data_5EHE
# 
_entry.id   5EHE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_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   5EHE         pdb_00005ehe 10.2210/pdb5ehe/pdb 
WWPDB D_1000214916 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2016-11-09 
2 'Structure model' 1 1 2017-01-18 
3 'Structure model' 1 2 2017-02-01 
4 'Structure model' 1 3 2019-07-17 
5 'Structure model' 1 4 2024-01-10 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Database references'    
3 4 'Structure model' 'Data collection'        
4 5 'Structure model' 'Data collection'        
5 5 'Structure model' 'Database references'    
6 5 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' diffrn_source                 
2 5 'Structure model' chem_comp_atom                
3 5 'Structure model' chem_comp_bond                
4 5 'Structure model' database_2                    
5 5 'Structure model' pdbx_initial_refinement_model 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
2 5 'Structure model' '_database_2.pdbx_DOI'                 
3 5 'Structure model' '_database_2.pdbx_database_accession'  
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5EHE 
_pdbx_database_status.recvd_initial_deposition_date   2015-10-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        '4QTL contains the same inhibitor in different binding mode.' 
_pdbx_database_related.db_id          4QTL 
_pdbx_database_related.content_type   unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_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                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            ChemMedChem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1860-7187 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            12 
_citation.language                  ? 
_citation.page_first                161 
_citation.page_last                 176 
_citation.title                     
'Intrinsic Thermodynamics and Structures of 2,4- and 3,4-Substituted Fluorinated Benzenesulfonamides Binding to Carbonic Anhydrases.' 
_citation.year                      2017 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cmdc.201600509 
_citation.pdbx_database_id_PubMed   28001003 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zubriene, A.'      1  ? 
primary 'Smirnov, A.'       2  ? 
primary 'Dudutiene, V.'     3  ? 
primary 'Timm, D.D.'        4  ? 
primary 'Matuliene, J.'     5  ? 
primary 'Michailoviene, V.' 6  ? 
primary 'Zaksauskas, A.'    7  ? 
primary 'Manakova, E.'      8  ? 
primary 'Grazulis, S.'      9  ? 
primary 'Matulis, D.'       10 ? 
# 
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 'Carbonic anhydrase 2'                                                           29289.062 1   4.2.1.1 ? 
'human carbonic anhydrase II'                                                    ? 
2 non-polymer syn 'ZINC ION'                                                                       65.409    1   ?       ? 
'3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                             78.133    2   ?       ? Zn ? 
4 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                           195.237   1   ?       ? BICINE 
? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                          106.120   1   ?       ? 
'DIMETHYL SULFOXIDE'                                                             ? 
6 non-polymer syn '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 424.415   1   ?       ? 
'N-(EHTYLSULFITE)MORPHOLINE'                                                     ? 
7 water       nat water                                                                            18.015    218 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                       ZN  
3 'DIMETHYL SULFOXIDE'                                                             DMS 
4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                           MES 
5 'DI(HYDROXYETHYL)ETHER'                                                          PEG 
6 '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' WWO 
7 water                                                                            HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS 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                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
CYS 'L-peptide linking' y CYSTEINE                                                                         ? 'C3 H7 N O2 S'        
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                             ? 'C2 H6 O S'           
78.133  
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 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                           ? 'C6 H13 N O4 S'       
195.237 
MET 'L-peptide linking' y METHIONINE                                                                       ? 'C5 H11 N O2 S'       
149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                          ? 'C4 H10 O3'           
106.120 
PHE 'L-peptide linking' y PHENYLALANINE                                                                    ? 'C9 H11 N O2'         
165.189 
PRO 'L-peptide linking' y PROLINE                                                                          ? 'C5 H9 N O2'          
115.130 
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 
WWO non-polymer         . '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 'C15 H15 F3 N2 O5 S2' 
424.415 
ZN  non-polymer         . 'ZINC ION'                                                                       ? 'Zn 2'                
65.409  
# 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
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 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 DMS 1   302 1   DMS DMS A . 
D 4 MES 1   303 3   MES MES A . 
E 5 PEG 1   304 5   PEG PEG A . 
F 3 DMS 1   305 7   DMS DMS A . 
G 6 WWO 1   306 1   WWO WWO A . 
H 7 HOH 1   401 203 HOH HOH A . 
H 7 HOH 2   402 185 HOH HOH A . 
H 7 HOH 3   403 115 HOH HOH A . 
H 7 HOH 4   404 17  HOH HOH A . 
H 7 HOH 5   405 196 HOH HOH A . 
H 7 HOH 6   406 210 HOH HOH A . 
H 7 HOH 7   407 192 HOH HOH A . 
H 7 HOH 8   408 172 HOH HOH A . 
H 7 HOH 9   409 199 HOH HOH A . 
H 7 HOH 10  410 62  HOH HOH A . 
H 7 HOH 11  411 119 HOH HOH A . 
H 7 HOH 12  412 67  HOH HOH A . 
H 7 HOH 13  413 126 HOH HOH A . 
H 7 HOH 14  414 86  HOH HOH A . 
H 7 HOH 15  415 54  HOH HOH A . 
H 7 HOH 16  416 179 HOH HOH A . 
H 7 HOH 17  417 55  HOH HOH A . 
H 7 HOH 18  418 56  HOH HOH A . 
H 7 HOH 19  419 215 HOH HOH A . 
H 7 HOH 20  420 131 HOH HOH A . 
H 7 HOH 21  421 18  HOH HOH A . 
H 7 HOH 22  422 52  HOH HOH A . 
H 7 HOH 23  423 134 HOH HOH A . 
H 7 HOH 24  424 75  HOH HOH A . 
H 7 HOH 25  425 5   HOH HOH A . 
H 7 HOH 26  426 177 HOH HOH A . 
H 7 HOH 27  427 111 HOH HOH A . 
H 7 HOH 28  428 116 HOH HOH A . 
H 7 HOH 29  429 46  HOH HOH A . 
H 7 HOH 30  430 43  HOH HOH A . 
H 7 HOH 31  431 200 HOH HOH A . 
H 7 HOH 32  432 205 HOH HOH A . 
H 7 HOH 33  433 31  HOH HOH A . 
H 7 HOH 34  434 107 HOH HOH A . 
H 7 HOH 35  435 159 HOH HOH A . 
H 7 HOH 36  436 202 HOH HOH A . 
H 7 HOH 37  437 79  HOH HOH A . 
H 7 HOH 38  438 22  HOH HOH A . 
H 7 HOH 39  439 105 HOH HOH A . 
H 7 HOH 40  440 122 HOH HOH A . 
H 7 HOH 41  441 38  HOH HOH A . 
H 7 HOH 42  442 11  HOH HOH A . 
H 7 HOH 43  443 81  HOH HOH A . 
H 7 HOH 44  444 114 HOH HOH A . 
H 7 HOH 45  445 133 HOH HOH A . 
H 7 HOH 46  446 149 HOH HOH A . 
H 7 HOH 47  447 3   HOH HOH A . 
H 7 HOH 48  448 44  HOH HOH A . 
H 7 HOH 49  449 165 HOH HOH A . 
H 7 HOH 50  450 175 HOH HOH A . 
H 7 HOH 51  451 64  HOH HOH A . 
H 7 HOH 52  452 50  HOH HOH A . 
H 7 HOH 53  453 206 HOH HOH A . 
H 7 HOH 54  454 6   HOH HOH A . 
H 7 HOH 55  455 84  HOH HOH A . 
H 7 HOH 56  456 181 HOH HOH A . 
H 7 HOH 57  457 24  HOH HOH A . 
H 7 HOH 58  458 4   HOH HOH A . 
H 7 HOH 59  459 167 HOH HOH A . 
H 7 HOH 60  460 110 HOH HOH A . 
H 7 HOH 61  461 176 HOH HOH A . 
H 7 HOH 62  462 201 HOH HOH A . 
H 7 HOH 63  463 88  HOH HOH A . 
H 7 HOH 64  464 40  HOH HOH A . 
H 7 HOH 65  465 108 HOH HOH A . 
H 7 HOH 66  466 71  HOH HOH A . 
H 7 HOH 67  467 15  HOH HOH A . 
H 7 HOH 68  468 63  HOH HOH A . 
H 7 HOH 69  469 32  HOH HOH A . 
H 7 HOH 70  470 1   HOH HOH A . 
H 7 HOH 71  471 9   HOH HOH A . 
H 7 HOH 72  472 12  HOH HOH A . 
H 7 HOH 73  473 28  HOH HOH A . 
H 7 HOH 74  474 118 HOH HOH A . 
H 7 HOH 75  475 162 HOH HOH A . 
H 7 HOH 76  476 2   HOH HOH A . 
H 7 HOH 77  477 45  HOH HOH A . 
H 7 HOH 78  478 42  HOH HOH A . 
H 7 HOH 79  479 189 HOH HOH A . 
H 7 HOH 80  480 74  HOH HOH A . 
H 7 HOH 81  481 94  HOH HOH A . 
H 7 HOH 82  482 29  HOH HOH A . 
H 7 HOH 83  483 7   HOH HOH A . 
H 7 HOH 84  484 204 HOH HOH A . 
H 7 HOH 85  485 187 HOH HOH A . 
H 7 HOH 86  486 26  HOH HOH A . 
H 7 HOH 87  487 80  HOH HOH A . 
H 7 HOH 88  488 30  HOH HOH A . 
H 7 HOH 89  489 10  HOH HOH A . 
H 7 HOH 90  490 207 HOH HOH A . 
H 7 HOH 91  491 13  HOH HOH A . 
H 7 HOH 92  492 70  HOH HOH A . 
H 7 HOH 93  493 8   HOH HOH A . 
H 7 HOH 94  494 19  HOH HOH A . 
H 7 HOH 95  495 96  HOH HOH A . 
H 7 HOH 96  496 76  HOH HOH A . 
H 7 HOH 97  497 69  HOH HOH A . 
H 7 HOH 98  498 35  HOH HOH A . 
H 7 HOH 99  499 37  HOH HOH A . 
H 7 HOH 100 500 23  HOH HOH A . 
H 7 HOH 101 501 112 HOH HOH A . 
H 7 HOH 102 502 113 HOH HOH A . 
H 7 HOH 103 503 39  HOH HOH A . 
H 7 HOH 104 504 197 HOH HOH A . 
H 7 HOH 105 505 123 HOH HOH A . 
H 7 HOH 106 506 73  HOH HOH A . 
H 7 HOH 107 507 145 HOH HOH A . 
H 7 HOH 108 508 160 HOH HOH A . 
H 7 HOH 109 509 14  HOH HOH A . 
H 7 HOH 110 510 169 HOH HOH A . 
H 7 HOH 111 511 147 HOH HOH A . 
H 7 HOH 112 512 25  HOH HOH A . 
H 7 HOH 113 513 21  HOH HOH A . 
H 7 HOH 114 514 144 HOH HOH A . 
H 7 HOH 115 515 60  HOH HOH A . 
H 7 HOH 116 516 82  HOH HOH A . 
H 7 HOH 117 517 190 HOH HOH A . 
H 7 HOH 118 518 143 HOH HOH A . 
H 7 HOH 119 519 66  HOH HOH A . 
H 7 HOH 120 520 157 HOH HOH A . 
H 7 HOH 121 521 59  HOH HOH A . 
H 7 HOH 122 522 98  HOH HOH A . 
H 7 HOH 123 523 158 HOH HOH A . 
H 7 HOH 124 524 87  HOH HOH A . 
H 7 HOH 125 525 125 HOH HOH A . 
H 7 HOH 126 526 77  HOH HOH A . 
H 7 HOH 127 527 65  HOH HOH A . 
H 7 HOH 128 528 16  HOH HOH A . 
H 7 HOH 129 529 120 HOH HOH A . 
H 7 HOH 130 530 117 HOH HOH A . 
H 7 HOH 131 531 188 HOH HOH A . 
H 7 HOH 132 532 47  HOH HOH A . 
H 7 HOH 133 533 164 HOH HOH A . 
H 7 HOH 134 534 72  HOH HOH A . 
H 7 HOH 135 535 130 HOH HOH A . 
H 7 HOH 136 536 83  HOH HOH A . 
H 7 HOH 137 537 92  HOH HOH A . 
H 7 HOH 138 538 61  HOH HOH A . 
H 7 HOH 139 539 156 HOH HOH A . 
H 7 HOH 140 540 20  HOH HOH A . 
H 7 HOH 141 541 184 HOH HOH A . 
H 7 HOH 142 542 139 HOH HOH A . 
H 7 HOH 143 543 180 HOH HOH A . 
H 7 HOH 144 544 89  HOH HOH A . 
H 7 HOH 145 545 101 HOH HOH A . 
H 7 HOH 146 546 99  HOH HOH A . 
H 7 HOH 147 547 36  HOH HOH A . 
H 7 HOH 148 548 51  HOH HOH A . 
H 7 HOH 149 549 49  HOH HOH A . 
H 7 HOH 150 550 85  HOH HOH A . 
H 7 HOH 151 551 33  HOH HOH A . 
H 7 HOH 152 552 34  HOH HOH A . 
H 7 HOH 153 553 104 HOH HOH A . 
H 7 HOH 154 554 100 HOH HOH A . 
H 7 HOH 155 555 132 HOH HOH A . 
H 7 HOH 156 556 27  HOH HOH A . 
H 7 HOH 157 557 217 HOH HOH A . 
H 7 HOH 158 558 103 HOH HOH A . 
H 7 HOH 159 559 191 HOH HOH A . 
H 7 HOH 160 560 213 HOH HOH A . 
H 7 HOH 161 561 41  HOH HOH A . 
H 7 HOH 162 562 91  HOH HOH A . 
H 7 HOH 163 563 102 HOH HOH A . 
H 7 HOH 164 564 138 HOH HOH A . 
H 7 HOH 165 565 141 HOH HOH A . 
H 7 HOH 166 566 78  HOH HOH A . 
H 7 HOH 167 567 57  HOH HOH A . 
H 7 HOH 168 568 109 HOH HOH A . 
H 7 HOH 169 569 186 HOH HOH A . 
H 7 HOH 170 570 208 HOH HOH A . 
H 7 HOH 171 571 58  HOH HOH A . 
H 7 HOH 172 572 90  HOH HOH A . 
H 7 HOH 173 573 170 HOH HOH A . 
H 7 HOH 174 574 195 HOH HOH A . 
H 7 HOH 175 575 150 HOH HOH A . 
H 7 HOH 176 576 166 HOH HOH A . 
H 7 HOH 177 577 53  HOH HOH A . 
H 7 HOH 178 578 140 HOH HOH A . 
H 7 HOH 179 579 168 HOH HOH A . 
H 7 HOH 180 580 214 HOH HOH A . 
H 7 HOH 181 581 146 HOH HOH A . 
H 7 HOH 182 582 163 HOH HOH A . 
H 7 HOH 183 583 124 HOH HOH A . 
H 7 HOH 184 584 152 HOH HOH A . 
H 7 HOH 185 585 161 HOH HOH A . 
H 7 HOH 186 586 212 HOH HOH A . 
H 7 HOH 187 587 216 HOH HOH A . 
H 7 HOH 188 588 171 HOH HOH A . 
H 7 HOH 189 589 183 HOH HOH A . 
H 7 HOH 190 590 136 HOH HOH A . 
H 7 HOH 191 591 218 HOH HOH A . 
H 7 HOH 192 592 209 HOH HOH A . 
H 7 HOH 193 593 154 HOH HOH A . 
H 7 HOH 194 594 68  HOH HOH A . 
H 7 HOH 195 595 93  HOH HOH A . 
H 7 HOH 196 596 97  HOH HOH A . 
H 7 HOH 197 597 106 HOH HOH A . 
H 7 HOH 198 598 198 HOH HOH A . 
H 7 HOH 199 599 155 HOH HOH A . 
H 7 HOH 200 600 194 HOH HOH A . 
H 7 HOH 201 601 151 HOH HOH A . 
H 7 HOH 202 602 178 HOH HOH A . 
H 7 HOH 203 603 142 HOH HOH A . 
H 7 HOH 204 604 127 HOH HOH A . 
H 7 HOH 205 605 211 HOH HOH A . 
H 7 HOH 206 606 137 HOH HOH A . 
H 7 HOH 207 607 182 HOH HOH A . 
H 7 HOH 208 608 121 HOH HOH A . 
H 7 HOH 209 609 193 HOH HOH A . 
H 7 HOH 210 610 129 HOH HOH A . 
H 7 HOH 211 611 148 HOH HOH A . 
H 7 HOH 212 612 128 HOH HOH A . 
H 7 HOH 213 613 48  HOH HOH A . 
H 7 HOH 214 614 135 HOH HOH A . 
H 7 HOH 215 615 153 HOH HOH A . 
H 7 HOH 216 616 174 HOH HOH A . 
H 7 HOH 217 617 173 HOH HOH A . 
H 7 HOH 218 618 95  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
3  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
4  1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
5  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
6  1 Y 1 A LYS 133 ? CE  ? A LYS 132 CE  
7  1 Y 1 A LYS 133 ? NZ  ? A LYS 132 NZ  
8  1 Y 1 A LYS 172 ? CE  ? A LYS 171 CE  
9  1 Y 1 A LYS 172 ? NZ  ? A LYS 171 NZ  
10 1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
11 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
12 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
13 1 N 1 A MES 303 ? S   ? D MES 1   S   
14 1 N 1 A MES 303 ? O1S ? D MES 1   O1S 
15 1 N 1 A MES 303 ? O2S ? D MES 1   O2S 
16 1 N 1 A MES 303 ? O3S ? D MES 1   O3S 
# 
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 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.006    1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? .        2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .        3 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5EHE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.200 
_cell.length_a_esd                 ? 
_cell.length_b                     41.026 
_cell.length_b_esd                 ? 
_cell.length_c                     71.950 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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             ? 
# 
_symmetry.entry_id                         5EHE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   5EHE 
_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            2.01 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         38.5 
_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_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'Crystallization buffer contains 0.1M sodium bicine (pH 9) and 2.6M sodium malonate (pH 7.5)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_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_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MAR CCD 165 mm' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2011-11-20 
# 
_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   0.8123 
_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                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8123 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X13 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
# 
_reflns.B_iso_Wilson_estimate            14.855 
_reflns.entry_id                         5EHE 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.405 
_reflns.d_resolution_low                 20.511 
_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                       37863 
_reflns.number_obs                       37863 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             98.500 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  5.200 
_reflns.pdbx_Rmerge_I_obs                0.067 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.067 
_reflns.pdbx_netI_over_av_sigmaI         7.227 
_reflns.pdbx_netI_over_sigmaI            20.200 
_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                  0.082 
_reflns.pdbx_Rpim_I_all                  0.036 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         198008 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_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_Rsym_value 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.50 1.58  ? 2.7  28955 ? ? 5460 ? 97.70 ? ? ? 0.301 0.247 ? ? ? ? ? ? ? ? 5.30 0.247 ? ? 4.30  0.30 0.13 ? 1  1 ? ? 
1.58 1.68  ? 3.5  27324 ? ? 5173 ? 98.10 ? ? ? 0.228 0.189 ? ? ? ? ? ? ? ? 5.30 0.189 ? ? 6.40  0.23 0.10 ? 2  ? ? ? 
1.68 1.79  ? 4.8  25735 ? ? 4863 ? 98.30 ? ? ? 0.171 0.141 ? ? ? ? ? ? ? ? 5.30 0.141 ? ? 9.70  0.17 0.07 ? 3  ? ? ? 
1.79 1.94  ? 6.2  24103 ? ? 4560 ? 98.60 ? ? ? 0.131 0.108 ? ? ? ? ? ? ? ? 5.30 0.108 ? ? 15.60 0.13 0.06 ? 4  ? ? ? 
1.94 2.12  ? 7.9  22214 ? ? 4222 ? 98.90 ? ? ? 0.104 0.083 ? ? ? ? ? ? ? ? 5.30 0.083 ? ? 22.80 0.10 0.04 ? 5  ? ? ? 
2.12 2.37  ? 9.3  20150 ? ? 3826 ? 99.10 ? ? ? 0.088 0.070 ? ? ? ? ? ? ? ? 5.30 0.070 ? ? 29.00 0.09 0.04 ? 6  ? ? ? 
2.37 2.74  ? 10.8 17870 ? ? 3397 ? 99.30 ? ? ? 0.075 0.060 ? ? ? ? ? ? ? ? 5.30 0.060 ? ? 33.10 0.08 0.03 ? 7  ? ? ? 
2.74 3.35  ? 11.8 14996 ? ? 2880 ? 99.50 ? ? ? 0.064 0.051 ? ? ? ? ? ? ? ? 5.20 0.051 ? ? 39.50 0.06 0.03 ? 8  ? ? ? 
3.35 4.74  ? 13.0 11229 ? ? 2257 ? 99.30 ? ? ? 0.058 0.047 ? ? ? ? ? ? ? ? 5.00 0.047 ? ? 45.40 0.06 0.03 ? 9  ? ? ? 
4.74 20.51 ? 13.0 5432  ? ? 1225 ? 95.70 ? ? ? 0.060 0.049 ? ? ? ? ? ? ? ? 4.40 0.049 ? ? 42.90 0.06 0.03 ? 10 ? ? ? 
# 
_refine.aniso_B[1][1]                            0.340 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.050 
_refine.aniso_B[2][2]                            -0.870 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.560 
_refine.B_iso_max                                62.54 
_refine.B_iso_mean                               16.823 
_refine.B_iso_min                                5.03 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_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                                 5EHE 
_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                            1.500 
_refine.ls_d_res_low                             19.890 
_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                     37850 
_refine.ls_number_reflns_R_free                  3808 
_refine.ls_number_reflns_R_work                  34042 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.210 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.183 
_refine.ls_R_factor_R_free                       0.211 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.180 
_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                      0.210 
_refine.ls_wR_factor_R_work                      0.179 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          0.00 
_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                      3HLJ 
_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                       0.088 
_refine.pdbx_overall_ESU_R_Free                  0.087 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.088 
_refine.overall_SU_R_free                        0.087 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   0.871 
_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.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             218 
_refine_hist.number_atoms_total               2318 
_refine_hist.d_res_high                       1.500 
_refine_hist.d_res_low                        19.890 
# 
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' ? 0.024  0.020  2250 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.302  1.966  3071 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.709  5.000  279  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 35.394 24.804 102  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.813 15.000 359  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 16.745 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.173  0.200  316  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.021  1760 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.500 
_refine_ls_shell.d_res_low                        1.539 
_refine_ls_shell.number_reflns_all                2755 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             269 
_refine_ls_shell.number_reflns_R_work             2486 
_refine_ls_shell.percent_reflns_obs               97.380 
_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                  0.309 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.283 
_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_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     5EHE 
_struct.title                        
;Crystal structure of human carbonic anhydrase isozyme II with 3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5EHE 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 5 ? 
F N N 3 ? 
G N N 6 ? 
H N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              5EHE 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 1090  ? 
1 MORE         16    ? 
1 'SSA (A^2)'  11310 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            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 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_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 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 G WWO . N10 ? ? A ZN  301 A WWO 306 1_555 ? ? ? ? ? ? ? 1.814 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 105.3 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 113.3 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.5  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? G WWO .   ? A WWO 306 ? 1_555 101.5 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? G WWO .   ? A WWO 306 ? 1_555 121.3 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? G WWO .   ? A WWO 306 ? 1_555 116.9 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -2.53 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 13.01 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A DMS 302 ? 3  'binding site for residue DMS A 302' 
AC3 Software A MES 303 ? 5  'binding site for residue MES A 303' 
AC4 Software A PEG 304 ? 7  'binding site for residue PEG A 304' 
AC5 Software A DMS 305 ? 5  'binding site for residue DMS A 305' 
AC6 Software A WWO 306 ? 16 'binding site for residue WWO A 306' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  WWO G .   ? WWO A 306 . ? 1_555 ? 
