 19.247 4.711  1.00 54.73 ? 156 ASP A OD2 1 
ATOM   1206 N  N   . ILE A 1 162 ? 19.392 19.894 4.386  1.00 46.19 ? 157 ILE A N   1 
ATOM   1207 C  CA  . ILE A 1 162 ? 20.776 19.924 3.915  1.00 44.57 ? 157 ILE A CA  1 
ATOM   1208 C  C   . ILE A 1 162 ? 21.438 18.561 4.083  1.00 48.04 ? 157 ILE A C   1 
ATOM   1209 O  O   . ILE A 1 162 ? 22.133 18.077 3.180  1.00 46.33 ? 157 ILE A O   1 
ATOM   1210 C  CB  . ILE A 1 162 ? 21.570 21.017 4.654  1.00 46.09 ? 157 ILE A CB  1 
ATOM   1211 C  CG1 . ILE A 1 162 ? 20.928 22.397 4.476  1.00 50.48 ? 157 ILE A CG1 1 
ATOM   1212 C  CG2 . ILE A 1 162 ? 23.015 21.023 4.185  1.00 48.79 ? 157 ILE A CG2 1 
ATOM   1213 C  CD1 . ILE A 1 162 ? 21.681 23.505 5.224  1.00 47.03 ? 157 ILE A CD1 1 
ATOM   1214 N  N   . SER A 1 163 ? 21.245 17.922 5.245  1.00 43.90 ? 158 SER A N   1 
ATOM   1215 C  CA  . SER A 1 163 ? 21.977 16.695 5.537  1.00 44.75 ? 158 SER A CA  1 
ATOM   1216 C  C   . SER A 1 163 ? 21.576 15.558 4.598  1.00 45.13 ? 158 SER A C   1 
ATOM   1217 O  O   . SER A 1 163 ? 22.425 14.768 4.180  1.00 46.71 ? 158 SER A O   1 
ATOM   1218 C  CB  . SER A 1 163 ? 21.751 16.273 6.994  1.00 44.36 ? 158 SER A CB  1 
ATOM   1219 O  OG  . SER A 1 163 ? 20.407 15.878 7.217  1.00 48.25 ? 158 SER A OG  1 
ATOM   1220 N  N   . LYS A 1 164 ? 20.283 15.434 4.290  1.00 44.99 ? 159 LYS A N   1 
ATOM   1221 C  CA  . LYS A 1 164 ? 19.847 14.407 3.345  1.00 47.68 ? 159 LYS A CA  1 
ATOM   1222 C  C   . LYS A 1 164 ? 20.388 14.658 1.942  1.00 46.80 ? 159 LYS A C   1 
ATOM   1223 O  O   . LYS A 1 164 ? 20.672 13.704 1.211  1.00 50.53 ? 159 LYS A O   1 
ATOM   1224 C  CB  . LYS A 1 164 ? 18.324 14.337 3.300  1.00 51.83 ? 159 LYS A CB  1 
ATOM   1225 C  CG  . LYS A 1 164 ? 17.661 14.077 4.634  1.00 52.29 ? 159 LYS A CG  1 
ATOM   1226 C  CD  . LYS A 1 164 ? 16.175 13.852 4.409  1.00 59.28 ? 159 LYS A CD  1 
ATOM   1227 C  CE  . LYS A 1 164 ? 15.470 13.381 5.660  1.00 56.37 ? 159 LYS A CE  1 
ATOM   1228 N  NZ  . LYS A 1 164 ? 14.375 12.436 5.289  1.00 62.75 ? 159 LYS A NZ  1 
ATOM   1229 N  N   . LYS A 1 165 ? 20.550 15.924 1.557  1.00 47.35 ? 160 LYS A N   1 
ATOM   1230 C  CA  . LYS A 1 165 ? 21.069 16.228 0.233  1.00 53.06 ? 160 LYS A CA  1 
ATOM   1231 C  C   . LYS A 1 165 ? 22.588 16.111 0.155  1.00 52.89 ? 160 LYS A C   1 
ATOM   1232 O  O   . LYS A 1 165 ? 23.112 15.713 -0.890 1.00 49.95 ? 160 LYS A O   1 
ATOM   1233 C  CB  . LYS A 1 165 ? 20.610 17.627 -0.200 1.00 53.41 ? 160 LYS A CB  1 
ATOM   1234 C  CG  . LYS A 1 165 ? 19.110 17.701 -0.498 1.00 57.18 ? 160 LYS A CG  1 
ATOM   1235 C  CD  . LYS A 1 165 ? 18.578 19.130 -0.527 1.00 64.07 ? 160 LYS A CD  1 
ATOM   1236 C  CE  . LYS A 1 165 ? 17.285 19.258 0.301  1.00 64.51 ? 160 LYS A CE  1 
ATOM   1237 N  NZ  . LYS A 1 165 ? 16.408 20.379 -0.172 1.00 71.23 ? 160 LYS A NZ  1 
ATOM   1238 N  N   . GLU A 1 166 ? 23.320 16.419 1.226  1.00 44.57 ? 161 GLU A N   1 
ATOM   1239 C  CA  . GLU A 1 166 ? 24.770 16.518 1.122  1.00 44.57 ? 161 GLU A CA  1 
ATOM   1240 C  C   . GLU A 1 166 ? 25.565 15.474 1.895  1.00 46.57 ? 161 GLU A C   1 
ATOM   1241 O  O   . GLU A 1 166 ? 26.791 15.418 1.731  1.00 47.68 ? 161 GLU A O   1 
ATOM   1242 C  CB  . GLU A 1 166 ? 25.238 17.901 1.579  1.00 52.44 ? 161 GLU A CB  1 
ATOM   1243 C  CG  . GLU A 1 166 ? 24.327 19.035 1.208  1.00 56.08 ? 161 GLU A CG  1 
ATOM   1244 C  CD  . GLU A 1 166 ? 24.900 19.839 0.078  1.00 65.09 ? 161 GLU A CD  1 
ATOM   1245 O  OE1 . GLU A 1 166 ? 25.904 19.378 -0.516 1.00 63.55 ? 161 GLU A OE1 1 
ATOM   1246 O  OE2 . GLU A 1 166 ? 24.365 20.933 -0.205 1.00 74.42 ? 161 GLU A OE2 1 
ATOM   1247 N  N   . MET A 1 167 ? 24.937 14.659 2.730  1.00 41.43 ? 162 MET A N   1 
ATOM   1248 C  CA  . MET A 1 167 ? 25.763 13.763 3.521  1.00 43.52 ? 162 MET A CA  1 
ATOM   1249 C  C   . MET A 1 167 ? 25.255 12.334 3.433  1.00 40.83 ? 162 MET A C   1 
ATOM   1250 O  O   . MET A 1 167 ? 24.048 12.099 3.288  1.00 39.68 ? 162 MET A O   1 
ATOM   1251 C  CB  . MET A 1 167 ? 25.798 14.228 4.991  1.00 41.64 ? 162 MET A CB  1 
ATOM   1252 C  CG  . MET A 1 167 ? 26.661 15.505 5.145  1.00 47.83 ? 162 MET A CG  1 
ATOM   1253 S  SD  . MET A 1 167 ? 26.297 16.540 6.577  1.00 57.22 ? 162 MET A SD  1 
ATOM   1254 C  CE  . MET A 1 167 ? 25.185 15.477 7.416  1.00 42.30 ? 162 MET A CE  1 
ATOM   1255 N  N   . PRO A 1 168 ? 26.155 11.362 3.526  1.00 41.34 ? 163 PRO A N   1 
ATOM   1256 C  CA  . PRO A 1 168 ? 25.734 9.971  3.530  1.00 46.26 ? 163 PRO A CA  1 
ATOM   1257 C  C   . PRO A 1 168 ? 24.883 9.682  4.750  1.00 43.57 ? 163 PRO A C   1 
ATOM   1258 O  O   . PRO A 1 168 ? 24.949 10.407 5.755  1.00 42.46 ? 163 PRO A O   1 
ATOM   1259 C  CB  . PRO A 1 168 ? 27.060 9.196  3.565  1.00 44.90 ? 163 PRO A CB  1 
ATOM   1260 C  CG  . PRO A 1 168 ? 28.043 10.167 4.098  1.00 43.52 ? 163 PRO A CG  1 
ATOM   1261 C  CD  . PRO A 1 168 ? 27.617 11.492 3.593  1.00 43.05 ? 163 PRO A CD  1 
ATOM   1262 N  N   . PRO A 1 169 ? 24.057 8.640  4.689  1.00 45.38 ? 164 PRO A N   1 
ATOM   1263 C  CA  . PRO A 1 169 ? 23.162 8.340  5.811  1.00 44.04 ? 164 PRO A CA  1 
ATOM   1264 C  C   . PRO A 1 169 ? 23.870 7.832  7.069  1.00 41.10 ? 164 PRO A C   1 
ATOM   1265 O  O   . PRO A 1 169 ? 23.194 7.694  8.090  1.00 42.65 ? 164 PRO A O   1 
ATOM   1266 C  CB  . PRO A 1 169 ? 22.220 7.265  5.239  1.00 41.99 ? 164 PRO A CB  1 
ATOM   1267 C  CG  . PRO A 1 169 ? 22.586 7.099  3.775  1.00 46.78 ? 164 PRO A CG  1 
ATOM   1268 C  CD  . PRO A 1 169 ? 23.930 7.683  3.568  1.00 44.52 ? 164 PRO A CD  1 
ATOM   1269 N  N   . THR A 1 170 ? 25.171 7.526  7.040  1.00 39.78 ? 165 THR A N   1 
ATOM   1270 C  CA  . THR A 1 170 ? 25.888 7.158  8.261  1.00 40.58 ? 165 THR A CA  1 
ATOM   1271 C  C   . THR A 1 170 ? 26.677 8.317  8.858  1.00 37.01 ? 165 THR A C   1 
ATOM   1272 O  O   . THR A 1 170 ? 27.332 8.127  9.885  1.00 37.43 ? 165 THR A O   1 
ATOM   1273 C  CB  . THR A 1 170 ? 26.879 6.028  8.008  1.00 35.36 ? 165 THR A CB  1 
ATOM   1274 O  OG1 . THR A 1 170 ? 27.754 6.439  6.961  1.00 35.75 ? 165 THR A OG1 1 
ATOM   1275 C  CG2 . THR A 1 170 ? 26.188 4.687  7.658  1.00 36.88 ? 165 THR A CG2 1 
ATOM   1276 N  N   . ASN A 1 171 ? 26.685 9.481  8.212  1.00 36.03 ? 166 ASN A N   1 
ATOM   1277 C  CA  . ASN A 1 171 ? 27.474 10.612 8.704  1.00 36.93 ? 166 ASN A CA  1 
ATOM   1278 C  C   . ASN A 1 171 ? 27.066 10.958 10.138 1.00 35.78 ? 166 ASN A C   1 
ATOM   1279 O  O   . ASN A 1 171 ? 25.867 11.089 10.419 1.00 36.33 ? 166 ASN A O   1 
ATOM   1280 C  CB  . ASN A 1 171 ? 27.301 11.835 7.799  1.00 35.82 ? 166 ASN A CB  1 
ATOM   1281 C  CG  . ASN A 1 171 ? 28.036 13.073 8.336  1.00 37.04 ? 166 ASN A CG  1 
ATOM   1282 O  OD1 . ASN A 1 171 ? 27.531 13.774 9.220  1.00 40.12 ? 166 ASN A OD1 1 
ATOM   1283 N  ND2 . ASN A 1 171 ? 29.224 13.340 7.805  1.00 37.85 ? 166 ASN A ND2 1 
ATOM   1284 N  N   . PRO A 1 172 ? 28.026 11.134 11.052 1.00 36.78 ? 167 PRO A N   1 
ATOM   1285 C  CA  . PRO A 1 172 ? 27.666 11.311 12.481 1.00 35.65 ? 167 PRO A CA  1 
ATOM   1286 C  C   . PRO A 1 172 ? 26.885 12.586 12.774 1.00 35.35 ? 167 PRO A C   1 
ATOM   1287 O  O   . PRO A 1 172 ? 25.996 12.569 13.637 1.00 35.28 ? 167 PRO A O   1 
ATOM   1288 C  CB  . PRO A 1 172 ? 29.028 11.310 13.194 1.00 43.94 ? 167 PRO A CB  1 
ATOM   1289 C  CG  . PRO A 1 172 ? 30.041 10.919 12.182 1.00 44.98 ? 167 PRO A CG  1 
ATOM   1290 C  CD  . PRO A 1 172 ? 29.478 11.172 10.822 1.00 38.70 ? 167 PRO A CD  1 
ATOM   1291 N  N   . ILE A 1 173 ? 27.179 13.690 12.078 1.00 34.38 ? 168 ILE A N   1 
ATOM   1292 C  CA  . ILE A 1 173 ? 26.364 14.898 12.236 1.00 36.46 ? 168 ILE A CA  1 
ATOM   1293 C  C   . ILE A 1 173 ? 24.940 14.622 11.776 1.00 35.37 ? 168 ILE A C   1 
ATOM   1294 O  O   . ILE A 1 173 ? 23.968 14.974 12.450 1.00 37.48 ? 168 ILE A O   1 
ATOM   1295 C  CB  . ILE A 1 173 ? 26.990 16.082 11.464 1.00 36.28 ? 168 ILE A CB  1 
ATOM   1296 C  CG1 . ILE A 1 173 ? 28.425 16.342 11.920 1.00 34.73 ? 168 ILE A CG1 1 
ATOM   1297 C  CG2 . ILE A 1 173 ? 26.134 17.362 11.597 1.00 41.34 ? 168 ILE A CG2 1 
ATOM   1298 C  CD1 . ILE A 1 173 ? 29.236 17.168 10.942 1.00 43.93 ? 168 ILE A CD1 1 
ATOM   1299 N  N   . ARG A 1 174 ? 24.797 13.970 10.615 1.00 38.40 ? 169 ARG A N   1 
ATOM   1300 C  CA  . ARG A 1 174 ? 23.470 13.598 10.136 1.00 38.14 ? 169 ARG A CA  1 
ATOM   1301 C  C   . ARG A 1 174 ? 22.738 12.747 11.154 1.00 34.03 ? 169 ARG A C   1 
ATOM   1302 O  O   . ARG A 1 174 ? 21.576 13.005 11.471 1.00 36.66 ? 169 ARG A O   1 
ATOM   1303 C  CB  . ARG A 1 174 ? 23.565 12.833 8.812  1.00 37.31 ? 169 ARG A CB  1 
ATOM   1304 C  CG  . ARG A 1 174 ? 22.235 12.705 8.135  1.00 41.24 ? 169 ARG A CG  1 
ATOM   1305 C  CD  . ARG A 1 174 ? 22.361 12.186 6.695  1.00 39.58 ? 169 ARG A CD  1 
ATOM   1306 N  NE  . ARG A 1 174 ? 21.111 11.553 6.300  1.00 42.76 ? 169 ARG A NE  1 
ATOM   1307 C  CZ  . ARG A 1 174 ? 20.841 11.140 5.068  1.00 46.41 ? 169 ARG A CZ  1 
ATOM   1308 N  NH1 . ARG A 1 174 ? 21.736 11.230 4.101  1.00 41.00 ? 169 ARG A NH1 1 
