data_9EW3
# 
_entry.id   9EW3 
# 
_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   9EW3         pdb_00009ew3 10.2210/pdb9ew3/pdb 
WWPDB D_1292136897 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-16 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EW3 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              michelle.arkin@ucsf.edu 
_pdbx_contact_author.name_first         Michelle 
_pdbx_contact_author.name_last          Arkin 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9366-6770 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Konstantinidou, M.' 1  ? 
'Vickery, H.'        2  ? 
'Pennings, M.A.M.'   3  ? 
'Virta, J.'          4  ? 
'Visser, E.J.'       5  ? 
'Oetelaar, M.C.M.'   6  ? 
'Overmans, M.'       7  ? 
'Neitz, J.'          8  ? 
'Ottmann, C.'        9  ? 
'Brunsveld, L.'      10 ? 
'Arkin, M.R.'        11 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Small molecule stabilization of the 14-3-3sigma/CRAF complex inhibits the MAPK pathway' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Konstantinidou, M.' 1  ? 
primary 'Vickery, H.'        2  ? 
primary 'Pennings, M.A.M.'   3  ? 
primary 'Virta, J.'          4  ? 
primary 'Visser, E.J.'       5  ? 
primary 'Oetelaar, M.C.M.'   6  ? 
primary 'Overmans, M.'       7  ? 
primary 'Neitz, J.'          8  ? 
primary 'Ottmann, C.'        9  ? 
primary 'Brunsveld, L.'      10 ? 
primary 'Arkin, M.R.'        11 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '14-3-3 protein sigma'                                                                   26542.914 1   ?        
? ? ? 
2 polymer     syn 'RAF proto-oncogene serine/threonine-protein kinase'                                     1070.028  1   2.7.11.1 
? ? ? 
3 non-polymer nat 'CHLORIDE ION'                                                                           35.453    1   ?        
? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                                                          24.305    3   ?        
? ? ? 
5 non-polymer syn '1-[8-(4-bromophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone' 423.710   1   ?        
? ? ? 
6 non-polymer nat 'CALCIUM ION'                                                                            40.078    1   ?        
? ? ? 
7 water       nat water                                                                                    18.015    267 ?        
? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Epithelial cell marker protein 1,Stratifin' 
2 'Proto-oncogene c-RAF,cRaf,Raf-1'            
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
A ? 
2 'polypeptide(L)' no yes 'QRST(SEP)TPNV' QRSTSTPNV P ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CHLORIDE ION'                                                                           CL  
4 'MAGNESIUM ION'                                                                          MG  
5 '1-[8-(4-bromophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone' WQN 
6 'CALCIUM ION'                                                                            CA  
7 water                                                                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   GLY n 
1 5   SER n 
1 6   MET n 
1 7   GLU n 
1 8   ARG n 
1 9   ALA n 
1 10  SER n 
1 11  LEU n 
1 12  ILE n 
1 13  GLN n 
1 14  LYS n 
1 15  ALA n 
1 16  LYS n 
1 17  LEU n 
1 18  ALA n 
1 19  GLU n 
1 20  GLN n 
1 21  ALA n 
1 22  GLU n 
1 23  ARG n 
1 24  TYR n 
1 25  GLU n 
1 26  ASP n 
1 27  MET n 
1 28  ALA n 
1 29  ALA n 
1 30  PHE n 
1 31  MET n 
1 32  LYS n 
1 33  GLY n 
1 34  ALA n 
1 35  VAL n 
1 36  GLU n 
1 37  LYS n 
1 38  GLY n 
1 39  GLU n 
1 40  GLU n 
1 41  LEU n 
1 42  SER n 
1 43  CYS n 
1 44  GLU n 
1 45  GLU n 
1 46  ARG n 
1 47  ASN n 
1 48  LEU n 
1 49  LEU n 
1 50  SER n 
1 51  VAL n 
1 52  ALA n 
1 53  TYR n 
1 54  LYS n 
1 55  ASN n 
1 56  VAL n 
1 57  VAL n 
1 58  GLY n 
1 59  GLY n 
1 60  GLN n 
1 61  ARG n 
1 62  ALA n 
1 63  ALA n 
1 64  TRP n 
1 65  ARG n 
1 66  VAL n 
1 67  LEU n 
1 68  SER n 
1 69  SER n 
1 70  ILE n 
1 71  GLU n 
1 72  GLN n 
1 73  LYS n 
1 74  SER n 
1 75  ASN n 
1 76  GLU n 
1 77  GLU n 
1 78  GLY n 
1 79  SER n 
1 80  GLU n 
1 81  GLU n 
1 82  LYS n 
1 83  GLY n 
1 84  PRO n 
1 85  GLU n 
1 86  VAL n 
1 87  ARG n 
1 88  GLU n 
1 89  TYR n 
1 90  ARG n 
1 91  GLU n 
1 92  LYS n 
1 93  VAL n 
1 94  GLU n 
1 95  THR n 
1 96  GLU n 
1 97  LEU n 
1 98  GLN n 
1 99  GLY n 
1 100 VAL n 
1 101 CYS n 
1 102 ASP n 
1 103 THR n 
1 104 VAL n 
1 105 LEU n 
1 106 GLY n 
1 107 LEU n 
1 108 LEU n 
1 109 ASP n 
1 110 SER n 
1 111 HIS n 
1 112 LEU n 
1 113 ILE n 
1 114 LYS n 
1 115 GLU n 
1 116 ALA n 
1 117 GLY n 
1 118 ASP n 
1 119 ALA n 
1 120 GLU n 
1 121 SER n 
1 122 ARG n 
1 123 VAL n 
1 124 PHE n 
1 125 TYR n 
1 126 LEU n 
1 127 LYS n 
1 128 MET n 
1 129 LYS n 
1 130 GLY n 
1 131 ASP n 
1 132 TYR n 
1 133 TYR n 
1 134 ARG n 
1 135 TYR n 
1 136 LEU n 
1 137 ALA n 
1 138 GLU n 
1 139 VAL n 
1 140 ALA n 
1 141 THR n 
1 142 GLY n 
1 143 ASP n 
1 144 ASP n 
1 145 LYS n 
1 146 LYS n 
1 147 ARG n 
1 148 ILE n 
1 149 ILE n 
1 150 ASP n 
1 151 SER n 
1 152 ALA n 
1 153 ARG n 
1 154 SER n 
1 155 ALA n 
1 156 TYR n 
1 157 GLN n 
1 158 GLU n 
1 159 ALA n 
1 160 MET n 
1 161 ASP n 
1 162 ILE n 
1 163 SER n 
1 164 LYS n 
1 165 LYS n 
1 166 GLU n 
1 167 MET n 
1 168 PRO n 
1 169 PRO n 
1 170 THR n 
1 171 ASN n 
1 172 PRO n 
1 173 ILE n 
1 174 ARG n 
1 175 LEU n 
1 176 GLY n 
1 177 LEU n 
1 178 ALA n 
1 179 LEU n 
1 180 ASN n 
1 181 PHE n 
1 182 SER n 
1 183 VAL n 
1 184 PHE n 
1 185 HIS n 
1 186 TYR n 
1 187 GLU n 
1 188 ILE n 
1 189 ALA n 
1 190 ASN n 
1 191 SER n 
1 192 PRO n 
1 193 GLU n 
1 194 GLU n 
1 195 ALA n 
1 196 ILE n 
1 197 SER n 
1 198 LEU n 
1 199 ALA n 
1 200 LYS n 
1 201 THR n 
1 202 THR n 
1 203 PHE n 
1 204 ASP n 
1 205 GLU n 
1 206 ALA n 
1 207 MET n 
1 208 ALA n 
1 209 ASP n 
1 210 LEU n 
1 211 HIS n 
1 212 THR n 
1 213 LEU n 
1 214 SER n 
1 215 GLU n 
1 216 ASP n 
1 217 SER n 
1 218 TYR n 
1 219 LYS n 
1 220 ASP n 
1 221 SER n 
1 222 THR n 
1 223 LEU n 
1 224 ILE n 
1 225 MET n 
1 226 GLN n 
1 227 LEU n 
1 228 LEU n 
1 229 ARG n 
1 230 ASP n 
1 231 ASN n 
1 232 LEU n 
1 233 THR n 
1 234 LEU n 
1 235 TRP n 
1 236 THR n 
2 1   GLN n 
2 2   ARG n 
2 3   SER n 
2 4   THR n 
2 5   SEP n 
2 6   THR n 
2 7   PRO n 
2 8   ASN n 
2 9   VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   236 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SFN, HME1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       9 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                  ?               
'C3 H7 N O2'            89.093  
ARG 'L-peptide linking' y ARGININE                                                                                 ?               
'C6 H15 N4 O2 1'        175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                               ?               
'C4 H8 N2 O3'           132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                          ?               
'C4 H7 N O4'            133.103 
CA  non-polymer         . 'CALCIUM ION'                                                                            ?               
'Ca 2'                  40.078  
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 
WQN non-polymer         . '1-[8-(4-bromophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone' ?               
'C14 H16 Br Cl N2 O4 S' 423.710 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -4  -4  GLY GLY A . n 
A 1 2   ALA 2   -3  -3  ALA ALA A . n 
A 1 3   MET 3   -2  -2  MET MET A . n 
A 1 4   GLY 4   -1  -1  GLY GLY A . n 
A 1 5   SER 5   0   0   SER SER A . n 
A 1 6   MET 6   1   1   MET MET A . n 
A 1 7   GLU 7   2   2   GLU GLU A . n 
A 1 8   ARG 8   3   3   ARG ARG A . n 
A 1 9   ALA 9   4   4   ALA ALA A . n 
A 1 10  SER 10  5   5   SER SER A . n 
A 1 11  LEU 11  6   6   LEU LEU A . n 
A 1 12  ILE 12  7   7   ILE ILE A . n 
A 1 13  GLN 13  8   8   GLN GLN A . n 
A 1 14  LYS 14  9   9   LYS LYS A . n 
A 1 15  ALA 15  10  10  ALA ALA A . n 
A 1 16  LYS 16  11  11  LYS LYS A . n 
A 1 17  LEU 17  12  12  LEU LEU A . n 
A 1 18  ALA 18  13  13  ALA ALA A . n 
A 1 19  GLU 19  14  14  GLU GLU A . n 
A 1 20  GLN 20  15  15  GLN GLN A . n 
A 1 21  ALA 21  16  16  ALA ALA A . n 
A 1 22  GLU 22  17  17  GLU GLU A . n 
A 1 23  ARG 23  18  18  ARG ARG A . n 
A 1 24  TYR 24  19  19  TYR TYR A . n 
A 1 25  GLU 25  20  20  GLU GLU A . n 
A 1 26  ASP 26  21  21  ASP ASP A . n 
A 1 27  MET 27  22  22  MET MET A . n 
A 1 28  ALA 28  23  23  ALA ALA A . n 
A 1 29  ALA 29  24  24  ALA ALA A . n 
A 1 30  PHE 30  25  25  PHE PHE A . n 
A 1 31  MET 31  26  26  MET MET A . n 
A 1 32  LYS 32  27  27  LYS LYS A . n 
A 1 33  GLY 33  28  28  GLY GLY A . n 
A 1 34  ALA 34  29  29  ALA ALA A . n 
A 1 35  VAL 35  30  30  VAL VAL A . n 
A 1 36  GLU 36  31  31  GLU GLU A . n 
A 1 37  LYS 37  32  32  LYS LYS A . n 
A 1 38  GLY 38  33  33  GLY GLY A . n 
A 1 39  GLU 39  34  34  GLU GLU A . n 
A 1 40  GLU 40  35  35  GLU GLU A . n 
A 1 41  LEU 41  36  36  LEU LEU A . n 
A 1 42  SER 42  37  37  SER SER A . n 
A 1 43  CYS 43  38  38  CYS CYS A . n 
A 1 44  GLU 44  39  39  GLU GLU A . n 
A 1 45  GLU 45  40  40  GLU GLU A . n 
A 1 46  ARG 46  41  41  ARG ARG A . n 
A 1 47  ASN 47  42  42  ASN ASN A . n 
A 1 48  LEU 48  43  43  LEU LEU A . n 
A 1 49  LEU 49  44  44  LEU LEU A . n 
A 1 50  SER 50  45  45  SER SER A . n 
A 1 51  VAL 51  46  46  VAL VAL A . n 
A 1 52  ALA 52  47  47  ALA ALA A . n 
A 1 53  TYR 53  48  48  TYR TYR A . n 
A 1 54  LYS 54  49  49  LYS LYS A . n 
A 1 55  ASN 55  50  50  ASN ASN A . n 
A 1 56  VAL 56  51  51  VAL VAL A . n 
A 1 57  VAL 57  52  52  VAL VAL A . n 
A 1 58  GLY 58  53  53  GLY GLY A . n 
A 1 59  GLY 59  54  54  GLY GLY A . n 
A 1 60  GLN 60  55  55  GLN GLN A . n 
A 1 61  ARG 61  56  56  ARG ARG A . n 
A 1 62  ALA 62  57  57  ALA ALA A . n 
A 1 63  ALA 63  58  58  ALA ALA A . n 
A 1 64  TRP 64  59  59  TRP TRP A . n 
A 1 65  ARG 65  60  60  ARG ARG A . n 
A 1 66  VAL 66  61  61  VAL VAL A . n 
A 1 67  LEU 67  62  62  LEU LEU A . n 
A 1 68  SER 68  63  63  SER SER A . n 
A 1 69  SER 69  64  64  SER SER A . n 
A 1 70  ILE 70  65  65  ILE ILE A . n 
A 1 71  GLU 71  66  66  GLU GLU A . n 
A 1 72  GLN 72  67  67  GLN GLN A . n 
A 1 73  LYS 73  68  68  LYS LYS A . n 
A 1 74  SER 74  69  69  SER SER A . n 
A 1 75  ASN 75  70  70  ASN ASN A . n 
A 1 76  GLU 76  71  71  GLU GLU A . n 
A 1 77  GLU 77  72  72  GLU GLU A . n 
A 1 78  GLY 78  73  73  GLY GLY A . n 
A 1 79  SER 79  74  74  SER SER A . n 
A 1 80  GLU 80  75  75  GLU GLU A . n 
A 1 81  GLU 81  76  76  GLU GLU A . n 
A 1 82  LYS 82  77  77  LYS LYS A . n 
A 1 83  GLY 83  78  78  GLY GLY A . n 
A 1 84  PRO 84  79  79  PRO PRO A . n 
A 1 85  GLU 85  80  80  GLU GLU A . n 
A 1 86  VAL 86  81  81  VAL VAL A . n 
A 1 87  ARG 87  82  82  ARG ARG A . n 
A 1 88  GLU 88  83  83  GLU GLU A . n 
A 1 89  TYR 89  84  84  TYR TYR A . n 
A 1 90  ARG 90  85  85  ARG ARG A . n 
A 1 91  GLU 91  86  86  GLU GLU A . n 
A 1 92  LYS 92  87  87  LYS LYS A . n 
A 1 93  VAL 93  88  88  VAL VAL A . n 
A 1 94  GLU 94  89  89  GLU GLU A . n 
A 1 95  THR 95  90  90  THR THR A . n 
A 1 96  GLU 96  91  91  GLU GLU A . n 
A 1 97  LEU 97  92  92  LEU LEU A . n 
A 1 98  GLN 98  93  93  GLN GLN A . n 
A 1 99  GLY 99  94  94  GLY GLY A . n 
A 1 100 VAL 100 95  95  VAL VAL A . n 
A 1 101 CYS 101 96  96  CYS CYS A . n 
A 1 102 ASP 102 97  97  ASP ASP A . n 
A 1 103 THR 103 98  98  THR THR A . n 
A 1 104 VAL 104 99  99  VAL VAL A . n 
A 1 105 LEU 105 100 100 LEU LEU A . n 
A 1 106 GLY 106 101 101 GLY GLY A . n 
A 1 107 LEU 107 102 102 LEU LEU A . n 
A 1 108 LEU 108 103 103 LEU LEU A . n 
A 1 109 ASP 109 104 104 ASP ASP A . n 
A 1 110 SER 110 105 105 SER SER A . n 
A 1 111 HIS 111 106 106 HIS HIS A . n 
A 1 112 LEU 112 107 107 LEU LEU A . n 
A 1 113 ILE 113 108 108 ILE ILE A . n 
A 1 114 LYS 114 109 109 LYS LYS A . n 
A 1 115 GLU 115 110 110 GLU GLU A . n 
A 1 116 ALA 116 111 111 ALA ALA A . n 
A 1 117 GLY 117 112 112 GLY GLY A . n 
A 1 118 ASP 118 113 113 ASP ASP A . n 
A 1 119 ALA 119 114 114 ALA ALA A . n 
A 1 120 GLU 120 115 115 GLU GLU A . n 
A 1 121 SER 121 116 116 SER SER A . n 
A 1 122 ARG 122 117 117 ARG ARG A . n 
A 1 123 VAL 123 118 118 VAL VAL A . n 
A 1 124 PHE 124 119 119 PHE PHE A . n 
A 1 125 TYR 125 120 120 TYR TYR A . n 
A 1 126 LEU 126 121 121 LEU LEU A . n 
A 1 127 LYS 127 122 122 LYS LYS A . n 
A 1 128 MET 128 123 123 MET MET A . n 
A 1 129 LYS 129 124 124 LYS LYS A . n 
A 1 130 GLY 130 125 125 GLY GLY A . n 
A 1 131 ASP 131 126 126 ASP ASP A . n 
A 1 132 TYR 132 127 127 TYR TYR A . n 
A 1 133 TYR 133 128 128 TYR TYR A . n 
A 1 134 ARG 134 129 129 ARG ARG A . n 
A 1 135 TYR 135 130 130 TYR TYR A . n 
A 1 136 LEU 136 131 131 LEU LEU A . n 
A 1 137 ALA 137 132 132 ALA ALA A . n 
A 1 138 GLU 138 133 133 GLU GLU A . n 
A 1 139 VAL 139 134 134 VAL VAL A . n 
A 1 140 ALA 140 135 135 ALA ALA A . n 
A 1 141 THR 141 136 136 THR THR A . n 
A 1 142 GLY 142 137 137 GLY GLY A . n 
A 1 143 ASP 143 138 138 ASP ASP A . n 
A 1 144 ASP 144 139 139 ASP ASP A . n 
A 1 145 LYS 145 140 140 LYS LYS A . n 
A 1 146 LYS 146 141 141 LYS LYS A . n 
A 1 147 ARG 147 142 142 ARG ARG A . n 
A 1 148 ILE 148 143 143 ILE ILE A . n 
A 1 149 ILE 149 144 144 ILE ILE A . n 
A 1 150 ASP 150 145 145 ASP ASP A . n 
A 1 151 SER 151 146 146 SER SER A . n 
A 1 152 ALA 152 147 147 ALA ALA A . n 
A 1 153 ARG 153 148 148 ARG ARG A . n 
A 1 154 SER 154 149 149 SER SER A . n 
A 1 155 ALA 155 150 150 ALA ALA A . n 
A 1 156 TYR 156 151 151 TYR TYR A . n 
A 1 157 GLN 157 152 152 GLN GLN A . n 
A 1 158 GLU 158 153 153 GLU GLU A . n 
A 1 159 ALA 159 154 154 ALA ALA A . n 
A 1 160 MET 160 155 155 MET MET A . n 
A 1 161 ASP 161 156 156 ASP ASP A . n 
A 1 162 ILE 162 157 157 ILE ILE A . n 
A 1 163 SER 163 158 158 SER SER A . n 
A 1 164 LYS 164 159 159 LYS LYS A . n 
A 1 165 LYS 165 160 160 LYS LYS A . n 
A 1 166 GLU 166 161 161 GLU GLU A . n 
A 1 167 MET 167 162 162 MET MET A . n 
A 1 168 PRO 168 163 163 PRO PRO A . n 
A 1 169 PRO 169 164 164 PRO PRO A . n 
A 1 170 THR 170 165 165 THR THR A . n 
A 1 171 ASN 171 166 166 ASN ASN A . n 
A 1 172 PRO 172 167 167 PRO PRO A . n 
A 1 173 ILE 173 168 168 ILE ILE A . n 
A 1 174 ARG 174 169 169 ARG ARG A . n 
A 1 175 LEU 175 170 170 LEU LEU A . n 
A 1 176 GLY 176 171 171 GLY GLY A . n 
A 1 177 LEU 177 172 172 LEU LEU A . n 
A 1 178 ALA 178 173 173 ALA ALA A . n 
A 1 179 LEU 179 174 174 LEU LEU A . n 
A 1 180 ASN 180 175 175 ASN ASN A . n 
A 1 181 PHE 181 176 176 PHE PHE A . n 
A 1 182 SER 182 177 177 SER SER A . n 
A 1 183 VAL 183 178 178 VAL VAL A . n 
A 1 184 PHE 184 179 179 PHE PHE A . n 
A 1 185 HIS 185 180 180 HIS HIS A . n 
A 1 186 TYR 186 181 181 TYR TYR A . n 
A 1 187 GLU 187 182 182 GLU GLU A . n 
A 1 188 ILE 188 183 183 ILE ILE A . n 
A 1 189 ALA 189 184 184 ALA ALA A . n 
A 1 190 ASN 190 185 185 ASN ASN A . n 
A 1 191 SER 191 186 186 SER SER A . n 
A 1 192 PRO 192 187 187 PRO PRO A . n 
A 1 193 GLU 193 188 188 GLU GLU A . n 
A 1 194 GLU 194 189 189 GLU GLU A . n 
A 1 195 ALA 195 190 190 ALA ALA A . n 
A 1 196 ILE 196 191 191 ILE ILE A . n 
A 1 197 SER 197 192 192 SER SER A . n 
A 1 198 LEU 198 193 193 LEU LEU A . n 
A 1 199 ALA 199 194 194 ALA ALA A . n 
A 1 200 LYS 200 195 195 LYS LYS A . n 
A 1 201 THR 201 196 196 THR THR A . n 
A 1 202 THR 202 197 197 THR THR A . n 
A 1 203 PHE 203 198 198 PHE PHE A . n 
A 1 204 ASP 204 199 199 ASP ASP A . n 
A 1 205 GLU 205 200 200 GLU GLU A . n 
A 1 206 ALA 206 201 201 ALA ALA A . n 
A 1 207 MET 207 202 202 MET MET A . n 
A 1 208 ALA 208 203 203 ALA ALA A . n 
A 1 209 ASP 209 204 204 ASP ASP A . n 
A 1 210 LEU 210 205 205 LEU LEU A . n 
A 1 211 HIS 211 206 206 HIS HIS A . n 
A 1 212 THR 212 207 207 THR THR A . n 
A 1 213 LEU 213 208 208 LEU LEU A . n 
A 1 214 SER 214 209 209 SER SER A . n 
A 1 215 GLU 215 210 210 GLU GLU A . n 
A 1 216 ASP 216 211 211 ASP ASP A . n 
A 1 217 SER 217 212 212 SER SER A . n 
A 1 218 TYR 218 213 213 TYR TYR A . n 
A 1 219 LYS 219 214 214 LYS LYS A . n 
A 1 220 ASP 220 215 215 ASP ASP A . n 
A 1 221 SER 221 216 216 SER SER A . n 
A 1 222 THR 222 217 217 THR THR A . n 
A 1 223 LEU 223 218 218 LEU LEU A . n 
A 1 224 ILE 224 219 219 ILE ILE A . n 
A 1 225 MET 225 220 220 MET MET A . n 
A 1 226 GLN 226 221 221 GLN GLN A . n 
A 1 227 LEU 227 222 222 LEU LEU A . n 
A 1 228 LEU 228 223 223 LEU LEU A . n 
A 1 229 ARG 229 224 224 ARG ARG A . n 
A 1 230 ASP 230 225 225 ASP ASP A . n 
A 1 231 ASN 231 226 226 ASN ASN A . n 
A 1 232 LEU 232 227 227 LEU LEU A . n 
A 1 233 THR 233 228 228 THR THR A . n 
A 1 234 LEU 234 229 229 LEU LEU A . n 
A 1 235 TRP 235 230 230 TRP TRP A . n 
A 1 236 THR 236 231 231 THR THR A . n 
B 2 1   GLN 1   255 255 GLN GLN P . n 
B 2 2   ARG 2   256 256 ARG ARG P . n 
B 2 3   SER 3   257 257 SER SER P . n 
B 2 4   THR 4   258 258 THR THR P . n 
B 2 5   SEP 5   259 259 SEP SEP P . n 
B 2 6   THR 6   260 260 THR THR P . n 
B 2 7   PRO 7   261 261 PRO PRO P . n 
B 2 8   ASN 8   262 262 ASN ASN P . n 
B 2 9   VAL 9   263 263 VAL VAL P . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WQN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WQN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 CL  1   301 232 CL  CL  A . 
D 4 MG  1   302 233 MG  MG  A . 
E 4 MG  1   303 234 MG  MG  A . 
F 4 MG  1   304 235 MG  MG  A . 
G 5 WQN 1   305 236 WQN DRG A . 
H 6 CA  1   306 1   CA  CA  A . 
I 7 HOH 1   401 3   HOH HOH A . 
I 7 HOH 2   402 4   HOH HOH A . 
I 7 HOH 3   403 129 HOH HOH A . 
I 7 HOH 4   404 212 HOH HOH A . 
I 7 HOH 5   405 144 HOH HOH A . 
I 7 HOH 6   406 21  HOH HOH A . 
I 7 HOH 7   407 48  HOH HOH A . 
I 7 HOH 8   408 165 HOH HOH A . 
I 7 HOH 9   409 125 HOH HOH A . 
I 7 HOH 10  410 188 HOH HOH A . 
I 7 HOH 11  411 81  HOH HOH A . 
I 7 HOH 12  412 123 HOH HOH A . 
I 7 HOH 13  413 182 HOH HOH A . 
I 7 HOH 14  414 26  HOH HOH A . 
I 7 HOH 15  415 262 HOH HOH A . 
I 7 HOH 16  416 141 HOH HOH A . 
I 7 HOH 17  417 29  HOH HOH A . 
I 7 HOH 18  418 245 HOH HOH A . 
I 7 HOH 19  419 105 HOH HOH A . 
I 7 HOH 20  420 146 HOH HOH A . 
I 7 HOH 21  421 97  HOH HOH A . 
I 7 HOH 22  422 193 HOH HOH A . 
I 7 HOH 23  423 102 HOH HOH A . 
I 7 HOH 24  424 178 HOH HOH A . 
I 7 HOH 25  425 82  HOH HOH A . 
I 7 HOH 26  426 9   HOH HOH A . 
I 7 HOH 27  427 116 HOH HOH A . 
I 7 HOH 28  428 27  HOH HOH A . 
I 7 HOH 29  429 198 HOH HOH A . 
I 7 HOH 30  430 83  HOH HOH A . 
I 7 HOH 31  431 5   HOH HOH A . 
I 7 HOH 32  432 52  HOH HOH A . 
I 7 HOH 33  433 20  HOH HOH A . 
I 7 HOH 34  434 13  HOH HOH A . 
I 7 HOH 35  435 12  HOH HOH A . 
I 7 HOH 36  436 162 HOH HOH A . 
I 7 HOH 37  437 24  HOH HOH A . 
I 7 HOH 38  438 90  HOH HOH A . 
I 7 HOH 39  439 153 HOH HOH A . 
I 7 HOH 40  440 8   HOH HOH A . 
I 7 HOH 41  441 51  HOH HOH A . 
I 7 HOH 42  442 159 HOH HOH A . 
I 7 HOH 43  443 100 HOH HOH A . 
I 7 HOH 44  444 45  HOH HOH A . 
I 7 HOH 45  445 98  HOH HOH A . 
I 7 HOH 46  446 85  HOH HOH A . 
I 7 HOH 47  447 208 HOH HOH A . 
I 7 HOH 48  448 61  HOH HOH A . 
I 7 HOH 49  449 113 HOH HOH A . 
I 7 HOH 50  450 233 HOH HOH A . 
I 7 HOH 51  451 130 HOH HOH A . 
I 7 HOH 52  452 78  HOH HOH A . 
I 7 HOH 53  453 199 HOH HOH A . 
I 7 HOH 54  454 54  HOH HOH A . 
I 7 HOH 55  455 6   HOH HOH A . 
I 7 HOH 56  456 203 HOH HOH A . 
I 7 HOH 57  457 196 HOH HOH A . 
I 7 HOH 58  458 79  HOH HOH A . 
I 7 HOH 59  459 73  HOH HOH A . 
I 7 HOH 60  460 101 HOH HOH A . 
I 7 HOH 61  461 42  HOH HOH A . 
I 7 HOH 62  462 112 HOH HOH A . 
I 7 HOH 63  463 258 HOH HOH A . 
I 7 HOH 64  464 66  HOH HOH A . 
I 7 HOH 65  465 12  HOH HOH A . 
I 7 HOH 66  466 3   HOH HOH A . 
I 7 HOH 67  467 65  HOH HOH A . 
I 7 HOH 68  468 10  HOH HOH A . 
I 7 HOH 69  469 145 HOH HOH A . 
I 7 HOH 70  470 176 HOH HOH A . 
I 7 HOH 71  471 19  HOH HOH A . 
I 7 HOH 72  472 33  HOH HOH A . 
I 7 HOH 73  473 46  HOH HOH A . 
I 7 HOH 74  474 96  HOH HOH A . 
I 7 HOH 75  475 174 HOH HOH A . 
I 7 HOH 76  476 156 HOH HOH A . 
I 7 HOH 77  477 71  HOH HOH A . 
I 7 HOH 78  478 15  HOH HOH A . 
I 7 HOH 79  479 25  HOH HOH A . 
I 7 HOH 80  480 53  HOH HOH A . 
I 7 HOH 81  481 76  HOH HOH A . 
I 7 HOH 82  482 249 HOH HOH A . 
I 7 HOH 83  483 8   HOH HOH A . 
I 7 HOH 84  484 63  HOH HOH A . 
I 7 HOH 85  485 30  HOH HOH A . 
I 7 HOH 86  486 11  HOH HOH A . 
I 7 HOH 87  487 77  HOH HOH A . 
I 7 HOH 88  488 14  HOH HOH A . 
I 7 HOH 89  489 44  HOH HOH A . 
I 7 HOH 90  490 88  HOH HOH A . 
I 7 HOH 91  491 67  HOH HOH A . 
I 7 HOH 92  492 35  HOH HOH A . 
I 7 HOH 93  493 150 HOH HOH A . 
I 7 HOH 94  494 133 HOH HOH A . 
I 7 HOH 95  495 47  HOH HOH A . 
I 7 HOH 96  496 2   HOH HOH A . 
I 7 HOH 97  497 110 HOH HOH A . 
I 7 HOH 98  498 117 HOH HOH A . 
I 7 HOH 99  499 246 HOH HOH A . 
I 7 HOH 100 500 31  HOH HOH A . 
I 7 HOH 101 501 37  HOH HOH A . 
I 7 HOH 102 502 62  HOH HOH A . 
I 7 HOH 103 503 18  HOH HOH A . 
I 7 HOH 104 504 74  HOH HOH A . 
I 7 HOH 105 505 92  HOH HOH A . 
I 7 HOH 106 506 186 HOH HOH A . 
I 7 HOH 107 507 127 HOH HOH A . 
I 7 HOH 108 508 192 HOH HOH A . 
I 7 HOH 109 509 2   HOH HOH A . 
I 7 HOH 110 510 19  HOH HOH A . 
I 7 HOH 111 511 122 HOH HOH A . 
I 7 HOH 112 512 34  HOH HOH A . 
I 7 HOH 113 513 13  HOH HOH A . 
I 7 HOH 114 514 39  HOH HOH A . 
I 7 HOH 115 515 49  HOH HOH A . 
I 7 HOH 116 516 91  HOH HOH A . 
I 7 HOH 117 517 128 HOH HOH A . 
I 7 HOH 118 518 64  HOH HOH A . 
I 7 HOH 119 519 119 HOH HOH A . 
I 7 HOH 120 520 6   HOH HOH A . 
I 7 HOH 121 521 154 HOH HOH A . 
I 7 HOH 122 522 43  HOH HOH A . 
I 7 HOH 123 523 120 HOH HOH A . 
I 7 HOH 124 524 149 HOH HOH A . 
I 7 HOH 125 525 84  HOH HOH A . 
I 7 HOH 126 526 23  HOH HOH A . 
I 7 HOH 127 527 195 HOH HOH A . 
I 7 HOH 128 528 86  HOH HOH A . 
I 7 HOH 129 529 219 HOH HOH A . 
I 7 HOH 130 530 7   HOH HOH A . 
I 7 HOH 131 531 58  HOH HOH A . 
I 7 HOH 132 532 143 HOH HOH A . 
I 7 HOH 133 533 190 HOH HOH A . 
I 7 HOH 134 534 202 HOH HOH A . 
I 7 HOH 135 535 99  HOH HOH A . 
I 7 HOH 136 536 18  HOH HOH A . 
I 7 HOH 137 537 7   HOH HOH A . 
I 7 HOH 138 538 134 HOH HOH A . 
I 7 HOH 139 539 75  HOH HOH A . 
I 7 HOH 140 540 142 HOH HOH A . 
I 7 HOH 141 541 147 HOH HOH A . 
I 7 HOH 142 542 163 HOH HOH A . 
I 7 HOH 143 543 40  HOH HOH A . 
I 7 HOH 144 544 108 HOH HOH A . 
I 7 HOH 145 545 60  HOH HOH A . 
I 7 HOH 146 546 87  HOH HOH A . 
I 7 HOH 147 547 260 HOH HOH A . 
I 7 HOH 148 548 107 HOH HOH A . 
I 7 HOH 149 549 169 HOH HOH A . 
I 7 HOH 150 550 254 HOH HOH A . 
I 7 HOH 151 551 55  HOH HOH A . 
I 7 HOH 152 552 32  HOH HOH A . 
I 7 HOH 153 553 238 HOH HOH A . 
I 7 HOH 154 554 204 HOH HOH A . 
I 7 HOH 155 555 36  HOH HOH A . 
I 7 HOH 156 556 232 HOH HOH A . 
I 7 HOH 157 557 231 HOH HOH A . 
I 7 HOH 158 558 104 HOH HOH A . 
I 7 HOH 159 559 218 HOH HOH A . 
I 7 HOH 160 560 183 HOH HOH A . 
I 7 HOH 161 561 103 HOH HOH A . 
I 7 HOH 162 562 106 HOH HOH A . 
I 7 HOH 163 563 207 HOH HOH A . 
I 7 HOH 164 564 115 HOH HOH A . 
I 7 HOH 165 565 70  HOH HOH A . 
I 7 HOH 166 566 68  HOH HOH A . 
I 7 HOH 167 567 222 HOH HOH A . 
I 7 HOH 168 568 224 HOH HOH A . 
I 7 HOH 169 569 201 HOH HOH A . 
I 7 HOH 170 570 22  HOH HOH A . 
I 7 HOH 171 571 138 HOH HOH A . 
I 7 HOH 172 572 10  HOH HOH A . 
I 7 HOH 173 573 131 HOH HOH A . 
I 7 HOH 174 574 241 HOH HOH A . 
I 7 HOH 175 575 4   HOH HOH A . 
I 7 HOH 176 576 11  HOH HOH A . 
I 7 HOH 177 577 124 HOH HOH A . 
I 7 HOH 178 578 228 HOH HOH A . 
I 7 HOH 179 579 200 HOH HOH A . 
I 7 HOH 180 580 20  HOH HOH A . 
I 7 HOH 181 581 94  HOH HOH A . 
I 7 HOH 182 582 173 HOH HOH A . 
I 7 HOH 183 583 175 HOH HOH A . 
I 7 HOH 184 584 265 HOH HOH A . 
I 7 HOH 185 585 17  HOH HOH A . 
I 7 HOH 186 586 213 HOH HOH A . 
I 7 HOH 187 587 215 HOH HOH A . 
I 7 HOH 188 588 244 HOH HOH A . 
I 7 HOH 189 589 89  HOH HOH A . 
I 7 HOH 190 590 172 HOH HOH A . 
I 7 HOH 191 591 139 HOH HOH A . 
I 7 HOH 192 592 136 HOH HOH A . 
I 7 HOH 193 593 59  HOH HOH A . 
I 7 HOH 194 594 114 HOH HOH A . 
I 7 HOH 195 595 93  HOH HOH A . 
I 7 HOH 196 596 72  HOH HOH A . 
I 7 HOH 197 597 266 HOH HOH A . 
I 7 HOH 198 598 194 HOH HOH A . 
I 7 HOH 199 599 109 HOH HOH A . 
I 7 HOH 200 600 15  HOH HOH A . 
I 7 HOH 201 601 217 HOH HOH A . 
I 7 HOH 202 602 247 HOH HOH A . 
I 7 HOH 203 603 221 HOH HOH A . 
I 7 HOH 204 604 166 HOH HOH A . 
I 7 HOH 205 605 216 HOH HOH A . 
I 7 HOH 206 606 268 HOH HOH A . 
I 7 HOH 207 607 180 HOH HOH A . 
I 7 HOH 208 608 140 HOH HOH A . 
I 7 HOH 209 609 21  HOH HOH A . 
I 7 HOH 210 610 261 HOH HOH A . 
I 7 HOH 211 611 236 HOH HOH A . 
I 7 HOH 212 612 50  HOH HOH A . 
I 7 HOH 213 613 189 HOH HOH A . 
I 7 HOH 214 614 210 HOH HOH A . 
I 7 HOH 215 615 137 HOH HOH A . 
I 7 HOH 216 616 263 HOH HOH A . 
I 7 HOH 217 617 38  HOH HOH A . 
I 7 HOH 218 618 267 HOH HOH A . 
I 7 HOH 219 619 14  HOH HOH A . 
I 7 HOH 220 620 41  HOH HOH A . 
I 7 HOH 221 621 168 HOH HOH A . 
I 7 HOH 222 622 5   HOH HOH A . 
I 7 HOH 223 623 171 HOH HOH A . 
I 7 HOH 224 624 250 HOH HOH A . 
I 7 HOH 225 625 177 HOH HOH A . 
I 7 HOH 226 626 69  HOH HOH A . 
I 7 HOH 227 627 111 HOH HOH A . 
I 7 HOH 228 628 121 HOH HOH A . 
I 7 HOH 229 629 226 HOH HOH A . 
I 7 HOH 230 630 9   HOH HOH A . 
I 7 HOH 231 631 220 HOH HOH A . 
I 7 HOH 232 632 184 HOH HOH A . 
I 7 HOH 233 633 264 HOH HOH A . 
I 7 HOH 234 634 271 HOH HOH A . 
I 7 HOH 235 635 229 HOH HOH A . 
I 7 HOH 236 636 118 HOH HOH A . 
I 7 HOH 237 637 179 HOH HOH A . 
I 7 HOH 238 638 135 HOH HOH A . 
I 7 HOH 239 639 148 HOH HOH A . 
I 7 HOH 240 640 158 HOH HOH A . 
I 7 HOH 241 641 164 HOH HOH A . 
I 7 HOH 242 642 152 HOH HOH A . 
I 7 HOH 243 643 269 HOH HOH A . 
I 7 HOH 244 644 253 HOH HOH A . 
I 7 HOH 245 645 259 HOH HOH A . 
I 7 HOH 246 646 1   HOH HOH A . 
I 7 HOH 247 647 255 HOH HOH A . 
I 7 HOH 248 648 16  HOH HOH A . 
I 7 HOH 249 649 239 HOH HOH A . 
I 7 HOH 250 650 56  HOH HOH A . 
I 7 HOH 251 651 160 HOH HOH A . 
I 7 HOH 252 652 185 HOH HOH A . 
I 7 HOH 253 653 80  HOH HOH A . 
I 7 HOH 254 654 187 HOH HOH A . 
J 7 HOH 1   301 132 HOH HOH P . 
J 7 HOH 2   302 223 HOH HOH P . 
J 7 HOH 3   303 17  HOH HOH P . 
J 7 HOH 4   304 126 HOH HOH P . 
J 7 HOH 5   305 161 HOH HOH P . 
J 7 HOH 6   306 22  HOH HOH P . 
J 7 HOH 7   307 57  HOH HOH P . 
J 7 HOH 8   308 28  HOH HOH P . 
J 7 HOH 9   309 95  HOH HOH P . 
J 7 HOH 10  310 151 HOH HOH P . 
J 7 HOH 11  311 16  HOH HOH P . 
J 7 HOH 12  312 206 HOH HOH P . 
J 7 HOH 13  313 191 HOH HOH P . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     N 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     WQN 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      305 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     CL1 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    G 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    WQN 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     1 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    CL1 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PDB-REDO ? ? ? . 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? . 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? . 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? . 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EW3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.543 
_cell.length_a_esd                 ? 
_cell.length_b                     112.940 
_cell.length_b_esd                 ? 
_cell.length_c                     63.064 
_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                         9EW3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EW3 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.66 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.78 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.095 M HEPES pH=7.1-7.7
0.19 M CaCl2 
5% glycerol
24-29% PEG400
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.873128 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID23-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.873128 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-2 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EW3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.40 
_reflns.d_resolution_low                               45.81 
_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                                     57943 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.40 
_reflns_shell.d_res_low                                     1.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2819 
_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                                  0.639 
_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]                            0.61 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.23 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.38 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               21.037 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.955 
_refine.details                                  
;HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
U VALUES : REFINED INDIVIDUALLY
;
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EW3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.40 
_refine.ls_d_res_low                             45.81 
_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                     54895 
_refine.ls_number_reflns_R_free                  2850 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.11 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20039 
_refine.ls_R_factor_R_free                       0.22924 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19891 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.063 
_refine.pdbx_overall_ESU_R_Free                  0.066 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             0.70 
_refine.pdbx_solvent_shrinkage_radii             0.70 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.543 
_refine.overall_SU_ML                            0.056 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.40 
_refine_hist.d_res_low                        45.81 
_refine_hist.number_atoms_solvent             267 
_refine_hist.number_atoms_total               2223 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1929 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         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' ? 0.008  0.016  2002 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1895 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 1.097  1.830  2706 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 0.459  1.571  4382 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 7.439  5.282  266  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 4.381  20.000 2    ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.351 10.000 375  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 0.051  0.200  300  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.020  2341 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  435  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 2.872  1.789  986  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.849  1.787  986  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 3.974  3.203  1231 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 3.981  3.207  1232 ? r_mcangle_other        ? ? 
'X-RAY DIFFRACTION' ? 5.298  2.210  1016 ? r_scbond_it            ? ? 
'X-RAY DIFFRACTION' ? 5.296  2.210  1017 ? r_scbond_other         ? ? 
'X-RAY DIFFRACTION' ? 7.520  3.844  1470 ? r_scangle_other        ? ? 
'X-RAY DIFFRACTION' ? 9.146  22.400 2399 ? r_long_range_B_refined ? ? 
'X-RAY DIFFRACTION' ? 9.134  20.840 2320 ? r_long_range_B_other   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.400 
_refine_ls_shell.d_res_low                        1.436 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             208 
_refine_ls_shell.number_reflns_R_work             3938 
_refine_ls_shell.percent_reflns_obs               98.04 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.405 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.429 
# 
_struct.entry_id                     9EW3 
_struct.title                        'Ternary structure of 14-3-3s, C-RAF phosphopeptide 12-mer (pS259) and compound 78 (1084378)' 
_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        9EW3 
_struct_keywords.text            'Stabilizer, protein-protein interaction, PEPTIDE BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'PEPTIDE BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 7 ? 
J N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP 1433S_HUMAN P31947 ? 1 
;MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPE
VREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKK
EMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
1   
2 UNP RAF1_HUMAN  P04049 ? 2 QRSTSTPNV 255 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EW3 A 6 ? 236 ? P31947 1   ? 231 ? 1   231 
2 2 9EW3 P 1 ? 9   ? P04049 255 ? 263 ? 255 263 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9EW3 GLY A 1 ? UNP P31947 ? ? 'expression tag' -4 1 
1 9EW3 ALA A 2 ? UNP P31947 ? ? 'expression tag' -3 2 
1 9EW3 MET A 3 ? UNP P31947 ? ? 'expression tag' -2 3 
1 9EW3 GLY A 4 ? UNP P31947 ? ? 'expression tag' -1 4 
1 9EW3 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)' 5600  ? 
1 MORE         -86   ? 
1 'SSA (A^2)'  24270 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 4_555 x,-y,-z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 7   ? ALA A 21  ? GLU A 2   ALA A 16  1 ? 15 
HELX_P HELX_P2  AA2 ARG A 23  ? LYS A 37  ? ARG A 18  LYS A 32  1 ? 15 
HELX_P HELX_P3  AA3 SER A 42  ? ASN A 75  ? SER A 37  ASN A 70  1 ? 34 
HELX_P HELX_P4  AA4 PRO A 84  ? SER A 110 ? PRO A 79  SER A 105 1 ? 27 
HELX_P HELX_P5  AA5 HIS A 111 ? ALA A 116 ? HIS A 106 ALA A 111 1 ? 6  
HELX_P HELX_P6  AA6 ASP A 118 ? ALA A 140 ? ASP A 113 ALA A 135 1 ? 23 
HELX_P HELX_P7  AA7 ASP A 144 ? MET A 167 ? ASP A 139 MET A 162 1 ? 24 
HELX_P HELX_P8  AA8 ASN A 171 ? ILE A 188 ? ASN A 166 ILE A 183 1 ? 18 
HELX_P HELX_P9  AA9 SER A 191 ? ALA A 208 ? SER A 186 ALA A 203 1 ? 18 
HELX_P HELX_P10 AB1 ASP A 209 ? LEU A 213 ? ASP A 204 LEU A 208 5 ? 5  
HELX_P HELX_P11 AB2 SER A 214 ? THR A 236 ? SER A 209 THR A 231 1 ? 23 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? B THR 4   C   ? ? ? 1_555 B SEP 5 N  ? ? P THR 258 P SEP 259 1_555 ? ? ? ? ? ? ? 1.343 ? ? 
covale2  covale both ? B SEP 5   C   ? ? ? 1_555 B THR 6 N  ? ? P SEP 259 P THR 260 1_555 ? ? ? ? ? ? ? 1.337 ? ? 
metalc1  metalc ?    ? A GLU 7   OE1 ? ? ? 1_555 F MG  . MG ? ? A GLU 2   A MG  304 1_555 ? ? ? ? ? ? ? 2.404 ? ? 
metalc2  metalc ?    ? A GLU 7   OE1 ? ? ? 1_555 F MG  . MG ? ? A GLU 2   A MG  304 3_554 ? ? ? ? ? ? ? 2.404 ? ? 
metalc3  metalc ?    ? A GLU 40  OE1 ? ? ? 1_555 H CA  . CA ? ? A GLU 35  A CA  306 1_555 ? ? ? ? ? ? ? 2.614 ? ? 
metalc4  metalc ?    ? A GLU 40  OE2 ? ? ? 1_555 H CA  . CA ? ? A GLU 35  A CA  306 1_555 ? ? ? ? ? ? ? 2.426 ? ? 
metalc5  metalc ?    ? A GLU 80  OE1 ? ? ? 1_555 E MG  . MG ? ? A GLU 75  A MG  303 1_555 ? ? ? ? ? ? ? 2.459 ? ? 
metalc6  metalc ?    ? A GLU 94  OE2 ? ? ? 1_555 D MG  . MG ? ? A GLU 89  A MG  302 1_555 ? ? ? ? ? ? ? 2.485 ? ? 
metalc7  metalc ?    ? A GLU 115 O   ? ? ? 1_555 H CA  . CA ? ? A GLU 110 A CA  306 1_555 ? ? ? ? ? ? ? 2.285 ? ? 
metalc8  metalc ?    ? A GLU 166 O   ? ? ? 1_555 E MG  . MG ? ? A GLU 161 A MG  303 7_455 ? ? ? ? ? ? ? 2.207 ? ? 
metalc9  metalc ?    ? A GLU 193 OE2 ? ? ? 1_555 H CA  . CA ? ? A GLU 188 A CA  306 6_455 ? ? ? ? ? ? ? 2.328 ? ? 
metalc10 metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  302 A HOH 406 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc11 metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  302 A HOH 453 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc12 metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  302 A HOH 570 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc13 metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  302 A HOH 597 1_555 ? ? ? ? ? ? ? 2.166 ? ? 
metalc14 metalc ?    ? E MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  303 A HOH 447 1_555 ? ? ? ? ? ? ? 2.182 ? ? 
metalc15 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  304 A HOH 434 1_555 ? ? ? ? ? ? ? 2.562 ? ? 
metalc16 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  304 A HOH 434 3_554 ? ? ? ? ? ? ? 2.562 ? ? 
metalc17 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  304 A HOH 513 1_555 ? ? ? ? ? ? ? 2.056 ? ? 
metalc18 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  304 A HOH 513 3_554 ? ? ? ? ? ? ? 2.056 ? ? 
metalc19 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  304 A HOH 619 1_555 ? ? ? ? ? ? ? 2.909 ? ? 
metalc20 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  304 A HOH 619 3_554 ? ? ? ? ? ? ? 2.909 ? ? 
metalc21 metalc ?    ? H CA  .   CA  ? ? ? 1_555 I HOH . O  ? ? A CA  306 A HOH 483 6_454 ? ? ? ? ? ? ? 2.369 ? ? 
metalc22 metalc ?    ? H CA  .   CA  ? ? ? 1_555 I HOH . O  ? ? A CA  306 A HOH 530 1_555 ? ? ? ? ? ? ? 2.289 ? ? 
metalc23 metalc ?    ? H CA  .   CA  ? ? ? 1_555 I HOH . O  ? ? A CA  306 A HOH 577 1_555 ? ? ? ? ? ? ? 2.378 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 OE1 ? A GLU 7   ? A GLU 2   ? 1_555 0.0   ? 