5  AC2 3  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC3 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
9  AC3 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
10 AC3 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
11 AC3 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
12 AC3 5  HOH H .   ? HOH A 504 . ? 1_555 ? 
13 AC4 7  PRO A 13  ? PRO A 13  . ? 1_555 ? 
14 AC4 7  GLU A 14  ? GLU A 14  . ? 1_555 ? 
15 AC4 7  TRP A 16  ? TRP A 16  . ? 1_555 ? 
16 AC4 7  HIS A 17  ? HIS A 17  . ? 1_555 ? 
17 AC4 7  LYS A 24  ? LYS A 24  . ? 1_555 ? 
18 AC4 7  GLN A 248 ? GLN A 249 . ? 1_555 ? 
19 AC4 7  HOH H .   ? HOH A 425 . ? 1_555 ? 
20 AC5 5  LYS A 153 ? LYS A 154 . ? 1_555 ? 
21 AC5 5  ILE A 215 ? ILE A 216 . ? 1_555 ? 
22 AC5 5  SER A 216 ? SER A 217 . ? 1_555 ? 
23 AC5 5  HOH H .   ? HOH A 415 . ? 1_555 ? 
24 AC5 5  HOH H .   ? HOH A 440 . ? 1_555 ? 
25 AC6 16 ILE A 91  ? ILE A 91  . ? 1_555 ? 
26 AC6 16 GLN A 92  ? GLN A 92  . ? 1_555 ? 
27 AC6 16 HIS A 94  ? HIS A 94  . ? 1_555 ? 
28 AC6 16 HIS A 96  ? HIS A 96  . ? 1_555 ? 
29 AC6 16 HIS A 119 ? HIS A 119 . ? 1_555 ? 
30 AC6 16 VAL A 121 ? VAL A 121 . ? 1_555 ? 
31 AC6 16 PHE A 130 ? PHE A 131 . ? 1_555 ? 
32 AC6 16 LEU A 197 ? LEU A 198 . ? 1_555 ? 
33 AC6 16 THR A 198 ? THR A 199 . ? 1_555 ? 
34 AC6 16 THR A 199 ? THR A 200 . ? 1_555 ? 
35 AC6 16 PRO A 200 ? PRO A 201 . ? 1_555 ? 
36 AC6 16 PRO A 201 ? PRO A 202 . ? 1_555 ? 
37 AC6 16 TRP A 208 ? TRP A 209 . ? 1_555 ? 
38 AC6 16 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
39 AC6 16 HOH H .   ? HOH A 510 . ? 1_555 ? 
40 AC6 16 HOH H .   ? HOH A 579 . ? 1_555 ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NE2 A GLN 92  ? A C14 A WWO 306 ? ? 2.07 
2 1 NZ  A LYS 111 ? ? O   A HOH 401 ? ? 2.07 
3 1 OG  A SER 217 ? B O   A HOH 402 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A HIS 4   ? ? CD2 A HIS 4   ? ? 1.425 1.354 0.071 0.009 N 
2 1 CG A HIS 122 ? ? CD2 A HIS 122 ? ? 1.418 1.354 0.064 0.009 N 
# 
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 ASN A 11  ? ? -141.79 17.05   
2 1 ARG A 27  ? ? -144.92 58.95   
3 1 LYS A 76  ? B -87.30  -77.14  
4 1 LYS A 170 ? ? -38.56  125.90  
5 1 PHE A 176 ? ? -152.73 79.74   
6 1 ASN A 244 ? ? -97.88  51.41   
7 1 LYS A 252 ? ? 62.26   -139.69 
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
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  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MES O1   O  N N 240 
MES C2   C  N N 241 
MES C3   C  N N 242 
MES N4   N  N N 243 
MES C5   C  N N 244 
MES C6   C  N N 245 
MES C7   C  N N 246 
MES C8   C  N N 247 
MES S    S  N N 248 
MES O1S  O  N N 249 
MES O2S  O  N N 250 
MES O3S  O  N N 251 
MES H21  H  N N 252 
MES H22  H  N N 253 
MES H31  H  N N 254 
MES H32  H  N N 255 
MES HN4  H  N N 256 
MES H51  H  N N 257 
MES H52  H  N N 258 
MES H61  H  N N 259 
MES H62  H  N N 260 
MES H71  H  N N 261 
MES H72  H  N N 262 
MES H81  H  N N 263 
MES H82  H  N N 264 
MET N    N  N N 265 
MET CA   C  N S 266 
MET C    C  N N 267 
MET O    O  N N 268 
MET CB   C  N N 269 
MET CG   C  N N 270 
MET SD   S  N N 271 
MET CE   C  N N 272 
MET OXT  O  N N 273 
MET H    H  N N 274 
MET H2   H  N N 275 
MET HA   H  N N 276 
MET HB2  H  N N 277 
MET HB3  H  N N 278 
MET HG2  H  N N 279 
MET HG3  H  N N 280 
MET HE1  H  N N 281 
MET HE2  H  N N 282 
MET HE3  H  N N 283 
MET HXT  H  N N 284 
PEG C1   C  N N 285 
PEG O1   O  N N 286 
PEG C2   C  N N 287 
PEG O2   O  N N 288 
PEG C3   C  N N 289 
PEG C4   C  N N 290 
PEG O4   O  N N 291 
PEG H11  H  N N 292 
PEG H12  H  N N 293 
PEG HO1  H  N N 294 
PEG H21  H  N N 295 
PEG H22  H  N N 296 
PEG H31  H  N N 297 
PEG H32  H  N N 298 
PEG H41  H  N N 299 
PEG H42  H  N N 300 
PEG HO4  H  N N 301 
PHE N    N  N N 302 
PHE CA   C  N S 303 
PHE C    C  N N 304 
PHE O    O  N N 305 
PHE CB   C  N N 306 
PHE CG   C  Y N 307 
PHE CD1  C  Y N 308 
PHE CD2  C  Y N 309 
PHE CE1  C  Y N 310 
PHE CE2  C  Y N 311 
PHE CZ   C  Y N 312 
PHE OXT  O  N N 313 
PHE H    H  N N 314 
PHE H2   H  N N 315 
PHE HA   H  N N 316 
PHE HB2  H  N N 317 
PHE HB3  H  N N 318 
PHE HD1  H  N N 319 
PHE HD2  H  N N 320 
PHE HE1  H  N N 321 
PHE HE2  H  N N 322 
PHE HZ   H  N N 323 
PHE HXT  H  N N 324 
PRO N    N  N N 325 
PRO CA   C  N S 326 
PRO C    C  N N 327 
PRO O    O  N N 328 
PRO CB   C  N N 329 
PRO CG   C  N N 330 
PRO CD   C  N N 331 
PRO OXT  O  N N 332 
PRO H    H  N N 333 
PRO HA   H  N N 334 
PRO HB2  H  N N 335 
PRO HB3  H  N N 336 
PRO HG2  H  N N 337 
PRO HG3  H  N N 338 
PRO HD2  H  N N 339 
PRO HD3  H  N N 340 
PRO HXT  H  N N 341 
SER N    N  N N 342 
SER CA   C  N S 343 
SER C    C  N N 344 
SER O    O  N N 345 
SER CB   C  N N 346 
SER OG   O  N N 347 
SER OXT  O  N N 348 
SER H    H  N N 349 
SER H2   H  N N 350 
SER HA   H  N N 351 
SER HB2  H  N N 352 
SER HB3  H  N N 353 
SER HG   H  N N 354 
SER HXT  H  N N 355 
THR N    N  N N 356 
THR CA   C  N S 357 
THR C    C  N N 358 
THR O    O  N N 359 
THR CB   C  N R 360 
THR OG1  O  N N 361 
THR CG2  C  N N 362 
THR OXT  O  N N 363 
THR H    H  N N 364 
THR H2   H  N N 365 
THR HA   H  N N 366 
THR HB   H  N N 367 
THR HG1  H  N N 368 
THR HG21 H  N N 369 
THR HG22 H  N N 370 
THR HG23 H  N N 371 
THR HXT  H  N N 372 
TRP N    N  N N 373 
TRP CA   C  N S 374 
TRP C    C  N N 375 
TRP O    O  N N 376 
TRP CB   C  N N 377 
TRP CG   C  Y N 378 
TRP CD1  C  Y N 379 
TRP CD2  C  Y N 380 
TRP NE1  N  Y N 381 
TRP CE2  C  Y N 382 
TRP CE3  C  Y N 383 
TRP CZ2  C  Y N 384 
TRP CZ3  C  Y N 385 
TRP CH2  C  Y N 386 
TRP OXT  O  N N 387 
TRP H    H  N N 388 
TRP H2   H  N N 389 
TRP HA   H  N N 390 
TRP HB2  H  N N 391 
TRP HB3  H  N N 392 
TRP HD1  H  N N 393 
TRP HE1  H  N N 394 
TRP HE3  H  N N 395 
TRP HZ2  H  N N 396 
TRP HZ3  H  N N 397 
TRP HH2  H  N N 398 
TRP HXT  H  N N 399 
TYR N    N  N N 400 
TYR CA   C  N S 401 
TYR C    C  N N 402 
TYR O    O  N N 403 
TYR CB   C  N N 404 
TYR CG   C  Y N 405 
TYR CD1  C  Y N 406 
TYR CD2  C  Y N 407 
TYR CE1  C  Y N 408 
TYR CE2  C  Y N 409 
TYR CZ   C  Y N 410 
TYR OH   O  N N 411 
TYR OXT  O  N N 412 
TYR H    H  N N 413 
TYR H2   H  N N 414 
TYR HA   H  N N 415 
TYR HB2  H  N N 416 
TYR HB3  H  N N 417 
TYR HD1  H  N N 418 
TYR HD2  H  N N 419 
TYR HE1  H  N N 420 
TYR HE2  H  N N 421 
TYR HH   H  N N 422 
TYR HXT  H  N N 423 
VAL N    N  N N 424 
VAL CA   C  N S 425 
VAL C    C  N N 426 
VAL O    O  N N 427 
VAL CB   C  N N 428 
VAL CG1  C  N N 429 
VAL CG2  C  N N 430 
VAL OXT  O  N N 431 
VAL H    H  N N 432 
VAL H2   H  N N 433 
VAL HA   H  N N 434 
VAL HB   H  N N 435 
VAL HG11 H  N N 436 
VAL HG12 H  N N 437 
VAL HG13 H  N N 438 
VAL HG21 H  N N 439 
VAL HG22 H  N N 440 
VAL HG23 H  N N 441 
VAL HXT  H  N N 442 
WWO F27  F  N N 443 
WWO C5   C  Y N 444 
WWO C4   C  Y N 445 
WWO S7   S  N N 446 
WWO O9   O  N N 447 
WWO N10  N  N N 448 
WWO O8   O  N N 449 
WWO C3   C  Y N 450 
WWO F12  F  N N 451 
WWO C2   C  Y N 452 
WWO F13  F  N N 453 
WWO C6   C  Y N 454 
WWO C1   C  Y N 455 
WWO S11  S  N N 456 
WWO O22  O  N N 457 
WWO O23  O  N N 458 
WWO C21  C  N N 459 
WWO C24  C  N N 460 
WWO O25  O  N N 461 
WWO N26  N  N N 462 
WWO C14  C  N N 463 
WWO C15  C  Y N 464 
WWO C20  C  Y N 465 
WWO C19  C  Y N 466 
WWO C18  C  Y N 467 
WWO C17  C  Y N 468 
WWO C16  C  Y N 469 
WWO H1   H  N N 470 
WWO H2   H  N N 471 
WWO H3   H  N N 472 
WWO H4   H  N N 473 
WWO H5   H  N N 474 
WWO H6   H  N N 475 
WWO H7   H  N N 476 
WWO H8   H  N N 477 
WWO H9   H  N N 478 
WWO H10  H  N N 479 
WWO H11  H  N N 480 
WWO H12  H  N N 481 
WWO H13  H  N N 482 
WWO H14  H  N N 483 
WWO H15  H  N N 484 
ZN  ZN   ZN N N 485 
# 
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  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MES O1  C2   sing N N 227 
MES O1  C6   sing N N 228 
MES C2  C3   sing N N 229 
MES C2  H21  sing N N 230 
MES C2  H22  sing N N 231 
MES C3  N4   sing N N 232 
MES C3  H31  sing N N 233 
MES C3  H32  sing N N 234 
MES N4  C5   sing N N 235 
MES N4  C7   sing N N 236 
MES N4  HN4  sing N N 237 
MES C5  C6   sing N N 238 
MES C5  H51  sing N N 239 
MES C5  H52  sing N N 240 
MES C6  H61  sing N N 241 
MES C6  H62  sing N N 242 
MES C7  C8   sing N N 243 
MES C7  H71  sing N N 244 
MES C7  H72  sing N N 245 
MES C8  S    sing N N 246 
MES C8  H81  sing N N 247 
MES C8  H82  sing N N 248 
MES S   O1S  doub N N 249 
MES S   O2S  doub N N 250 
MES S   O3S  sing N N 251 
MET N   CA   sing N N 252 
MET N   H    sing N N 253 
MET N   H2   sing N N 254 
MET CA  C    sing N N 255 
MET CA  CB   sing N N 256 
MET CA  HA   sing N N 257 
MET C   O    doub N N 258 
MET C   OXT  sing N N 259 
MET CB  CG   sing N N 260 
MET CB  HB2  sing N N 261 
MET CB  HB3  sing N N 262 
MET CG  SD   sing N N 263 
MET CG  HG2  sing N N 264 
MET CG  HG3  sing N N 265 
MET SD  CE   sing N N 266 
MET CE  HE1  sing N N 267 
MET CE  HE2  sing N N 268 
MET CE  HE3  sing N N 269 
MET OXT HXT  sing N N 270 
PEG C1  O1   sing N N 271 
PEG C1  C2   sing N N 272 
PEG C1  H11  sing N N 273 
PEG C1  H12  sing N N 274 
PEG O1  HO1  sing N N 275 
PEG C2  O2   sing N N 276 
PEG C2  H21  sing N N 277 
PEG C2  H22  sing N N 278 
PEG O2  C3   sing N N 279 
PEG C3  C4   sing N N 280 
PEG C3  H31  sing N N 281 
PEG C3  H32  sing N N 282 
PEG C4  O4   sing N N 283 
PEG C4  H41  sing N N 284 
PEG C4  H42  sing N N 285 
PEG O4  HO4  sing N N 286 
PHE N   CA   sing N N 287 
PHE N   H    sing N N 288 
PHE N   H2   sing N N 289 
PHE CA  C    sing N N 290 
PHE CA  CB   sing N N 291 
PHE CA  HA   sing N N 292 
PHE C   O    doub N N 293 
PHE C   OXT  sing N N 294 
PHE CB  CG   sing N N 295 
PHE CB  HB2  sing N N 296 
PHE CB  HB3  sing N N 297 
PHE CG  CD1  doub Y N 298 
PHE CG  CD2  sing Y N 299 
PHE CD1 CE1  sing Y N 300 
PHE CD1 HD1  sing N N 301 
PHE CD2 CE2  doub Y N 302 
PHE CD2 HD2  sing N N 303 
PHE CE1 CZ   doub Y N 304 
PHE CE1 HE1  sing N N 305 
PHE CE2 CZ   sing Y N 306 
PHE CE2 HE2  sing N N 307 
PHE CZ  HZ   sing N N 308 
PHE OXT HXT  sing N N 309 
PRO N   CA   sing N N 310 
PRO N   CD   sing N N 311 
PRO N   H    sing N N 312 
PRO CA  C    sing N N 313 
PRO CA  CB   sing N N 314 
PRO CA  HA   sing N N 315 
PRO C   O    doub N N 316 
PRO C   OXT  sing N N 317 
PRO CB  CG   sing N N 318 
PRO CB  HB2  sing N N 319 
PRO CB  HB3  sing N N 320 
PRO CG  CD   sing N N 321 
PRO CG  HG2  sing N N 322 
PRO CG  HG3  sing N N 323 
PRO CD  HD2  sing N N 324 
PRO CD  HD3  sing N N 325 
PRO OXT HXT  sing N N 326 
SER N   CA   sing N N 327 
SER N   H    sing N N 328 
SER N   H2   sing N N 329 
SER CA  C    sing N N 330 
SER CA  CB   sing N N 331 
SER CA  HA   sing N N 332 
SER C   O    doub N N 333 
SER C   OXT  sing N N 334 
SER CB  OG   sing N N 335 
SER CB  HB2  sing N N 336 
SER CB  HB3  sing N N 337 
SER OG  HG   sing N N 338 
SER OXT HXT  sing N N 339 
THR N   CA   sing N N 340 
THR N   H    sing N N 341 
THR N   H2   sing N N 342 
THR CA  C    sing N N 343 
THR CA  CB   sing N N 344 
THR CA  HA   sing N N 345 
THR C   O    doub N N 346 
THR C   OXT  sing N N 347 
THR CB  OG1  sing N N 348 
THR CB  CG2  sing N N 349 
THR CB  HB   sing N N 350 
THR OG1 HG1  sing N N 351 
THR CG2 HG21 sing N N 352 
THR CG2 HG22 sing N N 353 
THR CG2 HG23 sing N N 354 
THR OXT HXT  sing N N 355 
TRP N   CA   sing N N 356 
TRP N   H    sing N N 357 
TRP N   H2   sing N N 358 
TRP CA  C    sing N N 359 
TRP CA  CB   sing N N 360 
TRP CA  HA   sing N N 361 
TRP C   O    doub N N 362 
TRP C   OXT  sing N N 363 
TRP CB  CG   sing N N 364 
TRP CB  HB2  sing N N 365 
TRP CB  HB3  sing N N 366 
TRP CG  CD1  doub Y N 367 
TRP CG  CD2  sing Y N 368 
TRP CD1 NE1  sing Y N 369 
TRP CD1 HD1  sing N N 370 
TRP CD2 CE2  doub Y N 371 
TRP CD2 CE3  sing Y N 372 
TRP NE1 CE2  sing Y N 373 
TRP NE1 HE1  sing N N 374 
TRP CE2 CZ2  sing Y N 375 
TRP CE3 CZ3  doub Y N 376 
TRP CE3 HE3  sing N N 377 
TRP CZ2 CH2  doub Y N 378 
TRP CZ2 HZ2  sing N N 379 
TRP CZ3 CH2  sing Y N 380 
TRP CZ3 HZ3  sing N N 381 
TRP CH2 HH2  sing N N 382 
TRP OXT HXT  sing N N 383 
TYR N   CA   sing N N 384 
TYR N   H    sing N N 385 
TYR N   H2   sing N N 386 
TYR CA  C    sing N N 387 
TYR CA  CB   sing N N 388 
TYR CA  HA   sing N N 389 
TYR C   O    doub N N 390 
TYR C   OXT  sing N N 391 
TYR CB  CG   sing N N 392 
TYR CB  HB2  sing N N 393 
TYR CB  HB3  sing N N 394 
TYR CG  CD1  doub Y N 395 
TYR CG  CD2  sing Y N 396 
TYR CD1 CE1  sing Y N 397 
TYR CD1 HD1  sing N N 398 
TYR CD2 CE2  doub Y N 399 
TYR CD2 HD2  sing N N 400 
TYR CE1 CZ   doub Y N 401 
TYR CE1 HE1  sing N N 402 
TYR CE2 CZ   sing Y N 403 
TYR CE2 HE2  sing N N 404 
TYR CZ  OH   sing N N 405 
TYR OH  HH   sing N N 406 
TYR OXT HXT  sing N N 407 
VAL N   CA   sing N N 408 
VAL N   H    sing N N 409 
VAL N   H2   sing N N 410 
VAL CA  C    sing N N 411 
VAL CA  CB   sing N N 412 
VAL CA  HA   sing N N 413 
VAL C   O    doub N N 414 
VAL C   OXT  sing N N 415 
VAL CB  CG1  sing N N 416 
VAL CB  CG2  sing N N 417 
VAL CB  HB   sing N N 418 
VAL CG1 HG11 sing N N 419 
VAL CG1 HG12 sing N N 420 
VAL CG1 HG13 sing N N 421 
VAL CG2 HG21 sing N N 422 
VAL CG2 HG22 sing N N 423 
VAL CG2 HG23 sing N N 424 
VAL OXT HXT  sing N N 425 
WWO O9  S7   doub N N 426 
WWO S7  N10  sing N N 427 
WWO S7  C4   sing N N 428 
WWO S7  O8   doub N N 429 
WWO C16 C17  doub Y N 430 
WWO C16 C15  sing Y N 431 
WWO F27 C5   sing N N 432 
WWO C17 C18  sing Y N 433 
WWO C14 C15  sing N N 434 
WWO C14 N26  sing N N 435 
WWO C4  C5   doub Y N 436 
WWO C4  C3   sing Y N 437 
WWO C5  C6   sing Y N 438 
WWO C15 C20  doub Y N 439 
WWO C3  F12  sing N N 440 
WWO C3  C2   doub Y N 441 
WWO C6  N26  sing N N 442 
WWO C6  C1   doub Y N 443 
WWO O23 S11  doub N N 444 
WWO C18 C19  doub Y N 445 
WWO C2  C1   sing Y N 446 
WWO C2  F13  sing N N 447 
WWO C1  S11  sing N N 448 
WWO O22 S11  doub N N 449 
WWO C20 C19  sing Y N 450 
WWO S11 C21  sing N N 451 
WWO C21 C24  sing N N 452 
WWO O25 C24  sing N N 453 
WWO N10 H1   sing N N 454 
WWO N10 H2   sing N N 455 
WWO C21 H3   sing N N 456 
WWO C21 H4   sing N N 457 
WWO C24 H5   sing N N 458 
WWO C24 H6   sing N N 459 
WWO O25 H7   sing N N 460 
WWO N26 H8   sing N N 461 
WWO C14 H9   sing N N 462 
WWO C14 H10  sing N N 463 
WWO C20 H11  sing N N 464 
WWO C19 H12  sing N N 465 
WWO C18 H13  sing N N 466 
WWO C17 H14  sing N N 467 
WWO C16 H15  sing N N 468 
# 
_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   3HLJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    5EHE 
_atom_sites.fract_transf_matrix[1][1]   0.023697 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005908 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024375 
_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]   0.014324 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
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   . HIS A 1 4   ? 30.837  3.022   8.465   1.00 29.86 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 31.602  1.801   8.856   1.00 29.90 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.671  0.834   9.561   1.00 24.15 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.707  -0.324  9.233   1.00 22.70 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 32.843  2.094   9.741   1.00 36.20 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 33.862  0.939   9.807   1.00 36.10 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 34.724  0.653   8.782   1.00 43.95 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 34.150  -0.001  10.839  1.00 40.79 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 35.512  -0.426  9.130   1.00 41.16 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 35.152  -0.826  10.388  1.00 36.31 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.816  1.287   10.486  1.00 20.61 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 29.029  0.343   11.334  1.00 15.36 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 28.027  -0.427  10.574  1.00 14.38 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.521  0.021   9.553   1.00 15.26 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.370  1.066   12.511  1.00 15.50 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 27.175  1.925   12.113  1.00 16.12 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 27.137  3.288   11.761  1.00 13.61 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.757  1.468   12.028  1.00 14.55 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.837  3.688   11.489  1.00 16.90 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.983  2.617   11.612  1.00 14.80 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 25.098  0.241   12.286  1.00 13.26 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.616  2.560   11.443  1.00 14.19 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.688  0.196   12.062  1.00 12.17 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 22.980  1.354   11.718  1.00 14.41 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.779  -1.608  11.084  1.00 13.95 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.760  -2.461  10.467  1.00 14.16 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.472  -3.595  11.379  1.00 13.44 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.455  -3.459  12.582  1.00 13.76 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 26.187  -4.769  10.785  1.00 15.11 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.783  -5.920  11.607  1.00 15.95 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.678  -7.214  11.627  1.00 21.34 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 26.381  -8.245  12.320  1.00 22.78 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 24.311  -6.239  11.233  1.00 13.29 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.350  -5.155  11.779  1.00 11.42 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.986  -5.176  13.145  1.00 11.54 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.892  -4.116  10.967  1.00 10.53 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 22.095  -4.123  13.635  1.00 10.25 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 22.003  -3.101  11.421  1.00 9.82  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.595  -3.150  12.764  1.00 10.65 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.731  -2.162  13.188  1.00 11.30 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.853  -7.083  10.999  1.00 21.03 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 28.837  -8.227  10.897  1.00 21.00 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.844  -8.526  11.943  1.00 24.21 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.910  -7.939  13.059  1.00 22.27 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 30.690  -9.515  11.602  1.00 23.42 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 31.743  -9.995  12.493  1.00 27.65 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 32.667  -8.874  12.869  1.00 25.38 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 33.158  -8.834  14.036  1.00 27.08 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 32.519  -11.150 11.846  1.00 32.27 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 33.606  -11.763 12.730  1.00 37.11 ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? 32.878  -7.982  11.891  1.00 25.01 ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? 33.890  -6.925  12.011  1.00 23.81 ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? 33.366  -5.561  12.213  1.00 20.87 ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? 34.172  -4.694  12.624  1.00 20.87 ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? 34.903  -6.951  10.810  1.00 22.11 ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? 35.621  -8.298  10.675  1.00 21.79 ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? 36.605  -8.684  11.531  1.00 24.89 ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? 