ATOM   1309 N  NH2 . ARG A 1 174 ? 19.648 10.616 4.805  1.00 42.77 ? 169 ARG A NH2 1 
ATOM   1310 N  N   . LEU A 1 175 ? 23.394 11.695 11.639 1.00 33.57 ? 170 LEU A N   1 
ATOM   1311 C  CA  . LEU A 1 175 ? 22.772 10.811 12.622 1.00 37.07 ? 170 LEU A CA  1 
ATOM   1312 C  C   . LEU A 1 175 ? 22.450 11.559 13.916 1.00 39.13 ? 170 LEU A C   1 
ATOM   1313 O  O   . LEU A 1 175 ? 21.338 11.448 14.456 1.00 37.39 ? 170 LEU A O   1 
ATOM   1314 C  CB  . LEU A 1 175 ? 23.700 9.636  12.903 1.00 34.72 ? 170 LEU A CB  1 
ATOM   1315 C  CG  . LEU A 1 175 ? 23.918 8.675  11.721 1.00 38.32 ? 170 LEU A CG  1 
ATOM   1316 C  CD1 . LEU A 1 175 ? 25.031 7.685  12.036 1.00 34.18 ? 170 LEU A CD1 1 
ATOM   1317 C  CD2 . LEU A 1 175 ? 22.628 7.961  11.360 1.00 38.27 ? 170 LEU A CD2 1 
ATOM   1318 N  N   . GLY A 1 176 ? 23.425 12.315 14.436 1.00 36.48 ? 171 GLY A N   1 
ATOM   1319 C  CA  . GLY A 1 176 ? 23.213 12.986 15.713 1.00 37.50 ? 171 GLY A CA  1 
ATOM   1320 C  C   . GLY A 1 176 ? 22.101 14.005 15.615 1.00 36.96 ? 171 GLY A C   1 
ATOM   1321 O  O   . GLY A 1 176 ? 21.245 14.090 16.497 1.00 37.89 ? 171 GLY A O   1 
ATOM   1322 N  N   . LEU A 1 177 ? 22.063 14.743 14.499 1.00 38.25 ? 172 LEU A N   1 
ATOM   1323 C  CA  . LEU A 1 177 ? 20.960 15.658 14.236 1.00 36.88 ? 172 LEU A CA  1 
ATOM   1324 C  C   . LEU A 1 177 ? 19.626 14.924 14.240 1.00 38.08 ? 172 LEU A C   1 
ATOM   1325 O  O   . LEU A 1 177 ? 18.674 15.354 14.899 1.00 40.05 ? 172 LEU A O   1 
ATOM   1326 C  CB  . LEU A 1 177 ? 21.186 16.374 12.900 1.00 37.29 ? 172 LEU A CB  1 
ATOM   1327 C  CG  . LEU A 1 177 ? 19.936 16.911 12.200 1.00 37.60 ? 172 LEU A CG  1 
ATOM   1328 C  CD1 . LEU A 1 177 ? 19.366 18.111 12.976 1.00 45.03 ? 172 LEU A CD1 1 
ATOM   1329 C  CD2 . LEU A 1 177 ? 20.260 17.334 10.761 1.00 41.45 ? 172 LEU A CD2 1 
ATOM   1330 N  N   . ALA A 1 178 ? 19.534 13.812 13.493 1.00 41.24 ? 173 ALA A N   1 
ATOM   1331 C  CA  . ALA A 1 178 ? 18.273 13.080 13.410 1.00 40.13 ? 173 ALA A CA  1 
ATOM   1332 C  C   . ALA A 1 178 ? 17.874 12.507 14.766 1.00 40.09 ? 173 ALA A C   1 
ATOM   1333 O  O   . ALA A 1 178 ? 16.692 12.512 15.127 1.00 41.90 ? 173 ALA A O   1 
ATOM   1334 C  CB  . ALA A 1 178 ? 18.377 11.959 12.377 1.00 40.82 ? 173 ALA A CB  1 
ATOM   1335 N  N   . LEU A 1 179 ? 18.842 11.982 15.517 1.00 39.02 ? 174 LEU A N   1 
ATOM   1336 C  CA  . LEU A 1 179 ? 18.563 11.570 16.894 1.00 38.57 ? 174 LEU A CA  1 
ATOM   1337 C  C   . LEU A 1 179 ? 17.997 12.728 17.711 1.00 38.00 ? 174 LEU A C   1 
ATOM   1338 O  O   . LEU A 1 179 ? 16.996 12.565 18.419 1.00 42.42 ? 174 LEU A O   1 
ATOM   1339 C  CB  . LEU A 1 179 ? 19.829 11.011 17.550 1.00 38.20 ? 174 LEU A CB  1 
ATOM   1340 C  CG  . LEU A 1 179 ? 19.777 10.626 19.040 1.00 40.81 ? 174 LEU A CG  1 
ATOM   1341 C  CD1 . LEU A 1 179 ? 18.922 9.396  19.262 1.00 37.39 ? 174 LEU A CD1 1 
ATOM   1342 C  CD2 . LEU A 1 179 ? 21.173 10.386 19.543 1.00 39.20 ? 174 LEU A CD2 1 
ATOM   1343 N  N   . ASN A 1 180 ? 18.602 13.920 17.616 1.00 39.12 ? 175 ASN A N   1 
ATOM   1344 C  CA  . ASN A 1 180 ? 18.119 15.010 18.464 1.00 40.44 ? 175 ASN A CA  1 
ATOM   1345 C  C   . ASN A 1 180 ? 16.792 15.587 17.984 1.00 45.12 ? 175 ASN A C   1 
ATOM   1346 O  O   . ASN A 1 180 ? 15.970 16.005 18.811 1.00 44.37 ? 175 ASN A O   1 
ATOM   1347 C  CB  . ASN A 1 180 ? 19.161 16.126 18.571 1.00 40.44 ? 175 ASN A CB  1 
ATOM   1348 C  CG  . ASN A 1 180 ? 20.340 15.733 19.428 1.00 40.37 ? 175 ASN A CG  1 
ATOM   1349 O  OD1 . ASN A 1 180 ? 20.467 14.569 19.837 1.00 40.97 ? 175 ASN A OD1 1 
ATOM   1350 N  ND2 . ASN A 1 180 ? 21.220 16.682 19.692 1.00 37.22 ? 175 ASN A ND2 1 
ATOM   1351 N  N   . PHE A 1 181 ? 16.562 15.638 16.665 1.00 46.69 ? 176 PHE A N   1 
ATOM   1352 C  CA  . PHE A 1 181 ? 15.254 16.050 16.157 1.00 44.58 ? 176 PHE A CA  1 
ATOM   1353 C  C   . PHE A 1 181 ? 14.158 15.126 16.666 1.00 45.22 ? 176 PHE A C   1 
ATOM   1354 O  O   . PHE A 1 181 ? 13.047 15.574 16.975 1.00 48.81 ? 176 PHE A O   1 
ATOM   1355 C  CB  . PHE A 1 181 ? 15.258 16.049 14.625 1.00 46.42 ? 176 PHE A CB  1 
ATOM   1356 C  CG  . PHE A 1 181 ? 14.202 16.926 14.004 1.00 49.85 ? 176 PHE A CG  1 
ATOM   1357 C  CD1 . PHE A 1 181 ? 13.467 17.818 14.776 1.00 52.34 ? 176 PHE A CD1 1 
ATOM   1358 C  CD2 . PHE A 1 181 ? 13.927 16.843 12.640 1.00 51.11 ? 176 PHE A CD2 1 
ATOM   1359 C  CE1 . PHE A 1 181 ? 12.494 18.636 14.197 1.00 52.20 ? 176 PHE A CE1 1 
ATOM   1360 C  CE2 . PHE A 1 181 ? 12.951 17.648 12.055 1.00 51.86 ? 176 PHE A CE2 1 
ATOM   1361 C  CZ  . PHE A 1 181 ? 12.237 18.543 12.833 1.00 52.56 ? 176 PHE A CZ  1 
ATOM   1362 N  N   . SER A 1 182 ? 14.447 13.829 16.752 1.00 45.21 ? 177 SER A N   1 
ATOM   1363 C  CA  . SER A 1 182 ? 13.412 12.886 17.164 1.00 47.61 ? 177 SER A CA  1 
ATOM   1364 C  C   . SER A 1 182 ? 13.113 13.021 18.654 1.00 49.87 ? 177 SER A C   1 
ATOM   1365 O  O   . SER A 1 182 ? 11.956 12.911 19.074 1.00 51.65 ? 177 SER A O   1 
ATOM   1366 C  CB  . SER A 1 182 ? 13.822 11.459 16.800 1.00 48.67 ? 177 SER A CB  1 
ATOM   1367 O  OG  . SER A 1 182 ? 14.589 10.824 17.810 1.00 49.85 ? 177 SER A OG  1 
ATOM   1368 N  N   . VAL A 1 183 ? 14.142 13.258 19.470 1.00 51.76 ? 178 VAL A N   1 
ATOM   1369 C  CA  . VAL A 1 183 ? 13.916 13.550 20.888 1.00 45.18 ? 178 VAL A CA  1 
ATOM   1370 C  C   . VAL A 1 183 ? 13.082 14.820 21.034 1.00 47.29 ? 178 VAL A C   1 
ATOM   1371 O  O   . VAL A 1 183 ? 12.191 14.906 21.888 1.00 52.98 ? 178 VAL A O   1 
ATOM   1372 C  CB  . VAL A 1 183 ? 15.263 13.647 21.629 1.00 43.80 ? 178 VAL A CB  1 
ATOM   1373 C  CG1 . VAL A 1 183 ? 15.051 14.125 23.062 1.00 50.42 ? 178 VAL A CG1 1 
ATOM   1374 C  CG2 . VAL A 1 183 ? 15.982 12.311 21.636 1.00 43.87 ? 178 VAL A CG2 1 
ATOM   1375 N  N   . PHE A 1 184 ? 13.342 15.818 20.189 1.00 48.46 ? 179 PHE A N   1 
ATOM   1376 C  CA  . PHE A 1 184 ? 12.474 16.991 20.125 1.00 49.89 ? 179 PHE A CA  1 
ATOM   1377 C  C   . PHE A 1 184 ? 11.024 16.590 19.872 1.00 53.82 ? 179 PHE A C   1 
ATOM   1378 O  O   . PHE A 1 184 ? 10.111 17.055 20.565 1.00 53.60 ? 179 PHE A O   1 
ATOM   1379 C  CB  . PHE A 1 184 ? 12.974 17.952 19.043 1.00 47.22 ? 179 PHE A CB  1 
ATOM   1380 C  CG  . PHE A 1 184 ? 12.021 19.064 18.722 1.00 51.39 ? 179 PHE A CG  1 
ATOM   1381 C  CD1 . PHE A 1 184 ? 12.035 20.237 19.450 1.00 49.67 ? 179 PHE A CD1 1 
ATOM   1382 C  CD2 . PHE A 1 184 ? 11.120 18.948 17.673 1.00 49.23 ? 179 PHE A CD2 1 
ATOM   1383 C  CE1 . PHE A 1 184 ? 11.164 21.280 19.141 1.00 52.01 ? 179 PHE A CE1 1 
ATOM   1384 C  CE2 . PHE A 1 184 ? 10.246 19.979 17.368 1.00 53.93 ? 179 PHE A CE2 1 
ATOM   1385 C  CZ  . PHE A 1 184 ? 10.269 21.148 18.107 1.00 54.84 ? 179 PHE A CZ  1 
ATOM   1386 N  N   . HIS A 1 185 ? 10.789 15.723 18.879 1.00 54.63 ? 180 HIS A N   1 
ATOM   1387 C  CA  . HIS A 1 185 ? 9.421  15.314 18.567 1.00 53.67 ? 180 HIS A CA  1 
ATOM   1388 C  C   . HIS A 1 185 ? 8.757  14.656 19.771 1.00 53.21 ? 180 HIS A C   1 
ATOM   1389 O  O   . HIS A 1 185 ? 7.613  14.972 20.116 1.00 53.29 ? 180 HIS A O   1 
ATOM   1390 C  CB  . HIS A 1 185 ? 9.407  14.362 17.364 1.00 54.96 ? 180 HIS A CB  1 
ATOM   1391 C  CG  . HIS A 1 185 ? 9.610  15.040 16.045 1.00 53.01 ? 180 HIS A CG  1 
ATOM   1392 N  ND1 . HIS A 1 185 ? 8.998  16.230 15.714 1.00 54.38 ? 180 HIS A ND1 1 
ATOM   1393 C  CD2 . HIS A 1 185 ? 10.365 14.695 14.973 1.00 56.33 ? 180 HIS A CD2 1 
ATOM   1394 C  CE1 . HIS A 1 185 ? 9.367  16.589 14.497 1.00 53.72 ? 180 HIS A CE1 1 
ATOM   1395 N  NE2 . HIS A 1 185 ? 10.197 15.677 14.025 1.00 51.81 ? 180 HIS A NE2 1 
ATOM   1396 N  N   . TYR A 1 186 ? 9.466  13.737 20.426 1.00 48.65 ? 181 TYR A N   1 
ATOM   1397 C  CA  . TYR A 1 186 ? 8.859  12.948 21.490 1.00 54.21 ? 181 TYR A CA  1 
ATOM   1398 C  C   . TYR A 1 186 ? 8.661  13.765 22.759 1.00 57.45 ? 181 TYR A C   1 
ATOM   1399 O  O   . TYR A 1 186 ? 7.634  13.622 23.428 1.00 61.40 ? 181 TYR A O   1 
ATOM   1400 C  CB  . TYR A 1 186 ? 9.716  11.723 21.789 1.00 53.34 ? 181 TYR A CB  1 
ATOM   1401 C  CG  . TYR A 1 186 ? 9.060  10.696 22.695 1.00 58.66 ? 181 TYR A CG  1 
ATOM   1402 C  CD1 . TYR A 1 186 ? 8.354  9.624  22.163 1.00 60.50 ? 181 TYR A CD1 1 
ATOM   1403 C  CD2 . TYR A 1 186 ? 9.164  10.786 24.077 1.00 59.21 ? 181 TYR A CD2 1 
ATOM   1404 C  CE1 . TYR A 1 186 ? 7.763  8.679  22.973 1.00 58.42 ? 181 TYR A CE1 1 
ATOM   1405 C  CE2 . TYR A 1 186 ? 8.576  9.840  24.902 1.00 59.78 ? 181 TYR A CE2 1 
ATOM   1406 C  CZ  . TYR A 1 186 ? 7.876  8.790  24.340 1.00 61.28 ? 181 TYR A CZ  1 
ATOM   1407 O  OH  . TYR A 1 186 ? 7.290  7.842  25.146 1.00 64.78 ? 181 TYR A OH  1 
ATOM   1408 N  N   . GLU A 1 187 ? 9.630  14.620 23.110 1.00 52.96 ? 182 GLU A N   1 
ATOM   1409 C  CA  . GLU A 1 187 ? 9.658  15.278 24.417 1.00 56.69 ? 182 GLU A CA  1 
ATOM   1410 C  C   . GLU A 1 187 ? 9.132  16.708 24.402 1.00 55.80 ? 182 GLU A C   1 
ATOM   1411 O  O   . GLU A 1 187 ? 8.498  17.130 25.371 1.00 60.96 ? 182 GLU A O   1 