2  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 434 ? 1_555 75.2  ? 
3  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 434 ? 1_555 75.2  ? 
4  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 434 ? 3_554 80.8  ? 
5  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 434 ? 3_554 80.8  ? 
6  O   ? I HOH .   ? A HOH 434 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 434 ? 3_554 147.6 ? 
7  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 513 ? 1_555 79.1  ? 
8  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 513 ? 1_555 79.1  ? 
9  O   ? I HOH .   ? A HOH 434 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 513 ? 1_555 131.4 ? 
10 O   ? I HOH .   ? A HOH 434 ? 3_554 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 513 ? 1_555 62.6  ? 
11 OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 513 ? 3_554 136.3 ? 
12 OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 513 ? 3_554 136.3 ? 
13 O   ? I HOH .   ? A HOH 434 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 513 ? 3_554 62.6  ? 
14 O   ? I HOH .   ? A HOH 434 ? 3_554 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 513 ? 3_554 131.4 ? 
15 O   ? I HOH .   ? A HOH 513 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 513 ? 3_554 137.9 ? 
16 OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 1_555 96.1  ? 
17 OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 1_555 96.1  ? 
18 O   ? I HOH .   ? A HOH 434 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 1_555 86.4  ? 
19 O   ? I HOH .   ? A HOH 434 ? 3_554 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 1_555 117.9 ? 
20 O   ? I HOH .   ? A HOH 513 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 1_555 56.2  ? 
21 O   ? I HOH .   ? A HOH 513 ? 3_554 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 1_555 92.0  ? 
22 OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 3_554 166.7 ? 
23 OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 3_554 166.7 ? 
24 O   ? I HOH .   ? A HOH 434 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 3_554 117.9 ? 
25 O   ? I HOH .   ? A HOH 434 ? 3_554 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 3_554 86.4  ? 
26 O   ? I HOH .   ? A HOH 513 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 3_554 92.0  ? 
27 O   ? I HOH .   ? A HOH 513 ? 3_554 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 3_554 56.2  ? 
28 O   ? I HOH .   ? A HOH 619 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 619 ? 3_554 86.8  ? 
29 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 51.4  ? 
30 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? A GLU 115 ? A GLU 110 ? 1_555 85.5  ? 
31 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? A GLU 115 ? A GLU 110 ? 1_555 87.3  ? 
32 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 86.9  ? 
33 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 121.9 ? 
34 O   ? A GLU 115 ? A GLU 110 ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 45.9  ? 
35 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 483 ? 6_454 144.6 ? 
36 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 483 ? 6_454 160.5 ? 
37 O   ? A GLU 115 ? A GLU 110 ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 483 ? 6_454 103.1 ? 
38 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 483 ? 6_454 76.1  ? 
39 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 530 ? 1_555 131.0 ? 
40 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 530 ? 1_555 80.0  ? 
41 O   ? A GLU 115 ? A GLU 110 ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 530 ? 1_555 85.9  ? 
42 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 530 ? 1_555 119.0 ? 
43 O   ? I HOH .   ? A HOH 483 ? 6_454 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 530 ? 1_555 84.2  ? 
44 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 577 ? 1_555 87.9  ? 
45 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 577 ? 1_555 81.1  ? 
46 O   ? A GLU 115 ? A GLU 110 ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 577 ? 1_555 168.3 ? 
47 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 577 ? 1_555 143.3 ? 
48 O   ? I HOH .   ? A HOH 483 ? 6_454 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 577 ? 1_555 87.8  ? 
49 O   ? I HOH .   ? A HOH 530 ? 1_555 CA ? H CA . ? A CA 306 ? 1_555 O   ? I HOH .   ? A HOH 577 ? 1_555 91.2  ? 
50 OE1 ? A GLU 80  ? A GLU 75  ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? A GLU 166 ? A GLU 161 ? 1_555 71.5  ? 
51 OE1 ? A GLU 80  ? A GLU 75  ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? I HOH .   ? A HOH 447 ? 1_555 71.2  ? 
52 O   ? A GLU 166 ? A GLU 161 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? I HOH .   ? A HOH 447 ? 1_555 126.3 ? 
53 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 406 ? 1_555 66.6  ? 
54 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 453 ? 1_555 87.4  ? 
55 O   ? I HOH .   ? A HOH 406 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 453 ? 1_555 131.7 ? 
56 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 570 ? 1_555 79.9  ? 
57 O   ? I HOH .   ? A HOH 406 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 570 ? 1_555 70.1  ? 
58 O   ? I HOH .   ? A HOH 453 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 570 ? 1_555 65.5  ? 
59 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 597 ? 1_555 107.0 ? 
60 O   ? I HOH .   ? A HOH 406 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 597 ? 1_555 148.7 ? 
61 O   ? I HOH .   ? A HOH 453 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 597 ? 1_555 76.0  ? 
62 O   ? I HOH .   ? A HOH 570 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 597 ? 1_555 140.6 ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      SEP 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       5 
_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                       SEP 
_pdbx_modification_feature.auth_asym_id                       P 
_pdbx_modification_feature.auth_seq_id                        259 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_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                SER 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        SEP 
_pdbx_modification_feature.type                               Phosphorylation 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           110 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            105 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   HIS 
_struct_mon_prot_cis.pdbx_label_seq_id_2    111 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    HIS 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     106 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       10.04 
# 
_pdbx_entry_details.entry_id                   9EW3 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 18  ? ? -108.06 76.43 
2 1 ASN A 70  ? ? -99.03  32.20 
3 1 HIS A 106 ? ? -145.56 36.48 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 41  ? ? 0.076 'SIDE CHAIN' 
2 1 ARG A 142 ? ? 0.097 'SIDE CHAIN' 
3 1 ARG A 148 ? ? 0.277 'SIDE CHAIN' 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    B 
_pdbx_struct_mod_residue.label_comp_id    SEP 
_pdbx_struct_mod_residue.label_seq_id     5 
_pdbx_struct_mod_residue.auth_asym_id     P 
_pdbx_struct_mod_residue.auth_comp_id     SEP 
_pdbx_struct_mod_residue.auth_seq_id      259 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   SER 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    MG 
_pdbx_struct_special_symmetry.auth_seq_id     304 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   MG 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CA  CA   CA N N 74  
CL  CL   CL N N 75  
CYS N    N  N N 76  
CYS CA   C  N R 77  
CYS C    C  N N 78  
CYS O    O  N N 79  
CYS CB   C  N N 80  
CYS SG   S  N N 81  
CYS OXT  O  N N 82  
CYS H    H  N N 83  
CYS H2   H  N N 84  
CYS HA   H  N N 85  
CYS HB2  H  N N 86  
CYS HB3  H  N N 87  
CYS HG   H  N N 88  
CYS HXT  H  N N 89  
GLN N    N  N N 90  
GLN CA   C  N S 91  
GLN C    C  N N 92  
GLN O    O  N N 93  
GLN CB   C  N N 94  
GLN CG   C  N N 95  
GLN CD   C  N N 96  
GLN OE1  O  N N 97  
GLN NE2  N  N N 98  
GLN OXT  O  N N 99  
GLN H    H  N N 100 
GLN H2   H  N N 101 
GLN HA   H  N N 102 
GLN HB2  H  N N 103 
GLN HB3  H  N N 104 
GLN HG2  H  N N 105 
GLN HG3  H  N N 106 
GLN HE21 H  N N 107 
GLN HE22 H  N N 108 
GLN HXT  H  N N 109 
GLU N    N  N N 110 
GLU CA   C  N S 111 
GLU C    C  N N 112 
GLU O    O  N N 113 
GLU CB   C  N N 114 
GLU CG   C  N N 115 
GLU CD   C  N N 116 
GLU OE1  O  N N 117 
GLU OE2  O  N N 118 
GLU OXT  O  N N 119 
GLU H    H  N N 120 
GLU H2   H  N N 121 
GLU HA   H  N N 122 
GLU HB2  H  N N 123 
GLU HB3  H  N N 124 
GLU HG2  H  N N 125 
GLU HG3  H  N N 126 
GLU HE2  H  N N 127 
GLU HXT  H  N N 128 
GLY N    N  N N 129 
GLY CA   C  N N 130 
GLY C    C  N N 131 
GLY O    O  N N 132 
GLY OXT  O  N N 133 
GLY H    H  N N 134 
GLY H2   H  N N 135 
GLY HA2  H  N N 136 
GLY HA3  H  N N 137 
GLY HXT  H  N N 138 
HIS N    N  N N 139 
HIS CA   C  N S 140 
HIS C    C  N N 141 
HIS O    O  N N 142 
HIS CB   C  N N 143 
HIS CG   C  Y N 144 
HIS ND1  N  Y N 145 
HIS CD2  C  Y N 146 
HIS CE1  C  Y N 147 
HIS NE2  N  Y N 148 
HIS OXT  O  N N 149 
HIS H    H  N N 150 
HIS H2   H  N N 151 
HIS HA   H  N N 152 
HIS HB2  H  N N 153 
HIS HB3  H  N N 154 
HIS HD1  H  N N 155 
HIS HD2  H  N N 156 
HIS HE1  H  N N 157 
HIS HE2  H  N N 158 
HIS HXT  H  N N 159 
HOH O    O  N N 160 
HOH H1   H  N N 161 
HOH H2   H  N N 162 
ILE N    N  N N 163 
ILE CA   C  N S 164 
ILE C    C  N N 165 
ILE O    O  N N 166 
ILE CB   C  N S 167 
ILE CG1  C  N N 168 
ILE CG2  C  N N 169 
ILE CD1  C  N N 170 
ILE OXT  O  N N 171 
ILE H    H  N N 172 
ILE H2   H  N N 173 
ILE HA   H  N N 174 
ILE HB   H  N N 175 
ILE HG12 H  N N 176 
ILE HG13 H  N N 177 
ILE HG21 H  N N 178 
ILE HG22 H  N N 179 
ILE HG23 H  N N 180 
ILE HD11 H  N N 181 
ILE HD12 H  N N 182 
ILE HD13 H  N N 183 
ILE HXT  H  N N 184 
LEU N    N  N N 185 
LEU CA   C  N S 186 
LEU C    C  N N 187 
LEU O    O  N N 188 
LEU CB   C  N N 189 
LEU CG   C  N N 190 
LEU CD1  C  N N 191 
LEU CD2  C  N N 192 
LEU OXT  O  N N 193 
LEU H    H  N N 194 
LEU H2   H  N N 195 
LEU HA   H  N N 196 
LEU HB2  H  N N 197 
LEU HB3  H  N N 198 
LEU HG   H  N N 199 
LEU HD11 H  N N 200 
LEU HD12 H  N N 201 
LEU HD13 H  N N 202 
LEU HD21 H  N N 203 
LEU HD22 H  N N 204 
LEU HD23 H  N N 205 
LEU HXT  H  N N 206 
LYS N    N  N N 207 
LYS CA   C  N S 208 
LYS C    C  N N 209 
LYS O    O  N N 210 
LYS CB   C  N N 211 
LYS CG   C  N N 212 
LYS CD   C  N N 213 
LYS CE   C  N N 214 
LYS NZ   N  N N 215 
LYS OXT  O  N N 216 
LYS H    H  N N 217 
LYS H2   H  N N 218 
LYS HA   H  N N 219 
LYS HB2  H  N N 220 
LYS HB3  H  N N 221 
LYS HG2  H  N N 222 
LYS HG3  H  N N 223 
LYS HD2  H  N N 224 
LYS HD3  H  N N 225 
LYS HE2  H  N N 226 
LYS HE3  H  N N 227 
LYS HZ1  H  N N 228 
LYS HZ2  H  N N 229 
LYS HZ3  H  N N 230 
LYS HXT  H  N N 231 
MET N    N  N N 232 
MET CA   C  N S 233 
MET C    C  N N 234 
MET O    O  N N 235 
MET CB   C  N N 236 
MET CG   C  N N 237 
MET SD   S  N N 238 
MET CE   C  N N 239 
MET OXT  O  N N 240 
MET H    H  N N 241 
MET H2   H  N N 242 
MET HA   H  N N 243 
MET HB2  H  N N 244 
MET HB3  H  N N 245 
MET HG2  H  N N 246 
MET HG3  H  N N 247 
MET HE1  H  N N 248 
MET HE2  H  N N 249 
MET HE3  H  N N 250 
MET HXT  H  N N 251 
MG  MG   MG N N 252 
PHE N    N  N N 253 
PHE CA   C  N S 254 
PHE C    C  N N 255 
PHE O    O  N N 256 
PHE CB   C  N N 257 
PHE CG   C  Y N 258 
PHE CD1  C  Y N 259 
PHE CD2  C  Y N 260 
PHE CE1  C  Y N 261 
PHE CE2  C  Y N 262 
PHE CZ   C  Y N 263 
PHE OXT  O  N N 264 
PHE H    H  N N 265 
PHE H2   H  N N 266 
PHE HA   H  N N 267 
PHE HB2  H  N N 268 
PHE HB3  H  N N 269 
PHE HD1  H  N N 270 
PHE HD2  H  N N 271 
PHE HE1  H  N N 272 
PHE HE2  H  N N 273 
PHE HZ   H  N N 274 
PHE HXT  H  N N 275 
PRO N    N  N N 276 
PRO CA   C  N S 277 
PRO C    C  N N 278 
PRO O    O  N N 279 
PRO CB   C  N N 280 
PRO CG   C  N N 281 
PRO CD   C  N N 282 
PRO OXT  O  N N 283 
PRO H    H  N N 284 
PRO HA   H  N N 285 
PRO HB2  H  N N 286 
PRO HB3  H  N N 287 
PRO HG2  H  N N 288 
PRO HG3  H  N N 289 
PRO HD2  H  N N 290 
PRO HD3  H  N N 291 
PRO HXT  H  N N 292 
SEP N    N  N N 293 
SEP CA   C  N S 294 
SEP CB   C  N N 295 
SEP OG   O  N N 296 
SEP C    C  N N 297 
SEP O    O  N N 298 
SEP OXT  O  N N 299 
SEP P    P  N N 300 
SEP O1P  O  N N 301 
SEP O2P  O  N N 302 
SEP O3P  O  N N 303 
SEP H    H  N N 304 
SEP H2   H  N N 305 
SEP HA   H  N N 306 
SEP HB2  H  N N 307 
SEP HB3  H  N N 308 
SEP HXT  H  N N 309 
SEP HOP2 H  N N 310 
SEP HOP3 H  N N 311 
SER N    N  N N 312 
SER CA   C  N S 313 
SER C    C  N N 314 
SER O    O  N N 315 
SER CB   C  N N 316 
SER OG   O  N N 317 
SER OXT  O  N N 318 
SER H    H  N N 319 
SER H2   H  N N 320 
SER HA   H  N N 321 
SER HB2  H  N N 322 
SER HB3  H  N N 323 
SER HG   H  N N 324 
SER HXT  H  N N 325 
THR N    N  N N 326 
THR CA   C  N S 327 
THR C    C  N N 328 
THR O    O  N N 329 
THR CB   C  N R 330 
THR OG1  O  N N 331 
THR CG2  C  N N 332 
THR OXT  O  N N 333 
THR H    H  N N 334 
THR H2   H  N N 335 
THR HA   H  N N 336 
THR HB   H  N N 337 
THR HG1  H  N N 338 
THR HG21 H  N N 339 
THR HG22 H  N N 340 
THR HG23 H  N N 341 
THR HXT  H  N N 342 
TRP N    N  N N 343 
TRP CA   C  N S 344 
TRP C    C  N N 345 
TRP O    O  N N 346 
TRP CB   C  N N 347 
TRP CG   C  Y N 348 
TRP CD1  C  Y N 349 
TRP CD2  C  Y N 350 
TRP NE1  N  Y N 351 
TRP CE2  C  Y N 352 
TRP CE3  C  Y N 353 
TRP CZ2  C  Y N 354 
TRP CZ3  C  Y N 355 
TRP CH2  C  Y N 356 
TRP OXT  O  N N 357 
TRP H    H  N N 358 
TRP H2   H  N N 359 
TRP HA   H  N N 360 
TRP HB2  H  N N 361 
TRP HB3  H  N N 362 
TRP HD1  H  N N 363 
TRP HE1  H  N N 364 
TRP HE3  H  N N 365 
TRP HZ2  H  N N 366 
TRP HZ3  H  N N 367 
TRP HH2  H  N N 368 
TRP HXT  H  N N 369 
TYR N    N  N N 370 
TYR CA   C  N S 371 
TYR C    C  N N 372 
TYR O    O  N N 373 
TYR CB   C  N N 374 
TYR CG   C  Y N 375 
TYR CD1  C  Y N 376 
TYR CD2  C  Y N 377 
TYR CE1  C  Y N 378 
TYR CE2  C  Y N 379 
TYR CZ   C  Y N 380 
TYR OH   O  N N 381 
TYR OXT  O  N N 382 
TYR H    H  N N 383 
TYR H2   H  N N 384 
TYR HA   H  N N 385 
TYR HB2  H  N N 386 
TYR HB3  H  N N 387 
TYR HD1  H  N N 388 
TYR HD2  H  N N 389 
TYR HE1  H  N N 390 
TYR HE2  H  N N 391 
TYR HH   H  N N 392 
TYR HXT  H  N N 393 
VAL N    N  N N 394 
VAL CA   C  N S 395 
VAL C    C  N N 396 
VAL O    O  N N 397 
VAL CB   C  N N 398 
VAL CG1  C  N N 399 
VAL CG2  C  N N 400 
VAL OXT  O  N N 401 
VAL H    H  N N 402 
VAL H2   H  N N 403 
VAL HA   H  N N 404 
VAL HB   H  N N 405 
VAL HG11 H  N N 406 
VAL HG12 H  N N 407 
VAL HG13 H  N N 408 
VAL HG21 H  N N 409 
VAL HG22 H  N N 410 
VAL HG23 H  N N 411 
VAL HXT  H  N N 412 
WQN C1   C  N N 413 
WQN C10  C  Y N 414 
WQN C11  C  Y N 415 
WQN C12  C  Y N 416 
WQN C13  C  N N 417 
WQN C14  C  N N 418 
WQN C2   C  N N 419 
WQN C3   C  N N 420 
WQN C4   C  N N 421 
WQN C5   C  N N 422 
WQN C6   C  N N 423 
WQN C7   C  Y N 424 
WQN C8   C  Y N 425 
WQN C9   C  Y N 426 
WQN N1   N  N N 427 
WQN N2   N  N N 428 
WQN O1   O  N N 429 
WQN O2   O  N N 430 
WQN O3   O  N N 431 
WQN O4   O  N N 432 
WQN S1   S  N N 433 
WQN BR1  BR N N 434 
WQN H1   H  N N 435 
WQN H2   H  N N 436 
WQN H3   H  N N 437 
WQN H4   H  N N 438 
WQN H5   H  N N 439 
WQN H6   H  N N 440 
WQN H7   H  N N 441 
WQN H8   H  N N 442 
WQN H10  H  N N 443 
WQN H11  H  N N 444 
WQN H12  H  N N 445 
WQN H13  H  N N 446 
WQN H14  H  N N 447 
WQN H15  H  N N 448 
WQN H16  H  N N 449 
WQN H17  H  N N 450 
WQN 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 
WQN C2  C1   sing N N 394 
WQN O1  C1   doub N N 395 
WQN C1  N1   sing N N 396 
WQN N1  C5   sing N N 397 
WQN N1  C3   sing N N 398 
WQN C5  C4   sing N N 399 
WQN C3  C4   sing N N 400 
WQN O3  S1   doub N N 401 
WQN C4  C6   sing N N 402 
WQN C4  O4   sing N N 403 
WQN C6  N2   sing N N 404 
WQN C12 C11  doub Y N 405 
WQN C12 C7   sing Y N 406 
WQN S1  N2   sing N N 407 
WQN S1  C7   sing N N 408 
WQN S1  O2   doub N N 409 
WQN N2  C13  sing N N 410 
WQN C11 C10  sing Y N 411 
WQN O4  C14  sing N N 412 
WQN C7  C8   doub Y N 413 
WQN C14 C13  sing N N 414 
WQN C10 BR1  sing N N 415 
WQN C10 C9   doub Y N 416 
WQN C8  C9   sing Y N 417 
WQN C11 H1   sing N N 418 
WQN C12 H2   sing N N 419 
WQN C13 H3   sing N N 420 
WQN C13 H4   sing N N 421 
WQN C14 H5   sing N N 422 
WQN C14 H6   sing N N 423 
WQN C2  H7   sing N N 424 
WQN C2  H8   sing N N 425 
WQN C3  H10  sing N N 426 
WQN C3  H11  sing N N 427 
WQN C5  H12  sing N N 428 
WQN C5  H13  sing N N 429 
WQN C6  H14  sing N N 430 
WQN C6  H15  sing N N 431 
WQN C8  H16  sing N N 432 
WQN C9  H17  sing N N 433 
WQN C2  CL1  sing N N 434 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM147696 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3IQU 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EW3 
_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]   0.012115 
_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]   0.008854 
_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]   0.015857 
_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  
CA 
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   ? 4.447   12.350  -4.099  1.00 45.72  ? -4  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1   ? 3.080   11.861  -4.200  1.00 39.01  ? -4  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1   ? 2.842   11.133  -5.518  1.00 35.20  ? -4  GLY A C   1 
ATOM   4    O  O   . GLY A 1 1   ? 3.352   11.555  -6.559  1.00 29.59  ? -4  GLY A O   1 
ATOM   5    N  N   . ALA A 1 2   ? 2.057   10.048  -5.455  1.00 27.00  ? -3  ALA A N   1 
ATOM   6    C  CA  . ALA A 1 2   ? 1.798   9.205   -6.610  1.00 27.61  ? -3  ALA A CA  1 
ATOM   7    C  C   . ALA A 1 2   ? 1.048   9.927   -7.730  1.00 22.47  ? -3  ALA A C   1 
ATOM   8    O  O   . ALA A 1 2   ? 1.100   9.487   -8.877  1.00 27.88  ? -3  ALA A O   1 
ATOM   9    C  CB  . ALA A 1 2   ? 1.029   7.962   -6.192  1.00 34.42  ? -3  ALA A CB  1 
ATOM   10   N  N   . MET A 1 3   ? 0.352   11.029  -7.404  1.00 19.40  ? -2  MET A N   1 
ATOM   11   C  CA  . MET A 1 3   ? -0.368  11.807  -8.407  1.00 15.94  ? -2  MET A CA  1 
ATOM   12   C  C   . MET A 1 3   ? 0.418   12.999  -8.951  1.00 14.26  ? -2  MET A C   1 
ATOM   13   O  O   . MET A 1 3   ? -0.086  13.757  -9.777  1.00 15.06  ? -2  MET A O   1 
ATOM   14   C  CB  . MET A 1 3   ? -1.700  12.322  -7.814  1.00 16.87  ? -2  MET A CB  1 
ATOM   15   C  CG  . MET A 1 3   ? -2.580  11.219  -7.316  1.00 17.83  ? -2  MET A CG  1 
ATOM   16   S  SD  . MET A 1 3   ? -3.048  10.019  -8.561  1.00 19.75  ? -2  MET A SD  1 
ATOM   17   C  CE  . MET A 1 3   ? -3.997  8.902   -7.551  1.00 28.47  ? -2  MET A CE  1 
ATOM   18   N  N   . GLY A 1 4   ? 1.680   13.139  -8.532  1.00 16.51  ? -1  GLY A N   1 
ATOM   19   C  CA  . GLY A 1 4   ? 2.520   14.253  -8.947  1.00 15.67  ? -1  GLY A CA  1 
ATOM   20   C  C   . GLY A 1 4   ? 2.737   14.384  -10.453 1.00 16.17  ? -1  GLY A C   1 
ATOM   21   O  O   . GLY A 1 4   ? 2.957   15.484  -10.963 1.00 16.44  ? -1  GLY A O   1 
ATOM   22   N  N   . SER A 1 5   ? 2.675   13.254  -11.163 1.00 13.46  ? 0   SER A N   1 
ATOM   23   C  CA  . SER A 1 5   ? 2.875   13.260  -12.601 1.00 12.52  ? 0   SER A CA  1 
ATOM   24   C  C   . SER A 1 5   ? 1.619   13.463  -13.444 1.00 12.10  ? 0   SER A C   1 
ATOM   25   O  O   . SER A 1 5   ? 1.726   13.552  -14.668 1.00 13.79  ? 0   SER A O   1 
ATOM   26   C  CB  . SER A 1 5   ? 3.558   11.965  -13.044 1.00 16.76  ? 0   SER A CB  1 
ATOM   27   O  OG  . SER A 1 5   ? 2.733   10.851  -12.759 1.00 20.44  ? 0   SER A OG  1 
ATOM   28   N  N   . MET A 1 6   ? 0.426   13.497  -12.825 1.00 12.37  ? 1   MET A N   1 
ATOM   29   C  CA  . MET A 1 6   ? -0.815  13.661  -13.570 1.00 11.27  ? 1   MET A CA  1 
ATOM   30   C  C   . MET A 1 6   ? -1.263  15.122  -13.604 1.00 12.25  ? 1   MET A C   1 
ATOM   31   O  O   . MET A 1 6   ? -1.202  15.817  -12.591 1.00 13.82  ? 1   MET A O   1 
ATOM   32   C  CB  . MET A 1 6   ? -1.922  12.790  -12.971 1.00 14.03  ? 1   MET A CB  1 
ATOM   33   C  CG  . MET A 1 6   ? -2.997  12.470  -13.993 1.00 14.31  ? 1   MET A CG  1 
ATOM   34   S  SD  . MET A 1 6   ? -4.431  11.533  -13.388 1.00 16.20  ? 1   MET A SD  1 
ATOM   35   C  CE  . MET A 1 6   ? -3.622  10.191  -12.498 1.00 17.85  ? 1   MET A CE  1 
ATOM   36   N  N   . GLU A 1 7   ? -1.767  15.557  -14.767 1.00 11.89  ? 2   GLU A N   1 
ATOM   37   C  CA  . GLU A 1 7   ? -2.332  16.890  -14.914 1.00 14.00  ? 2   GLU A CA  1 
ATOM   38   C  C   . GLU A 1 7   ? -3.458  17.155  -13.915 1.00 12.22  ? 2   GLU A C   1 
ATOM   39   O  O   . GLU A 1 7   ? -4.297  16.286  -13.669 1.00 12.91  ? 2   GLU A O   1 
ATOM   40   C  CB  . GLU A 1 7   ? -2.917  17.081  -16.312 1.00 14.23  ? 2   GLU A CB  1 
ATOM   41   C  CG  . GLU A 1 7   ? -1.895  17.126  -17.427 1.00 14.86  ? 2   GLU A CG  1 
ATOM   42   C  CD  . GLU A 1 7   ? -1.252  18.476  -17.609 1.00 19.26  ? 2   GLU A CD  1 
ATOM   43   O  OE1 . GLU A 1 7   ? -1.323  19.311  -16.679 1.00 18.34  ? 2   GLU A OE1 1 
ATOM   44   O  OE2 . GLU A 1 7   ? -0.684  18.705  -18.700 1.00 17.99  ? 2   GLU A OE2 1 
ATOM   45   N  N   . ARG A 1 8   ? -3.513  18.395  -13.406 1.00 14.21  ? 3   ARG A N   1 
ATOM   46   C  CA  . ARG A 1 8   ? -4.615  18.821  -12.559 1.00 12.22  ? 3   ARG A CA  1 
ATOM   47   C  C   . ARG A 1 8   ? -5.974  18.496  -13.184 1.00 12.80  ? 3   ARG A C   1 
ATOM   48   O  O   . ARG A 1 8   ? -6.834  17.934  -12.505 1.00 11.79  ? 3   ARG A O   1 
ATOM   49   C  CB  . ARG A 1 8   ? -4.518  20.327  -12.258 1.00 13.26  ? 3   ARG A CB  1 
ATOM   50   C  CG  . ARG A 1 8   ? -5.474  20.816  -11.178 1.00 11.72  ? 3   ARG A CG  1 
ATOM   51   C  CD  . ARG A 1 8   ? -5.360  22.330  -11.004 1.00 14.20  ? 3   ARG A CD  1 
ATOM   52   N  NE  . ARG A 1 8   ? -6.133  22.808  -9.864  1.00 14.81  ? 3   ARG A NE  1 
ATOM   53   C  CZ  . ARG A 1 8   ? -7.448  22.976  -9.855  1.00 15.68  ? 3   ARG A CZ  1 
ATOM   54   N  NH1 . ARG A 1 8   ? -8.186  22.749  -10.931 1.00 15.08  ? 3   ARG A NH1 1 
ATOM   55   N  NH2 . ARG A 1 8   ? -8.038  23.400  -8.737  1.00 17.58  ? 3   ARG A NH2 1 
ATOM   56   N  N   . ALA A 1 9   ? -6.189  18.888  -14.451 1.00 13.44  ? 4   ALA A N   1 
ATOM   57   C  CA  . ALA A 1 9   ? -7.480  18.676  -15.092 1.00 13.23  ? 4   ALA A CA  1 
ATOM   58   C  C   . ALA A 1 9   ? -7.842  17.191  -15.217 1.00 11.98  ? 4   ALA A C   1 
ATOM   59   O  O   . ALA A 1 9   ? -9.008  16.821  -15.089 1.00 13.31  ? 4   ALA A O   1 
ATOM   60   C  CB  . ALA A 1 9   ? -7.512  19.342  -16.460 1.00 12.33  ? 4   ALA A CB  1 
ATOM   61   N  N   . SER A 1 10  ? -6.828  16.343  -15.429 1.00 12.06  ? 5   SER A N   1 
ATOM   62   C  CA  . SER A 1 10  ? -7.026  14.900  -15.507 1.00 12.21  ? 5   SER A CA  1 
ATOM   63   C  C   . SER A 1 10  ? -7.418  14.305  -14.153 1.00 11.67  ? 5   SER A C   1 
ATOM   64   O  O   . SER A 1 10  ? -8.249  13.395  -14.088 1.00 12.93  ? 5   SER A O   1 
ATOM   65   C  CB  . SER A 1 10  ? -5.766  14.222  -16.047 1.00 12.97  ? 5   SER A CB  1 
ATOM   66   O  OG  . SER A 1 10  ? -5.467  14.668  -17.361 1.00 13.57  ? 5   SER A OG  1 
ATOM   67   N  N   . LEU A 1 11  ? -6.798  14.803  -13.079 1.00 11.92  ? 6   LEU A N   1 
ATOM   68   C  CA  . LEU A 1 11  ? -7.158  14.389  -11.728 1.00 11.94  ? 6   LEU A CA  1 
ATOM   69   C  C   . LEU A 1 11  ? -8.612  14.730  -11.412 1.00 13.89  ? 6   LEU A C   1 
ATOM   70   O  O   . LEU A 1 11  ? -9.331  13.919  -10.826 1.00 12.52  ? 6   LEU A O   1 
ATOM   71   C  CB  . LEU A 1 11  ? -6.217  15.045  -10.713 1.00 13.35  ? 6   LEU A CB  1 
ATOM   72   C  CG  . LEU A 1 11  ? -4.778  14.522  -10.728 1.00 13.96  ? 6   LEU A CG  1 
ATOM   73   C  CD1 . LEU A 1 11  ? -3.842  15.428  -9.986  1.00 14.79  ? 6   LEU A CD1 1 
ATOM   74   C  CD2 . LEU A 1 11  ? -4.681  13.128  -10.084 1.00 13.35  ? 6   LEU A CD2 1 
ATOM   75   N  N   . ILE A 1 12  ? -9.057  15.923  -11.819 1.00 13.27  ? 7   ILE A N   1 
ATOM   76   C  CA  . ILE A 1 12  ? -10.435 16.332  -11.585 1.00 12.94  ? 7   ILE A CA  1 
ATOM   77   C  C   . ILE A 1 12  ? -11.388 15.456  -12.397 1.00 12.68  ? 7   ILE A C   1 
ATOM   78   O  O   . ILE A 1 12  ? -12.398 14.980  -11.885 1.00 12.35  ? 7   ILE A O   1 
ATOM   79   C  CB  . ILE A 1 12  ? -10.617 17.845  -11.885 1.00 14.64  ? 7   ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 12  ? -9.764  18.734  -10.930 1.00 19.88  ? 7   ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 12  ? -12.094 18.218  -11.865 1.00 15.01  ? 7   ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 12  ? -10.097 18.596  -9.459  1.00 20.47  ? 7   ILE A CD1 1 
ATOM   83   N  N   . GLN A 1 13  ? -11.063 15.248  -13.681 1.00 13.09  ? 8   GLN A N   1 
ATOM   84   C  CA  . GLN A 1 13  ? -11.844 14.364  -14.533 1.00 13.90  ? 8   GLN A CA  1 
ATOM   85   C  C   . GLN A 1 13  ? -11.982 12.961  -13.932 1.00 12.37  ? 8   GLN A C   1 
ATOM   86   O  O   . GLN A 1 13  ? -13.078 12.396  -13.909 1.00 15.32  ? 8   GLN A O   1 
ATOM   87   C  CB  . GLN A 1 13  ? -11.211 14.291  -15.936 1.00 15.70  ? 8   GLN A CB  1 
ATOM   88   C  CG  . GLN A 1 13  ? -12.048 13.539  -16.981 1.00 20.24  ? 8   GLN A CG  1 
ATOM   89   C  CD  . GLN A 1 13  ? -11.385 13.534  -18.354 1.00 22.50  ? 8   GLN A CD  1 
ATOM   90   O  OE1 . GLN A 1 13  ? -10.369 14.211  -18.582 1.00 23.81  ? 8   GLN A OE1 1 
ATOM   91   N  NE2 . GLN A 1 13  ? -11.948 12.789  -19.301 1.00 25.10  ? 8   GLN A NE2 1 
ATOM   92   N  N   . LYS A 1 14  ? -10.871 12.400  -13.430 1.00 11.57  ? 9   LYS A N   1 
ATOM   93   C  CA  . LYS A 1 14  ? -10.912 11.052  -12.883 1.00 12.54  ? 9   LYS A CA  1 
ATOM   94   C  C   . LYS A 1 14  ? -11.632 10.994  -11.534 1.00 12.29  ? 9   LYS A C   1 
ATOM   95   O  O   . LYS A 1 14  ? -12.226 9.966   -11.213 1.00 13.36  ? 9   LYS A O   1 
ATOM   96   C  CB  . LYS A 1 14  ? -9.508  10.453  -12.804 1.00 13.10  ? 9   LYS A CB  1 
ATOM   97   C  CG  . LYS A 1 14  ? -8.895  10.168  -14.171 1.00 13.65  ? 9   LYS A CG  1 
ATOM   98   C  CD  . LYS A 1 14  ? -7.487  9.615   -14.089 1.00 13.81  ? 9   LYS A CD  1 
ATOM   99   C  CE  . LYS A 1 14  ? -6.870  9.439   -15.451 1.00 13.83  ? 9   LYS A CE  1 
ATOM   100  N  NZ  . LYS A 1 14  ? -5.485  8.910   -15.391 1.00 14.56  ? 9   LYS A NZ  1 
ATOM   101  N  N   . ALA A 1 15  ? -11.572 12.077  -10.739 1.00 11.80  ? 10  ALA A N   1 
ATOM   102  C  CA  . ALA A 1 15  ? -12.382 12.145  -9.527  1.00 12.70  ? 10  ALA A CA  1 
ATOM   103  C  C   . ALA A 1 15  ? -13.872 12.014  -9.860  1.00 12.13  ? 10  ALA A C   1 
ATOM   104  O  O   . ALA A 1 15  ? -14.612 11.323  -9.156  1.00 11.41  ? 10  ALA A O   1 
ATOM   105  C  CB  . ALA A 1 15  ? -12.101 13.439  -8.755  1.00 10.46  ? 10  ALA A CB  1 
ATOM   106  N  N   . LYS A 1 16  ? -14.327 12.681  -10.930 1.00 11.68  ? 11  LYS A N   1 
ATOM   107  C  CA  . LYS A 1 16  ? -15.717 12.596  -11.342 1.00 12.41  ? 11  LYS A CA  1 
ATOM   108  C  C   . LYS A 1 16  ? -16.098 11.188  -11.800 1.00 12.00  ? 11  LYS A C   1 
ATOM   109  O  O   . LYS A 1 16  ? -17.186 10.703  -11.473 1.00 15.29  ? 11  LYS A O   1 
ATOM   110  C  CB  . LYS A 1 16  ? -16.004 13.632  -12.426 1.00 13.29  ? 11  LYS A CB  1 
ATOM   111  C  CG  . LYS A 1 16  ? -15.978 15.062  -11.901 1.00 14.79  ? 11  LYS A CG  1 
ATOM   112  C  CD  . LYS A 1 16  ? -16.099 16.078  -13.028 1.00 15.80  ? 11  LYS A CD  1 
ATOM   113  C  CE  . LYS A 1 16  ? -15.829 17.499  -12.598 1.00 22.53  ? 11  LYS A CE  1 
ATOM   114  N  NZ  . LYS A 1 16  ? -15.912 18.448  -13.746 1.00 25.46  ? 11  LYS A NZ  1 
ATOM   115  N  N   . LEU A 1 17  ? -15.197 10.537  -12.539 1.00 12.51  ? 12  LEU A N   1 
ATOM   116  C  CA  . LEU A 1 17  ? -15.382 9.147   -12.944 1.00 12.42  ? 12  LEU A CA  1 
ATOM   117  C  C   . LEU A 1 17  ? -15.460 8.201   -11.742 1.00 14.03  ? 12  LEU A C   1 
ATOM   118  O  O   . LEU A 1 17  ? -16.332 7.340   -11.688 1.00 13.71  ? 12  LEU A O   1 
ATOM   119  C  CB  . LEU A 1 17  ? -14.238 8.691   -13.868 1.00 11.89  ? 12  LEU A CB  1 
ATOM   120  C  CG  . LEU A 1 17  ? -14.181 9.341   -15.260 1.00 13.90  ? 12  LEU A CG  1 
ATOM   121  C  CD1 . LEU A 1 17  ? -12.910 9.000   -15.982 1.00 14.90  ? 12  LEU A CD1 1 
ATOM   122  C  CD2 . LEU A 1 17  ? -15.364 8.939   -16.126 1.00 16.44  ? 12  LEU A CD2 1 
ATOM   123  N  N   . ALA A 1 18  ? -14.562 8.383   -10.770 1.00 13.04  ? 13  ALA A N   1 
ATOM   124  C  CA  . ALA A 1 18  ? -14.534 7.564   -9.567  1.00 12.86  ? 13  ALA A CA  1 
ATOM   125  C  C   . ALA A 1 18  ? -15.825 7.719   -8.763  1.00 13.43  ? 13  ALA A C   1 
ATOM   126  O  O   . ALA A 1 18  ? -16.358 6.735   -8.240  1.00 13.92  ? 13  ALA A O   1 
ATOM   127  C  CB  . ALA A 1 18  ? -13.318 7.922   -8.719  1.00 15.82  ? 13  ALA A CB  1 
ATOM   128  N  N   . GLU A 1 19  ? -16.347 8.948   -8.676  1.00 15.34  ? 14  GLU A N   1 
ATOM   129  C  CA  . GLU A 1 19  ? -17.638 9.174   -8.040  1.00 15.34  ? 14  GLU A CA  1 
ATOM   130  C  C   . GLU A 1 19  ? -18.744 8.354   -8.714  1.00 16.05  ? 14  GLU A C   1 
ATOM   131  O  O   . GLU A 1 19  ? -19.517 7.684   -8.033  1.00 17.32  ? 14  GLU A O   1 
ATOM   132  C  CB  . GLU A 1 19  ? -18.010 10.662  -8.046  1.00 16.37  ? 14  GLU A CB  1 
ATOM   133  C  CG  . GLU A 1 19  ? -19.233 10.993  -7.217  1.00 18.39  ? 14  GLU A CG  1 
ATOM   134  C  CD  . GLU A 1 19  ? -19.659 12.449  -7.260  1.00 23.28  ? 14  GLU A CD  1 
ATOM   135  O  OE1 . GLU A 1 19  ? -19.250 13.170  -8.198  1.00 25.23  ? 14  GLU A OE1 1 
ATOM   136  O  OE2 . GLU A 1 19  ? -20.398 12.869  -6.341  1.00 27.62  ? 14  GLU A OE2 1 
ATOM   137  N  N   . GLN A 1 20  ? -18.799 8.383   -10.049 1.00 16.58  ? 15  GLN A N   1 
ATOM   138  C  CA  . GLN A 1 20  ? -19.809 7.630   -10.784 1.00 17.60  ? 15  GLN A CA  1 
ATOM   139  C  C   . GLN A 1 20  ? -19.700 6.122   -10.562 1.00 17.80  ? 15  GLN A C   1 
ATOM   140  O  O   . GLN A 1 20  ? -20.713 5.422   -10.544 1.00 22.51  ? 15  GLN A O   1 
ATOM   141  C  CB  . GLN A 1 20  ? -19.711 7.910   -12.285 1.00 18.87  ? 15  GLN A CB  1 
ATOM   142  C  CG  . GLN A 1 20  ? -20.097 9.337   -12.659 1.00 21.62  ? 15  GLN A CG  1 
ATOM   143  C  CD  . GLN A 1 20  ? -19.979 9.557   -14.149 1.00 33.58  ? 15  GLN A CD  1 
ATOM   144  O  OE1 . GLN A 1 20  ? -20.865 9.201   -14.934 1.00 30.93  ? 15  GLN A OE1 1 
ATOM   145  N  NE2 . GLN A 1 20  ? -18.873 10.142  -14.571 1.00 32.56  ? 15  GLN A NE2 1 
ATOM   146  N  N   . ALA A 1 21  ? -18.465 5.636   -10.407 1.00 14.92  ? 16  ALA A N   1 
ATOM   147  C  CA  . ALA A 1 21  ? -18.173 4.229   -10.164 1.00 15.11  ? 16  ALA A CA  1 
ATOM   148  C  C   . ALA A 1 21  ? -18.233 3.835   -8.686  1.00 17.67  ? 16  ALA A C   1 
ATOM   149  O  O   . ALA A 1 21  ? -17.965 2.683   -8.348  1.00 16.00  ? 16  ALA A O   1 
ATOM   150  C  CB  . ALA A 1 21  ? -16.799 3.907   -10.736 1.00 16.60  ? 16  ALA A CB  1 
ATOM   151  N  N   . GLU A 1 22  ? -18.557 4.796   -7.808  1.00 14.83  ? 17  GLU A N   1 
ATOM   152  C  CA  . GLU A 1 22  ? -18.582 4.570   -6.365  1.00 15.49  ? 17  GLU A CA  1 
ATOM   153  C  C   . GLU A 1 22  ? -17.243 4.055   -5.823  1.00 16.99  ? 17  GLU A C   1 
ATOM   154  O  O   . GLU A 1 22  ? -17.192 3.221   -4.918  1.00 19.43  ? 17  GLU A O   1 
ATOM   155  C  CB  . GLU A 1 22  ? -19.784 3.657   -5.982  1.00 18.66  ? 17  GLU A CB  1 
ATOM   156  C  CG  . GLU A 1 22  ? -21.126 4.313   -6.288  1.00 24.65  ? 17  GLU A CG  1 
ATOM   157  C  CD  . GLU A 1 22  ? -22.372 3.591   -5.806  1.00 33.60  ? 17  GLU A CD  1 