35.366  -9.370  9.849   1.00 24.49 ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? 36.981  -9.943  11.238  1.00 23.58 ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? 36.213  -10.371 10.203  1.00 23.32 ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? 32.029  -5.352  12.042  1.00 20.46 ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? 31.497  -4.004  12.295  1.00 16.90 ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? 30.132  -4.033  12.968  1.00 18.89 ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? 29.430  -3.023  12.887  1.00 16.54 ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? 31.309  -3.281  11.015  1.00 15.36 ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? 30.256  -3.916  10.146  1.00 17.30 ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? 29.778  -5.012  10.491  1.00 17.21 ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? 29.954  -3.330  9.014   1.00 16.81 ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? 29.797  -5.194  13.535  1.00 16.99 ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? 28.508  -5.414  14.211  1.00 17.75 ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? 28.415  -4.739  15.557  1.00 16.56 ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? 29.290  -4.014  16.029  1.00 14.76 ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? 27.326  -5.021  16.274  1.00 14.32 ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? 27.067  -4.400  17.563  1.00 15.49 ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? 28.174  -4.399  18.560  1.00 13.49 ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? 28.370  -3.391  19.251  1.00 15.27 ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? 25.878  -5.253  18.104  1.00 15.24 ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? 25.157  -5.576  16.862  1.00 14.30 ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? 26.171  -5.798  15.761  1.00 13.31 ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? 28.934  -5.485  18.634  1.00 15.91 ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? 30.030  -5.552  19.568  1.00 17.68 ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? 31.197  -4.559  19.238  1.00 15.77 ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? 32.039  -4.355  20.098  1.00 16.72 ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? 30.582  -7.004  19.597  1.00 19.02 ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? 31.203  -7.371  18.244  1.00 22.94 ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? 30.345  -8.045  17.173  1.00 29.72 ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? 29.095  -7.801  17.035  1.00 22.62 ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? 30.998  -8.822  16.384  1.00 32.70 ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? 31.215  -4.017  18.028  1.00 14.47 ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? 32.187  -3.011  17.607  1.00 15.09 ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? 31.785  -1.578  17.794  1.00 14.75 ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? 32.590  -0.662  17.791  1.00 14.77 ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? 32.556  -3.235  16.129  1.00 15.01 ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? 33.307  -4.518  15.893  1.00 17.37 ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? 34.674  -4.597  16.071  1.00 18.55 ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? 32.862  -5.798  15.629  1.00 19.16 ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? 35.057  -5.875  15.862  1.00 19.94 ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? 33.987  -6.608  15.599  1.00 19.59 ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? 30.484  -1.324  17.936  1.00 12.30 ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? 29.991  0.030   17.946  1.00 11.91 ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? 30.555  0.998   18.902  1.00 11.84 ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? 30.619  2.200   18.590  1.00 11.70 ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? 28.430  -0.009  18.081  1.00 10.88 ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? 27.732  -0.687  16.916  1.00 12.26 ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? 28.280  -1.152  15.715  1.00 11.37 ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? 26.308  -0.991  16.823  1.00 11.17 ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? 27.306  -1.702  14.913  1.00 11.86 ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? 26.099  -1.638  15.524  1.00 10.80 ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? 25.225  -0.799  17.660  1.00 11.46 ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? 24.844  -2.058  15.112  1.00 11.18 ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? 23.968  -1.221  17.238  1.00 10.80 ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? 23.781  -1.840  15.998  1.00 11.14 ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? 30.994  0.530   20.060  1.00 12.67 ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? 31.438  1.400   21.121  1.00 13.03 ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? 32.722  2.131   20.710  1.00 12.99 ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? 32.940  3.198   21.324  1.00 14.61 ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? 31.694  0.683   22.425  1.00 12.63 ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? 32.908  -0.243  22.352  1.00 14.23 ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? 34.078  0.118   22.902  1.00 17.35 ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? 33.097  -1.448  21.749  1.00 15.31 ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? 35.015  -0.815  22.621  1.00 16.63 ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? 34.454  -1.773  21.932  1.00 15.90 ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? 33.427  1.634   19.672  1.00 15.92 ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? 34.705  2.308   19.325  1.00 15.19 ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? 34.371  3.626   18.625  1.00 17.58 ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? 35.024  4.666   18.887  1.00 20.49 ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? 35.517  1.419   18.397  1.00 17.78 ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? 36.119  0.278   19.181  1.00 17.80 ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? 36.807  -0.690  18.251  1.00 17.99 ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? 35.831  -1.674  17.612  1.00 17.55 ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? 36.486  -2.521  16.568  1.00 15.66 ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 19  ? 33.319  3.652   17.790  1.00 17.11 ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 19  ? 32.907  4.951   17.168  1.00 18.01 ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 19  ? 31.894  5.733   18.033  1.00 17.48 ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 19  ? 31.794  6.935   17.929  1.00 18.41 ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 19  ? 32.366  4.810   15.748  1.00 22.07 ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 19  ? 33.454  4.794   14.682  1.00 27.35 ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 19  ? 34.466  5.485   14.856  1.00 32.24 ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 19  ? 33.267  4.108   13.659  1.00 35.93 ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 20  ? 31.117  5.001   18.861  1.00 15.52 ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 20  ? 29.966  5.595   19.639  1.00 14.12 ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 20  ? 30.062  5.095   21.074  1.00 14.39 ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 20  ? 29.454  4.091   21.470  1.00 14.25 ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 20  ? 28.593  5.180   19.001  1.00 13.24 ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 20  ? 28.497  5.595   17.596  1.00 13.97 ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 20  ? 28.173  6.924   17.241  1.00 15.32 ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 20  ? 28.806  4.677   16.569  1.00 14.14 ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 20  ? 28.153  7.257   15.895  1.00 16.81 ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 20  ? 28.842  5.015   15.254  1.00 15.82 ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 20  ? 28.487  6.347   14.902  1.00 16.76 ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 21  ? 30.936  5.737   21.899  1.00 14.41 ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 21  ? 31.184  5.224   23.232  1.00 13.54 ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 21  ? 29.972  5.097   24.166  1.00 13.43 ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 21  ? 29.987  4.358   25.157  1.00 16.42 ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 21  ? 32.298  6.197   23.822  1.00 14.96 ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 21  ? 32.671  7.035   22.668  1.00 16.59 ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 21  ? 31.877  6.750   21.437  1.00 16.53 ? 21  PRO A CD  1 
ATOM   158  N  N   . ILE A 1 22  ? 28.904  5.879   23.844  1.00 12.96 ? 22  ILE A N   1 
ATOM   159  C  CA  . ILE A 1 22  ? 27.657  5.765   24.598  1.00 13.46 ? 22  ILE A CA  1 
ATOM   160  C  C   . ILE A 1 22  ? 27.084  4.354   24.417  1.00 12.88 ? 22  ILE A C   1 
ATOM   161  O  O   . ILE A 1 22  ? 26.188  4.017   25.172  1.00 11.95 ? 22  ILE A O   1 
ATOM   162  C  CB  . ILE A 1 22  ? 26.651  6.885   24.156  1.00 11.56 ? 22  ILE A CB  1 
ATOM   163  C  CG1 . ILE A 1 22  ? 25.547  7.106   25.165  1.00 12.15 ? 22  ILE A CG1 1 
ATOM   164  C  CG2 . ILE A 1 22  ? 25.989  6.499   22.800  1.00 12.61 ? 22  ILE A CG2 1 
ATOM   165  C  CD1 . ILE A 1 22  ? 24.579  8.214   24.729  1.00 15.84 ? 22  ILE A CD1 1 
ATOM   166  N  N   . ALA A 1 23  ? 27.611  3.568   23.475  1.00 11.23 ? 23  ALA A N   1 
ATOM   167  C  CA  . ALA A 1 23  ? 27.149  2.129   23.399  1.00 11.57 ? 23  ALA A CA  1 
ATOM   168  C  C   . ALA A 1 23  ? 27.250  1.392   24.755  1.00 11.48 ? 23  ALA A C   1 
ATOM   169  O  O   . ALA A 1 23  ? 26.544  0.375   24.990  1.00 11.72 ? 23  ALA A O   1 
ATOM   170  C  CB  . ALA A 1 23  ? 27.988  1.333   22.353  1.00 10.98 ? 23  ALA A CB  1 
ATOM   171  N  N   . LYS A 1 24  ? 28.146  1.830   25.661  1.00 12.60 ? 24  LYS A N   1 
ATOM   172  C  CA  . LYS A 1 24  ? 28.294  1.166   26.963  1.00 12.99 ? 24  LYS A CA  1 
ATOM   173  C  C   . LYS A 1 24  ? 27.717  2.106   28.010  1.00 15.78 ? 24  LYS A C   1 
ATOM   174  O  O   . LYS A 1 24  ? 28.073  2.040   29.208  1.00 16.96 ? 24  LYS A O   1 
ATOM   175  C  CB  . LYS A 1 24  ? 29.792  0.886   27.306  1.00 13.46 ? 24  LYS A CB  1 
ATOM   176  C  CG  . LYS A 1 24  ? 30.412  -0.050  26.341  1.00 14.81 ? 24  LYS A CG  1 
ATOM   177  C  CD  . LYS A 1 24  ? 31.910  -0.190  26.728  1.00 18.14 ? 24  LYS A CD  1 
ATOM   178  C  CE  . LYS A 1 24  ? 32.584  -1.214  25.784  1.00 19.58 ? 24  LYS A CE  1 
ATOM   179  N  NZ  . LYS A 1 24  ? 32.304  -2.578  26.342  1.00 23.42 ? 24  LYS A NZ  1 
ATOM   180  N  N   . GLY A 1 25  ? 26.712  2.918   27.611  1.00 13.91 ? 25  GLY A N   1 
ATOM   181  C  CA  . GLY A 1 25  ? 26.116  3.870   28.518  1.00 15.45 ? 25  GLY A CA  1 
ATOM   182  C  C   . GLY A 1 25  ? 25.181  3.355   29.626  1.00 14.22 ? 25  GLY A C   1 
ATOM   183  O  O   . GLY A 1 25  ? 24.922  2.168   29.758  1.00 15.44 ? 25  GLY A O   1 
ATOM   184  N  N   . GLU A 1 26  ? 24.565  4.291   30.357  1.00 14.91 ? 26  GLU A N   1 
ATOM   185  C  CA  . GLU A 1 26  ? 23.696  3.912   31.448  1.00 16.71 ? 26  GLU A CA  1 
ATOM   186  C  C   . GLU A 1 26  ? 22.245  3.541   31.094  1.00 14.08 ? 26  GLU A C   1 
ATOM   187  O  O   . GLU A 1 26  ? 21.508  3.001   31.938  1.00 12.13 ? 26  GLU A O   1 
ATOM   188  C  CB  . GLU A 1 26  ? 23.671  5.067   32.506  1.00 21.85 ? 26  GLU A CB  1 
ATOM   189  C  CG  . GLU A 1 26  ? 25.036  5.361   33.162  1.00 24.70 ? 26  GLU A CG  1 
ATOM   190  C  CD  . GLU A 1 26  ? 25.703  4.084   33.715  1.00 33.99 ? 26  GLU A CD  1 
ATOM   191  O  OE1 . GLU A 1 26  ? 25.083  3.335   34.549  1.00 36.61 ? 26  GLU A OE1 1 
ATOM   192  O  OE2 . GLU A 1 26  ? 26.853  3.810   33.306  1.00 32.23 ? 26  GLU A OE2 1 
ATOM   193  N  N   . ARG A 1 27  ? 21.794  3.855   29.856  1.00 11.77 ? 27  ARG A N   1 
ATOM   194  C  CA  . ARG A 1 27  ? 20.367  3.539   29.568  1.00 11.33 ? 27  ARG A CA  1 
ATOM   195  C  C   . ARG A 1 27  ? 20.277  3.108   28.068  1.00 9.83  ? 27  ARG A C   1 
ATOM   196  O  O   . ARG A 1 27  ? 19.561  3.721   27.249  1.00 9.53  ? 27  ARG A O   1 
ATOM   197  C  CB  . ARG A 1 27  ? 19.432  4.780   29.904  1.00 12.07 ? 27  ARG A CB  1 
ATOM   198  C  CG  . ARG A 1 27  ? 19.707  6.081   29.169  1.00 15.23 ? 27  ARG A CG  1 
ATOM   199  C  CD  . ARG A 1 27  ? 18.755  7.319   29.502  1.00 21.24 ? 27  ARG A CD  1 
ATOM   200  N  NE  . ARG A 1 27  ? 17.575  7.231   28.625  1.00 18.45 ? 27  ARG A NE  1 
ATOM   201  C  CZ  . ARG A 1 27  ? 16.664  8.183   28.431  1.00 16.83 ? 27  ARG A CZ  1 
ATOM   202  N  NH1 . ARG A 1 27  ? 16.751  9.349   29.052  1.00 14.17 ? 27  ARG A NH1 1 
ATOM   203  N  NH2 . ARG A 1 27  ? 15.649  7.960   27.601  1.00 15.38 ? 27  ARG A NH2 1 
ATOM   204  N  N   . GLN A 1 28  ? 21.016  2.050   27.713  1.00 10.59 ? 28  GLN A N   1 
ATOM   205  C  CA  . GLN A 1 28  ? 21.067  1.556   26.337  1.00 8.73  ? 28  GLN A CA  1 
ATOM   206  C  C   . GLN A 1 28  ? 19.881  0.567   26.086  1.00 8.33  ? 28  GLN A C   1 
ATOM   207  O  O   . GLN A 1 28  ? 19.355  -0.066  27.006  1.00 7.93  ? 28  GLN A O   1 
ATOM   208  C  CB  . GLN A 1 28  ? 22.411  0.861   26.079  1.00 8.42  ? 28  GLN A CB  1 
ATOM   209  C  CG  . GLN A 1 28  ? 23.521  1.879   26.015  1.00 7.68  ? 28  GLN A CG  1 
ATOM   210  C  CD  . GLN A 1 28  ? 23.373  2.734   24.706  1.00 8.06  ? 28  GLN A CD  1 
ATOM   211  O  OE1 . GLN A 1 28  ? 23.581  2.228   23.616  1.00 8.32  ? 28  GLN A OE1 1 
ATOM   212  N  NE2 . GLN A 1 28  ? 23.067  4.028   24.832  1.00 7.98  ? 28  GLN A NE2 1 
ATOM   213  N  N   . SER A 1 29  ? 19.506  0.501   24.803  1.00 6.94  ? 29  SER A N   1 
ATOM   214  C  CA  . SER A 1 29  ? 18.439  -0.416  24.399  1.00 6.72  ? 29  SER A CA  1 
ATOM   215  C  C   . SER A 1 29  ? 18.975  -1.284  23.252  1.00 6.73  ? 29  SER A C   1 
ATOM   216  O  O   . SER A 1 29  ? 19.909  -0.882  22.564  1.00 6.77  ? 29  SER A O   1 
ATOM   217  C  CB  . SER A 1 29  ? 17.318  0.471   23.799  1.00 6.94  ? 29  SER A CB  1 
ATOM   218  O  OG  . SER A 1 29  ? 16.591  1.111   24.920  1.00 7.04  ? 29  SER A OG  1 
ATOM   219  N  N   . PRO A 1 30  ? 18.339  -2.434  22.957  1.00 6.21  ? 30  PRO A N   1 
ATOM   220  C  CA  . PRO A 1 30  ? 17.185  -2.951  23.697  1.00 7.07  ? 30  PRO A CA  1 
ATOM   221  C  C   . PRO A 1 30  ? 17.549  -3.623  24.983  1.00 7.46  ? 30  PRO A C   1 
ATOM   222  O  O   . PRO A 1 30  ? 18.740  -3.646  25.378  1.00 7.72  ? 30  PRO A O   1 
ATOM   223  C  CB  . PRO A 1 30  ? 16.672  -4.041  22.742  1.00 6.72  ? 30  PRO A CB  1 
ATOM   224  C  CG  . PRO A 1 30  ? 17.966  -4.611  22.107  1.00 7.57  ? 30  PRO A CG  1 
ATOM   225  C  CD  . PRO A 1 30  ? 18.783  -3.348  21.877  1.00 7.76  ? 30  PRO A CD  1 
ATOM   226  N  N   . VAL A 1 31  ? 16.582  -4.211  25.674  1.00 7.49  ? 31  VAL A N   1 
ATOM   227  C  CA  . VAL A 1 31  ? 16.780  -4.982  26.917  1.00 8.69  ? 31  VAL A CA  1 
ATOM   228  C  C   . VAL A 1 31  ? 15.911  -6.210  26.894  1.00 8.82  ? 31  VAL A C   1 
ATOM   229  O  O   . VAL A 1 31  ? 14.899  -6.282  26.148  1.00 8.57  ? 31  VAL A O   1 
ATOM   230  C  CB  . VAL A 1 31  ? 16.405  -4.159  28.209  1.00 8.03  ? 31  VAL A CB  1 
ATOM   231  C  CG1 . VAL A 1 31  ? 17.395  -2.963  28.342  1.00 8.36  ? 31  VAL A CG1 1 
ATOM   232  C  CG2 . VAL A 1 31  ? 14.887  -3.703  28.171  1.00 8.80  ? 31  VAL A CG2 1 
ATOM   233  N  N   . ASP A 1 32  ? 16.231  -7.221  27.740  1.00 8.73  ? 32  ASP A N   1 
ATOM   234  C  CA  . ASP A 1 32  ? 15.295  -8.264  28.018  1.00 8.32  ? 32  ASP A CA  1 
ATOM   235  C  C   . ASP A 1 32  ? 14.210  -7.786  28.987  1.00 8.32  ? 32  ASP A C   1 
ATOM   236  O  O   . ASP A 1 32  ? 14.528  -7.134  29.971  1.00 10.61 ? 32  ASP A O   1 
ATOM   237  C  CB  . ASP A 1 32  ? 16.036  -9.470  28.614  1.00 9.93  ? 32  ASP A CB  1 
ATOM   238  C  CG  . ASP A 1 32  ? 15.089  -10.620 28.913  1.00 12.32 ? 32  ASP A CG  1 
ATOM   239  O  OD1 . ASP A 1 32  ? 14.373  -11.063 27.993  1.00 11.77 ? 32  ASP A OD1 1 
ATOM   240  O  OD2 . ASP A 1 32  ? 14.975  -11.108 30.131  1.00 13.31 ? 32  ASP A OD2 1 
ATOM   241  N  N   . ILE A 1 33  ? 12.947  -8.032  28.667  1.00 9.52  ? 33  ILE A N   1 
ATOM   242  C  CA  . ILE A 1 33  ? 11.835  -7.692  29.535  1.00 9.98  ? 33  ILE A CA  1 
ATOM   243  C  C   . ILE A 1 33  ? 11.500  -8.930  30.359  1.00 11.67 ? 33  ILE A C   1 
ATOM   244  O  O   . ILE A 1 33  ? 10.995  -9.954  29.831  1.00 12.18 ? 33  ILE A O   1 
ATOM   245  C  CB  . ILE A 1 33  ? 10.625  -7.190  28.707  1.00 10.35 ? 33  ILE A CB  1 
ATOM   246  C  CG1 . ILE A 1 33  ? 11.004  -5.961  27.895  1.00 9.74  ? 33  ILE A CG1 1 
ATOM   247  C  CG2 . ILE A 1 33  ? 9.366   -6.945  29.620  1.00 11.03 ? 33  ILE A CG2 1 
ATOM   248  C  CD1 . ILE A 1 33  ? 9.960   -5.691  26.761  1.00 10.65 ? 33  ILE A CD1 1 
ATOM   249  N  N   A ASP A 1 34  ? 11.860  -8.854  31.648  0.50 13.16 ? 34  ASP A N   1 
ATOM   250  N  N   B ASP A 1 34  ? 11.842  -8.848  31.639  0.50 13.38 ? 34  ASP A N   1 
ATOM   251  C  CA  A ASP A 1 34  ? 11.588  -9.966  32.599  0.50 13.08 ? 34  ASP A CA  1 
ATOM   252  C  CA  B ASP A 1 34  ? 11.565  -9.984  32.519  0.50 13.40 ? 34  ASP A CA  1 
ATOM   253  C  C   A ASP A 1 34  ? 10.160  -9.731  33.132  0.50 13.70 ? 34  ASP A C   1 
ATOM   254  C  C   B ASP A 1 34  ? 10.176  -9.738  33.107  0.50 13.89 ? 34  ASP A C   1 
ATOM   255  O  O   A ASP A 1 34  ? 9.937   -8.808  33.905  0.50 15.19 ? 34  ASP A O   1 
ATOM   256  O  O   B ASP A 1 34  ? 10.003  -8.821  33.901  0.50 15.23 ? 34  ASP A O   1 
ATOM   257  C  CB  A ASP A 1 34  ? 12.680  -9.971  33.698  0.50 13.79 ? 34  ASP A CB  1 
ATOM   258  C  CB  B ASP A 1 34  ? 12.647  -10.059 33.581  0.50 14.51 ? 34  ASP A CB  1 
ATOM   259  C  CG  A ASP A 1 34  ? 12.467  -11.079 34.786  0.50 14.61 ? 34  ASP A CG  1 
ATOM   260  C  CG  B ASP A 1 34  ? 12.508  -11.285 34.459  0.50 16.75 ? 34  ASP A CG  1 
ATOM   261  O  OD1 A ASP A 1 34  ? 11.308  -11.492 34.992  0.50 13.25 ? 34  ASP A OD1 1 
ATOM   262  O  OD1 B ASP A 1 34  ? 12.972  -12.368 34.014  0.50 16.47 ? 34  ASP A OD1 1 
ATOM   263  O  OD2 A ASP A 1 34  ? 13.487  -11.556 35.395  0.50 15.81 ? 34  ASP A OD2 1 
ATOM   264  O  OD2 B ASP A 1 34  ? 12.004  -11.131 35.593  0.50 17.02 ? 34  ASP A OD2 1 
ATOM   265  N  N   . THR A 1 35  ? 9.193   -10.475 32.623  1.00 14.23 ? 35  THR A N   1 
ATOM   266  C  CA  . THR A 1 35  ? 7.759   -10.158 32.838  1.00 14.78 ? 35  THR A CA  1 
ATOM   267  C  C   . THR A 1 35  ? 7.356   -10.285 34.303  1.00 14.50 ? 35  THR A C   1 
ATOM   268  O  O   . THR A 1 35  ? 6.365   -9.629  34.751  1.00 18.15 ? 35  THR A O   1 
ATOM   269  C  CB  . THR A 1 35  ? 6.841   -11.087 32.037  1.00 17.40 ? 35  THR A CB  1 
ATOM   270  O  OG1 . THR A 1 35  ? 7.065   -12.439 32.495  1.00 16.17 ? 35  THR A OG1 1 
ATOM   271  C  CG2 . THR A 1 35  ? 7.171   -11.076 30.507  1.00 15.06 ? 35  THR A CG2 1 
ATOM   272  N  N   . HIS A 1 36  ? 8.171   -11.061 35.039  1.00 16.71 ? 36  HIS A N   1 
ATOM   273  C  CA  . HIS A 1 36  ? 7.847   -11.284 36.449  1.00 17.27 ? 36  HIS A CA  1 
ATOM   274  C  C   . HIS A 1 36  ? 8.313   -10.177 37.302  1.00 18.67 ? 36  HIS A C   1 
ATOM   275  O  O   . HIS A 1 36  ? 7.630   -9.868  38.297  1.00 21.81 ? 36  HIS A O   1 
ATOM   276  C  CB  . HIS A 1 36  ? 8.316   -12.711 36.862  1.00 17.41 ? 36  HIS A CB  1 
ATOM   277  C  CG  . HIS A 1 36  ? 7.397   -13.757 36.338  1.00 18.42 ? 36  HIS A CG  1 