ATOM   1412 C  CB  . GLU A 1 187 ? 11.080 15.283 24.993 1.00 53.25 ? 182 GLU A CB  1 
ATOM   1413 C  CG  . GLU A 1 187 ? 11.734 13.905 25.146 1.00 49.94 ? 182 GLU A CG  1 
ATOM   1414 C  CD  . GLU A 1 187 ? 11.124 13.042 26.243 1.00 58.70 ? 182 GLU A CD  1 
ATOM   1415 O  OE1 . GLU A 1 187 ? 10.275 13.550 27.003 1.00 63.34 ? 182 GLU A OE1 1 
ATOM   1416 O  OE2 . GLU A 1 187 ? 11.508 11.849 26.354 1.00 58.99 ? 182 GLU A OE2 1 
ATOM   1417 N  N   . ILE A 1 188 ? 9.390  17.479 23.353 1.00 51.87 ? 183 ILE A N   1 
ATOM   1418 C  CA  . ILE A 1 188 ? 8.980  18.875 23.303 1.00 54.66 ? 183 ILE A CA  1 
ATOM   1419 C  C   . ILE A 1 188 ? 7.701  19.065 22.495 1.00 60.53 ? 183 ILE A C   1 
ATOM   1420 O  O   . ILE A 1 188 ? 6.824  19.838 22.888 1.00 57.39 ? 183 ILE A O   1 
ATOM   1421 C  CB  . ILE A 1 188 ? 10.126 19.748 22.741 1.00 57.63 ? 183 ILE A CB  1 
ATOM   1422 C  CG1 . ILE A 1 188 ? 11.448 19.452 23.462 1.00 56.07 ? 183 ILE A CG1 1 
ATOM   1423 C  CG2 . ILE A 1 188 ? 9.763  21.214 22.775 1.00 53.27 ? 183 ILE A CG2 1 
ATOM   1424 C  CD1 . ILE A 1 188 ? 11.544 20.024 24.860 1.00 53.25 ? 183 ILE A CD1 1 
ATOM   1425 N  N   . ALA A 1 189 ? 7.591  18.395 21.346 1.00 59.77 ? 184 ALA A N   1 
ATOM   1426 C  CA  . ALA A 1 189 ? 6.444  18.565 20.465 1.00 60.39 ? 184 ALA A CA  1 
ATOM   1427 C  C   . ALA A 1 189 ? 5.317  17.595 20.771 1.00 60.77 ? 184 ALA A C   1 
ATOM   1428 O  O   . ALA A 1 189 ? 4.235  17.727 20.192 1.00 65.07 ? 184 ALA A O   1 
ATOM   1429 C  CB  . ALA A 1 189 ? 6.864  18.403 18.999 1.00 58.92 ? 184 ALA A CB  1 
ATOM   1430 N  N   . ASN A 1 190 ? 5.543  16.644 21.672 1.00 57.90 ? 185 ASN A N   1 
ATOM   1431 C  CA  . ASN A 1 190 ? 4.588  15.578 21.943 1.00 65.53 ? 185 ASN A CA  1 
ATOM   1432 C  C   . ASN A 1 190 ? 4.016  15.001 20.654 1.00 67.57 ? 185 ASN A C   1 
ATOM   1433 O  O   . ASN A 1 190 ? 2.823  15.153 20.367 1.00 66.48 ? 185 ASN A O   1 
ATOM   1434 C  CB  . ASN A 1 190 ? 3.459  16.066 22.846 1.00 68.06 ? 185 ASN A CB  1 
ATOM   1435 C  CG  . ASN A 1 190 ? 2.844  14.936 23.641 1.00 73.93 ? 185 ASN A CG  1 
ATOM   1436 O  OD1 . ASN A 1 190 ? 3.445  14.429 24.593 1.00 78.82 ? 185 ASN A OD1 1 
ATOM   1437 N  ND2 . ASN A 1 190 ? 1.652  14.508 23.233 1.00 74.61 ? 185 ASN A ND2 1 
ATOM   1438 N  N   . SER A 1 191 ? 4.875  14.358 19.868 1.00 67.46 ? 186 SER A N   1 
ATOM   1439 C  CA  . SER A 1 191 ? 4.480  13.692 18.628 1.00 61.52 ? 186 SER A CA  1 
ATOM   1440 C  C   . SER A 1 191 ? 5.225  12.376 18.573 1.00 62.55 ? 186 SER A C   1 
ATOM   1441 O  O   . SER A 1 191 ? 6.143  12.197 17.764 1.00 64.31 ? 186 SER A O   1 
ATOM   1442 C  CB  . SER A 1 191 ? 4.801  14.562 17.416 1.00 61.99 ? 186 SER A CB  1 
ATOM   1443 O  OG  . SER A 1 191 ? 4.439  15.901 17.684 1.00 67.50 ? 186 SER A OG  1 
ATOM   1444 N  N   . PRO A 1 192 ? 4.862  11.427 19.442 1.00 62.70 ? 187 PRO A N   1 
ATOM   1445 C  CA  . PRO A 1 192 ? 5.628  10.171 19.522 1.00 66.30 ? 187 PRO A CA  1 
ATOM   1446 C  C   . PRO A 1 192 ? 5.713  9.438  18.196 1.00 66.50 ? 187 PRO A C   1 
ATOM   1447 O  O   . PRO A 1 192 ? 6.735  8.798  17.910 1.00 66.37 ? 187 PRO A O   1 
ATOM   1448 C  CB  . PRO A 1 192 ? 4.856  9.351  20.569 1.00 65.80 ? 187 PRO A CB  1 
ATOM   1449 C  CG  . PRO A 1 192 ? 4.031  10.344 21.319 1.00 68.76 ? 187 PRO A CG  1 
ATOM   1450 C  CD  . PRO A 1 192 ? 3.698  11.426 20.343 1.00 64.84 ? 187 PRO A CD  1 
ATOM   1451 N  N   . GLU A 1 193 ? 4.660  9.521  17.378 1.00 69.55 ? 188 GLU A N   1 
ATOM   1452 C  CA  . GLU A 1 193 ? 4.658  8.879  16.067 1.00 65.88 ? 188 GLU A CA  1 
ATOM   1453 C  C   . GLU A 1 193 ? 5.666  9.544  15.135 1.00 64.25 ? 188 GLU A C   1 
ATOM   1454 O  O   . GLU A 1 193 ? 6.427  8.859  14.441 1.00 64.97 ? 188 GLU A O   1 
ATOM   1455 C  CB  . GLU A 1 193 ? 3.241  8.924  15.481 1.00 67.01 ? 188 GLU A CB  1 
ATOM   1456 C  CG  . GLU A 1 193 ? 2.695  10.352 15.219 1.00 69.77 ? 188 GLU A CG  1 
ATOM   1457 C  CD  . GLU A 1 193 ? 2.426  11.166 16.495 1.00 71.37 ? 188 GLU A CD  1 
ATOM   1458 O  OE1 . GLU A 1 193 ? 2.495  10.590 17.601 1.00 70.02 ? 188 GLU A OE1 1 
ATOM   1459 O  OE2 . GLU A 1 193 ? 2.195  12.395 16.398 1.00 68.89 ? 188 GLU A OE2 1 
ATOM   1460 N  N   . GLU A 1 194 ? 5.697  10.878 15.122 1.00 63.63 ? 189 GLU A N   1 
ATOM   1461 C  CA  . GLU A 1 194 ? 6.663  11.600 14.303 1.00 62.21 ? 189 GLU A CA  1 
ATOM   1462 C  C   . GLU A 1 194 ? 8.086  11.323 14.760 1.00 63.53 ? 189 GLU A C   1 
ATOM   1463 O  O   . GLU A 1 194 ? 9.006  11.284 13.934 1.00 61.68 ? 189 GLU A O   1 
ATOM   1464 C  CB  . GLU A 1 194 ? 6.367  13.094 14.358 1.00 61.14 ? 189 GLU A CB  1 
ATOM   1465 C  CG  . GLU A 1 194 ? 7.014  13.901 13.259 1.00 64.39 ? 189 GLU A CG  1 
ATOM   1466 C  CD  . GLU A 1 194 ? 6.116  15.028 12.787 1.00 69.31 ? 189 GLU A CD  1 
ATOM   1467 O  OE1 . GLU A 1 194 ? 5.021  15.183 13.373 1.00 72.15 ? 189 GLU A OE1 1 
ATOM   1468 O  OE2 . GLU A 1 194 ? 6.498  15.750 11.834 1.00 68.40 ? 189 GLU A OE2 1 
ATOM   1469 N  N   . ALA A 1 195 ? 8.274  11.127 16.067 1.00 60.60 ? 190 ALA A N   1 
ATOM   1470 C  CA  . ALA A 1 195 ? 9.579  10.760 16.603 1.00 59.97 ? 190 ALA A CA  1 
ATOM   1471 C  C   . ALA A 1 195 ? 9.968  9.357  16.174 1.00 57.40 ? 190 ALA A C   1 
ATOM   1472 O  O   . ALA A 1 195 ? 11.076 9.134  15.679 1.00 57.60 ? 190 ALA A O   1 
ATOM   1473 C  CB  . ALA A 1 195 ? 9.567  10.855 18.134 1.00 57.72 ? 190 ALA A CB  1 
ATOM   1474 N  N   . ILE A 1 196 ? 9.070  8.394  16.386 1.00 59.24 ? 191 ILE A N   1 
ATOM   1475 C  CA  . ILE A 1 196 ? 9.354  6.999  16.063 1.00 59.01 ? 191 ILE A CA  1 
ATOM   1476 C  C   . ILE A 1 196 ? 9.579  6.836  14.564 1.00 55.77 ? 191 ILE A C   1 
ATOM   1477 O  O   . ILE A 1 196 ? 10.461 6.086  14.130 1.00 57.17 ? 191 ILE A O   1 
ATOM   1478 C  CB  . ILE A 1 196 ? 8.208  6.108  16.579 1.00 62.96 ? 191 ILE A CB  1 
ATOM   1479 C  CG1 . ILE A 1 196 ? 8.482  5.690  18.027 1.00 61.63 ? 191 ILE A CG1 1 
ATOM   1480 C  CG2 . ILE A 1 196 ? 8.027  4.889  15.695 1.00 62.65 ? 191 ILE A CG2 1 
ATOM   1481 C  CD1 . ILE A 1 196 ? 7.306  5.046  18.720 1.00 61.50 ? 191 ILE A CD1 1 
ATOM   1482 N  N   . SER A 1 197 ? 8.808  7.554  13.753 1.00 54.74 ? 192 SER A N   1 
ATOM   1483 C  CA  . SER A 1 197 ? 9.000  7.482  12.308 1.00 58.91 ? 192 SER A CA  1 
ATOM   1484 C  C   . SER A 1 197 ? 10.379 8.001  11.907 1.00 57.14 ? 192 SER A C   1 
ATOM   1485 O  O   . SER A 1 197 ? 11.055 7.399  11.062 1.00 52.69 ? 192 SER A O   1 
ATOM   1486 C  CB  . SER A 1 197 ? 7.894  8.263  11.598 1.00 54.85 ? 192 SER A CB  1 
ATOM   1487 O  OG  . SER A 1 197 ? 8.389  8.905  10.441 1.00 64.98 ? 192 SER A OG  1 
ATOM   1488 N  N   . LEU A 1 198 ? 10.821 9.107  12.516 1.00 54.35 ? 193 LEU A N   1 
ATOM   1489 C  CA  . LEU A 1 198 ? 12.126 9.662  12.172 1.00 51.55 ? 193 LEU A CA  1 
ATOM   1490 C  C   . LEU A 1 198 ? 13.251 8.746  12.646 1.00 52.37 ? 193 LEU A C   1 
ATOM   1491 O  O   . LEU A 1 198 ? 14.197 8.458  11.893 1.00 50.27 ? 193 LEU A O   1 
ATOM   1492 C  CB  . LEU A 1 198 ? 12.268 11.070 12.756 1.00 50.93 ? 193 LEU A CB  1 
ATOM   1493 C  CG  . LEU A 1 198 ? 13.614 11.769 12.567 1.00 45.95 ? 193 LEU A CG  1 
ATOM   1494 C  CD1 . LEU A 1 198 ? 14.057 11.637 11.142 1.00 48.74 ? 193 LEU A CD1 1 
ATOM   1495 C  CD2 . LEU A 1 198 ? 13.549 13.242 12.982 1.00 48.12 ? 193 LEU A CD2 1 
ATOM   1496 N  N   . ALA A 1 199 ? 13.157 8.262  13.885 1.00 49.42 ? 194 ALA A N   1 
ATOM   1497 C  CA  . ALA A 1 199 ? 14.207 7.411  14.423 1.00 45.09 ? 194 ALA A CA  1 
ATOM   1498 C  C   . ALA A 1 199 ? 14.315 6.109  13.644 1.00 49.79 ? 194 ALA A C   1 
ATOM   1499 O  O   . ALA A 1 199 ? 15.422 5.651  13.343 1.00 48.31 ? 194 ALA A O   1 
ATOM   1500 C  CB  . ALA A 1 199 ? 13.941 7.117  15.898 1.00 49.66 ? 194 ALA A CB  1 
ATOM   1501 N  N   . LYS A 1 200 ? 13.175 5.472  13.353 1.00 52.21 ? 195 LYS A N   1 
ATOM   1502 C  CA  . LYS A 1 200 ? 13.199 4.197  12.637 1.00 53.78 ? 195 LYS A CA  1 
ATOM   1503 C  C   . LYS A 1 200 ? 13.753 4.379  11.234 1.00 46.70 ? 195 LYS A C   1 
ATOM   1504 O  O   . LYS A 1 200 ? 14.622 3.620  10.799 1.00 48.38 ? 195 LYS A O   1 
ATOM   1505 C  CB  . LYS A 1 200 ? 11.797 3.590  12.584 1.00 52.35 ? 195 LYS A CB  1 
ATOM   1506 C  CG  . LYS A 1 200 ? 11.644 2.481  11.525 1.00 55.64 ? 195 LYS A CG  1 
ATOM   1507 C  CD  . LYS A 1 200 ? 10.791 1.324  12.034 1.00 56.96 ? 195 LYS A CD  1 
ATOM   1508 C  CE  . LYS A 1 200 ? 11.047 0.062  11.238 1.00 57.97 ? 195 LYS A CE  1 
ATOM   1509 N  NZ  . LYS A 1 200 ? 12.366 -0.521 11.606 1.00 62.96 ? 195 LYS A NZ  1 
ATOM   1510 N  N   . THR A 1 201 ? 13.309 5.424  10.542 1.00 48.92 ? 196 THR A N   1 
ATOM   1511 C  CA  . THR A 1 201 ? 13.798 5.684  9.198  1.00 51.70 ? 196 THR A CA  1 
ATOM   1512 C  C   . THR A 1 201 ? 15.299 5.940  9.212  1.00 51.75 ? 196 THR A C   1 
ATOM   1513 O  O   . THR A 1 201 ? 16.047 5.403  8.383  1.00 49.94 ? 196 THR A O   1 
ATOM   1514 C  CB  . THR A 1 201 ? 13.055 6.883  8.614  1.00 54.52 ? 196 THR A CB  1 