ATOM   158  O  OE1 . GLU A 1 22  ? -22.259 2.474   -5.254  1.00 33.60  ? 17  GLU A OE1 1 
ATOM   159  O  OE2 . GLU A 1 22  ? -23.471 4.157   -5.988  1.00 49.32  ? 17  GLU A OE2 1 
ATOM   160  N  N   . ARG A 1 23  ? -16.146 4.615   -6.350  1.00 14.10  ? 18  ARG A N   1 
ATOM   161  C  CA  . ARG A 1 23  ? -14.790 4.273   -5.945  1.00 13.36  ? 18  ARG A CA  1 
ATOM   162  C  C   . ARG A 1 23  ? -14.234 5.449   -5.146  1.00 16.78  ? 18  ARG A C   1 
ATOM   163  O  O   . ARG A 1 23  ? -13.421 6.225   -5.647  1.00 13.92  ? 18  ARG A O   1 
ATOM   164  C  CB  . ARG A 1 23  ? -13.928 3.986   -7.185  1.00 15.54  ? 18  ARG A CB  1 
ATOM   165  C  CG  . ARG A 1 23  ? -14.329 2.694   -7.888  1.00 15.76  ? 18  ARG A CG  1 
ATOM   166  C  CD  . ARG A 1 23  ? -13.587 1.513   -7.300  1.00 16.48  ? 18  ARG A CD  1 
ATOM   167  N  NE  . ARG A 1 23  ? -12.173 1.604   -7.645  1.00 18.13  ? 18  ARG A NE  1 
ATOM   168  C  CZ  . ARG A 1 23  ? -11.294 0.617   -7.533  1.00 20.24  ? 18  ARG A CZ  1 
ATOM   169  N  NH1 . ARG A 1 23  ? -11.661 -0.601  -7.168  1.00 19.73  ? 18  ARG A NH1 1 
ATOM   170  N  NH2 . ARG A 1 23  ? -10.016 0.857   -7.798  1.00 19.24  ? 18  ARG A NH2 1 
ATOM   171  N  N   . TYR A 1 24  ? -14.674 5.570   -3.889  1.00 13.42  ? 19  TYR A N   1 
ATOM   172  C  CA  . TYR A 1 24  ? -14.424 6.788   -3.134  1.00 14.24  ? 19  TYR A CA  1 
ATOM   173  C  C   . TYR A 1 24  ? -12.990 6.932   -2.625  1.00 14.83  ? 19  TYR A C   1 
ATOM   174  O  O   . TYR A 1 24  ? -12.506 8.044   -2.473  1.00 12.30  ? 19  TYR A O   1 
ATOM   175  C  CB  . TYR A 1 24  ? -15.455 6.910   -1.997  1.00 15.50  ? 19  TYR A CB  1 
ATOM   176  C  CG  . TYR A 1 24  ? -16.871 7.010   -2.523  1.00 17.99  ? 19  TYR A CG  1 
ATOM   177  C  CD1 . TYR A 1 24  ? -17.291 8.124   -3.241  1.00 18.80  ? 19  TYR A CD1 1 
ATOM   178  C  CD2 . TYR A 1 24  ? -17.780 5.978   -2.330  1.00 19.99  ? 19  TYR A CD2 1 
ATOM   179  C  CE1 . TYR A 1 24  ? -18.579 8.208   -3.751  1.00 19.95  ? 19  TYR A CE1 1 
ATOM   180  C  CE2 . TYR A 1 24  ? -19.075 6.054   -2.833  1.00 21.36  ? 19  TYR A CE2 1 
ATOM   181  C  CZ  . TYR A 1 24  ? -19.470 7.172   -3.537  1.00 19.87  ? 19  TYR A CZ  1 
ATOM   182  O  OH  . TYR A 1 24  ? -20.745 7.265   -4.030  1.00 27.39  ? 19  TYR A OH  1 
ATOM   183  N  N   . GLU A 1 25  ? -12.297 5.816   -2.358  1.00 14.10  ? 20  GLU A N   1 
ATOM   184  C  CA  . GLU A 1 25  ? -10.883 5.876   -2.012  1.00 14.26  ? 20  GLU A CA  1 
ATOM   185  C  C   . GLU A 1 25  ? -10.076 6.465   -3.172  1.00 11.37  ? 20  GLU A C   1 
ATOM   186  O  O   . GLU A 1 25  ? -9.258  7.364   -2.973  1.00 12.57  ? 20  GLU A O   1 
ATOM   187  C  CB  . GLU A 1 25  ? -10.378 4.490   -1.602  1.00 15.77  ? 20  GLU A CB  1 
ATOM   188  C  CG  . GLU A 1 25  ? -8.947  4.447   -1.130  1.00 28.29  ? 20  GLU A CG  1 
ATOM   189  C  CD  . GLU A 1 25  ? -8.534  3.084   -0.605  1.00 45.07  ? 20  GLU A CD  1 
ATOM   190  O  OE1 . GLU A 1 25  ? -9.235  2.562   0.292   1.00 49.84  ? 20  GLU A OE1 1 
ATOM   191  O  OE2 . GLU A 1 25  ? -7.519  2.536   -1.093  1.00 53.05  ? 20  GLU A OE2 1 
ATOM   192  N  N   . ASP A 1 26  ? -10.333 5.995   -4.399  1.00 12.50  ? 21  ASP A N   1 
ATOM   193  C  CA  . ASP A 1 26  ? -9.680  6.567   -5.567  1.00 11.91  ? 21  ASP A CA  1 
ATOM   194  C  C   . ASP A 1 26  ? -10.031 8.049   -5.715  1.00 13.47  ? 21  ASP A C   1 
ATOM   195  O  O   . ASP A 1 26  ? -9.168  8.872   -6.015  1.00 13.17  ? 21  ASP A O   1 
ATOM   196  C  CB  . ASP A 1 26  ? -10.096 5.844   -6.854  1.00 12.95  ? 21  ASP A CB  1 
ATOM   197  C  CG  . ASP A 1 26  ? -9.621  4.418   -7.022  1.00 13.95  ? 21  ASP A CG  1 
ATOM   198  O  OD1 . ASP A 1 26  ? -8.706  4.007   -6.277  1.00 17.54  ? 21  ASP A OD1 1 
ATOM   199  O  OD2 . ASP A 1 26  ? -10.206 3.695   -7.891  1.00 15.56  ? 21  ASP A OD2 1 
ATOM   200  N  N   . MET A 1 27  ? -11.315 8.381   -5.549  1.00 13.07  ? 22  MET A N   1 
ATOM   201  C  CA  . MET A 1 27  ? -11.777 9.755   -5.701  1.00 12.75  ? 22  MET A CA  1 
ATOM   202  C  C   . MET A 1 27  ? -11.004 10.677  -4.756  1.00 12.07  ? 22  MET A C   1 
ATOM   203  O  O   . MET A 1 27  ? -10.598 11.770  -5.148  1.00 11.53  ? 22  MET A O   1 
ATOM   204  C  CB  . MET A 1 27  ? -13.295 9.822   -5.428  1.00 11.99  ? 22  MET A CB  1 
ATOM   205  C  CG  . MET A 1 27  ? -13.917 11.169  -5.726  1.00 12.27  ? 22  MET A CG  1 
ATOM   206  S  SD  . MET A 1 27  ? -15.644 11.218  -5.210  1.00 13.72  ? 22  MET A SD  1 
ATOM   207  C  CE  . MET A 1 27  ? -16.118 12.903  -5.748  1.00 13.26  ? 22  MET A CE  1 
ATOM   208  N  N   . ALA A 1 28  ? -10.842 10.245  -3.501  1.00 9.98   ? 23  ALA A N   1 
ATOM   209  C  CA  . ALA A 1 28  ? -10.115 11.020  -2.510  1.00 12.71  ? 23  ALA A CA  1 
ATOM   210  C  C   . ALA A 1 28  ? -8.643  11.189  -2.892  1.00 12.18  ? 23  ALA A C   1 
ATOM   211  O  O   . ALA A 1 28  ? -8.076  12.276  -2.758  1.00 12.96  ? 23  ALA A O   1 
ATOM   212  C  CB  . ALA A 1 28  ? -10.250 10.362  -1.145  1.00 13.72  ? 23  ALA A CB  1 
ATOM   213  N  N   . ALA A 1 29  ? -8.003  10.115  -3.374  1.00 12.39  ? 24  ALA A N   1 
ATOM   214  C  CA  . ALA A 1 29  ? -6.616  10.219  -3.794  1.00 12.63  ? 24  ALA A CA  1 
ATOM   215  C  C   . ALA A 1 29  ? -6.439  11.188  -4.966  1.00 10.99  ? 24  ALA A C   1 
ATOM   216  O  O   . ALA A 1 29  ? -5.464  11.938  -5.025  1.00 11.46  ? 24  ALA A O   1 
ATOM   217  C  CB  . ALA A 1 29  ? -6.065  8.857   -4.148  1.00 13.62  ? 24  ALA A CB  1 
ATOM   218  N  N   . PHE A 1 30  ? -7.379  11.162  -5.915  1.00 11.96  ? 25  PHE A N   1 
ATOM   219  C  CA  . PHE A 1 30  ? -7.312  12.067  -7.048  1.00 13.43  ? 25  PHE A CA  1 
ATOM   220  C  C   . PHE A 1 30  ? -7.454  13.517  -6.582  1.00 11.76  ? 25  PHE A C   1 
ATOM   221  O  O   . PHE A 1 30  ? -6.713  14.397  -7.029  1.00 12.10  ? 25  PHE A O   1 
ATOM   222  C  CB  . PHE A 1 30  ? -8.387  11.706  -8.096  1.00 12.79  ? 25  PHE A CB  1 
ATOM   223  C  CG  . PHE A 1 30  ? -8.193  10.405  -8.856  1.00 11.19  ? 25  PHE A CG  1 
ATOM   224  C  CD1 . PHE A 1 30  ? -6.952  10.057  -9.359  1.00 13.88  ? 25  PHE A CD1 1 
ATOM   225  C  CD2 . PHE A 1 30  ? -9.273  9.574   -9.130  1.00 12.86  ? 25  PHE A CD2 1 
ATOM   226  C  CE1 . PHE A 1 30  ? -6.775  8.874   -10.072 1.00 13.92  ? 25  PHE A CE1 1 
ATOM   227  C  CE2 . PHE A 1 30  ? -9.094  8.395   -9.857  1.00 13.33  ? 25  PHE A CE2 1 
ATOM   228  C  CZ  . PHE A 1 30  ? -7.847  8.055   -10.319 1.00 14.88  ? 25  PHE A CZ  1 
ATOM   229  N  N   . MET A 1 31  ? -8.401  13.769  -5.663  1.00 10.78  ? 26  MET A N   1 
ATOM   230  C  CA  . MET A 1 31  ? -8.624  15.121  -5.178  1.00 10.90  ? 26  MET A CA  1 
ATOM   231  C  C   . MET A 1 31  ? -7.472  15.603  -4.298  1.00 12.15  ? 26  MET A C   1 
ATOM   232  O  O   . MET A 1 31  ? -7.123  16.779  -4.349  1.00 11.64  ? 26  MET A O   1 
ATOM   233  C  CB  . MET A 1 31  ? -9.976  15.246  -4.474  1.00 12.11  ? 26  MET A CB  1 
ATOM   234  C  CG  . MET A 1 31  ? -11.177 15.174  -5.442  1.00 13.37  ? 26  MET A CG  1 
ATOM   235  S  SD  . MET A 1 31  ? -11.037 16.281  -6.885  1.00 14.01  ? 26  MET A SD  1 
ATOM   236  C  CE  . MET A 1 31  ? -10.888 17.881  -6.099  1.00 12.25  ? 26  MET A CE  1 
ATOM   237  N  N   . LYS A 1 32  ? -6.878  14.716  -3.493  1.00 11.76  ? 27  LYS A N   1 
ATOM   238  C  CA  . LYS A 1 32  ? -5.659  15.065  -2.780  1.00 12.03  ? 27  LYS A CA  1 
ATOM   239  C  C   . LYS A 1 32  ? -4.571  15.515  -3.758  1.00 12.05  ? 27  LYS A C   1 
ATOM   240  O  O   . LYS A 1 32  ? -3.904  16.537  -3.545  1.00 12.97  ? 27  LYS A O   1 
ATOM   241  C  CB  . LYS A 1 32  ? -5.190  13.883  -1.916  1.00 11.87  ? 27  LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 32  ? -3.883  14.149  -1.103  1.00 13.63  ? 27  LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 32  ? -3.541  12.996  -0.152  1.00 16.86  ? 27  LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 32  ? -2.357  13.222  0.775   1.00 19.54  ? 27  LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 32  ? -1.057  13.191  0.060   1.00 22.60  ? 27  LYS A NZ  1 
ATOM   246  N  N   . GLY A 1 33  ? -4.411  14.757  -4.853  1.00 11.83  ? 28  GLY A N   1 
ATOM   247  C  CA  . GLY A 1 33  ? -3.459  15.110  -5.893  1.00 11.91  ? 28  GLY A CA  1 
ATOM   248  C  C   . GLY A 1 33  ? -3.745  16.493  -6.471  1.00 13.17  ? 28  GLY A C   1 
ATOM   249  O  O   . GLY A 1 33  ? -2.830  17.290  -6.675  1.00 11.97  ? 28  GLY A O   1 
ATOM   250  N  N   . ALA A 1 34  ? -5.021  16.777  -6.743  1.00 11.19  ? 29  ALA A N   1 
ATOM   251  C  CA  . ALA A 1 34  ? -5.397  18.070  -7.291  1.00 12.91  ? 29  ALA A CA  1 
ATOM   252  C  C   . ALA A 1 34  ? -5.088  19.210  -6.319  1.00 11.52  ? 29  ALA A C   1 
ATOM   253  O  O   . ALA A 1 34  ? -4.542  20.243  -6.717  1.00 12.54  ? 29  ALA A O   1 
ATOM   254  C  CB  . ALA A 1 34  ? -6.857  18.089  -7.702  1.00 12.52  ? 29  ALA A CB  1 
ATOM   255  N  N   . VAL A 1 35  ? -5.401  19.027  -5.035  1.00 13.26  ? 30  VAL A N   1 
ATOM   256  C  CA  . VAL A 1 35  ? -5.067  20.040  -4.042  1.00 12.42  ? 30  VAL A CA  1 
ATOM   257  C  C   . VAL A 1 35  ? -3.562  20.315  -4.009  1.00 14.19  ? 30  VAL A C   1 
ATOM   258  O  O   . VAL A 1 35  ? -3.131  21.474  -3.939  1.00 13.09  ? 30  VAL A O   1 
ATOM   259  C  CB  . VAL A 1 35  ? -5.570  19.642  -2.636  1.00 14.42  ? 30  VAL A CB  1 
ATOM   260  C  CG1 . VAL A 1 35  ? -4.997  20.575  -1.562  1.00 14.03  ? 30  VAL A CG1 1 
ATOM   261  C  CG2 . VAL A 1 35  ? -7.086  19.629  -2.581  1.00 13.12  ? 30  VAL A CG2 1 
ATOM   262  N  N   . GLU A 1 36  ? -2.759  19.246  -4.073  1.00 13.22  ? 31  GLU A N   1 
ATOM   263  C  CA  . GLU A 1 36  ? -1.313  19.391  -3.966  1.00 15.12  ? 31  GLU A CA  1 
ATOM   264  C  C   . GLU A 1 36  ? -0.655  20.078  -5.168  1.00 12.29  ? 31  GLU A C   1 
ATOM   265  O  O   . GLU A 1 36  ? 0.520   20.429  -5.104  1.00 13.23  ? 31  GLU A O   1 
ATOM   266  C  CB  . GLU A 1 36  ? -0.659  18.030  -3.675  1.00 14.66  ? 31  GLU A CB  1 
ATOM   267  C  CG  . GLU A 1 36  ? -0.997  17.558  -2.272  1.00 15.70  ? 31  GLU A CG  1 
ATOM   268  C  CD  . GLU A 1 36  ? -0.560  16.162  -1.877  1.00 18.84  ? 31  GLU A CD  1 
ATOM   269  O  OE1 . GLU A 1 36  ? -0.112  15.391  -2.751  1.00 24.21  ? 31  GLU A OE1 1 
ATOM   270  O  OE2 . GLU A 1 36  ? -0.700  15.838  -0.675  1.00 21.06  ? 31  GLU A OE2 1 
ATOM   271  N  N   . LYS A 1 37  ? -1.414  20.337  -6.236  1.00 13.00  ? 32  LYS A N   1 
ATOM   272  C  CA  . LYS A 1 37  ? -0.921  21.159  -7.334  1.00 13.17  ? 32  LYS A CA  1 
ATOM   273  C  C   . LYS A 1 37  ? -0.702  22.611  -6.908  1.00 13.74  ? 32  LYS A C   1 
ATOM   274  O  O   . LYS A 1 37  ? 0.015   23.358  -7.578  1.00 13.74  ? 32  LYS A O   1 
ATOM   275  C  CB  . LYS A 1 37  ? -1.881  21.128  -8.518  1.00 13.21  ? 32  LYS A CB  1 
ATOM   276  C  CG  . LYS A 1 37  ? -2.078  19.732  -9.155  1.00 12.08  ? 32  LYS A CG  1 
ATOM   277  C  CD  . LYS A 1 37  ? -0.820  19.123  -9.716  1.00 12.91  ? 32  LYS A CD  1 
ATOM   278  C  CE  . LYS A 1 37  ? -1.030  17.693  -10.148 1.00 13.43  ? 32  LYS A CE  1 
ATOM   279  N  NZ  . LYS A 1 37  ? 0.238   17.018  -10.565 1.00 15.60  ? 32  LYS A NZ  1 
ATOM   280  N  N   . GLY A 1 38  ? -1.362  23.007  -5.813  1.00 14.28  ? 33  GLY A N   1 
ATOM   281  C  CA  . GLY A 1 38  ? -1.112  24.294  -5.179  1.00 14.03  ? 33  GLY A CA  1 
ATOM   282  C  C   . GLY A 1 38  ? -2.039  25.438  -5.585  1.00 13.88  ? 33  GLY A C   1 
ATOM   283  O  O   . GLY A 1 38  ? -1.956  26.540  -5.027  1.00 16.90  ? 33  GLY A O   1 
ATOM   284  N  N   . GLU A 1 39  ? -2.903  25.208  -6.580  1.00 14.78  ? 34  GLU A N   1 
ATOM   285  C  CA  . GLU A 1 39  ? -3.885  26.198  -6.990  1.00 16.94  ? 34  GLU A CA  1 
ATOM   286  C  C   . GLU A 1 39  ? -5.110  26.139  -6.079  1.00 15.65  ? 34  GLU A C   1 
ATOM   287  O  O   . GLU A 1 39  ? -5.432  25.100  -5.505  1.00 15.93  ? 34  GLU A O   1 
ATOM   288  C  CB  . GLU A 1 39  ? -4.314  25.996  -8.443  1.00 19.44  ? 34  GLU A CB  1 
ATOM   289  C  CG  . GLU A 1 39  ? -3.173  26.060  -9.441  1.00 21.36  ? 34  GLU A CG  1 
ATOM   290  C  CD  . GLU A 1 39  ? -2.653  27.444  -9.791  1.00 36.60  ? 34  GLU A CD  1 
ATOM   291  O  OE1 . GLU A 1 39  ? -3.136  28.450  -9.221  1.00 32.26  ? 34  GLU A OE1 1 
ATOM   292  O  OE2 . GLU A 1 39  ? -1.762  27.520  -10.666 1.00 49.30  ? 34  GLU A OE2 1 
ATOM   293  N  N   . GLU A 1 40  ? -5.802  27.270  -5.942  1.00 14.94  ? 35  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 40  ? -7.063  27.283  -5.223  1.00 14.30  ? 35  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 40  ? -8.099  26.402  -5.938  1.00 16.92  ? 35  GLU A C   1 
ATOM   296  O  O   . GLU A 1 40  ? -7.932  26.041  -7.105  1.00 16.20  ? 35  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 40  ? -7.541  28.748  -5.024  1.00 16.61  ? 35  GLU A CB  1 
ATOM   298  C  CG  . GLU A 1 40  ? -6.610  29.534  -4.082  1.00 17.36  ? 35  GLU A CG  1 
ATOM   299  C  CD  . GLU A 1 40  ? -6.984  30.981  -3.782  1.00 26.93  ? 35  GLU A CD  1 
ATOM   300  O  OE1 . GLU A 1 40  ? -8.187  31.272  -3.605  1.00 26.11  ? 35  GLU A OE1 1 
ATOM   301  O  OE2 . GLU A 1 40  ? -6.066  31.820  -3.662  1.00 20.63  ? 35  GLU A OE2 1 
ATOM   302  N  N   . LEU A 1 41  ? -9.119  25.957  -5.193  1.00 13.08  ? 36  LEU A N   1 
ATOM   303  C  CA  . LEU A 1 41  ? -10.185 25.131  -5.736  1.00 13.32  ? 36  LEU A CA  1 
ATOM   304  C  C   . LEU A 1 41  ? -11.439 25.952  -6.012  1.00 16.00  ? 36  LEU A C   1 
ATOM   305  O  O   . LEU A 1 41  ? -11.834 26.795  -5.204  1.00 16.70  ? 36  LEU A O   1 
ATOM   306  C  CB  . LEU A 1 41  ? -10.605 24.019  -4.753  1.00 16.19  ? 36  LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 41  ? -9.543  23.050  -4.254  1.00 27.94  ? 36  LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 41  ? -10.184 21.814  -3.632  1.00 22.76  ? 36  LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 41  ? -8.611  22.647  -5.323  1.00 24.99  ? 36  LEU A CD2 1 
ATOM   310  N  N   . SER A 1 42  ? -12.102 25.647  -7.126  1.00 13.59  ? 37  SER A N   1 
ATOM   311  C  CA  . SER A 1 42  ? -13.443 26.157  -7.376  1.00 12.64  ? 37  SER A CA  1 
ATOM   312  C  C   . SER A 1 42  ? -14.512 25.543  -6.466  1.00 13.84  ? 37  SER A C   1 
ATOM   313  O  O   . SER A 1 42  ? -14.266 24.560  -5.767  1.00 12.58  ? 37  SER A O   1 
ATOM   314  C  CB  . SER A 1 42  ? -13.835 25.866  -8.815  1.00 14.77  ? 37  SER A CB  1 
ATOM   315  O  OG  . SER A 1 42  ? -14.078 24.476  -8.958  1.00 14.19  ? 37  SER A OG  1 
ATOM   316  N  N   . CYS A 1 43  ? -15.738 26.082  -6.515  1.00 14.36  ? 38  CYS A N   1 
ATOM   317  C  CA  . CYS A 1 43  ? -16.839 25.542  -5.730  1.00 13.92  ? 38  CYS A CA  1 
ATOM   318  C  C   . CYS A 1 43  ? -17.082 24.064  -6.035  1.00 13.71  ? 38  CYS A C   1 
ATOM   319  O  O   . CYS A 1 43  ? -17.216 23.236  -5.122  1.00 14.07  ? 38  CYS A O   1 
ATOM   320  C  CB  . CYS A 1 43  ? -18.109 26.373  -5.961  1.00 15.39  ? 38  CYS A CB  1 
ATOM   321  S  SG  . CYS A 1 43  ? -19.604 25.684  -5.202  1.00 21.52  ? 38  CYS A SG  1 
ATOM   322  N  N   . GLU A 1 44  ? -17.147 23.739  -7.330  1.00 13.09  ? 39  GLU A N   1 
ATOM   323  C  CA  . GLU A 1 44  ? -17.369 22.365  -7.766  1.00 13.35  ? 39  GLU A CA  1 
ATOM   324  C  C   . GLU A 1 44  ? -16.256 21.438  -7.285  1.00 13.17  ? 39  GLU A C   1 
ATOM   325  O  O   . GLU A 1 44  ? -16.523 20.327  -6.841  1.00 12.33  ? 39  GLU A O   1 
ATOM   326  C  CB  . GLU A 1 44  ? -17.481 22.287  -9.302  1.00 18.56  ? 39  GLU A CB  1 
ATOM   327  C  CG  . GLU A 1 44  ? -17.902 20.921  -9.825  1.00 23.40  ? 39  GLU A CG  1 
ATOM   328  C  CD  . GLU A 1 44  ? -18.041 20.810  -11.337 1.00 34.78  ? 39  GLU A CD  1 
ATOM   329  O  OE1 . GLU A 1 44  ? -17.719 21.785  -12.054 1.00 30.51  ? 39  GLU A OE1 1 
ATOM   330  O  OE2 . GLU A 1 44  ? -18.476 19.734  -11.805 1.00 31.93  ? 39  GLU A OE2 1 
ATOM   331  N  N   . GLU A 1 45  ? -15.010 21.903  -7.373  1.00 11.66  ? 40  GLU A N   1 
ATOM   332  C  CA  . GLU A 1 45  ? -13.853 21.135  -6.922  1.00 11.78  ? 40  GLU A CA  1 
ATOM   333  C  C   . GLU A 1 45  ? -13.832 20.930  -5.403  1.00 14.14  ? 40  GLU A C   1 
ATOM   334  O  O   . GLU A 1 45  ? -13.498 19.840  -4.933  1.00 13.26  ? 40  GLU A O   1 
ATOM   335  C  CB  . GLU A 1 45  ? -12.559 21.807  -7.397  1.00 12.77  ? 40  GLU A CB  1 
ATOM   336  C  CG  . GLU A 1 45  ? -12.399 21.792  -8.920  1.00 13.43  ? 40  GLU A CG  1 
ATOM   337  C  CD  . GLU A 1 45  ? -11.373 22.769  -9.473  1.00 13.07  ? 40  GLU A CD  1 
ATOM   338  O  OE1 . GLU A 1 45  ? -10.855 23.586  -8.688  1.00 13.63  ? 40  GLU A OE1 1 
ATOM   339  O  OE2 . GLU A 1 45  ? -11.087 22.724  -10.698 1.00 15.49  ? 40  GLU A OE2 1 
ATOM   340  N  N   . ARG A 1 46  ? -14.201 21.962  -4.628  1.00 12.34  ? 41  ARG A N   1 
ATOM   341  C  CA  . ARG A 1 46  ? -14.368 21.789  -3.189  1.00 11.97  ? 41  ARG A CA  1 
ATOM   342  C  C   . ARG A 1 46  ? -15.410 20.710  -2.879  1.00 13.16  ? 41  ARG A C   1 
ATOM   343  O  O   . ARG A 1 46  ? -15.232 19.900  -1.968  1.00 14.40  ? 41  ARG A O   1 
ATOM   344  C  CB  . ARG A 1 46  ? -14.759 23.117  -2.502  1.00 13.36  ? 41  ARG A CB  1 
ATOM   345  C  CG  . ARG A 1 46  ? -13.684 24.163  -2.512  1.00 16.11  ? 41  ARG A CG  1 
ATOM   346  C  CD  . ARG A 1 46  ? -14.030 25.390  -1.681  1.00 15.70  ? 41  ARG A CD  1 
ATOM   347  N  NE  . ARG A 1 46  ? -15.198 26.108  -2.183  1.00 15.82  ? 41  ARG A NE  1 
ATOM   348  C  CZ  . ARG A 1 46  ? -15.163 27.230  -2.891  1.00 15.75  ? 41  ARG A CZ  1 
ATOM   349  N  NH1 . ARG A 1 46  ? -14.062 27.633  -3.506  1.00 17.60  ? 41  ARG A NH1 1 
ATOM   350  N  NH2 . ARG A 1 46  ? -16.278 27.943  -3.031  1.00 17.69  ? 41  ARG A NH2 1 
ATOM   351  N  N   . ASN A 1 47  ? -16.508 20.690  -3.638  1.00 13.61  ? 42  ASN A N   1 
ATOM   352  C  CA  . ASN A 1 47  ? -17.520 19.662  -3.465  1.00 15.83  ? 42  ASN A CA  1 
ATOM   353  C  C   . ASN A 1 47  ? -16.975 18.260  -3.725  1.00 13.19  ? 42  ASN A C   1 
ATOM   354  O  O   . ASN A 1 47  ? -17.308 17.325  -3.004  1.00 13.50  ? 42  ASN A O   1 
ATOM   355  C  CB  . ASN A 1 47  ? -18.724 19.902  -4.381  1.00 16.27  ? 42  ASN A CB  1 
ATOM   356  C  CG  . ASN A 1 47  ? -19.784 18.834  -4.249  1.00 32.41  ? 42  ASN A CG  1 
ATOM   357  O  OD1 . ASN A 1 47  ? -20.415 18.697  -3.203  1.00 36.01  ? 42  ASN A OD1 1 
ATOM   358  N  ND2 . ASN A 1 47  ? -19.979 18.026  -5.296  1.00 30.27  ? 42  ASN A ND2 1 
ATOM   359  N  N   . LEU A 1 48  ? -16.145 18.105  -4.768  1.00 12.02  ? 43  LEU A N   1 
ATOM   360  C  CA  . LEU A 1 48  ? -15.568 16.803  -5.061  1.00 11.65  ? 43  LEU A CA  1 
ATOM   361  C  C   . LEU A 1 48  ? -14.679 16.330  -3.909  1.00 12.86  ? 43  LEU A C   1 
ATOM   362  O  O   . LEU A 1 48  ? -14.708 15.147  -3.538  1.00 12.70  ? 43  LEU A O   1 
ATOM   363  C  CB  . LEU A 1 48  ? -14.771 16.830  -6.365  1.00 12.15  ? 43  LEU A CB  1 
ATOM   364  C  CG  . LEU A 1 48  ? -15.587 17.052  -7.641  1.00 12.75  ? 43  LEU A CG  1 
ATOM   365  C  CD1 . LEU A 1 48  ? -14.682 17.303  -8.814  1.00 13.97  ? 43  LEU A CD1 1 
ATOM   366  C  CD2 . LEU A 1 48  ? -16.477 15.870  -7.945  1.00 15.40  ? 43  LEU A CD2 1 
ATOM   367  N  N   . LEU A 1 49  ? -13.891 17.260  -3.359  1.00 12.66  ? 44  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 49  ? -13.001 16.957  -2.243  1.00 13.00  ? 44  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 49  ? -13.824 16.481  -1.047  1.00 14.78  ? 44  LEU A C   1 
ATOM   370  O  O   . LEU A 1 49  ? -13.499 15.469  -0.429  1.00 12.75  ? 44  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 49  ? -12.179 18.194  -1.861  1.00 13.86  ? 44  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 49  ? -11.179 18.038  -0.683  1.00 12.77  ? 44  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 49  ? -10.032 17.156  -1.048  1.00 13.98  ? 44  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 49  ? -10.665 19.386  -0.217  1.00 14.11  ? 44  LEU A CD2 1 
ATOM   375  N  N   . SER A 1 50  ? -14.876 17.248  -0.729  1.00 12.66  ? 45  SER A N   1 
ATOM   376  C  CA  . SER A 1 50  ? -15.770 16.950  0.377   1.00 11.37  ? 45  SER A CA  1 
ATOM   377  C  C   . SER A 1 50  ? -16.461 15.593  0.262   1.00 12.25  ? 45  SER A C   1 
ATOM   378  O  O   . SER A 1 50  ? -16.414 14.791  1.197   1.00 12.87  ? 45  SER A O   1 
ATOM   379  C  CB  . SER A 1 50  ? -16.822 18.049  0.477   1.00 13.97  ? 45  SER A CB  1 
ATOM   380  O  OG  . SER A 1 50  ? -17.726 17.817  1.542   1.00 15.78  ? 45  SER A OG  1 
ATOM   381  N  N   . VAL A 1 51  ? -17.083 15.331  -0.891  1.00 12.81  ? 46  VAL A N   1 
ATOM   382  C  CA  . VAL A 1 51  ? -17.777 14.072  -1.120  1.00 13.00  ? 46  VAL A CA  1 
ATOM   383  C  C   . VAL A 1 51  ? -16.833 12.878  -0.958  1.00 12.02  ? 46  VAL A C   1 
ATOM   384  O  O   . VAL A 1 51  ? -17.185 11.877  -0.337  1.00 13.71  ? 46  VAL A O   1 
ATOM   385  C  CB  . VAL A 1 51  ? -18.452 14.074  -2.513  1.00 14.31  ? 46  VAL A CB  1 
ATOM   386  C  CG1 . VAL A 1 51  ? -18.950 12.671  -2.905  1.00 15.19  ? 46  VAL A CG1 1 
ATOM   387  C  CG2 . VAL A 1 51  ? -19.603 15.090  -2.562  1.00 15.09  ? 46  VAL A CG2 1 
ATOM   388  N  N   . ALA A 1 52  ? -15.634 12.990  -1.532  1.00 11.82  ? 47  ALA A N   1 
ATOM   389  C  CA  . ALA A 1 52  ? -14.704 11.873  -1.539  1.00 12.75  ? 47  ALA A CA  1 
ATOM   390  C  C   . ALA A 1 52  ? -14.325 11.497  -0.109  1.00 13.37  ? 47  ALA A C   1 
ATOM   391  O  O   . ALA A 1 52  ? -14.480 10.344  0.301   1.00 13.08  ? 47  ALA A O   1 
ATOM   392  C  CB  . ALA A 1 52  ? -13.470 12.196  -2.361  1.00 12.61  ? 47  ALA A CB  1 
ATOM   393  N  N   . TYR A 1 53  ? -13.859 12.473  0.671   1.00 10.89  ? 48  TYR A N   1 
ATOM   394  C  CA  . TYR A 1 53  ? -13.389 12.155  2.009   1.00 11.83  ? 48  TYR A CA  1 
ATOM   395  C  C   . TYR A 1 53  ? -14.536 11.845  2.971   1.00 11.52  ? 48  TYR A C   1 
ATOM   396  O  O   . TYR A 1 53  ? -14.373 11.010  3.867   1.00 12.79  ? 48  TYR A O   1 
ATOM   397  C  CB  . TYR A 1 53  ? -12.463 13.282  2.538   1.00 11.77  ? 48  TYR A CB  1 
ATOM   398  C  CG  . TYR A 1 53  ? -11.048 13.125  2.026   1.00 11.98  ? 48  TYR A CG  1 
ATOM   399  C  CD1 . TYR A 1 53  ? -10.208 12.154  2.544   1.00 12.20  ? 48  TYR A CD1 1 
ATOM   400  C  CD2 . TYR A 1 53  ? -10.546 13.958  1.035   1.00 13.03  ? 48  TYR A CD2 1 
ATOM   401  C  CE1 . TYR A 1 53  ? -8.906  11.997  2.081   1.00 13.46  ? 48  TYR A CE1 1 
ATOM   402  C  CE2 . TYR A 1 53  ? -9.238  13.822  0.569   1.00 15.93  ? 48  TYR A CE2 1 
ATOM   403  C  CZ  . TYR A 1 53  ? -8.421  12.831  1.091   1.00 14.98  ? 48  TYR A CZ  1 
ATOM   404  O  OH  . TYR A 1 53  ? -7.120  12.669  0.646   1.00 15.75  ? 48  TYR A OH  1 
ATOM   405  N  N   . LYS A 1 54  ? -15.708 12.471  2.770   1.00 11.64  ? 49  LYS A N   1 
ATOM   406  C  CA  . LYS A 1 54  ? -16.847 12.167  3.625   1.00 13.21  ? 49  LYS A CA  1 
ATOM   407  C  C   . LYS A 1 54  ? -17.243 10.701  3.487   1.00 11.28  ? 49  LYS A C   1 
ATOM   408  O  O   . LYS A 1 54  ? -17.587 10.055  4.479   1.00 12.83  ? 49  LYS A O   1 
ATOM   409  C  CB  . LYS A 1 54  ? -18.086 13.015  3.313   1.00 15.80  ? 49  LYS A CB  1 
ATOM   410  C  CG  . LYS A 1 54  ? -19.248 12.798  4.276   1.00 32.17  ? 49  LYS A CG  1 
ATOM   411  C  CD  . LYS A 1 54  ? -19.149 13.681  5.528   1.00 46.49  ? 49  LYS A CD  1 
ATOM   412  C  CE  . LYS A 1 54  ? -20.115 13.300  6.642   1.00 43.14  ? 49  LYS A CE  1 
ATOM   413  N  NZ  . LYS A 1 54  ? -21.462 12.915  6.142   1.00 44.29  ? 49  LYS A NZ  1 
ATOM   414  N  N   . ASN A 1 55  ? -17.251 10.188  2.248   1.00 12.79  ? 50  ASN A N   1 
ATOM   415  C  CA  . ASN A 1 55  ? -17.557 8.789   2.003   1.00 11.81  ? 50  ASN A CA  1 
ATOM   416  C  C   . ASN A 1 55  ? -16.528 7.841   2.619   1.00 13.29  ? 50  ASN A C   1 
ATOM   417  O  O   . ASN A 1 55  ? -16.888 6.828   3.214   1.00 14.62  ? 50  ASN A O   1 
ATOM   418  C  CB  . ASN A 1 55  ? -17.664 8.537   0.500   1.00 14.47  ? 50  ASN A CB  1 
ATOM   419  C  CG  . ASN A 1 55  ? -19.024 8.811   -0.056  1.00 21.57  ? 50  ASN A CG  1 
ATOM   420  O  OD1 . ASN A 1 55  ? -19.273 9.804   -0.753  1.00 23.88  ? 50  ASN A OD1 1 
ATOM   421  N  ND2 . ASN A 1 55  ? -19.945 7.921   0.221   1.00 23.74  ? 50  ASN A ND2 1 
ATOM   422  N  N   . VAL A 1 56  ? -15.237 8.164   2.469   1.00 12.09  ? 51  VAL A N   1 
ATOM   423  C  CA  . VAL A 1 56  ? -14.189 7.325   3.029   1.00 13.95  ? 51  VAL A CA  1 
ATOM   424  C  C   . VAL A 1 56  ? -14.306 7.295   4.553   1.00 14.18  ? 51  VAL A C   1 
ATOM   425  O  O   . VAL A 1 56  ? -14.383 6.229   5.152   1.00 13.03  ? 51  VAL A O   1 
ATOM   426  C  CB  . VAL A 1 56  ? -12.786 7.760   2.557   1.00 11.65  ? 51  VAL A CB  1 
ATOM   427  C  CG1 . VAL A 1 56  ? -11.672 7.029   3.307   1.00 13.76  ? 51  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A 1 56  ? -12.621 7.547   1.054   1.00 13.98  ? 51  VAL A CG2 1 
ATOM   429  N  N   . VAL A 1 57  ? -14.340 8.470   5.193   1.00 12.39  ? 52  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 57  ? -14.373 8.477   6.647   1.00 15.16  ? 52  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 57  ? -15.710 7.951   7.160   1.00 14.12  ? 52  VAL A C   1 
ATOM   432  O  O   . VAL A 1 57  ? -15.774 7.392   8.253   1.00 14.93  ? 52  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 57  ? -13.993 9.866   7.225   1.00 12.10  ? 52  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 57  ? -15.155 10.843  7.160   1.00 13.93  ? 52  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 57  ? -13.452 9.740   8.648   1.00 15.69  ? 52  VAL A CG2 1 
ATOM   436  N  N   . GLY A 1 58  ? -16.779 8.106   6.367   1.00 12.99  ? 53  GLY A N   1 
ATOM   437  C  CA  . GLY A 1 58  ? -18.087 7.589   6.741   1.00 16.00  ? 53  GLY A CA  1 
ATOM   438  C  C   . GLY A 1 58  ? -18.090 6.072   6.915   1.00 17.64  ? 53  GLY A C   1 
ATOM   439  O  O   . GLY A 1 58  ? -18.677 5.556   7.868   1.00 17.89  ? 53  GLY A O   1 
ATOM   440  N  N   . GLY A 1 59  ? -17.422 5.367   5.991   1.00 16.48  ? 54  GLY A N   1 
ATOM   441  C  CA  . GLY A 1 59  ? -17.252 3.927   6.099   1.00 17.54  ? 54  GLY A CA  1 
ATOM   442  C  C   . GLY A 1 59  ? -16.456 3.522   7.338   1.00 15.09  ? 54  GLY A C   1 
ATOM   443  O  O   . GLY A 1 59  ? -16.800 2.551   8.020   1.00 16.08  ? 54  GLY A O   1 
ATOM   444  N  N   . GLN A 1 60  ? -15.389 4.274   7.622   1.00 14.00  ? 55  GLN A N   1 
ATOM   445  C  CA  . GLN A 1 60  ? -14.536 3.976   8.761   1.00 13.53  ? 55  GLN A CA  1 
ATOM   446  C  C   . GLN A 1 60  ? -15.297 4.197   10.071  1.00 15.91  ? 55  GLN A C   1 
ATOM   447  O  O   . GLN A 1 60  ? -15.160 3.403   11.007  1.00 13.21  ? 55  GLN A O   1 
ATOM   448  C  CB  . GLN A 1 60  ? -13.279 4.843   8.730   1.00 14.43  ? 55  GLN A CB  1 
ATOM   449  C  CG  . GLN A 1 60  ? -12.399 4.607   7.511   1.00 15.75  ? 55  GLN A CG  1 
ATOM   450  C  CD  . GLN A 1 60  ? -11.279 5.597   7.428   1.00 17.58  ? 55  GLN A CD  1 
ATOM   451  O  OE1 . GLN A 1 60  ? -11.469 6.803   7.620   1.00 17.18  ? 55  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A 1 60  ? -10.082 5.122   7.124   1.00 21.20  ? 55  GLN A NE2 1 
ATOM   453  N  N   . ARG A 1 61  ? -16.078 5.284   10.142  1.00 13.05  ? 56  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 61  ? -16.851 5.604   11.337  1.00 12.99  ? 56  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 61  ? -17.890 4.517   11.603  1.00 12.92  ? 56  ARG A C   1 
ATOM   456  O  O   . ARG A 1 61  ? -18.079 4.109   12.737  1.00 13.53  ? 56  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 61  ? -17.549 6.978   11.230  1.00 13.22  ? 56  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 61  ? -16.600 8.157   11.264  1.00 15.10  ? 56  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 61  ? -17.236 9.437   10.764  1.00 14.67  ? 56  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 61  ? -18.247 9.939   11.691  1.00 13.95  ? 56  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 61  ? -19.260 10.724  11.334  1.00 14.43  ? 56  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 61  ? -19.553 10.942  10.064  1.00 15.35  ? 56  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 61  ? -20.006 11.289  12.279  1.00 13.80  ? 56  ARG A NH2 1 
ATOM   464  N  N   . ALA A 1 62  ? -18.581 4.070   10.554  1.00 12.60  ? 57  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 62  ? -19.581 3.032   10.722  1.00 14.63  ? 57  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 62  ? -18.914 1.749   11.217  1.00 14.58  ? 57  ALA A C   1 
ATOM   467  O  O   . ALA A 1 62  ? -19.451 1.084   12.099  1.00 16.68  ? 57  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 62  ? -20.350 2.795   9.430   1.00 15.87  ? 57  ALA A CB  1 
ATOM   469  N  N   . ALA A 1 63  ? -17.749 1.408   10.655  1.00 13.59  ? 58  ALA A N   1 
ATOM   470  C  CA  . ALA A 1 63  ? -17.039 0.200   11.060  1.00 14.40  ? 58  ALA A CA  1 
ATOM   471  C  C   . ALA A 1 63  ? -16.569 0.310   12.509  1.00 14.08  ? 58  ALA A C   1 
ATOM   472  O  O   . ALA A 1 63  ? -16.718 -0.632  13.289  1.00 14.02  ? 58  ALA A O   1 
ATOM   473  C  CB  . ALA A 1 63  ? -15.857 -0.078  10.122  1.00 14.75  ? 58  ALA A CB  1 
ATOM   474  N  N   . TRP A 1 64  ? -15.999 1.467   12.869  1.00 14.21  ? 59  TRP A N   1 
ATOM   475  C  CA  . TRP A 1 64  ? -15.506 1.695   14.221  1.00 14.50  ? 59  TRP A CA  1 
ATOM   476  C  C   . TRP A 1 64  ? -16.620 1.520   15.253  1.00 15.98  ? 59  TRP A C   1 
ATOM   477  O  O   . TRP A 1 64  ? -16.396 0.954   16.325  1.00 14.92  ? 59  TRP A O   1 
ATOM   478  C  CB  . TRP A 1 64  ? -14.837 3.093   14.331  1.00 13.90  ? 59  TRP A CB  1 
ATOM   479  C  CG  . TRP A 1 64  ? -14.219 3.368   15.670  1.00 12.52  ? 59  TRP A CG  1 
ATOM   480  C  CD1 . TRP A 1 64  ? -12.921 3.173   16.022  1.00 14.14  ? 59  TRP A CD1 1 
ATOM   481  C  CD2 . TRP A 1 64  ? -14.874 3.889   16.832  1.00 12.94  ? 59  TRP A CD2 1 
ATOM   482  N  NE1 . TRP A 1 64  ? -12.720 3.547   17.327  1.00 14.77  ? 59  TRP A NE1 1 
ATOM   483  C  CE2 . TRP A 1 64  ? -13.910 3.970   17.856  1.00 14.37  ? 59  TRP A CE2 1 
ATOM   484  C  CE3 . TRP A 1 64  ? -16.184 4.286   17.110  1.00 15.03  ? 59  TRP A CE3 1 
ATOM   485  C  CZ2 . TRP A 1 64  ? -14.218 4.440   19.137  1.00 16.32  ? 59  TRP A CZ2 1 
ATOM   486  C  CZ3 . TRP A 1 64  ? -16.490 4.752   18.377  1.00 16.61  ? 59  TRP A CZ3 1 
ATOM   487  C  CH2 . TRP A 1 64  ? -15.508 4.844   19.366  1.00 14.40  ? 59  TRP A CH2 1 
ATOM   488  N  N   . ARG A 1 65  ? -17.825 2.004   14.922  1.00 14.48  ? 60  ARG A N   1 
ATOM   489  C  CA  . ARG A 1 65  ? -18.965 1.913   15.824  1.00 14.86  ? 60  ARG A CA  1 
ATOM   490  C  C   . ARG A 1 65  ? -19.395 0.467   16.068  1.00 16.10  ? 60  ARG A C   1 
ATOM   491  O  O   . ARG A 1 65  ? -19.691 0.098   17.205  1.00 16.38  ? 60  ARG A O   1 
ATOM   492  C  CB  . ARG A 1 65  ? -20.148 2.719   15.289  1.00 16.31  ? 60  ARG A CB  1 
ATOM   493  C  CG  . ARG A 1 65  ? -19.921 4.228   15.354  1.00 16.87  ? 60  ARG A CG  1 
ATOM   494  C  CD  . ARG A 1 65  ? -20.974 4.980   14.557  1.00 20.85  ? 60  ARG A CD  1 
ATOM   495  N  NE  . ARG A 1 65  ? -20.688 6.409   14.585  1.00 24.89  ? 60  ARG A NE  1 
ATOM   496  C  CZ  . ARG A 1 65  ? -21.272 7.310   13.808  1.00 30.55  ? 60  ARG A CZ  1 
ATOM   497  N  NH1 . ARG A 1 65  ? -22.144 6.959   12.878  1.00 32.94  ? 60  ARG A NH1 1 
ATOM   498  N  NH2 . ARG A 1 65  ? -20.974 8.596   13.973  1.00 29.33  ? 60  ARG A NH2 1 
ATOM   499  N  N   . VAL A 1 66  ? -19.421 -0.342  15.000  1.00 14.40  ? 61  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 66  ? -19.734 -1.758  15.126  1.00 15.77  ? 61  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 66  ? -18.756 -2.437  16.079  1.00 15.78  ? 61  VAL A C   1 