ATOM   278  N  ND1 . HIS A 1 36  ? 7.739   -14.629 35.373  1.00 22.63 ? 36  HIS A ND1 1 
ATOM   279  C  CD2 . HIS A 1 36  ? 6.051   -13.948 36.587  1.00 20.57 ? 36  HIS A CD2 1 
ATOM   280  C  CE1 . HIS A 1 36  ? 6.683   -15.371 35.054  1.00 21.17 ? 36  HIS A CE1 1 
ATOM   281  N  NE2 . HIS A 1 36  ? 5.647   -14.961 35.793  1.00 26.94 ? 36  HIS A NE2 1 
ATOM   282  N  N   . THR A 1 37  ? 9.427   -9.556  36.948  1.00 17.64 ? 37  THR A N   1 
ATOM   283  C  CA  . THR A 1 37  ? 9.933   -8.433  37.697  1.00 19.33 ? 37  THR A CA  1 
ATOM   284  C  C   . THR A 1 37  ? 9.561   -6.998  37.172  1.00 17.17 ? 37  THR A C   1 
ATOM   285  O  O   . THR A 1 37  ? 9.912   -5.989  37.819  1.00 19.04 ? 37  THR A O   1 
ATOM   286  C  CB  . THR A 1 37  ? 11.419  -8.536  37.934  1.00 21.65 ? 37  THR A CB  1 
ATOM   287  O  OG1 . THR A 1 37  ? 12.091  -8.446  36.690  1.00 23.65 ? 37  THR A OG1 1 
ATOM   288  C  CG2 . THR A 1 37  ? 11.835  -9.869  38.541  1.00 22.20 ? 37  THR A CG2 1 
ATOM   289  N  N   . ALA A 1 38  ? 8.841   -6.945  36.040  1.00 16.39 ? 38  ALA A N   1 
ATOM   290  C  CA  . ALA A 1 38  ? 8.203   -5.649  35.577  1.00 14.60 ? 38  ALA A CA  1 
ATOM   291  C  C   . ALA A 1 38  ? 7.178   -5.211  36.677  1.00 18.42 ? 38  ALA A C   1 
ATOM   292  O  O   . ALA A 1 38  ? 6.409   -6.038  37.207  1.00 19.69 ? 38  ALA A O   1 
ATOM   293  C  CB  . ALA A 1 38  ? 7.479   -5.867  34.255  1.00 17.00 ? 38  ALA A CB  1 
ATOM   294  N  N   . LYS A 1 39  ? 7.243   -3.944  37.067  1.00 17.21 ? 39  LYS A N   1 
ATOM   295  C  CA  . LYS A 1 39  ? 6.356   -3.398  38.123  1.00 17.78 ? 39  LYS A CA  1 
ATOM   296  C  C   . LYS A 1 39  ? 5.026   -2.922  37.482  1.00 17.91 ? 39  LYS A C   1 
ATOM   297  O  O   . LYS A 1 39  ? 5.024   -2.008  36.662  1.00 16.01 ? 39  LYS A O   1 
ATOM   298  C  CB  . LYS A 1 39  ? 7.119   -2.245  38.777  1.00 17.85 ? 39  LYS A CB  1 
ATOM   299  C  CG  . LYS A 1 39  ? 6.313   -1.337  39.737  1.00 21.49 ? 39  LYS A CG  1 
ATOM   300  C  CD  . LYS A 1 39  ? 6.182   -2.009  41.104  1.00 20.35 ? 39  LYS A CD  1 
ATOM   301  C  CE  . LYS A 1 39  ? 5.343   -1.142  42.036  1.00 23.47 ? 39  LYS A CE  1 
ATOM   302  N  NZ  . LYS A 1 39  ? 4.904   -2.018  43.158  1.00 27.03 ? 39  LYS A NZ  1 
ATOM   303  N  N   . TYR A 1 40  ? 3.898   -3.471  37.928  1.00 17.26 ? 40  TYR A N   1 
ATOM   304  C  CA  . TYR A 1 40  ? 2.601   -2.890  37.503  1.00 19.40 ? 40  TYR A CA  1 
ATOM   305  C  C   . TYR A 1 40  ? 2.412   -1.505  38.081  1.00 21.86 ? 40  TYR A C   1 
ATOM   306  O  O   . TYR A 1 40  ? 2.588   -1.291  39.326  1.00 21.43 ? 40  TYR A O   1 
ATOM   307  C  CB  . TYR A 1 40  ? 1.428   -3.843  37.848  1.00 22.06 ? 40  TYR A CB  1 
ATOM   308  C  CG  . TYR A 1 40  ? 0.045   -3.234  37.684  1.00 26.23 ? 40  TYR A CG  1 
ATOM   309  C  CD1 . TYR A 1 40  ? -0.453  -2.859  36.434  1.00 28.03 ? 40  TYR A CD1 1 
ATOM   310  C  CD2 . TYR A 1 40  ? -0.789  -3.098  38.800  1.00 32.67 ? 40  TYR A CD2 1 
ATOM   311  C  CE1 . TYR A 1 40  ? -1.714  -2.335  36.290  1.00 28.95 ? 40  TYR A CE1 1 
ATOM   312  C  CE2 . TYR A 1 40  ? -2.060  -2.548  38.673  1.00 32.19 ? 40  TYR A CE2 1 
ATOM   313  C  CZ  . TYR A 1 40  ? -2.505  -2.169  37.430  1.00 34.09 ? 40  TYR A CZ  1 
ATOM   314  O  OH  . TYR A 1 40  ? -3.746  -1.621  37.316  1.00 35.60 ? 40  TYR A OH  1 
ATOM   315  N  N   . ASP A 1 41  ? 2.062   -0.540  37.229  1.00 19.94 ? 41  ASP A N   1 
ATOM   316  C  CA  . ASP A 1 41  ? 1.873   0.832   37.728  1.00 22.87 ? 41  ASP A CA  1 
ATOM   317  C  C   . ASP A 1 41  ? 0.409   1.156   37.392  1.00 25.07 ? 41  ASP A C   1 
ATOM   318  O  O   . ASP A 1 41  ? 0.107   1.415   36.233  1.00 21.61 ? 41  ASP A O   1 
ATOM   319  C  CB  . ASP A 1 41  ? 2.841   1.810   37.115  1.00 25.53 ? 41  ASP A CB  1 
ATOM   320  C  CG  . ASP A 1 41  ? 2.668   3.212   37.673  1.00 30.87 ? 41  ASP A CG  1 
ATOM   321  O  OD1 . ASP A 1 41  ? 1.639   3.414   38.365  1.00 33.85 ? 41  ASP A OD1 1 
ATOM   322  O  OD2 . ASP A 1 41  ? 3.560   4.076   37.435  1.00 29.19 ? 41  ASP A OD2 1 
ATOM   323  N  N   . PRO A 1 42  ? -0.538  1.023   38.385  1.00 29.56 ? 42  PRO A N   1 
ATOM   324  C  CA  . PRO A 1 42  ? -1.951  1.331   38.084  1.00 28.30 ? 42  PRO A CA  1 
ATOM   325  C  C   . PRO A 1 42  ? -2.157  2.806   37.739  1.00 29.08 ? 42  PRO A C   1 
ATOM   326  O  O   . PRO A 1 42  ? -3.225  3.172   37.196  1.00 36.18 ? 42  PRO A O   1 
ATOM   327  C  CB  . PRO A 1 42  ? -2.707  0.940   39.387  1.00 32.90 ? 42  PRO A CB  1 
ATOM   328  C  CG  . PRO A 1 42  ? -1.652  1.016   40.459  1.00 34.51 ? 42  PRO A CG  1 
ATOM   329  C  CD  . PRO A 1 42  ? -0.363  0.584   39.792  1.00 29.70 ? 42  PRO A CD  1 
ATOM   330  N  N   . SER A 1 43  ? -1.160  3.655   37.988  1.00 26.53 ? 43  SER A N   1 
ATOM   331  C  CA  . SER A 1 43  ? -1.292  5.054   37.550  1.00 27.37 ? 43  SER A CA  1 
ATOM   332  C  C   . SER A 1 43  ? -0.865  5.334   36.051  1.00 27.41 ? 43  SER A C   1 
ATOM   333  O  O   . SER A 1 43  ? -1.040  6.449   35.537  1.00 31.55 ? 43  SER A O   1 
ATOM   334  C  CB  . SER A 1 43  ? -0.568  5.973   38.521  1.00 32.37 ? 43  SER A CB  1 
ATOM   335  O  OG  . SER A 1 43  ? 0.812   6.052   38.193  1.00 31.80 ? 43  SER A OG  1 
ATOM   336  N  N   . LEU A 1 44  ? -0.313  4.335   35.344  1.00 26.87 ? 44  LEU A N   1 
ATOM   337  C  CA  . LEU A 1 44  ? -0.028  4.533   33.910  1.00 21.88 ? 44  LEU A CA  1 
ATOM   338  C  C   . LEU A 1 44  ? -1.336  4.615   33.130  1.00 22.55 ? 44  LEU A C   1 
ATOM   339  O  O   . LEU A 1 44  ? -2.177  3.746   33.265  1.00 24.37 ? 44  LEU A O   1 
ATOM   340  C  CB  . LEU A 1 44  ? 0.766   3.368   33.351  1.00 21.67 ? 44  LEU A CB  1 
ATOM   341  C  CG  . LEU A 1 44  ? 2.253   3.352   33.680  1.00 19.79 ? 44  LEU A CG  1 
ATOM   342  C  CD1 . LEU A 1 44  ? 2.764   1.945   33.339  1.00 19.68 ? 44  LEU A CD1 1 
ATOM   343  C  CD2 . LEU A 1 44  ? 2.959   4.489   32.940  1.00 21.12 ? 44  LEU A CD2 1 
ATOM   344  N  N   . LYS A 1 45  ? -1.441  5.612   32.246  1.00 21.56 ? 45  LYS A N   1 
ATOM   345  C  CA  . LYS A 1 45  ? -2.679  5.858   31.426  1.00 20.91 ? 45  LYS A CA  1 
ATOM   346  C  C   . LYS A 1 45  ? -2.683  4.973   30.179  1.00 21.06 ? 45  LYS A C   1 
ATOM   347  O  O   . LYS A 1 45  ? -1.608  4.466   29.734  1.00 21.60 ? 45  LYS A O   1 
ATOM   348  C  CB  . LYS A 1 45  ? -2.749  7.309   30.980  1.00 24.77 ? 45  LYS A CB  1 
ATOM   349  C  CG  . LYS A 1 45  ? -2.629  8.390   32.066  1.00 30.41 ? 45  LYS A CG  1 
ATOM   350  C  CD  . LYS A 1 45  ? -2.970  9.774   31.491  1.00 36.26 ? 45  LYS A CD  1 
ATOM   351  C  CE  . LYS A 1 45  ? -2.186  10.891  32.179  1.00 41.80 ? 45  LYS A CE  1 
ATOM   352  N  NZ  . LYS A 1 45  ? -2.404  10.867  33.647  1.00 37.97 ? 45  LYS A NZ  1 
ATOM   353  N  N   . PRO A 1 46  ? -3.875  4.759   29.587  1.00 18.42 ? 46  PRO A N   1 
ATOM   354  C  CA  . PRO A 1 46  ? -3.962  4.077   28.293  1.00 17.86 ? 46  PRO A CA  1 
ATOM   355  C  C   . PRO A 1 46  ? -3.098  4.844   27.268  1.00 14.70 ? 46  PRO A C   1 
ATOM   356  O  O   . PRO A 1 46  ? -3.025  6.083   27.343  1.00 14.90 ? 46  PRO A O   1 
ATOM   357  C  CB  . PRO A 1 46  ? -5.456  4.181   27.930  1.00 18.86 ? 46  PRO A CB  1 
ATOM   358  C  CG  . PRO A 1 46  ? -6.105  4.236   29.267  1.00 18.44 ? 46  PRO A CG  1 
ATOM   359  C  CD  . PRO A 1 46  ? -5.204  5.026   30.188  1.00 19.88 ? 46  PRO A CD  1 
ATOM   360  N  N   . LEU A 1 47  ? -2.508  4.123   26.297  1.00 16.65 ? 47  LEU A N   1 
ATOM   361  C  CA  . LEU A 1 47  ? -1.749  4.740   25.235  1.00 15.66 ? 47  LEU A CA  1 
ATOM   362  C  C   . LEU A 1 47  ? -2.747  5.326   24.234  1.00 19.18 ? 47  LEU A C   1 
ATOM   363  O  O   . LEU A 1 47  ? -3.760  4.669   23.934  1.00 20.27 ? 47  LEU A O   1 
ATOM   364  C  CB  . LEU A 1 47  ? -0.828  3.687   24.573  1.00 18.94 ? 47  LEU A CB  1 
ATOM   365  C  CG  . LEU A 1 47  ? 0.116   4.155   23.494  1.00 20.48 ? 47  LEU A CG  1 
ATOM   366  C  CD1 . LEU A 1 47  ? 1.163   5.081   24.120  1.00 20.84 ? 47  LEU A CD1 1 
ATOM   367  C  CD2 . LEU A 1 47  ? 0.778   2.871   22.951  1.00 21.48 ? 47  LEU A CD2 1 
ATOM   368  N  N   . SER A 1 48  ? -2.515  6.540   23.764  1.00 14.37 ? 48  SER A N   1 
ATOM   369  C  CA  . SER A 1 48  ? -3.325  7.151   22.741  1.00 16.62 ? 48  SER A CA  1 
ATOM   370  C  C   . SER A 1 48  ? -2.550  7.188   21.445  1.00 16.74 ? 48  SER A C   1 
ATOM   371  O  O   . SER A 1 48  ? -1.590  7.951   21.311  1.00 15.80 ? 48  SER A O   1 
ATOM   372  C  CB  . SER A 1 48  ? -3.748  8.565   23.181  1.00 18.38 ? 48  SER A CB  1 
ATOM   373  O  OG  . SER A 1 48  ? -4.428  9.253   22.129  1.00 22.06 ? 48  SER A OG  1 
ATOM   374  N  N   . VAL A 1 49  ? -2.994  6.415   20.492  1.00 17.65 ? 49  VAL A N   1 
ATOM   375  C  CA  . VAL A 1 49  ? -2.476  6.352   19.138  1.00 20.91 ? 49  VAL A CA  1 
ATOM   376  C  C   . VAL A 1 49  ? -3.470  6.968   18.184  1.00 22.94 ? 49  VAL A C   1 
ATOM   377  O  O   . VAL A 1 49  ? -4.530  6.385   17.898  1.00 24.49 ? 49  VAL A O   1 
ATOM   378  C  CB  . VAL A 1 49  ? -2.243  4.873   18.711  1.00 23.86 ? 49  VAL A CB  1 
ATOM   379  C  CG1 . VAL A 1 49  ? -1.687  4.782   17.282  1.00 25.40 ? 49  VAL A CG1 1 
ATOM   380  C  CG2 . VAL A 1 49  ? -1.373  4.136   19.735  1.00 20.88 ? 49  VAL A CG2 1 
ATOM   381  N  N   . SER A 1 50  ? -3.178  8.150   17.689  1.00 19.33 ? 50  SER A N   1 
ATOM   382  C  CA  . SER A 1 50  ? -4.033  8.835   16.768  1.00 19.49 ? 50  SER A CA  1 
ATOM   383  C  C   . SER A 1 50  ? -3.422  8.931   15.385  1.00 18.54 ? 50  SER A C   1 
ATOM   384  O  O   . SER A 1 50  ? -2.775  9.906   15.037  1.00 19.15 ? 50  SER A O   1 
ATOM   385  C  CB  . SER A 1 50  ? -4.480  10.227  17.290  1.00 22.57 ? 50  SER A CB  1 
ATOM   386  O  OG  . SER A 1 50  ? -4.882  10.146  18.632  1.00 30.82 ? 50  SER A OG  1 
ATOM   387  N  N   . TYR A 1 51  ? -3.642  7.889   14.595  1.00 19.04 ? 51  TYR A N   1 
ATOM   388  C  CA  . TYR A 1 51  ? -3.100  7.735   13.259  1.00 18.86 ? 51  TYR A CA  1 
ATOM   389  C  C   . TYR A 1 51  ? -4.066  7.974   12.055  1.00 19.51 ? 51  TYR A C   1 
ATOM   390  O  O   . TYR A 1 51  ? -3.648  7.833   10.878  1.00 19.98 ? 51  TYR A O   1 
ATOM   391  C  CB  . TYR A 1 51  ? -2.447  6.360   13.122  1.00 16.83 ? 51  TYR A CB  1 
ATOM   392  C  CG  . TYR A 1 51  ? -1.119  6.046   13.908  1.00 15.46 ? 51  TYR A CG  1 
ATOM   393  C  CD1 . TYR A 1 51  ? -0.379  7.060   14.562  1.00 16.46 ? 51  TYR A CD1 1 
ATOM   394  C  CD2 . TYR A 1 51  ? -0.624  4.748   13.916  1.00 14.18 ? 51  TYR A CD2 1 
ATOM   395  C  CE1 . TYR A 1 51  ? 0.784   6.717   15.268  1.00 14.10 ? 51  TYR A CE1 1 
ATOM   396  C  CE2 . TYR A 1 51  ? 0.578   4.403   14.520  1.00 14.65 ? 51  TYR A CE2 1 
ATOM   397  C  CZ  . TYR A 1 51  ? 1.244   5.447   15.242  1.00 13.13 ? 51  TYR A CZ  1 
ATOM   398  O  OH  . TYR A 1 51  ? 2.378   5.082   15.886  1.00 12.19 ? 51  TYR A OH  1 
ATOM   399  N  N   . ASP A 1 52  ? -5.318  8.384   12.355  1.00 24.52 ? 52  ASP A N   1 
ATOM   400  C  CA  . ASP A 1 52  ? -6.337  8.641   11.303  1.00 26.72 ? 52  ASP A CA  1 
ATOM   401  C  C   . ASP A 1 52  ? -5.887  9.636   10.191  1.00 24.43 ? 52  ASP A C   1 
ATOM   402  O  O   . ASP A 1 52  ? -6.170  9.424   8.993   1.00 26.43 ? 52  ASP A O   1 
ATOM   403  C  CB  . ASP A 1 52  ? -7.677  9.061   11.907  1.00 29.04 ? 52  ASP A CB  1 
ATOM   404  C  CG  . ASP A 1 52  ? -7.537  10.056  13.058  1.00 33.99 ? 52  ASP A CG  1 
ATOM   405  O  OD1 . ASP A 1 52  ? -6.961  9.700   14.165  1.00 41.57 ? 52  ASP A OD1 1 
ATOM   406  O  OD2 . ASP A 1 52  ? -8.001  11.207  12.861  1.00 39.33 ? 52  ASP A OD2 1 
ATOM   407  N  N   . GLN A 1 53  ? -5.110  10.655  10.552  1.00 27.33 ? 53  GLN A N   1 
ATOM   408  C  CA  . GLN A 1 53  ? -4.657  11.597  9.508   1.00 28.49 ? 53  GLN A CA  1 
ATOM   409  C  C   . GLN A 1 53  ? -3.232  11.367  8.965   1.00 24.69 ? 53  GLN A C   1 
ATOM   410  O  O   . GLN A 1 53  ? -2.683  12.219  8.257   1.00 24.98 ? 53  GLN A O   1 
ATOM   411  C  CB  . GLN A 1 53  ? -4.919  13.056  9.945   1.00 30.77 ? 53  GLN A CB  1 
ATOM   412  C  CG  . GLN A 1 53  ? -6.417  13.372  10.005  1.00 38.16 ? 53  GLN A CG  1 
ATOM   413  C  CD  . GLN A 1 53  ? -7.103  13.112  8.666   1.00 42.56 ? 53  GLN A CD  1 
ATOM   414  O  OE1 . GLN A 1 53  ? -6.668  13.639  7.605   1.00 40.59 ? 53  GLN A OE1 1 
ATOM   415  N  NE2 . GLN A 1 53  ? -8.155  12.262  8.684   1.00 40.34 ? 53  GLN A NE2 1 
ATOM   416  N  N   . ALA A 1 54  ? -2.647  10.177  9.204   1.00 20.05 ? 54  ALA A N   1 
ATOM   417  C  CA  . ALA A 1 54  ? -1.306  9.933   8.757   1.00 17.20 ? 54  ALA A CA  1 
ATOM   418  C  C   . ALA A 1 54  ? -1.076  10.143  7.245   1.00 18.85 ? 54  ALA A C   1 
ATOM   419  O  O   . ALA A 1 54  ? -1.924  9.709   6.418   1.00 18.67 ? 54  ALA A O   1 
ATOM   420  C  CB  . ALA A 1 54  ? -0.814  8.521   9.185   1.00 18.18 ? 54  ALA A CB  1 
ATOM   421  N  N   . THR A 1 55  ? 0.043   10.717  6.879   1.00 16.29 ? 55  THR A N   1 
ATOM   422  C  CA  . THR A 1 55  ? 0.491   10.850  5.511   1.00 14.33 ? 55  THR A CA  1 
ATOM   423  C  C   . THR A 1 55  ? 1.858   10.215  5.259   1.00 15.44 ? 55  THR A C   1 
ATOM   424  O  O   . THR A 1 55  ? 2.863   10.833  5.535   1.00 14.19 ? 55  THR A O   1 
ATOM   425  C  CB  . THR A 1 55  ? 0.644   12.373  5.139   1.00 16.39 ? 55  THR A CB  1 
ATOM   426  O  OG1 . THR A 1 55  ? -0.628  12.970  5.203   1.00 20.40 ? 55  THR A OG1 1 
ATOM   427  C  CG2 . THR A 1 55  ? 1.205   12.527  3.704   1.00 18.66 ? 55  THR A CG2 1 
ATOM   428  N  N   . SER A 1 56  ? 1.934   8.944   4.699   1.00 13.07 ? 56  SER A N   1 
ATOM   429  C  CA  . SER A 1 56  ? 3.197   8.362   4.334   1.00 15.94 ? 56  SER A CA  1 
ATOM   430  C  C   . SER A 1 56  ? 3.687   9.058   3.052   1.00 15.60 ? 56  SER A C   1 
ATOM   431  O  O   . SER A 1 56  ? 2.807   9.537   2.229   1.00 17.47 ? 56  SER A O   1 
ATOM   432  C  CB  . SER A 1 56  ? 3.140   6.811   4.105   1.00 14.90 ? 56  SER A CB  1 
ATOM   433  O  OG  . SER A 1 56  ? 2.111   6.540   3.091   1.00 17.49 ? 56  SER A OG  1 
ATOM   434  N  N   . LEU A 1 57  ? 4.983   9.103   2.904   1.00 15.94 ? 57  LEU A N   1 
ATOM   435  C  CA  . LEU A 1 57  ? 5.627   9.790   1.761   1.00 18.29 ? 57  LEU A CA  1 
ATOM   436  C  C   . LEU A 1 57  ? 6.481   8.873   0.883   1.00 20.52 ? 57  LEU A C   1 
ATOM   437  O  O   . LEU A 1 57  ? 6.370   8.887   -0.380  1.00 18.36 ? 57  LEU A O   1 
ATOM   438  C  CB  . LEU A 1 57  ? 6.465   10.984  2.264   1.00 17.74 ? 57  LEU A CB  1 
ATOM   439  C  CG  . LEU A 1 57  ? 5.643   12.148  2.821   1.00 22.39 ? 57  LEU A CG  1 
ATOM   440  C  CD1 . LEU A 1 57  ? 6.625   13.194  3.284   1.00 23.31 ? 57  LEU A CD1 1 
ATOM   441  C  CD2 . LEU A 1 57  ? 4.651   12.731  1.803   1.00 22.84 ? 57  LEU A CD2 1 
ATOM   442  N  N   . ARG A 1 58  ? 7.372   8.117   1.512   1.00 17.12 ? 58  ARG A N   1 
ATOM   443  C  CA  . ARG A 1 58  ? 8.327   7.412   0.780   1.00 18.92 ? 58  ARG A CA  1 
ATOM   444  C  C   . ARG A 1 58  ? 8.611   6.210   1.620   1.00 18.48 ? 58  ARG A C   1 
ATOM   445  O  O   . ARG A 1 58  ? 8.301   6.198   2.834   1.00 16.86 ? 58  ARG A O   1 
ATOM   446  C  CB  . ARG A 1 58  ? 9.637   8.198   0.638   1.00 22.37 ? 58  ARG A CB  1 
ATOM   447  C  CG  . ARG A 1 58  ? 9.693   9.162   -0.523  1.00 30.27 ? 58  ARG A CG  1 
ATOM   448  C  CD  . ARG A 1 58  ? 11.144  9.473   -0.735  1.00 28.58 ? 58  ARG A CD  1 
ATOM   449  N  NE  . ARG A 1 58  ? 11.844  9.366   0.546   1.00 28.50 ? 58  ARG A NE  1 
ATOM   450  C  CZ  . ARG A 1 58  ? 13.171  9.446   0.678   1.00 26.79 ? 58  ARG A CZ  1 
ATOM   451  N  NH1 . ARG A 1 58  ? 13.906  9.611   -0.394  1.00 25.55 ? 58  ARG A NH1 1 
ATOM   452  N  NH2 . ARG A 1 58  ? 13.733  9.424   1.886   1.00 24.20 ? 58  ARG A NH2 1 
ATOM   453  N  N   . ILE A 1 59  ? 9.192   5.233   0.938   1.00 15.93 ? 59  ILE A N   1 
ATOM   454  C  CA  . ILE A 1 59  ? 9.857   4.104   1.579   1.00 15.93 ? 59  ILE A CA  1 
ATOM   455  C  C   . ILE A 1 59  ? 11.283  4.073   1.061   1.00 16.65 ? 59  ILE A C   1 
ATOM   456  O  O   . ILE A 1 59  ? 11.558  4.260   -0.149  1.00 17.58 ? 59  ILE A O   1 
ATOM   457  C  CB  . ILE A 1 59  ? 9.086   2.791   1.239   1.00 14.14 ? 59  ILE A CB  1 
ATOM   458  C  CG1 . ILE A 1 59  ? 9.634   1.664   2.160   1.00 15.66 ? 59  ILE A CG1 1 
ATOM   459  C  CG2 . ILE A 1 59  ? 9.243   2.380   -0.276  1.00 13.32 ? 59  ILE A CG2 1 
ATOM   460  C  CD1 . ILE A 1 59  ? 8.852   0.332   2.010   1.00 15.49 ? 59  ILE A CD1 1 
ATOM   461  N  N   . LEU A 1 60  ? 12.250  3.806   1.935   1.00 17.81 ? 60  LEU A N   1 
ATOM   462  C  CA  . LEU A 1 60  ? 13.660  3.923   1.699   1.00 15.11 ? 60  LEU A CA  1 
ATOM   463  C  C   . LEU A 1 60  ? 14.493  2.771   2.220   1.00 16.39 ? 60  LEU A C   1 
ATOM   464  O  O   . LEU A 1 60  ? 14.287  2.375   3.381   1.00 17.73 ? 60  LEU A O   1 
ATOM   465  C  CB  . LEU A 1 60  ? 14.137  5.263   2.408   1.00 18.97 ? 60  LEU A CB  1 
ATOM   466  C  CG  . LEU A 1 60  ? 15.599  5.549   2.317   1.00 18.52 ? 60  LEU A CG  1 
ATOM   467  C  CD1 . LEU A 1 60  ? 16.108  5.795   0.888   1.00 21.36 ? 60  LEU A CD1 1 
ATOM   468  C  CD2 . LEU A 1 60  ? 16.139  6.630   3.284   1.00 20.71 ? 60  LEU A CD2 1 
ATOM   469  N  N   . ASN A 1 61  ? 15.422  2.234   1.435   1.00 13.43 ? 61  ASN A N   1 
ATOM   470  C  CA  . ASN A 1 61  ? 16.424  1.330   1.901   1.00 14.49 ? 61  ASN A CA  1 
ATOM   471  C  C   . ASN A 1 61  ? 17.655  2.165   2.289   1.00 19.27 ? 61  ASN A C   1 
ATOM   472  O  O   . ASN A 1 61  ? 18.411  2.679   1.423   1.00 21.43 ? 61  ASN A O   1 
ATOM   473  C  CB  . ASN A 1 61  ? 16.803  0.221   0.863   1.00 14.60 ? 61  ASN A CB  1 
ATOM   474  C  CG  . ASN A 1 61  ? 17.888  -0.719  1.305   1.00 16.70 ? 61  ASN A CG  1 
ATOM   475  O  OD1 . ASN A 1 61  ? 18.777  -0.471  2.188   1.00 17.73 ? 61  ASN A OD1 1 
ATOM   476  N  ND2 . ASN A 1 61  ? 17.889  -1.894  0.696   1.00 17.48 ? 61  ASN A ND2 1 
ATOM   477  N  N   . ASN A 1 62  ? 17.953  2.200   3.577   1.00 16.76 ? 62  ASN A N   1 
ATOM   478  C  CA  . ASN A 1 62  ? 19.073  3.054   4.029   1.00 16.59 ? 62  ASN A CA  1 
ATOM   479  C  C   . ASN A 1 62  ? 20.334  2.270   4.276   1.00 19.64 ? 62  ASN A C   1 
ATOM   480  O  O   . ASN A 1 62  ? 21.334  2.804   4.895   1.00 22.31 ? 62  ASN A O   1 
ATOM   481  C  CB  . ASN A 1 62  ? 18.715  3.876   5.265   1.00 19.84 ? 62  ASN A CB  1 
ATOM   482  C  CG  . ASN A 1 62  ? 18.392  3.008   6.480   1.00 18.60 ? 62  ASN A CG  1 
ATOM   483  O  OD1 . ASN A 1 62  ? 18.703  1.822   6.542   1.00 16.71 ? 62  ASN A OD1 1 
ATOM   484  N  ND2 . ASN A 1 62  ? 17.739  3.643   7.452   1.00 23.77 ? 62  ASN A ND2 1 
ATOM   485  N  N   . GLY A 1 63  ? 20.365  0.984   3.850   1.00 16.81 ? 63  GLY A N   1 
ATOM   486  C  CA  . GLY A 1 63  ? 21.471  0.165   4.098   1.00 16.64 ? 63  GLY A CA  1 
ATOM   487  C  C   . GLY A 1 63  ? 21.535  -0.587  5.411   1.00 15.74 ? 63  GLY A C   1 
ATOM   488  O  O   . GLY A 1 63  ? 22.367  -1.449  5.590   1.00 16.19 ? 63  GLY A O   1 
ATOM   489  N  N   A HIS A 1 64  ? 20.609  -0.240  6.292   0.50 14.87 ? 64  HIS A N   1 
ATOM   490  N  N   B HIS A 1 64  ? 20.651  -0.232  6.354   0.50 15.91 ? 64  HIS A N   1 
ATOM   491  C  CA  A HIS A 1 64  ? 20.548  -0.938  7.576   0.50 15.35 ? 64  HIS A CA  1 
ATOM   492  C  CA  B HIS A 1 64  ? 20.518  -1.037  7.618   0.50 16.62 ? 64  HIS A CA  1 
ATOM   493  C  C   A HIS A 1 64  ? 19.189  -1.587  7.753   0.50 14.35 ? 64  HIS A C   1 
ATOM   494  C  C   B HIS A 1 64  ? 19.120  -1.494  7.931   0.50 14.91 ? 64  HIS A C   1 
ATOM   495  O  O   A HIS A 1 64  ? 19.100  -2.724  8.291   0.50 17.66 ? 64  HIS A O   1 
ATOM   496  O  O   B HIS A 1 64  ? 18.911  -2.338  8.830   0.50 17.27 ? 64  HIS A O   1 
ATOM   497  C  CB  A HIS A 1 64  ? 20.899  0.000   8.726   0.50 14.95 ? 64  HIS A CB  1 
ATOM   498  C  CB  B HIS A 1 64  ? 21.083  -0.375  8.880   0.50 17.57 ? 64  HIS A CB  1 
ATOM   499  C  CG  A HIS A 1 64  ? 22.262  0.671   8.574   0.50 14.70 ? 64  HIS A CG  1 