ATOM   1515 O  OG1 . THR A 1 201 ? 11.731 6.480  8.243  1.00 58.18 ? 196 THR A OG1 1 
ATOM   1516 C  CG2 . THR A 1 201 ? 13.780 7.398  7.391  1.00 52.33 ? 196 THR A CG2 1 
ATOM   1517 N  N   . THR A 1 202 ? 15.754 6.760  10.162 1.00 48.45 ? 197 THR A N   1 
ATOM   1518 C  CA  . THR A 1 202 ? 17.166 7.107  10.252 1.00 44.75 ? 197 THR A CA  1 
ATOM   1519 C  C   . THR A 1 202 ? 18.035 5.880  10.480 1.00 41.35 ? 197 THR A C   1 
ATOM   1520 O  O   . THR A 1 202 ? 19.083 5.724  9.845  1.00 41.89 ? 197 THR A O   1 
ATOM   1521 C  CB  . THR A 1 202 ? 17.376 8.108  11.388 1.00 43.75 ? 197 THR A CB  1 
ATOM   1522 O  OG1 . THR A 1 202 ? 16.574 9.267  11.138 1.00 43.56 ? 197 THR A OG1 1 
ATOM   1523 C  CG2 . THR A 1 202 ? 18.835 8.496  11.453 1.00 40.57 ? 197 THR A CG2 1 
ATOM   1524 N  N   . PHE A 1 203 ? 17.644 5.021  11.424 1.00 38.94 ? 198 PHE A N   1 
ATOM   1525 C  CA  . PHE A 1 203 ? 18.417 3.813  11.682 1.00 39.82 ? 198 PHE A CA  1 
ATOM   1526 C  C   . PHE A 1 203 ? 18.411 2.896  10.456 1.00 42.92 ? 198 PHE A C   1 
ATOM   1527 O  O   . PHE A 1 203 ? 19.454 2.368  10.053 1.00 41.44 ? 198 PHE A O   1 
ATOM   1528 C  CB  . PHE A 1 203 ? 17.866 3.075  12.917 1.00 40.76 ? 198 PHE A CB  1 
ATOM   1529 C  CG  . PHE A 1 203 ? 18.557 1.777  13.197 1.00 43.48 ? 198 PHE A CG  1 
ATOM   1530 C  CD1 . PHE A 1 203 ? 19.666 1.727  14.029 1.00 46.49 ? 198 PHE A CD1 1 
ATOM   1531 C  CD2 . PHE A 1 203 ? 18.105 0.594  12.625 1.00 46.72 ? 198 PHE A CD2 1 
ATOM   1532 C  CE1 . PHE A 1 203 ? 20.320 0.518  14.261 1.00 46.61 ? 198 PHE A CE1 1 
ATOM   1533 C  CE2 . PHE A 1 203 ? 18.748 -0.606 12.852 1.00 46.08 ? 198 PHE A CE2 1 
ATOM   1534 C  CZ  . PHE A 1 203 ? 19.853 -0.650 13.672 1.00 50.27 ? 198 PHE A CZ  1 
ATOM   1535 N  N   . ASP A 1 204 ? 17.237 2.693  9.858  1.00 40.30 ? 199 ASP A N   1 
ATOM   1536 C  CA  . ASP A 1 204 ? 17.129 1.754  8.739  1.00 45.88 ? 199 ASP A CA  1 
ATOM   1537 C  C   . ASP A 1 204 ? 17.931 2.233  7.533  1.00 42.16 ? 199 ASP A C   1 
ATOM   1538 O  O   . ASP A 1 204 ? 18.602 1.433  6.864  1.00 47.68 ? 199 ASP A O   1 
ATOM   1539 C  CB  . ASP A 1 204 ? 15.663 1.557  8.363  1.00 45.95 ? 199 ASP A CB  1 
ATOM   1540 C  CG  . ASP A 1 204 ? 14.919 0.658  9.334  1.00 46.67 ? 199 ASP A CG  1 
ATOM   1541 O  OD1 . ASP A 1 204 ? 15.564 -0.105 10.091 1.00 47.49 ? 199 ASP A OD1 1 
ATOM   1542 O  OD2 . ASP A 1 204 ? 13.672 0.701  9.313  1.00 49.76 ? 199 ASP A OD2 1 
ATOM   1543 N  N   . GLU A 1 205 ? 17.884 3.534  7.241  1.00 42.61 ? 200 GLU A N   1 
ATOM   1544 C  CA  . GLU A 1 205 ? 18.672 4.040  6.127  1.00 46.59 ? 200 GLU A CA  1 
ATOM   1545 C  C   . GLU A 1 205 ? 20.169 3.958  6.410  1.00 45.84 ? 200 GLU A C   1 
ATOM   1546 O  O   . GLU A 1 205 ? 20.953 3.677  5.492  1.00 44.12 ? 200 GLU A O   1 
ATOM   1547 C  CB  . GLU A 1 205 ? 18.235 5.460  5.782  1.00 46.96 ? 200 GLU A CB  1 
ATOM   1548 C  CG  . GLU A 1 205 ? 16.792 5.510  5.318  1.00 49.74 ? 200 GLU A CG  1 
ATOM   1549 C  CD  . GLU A 1 205 ? 16.405 6.836  4.710  1.00 54.47 ? 200 GLU A CD  1 
ATOM   1550 O  OE1 . GLU A 1 205 ? 17.165 7.819  4.868  1.00 56.13 ? 200 GLU A OE1 1 
ATOM   1551 O  OE2 . GLU A 1 205 ? 15.333 6.893  4.067  1.00 57.32 ? 200 GLU A OE2 1 
ATOM   1552 N  N   . ALA A 1 206 ? 20.587 4.161  7.664  1.00 40.82 ? 201 ALA A N   1 
ATOM   1553 C  CA  . ALA A 1 206 ? 21.995 3.972  8.008  1.00 38.83 ? 201 ALA A CA  1 
ATOM   1554 C  C   . ALA A 1 206 ? 22.430 2.536  7.753  1.00 39.14 ? 201 ALA A C   1 
ATOM   1555 O  O   . ALA A 1 206 ? 23.504 2.291  7.194  1.00 38.10 ? 201 ALA A O   1 
ATOM   1556 C  CB  . ALA A 1 206 ? 22.245 4.347  9.475  1.00 36.28 ? 201 ALA A CB  1 
ATOM   1557 N  N   . MET A 1 207 ? 21.623 1.572  8.212  1.00 35.89 ? 202 MET A N   1 
ATOM   1558 C  CA  . MET A 1 207 ? 21.889 0.153  7.967  1.00 40.82 ? 202 MET A CA  1 
ATOM   1559 C  C   . MET A 1 207 ? 21.954 -0.150 6.475  1.00 42.42 ? 202 MET A C   1 
ATOM   1560 O  O   . MET A 1 207 ? 22.856 -0.849 6.004  1.00 39.95 ? 202 MET A O   1 
ATOM   1561 C  CB  . MET A 1 207 ? 20.777 -0.686 8.585  1.00 43.08 ? 202 MET A CB  1 
ATOM   1562 C  CG  . MET A 1 207 ? 21.216 -1.851 9.417  1.00 54.97 ? 202 MET A CG  1 
ATOM   1563 S  SD  . MET A 1 207 ? 22.368 -1.434 10.735 1.00 51.35 ? 202 MET A SD  1 
ATOM   1564 C  CE  . MET A 1 207 ? 22.912 -3.072 11.101 1.00 52.56 ? 202 MET A CE  1 
ATOM   1565 N  N   . ALA A 1 208 ? 20.951 0.312  5.736  1.00 42.89 ? 203 ALA A N   1 
ATOM   1566 C  CA  . ALA A 1 208 ? 20.911 0.066  4.299  1.00 44.47 ? 203 ALA A CA  1 
ATOM   1567 C  C   . ALA A 1 208 ? 22.173 0.583  3.622  1.00 42.92 ? 203 ALA A C   1 
ATOM   1568 O  O   . ALA A 1 208 ? 22.713 -0.064 2.725  1.00 40.90 ? 203 ALA A O   1 
ATOM   1569 C  CB  . ALA A 1 208 ? 19.660 0.705  3.702  1.00 42.05 ? 203 ALA A CB  1 
ATOM   1570 N  N   . ASP A 1 209 ? 22.690 1.729  4.061  1.00 39.81 ? 204 ASP A N   1 
ATOM   1571 C  CA  . ASP A 1 209 ? 23.925 2.209  3.453  1.00 39.74 ? 204 ASP A CA  1 
ATOM   1572 C  C   . ASP A 1 209 ? 25.083 2.131  4.443  1.00 39.95 ? 204 ASP A C   1 
ATOM   1573 O  O   . ASP A 1 209 ? 25.895 3.063  4.537  1.00 36.66 ? 204 ASP A O   1 
ATOM   1574 C  CB  . ASP A 1 209 ? 23.725 3.624  2.894  1.00 35.56 ? 204 ASP A CB  1 
ATOM   1575 C  CG  . ASP A 1 209 ? 22.953 3.611  1.586  1.00 43.05 ? 204 ASP A CG  1 
ATOM   1576 O  OD1 . ASP A 1 209 ? 23.114 2.636  0.829  1.00 40.89 ? 204 ASP A OD1 1 
ATOM   1577 O  OD2 . ASP A 1 209 ? 22.148 4.518  1.339  1.00 44.22 ? 204 ASP A OD2 1 
ATOM   1578 N  N   . LEU A 1 210 ? 25.201 0.978  5.125  1.00 36.54 ? 205 LEU A N   1 
ATOM   1579 C  CA  . LEU A 1 210 ? 26.235 0.802  6.138  1.00 37.47 ? 205 LEU A CA  1 
ATOM   1580 C  C   . LEU A 1 210 ? 27.627 0.957  5.560  1.00 41.92 ? 205 LEU A C   1 
ATOM   1581 O  O   . LEU A 1 210 ? 28.547 1.377  6.269  1.00 37.19 ? 205 LEU A O   1 
ATOM   1582 C  CB  . LEU A 1 210 ? 26.111 -0.575 6.801  1.00 38.09 ? 205 LEU A CB  1 
ATOM   1583 C  CG  . LEU A 1 210 ? 27.004 -0.836 8.006  1.00 39.76 ? 205 LEU A CG  1 
ATOM   1584 C  CD1 . LEU A 1 210 ? 26.594 0.083  9.170  1.00 38.11 ? 205 LEU A CD1 1 
ATOM   1585 C  CD2 . LEU A 1 210 ? 26.953 -2.332 8.413  1.00 37.66 ? 205 LEU A CD2 1 
ATOM   1586 N  N   . HIS A 1 211 ? 27.808 0.611  4.278  1.00 39.65 ? 206 HIS A N   1 
ATOM   1587 C  CA  . HIS A 1 211 ? 29.100 0.760  3.622  1.00 38.56 ? 206 HIS A CA  1 
ATOM   1588 C  C   . HIS A 1 211 ? 29.605 2.211  3.579  1.00 37.43 ? 206 HIS A C   1 
ATOM   1589 O  O   . HIS A 1 211 ? 30.765 2.420  3.215  1.00 39.10 ? 206 HIS A O   1 
ATOM   1590 C  CB  . HIS A 1 211 ? 29.007 0.219  2.181  1.00 37.70 ? 206 HIS A CB  1 
ATOM   1591 C  CG  . HIS A 1 211 ? 28.162 1.070  1.280  1.00 36.32 ? 206 HIS A CG  1 
ATOM   1592 N  ND1 . HIS A 1 211 ? 26.785 1.009  1.279  1.00 38.05 ? 206 HIS A ND1 1 
ATOM   1593 C  CD2 . HIS A 1 211 ? 28.496 2.018  0.366  1.00 38.40 ? 206 HIS A CD2 1 
ATOM   1594 C  CE1 . HIS A 1 211 ? 26.307 1.886  0.411  1.00 36.82 ? 206 HIS A CE1 1 
ATOM   1595 N  NE2 . HIS A 1 211 ? 27.325 2.512  -0.154 1.00 35.10 ? 206 HIS A NE2 1 
ATOM   1596 N  N   . THR A 1 212 ? 28.783 3.213  3.897  1.00 36.19 ? 207 THR A N   1 
ATOM   1597 C  CA  . THR A 1 212 ? 29.266 4.598  3.842  1.00 36.61 ? 207 THR A CA  1 
ATOM   1598 C  C   . THR A 1 212 ? 29.993 5.042  5.119  1.00 41.32 ? 207 THR A C   1 
ATOM   1599 O  O   . THR A 1 212 ? 30.446 6.190  5.191  1.00 36.85 ? 207 THR A O   1 
ATOM   1600 C  CB  . THR A 1 212 ? 28.112 5.577  3.538  1.00 37.15 ? 207 THR A CB  1 
ATOM   1601 O  OG1 . THR A 1 212 ? 27.110 5.509  4.572  1.00 37.45 ? 207 THR A OG1 1 
ATOM   1602 C  CG2 . THR A 1 212 ? 27.461 5.253  2.148  1.00 37.42 ? 207 THR A CG2 1 
ATOM   1603 N  N   . LEU A 1 213 ? 30.146 4.162  6.106  1.00 38.03 ? 208 LEU A N   1 
ATOM   1604 C  CA  . LEU A 1 213 ? 30.887 4.504  7.316  1.00 34.46 ? 208 LEU A CA  1 
ATOM   1605 C  C   . LEU A 1 213 ? 32.278 5.024  6.978  1.00 39.52 ? 208 LEU A C   1 
ATOM   1606 O  O   . LEU A 1 213 ? 32.969 4.482  6.112  1.00 38.71 ? 208 LEU A O   1 
ATOM   1607 C  CB  . LEU A 1 213 ? 31.009 3.269  8.222  1.00 36.65 ? 208 LEU A CB  1 
ATOM   1608 C  CG  . LEU A 1 213 ? 29.731 2.832  8.911  1.00 32.99 ? 208 LEU A CG  1 
ATOM   1609 C  CD1 . LEU A 1 213 ? 29.993 1.474  9.541  1.00 39.04 ? 208 LEU A CD1 1 
ATOM   1610 C  CD2 . LEU A 1 213 ? 29.327 3.875  10.001 1.00 33.32 ? 208 LEU A CD2 1 
ATOM   1611 N  N   . SER A 1 214 ? 32.704 6.070  7.683  1.00 36.79 ? 209 SER A N   1 
ATOM   1612 C  CA  . SER A 1 214 ? 34.009 6.669  7.444  1.00 39.31 ? 209 SER A CA  1 
ATOM   1613 C  C   . SER A 1 214 ? 35.039 6.119  8.424  1.00 39.46 ? 209 SER A C   1 
ATOM   1614 O  O   . SER A 1 214 ? 34.757 5.950  9.619  1.00 41.96 ? 209 SER A O   1 
ATOM   1615 C  CB  . SER A 1 214 ? 33.928 8.199  7.547  1.00 43.77 ? 209 SER A CB  1 
ATOM   1616 O  OG  . SER A 1 214 ? 35.216 8.785  7.624  1.00 47.45 ? 209 SER A OG  1 
ATOM   1617 N  N   . GLU A 1 215 ? 36.243 5.852  7.906  1.00 37.05 ? 210 GLU A N   1 