ATOM   502  O  O   . VAL A 1 66  ? -19.173 -3.133  17.008  1.00 17.04  ? 61  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 66  ? -19.733 -2.454  13.748  1.00 15.81  ? 61  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 66  ? -19.715 -3.991  13.881  1.00 15.03  ? 61  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 66  ? -20.904 -1.989  12.891  1.00 19.35  ? 61  VAL A CG2 1 
ATOM   506  N  N   . LEU A 1 67  ? -17.457 -2.241  15.826  1.00 15.60  ? 62  LEU A N   1 
ATOM   507  C  CA  . LEU A 1 67  ? -16.395 -2.860  16.607  1.00 16.46  ? 62  LEU A CA  1 
ATOM   508  C  C   . LEU A 1 67  ? -16.359 -2.366  18.053  1.00 18.64  ? 62  LEU A C   1 
ATOM   509  O  O   . LEU A 1 67  ? -16.134 -3.157  18.974  1.00 17.74  ? 62  LEU A O   1 
ATOM   510  C  CB  . LEU A 1 67  ? -15.026 -2.635  15.917  1.00 16.98  ? 62  LEU A CB  1 
ATOM   511  C  CG  . LEU A 1 67  ? -14.895 -3.213  14.502  1.00 15.44  ? 62  LEU A CG  1 
ATOM   512  C  CD1 . LEU A 1 67  ? -13.581 -2.796  13.881  1.00 17.49  ? 62  LEU A CD1 1 
ATOM   513  C  CD2 . LEU A 1 67  ? -15.032 -4.741  14.495  1.00 16.76  ? 62  LEU A CD2 1 
ATOM   514  N  N   . SER A 1 68  ? -16.604 -1.067  18.264  1.00 15.98  ? 63  SER A N   1 
ATOM   515  C  CA  A SER A 1 68  ? -16.622 -0.508  19.607  0.50 16.36  ? 63  SER A CA  1 
ATOM   516  C  CA  B SER A 1 68  ? -16.627 -0.508  19.605  0.50 18.06  ? 63  SER A CA  1 
ATOM   517  C  C   . SER A 1 68  ? -17.753 -1.117  20.433  1.00 17.25  ? 63  SER A C   1 
ATOM   518  O  O   . SER A 1 68  ? -17.574 -1.409  21.615  1.00 18.06  ? 63  SER A O   1 
ATOM   519  C  CB  A SER A 1 68  ? -16.754 1.014   19.557  0.50 16.64  ? 63  SER A CB  1 
ATOM   520  C  CB  B SER A 1 68  ? -16.771 1.006   19.541  0.50 20.34  ? 63  SER A CB  1 
ATOM   521  O  OG  A SER A 1 68  ? -16.661 1.578   20.860  0.50 14.06  ? 63  SER A OG  1 
ATOM   522  O  OG  B SER A 1 68  ? -15.547 1.577   19.123  0.50 22.25  ? 63  SER A OG  1 
ATOM   523  N  N   . SER A 1 69  ? -18.910 -1.302  19.794  1.00 17.15  ? 64  SER A N   1 
ATOM   524  C  CA  . SER A 1 69  ? -20.061 -1.912  20.440  1.00 20.01  ? 64  SER A CA  1 
ATOM   525  C  C   . SER A 1 69  ? -19.777 -3.356  20.853  1.00 22.53  ? 64  SER A C   1 
ATOM   526  O  O   . SER A 1 69  ? -20.123 -3.760  21.961  1.00 23.34  ? 64  SER A O   1 
ATOM   527  C  CB  . SER A 1 69  ? -21.273 -1.860  19.525  1.00 21.16  ? 64  SER A CB  1 
ATOM   528  O  OG  . SER A 1 69  ? -22.320 -2.632  20.082  1.00 29.18  ? 64  SER A OG  1 
ATOM   529  N  N   . ILE A 1 70  ? -19.136 -4.120  19.961  1.00 16.27  ? 65  ILE A N   1 
ATOM   530  C  CA  . ILE A 1 70  ? -18.732 -5.486  20.282  1.00 19.72  ? 65  ILE A CA  1 
ATOM   531  C  C   . ILE A 1 70  ? -17.731 -5.511  21.436  1.00 24.30  ? 65  ILE A C   1 
ATOM   532  O  O   . ILE A 1 70  ? -17.811 -6.365  22.323  1.00 25.39  ? 65  ILE A O   1 
ATOM   533  C  CB  . ILE A 1 70  ? -18.169 -6.188  19.032  1.00 17.32  ? 65  ILE A CB  1 
ATOM   534  C  CG1 . ILE A 1 70  ? -19.254 -6.356  17.964  1.00 18.07  ? 65  ILE A CG1 1 
ATOM   535  C  CG2 . ILE A 1 70  ? -17.500 -7.533  19.416  1.00 20.71  ? 65  ILE A CG2 1 
ATOM   536  C  CD1 . ILE A 1 70  ? -18.769 -6.735  16.640  1.00 19.50  ? 65  ILE A CD1 1 
ATOM   537  N  N   . GLU A 1 71  ? -16.793 -4.558  21.424  1.00 18.86  ? 66  GLU A N   1 
ATOM   538  C  CA  . GLU A 1 71  ? -15.764 -4.476  22.448  1.00 18.57  ? 66  GLU A CA  1 
ATOM   539  C  C   . GLU A 1 71  ? -16.377 -4.161  23.814  1.00 26.44  ? 66  GLU A C   1 
ATOM   540  O  O   . GLU A 1 71  ? -16.036 -4.795  24.811  1.00 26.24  ? 66  GLU A O   1 
ATOM   541  C  CB  . GLU A 1 71  ? -14.734 -3.424  22.051  1.00 20.52  ? 66  GLU A CB  1 
ATOM   542  C  CG  . GLU A 1 71  ? -13.509 -3.368  22.935  1.00 20.21  ? 66  GLU A CG  1 
ATOM   543  C  CD  . GLU A 1 71  ? -12.541 -2.273  22.556  1.00 20.73  ? 66  GLU A CD  1 
ATOM   544  O  OE1 . GLU A 1 71  ? -12.895 -1.437  21.693  1.00 25.10  ? 66  GLU A OE1 1 
ATOM   545  O  OE2 . GLU A 1 71  ? -11.442 -2.224  23.151  1.00 22.92  ? 66  GLU A OE2 1 
ATOM   546  N  N   . GLN A 1 72  ? -17.299 -3.194  23.845  1.00 23.52  ? 67  GLN A N   1 
ATOM   547  C  CA  . GLN A 1 72  ? -17.985 -2.828  25.077  1.00 27.64  ? 67  GLN A CA  1 
ATOM   548  C  C   . GLN A 1 72  ? -18.749 -4.008  25.675  1.00 33.66  ? 67  GLN A C   1 
ATOM   549  O  O   . GLN A 1 72  ? -18.739 -4.201  26.890  1.00 38.63  ? 67  GLN A O   1 
ATOM   550  C  CB  . GLN A 1 72  ? -18.958 -1.671  24.832  1.00 33.00  ? 67  GLN A CB  1 
ATOM   551  C  CG  . GLN A 1 72  ? -18.276 -0.332  24.568  1.00 46.17  ? 67  GLN A CG  1 
ATOM   552  C  CD  . GLN A 1 72  ? -19.289 0.736   24.227  1.00 69.08  ? 67  GLN A CD  1 
ATOM   553  O  OE1 . GLN A 1 72  ? -20.083 1.162   25.075  1.00 92.07  ? 67  GLN A OE1 1 
ATOM   554  N  NE2 . GLN A 1 72  ? -19.293 1.198   22.981  1.00 69.42  ? 67  GLN A NE2 1 
ATOM   555  N  N   . LYS A 1 73  ? -19.408 -4.792  24.816  1.00 27.29  ? 68  LYS A N   1 
ATOM   556  C  CA  . LYS A 1 73  ? -20.146 -5.965  25.260  1.00 36.46  ? 68  LYS A CA  1 
ATOM   557  C  C   . LYS A 1 73  ? -19.245 -7.062  25.824  1.00 42.47  ? 68  LYS A C   1 
ATOM   558  O  O   . LYS A 1 73  ? -19.651 -7.778  26.737  1.00 44.20  ? 68  LYS A O   1 
ATOM   559  C  CB  . LYS A 1 73  ? -21.002 -6.522  24.122  1.00 36.48  ? 68  LYS A CB  1 
ATOM   560  C  CG  . LYS A 1 73  ? -22.200 -5.638  23.809  1.00 45.59  ? 68  LYS A CG  1 
ATOM   561  C  CD  . LYS A 1 73  ? -23.120 -6.238  22.758  1.00 56.77  ? 68  LYS A CD  1 
ATOM   562  C  CE  . LYS A 1 73  ? -24.128 -5.238  22.241  1.00 65.58  ? 68  LYS A CE  1 
ATOM   563  N  NZ  . LYS A 1 73  ? -24.993 -4.706  23.329  1.00 78.40  ? 68  LYS A NZ  1 
ATOM   564  N  N   . SER A 1 74  ? -18.022 -7.180  25.291  1.00 32.56  ? 69  SER A N   1 
ATOM   565  C  CA  . SER A 1 74  ? -17.067 -8.166  25.777  1.00 45.67  ? 69  SER A CA  1 
ATOM   566  C  C   . SER A 1 74  ? -16.541 -7.839  27.174  1.00 48.00  ? 69  SER A C   1 
ATOM   567  O  O   . SER A 1 74  ? -16.138 -8.740  27.908  1.00 54.84  ? 69  SER A O   1 
ATOM   568  C  CB  . SER A 1 74  ? -15.894 -8.304  24.814  1.00 46.38  ? 69  SER A CB  1 
ATOM   569  O  OG  . SER A 1 74  ? -15.033 -7.179  24.883  1.00 51.72  ? 69  SER A OG  1 
ATOM   570  N  N   . ASN A 1 75  ? -16.550 -6.547  27.532  1.00 47.48  ? 70  ASN A N   1 
ATOM   571  C  CA  . ASN A 1 75  ? -16.044 -6.085  28.816  1.00 55.16  ? 70  ASN A CA  1 
ATOM   572  C  C   . ASN A 1 75  ? -17.141 -5.846  29.856  1.00 50.28  ? 70  ASN A C   1 
ATOM   573  O  O   . ASN A 1 75  ? -17.014 -4.959  30.697  1.00 68.81  ? 70  ASN A O   1 
ATOM   574  C  CB  . ASN A 1 75  ? -15.219 -4.804  28.599  1.00 49.97  ? 70  ASN A CB  1 
ATOM   575  C  CG  . ASN A 1 75  ? -14.004 -5.028  27.732  1.00 50.34  ? 70  ASN A CG  1 
ATOM   576  O  OD1 . ASN A 1 75  ? -13.509 -6.153  27.588  1.00 66.82  ? 70  ASN A OD1 1 
ATOM   577  N  ND2 . ASN A 1 75  ? -13.482 -3.962  27.135  1.00 43.65  ? 70  ASN A ND2 1 
ATOM   578  N  N   . GLU A 1 76  ? -18.218 -6.639  29.785  1.00 55.25  ? 71  GLU A N   1 
ATOM   579  C  CA  . GLU A 1 76  ? -19.232 -6.683  30.827  1.00 57.72  ? 71  GLU A CA  1 
ATOM   580  C  C   . GLU A 1 76  ? -18.967 -7.860  31.763  1.00 62.78  ? 71  GLU A C   1 
ATOM   581  O  O   . GLU A 1 76  ? -18.105 -8.693  31.488  1.00 68.90  ? 71  GLU A O   1 
ATOM   582  C  CB  . GLU A 1 76  ? -20.629 -6.840  30.216  1.00 62.09  ? 71  GLU A CB  1 
ATOM   583  C  CG  . GLU A 1 76  ? -21.095 -5.657  29.392  1.00 62.95  ? 71  GLU A CG  1 
ATOM   584  C  CD  . GLU A 1 76  ? -22.390 -5.901  28.642  1.00 67.23  ? 71  GLU A CD  1 
ATOM   585  O  OE1 . GLU A 1 76  ? -22.886 -7.052  28.659  1.00 73.56  ? 71  GLU A OE1 1 
ATOM   586  O  OE2 . GLU A 1 76  ? -22.914 -4.937  28.039  1.00 90.22  ? 71  GLU A OE2 1 
ATOM   587  N  N   . GLU A 1 77  ? -19.729 -7.921  32.863  1.00 77.43  ? 72  GLU A N   1 
ATOM   588  C  CA  . GLU A 1 77  ? -19.713 -9.069  33.757  1.00 80.38  ? 72  GLU A CA  1 
ATOM   589  C  C   . GLU A 1 77  ? -20.537 -10.194 33.133  1.00 72.47  ? 72  GLU A C   1 
ATOM   590  O  O   . GLU A 1 77  ? -21.621 -9.952  32.608  1.00 67.11  ? 72  GLU A O   1 
ATOM   591  C  CB  . GLU A 1 77  ? -20.271 -8.690  35.139  1.00 87.44  ? 72  GLU A CB  1 
ATOM   592  C  CG  . GLU A 1 77  ? -19.980 -9.717  36.222  1.00 87.68  ? 72  GLU A CG  1 
ATOM   593  C  CD  . GLU A 1 77  ? -20.619 -9.433  37.569  1.00 93.33  ? 72  GLU A CD  1 
ATOM   594  O  OE1 . GLU A 1 77  ? -21.312 -8.398  37.697  1.00 95.48  ? 72  GLU A OE1 1 
ATOM   595  O  OE2 . GLU A 1 77  ? -20.429 -10.250 38.498  1.00 89.19  ? 72  GLU A OE2 1 
ATOM   596  N  N   . GLY A 1 78  ? -20.005 -11.422 33.188  1.00 72.90  ? 73  GLY A N   1 
ATOM   597  C  CA  . GLY A 1 78  ? -20.650 -12.577 32.581  1.00 67.72  ? 73  GLY A CA  1 
ATOM   598  C  C   . GLY A 1 78  ? -20.117 -12.913 31.190  1.00 66.16  ? 73  GLY A C   1 
ATOM   599  O  O   . GLY A 1 78  ? -20.208 -14.059 30.753  1.00 60.44  ? 73  GLY A O   1 
ATOM   600  N  N   . SER A 1 79  ? -19.573 -11.901 30.500  1.00 67.60  ? 74  SER A N   1 
ATOM   601  C  CA  . SER A 1 79  ? -18.979 -12.080 29.184  1.00 62.57  ? 74  SER A CA  1 
ATOM   602  C  C   . SER A 1 79  ? -17.721 -12.943 29.260  1.00 55.70  ? 74  SER A C   1 
ATOM   603  O  O   . SER A 1 79  ? -16.872 -12.731 30.122  1.00 66.02  ? 74  SER A O   1 
ATOM   604  C  CB  . SER A 1 79  ? -18.640 -10.731 28.557  1.00 64.24  ? 74  SER A CB  1 
ATOM   605  O  OG  . SER A 1 79  ? -19.788 -9.903  28.454  1.00 68.23  ? 74  SER A OG  1 
ATOM   606  N  N   . GLU A 1 80  ? -17.619 -13.912 28.343  1.00 51.46  ? 75  GLU A N   1 
ATOM   607  C  CA  . GLU A 1 80  ? -16.481 -14.815 28.283  1.00 52.68  ? 75  GLU A CA  1 
ATOM   608  C  C   . GLU A 1 80  ? -15.281 -14.091 27.673  1.00 56.78  ? 75  GLU A C   1 
ATOM   609  O  O   . GLU A 1 80  ? -15.445 -13.246 26.795  1.00 57.32  ? 75  GLU A O   1 
ATOM   610  C  CB  . GLU A 1 80  ? -16.863 -16.073 27.467  1.00 51.00  ? 75  GLU A CB  1 
ATOM   611  C  CG  . GLU A 1 80  ? -15.934 -17.261 27.648  1.00 51.51  ? 75  GLU A CG  1 
ATOM   612  C  CD  . GLU A 1 80  ? -15.819 -17.743 29.079  1.00 45.72  ? 75  GLU A CD  1 
ATOM   613  O  OE1 . GLU A 1 80  ? -16.872 -17.965 29.721  1.00 48.04  ? 75  GLU A OE1 1 
ATOM   614  O  OE2 . GLU A 1 80  ? -14.674 -17.889 29.564  1.00 55.93  ? 75  GLU A OE2 1 
ATOM   615  N  N   . GLU A 1 81  ? -14.078 -14.422 28.162  1.00 51.65  ? 76  GLU A N   1 
ATOM   616  C  CA  . GLU A 1 81  ? -12.842 -13.817 27.690  1.00 49.93  ? 76  GLU A CA  1 
ATOM   617  C  C   . GLU A 1 81  ? -12.474 -14.359 26.312  1.00 44.40  ? 76  GLU A C   1 
ATOM   618  O  O   . GLU A 1 81  ? -12.338 -15.570 26.143  1.00 43.90  ? 76  GLU A O   1 
ATOM   619  C  CB  . GLU A 1 81  ? -11.711 -14.098 28.696  1.00 56.76  ? 76  GLU A CB  1 
ATOM   620  C  CG  . GLU A 1 81  ? -10.347 -13.560 28.298  1.00 55.29  ? 76  GLU A CG  1 
ATOM   621  C  CD  . GLU A 1 81  ? -10.304 -12.064 28.064  1.00 59.16  ? 76  GLU A CD  1 
ATOM   622  O  OE1 . GLU A 1 81  ? -10.783 -11.313 28.943  1.00 56.10  ? 76  GLU A OE1 1 
ATOM   623  O  OE2 . GLU A 1 81  ? -9.777  -11.641 27.010  1.00 56.02  ? 76  GLU A OE2 1 
ATOM   624  N  N   . LYS A 1 82  ? -12.309 -13.459 25.332  1.00 38.56  ? 77  LYS A N   1 
ATOM   625  C  CA  . LYS A 1 82  ? -12.003 -13.867 23.968  1.00 47.15  ? 77  LYS A CA  1 
ATOM   626  C  C   . LYS A 1 82  ? -10.626 -13.414 23.483  1.00 43.81  ? 77  LYS A C   1 
ATOM   627  O  O   . LYS A 1 82  ? -10.310 -13.558 22.303  1.00 39.71  ? 77  LYS A O   1 
ATOM   628  C  CB  . LYS A 1 82  ? -13.087 -13.343 23.003  1.00 52.99  ? 77  LYS A CB  1 
ATOM   629  C  CG  . LYS A 1 82  ? -14.492 -13.891 23.264  1.00 64.38  ? 77  LYS A CG  1 
ATOM   630  C  CD  . LYS A 1 82  ? -14.530 -15.414 23.498  1.00 65.42  ? 77  LYS A CD  1 
ATOM   631  C  CE  . LYS A 1 82  ? -15.889 -16.027 23.241  1.00 64.13  ? 77  LYS A CE  1 
ATOM   632  N  NZ  . LYS A 1 82  ? -16.993 -15.235 23.847  1.00 65.08  ? 77  LYS A NZ  1 
ATOM   633  N  N   . GLY A 1 83  ? -9.805  -12.883 24.397  1.00 30.80  ? 78  GLY A N   1 
ATOM   634  C  CA  . GLY A 1 83  ? -8.458  -12.464 24.052  1.00 24.24  ? 78  GLY A CA  1 
ATOM   635  C  C   . GLY A 1 83  ? -8.410  -11.051 23.475  1.00 20.21  ? 78  GLY A C   1 
ATOM   636  O  O   . GLY A 1 83  ? -9.412  -10.338 23.498  1.00 23.65  ? 78  GLY A O   1 
ATOM   637  N  N   . PRO A 1 84  ? -7.243  -10.630 22.939  1.00 20.07  ? 79  PRO A N   1 
ATOM   638  C  CA  . PRO A 1 84  ? -7.017  -9.246  22.520  1.00 18.57  ? 79  PRO A CA  1 
ATOM   639  C  C   . PRO A 1 84  ? -7.565  -8.840  21.151  1.00 16.75  ? 79  PRO A C   1 
ATOM   640  O  O   . PRO A 1 84  ? -7.411  -7.684  20.755  1.00 15.79  ? 79  PRO A O   1 
ATOM   641  C  CB  . PRO A 1 84  ? -5.490  -9.178  22.511  1.00 17.96  ? 79  PRO A CB  1 
ATOM   642  C  CG  . PRO A 1 84  ? -5.070  -10.572 22.050  1.00 19.01  ? 79  PRO A CG  1 
ATOM   643  C  CD  . PRO A 1 84  ? -6.051  -11.476 22.758  1.00 20.79  ? 79  PRO A CD  1 
ATOM   644  N  N   . GLU A 1 85  ? -8.196  -9.778  20.435  1.00 15.49  ? 80  GLU A N   1 
ATOM   645  C  CA  . GLU A 1 85  ? -8.476  -9.589  19.017  1.00 16.01  ? 80  GLU A CA  1 
ATOM   646  C  C   . GLU A 1 85  ? -9.463  -8.457  18.717  1.00 13.90  ? 80  GLU A C   1 
ATOM   647  O  O   . GLU A 1 85  ? -9.249  -7.705  17.768  1.00 13.54  ? 80  GLU A O   1 
ATOM   648  C  CB  . GLU A 1 85  ? -8.975  -10.901 18.367  1.00 13.71  ? 80  GLU A CB  1 
ATOM   649  C  CG  . GLU A 1 85  ? -7.895  -11.979 18.229  1.00 15.76  ? 80  GLU A CG  1 
ATOM   650  C  CD  . GLU A 1 85  ? -7.687  -12.876 19.432  1.00 19.89  ? 80  GLU A CD  1 
ATOM   651  O  OE1 . GLU A 1 85  ? -8.353  -12.658 20.471  1.00 18.41  ? 80  GLU A OE1 1 
ATOM   652  O  OE2 . GLU A 1 85  ? -6.865  -13.816 19.329  1.00 21.36  ? 80  GLU A OE2 1 
ATOM   653  N  N   . VAL A 1 86  ? -10.539 -8.337  19.506  1.00 13.99  ? 81  VAL A N   1 
ATOM   654  C  CA  . VAL A 1 86  ? -11.535 -7.295  19.285  1.00 15.39  ? 81  VAL A CA  1 
ATOM   655  C  C   . VAL A 1 86  ? -10.904 -5.914  19.448  1.00 16.57  ? 81  VAL A C   1 
ATOM   656  O  O   . VAL A 1 86  ? -11.074 -5.046  18.591  1.00 14.82  ? 81  VAL A O   1 
ATOM   657  C  CB  . VAL A 1 86  ? -12.771 -7.462  20.211  1.00 18.03  ? 81  VAL A CB  1 
ATOM   658  C  CG1 . VAL A 1 86  ? -13.677 -6.235  20.137  1.00 24.71  ? 81  VAL A CG1 1 
ATOM   659  C  CG2 . VAL A 1 86  ? -13.565 -8.724  19.877  1.00 21.16  ? 81  VAL A CG2 1 
ATOM   660  N  N   . ARG A 1 87  ? -10.189 -5.712  20.561  1.00 14.91  ? 82  ARG A N   1 
ATOM   661  C  CA  . ARG A 1 87  ? -9.459  -4.476  20.801  1.00 15.45  ? 82  ARG A CA  1 
ATOM   662  C  C   . ARG A 1 87  ? -8.441  -4.182  19.700  1.00 15.24  ? 82  ARG A C   1 
ATOM   663  O  O   . ARG A 1 87  ? -8.337  -3.052  19.228  1.00 14.13  ? 82  ARG A O   1 
ATOM   664  C  CB  . ARG A 1 87  ? -8.736  -4.511  22.174  1.00 17.46  ? 82  ARG A CB  1 
ATOM   665  C  CG  . ARG A 1 87  ? -7.772  -3.327  22.400  1.00 20.57  ? 82  ARG A CG  1 
ATOM   666  C  CD  . ARG A 1 87  ? -7.001  -3.384  23.721  1.00 22.21  ? 82  ARG A CD  1 
ATOM   667  N  NE  . ARG A 1 87  ? -6.169  -4.578  23.846  1.00 29.89  ? 82  ARG A NE  1 
ATOM   668  C  CZ  . ARG A 1 87  ? -5.070  -4.838  23.142  1.00 28.74  ? 82  ARG A CZ  1 
ATOM   669  N  NH1 . ARG A 1 87  ? -4.570  -3.968  22.282  1.00 30.05  ? 82  ARG A NH1 1 
ATOM   670  N  NH2 . ARG A 1 87  ? -4.440  -5.995  23.330  1.00 24.26  ? 82  ARG A NH2 1 
ATOM   671  N  N   . GLU A 1 88  ? -7.653  -5.192  19.316  1.00 12.28  ? 83  GLU A N   1 
ATOM   672  C  CA  . GLU A 1 88  ? -6.645  -5.007  18.285  1.00 14.17  ? 83  GLU A CA  1 
ATOM   673  C  C   . GLU A 1 88  ? -7.270  -4.510  16.984  1.00 13.16  ? 83  GLU A C   1 
ATOM   674  O  O   . GLU A 1 88  ? -6.740  -3.601  16.349  1.00 14.05  ? 83  GLU A O   1 
ATOM   675  C  CB  . GLU A 1 88  ? -5.880  -6.309  18.007  1.00 14.35  ? 83  GLU A CB  1 
ATOM   676  C  CG  . GLU A 1 88  ? -4.866  -6.683  19.073  1.00 14.41  ? 83  GLU A CG  1 
ATOM   677  C  CD  . GLU A 1 88  ? -4.307  -8.090  18.958  1.00 18.59  ? 83  GLU A CD  1 
ATOM   678  O  OE1 . GLU A 1 88  ? -4.784  -8.868  18.097  1.00 17.19  ? 83  GLU A OE1 1 
ATOM   679  O  OE2 . GLU A 1 88  ? -3.371  -8.410  19.726  1.00 17.82  ? 83  GLU A OE2 1 
ATOM   680  N  N   . TYR A 1 89  ? -8.374  -5.140  16.569  1.00 11.60  ? 84  TYR A N   1 
ATOM   681  C  CA  . TYR A 1 89  ? -8.974  -4.807  15.286  1.00 11.67  ? 84  TYR A CA  1 
ATOM   682  C  C   . TYR A 1 89  ? -9.685  -3.451  15.354  1.00 14.58  ? 84  TYR A C   1 
ATOM   683  O  O   . TYR A 1 89  ? -9.615  -2.666  14.410  1.00 14.59  ? 84  TYR A O   1 
ATOM   684  C  CB  . TYR A 1 89  ? -9.893  -5.923  14.787  1.00 13.30  ? 84  TYR A CB  1 
ATOM   685  C  CG  . TYR A 1 89  ? -10.425 -5.683  13.386  1.00 12.71  ? 84  TYR A CG  1 
ATOM   686  C  CD1 . TYR A 1 89  ? -9.580  -5.313  12.353  1.00 12.37  ? 84  TYR A CD1 1 
ATOM   687  C  CD2 . TYR A 1 89  ? -11.775 -5.795  13.109  1.00 13.77  ? 84  TYR A CD2 1 
ATOM   688  C  CE1 . TYR A 1 89  ? -10.072 -5.053  11.073  1.00 12.41  ? 84  TYR A CE1 1 
ATOM   689  C  CE2 . TYR A 1 89  ? -12.276 -5.542  11.839  1.00 15.33  ? 84  TYR A CE2 1 
ATOM   690  C  CZ  . TYR A 1 89  ? -11.419 -5.170  10.826  1.00 13.48  ? 84  TYR A CZ  1 
ATOM   691  O  OH  . TYR A 1 89  ? -11.927 -4.894  9.589   1.00 14.78  ? 84  TYR A OH  1 
ATOM   692  N  N   . ARG A 1 90  ? -10.355 -3.160  16.475  1.00 13.09  ? 85  ARG A N   1 
ATOM   693  C  CA  . ARG A 1 90  ? -10.887 -1.817  16.682  1.00 13.47  ? 85  ARG A CA  1 
ATOM   694  C  C   . ARG A 1 90  ? -9.792  -0.745  16.618  1.00 15.09  ? 85  ARG A C   1 
ATOM   695  O  O   . ARG A 1 90  ? -9.971  0.308   16.000  1.00 14.73  ? 85  ARG A O   1 
ATOM   696  C  CB  . ARG A 1 90  ? -11.651 -1.737  18.011  1.00 16.38  ? 85  ARG A CB  1 
ATOM   697  C  CG  . ARG A 1 90  ? -12.433 -0.437  18.239  1.00 16.33  ? 85  ARG A CG  1 
ATOM   698  C  CD  . ARG A 1 90  ? -11.630 0.637   18.947  1.00 14.47  ? 85  ARG A CD  1 
ATOM   699  N  NE  . ARG A 1 90  ? -11.249 0.221   20.294  1.00 14.84  ? 85  ARG A NE  1 
ATOM   700  C  CZ  . ARG A 1 90  ? -10.194 0.669   20.965  1.00 18.25  ? 85  ARG A CZ  1 
ATOM   701  N  NH1 . ARG A 1 90  ? -9.453  1.669   20.512  1.00 20.65  ? 85  ARG A NH1 1 
ATOM   702  N  NH2 . ARG A 1 90  ? -9.862  0.083   22.114  1.00 22.22  ? 85  ARG A NH2 1 
ATOM   703  N  N   . GLU A 1 91  ? -8.642  -1.007  17.248  1.00 15.04  ? 86  GLU A N   1 
ATOM   704  C  CA  . GLU A 1 91  ? -7.504  -0.100  17.186  1.00 15.24  ? 86  GLU A CA  1 
ATOM   705  C  C   . GLU A 1 91  ? -6.983  0.093   15.762  1.00 13.62  ? 86  GLU A C   1 
ATOM   706  O  O   . GLU A 1 91  ? -6.600  1.197   15.384  1.00 16.37  ? 86  GLU A O   1 
ATOM   707  C  CB  . GLU A 1 91  ? -6.356  -0.595  18.089  1.00 16.83  ? 86  GLU A CB  1 
ATOM   708  C  CG  . GLU A 1 91  ? -6.619  -0.402  19.579  1.00 19.51  ? 86  GLU A CG  1 
ATOM   709  C  CD  . GLU A 1 91  ? -5.554  -0.940  20.525  1.00 31.13  ? 86  GLU A CD  1 
ATOM   710  O  OE1 . GLU A 1 91  ? -4.627  -1.643  20.063  1.00 33.73  ? 86  GLU A OE1 1 
ATOM   711  O  OE2 . GLU A 1 91  ? -5.645  -0.644  21.737  1.00 35.55  ? 86  GLU A OE2 1 
ATOM   712  N  N   . LYS A 1 92  ? -6.972  -0.982  14.969  1.00 14.70  ? 87  LYS A N   1 
ATOM   713  C  CA  . LYS A 1 92  ? -6.549  -0.911  13.576  1.00 16.46  ? 87  LYS A CA  1 
ATOM   714  C  C   . LYS A 1 92  ? -7.436  0.040   12.772  1.00 14.20  ? 87  LYS A C   1 
ATOM   715  O  O   . LYS A 1 92  ? -6.945  0.924   12.075  1.00 14.33  ? 87  LYS A O   1 
ATOM   716  C  CB  . LYS A 1 92  ? -6.572  -2.310  12.943  1.00 17.63  ? 87  LYS A CB  1 
ATOM   717  C  CG  . LYS A 1 92  ? -6.129  -2.352  11.473  1.00 23.21  ? 87  LYS A CG  1 
ATOM   718  C  CD  . LYS A 1 92  ? -6.451  -3.695  10.803  1.00 27.00  ? 87  LYS A CD  1 
ATOM   719  C  CE  . LYS A 1 92  ? -6.273  -3.677  9.303   1.00 35.90  ? 87  LYS A CE  1 
ATOM   720  N  NZ  . LYS A 1 92  ? -4.851  -3.480  8.920   1.00 41.81  ? 87  LYS A NZ  1 
ATOM   721  N  N   . VAL A 1 93  ? -8.748  -0.167  12.858  1.00 13.88  ? 88  VAL A N   1 
ATOM   722  C  CA  . VAL A 1 93  ? -9.686  0.682   12.141  1.00 13.79  ? 88  VAL A CA  1 
ATOM   723  C  C   . VAL A 1 93  ? -9.578  2.120   12.651  1.00 13.51  ? 88  VAL A C   1 
ATOM   724  O  O   . VAL A 1 93  ? -9.568  3.053   11.860  1.00 14.05  ? 88  VAL A O   1 
ATOM   725  C  CB  . VAL A 1 93  ? -11.111 0.131   12.235  1.00 12.76  ? 88  VAL A CB  1 
ATOM   726  C  CG1 . VAL A 1 93  ? -12.121 1.106   11.635  1.00 15.11  ? 88  VAL A CG1 1 
ATOM   727  C  CG2 . VAL A 1 93  ? -11.215 -1.242  11.574  1.00 15.51  ? 88  VAL A CG2 1 
ATOM   728  N  N   . GLU A 1 94  ? -9.498  2.294   13.976  1.00 13.18  ? 89  GLU A N   1 
ATOM   729  C  CA  . GLU A 1 94  ? -9.342  3.610   14.586  1.00 14.57  ? 89  GLU A CA  1 
ATOM   730  C  C   . GLU A 1 94  ? -8.113  4.366   14.077  1.00 15.15  ? 89  GLU A C   1 
ATOM   731  O  O   . GLU A 1 94  ? -8.174  5.558   13.775  1.00 14.87  ? 89  GLU A O   1 
ATOM   732  C  CB  . GLU A 1 94  ? -9.273  3.432   16.103  1.00 14.23  ? 89  GLU A CB  1 
ATOM   733  C  CG  . GLU A 1 94  ? -9.200  4.712   16.908  1.00 14.85  ? 89  GLU A CG  1 
ATOM   734  C  CD  . GLU A 1 94  ? -9.307  4.450   18.394  1.00 14.78  ? 89  GLU A CD  1 
ATOM   735  O  OE1 . GLU A 1 94  ? -10.323 3.846   18.818  1.00 14.77  ? 89  GLU A OE1 1 
ATOM   736  O  OE2 . GLU A 1 94  ? -8.376  4.859   19.125  1.00 22.07  ? 89  GLU A OE2 1 
ATOM   737  N  N   . THR A 1 95  ? -6.972  3.673   13.991  1.00 13.64  ? 90  THR A N   1 
ATOM   738  C  CA  . THR A 1 95  ? -5.750  4.278   13.490  1.00 13.41  ? 90  THR A CA  1 
ATOM   739  C  C   . THR A 1 95  ? -5.905  4.738   12.038  1.00 11.83  ? 90  THR A C   1 
ATOM   740  O  O   . THR A 1 95  ? -5.410  5.804   11.675  1.00 14.56  ? 90  THR A O   1 
ATOM   741  C  CB  . THR A 1 95  ? -4.567  3.294   13.705  1.00 18.17  ? 90  THR A CB  1 
ATOM   742  O  OG1 . THR A 1 95  ? -4.437  3.008   15.106  1.00 19.26  ? 90  THR A OG1 1 
ATOM   743  C  CG2 . THR A 1 95  ? -3.277  3.841   13.192  1.00 21.50  ? 90  THR A CG2 1 
ATOM   744  N  N   . GLU A 1 96  ? -6.577  3.934   11.204  1.00 13.61  ? 91  GLU A N   1 
ATOM   745  C  CA  . GLU A 1 96  ? -6.783  4.291   9.806   1.00 14.65  ? 91  GLU A CA  1 
ATOM   746  C  C   . GLU A 1 96  ? -7.700  5.506   9.686   1.00 13.56  ? 91  GLU A C   1 
ATOM   747  O  O   . GLU A 1 96  ? -7.452  6.403   8.873   1.00 14.52  ? 91  GLU A O   1 
ATOM   748  C  CB  . GLU A 1 96  ? -7.357  3.129   8.988   1.00 17.58  ? 91  GLU A CB  1 
ATOM   749  C  CG  . GLU A 1 96  ? -6.385  1.972   8.897   1.00 25.62  ? 91  GLU A CG  1 
ATOM   750  C  CD  . GLU A 1 96  ? -6.760  0.819   7.984   1.00 37.80  ? 91  GLU A CD  1 
ATOM   751  O  OE1 . GLU A 1 96  ? -7.750  0.924   7.219   1.00 25.52  ? 91  GLU A OE1 1 
ATOM   752  O  OE2 . GLU A 1 96  ? -6.035  -0.202  8.042   1.00 34.77  ? 91  GLU A OE2 1 
ATOM   753  N  N   . LEU A 1 97  ? -8.754  5.522   10.508  1.00 12.94  ? 92  LEU A N   1 
ATOM   754  C  CA  . LEU A 1 97  ? -9.658  6.663   10.593  1.00 14.29  ? 92  LEU A CA  1 
ATOM   755  C  C   . LEU A 1 97  ? -8.908  7.938   10.975  1.00 16.24  ? 92  LEU A C   1 
ATOM   756  O  O   . LEU A 1 97  ? -9.083  8.974   10.332  1.00 14.69  ? 92  LEU A O   1 
ATOM   757  C  CB  . LEU A 1 97  ? -10.782 6.318   11.604  1.00 14.60  ? 92  LEU A CB  1 
ATOM   758  C  CG  . LEU A 1 97  ? -11.955 7.307   11.786  1.00 14.98  ? 92  LEU A CG  1 
ATOM   759  C  CD1 . LEU A 1 97  ? -13.137 6.621   12.420  1.00 16.64  ? 92  LEU A CD1 1 
ATOM   760  C  CD2 . LEU A 1 97  ? -11.556 8.482   12.629  1.00 17.32  ? 92  LEU A CD2 1 
ATOM   761  N  N   . GLN A 1 98  ? -8.074  7.861   12.017  1.00 13.64  ? 93  GLN A N   1 
ATOM   762  C  CA  . GLN A 1 98  ? -7.299  9.012   12.449  1.00 12.61  ? 93  GLN A CA  1 
ATOM   763  C  C   . GLN A 1 98  ? -6.357  9.474   11.340  1.00 14.87  ? 93  GLN A C   1 
ATOM   764  O  O   . GLN A 1 98  ? -6.142  10.670  11.163  1.00 14.07  ? 93  GLN A O   1 
ATOM   765  C  CB  . GLN A 1 98  ? -6.541  8.704   13.740  1.00 14.37  ? 93  GLN A CB  1 
ATOM   766  C  CG  . GLN A 1 98  ? -7.453  8.525   14.922  1.00 14.57  ? 93  GLN A CG  1 
ATOM   767  C  CD  . GLN A 1 98  ? -6.727  7.938   16.117  1.00 18.04  ? 93  GLN A CD  1 
ATOM   768  O  OE1 . GLN A 1 98  ? -5.831  7.084   15.974  1.00 16.92  ? 93  GLN A OE1 1 
ATOM   769  N  NE2 . GLN A 1 98  ? -7.089  8.386   17.313  1.00 17.43  ? 93  GLN A NE2 1 
ATOM   770  N  N   . GLY A 1 99  ? -5.816  8.522   10.571  1.00 15.95  ? 94  GLY A N   1 
ATOM   771  C  CA  . GLY A 1 99  ? -4.956  8.855   9.447   1.00 13.06  ? 94  GLY A CA  1 
ATOM   772  C  C   . GLY A 1 99  ? -5.650  9.656   8.347   1.00 11.76  ? 94  GLY A C   1 
ATOM   773  O  O   . GLY A 1 99  ? -5.063  10.586  7.800   1.00 14.81  ? 94  GLY A O   1 
ATOM   774  N  N   . VAL A 1 100 ? -6.897  9.287   8.026   1.00 13.42  ? 95  VAL A N   1 
ATOM   775  C  CA  . VAL A 1 100 ? -7.697  10.014  7.051   1.00 12.99  ? 95  VAL A CA  1 
ATOM   776  C  C   . VAL A 1 100 ? -7.984  11.427  7.565   1.00 12.99  ? 95  VAL A C   1 
ATOM   777  O  O   . VAL A 1 100 ? -7.815  12.399  6.840   1.00 13.08  ? 95  VAL A O   1 
ATOM   778  C  CB  . VAL A 1 100 ? -8.982  9.256   6.701   1.00 14.38  ? 95  VAL A CB  1 
ATOM   779  C  CG1 . VAL A 1 100 ? -9.982  10.152  5.932   1.00 15.55  ? 95  VAL A CG1 1 
ATOM   780  C  CG2 . VAL A 1 100 ? -8.659  7.993   5.911   1.00 17.67  ? 95  VAL A CG2 1 
ATOM   781  N  N   . CYS A 1 101 ? -8.385  11.550  8.833   1.00 12.53  ? 96  CYS A N   1 
ATOM   782  C  CA  . CYS A 1 101 ? -8.633  12.858  9.426   1.00 12.85  ? 96  CYS A CA  1 
ATOM   783  C  C   . CYS A 1 101 ? -7.386  13.744  9.370   1.00 12.60  ? 96  CYS A C   1 
ATOM   784  O  O   . CYS A 1 101 ? -7.475  14.911  8.998   1.00 14.39  ? 96  CYS A O   1 
ATOM   785  C  CB  . CYS A 1 101 ? -9.158  12.738  10.859  1.00 12.82  ? 96  CYS A CB  1 
ATOM   786  S  SG  . CYS A 1 101 ? -10.811 11.999  11.013  1.00 15.33  ? 96  CYS A SG  1 
ATOM   787  N  N   . ASP A 1 102 ? -6.228  13.184  9.750   1.00 13.23  ? 97  ASP A N   1 
ATOM   788  C  CA  . ASP A 1 102 ? -4.966  13.909  9.705   1.00 13.82  ? 97  ASP A CA  1 
ATOM   789  C  C   . ASP A 1 102 ? -4.596  14.349  8.291   1.00 13.98  ? 97  ASP A C   1 
ATOM   790  O  O   . ASP A 1 102 ? -4.091  15.454  8.108   1.00 14.14  ? 97  ASP A O   1 
ATOM   791  C  CB  . ASP A 1 102 ? -3.836  13.064  10.321  1.00 17.36  ? 97  ASP A CB  1 
ATOM   792  C  CG  . ASP A 1 102 ? -3.923  12.908  11.835  1.00 25.19  ? 97  ASP A CG  1 
ATOM   793  O  OD1 . ASP A 1 102 ? -4.710  13.633  12.459  1.00 24.04  ? 97  ASP A OD1 1 
ATOM   794  O  OD2 . ASP A 1 102 ? -3.198  12.055  12.385  1.00 28.11  ? 97  ASP A OD2 1 
ATOM   795  N  N   . THR A 1 103 ? -4.870  13.495  7.298   1.00 15.23  ? 98  THR A N   1 
ATOM   796  C  CA  . THR A 1 103 ? -4.634  13.864  5.909   1.00 12.86  ? 98  THR A CA  1 
ATOM   797  C  C   . THR A 1 103 ? -5.468  15.076  5.498   1.00 12.98  ? 98  THR A C   1 
ATOM   798  O  O   . THR A 1 103 ? -4.958  16.017  4.902   1.00 14.43  ? 98  THR A O   1 
ATOM   799  C  CB  . THR A 1 103 ? -4.932  12.681  4.986   1.00 16.74  ? 98  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 103 ? -3.977  11.646  5.236   1.00 16.81  ? 98  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 103 ? -4.905  13.068  3.513   1.00 17.39  ? 98  THR A CG2 1 
ATOM   802  N  N   . VAL A 1 104 ? -6.763  15.056  5.826   1.00 12.29  ? 99  VAL A N   1 
ATOM   803  C  CA  . VAL A 1 104 ? -7.633  16.166  5.461   1.00 12.60  ? 99  VAL A CA  1 
ATOM   804  C  C   . VAL A 1 104 ? -7.185  17.449  6.163   1.00 13.03  ? 99  VAL A C   1 
ATOM   805  O  O   . VAL A 1 104 ? -7.094  18.511  5.549   1.00 12.29  ? 99  VAL A O   1 
ATOM   806  C  CB  . VAL A 1 104 ? -9.107  15.845  5.768   1.00 11.91  ? 99  VAL A CB  1 
ATOM   807  C  CG1 . VAL A 1 104 ? -9.969  17.099  5.652   1.00 13.95  ? 99  VAL A CG1 1 
ATOM   808  C  CG2 . VAL A 1 104 ? -9.648  14.724  4.871   1.00 13.80  ? 99  VAL A CG2 1 
ATOM   809  N  N   . LEU A 1 105 ? -6.929  17.356  7.476   1.00 11.74  ? 100 LEU A N   1 
ATOM   810  C  CA  . LEU A 1 105 ? -6.539  18.528  8.245   1.00 12.22  ? 100 LEU A CA  1 
ATOM   811  C  C   . LEU A 1 105 ? -5.222  19.084  7.723   1.00 12.57  ? 100 LEU A C   1 
ATOM   812  O  O   . LEU A 1 105 ? -5.010  20.299  7.724   1.00 15.22  ? 100 LEU A O   1 
ATOM   813  C  CB  . LEU A 1 105 ? -6.443  18.184  9.733   1.00 11.81  ? 100 LEU A CB  1 
ATOM   814  C  CG  . LEU A 1 105 ? -7.783  17.841  10.374  1.00 12.61  ? 100 LEU A CG  1 
ATOM   815  C  CD1 . LEU A 1 105 ? -7.606  17.260  11.735  1.00 12.91  ? 100 LEU A CD1 1 
ATOM   816  C  CD2 . LEU A 1 105 ? -8.697  19.075  10.475  1.00 12.60  ? 100 LEU A CD2 1 
ATOM   817  N  N   . GLY A 1 106 ? -4.359  18.174  7.244   1.00 11.97  ? 101 GLY A N   1 
ATOM   818  C  CA  . GLY A 1 106 ? -3.095  18.561  6.639   1.00 14.31  ? 101 GLY A CA  1 
ATOM   819  C  C   . GLY A 1 106 ? -3.271  19.371  5.356   1.00 15.00  ? 101 GLY A C   1 
ATOM   820  O  O   . GLY A 1 106 ? -2.576  20.362  5.149   1.00 17.26  ? 101 GLY A O   1 
ATOM   821  N  N   . LEU A 1 107 ? -4.211  18.950  4.499   1.00 11.67  ? 102 LEU A N   1 
ATOM   822  C  CA  . LEU A 1 107 ? -4.522  19.698  3.288   1.00 11.98  ? 102 LEU A CA  1 
ATOM   823  C  C   . LEU A 1 107 ? -5.092  21.081  3.606   1.00 13.17  ? 102 LEU A C   1 
ATOM   824  O  O   . LEU A 1 107 ? -4.760  22.064  2.941   1.00 12.72  ? 102 LEU A O   1 
ATOM   825  C  CB  . LEU A 1 107 ? -5.523  18.922  2.414   1.00 14.17  ? 102 LEU A CB  1 
ATOM   826  C  CG  . LEU A 1 107 ? -5.021  17.593  1.822   1.00 14.81  ? 102 LEU A CG  1 
ATOM   827  C  CD1 . LEU A 1 107 ? -6.124  16.896  1.080   1.00 19.02  ? 102 LEU A CD1 1 
ATOM   828  C  CD2 . LEU A 1 107 ? -3.831  17.801  0.893   1.00 17.70  ? 102 LEU A CD2 1 
ATOM   829  N  N   . LEU A 1 108 ? -5.950  21.155  4.635   1.00 13.75  ? 103 LEU A N   1 
ATOM   830  C  CA  . LEU A 1 108 ? -6.537  22.429  5.032   1.00 13.87  ? 103 LEU A CA  1 
ATOM   831  C  C   . LEU A 1 108 ? -5.470  23.390  5.550   1.00 12.32  ? 103 LEU A C   1 
ATOM   832  O  O   . LEU A 1 108 ? -5.504  24.588  5.258   1.00 14.66  ? 103 LEU A O   1 
ATOM   833  C  CB  . LEU A 1 108 ? -7.646  22.191  6.086   1.00 13.37  ? 103 LEU A CB  1 
ATOM   834  C  CG  . LEU A 1 108 ? -8.869  21.464  5.552   1.00 13.56  ? 103 LEU A CG  1 
ATOM   835  C  CD1 . LEU A 1 108 ? -9.805  21.054  6.676   1.00 15.26  ? 103 LEU A CD1 1 
ATOM   836  C  CD2 . LEU A 1 108 ? -9.660  22.301  4.562   1.00 15.73  ? 103 LEU A CD2 1 
ATOM   837  N  N   . ASP A 1 109 ? -4.517  22.852  6.314   1.00 11.91  ? 104 ASP A N   1 
ATOM   838  C  CA  . ASP A 1 109 ? -3.456  23.654  6.900   1.00 15.10  ? 104 ASP A CA  1 
ATOM   839  C  C   . ASP A 1 109 ? -2.329  23.977  5.921   1.00 16.68  ? 104 ASP A C   1 
ATOM   840  O  O   . ASP A 1 109 ? -1.561  24.915  6.155   1.00 18.46  ? 104 ASP A O   1 
ATOM   841  C  CB  . ASP A 1 109 ? -2.855  22.935  8.112   1.00 19.08  ? 104 ASP A CB  1 
ATOM   842  C  CG  . ASP A 1 109 ? -2.136  23.880  9.060   1.00 28.34  ? 104 ASP A CG  1 
ATOM   843  O  OD1 . ASP A 1 109 ? -2.733  24.919  9.428   1.00 34.43  ? 104 ASP A OD1 1 
ATOM   844  O  OD2 . ASP A 1 109 ? -0.984  23.573  9.449   1.00 29.30  ? 104 ASP A OD2 1 
ATOM   845  N  N   . SER A 1 110 ? -2.214  23.183  4.848   1.00 17.19  ? 105 SER A N   1 
ATOM   846  C  CA  . SER A 1 110 ? -1.141  23.333  3.876   1.00 17.29  ? 105 SER A CA  1 
ATOM   847  C  C   . SER A 1 110 ? -1.642  23.155  2.442   1.00 18.50  ? 105 SER A C   1 
ATOM   848  O  O   . SER A 1 110 ? -1.409  22.101  1.846   1.00 20.67  ? 105 SER A O   1 