ATOM   500  C  CG  B HIS A 1 64  ? 20.853  1.124   8.981   0.50 19.18 ? 64  HIS A CG  1 
ATOM   501  N  ND1 A HIS A 1 64  ? 23.406  0.015   8.727   0.50 14.92 ? 64  HIS A ND1 1 
ATOM   502  N  ND1 B HIS A 1 64  ? 19.812  1.678   9.656   0.50 21.56 ? 64  HIS A ND1 1 
ATOM   503  C  CD2 A HIS A 1 64  ? 22.599  1.968   8.247   0.50 17.23 ? 64  HIS A CD2 1 
ATOM   504  C  CD2 B HIS A 1 64  ? 21.648  2.184   8.539   0.50 19.00 ? 64  HIS A CD2 1 
ATOM   505  C  CE1 A HIS A 1 64  ? 24.439  0.862   8.535   0.50 15.33 ? 64  HIS A CE1 1 
ATOM   506  C  CE1 B HIS A 1 64  ? 19.938  3.031   9.618   0.50 21.10 ? 64  HIS A CE1 1 
ATOM   507  N  NE2 A HIS A 1 64  ? 23.945  2.049   8.274   0.50 13.39 ? 64  HIS A NE2 1 
ATOM   508  N  NE2 B HIS A 1 64  ? 21.062  3.323   8.917   0.50 21.55 ? 64  HIS A NE2 1 
ATOM   509  N  N   . ALA A 1 65  ? 18.143  -0.944  7.247   1.00 14.22 ? 65  ALA A N   1 
ATOM   510  C  CA  . ALA A 1 65  ? 16.748  -1.438  7.357   1.00 12.90 ? 65  ALA A CA  1 
ATOM   511  C  C   . ALA A 1 65  ? 16.002  -0.742  6.214   1.00 13.00 ? 65  ALA A C   1 
ATOM   512  O  O   . ALA A 1 65  ? 16.634  -0.056  5.378   1.00 14.96 ? 65  ALA A O   1 
ATOM   513  C  CB  . ALA A 1 65  ? 16.123  -1.104  8.747   1.00 12.07 ? 65  ALA A CB  1 
ATOM   514  N  N   . PHE A 1 66  ? 14.671  -0.871  6.095   1.00 11.67 ? 66  PHE A N   1 
ATOM   515  C  CA  . PHE A 1 66  ? 13.883  0.068   5.267   1.00 13.08 ? 66  PHE A CA  1 
ATOM   516  C  C   . PHE A 1 66  ? 13.018  0.938   6.137   1.00 13.16 ? 66  PHE A C   1 
ATOM   517  O  O   . PHE A 1 66  ? 12.379  0.454   7.129   1.00 12.95 ? 66  PHE A O   1 
ATOM   518  C  CB  . PHE A 1 66  ? 13.065  -0.663  4.126   1.00 12.08 ? 66  PHE A CB  1 
ATOM   519  C  CG  . PHE A 1 66  ? 12.046  -1.638  4.669   1.00 12.05 ? 66  PHE A CG  1 
ATOM   520  C  CD1 . PHE A 1 66  ? 10.776  -1.144  4.972   1.00 12.33 ? 66  PHE A CD1 1 
ATOM   521  C  CD2 . PHE A 1 66  ? 12.323  -3.016  4.855   1.00 12.92 ? 66  PHE A CD2 1 
ATOM   522  C  CE1 . PHE A 1 66  ? 9.799   -1.989  5.482   1.00 13.82 ? 66  PHE A CE1 1 
ATOM   523  C  CE2 . PHE A 1 66  ? 11.361  -3.821  5.453   1.00 13.07 ? 66  PHE A CE2 1 
ATOM   524  C  CZ  . PHE A 1 66  ? 10.110  -3.332  5.715   1.00 11.69 ? 66  PHE A CZ  1 
ATOM   525  N  N   . ASN A 1 67  ? 12.911  2.234   5.803   1.00 14.27 ? 67  ASN A N   1 
ATOM   526  C  CA  . ASN A 1 67  ? 12.069  3.137   6.554   1.00 15.48 ? 67  ASN A CA  1 
ATOM   527  C  C   . ASN A 1 67  ? 10.837  3.550   5.770   1.00 14.46 ? 67  ASN A C   1 
ATOM   528  O  O   . ASN A 1 67  ? 10.996  3.978   4.619   1.00 18.86 ? 67  ASN A O   1 
ATOM   529  C  CB  . ASN A 1 67  ? 12.830  4.434   6.880   1.00 14.70 ? 67  ASN A CB  1 
ATOM   530  C  CG  . ASN A 1 67  ? 13.863  4.271   7.950   1.00 18.36 ? 67  ASN A CG  1 
ATOM   531  O  OD1 . ASN A 1 67  ? 14.084  3.191   8.493   1.00 15.58 ? 67  ASN A OD1 1 
ATOM   532  N  ND2 . ASN A 1 67  ? 14.594  5.380   8.217   1.00 19.82 ? 67  ASN A ND2 1 
ATOM   533  N  N   . VAL A 1 68  ? 9.673   3.542   6.360   1.00 12.46 ? 68  VAL A N   1 
ATOM   534  C  CA  . VAL A 1 68  ? 8.500   4.183   5.775   1.00 13.16 ? 68  VAL A CA  1 
ATOM   535  C  C   . VAL A 1 68  ? 8.420   5.551   6.450   1.00 15.84 ? 68  VAL A C   1 
ATOM   536  O  O   . VAL A 1 68  ? 8.117   5.610   7.656   1.00 14.03 ? 68  VAL A O   1 
ATOM   537  C  CB  . VAL A 1 68  ? 7.217   3.404   5.929   1.00 13.81 ? 68  VAL A CB  1 
ATOM   538  C  CG1 . VAL A 1 68  ? 6.000   4.230   5.440   1.00 14.49 ? 68  VAL A CG1 1 
ATOM   539  C  CG2 . VAL A 1 68  ? 7.342   2.107   5.112   1.00 13.44 ? 68  VAL A CG2 1 
ATOM   540  N  N   . GLU A 1 69  ? 8.669   6.628   5.675   1.00 18.39 ? 69  GLU A N   1 
ATOM   541  C  CA  . GLU A 1 69  ? 8.604   8.036   6.180   1.00 17.50 ? 69  GLU A CA  1 
ATOM   542  C  C   . GLU A 1 69  ? 7.299   8.723   6.059   1.00 17.62 ? 69  GLU A C   1 
ATOM   543  O  O   . GLU A 1 69  ? 6.506   8.476   5.079   1.00 19.95 ? 69  GLU A O   1 
ATOM   544  C  CB  . GLU A 1 69  ? 9.445   8.843   5.312   1.00 18.47 ? 69  GLU A CB  1 
ATOM   545  C  CG  . GLU A 1 69  ? 10.825  8.366   5.409   1.00 18.49 ? 69  GLU A CG  1 
ATOM   546  C  CD  . GLU A 1 69  ? 11.644  8.858   4.232   1.00 25.73 ? 69  GLU A CD  1 
ATOM   547  O  OE1 . GLU A 1 69  ? 11.045  9.470   3.321   1.00 22.45 ? 69  GLU A OE1 1 
ATOM   548  O  OE2 . GLU A 1 69  ? 12.872  8.642   4.212   1.00 25.89 ? 69  GLU A OE2 1 
ATOM   549  N  N   . PHE A 1 70  ? 7.023   9.586   7.028   1.00 14.24 ? 70  PHE A N   1 
ATOM   550  C  CA  . PHE A 1 70  ? 5.736   10.280  7.098   1.00 13.42 ? 70  PHE A CA  1 
ATOM   551  C  C   . PHE A 1 70  ? 5.949   11.790  7.062   1.00 12.86 ? 70  PHE A C   1 
ATOM   552  O  O   . PHE A 1 70  ? 7.047   12.266  7.422   1.00 14.17 ? 70  PHE A O   1 
ATOM   553  C  CB  . PHE A 1 70  ? 4.919   9.924   8.357   1.00 12.73 ? 70  PHE A CB  1 
ATOM   554  C  CG  . PHE A 1 70  ? 4.374   8.520   8.303   1.00 12.86 ? 70  PHE A CG  1 
ATOM   555  C  CD1 . PHE A 1 70  ? 5.204   7.437   8.594   1.00 12.92 ? 70  PHE A CD1 1 
ATOM   556  C  CD2 . PHE A 1 70  ? 3.097   8.293   7.994   1.00 11.75 ? 70  PHE A CD2 1 
ATOM   557  C  CE1 . PHE A 1 70  ? 4.694   6.120   8.432   1.00 13.24 ? 70  PHE A CE1 1 
ATOM   558  C  CE2 . PHE A 1 70  ? 2.577   6.996   7.816   1.00 11.62 ? 70  PHE A CE2 1 
ATOM   559  C  CZ  . PHE A 1 70  ? 3.405   5.912   8.092   1.00 13.93 ? 70  PHE A CZ  1 
ATOM   560  N  N   . ASP A 1 71  ? 4.906   12.511  6.681   1.00 13.73 ? 71  ASP A N   1 
ATOM   561  C  CA  . ASP A 1 71  ? 4.928   13.984  6.848   1.00 13.52 ? 71  ASP A CA  1 
ATOM   562  C  C   . ASP A 1 71  ? 4.682   14.300  8.291   1.00 13.06 ? 71  ASP A C   1 
ATOM   563  O  O   . ASP A 1 71  ? 3.592   14.109  8.823   1.00 16.34 ? 71  ASP A O   1 
ATOM   564  C  CB  . ASP A 1 71  ? 3.785   14.538  5.987   1.00 14.46 ? 71  ASP A CB  1 
ATOM   565  C  CG  . ASP A 1 71  ? 3.482   16.057  6.269   1.00 17.53 ? 71  ASP A CG  1 
ATOM   566  O  OD1 . ASP A 1 71  ? 4.371   16.727  6.846   1.00 15.19 ? 71  ASP A OD1 1 
ATOM   567  O  OD2 . ASP A 1 71  ? 2.368   16.564  6.007   1.00 19.54 ? 71  ASP A OD2 1 
ATOM   568  N  N   . ASP A 1 72  ? 5.758   14.790  8.955   1.00 11.86 ? 72  ASP A N   1 
ATOM   569  C  CA  . ASP A 1 72  ? 5.657   15.191  10.367  1.00 11.92 ? 72  ASP A CA  1 
ATOM   570  C  C   . ASP A 1 72  ? 5.714   16.699  10.543  1.00 13.06 ? 72  ASP A C   1 
ATOM   571  O  O   . ASP A 1 72  ? 6.192   17.211  11.569  1.00 14.10 ? 72  ASP A O   1 
ATOM   572  C  CB  . ASP A 1 72  ? 6.855   14.560  11.135  1.00 12.80 ? 72  ASP A CB  1 
ATOM   573  C  CG  . ASP A 1 72  ? 8.189   15.034  10.653  1.00 14.98 ? 72  ASP A CG  1 
ATOM   574  O  OD1 . ASP A 1 72  ? 8.337   15.676  9.574   1.00 14.77 ? 72  ASP A OD1 1 
ATOM   575  O  OD2 . ASP A 1 72  ? 9.202   14.732  11.328  1.00 15.56 ? 72  ASP A OD2 1 
ATOM   576  N  N   . SER A 1 73  ? 5.203   17.415  9.560   1.00 13.76 ? 73  SER A N   1 
ATOM   577  C  CA  . SER A 1 73  ? 5.241   18.926  9.607   1.00 13.71 ? 73  SER A CA  1 
ATOM   578  C  C   . SER A 1 73  ? 3.938   19.455  10.230  1.00 14.73 ? 73  SER A C   1 
ATOM   579  O  O   . SER A 1 73  ? 3.783   20.676  10.406  1.00 14.20 ? 73  SER A O   1 
ATOM   580  C  CB  . SER A 1 73  ? 5.500   19.482  8.192   1.00 15.33 ? 73  SER A CB  1 
ATOM   581  O  OG  . SER A 1 73  ? 4.326   19.344  7.382   1.00 13.37 ? 73  SER A OG  1 
ATOM   582  N  N   . GLN A 1 74  ? 2.996   18.576  10.578  1.00 18.05 ? 74  GLN A N   1 
ATOM   583  C  CA  . GLN A 1 74  ? 1.832   18.941  11.347  1.00 16.41 ? 74  GLN A CA  1 
ATOM   584  C  C   . GLN A 1 74  ? 1.495   17.774  12.219  1.00 17.78 ? 74  GLN A C   1 
ATOM   585  O  O   . GLN A 1 74  ? 2.042   16.674  12.005  1.00 18.31 ? 74  GLN A O   1 
ATOM   586  C  CB  . GLN A 1 74  ? 0.574   19.231  10.471  1.00 21.23 ? 74  GLN A CB  1 
ATOM   587  C  CG  . GLN A 1 74  ? 0.682   20.267  9.419   1.00 21.77 ? 74  GLN A CG  1 
ATOM   588  C  CD  . GLN A 1 74  ? -0.672  20.426  8.761   1.00 24.06 ? 74  GLN A CD  1 
ATOM   589  O  OE1 . GLN A 1 74  ? -1.576  21.040  9.324   1.00 29.33 ? 74  GLN A OE1 1 
ATOM   590  N  NE2 . GLN A 1 74  ? -0.812  19.868  7.607   1.00 20.46 ? 74  GLN A NE2 1 
ATOM   591  N  N   . ASP A 1 75  ? 0.585   17.994  13.176  1.00 18.15 ? 75  ASP A N   1 
ATOM   592  C  CA  . ASP A 1 75  ? 0.137   16.974  14.135  1.00 20.37 ? 75  ASP A CA  1 
ATOM   593  C  C   . ASP A 1 75  ? -0.856  15.969  13.527  1.00 21.72 ? 75  ASP A C   1 
ATOM   594  O  O   . ASP A 1 75  ? -2.013  15.892  13.955  1.00 30.35 ? 75  ASP A O   1 
ATOM   595  C  CB  . ASP A 1 75  ? -0.515  17.607  15.377  1.00 28.49 ? 75  ASP A CB  1 
ATOM   596  C  CG  . ASP A 1 75  ? 0.496   18.113  16.389  1.00 29.98 ? 75  ASP A CG  1 
ATOM   597  O  OD1 . ASP A 1 75  ? 1.723   18.109  16.118  1.00 33.90 ? 75  ASP A OD1 1 
ATOM   598  O  OD2 . ASP A 1 75  ? 0.022   18.544  17.476  1.00 36.93 ? 75  ASP A OD2 1 
ATOM   599  N  N   A LYS A 1 76  ? -0.375  15.140  12.599  0.50 19.02 ? 76  LYS A N   1 
ATOM   600  N  N   B LYS A 1 76  ? -0.428  15.198  12.578  0.50 18.72 ? 76  LYS A N   1 
ATOM   601  C  CA  A LYS A 1 76  ? -1.186  14.248  11.710  0.50 18.02 ? 76  LYS A CA  1 
ATOM   602  C  CA  B LYS A 1 76  ? -1.380  14.293  12.044  0.50 17.82 ? 76  LYS A CA  1 
ATOM   603  C  C   A LYS A 1 76  ? -1.372  12.786  12.210  0.50 17.52 ? 76  LYS A C   1 
ATOM   604  C  C   B LYS A 1 76  ? -1.306  13.054  12.927  0.50 17.80 ? 76  LYS A C   1 
ATOM   605  O  O   A LYS A 1 76  ? -2.432  12.133  12.091  0.50 16.90 ? 76  LYS A O   1 
ATOM   606  O  O   B LYS A 1 76  ? -2.139  12.892  13.854  0.50 19.20 ? 76  LYS A O   1 
ATOM   607  C  CB  A LYS A 1 76  ? -0.492  14.149  10.341  0.50 18.75 ? 76  LYS A CB  1 
ATOM   608  C  CB  B LYS A 1 76  ? -1.090  14.055  10.590  0.50 17.73 ? 76  LYS A CB  1 
ATOM   609  C  CG  A LYS A 1 76  ? -0.648  15.362  9.444   0.50 20.13 ? 76  LYS A CG  1 
ATOM   610  C  CG  B LYS A 1 76  ? -1.374  15.294  9.782   0.50 16.42 ? 76  LYS A CG  1 
ATOM   611  C  CD  A LYS A 1 76  ? -0.147  15.055  8.045   0.50 20.33 ? 76  LYS A CD  1 
ATOM   612  C  CD  B LYS A 1 76  ? -0.694  15.140  8.447   0.50 17.01 ? 76  LYS A CD  1 
ATOM   613  C  CE  A LYS A 1 76  ? -1.090  15.740  7.058   0.50 21.59 ? 76  LYS A CE  1 
ATOM   614  C  CE  B LYS A 1 76  ? -0.975  16.322  7.542   0.50 17.10 ? 76  LYS A CE  1 
ATOM   615  N  NZ  A LYS A 1 76  ? -0.526  15.898  5.701   0.50 22.61 ? 76  LYS A NZ  1 
ATOM   616  N  NZ  B LYS A 1 76  ? -0.360  16.026  6.237   0.50 15.24 ? 76  LYS A NZ  1 
ATOM   617  N  N   . ALA A 1 77  ? -0.268  12.264  12.699  1.00 17.98 ? 77  ALA A N   1 
ATOM   618  C  CA  . ALA A 1 77  ? -0.136  10.907  13.309  1.00 17.44 ? 77  ALA A CA  1 
ATOM   619  C  C   . ALA A 1 77  ? 0.604   11.111  14.631  1.00 15.86 ? 77  ALA A C   1 
ATOM   620  O  O   . ALA A 1 77  ? 1.795   11.367  14.604  1.00 17.75 ? 77  ALA A O   1 
ATOM   621  C  CB  . ALA A 1 77  ? 0.691   10.089  12.355  1.00 18.77 ? 77  ALA A CB  1 
ATOM   622  N  N   . VAL A 1 78  ? -0.065  11.005  15.750  1.00 14.63 ? 78  VAL A N   1 
ATOM   623  C  CA  . VAL A 1 78  ? 0.562   11.318  17.040  1.00 14.83 ? 78  VAL A CA  1 
ATOM   624  C  C   . VAL A 1 78  ? 0.327   10.263  18.140  1.00 14.96 ? 78  VAL A C   1 
ATOM   625  O  O   . VAL A 1 78  ? -0.657  9.528   18.186  1.00 15.00 ? 78  VAL A O   1 
ATOM   626  C  CB  . VAL A 1 78  ? 0.205   12.736  17.631  1.00 17.58 ? 78  VAL A CB  1 
ATOM   627  C  CG1 . VAL A 1 78  ? 0.490   13.920  16.671  1.00 18.85 ? 78  VAL A CG1 1 
ATOM   628  C  CG2 . VAL A 1 78  ? -1.237  12.698  18.134  1.00 18.47 ? 78  VAL A CG2 1 
ATOM   629  N  N   . LEU A 1 79  ? 1.360   10.119  18.960  1.00 12.40 ? 79  LEU A N   1 
ATOM   630  C  CA  . LEU A 1 79  ? 1.293   9.319   20.130  1.00 14.08 ? 79  LEU A CA  1 
ATOM   631  C  C   . LEU A 1 79  ? 1.300   10.220  21.329  1.00 15.60 ? 79  LEU A C   1 
ATOM   632  O  O   . LEU A 1 79  ? 2.068   11.222  21.418  1.00 13.20 ? 79  LEU A O   1 
ATOM   633  C  CB  . LEU A 1 79  ? 2.512   8.352   20.123  1.00 14.44 ? 79  LEU A CB  1 
ATOM   634  C  CG  . LEU A 1 79  ? 2.624   7.336   21.218  1.00 13.85 ? 79  LEU A CG  1 
ATOM   635  C  CD1 . LEU A 1 79  ? 1.522   6.279   21.016  1.00 15.28 ? 79  LEU A CD1 1 
ATOM   636  C  CD2 . LEU A 1 79  ? 3.947   6.628   21.118  1.00 13.67 ? 79  LEU A CD2 1 
ATOM   637  N  N   . LYS A 1 80  ? 0.393   9.948   22.244  1.00 15.44 ? 80  LYS A N   1 
ATOM   638  C  CA  . LYS A 1 80  ? 0.359   10.601  23.542  1.00 16.24 ? 80  LYS A CA  1 
ATOM   639  C  C   . LYS A 1 80  ? -0.203  9.704   24.634  1.00 15.06 ? 80  LYS A C   1 
ATOM   640  O  O   . LYS A 1 80  ? -0.456  8.495   24.359  1.00 14.48 ? 80  LYS A O   1 
ATOM   641  C  CB  . LYS A 1 80  ? -0.315  11.978  23.515  1.00 21.63 ? 80  LYS A CB  1 
ATOM   642  C  CG  . LYS A 1 80  ? -1.708  11.887  22.918  1.00 26.20 ? 80  LYS A CG  1 
ATOM   643  C  CD  . LYS A 1 80  ? -2.344  13.249  22.628  1.00 29.96 ? 80  LYS A CD  1 
ATOM   644  N  N   . GLY A 1 81  ? -0.360  10.249  25.843  1.00 15.41 ? 81  GLY A N   1 
ATOM   645  C  CA  . GLY A 1 81  ? -0.884  9.445   26.924  1.00 16.98 ? 81  GLY A CA  1 
ATOM   646  C  C   . GLY A 1 81  ? 0.099   8.358   27.275  1.00 18.56 ? 81  GLY A C   1 
ATOM   647  O  O   . GLY A 1 81  ? 1.330   8.549   27.158  1.00 15.67 ? 81  GLY A O   1 
ATOM   648  N  N   . GLY A 1 82  ? -0.404  7.196   27.681  1.00 16.77 ? 82  GLY A N   1 
ATOM   649  C  CA  . GLY A 1 82  ? 0.566   6.172   28.135  1.00 17.77 ? 82  GLY A CA  1 
ATOM   650  C  C   . GLY A 1 82  ? 1.466   6.757   29.244  1.00 18.19 ? 82  GLY A C   1 
ATOM   651  O  O   . GLY A 1 82  ? 0.985   7.477   30.150  1.00 24.46 ? 82  GLY A O   1 
ATOM   652  N  N   . PRO A 1 83  ? 2.803   6.570   29.181  1.00 16.99 ? 83  PRO A N   1 
ATOM   653  C  CA  . PRO A 1 83  ? 3.663   7.159   30.168  1.00 15.30 ? 83  PRO A CA  1 
ATOM   654  C  C   . PRO A 1 83  ? 4.142   8.578   29.789  1.00 18.32 ? 83  PRO A C   1 
ATOM   655  O  O   . PRO A 1 83  ? 4.955   9.177   30.462  1.00 19.43 ? 83  PRO A O   1 
ATOM   656  C  CB  . PRO A 1 83  ? 4.897   6.207   30.142  1.00 17.51 ? 83  PRO A CB  1 
ATOM   657  C  CG  . PRO A 1 83  ? 4.985   5.844   28.698  1.00 14.29 ? 83  PRO A CG  1 
ATOM   658  C  CD  . PRO A 1 83  ? 3.554   5.702   28.234  1.00 14.16 ? 83  PRO A CD  1 
ATOM   659  N  N   . LEU A 1 84  ? 3.590   9.140   28.740  1.00 17.02 ? 84  LEU A N   1 
ATOM   660  C  CA  . LEU A 1 84  ? 4.181   10.341  28.110  1.00 16.72 ? 84  LEU A CA  1 
ATOM   661  C  C   . LEU A 1 84  ? 3.473   11.592  28.634  1.00 21.02 ? 84  LEU A C   1 
ATOM   662  O  O   . LEU A 1 84  ? 2.284   11.554  28.924  1.00 19.66 ? 84  LEU A O   1 
ATOM   663  C  CB  . LEU A 1 84  ? 4.024   10.318  26.579  1.00 14.94 ? 84  LEU A CB  1 
ATOM   664  C  CG  . LEU A 1 84  ? 4.617   9.021   25.944  1.00 12.38 ? 84  LEU A CG  1 
ATOM   665  C  CD1 . LEU A 1 84  ? 4.206   8.938   24.486  1.00 13.40 ? 84  LEU A CD1 1 
ATOM   666  C  CD2 . LEU A 1 84  ? 6.184   9.007   26.101  1.00 12.83 ? 84  LEU A CD2 1 
ATOM   667  N  N   . ASP A 1 85  ? 4.198   12.694  28.673  1.00 21.11 ? 85  ASP A N   1 
ATOM   668  C  CA  . ASP A 1 85  ? 3.624   13.970  29.040  1.00 22.23 ? 85  ASP A CA  1 
ATOM   669  C  C   . ASP A 1 85  ? 3.436   14.772  27.802  1.00 19.33 ? 85  ASP A C   1 
ATOM   670  O  O   . ASP A 1 85  ? 2.598   15.595  27.702  1.00 21.95 ? 85  ASP A O   1 
ATOM   671  C  CB  . ASP A 1 85  ? 4.550   14.652  30.027  1.00 23.12 ? 85  ASP A CB  1 
ATOM   672  C  CG  . ASP A 1 85  ? 4.379   14.147  31.421  1.00 26.68 ? 85  ASP A CG  1 
ATOM   673  O  OD1 . ASP A 1 85  ? 3.290   13.742  31.802  1.00 30.16 ? 85  ASP A OD1 1 
ATOM   674  O  OD2 . ASP A 1 85  ? 5.362   14.179  32.169  1.00 29.24 ? 85  ASP A OD2 1 
ATOM   675  N  N   . GLY A 1 86  ? 4.210   14.530  26.805  1.00 18.22 ? 86  GLY A N   1 
ATOM   676  C  CA  . GLY A 1 86  ? 4.015   15.286  25.642  1.00 17.62 ? 86  GLY A CA  1 
ATOM   677  C  C   . GLY A 1 86  ? 3.196   14.687  24.549  1.00 17.36 ? 86  GLY A C   1 
ATOM   678  O  O   . GLY A 1 86  ? 2.618   13.655  24.744  1.00 16.24 ? 86  GLY A O   1 
ATOM   679  N  N   . THR A 1 87  ? 3.157   15.376  23.424  1.00 17.79 ? 87  THR A N   1 
ATOM   680  C  CA  . THR A 1 87  ? 2.613   14.906  22.198  1.00 18.12 ? 87  THR A CA  1 
ATOM   681  C  C   . THR A 1 87  ? 3.780   14.592  21.322  1.00 14.93 ? 87  THR A C   1 
ATOM   682  O  O   . THR A 1 87  ? 4.668   15.351  21.234  1.00 16.10 ? 87  THR A O   1 
ATOM   683  C  CB  . THR A 1 87  ? 1.799   16.005  21.526  1.00 22.38 ? 87  THR A CB  1 
ATOM   684  O  OG1 . THR A 1 87  ? 0.619   16.194  22.298  1.00 27.69 ? 87  THR A OG1 1 
ATOM   685  C  CG2 . THR A 1 87  ? 1.444   15.608  20.114  1.00 22.23 ? 87  THR A CG2 1 
ATOM   686  N  N   . TYR A 1 88  ? 3.774   13.431  20.700  1.00 14.09 ? 88  TYR A N   1 
ATOM   687  C  CA  . TYR A 1 88  ? 4.897   12.984  19.908  1.00 13.34 ? 88  TYR A CA  1 
ATOM   688  C  C   . TYR A 1 88  ? 4.447   12.642  18.523  1.00 13.40 ? 88  TYR A C   1 
ATOM   689  O  O   . TYR A 1 88  ? 3.423   11.913  18.379  1.00 16.25 ? 88  TYR A O   1 
ATOM   690  C  CB  . TYR A 1 88  ? 5.513   11.740  20.544  1.00 11.73 ? 88  TYR A CB  1 
ATOM   691  C  CG  . TYR A 1 88  ? 6.312   11.955  21.833  1.00 9.83  ? 88  TYR A CG  1 
ATOM   692  C  CD1 . TYR A 1 88  ? 5.647   12.248  22.988  1.00 10.05 ? 88  TYR A CD1 1 
ATOM   693  C  CD2 . TYR A 1 88  ? 7.737   11.802  21.883  1.00 9.96  ? 88  TYR A CD2 1 
ATOM   694  C  CE1 . TYR A 1 88  ? 6.292   12.456  24.234  1.00 10.24 ? 88  TYR A CE1 1 
ATOM   695  C  CE2 . TYR A 1 88  ? 8.445   12.005  23.104  1.00 9.71  ? 88  TYR A CE2 1 
ATOM   696  C  CZ  . TYR A 1 88  ? 7.711   12.268  24.270  1.00 10.07 ? 88  TYR A CZ  1 
ATOM   697  O  OH  . TYR A 1 88  ? 8.350   12.436  25.459  1.00 12.17 ? 88  TYR A OH  1 
ATOM   698  N  N   . ARG A 1 89  ? 5.117   13.170  17.523  1.00 10.98 ? 89  ARG A N   1 
ATOM   699  C  CA  . ARG A 1 89  ? 4.716   13.053  16.099  1.00 14.03 ? 89  ARG A CA  1 
ATOM   700  C  C   . ARG A 1 89  ? 5.384   11.879  15.468  1.00 9.81  ? 89  ARG A C   1 
ATOM   701  O  O   . ARG A 1 89  ? 6.646   11.754  15.509  1.00 9.29  ? 89  ARG A O   1 
ATOM   702  C  CB  . ARG A 1 89  ? 5.109   14.244  15.223  1.00 16.19 ? 89  ARG A CB  1 
ATOM   703  C  CG  . ARG A 1 89  ? 4.261   15.476  15.438  1.00 18.97 ? 89  ARG A CG  1 
ATOM   704  C  CD  . ARG A 1 89  ? 4.569   16.485  14.348  1.00 18.61 ? 89  ARG A CD  1 
ATOM   705  N  NE  . ARG A 1 89  ? 3.850   17.710  14.649  1.00 21.34 ? 89  ARG A NE  1 
ATOM   706  C  CZ  . ARG A 1 89  ? 4.166   18.911  14.213  1.00 21.14 ? 89  ARG A CZ  1 
ATOM   707  N  NH1 . ARG A 1 89  ? 5.247   19.125  13.521  1.00 18.25 ? 89  ARG A NH1 1 
ATOM   708  N  NH2 . ARG A 1 89  ? 3.385   19.950  14.594  1.00 28.01 ? 89  ARG A NH2 1 
ATOM   709  N  N   . LEU A 1 90  ? 4.635   11.047  14.732  1.00 9.66  ? 90  LEU A N   1 
ATOM   710  C  CA  . LEU A 1 90  ? 5.255   9.997   13.929  1.00 9.68  ? 90  LEU A CA  1 
ATOM   711  C  C   . LEU A 1 90  ? 6.097   10.477  12.803  1.00 9.72  ? 90  LEU A C   1 
ATOM   712  O  O   . LEU A 1 90  ? 5.561   11.262  11.924  1.00 12.93 ? 90  LEU A O   1 
ATOM   713  C  CB  . LEU A 1 90  ? 4.135   9.064   13.378  1.00 10.60 ? 90  LEU A CB  1 
ATOM   714  C  CG  . LEU A 1 90  ? 4.623   7.896   12.493  1.00 9.87  ? 90  LEU A CG  1 
ATOM   715  C  CD1 . LEU A 1 90  ? 5.387   6.840   13.265  1.00 10.21 ? 90  LEU A CD1 1 
ATOM   716  C  CD2 . LEU A 1 90  ? 3.403   7.189   11.860  1.00 11.84 ? 90  LEU A CD2 1 
ATOM   717  N  N   . ILE A 1 91  ? 7.348   10.096  12.726  1.00 9.00  ? 91  ILE A N   1 
ATOM   718  C  CA  . ILE A 1 91  ? 8.253   10.440  11.635  1.00 8.76  ? 91  ILE A CA  1 
ATOM   719  C  C   . ILE A 1 91  ? 8.528   9.267   10.681  1.00 10.00 ? 91  ILE A C   1 
ATOM   720  O  O   . ILE A 1 91  ? 8.534   9.450   9.443   1.00 10.69 ? 91  ILE A O   1 
ATOM   721  C  CB  . ILE A 1 91  ? 9.566   11.157  12.159  1.00 9.32  ? 91  ILE A CB  1 