ATOM   1618 C  CA  . GLU A 1 215 ? 37.341 5.387  8.746  1.00 42.37 ? 210 GLU A CA  1 
ATOM   1619 C  C   . GLU A 1 215 ? 37.557 6.279  9.962  1.00 47.93 ? 210 GLU A C   1 
ATOM   1620 O  O   . GLU A 1 215 ? 37.877 5.782  11.045 1.00 46.57 ? 210 GLU A O   1 
ATOM   1621 C  CB  . GLU A 1 215 ? 38.640 5.319  7.952  1.00 43.88 ? 210 GLU A CB  1 
ATOM   1622 C  CG  . GLU A 1 215 ? 38.572 4.556  6.681  1.00 51.62 ? 210 GLU A CG  1 
ATOM   1623 C  CD  . GLU A 1 215 ? 39.896 4.593  5.971  1.00 56.07 ? 210 GLU A CD  1 
ATOM   1624 O  OE1 . GLU A 1 215 ? 40.927 4.457  6.673  1.00 58.55 ? 210 GLU A OE1 1 
ATOM   1625 O  OE2 . GLU A 1 215 ? 39.904 4.749  4.728  1.00 65.42 ? 210 GLU A OE2 1 
ATOM   1626 N  N   . ASP A 1 216 ? 37.410 7.594  9.813  1.00 41.61 ? 211 ASP A N   1 
ATOM   1627 C  CA  . ASP A 1 216 ? 37.744 8.460  10.942 1.00 45.23 ? 211 ASP A CA  1 
ATOM   1628 C  C   . ASP A 1 216 ? 36.564 8.771  11.859 1.00 46.07 ? 211 ASP A C   1 
ATOM   1629 O  O   . ASP A 1 216 ? 36.759 9.434  12.888 1.00 47.96 ? 211 ASP A O   1 
ATOM   1630 C  CB  . ASP A 1 216 ? 38.388 9.764  10.448 1.00 52.75 ? 211 ASP A CB  1 
ATOM   1631 C  CG  . ASP A 1 216 ? 37.553 10.473 9.419  1.00 53.81 ? 211 ASP A CG  1 
ATOM   1632 O  OD1 . ASP A 1 216 ? 36.313 10.460 9.554  1.00 57.37 ? 211 ASP A OD1 1 
ATOM   1633 O  OD2 . ASP A 1 216 ? 38.140 11.052 8.473  1.00 64.21 ? 211 ASP A OD2 1 
ATOM   1634 N  N   . SER A 1 217 ? 35.351 8.290  11.560 1.00 40.93 ? 212 SER A N   1 
ATOM   1635 C  CA  . SER A 1 217 ? 34.246 8.554  12.477 1.00 41.63 ? 212 SER A CA  1 
ATOM   1636 C  C   . SER A 1 217 ? 33.291 7.380  12.681 1.00 37.07 ? 212 SER A C   1 
ATOM   1637 O  O   . SER A 1 217 ? 32.195 7.595  13.214 1.00 36.68 ? 212 SER A O   1 
ATOM   1638 C  CB  . SER A 1 217 ? 33.442 9.752  11.985 1.00 40.49 ? 212 SER A CB  1 
ATOM   1639 O  OG  . SER A 1 217 ? 32.897 9.445  10.718 1.00 38.95 ? 212 SER A OG  1 
ATOM   1640 N  N   . TYR A 1 218 ? 33.647 6.158  12.273 1.00 37.78 ? 213 TYR A N   1 
ATOM   1641 C  CA  . TYR A 1 218 ? 32.663 5.074  12.304 1.00 38.59 ? 213 TYR A CA  1 
ATOM   1642 C  C   . TYR A 1 218 ? 32.243 4.724  13.736 1.00 39.83 ? 213 TYR A C   1 
ATOM   1643 O  O   . TYR A 1 218 ? 31.091 4.323  13.961 1.00 37.95 ? 213 TYR A O   1 
ATOM   1644 C  CB  . TYR A 1 218 ? 33.208 3.837  11.570 1.00 38.15 ? 213 TYR A CB  1 
ATOM   1645 C  CG  . TYR A 1 218 ? 34.309 3.114  12.301 1.00 40.84 ? 213 TYR A CG  1 
ATOM   1646 C  CD1 . TYR A 1 218 ? 34.014 2.125  13.243 1.00 40.52 ? 213 TYR A CD1 1 
ATOM   1647 C  CD2 . TYR A 1 218 ? 35.644 3.414  12.067 1.00 39.79 ? 213 TYR A CD2 1 
ATOM   1648 C  CE1 . TYR A 1 218 ? 35.012 1.453  13.922 1.00 39.10 ? 213 TYR A CE1 1 
ATOM   1649 C  CE2 . TYR A 1 218 ? 36.649 2.747  12.754 1.00 41.96 ? 213 TYR A CE2 1 
ATOM   1650 C  CZ  . TYR A 1 218 ? 36.326 1.759  13.676 1.00 42.32 ? 213 TYR A CZ  1 
ATOM   1651 O  OH  . TYR A 1 218 ? 37.312 1.078  14.367 1.00 40.34 ? 213 TYR A OH  1 
ATOM   1652 N  N   . LYS A 1 219 ? 33.137 4.897  14.720 1.00 38.13 ? 214 LYS A N   1 
ATOM   1653 C  CA  . LYS A 1 219 ? 32.740 4.654  16.106 1.00 43.11 ? 214 LYS A CA  1 
ATOM   1654 C  C   . LYS A 1 219 ? 31.636 5.611  16.536 1.00 43.69 ? 214 LYS A C   1 
ATOM   1655 O  O   . LYS A 1 219 ? 30.720 5.217  17.274 1.00 41.44 ? 214 LYS A O   1 
ATOM   1656 C  CB  . LYS A 1 219 ? 33.948 4.771  17.045 1.00 43.73 ? 214 LYS A CB  1 
ATOM   1657 C  CG  . LYS A 1 219 ? 35.024 3.733  16.779 1.00 47.78 ? 214 LYS A CG  1 
ATOM   1658 C  CD  . LYS A 1 219 ? 35.934 3.504  17.983 1.00 52.77 ? 214 LYS A CD  1 
ATOM   1659 C  CE  . LYS A 1 219 ? 37.264 4.222  17.793 1.00 56.85 ? 214 LYS A CE  1 
ATOM   1660 N  NZ  . LYS A 1 219 ? 38.122 3.555  16.761 1.00 58.08 ? 214 LYS A NZ  1 
ATOM   1661 N  N   . ASP A 1 220 ? 31.710 6.878  16.094 1.00 39.87 ? 215 ASP A N   1 
ATOM   1662 C  CA  . ASP A 1 220 ? 30.655 7.829  16.424 1.00 41.82 ? 215 ASP A CA  1 
ATOM   1663 C  C   . ASP A 1 220 ? 29.358 7.444  15.749 1.00 38.96 ? 215 ASP A C   1 
ATOM   1664 O  O   . ASP A 1 220 ? 28.282 7.518  16.360 1.00 38.20 ? 215 ASP A O   1 
ATOM   1665 C  CB  . ASP A 1 220 ? 31.052 9.254  16.010 1.00 42.09 ? 215 ASP A CB  1 
ATOM   1666 C  CG  . ASP A 1 220 ? 32.286 9.744  16.731 1.00 46.98 ? 215 ASP A CG  1 
ATOM   1667 O  OD1 . ASP A 1 220 ? 32.592 9.192  17.809 1.00 49.11 ? 215 ASP A OD1 1 
ATOM   1668 O  OD2 . ASP A 1 220 ? 32.944 10.676 16.226 1.00 51.72 ? 215 ASP A OD2 1 
ATOM   1669 N  N   . SER A 1 221 ? 29.440 7.036  14.480 1.00 35.04 ? 216 SER A N   1 
ATOM   1670 C  CA  . SER A 1 221 ? 28.236 6.633  13.763 1.00 36.05 ? 216 SER A CA  1 
ATOM   1671 C  C   . SER A 1 221 ? 27.536 5.470  14.460 1.00 33.34 ? 216 SER A C   1 
ATOM   1672 O  O   . SER A 1 221 ? 26.331 5.521  14.720 1.00 34.15 ? 216 SER A O   1 
ATOM   1673 C  CB  . SER A 1 221 ? 28.591 6.270  12.324 1.00 33.54 ? 216 SER A CB  1 
ATOM   1674 O  OG  . SER A 1 221 ? 29.087 7.400  11.633 1.00 37.93 ? 216 SER A OG  1 
ATOM   1675 N  N   . THR A 1 222 ? 28.269 4.401  14.750 1.00 35.97 ? 217 THR A N   1 
ATOM   1676 C  CA  . THR A 1 222 ? 27.603 3.228  15.313 1.00 40.24 ? 217 THR A CA  1 
ATOM   1677 C  C   . THR A 1 222 ? 27.064 3.511  16.711 1.00 39.05 ? 217 THR A C   1 
ATOM   1678 O  O   . THR A 1 222 ? 26.017 2.964  17.101 1.00 37.11 ? 217 THR A O   1 
ATOM   1679 C  CB  . THR A 1 222 ? 28.552 2.037  15.288 1.00 36.90 ? 217 THR A CB  1 
ATOM   1680 O  OG1 . THR A 1 222 ? 29.751 2.336  16.012 1.00 40.05 ? 217 THR A OG1 1 
ATOM   1681 C  CG2 . THR A 1 222 ? 28.924 1.717  13.847 1.00 38.97 ? 217 THR A CG2 1 
ATOM   1682 N  N   . LEU A 1 223 ? 27.709 4.419  17.449 1.00 38.86 ? 218 LEU A N   1 
ATOM   1683 C  CA  . LEU A 1 223 ? 27.162 4.816  18.745 1.00 39.59 ? 218 LEU A CA  1 
ATOM   1684 C  C   . LEU A 1 223 ? 25.780 5.434  18.582 1.00 39.29 ? 218 LEU A C   1 
ATOM   1685 O  O   . LEU A 1 223 ? 24.836 5.063  19.289 1.00 37.40 ? 218 LEU A O   1 
ATOM   1686 C  CB  . LEU A 1 223 ? 28.110 5.788  19.454 1.00 39.90 ? 218 LEU A CB  1 
ATOM   1687 C  CG  . LEU A 1 223 ? 27.621 6.307  20.814 1.00 41.07 ? 218 LEU A CG  1 
ATOM   1688 C  CD1 . LEU A 1 223 ? 27.165 5.148  21.730 1.00 45.01 ? 218 LEU A CD1 1 
ATOM   1689 C  CD2 . LEU A 1 223 ? 28.751 7.106  21.444 1.00 42.42 ? 218 LEU A CD2 1 
ATOM   1690 N  N   . ILE A 1 224 ? 25.635 6.376  17.643 1.00 37.30 ? 219 ILE A N   1 
ATOM   1691 C  CA  . ILE A 1 224 ? 24.337 7.021  17.462 1.00 37.56 ? 219 ILE A CA  1 
ATOM   1692 C  C   . ILE A 1 224 ? 23.298 6.019  16.980 1.00 38.42 ? 219 ILE A C   1 
ATOM   1693 O  O   . ILE A 1 224 ? 22.129 6.079  17.378 1.00 41.98 ? 219 ILE A O   1 
ATOM   1694 C  CB  . ILE A 1 224 ? 24.438 8.215  16.496 1.00 35.34 ? 219 ILE A CB  1 
ATOM   1695 C  CG1 . ILE A 1 224 ? 25.466 9.228  17.009 1.00 40.62 ? 219 ILE A CG1 1 
ATOM   1696 C  CG2 . ILE A 1 224 ? 23.075 8.893  16.375 1.00 36.70 ? 219 ILE A CG2 1 
ATOM   1697 C  CD1 . ILE A 1 224 ? 25.033 9.886  18.290 1.00 39.33 ? 219 ILE A CD1 1 
ATOM   1698 N  N   . MET A 1 225 ? 23.688 5.103  16.094 1.00 36.57 ? 220 MET A N   1 
ATOM   1699 C  CA  . MET A 1 225 ? 22.722 4.115  15.613 1.00 36.45 ? 220 MET A CA  1 
ATOM   1700 C  C   . MET A 1 225 ? 22.160 3.301  16.764 1.00 40.47 ? 220 MET A C   1 
ATOM   1701 O  O   . MET A 1 225 ? 20.946 3.068  16.835 1.00 43.55 ? 220 MET A O   1 
ATOM   1702 C  CB  . MET A 1 225 ? 23.367 3.202  14.573 1.00 37.98 ? 220 MET A CB  1 
ATOM   1703 C  CG  . MET A 1 225 ? 23.860 3.973  13.323 1.00 39.11 ? 220 MET A CG  1 
ATOM   1704 S  SD  . MET A 1 225 ? 24.836 2.991  12.174 1.00 43.97 ? 220 MET A SD  1 
ATOM   1705 C  CE  . MET A 1 225 ? 23.694 1.620  11.867 1.00 38.15 ? 220 MET A CE  1 
ATOM   1706 N  N   . GLN A 1 226 ? 23.034 2.875  17.683 1.00 38.08 ? 221 GLN A N   1 
ATOM   1707 C  CA  . GLN A 1 226 ? 22.590 2.197  18.901 1.00 39.88 ? 221 GLN A CA  1 
ATOM   1708 C  C   . GLN A 1 226 ? 21.674 3.082  19.742 1.00 48.10 ? 221 GLN A C   1 
ATOM   1709 O  O   . GLN A 1 226 ? 20.660 2.610  20.277 1.00 49.48 ? 221 GLN A O   1 
ATOM   1710 C  CB  . GLN A 1 226 ? 23.799 1.775  19.720 1.00 39.82 ? 221 GLN A CB  1 
ATOM   1711 C  CG  . GLN A 1 226 ? 23.423 1.018  20.976 1.00 49.56 ? 221 GLN A CG  1 
ATOM   1712 C  CD  . GLN A 1 226 ? 22.642 -0.236 20.638 1.00 51.99 ? 221 GLN A CD  1 
ATOM   1713 O  OE1 . GLN A 1 226 ? 23.051 -1.018 19.773 1.00 53.51 ? 221 GLN A OE1 1 
ATOM   1714 N  NE2 . GLN A 1 226 ? 21.500 -0.418 21.291 1.00 52.28 ? 221 GLN A NE2 1 
ATOM   1715 N  N   . LEU A 1 227 ? 22.026 4.364  19.902 1.00 43.55 ? 222 LEU A N   1 
ATOM   1716 C  CA  . LEU A 1 227 ? 21.160 5.258  20.671 1.00 42.66 ? 222 LEU A CA  1 
ATOM   1717 C  C   . LEU A 1 227 ? 19.800 5.411  20.006 1.00 43.43 ? 222 LEU A C   1 
ATOM   1718 O  O   . LEU A 1 227 ? 18.775 5.472  20.692 1.00 40.95 ? 222 LEU A O   1 
ATOM   1719 C  CB  . LEU A 1 227 ? 21.823 6.625  20.860 1.00 42.43 ? 222 LEU A CB  1 
ATOM   1720 C  CG  . LEU A 1 227 ? 23.043 6.640  21.786 1.00 40.67 ? 222 LEU A CG  1 