ATOM   849  C  CB  . SER A 1 110 ? -0.026  22.322  4.165   1.00 20.24  ? 105 SER A CB  1 
ATOM   850  O  OG  . SER A 1 110 ? 0.488   22.472  5.477   1.00 27.22  ? 105 SER A OG  1 
ATOM   851  N  N   . HIS A 1 111 ? -2.312  24.165  1.856   1.00 17.81  ? 106 HIS A N   1 
ATOM   852  C  CA  . HIS A 1 111 ? -2.446  25.519  2.376   1.00 17.70  ? 106 HIS A CA  1 
ATOM   853  C  C   . HIS A 1 111 ? -3.810  26.117  2.031   1.00 16.81  ? 106 HIS A C   1 
ATOM   854  O  O   . HIS A 1 111 ? -3.919  27.312  1.772   1.00 17.73  ? 106 HIS A O   1 
ATOM   855  C  CB  . HIS A 1 111 ? -1.310  26.404  1.797   1.00 17.18  ? 106 HIS A CB  1 
ATOM   856  C  CG  . HIS A 1 111 ? 0.054   26.005  2.271   1.00 18.48  ? 106 HIS A CG  1 
ATOM   857  N  ND1 . HIS A 1 111 ? 0.860   25.141  1.551   1.00 24.31  ? 106 HIS A ND1 1 
ATOM   858  C  CD2 . HIS A 1 111 ? 0.687   26.321  3.417   1.00 16.20  ? 106 HIS A CD2 1 
ATOM   859  C  CE1 . HIS A 1 111 ? 1.963   24.981  2.280   1.00 20.04  ? 106 HIS A CE1 1 
ATOM   860  N  NE2 . HIS A 1 111 ? 1.898   25.677  3.407   1.00 23.63  ? 106 HIS A NE2 1 
ATOM   861  N  N   . LEU A 1 112 ? -4.860  25.283  2.046   1.00 14.88  ? 107 LEU A N   1 
ATOM   862  C  CA  . LEU A 1 112 ? -6.166  25.701  1.556   1.00 12.71  ? 107 LEU A CA  1 
ATOM   863  C  C   . LEU A 1 112 ? -6.779  26.865  2.342   1.00 13.23  ? 107 LEU A C   1 
ATOM   864  O  O   . LEU A 1 112 ? -7.296  27.816  1.747   1.00 16.54  ? 107 LEU A O   1 
ATOM   865  C  CB  . LEU A 1 112 ? -7.129  24.516  1.579   1.00 14.39  ? 107 LEU A CB  1 
ATOM   866  C  CG  . LEU A 1 112 ? -6.864  23.418  0.542   1.00 16.04  ? 107 LEU A CG  1 
ATOM   867  C  CD1 . LEU A 1 112 ? -7.732  22.208  0.809   1.00 14.89  ? 107 LEU A CD1 1 
ATOM   868  C  CD2 . LEU A 1 112 ? -7.100  23.915  -0.872  1.00 18.73  ? 107 LEU A CD2 1 
ATOM   869  N  N   . ILE A 1 113 ? -6.728  26.799  3.677   1.00 13.60  ? 108 ILE A N   1 
ATOM   870  C  CA  . ILE A 1 113 ? -7.362  27.821  4.492   1.00 13.73  ? 108 ILE A CA  1 
ATOM   871  C  C   . ILE A 1 113 ? -6.677  29.179  4.325   1.00 14.59  ? 108 ILE A C   1 
ATOM   872  O  O   . ILE A 1 113 ? -7.348  30.190  4.132   1.00 15.59  ? 108 ILE A O   1 
ATOM   873  C  CB  . ILE A 1 113 ? -7.456  27.405  5.971   1.00 14.58  ? 108 ILE A CB  1 
ATOM   874  C  CG1 . ILE A 1 113 ? -8.489  26.272  6.112   1.00 13.94  ? 108 ILE A CG1 1 
ATOM   875  C  CG2 . ILE A 1 113 ? -7.827  28.598  6.868   1.00 16.63  ? 108 ILE A CG2 1 
ATOM   876  C  CD1 . ILE A 1 113 ? -8.591  25.664  7.491   1.00 16.14  ? 108 ILE A CD1 1 
ATOM   877  N  N   . LYS A 1 114 ? -5.342  29.202  4.379   1.00 16.50  ? 109 LYS A N   1 
ATOM   878  C  CA  . LYS A 1 114 ? -4.640  30.476  4.368   1.00 15.40  ? 109 LYS A CA  1 
ATOM   879  C  C   . LYS A 1 114 ? -4.792  31.237  3.053   1.00 17.61  ? 109 LYS A C   1 
ATOM   880  O  O   . LYS A 1 114 ? -4.639  32.461  3.042   1.00 19.39  ? 109 LYS A O   1 
ATOM   881  C  CB  . LYS A 1 114 ? -3.149  30.341  4.732   1.00 17.99  ? 109 LYS A CB  1 
ATOM   882  C  CG  . LYS A 1 114 ? -2.320  29.537  3.761   1.00 20.97  ? 109 LYS A CG  1 
ATOM   883  C  CD  . LYS A 1 114 ? -0.824  29.588  4.099   1.00 19.90  ? 109 LYS A CD  1 
ATOM   884  C  CE  . LYS A 1 114 ? -0.489  29.108  5.497   1.00 24.23  ? 109 LYS A CE  1 
ATOM   885  N  NZ  . LYS A 1 114 ? -0.935  27.708  5.740   1.00 28.15  ? 109 LYS A NZ  1 
ATOM   886  N  N   . GLU A 1 115 ? -5.091  30.531  1.953   1.00 12.73  ? 110 GLU A N   1 
ATOM   887  C  CA  . GLU A 1 115 ? -5.310  31.199  0.681   1.00 17.39  ? 110 GLU A CA  1 
ATOM   888  C  C   . GLU A 1 115 ? -6.778  31.523  0.404   1.00 16.73  ? 110 GLU A C   1 
ATOM   889  O  O   . GLU A 1 115 ? -7.080  32.182  -0.593  1.00 19.68  ? 110 GLU A O   1 
ATOM   890  C  CB  . GLU A 1 115 ? -4.710  30.373  -0.472  1.00 16.32  ? 110 GLU A CB  1 
ATOM   891  C  CG  . GLU A 1 115 ? -3.181  30.301  -0.448  1.00 20.96  ? 110 GLU A CG  1 
ATOM   892  C  CD  . GLU A 1 115 ? -2.465  31.632  -0.631  1.00 32.71  ? 110 GLU A CD  1 
ATOM   893  O  OE1 . GLU A 1 115 ? -3.127  32.655  -0.935  1.00 29.71  ? 110 GLU A OE1 1 
ATOM   894  O  OE2 . GLU A 1 115 ? -1.225  31.652  -0.453  1.00 39.36  ? 110 GLU A OE2 1 
ATOM   895  N  N   . ALA A 1 116 ? -7.685  31.077  1.289   1.00 14.69  ? 111 ALA A N   1 
ATOM   896  C  CA  . ALA A 1 116 ? -9.118  31.239  1.094   1.00 16.23  ? 111 ALA A CA  1 
ATOM   897  C  C   . ALA A 1 116 ? -9.596  32.580  1.652   1.00 19.87  ? 111 ALA A C   1 
ATOM   898  O  O   . ALA A 1 116 ? -9.688  32.754  2.866   1.00 19.75  ? 111 ALA A O   1 
ATOM   899  C  CB  . ALA A 1 116 ? -9.870  30.086  1.764   1.00 15.66  ? 111 ALA A CB  1 
ATOM   900  N  N   . GLY A 1 117 ? -9.905  33.520  0.752   1.00 20.43  ? 112 GLY A N   1 
ATOM   901  C  CA  . GLY A 1 117 ? -10.287 34.877  1.124   1.00 21.15  ? 112 GLY A CA  1 
ATOM   902  C  C   . GLY A 1 117 ? -11.765 35.221  0.943   1.00 22.81  ? 112 GLY A C   1 
ATOM   903  O  O   . GLY A 1 117 ? -12.276 36.135  1.591   1.00 25.48  ? 112 GLY A O   1 
ATOM   904  N  N   . ASP A 1 118 ? -12.452 34.503  0.050   1.00 17.97  ? 113 ASP A N   1 
ATOM   905  C  CA  . ASP A 1 118 ? -13.881 34.697  -0.117  1.00 16.21  ? 113 ASP A CA  1 
ATOM   906  C  C   . ASP A 1 118 ? -14.665 33.932  0.948   1.00 18.78  ? 113 ASP A C   1 
ATOM   907  O  O   . ASP A 1 118 ? -14.220 32.893  1.436   1.00 17.40  ? 113 ASP A O   1 
ATOM   908  C  CB  . ASP A 1 118 ? -14.323 34.266  -1.511  1.00 15.26  ? 113 ASP A CB  1 
ATOM   909  C  CG  . ASP A 1 118 ? -13.780 35.117  -2.635  1.00 17.86  ? 113 ASP A CG  1 
ATOM   910  O  OD1 . ASP A 1 118 ? -13.075 36.107  -2.341  1.00 20.97  ? 113 ASP A OD1 1 
ATOM   911  O  OD2 . ASP A 1 118 ? -14.050 34.780  -3.815  1.00 18.66  ? 113 ASP A OD2 1 
ATOM   912  N  N   . ALA A 1 119 ? -15.839 34.454  1.315   1.00 17.27  ? 114 ALA A N   1 
ATOM   913  C  CA  . ALA A 1 119 ? -16.644 33.835  2.358   1.00 19.47  ? 114 ALA A CA  1 
ATOM   914  C  C   . ALA A 1 119 ? -16.989 32.374  2.069   1.00 18.37  ? 114 ALA A C   1 
ATOM   915  O  O   . ALA A 1 119 ? -16.890 31.525  2.952   1.00 16.95  ? 114 ALA A O   1 
ATOM   916  C  CB  . ALA A 1 119 ? -17.916 34.642  2.575   1.00 22.66  ? 114 ALA A CB  1 
ATOM   917  N  N   . GLU A 1 120 ? -17.375 32.077  0.824   1.00 18.45  ? 115 GLU A N   1 
ATOM   918  C  CA  . GLU A 1 120 ? -17.809 30.737  0.462   1.00 18.55  ? 115 GLU A CA  1 
ATOM   919  C  C   . GLU A 1 120 ? -16.684 29.718  0.663   1.00 16.34  ? 115 GLU A C   1 
ATOM   920  O  O   . GLU A 1 120 ? -16.885 28.666  1.274   1.00 20.23  ? 115 GLU A O   1 
ATOM   921  C  CB  . GLU A 1 120 ? -18.349 30.736  -0.986  1.00 23.91  ? 115 GLU A CB  1 
ATOM   922  C  CG  . GLU A 1 120 ? -19.615 31.587  -1.157  1.00 33.80  ? 115 GLU A CG  1 
ATOM   923  C  CD  . GLU A 1 120 ? -19.505 33.105  -1.006  1.00 45.45  ? 115 GLU A CD  1 
ATOM   924  O  OE1 . GLU A 1 120 ? -18.421 33.686  -1.267  1.00 25.02  ? 115 GLU A OE1 1 
ATOM   925  O  OE2 . GLU A 1 120 ? -20.520 33.715  -0.594  1.00 46.98  ? 115 GLU A OE2 1 
ATOM   926  N  N   . SER A 1 121 ? -15.471 30.059  0.219   1.00 14.98  ? 116 SER A N   1 
ATOM   927  C  CA  . SER A 1 121 ? -14.349 29.152  0.366   1.00 14.18  ? 116 SER A CA  1 
ATOM   928  C  C   . SER A 1 121 ? -13.847 29.058  1.806   1.00 15.77  ? 116 SER A C   1 
ATOM   929  O  O   . SER A 1 121 ? -13.613 27.961  2.308   1.00 16.14  ? 116 SER A O   1 
ATOM   930  C  CB  . SER A 1 121 ? -13.212 29.534  -0.573  1.00 16.45  ? 116 SER A CB  1 
ATOM   931  O  OG  . SER A 1 121 ? -12.680 30.810  -0.273  1.00 19.83  ? 116 SER A OG  1 
ATOM   932  N  N   . ARG A 1 122 ? -13.700 30.208  2.480   1.00 14.06  ? 117 ARG A N   1 
ATOM   933  C  CA  . ARG A 1 122 ? -13.189 30.214  3.841   1.00 13.96  ? 117 ARG A CA  1 
ATOM   934  C  C   . ARG A 1 122 ? -14.135 29.514  4.821   1.00 14.07  ? 117 ARG A C   1 
ATOM   935  O  O   . ARG A 1 122 ? -13.693 28.689  5.629   1.00 15.11  ? 117 ARG A O   1 
ATOM   936  C  CB  . ARG A 1 122 ? -12.869 31.634  4.313   1.00 15.10  ? 117 ARG A CB  1 
ATOM   937  C  CG  . ARG A 1 122 ? -12.013 31.640  5.543   1.00 20.74  ? 117 ARG A CG  1 
ATOM   938  C  CD  . ARG A 1 122 ? -11.467 33.007  5.850   1.00 20.51  ? 117 ARG A CD  1 
ATOM   939  N  NE  . ARG A 1 122 ? -10.518 32.916  6.952   1.00 21.92  ? 117 ARG A NE  1 
ATOM   940  C  CZ  . ARG A 1 122 ? -9.296  32.407  6.853   1.00 28.23  ? 117 ARG A CZ  1 
ATOM   941  N  NH1 . ARG A 1 122 ? -8.743  32.156  5.676   1.00 28.05  ? 117 ARG A NH1 1 
ATOM   942  N  NH2 . ARG A 1 122 ? -8.602  32.170  7.962   1.00 31.65  ? 117 ARG A NH2 1 
ATOM   943  N  N   . VAL A 1 123 ? -15.446 29.789  4.726   1.00 12.48  ? 118 VAL A N   1 
ATOM   944  C  CA  . VAL A 1 123 ? -16.405 29.126  5.599   1.00 12.24  ? 118 VAL A CA  1 
ATOM   945  C  C   . VAL A 1 123 ? -16.452 27.620  5.330   1.00 13.36  ? 118 VAL A C   1 
ATOM   946  O  O   . VAL A 1 123 ? -16.499 26.831  6.271   1.00 12.93  ? 118 VAL A O   1 
ATOM   947  C  CB  . VAL A 1 123 ? -17.812 29.747  5.480   1.00 14.59  ? 118 VAL A CB  1 
ATOM   948  C  CG1 . VAL A 1 123 ? -18.831 28.934  6.272   1.00 15.77  ? 118 VAL A CG1 1 
ATOM   949  C  CG2 . VAL A 1 123 ? -17.803 31.203  5.931   1.00 16.85  ? 118 VAL A CG2 1 
ATOM   950  N  N   . PHE A 1 124 ? -16.432 27.215  4.050   1.00 13.27  ? 119 PHE A N   1 
ATOM   951  C  CA  . PHE A 1 124 ? -16.443 25.800  3.714   1.00 13.18  ? 119 PHE A CA  1 
ATOM   952  C  C   . PHE A 1 124 ? -15.250 25.082  4.353   1.00 11.16  ? 119 PHE A C   1 
ATOM   953  O  O   . PHE A 1 124 ? -15.399 24.027  4.969   1.00 12.32  ? 119 PHE A O   1 
ATOM   954  C  CB  . PHE A 1 124 ? -16.446 25.585  2.193   1.00 14.00  ? 119 PHE A CB  1 
ATOM   955  C  CG  . PHE A 1 124 ? -16.216 24.123  1.883   1.00 16.68  ? 119 PHE A CG  1 
ATOM   956  C  CD1 . PHE A 1 124 ? -17.218 23.193  2.075   1.00 20.42  ? 119 PHE A CD1 1 
ATOM   957  C  CD2 . PHE A 1 124 ? -14.962 23.669  1.540   1.00 20.16  ? 119 PHE A CD2 1 
ATOM   958  C  CE1 . PHE A 1 124 ? -16.980 21.837  1.838   1.00 24.07  ? 119 PHE A CE1 1 
ATOM   959  C  CE2 . PHE A 1 124 ? -14.730 22.318  1.303   1.00 24.05  ? 119 PHE A CE2 1 
ATOM   960  C  CZ  . PHE A 1 124 ? -15.738 21.417  1.455   1.00 24.83  ? 119 PHE A CZ  1 
ATOM   961  N  N   . TYR A 1 125 ? -14.052 25.639  4.182   1.00 11.07  ? 120 TYR A N   1 
ATOM   962  C  CA  . TYR A 1 125 ? -12.861 24.979  4.699   1.00 12.56  ? 120 TYR A CA  1 
ATOM   963  C  C   . TYR A 1 125 ? -12.817 24.943  6.227   1.00 11.14  ? 120 TYR A C   1 
ATOM   964  O  O   . TYR A 1 125 ? -12.366 23.956  6.813   1.00 12.30  ? 120 TYR A O   1 
ATOM   965  C  CB  . TYR A 1 125 ? -11.580 25.604  4.152   1.00 11.86  ? 120 TYR A CB  1 
ATOM   966  C  CG  . TYR A 1 125 ? -11.335 25.447  2.662   1.00 12.71  ? 120 TYR A CG  1 
ATOM   967  C  CD1 . TYR A 1 125 ? -11.482 24.214  2.036   1.00 11.15  ? 120 TYR A CD1 1 
ATOM   968  C  CD2 . TYR A 1 125 ? -10.928 26.518  1.890   1.00 11.67  ? 120 TYR A CD2 1 
ATOM   969  C  CE1 . TYR A 1 125 ? -11.252 24.060  0.676   1.00 12.70  ? 120 TYR A CE1 1 
ATOM   970  C  CE2 . TYR A 1 125 ? -10.678 26.372  0.520   1.00 12.30  ? 120 TYR A CE2 1 
ATOM   971  C  CZ  . TYR A 1 125 ? -10.860 25.143  -0.084  1.00 13.16  ? 120 TYR A CZ  1 
ATOM   972  O  OH  . TYR A 1 125 ? -10.625 24.977  -1.437  1.00 14.99  ? 120 TYR A OH  1 
ATOM   973  N  N   . LEU A 1 126 ? -13.267 26.013  6.902   1.00 12.55  ? 121 LEU A N   1 
ATOM   974  C  CA  . LEU A 1 126 ? -13.280 26.022  8.358   1.00 13.47  ? 121 LEU A CA  1 
ATOM   975  C  C   . LEU A 1 126 ? -14.327 25.055  8.914   1.00 11.94  ? 121 LEU A C   1 
ATOM   976  O  O   . LEU A 1 126 ? -14.074 24.382  9.920   1.00 13.04  ? 121 LEU A O   1 
ATOM   977  C  CB  . LEU A 1 126 ? -13.499 27.436  8.883   1.00 13.40  ? 121 LEU A CB  1 
ATOM   978  C  CG  . LEU A 1 126 ? -12.325 28.399  8.739   1.00 15.23  ? 121 LEU A CG  1 
ATOM   979  C  CD1 . LEU A 1 126 ? -12.779 29.813  9.011   1.00 17.59  ? 121 LEU A CD1 1 
ATOM   980  C  CD2 . LEU A 1 126 ? -11.193 28.018  9.682   1.00 15.37  ? 121 LEU A CD2 1 
ATOM   981  N  N   . LYS A 1 127 ? -15.470 24.928  8.224   1.00 11.18  ? 122 LYS A N   1 
ATOM   982  C  CA  . LYS A 1 127 ? -16.441 23.900  8.561   1.00 12.05  ? 122 LYS A CA  1 
ATOM   983  C  C   . LYS A 1 127 ? -15.817 22.510  8.443   1.00 10.95  ? 122 LYS A C   1 
ATOM   984  O  O   . LYS A 1 127 ? -15.992 21.674  9.329   1.00 10.82  ? 122 LYS A O   1 
ATOM   985  C  CB  . LYS A 1 127 ? -17.666 23.997  7.660   1.00 11.84  ? 122 LYS A CB  1 
ATOM   986  C  CG  . LYS A 1 127 ? -18.721 22.903  7.874   1.00 12.16  ? 122 LYS A CG  1 
ATOM   987  C  CD  . LYS A 1 127 ? -19.750 22.910  6.743   1.00 15.59  ? 122 LYS A CD  1 
ATOM   988  C  CE  . LYS A 1 127 ? -20.610 21.676  6.700   1.00 17.89  ? 122 LYS A CE  1 
ATOM   989  N  NZ  . LYS A 1 127 ? -19.809 20.469  6.287   1.00 17.69  ? 122 LYS A NZ  1 
ATOM   990  N  N   . MET A 1 128 ? -15.082 22.268  7.347   1.00 12.52  ? 123 MET A N   1 
ATOM   991  C  CA  . MET A 1 128 ? -14.424 20.983  7.151   1.00 12.45  ? 123 MET A CA  1 
ATOM   992  C  C   . MET A 1 128 ? -13.438 20.678  8.282   1.00 10.41  ? 123 MET A C   1 
ATOM   993  O  O   . MET A 1 128 ? -13.369 19.559  8.778   1.00 10.76  ? 123 MET A O   1 
ATOM   994  C  CB  . MET A 1 128 ? -13.699 20.970  5.799   1.00 14.46  ? 123 MET A CB  1 
ATOM   995  C  CG  . MET A 1 128 ? -13.220 19.638  5.403   1.00 16.22  ? 123 MET A CG  1 
ATOM   996  S  SD  . MET A 1 128 ? -12.556 19.682  3.715   1.00 22.58  ? 123 MET A SD  1 
ATOM   997  C  CE  . MET A 1 128 ? -12.977 18.054  3.172   1.00 22.25  ? 123 MET A CE  1 
ATOM   998  N  N   . LYS A 1 129 ? -12.644 21.690  8.660   1.00 10.69  ? 124 LYS A N   1 
ATOM   999  C  CA  . LYS A 1 129 ? -11.714 21.559  9.764   1.00 11.77  ? 124 LYS A CA  1 
ATOM   1000 C  C   . LYS A 1 129 ? -12.450 21.164  11.045  1.00 10.86  ? 124 LYS A C   1 
ATOM   1001 O  O   . LYS A 1 129 ? -12.019 20.254  11.749  1.00 10.91  ? 124 LYS A O   1 
ATOM   1002 C  CB  . LYS A 1 129 ? -10.936 22.861  9.935   1.00 11.80  ? 124 LYS A CB  1 
ATOM   1003 C  CG  . LYS A 1 129 ? -9.862  22.800  11.010  1.00 13.23  ? 124 LYS A CG  1 
ATOM   1004 C  CD  . LYS A 1 129 ? -9.028  24.059  11.029  1.00 17.00  ? 124 LYS A CD  1 
ATOM   1005 C  CE  . LYS A 1 129 ? -8.016  24.072  12.140  1.00 20.76  ? 124 LYS A CE  1 
ATOM   1006 N  NZ  . LYS A 1 129 ? -7.034  25.179  11.968  1.00 25.84  ? 124 LYS A NZ  1 
ATOM   1007 N  N   . GLY A 1 130 ? -13.553 21.856  11.351  1.00 11.10  ? 125 GLY A N   1 
ATOM   1008 C  CA  . GLY A 1 130 ? -14.409 21.479  12.474  1.00 12.02  ? 125 GLY A CA  1 
ATOM   1009 C  C   . GLY A 1 130 ? -14.885 20.030  12.409  1.00 11.30  ? 125 GLY A C   1 
ATOM   1010 O  O   . GLY A 1 130 ? -14.872 19.300  13.406  1.00 10.48  ? 125 GLY A O   1 
ATOM   1011 N  N   . ASP A 1 131 ? -15.353 19.620  11.227  1.00 10.46  ? 126 ASP A N   1 
ATOM   1012 C  CA  . ASP A 1 131 ? -15.887 18.288  11.030  1.00 9.86   ? 126 ASP A CA  1 
ATOM   1013 C  C   . ASP A 1 131 ? -14.854 17.191  11.297  1.00 10.54  ? 126 ASP A C   1 
ATOM   1014 O  O   . ASP A 1 131 ? -15.160 16.210  11.979  1.00 12.34  ? 126 ASP A O   1 
ATOM   1015 C  CB  . ASP A 1 131 ? -16.460 18.119  9.616   1.00 10.30  ? 126 ASP A CB  1 
ATOM   1016 C  CG  . ASP A 1 131 ? -17.767 18.854  9.308   1.00 12.08  ? 126 ASP A CG  1 
ATOM   1017 O  OD1 . ASP A 1 131 ? -18.479 19.248  10.277  1.00 12.56  ? 126 ASP A OD1 1 
ATOM   1018 O  OD2 . ASP A 1 131 ? -18.078 19.030  8.101   1.00 13.65  ? 126 ASP A OD2 1 
ATOM   1019 N  N   . TYR A 1 132 ? -13.631 17.361  10.776  1.00 11.16  ? 127 TYR A N   1 
ATOM   1020 C  CA  . TYR A 1 132 ? -12.616 16.325  10.909  1.00 12.39  ? 127 TYR A CA  1 
ATOM   1021 C  C   . TYR A 1 132 ? -12.020 16.283  12.316  1.00 12.22  ? 127 TYR A C   1 
ATOM   1022 O  O   . TYR A 1 132 ? -11.664 15.197  12.789  1.00 12.32  ? 127 TYR A O   1 
ATOM   1023 C  CB  . TYR A 1 132 ? -11.571 16.374  9.738   1.00 11.88  ? 127 TYR A CB  1 
ATOM   1024 C  CG  . TYR A 1 132 ? -12.220 15.792  8.490   1.00 11.52  ? 127 TYR A CG  1 
ATOM   1025 C  CD1 . TYR A 1 132 ? -13.041 16.567  7.683   1.00 11.02  ? 127 TYR A CD1 1 
ATOM   1026 C  CD2 . TYR A 1 132 ? -12.115 14.440  8.193   1.00 12.31  ? 127 TYR A CD2 1 
ATOM   1027 C  CE1 . TYR A 1 132 ? -13.713 16.016  6.588   1.00 11.86  ? 127 TYR A CE1 1 
ATOM   1028 C  CE2 . TYR A 1 132 ? -12.791 13.874  7.114   1.00 11.76  ? 127 TYR A CE2 1 
ATOM   1029 C  CZ  . TYR A 1 132 ? -13.579 14.667  6.301   1.00 14.53  ? 127 TYR A CZ  1 
ATOM   1030 O  OH  . TYR A 1 132 ? -14.249 14.119  5.218   1.00 13.58  ? 127 TYR A OH  1 
ATOM   1031 N  N   . TYR A 1 133 ? -11.970 17.427  13.019  1.00 12.23  ? 128 TYR A N   1 
ATOM   1032 C  CA  . TYR A 1 133 ? -11.654 17.380  14.442  1.00 12.20  ? 128 TYR A CA  1 
ATOM   1033 C  C   . TYR A 1 133 ? -12.784 16.707  15.225  1.00 11.57  ? 128 TYR A C   1 
ATOM   1034 O  O   . TYR A 1 133 ? -12.524 15.986  16.185  1.00 12.76  ? 128 TYR A O   1 
ATOM   1035 C  CB  . TYR A 1 133 ? -11.305 18.781  15.018  1.00 11.56  ? 128 TYR A CB  1 
ATOM   1036 C  CG  . TYR A 1 133 ? -9.857  19.183  14.844  1.00 13.65  ? 128 TYR A CG  1 
ATOM   1037 C  CD1 . TYR A 1 133 ? -8.844  18.528  15.530  1.00 13.56  ? 128 TYR A CD1 1 
ATOM   1038 C  CD2 . TYR A 1 133 ? -9.503  20.229  14.012  1.00 14.55  ? 128 TYR A CD2 1 
ATOM   1039 C  CE1 . TYR A 1 133 ? -7.513  18.898  15.382  1.00 15.20  ? 128 TYR A CE1 1 
ATOM   1040 C  CE2 . TYR A 1 133 ? -8.173  20.604  13.849  1.00 15.41  ? 128 TYR A CE2 1 
ATOM   1041 C  CZ  . TYR A 1 133 ? -7.181  19.932  14.535  1.00 16.39  ? 128 TYR A CZ  1 
ATOM   1042 O  OH  . TYR A 1 133 ? -5.860  20.295  14.386  1.00 19.93  ? 128 TYR A OH  1 
ATOM   1043 N  N   . ARG A 1 134 ? -14.037 16.903  14.788  1.00 11.11  ? 129 ARG A N   1 
ATOM   1044 C  CA  . ARG A 1 134 ? -15.158 16.228  15.423  1.00 12.16  ? 129 ARG A CA  1 
ATOM   1045 C  C   . ARG A 1 134 ? -15.054 14.706  15.266  1.00 14.23  ? 129 ARG A C   1 
ATOM   1046 O  O   . ARG A 1 134 ? -15.262 13.956  16.220  1.00 13.04  ? 129 ARG A O   1 
ATOM   1047 C  CB  . ARG A 1 134 ? -16.486 16.784  14.874  1.00 12.14  ? 129 ARG A CB  1 
ATOM   1048 C  CG  . ARG A 1 134 ? -17.723 15.981  15.322  1.00 11.26  ? 129 ARG A CG  1 
ATOM   1049 C  CD  . ARG A 1 134 ? -19.011 16.781  15.211  1.00 11.77  ? 129 ARG A CD  1 
ATOM   1050 N  NE  . ARG A 1 134 ? -19.336 17.192  13.846  1.00 10.56  ? 129 ARG A NE  1 
ATOM   1051 C  CZ  . ARG A 1 134 ? -19.940 16.434  12.939  1.00 13.54  ? 129 ARG A CZ  1 
ATOM   1052 N  NH1 . ARG A 1 134 ? -20.418 15.240  13.242  1.00 11.78  ? 129 ARG A NH1 1 
ATOM   1053 N  NH2 . ARG A 1 134 ? -20.112 16.905  11.708  1.00 13.90  ? 129 ARG A NH2 1 
ATOM   1054 N  N   . TYR A 1 135 ? -14.657 14.232  14.084  1.00 11.25  ? 130 TYR A N   1 
ATOM   1055 C  CA  . TYR A 1 135 ? -14.493 12.795  13.896  1.00 12.63  ? 130 TYR A CA  1 
ATOM   1056 C  C   . TYR A 1 135 ? -13.354 12.236  14.748  1.00 13.49  ? 130 TYR A C   1 
ATOM   1057 O  O   . TYR A 1 135 ? -13.467 11.133  15.290  1.00 14.43  ? 130 TYR A O   1 
ATOM   1058 C  CB  . TYR A 1 135 ? -14.337 12.456  12.403  1.00 11.90  ? 130 TYR A CB  1 
ATOM   1059 C  CG  . TYR A 1 135 ? -15.422 13.035  11.502  1.00 12.93  ? 130 TYR A CG  1 
ATOM   1060 C  CD1 . TYR A 1 135 ? -16.733 13.176  11.947  1.00 11.86  ? 130 TYR A CD1 1 
ATOM   1061 C  CD2 . TYR A 1 135 ? -15.138 13.411  10.200  1.00 12.58  ? 130 TYR A CD2 1 
ATOM   1062 C  CE1 . TYR A 1 135 ? -17.727 13.700  11.115  1.00 12.78  ? 130 TYR A CE1 1 
ATOM   1063 C  CE2 . TYR A 1 135 ? -16.119 13.924  9.361   1.00 14.11  ? 130 TYR A CE2 1 
ATOM   1064 C  CZ  . TYR A 1 135 ? -17.416 14.076  9.821   1.00 14.68  ? 130 TYR A CZ  1 
ATOM   1065 O  OH  . TYR A 1 135 ? -18.365 14.615  8.953   1.00 15.27  ? 130 TYR A OH  1 
ATOM   1066 N  N   . LEU A 1 136 ? -12.261 12.994  14.879  1.00 13.00  ? 131 LEU A N   1 
ATOM   1067 C  CA  . LEU A 1 136 ? -11.210 12.631  15.824  1.00 12.82  ? 131 LEU A CA  1 
ATOM   1068 C  C   . LEU A 1 136 ? -11.738 12.573  17.259  1.00 14.51  ? 131 LEU A C   1 
ATOM   1069 O  O   . LEU A 1 136 ? -11.377 11.675  18.017  1.00 14.07  ? 131 LEU A O   1 
ATOM   1070 C  CB  . LEU A 1 136 ? -10.007 13.607  15.744  1.00 12.02  ? 131 LEU A CB  1 
ATOM   1071 C  CG  . LEU A 1 136 ? -9.166  13.533  14.475  1.00 12.47  ? 131 LEU A CG  1 
ATOM   1072 C  CD1 . LEU A 1 136 ? -8.089  14.578  14.473  1.00 14.81  ? 131 LEU A CD1 1 
ATOM   1073 C  CD2 . LEU A 1 136 ? -8.534  12.135  14.309  1.00 12.40  ? 131 LEU A CD2 1 
ATOM   1074 N  N   . ALA A 1 137 ? -12.603 13.522  17.634  1.00 13.08  ? 132 ALA A N   1 
ATOM   1075 C  CA  . ALA A 1 137 ? -13.154 13.542  18.982  1.00 14.04  ? 132 ALA A CA  1 
ATOM   1076 C  C   . ALA A 1 137 ? -14.050 12.344  19.288  1.00 14.04  ? 132 ALA A C   1 
ATOM   1077 O  O   . ALA A 1 137 ? -14.122 11.914  20.437  1.00 16.24  ? 132 ALA A O   1 
ATOM   1078 C  CB  . ALA A 1 137 ? -13.926 14.826  19.223  1.00 13.65  ? 132 ALA A CB  1 
ATOM   1079 N  N   . GLU A 1 138 ? -14.731 11.817  18.262  1.00 14.01  ? 133 GLU A N   1 
ATOM   1080 C  CA  . GLU A 1 138 ? -15.612 10.673  18.423  1.00 15.62  ? 133 GLU A CA  1 
ATOM   1081 C  C   . GLU A 1 138 ? -14.866 9.442   18.950  1.00 14.51  ? 133 GLU A C   1 
ATOM   1082 O  O   . GLU A 1 138 ? -15.461 8.614   19.636  1.00 15.47  ? 133 GLU A O   1 
ATOM   1083 C  CB  . GLU A 1 138 ? -16.317 10.309  17.084  1.00 15.35  ? 133 GLU A CB  1 
ATOM   1084 C  CG  . GLU A 1 138 ? -17.438 11.257  16.656  1.00 16.25  ? 133 GLU A CG  1 
ATOM   1085 C  CD  . GLU A 1 138 ? -18.079 10.931  15.314  1.00 20.03  ? 133 GLU A CD  1 
ATOM   1086 O  OE1 . GLU A 1 138 ? -17.478 10.203  14.488  1.00 17.96  ? 133 GLU A OE1 1 
ATOM   1087 O  OE2 . GLU A 1 138 ? -19.222 11.392  15.099  1.00 19.62  ? 133 GLU A OE2 1 
ATOM   1088 N  N   . VAL A 1 139 ? -13.576 9.308   18.624  1.00 15.07  ? 134 VAL A N   1 
ATOM   1089 C  CA  . VAL A 1 139 ? -12.804 8.139   19.032  1.00 16.64  ? 134 VAL A CA  1 
ATOM   1090 C  C   . VAL A 1 139 ? -11.747 8.438   20.093  1.00 18.82  ? 134 VAL A C   1 
ATOM   1091 O  O   . VAL A 1 139 ? -11.031 7.534   20.526  1.00 18.32  ? 134 VAL A O   1 
ATOM   1092 C  CB  . VAL A 1 139 ? -12.174 7.461   17.790  1.00 15.18  ? 134 VAL A CB  1 
ATOM   1093 C  CG1 . VAL A 1 139 ? -13.235 7.222   16.735  1.00 16.04  ? 134 VAL A CG1 1 
ATOM   1094 C  CG2 . VAL A 1 139 ? -11.011 8.257   17.202  1.00 18.06  ? 134 VAL A CG2 1 
ATOM   1095 N  N   . ALA A 1 140 ? -11.659 9.703   20.518  1.00 18.10  ? 135 ALA A N   1 
ATOM   1096 C  CA  . ALA A 1 140 ? -10.642 10.133  21.465  1.00 17.56  ? 135 ALA A CA  1 
ATOM   1097 C  C   . ALA A 1 140 ? -11.042 9.754   22.888  1.00 21.22  ? 135 ALA A C   1 
ATOM   1098 O  O   . ALA A 1 140 ? -12.217 9.826   23.233  1.00 21.77  ? 135 ALA A O   1 
ATOM   1099 C  CB  . ALA A 1 140 ? -10.432 11.639  21.354  1.00 19.85  ? 135 ALA A CB  1 
ATOM   1100 N  N   . THR A 1 141 ? -10.061 9.325   23.692  1.00 25.40  ? 136 THR A N   1 
ATOM   1101 C  CA  . THR A 1 141 ? -10.310 8.958   25.080  1.00 39.80  ? 136 THR A CA  1 
ATOM   1102 C  C   . THR A 1 141 ? -9.236  9.403   26.071  1.00 57.62  ? 136 THR A C   1 
ATOM   1103 O  O   . THR A 1 141 ? -9.401  9.220   27.275  1.00 69.83  ? 136 THR A O   1 
ATOM   1104 C  CB  . THR A 1 141 ? -10.457 7.428   25.204  1.00 38.26  ? 136 THR A CB  1 
ATOM   1105 O  OG1 . THR A 1 141 ? -9.235  6.807   24.790  1.00 34.38  ? 136 THR A OG1 1 
ATOM   1106 C  CG2 . THR A 1 141 ? -11.608 6.883   24.390  1.00 40.43  ? 136 THR A CG2 1 
ATOM   1107 N  N   . GLY A 1 142 ? -8.152  10.006  25.567  1.00 60.73  ? 137 GLY A N   1 
ATOM   1108 C  CA  . GLY A 1 142 ? -6.946  10.211  26.354  1.00 62.51  ? 137 GLY A CA  1 
ATOM   1109 C  C   . GLY A 1 142 ? -6.750  11.648  26.828  1.00 52.93  ? 137 GLY A C   1 
ATOM   1110 O  O   . GLY A 1 142 ? -7.718  12.385  27.019  1.00 54.74  ? 137 GLY A O   1 
ATOM   1111 N  N   . ASP A 1 143 ? -5.478  12.025  27.010  1.00 39.94  ? 138 ASP A N   1 
ATOM   1112 C  CA  . ASP A 1 143 ? -5.107  13.354  27.472  1.00 56.56  ? 138 ASP A CA  1 
ATOM   1113 C  C   . ASP A 1 143 ? -5.523  14.469  26.514  1.00 48.86  ? 138 ASP A C   1 
ATOM   1114 O  O   . ASP A 1 143 ? -5.729  15.601  26.945  1.00 65.74  ? 138 ASP A O   1 
ATOM   1115 C  CB  . ASP A 1 143 ? -3.580  13.446  27.695  1.00 52.95  ? 138 ASP A CB  1 
ATOM   1116 C  CG  . ASP A 1 143 ? -3.042  12.656  28.868  1.00 65.25  ? 138 ASP A CG  1 
ATOM   1117 O  OD1 . ASP A 1 143 ? -3.844  11.989  29.553  1.00 61.53  ? 138 ASP A OD1 1 
ATOM   1118 O  OD2 . ASP A 1 143 ? -1.813  12.707  29.103  1.00 74.03  ? 138 ASP A OD2 1 
ATOM   1119 N  N   . ASP A 1 144 ? -5.636  14.145  25.219  1.00 42.24  ? 139 ASP A N   1 
ATOM   1120 C  CA  . ASP A 1 144 ? -5.925  15.147  24.205  1.00 51.31  ? 139 ASP A CA  1 
ATOM   1121 C  C   . ASP A 1 144 ? -7.386  15.227  23.759  1.00 38.20  ? 139 ASP A C   1 
ATOM   1122 O  O   . ASP A 1 144 ? -7.694  16.002  22.863  1.00 29.78  ? 139 ASP A O   1 
ATOM   1123 C  CB  . ASP A 1 144 ? -5.025  14.920  22.966  1.00 56.72  ? 139 ASP A CB  1 
ATOM   1124 C  CG  . ASP A 1 144 ? -3.579  15.334  23.160  1.00 61.11  ? 139 ASP A CG  1 
ATOM   1125 O  OD1 . ASP A 1 144 ? -3.341  16.486  23.587  1.00 54.39  ? 139 ASP A OD1 1 
ATOM   1126 O  OD2 . ASP A 1 144 ? -2.686  14.516  22.866  1.00 60.71  ? 139 ASP A OD2 1 
ATOM   1127 N  N   . LYS A 1 145 ? -8.292  14.464  24.384  1.00 31.19  ? 140 LYS A N   1 
ATOM   1128 C  CA  . LYS A 1 145 ? -9.699  14.563  24.027  1.00 29.62  ? 140 LYS A CA  1 
ATOM   1129 C  C   . LYS A 1 145 ? -10.200 16.003  24.165  1.00 26.85  ? 140 LYS A C   1 
ATOM   1130 O  O   . LYS A 1 145 ? -10.893 16.509  23.281  1.00 19.61  ? 140 LYS A O   1 
ATOM   1131 C  CB  . LYS A 1 145 ? -10.590 13.639  24.865  1.00 30.71  ? 140 LYS A CB  1 
ATOM   1132 C  CG  . LYS A 1 145 ? -11.971 13.486  24.247  1.00 39.21  ? 140 LYS A CG  1 
ATOM   1133 C  CD  . LYS A 1 145 ? -12.948 12.691  25.080  1.00 52.01  ? 140 LYS A CD  1 
ATOM   1134 C  CE  . LYS A 1 145 ? -14.255 12.522  24.342  1.00 44.62  ? 140 LYS A CE  1 
ATOM   1135 N  NZ  . LYS A 1 145 ? -15.316 11.968  25.214  1.00 46.98  ? 140 LYS A NZ  1 
ATOM   1136 N  N   . LYS A 1 146 ? -9.843  16.665  25.270  1.00 24.70  ? 141 LYS A N   1 
ATOM   1137 C  CA  . LYS A 1 146 ? -10.279 18.033  25.501  1.00 24.76  ? 141 LYS A CA  1 
ATOM   1138 C  C   . LYS A 1 146 ? -9.717  18.994  24.461  1.00 19.47  ? 141 LYS A C   1 
ATOM   1139 O  O   . LYS A 1 146 ? -10.427 19.888  24.007  1.00 18.95  ? 141 LYS A O   1 
ATOM   1140 C  CB  . LYS A 1 146 ? -9.905  18.510  26.915  1.00 24.33  ? 141 LYS A CB  1 
ATOM   1141 C  CG  . LYS A 1 146 ? -10.735 17.855  27.977  1.00 27.59  ? 141 LYS A CG  1 
ATOM   1142 C  CD  . LYS A 1 146 ? -10.331 18.297  29.392  1.00 36.52  ? 141 LYS A CD  1 
ATOM   1143 C  CE  . LYS A 1 146 ? -11.081 17.550  30.466  1.00 46.98  ? 141 LYS A CE  1 
ATOM   1144 N  NZ  . LYS A 1 146 ? -10.744 18.063  31.823  1.00 47.80  ? 141 LYS A NZ  1 
ATOM   1145 N  N   . ARG A 1 147 ? -8.433  18.842  24.111  1.00 20.02  ? 142 ARG A N   1 
ATOM   1146 C  CA  . ARG A 1 147 ? -7.817  19.736  23.145  1.00 20.64  ? 142 ARG A CA  1 
ATOM   1147 C  C   . ARG A 1 147 ? -8.412  19.502  21.756  1.00 15.25  ? 142 ARG A C   1 
ATOM   1148 O  O   . ARG A 1 147 ? -8.593  20.457  21.011  1.00 16.65  ? 142 ARG A O   1 
ATOM   1149 C  CB  . ARG A 1 147 ? -6.271  19.628  23.138  1.00 26.61  ? 142 ARG A CB  1 
ATOM   1150 C  CG  . ARG A 1 147 ? -5.591  20.617  24.112  1.00 32.08  ? 142 ARG A CG  1 
ATOM   1151 C  CD  . ARG A 1 147 ? -4.068  20.561  24.035  1.00 33.99  ? 142 ARG A CD  1 
ATOM   1152 N  NE  . ARG A 1 147 ? -3.507  19.475  24.833  1.00 31.71  ? 142 ARG A NE  1 
ATOM   1153 C  CZ  . ARG A 1 147 ? -3.337  19.512  26.150  1.00 32.75  ? 142 ARG A CZ  1 
ATOM   1154 N  NH1 . ARG A 1 147 ? -3.279  20.659  26.810  1.00 27.12  ? 142 ARG A NH1 1 
ATOM   1155 N  NH2 . ARG A 1 147 ? -3.199  18.370  26.818  1.00 38.83  ? 142 ARG A NH2 1 
ATOM   1156 N  N   . ILE A 1 148 ? -8.735  18.245  21.422  1.00 16.81  ? 143 ILE A N   1 
ATOM   1157 C  CA  . ILE A 1 148 ? -9.357  17.951  20.140  1.00 14.62  ? 143 ILE A CA  1 
ATOM   1158 C  C   . ILE A 1 148 ? -10.737 18.605  20.043  1.00 15.32  ? 143 ILE A C   1 
ATOM   1159 O  O   . ILE A 1 148 ? -11.082 19.199  19.019  1.00 15.13  ? 143 ILE A O   1 
ATOM   1160 C  CB  . ILE A 1 148 ? -9.414  16.436  19.892  1.00 18.29  ? 143 ILE A CB  1 
ATOM   1161 C  CG1 . ILE A 1 148 ? -8.002  15.854  19.708  1.00 23.06  ? 143 ILE A CG1 1 
ATOM   1162 C  CG2 . ILE A 1 148 ? -10.296 16.137  18.702  1.00 17.13  ? 143 ILE A CG2 1 
ATOM   1163 C  CD1 . ILE A 1 148 ? -7.940  14.328  19.848  1.00 28.58  ? 143 ILE A CD1 1 
ATOM   1164 N  N   . ILE A 1 149 ? -11.527 18.492  21.116  1.00 14.51  ? 144 ILE A N   1 
ATOM   1165 C  CA  . ILE A 1 149 ? -12.826 19.136  21.188  1.00 14.25  ? 144 ILE A CA  1 
ATOM   1166 C  C   . ILE A 1 149 ? -12.693 20.645  21.026  1.00 15.64  ? 144 ILE A C   1 
ATOM   1167 O  O   . ILE A 1 149 ? -13.458 21.260  20.282  1.00 15.81  ? 144 ILE A O   1 
ATOM   1168 C  CB  . ILE A 1 149 ? -13.563 18.731  22.486  1.00 15.29  ? 144 ILE A CB  1 
ATOM   1169 C  CG1 . ILE A 1 149 ? -13.974 17.238  22.420  1.00 17.48  ? 144 ILE A CG1 1 
ATOM   1170 C  CG2 . ILE A 1 149 ? -14.777 19.607  22.763  1.00 16.05  ? 144 ILE A CG2 1 
ATOM   1171 C  CD1 . ILE A 1 149 ? -14.535 16.662  23.722  1.00 20.30  ? 144 ILE A CD1 1 
ATOM   1172 N  N   . ASP A 1 150 ? -11.716 21.259  21.698  1.00 14.70  ? 145 ASP A N   1 
ATOM   1173 C  CA  . ASP A 1 150 ? -11.566 22.698  21.584  1.00 14.75  ? 145 ASP A CA  1 
ATOM   1174 C  C   . ASP A 1 150 ? -11.140 23.131  20.180  1.00 14.08  ? 145 ASP A C   1 
ATOM   1175 O  O   . ASP A 1 150 ? -11.526 24.209  19.720  1.00 16.38  ? 145 ASP A O   1 
ATOM   1176 C  CB  . ASP A 1 150 ? -10.598 23.283  22.618  1.00 18.27  ? 145 ASP A CB  1 
ATOM   1177 C  CG  . ASP A 1 150 ? -10.886 24.771  22.864  1.00 25.63  ? 145 ASP A CG  1 
ATOM   1178 O  OD1 . ASP A 1 150 ? -12.039 25.106  23.247  1.00 31.17  ? 145 ASP A OD1 1 
ATOM   1179 O  OD2 . ASP A 1 150 ? -9.979  25.591  22.659  1.00 29.81  ? 145 ASP A OD2 1 
ATOM   1180 N  N   . SER A 1 151 ? -10.338 22.296  19.507  1.00 13.88  ? 146 SER A N   1 
ATOM   1181 C  CA  . SER A 1 151 ? -9.954  22.564  18.128  1.00 13.26  ? 146 SER A CA  1 
ATOM   1182 C  C   . SER A 1 151 ? -11.166 22.556  17.194  1.00 11.49  ? 146 SER A C   1 
ATOM   1183 O  O   . SER A 1 151 ? -11.294 23.421  16.323  1.00 14.25  ? 146 SER A O   1 
ATOM   1184 C  CB  . SER A 1 151 ? -8.901  21.565  17.660  1.00 16.18  ? 146 SER A CB  1 
ATOM   1185 O  OG  . SER A 1 151 ? -7.643  21.833  18.275  1.00 18.35  ? 146 SER A OG  1 
ATOM   1186 N  N   . ALA A 1 152 ? -12.050 21.568  17.373  1.00 12.70  ? 147 ALA A N   1 
ATOM   1187 C  CA  . ALA A 1 152 ? -13.289 21.546  16.607  1.00 13.71  ? 147 ALA A CA  1 
ATOM   1188 C  C   . ALA A 1 152 ? -14.137 22.795  16.869  1.00 13.91  ? 147 ALA A C   1 
ATOM   1189 O  O   . ALA A 1 152 ? -14.584 23.461  15.933  1.00 13.50  ? 147 ALA A O   1 
ATOM   1190 C  CB  . ALA A 1 152 ? -14.073 20.278  16.904  1.00 12.19  ? 147 ALA A CB  1 
ATOM   1191 N  N   . ARG A 1 153 ? -14.361 23.103  18.153  1.00 12.87  ? 148 ARG A N   1 
ATOM   1192 C  CA  A ARG A 1 153 ? -15.168 24.251  18.533  0.50 13.33  ? 148 ARG A CA  1 
ATOM   1193 C  CA  B ARG A 1 153 ? -15.134 24.261  18.571  0.50 15.22  ? 148 ARG A CA  1 
ATOM   1194 C  C   . ARG A 1 153 ? -14.626 25.540  17.916  1.00 13.62  ? 148 ARG A C   1 
ATOM   1195 O  O   . ARG A 1 153 ? -15.400 26.334  17.401  1.00 14.47  ? 148 ARG A O   1 
ATOM   1196 C  CB  A ARG A 1 153 ? -15.208 24.383  20.072  0.50 13.48  ? 148 ARG A CB  1 
ATOM   1197 C  CB  B ARG A 1 153 ? -15.015 24.417  20.100  0.50 16.79  ? 148 ARG A CB  1 