ATOM   722  C  CG1 . ILE A 1 91  ? 10.506  11.468  10.961  1.00 11.37 ? 91  ILE A CG1 1 
ATOM   723  C  CG2 . ILE A 1 91  ? 10.349  10.324  13.133  1.00 10.69 ? 91  ILE A CG2 1 
ATOM   724  C  CD1 . ILE A 1 91  ? 11.664  12.388  11.343  1.00 14.68 ? 91  ILE A CD1 1 
ATOM   725  N  N   A GLN A 1 92  ? 8.692   8.044   11.207  0.50 9.30  ? 92  GLN A N   1 
ATOM   726  N  N   B GLN A 1 92  ? 8.776   8.064   11.198  0.50 9.54  ? 92  GLN A N   1 
ATOM   727  C  CA  A GLN A 1 92  ? 8.987   6.893   10.328  0.50 8.57  ? 92  GLN A CA  1 
ATOM   728  C  CA  B GLN A 1 92  ? 8.892   6.912   10.305  0.50 8.84  ? 92  GLN A CA  1 
ATOM   729  C  C   A GLN A 1 92  ? 8.855   5.623   11.098  0.50 7.71  ? 92  GLN A C   1 
ATOM   730  C  C   B GLN A 1 92  ? 8.674   5.654   11.133  0.50 7.97  ? 92  GLN A C   1 
ATOM   731  O  O   A GLN A 1 92  ? 9.015   5.619   12.264  0.50 6.97  ? 92  GLN A O   1 
ATOM   732  O  O   B GLN A 1 92  ? 8.468   5.729   12.360  0.50 7.13  ? 92  GLN A O   1 
ATOM   733  C  CB  A GLN A 1 92  ? 10.430  6.885   9.870   0.50 10.18 ? 92  GLN A CB  1 
ATOM   734  C  CB  B GLN A 1 92  ? 10.214  6.908   9.482   0.50 10.63 ? 92  GLN A CB  1 
ATOM   735  C  CG  A GLN A 1 92  ? 11.431  7.017   11.005  0.50 9.11  ? 92  GLN A CG  1 
ATOM   736  C  CG  B GLN A 1 92  ? 11.571  6.907   10.263  0.50 9.91  ? 92  GLN A CG  1 
ATOM   737  C  CD  A GLN A 1 92  ? 12.219  5.758   11.335  0.50 8.76  ? 92  GLN A CD  1 
ATOM   738  C  CD  B GLN A 1 92  ? 12.112  5.535   10.643  0.50 12.66 ? 92  GLN A CD  1 
ATOM   739  O  OE1 A GLN A 1 92  ? 11.862  4.582   11.015  0.50 7.48  ? 92  GLN A OE1 1 
ATOM   740  O  OE1 B GLN A 1 92  ? 11.527  4.791   11.418  0.50 10.79 ? 92  GLN A OE1 1 
ATOM   741  N  NE2 A GLN A 1 92  ? 13.305  5.992   11.954  0.50 10.36 ? 92  GLN A NE2 1 
ATOM   742  N  NE2 B GLN A 1 92  ? 13.170  5.177   10.024  0.50 12.81 ? 92  GLN A NE2 1 
ATOM   743  N  N   . PHE A 1 93  ? 8.529   4.535   10.415  1.00 7.61  ? 93  PHE A N   1 
ATOM   744  C  CA  . PHE A 1 93  ? 8.693   3.220   11.027  1.00 7.31  ? 93  PHE A CA  1 
ATOM   745  C  C   . PHE A 1 93  ? 9.601   2.359   10.200  1.00 7.50  ? 93  PHE A C   1 
ATOM   746  O  O   . PHE A 1 93  ? 9.900   2.569   9.007   1.00 8.39  ? 93  PHE A O   1 
ATOM   747  C  CB  . PHE A 1 93  ? 7.298   2.539   11.268  1.00 8.06  ? 93  PHE A CB  1 
ATOM   748  C  CG  . PHE A 1 93  ? 6.563   2.051   10.004  1.00 8.93  ? 93  PHE A CG  1 
ATOM   749  C  CD1 . PHE A 1 93  ? 6.967   0.912   9.304   1.00 10.49 ? 93  PHE A CD1 1 
ATOM   750  C  CD2 . PHE A 1 93  ? 5.440   2.801   9.569   1.00 9.77  ? 93  PHE A CD2 1 
ATOM   751  C  CE1 . PHE A 1 93  ? 6.262   0.441   8.200   1.00 11.22 ? 93  PHE A CE1 1 
ATOM   752  C  CE2 . PHE A 1 93  ? 4.746   2.282   8.467   1.00 11.39 ? 93  PHE A CE2 1 
ATOM   753  C  CZ  . PHE A 1 93  ? 5.189   1.164   7.779   1.00 11.38 ? 93  PHE A CZ  1 
ATOM   754  N  N   . HIS A 1 94  ? 10.165  1.318   10.849  1.00 7.10  ? 94  HIS A N   1 
ATOM   755  C  CA  . HIS A 1 94  ? 11.034  0.365   10.283  1.00 7.10  ? 94  HIS A CA  1 
ATOM   756  C  C   . HIS A 1 94  ? 10.995  -0.877  11.115  1.00 6.92  ? 94  HIS A C   1 
ATOM   757  O  O   . HIS A 1 94  ? 10.276  -0.928  12.122  1.00 7.88  ? 94  HIS A O   1 
ATOM   758  C  CB  . HIS A 1 94  ? 12.519  0.849   10.193  1.00 7.26  ? 94  HIS A CB  1 
ATOM   759  C  CG  . HIS A 1 94  ? 13.091  1.147   11.576  1.00 7.00  ? 94  HIS A CG  1 
ATOM   760  N  ND1 . HIS A 1 94  ? 12.873  2.374   12.188  1.00 8.81  ? 94  HIS A ND1 1 
ATOM   761  C  CD2 . HIS A 1 94  ? 13.723  0.323   12.524  1.00 7.79  ? 94  HIS A CD2 1 
ATOM   762  C  CE1 . HIS A 1 94  ? 13.378  2.305   13.391  1.00 6.55  ? 94  HIS A CE1 1 
ATOM   763  N  NE2 . HIS A 1 94  ? 13.883  1.079   13.636  1.00 7.28  ? 94  HIS A NE2 1 
ATOM   764  N  N   . PHE A 1 95  ? 11.635  -1.911  10.624  1.00 7.26  ? 95  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 95  ? 11.684  -3.199  11.292  1.00 6.89  ? 95  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 95  ? 13.128  -3.683  11.446  1.00 7.08  ? 95  PHE A C   1 
ATOM   767  O  O   . PHE A 1 95  ? 14.044  -3.222  10.769  1.00 8.44  ? 95  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 95  ? 11.007  -4.307  10.430  1.00 7.43  ? 95  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 95  ? 9.522   -4.037  10.110  1.00 7.47  ? 95  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 95  ? 9.168   -3.164  9.066   1.00 7.53  ? 95  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 95  ? 8.495   -4.691  10.824  1.00 8.13  ? 95  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 95  ? 7.824   -2.967  8.726   1.00 7.72  ? 95  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 95  ? 7.158   -4.440  10.546  1.00 8.05  ? 95  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 95  ? 6.808   -3.581  9.445   1.00 7.67  ? 95  PHE A CZ  1 
ATOM   775  N  N   . HIS A 1 96  ? 13.263  -4.644  12.367  1.00 7.30  ? 96  HIS A N   1 
ATOM   776  C  CA  . HIS A 1 96  ? 14.473  -5.444  12.593  1.00 7.74  ? 96  HIS A CA  1 
ATOM   777  C  C   . HIS A 1 96  ? 14.055  -6.868  12.423  1.00 8.43  ? 96  HIS A C   1 
ATOM   778  O  O   . HIS A 1 96  ? 13.014  -7.257  12.978  1.00 8.07  ? 96  HIS A O   1 
ATOM   779  C  CB  . HIS A 1 96  ? 15.100  -5.209  13.962  1.00 7.51  ? 96  HIS A CB  1 
ATOM   780  C  CG  . HIS A 1 96  ? 15.398  -3.760  14.227  1.00 7.59  ? 96  HIS A CG  1 
ATOM   781  N  ND1 . HIS A 1 96  ? 16.663  -3.253  14.051  1.00 7.25  ? 96  HIS A ND1 1 
ATOM   782  C  CD2 . HIS A 1 96  ? 14.578  -2.714  14.610  1.00 8.07  ? 96  HIS A CD2 1 
ATOM   783  C  CE1 . HIS A 1 96  ? 16.625  -1.911  14.426  1.00 8.21  ? 96  HIS A CE1 1 
ATOM   784  N  NE2 . HIS A 1 96  ? 15.330  -1.594  14.706  1.00 8.81  ? 96  HIS A NE2 1 
ATOM   785  N  N   . TRP A 1 97  ? 14.827  -7.685  11.686  1.00 7.78  ? 97  TRP A N   1 
ATOM   786  C  CA  . TRP A 1 97  ? 14.424  -9.112  11.550  1.00 7.62  ? 97  TRP A CA  1 
ATOM   787  C  C   . TRP A 1 97  ? 15.619  -10.025 11.443  1.00 7.95  ? 97  TRP A C   1 
ATOM   788  O  O   . TRP A 1 97  ? 16.824  -9.573  11.327  1.00 8.50  ? 97  TRP A O   1 
ATOM   789  C  CB  . TRP A 1 97  ? 13.530  -9.300  10.312  1.00 8.56  ? 97  TRP A CB  1 
ATOM   790  C  CG  . TRP A 1 97  ? 14.205  -8.870  9.019   1.00 8.48  ? 97  TRP A CG  1 
ATOM   791  C  CD1 . TRP A 1 97  ? 14.961  -9.670  8.197   1.00 9.30  ? 97  TRP A CD1 1 
ATOM   792  C  CD2 . TRP A 1 97  ? 14.294  -7.493  8.498   1.00 8.55  ? 97  TRP A CD2 1 
ATOM   793  N  NE1 . TRP A 1 97  ? 15.381  -8.939  7.085   1.00 10.52 ? 97  TRP A NE1 1 
ATOM   794  C  CE2 . TRP A 1 97  ? 15.053  -7.590  7.250   1.00 9.52  ? 97  TRP A CE2 1 
ATOM   795  C  CE3 . TRP A 1 97  ? 13.748  -6.268  8.890   1.00 8.76  ? 97  TRP A CE3 1 
ATOM   796  C  CZ2 . TRP A 1 97  ? 15.264  -6.499  6.438   1.00 10.45 ? 97  TRP A CZ2 1 
ATOM   797  C  CZ3 . TRP A 1 97  ? 14.004  -5.122  8.078   1.00 9.29  ? 97  TRP A CZ3 1 
ATOM   798  C  CH2 . TRP A 1 97  ? 14.758  -5.246  6.910   1.00 9.58  ? 97  TRP A CH2 1 
ATOM   799  N  N   . GLY A 1 98  ? 15.355  -11.341 11.449  1.00 7.56  ? 98  GLY A N   1 
ATOM   800  C  CA  . GLY A 1 98  ? 16.386  -12.366 11.472  1.00 9.32  ? 98  GLY A CA  1 
ATOM   801  C  C   . GLY A 1 98  ? 16.595  -13.106 10.125  1.00 9.04  ? 98  GLY A C   1 
ATOM   802  O  O   . GLY A 1 98  ? 15.875  -12.867 9.169   1.00 9.88  ? 98  GLY A O   1 
ATOM   803  N  N   . SER A 1 99  ? 17.592  -13.984 10.187  1.00 10.28 ? 99  SER A N   1 
ATOM   804  C  CA  . SER A 1 99  ? 17.883  -14.885 9.068   1.00 10.86 ? 99  SER A CA  1 
ATOM   805  C  C   . SER A 1 99  ? 16.980  -16.123 9.182   1.00 12.82 ? 99  SER A C   1 
ATOM   806  O  O   . SER A 1 99  ? 16.914  -16.900 8.184   1.00 15.62 ? 99  SER A O   1 
ATOM   807  C  CB  . SER A 1 99  ? 19.376  -15.231 9.143   1.00 11.96 ? 99  SER A CB  1 
ATOM   808  O  OG  . SER A 1 99  ? 19.770  -15.807 10.344  1.00 14.75 ? 99  SER A OG  1 
ATOM   809  N  N   . LEU A 1 100 ? 16.343  -16.352 10.350  1.00 12.49 ? 100 LEU A N   1 
ATOM   810  C  CA  . LEU A 1 100 ? 15.534  -17.505 10.671  1.00 13.33 ? 100 LEU A CA  1 
ATOM   811  C  C   . LEU A 1 100 ? 14.407  -17.011 11.519  1.00 11.43 ? 100 LEU A C   1 
ATOM   812  O  O   . LEU A 1 100 ? 14.552  -15.983 12.201  1.00 11.33 ? 100 LEU A O   1 
ATOM   813  C  CB  . LEU A 1 100 ? 16.341  -18.440 11.588  1.00 18.58 ? 100 LEU A CB  1 
ATOM   814  C  CG  . LEU A 1 100 ? 17.655  -18.876 10.999  1.00 24.61 ? 100 LEU A CG  1 
ATOM   815  C  CD1 . LEU A 1 100 ? 18.709  -18.980 12.082  1.00 30.81 ? 100 LEU A CD1 1 
ATOM   816  C  CD2 . LEU A 1 100 ? 17.414  -20.183 10.228  1.00 28.18 ? 100 LEU A CD2 1 
ATOM   817  N  N   . ASP A 1 101 ? 13.283  -17.699 11.509  1.00 10.84 ? 101 ASP A N   1 
ATOM   818  C  CA  . ASP A 1 101 ? 12.126  -17.265 12.330  1.00 11.14 ? 101 ASP A CA  1 
ATOM   819  C  C   . ASP A 1 101 ? 12.363  -17.195 13.819  1.00 12.71 ? 101 ASP A C   1 
ATOM   820  O  O   . ASP A 1 101 ? 11.648  -16.464 14.539  1.00 14.07 ? 101 ASP A O   1 
ATOM   821  C  CB  . ASP A 1 101 ? 10.916  -18.169 12.060  1.00 11.53 ? 101 ASP A CB  1 
ATOM   822  C  CG  . ASP A 1 101 ? 10.434  -18.084 10.625  1.00 14.95 ? 101 ASP A CG  1 
ATOM   823  O  OD1 . ASP A 1 101 ? 10.916  -17.206 9.883   1.00 13.90 ? 101 ASP A OD1 1 
ATOM   824  O  OD2 . ASP A 1 101 ? 9.568   -18.901 10.240  1.00 17.65 ? 101 ASP A OD2 1 
ATOM   825  N  N   . GLY A 1 102 ? 13.374  -17.948 14.331  1.00 11.38 ? 102 GLY A N   1 
ATOM   826  C  CA  . GLY A 1 102 ? 13.752  -17.948 15.738  1.00 12.16 ? 102 GLY A CA  1 
ATOM   827  C  C   . GLY A 1 102 ? 14.518  -16.786 16.319  1.00 10.95 ? 102 GLY A C   1 
ATOM   828  O  O   . GLY A 1 102 ? 14.844  -16.780 17.501  1.00 12.88 ? 102 GLY A O   1 
ATOM   829  N  N   . GLN A 1 103 ? 14.765  -15.771 15.472  1.00 10.30 ? 103 GLN A N   1 
ATOM   830  C  CA  . GLN A 1 103 ? 15.506  -14.563 15.952  1.00 9.09  ? 103 GLN A CA  1 
ATOM   831  C  C   . GLN A 1 103 ? 15.168  -13.409 15.103  1.00 8.10  ? 103 GLN A C   1 
ATOM   832  O  O   . GLN A 1 103 ? 14.579  -13.602 14.001  1.00 9.19  ? 103 GLN A O   1 
ATOM   833  C  CB  . GLN A 1 103 ? 17.015  -14.812 15.985  1.00 11.71 ? 103 GLN A CB  1 
ATOM   834  C  CG  . GLN A 1 103 ? 17.621  -14.962 14.573  1.00 13.13 ? 103 GLN A CG  1 
ATOM   835  C  CD  . GLN A 1 103 ? 19.011  -15.599 14.633  1.00 18.84 ? 103 GLN A CD  1 
ATOM   836  O  OE1 . GLN A 1 103 ? 19.191  -16.616 15.316  1.00 21.47 ? 103 GLN A OE1 1 
ATOM   837  N  NE2 . GLN A 1 103 ? 19.944  -15.080 13.871  1.00 17.20 ? 103 GLN A NE2 1 
ATOM   838  N  N   . GLY A 1 104 ? 15.514  -12.210 15.586  1.00 8.28  ? 104 GLY A N   1 
ATOM   839  C  CA  . GLY A 1 104 ? 15.197  -11.047 14.785  1.00 8.00  ? 104 GLY A CA  1 
ATOM   840  C  C   . GLY A 1 104 ? 14.768  -9.844  15.639  1.00 7.24  ? 104 GLY A C   1 
ATOM   841  O  O   . GLY A 1 104 ? 15.005  -8.673  15.279  1.00 7.53  ? 104 GLY A O   1 
ATOM   842  N  N   . SER A 1 105 ? 14.012  -10.116 16.717  1.00 6.14  ? 105 SER A N   1 
ATOM   843  C  CA  . SER A 1 105 ? 13.620  -8.971  17.559  1.00 6.89  ? 105 SER A CA  1 
ATOM   844  C  C   . SER A 1 105 ? 14.823  -8.431  18.319  1.00 6.69  ? 105 SER A C   1 
ATOM   845  O  O   . SER A 1 105 ? 15.876  -9.150  18.558  1.00 6.77  ? 105 SER A O   1 
ATOM   846  C  CB  . SER A 1 105 ? 12.505  -9.329  18.550  1.00 6.42  ? 105 SER A CB  1 
ATOM   847  O  OG  . SER A 1 105 ? 12.907  -10.291 19.524  1.00 6.61  ? 105 SER A OG  1 
ATOM   848  N  N   . GLU A 1 106 ? 14.681  -7.181  18.702  1.00 6.42  ? 106 GLU A N   1 
ATOM   849  C  CA  . GLU A 1 106 ? 15.763  -6.505  19.588  1.00 6.20  ? 106 GLU A CA  1 
ATOM   850  C  C   . GLU A 1 106 ? 15.402  -6.699  21.084  1.00 6.37  ? 106 GLU A C   1 
ATOM   851  O  O   . GLU A 1 106 ? 16.157  -7.296  21.910  1.00 6.88  ? 106 GLU A O   1 
ATOM   852  C  CB  . GLU A 1 106 ? 15.817  -5.032  19.134  1.00 6.14  ? 106 GLU A CB  1 
ATOM   853  C  CG  . GLU A 1 106 ? 16.323  -4.910  17.737  1.00 6.99  ? 106 GLU A CG  1 
ATOM   854  C  CD  . GLU A 1 106 ? 16.884  -3.572  17.429  1.00 8.56  ? 106 GLU A CD  1 
ATOM   855  O  OE1 . GLU A 1 106 ? 16.295  -2.461  17.590  1.00 7.58  ? 106 GLU A OE1 1 
ATOM   856  O  OE2 . GLU A 1 106 ? 18.043  -3.646  16.952  1.00 8.23  ? 106 GLU A OE2 1 
ATOM   857  N  N   . HIS A 1 107 ? 14.187  -6.207  21.472  1.00 6.23  ? 107 HIS A N   1 
ATOM   858  C  CA  . HIS A 1 107 ? 13.722  -6.609  22.806  1.00 5.79  ? 107 HIS A CA  1 
ATOM   859  C  C   . HIS A 1 107 ? 13.398  -8.078  22.817  1.00 6.65  ? 107 HIS A C   1 
ATOM   860  O  O   . HIS A 1 107 ? 13.085  -8.712  21.769  1.00 6.80  ? 107 HIS A O   1 
ATOM   861  C  CB  . HIS A 1 107 ? 12.487  -5.774  23.208  1.00 5.69  ? 107 HIS A CB  1 
ATOM   862  C  CG  . HIS A 1 107 ? 12.840  -4.320  23.363  1.00 5.53  ? 107 HIS A CG  1 
ATOM   863  N  ND1 . HIS A 1 107 ? 12.768  -3.416  22.294  1.00 5.78  ? 107 HIS A ND1 1 
ATOM   864  C  CD2 . HIS A 1 107 ? 13.255  -3.602  24.462  1.00 6.01  ? 107 HIS A CD2 1 
ATOM   865  C  CE1 . HIS A 1 107 ? 13.189  -2.227  22.709  1.00 6.18  ? 107 HIS A CE1 1 
ATOM   866  N  NE2 . HIS A 1 107 ? 13.479  -2.322  24.034  1.00 5.50  ? 107 HIS A NE2 1 
ATOM   867  N  N   . THR A 1 108 ? 13.575  -8.659  23.999  1.00 7.03  ? 108 THR A N   1 
ATOM   868  C  CA  . THR A 1 108 ? 13.201  -10.063 24.213  1.00 6.86  ? 108 THR A CA  1 
ATOM   869  C  C   . THR A 1 108 ? 12.194  -10.069 25.409  1.00 6.93  ? 108 THR A C   1 
ATOM   870  O  O   . THR A 1 108 ? 12.183  -9.156  26.217  1.00 8.08  ? 108 THR A O   1 
ATOM   871  C  CB  . THR A 1 108 ? 14.405  -10.995 24.446  1.00 7.11  ? 108 THR A CB  1 
ATOM   872  O  OG1 . THR A 1 108 ? 15.200  -10.481 25.544  1.00 9.54  ? 108 THR A OG1 1 
ATOM   873  C  CG2 . THR A 1 108 ? 15.251  -11.132 23.175  1.00 7.47  ? 108 THR A CG2 1 
ATOM   874  N  N   . VAL A 1 109 ? 11.429  -11.162 25.548  1.00 8.67  ? 109 VAL A N   1 
ATOM   875  C  CA  . VAL A 1 109 ? 10.415  -11.252 26.674  1.00 8.99  ? 109 VAL A CA  1 
ATOM   876  C  C   . VAL A 1 109 ? 10.756  -12.565 27.369  1.00 10.63 ? 109 VAL A C   1 
ATOM   877  O  O   . VAL A 1 109 ? 10.609  -13.662 26.788  1.00 10.19 ? 109 VAL A O   1 
ATOM   878  C  CB  . VAL A 1 109 ? 8.979   -11.293 26.106  1.00 9.28  ? 109 VAL A CB  1 
ATOM   879  C  CG1 . VAL A 1 109 ? 7.934   -11.387 27.212  1.00 10.11 ? 109 VAL A CG1 1 
ATOM   880  C  CG2 . VAL A 1 109 ? 8.692   -9.984  25.291  1.00 9.52  ? 109 VAL A CG2 1 
ATOM   881  N  N   . ASP A 1 110 ? 11.182  -12.466 28.613  1.00 9.69  ? 110 ASP A N   1 
ATOM   882  C  CA  . ASP A 1 110 ? 11.685  -13.710 29.358  1.00 10.75 ? 110 ASP A CA  1 
ATOM   883  C  C   . ASP A 1 110 ? 12.662  -14.490 28.455  1.00 10.99 ? 110 ASP A C   1 
ATOM   884  O  O   . ASP A 1 110 ? 12.652  -15.740 28.351  1.00 11.78 ? 110 ASP A O   1 
ATOM   885  C  CB  . ASP A 1 110 ? 10.491  -14.563 29.849  1.00 11.64 ? 110 ASP A CB  1 
ATOM   886  C  CG  . ASP A 1 110 ? 9.585   -13.793 30.810  1.00 11.15 ? 110 ASP A CG  1 
ATOM   887  O  OD1 . ASP A 1 110 ? 10.124  -12.968 31.509  1.00 13.47 ? 110 ASP A OD1 1 
ATOM   888  O  OD2 . ASP A 1 110 ? 8.372   -14.094 30.850  1.00 16.79 ? 110 ASP A OD2 1 
ATOM   889  N  N   . LYS A 1 111 ? 13.566  -13.748 27.826  1.00 11.10 ? 111 LYS A N   1 
ATOM   890  C  CA  . LYS A 1 111 ? 14.635  -14.243 26.929  1.00 12.54 ? 111 LYS A CA  1 
ATOM   891  C  C   . LYS A 1 111 ? 14.134  -14.799 25.585  1.00 10.27 ? 111 LYS A C   1 
ATOM   892  O  O   . LYS A 1 111 ? 14.957  -15.113 24.719  1.00 10.50 ? 111 LYS A O   1 
ATOM   893  C  CB  . LYS A 1 111 ? 15.510  -15.284 27.645  1.00 14.47 ? 111 LYS A CB  1 
ATOM   894  C  CG  . LYS A 1 111 ? 16.061  -14.815 28.965  1.00 17.30 ? 111 LYS A CG  1 
ATOM   895  C  CD  . LYS A 1 111 ? 17.111  -13.829 28.636  1.00 19.42 ? 111 LYS A CD  1 
ATOM   896  C  CE  . LYS A 1 111 ? 17.760  -13.302 29.895  1.00 24.81 ? 111 LYS A CE  1 
ATOM   897  N  NZ  . LYS A 1 111 ? 19.164  -13.720 29.769  1.00 27.51 ? 111 LYS A NZ  1 
ATOM   898  N  N   . LYS A 1 112 ? 12.805  -14.735 25.292  1.00 10.41 ? 112 LYS A N   1 
ATOM   899  C  CA  . LYS A 1 112 ? 12.255  -15.207 24.039  1.00 11.11 ? 112 LYS A CA  1 
ATOM   900  C  C   . LYS A 1 112 ? 12.504  -14.093 22.968  1.00 10.35 ? 112 LYS A C   1 
ATOM   901  O  O   . LYS A 1 112 ? 12.222  -12.871 23.155  1.00 9.81  ? 112 LYS A O   1 
ATOM   902  C  CB  . LYS A 1 112 ? 10.725  -15.457 24.140  1.00 13.02 ? 112 LYS A CB  1 
ATOM   903  C  CG  . LYS A 1 112 ? 9.932   -15.508 22.807  1.00 17.21 ? 112 LYS A CG  1 
ATOM   904  C  CD  . LYS A 1 112 ? 8.426   -15.655 23.133  1.00 20.57 ? 112 LYS A CD  1 
ATOM   905  C  CE  . LYS A 1 112 ? 7.592   -15.818 21.855  1.00 25.87 ? 112 LYS A CE  1 
ATOM   906  N  NZ  . LYS A 1 112 ? 8.167   -16.844 20.998  1.00 26.19 ? 112 LYS A NZ  1 
ATOM   907  N  N   A LYS A 1 113 ? 13.043  -14.554 21.845  0.40 9.43  ? 113 LYS A N   1 
ATOM   908  N  N   B LYS A 1 113 ? 13.074  -14.550 21.867  0.60 9.76  ? 113 LYS A N   1 
ATOM   909  C  CA  A LYS A 1 113 ? 13.261  -13.736 20.644  0.40 9.03  ? 113 LYS A CA  1 
ATOM   910  C  CA  B LYS A 1 113 ? 13.225  -13.750 20.653  0.60 9.80  ? 113 LYS A CA  1 
ATOM   911  C  C   A LYS A 1 113 ? 12.184  -13.965 19.614  0.40 8.33  ? 113 LYS A C   1 
ATOM   912  C  C   B LYS A 1 113 ? 12.036  -13.972 19.747  0.60 8.62  ? 113 LYS A C   1 
ATOM   913  O  O   A LYS A 1 113 ? 11.991  -15.115 19.164  0.40 8.67  ? 113 LYS A O   1 
ATOM   914  O  O   B LYS A 1 113 ? 11.524  -15.124 19.594  0.60 9.34  ? 113 LYS A O   1 
ATOM   915  C  CB  A LYS A 1 113 ? 14.551  -14.137 19.939  0.40 8.59  ? 113 LYS A CB  1 
ATOM   916  C  CB  B LYS A 1 113 ? 14.527  -14.103 19.906  0.60 9.85  ? 113 LYS A CB  1 
ATOM   917  C  CG  A LYS A 1 113 ? 15.818  -13.980 20.735  0.40 8.38  ? 113 LYS A CG  1 
ATOM   918  C  CG  B LYS A 1 113 ? 15.767  -13.621 20.640  0.60 10.40 ? 113 LYS A CG  1 
ATOM   919  C  CD  A LYS A 1 113 ? 17.011  -14.314 19.826  0.40 8.63  ? 113 LYS A CD  1 
ATOM   920  C  CD  B LYS A 1 113 ? 17.032  -14.365 20.247  0.60 12.07 ? 113 LYS A CD  1 
ATOM   921  C  CE  A LYS A 1 113 ? 18.342  -13.868 20.439  0.40 8.24  ? 113 LYS A CE  1 
ATOM   922  C  CE  B LYS A 1 113 ? 18.222  -13.691 20.935  0.60 11.63 ? 113 LYS A CE  1 
ATOM   923  N  NZ  A LYS A 1 113 ? 18.659  -14.509 21.785  0.40 8.68  ? 113 LYS A NZ  1 
ATOM   924  N  NZ  B LYS A 1 113 ? 19.492  -14.496 20.822  0.60 16.22 ? 113 LYS A NZ  1 
ATOM   925  N  N   . TYR A 1 114 ? 11.563  -12.883 19.144  1.00 8.30  ? 114 TYR A N   1 
ATOM   926  C  CA  . TYR A 1 114 ? 10.552  -12.983 18.102  1.00 8.12  ? 114 TYR A CA  1 
ATOM   927  C  C   . TYR A 1 114 ? 11.121  -12.893 16.699  1.00 7.76  ? 114 TYR A C   1 
ATOM   928  O  O   . TYR A 1 114 ? 12.280  -12.573 16.576  1.00 8.63  ? 114 TYR A O   1 
ATOM   929  C  CB  . TYR A 1 114 ? 9.462   -11.863 18.245  1.00 8.74  ? 114 TYR A CB  1 
ATOM   930  C  CG  . TYR A 1 114 ? 8.503   -12.092 19.400  1.00 9.14  ? 114 TYR A CG  1 
ATOM   931  C  CD1 . TYR A 1 114 ? 8.823   -11.664 20.676  1.00 9.00  ? 114 TYR A CD1 1 
ATOM   932  C  CD2 . TYR A 1 114 ? 7.282   -12.739 19.210  1.00 9.73  ? 114 TYR A CD2 1 
ATOM   933  C  CE1 . TYR A 1 114 ? 7.957   -11.870 21.743  1.00 11.68 ? 114 TYR A CE1 1 
ATOM   934  C  CE2 . TYR A 1 114 ? 6.410   -12.950 20.266  1.00 12.43 ? 114 TYR A CE2 1 
ATOM   935  C  CZ  . TYR A 1 114 ? 6.753   -12.513 21.531  1.00 12.34 ? 114 TYR A CZ  1 
ATOM   936  O  OH  . TYR A 1 114 ? 5.877   -12.732 22.562  1.00 17.23 ? 114 TYR A OH  1 
ATOM   937  N  N   . ALA A 1 115 ? 10.374  -13.180 15.632  1.00 7.00  ? 115 ALA A N   1 
ATOM   938  C  CA  . ALA A 1 115 ? 10.997  -13.156 14.307  1.00 8.10  ? 115 ALA A CA  1 
ATOM   939  C  C   . ALA A 1 115 ? 11.418  -11.782 13.809  1.00 7.43  ? 115 ALA A C   1 
ATOM   940  O  O   . ALA A 1 115 ? 12.203  -11.633 12.841  1.00 8.25  ? 115 ALA A O   1 
ATOM   941  C  CB  . ALA A 1 115 ? 9.972   -13.739 13.308  1.00 8.76  ? 115 ALA A CB  1 