ATOM   1721 C  CD1 . LEU A 1 227 ? 23.424 8.090  22.121 1.00 41.00 ? 222 LEU A CD1 1 
ATOM   1722 C  CD2 . LEU A 1 227 ? 22.785 5.845  23.058 1.00 42.21 ? 222 LEU A CD2 1 
ATOM   1723 N  N   . LEU A 1 228 ? 19.762 5.444  18.664 1.00 43.25 ? 223 LEU A N   1 
ATOM   1724 C  CA  . LEU A 1 228 ? 18.477 5.385  17.966 1.00 43.74 ? 223 LEU A CA  1 
ATOM   1725 C  C   . LEU A 1 228 ? 17.695 4.120  18.341 1.00 44.27 ? 223 LEU A C   1 
ATOM   1726 O  O   . LEU A 1 228 ? 16.492 4.191  18.626 1.00 46.47 ? 223 LEU A O   1 
ATOM   1727 C  CB  . LEU A 1 228 ? 18.697 5.471  16.447 1.00 39.50 ? 223 LEU A CB  1 
ATOM   1728 C  CG  . LEU A 1 228 ? 19.096 6.859  15.930 1.00 38.71 ? 223 LEU A CG  1 
ATOM   1729 C  CD1 . LEU A 1 228 ? 19.752 6.801  14.540 1.00 40.35 ? 223 LEU A CD1 1 
ATOM   1730 C  CD2 . LEU A 1 228 ? 17.893 7.785  15.913 1.00 43.34 ? 223 LEU A CD2 1 
ATOM   1731 N  N   . ARG A 1 229 ? 18.366 2.959  18.373 1.00 48.90 ? 224 ARG A N   1 
ATOM   1732 C  CA  . ARG A 1 229 ? 17.693 1.708  18.749 1.00 48.42 ? 224 ARG A CA  1 
ATOM   1733 C  C   . ARG A 1 229 ? 17.182 1.760  20.182 1.00 54.32 ? 224 ARG A C   1 
ATOM   1734 O  O   . ARG A 1 229 ? 16.091 1.257  20.478 1.00 56.81 ? 224 ARG A O   1 
ATOM   1735 C  CB  . ARG A 1 229 ? 18.635 0.511  18.610 1.00 50.47 ? 224 ARG A CB  1 
ATOM   1736 C  CG  . ARG A 1 229 ? 19.014 0.139  17.193 1.00 55.14 ? 224 ARG A CG  1 
ATOM   1737 C  CD  . ARG A 1 229 ? 18.250 -1.098 16.682 1.00 62.86 ? 224 ARG A CD  1 
ATOM   1738 N  NE  . ARG A 1 229 ? 16.922 -0.746 16.185 1.00 64.63 ? 224 ARG A NE  1 
ATOM   1739 C  CZ  . ARG A 1 229 ? 16.197 -1.501 15.369 1.00 68.94 ? 224 ARG A CZ  1 
ATOM   1740 N  NH1 . ARG A 1 229 ? 16.640 -2.674 14.936 1.00 63.75 ? 224 ARG A NH1 1 
ATOM   1741 N  NH2 . ARG A 1 229 ? 15.004 -1.063 14.964 1.00 69.71 ? 224 ARG A NH2 1 
ATOM   1742 N  N   . ASP A 1 230 ? 17.977 2.334  21.094 1.00 52.17 ? 225 ASP A N   1 
ATOM   1743 C  CA  . ASP A 1 230 ? 17.549 2.434  22.486 1.00 51.77 ? 225 ASP A CA  1 
ATOM   1744 C  C   . ASP A 1 230 ? 16.276 3.261  22.606 1.00 52.57 ? 225 ASP A C   1 
ATOM   1745 O  O   . ASP A 1 230 ? 15.343 2.876  23.320 1.00 54.71 ? 225 ASP A O   1 
ATOM   1746 C  CB  . ASP A 1 230 ? 18.671 3.029  23.337 1.00 47.70 ? 225 ASP A CB  1 
ATOM   1747 C  CG  . ASP A 1 230 ? 19.922 2.153  23.366 1.00 49.43 ? 225 ASP A CG  1 
ATOM   1748 O  OD1 . ASP A 1 230 ? 19.831 0.950  23.034 1.00 53.23 ? 225 ASP A OD1 1 
ATOM   1749 O  OD2 . ASP A 1 230 ? 21.003 2.667  23.728 1.00 50.56 ? 225 ASP A OD2 1 
ATOM   1750 N  N   . ASN A 1 231 ? 16.212 4.393  21.898 1.00 49.29 ? 226 ASN A N   1 
ATOM   1751 C  CA  . ASN A 1 231 ? 15.027 5.246  21.949 1.00 52.12 ? 226 ASN A CA  1 
ATOM   1752 C  C   . ASN A 1 231 ? 13.803 4.532  21.384 1.00 57.35 ? 226 ASN A C   1 
ATOM   1753 O  O   . ASN A 1 231 ? 12.691 4.682  21.904 1.00 58.97 ? 226 ASN A O   1 
ATOM   1754 C  CB  . ASN A 1 231 ? 15.283 6.552  21.190 1.00 49.01 ? 226 ASN A CB  1 
ATOM   1755 C  CG  . ASN A 1 231 ? 16.007 7.596  22.039 1.00 49.67 ? 226 ASN A CG  1 
ATOM   1756 O  OD1 . ASN A 1 231 ? 16.161 7.429  23.253 1.00 50.34 ? 226 ASN A OD1 1 
ATOM   1757 N  ND2 . ASN A 1 231 ? 16.460 8.671  21.401 1.00 46.50 ? 226 ASN A ND2 1 
ATOM   1758 N  N   . LEU A 1 232 ? 13.980 3.758  20.311 1.00 54.04 ? 227 LEU A N   1 
ATOM   1759 C  CA  . LEU A 1 232 ? 12.848 3.019  19.762 1.00 57.50 ? 227 LEU A CA  1 
ATOM   1760 C  C   . LEU A 1 232 ? 12.333 1.983  20.754 1.00 58.10 ? 227 LEU A C   1 
ATOM   1761 O  O   . LEU A 1 232 ? 11.118 1.829  20.916 1.00 62.49 ? 227 LEU A O   1 
ATOM   1762 C  CB  . LEU A 1 232 ? 13.242 2.377  18.434 1.00 53.38 ? 227 LEU A CB  1 
ATOM   1763 C  CG  . LEU A 1 232 ? 13.419 3.491  17.396 1.00 50.88 ? 227 LEU A CG  1 
ATOM   1764 C  CD1 . LEU A 1 232 ? 14.390 3.095  16.306 1.00 52.81 ? 227 LEU A CD1 1 
ATOM   1765 C  CD2 . LEU A 1 232 ? 12.077 3.928  16.827 1.00 48.13 ? 227 LEU A CD2 1 
ATOM   1766 N  N   . THR A 1 233 ? 13.242 1.281  21.445 1.00 56.88 ? 228 THR A N   1 
ATOM   1767 C  CA  . THR A 1 233 ? 12.835 0.323  22.474 1.00 60.86 ? 228 THR A CA  1 
ATOM   1768 C  C   . THR A 1 233 ? 12.101 1.008  23.626 1.00 65.60 ? 228 THR A C   1 
ATOM   1769 O  O   . THR A 1 233 ? 11.104 0.483  24.141 1.00 67.42 ? 228 THR A O   1 
ATOM   1770 C  CB  . THR A 1 233 ? 14.057 -0.432 23.002 1.00 61.76 ? 228 THR A CB  1 
ATOM   1771 O  OG1 . THR A 1 233 ? 14.734 -1.079 21.917 1.00 63.90 ? 228 THR A OG1 1 
ATOM   1772 C  CG2 . THR A 1 233 ? 13.654 -1.467 24.041 1.00 60.03 ? 228 THR A CG2 1 
ATOM   1773 N  N   . LEU A 1 234 ? 12.598 2.164  24.068 1.00 63.27 ? 229 LEU A N   1 
ATOM   1774 C  CA  . LEU A 1 234 ? 11.860 2.954  25.046 1.00 62.09 ? 229 LEU A CA  1 
ATOM   1775 C  C   . LEU A 1 234 ? 10.460 3.284  24.537 1.00 65.19 ? 229 LEU A C   1 
ATOM   1776 O  O   . LEU A 1 234 ? 9.465  3.100  25.247 1.00 68.97 ? 229 LEU A O   1 
ATOM   1777 C  CB  . LEU A 1 234 ? 12.625 4.238  25.369 1.00 63.55 ? 229 LEU A CB  1 
ATOM   1778 C  CG  . LEU A 1 234 ? 12.913 4.525  26.838 1.00 65.71 ? 229 LEU A CG  1 
ATOM   1779 C  CD1 . LEU A 1 234 ? 13.272 6.004  27.008 1.00 64.19 ? 229 LEU A CD1 1 
ATOM   1780 C  CD2 . LEU A 1 234 ? 11.706 4.154  27.673 1.00 61.87 ? 229 LEU A CD2 1 
ATOM   1781 N  N   . TRP A 1 235 ? 10.363 3.759  23.299 1.00 59.35 ? 230 TRP A N   1 
ATOM   1782 C  CA  . TRP A 1 235 ? 9.108  4.262  22.759 1.00 61.09 ? 230 TRP A CA  1 
ATOM   1783 C  C   . TRP A 1 235 ? 8.196  3.165  22.210 1.00 65.28 ? 230 TRP A C   1 
ATOM   1784 O  O   . TRP A 1 235 ? 7.107  3.483  21.721 1.00 64.10 ? 230 TRP A O   1 
ATOM   1785 C  CB  . TRP A 1 235 ? 9.396  5.288  21.658 1.00 62.64 ? 230 TRP A CB  1 
ATOM   1786 C  CG  . TRP A 1 235 ? 10.294 6.424  22.079 1.00 63.25 ? 230 TRP A CG  1 
ATOM   1787 C  CD1 . TRP A 1 235 ? 10.622 6.784  23.358 1.00 57.93 ? 230 TRP A CD1 1 
ATOM   1788 C  CD2 . TRP A 1 235 ? 10.998 7.329  21.213 1.00 56.02 ? 230 TRP A CD2 1 
ATOM   1789 N  NE1 . TRP A 1 235 ? 11.471 7.868  23.341 1.00 58.86 ? 230 TRP A NE1 1 
ATOM   1790 C  CE2 . TRP A 1 235 ? 11.720 8.219  22.037 1.00 55.90 ? 230 TRP A CE2 1 
ATOM   1791 C  CE3 . TRP A 1 235 ? 11.085 7.473  19.821 1.00 59.52 ? 230 TRP A CE3 1 
ATOM   1792 C  CZ2 . TRP A 1 235 ? 12.513 9.245  21.518 1.00 54.12 ? 230 TRP A CZ2 1 
ATOM   1793 C  CZ3 . TRP A 1 235 ? 11.876 8.491  19.304 1.00 59.57 ? 230 TRP A CZ3 1 
ATOM   1794 C  CH2 . TRP A 1 235 ? 12.580 9.367  20.156 1.00 54.87 ? 230 TRP A CH2 1 
ATOM   1795 N  N   . THR A 1 236 ? 8.606  1.899  22.259 1.00 66.52 ? 231 THR A N   1 
ATOM   1796 C  CA  . THR A 1 236 ? 7.734  0.796  21.853 1.00 66.58 ? 231 THR A CA  1 
ATOM   1797 C  C   . THR A 1 236 ? 7.589  -0.222 22.986 1.00 67.67 ? 231 THR A C   1 
ATOM   1798 O  O   . THR A 1 236 ? 6.522  -0.810 23.157 1.00 73.39 ? 231 THR A O   1 
ATOM   1799 C  CB  . THR A 1 236 ? 8.250  0.075  20.583 1.00 68.14 ? 231 THR A CB  1 
ATOM   1800 O  OG1 . THR A 1 236 ? 9.515  -0.547 20.846 1.00 68.60 ? 231 THR A OG1 1 
ATOM   1801 C  CG2 . THR A 1 236 ? 8.389  1.049  19.425 1.00 61.78 ? 231 THR A CG2 1 
ATOM   1802 O  OXT . THR A 1 236 ? 8.515  -0.478 23.765 1.00 70.60 ? 231 THR A OXT 1 
ATOM   1803 N  N   . GLN B 2 1   ? 13.215 6.947  33.127 1.00 81.68 ? 255 GLN P N   1 
ATOM   1804 C  CA  . GLN B 2 1   ? 13.897 6.735  31.852 1.00 73.90 ? 255 GLN P CA  1 
ATOM   1805 C  C   . GLN B 2 1   ? 13.511 7.811  30.859 1.00 74.68 ? 255 GLN P C   1 
ATOM   1806 O  O   . GLN B 2 1   ? 12.368 7.875  30.401 1.00 77.16 ? 255 GLN P O   1 
ATOM   1807 C  CB  . GLN B 2 1   ? 13.569 5.359  31.280 1.00 73.53 ? 255 GLN P CB  1 
ATOM   1808 C  CG  . GLN B 2 1   ? 14.643 4.782  30.363 1.00 72.89 ? 255 GLN P CG  1 
ATOM   1809 C  CD  . GLN B 2 1   ? 14.650 3.258  30.378 1.00 78.25 ? 255 GLN P CD  1 
ATOM   1810 O  OE1 . GLN B 2 1   ? 13.873 2.630  31.103 1.00 74.77 ? 255 GLN P OE1 1 
ATOM   1811 N  NE2 . GLN B 2 1   ? 15.526 2.658  29.573 1.00 77.32 ? 255 GLN P NE2 1 
ATOM   1812 N  N   . ARG B 2 2   ? 14.477 8.654  30.526 1.00 71.17 ? 256 ARG P N   1 
ATOM   1813 C  CA  . ARG B 2 2   ? 14.288 9.749  29.591 1.00 67.79 ? 256 ARG P CA  1 
ATOM   1814 C  C   . ARG B 2 2   ? 14.907 9.404  28.236 1.00 60.03 ? 256 ARG P C   1 
ATOM   1815 O  O   . ARG B 2 2   ? 15.741 8.502  28.120 1.00 59.98 ? 256 ARG P O   1 
ATOM   1816 C  CB  . ARG B 2 2   ? 14.908 11.027 30.159 1.00 64.48 ? 256 ARG P CB  1 
ATOM   1817 C  CG  . ARG B 2 2   ? 14.360 12.292 29.572 1.00 63.43 ? 256 ARG P CG  1 
ATOM   1818 C  CD  . ARG B 2 2   ? 15.382 12.921 28.652 1.00 63.69 ? 256 ARG P CD  1 
ATOM   1819 N  NE  . ARG B 2 2   ? 14.737 13.878 27.766 1.00 65.81 ? 256 ARG P NE  1 
ATOM   1820 C  CZ  . ARG B 2 2   ? 15.298 14.434 26.702 1.00 57.56 ? 256 ARG P CZ  1 
ATOM   1821 N  NH1 . ARG B 2 2   ? 16.553 14.161 26.352 1.00 51.66 ? 256 ARG P NH1 1 
ATOM   1822 N  NH2 . ARG B 2 2   ? 14.589 15.296 25.982 1.00 53.97 ? 256 ARG P NH2 1 
ATOM   1823 N  N   . SER B 2 3   ? 14.471 10.125 27.203 1.00 62.04 ? 257 SER P N   1 