ATOM   1198 C  CG  A ARG A 1 153 ? -16.210 25.415  20.586  0.50 12.56  ? 148 ARG A CG  1 
ATOM   1199 C  CG  B ARG A 1 153 ? -15.782 25.597  20.671  0.50 18.17  ? 148 ARG A CG  1 
ATOM   1200 C  CD  A ARG A 1 153 ? -16.000 25.706  22.065  0.50 12.98  ? 148 ARG A CD  1 
ATOM   1201 C  CD  B ARG A 1 153 ? -15.396 25.876  22.114  0.50 20.78  ? 148 ARG A CD  1 
ATOM   1202 N  NE  A ARG A 1 153 ? -15.975 24.489  22.867  0.50 15.93  ? 148 ARG A NE  1 
ATOM   1203 N  NE  B ARG A 1 153 ? -14.638 27.113  22.277  0.50 29.82  ? 148 ARG A NE  1 
ATOM   1204 C  CZ  A ARG A 1 153 ? -17.051 23.827  23.263  0.50 15.23  ? 148 ARG A CZ  1 
ATOM   1205 C  CZ  B ARG A 1 153 ? -13.919 27.704  21.333  0.50 20.54  ? 148 ARG A CZ  1 
ATOM   1206 N  NH1 A ARG A 1 153 ? -18.262 24.349  23.148  0.50 13.61  ? 148 ARG A NH1 1 
ATOM   1207 N  NH1 B ARG A 1 153 ? -12.609 27.537  21.256  0.50 19.40  ? 148 ARG A NH1 1 
ATOM   1208 N  NH2 A ARG A 1 153 ? -16.905 22.622  23.811  0.50 16.77  ? 148 ARG A NH2 1 
ATOM   1209 N  NH2 B ARG A 1 153 ? -14.505 28.597  20.542  0.50 17.17  ? 148 ARG A NH2 1 
ATOM   1210 N  N   . SER A 1 154 ? -13.304 25.727  17.986  1.00 15.11  ? 149 SER A N   1 
ATOM   1211 C  CA  . SER A 1 154 ? -12.632 26.918  17.493  1.00 16.06  ? 149 SER A CA  1 
ATOM   1212 C  C   . SER A 1 154 ? -12.822 27.113  15.991  1.00 15.42  ? 149 SER A C   1 
ATOM   1213 O  O   . SER A 1 154 ? -13.097 28.220  15.530  1.00 15.35  ? 149 SER A O   1 
ATOM   1214 C  CB  . SER A 1 154 ? -11.148 26.851  17.834  1.00 18.00  ? 149 SER A CB  1 
ATOM   1215 O  OG  . SER A 1 154 ? -10.502 28.062  17.493  1.00 25.89  ? 149 SER A OG  1 
ATOM   1216 N  N   . ALA A 1 155 ? -12.697 26.024  15.231  1.00 12.81  ? 150 ALA A N   1 
ATOM   1217 C  CA  . ALA A 1 155 ? -12.893 26.080  13.791  1.00 14.95  ? 150 ALA A CA  1 
ATOM   1218 C  C   . ALA A 1 155 ? -14.344 26.409  13.426  1.00 12.52  ? 150 ALA A C   1 
ATOM   1219 O  O   . ALA A 1 155 ? -14.594 27.298  12.603  1.00 13.40  ? 150 ALA A O   1 
ATOM   1220 C  CB  . ALA A 1 155 ? -12.442 24.758  13.152  1.00 13.81  ? 150 ALA A CB  1 
ATOM   1221 N  N   . TYR A 1 156 ? -15.298 25.714  14.058  1.00 12.30  ? 151 TYR A N   1 
ATOM   1222 C  CA  . TYR A 1 156 ? -16.710 25.984  13.836  1.00 12.86  ? 151 TYR A CA  1 
ATOM   1223 C  C   . TYR A 1 156 ? -17.073 27.427  14.202  1.00 14.03  ? 151 TYR A C   1 
ATOM   1224 O  O   . TYR A 1 156 ? -17.831 28.081  13.486  1.00 12.66  ? 151 TYR A O   1 
ATOM   1225 C  CB  . TYR A 1 156 ? -17.579 25.013  14.633  1.00 12.70  ? 151 TYR A CB  1 
ATOM   1226 C  CG  . TYR A 1 156 ? -17.680 23.584  14.127  1.00 12.09  ? 151 TYR A CG  1 
ATOM   1227 C  CD1 . TYR A 1 156 ? -17.977 23.311  12.794  1.00 11.80  ? 151 TYR A CD1 1 
ATOM   1228 C  CD2 . TYR A 1 156 ? -17.616 22.507  15.004  1.00 12.51  ? 151 TYR A CD2 1 
ATOM   1229 C  CE1 . TYR A 1 156 ? -18.155 22.007  12.341  1.00 11.98  ? 151 TYR A CE1 1 
ATOM   1230 C  CE2 . TYR A 1 156 ? -17.793 21.200  14.561  1.00 12.85  ? 151 TYR A CE2 1 
ATOM   1231 C  CZ  . TYR A 1 156 ? -18.068 20.951  13.228  1.00 13.14  ? 151 TYR A CZ  1 
ATOM   1232 O  OH  . TYR A 1 156 ? -18.247 19.641  12.798  1.00 11.68  ? 151 TYR A OH  1 
ATOM   1233 N  N   . GLN A 1 157 ? -16.490 27.941  15.293  1.00 13.19  ? 152 GLN A N   1 
ATOM   1234 C  CA  . GLN A 1 157 ? -16.810 29.284  15.756  1.00 14.38  ? 152 GLN A CA  1 
ATOM   1235 C  C   . GLN A 1 157 ? -16.330 30.351  14.775  1.00 13.58  ? 152 GLN A C   1 
ATOM   1236 O  O   . GLN A 1 157 ? -17.053 31.318  14.516  1.00 15.32  ? 152 GLN A O   1 
ATOM   1237 C  CB  . GLN A 1 157 ? -16.218 29.567  17.144  1.00 15.05  ? 152 GLN A CB  1 
ATOM   1238 C  CG  . GLN A 1 157 ? -16.755 30.861  17.784  1.00 20.60  ? 152 GLN A CG  1 
ATOM   1239 C  CD  . GLN A 1 157 ? -18.259 30.858  17.890  1.00 20.72  ? 152 GLN A CD  1 
ATOM   1240 O  OE1 . GLN A 1 157 ? -18.839 30.025  18.609  1.00 24.58  ? 152 GLN A OE1 1 
ATOM   1241 N  NE2 . GLN A 1 157 ? -18.936 31.781  17.177  1.00 23.52  ? 152 GLN A NE2 1 
ATOM   1242 N  N   . GLU A 1 158 ? -15.100 30.196  14.257  1.00 14.05  ? 153 GLU A N   1 
ATOM   1243 C  CA  . GLU A 1 158 ? -14.552 31.143  13.287  1.00 15.05  ? 153 GLU A CA  1 
ATOM   1244 C  C   . GLU A 1 158 ? -15.403 31.132  12.018  1.00 14.81  ? 153 GLU A C   1 
ATOM   1245 O  O   . GLU A 1 158 ? -15.712 32.186  11.454  1.00 16.58  ? 153 GLU A O   1 
ATOM   1246 C  CB  . GLU A 1 158 ? -13.076 30.852  12.951  1.00 17.72  ? 153 GLU A CB  1 
ATOM   1247 C  CG  . GLU A 1 158 ? -12.483 31.838  11.953  1.00 24.77  ? 153 GLU A CG  1 
ATOM   1248 C  CD  . GLU A 1 158 ? -11.000 31.700  11.652  1.00 37.65  ? 153 GLU A CD  1 
ATOM   1249 O  OE1 . GLU A 1 158 ? -10.319 30.861  12.286  1.00 33.81  ? 153 GLU A OE1 1 
ATOM   1250 O  OE2 . GLU A 1 158 ? -10.520 32.444  10.765  1.00 45.25  ? 153 GLU A OE2 1 
ATOM   1251 N  N   . ALA A 1 159 ? -15.800 29.928  11.591  1.00 11.29  ? 154 ALA A N   1 
ATOM   1252 C  CA  . ALA A 1 159 ? -16.677 29.779  10.440  1.00 14.54  ? 154 ALA A CA  1 
ATOM   1253 C  C   . ALA A 1 159 ? -18.022 30.463  10.674  1.00 14.32  ? 154 ALA A C   1 
ATOM   1254 O  O   . ALA A 1 159 ? -18.537 31.120  9.776   1.00 14.07  ? 154 ALA A O   1 
ATOM   1255 C  CB  . ALA A 1 159 ? -16.891 28.306  10.116  1.00 13.04  ? 154 ALA A CB  1 
ATOM   1256 N  N   . MET A 1 160 ? -18.600 30.274  11.871  1.00 14.08  ? 155 MET A N   1 
ATOM   1257 C  CA  . MET A 1 160 ? -19.890 30.867  12.201  1.00 15.18  ? 155 MET A CA  1 
ATOM   1258 C  C   . MET A 1 160 ? -19.790 32.391  12.145  1.00 14.12  ? 155 MET A C   1 
ATOM   1259 O  O   . MET A 1 160 ? -20.679 33.060  11.611  1.00 14.34  ? 155 MET A O   1 
ATOM   1260 C  CB  . MET A 1 160 ? -20.387 30.456  13.596  1.00 15.40  ? 155 MET A CB  1 
ATOM   1261 C  CG  . MET A 1 160 ? -20.824 29.011  13.718  1.00 16.88  ? 155 MET A CG  1 
ATOM   1262 S  SD  . MET A 1 160 ? -22.399 28.582  12.925  1.00 20.83  ? 155 MET A SD  1 
ATOM   1263 C  CE  . MET A 1 160 ? -23.442 29.812  13.601  1.00 26.18  ? 155 MET A CE  1 
ATOM   1264 N  N   . ASP A 1 161 ? -18.712 32.952  12.706  1.00 14.74  ? 156 ASP A N   1 
ATOM   1265 C  CA  . ASP A 1 161 ? -18.587 34.407  12.758  1.00 16.85  ? 156 ASP A CA  1 
ATOM   1266 C  C   . ASP A 1 161 ? -18.540 35.009  11.349  1.00 18.03  ? 156 ASP A C   1 
ATOM   1267 O  O   . ASP A 1 161 ? -19.179 36.025  11.080  1.00 19.70  ? 156 ASP A O   1 
ATOM   1268 C  CB  . ASP A 1 161 ? -17.364 34.832  13.578  1.00 18.84  ? 156 ASP A CB  1 
ATOM   1269 C  CG  . ASP A 1 161 ? -17.370 34.478  15.053  1.00 21.80  ? 156 ASP A CG  1 
ATOM   1270 O  OD1 . ASP A 1 161 ? -18.441 34.190  15.587  1.00 25.23  ? 156 ASP A OD1 1 
ATOM   1271 O  OD2 . ASP A 1 161 ? -16.278 34.487  15.669  1.00 25.66  ? 156 ASP A OD2 1 
ATOM   1272 N  N   . ILE A 1 162 ? -17.810 34.360  10.429  1.00 15.30  ? 157 ILE A N   1 
ATOM   1273 C  CA  . ILE A 1 162 ? -17.716 34.843  9.061   1.00 14.90  ? 157 ILE A CA  1 
ATOM   1274 C  C   . ILE A 1 162 ? -19.061 34.689  8.358   1.00 13.92  ? 157 ILE A C   1 
ATOM   1275 O  O   . ILE A 1 162 ? -19.531 35.611  7.697   1.00 16.56  ? 157 ILE A O   1 
ATOM   1276 C  CB  . ILE A 1 162 ? -16.570 34.124  8.283   1.00 14.48  ? 157 ILE A CB  1 
ATOM   1277 C  CG1 . ILE A 1 162 ? -15.217 34.392  8.934   1.00 16.55  ? 157 ILE A CG1 1 
ATOM   1278 C  CG2 . ILE A 1 162 ? -16.568 34.512  6.788   1.00 15.63  ? 157 ILE A CG2 1 
ATOM   1279 C  CD1 . ILE A 1 162 ? -14.115 33.490  8.442   1.00 18.51  ? 157 ILE A CD1 1 
ATOM   1280 N  N   . SER A 1 163 ? -19.696 33.522  8.529   1.00 12.43  ? 158 SER A N   1 
ATOM   1281 C  CA  . SER A 1 163 ? -20.942 33.240  7.833   1.00 14.03  ? 158 SER A CA  1 
ATOM   1282 C  C   . SER A 1 163 ? -22.050 34.230  8.204   1.00 14.32  ? 158 SER A C   1 
ATOM   1283 O  O   . SER A 1 163 ? -22.864 34.605  7.357   1.00 16.81  ? 158 SER A O   1 
ATOM   1284 C  CB  . SER A 1 163 ? -21.402 31.796  8.086   1.00 15.10  ? 158 SER A CB  1 
ATOM   1285 O  OG  . SER A 1 163 ? -21.932 31.584  9.385   1.00 18.99  ? 158 SER A OG  1 
ATOM   1286 N  N   . LYS A 1 164 ? -22.106 34.637  9.476   1.00 15.93  ? 159 LYS A N   1 
ATOM   1287 C  CA  . LYS A 1 164 ? -23.151 35.544  9.921   1.00 16.37  ? 159 LYS A CA  1 
ATOM   1288 C  C   . LYS A 1 164 ? -22.938 36.962  9.394   1.00 18.91  ? 159 LYS A C   1 
ATOM   1289 O  O   . LYS A 1 164 ? -23.904 37.685  9.162   1.00 22.65  ? 159 LYS A O   1 
ATOM   1290 C  CB  . LYS A 1 164 ? -23.247 35.539  11.454  1.00 23.15  ? 159 LYS A CB  1 
ATOM   1291 C  CG  . LYS A 1 164 ? -23.865 34.263  12.016  1.00 29.79  ? 159 LYS A CG  1 
ATOM   1292 C  CD  . LYS A 1 164 ? -24.051 34.331  13.538  1.00 29.90  ? 159 LYS A CD  1 
ATOM   1293 C  CE  . LYS A 1 164 ? -24.986 33.285  14.057  1.00 45.48  ? 159 LYS A CE  1 
ATOM   1294 N  NZ  . LYS A 1 164 ? -25.352 33.543  15.476  1.00 53.62  ? 159 LYS A NZ  1 
ATOM   1295 N  N   . LYS A 1 165 ? -21.672 37.341  9.208   1.00 16.46  ? 160 LYS A N   1 
ATOM   1296 C  CA  . LYS A 1 165 ? -21.321 38.636  8.649   1.00 19.87  ? 160 LYS A CA  1 
ATOM   1297 C  C   . LYS A 1 165 ? -21.494 38.711  7.134   1.00 22.15  ? 160 LYS A C   1 
ATOM   1298 O  O   . LYS A 1 165 ? -21.879 39.752  6.610   1.00 20.74  ? 160 LYS A O   1 
ATOM   1299 C  CB  . LYS A 1 165 ? -19.868 38.991  8.977   1.00 27.01  ? 160 LYS A CB  1 
ATOM   1300 C  CG  . LYS A 1 165 ? -19.661 39.485  10.391  1.00 39.57  ? 160 LYS A CG  1 
ATOM   1301 C  CD  . LYS A 1 165 ? -18.258 40.040  10.609  1.00 53.58  ? 160 LYS A CD  1 
ATOM   1302 C  CE  . LYS A 1 165 ? -18.053 40.534  12.022  1.00 66.73  ? 160 LYS A CE  1 
ATOM   1303 N  NZ  . LYS A 1 165 ? -16.741 41.217  12.183  1.00 70.23  ? 160 LYS A NZ  1 
ATOM   1304 N  N   . GLU A 1 166 ? -21.160 37.619  6.435   1.00 16.36  ? 161 GLU A N   1 
ATOM   1305 C  CA  . GLU A 1 166 ? -20.945 37.670  4.999   1.00 16.37  ? 161 GLU A CA  1 
ATOM   1306 C  C   . GLU A 1 166 ? -21.955 36.938  4.115   1.00 18.31  ? 161 GLU A C   1 
ATOM   1307 O  O   . GLU A 1 166 ? -21.970 37.160  2.903   1.00 21.74  ? 161 GLU A O   1 
ATOM   1308 C  CB  . GLU A 1 166 ? -19.537 37.121  4.697   1.00 17.06  ? 161 GLU A CB  1 
ATOM   1309 C  CG  . GLU A 1 166 ? -18.408 37.919  5.329   1.00 21.54  ? 161 GLU A CG  1 
ATOM   1310 C  CD  . GLU A 1 166 ? -18.289 39.364  4.880   1.00 34.30  ? 161 GLU A CD  1 
ATOM   1311 O  OE1 . GLU A 1 166 ? -18.896 39.727  3.846   1.00 38.02  ? 161 GLU A OE1 1 
ATOM   1312 O  OE2 . GLU A 1 166 ? -17.596 40.140  5.578   1.00 39.23  ? 161 GLU A OE2 1 
ATOM   1313 N  N   . MET A 1 167 ? -22.800 36.084  4.708   1.00 16.42  ? 162 MET A N   1 
ATOM   1314 C  CA  . MET A 1 167 ? -23.732 35.269  3.946   1.00 16.04  ? 162 MET A CA  1 
ATOM   1315 C  C   . MET A 1 167 ? -25.169 35.460  4.403   1.00 17.14  ? 162 MET A C   1 
ATOM   1316 O  O   . MET A 1 167 ? -25.413 35.678  5.588   1.00 16.71  ? 162 MET A O   1 
ATOM   1317 C  CB  . MET A 1 167 ? -23.407 33.767  4.121   1.00 18.12  ? 162 MET A CB  1 
ATOM   1318 C  CG  . MET A 1 167 ? -22.138 33.333  3.458   1.00 19.98  ? 162 MET A CG  1 
ATOM   1319 S  SD  . MET A 1 167 ? -21.689 31.691  4.105   1.00 22.01  ? 162 MET A SD  1 
ATOM   1320 C  CE  . MET A 1 167 ? -20.536 31.195  2.914   1.00 25.10  ? 162 MET A CE  1 
ATOM   1321 N  N   . PRO A 1 168 ? -26.169 35.311  3.502   1.00 16.24  ? 163 PRO A N   1 
ATOM   1322 C  CA  . PRO A 1 168 ? -27.573 35.326  3.919   1.00 15.89  ? 163 PRO A CA  1 
ATOM   1323 C  C   . PRO A 1 168 ? -27.923 34.086  4.740   1.00 15.61  ? 163 PRO A C   1 
ATOM   1324 O  O   . PRO A 1 168 ? -27.291 33.035  4.585   1.00 17.28  ? 163 PRO A O   1 
ATOM   1325 C  CB  . PRO A 1 168 ? -28.340 35.365  2.598   1.00 17.54  ? 163 PRO A CB  1 
ATOM   1326 C  CG  . PRO A 1 168 ? -27.414 34.749  1.603   1.00 21.72  ? 163 PRO A CG  1 
ATOM   1327 C  CD  . PRO A 1 168 ? -26.007 35.104  2.053   1.00 20.97  ? 163 PRO A CD  1 
ATOM   1328 N  N   . PRO A 1 169 ? -28.946 34.167  5.623   1.00 15.99  ? 164 PRO A N   1 
ATOM   1329 C  CA  . PRO A 1 169 ? -29.313 33.031  6.472   1.00 16.43  ? 164 PRO A CA  1 
ATOM   1330 C  C   . PRO A 1 169 ? -29.738 31.756  5.748   1.00 18.45  ? 164 PRO A C   1 
ATOM   1331 O  O   . PRO A 1 169 ? -29.739 30.688  6.360   1.00 17.05  ? 164 PRO A O   1 
ATOM   1332 C  CB  . PRO A 1 169 ? -30.469 33.568  7.334   1.00 19.98  ? 164 PRO A CB  1 
ATOM   1333 C  CG  . PRO A 1 169 ? -30.521 35.048  7.110   1.00 22.02  ? 164 PRO A CG  1 
ATOM   1334 C  CD  . PRO A 1 169 ? -29.760 35.372  5.871   1.00 20.04  ? 164 PRO A CD  1 
ATOM   1335 N  N   . THR A 1 170 ? -30.084 31.866  4.455   1.00 18.11  ? 165 THR A N   1 
ATOM   1336 C  CA  . THR A 1 170 ? -30.442 30.702  3.662   1.00 14.57  ? 165 THR A CA  1 
ATOM   1337 C  C   . THR A 1 170 ? -29.289 30.086  2.869   1.00 12.99  ? 165 THR A C   1 
ATOM   1338 O  O   . THR A 1 170 ? -29.488 29.097  2.176   1.00 15.23  ? 165 THR A O   1 
ATOM   1339 C  CB  . THR A 1 170 ? -31.564 31.060  2.674   1.00 15.68  ? 165 THR A CB  1 
ATOM   1340 O  OG1 . THR A 1 170 ? -31.192 32.254  1.996   1.00 19.75  ? 165 THR A OG1 1 
ATOM   1341 C  CG2 . THR A 1 170 ? -32.903 31.234  3.360   1.00 21.24  ? 165 THR A CG2 1 
ATOM   1342 N  N   . ASN A 1 171 ? -28.103 30.695  2.917   1.00 14.25  ? 166 ASN A N   1 
ATOM   1343 C  CA  . ASN A 1 171 ? -26.978 30.153  2.167   1.00 13.74  ? 166 ASN A CA  1 
ATOM   1344 C  C   . ASN A 1 171 ? -26.732 28.697  2.582   1.00 12.88  ? 166 ASN A C   1 
ATOM   1345 O  O   . ASN A 1 171 ? -26.617 28.415  3.777   1.00 13.96  ? 166 ASN A O   1 
ATOM   1346 C  CB  . ASN A 1 171 ? -25.738 30.990  2.399   1.00 16.69  ? 166 ASN A CB  1 
ATOM   1347 C  CG  . ASN A 1 171 ? -24.541 30.428  1.691   1.00 20.29  ? 166 ASN A CG  1 
ATOM   1348 O  OD1 . ASN A 1 171 ? -23.874 29.507  2.179   1.00 19.53  ? 166 ASN A OD1 1 
ATOM   1349 N  ND2 . ASN A 1 171 ? -24.231 30.991  0.531   1.00 24.13  ? 166 ASN A ND2 1 
ATOM   1350 N  N   . PRO A 1 172 ? -26.688 27.716  1.648   1.00 12.97  ? 167 PRO A N   1 
ATOM   1351 C  CA  . PRO A 1 172 ? -26.503 26.316  2.039   1.00 13.55  ? 167 PRO A CA  1 
ATOM   1352 C  C   . PRO A 1 172 ? -25.255 26.010  2.863   1.00 13.54  ? 167 PRO A C   1 
ATOM   1353 O  O   . PRO A 1 172 ? -25.288 25.136  3.727   1.00 14.62  ? 167 PRO A O   1 
ATOM   1354 C  CB  . PRO A 1 172 ? -26.477 25.586  0.698   1.00 15.30  ? 167 PRO A CB  1 
ATOM   1355 C  CG  . PRO A 1 172 ? -27.251 26.463  -0.227  1.00 19.44  ? 167 PRO A CG  1 
ATOM   1356 C  CD  . PRO A 1 172 ? -26.958 27.857  0.207   1.00 18.73  ? 167 PRO A CD  1 
ATOM   1357 N  N   . ILE A 1 173 ? -24.143 26.701  2.576   1.00 14.44  ? 168 ILE A N   1 
ATOM   1358 C  CA  . ILE A 1 173 ? -22.931 26.498  3.355   1.00 14.75  ? 168 ILE A CA  1 
ATOM   1359 C  C   . ILE A 1 173 ? -23.158 26.971  4.791   1.00 15.39  ? 168 ILE A C   1 
ATOM   1360 O  O   . ILE A 1 173 ? -22.804 26.270  5.730   1.00 13.05  ? 168 ILE A O   1 
ATOM   1361 C  CB  . ILE A 1 173 ? -21.706 27.165  2.712   1.00 18.22  ? 168 ILE A CB  1 
ATOM   1362 C  CG1 . ILE A 1 173 ? -21.506 26.682  1.262   1.00 22.08  ? 168 ILE A CG1 1 
ATOM   1363 C  CG2 . ILE A 1 173 ? -20.452 26.912  3.556   1.00 15.95  ? 168 ILE A CG2 1 
ATOM   1364 C  CD1 . ILE A 1 173 ? -20.493 27.386  0.563   1.00 22.21  ? 168 ILE A CD1 1 
ATOM   1365 N  N   . ARG A 1 174 ? -23.734 28.167  4.956   1.00 14.52  ? 169 ARG A N   1 
ATOM   1366 C  CA  . ARG A 1 174 ? -24.088 28.675  6.278   1.00 13.16  ? 169 ARG A CA  1 
ATOM   1367 C  C   . ARG A 1 174 ? -25.017 27.711  7.020   1.00 12.16  ? 169 ARG A C   1 
ATOM   1368 O  O   . ARG A 1 174 ? -24.792 27.391  8.194   1.00 12.93  ? 169 ARG A O   1 
ATOM   1369 C  CB  . ARG A 1 174 ? -24.728 30.073  6.182   1.00 13.92  ? 169 ARG A CB  1 
ATOM   1370 C  CG  . ARG A 1 174 ? -25.054 30.695  7.548   1.00 15.03  ? 169 ARG A CG  1 
ATOM   1371 C  CD  . ARG A 1 174 ? -25.491 32.152  7.477   1.00 14.88  ? 169 ARG A CD  1 
ATOM   1372 N  NE  . ARG A 1 174 ? -26.117 32.582  8.724   1.00 15.62  ? 169 ARG A NE  1 
ATOM   1373 C  CZ  . ARG A 1 174 ? -26.623 33.791  8.941   1.00 17.40  ? 169 ARG A CZ  1 
ATOM   1374 N  NH1 . ARG A 1 174 ? -26.501 34.766  8.053   1.00 17.55  ? 169 ARG A NH1 1 
ATOM   1375 N  NH2 . ARG A 1 174 ? -27.277 34.023  10.074  1.00 16.23  ? 169 ARG A NH2 1 
ATOM   1376 N  N   . LEU A 1 175 ? -26.058 27.223  6.338   1.00 12.13  ? 170 LEU A N   1 
ATOM   1377 C  CA  . LEU A 1 175 ? -26.968 26.270  6.943   1.00 11.71  ? 170 LEU A CA  1 
ATOM   1378 C  C   . LEU A 1 175 ? -26.302 24.951  7.333   1.00 10.94  ? 170 LEU A C   1 
ATOM   1379 O  O   . LEU A 1 175 ? -26.544 24.412  8.414   1.00 13.83  ? 170 LEU A O   1 
ATOM   1380 C  CB  . LEU A 1 175 ? -28.127 25.993  6.001   1.00 12.72  ? 170 LEU A CB  1 
ATOM   1381 C  CG  . LEU A 1 175 ? -29.139 27.110  5.807   1.00 13.02  ? 170 LEU A CG  1 
ATOM   1382 C  CD1 . LEU A 1 175 ? -30.170 26.715  4.785   1.00 16.18  ? 170 LEU A CD1 1 
ATOM   1383 C  CD2 . LEU A 1 175 ? -29.830 27.465  7.075   1.00 15.85  ? 170 LEU A CD2 1 
ATOM   1384 N  N   . GLY A 1 176 ? -25.469 24.414  6.442   1.00 11.87  ? 171 GLY A N   1 
ATOM   1385 C  CA  . GLY A 1 176 ? -24.795 23.154  6.733   1.00 11.53  ? 171 GLY A CA  1 
ATOM   1386 C  C   . GLY A 1 176 ? -23.794 23.251  7.882   1.00 11.63  ? 171 GLY A C   1 
ATOM   1387 O  O   . GLY A 1 176 ? -23.658 22.324  8.685   1.00 12.35  ? 171 GLY A O   1 
ATOM   1388 N  N   . LEU A 1 177 ? -23.122 24.399  7.961   1.00 11.64  ? 172 LEU A N   1 
ATOM   1389 C  CA  . LEU A 1 177 ? -22.237 24.694  9.072   1.00 11.36  ? 172 LEU A CA  1 
ATOM   1390 C  C   . LEU A 1 177 ? -23.008 24.691  10.387  1.00 12.41  ? 172 LEU A C   1 
ATOM   1391 O  O   . LEU A 1 177 ? -22.591 24.058  11.348  1.00 12.21  ? 172 LEU A O   1 
ATOM   1392 C  CB  . LEU A 1 177 ? -21.555 26.047  8.854   1.00 10.11  ? 172 LEU A CB  1 
ATOM   1393 C  CG  . LEU A 1 177 ? -20.877 26.670  10.050  1.00 12.41  ? 172 LEU A CG  1 
ATOM   1394 C  CD1 . LEU A 1 177 ? -19.745 25.791  10.579  1.00 13.99  ? 172 LEU A CD1 1 
ATOM   1395 C  CD2 . LEU A 1 177 ? -20.372 28.018  9.709   1.00 14.82  ? 172 LEU A CD2 1 
ATOM   1396 N  N   . ALA A 1 178 ? -24.126 25.422  10.432  1.00 11.43  ? 173 ALA A N   1 
ATOM   1397 C  CA  . ALA A 1 178 ? -24.912 25.491  11.659  1.00 12.66  ? 173 ALA A CA  1 
ATOM   1398 C  C   . ALA A 1 178 ? -25.467 24.123  12.068  1.00 11.55  ? 173 ALA A C   1 
ATOM   1399 O  O   . ALA A 1 178 ? -25.464 23.767  13.243  1.00 11.91  ? 173 ALA A O   1 
ATOM   1400 C  CB  . ALA A 1 178 ? -26.031 26.516  11.513  1.00 13.61  ? 173 ALA A CB  1 
ATOM   1401 N  N   . LEU A 1 179 ? -25.955 23.341  11.096  1.00 10.71  ? 174 LEU A N   1 
ATOM   1402 C  CA  . LEU A 1 179 ? -26.362 21.968  11.359  1.00 11.26  ? 174 LEU A CA  1 
ATOM   1403 C  C   . LEU A 1 179 ? -25.239 21.185  12.043  1.00 11.48  ? 174 LEU A C   1 
ATOM   1404 O  O   . LEU A 1 179 ? -25.441 20.605  13.114  1.00 11.93  ? 174 LEU A O   1 
ATOM   1405 C  CB  . LEU A 1 179 ? -26.797 21.267  10.050  1.00 13.22  ? 174 LEU A CB  1 
ATOM   1406 C  CG  . LEU A 1 179 ? -27.198 19.777  10.143  1.00 12.81  ? 174 LEU A CG  1 
ATOM   1407 C  CD1 . LEU A 1 179 ? -28.391 19.592  11.013  1.00 16.19  ? 174 LEU A CD1 1 
ATOM   1408 C  CD2 . LEU A 1 179 ? -27.469 19.216  8.758   1.00 15.03  ? 174 LEU A CD2 1 
ATOM   1409 N  N   . ASN A 1 180 ? -24.054 21.173  11.430  1.00 10.47  ? 175 ASN A N   1 
ATOM   1410 C  CA  . ASN A 1 180 ? -22.962 20.378  11.976  1.00 11.03  ? 175 ASN A CA  1 
ATOM   1411 C  C   . ASN A 1 180 ? -22.459 20.895  13.325  1.00 10.93  ? 175 ASN A C   1 
ATOM   1412 O  O   . ASN A 1 180 ? -22.123 20.091  14.198  1.00 12.42  ? 175 ASN A O   1 
ATOM   1413 C  CB  . ASN A 1 180 ? -21.832 20.281  10.982  1.00 12.38  ? 175 ASN A CB  1 
ATOM   1414 C  CG  . ASN A 1 180 ? -22.161 19.354  9.843   1.00 12.40  ? 175 ASN A CG  1 
ATOM   1415 O  OD1 . ASN A 1 180 ? -23.305 18.943  9.636   1.00 11.98  ? 175 ASN A OD1 1 
ATOM   1416 N  ND2 . ASN A 1 180 ? -21.169 18.973  9.071   1.00 12.39  ? 175 ASN A ND2 1 
ATOM   1417 N  N   . PHE A 1 181 ? -22.434 22.225  13.517  1.00 10.03  ? 176 PHE A N   1 
ATOM   1418 C  CA  . PHE A 1 181 ? -22.087 22.770  14.822  1.00 10.77  ? 176 PHE A CA  1 
ATOM   1419 C  C   . PHE A 1 181 ? -23.103 22.377  15.899  1.00 10.62  ? 176 PHE A C   1 
ATOM   1420 O  O   . PHE A 1 181 ? -22.709 22.045  17.020  1.00 11.91  ? 176 PHE A O   1 
ATOM   1421 C  CB  . PHE A 1 181 ? -21.876 24.295  14.742  1.00 11.68  ? 176 PHE A CB  1 
ATOM   1422 C  CG  . PHE A 1 181 ? -21.101 24.993  15.848  1.00 11.99  ? 176 PHE A CG  1 
ATOM   1423 C  CD1 . PHE A 1 181 ? -20.297 24.279  16.725  1.00 12.23  ? 176 PHE A CD1 1 
ATOM   1424 C  CD2 . PHE A 1 181 ? -21.189 26.364  16.012  1.00 13.31  ? 176 PHE A CD2 1 
ATOM   1425 C  CE1 . PHE A 1 181 ? -19.580 24.933  17.726  1.00 13.30  ? 176 PHE A CE1 1 
ATOM   1426 C  CE2 . PHE A 1 181 ? -20.474 27.013  17.015  1.00 16.26  ? 176 PHE A CE2 1 
ATOM   1427 C  CZ  . PHE A 1 181 ? -19.666 26.291  17.861  1.00 14.08  ? 176 PHE A CZ  1 
ATOM   1428 N  N   . SER A 1 182 ? -24.399 22.333  15.546  1.00 12.22  ? 177 SER A N   1 
ATOM   1429 C  CA  . SER A 1 182 ? -25.420 21.870  16.483  1.00 10.53  ? 177 SER A CA  1 
ATOM   1430 C  C   . SER A 1 182 ? -25.195 20.395  16.835  1.00 11.69  ? 177 SER A C   1 
ATOM   1431 O  O   . SER A 1 182 ? -25.374 20.020  17.989  1.00 13.19  ? 177 SER A O   1 
ATOM   1432 C  CB  . SER A 1 182 ? -26.836 22.123  15.953  1.00 14.14  ? 177 SER A CB  1 
ATOM   1433 O  OG  . SER A 1 182 ? -27.177 21.272  14.865  1.00 13.96  ? 177 SER A OG  1 
ATOM   1434 N  N   . VAL A 1 183 ? -24.789 19.568  15.855  1.00 11.87  ? 178 VAL A N   1 
ATOM   1435 C  CA  . VAL A 1 183 ? -24.454 18.172  16.128  1.00 12.31  ? 178 VAL A CA  1 
ATOM   1436 C  C   . VAL A 1 183 ? -23.243 18.069  17.064  1.00 12.60  ? 178 VAL A C   1 
ATOM   1437 O  O   . VAL A 1 183 ? -23.259 17.289  18.014  1.00 14.32  ? 178 VAL A O   1 
ATOM   1438 C  CB  . VAL A 1 183 ? -24.227 17.372  14.816  1.00 13.08  ? 178 VAL A CB  1 
ATOM   1439 C  CG1 . VAL A 1 183 ? -23.639 15.977  15.092  1.00 13.93  ? 178 VAL A CG1 1 
ATOM   1440 C  CG2 . VAL A 1 183 ? -25.521 17.265  14.008  1.00 14.14  ? 178 VAL A CG2 1 
ATOM   1441 N  N   . PHE A 1 184 ? -22.212 18.889  16.824  1.00 12.33  ? 179 PHE A N   1 
ATOM   1442 C  CA  . PHE A 1 184 ? -21.079 18.979  17.734  1.00 11.59  ? 179 PHE A CA  1 
ATOM   1443 C  C   . PHE A 1 184 ? -21.551 19.215  19.170  1.00 12.31  ? 179 PHE A C   1 
ATOM   1444 O  O   . PHE A 1 184 ? -21.145 18.518  20.098  1.00 12.98  ? 179 PHE A O   1 
ATOM   1445 C  CB  . PHE A 1 184 ? -20.133 20.088  17.281  1.00 12.32  ? 179 PHE A CB  1 
ATOM   1446 C  CG  . PHE A 1 184 ? -19.071 20.446  18.293  1.00 11.94  ? 179 PHE A CG  1 
ATOM   1447 C  CD1 . PHE A 1 184 ? -17.925 19.683  18.421  1.00 13.12  ? 179 PHE A CD1 1 
ATOM   1448 C  CD2 . PHE A 1 184 ? -19.234 21.530  19.138  1.00 14.11  ? 179 PHE A CD2 1 
ATOM   1449 C  CE1 . PHE A 1 184 ? -16.953 20.011  19.355  1.00 13.43  ? 179 PHE A CE1 1 
ATOM   1450 C  CE2 . PHE A 1 184 ? -18.269 21.842  20.087  1.00 14.59  ? 179 PHE A CE2 1 
ATOM   1451 C  CZ  . PHE A 1 184 ? -17.126 21.085  20.179  1.00 16.10  ? 179 PHE A CZ  1 
ATOM   1452 N  N   . HIS A 1 185 ? -22.419 20.217  19.357  1.00 11.89  ? 180 HIS A N   1 
ATOM   1453 C  CA  . HIS A 1 185 ? -22.873 20.550  20.698  1.00 13.08  ? 180 HIS A CA  1 
ATOM   1454 C  C   . HIS A 1 185 ? -23.607 19.396  21.379  1.00 14.36  ? 180 HIS A C   1 
ATOM   1455 O  O   . HIS A 1 185 ? -23.418 19.142  22.573  1.00 14.19  ? 180 HIS A O   1 
ATOM   1456 C  CB  . HIS A 1 185 ? -23.784 21.812  20.688  1.00 13.42  ? 180 HIS A CB  1 
ATOM   1457 C  CG  . HIS A 1 185 ? -23.108 23.120  20.388  1.00 13.83  ? 180 HIS A CG  1 
ATOM   1458 N  ND1 . HIS A 1 185 ? -21.992 23.560  21.101  1.00 16.82  ? 180 HIS A ND1 1 
ATOM   1459 C  CD2 . HIS A 1 185 ? -23.435 24.066  19.472  1.00 14.90  ? 180 HIS A CD2 1 
ATOM   1460 C  CE1 . HIS A 1 185 ? -21.677 24.748  20.593  1.00 14.58  ? 180 HIS A CE1 1 
ATOM   1461 N  NE2 . HIS A 1 185 ? -22.523 25.094  19.604  1.00 14.56  ? 180 HIS A NE2 1 
ATOM   1462 N  N   . TYR A 1 186 ? -24.477 18.722  20.622  1.00 12.45  ? 181 TYR A N   1 
ATOM   1463 C  CA  . TYR A 1 186 ? -25.306 17.663  21.182  1.00 13.68  ? 181 TYR A CA  1 
ATOM   1464 C  C   . TYR A 1 186 ? -24.511 16.381  21.432  1.00 14.62  ? 181 TYR A C   1 
ATOM   1465 O  O   . TYR A 1 186 ? -24.608 15.774  22.500  1.00 15.37  ? 181 TYR A O   1 
ATOM   1466 C  CB  . TYR A 1 186 ? -26.498 17.366  20.250  1.00 15.85  ? 181 TYR A CB  1 
ATOM   1467 C  CG  . TYR A 1 186 ? -27.562 16.510  20.888  1.00 17.71  ? 181 TYR A CG  1 
ATOM   1468 C  CD1 . TYR A 1 186 ? -27.483 15.127  20.855  1.00 17.30  ? 181 TYR A CD1 1 
ATOM   1469 C  CD2 . TYR A 1 186 ? -28.631 17.085  21.562  1.00 17.94  ? 181 TYR A CD2 1 
ATOM   1470 C  CE1 . TYR A 1 186 ? -28.460 14.333  21.461  1.00 21.00  ? 181 TYR A CE1 1 
ATOM   1471 C  CE2 . TYR A 1 186 ? -29.605 16.302  22.177  1.00 20.49  ? 181 TYR A CE2 1 
ATOM   1472 C  CZ  . TYR A 1 186 ? -29.518 14.926  22.117  1.00 21.45  ? 181 TYR A CZ  1 
ATOM   1473 O  OH  . TYR A 1 186 ? -30.497 14.151  22.718  1.00 25.08  ? 181 TYR A OH  1 
ATOM   1474 N  N   . GLU A 1 187 ? -23.716 15.979  20.437  1.00 13.71  ? 182 GLU A N   1 
ATOM   1475 C  CA  . GLU A 1 187 ? -23.119 14.652  20.422  1.00 16.59  ? 182 GLU A CA  1 
ATOM   1476 C  C   . GLU A 1 187 ? -21.715 14.610  21.030  1.00 16.73  ? 182 GLU A C   1 
ATOM   1477 O  O   . GLU A 1 187 ? -21.304 13.563  21.528  1.00 20.92  ? 182 GLU A O   1 
ATOM   1478 C  CB  . GLU A 1 187 ? -23.093 14.115  18.976  1.00 15.96  ? 182 GLU A CB  1 
ATOM   1479 C  CG  . GLU A 1 187 ? -24.457 13.832  18.359  1.00 18.93  ? 182 GLU A CG  1 
ATOM   1480 C  CD  . GLU A 1 187 ? -25.207 12.609  18.879  1.00 21.35  ? 182 GLU A CD  1 
ATOM   1481 O  OE1 . GLU A 1 187 ? -24.634 11.872  19.715  1.00 27.64  ? 182 GLU A OE1 1 
ATOM   1482 O  OE2 . GLU A 1 187 ? -26.372 12.398  18.470  1.00 21.20  ? 182 GLU A OE2 1 
ATOM   1483 N  N   . ILE A 1 188 ? -20.987 15.738  21.006  1.00 15.35  ? 183 ILE A N   1 
ATOM   1484 C  CA  . ILE A 1 188 ? -19.598 15.782  21.452  1.00 14.48  ? 183 ILE A CA  1 
ATOM   1485 C  C   . ILE A 1 188 ? -19.370 16.592  22.724  1.00 17.12  ? 183 ILE A C   1 
ATOM   1486 O  O   . ILE A 1 188 ? -18.628 16.165  23.610  1.00 17.08  ? 183 ILE A O   1 
ATOM   1487 C  CB  . ILE A 1 188 ? -18.682 16.374  20.349  1.00 14.95  ? 183 ILE A CB  1 
ATOM   1488 C  CG1 . ILE A 1 188 ? -18.862 15.682  19.000  1.00 18.98  ? 183 ILE A CG1 1 
ATOM   1489 C  CG2 . ILE A 1 188 ? -17.207 16.366  20.784  1.00 15.50  ? 183 ILE A CG2 1 
ATOM   1490 C  CD1 . ILE A 1 188 ? -18.529 14.220  18.984  1.00 19.64  ? 183 ILE A CD1 1 
ATOM   1491 N  N   . ALA A 1 189 ? -19.981 17.786  22.784  1.00 15.47  ? 184 ALA A N   1 
ATOM   1492 C  CA  . ALA A 1 189 ? -19.686 18.755  23.832  1.00 14.64  ? 184 ALA A CA  1 
ATOM   1493 C  C   . ALA A 1 189 ? -20.607 18.671  25.050  1.00 14.74  ? 184 ALA A C   1 
ATOM   1494 O  O   . ALA A 1 189 ? -20.501 19.501  25.946  1.00 20.69  ? 184 ALA A O   1 
ATOM   1495 C  CB  . ALA A 1 189 ? -19.749 20.163  23.252  1.00 17.10  ? 184 ALA A CB  1 
ATOM   1496 N  N   . ASN A 1 190 ? -21.524 17.701  25.061  1.00 15.06  ? 185 ASN A N   1 
ATOM   1497 C  CA  . ASN A 1 190 ? -22.478 17.541  26.153  1.00 19.13  ? 185 ASN A CA  1 
ATOM   1498 C  C   . ASN A 1 190 ? -23.264 18.827  26.421  1.00 19.93  ? 185 ASN A C   1 
ATOM   1499 O  O   . ASN A 1 190 ? -23.479 19.207  27.575  1.00 19.33  ? 185 ASN A O   1 
ATOM   1500 C  CB  . ASN A 1 190 ? -21.762 17.086  27.446  1.00 20.54  ? 185 ASN A CB  1 
ATOM   1501 C  CG  . ASN A 1 190 ? -22.717 16.560  28.495  1.00 25.95  ? 185 ASN A CG  1 
ATOM   1502 O  OD1 . ASN A 1 190 ? -23.795 16.049  28.186  1.00 28.46  ? 185 ASN A OD1 1 
ATOM   1503 N  ND2 . ASN A 1 190 ? -22.341 16.652  29.758  1.00 27.56  ? 185 ASN A ND2 1 
ATOM   1504 N  N   . SER A 1 191 ? -23.685 19.496  25.340  1.00 15.28  ? 186 SER A N   1 
ATOM   1505 C  CA  . SER A 1 191 ? -24.406 20.759  25.438  1.00 14.33  ? 186 SER A CA  1 
ATOM   1506 C  C   . SER A 1 191 ? -25.706 20.700  24.643  1.00 13.99  ? 186 SER A C   1 
ATOM   1507 O  O   . SER A 1 191 ? -25.858 21.443  23.669  1.00 14.97  ? 186 SER A O   1 
ATOM   1508 C  CB  . SER A 1 191 ? -23.542 21.914  24.929  1.00 15.62  ? 186 SER A CB  1 
ATOM   1509 O  OG  . SER A 1 191 ? -22.325 22.036  25.646  1.00 18.08  ? 186 SER A OG  1 
ATOM   1510 N  N   . PRO A 1 192 ? -26.680 19.832  25.016  1.00 15.28  ? 187 PRO A N   1 
ATOM   1511 C  CA  . PRO A 1 192 ? -27.904 19.697  24.222  1.00 14.45  ? 187 PRO A CA  1 
ATOM   1512 C  C   . PRO A 1 192 ? -28.701 20.997  24.118  1.00 15.44  ? 187 PRO A C   1 
ATOM   1513 O  O   . PRO A 1 192 ? -29.304 21.271  23.085  1.00 15.32  ? 187 PRO A O   1 
ATOM   1514 C  CB  . PRO A 1 192 ? -28.687 18.599  24.945  1.00 15.99  ? 187 PRO A CB  1 
ATOM   1515 C  CG  . PRO A 1 192 ? -28.074 18.539  26.350  1.00 17.22  ? 187 PRO A CG  1 
ATOM   1516 C  CD  . PRO A 1 192 ? -26.647 18.929  26.184  1.00 16.46  ? 187 PRO A CD  1 
ATOM   1517 N  N   . GLU A 1 193 ? -28.714 21.807  25.179  1.00 14.77  ? 188 GLU A N   1 
ATOM   1518 C  CA  . GLU A 1 193 ? -29.445 23.063  25.128  1.00 15.77  ? 188 GLU A CA  1 
ATOM   1519 C  C   . GLU A 1 193 ? -28.863 24.045  24.108  1.00 15.45  ? 188 GLU A C   1 
ATOM   1520 O  O   . GLU A 1 193 ? -29.623 24.703  23.391  1.00 15.14  ? 188 GLU A O   1 
ATOM   1521 C  CB  . GLU A 1 193 ? -29.524 23.696  26.519  1.00 15.77  ? 188 GLU A CB  1 
ATOM   1522 C  CG  . GLU A 1 193 ? -30.527 22.984  27.405  1.00 17.46  ? 188 GLU A CG  1 
ATOM   1523 C  CD  . GLU A 1 193 ? -30.573 23.412  28.859  1.00 18.88  ? 188 GLU A CD  1 
ATOM   1524 O  OE1 . GLU A 1 193 ? -29.595 24.010  29.364  1.00 19.99  ? 188 GLU A OE1 1 
ATOM   1525 O  OE2 . GLU A 1 193 ? -31.618 23.143  29.497  1.00 23.86  ? 188 GLU A OE2 1 
ATOM   1526 N  N   . GLU A 1 194 ? -27.526 24.117  24.017  1.00 15.28  ? 189 GLU A N   1 
ATOM   1527 C  CA  . GLU A 1 194 ? -26.870 24.937  23.006  1.00 13.88  ? 189 GLU A CA  1 
ATOM   1528 C  C   . GLU A 1 194 ? -27.219 24.430  21.609  1.00 14.19  ? 189 GLU A C   1 
ATOM   1529 O  O   . GLU A 1 194 ? -27.481 25.227  20.708  1.00 15.04  ? 189 GLU A O   1 
ATOM   1530 C  CB  . GLU A 1 194 ? -25.353 24.946  23.203  1.00 13.47  ? 189 GLU A CB  1 
ATOM   1531 C  CG  . GLU A 1 194 ? -24.612 25.961  22.351  1.00 14.70  ? 189 GLU A CG  1 
ATOM   1532 C  CD  . GLU A 1 194 ? -24.824 27.431  22.710  1.00 18.60  ? 189 GLU A CD  1 
ATOM   1533 O  OE1 . GLU A 1 194 ? -25.368 27.721  23.800  1.00 17.84  ? 189 GLU A OE1 1 
ATOM   1534 O  OE2 . GLU A 1 194 ? -24.455 28.291  21.880  1.00 19.78  ? 189 GLU A OE2 1 
ATOM   1535 N  N   . ALA A 1 195 ? -27.223 23.100  21.449  1.00 12.52  ? 190 ALA A N   1 
ATOM   1536 C  CA  . ALA A 1 195 ? -27.593 22.465  20.189  1.00 12.73  ? 190 ALA A CA  1 
ATOM   1537 C  C   . ALA A 1 195 ? -28.997 22.844  19.726  1.00 15.51  ? 190 ALA A C   1 
ATOM   1538 O  O   . ALA A 1 195 ? -29.197 23.225  18.572  1.00 14.28  ? 190 ALA A O   1 
ATOM   1539 C  CB  . ALA A 1 195 ? -27.490 20.955  20.297  1.00 12.56  ? 190 ALA A CB  1 
ATOM   1540 N  N   . ILE A 1 196 ? -29.967 22.717  20.641  1.00 13.41  ? 191 ILE A N   1 
ATOM   1541 C  CA  . ILE A 1 196 ? -31.356 23.030  20.342  1.00 14.68  ? 191 ILE A CA  1 
ATOM   1542 C  C   . ILE A 1 196 ? -31.522 24.511  19.997  1.00 13.75  ? 191 ILE A C   1 
ATOM   1543 O  O   . ILE A 1 196 ? -32.198 24.864  19.030  1.00 14.80  ? 191 ILE A O   1 
ATOM   1544 C  CB  . ILE A 1 196 ? -32.242 22.589  21.537  1.00 16.20  ? 191 ILE A CB  1 
ATOM   1545 C  CG1 . ILE A 1 196 ? -32.275 21.047  21.688  1.00 15.98  ? 191 ILE A CG1 1 