ATOM   942  N  N   . ALA A 1 116 ? 10.706  -10.769 14.345  1.00 6.90  ? 116 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 116 ? 11.015  -9.422  13.927  1.00 7.53  ? 116 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 116 ? 10.397  -8.441  14.983  1.00 6.71  ? 116 ALA A C   1 
ATOM   945  O  O   . ALA A 1 116 ? 9.634   -8.807  15.869  1.00 6.24  ? 116 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 116 ? 10.465  -9.123  12.499  1.00 7.66  ? 116 ALA A CB  1 
ATOM   947  N  N   . GLU A 1 117 ? 10.763  -7.143  14.825  1.00 7.71  ? 117 GLU A N   1 
ATOM   948  C  CA  . GLU A 1 117 ? 10.239  -6.111  15.689  1.00 6.88  ? 117 GLU A CA  1 
ATOM   949  C  C   . GLU A 1 117 ? 10.047  -4.858  14.883  1.00 6.90  ? 117 GLU A C   1 
ATOM   950  O  O   . GLU A 1 117 ? 10.957  -4.459  14.140  1.00 7.84  ? 117 GLU A O   1 
ATOM   951  C  CB  . GLU A 1 117 ? 11.217  -5.890  16.890  1.00 6.51  ? 117 GLU A CB  1 
ATOM   952  C  CG  . GLU A 1 117 ? 10.674  -4.916  17.972  1.00 6.38  ? 117 GLU A CG  1 
ATOM   953  C  CD  . GLU A 1 117 ? 11.627  -4.839  19.171  1.00 6.62  ? 117 GLU A CD  1 
ATOM   954  O  OE1 . GLU A 1 117 ? 12.277  -5.874  19.470  1.00 6.75  ? 117 GLU A OE1 1 
ATOM   955  O  OE2 . GLU A 1 117 ? 11.722  -3.745  19.822  1.00 6.66  ? 117 GLU A OE2 1 
ATOM   956  N  N   . LEU A 1 118 ? 8.831   -4.305  14.967  1.00 6.39  ? 118 LEU A N   1 
ATOM   957  C  CA  . LEU A 1 118 ? 8.487   -3.027  14.334  1.00 5.43  ? 118 LEU A CA  1 
ATOM   958  C  C   . LEU A 1 118 ? 8.758   -1.889  15.341  1.00 5.86  ? 118 LEU A C   1 
ATOM   959  O  O   . LEU A 1 118 ? 8.319   -1.948  16.488  1.00 5.48  ? 118 LEU A O   1 
ATOM   960  C  CB  . LEU A 1 118 ? 6.973   -3.110  13.998  1.00 6.29  ? 118 LEU A CB  1 
ATOM   961  C  CG  . LEU A 1 118 ? 6.235   -1.794  13.648  1.00 7.16  ? 118 LEU A CG  1 
ATOM   962  C  CD1 . LEU A 1 118 ? 6.746   -1.167  12.408  1.00 7.69  ? 118 LEU A CD1 1 
ATOM   963  C  CD2 . LEU A 1 118 ? 4.752   -2.189  13.387  1.00 7.33  ? 118 LEU A CD2 1 
ATOM   964  N  N   . HIS A 1 119 ? 9.348   -0.799  14.842  1.00 5.42  ? 119 HIS A N   1 
ATOM   965  C  CA  . HIS A 1 119 ? 9.562   0.425   15.621  1.00 5.38  ? 119 HIS A CA  1 
ATOM   966  C  C   . HIS A 1 119 ? 8.863   1.582   14.924  1.00 5.83  ? 119 HIS A C   1 
ATOM   967  O  O   . HIS A 1 119 ? 9.283   1.921   13.778  1.00 6.63  ? 119 HIS A O   1 
ATOM   968  C  CB  . HIS A 1 119 ? 11.082  0.682   15.690  1.00 5.03  ? 119 HIS A CB  1 
ATOM   969  C  CG  . HIS A 1 119 ? 11.760  -0.280  16.586  1.00 5.99  ? 119 HIS A CG  1 
ATOM   970  N  ND1 . HIS A 1 119 ? 13.142  -0.452  16.557  1.00 5.92  ? 119 HIS A ND1 1 
ATOM   971  C  CD2 . HIS A 1 119 ? 11.276  -1.057  17.600  1.00 5.69  ? 119 HIS A CD2 1 
ATOM   972  C  CE1 . HIS A 1 119 ? 13.462  -1.389  17.439  1.00 5.65  ? 119 HIS A CE1 1 
ATOM   973  N  NE2 . HIS A 1 119 ? 12.315  -1.781  18.101  1.00 5.94  ? 119 HIS A NE2 1 
ATOM   974  N  N   . LEU A 1 120 ? 7.859   2.158   15.589  1.00 5.48  ? 120 LEU A N   1 
ATOM   975  C  CA  . LEU A 1 120 ? 7.225   3.403   15.109  1.00 5.98  ? 120 LEU A CA  1 
ATOM   976  C  C   . LEU A 1 120 ? 7.819   4.542   15.921  1.00 6.08  ? 120 LEU A C   1 
ATOM   977  O  O   . LEU A 1 120 ? 7.674   4.562   17.145  1.00 5.67  ? 120 LEU A O   1 
ATOM   978  C  CB  . LEU A 1 120 ? 5.718   3.264   15.365  1.00 7.06  ? 120 LEU A CB  1 
ATOM   979  C  CG  . LEU A 1 120 ? 5.003   2.165   14.477  1.00 7.85  ? 120 LEU A CG  1 
ATOM   980  C  CD1 . LEU A 1 120 ? 4.152   1.313   15.393  1.00 10.21 ? 120 LEU A CD1 1 
ATOM   981  C  CD2 . LEU A 1 120 ? 4.115   2.912   13.407  1.00 9.37  ? 120 LEU A CD2 1 
ATOM   982  N  N   . VAL A 1 121 ? 8.572   5.349   15.177  1.00 5.75  ? 121 VAL A N   1 
ATOM   983  C  CA  . VAL A 1 121 ? 9.402   6.382   15.810  1.00 7.11  ? 121 VAL A CA  1 
ATOM   984  C  C   . VAL A 1 121 ? 8.711   7.695   15.892  1.00 7.67  ? 121 VAL A C   1 
ATOM   985  O  O   . VAL A 1 121 ? 8.261   8.202   14.834  1.00 7.43  ? 121 VAL A O   1 
ATOM   986  C  CB  . VAL A 1 121 ? 10.761  6.464   15.111  1.00 6.89  ? 121 VAL A CB  1 
ATOM   987  C  CG1 . VAL A 1 121 ? 11.660  7.557   15.788  1.00 7.53  ? 121 VAL A CG1 1 
ATOM   988  C  CG2 . VAL A 1 121 ? 11.488  5.113   14.936  1.00 8.02  ? 121 VAL A CG2 1 
ATOM   989  N  N   . HIS A 1 122 ? 8.630   8.318   17.090  1.00 6.69  ? 122 HIS A N   1 
ATOM   990  C  CA  . HIS A 1 122 ? 7.902   9.604   17.225  1.00 7.72  ? 122 HIS A CA  1 
ATOM   991  C  C   . HIS A 1 122 ? 8.797   10.581  17.992  1.00 9.11  ? 122 HIS A C   1 
ATOM   992  O  O   . HIS A 1 122 ? 9.537   10.216  18.892  1.00 8.90  ? 122 HIS A O   1 
ATOM   993  C  CB  . HIS A 1 122 ? 6.621   9.452   18.053  1.00 7.58  ? 122 HIS A CB  1 
ATOM   994  C  CG  . HIS A 1 122 ? 5.732   8.295   17.629  1.00 7.80  ? 122 HIS A CG  1 
ATOM   995  N  ND1 . HIS A 1 122 ? 6.034   6.995   17.919  1.00 7.49  ? 122 HIS A ND1 1 
ATOM   996  C  CD2 . HIS A 1 122 ? 4.462   8.276   16.999  1.00 8.59  ? 122 HIS A CD2 1 
ATOM   997  C  CE1 . HIS A 1 122 ? 5.048   6.192   17.437  1.00 8.43  ? 122 HIS A CE1 1 
ATOM   998  N  NE2 . HIS A 1 122 ? 4.097   6.971   16.885  1.00 8.63  ? 122 HIS A NE2 1 
ATOM   999  N  N   . TRP A 1 123 ? 8.651   11.866  17.681  1.00 8.48  ? 123 TRP A N   1 
ATOM   1000 C  CA  . TRP A 1 123 ? 9.460   12.919  18.390  1.00 8.50  ? 123 TRP A CA  1 
ATOM   1001 C  C   . TRP A 1 123 ? 8.623   13.921  19.075  1.00 9.77  ? 123 TRP A C   1 
ATOM   1002 O  O   . TRP A 1 123 ? 7.504   14.291  18.590  1.00 9.93  ? 123 TRP A O   1 
ATOM   1003 C  CB  . TRP A 1 123 ? 10.517  13.553  17.460  1.00 9.40  ? 123 TRP A CB  1 
ATOM   1004 C  CG  . TRP A 1 123 ? 9.905   14.186  16.241  1.00 11.24 ? 123 TRP A CG  1 
ATOM   1005 C  CD1 . TRP A 1 123 ? 9.654   13.590  15.010  1.00 12.11 ? 123 TRP A CD1 1 
ATOM   1006 C  CD2 . TRP A 1 123 ? 9.420   15.567  16.110  1.00 11.93 ? 123 TRP A CD2 1 
ATOM   1007 N  NE1 . TRP A 1 123 ? 9.076   14.488  14.149  1.00 12.12 ? 123 TRP A NE1 1 
ATOM   1008 C  CE2 . TRP A 1 123 ? 8.908   15.687  14.748  1.00 11.99 ? 123 TRP A CE2 1 
ATOM   1009 C  CE3 . TRP A 1 123 ? 9.368   16.668  16.952  1.00 12.20 ? 123 TRP A CE3 1 
ATOM   1010 C  CZ2 . TRP A 1 123 ? 8.370   16.874  14.271  1.00 13.91 ? 123 TRP A CZ2 1 
ATOM   1011 C  CZ3 . TRP A 1 123 ? 8.826   17.859  16.462  1.00 12.92 ? 123 TRP A CZ3 1 
ATOM   1012 C  CH2 . TRP A 1 123 ? 8.338   17.957  15.152  1.00 13.76 ? 123 TRP A CH2 1 
ATOM   1013 N  N   . ASN A 1 124 ? 9.115   14.395  20.226  1.00 9.65  ? 124 ASN A N   1 
ATOM   1014 C  CA  . ASN A 1 124 ? 8.342   15.288  21.111  1.00 10.57 ? 124 ASN A CA  1 
ATOM   1015 C  C   . ASN A 1 124 ? 8.206   16.682  20.476  1.00 11.21 ? 124 ASN A C   1 
ATOM   1016 O  O   . ASN A 1 124 ? 9.201   17.355  20.187  1.00 11.62 ? 124 ASN A O   1 
ATOM   1017 C  CB  . ASN A 1 124 ? 9.165   15.391  22.414  1.00 10.80 ? 124 ASN A CB  1 
ATOM   1018 C  CG  . ASN A 1 124 ? 8.353   15.974  23.567  1.00 11.50 ? 124 ASN A CG  1 
ATOM   1019 O  OD1 . ASN A 1 124 ? 7.573   16.862  23.323  1.00 13.79 ? 124 ASN A OD1 1 
ATOM   1020 N  ND2 . ASN A 1 124 ? 8.541   15.480  24.770  1.00 13.90 ? 124 ASN A ND2 1 
ATOM   1021 N  N   . THR A 1 125 ? 6.945   17.112  20.304  1.00 11.24 ? 125 THR A N   1 
ATOM   1022 C  CA  . THR A 1 125 ? 6.733   18.388  19.598  1.00 12.49 ? 125 THR A CA  1 
ATOM   1023 C  C   . THR A 1 125 ? 7.278   19.661  20.308  1.00 13.19 ? 125 THR A C   1 
ATOM   1024 O  O   . THR A 1 125 ? 7.522   20.646  19.601  1.00 15.26 ? 125 THR A O   1 
ATOM   1025 C  CB  . THR A 1 125 ? 5.258   18.547  19.240  1.00 13.67 ? 125 THR A CB  1 
ATOM   1026 O  OG1 . THR A 1 125 ? 4.502   18.554  20.437  1.00 15.07 ? 125 THR A OG1 1 
ATOM   1027 C  CG2 . THR A 1 125 ? 4.861   17.409  18.244  1.00 14.30 ? 125 THR A CG2 1 
ATOM   1028 N  N   . LYS A 1 126 ? 7.621   19.443  21.662  1.00 12.21 ? 127 LYS A N   1 
ATOM   1029 C  CA  . LYS A 1 126 ? 8.162   20.642  22.309  1.00 14.75 ? 127 LYS A CA  1 
ATOM   1030 C  C   . LYS A 1 126 ? 9.535   20.981  21.732  1.00 16.79 ? 127 LYS A C   1 
ATOM   1031 O  O   . LYS A 1 126 ? 10.034  22.123  21.896  1.00 17.33 ? 127 LYS A O   1 
ATOM   1032 C  CB  . LYS A 1 126 ? 8.067   20.421  23.806  1.00 18.28 ? 127 LYS A CB  1 
ATOM   1033 C  CG  . LYS A 1 126 ? 9.108   19.572  24.450  1.00 19.42 ? 127 LYS A CG  1 
ATOM   1034 C  CD  . LYS A 1 126 ? 8.573   19.356  25.862  1.00 25.59 ? 127 LYS A CD  1 
ATOM   1035 C  CE  . LYS A 1 126 ? 9.411   18.307  26.509  1.00 27.98 ? 127 LYS A CE  1 
ATOM   1036 N  NZ  . LYS A 1 126 ? 9.257   18.364  27.979  1.00 34.30 ? 127 LYS A NZ  1 
ATOM   1037 N  N   . TYR A 1 127 ? 10.171  20.044  21.036  1.00 13.45 ? 128 TYR A N   1 
ATOM   1038 C  CA  . TYR A 1 127 ? 11.519  20.276  20.491  1.00 12.31 ? 128 TYR A CA  1 
ATOM   1039 C  C   . TYR A 1 127 ? 11.620  20.695  19.050  1.00 11.98 ? 128 TYR A C   1 
ATOM   1040 O  O   . TYR A 1 127 ? 12.725  20.864  18.464  1.00 13.68 ? 128 TYR A O   1 
ATOM   1041 C  CB  . TYR A 1 127 ? 12.487  19.083  20.758  1.00 12.72 ? 128 TYR A CB  1 
ATOM   1042 C  CG  . TYR A 1 127 ? 12.594  18.841  22.191  1.00 11.22 ? 128 TYR A CG  1 
ATOM   1043 C  CD1 . TYR A 1 127 ? 13.033  19.863  23.063  1.00 13.47 ? 128 TYR A CD1 1 
ATOM   1044 C  CD2 . TYR A 1 127 ? 12.318  17.583  22.778  1.00 11.10 ? 128 TYR A CD2 1 
ATOM   1045 C  CE1 . TYR A 1 127 ? 13.092  19.624  24.422  1.00 12.67 ? 128 TYR A CE1 1 
ATOM   1046 C  CE2 . TYR A 1 127 ? 12.421  17.326  24.154  1.00 12.90 ? 128 TYR A CE2 1 
ATOM   1047 C  CZ  . TYR A 1 127 ? 12.852  18.415  24.984  1.00 13.27 ? 128 TYR A CZ  1 
ATOM   1048 O  OH  . TYR A 1 127 ? 12.938  18.173  26.286  1.00 14.13 ? 128 TYR A OH  1 
ATOM   1049 N  N   . GLY A 1 128 ? 10.426  20.724  18.419  1.00 11.79 ? 129 GLY A N   1 
ATOM   1050 C  CA  . GLY A 1 128 ? 10.257  21.322  17.112  1.00 14.08 ? 129 GLY A CA  1 
ATOM   1051 C  C   . GLY A 1 128 ? 10.733  20.522  15.886  1.00 14.40 ? 129 GLY A C   1 
ATOM   1052 O  O   . GLY A 1 128 ? 10.181  20.664  14.713  1.00 16.30 ? 129 GLY A O   1 
ATOM   1053 N  N   . ASP A 1 129 ? 11.703  19.613  16.065  1.00 13.41 ? 130 ASP A N   1 
ATOM   1054 C  CA  . ASP A 1 129 ? 12.071  18.697  14.963  1.00 15.02 ? 130 ASP A CA  1 
ATOM   1055 C  C   . ASP A 1 129 ? 12.839  17.510  15.516  1.00 15.74 ? 130 ASP A C   1 
ATOM   1056 O  O   . ASP A 1 129 ? 13.277  17.522  16.692  1.00 15.01 ? 130 ASP A O   1 
ATOM   1057 C  CB  . ASP A 1 129 ? 12.686  19.351  13.724  1.00 17.74 ? 130 ASP A CB  1 
ATOM   1058 C  CG  . ASP A 1 129 ? 14.119  19.799  13.916  1.00 20.77 ? 130 ASP A CG  1 
ATOM   1059 O  OD1 . ASP A 1 129 ? 14.773  19.460  14.928  1.00 25.14 ? 130 ASP A OD1 1 
ATOM   1060 O  OD2 . ASP A 1 129 ? 14.597  20.509  13.013  1.00 26.18 ? 130 ASP A OD2 1 
ATOM   1061 N  N   . PHE A 1 130 ? 12.936  16.460  14.686  1.00 13.88 ? 131 PHE A N   1 
ATOM   1062 C  CA  . PHE A 1 130 ? 13.595  15.225  15.098  1.00 13.94 ? 131 PHE A CA  1 
ATOM   1063 C  C   . PHE A 1 130 ? 15.029  15.478  15.472  1.00 13.87 ? 131 PHE A C   1 
ATOM   1064 O  O   . PHE A 1 130 ? 15.526  14.886  16.467  1.00 11.79 ? 131 PHE A O   1 
ATOM   1065 C  CB  . PHE A 1 130 ? 13.487  14.175  13.947  1.00 12.11 ? 131 PHE A CB  1 
ATOM   1066 C  CG  . PHE A 1 130 ? 14.114  12.810  14.257  1.00 12.84 ? 131 PHE A CG  1 
ATOM   1067 C  CD1 . PHE A 1 130 ? 13.403  11.833  14.953  1.00 12.22 ? 131 PHE A CD1 1 
ATOM   1068 C  CD2 . PHE A 1 130 ? 15.455  12.532  13.881  1.00 12.93 ? 131 PHE A CD2 1 
ATOM   1069 C  CE1 . PHE A 1 130 ? 14.009  10.661  15.244  1.00 14.04 ? 131 PHE A CE1 1 
ATOM   1070 C  CE2 . PHE A 1 130 ? 16.056  11.331  14.177  1.00 15.99 ? 131 PHE A CE2 1 
ATOM   1071 C  CZ  . PHE A 1 130 ? 15.313  10.415  14.872  1.00 14.64 ? 131 PHE A CZ  1 
ATOM   1072 N  N   . GLY A 1 131 ? 15.732  16.318  14.671  1.00 13.20 ? 132 GLY A N   1 
ATOM   1073 C  CA  . GLY A 1 131 ? 17.173  16.405  14.976  1.00 13.42 ? 132 GLY A CA  1 
ATOM   1074 C  C   . GLY A 1 131 ? 17.448  17.069  16.329  1.00 12.87 ? 132 GLY A C   1 
ATOM   1075 O  O   . GLY A 1 131 ? 18.429  16.748  17.008  1.00 15.39 ? 132 GLY A O   1 
ATOM   1076 N  N   . LYS A 1 132 ? 16.603  18.014  16.696  1.00 14.04 ? 133 LYS A N   1 
ATOM   1077 C  CA  . LYS A 1 132 ? 16.730  18.560  18.029  1.00 14.53 ? 133 LYS A CA  1 
ATOM   1078 C  C   . LYS A 1 132 ? 16.257  17.619  19.153  1.00 13.16 ? 133 LYS A C   1 
ATOM   1079 O  O   . LYS A 1 132 ? 16.820  17.538  20.248  1.00 13.22 ? 133 LYS A O   1 
ATOM   1080 C  CB  . LYS A 1 132 ? 15.972  19.886  18.116  1.00 16.73 ? 133 LYS A CB  1 
ATOM   1081 C  CG  . LYS A 1 132 ? 16.732  21.109  17.618  1.00 23.42 ? 133 LYS A CG  1 
ATOM   1082 C  CD  . LYS A 1 132 ? 17.517  21.565  18.873  1.00 30.45 ? 133 LYS A CD  1 
ATOM   1083 N  N   . ALA A 1 133 ? 15.134  16.909  18.867  1.00 11.94 ? 134 ALA A N   1 
ATOM   1084 C  CA  . ALA A 1 133 ? 14.592  15.979  19.865  1.00 12.11 ? 134 ALA A CA  1 
ATOM   1085 C  C   . ALA A 1 133 ? 15.632  14.895  20.296  1.00 11.62 ? 134 ALA A C   1 
ATOM   1086 O  O   . ALA A 1 133 ? 15.652  14.459  21.471  1.00 10.86 ? 134 ALA A O   1 
ATOM   1087 C  CB  . ALA A 1 133 ? 13.367  15.267  19.262  1.00 11.79 ? 134 ALA A CB  1 
ATOM   1088 N  N   . VAL A 1 134 ? 16.431  14.368  19.365  1.00 10.44 ? 135 VAL A N   1 
ATOM   1089 C  CA  . VAL A 1 134 ? 17.330  13.230  19.768  1.00 11.38 ? 135 VAL A CA  1 
ATOM   1090 C  C   . VAL A 1 134 ? 18.426  13.683  20.719  1.00 10.87 ? 135 VAL A C   1 
ATOM   1091 O  O   . VAL A 1 134 ? 19.100  12.881  21.331  1.00 12.15 ? 135 VAL A O   1 
ATOM   1092 C  CB  . VAL A 1 134 ? 18.024  12.488  18.583  1.00 11.24 ? 135 VAL A CB  1 
ATOM   1093 C  CG1 . VAL A 1 134 ? 16.985  11.717  17.766  1.00 11.68 ? 135 VAL A CG1 1 
ATOM   1094 C  CG2 . VAL A 1 134 ? 18.900  13.376  17.696  1.00 11.95 ? 135 VAL A CG2 1 
ATOM   1095 N  N   . GLN A 1 135 ? 18.581  14.996  20.860  1.00 11.66 ? 136 GLN A N   1 
ATOM   1096 C  CA  . GLN A 1 135 ? 19.570  15.531  21.797  1.00 13.91 ? 136 GLN A CA  1 
ATOM   1097 C  C   . GLN A 1 135 ? 19.004  15.687  23.223  1.00 13.26 ? 136 GLN A C   1 
ATOM   1098 O  O   . GLN A 1 135 ? 19.693  16.244  24.124  1.00 15.62 ? 136 GLN A O   1 
ATOM   1099 C  CB  . GLN A 1 135 ? 20.074  16.893  21.221  1.00 15.71 ? 136 GLN A CB  1 
ATOM   1100 C  CG  . GLN A 1 135 ? 20.878  16.747  19.920  1.00 18.42 ? 136 GLN A CG  1 
ATOM   1101 C  CD  . GLN A 1 135 ? 22.153  15.821  20.039  1.00 26.29 ? 136 GLN A CD  1 
ATOM   1102 O  OE1 . GLN A 1 135 ? 22.801  15.722  21.101  1.00 33.29 ? 136 GLN A OE1 1 
ATOM   1103 N  NE2 . GLN A 1 135 ? 22.519  15.152  18.920  1.00 28.35 ? 136 GLN A NE2 1 
ATOM   1104 N  N   . GLN A 1 136 ? 17.765  15.281  23.450  1.00 12.11 ? 137 GLN A N   1 
ATOM   1105 C  CA  . GLN A 1 136 ? 17.038  15.502  24.739  1.00 10.89 ? 137 GLN A CA  1 
ATOM   1106 C  C   . GLN A 1 136 ? 16.665  14.184  25.368  1.00 11.50 ? 137 GLN A C   1 
ATOM   1107 O  O   . GLN A 1 136 ? 16.318  13.205  24.666  1.00 9.80  ? 137 GLN A O   1 
ATOM   1108 C  CB  . GLN A 1 136 ? 15.758  16.340  24.505  1.00 13.43 ? 137 GLN A CB  1 
ATOM   1109 C  CG  . GLN A 1 136 ? 16.020  17.629  23.710  1.00 17.61 ? 137 GLN A CG  1 
ATOM   1110 C  CD  . GLN A 1 136 ? 17.000  18.570  24.397  1.00 21.04 ? 137 GLN A CD  1 
ATOM   1111 O  OE1 . GLN A 1 136 ? 17.076  18.575  25.608  1.00 20.81 ? 137 GLN A OE1 1 
ATOM   1112 N  NE2 . GLN A 1 136 ? 17.830  19.304  23.594  1.00 29.28 ? 137 GLN A NE2 1 
ATOM   1113 N  N   A PRO A 1 137 ? 16.674  14.086  26.716  0.50 10.90 ? 138 PRO A N   1 
ATOM   1114 N  N   B PRO A 1 137 ? 16.681  14.071  26.702  0.50 11.14 ? 138 PRO A N   1 
ATOM   1115 C  CA  A PRO A 1 137 ? 16.423  12.820  27.383  0.50 10.86 ? 138 PRO A CA  1 
ATOM   1116 C  CA  B PRO A 1 137 ? 16.414  12.798  27.359  0.50 11.18 ? 138 PRO A CA  1 
ATOM   1117 C  C   A PRO A 1 137 ? 14.972  12.336  27.231  0.50 10.64 ? 138 PRO A C   1 
ATOM   1118 C  C   B PRO A 1 137 ? 14.981  12.323  27.179  0.50 10.86 ? 138 PRO A C   1 
ATOM   1119 O  O   A PRO A 1 137 ? 14.721  11.137  27.435  0.50 11.44 ? 138 PRO A O   1 
ATOM   1120 O  O   B PRO A 1 137 ? 14.759  11.114  27.316  0.50 11.73 ? 138 PRO A O   1 
ATOM   1121 C  CB  A PRO A 1 137 ? 16.810  13.091  28.869  0.50 11.22 ? 138 PRO A CB  1 
ATOM   1122 C  CB  B PRO A 1 137 ? 16.758  13.047  28.855  0.50 11.80 ? 138 PRO A CB  1 
ATOM   1123 C  CG  A PRO A 1 137 ? 16.565  14.551  29.010  0.50 10.78 ? 138 PRO A CG  1 
ATOM   1124 C  CG  B PRO A 1 137 ? 17.613  14.242  28.780  0.50 11.67 ? 138 PRO A CG  1 
ATOM   1125 C  CD  A PRO A 1 137 ? 16.897  15.199  27.681  0.50 10.55 ? 138 PRO A CD  1 
ATOM   1126 C  CD  B PRO A 1 137 ? 17.142  15.106  27.646  0.50 10.94 ? 138 PRO A CD  1 
ATOM   1127 N  N   . ASP A 1 138 ? 14.064  13.253  26.871  1.00 9.63  ? 139 ASP A N   1 
ATOM   1128 C  CA  . ASP A 1 138 ? 12.663  12.900  26.643  1.00 11.43 ? 139 ASP A CA  1 
ATOM   1129 C  C   . ASP A 1 138 ? 12.253  13.242  25.184  1.00 9.98  ? 139 ASP A C   1 
ATOM   1130 O  O   . ASP A 1 138 ? 11.106  13.622  24.917  1.00 11.15 ? 139 ASP A O   1 
ATOM   1131 C  CB  . ASP A 1 138 ? 11.657  13.620  27.574  1.00 12.51 ? 139 ASP A CB  1 
ATOM   1132 C  CG  . ASP A 1 138 ? 11.831  15.114  27.550  1.00 15.26 ? 139 ASP A CG  1 
ATOM   1133 O  OD1 . ASP A 1 138 ? 12.771  15.594  26.879  1.00 15.55 ? 139 ASP A OD1 1 
ATOM   1134 O  OD2 . ASP A 1 138 ? 11.026  15.801  28.202  1.00 19.69 ? 139 ASP A OD2 1 
ATOM   1135 N  N   . GLY A 1 139 ? 13.211  13.136  24.273  1.00 8.72  ? 140 GLY A N   1 
ATOM   1136 C  CA  . GLY A 1 139 ? 12.982  13.602  22.876  1.00 8.60  ? 140 GLY A CA  1 
ATOM   1137 C  C   . GLY A 1 139 ? 12.158  12.636  22.013  1.00 8.41  ? 140 GLY A C   1 
ATOM   1138 O  O   . GLY A 1 139 ? 11.427  13.110  21.149  1.00 8.04  ? 140 GLY A O   1 
ATOM   1139 N  N   . LEU A 1 140 ? 12.299  11.317  22.194  1.00 6.35  ? 141 LEU A N   1 
ATOM   1140 C  CA  . LEU A 1 140 ? 11.601  10.328  21.365  1.00 7.18  ? 141 LEU A CA  1 
ATOM   1141 C  C   . LEU A 1 140 ? 10.712  9.466   22.152  1.00 7.15  ? 141 LEU A C   1 
ATOM   1142 O  O   . LEU A 1 140 ? 10.956  9.186   23.327  1.00 7.77  ? 141 LEU A O   1 
ATOM   1143 C  CB  . LEU A 1 140 ? 12.578  9.453   20.640  1.00 7.53  ? 141 LEU A CB  1 
ATOM   1144 C  CG  . LEU A 1 140 ? 13.499  10.092  19.619  1.00 8.77  ? 141 LEU A CG  1 
ATOM   1145 C  CD1 . LEU A 1 140 ? 14.156  9.097   18.695  1.00 10.42 ? 141 LEU A CD1 1 
ATOM   1146 C  CD2 . LEU A 1 140 ? 12.943  11.197  18.714  1.00 10.57 ? 141 LEU A CD2 1 
ATOM   1147 N  N   . ALA A 1 141 ? 9.672   8.985   21.462  1.00 6.97  ? 142 ALA A N   1 
ATOM   1148 C  CA  . ALA A 1 141 ? 8.867   7.860   22.000  1.00 6.62  ? 142 ALA A CA  1 
ATOM   1149 C  C   . ALA A 1 141 ? 8.792   6.829   20.872  1.00 6.49  ? 142 ALA A C   1 
ATOM   1150 O  O   . ALA A 1 141 ? 8.361   7.183   19.793  1.00 7.51  ? 142 ALA A O   1 
ATOM   1151 C  CB  . ALA A 1 141 ? 7.430   8.267   22.426  1.00 8.13  ? 142 ALA A CB  1 
ATOM   1152 N  N   . VAL A 1 142 ? 9.327   5.612   21.134  1.00 6.65  ? 143 VAL A N   1 
ATOM   1153 C  CA  . VAL A 1 142 ? 9.357   4.579   20.112  1.00 6.84  ? 143 VAL A CA  1 
ATOM   1154 C  C   . VAL A 1 142 ? 8.370   3.514   20.586  1.00 7.33  ? 143 VAL A C   1 
ATOM   1155 O  O   . VAL A 1 142 ? 8.461   2.961   21.694  1.00 6.74  ? 143 VAL A O   1 
ATOM   1156 C  CB  . VAL A 1 142 ? 10.753  3.982   19.804  1.00 7.68  ? 143 VAL A CB  1 
ATOM   1157 C  CG1 . VAL A 1 142 ? 10.572  2.997   18.633  1.00 7.41  ? 143 VAL A CG1 1 
ATOM   1158 C  CG2 . VAL A 1 142 ? 11.665  5.103   19.339  1.00 8.62  ? 143 VAL A CG2 1 
ATOM   1159 N  N   . LEU A 1 143 ? 7.380   3.221   19.717  1.00 6.63  ? 144 LEU A N   1 
ATOM   1160 C  CA  . LEU A 1 143 ? 6.402   2.136   19.992  1.00 6.75  ? 144 LEU A CA  1 
ATOM   1161 C  C   . LEU A 1 143 ? 6.929   0.892   19.288  1.00 6.91  ? 144 LEU A C   1 
ATOM   1162 O  O   . LEU A 1 143 ? 7.126   0.864   18.077  1.00 7.93  ? 144 LEU A O   1 
ATOM   1163 C  CB  . LEU A 1 143 ? 5.017   2.578   19.478  1.00 7.55  ? 144 LEU A CB  1 