ATOM   1824 C  CA  . SER B 2 3   ? 15.015 9.903  25.865 1.00 57.85 ? 257 SER P CA  1 
ATOM   1825 C  C   . SER B 2 3   ? 16.494 10.267 25.835 1.00 55.45 ? 257 SER P C   1 
ATOM   1826 O  O   . SER B 2 3   ? 16.933 11.215 26.493 1.00 49.93 ? 257 SER P O   1 
ATOM   1827 C  CB  . SER B 2 3   ? 14.257 10.734 24.828 1.00 53.65 ? 257 SER P CB  1 
ATOM   1828 O  OG  . SER B 2 3   ? 12.924 10.292 24.666 1.00 54.36 ? 257 SER P OG  1 
ATOM   1829 N  N   . THR B 2 4   ? 17.265 9.508  25.068 1.00 50.30 ? 258 THR P N   1 
ATOM   1830 C  CA  . THR B 2 4   ? 18.690 9.793  24.929 1.00 49.41 ? 258 THR P CA  1 
ATOM   1831 C  C   . THR B 2 4   ? 18.981 10.650 23.695 1.00 46.99 ? 258 THR P C   1 
ATOM   1832 O  O   . THR B 2 4   ? 18.642 10.271 22.570 1.00 45.11 ? 258 THR P O   1 
ATOM   1833 C  CB  . THR B 2 4   ? 19.497 8.501  24.836 1.00 45.23 ? 258 THR P CB  1 
ATOM   1834 O  OG1 . THR B 2 4   ? 19.111 7.640  25.910 1.00 52.19 ? 258 THR P OG1 1 
ATOM   1835 C  CG2 . THR B 2 4   ? 20.979 8.793  24.955 1.00 43.84 ? 258 THR P CG2 1 
HETATM 1836 N  N   . SEP B 2 5   ? 19.621 11.793 23.903 1.00 40.22 ? 259 SEP P N   1 
HETATM 1837 C  CA  . SEP B 2 5   ? 20.057 12.645 22.793 1.00 41.37 ? 259 SEP P CA  1 
HETATM 1838 C  CB  . SEP B 2 5   ? 19.810 14.135 23.103 1.00 39.99 ? 259 SEP P CB  1 
HETATM 1839 O  OG  . SEP B 2 5   ? 20.487 14.476 24.305 1.00 44.67 ? 259 SEP P OG  1 
HETATM 1840 C  C   . SEP B 2 5   ? 21.533 12.395 22.528 1.00 41.35 ? 259 SEP P C   1 
HETATM 1841 O  O   . SEP B 2 5   ? 22.154 11.554 23.184 1.00 39.26 ? 259 SEP P O   1 
HETATM 1842 P  P   . SEP B 2 5   ? 20.295 15.981 24.853 1.00 42.57 ? 259 SEP P P   1 
HETATM 1843 O  O1P . SEP B 2 5   ? 20.723 17.055 23.734 1.00 38.40 ? 259 SEP P O1P 1 
HETATM 1844 O  O2P . SEP B 2 5   ? 18.773 16.186 25.294 1.00 42.59 ? 259 SEP P O2P 1 
HETATM 1845 O  O3P . SEP B 2 5   ? 21.316 16.076 26.077 1.00 42.16 ? 259 SEP P O3P 1 
ATOM   1846 N  N   . THR B 2 6   ? 22.104 13.135 21.584 1.00 37.79 ? 260 THR P N   1 
ATOM   1847 C  CA  . THR B 2 6   ? 23.516 12.981 21.260 1.00 38.73 ? 260 THR P CA  1 
ATOM   1848 C  C   . THR B 2 6   ? 24.414 13.240 22.474 1.00 45.90 ? 260 THR P C   1 
ATOM   1849 O  O   . THR B 2 6   ? 24.223 14.236 23.172 1.00 41.07 ? 260 THR P O   1 
ATOM   1850 C  CB  . THR B 2 6   ? 23.916 13.913 20.119 1.00 46.46 ? 260 THR P CB  1 
ATOM   1851 O  OG1 . THR B 2 6   ? 23.308 13.463 18.892 1.00 43.70 ? 260 THR P OG1 1 
ATOM   1852 C  CG2 . THR B 2 6   ? 25.397 13.905 19.959 1.00 46.10 ? 260 THR P CG2 1 
ATOM   1853 N  N   . PRO B 2 7   ? 25.361 12.337 22.735 1.00 45.95 ? 261 PRO P N   1 
ATOM   1854 C  CA  . PRO B 2 7   ? 26.285 12.503 23.857 1.00 46.88 ? 261 PRO P CA  1 
ATOM   1855 C  C   . PRO B 2 7   ? 27.533 13.297 23.476 1.00 47.52 ? 261 PRO P C   1 
ATOM   1856 O  O   . PRO B 2 7   ? 27.759 13.630 22.315 1.00 41.07 ? 261 PRO P O   1 
ATOM   1857 C  CB  . PRO B 2 7   ? 26.661 11.056 24.195 1.00 42.92 ? 261 PRO P CB  1 
ATOM   1858 C  CG  . PRO B 2 7   ? 26.682 10.387 22.831 1.00 42.14 ? 261 PRO P CG  1 
ATOM   1859 C  CD  . PRO B 2 7   ? 25.546 11.034 22.060 1.00 43.27 ? 261 PRO P CD  1 
ATOM   1860 N  N   . ASN B 2 8   ? 28.354 13.586 24.494 1.00 50.37 ? 262 ASN P N   1 
ATOM   1861 C  CA  . ASN B 2 8   ? 29.672 14.175 24.272 1.00 48.26 ? 262 ASN P CA  1 
ATOM   1862 C  C   . ASN B 2 8   ? 30.726 13.103 24.023 1.00 53.52 ? 262 ASN P C   1 
ATOM   1863 O  O   . ASN B 2 8   ? 30.783 12.090 24.730 1.00 62.07 ? 262 ASN P O   1 
ATOM   1864 C  CB  . ASN B 2 8   ? 30.079 15.018 25.473 1.00 51.59 ? 262 ASN P CB  1 
ATOM   1865 C  CG  . ASN B 2 8   ? 29.301 16.297 25.541 1.00 49.31 ? 262 ASN P CG  1 
ATOM   1866 O  OD1 . ASN B 2 8   ? 29.400 17.142 24.654 1.00 44.06 ? 262 ASN P OD1 1 
ATOM   1867 N  ND2 . ASN B 2 8   ? 28.466 16.419 26.552 1.00 49.65 ? 262 ASN P ND2 1 
ATOM   1868 N  N   . VAL B 2 9   ? 31.584 13.348 23.038 1.00 53.17 ? 263 VAL P N   1 
ATOM   1869 C  CA  . VAL B 2 9   ? 32.629 12.409 22.654 1.00 58.32 ? 263 VAL P CA  1 
ATOM   1870 C  C   . VAL B 2 9   ? 33.871 13.198 22.267 1.00 60.28 ? 263 VAL P C   1 
ATOM   1871 O  O   . VAL B 2 9   ? 33.766 14.301 21.718 1.00 60.28 ? 263 VAL P O   1 
ATOM   1872 C  CB  . VAL B 2 9   ? 32.148 11.494 21.502 1.00 61.46 ? 263 VAL P CB  1 
ATOM   1873 C  CG1 . VAL B 2 9   ? 33.303 11.007 20.629 1.00 60.82 ? 263 VAL P CG1 1 
ATOM   1874 C  CG2 . VAL B 2 9   ? 31.362 10.324 22.065 1.00 59.02 ? 263 VAL P CG2 1 
ATOM   1875 N  N   . HIS B 2 10  ? 35.045 12.665 22.611 1.00 63.98 ? 264 HIS P N   1 
ATOM   1876 C  CA  . HIS B 2 10  ? 36.302 13.100 21.992 1.00 66.31 ? 264 HIS P CA  1 
ATOM   1877 C  C   . HIS B 2 10  ? 36.705 14.547 22.343 1.00 63.50 ? 264 HIS P C   1 
ATOM   1878 O  O   . HIS B 2 10  ? 37.577 15.142 21.704 1.00 62.38 ? 264 HIS P O   1 
ATOM   1879 C  CB  . HIS B 2 10  ? 36.187 12.940 20.468 1.00 66.34 ? 264 HIS P CB  1 
ATOM   1880 C  CG  . HIS B 2 10  ? 37.397 12.346 19.818 1.00 74.43 ? 264 HIS P CG  1 
ATOM   1881 N  ND1 . HIS B 2 10  ? 37.801 11.046 20.037 1.00 73.65 ? 264 HIS P ND1 1 
ATOM   1882 C  CD2 . HIS B 2 10  ? 38.279 12.872 18.933 1.00 76.94 ? 264 HIS P CD2 1 
ATOM   1883 C  CE1 . HIS B 2 10  ? 38.887 10.800 19.324 1.00 79.90 ? 264 HIS P CE1 1 
ATOM   1884 N  NE2 . HIS B 2 10  ? 39.198 11.891 18.645 1.00 78.13 ? 264 HIS P NE2 1 
ATOM   1885 O  OXT . HIS B 2 10  ? 36.190 15.172 23.276 1.00 60.00 ? 264 HIS P OXT 1 
HETATM 1886 CL CL  . CL  C 3 .   ? 17.769 31.832 45.218 1.00 49.24 ? 301 CL  A CL  1 
HETATM 1887 CL CL  . CL  D 3 .   ? 21.749 22.205 0.588  1.00 83.51 ? 302 CL  A CL  1 
HETATM 1888 MG MG  . MG  E 4 .   ? 44.069 35.981 17.241 1.00 52.49 ? 303 MG  A MG  1 
HETATM 1889 MG MG  . MG  F 4 .   ? 10.114 31.130 36.592 1.00 75.87 ? 304 MG  A MG  1 
HETATM 1890 MG MG  . MG  G 4 .   ? 1.426  19.890 51.697 1.00 88.89 ? 305 MG  A MG  1 
HETATM 1891 C  C1  . WPN H 5 .   ? 32.873 18.490 12.896 1.00 50.51 ? 306 WPN A C1  1 
HETATM 1892 C  C2  . WPN H 5 .   ? 33.950 17.554 12.361 1.00 53.16 ? 306 WPN A C2  1 
HETATM 1893 C  C3  . WPN H 5 .   ? 32.769 17.654 15.231 1.00 53.27 ? 306 WPN A C3  1 
HETATM 1894 C  C4  . WPN H 5 .   ? 31.314 17.575 15.669 1.00 47.97 ? 306 WPN A C4  1 
HETATM 1895 C  C5  . WPN H 5 .   ? 30.491 16.749 14.688 1.00 42.35 ? 306 WPN A C5  1 
HETATM 1896 C  C6  . WPN H 5 .   ? 29.507 15.847 15.404 1.00 47.98 ? 306 WPN A C6  1 
HETATM 1897 C  C10 . WPN H 5 .   ? 28.485 11.862 18.472 1.00 47.16 ? 306 WPN A C10 1 
HETATM 1898 C  C11 . WPN H 5 .   ? 28.746 12.964 19.261 1.00 42.97 ? 306 WPN A C11 1 
HETATM 1899 C  C14 . WPN H 5 .   ? 31.116 17.125 17.097 1.00 49.73 ? 306 WPN A C14 1 
HETATM 1900 C  C12 . WPN H 5 .   ? 28.421 14.217 18.784 1.00 44.00 ? 306 WPN A C12 1 
HETATM 1901 C  C13 . WPN H 5 .   ? 29.657 17.205 17.490 1.00 50.17 ? 306 WPN A C13 1 
HETATM 1902 C  C7  . WPN H 5 .   ? 27.800 14.354 17.559 1.00 41.68 ? 306 WPN A C7  1 
HETATM 1903 C  C8  . WPN H 5 .   ? 27.557 13.248 16.769 1.00 40.35 ? 306 WPN A C8  1 
HETATM 1904 C  C9  . WPN H 5 .   ? 27.897 11.990 17.228 1.00 42.21 ? 306 WPN A C9  1 
HETATM 1905 N  N1  . WPN H 5 .   ? 32.553 18.624 14.181 1.00 50.53 ? 306 WPN A N1  1 
HETATM 1906 N  N2  . WPN H 5 .   ? 28.794 16.607 16.450 1.00 47.50 ? 306 WPN A N2  1 
HETATM 1907 O  O1  . WPN H 5 .   ? 32.371 19.240 12.077 1.00 45.88 ? 306 WPN A O1  1 
HETATM 1908 O  O2  . WPN H 5 .   ? 26.977 16.751 18.096 1.00 48.60 ? 306 WPN A O2  1 
HETATM 1909 O  O3  . WPN H 5 .   ? 26.538 15.832 15.843 1.00 45.15 ? 306 WPN A O3  1 
HETATM 1910 S  S1  . WPN H 5 .   ? 27.396 15.957 16.980 1.00 46.86 ? 306 WPN A S1  1 
HETATM 1911 BR BR1 . WPN H 5 .   ? 28.951 10.138 19.126 1.00 64.94 ? 306 WPN A BR1 1 
HETATM 1912 MG MG  . MG  I 4 .   ? 40.082 41.631 20.270 1.00 62.16 ? 307 MG  A MG  1 
HETATM 1913 O  O   . HOH J 6 .   ? 6.761  31.069 27.782 1.00 71.94 ? 401 HOH A O   1 
HETATM 1914 O  O   . HOH J 6 .   ? 10.923 20.641 30.850 1.00 57.58 ? 402 HOH A O   1 
HETATM 1915 O  O   . HOH J 6 .   ? 32.387 7.751  19.516 1.00 49.78 ? 403 HOH A O   1 
HETATM 1916 O  O   . HOH J 6 .   ? 14.196 -1.352 12.603 1.00 61.80 ? 404 HOH A O   1 
HETATM 1917 O  O   . HOH J 6 .   ? 19.106 15.016 34.070 1.00 62.73 ? 405 HOH A O   1 
HETATM 1918 O  O   . HOH J 6 .   ? 30.989 29.612 10.489 1.00 48.97 ? 406 HOH A O   1 
HETATM 1919 O  O   . HOH J 6 .   ? 41.179 18.254 20.596 1.00 52.25 ? 407 HOH A O   1 
HETATM 1920 O  O   . HOH J 6 .   ? 46.457 19.633 25.753 1.00 57.46 ? 408 HOH A O   1 
HETATM 1921 O  O   . HOH J 6 .   ? 42.664 21.810 16.851 1.00 54.05 ? 409 HOH A O   1 
HETATM 1922 O  O   . HOH J 6 .   ? 37.487 32.144 14.716 1.00 40.11 ? 410 HOH A O   1 
HETATM 1923 O  O   . HOH J 6 .   ? 42.780 3.338  5.405  1.00 51.87 ? 411 HOH A O   1 
HETATM 1924 O  O   . HOH J 6 .   ? 17.881 -0.963 6.567  1.00 45.40 ? 412 HOH A O   1 
HETATM 1925 O  O   . HOH J 6 .   ? 43.334 24.779 15.862 1.00 42.12 ? 413 HOH A O   1 
HETATM 1926 O  O   . HOH J 6 .   ? 31.422 7.887  3.598  1.00 42.95 ? 414 HOH A O   1 