ATOM   1546 C  CG2 . ILE A 1 196 ? -33.642 23.146  21.404  1.00 16.69  ? 191 ILE A CG2 1 
ATOM   1547 C  CD1 . ILE A 1 196 ? -32.743 20.548  23.048  1.00 16.83  ? 191 ILE A CD1 1 
ATOM   1548 N  N   . SER A 1 197 ? -30.886 25.372  20.788  1.00 13.72  ? 192 SER A N   1 
ATOM   1549 C  CA  . SER A 1 197 ? -30.983 26.806  20.576  1.00 13.78  ? 192 SER A CA  1 
ATOM   1550 C  C   . SER A 1 197 ? -30.448 27.203  19.204  1.00 14.86  ? 192 SER A C   1 
ATOM   1551 O  O   . SER A 1 197 ? -31.076 27.976  18.474  1.00 15.87  ? 192 SER A O   1 
ATOM   1552 C  CB  . SER A 1 197 ? -30.261 27.559  21.681  1.00 16.54  ? 192 SER A CB  1 
ATOM   1553 O  OG  . SER A 1 197 ? -30.424 28.962  21.512  1.00 22.40  ? 192 SER A OG  1 
ATOM   1554 N  N   . LEU A 1 198 ? -29.277 26.666  18.846  1.00 14.36  ? 193 LEU A N   1 
ATOM   1555 C  CA  . LEU A 1 198 ? -28.686 26.965  17.553  1.00 13.66  ? 193 LEU A CA  1 
ATOM   1556 C  C   . LEU A 1 198 ? -29.570 26.464  16.412  1.00 14.74  ? 193 LEU A C   1 
ATOM   1557 O  O   . LEU A 1 198 ? -29.794 27.193  15.445  1.00 13.88  ? 193 LEU A O   1 
ATOM   1558 C  CB  . LEU A 1 198 ? -27.276 26.366  17.468  1.00 12.89  ? 193 LEU A CB  1 
ATOM   1559 C  CG  . LEU A 1 198 ? -26.547 26.547  16.135  1.00 13.57  ? 193 LEU A CG  1 
ATOM   1560 C  CD1 . LEU A 1 198 ? -26.472 28.004  15.732  1.00 15.35  ? 193 LEU A CD1 1 
ATOM   1561 C  CD2 . LEU A 1 198 ? -25.131 25.962  16.215  1.00 15.37  ? 193 LEU A CD2 1 
ATOM   1562 N  N   . ALA A 1 199 ? -30.049 25.217  16.515  1.00 13.21  ? 194 ALA A N   1 
ATOM   1563 C  CA  . ALA A 1 199 ? -30.906 24.651  15.478  1.00 13.95  ? 194 ALA A CA  1 
ATOM   1564 C  C   . ALA A 1 199 ? -32.175 25.478  15.259  1.00 15.54  ? 194 ALA A C   1 
ATOM   1565 O  O   . ALA A 1 199 ? -32.551 25.744  14.118  1.00 14.48  ? 194 ALA A O   1 
ATOM   1566 C  CB  . ALA A 1 199 ? -31.267 23.204  15.799  1.00 16.56  ? 194 ALA A CB  1 
ATOM   1567 N  N   . LYS A 1 200 ? -32.829 25.867  16.362  1.00 13.48  ? 195 LYS A N   1 
ATOM   1568 C  CA  . LYS A 1 200 ? -34.045 26.667  16.313  1.00 15.23  ? 195 LYS A CA  1 
ATOM   1569 C  C   . LYS A 1 200 ? -33.827 28.047  15.689  1.00 14.62  ? 195 LYS A C   1 
ATOM   1570 O  O   . LYS A 1 200 ? -34.564 28.442  14.782  1.00 15.31  ? 195 LYS A O   1 
ATOM   1571 C  CB  . LYS A 1 200 ? -34.636 26.834  17.725  1.00 16.85  ? 195 LYS A CB  1 
ATOM   1572 C  CG  . LYS A 1 200 ? -35.431 25.668  18.246  1.00 24.80  ? 195 LYS A CG  1 
ATOM   1573 C  CD  . LYS A 1 200 ? -35.964 25.964  19.657  1.00 36.11  ? 195 LYS A CD  1 
ATOM   1574 C  CE  . LYS A 1 200 ? -36.883 24.896  20.183  1.00 41.28  ? 195 LYS A CE  1 
ATOM   1575 N  NZ  . LYS A 1 200 ? -37.225 25.129  21.609  1.00 50.91  ? 195 LYS A NZ  1 
ATOM   1576 N  N   . THR A 1 201 ? -32.830 28.793  16.177  1.00 13.96  ? 196 THR A N   1 
ATOM   1577 C  CA  A THR A 1 201 ? -32.543 30.119  15.655  0.50 14.58  ? 196 THR A CA  1 
ATOM   1578 C  CA  B THR A 1 201 ? -32.558 30.121  15.647  0.50 15.75  ? 196 THR A CA  1 
ATOM   1579 C  C   . THR A 1 201 ? -32.172 30.055  14.172  1.00 15.56  ? 196 THR A C   1 
ATOM   1580 O  O   . THR A 1 201 ? -32.618 30.883  13.376  1.00 15.35  ? 196 THR A O   1 
ATOM   1581 C  CB  A THR A 1 201 ? -31.457 30.786  16.510  0.50 14.78  ? 196 THR A CB  1 
ATOM   1582 C  CB  B THR A 1 201 ? -31.476 30.868  16.431  0.50 17.47  ? 196 THR A CB  1 
ATOM   1583 O  OG1 A THR A 1 201 ? -31.970 31.005  17.835  0.50 16.43  ? 196 THR A OG1 1 
ATOM   1584 O  OG1 B THR A 1 201 ? -30.353 30.008  16.643  0.50 23.55  ? 196 THR A OG1 1 
ATOM   1585 C  CG2 A THR A 1 201 ? -30.987 32.111  15.929  0.50 12.53  ? 196 THR A CG2 1 
ATOM   1586 C  CG2 B THR A 1 201 ? -31.997 31.398  17.757  0.50 14.90  ? 196 THR A CG2 1 
ATOM   1587 N  N   . THR A 1 202 ? -31.340 29.072  13.804  1.00 14.56  ? 197 THR A N   1 
ATOM   1588 C  CA  . THR A 1 202 ? -30.956 28.902  12.407  1.00 12.63  ? 197 THR A CA  1 
ATOM   1589 C  C   . THR A 1 202 ? -32.174 28.682  11.514  1.00 14.93  ? 197 THR A C   1 
ATOM   1590 O  O   . THR A 1 202 ? -32.298 29.291  10.447  1.00 14.19  ? 197 THR A O   1 
ATOM   1591 C  CB  . THR A 1 202 ? -29.966 27.733  12.268  1.00 12.26  ? 197 THR A CB  1 
ATOM   1592 O  OG1 . THR A 1 202 ? -28.819 27.976  13.105  1.00 13.95  ? 197 THR A OG1 1 
ATOM   1593 C  CG2 . THR A 1 202 ? -29.497 27.528  10.814  1.00 12.55  ? 197 THR A CG2 1 
ATOM   1594 N  N   . PHE A 1 203 ? -33.065 27.798  11.964  1.00 12.52  ? 198 PHE A N   1 
ATOM   1595 C  CA  . PHE A 1 203 ? -34.253 27.449  11.199  1.00 13.26  ? 198 PHE A CA  1 
ATOM   1596 C  C   . PHE A 1 203 ? -35.141 28.674  11.002  1.00 16.39  ? 198 PHE A C   1 
ATOM   1597 O  O   . PHE A 1 203 ? -35.548 28.980  9.881   1.00 14.72  ? 198 PHE A O   1 
ATOM   1598 C  CB  . PHE A 1 203 ? -35.012 26.318  11.893  1.00 16.04  ? 198 PHE A CB  1 
ATOM   1599 C  CG  . PHE A 1 203 ? -36.237 25.859  11.136  1.00 17.19  ? 198 PHE A CG  1 
ATOM   1600 C  CD1 . PHE A 1 203 ? -37.443 26.536  11.253  1.00 17.48  ? 198 PHE A CD1 1 
ATOM   1601 C  CD2 . PHE A 1 203 ? -36.177 24.774  10.285  1.00 17.80  ? 198 PHE A CD2 1 
ATOM   1602 C  CE1 . PHE A 1 203 ? -38.563 26.116  10.552  1.00 19.03  ? 198 PHE A CE1 1 
ATOM   1603 C  CE2 . PHE A 1 203 ? -37.302 24.356  9.588   1.00 19.44  ? 198 PHE A CE2 1 
ATOM   1604 C  CZ  . PHE A 1 203 ? -38.488 25.025  9.727   1.00 20.14  ? 198 PHE A CZ  1 
ATOM   1605 N  N   . ASP A 1 204 ? -35.409 29.385  12.096  1.00 15.80  ? 199 ASP A N   1 
ATOM   1606 C  CA  . ASP A 1 204 ? -36.321 30.516  12.060  1.00 19.53  ? 199 ASP A CA  1 
ATOM   1607 C  C   . ASP A 1 204 ? -35.785 31.650  11.182  1.00 16.53  ? 199 ASP A C   1 
ATOM   1608 O  O   . ASP A 1 204 ? -36.534 32.243  10.412  1.00 17.68  ? 199 ASP A O   1 
ATOM   1609 C  CB  . ASP A 1 204 ? -36.644 30.954  13.504  1.00 19.17  ? 199 ASP A CB  1 
ATOM   1610 C  CG  . ASP A 1 204 ? -37.498 29.956  14.274  1.00 22.74  ? 199 ASP A CG  1 
ATOM   1611 O  OD1 . ASP A 1 204 ? -38.099 29.066  13.635  1.00 35.41  ? 199 ASP A OD1 1 
ATOM   1612 O  OD2 . ASP A 1 204 ? -37.555 30.057  15.513  1.00 30.05  ? 199 ASP A OD2 1 
ATOM   1613 N  N   . GLU A 1 205 ? -34.480 31.931  11.243  1.00 14.75  ? 200 GLU A N   1 
ATOM   1614 C  CA  . GLU A 1 205 ? -33.906 33.003  10.443  1.00 14.41  ? 200 GLU A CA  1 
ATOM   1615 C  C   . GLU A 1 205 ? -33.861 32.626  8.962   1.00 16.79  ? 200 GLU A C   1 
ATOM   1616 O  O   . GLU A 1 205 ? -34.036 33.482  8.100   1.00 15.89  ? 200 GLU A O   1 
ATOM   1617 C  CB  . GLU A 1 205 ? -32.523 33.400  10.987  1.00 17.54  ? 200 GLU A CB  1 
ATOM   1618 C  CG  . GLU A 1 205 ? -32.634 34.030  12.365  1.00 27.51  ? 200 GLU A CG  1 
ATOM   1619 C  CD  . GLU A 1 205 ? -31.340 34.381  13.073  1.00 42.49  ? 200 GLU A CD  1 
ATOM   1620 O  OE1 . GLU A 1 205 ? -30.258 34.319  12.443  1.00 35.68  ? 200 GLU A OE1 1 
ATOM   1621 O  OE2 . GLU A 1 205 ? -31.417 34.715  14.278  1.00 50.07  ? 200 GLU A OE2 1 
ATOM   1622 N  N   . ALA A 1 206 ? -33.675 31.339  8.657   1.00 15.01  ? 201 ALA A N   1 
ATOM   1623 C  CA  . ALA A 1 206 ? -33.748 30.903  7.270   1.00 13.06  ? 201 ALA A CA  1 
ATOM   1624 C  C   . ALA A 1 206 ? -35.183 31.019  6.741   1.00 14.44  ? 201 ALA A C   1 
ATOM   1625 O  O   . ALA A 1 206 ? -35.419 31.526  5.642   1.00 15.74  ? 201 ALA A O   1 
ATOM   1626 C  CB  . ALA A 1 206 ? -33.222 29.475  7.118   1.00 14.90  ? 201 ALA A CB  1 
ATOM   1627 N  N   . MET A 1 207 ? -36.151 30.560  7.538   1.00 13.80  ? 202 MET A N   1 
ATOM   1628 C  CA  . MET A 1 207 ? -37.555 30.625  7.158   1.00 14.41  ? 202 MET A CA  1 
ATOM   1629 C  C   . MET A 1 207 ? -37.923 32.034  6.697   1.00 14.04  ? 202 MET A C   1 
ATOM   1630 O  O   . MET A 1 207 ? -38.589 32.208  5.672   1.00 14.04  ? 202 MET A O   1 
ATOM   1631 C  CB  . MET A 1 207 ? -38.427 30.210  8.363   1.00 19.53  ? 202 MET A CB  1 
ATOM   1632 C  CG  . MET A 1 207 ? -39.919 30.218  8.114   1.00 29.83  ? 202 MET A CG  1 
ATOM   1633 S  SD  . MET A 1 207 ? -40.477 29.059  6.836   1.00 39.96  ? 202 MET A SD  1 
ATOM   1634 C  CE  . MET A 1 207 ? -39.654 27.690  7.319   1.00 19.20  ? 202 MET A CE  1 
ATOM   1635 N  N   . ALA A 1 208 ? -37.458 33.036  7.450   1.00 15.24  ? 203 ALA A N   1 
ATOM   1636 C  CA  . ALA A 1 208 ? -37.793 34.426  7.187   1.00 13.89  ? 203 ALA A CA  1 
ATOM   1637 C  C   . ALA A 1 208 ? -37.118 35.024  5.955   1.00 17.46  ? 203 ALA A C   1 
ATOM   1638 O  O   . ALA A 1 208 ? -37.499 36.110  5.521   1.00 16.39  ? 203 ALA A O   1 
ATOM   1639 C  CB  . ALA A 1 208 ? -37.461 35.274  8.412   1.00 19.68  ? 203 ALA A CB  1 
ATOM   1640 N  N   . ASP A 1 209 ? -36.132 34.317  5.383   1.00 14.54  ? 204 ASP A N   1 
ATOM   1641 C  CA  . ASP A 1 209 ? -35.403 34.801  4.216   1.00 17.11  ? 204 ASP A CA  1 
ATOM   1642 C  C   . ASP A 1 209 ? -35.732 34.037  2.928   1.00 15.15  ? 204 ASP A C   1 
ATOM   1643 O  O   . ASP A 1 209 ? -35.264 34.399  1.844   1.00 16.77  ? 204 ASP A O   1 
ATOM   1644 C  CB  . ASP A 1 209 ? -33.889 34.728  4.534   1.00 20.75  ? 204 ASP A CB  1 
ATOM   1645 C  CG  . ASP A 1 209 ? -32.933 35.337  3.518   1.00 22.62  ? 204 ASP A CG  1 
ATOM   1646 O  OD1 . ASP A 1 209 ? -33.023 36.564  3.278   1.00 25.51  ? 204 ASP A OD1 1 
ATOM   1647 O  OD2 . ASP A 1 209 ? -32.047 34.586  2.998   1.00 24.74  ? 204 ASP A OD2 1 
ATOM   1648 N  N   . LEU A 1 210 ? -36.554 32.984  3.037   1.00 13.86  ? 205 LEU A N   1 
ATOM   1649 C  CA  . LEU A 1 210 ? -36.918 32.155  1.896   1.00 16.82  ? 205 LEU A CA  1 
ATOM   1650 C  C   . LEU A 1 210 ? -37.591 32.932  0.765   1.00 18.73  ? 205 LEU A C   1 
ATOM   1651 O  O   . LEU A 1 210 ? -37.427 32.572  -0.396  1.00 16.94  ? 205 LEU A O   1 
ATOM   1652 C  CB  . LEU A 1 210 ? -37.850 31.017  2.331   1.00 15.70  ? 205 LEU A CB  1 
ATOM   1653 C  CG  . LEU A 1 210 ? -37.198 29.891  3.128   1.00 17.70  ? 205 LEU A CG  1 
ATOM   1654 C  CD1 . LEU A 1 210 ? -38.237 28.915  3.587   1.00 18.12  ? 205 LEU A CD1 1 
ATOM   1655 C  CD2 . LEU A 1 210 ? -36.115 29.186  2.296   1.00 17.33  ? 205 LEU A CD2 1 
ATOM   1656 N  N   . HIS A 1 211 ? -38.327 33.996  1.106   1.00 16.39  ? 206 HIS A N   1 
ATOM   1657 C  CA  . HIS A 1 211 ? -39.053 34.780  0.114   1.00 18.45  ? 206 HIS A CA  1 
ATOM   1658 C  C   . HIS A 1 211 ? -38.148 35.452  -0.922  1.00 21.56  ? 206 HIS A C   1 
ATOM   1659 O  O   . HIS A 1 211 ? -38.616 35.814  -1.999  1.00 20.64  ? 206 HIS A O   1 
ATOM   1660 C  CB  . HIS A 1 211 ? -39.931 35.842  0.816   1.00 18.29  ? 206 HIS A CB  1 
ATOM   1661 C  CG  . HIS A 1 211 ? -39.173 37.020  1.350   1.00 17.79  ? 206 HIS A CG  1 
ATOM   1662 N  ND1 . HIS A 1 211 ? -38.596 37.006  2.607   1.00 19.61  ? 206 HIS A ND1 1 
ATOM   1663 C  CD2 . HIS A 1 211 ? -38.930 38.216  0.778   1.00 17.67  ? 206 HIS A CD2 1 
ATOM   1664 C  CE1 . HIS A 1 211 ? -38.011 38.188  2.750   1.00 21.12  ? 206 HIS A CE1 1 
ATOM   1665 N  NE2 . HIS A 1 211 ? -38.190 38.942  1.670   1.00 24.03  ? 206 HIS A NE2 1 
ATOM   1666 N  N   . THR A 1 212 ? -36.858 35.626  -0.592  1.00 18.59  ? 207 THR A N   1 
ATOM   1667 C  CA  . THR A 1 212 ? -35.902 36.270  -1.485  1.00 18.25  ? 207 THR A CA  1 
ATOM   1668 C  C   . THR A 1 212 ? -35.337 35.365  -2.577  1.00 17.86  ? 207 THR A C   1 
ATOM   1669 O  O   . THR A 1 212 ? -34.645 35.852  -3.469  1.00 20.12  ? 207 THR A O   1 
ATOM   1670 C  CB  . THR A 1 212 ? -34.710 36.820  -0.687  1.00 18.11  ? 207 THR A CB  1 
ATOM   1671 O  OG1 . THR A 1 212 ? -33.984 35.711  -0.126  1.00 18.03  ? 207 THR A OG1 1 
ATOM   1672 C  CG2 . THR A 1 212 ? -35.130 37.805  0.410   1.00 18.21  ? 207 THR A CG2 1 
ATOM   1673 N  N   . LEU A 1 213 ? -35.629 34.062  -2.490  1.00 17.51  ? 208 LEU A N   1 
ATOM   1674 C  CA  . LEU A 1 213 ? -34.972 33.045  -3.295  1.00 17.12  ? 208 LEU A CA  1 
ATOM   1675 C  C   . LEU A 1 213 ? -35.737 32.650  -4.556  1.00 21.53  ? 208 LEU A C   1 
ATOM   1676 O  O   . LEU A 1 213 ? -36.961 32.728  -4.602  1.00 19.72  ? 208 LEU A O   1 
ATOM   1677 C  CB  . LEU A 1 213 ? -34.789 31.789  -2.455  1.00 19.36  ? 208 LEU A CB  1 
ATOM   1678 C  CG  . LEU A 1 213 ? -33.971 31.976  -1.180  1.00 17.74  ? 208 LEU A CG  1 
ATOM   1679 C  CD1 . LEU A 1 213 ? -33.719 30.654  -0.503  1.00 17.63  ? 208 LEU A CD1 1 
ATOM   1680 C  CD2 . LEU A 1 213 ? -32.648 32.668  -1.450  1.00 20.01  ? 208 LEU A CD2 1 
ATOM   1681 N  N   . SER A 1 214 ? -34.984 32.200  -5.567  1.00 20.72  ? 209 SER A N   1 
ATOM   1682 C  CA  . SER A 1 214 ? -35.553 31.502  -6.708  1.00 21.71  ? 209 SER A CA  1 
ATOM   1683 C  C   . SER A 1 214 ? -36.061 30.115  -6.330  1.00 24.58  ? 209 SER A C   1 
ATOM   1684 O  O   . SER A 1 214 ? -35.767 29.612  -5.247  1.00 21.88  ? 209 SER A O   1 
ATOM   1685 C  CB  . SER A 1 214 ? -34.497 31.340  -7.796  1.00 19.73  ? 209 SER A CB  1 
ATOM   1686 O  OG  . SER A 1 214 ? -33.472 30.470  -7.324  1.00 21.33  ? 209 SER A OG  1 
ATOM   1687 N  N   . GLU A 1 215 ? -36.787 29.479  -7.257  1.00 22.41  ? 210 GLU A N   1 
ATOM   1688 C  CA  . GLU A 1 215 ? -37.276 28.128  -7.040  1.00 23.45  ? 210 GLU A CA  1 
ATOM   1689 C  C   . GLU A 1 215 ? -36.153 27.137  -6.730  1.00 26.78  ? 210 GLU A C   1 
ATOM   1690 O  O   . GLU A 1 215 ? -36.280 26.337  -5.807  1.00 25.10  ? 210 GLU A O   1 
ATOM   1691 C  CB  . GLU A 1 215 ? -38.074 27.651  -8.261  1.00 27.63  ? 210 GLU A CB  1 
ATOM   1692 C  CG  . GLU A 1 215 ? -38.668 26.262  -8.087  1.00 35.03  ? 210 GLU A CG  1 
ATOM   1693 C  CD  . GLU A 1 215 ? -39.594 25.831  -9.207  1.00 49.20  ? 210 GLU A CD  1 
ATOM   1694 O  OE1 . GLU A 1 215 ? -39.735 26.587  -10.196 1.00 51.89  ? 210 GLU A OE1 1 
ATOM   1695 O  OE2 . GLU A 1 215 ? -40.188 24.735  -9.088  1.00 61.80  ? 210 GLU A OE2 1 
ATOM   1696 N  N   . ASP A 1 216 ? -35.055 27.194  -7.495  1.00 25.10  ? 211 ASP A N   1 
ATOM   1697 C  CA  . ASP A 1 216 ? -33.957 26.260  -7.294  1.00 24.67  ? 211 ASP A CA  1 
ATOM   1698 C  C   . ASP A 1 216 ? -33.237 26.478  -5.962  1.00 21.18  ? 211 ASP A C   1 
ATOM   1699 O  O   . ASP A 1 216 ? -32.920 25.509  -5.273  1.00 23.86  ? 211 ASP A O   1 
ATOM   1700 C  CB  . ASP A 1 216 ? -32.959 26.336  -8.458  1.00 27.93  ? 211 ASP A CB  1 
ATOM   1701 C  CG  . ASP A 1 216 ? -33.448 25.692  -9.752  1.00 37.38  ? 211 ASP A CG  1 
ATOM   1702 O  OD1 . ASP A 1 216 ? -34.631 25.281  -9.808  1.00 32.09  ? 211 ASP A OD1 1 
ATOM   1703 O  OD2 . ASP A 1 216 ? -32.644 25.589  -10.702 1.00 50.26  ? 211 ASP A OD2 1 
ATOM   1704 N  N   . SER A 1 217 ? -32.985 27.743  -5.601  1.00 21.07  ? 212 SER A N   1 
ATOM   1705 C  CA  . SER A 1 217 ? -32.317 28.050  -4.344  1.00 20.22  ? 212 SER A CA  1 
ATOM   1706 C  C   . SER A 1 217 ? -33.201 27.690  -3.148  1.00 22.18  ? 212 SER A C   1 
ATOM   1707 O  O   . SER A 1 217 ? -32.720 27.195  -2.128  1.00 20.23  ? 212 SER A O   1 
ATOM   1708 C  CB  . SER A 1 217 ? -31.909 29.513  -4.291  1.00 21.14  ? 212 SER A CB  1 
ATOM   1709 O  OG  . SER A 1 217 ? -30.946 29.838  -5.286  1.00 21.53  ? 212 SER A OG  1 
ATOM   1710 N  N   . TYR A 1 218 ? -34.508 27.923  -3.296  1.00 20.38  ? 213 TYR A N   1 
ATOM   1711 C  CA  . TYR A 1 218 ? -35.480 27.512  -2.293  1.00 17.92  ? 213 TYR A CA  1 
ATOM   1712 C  C   . TYR A 1 218 ? -35.397 26.016  -1.999  1.00 19.78  ? 213 TYR A C   1 
ATOM   1713 O  O   . TYR A 1 218 ? -35.413 25.606  -0.836  1.00 18.96  ? 213 TYR A O   1 
ATOM   1714 C  CB  . TYR A 1 218 ? -36.877 27.909  -2.769  1.00 17.48  ? 213 TYR A CB  1 
ATOM   1715 C  CG  . TYR A 1 218 ? -38.019 27.559  -1.844  1.00 17.81  ? 213 TYR A CG  1 
ATOM   1716 C  CD1 . TYR A 1 218 ? -38.637 26.312  -1.902  1.00 25.31  ? 213 TYR A CD1 1 
ATOM   1717 C  CD2 . TYR A 1 218 ? -38.520 28.490  -0.955  1.00 20.33  ? 213 TYR A CD2 1 
ATOM   1718 C  CE1 . TYR A 1 218 ? -39.713 26.000  -1.073  1.00 28.29  ? 213 TYR A CE1 1 
ATOM   1719 C  CE2 . TYR A 1 218 ? -39.592 28.192  -0.123  1.00 29.50  ? 213 TYR A CE2 1 
ATOM   1720 C  CZ  . TYR A 1 218 ? -40.182 26.947  -0.183  1.00 23.06  ? 213 TYR A CZ  1 
ATOM   1721 O  OH  . TYR A 1 218 ? -41.235 26.690  0.662   1.00 32.35  ? 213 TYR A OH  1 
ATOM   1722 N  N   . LYS A 1 219 ? -35.306 25.196  -3.055  1.00 21.05  ? 214 LYS A N   1 
ATOM   1723 C  CA  . LYS A 1 219 ? -35.222 23.756  -2.873  1.00 21.68  ? 214 LYS A CA  1 
ATOM   1724 C  C   . LYS A 1 219 ? -33.961 23.386  -2.099  1.00 21.89  ? 214 LYS A C   1 
ATOM   1725 O  O   . LYS A 1 219 ? -34.008 22.551  -1.199  1.00 23.63  ? 214 LYS A O   1 
ATOM   1726 C  CB  . LYS A 1 219 ? -35.248 23.012  -4.223  1.00 31.52  ? 214 LYS A CB  1 
ATOM   1727 C  CG  . LYS A 1 219 ? -36.587 23.065  -4.963  1.00 46.58  ? 214 LYS A CG  1 
ATOM   1728 C  CD  . LYS A 1 219 ? -37.799 22.704  -4.105  1.00 60.44  ? 214 LYS A CD  1 
ATOM   1729 C  CE  . LYS A 1 219 ? -39.072 22.628  -4.909  1.00 66.02  ? 214 LYS A CE  1 
ATOM   1730 N  NZ  . LYS A 1 219 ? -40.270 22.685  -4.033  1.00 74.16  ? 214 LYS A NZ  1 
ATOM   1731 N  N   . ASP A 1 220 ? -32.835 24.010  -2.456  1.00 21.56  ? 215 ASP A N   1 
ATOM   1732 C  CA  . ASP A 1 220 ? -31.572 23.768  -1.774  1.00 25.03  ? 215 ASP A CA  1 
ATOM   1733 C  C   . ASP A 1 220 ? -31.622 24.103  -0.281  1.00 23.75  ? 215 ASP A C   1 
ATOM   1734 O  O   . ASP A 1 220 ? -31.215 23.295  0.557   1.00 21.67  ? 215 ASP A O   1 
ATOM   1735 C  CB  . ASP A 1 220 ? -30.449 24.579  -2.432  1.00 26.62  ? 215 ASP A CB  1 
ATOM   1736 C  CG  . ASP A 1 220 ? -29.978 24.107  -3.803  1.00 36.54  ? 215 ASP A CG  1 
ATOM   1737 O  OD1 . ASP A 1 220 ? -30.252 22.938  -4.165  1.00 31.65  ? 215 ASP A OD1 1 
ATOM   1738 O  OD2 . ASP A 1 220 ? -29.350 24.908  -4.511  1.00 36.41  ? 215 ASP A OD2 1 
ATOM   1739 N  N   . SER A 1 221 ? -32.093 25.316  0.044   1.00 20.42  ? 216 SER A N   1 
ATOM   1740 C  CA  . SER A 1 221 ? -32.161 25.751  1.432   1.00 20.42  ? 216 SER A CA  1 
ATOM   1741 C  C   . SER A 1 221 ? -33.123 24.907  2.276   1.00 17.93  ? 216 SER A C   1 
ATOM   1742 O  O   . SER A 1 221 ? -32.794 24.528  3.399   1.00 19.03  ? 216 SER A O   1 
ATOM   1743 C  CB  . SER A 1 221 ? -32.542 27.230  1.513   1.00 17.53  ? 216 SER A CB  1 
ATOM   1744 O  OG  . SER A 1 221 ? -31.545 28.060  0.936   1.00 19.08  ? 216 SER A OG  1 
ATOM   1745 N  N   . THR A 1 222 ? -34.308 24.586  1.736   1.00 17.57  ? 217 THR A N   1 
ATOM   1746 C  CA  . THR A 1 222 ? -35.315 23.876  2.511   1.00 18.22  ? 217 THR A CA  1 
ATOM   1747 C  C   . THR A 1 222 ? -34.901 22.435  2.812   1.00 17.15  ? 217 THR A C   1 
ATOM   1748 O  O   . THR A 1 222 ? -35.270 21.895  3.853   1.00 17.66  ? 217 THR A O   1 
ATOM   1749 C  CB  . THR A 1 222 ? -36.683 23.942  1.838   1.00 22.97  ? 217 THR A CB  1 
ATOM   1750 O  OG1 . THR A 1 222 ? -36.569 23.472  0.493   1.00 22.01  ? 217 THR A OG1 1 
ATOM   1751 C  CG2 . THR A 1 222 ? -37.271 25.354  1.875   1.00 19.05  ? 217 THR A CG2 1 
ATOM   1752 N  N   . LEU A 1 223 ? -34.110 21.825  1.921   1.00 19.36  ? 218 LEU A N   1 
ATOM   1753 C  CA  . LEU A 1 223 ? -33.582 20.496  2.195   1.00 21.74  ? 218 LEU A CA  1 
ATOM   1754 C  C   . LEU A 1 223 ? -32.774 20.468  3.493   1.00 19.07  ? 218 LEU A C   1 
ATOM   1755 O  O   . LEU A 1 223 ? -32.966 19.592  4.331   1.00 21.09  ? 218 LEU A O   1 
ATOM   1756 C  CB  . LEU A 1 223 ? -32.731 19.993  1.021   1.00 24.09  ? 218 LEU A CB  1 
ATOM   1757 C  CG  . LEU A 1 223 ? -32.252 18.537  1.144   1.00 35.35  ? 218 LEU A CG  1 
ATOM   1758 C  CD1 . LEU A 1 223 ? -32.119 17.883  -0.222  1.00 37.13  ? 218 LEU A CD1 1 
ATOM   1759 C  CD2 . LEU A 1 223 ? -30.913 18.436  1.877   1.00 38.89  ? 218 LEU A CD2 1 
ATOM   1760 N  N   . ILE A 1 224 ? -31.910 21.460  3.700   1.00 19.18  ? 219 ILE A N   1 
ATOM   1761 C  CA  . ILE A 1 224 ? -31.096 21.489  4.907   1.00 17.77  ? 219 ILE A CA  1 
ATOM   1762 C  C   . ILE A 1 224 ? -31.926 21.860  6.133   1.00 18.69  ? 219 ILE A C   1 
ATOM   1763 O  O   . ILE A 1 224 ? -31.695 21.367  7.236   1.00 17.52  ? 219 ILE A O   1 
ATOM   1764 C  CB  . ILE A 1 224 ? -29.909 22.448  4.738   1.00 22.29  ? 219 ILE A CB  1 
ATOM   1765 C  CG1 . ILE A 1 224 ? -29.080 22.106  3.483   1.00 28.94  ? 219 ILE A CG1 1 
ATOM   1766 C  CG2 . ILE A 1 224 ? -29.033 22.442  5.980   1.00 23.83  ? 219 ILE A CG2 1 
ATOM   1767 C  CD1 . ILE A 1 224 ? -28.356 23.279  2.896   1.00 28.37  ? 219 ILE A CD1 1 
ATOM   1768 N  N   . MET A 1 225 ? -32.880 22.772  5.935   1.00 18.21  ? 220 MET A N   1 
ATOM   1769 C  CA  . MET A 1 225 ? -33.781 23.167  7.004   1.00 16.02  ? 220 MET A CA  1 
ATOM   1770 C  C   . MET A 1 225 ? -34.544 21.973  7.568   1.00 16.11  ? 220 MET A C   1 
ATOM   1771 O  O   . MET A 1 225 ? -34.767 21.880  8.775   1.00 14.94  ? 220 MET A O   1 
ATOM   1772 C  CB  . MET A 1 225 ? -34.755 24.229  6.495   1.00 14.45  ? 220 MET A CB  1 
ATOM   1773 C  CG  . MET A 1 225 ? -34.127 25.564  6.330   1.00 16.08  ? 220 MET A CG  1 
ATOM   1774 S  SD  . MET A 1 225 ? -35.206 26.744  5.449   1.00 19.57  ? 220 MET A SD  1 
ATOM   1775 C  CE  . MET A 1 225 ? -36.324 27.071  6.672   1.00 20.89  ? 220 MET A CE  1 
ATOM   1776 N  N   . GLN A 1 226 ? -34.933 21.042  6.691   1.00 14.69  ? 221 GLN A N   1 
ATOM   1777 C  CA  . GLN A 1 226 ? -35.613 19.843  7.144   1.00 15.38  ? 221 GLN A CA  1 
ATOM   1778 C  C   . GLN A 1 226 ? -34.736 18.994  8.071   1.00 16.63  ? 221 GLN A C   1 
ATOM   1779 O  O   . GLN A 1 226 ? -35.240 18.376  9.008   1.00 16.50  ? 221 GLN A O   1 
ATOM   1780 C  CB  . GLN A 1 226 ? -36.085 19.011  5.930   1.00 21.04  ? 221 GLN A CB  1 
ATOM   1781 C  CG  . GLN A 1 226 ? -36.880 17.750  6.292   1.00 24.42  ? 221 GLN A CG  1 
ATOM   1782 C  CD  . GLN A 1 226 ? -38.139 18.054  7.069   1.00 33.98  ? 221 GLN A CD  1 
ATOM   1783 O  OE1 . GLN A 1 226 ? -38.981 18.846  6.637   1.00 35.29  ? 221 GLN A OE1 1 
ATOM   1784 N  NE2 . GLN A 1 226 ? -38.301 17.443  8.236   1.00 28.95  ? 221 GLN A NE2 1 
ATOM   1785 N  N   . LEU A 1 227 ? -33.424 18.974  7.821   1.00 16.41  ? 222 LEU A N   1 
ATOM   1786 C  CA  . LEU A 1 227 ? -32.515 18.238  8.689   1.00 15.80  ? 222 LEU A CA  1 
ATOM   1787 C  C   . LEU A 1 227 ? -32.405 18.877  10.079  1.00 16.68  ? 222 LEU A C   1 
ATOM   1788 O  O   . LEU A 1 227 ? -32.360 18.173  11.081  1.00 16.18  ? 222 LEU A O   1 
ATOM   1789 C  CB  . LEU A 1 227 ? -31.135 18.111  8.036   1.00 17.85  ? 222 LEU A CB  1 
ATOM   1790 C  CG  . LEU A 1 227 ? -31.125 17.485  6.644   1.00 19.38  ? 222 LEU A CG  1 
ATOM   1791 C  CD1 . LEU A 1 227 ? -29.713 17.355  6.127   1.00 21.90  ? 222 LEU A CD1 1 
ATOM   1792 C  CD2 . LEU A 1 227 ? -31.836 16.154  6.640   1.00 21.21  ? 222 LEU A CD2 1 
ATOM   1793 N  N   . LEU A 1 228 ? -32.397 20.216  10.153  1.00 15.12  ? 223 LEU A N   1 
ATOM   1794 C  CA  . LEU A 1 228 ? -32.461 20.887  11.440  1.00 15.92  ? 223 LEU A CA  1 
ATOM   1795 C  C   . LEU A 1 228 ? -33.733 20.489  12.192  1.00 18.10  ? 223 LEU A C   1 
ATOM   1796 O  O   . LEU A 1 228 ? -33.677 20.201  13.383  1.00 17.54  ? 223 LEU A O   1 
ATOM   1797 C  CB  . LEU A 1 228 ? -32.416 22.410  11.250  1.00 14.00  ? 223 LEU A CB  1 
ATOM   1798 C  CG  . LEU A 1 228 ? -31.112 22.989  10.708  1.00 15.53  ? 223 LEU A CG  1 
ATOM   1799 C  CD1 . LEU A 1 228 ? -31.349 24.369  10.135  1.00 17.76  ? 223 LEU A CD1 1 
ATOM   1800 C  CD2 . LEU A 1 228 ? -30.048 23.054  11.792  1.00 16.95  ? 223 LEU A CD2 1 
ATOM   1801 N  N   . ARG A 1 229 ? -34.878 20.472  11.492  1.00 18.24  ? 224 ARG A N   1 
ATOM   1802 C  CA  . ARG A 1 229 ? -36.144 20.071  12.095  1.00 17.39  ? 224 ARG A CA  1 
ATOM   1803 C  C   . ARG A 1 229 ? -36.116 18.612  12.560  1.00 15.15  ? 224 ARG A C   1 
ATOM   1804 O  O   . ARG A 1 229 ? -36.581 18.298  13.656  1.00 18.59  ? 224 ARG A O   1 
ATOM   1805 C  CB  . ARG A 1 229 ? -37.294 20.309  11.094  1.00 19.64  ? 224 ARG A CB  1 
ATOM   1806 C  CG  . ARG A 1 229 ? -38.706 19.944  11.589  1.00 29.99  ? 224 ARG A CG  1 
ATOM   1807 C  CD  . ARG A 1 229 ? -39.110 20.662  12.864  1.00 39.32  ? 224 ARG A CD  1 
ATOM   1808 N  NE  . ARG A 1 229 ? -39.067 22.115  12.740  1.00 45.29  ? 224 ARG A NE  1 
ATOM   1809 C  CZ  . ARG A 1 229 ? -39.114 22.958  13.766  1.00 59.35  ? 224 ARG A CZ  1 
ATOM   1810 N  NH1 . ARG A 1 229 ? -39.236 22.527  15.013  1.00 59.50  ? 224 ARG A NH1 1 
ATOM   1811 N  NH2 . ARG A 1 229 ? -39.027 24.265  13.537  1.00 50.90  ? 224 ARG A NH2 1 
ATOM   1812 N  N   . ASP A 1 230 ? -35.531 17.726  11.748  1.00 17.45  ? 225 ASP A N   1 
ATOM   1813 C  CA  . ASP A 1 230 ? -35.406 16.320  12.110  1.00 17.31  ? 225 ASP A CA  1 
ATOM   1814 C  C   . ASP A 1 230 ? -34.631 16.168  13.420  1.00 17.24  ? 225 ASP A C   1 
ATOM   1815 O  O   . ASP A 1 230 ? -35.016 15.389  14.292  1.00 19.00  ? 225 ASP A O   1 
ATOM   1816 C  CB  . ASP A 1 230 ? -34.681 15.518  11.024  1.00 19.19  ? 225 ASP A CB  1 
ATOM   1817 C  CG  . ASP A 1 230 ? -35.381 15.302  9.700   1.00 24.04  ? 225 ASP A CG  1 
ATOM   1818 O  OD1 . ASP A 1 230 ? -36.612 15.474  9.646   1.00 23.90  ? 225 ASP A OD1 1 
ATOM   1819 O  OD2 . ASP A 1 230 ? -34.683 14.956  8.711   1.00 25.52  ? 225 ASP A OD2 1 
ATOM   1820 N  N   . ASN A 1 231 ? -33.538 16.927  13.569  1.00 16.89  ? 226 ASN A N   1 
ATOM   1821 C  CA  . ASN A 1 231 ? -32.765 16.875  14.797  1.00 16.85  ? 226 ASN A CA  1 
ATOM   1822 C  C   . ASN A 1 231 ? -33.553 17.445  15.974  1.00 17.47  ? 226 ASN A C   1 
ATOM   1823 O  O   . ASN A 1 231 ? -33.587 16.851  17.044  1.00 17.47  ? 226 ASN A O   1 
ATOM   1824 C  CB  . ASN A 1 231 ? -31.426 17.586  14.630  1.00 14.16  ? 226 ASN A CB  1 
ATOM   1825 C  CG  . ASN A 1 231 ? -30.404 16.757  13.881  1.00 16.22  ? 226 ASN A CG  1 
ATOM   1826 O  OD1 . ASN A 1 231 ? -30.515 15.516  13.774  1.00 16.26  ? 226 ASN A OD1 1 
ATOM   1827 N  ND2 . ASN A 1 231 ? -29.361 17.407  13.385  1.00 15.10  ? 226 ASN A ND2 1 
ATOM   1828 N  N   . LEU A 1 232 ? -34.187 18.603  15.788  1.00 16.22  ? 227 LEU A N   1 
ATOM   1829 C  CA  . LEU A 1 232 ? -35.018 19.154  16.849  1.00 16.13  ? 227 LEU A CA  1 
ATOM   1830 C  C   . LEU A 1 232 ? -36.088 18.174  17.332  1.00 18.77  ? 227 LEU A C   1 
ATOM   1831 O  O   . LEU A 1 232 ? -36.333 18.103  18.531  1.00 20.87  ? 227 LEU A O   1 
ATOM   1832 C  CB  . LEU A 1 232 ? -35.655 20.457  16.373  1.00 16.72  ? 227 LEU A CB  1 
ATOM   1833 C  CG  . LEU A 1 232 ? -34.697 21.635  16.339  1.00 15.50  ? 227 LEU A CG  1 
ATOM   1834 C  CD1 . LEU A 1 232 ? -35.293 22.778  15.560  1.00 17.36  ? 227 LEU A CD1 1 
ATOM   1835 C  CD2 . LEU A 1 232 ? -34.321 22.061  17.744  1.00 15.33  ? 227 LEU A CD2 1 
ATOM   1836 N  N   . THR A 1 233 ? -36.679 17.396  16.411  1.00 19.43  ? 228 THR A N   1 
ATOM   1837 C  CA  . THR A 1 233 ? -37.665 16.377  16.763  1.00 23.26  ? 228 THR A CA  1 
ATOM   1838 C  C   . THR A 1 233 ? -37.044 15.247  17.587  1.00 28.58  ? 228 THR A C   1 
ATOM   1839 O  O   . THR A 1 233 ? -37.643 14.763  18.551  1.00 25.50  ? 228 THR A O   1 
ATOM   1840 C  CB  . THR A 1 233 ? -38.336 15.841  15.492  1.00 21.91  ? 228 THR A CB  1 
ATOM   1841 O  OG1 . THR A 1 233 ? -39.021 16.910  14.849  1.00 24.82  ? 228 THR A OG1 1 
ATOM   1842 C  CG2 . THR A 1 233 ? -39.311 14.697  15.770  1.00 24.91  ? 228 THR A CG2 1 
ATOM   1843 N  N   . LEU A 1 234 ? -35.829 14.840  17.200  1.00 23.09  ? 229 LEU A N   1 
ATOM   1844 C  CA  . LEU A 1 234 ? -35.083 13.815  17.908  1.00 22.40  ? 229 LEU A CA  1 
ATOM   1845 C  C   . LEU A 1 234 ? -34.679 14.293  19.300  1.00 24.54  ? 229 LEU A C   1 
ATOM   1846 O  O   . LEU A 1 234 ? -34.667 13.503  20.240  1.00 26.84  ? 229 LEU A O   1 
ATOM   1847 C  CB  . LEU A 1 234 ? -33.832 13.433  17.092  1.00 25.29  ? 229 LEU A CB  1 
ATOM   1848 C  CG  . LEU A 1 234 ? -32.932 12.348  17.673  1.00 28.78  ? 229 LEU A CG  1 
ATOM   1849 C  CD1 . LEU A 1 234 ? -33.591 10.980  17.579  1.00 33.23  ? 229 LEU A CD1 1 
ATOM   1850 C  CD2 . LEU A 1 234 ? -31.592 12.318  16.957  1.00 30.74  ? 229 LEU A CD2 1 
ATOM   1851 N  N   . TRP A 1 235 ? -34.379 15.596  19.426  1.00 20.40  ? 230 TRP A N   1 
ATOM   1852 C  CA  . TRP A 1 235 ? -33.809 16.146  20.645  1.00 22.08  ? 230 TRP A CA  1 
ATOM   1853 C  C   . TRP A 1 235 ? -34.828 16.624  21.681  1.00 25.78  ? 230 TRP A C   1 
ATOM   1854 O  O   . TRP A 1 235 ? -34.476 16.806  22.843  1.00 26.19  ? 230 TRP A O   1 
ATOM   1855 C  CB  . TRP A 1 235 ? -32.877 17.319  20.286  1.00 18.94  ? 230 TRP A CB  1 
ATOM   1856 C  CG  . TRP A 1 235 ? -31.666 16.952  19.474  1.00 18.27  ? 230 TRP A CG  1 
ATOM   1857 C  CD1 . TRP A 1 235 ? -31.146 15.709  19.272  1.00 18.45  ? 230 TRP A CD1 1 
ATOM   1858 C  CD2 . TRP A 1 235 ? -30.848 17.857  18.725  1.00 17.72  ? 230 TRP A CD2 1 
ATOM   1859 N  NE1 . TRP A 1 235 ? -30.043 15.785  18.458  1.00 16.24  ? 230 TRP A NE1 1 
ATOM   1860 C  CE2 . TRP A 1 235 ? -29.847 17.092  18.095  1.00 15.75  ? 230 TRP A CE2 1 
ATOM   1861 C  CE3 . TRP A 1 235 ? -30.875 19.245  18.517  1.00 15.68  ? 230 TRP A CE3 1 
ATOM   1862 C  CZ2 . TRP A 1 235 ? -28.852 17.669  17.306  1.00 17.17  ? 230 TRP A CZ2 1 
ATOM   1863 C  CZ3 . TRP A 1 235 ? -29.900 19.814  17.716  1.00 15.15  ? 230 TRP A CZ3 1 
ATOM   1864 C  CH2 . TRP A 1 235 ? -28.901 19.028  17.129  1.00 16.41  ? 230 TRP A CH2 1 
ATOM   1865 N  N   . THR A 1 236 ? -36.075 16.857  21.249  1.00 26.52  ? 231 THR A N   1 
ATOM   1866 C  CA  . THR A 1 236 ? -37.106 17.392  22.126  1.00 27.92  ? 231 THR A CA  1 
ATOM   1867 C  C   . THR A 1 236 ? -38.327 16.476  22.160  1.00 40.73  ? 231 THR A C   1 
ATOM   1868 O  O   . THR A 1 236 ? -39.350 16.832  22.750  1.00 46.40  ? 231 THR A O   1 
ATOM   1869 C  CB  . THR A 1 236 ? -37.476 18.824  21.701  1.00 32.20  ? 231 THR A CB  1 
ATOM   1870 O  OG1 . THR A 1 236 ? -38.136 18.792  20.431  1.00 29.44  ? 231 THR A OG1 1 
ATOM   1871 C  CG2 . THR A 1 236 ? -36.266 19.734  21.631  1.00 35.61  ? 231 THR A CG2 1 
ATOM   1872 O  OXT . THR A 1 236 ? -38.292 15.377  21.611  1.00 42.87  ? 231 THR A OXT 1 
ATOM   1873 N  N   . GLN B 2 1   ? -30.914 6.747   18.246  1.00 47.86  ? 255 GLN P N   1 
ATOM   1874 C  CA  . GLN B 2 1   ? -30.260 7.046   16.974  1.00 53.34  ? 255 GLN P CA  1 
ATOM   1875 C  C   . GLN B 2 1   ? -29.467 8.349   17.059  1.00 35.98  ? 255 GLN P C   1 
ATOM   1876 O  O   . GLN B 2 1   ? -29.766 9.219   17.877  1.00 38.39  ? 255 GLN P O   1 
ATOM   1877 C  CB  . GLN B 2 1   ? -31.281 7.123   15.833  1.00 55.78  ? 255 GLN P CB  1 
ATOM   1878 C  CG  . GLN B 2 1   ? -32.366 8.156   16.044  1.00 56.76  ? 255 GLN P CG  1 
ATOM   1879 C  CD  . GLN B 2 1   ? -33.240 8.283   14.828  1.00 52.95  ? 255 GLN P CD  1 
ATOM   1880 O  OE1 . GLN B 2 1   ? -32.777 8.631   13.738  1.00 67.32  ? 255 GLN P OE1 1 
ATOM   1881 N  NE2 . GLN B 2 1   ? -34.522 8.005   14.986  1.00 60.40  ? 255 GLN P NE2 1 
ATOM   1882 N  N   . ARG B 2 2   ? -28.460 8.464   16.190  1.00 34.69  ? 256 ARG P N   1 
ATOM   1883 C  CA  . ARG B 2 2   ? -27.560 9.603   16.195  1.00 30.42  ? 256 ARG P CA  1 
ATOM   1884 C  C   . ARG B 2 2   ? -28.129 10.771  15.401  1.00 24.79  ? 256 ARG P C   1 
ATOM   1885 O  O   . ARG B 2 2   ? -28.902 10.586  14.466  1.00 25.36  ? 256 ARG P O   1 
ATOM   1886 C  CB  . ARG B 2 2   ? -26.206 9.208   15.620  1.00 33.05  ? 256 ARG P CB  1 
ATOM   1887 C  CG  . ARG B 2 2   ? -25.518 8.162   16.467  1.00 45.36  ? 256 ARG P CG  1 
ATOM   1888 C  CD  . ARG B 2 2   ? -24.170 7.780   15.928  1.00 44.36  ? 256 ARG P CD  1 
ATOM   1889 N  NE  . ARG B 2 2   ? -23.688 6.572   16.586  1.00 50.22  ? 256 ARG P NE  1 
ATOM   1890 C  CZ  . ARG B 2 2   ? -22.685 6.530   17.451  1.00 41.49  ? 256 ARG P CZ  1 
ATOM   1891 N  NH1 . ARG B 2 2   ? -21.973 7.609   17.740  1.00 38.70  ? 256 ARG P NH1 1 
ATOM   1892 N  NH2 . ARG B 2 2   ? -22.385 5.375   18.037  1.00 49.36  ? 256 ARG P NH2 1 
ATOM   1893 N  N   . SER B 2 3   ? -27.722 11.976  15.794  1.00 25.89  ? 257 SER P N   1 
ATOM   1894 C  CA  . SER B 2 3   ? -28.100 13.181  15.081  1.00 21.49  ? 257 SER P CA  1 