HETATM 1927 O  O   . HOH J 6 .   ? 36.348 38.125 22.991 1.00 50.20 ? 415 HOH A O   1 
HETATM 1928 O  O   . HOH J 6 .   ? 41.806 21.975 13.953 1.00 51.42 ? 416 HOH A O   1 
HETATM 1929 O  O   . HOH J 6 .   ? 25.046 -1.064 2.562  1.00 42.40 ? 417 HOH A O   1 
HETATM 1930 O  O   . HOH J 6 .   ? 41.865 38.781 26.842 1.00 57.56 ? 418 HOH A O   1 
HETATM 1931 O  O   . HOH J 6 .   ? 15.637 19.678 31.145 1.00 48.33 ? 419 HOH A O   1 
HETATM 1932 O  O   . HOH J 6 .   ? 29.155 17.397 21.848 1.00 44.37 ? 420 HOH A O   1 
HETATM 1933 O  O   . HOH J 6 .   ? 37.873 6.141  13.591 1.00 49.32 ? 421 HOH A O   1 
HETATM 1934 O  O   . HOH J 6 .   ? 10.186 31.120 54.366 1.00 49.34 ? 422 HOH A O   1 
HETATM 1935 O  O   . HOH J 6 .   ? 41.898 18.356 25.677 1.00 40.61 ? 423 HOH A O   1 
HETATM 1936 O  O   . HOH J 6 .   ? 36.710 -0.366 16.450 1.00 41.35 ? 424 HOH A O   1 
HETATM 1937 O  O   . HOH J 6 .   ? 18.469 15.858 37.361 1.00 47.37 ? 425 HOH A O   1 
HETATM 1938 O  O   . HOH J 6 .   ? 8.962  23.658 38.090 1.00 58.71 ? 426 HOH A O   1 
HETATM 1939 O  O   . HOH J 6 .   ? 8.308  27.165 46.604 1.00 47.12 ? 427 HOH A O   1 
HETATM 1940 O  O   . HOH J 6 .   ? 9.977  27.078 34.021 1.00 49.58 ? 428 HOH A O   1 
HETATM 1941 O  O   . HOH J 6 .   ? 29.935 37.866 20.602 1.00 67.49 ? 429 HOH A O   1 
HETATM 1942 O  O   . HOH J 6 .   ? 18.283 9.033  6.971  1.00 45.03 ? 430 HOH A O   1 
HETATM 1943 O  O   . HOH J 6 .   ? 17.371 -2.026 9.641  1.00 65.32 ? 431 HOH A O   1 
HETATM 1944 O  O   . HOH J 6 .   ? 30.643 31.362 27.905 1.00 44.91 ? 432 HOH A O   1 
HETATM 1945 O  O   . HOH J 6 .   ? 16.894 5.800  25.249 1.00 55.99 ? 433 HOH A O   1 
HETATM 1946 O  O   . HOH J 6 .   ? 9.383  35.056 45.939 1.00 49.35 ? 434 HOH A O   1 
HETATM 1947 O  O   . HOH J 6 .   ? 16.707 22.854 29.656 1.00 40.18 ? 435 HOH A O   1 
HETATM 1948 O  O   . HOH J 6 .   ? 31.138 7.466  9.872  1.00 36.28 ? 436 HOH A O   1 
HETATM 1949 O  O   . HOH J 6 .   ? 23.454 27.865 6.518  1.00 59.79 ? 437 HOH A O   1 
HETATM 1950 O  O   . HOH J 6 .   ? 10.015 26.200 49.467 1.00 49.83 ? 438 HOH A O   1 
HETATM 1951 O  O   . HOH J 6 .   ? 34.821 34.261 26.628 1.00 39.41 ? 439 HOH A O   1 
HETATM 1952 O  O   . HOH J 6 .   ? 26.921 23.456 34.785 1.00 44.96 ? 440 HOH A O   1 
HETATM 1953 O  O   . HOH J 6 .   ? 23.111 0.000  0.000  0.50 36.64 ? 441 HOH A O   1 
HETATM 1954 O  O   . HOH J 6 .   ? 19.645 14.287 9.340  1.00 46.44 ? 442 HOH A O   1 
HETATM 1955 O  O   . HOH J 6 .   ? 16.634 10.484 8.656  1.00 50.63 ? 443 HOH A O   1 
HETATM 1956 O  O   . HOH J 6 .   ? 46.127 23.551 20.135 1.00 44.27 ? 444 HOH A O   1 
HETATM 1957 O  O   . HOH J 6 .   ? 13.212 29.395 28.161 1.00 49.04 ? 445 HOH A O   1 
HETATM 1958 O  O   . HOH J 6 .   ? 32.645 15.647 28.399 1.00 56.20 ? 446 HOH A O   1 
HETATM 1959 O  O   . HOH J 6 .   ? 38.152 37.102 20.916 1.00 44.19 ? 447 HOH A O   1 
HETATM 1960 O  O   . HOH J 6 .   ? 46.460 26.124 19.035 1.00 39.00 ? 448 HOH A O   1 
HETATM 1961 O  O   . HOH J 6 .   ? 20.317 7.664  8.199  1.00 43.74 ? 449 HOH A O   1 
HETATM 1962 O  O   . HOH J 6 .   ? 31.558 13.058 15.584 1.00 49.01 ? 450 HOH A O   1 
HETATM 1963 O  O   . HOH J 6 .   ? 31.734 29.907 30.194 1.00 41.42 ? 451 HOH A O   1 
HETATM 1964 O  O   . HOH J 6 .   ? 12.232 14.697 44.126 1.00 60.11 ? 452 HOH A O   1 
HETATM 1965 O  O   . HOH J 6 .   ? 32.973 27.305 11.006 1.00 50.07 ? 453 HOH A O   1 
HETATM 1966 O  O   . HOH J 6 .   ? 32.768 11.608 8.866  1.00 45.40 ? 454 HOH A O   1 
HETATM 1967 O  O   . HOH J 6 .   ? 19.892 4.949  3.147  1.00 48.27 ? 455 HOH A O   1 
HETATM 1968 O  O   . HOH J 6 .   ? 49.692 31.511 20.214 1.00 46.38 ? 456 HOH A O   1 
HETATM 1969 O  O   . HOH J 6 .   ? 40.021 17.695 37.235 1.00 50.14 ? 457 HOH A O   1 
HETATM 1970 O  O   . HOH J 6 .   ? 26.831 35.344 22.414 1.00 46.17 ? 458 HOH A O   1 
HETATM 1971 O  O   . HOH J 6 .   ? 24.375 32.225 32.595 1.00 42.59 ? 459 HOH A O   1 
HETATM 1972 O  O   . HOH J 6 .   ? 23.362 35.688 28.014 1.00 51.13 ? 460 HOH A O   1 
HETATM 1973 O  O   . HOH J 6 .   ? 31.034 2.848  18.959 1.00 47.45 ? 461 HOH A O   1 
HETATM 1974 O  O   . HOH J 6 .   ? 32.866 13.968 18.156 1.00 54.24 ? 462 HOH A O   1 
HETATM 1975 O  O   . HOH J 6 .   ? 46.819 22.409 24.591 1.00 47.77 ? 463 HOH A O   1 
HETATM 1976 O  O   . HOH J 6 .   ? 46.641 32.876 16.830 1.00 42.37 ? 464 HOH A O   1 
HETATM 1977 O  O   . HOH J 6 .   ? 38.084 20.599 9.645  1.00 44.58 ? 465 HOH A O   1 
HETATM 1978 O  O   . HOH J 6 .   ? 26.337 20.957 19.976 1.00 41.36 ? 466 HOH A O   1 
HETATM 1979 O  O   . HOH J 6 .   ? 3.860  37.923 24.917 1.00 60.72 ? 467 HOH A O   1 
HETATM 1980 O  O   . HOH J 6 .   ? 40.985 26.578 12.347 1.00 43.87 ? 468 HOH A O   1 
HETATM 1981 O  O   . HOH J 6 .   ? 24.198 19.502 38.294 1.00 63.45 ? 469 HOH A O   1 
HETATM 1982 O  O   . HOH J 6 .   ? 35.494 15.981 27.154 1.00 50.06 ? 470 HOH A O   1 
HETATM 1983 O  O   . HOH J 6 .   ? 18.678 12.392 7.790  1.00 49.41 ? 471 HOH A O   1 
HETATM 1984 O  O   . HOH J 6 .   ? 39.917 19.459 12.516 1.00 44.11 ? 472 HOH A O   1 
HETATM 1985 O  O   . HOH J 6 .   ? 30.009 8.298  7.560  1.00 38.83 ? 473 HOH A O   1 
HETATM 1986 O  O   . HOH J 6 .   ? 38.275 18.207 19.726 1.00 39.43 ? 474 HOH A O   1 
HETATM 1987 O  O   . HOH J 6 .   ? 36.373 21.369 37.643 1.00 49.94 ? 475 HOH A O   1 
HETATM 1988 O  O   . HOH J 6 .   ? 37.054 23.432 39.295 1.00 41.96 ? 476 HOH A O   1 
HETATM 1989 O  O   . HOH J 6 .   ? 44.180 29.443 15.988 1.00 39.79 ? 477 HOH A O   1 
HETATM 1990 O  O   . HOH J 6 .   ? 38.114 31.708 8.278  1.00 53.21 ? 478 HOH A O   1 
HETATM 1991 O  O   . HOH J 6 .   ? 42.461 5.703  9.000  1.00 59.59 ? 479 HOH A O   1 
HETATM 1992 O  O   . HOH J 6 .   ? 20.299 33.560 45.578 1.00 50.78 ? 480 HOH A O   1 
HETATM 1993 O  O   . HOH J 6 .   ? 35.763 25.898 34.620 1.00 37.59 ? 481 HOH A O   1 
HETATM 1994 O  O   . HOH J 6 .   ? 36.245 43.234 27.588 1.00 56.70 ? 482 HOH A O   1 
HETATM 1995 O  O   . HOH J 6 .   ? 24.392 19.649 21.673 1.00 46.43 ? 483 HOH A O   1 
HETATM 1996 O  O   . HOH J 6 .   ? 34.766 36.741 25.395 1.00 51.06 ? 484 HOH A O   1 
HETATM 1997 O  O   . HOH J 6 .   ? 15.909 32.503 14.571 1.00 62.98 ? 485 HOH A O   1 
HETATM 1998 O  O   . HOH J 6 .   ? 10.727 14.928 11.015 1.00 53.70 ? 486 HOH A O   1 
HETATM 1999 O  O   . HOH J 6 .   ? 35.871 6.463  14.654 1.00 42.84 ? 487 HOH A O   1 
HETATM 2000 O  O   . HOH J 6 .   ? 49.250 32.505 17.302 1.00 50.46 ? 488 HOH A O   1 
HETATM 2001 O  O   . HOH J 6 .   ? 33.092 26.032 8.764  1.00 51.03 ? 489 HOH A O   1 
HETATM 2002 O  O   . HOH J 6 .   ? 30.722 10.774 6.437  1.00 42.63 ? 490 HOH A O   1 
HETATM 2003 O  O   . HOH J 6 .   ? 14.198 15.568 43.105 1.00 57.25 ? 491 HOH A O   1 
HETATM 2004 O  O   . HOH J 6 .   ? 35.066 28.020 36.185 1.00 50.92 ? 492 HOH A O   1 
HETATM 2005 O  O   . HOH J 6 .   ? 25.944 33.122 30.273 1.00 55.94 ? 493 HOH A O   1 
HETATM 2006 O  O   . HOH J 6 .   ? 27.748 36.497 20.305 1.00 49.34 ? 494 HOH A O   1 
HETATM 2007 O  O   . HOH J 6 .   ? 19.319 7.677  1.890  1.00 60.03 ? 495 HOH A O   1 
HETATM 2008 O  O   . HOH J 6 .   ? 38.260 39.430 19.471 1.00 47.39 ? 496 HOH A O   1 
HETATM 2009 O  O   . HOH J 6 .   ? 16.068 22.084 32.155 1.00 43.23 ? 497 HOH A O   1 
HETATM 2010 O  O   . HOH J 6 .   ? 16.008 14.559 38.450 1.00 56.48 ? 498 HOH A O   1 
HETATM 2011 O  O   . HOH J 6 .   ? 16.929 34.223 43.621 1.00 53.83 ? 499 HOH A O   1 
HETATM 2012 O  O   . HOH J 6 .   ? 28.039 31.429 29.142 1.00 46.26 ? 500 HOH A O   1 
HETATM 2013 O  O   . HOH J 6 .   ? 28.016 29.417 33.247 1.00 45.40 ? 501 HOH A O   1 
HETATM 2014 O  O   . HOH J 6 .   ? 46.507 35.407 16.142 1.00 59.49 ? 502 HOH A O   1 
HETATM 2015 O  O   . HOH J 6 .   ? 45.618 31.415 14.582 1.00 48.79 ? 503 HOH A O   1 
HETATM 2016 O  O   . HOH J 6 .   ? 47.382 22.273 22.184 1.00 56.08 ? 504 HOH A O   1 
HETATM 2017 O  O   . HOH J 6 .   ? 45.238 26.884 16.835 1.00 48.83 ? 505 HOH A O   1 
HETATM 2018 O  O   . HOH J 6 .   ? 15.232 14.116 40.816 1.00 61.56 ? 506 HOH A O   1 
HETATM 2019 O  O   . HOH J 6 .   ? 29.813 8.099  1.048  1.00 53.28 ? 507 HOH A O   1 
HETATM 2020 O  O   . HOH J 6 .   ? 27.892 1.787  21.424 1.00 57.58 ? 508 HOH A O   1 
HETATM 2021 O  O   . HOH J 6 .   ? 29.160 29.337 30.854 1.00 48.70 ? 509 HOH A O   1 
HETATM 2022 O  O   . HOH J 6 .   ? 3.473  19.016 52.512 1.00 66.12 ? 510 HOH A O   1 
HETATM 2023 O  O   . HOH K 6 .   ? 14.739 17.404 25.043 1.00 46.88 ? 301 HOH P O   1 
HETATM 2024 O  O   . HOH K 6 .   ? 35.126 10.840 24.332 1.00 65.11 ? 302 HOH P O   1 
HETATM 2025 O  O   . HOH K 6 .   ? 22.725 16.367 22.267 1.00 42.97 ? 303 HOH P O   1 
HETATM 2026 O  O   . HOH K 6 .   ? 27.825 12.887 27.102 1.00 45.37 ? 304 HOH P O   1 
HETATM 2027 O  O   . HOH K 6 .   ? 23.203 11.340 25.863 1.00 43.53 ? 305 HOH P O   1 
HETATM 2028 O  O   . HOH K 6 .   ? 20.905 12.068 26.850 1.00 43.81 ? 306 HOH P O   1 
HETATM 2029 O  O   . HOH K 6 .   ? 26.494 7.528  24.920 1.00 47.52 ? 307 HOH P O   1 
# 