ATOM   1895 C  C   . SER B 2 3   ? -27.662 13.122  13.620  1.00 22.87  ? 257 SER P C   1 
ATOM   1896 O  O   . SER B 2 3   ? -26.674 12.467  13.280  1.00 21.47  ? 257 SER P O   1 
ATOM   1897 C  CB  . SER B 2 3   ? -27.482 14.389  15.762  1.00 19.22  ? 257 SER P CB  1 
ATOM   1898 O  OG  . SER B 2 3   ? -27.803 14.400  17.143  1.00 19.51  ? 257 SER P OG  1 
ATOM   1899 N  N   . THR B 2 4   ? -28.415 13.822  12.767  1.00 18.57  ? 258 THR P N   1 
ATOM   1900 C  CA  . THR B 2 4   ? -28.103 13.952  11.357  1.00 19.42  ? 258 THR P CA  1 
ATOM   1901 C  C   . THR B 2 4   ? -27.197 15.149  11.109  1.00 17.65  ? 258 THR P C   1 
ATOM   1902 O  O   . THR B 2 4   ? -27.535 16.265  11.497  1.00 15.73  ? 258 THR P O   1 
ATOM   1903 C  CB  . THR B 2 4   ? -29.382 14.137  10.534  1.00 21.09  ? 258 THR P CB  1 
ATOM   1904 O  OG1 . THR B 2 4   ? -30.296 13.095  10.845  1.00 22.16  ? 258 THR P OG1 1 
ATOM   1905 C  CG2 . THR B 2 4   ? -29.102 14.169  9.030   1.00 23.06  ? 258 THR P CG2 1 
HETATM 1906 N  N   . SEP B 2 5   ? -26.059 14.908  10.438  1.00 16.31  ? 259 SEP P N   1 
HETATM 1907 C  CA  . SEP B 2 5   ? -25.181 15.967  9.977   1.00 16.56  ? 259 SEP P CA  1 
HETATM 1908 C  CB  . SEP B 2 5   ? -23.741 15.659  10.363  1.00 15.86  ? 259 SEP P CB  1 
HETATM 1909 O  OG  . SEP B 2 5   ? -23.333 14.456  9.694   1.00 13.09  ? 259 SEP P OG  1 
HETATM 1910 C  C   . SEP B 2 5   ? -25.370 16.167  8.473   1.00 15.96  ? 259 SEP P C   1 
HETATM 1911 O  O   . SEP B 2 5   ? -26.170 15.469  7.846   1.00 16.77  ? 259 SEP P O   1 
HETATM 1912 P  P   . SEP B 2 5   ? -21.904 13.833  10.075  1.00 14.97  ? 259 SEP P P   1 
HETATM 1913 O  O1P . SEP B 2 5   ? -21.807 12.642  9.131   1.00 15.15  ? 259 SEP P O1P 1 
HETATM 1914 O  O2P . SEP B 2 5   ? -20.891 14.895  9.776   1.00 15.08  ? 259 SEP P O2P 1 
HETATM 1915 O  O3P . SEP B 2 5   ? -21.935 13.444  11.541  1.00 15.17  ? 259 SEP P O3P 1 
ATOM   1916 N  N   . THR B 2 6   ? -24.653 17.134  7.891   1.00 14.73  ? 260 THR P N   1 
ATOM   1917 C  CA  A THR B 2 6   ? -24.870 17.491  6.502   0.50 16.93  ? 260 THR P CA  1 
ATOM   1918 C  CA  B THR B 2 6   ? -24.849 17.491  6.493   0.50 15.57  ? 260 THR P CA  1 
ATOM   1919 C  C   . THR B 2 6   ? -24.555 16.298  5.595   1.00 20.59  ? 260 THR P C   1 
ATOM   1920 O  O   . THR B 2 6   ? -23.516 15.663  5.732   1.00 20.16  ? 260 THR P O   1 
ATOM   1921 C  CB  A THR B 2 6   ? -24.073 18.744  6.204   0.50 18.41  ? 260 THR P CB  1 
ATOM   1922 C  CB  B THR B 2 6   ? -23.962 18.633  5.997   0.50 15.04  ? 260 THR P CB  1 
ATOM   1923 O  OG1 A THR B 2 6   ? -24.461 19.765  7.133   0.50 19.47  ? 260 THR P OG1 1 
ATOM   1924 O  OG1 B THR B 2 6   ? -22.580 18.265  6.147   0.50 14.86  ? 260 THR P OG1 1 
ATOM   1925 C  CG2 A THR B 2 6   ? -24.290 19.228  4.824   0.50 18.96  ? 260 THR P CG2 1 
ATOM   1926 C  CG2 B THR B 2 6   ? -24.260 19.932  6.698   0.50 15.10  ? 260 THR P CG2 1 
ATOM   1927 N  N   . PRO B 2 7   ? -25.443 15.960  4.637   1.00 16.86  ? 261 PRO P N   1 
ATOM   1928 C  CA  . PRO B 2 7   ? -25.160 14.872  3.700   1.00 21.37  ? 261 PRO P CA  1 
ATOM   1929 C  C   . PRO B 2 7   ? -24.310 15.311  2.508   1.00 20.35  ? 261 PRO P C   1 
ATOM   1930 O  O   . PRO B 2 7   ? -23.959 16.483  2.385   1.00 21.76  ? 261 PRO P O   1 
ATOM   1931 C  CB  . PRO B 2 7   ? -26.574 14.455  3.274   1.00 20.21  ? 261 PRO P CB  1 
ATOM   1932 C  CG  . PRO B 2 7   ? -27.334 15.757  3.254   1.00 21.87  ? 261 PRO P CG  1 
ATOM   1933 C  CD  . PRO B 2 7   ? -26.772 16.562  4.420   1.00 18.41  ? 261 PRO P CD  1 
ATOM   1934 N  N   . ASN B 2 8   ? -23.991 14.345  1.632   1.00 24.11  ? 262 ASN P N   1 
ATOM   1935 C  CA  . ASN B 2 8   ? -23.390 14.620  0.333   1.00 27.00  ? 262 ASN P CA  1 
ATOM   1936 C  C   . ASN B 2 8   ? -24.455 15.023  -0.688  1.00 34.96  ? 262 ASN P C   1 
ATOM   1937 O  O   . ASN B 2 8   ? -25.496 14.376  -0.772  1.00 47.09  ? 262 ASN P O   1 
ATOM   1938 C  CB  . ASN B 2 8   ? -22.642 13.383  -0.180  1.00 30.84  ? 262 ASN P CB  1 
ATOM   1939 C  CG  . ASN B 2 8   ? -21.538 12.928  0.734   1.00 31.79  ? 262 ASN P CG  1 
ATOM   1940 O  OD1 . ASN B 2 8   ? -21.526 11.796  1.229   1.00 39.64  ? 262 ASN P OD1 1 
ATOM   1941 N  ND2 . ASN B 2 8   ? -20.598 13.819  0.991   1.00 25.70  ? 262 ASN P ND2 1 
ATOM   1942 N  N   . VAL B 2 9   ? -24.187 16.078  -1.468  1.00 36.13  ? 263 VAL P N   1 
ATOM   1943 C  CA  . VAL B 2 9   ? -25.112 16.530  -2.499  1.00 52.14  ? 263 VAL P CA  1 
ATOM   1944 C  C   . VAL B 2 9   ? -24.537 16.260  -3.892  1.00 58.98  ? 263 VAL P C   1 
ATOM   1945 O  O   . VAL B 2 9   ? -23.366 16.532  -4.144  1.00 70.73  ? 263 VAL P O   1 
ATOM   1946 C  CB  . VAL B 2 9   ? -25.492 18.027  -2.328  1.00 55.29  ? 263 VAL P CB  1 
ATOM   1947 C  CG1 . VAL B 2 9   ? -25.723 18.359  -0.866  1.00 44.42  ? 263 VAL P CG1 1 
ATOM   1948 C  CG2 . VAL B 2 9   ? -24.449 18.971  -2.926  1.00 62.01  ? 263 VAL P CG2 1 
HETATM 1949 CL CL  . CL  C 3 .   ? -5.822  -6.291  13.635  1.00 18.89  ? 301 CL  A CL  1 
HETATM 1950 MG MG  . MG  D 4 .   ? -6.015  4.241   19.593  1.00 28.61  2 302 MG  A MG  1 
HETATM 1951 MG MG  . MG  E 4 .   ? -19.084 -18.481 30.663  1.00 28.28  2 303 MG  A MG  1 
HETATM 1952 MG MG  . MG  F 4 .   ? 0.000   21.099  -15.766 0.50 13.92  2 304 MG  A MG  1 
HETATM 1953 C  C1  . WQN G 5 .   ? -19.066 25.553  -2.276  1.00 31.94  ? 305 WQN A C1  1 
HETATM 1954 C  C10 . WQN G 5 .   ? -25.431 20.591  1.970   1.00 51.49  ? 305 WQN A C10 1 
HETATM 1955 C  C11 . WQN G 5 .   ? -25.157 21.925  2.206   1.00 41.72  ? 305 WQN A C11 1 
HETATM 1956 C  C12 . WQN G 5 .   ? -23.845 22.318  2.417   1.00 36.58  ? 305 WQN A C12 1 
HETATM 1957 C  C13 . WQN G 5 .   ? -20.324 20.344  0.644   1.00 23.96  ? 305 WQN A C13 1 
HETATM 1958 C  C14 . WQN G 5 .   ? -19.489 20.347  -0.617  1.00 22.26  ? 305 WQN A C14 1 
HETATM 1959 C  C2  . WQN G 5 .   ? -20.012 26.401  -3.101  1.00 32.62  ? 305 WQN A C2  1 
HETATM 1960 C  C3  . WQN G 5 .   ? -18.817 23.268  -1.171  1.00 25.55  ? 305 WQN A C3  1 
HETATM 1961 C  C4  . WQN G 5 .   ? -20.168 22.532  -1.210  1.00 21.05  ? 305 WQN A C4  1 
HETATM 1962 C  C5  . WQN G 5 .   ? -20.576 23.449  -2.383  1.00 21.72  ? 305 WQN A C5  1 
HETATM 1963 C  C6  . WQN G 5 .   ? -21.034 22.592  0.059   1.00 22.98  ? 305 WQN A C6  1 
HETATM 1964 C  C7  . WQN G 5 .   ? -22.836 21.376  2.399   1.00 33.31  ? 305 WQN A C7  1 
HETATM 1965 C  C8  . WQN G 5 .   ? -23.125 20.051  2.148   1.00 36.20  ? 305 WQN A C8  1 
HETATM 1966 C  C9  . WQN G 5 .   ? -24.428 19.650  1.937   1.00 38.35  ? 305 WQN A C9  1 
HETATM 1967 N  N1  . WQN G 5 .   ? -19.440 24.310  -2.005  1.00 24.26  ? 305 WQN A N1  1 
HETATM 1968 N  N2  . WQN G 5 .   ? -20.491 21.727  1.128   1.00 24.44  ? 305 WQN A N2  1 
HETATM 1969 O  O1  . WQN G 5 .   ? -18.001 26.011  -1.871  1.00 23.18  ? 305 WQN A O1  1 
HETATM 1970 O  O2  . WQN G 5 .   ? -21.110 23.241  2.967   1.00 28.80  ? 305 WQN A O2  1 
HETATM 1971 O  O3  . WQN G 5 .   ? -20.523 20.882  3.458   1.00 30.49  ? 305 WQN A O3  1 
HETATM 1972 O  O4  . WQN G 5 .   ? -20.061 21.182  -1.641  1.00 19.93  ? 305 WQN A O4  1 
HETATM 1973 S  S1  . WQN G 5 .   ? -21.162 21.853  2.621   1.00 30.59  ? 305 WQN A S1  1 
HETATM 1974 BR BR1 . WQN G 5 .   ? -27.219 20.017  1.681   1.00 141.91 ? 305 WQN A BR1 1 
HETATM 1975 CA CA  . CA  H 6 .   ? -7.369  33.473  -2.456  1.00 19.84  2 306 CA  A CA  1 
HETATM 1976 O  O   . HOH I 7 .   ? -9.217  -14.980 20.882  1.00 26.42  ? 401 HOH A O   1 
HETATM 1977 O  O   . HOH I 7 .   ? -39.336 13.817  19.904  1.00 27.13  ? 402 HOH A O   1 
HETATM 1978 O  O   . HOH I 7 .   ? -3.120  -2.915  18.670  1.00 33.84  ? 403 HOH A O   1 
HETATM 1979 O  O   . HOH I 7 .   ? -18.293 -3.098  29.041  1.00 49.15  ? 404 HOH A O   1 
HETATM 1980 O  O   . HOH I 7 .   ? 4.556   17.291  -10.447 1.00 27.60  ? 405 HOH A O   1 
HETATM 1981 O  O   . HOH I 7 .   ? -6.967  5.022   21.181  1.00 40.47  ? 406 HOH A O   1 
HETATM 1982 O  O   . HOH I 7 .   ? -2.405  -7.088  21.638  1.00 22.28  ? 407 HOH A O   1 
HETATM 1983 O  O   . HOH I 7 .   ? -17.720 12.191  -15.474 1.00 30.19  ? 408 HOH A O   1 
HETATM 1984 O  O   . HOH I 7 .   ? -9.659  2.355   6.408   1.00 25.94  ? 409 HOH A O   1 
HETATM 1985 O  O   . HOH I 7 .   ? -36.094 31.434  17.040  1.00 33.24  ? 410 HOH A O   1 
HETATM 1986 O  O   . HOH I 7 .   ? -23.823 30.778  22.013  1.00 19.03  ? 411 HOH A O   1 
HETATM 1987 O  O   . HOH I 7 .   ? -11.038 -3.745  25.191  1.00 29.64  ? 412 HOH A O   1 
HETATM 1988 O  O   . HOH I 7 .   ? -0.709  16.998  1.632   1.00 35.92  ? 413 HOH A O   1 
HETATM 1989 O  O   . HOH I 7 .   ? -33.858 36.061  8.333   1.00 25.95  ? 414 HOH A O   1 
HETATM 1990 O  O   . HOH I 7 .   ? -14.086 38.314  -1.414  1.00 25.59  ? 415 HOH A O   1 
HETATM 1991 O  O   . HOH I 7 .   ? -18.971 17.708  -10.245 1.00 34.38  ? 416 HOH A O   1 
HETATM 1992 O  O   . HOH I 7 .   ? -12.370 21.909  -12.818 1.00 20.97  ? 417 HOH A O   1 
HETATM 1993 O  O   . HOH I 7 .   ? -19.196 -13.814 23.854  1.00 52.80  ? 418 HOH A O   1 
HETATM 1994 O  O   . HOH I 7 .   ? -18.437 7.501   15.380  1.00 26.06  ? 419 HOH A O   1 
HETATM 1995 O  O   . HOH I 7 .   ? -32.403 15.531  23.887  1.00 36.30  ? 420 HOH A O   1 
HETATM 1996 O  O   . HOH I 7 .   ? -2.271  20.254  -20.122 1.00 24.35  ? 421 HOH A O   1 
HETATM 1997 O  O   . HOH I 7 .   ? -7.457  1.696   -6.021  1.00 36.44  ? 422 HOH A O   1 
HETATM 1998 O  O   . HOH I 7 .   ? 0.707   14.935  -5.219  1.00 25.98  ? 423 HOH A O   1 
HETATM 1999 O  O   . HOH I 7 .   ? -13.191 30.609  19.437  1.00 33.53  ? 424 HOH A O   1 
HETATM 2000 O  O   . HOH I 7 .   ? -14.311 1.073   21.967  1.00 30.60  ? 425 HOH A O   1 
HETATM 2001 O  O   . HOH I 7 .   ? -15.076 9.148   14.114  1.00 14.24  ? 426 HOH A O   1 
HETATM 2002 O  O   . HOH I 7 .   ? -17.017 -12.122 24.963  1.00 38.99  ? 427 HOH A O   1 
HETATM 2003 O  O   . HOH I 7 .   ? -15.604 15.856  3.722   1.00 22.46  ? 428 HOH A O   1 
HETATM 2004 O  O   . HOH I 7 .   ? -20.923 15.428  -6.860  1.00 41.72  ? 429 HOH A O   1 
HETATM 2005 O  O   . HOH I 7 .   ? -5.014  21.446  12.136  1.00 25.91  ? 430 HOH A O   1 
HETATM 2006 O  O   . HOH I 7 .   ? 1.569   22.519  -3.811  1.00 15.48  ? 431 HOH A O   1 
HETATM 2007 O  O   . HOH I 7 .   ? -20.760 6.743   9.056   1.00 32.97  ? 432 HOH A O   1 
HETATM 2008 O  O   . HOH I 7 .   ? -4.139  -2.968  16.311  1.00 19.25  ? 433 HOH A O   1 
HETATM 2009 O  O   . HOH I 7 .   ? 1.243   20.385  -17.889 1.00 16.87  ? 434 HOH A O   1 
HETATM 2010 O  O   . HOH I 7 .   ? -9.452  27.139  -2.514  1.00 15.15  ? 435 HOH A O   1 
HETATM 2011 O  O   . HOH I 7 .   ? -19.753 0.778   -8.989  1.00 28.73  ? 436 HOH A O   1 
HETATM 2012 O  O   . HOH I 7 .   ? -4.901  29.519  -7.493  1.00 23.52  ? 437 HOH A O   1 
HETATM 2013 O  O   . HOH I 7 .   ? -27.998 10.866  19.977  1.00 37.12  ? 438 HOH A O   1 
HETATM 2014 O  O   . HOH I 7 .   ? -18.967 18.685  -7.709  1.00 28.73  ? 439 HOH A O   1 
HETATM 2015 O  O   . HOH I 7 .   ? -11.073 4.889   21.193  1.00 17.80  ? 440 HOH A O   1 
HETATM 2016 O  O   . HOH I 7 .   ? -9.181  24.777  15.323  1.00 22.99  ? 441 HOH A O   1 
HETATM 2017 O  O   . HOH I 7 .   ? -11.353 29.412  -5.698  1.00 28.88  ? 442 HOH A O   1 
HETATM 2018 O  O   . HOH I 7 .   ? -18.538 0.704   7.071   1.00 30.78  ? 443 HOH A O   1 
HETATM 2019 O  O   . HOH I 7 .   ? -14.253 3.716   4.151   1.00 23.57  ? 444 HOH A O   1 
HETATM 2020 O  O   . HOH I 7 .   ? -7.956  27.101  -9.598  1.00 23.97  ? 445 HOH A O   1 
HETATM 2021 O  O   . HOH I 7 .   ? -27.220 31.579  15.574  1.00 28.90  ? 446 HOH A O   1 
HETATM 2022 O  O   . HOH I 7 .   ? -17.551 -19.149 32.065  1.00 55.04  ? 447 HOH A O   1 
HETATM 2023 O  O   . HOH I 7 .   ? -30.007 30.998  19.767  1.00 22.79  ? 448 HOH A O   1 
HETATM 2024 O  O   . HOH I 7 .   ? -6.386  18.157  26.306  1.00 31.19  ? 449 HOH A O   1 
HETATM 2025 O  O   . HOH I 7 .   ? -0.348  26.870  8.258   1.00 40.77  ? 450 HOH A O   1 
HETATM 2026 O  O   . HOH I 7 .   ? -6.146  -15.057 21.638  1.00 25.87  ? 451 HOH A O   1 
HETATM 2027 O  O   . HOH I 7 .   ? -23.256 23.634  27.648  1.00 25.13  ? 452 HOH A O   1 
HETATM 2028 O  O   . HOH I 7 .   ? -5.540  5.038   17.751  1.00 28.23  ? 453 HOH A O   1 
HETATM 2029 O  O   . HOH I 7 .   ? -17.537 13.675  23.844  1.00 27.82  ? 454 HOH A O   1 
HETATM 2030 O  O   . HOH I 7 .   ? -10.439 36.809  -2.246  1.00 26.18  ? 455 HOH A O   1 
HETATM 2031 O  O   . HOH I 7 .   ? -36.443 13.113  13.803  1.00 32.78  ? 456 HOH A O   1 
HETATM 2032 O  O   . HOH I 7 .   ? -18.295 2.212   -2.632  1.00 32.73  ? 457 HOH A O   1 
HETATM 2033 O  O   . HOH I 7 .   ? -15.058 24.201  -11.496 1.00 26.91  ? 458 HOH A O   1 
HETATM 2034 O  O   . HOH I 7 .   ? -20.407 37.509  13.021  1.00 23.44  ? 459 HOH A O   1 
HETATM 2035 O  O   . HOH I 7 .   ? -32.077 25.404  24.374  1.00 27.17  ? 460 HOH A O   1 
HETATM 2036 O  O   . HOH I 7 .   ? -4.116  23.932  -3.251  1.00 20.51  ? 461 HOH A O   1 
HETATM 2037 O  O   . HOH I 7 .   ? -32.181 13.555  12.836  1.00 26.79  ? 462 HOH A O   1 
HETATM 2038 O  O   . HOH I 7 .   ? 0.446   23.513  -10.280 1.00 25.25  ? 463 HOH A O   1 
HETATM 2039 O  O   . HOH I 7 .   ? -11.077 18.531  -15.655 1.00 19.72  ? 464 HOH A O   1 
HETATM 2040 O  O   . HOH I 7 .   ? -18.143 8.046   19.747  1.00 29.72  ? 465 HOH A O   1 
HETATM 2041 O  O   . HOH I 7 .   ? -4.979  22.957  -7.160  1.00 13.42  ? 466 HOH A O   1 
HETATM 2042 O  O   . HOH I 7 .   ? -10.105 20.729  31.966  1.00 25.07  ? 467 HOH A O   1 
HETATM 2043 O  O   . HOH I 7 .   ? -7.368  27.879  -0.997  1.00 15.90  ? 468 HOH A O   1 
HETATM 2044 O  O   . HOH I 7 .   ? -15.132 20.864  -12.123 1.00 37.16  ? 469 HOH A O   1 
HETATM 2045 O  O   . HOH I 7 .   ? -33.920 17.038  3.984   1.00 27.11  ? 470 HOH A O   1 
HETATM 2046 O  O   . HOH I 7 .   ? -15.389 32.628  -4.884  1.00 20.22  ? 471 HOH A O   1 
HETATM 2047 O  O   . HOH I 7 .   ? -12.458 21.020  25.479  1.00 20.80  ? 472 HOH A O   1 
HETATM 2048 O  O   . HOH I 7 .   ? -16.585 18.503  3.951   1.00 18.46  ? 473 HOH A O   1 
HETATM 2049 O  O   . HOH I 7 .   ? -26.315 15.738  24.666  1.00 27.11  ? 474 HOH A O   1 
HETATM 2050 O  O   . HOH I 7 .   ? 0.052   20.203  6.986   1.00 32.22  ? 475 HOH A O   1 
HETATM 2051 O  O   . HOH I 7 .   ? -17.843 16.660  26.218  1.00 35.26  ? 476 HOH A O   1 
HETATM 2052 O  O   . HOH I 7 .   ? -19.277 12.462  -11.013 1.00 21.57  ? 477 HOH A O   1 
HETATM 2053 O  O   . HOH I 7 .   ? -28.971 32.069  11.456  1.00 17.12  ? 478 HOH A O   1 
HETATM 2054 O  O   . HOH I 7 .   ? -27.560 30.449  13.105  1.00 17.14  ? 479 HOH A O   1 
HETATM 2055 O  O   . HOH I 7 .   ? -6.181  10.063  0.479   1.00 23.51  ? 480 HOH A O   1 
HETATM 2056 O  O   . HOH I 7 .   ? -5.394  16.971  -18.909 1.00 20.87  ? 481 HOH A O   1 
HETATM 2057 O  O   . HOH I 7 .   ? -22.540 -5.248  19.180  1.00 37.05  ? 482 HOH A O   1 
HETATM 2058 O  O   . HOH I 7 .   ? -33.215 20.913  29.968  1.00 25.94  ? 483 HOH A O   1 
HETATM 2059 O  O   . HOH I 7 .   ? -13.924 23.181  24.220  1.00 21.54  ? 484 HOH A O   1 
HETATM 2060 O  O   . HOH I 7 .   ? -13.817 17.676  -15.419 1.00 21.57  ? 485 HOH A O   1 
HETATM 2061 O  O   . HOH I 7 .   ? -0.122  16.741  -7.077  1.00 17.29  ? 486 HOH A O   1 
HETATM 2062 O  O   . HOH I 7 .   ? -17.315 28.839  20.628  1.00 21.96  ? 487 HOH A O   1 
HETATM 2063 O  O   . HOH I 7 .   ? -5.416  6.151   6.975   1.00 21.91  ? 488 HOH A O   1 
HETATM 2064 O  O   . HOH I 7 .   ? -30.895 35.538  16.902  1.00 21.61  ? 489 HOH A O   1 
HETATM 2065 O  O   . HOH I 7 .   ? -32.482 13.247  8.977   1.00 26.23  ? 490 HOH A O   1 
HETATM 2066 O  O   . HOH I 7 .   ? -7.601  7.676   -0.732  1.00 18.94  ? 491 HOH A O   1 
HETATM 2067 O  O   . HOH I 7 .   ? -22.218 1.428   12.400  1.00 23.97  ? 492 HOH A O   1 
HETATM 2068 O  O   . HOH I 7 .   ? -20.763 1.952   19.029  1.00 31.97  ? 493 HOH A O   1 
HETATM 2069 O  O   . HOH I 7 .   ? -21.532 17.516  -0.900  1.00 30.50  ? 494 HOH A O   1 
HETATM 2070 O  O   . HOH I 7 .   ? -2.286  15.763  4.036   1.00 21.10  ? 495 HOH A O   1 
HETATM 2071 O  O   . HOH I 7 .   ? -20.560 13.781  15.780  1.00 14.41  ? 496 HOH A O   1 
HETATM 2072 O  O   . HOH I 7 .   ? -12.586 30.613  16.945  1.00 27.09  ? 497 HOH A O   1 
HETATM 2073 O  O   . HOH I 7 .   ? -12.297 -6.729  24.327  1.00 39.11  ? 498 HOH A O   1 
HETATM 2074 O  O   . HOH I 7 .   ? -39.986 25.748  21.522  1.00 40.32  ? 499 HOH A O   1 
HETATM 2075 O  O   . HOH I 7 .   ? -5.558  24.741  9.488   1.00 23.98  ? 500 HOH A O   1 
HETATM 2076 O  O   . HOH I 7 .   ? -30.198 30.798  9.288   1.00 17.98  ? 501 HOH A O   1 
HETATM 2077 O  O   . HOH I 7 .   ? -6.076  22.105  9.630   1.00 20.45  ? 502 HOH A O   1 
HETATM 2078 O  O   . HOH I 7 .   ? -3.093  28.647  -3.507  1.00 33.43  ? 503 HOH A O   1 
HETATM 2079 O  O   . HOH I 7 .   ? -30.127 29.203  -1.241  1.00 24.33  ? 504 HOH A O   1 
HETATM 2080 O  O   . HOH I 7 .   ? -7.103  22.874  21.030  1.00 26.02  ? 505 HOH A O   1 
HETATM 2081 O  O   . HOH I 7 .   ? -35.076 15.019  5.899   1.00 35.68  ? 506 HOH A O   1 
HETATM 2082 O  O   . HOH I 7 .   ? -8.230  7.366   20.975  1.00 32.62  ? 507 HOH A O   1 
HETATM 2083 O  O   . HOH I 7 .   ? -38.702 23.468  17.643  1.00 42.64  ? 508 HOH A O   1 
HETATM 2084 O  O   . HOH I 7 .   ? 2.613   18.106  -9.439  1.00 21.36  ? 509 HOH A O   1 
HETATM 2085 O  O   . HOH I 7 .   ? -8.417  15.295  27.829  1.00 39.14  ? 510 HOH A O   1 
HETATM 2086 O  O   . HOH I 7 .   ? -0.332  19.493  2.226   1.00 27.64  ? 511 HOH A O   1 
HETATM 2087 O  O   . HOH I 7 .   ? -3.072  11.140  -3.699  1.00 19.35  ? 512 HOH A O   1 
HETATM 2088 O  O   . HOH I 7 .   ? -1.898  21.837  -15.486 1.00 44.42  ? 513 HOH A O   1 
HETATM 2089 O  O   . HOH I 7 .   ? -7.788  21.800  -13.592 1.00 22.20  ? 514 HOH A O   1 
HETATM 2090 O  O   . HOH I 7 .   ? -21.004 23.761  23.772  1.00 19.50  ? 515 HOH A O   1 
HETATM 2091 O  O   . HOH I 7 .   ? -3.066  7.263   12.412  1.00 27.04  ? 516 HOH A O   1 
HETATM 2092 O  O   . HOH I 7 .   ? -23.682 29.154  10.150  1.00 22.42  ? 517 HOH A O   1 
HETATM 2093 O  O   . HOH I 7 .   ? -23.156 27.866  19.309  1.00 21.64  ? 518 HOH A O   1 
HETATM 2094 O  O   . HOH I 7 .   ? -11.375 -10.481 21.423  1.00 26.79  ? 519 HOH A O   1 
HETATM 2095 O  O   . HOH I 7 .   ? -3.857  26.921  5.440   1.00 16.57  ? 520 HOH A O   1 
HETATM 2096 O  O   . HOH I 7 .   ? -38.701 33.733  11.544  1.00 29.28  ? 521 HOH A O   1 
HETATM 2097 O  O   . HOH I 7 .   ? -10.434 29.689  -2.795  1.00 23.72  ? 522 HOH A O   1 
HETATM 2098 O  O   . HOH I 7 .   ? -29.780 20.295  14.173  1.00 21.35  ? 523 HOH A O   1 
HETATM 2099 O  O   . HOH I 7 .   ? -37.993 31.046  -9.333  1.00 28.60  ? 524 HOH A O   1 
HETATM 2100 O  O   . HOH I 7 .   ? -22.279 15.123  24.058  1.00 22.02  ? 525 HOH A O   1 
HETATM 2101 O  O   . HOH I 7 .   ? -39.134 38.124  6.747   1.00 19.08  ? 526 HOH A O   1 
HETATM 2102 O  O   . HOH I 7 .   ? 1.858   13.773  -1.426  1.00 33.87  ? 527 HOH A O   1 
HETATM 2103 O  O   . HOH I 7 .   ? 0.088   10.020  -11.515 1.00 31.30  ? 528 HOH A O   1 
HETATM 2104 O  O   . HOH I 7 .   ? -29.191 21.489  -0.422  1.00 38.46  ? 529 HOH A O   1 
HETATM 2105 O  O   . HOH I 7 .   ? -5.258  34.254  -2.042  1.00 24.25  ? 530 HOH A O   1 
HETATM 2106 O  O   . HOH I 7 .   ? -15.137 12.910  -15.871 1.00 19.20  ? 531 HOH A O   1 
HETATM 2107 O  O   . HOH I 7 .   ? -5.768  31.722  7.605   1.00 30.12  ? 532 HOH A O   1 
HETATM 2108 O  O   . HOH I 7 .   ? -2.176  10.759  7.737   1.00 33.70  ? 533 HOH A O   1 
HETATM 2109 O  O   . HOH I 7 .   ? -34.353 30.465  19.386  1.00 30.69  ? 534 HOH A O   1 
HETATM 2110 O  O   . HOH I 7 .   ? -14.554 11.909  -18.398 1.00 31.37  ? 535 HOH A O   1 
HETATM 2111 O  O   . HOH I 7 .   ? -29.240 31.966  -0.125  1.00 20.45  ? 536 HOH A O   1 
HETATM 2112 O  O   . HOH I 7 .   ? -8.613  10.802  18.001  1.00 15.59  ? 537 HOH A O   1 
HETATM 2113 O  O   . HOH I 7 .   ? -4.281  0.811   10.910  1.00 26.00  ? 538 HOH A O   1 
HETATM 2114 O  O   . HOH I 7 .   ? -35.025 28.718  -9.982  1.00 23.96  ? 539 HOH A O   1 
HETATM 2115 O  O   . HOH I 7 .   ? -21.889 -4.182  16.828  1.00 29.64  ? 540 HOH A O   1 
HETATM 2116 O  O   . HOH I 7 .   ? -25.740 30.749  10.962  1.00 24.89  ? 541 HOH A O   1 
HETATM 2117 O  O   . HOH I 7 .   ? -21.517 10.667  -4.775  1.00 38.05  ? 542 HOH A O   1 
HETATM 2118 O  O   . HOH I 7 .   ? -10.202 -7.576  22.941  1.00 22.78  ? 543 HOH A O   1 
HETATM 2119 O  O   . HOH I 7 .   ? -21.338 10.553  16.952  1.00 31.61  ? 544 HOH A O   1 
HETATM 2120 O  O   . HOH I 7 .   ? -26.805 26.616  26.110  1.00 24.73  ? 545 HOH A O   1 
HETATM 2121 O  O   . HOH I 7 .   ? -0.084  12.485  -4.888  1.00 30.62  ? 546 HOH A O   1 
HETATM 2122 O  O   . HOH I 7 .   ? -32.083 32.711  -5.606  1.00 24.20  ? 547 HOH A O   1 
HETATM 2123 O  O   . HOH I 7 .   ? -21.800 10.371  -2.161  1.00 28.00  ? 548 HOH A O   1 
HETATM 2124 O  O   . HOH I 7 .   ? -1.557  22.081  -1.099  1.00 27.88  ? 549 HOH A O   1 
HETATM 2125 O  O   . HOH I 7 .   ? -22.942 5.914   -12.413 1.00 39.66  ? 550 HOH A O   1 
HETATM 2126 O  O   . HOH I 7 .   ? -14.193 -1.402  -5.844  1.00 22.12  ? 551 HOH A O   1 
HETATM 2127 O  O   . HOH I 7 .   ? -18.814 10.682  7.113   1.00 19.91  ? 552 HOH A O   1 
HETATM 2128 O  O   . HOH I 7 .   ? -16.514 37.188  0.313   1.00 33.98  ? 553 HOH A O   1 
HETATM 2129 O  O   . HOH I 7 .   ? -38.562 28.224  17.651  1.00 38.80  ? 554 HOH A O   1 
HETATM 2130 O  O   . HOH I 7 .   ? -4.271  20.544  -16.043 1.00 17.51  ? 555 HOH A O   1 
HETATM 2131 O  O   . HOH I 7 .   ? -14.486 7.744   22.329  1.00 34.14  ? 556 HOH A O   1 
HETATM 2132 O  O   . HOH I 7 .   ? -8.990  4.522   22.866  1.00 39.45  ? 557 HOH A O   1 
HETATM 2133 O  O   . HOH I 7 .   ? -0.919  26.503  -2.214  1.00 26.15  ? 558 HOH A O   1 
HETATM 2134 O  O   . HOH I 7 .   ? -38.959 21.761  7.341   1.00 43.67  ? 559 HOH A O   1 
HETATM 2135 O  O   . HOH I 7 .   ? -13.940 35.919  4.089   1.00 43.57  ? 560 HOH A O   1 
HETATM 2136 O  O   . HOH I 7 .   ? -17.317 21.465  4.923   1.00 24.70  ? 561 HOH A O   1 
HETATM 2137 O  O   . HOH I 7 .   ? -8.011  -6.553  25.185  1.00 32.03  ? 562 HOH A O   1 
HETATM 2138 O  O   . HOH I 7 .   ? -16.582 0.367   -5.700  1.00 37.28  ? 563 HOH A O   1 
HETATM 2139 O  O   . HOH I 7 .   ? -19.144 26.885  21.761  1.00 22.09  ? 564 HOH A O   1 
HETATM 2140 O  O   . HOH I 7 .   ? -3.085  24.912  -0.985  1.00 27.44  ? 565 HOH A O   1 
HETATM 2141 O  O   . HOH I 7 .   ? -23.372 9.618   12.037  1.00 25.52  ? 566 HOH A O   1 
HETATM 2142 O  O   . HOH I 7 .   ? -3.758  16.521  12.672  1.00 41.75  ? 567 HOH A O   1 
HETATM 2143 O  O   . HOH I 7 .   ? -28.275 34.259  14.898  1.00 43.07  ? 568 HOH A O   1 
HETATM 2144 O  O   . HOH I 7 .   ? -4.712  8.666   5.207   1.00 39.64  ? 569 HOH A O   1 
HETATM 2145 O  O   . HOH I 7 .   ? -5.835  6.530   19.562  1.00 40.75  ? 570 HOH A O   1 
HETATM 2146 O  O   . HOH I 7 .   ? -5.558  19.630  18.782  1.00 35.89  ? 571 HOH A O   1 
HETATM 2147 O  O   . HOH I 7 .   ? -18.180 16.565  6.261   1.00 31.01  ? 572 HOH A O   1 
HETATM 2148 O  O   . HOH I 7 .   ? -27.923 30.495  18.473  1.00 36.03  ? 573 HOH A O   1 
HETATM 2149 O  O   . HOH I 7 .   ? -36.907 41.755  1.689   1.00 45.05  ? 574 HOH A O   1 
HETATM 2150 O  O   . HOH I 7 .   ? -11.794 3.268   -4.549  1.00 16.37  ? 575 HOH A O   1 
HETATM 2151 O  O   . HOH I 7 .   ? -6.807  7.258   -7.266  1.00 28.56  ? 576 HOH A O   1 
HETATM 2152 O  O   . HOH I 7 .   ? -7.377  34.493  -4.604  1.00 22.50  ? 577 HOH A O   1 
HETATM 2153 O  O   . HOH I 7 .   ? -28.733 27.814  -3.475  1.00 36.12  ? 578 HOH A O   1 
HETATM 2154 O  O   . HOH I 7 .   ? -6.751  11.935  23.269  1.00 35.05  ? 579 HOH A O   1 
HETATM 2155 O  O   . HOH I 7 .   ? -5.043  -7.727  25.911  1.00 36.66  ? 580 HOH A O   1 
HETATM 2156 O  O   . HOH I 7 .   ? -18.349 29.961  -4.330  1.00 34.43  ? 581 HOH A O   1 
HETATM 2157 O  O   . HOH I 7 .   ? -4.733  11.780  15.242  1.00 44.93  ? 582 HOH A O   1 
HETATM 2158 O  O   . HOH I 7 .   ? -2.850  1.478   17.503  1.00 36.77  ? 583 HOH A O   1 
HETATM 2159 O  O   . HOH I 7 .   ? -1.306  10.348  10.327  1.00 37.70  ? 584 HOH A O   1 
HETATM 2160 O  O   . HOH I 7 .   ? -23.156 3.979   11.894  1.00 32.85  ? 585 HOH A O   1 
HETATM 2161 O  O   . HOH I 7 .   ? -9.687  1.628   -4.172  1.00 32.08  ? 586 HOH A O   1 
HETATM 2162 O  O   . HOH I 7 .   ? -7.366  32.861  -6.553  1.00 35.44  ? 587 HOH A O   1 
HETATM 2163 O  O   . HOH I 7 .   ? -12.159 -0.208  25.764  1.00 48.97  ? 588 HOH A O   1 
HETATM 2164 O  O   . HOH I 7 .   ? -13.804 2.712   -2.298  1.00 37.40  ? 589 HOH A O   1 
HETATM 2165 O  O   . HOH I 7 .   ? -25.297 7.763   11.905  1.00 36.80  ? 590 HOH A O   1 
HETATM 2166 O  O   . HOH I 7 .   ? -24.545 11.757  5.308   1.00 38.51  ? 591 HOH A O   1 
HETATM 2167 O  O   . HOH I 7 .   ? -6.556  -9.965  26.210  1.00 40.83  ? 592 HOH A O   1 
HETATM 2168 O  O   . HOH I 7 .   ? -41.212 32.291  1.759   1.00 20.66  ? 593 HOH A O   1 
HETATM 2169 O  O   . HOH I 7 .   ? -3.596  28.013  7.858   1.00 39.08  ? 594 HOH A O   1 
HETATM 2170 O  O   . HOH I 7 .   ? -6.534  23.970  15.839  1.00 45.29  ? 595 HOH A O   1 
HETATM 2171 O  O   . HOH I 7 .   ? -9.413  27.078  13.542  1.00 35.12  ? 596 HOH A O   1 
HETATM 2172 O  O   . HOH I 7 .   ? -5.561  2.509   18.375  1.00 35.21  ? 597 HOH A O   1 
HETATM 2173 O  O   . HOH I 7 .   ? -4.141  31.745  -6.497  1.00 34.04  ? 598 HOH A O   1 
HETATM 2174 O  O   . HOH I 7 .   ? -3.475  -0.273  15.388  1.00 32.98  ? 599 HOH A O   1 
HETATM 2175 O  O   . HOH I 7 .   ? -6.620  35.198  2.312   1.00 38.33  ? 600 HOH A O   1 
HETATM 2176 O  O   . HOH I 7 .   ? -5.303  8.647   20.268  1.00 45.54  ? 601 HOH A O   1 
HETATM 2177 O  O   . HOH I 7 .   ? -6.027  5.656   -1.556  1.00 43.30  ? 602 HOH A O   1 
HETATM 2178 O  O   . HOH I 7 .   ? -36.431 13.919  24.293  1.00 63.67  ? 603 HOH A O   1 
HETATM 2179 O  O   . HOH I 7 .   ? -7.102  10.484  20.297  1.00 29.87  ? 604 HOH A O   1 
HETATM 2180 O  O   . HOH I 7 .   ? -15.283 24.317  26.634  1.00 39.24  ? 605 HOH A O   1 
HETATM 2181 O  O   . HOH I 7 .   ? -4.336  16.305  15.021  1.00 51.56  ? 606 HOH A O   1 
HETATM 2182 O  O   . HOH I 7 .   ? -23.070 0.409   14.972  1.00 36.10  ? 607 HOH A O   1 
HETATM 2183 O  O   . HOH I 7 .   ? -33.863 26.832  22.620  1.00 28.38  ? 608 HOH A O   1 
HETATM 2184 O  O   . HOH I 7 .   ? -15.973 6.679   14.814  1.00 17.93  ? 609 HOH A O   1 
HETATM 2185 O  O   . HOH I 7 .   ? 5.468   14.760  -6.998  1.00 30.01  ? 610 HOH A O   1 
HETATM 2186 O  O   . HOH I 7 .   ? -6.804  4.284   5.246   1.00 42.20  ? 611 HOH A O   1 
HETATM 2187 O  O   . HOH I 7 .   ? -3.476  -4.652  14.496  1.00 27.40  ? 612 HOH A O   1 
HETATM 2188 O  O   . HOH I 7 .   ? -8.421  5.110   3.130   1.00 34.26  ? 613 HOH A O   1 
HETATM 2189 O  O   . HOH I 7 .   ? -4.749  19.561  -18.626 1.00 30.39  ? 614 HOH A O   1 
HETATM 2190 O  O   . HOH I 7 .   ? -21.826 26.233  24.737  1.00 27.38  ? 615 HOH A O   1 
HETATM 2191 O  O   . HOH I 7 .   ? -37.295 11.306  16.172  1.00 41.80  ? 616 HOH A O   1 
HETATM 2192 O  O   . HOH I 7 .   ? -4.871  26.988  -2.063  1.00 24.34  ? 617 HOH A O   1 
HETATM 2193 O  O   . HOH I 7 .   ? -27.266 22.706  -1.566  1.00 30.96  ? 618 HOH A O   1 
HETATM 2194 O  O   . HOH I 7 .   ? -1.172  23.212  -17.386 1.00 40.67  ? 619 HOH A O   1 
HETATM 2195 O  O   . HOH I 7 .   ? -23.004 12.438  15.686  1.00 22.21  ? 620 HOH A O   1 
HETATM 2196 O  O   . HOH I 7 .   ? -3.059  2.952   9.638   1.00 34.74  ? 621 HOH A O   1 
HETATM 2197 O  O   . HOH I 7 .   ? -4.081  -6.721  11.168  1.00 24.05  ? 622 HOH A O   1 
HETATM 2198 O  O   . HOH I 7 .   ? -20.334 25.701  -8.890  1.00 33.11  ? 623 HOH A O   1 
HETATM 2199 O  O   . HOH I 7 .   ? -21.208 21.657  -6.621  1.00 39.36  ? 624 HOH A O   1 
HETATM 2200 O  O   . HOH I 7 .   ? -6.454  9.225   3.042   1.00 26.83  ? 625 HOH A O   1 
HETATM 2201 O  O   . HOH I 7 .   ? -6.142  22.871  -15.484 1.00 24.32  ? 626 HOH A O   1 
HETATM 2202 O  O   . HOH I 7 .   ? -6.339  12.433  17.266  1.00 28.26  ? 627 HOH A O   1 
HETATM 2203 O  O   . HOH I 7 .   ? -15.133 15.645  -16.699 1.00 25.66  ? 628 HOH A O   1 
HETATM 2204 O  O   . HOH I 7 .   ? -41.020 22.186  9.016   1.00 48.81  ? 629 HOH A O   1 
HETATM 2205 O  O   . HOH I 7 .   ? -32.039 19.651  26.701  1.00 27.01  ? 630 HOH A O   1 
HETATM 2206 O  O   . HOH I 7 .   ? -34.345 10.981  10.215  1.00 41.48  ? 631 HOH A O   1 
HETATM 2207 O  O   . HOH I 7 .   ? -19.198 14.343  -15.253 1.00 35.74  ? 632 HOH A O   1 
HETATM 2208 O  O   . HOH I 7 .   ? -11.692 21.874  30.104  1.00 22.09  ? 633 HOH A O   1 
HETATM 2209 O  O   . HOH I 7 .   ? -23.465 25.812  -2.095  1.00 34.06  ? 634 HOH A O   1 
HETATM 2210 O  O   . HOH I 7 .   ? -22.144 8.486   7.644   1.00 40.76  ? 635 HOH A O   1 
HETATM 2211 O  O   . HOH I 7 .   ? -12.766 3.452   22.735  1.00 27.88  ? 636 HOH A O   1 
HETATM 2212 O  O   . HOH I 7 .   ? -13.663 16.269  27.262  1.00 41.73  ? 637 HOH A O   1 
HETATM 2213 O  O   . HOH I 7 .   ? -20.564 -1.532  -5.672  1.00 40.60  ? 638 HOH A O   1 
HETATM 2214 O  O   . HOH I 7 .   ? -11.198 22.384  27.518  1.00 25.47  ? 639 HOH A O   1 
HETATM 2215 O  O   . HOH I 7 .   ? -20.675 29.355  -2.787  1.00 39.01  ? 640 HOH A O   1 
HETATM 2216 O  O   . HOH I 7 .   ? -1.934  8.618   -4.353  1.00 33.28  ? 641 HOH A O   1 
HETATM 2217 O  O   . HOH I 7 .   ? -2.721  -0.256  12.705  1.00 33.31  ? 642 HOH A O   1 
HETATM 2218 O  O   . HOH I 7 .   ? -24.250 22.961  -1.563  1.00 45.01  ? 643 HOH A O   1 
HETATM 2219 O  O   . HOH I 7 .   ? 1.050   -7.873  18.784  1.00 39.22  ? 644 HOH A O   1 
HETATM 2220 O  O   . HOH I 7 .   ? -23.312 29.931  17.366  1.00 30.44  ? 645 HOH A O   1 
HETATM 2221 O  O   . HOH I 7 .   ? 1.641   22.523  -19.685 1.00 19.23  ? 646 HOH A O   1 
HETATM 2222 O  O   . HOH I 7 .   ? -23.556 -2.392  15.551  1.00 44.02  ? 647 HOH A O   1 
HETATM 2223 O  O   . HOH I 7 .   ? -14.020 20.509  29.506  1.00 27.59  ? 648 HOH A O   1 
HETATM 2224 O  O   . HOH I 7 .   ? -3.913  9.522   -1.094  1.00 34.44  ? 649 HOH A O   1 
HETATM 2225 O  O   . HOH I 7 .   ? -14.202 19.089  26.975  1.00 24.41  ? 650 HOH A O   1 
HETATM 2226 O  O   . HOH I 7 .   ? -14.750 5.445   23.280  1.00 31.52  ? 651 HOH A O   1 
HETATM 2227 O  O   . HOH I 7 .   ? -39.575 24.774  4.847   1.00 46.23  ? 652 HOH A O   1 
HETATM 2228 O  O   . HOH I 7 .   ? -8.369  7.605   1.959   1.00 26.45  ? 653 HOH A O   1 
HETATM 2229 O  O   . HOH I 7 .   ? -0.526  3.144   10.769  1.00 39.45  ? 654 HOH A O   1 
HETATM 2230 O  O   . HOH J 7 .   ? -20.498 4.543   19.181  1.00 39.95  ? 301 HOH P O   1 
HETATM 2231 O  O   . HOH J 7 .   ? -20.332 17.826  5.034   1.00 35.92  ? 302 HOH P O   1 
HETATM 2232 O  O   . HOH J 7 .   ? -21.365 16.396  7.483   1.00 19.76  ? 303 HOH P O   1 
HETATM 2233 O  O   . HOH J 7 .   ? -23.383 10.541  9.427   1.00 28.00  ? 304 HOH P O   1 
HETATM 2234 O  O   . HOH J 7 .   ? -21.543 17.268  3.161   1.00 30.45  ? 305 HOH P O   1 
HETATM 2235 O  O   . HOH J 7 .   ? -26.473 12.982  6.903   1.00 26.39  ? 306 HOH P O   1 
HETATM 2236 O  O   . HOH J 7 .   ? -20.079 16.447  1.144   1.00 24.32  ? 307 HOH P O   1 
HETATM 2237 O  O   . HOH J 7 .   ? -23.881 12.255  13.001  1.00 19.65  ? 308 HOH P O   1 
HETATM 2238 O  O   . HOH J 7 .   ? -19.269 7.331   17.670  1.00 37.38  ? 309 HOH P O   1 
HETATM 2239 O  O   . HOH J 7 .   ? -28.502 5.296   18.611  1.00 46.37  ? 310 HOH P O   1 
HETATM 2240 O  O   . HOH J 7 .   ? -25.809 12.023  9.495   1.00 21.34  ? 311 HOH P O   1 
HETATM 2241 O  O   . HOH J 7 .   ? -24.671 11.460  2.598   1.00 32.20  ? 312 HOH P O   1 
HETATM 2242 O  O   . HOH J 7 .   ? -31.563 12.407  6.576   1.00 30.77  ? 313 HOH P O   1 
# 