ATOM   1164 C  CG  . LEU A 1 143 ? 3.888   1.546   19.532  1.00 8.34  ? 144 LEU A CG  1 
ATOM   1165 C  CD1 . LEU A 1 143 ? 3.668   1.163   20.993  1.00 9.66  ? 144 LEU A CD1 1 
ATOM   1166 C  CD2 . LEU A 1 143 ? 2.595   2.120   18.919  1.00 10.58 ? 144 LEU A CD2 1 
ATOM   1167 N  N   . GLY A 1 144 ? 7.223   -0.112  20.124  1.00 5.84  ? 145 GLY A N   1 
ATOM   1168 C  CA  . GLY A 1 144 ? 7.821   -1.378  19.695  1.00 5.98  ? 145 GLY A CA  1 
ATOM   1169 C  C   . GLY A 1 144 ? 6.760   -2.480  19.625  1.00 5.62  ? 145 GLY A C   1 
ATOM   1170 O  O   . GLY A 1 144 ? 6.013   -2.633  20.617  1.00 7.08  ? 145 GLY A O   1 
ATOM   1171 N  N   . ILE A 1 145 ? 6.681   -3.232  18.505  1.00 5.80  ? 146 ILE A N   1 
ATOM   1172 C  CA  . ILE A 1 145 ? 5.620   -4.283  18.341  1.00 6.60  ? 146 ILE A CA  1 
ATOM   1173 C  C   . ILE A 1 145 ? 6.378   -5.506  17.818  1.00 6.14  ? 146 ILE A C   1 
ATOM   1174 O  O   . ILE A 1 145 ? 7.035   -5.494  16.791  1.00 6.80  ? 146 ILE A O   1 
ATOM   1175 C  CB  . ILE A 1 145 ? 4.545   -3.781  17.329  1.00 7.60  ? 146 ILE A CB  1 
ATOM   1176 C  CG1 . ILE A 1 145 ? 3.902   -2.516  17.843  1.00 9.11  ? 146 ILE A CG1 1 
ATOM   1177 C  CG2 . ILE A 1 145 ? 3.446   -4.877  17.137  1.00 8.48  ? 146 ILE A CG2 1 
ATOM   1178 C  CD1 . ILE A 1 145 ? 2.786   -1.914  16.971  1.00 8.64  ? 146 ILE A CD1 1 
ATOM   1179 N  N   . PHE A 1 146 ? 6.200   -6.601  18.543  1.00 6.30  ? 147 PHE A N   1 
ATOM   1180 C  CA  . PHE A 1 146 ? 6.794   -7.901  18.103  1.00 6.67  ? 147 PHE A CA  1 
ATOM   1181 C  C   . PHE A 1 146 ? 6.028   -8.550  16.953  1.00 7.16  ? 147 PHE A C   1 
ATOM   1182 O  O   . PHE A 1 146 ? 4.791   -8.410  16.844  1.00 8.42  ? 147 PHE A O   1 
ATOM   1183 C  CB  . PHE A 1 146 ? 6.836   -8.890  19.263  1.00 6.00  ? 147 PHE A CB  1 
ATOM   1184 C  CG  . PHE A 1 146 ? 7.665   -8.386  20.417  1.00 5.55  ? 147 PHE A CG  1 
ATOM   1185 C  CD1 . PHE A 1 146 ? 9.047   -8.213  20.222  1.00 6.23  ? 147 PHE A CD1 1 
ATOM   1186 C  CD2 . PHE A 1 146 ? 7.101   -8.170  21.642  1.00 6.33  ? 147 PHE A CD2 1 
ATOM   1187 C  CE1 . PHE A 1 146 ? 9.836   -7.788  21.293  1.00 6.44  ? 147 PHE A CE1 1 
ATOM   1188 C  CE2 . PHE A 1 146 ? 7.872   -7.716  22.705  1.00 6.96  ? 147 PHE A CE2 1 
ATOM   1189 C  CZ  . PHE A 1 146 ? 9.254   -7.610  22.545  1.00 6.35  ? 147 PHE A CZ  1 
ATOM   1190 N  N   . LEU A 1 147 ? 6.805   -9.169  16.065  1.00 7.45  ? 148 LEU A N   1 
ATOM   1191 C  CA  . LEU A 1 147 ? 6.146   -10.030 14.978  1.00 6.91  ? 148 LEU A CA  1 
ATOM   1192 C  C   . LEU A 1 147 ? 6.486   -11.493 15.240  1.00 7.99  ? 148 LEU A C   1 
ATOM   1193 O  O   . LEU A 1 147 ? 7.687   -11.872 15.348  1.00 7.77  ? 148 LEU A O   1 
ATOM   1194 C  CB  . LEU A 1 147 ? 6.726   -9.633  13.585  1.00 7.16  ? 148 LEU A CB  1 
ATOM   1195 C  CG  . LEU A 1 147 ? 6.136   -8.354  12.923  1.00 7.24  ? 148 LEU A CG  1 
ATOM   1196 C  CD1 . LEU A 1 147 ? 6.317   -7.039  13.756  1.00 9.69  ? 148 LEU A CD1 1 
ATOM   1197 C  CD2 . LEU A 1 147 ? 6.707   -8.107  11.549  1.00 8.73  ? 148 LEU A CD2 1 
ATOM   1198 N  N   . LYS A 1 148 ? 5.429   -12.327 15.187  1.00 8.31  ? 149 LYS A N   1 
ATOM   1199 C  CA  . LYS A 1 148 ? 5.634   -13.782 15.150  1.00 8.71  ? 149 LYS A CA  1 
ATOM   1200 C  C   . LYS A 1 148 ? 5.141   -14.308 13.807  1.00 10.71 ? 149 LYS A C   1 
ATOM   1201 O  O   . LYS A 1 148 ? 4.343   -13.676 13.159  1.00 10.53 ? 149 LYS A O   1 
ATOM   1202 C  CB  . LYS A 1 148 ? 4.880   -14.516 16.248  1.00 10.73 ? 149 LYS A CB  1 
ATOM   1203 C  CG  . LYS A 1 148 ? 3.378   -14.322 16.267  1.00 14.04 ? 149 LYS A CG  1 
ATOM   1204 C  CD  . LYS A 1 148 ? 2.879   -15.072 17.523  1.00 20.46 ? 149 LYS A CD  1 
ATOM   1205 C  CE  . LYS A 1 148 ? 1.358   -14.986 17.593  1.00 24.10 ? 149 LYS A CE  1 
ATOM   1206 N  NZ  . LYS A 1 148 ? 0.895   -15.901 18.682  1.00 33.41 ? 149 LYS A NZ  1 
ATOM   1207 N  N   . VAL A 1 149 ? 5.645   -15.447 13.390  1.00 10.80 ? 150 VAL A N   1 
ATOM   1208 C  CA  . VAL A 1 149 ? 5.242   -16.030 12.106  1.00 11.55 ? 150 VAL A CA  1 
ATOM   1209 C  C   . VAL A 1 149 ? 4.029   -16.970 12.328  1.00 12.12 ? 150 VAL A C   1 
ATOM   1210 O  O   . VAL A 1 149 ? 4.069   -17.891 13.217  1.00 12.85 ? 150 VAL A O   1 
ATOM   1211 C  CB  . VAL A 1 149 ? 6.421   -16.758 11.451  1.00 11.50 ? 150 VAL A CB  1 
ATOM   1212 C  CG1 . VAL A 1 149 ? 5.984   -17.487 10.145  1.00 12.54 ? 150 VAL A CG1 1 
ATOM   1213 C  CG2 . VAL A 1 149 ? 7.553   -15.795 11.147  1.00 13.54 ? 150 VAL A CG2 1 
ATOM   1214 N  N   . GLY A 1 150 ? 3.005   -16.716 11.522  1.00 9.71  ? 151 GLY A N   1 
ATOM   1215 C  CA  . GLY A 1 150 ? 1.729   -17.477 11.565  1.00 11.75 ? 151 GLY A CA  1 
ATOM   1216 C  C   . GLY A 1 150 ? 0.874   -17.038 10.430  1.00 9.76  ? 151 GLY A C   1 
ATOM   1217 O  O   . GLY A 1 150 ? 1.281   -17.175 9.277   1.00 10.25 ? 151 GLY A O   1 
ATOM   1218 N  N   A SER A 1 151 ? -0.339  -16.592 10.778  0.50 11.81 ? 152 SER A N   1 
ATOM   1219 N  N   B SER A 1 151 ? -0.326  -16.574 10.802  0.50 11.70 ? 152 SER A N   1 
ATOM   1220 C  CA  A SER A 1 151 ? -1.239  -16.016 9.745   0.50 12.93 ? 152 SER A CA  1 
ATOM   1221 C  CA  B SER A 1 151 ? -1.237  -15.936 9.818   0.50 12.65 ? 152 SER A CA  1 
ATOM   1222 C  C   A SER A 1 151 ? -0.655  -14.721 9.185   0.50 13.94 ? 152 SER A C   1 
ATOM   1223 C  C   B SER A 1 151 ? -0.600  -14.694 9.171   0.50 13.89 ? 152 SER A C   1 
ATOM   1224 O  O   A SER A 1 151 ? 0.091   -14.047 9.907   0.50 13.43 ? 152 SER A O   1 
ATOM   1225 O  O   B SER A 1 151 ? 0.223   -14.016 9.808   0.50 13.28 ? 152 SER A O   1 
ATOM   1226 C  CB  A SER A 1 151 ? -2.628  -15.802 10.278  0.50 14.89 ? 152 SER A CB  1 
ATOM   1227 C  CB  B SER A 1 151 ? -2.554  -15.597 10.455  0.50 14.93 ? 152 SER A CB  1 
ATOM   1228 O  OG  A SER A 1 151 ? -2.585  -14.894 11.373  0.50 14.74 ? 152 SER A OG  1 
ATOM   1229 O  OG  B SER A 1 151 ? -2.958  -16.605 11.369  0.50 14.69 ? 152 SER A OG  1 
ATOM   1230 N  N   . ALA A 1 152 ? -0.941  -14.401 7.912   1.00 13.19 ? 153 ALA A N   1 
ATOM   1231 C  CA  . ALA A 1 152 ? -0.582  -13.104 7.301   1.00 12.73 ? 153 ALA A CA  1 
ATOM   1232 C  C   . ALA A 1 152 ? -1.216  -11.891 8.005   1.00 11.40 ? 153 ALA A C   1 
ATOM   1233 O  O   . ALA A 1 152 ? -2.291  -11.994 8.594   1.00 13.25 ? 153 ALA A O   1 
ATOM   1234 C  CB  . ALA A 1 152 ? -0.897  -13.057 5.788   1.00 14.08 ? 153 ALA A CB  1 
ATOM   1235 N  N   . LYS A 1 153 ? -0.458  -10.758 8.029   1.00 12.16 ? 154 LYS A N   1 
ATOM   1236 C  CA  . LYS A 1 153 ? -1.006  -9.478  8.433   1.00 12.67 ? 154 LYS A CA  1 
ATOM   1237 C  C   . LYS A 1 153 ? -1.365  -8.708  7.156   1.00 11.27 ? 154 LYS A C   1 
ATOM   1238 O  O   . LYS A 1 153 ? -0.516  -8.294  6.387   1.00 11.61 ? 154 LYS A O   1 
ATOM   1239 C  CB  . LYS A 1 153 ? 0.022   -8.652  9.223   1.00 12.96 ? 154 LYS A CB  1 
ATOM   1240 C  CG  . LYS A 1 153 ? -0.607  -7.504  9.988   1.00 14.62 ? 154 LYS A CG  1 
ATOM   1241 C  CD  . LYS A 1 153 ? -1.482  -7.913  11.156  1.00 13.44 ? 154 LYS A CD  1 
ATOM   1242 C  CE  . LYS A 1 153 ? -1.781  -6.770  12.181  1.00 15.83 ? 154 LYS A CE  1 
ATOM   1243 N  NZ  . LYS A 1 153 ? -2.935  -7.037  13.080  1.00 22.14 ? 154 LYS A NZ  1 
ATOM   1244 N  N   . PRO A 1 154 ? -2.694  -8.668  6.848   1.00 13.27 ? 155 PRO A N   1 
ATOM   1245 C  CA  . PRO A 1 154 ? -3.064  -8.071  5.519   1.00 14.49 ? 155 PRO A CA  1 
ATOM   1246 C  C   . PRO A 1 154 ? -2.623  -6.616  5.378   1.00 13.31 ? 155 PRO A C   1 
ATOM   1247 O  O   . PRO A 1 154 ? -2.152  -6.213  4.303   1.00 14.49 ? 155 PRO A O   1 
ATOM   1248 C  CB  . PRO A 1 154 ? -4.613  -8.156  5.533   1.00 15.40 ? 155 PRO A CB  1 
ATOM   1249 C  CG  . PRO A 1 154 ? -4.930  -9.185  6.558   1.00 17.47 ? 155 PRO A CG  1 
ATOM   1250 C  CD  . PRO A 1 154 ? -3.866  -9.044  7.642   1.00 15.15 ? 155 PRO A CD  1 
ATOM   1251 N  N   . GLY A 1 155 ? -2.589  -5.920  6.534   1.00 13.15 ? 156 GLY A N   1 
ATOM   1252 C  CA  . GLY A 1 155 ? -2.200  -4.475  6.537   1.00 12.63 ? 156 GLY A CA  1 
ATOM   1253 C  C   . GLY A 1 155 ? -0.703  -4.283  6.276   1.00 14.40 ? 156 GLY A C   1 
ATOM   1254 O  O   . GLY A 1 155 ? -0.230  -3.152  6.057   1.00 17.78 ? 156 GLY A O   1 
ATOM   1255 N  N   . LEU A 1 156 ? 0.071   -5.362  6.414   1.00 11.82 ? 157 LEU A N   1 
ATOM   1256 C  CA  . LEU A 1 156 ? 1.468   -5.334  6.013   1.00 10.54 ? 157 LEU A CA  1 
ATOM   1257 C  C   . LEU A 1 156 ? 1.812   -5.527  4.534   1.00 10.45 ? 157 LEU A C   1 
ATOM   1258 O  O   . LEU A 1 156 ? 2.928   -5.233  4.005   1.00 11.58 ? 157 LEU A O   1 
ATOM   1259 C  CB  . LEU A 1 156 ? 2.317   -6.309  6.884   1.00 10.70 ? 157 LEU A CB  1 
ATOM   1260 C  CG  . LEU A 1 156 ? 3.833   -6.508  6.674   1.00 10.80 ? 157 LEU A CG  1 
ATOM   1261 C  CD1 . LEU A 1 156 ? 4.618   -5.185  6.991   1.00 11.25 ? 157 LEU A CD1 1 
ATOM   1262 C  CD2 . LEU A 1 156 ? 4.433   -7.629  7.538   1.00 11.12 ? 157 LEU A CD2 1 
ATOM   1263 N  N   . GLN A 1 157 ? 0.814   -6.099  3.769   1.00 11.75 ? 158 GLN A N   1 
ATOM   1264 C  CA  . GLN A 1 157 ? 1.191   -6.518  2.440   1.00 12.64 ? 158 GLN A CA  1 
ATOM   1265 C  C   . GLN A 1 157 ? 1.584   -5.389  1.463   1.00 10.67 ? 158 GLN A C   1 
ATOM   1266 O  O   . GLN A 1 157 ? 2.482   -5.612  0.646   1.00 11.88 ? 158 GLN A O   1 
ATOM   1267 C  CB  . GLN A 1 157 ? 0.081   -7.390  1.847   1.00 13.95 ? 158 GLN A CB  1 
ATOM   1268 C  CG  . GLN A 1 157 ? 0.466   -8.091  0.556   1.00 17.17 ? 158 GLN A CG  1 
ATOM   1269 C  CD  . GLN A 1 157 ? 1.555   -9.113  0.791   1.00 16.17 ? 158 GLN A CD  1 
ATOM   1270 O  OE1 . GLN A 1 157 ? 1.636   -9.709  1.912   1.00 18.25 ? 158 GLN A OE1 1 
ATOM   1271 N  NE2 . GLN A 1 157 ? 2.397   -9.349  -0.184  1.00 17.34 ? 158 GLN A NE2 1 
ATOM   1272 N  N   A LYS A 1 158 ? 0.981   -4.192  1.582   0.50 13.53 ? 159 LYS A N   1 
ATOM   1273 N  N   B LYS A 1 158 ? 0.970   -4.199  1.593   0.50 13.67 ? 159 LYS A N   1 
ATOM   1274 C  CA  A LYS A 1 158 ? 1.426   -3.093  0.738   0.50 12.86 ? 159 LYS A CA  1 
ATOM   1275 C  CA  B LYS A 1 158 ? 1.394   -3.085  0.764   0.50 13.08 ? 159 LYS A CA  1 
ATOM   1276 C  C   A LYS A 1 158 ? 2.934   -2.776  0.909   0.50 13.34 ? 159 LYS A C   1 
ATOM   1277 C  C   B LYS A 1 158 ? 2.912   -2.764  0.918   0.50 13.53 ? 159 LYS A C   1 
ATOM   1278 O  O   A LYS A 1 158 ? 3.609   -2.453  -0.044  0.50 14.35 ? 159 LYS A O   1 
ATOM   1279 O  O   B LYS A 1 158 ? 3.577   -2.446  -0.042  0.50 14.48 ? 159 LYS A O   1 
ATOM   1280 C  CB  A LYS A 1 158 ? 0.579   -1.851  0.985   0.50 15.09 ? 159 LYS A CB  1 
ATOM   1281 C  CB  B LYS A 1 158 ? 0.510   -1.860  1.025   0.50 15.74 ? 159 LYS A CB  1 
ATOM   1282 C  CG  A LYS A 1 158 ? 0.976   -0.613  0.183   0.50 16.33 ? 159 LYS A CG  1 
ATOM   1283 C  CG  B LYS A 1 158 ? -0.904  -1.973  0.455   0.50 16.75 ? 159 LYS A CG  1 
ATOM   1284 C  CD  A LYS A 1 158 ? 0.065   0.570   0.572   0.50 16.89 ? 159 LYS A CD  1 
ATOM   1285 C  CD  B LYS A 1 158 ? -1.690  -0.657  0.553   0.50 18.82 ? 159 LYS A CD  1 
ATOM   1286 C  CE  A LYS A 1 158 ? 0.453   1.904   -0.103  0.50 17.20 ? 159 LYS A CE  1 
ATOM   1287 C  CE  B LYS A 1 158 ? -3.036  -0.769  -0.202  0.50 21.09 ? 159 LYS A CE  1 
ATOM   1288 N  NZ  A LYS A 1 158 ? 0.066   1.878   -1.569  0.50 17.89 ? 159 LYS A NZ  1 
ATOM   1289 N  NZ  B LYS A 1 158 ? -4.014  0.331   0.109   0.50 21.24 ? 159 LYS A NZ  1 
ATOM   1290 N  N   . VAL A 1 159 ? 3.452   -2.891  2.143   1.00 13.57 ? 160 VAL A N   1 
ATOM   1291 C  CA  . VAL A 1 159 ? 4.877   -2.701  2.378   1.00 13.81 ? 160 VAL A CA  1 
ATOM   1292 C  C   . VAL A 1 159 ? 5.681   -3.791  1.689   1.00 11.77 ? 160 VAL A C   1 
ATOM   1293 O  O   . VAL A 1 159 ? 6.594   -3.563  0.963   1.00 13.17 ? 160 VAL A O   1 
ATOM   1294 C  CB  . VAL A 1 159 ? 5.143   -2.730  3.886   1.00 13.47 ? 160 VAL A CB  1 
ATOM   1295 C  CG1 . VAL A 1 159 ? 6.642   -2.782  4.155   1.00 14.61 ? 160 VAL A CG1 1 
ATOM   1296 C  CG2 . VAL A 1 159 ? 4.533   -1.480  4.517   1.00 17.03 ? 160 VAL A CG2 1 
ATOM   1297 N  N   . VAL A 1 160 ? 5.289   -5.082  1.907   1.00 12.85 ? 161 VAL A N   1 
ATOM   1298 C  CA  . VAL A 1 160 ? 6.045   -6.192  1.352   1.00 14.49 ? 161 VAL A CA  1 
ATOM   1299 C  C   . VAL A 1 160 ? 6.073   -6.155  -0.181  1.00 12.37 ? 161 VAL A C   1 
ATOM   1300 O  O   . VAL A 1 160 ? 7.145   -6.406  -0.754  1.00 12.78 ? 161 VAL A O   1 
ATOM   1301 C  CB  . VAL A 1 160 ? 5.463   -7.589  1.861   1.00 16.42 ? 161 VAL A CB  1 
ATOM   1302 C  CG1 . VAL A 1 160 ? 5.840   -8.820  1.001   1.00 18.57 ? 161 VAL A CG1 1 
ATOM   1303 C  CG2 . VAL A 1 160 ? 5.835   -7.759  3.334   1.00 15.90 ? 161 VAL A CG2 1 
ATOM   1304 N  N   . ASP A 1 161 ? 4.947   -5.727  -0.771  1.00 13.92 ? 162 ASP A N   1 
ATOM   1305 C  CA  . ASP A 1 161 ? 4.889   -5.760  -2.234  1.00 18.20 ? 162 ASP A CA  1 
ATOM   1306 C  C   . ASP A 1 161 ? 5.811   -4.742  -2.949  1.00 20.49 ? 162 ASP A C   1 
ATOM   1307 O  O   . ASP A 1 161 ? 6.165   -4.931  -4.115  1.00 22.41 ? 162 ASP A O   1 
ATOM   1308 C  CB  . ASP A 1 161 ? 3.465   -5.606  -2.661  1.00 18.59 ? 162 ASP A CB  1 
ATOM   1309 C  CG  . ASP A 1 161 ? 2.708   -6.939  -2.649  1.00 20.10 ? 162 ASP A CG  1 
ATOM   1310 O  OD1 . ASP A 1 161 ? 3.397   -7.978  -2.731  1.00 21.12 ? 162 ASP A OD1 1 
ATOM   1311 O  OD2 . ASP A 1 161 ? 1.447   -6.937  -2.477  1.00 22.45 ? 162 ASP A OD2 1 
ATOM   1312 N  N   . VAL A 1 162 ? 6.233   -3.679  -2.245  1.00 17.30 ? 163 VAL A N   1 
ATOM   1313 C  CA  . VAL A 1 162 ? 7.095   -2.640  -2.851  1.00 19.52 ? 163 VAL A CA  1 
ATOM   1314 C  C   . VAL A 1 162 ? 8.594   -2.904  -2.638  1.00 15.11 ? 163 VAL A C   1 
ATOM   1315 O  O   . VAL A 1 162 ? 9.476   -2.209  -3.195  1.00 17.23 ? 163 VAL A O   1 
ATOM   1316 C  CB  . VAL A 1 162 ? 6.598   -1.279  -2.312  1.00 20.48 ? 163 VAL A CB  1 
ATOM   1317 C  CG1 . VAL A 1 162 ? 7.300   -0.902  -1.035  1.00 18.60 ? 163 VAL A CG1 1 
ATOM   1318 C  CG2 . VAL A 1 162 ? 6.785   -0.098  -3.266  1.00 21.80 ? 163 VAL A CG2 1 
ATOM   1319 N  N   . LEU A 1 163 ? 8.976   -3.903  -1.800  1.00 15.48 ? 164 LEU A N   1 
ATOM   1320 C  CA  . LEU A 1 163 ? 10.365  -4.124  -1.396  1.00 14.59 ? 164 LEU A CA  1 
ATOM   1321 C  C   . LEU A 1 163 ? 11.305  -4.393  -2.594  1.00 14.84 ? 164 LEU A C   1 
ATOM   1322 O  O   . LEU A 1 163 ? 12.423  -4.048  -2.583  1.00 16.77 ? 164 LEU A O   1 
ATOM   1323 C  CB  . LEU A 1 163 ? 10.509  -5.188  -0.283  1.00 14.38 ? 164 LEU A CB  1 
ATOM   1324 C  CG  . LEU A 1 163 ? 9.796   -4.792  1.021   1.00 14.02 ? 164 LEU A CG  1 
ATOM   1325 C  CD1 . LEU A 1 163 ? 10.019  -5.948  1.995   1.00 15.20 ? 164 LEU A CD1 1 
ATOM   1326 C  CD2 . LEU A 1 163 ? 10.356  -3.484  1.585   1.00 13.92 ? 164 LEU A CD2 1 
ATOM   1327 N  N   . ASP A 1 164 ? 10.792  -5.125  -3.563  1.00 19.58 ? 165 ASP A N   1 
ATOM   1328 C  CA  . ASP A 1 164 ? 11.617  -5.392  -4.704  1.00 22.20 ? 165 ASP A CA  1 
ATOM   1329 C  C   . ASP A 1 164 ? 11.981  -4.095  -5.500  1.00 24.37 ? 165 ASP A C   1 
ATOM   1330 O  O   . ASP A 1 164 ? 12.985  -4.120  -6.220  1.00 28.47 ? 165 ASP A O   1 
ATOM   1331 C  CB  . ASP A 1 164 ? 10.852  -6.369  -5.608  1.00 25.54 ? 165 ASP A CB  1 
ATOM   1332 C  CG  . ASP A 1 164 ? 9.889   -5.646  -6.451  1.00 22.38 ? 165 ASP A CG  1 
ATOM   1333 O  OD1 . ASP A 1 164 ? 8.824   -5.186  -5.990  1.00 27.66 ? 165 ASP A OD1 1 
ATOM   1334 O  OD2 . ASP A 1 164 ? 10.244  -5.434  -7.666  1.00 28.34 ? 165 ASP A OD2 1 
ATOM   1335 N  N   . SER A 1 165 ? 11.252  -2.980  -5.335  1.00 21.50 ? 166 SER A N   1 
ATOM   1336 C  CA  . SER A 1 165 ? 11.691  -1.699  -5.943  1.00 23.20 ? 166 SER A CA  1 
ATOM   1337 C  C   . SER A 1 165 ? 12.810  -0.985  -5.150  1.00 24.89 ? 166 SER A C   1 
ATOM   1338 O  O   . SER A 1 165 ? 13.490  -0.053  -5.648  1.00 21.61 ? 166 SER A O   1 
ATOM   1339 C  CB  . SER A 1 165 ? 10.510  -0.779  -6.130  1.00 24.19 ? 166 SER A CB  1 
ATOM   1340 O  OG  . SER A 1 165 ? 10.083  -0.213  -4.919  1.00 26.07 ? 166 SER A OG  1 
ATOM   1341 N  N   . ILE A 1 166 ? 12.967  -1.364  -3.873  1.00 19.05 ? 167 ILE A N   1 
ATOM   1342 C  CA  . ILE A 1 166 ? 14.055  -0.790  -3.069  1.00 17.46 ? 167 ILE A CA  1 
ATOM   1343 C  C   . ILE A 1 166 ? 15.021  -1.829  -2.541  1.00 16.98 ? 167 ILE A C   1 
ATOM   1344 O  O   . ILE A 1 166 ? 15.458  -1.836  -1.370  1.00 16.26 ? 167 ILE A O   1 
ATOM   1345 C  CB  . ILE A 1 166 ? 13.483  0.077   -1.912  1.00 16.53 ? 167 ILE A CB  1 
ATOM   1346 C  CG1 . ILE A 1 166 ? 12.648  -0.797  -0.969  1.00 16.97 ? 167 ILE A CG1 1 
ATOM   1347 C  CG2 . ILE A 1 166 ? 12.626  1.231   -2.456  1.00 18.35 ? 167 ILE A CG2 1 
ATOM   1348 C  CD1 . ILE A 1 166 ? 12.729  -0.316  0.491   1.00 18.44 ? 167 ILE A CD1 1 
ATOM   1349 N  N   . LYS A 1 167 ? 15.407  -2.737  -3.432  1.00 17.10 ? 168 LYS A N   1 
ATOM   1350 C  CA  . LYS A 1 167 ? 16.261  -3.811  -3.063  1.00 16.35 ? 168 LYS A CA  1 
ATOM   1351 C  C   . LYS A 1 167 ? 17.612  -3.462  -2.414  1.00 17.67 ? 168 LYS A C   1 
ATOM   1352 O  O   . LYS A 1 167 ? 18.029  -4.109  -1.467  1.00 15.30 ? 168 LYS A O   1 
ATOM   1353 C  CB  . LYS A 1 167 ? 16.530  -4.668  -4.354  1.00 17.11 ? 168 LYS A CB  1 
ATOM   1354 C  CG  . LYS A 1 167 ? 17.201  -5.952  -3.950  1.00 18.83 ? 168 LYS A CG  1 
ATOM   1355 C  CD  . LYS A 1 167 ? 17.502  -6.919  -5.129  1.00 24.20 ? 168 LYS A CD  1 
ATOM   1356 C  CE  . LYS A 1 167 ? 18.457  -7.992  -4.631  1.00 27.30 ? 168 LYS A CE  1 
ATOM   1357 N  NZ  . LYS A 1 167 ? 18.116  -9.358  -5.108  1.00 35.39 ? 168 LYS A NZ  1 
ATOM   1358 N  N   . THR A 1 168 ? 18.301  -2.421  -2.929  1.00 16.59 ? 169 THR A N   1 
ATOM   1359 C  CA  . THR A 1 168 ? 19.658  -2.149  -2.522  1.00 16.94 ? 169 THR A CA  1 
ATOM   1360 C  C   . THR A 1 168 ? 19.753  -0.767  -1.820  1.00 14.78 ? 169 THR A C   1 
ATOM   1361 O  O   . THR A 1 168 ? 18.922  0.041   -1.978  1.00 17.22 ? 169 THR A O   1 
ATOM   1362 C  CB  . THR A 1 168 ? 20.579  -2.173  -3.798  1.00 18.03 ? 169 THR A CB  1 
ATOM   1363 O  OG1 . THR A 1 168 ? 19.905  -1.384  -4.788  1.00 23.45 ? 169 THR A OG1 1 
ATOM   1364 C  CG2 . THR A 1 168 ? 20.774  -3.645  -4.203  1.00 18.70 ? 169 THR A CG2 1 
ATOM   1365 N  N   . LYS A 1 169 ? 20.762  -0.631  -0.993  1.00 20.52 ? 170 LYS A N   1 
ATOM   1366 C  CA  . LYS A 1 169 ? 21.112  0.634   -0.286  1.00 20.95 ? 170 LYS A CA  1 
ATOM   1367 C  C   . LYS A 1 169 ? 20.956  1.938   -1.065  1.00 24.51 ? 170 LYS A C   1 
ATOM   1368 O  O   . LYS A 1 169 ? 21.492  2.071   -2.184  1.00 28.64 ? 170 LYS A O   1 
ATOM   1369 C  CB  . LYS A 1 169 ? 22.495  0.507   0.259   1.00 22.19 ? 170 LYS A CB  1 
ATOM   1370 C  CG  . LYS A 1 169 ? 22.988  1.723   1.089   1.00 22.30 ? 170 LYS A CG  1 
ATOM   1371 C  CD  . LYS A 1 169 ? 24.290  1.295   1.700   1.00 26.13 ? 170 LYS A CD  1 
ATOM   1372 C  CE  . LYS A 1 169 ? 25.056  2.430   2.352   1.00 32.80 ? 170 LYS A CE  1 
ATOM   1373 N  NZ  . LYS A 1 169 ? 26.516  2.123   2.197   1.00 42.72 ? 170 LYS A NZ  1 
ATOM   1374 N  N   . GLY A 1 170 ? 20.219  2.868   -0.510  1.00 23.66 ? 171 GLY A N   1 
ATOM   1375 C  CA  . GLY A 1 170 ? 19.975  4.152   -1.155  1.00 26.34 ? 171 GLY A CA  1 
ATOM   1376 C  C   . GLY A 1 170 ? 18.814  4.213   -2.078  1.00 28.01 ? 171 GLY A C   1 
ATOM   1377 O  O   . GLY A 1 170 ? 18.368  5.314   -2.438  1.00 34.18 ? 171 GLY A O   1 
ATOM   1378 N  N   . LYS A 1 171 ? 18.260  3.059   -2.482  1.00 22.02 ? 172 LYS A N   1 
ATOM   1379 C  CA  . LYS A 1 171 ? 17.033  3.136   -3.229  1.00 21.05 ? 172 LYS A CA  1 
ATOM   1380 C  C   . LYS A 1 171 ? 15.837  3.595   -2.448  1.00 21.81 ? 172 LYS A C   1 
ATOM   1381 O  O   . LYS A 1 171 ? 15.698  3.230   -1.254  1.00 22.86 ? 172 LYS A O   1 
ATOM   1382 C  CB  . LYS A 1 171 ? 16.725  1.796   -3.984  1.00 24.77 ? 172 LYS A CB  1 
ATOM   1383 C  CG  . LYS A 1 171 ? 17.858  1.322   -4.893  1.00 27.70 ? 172 LYS A CG  1 
ATOM   1384 C  CD  . LYS A 1 171 ? 17.469  0.187   -5.857  1.00 32.76 ? 172 LYS A CD  1 
ATOM   1385 N  N   A SER A 1 172 ? 14.925  4.265   -3.132  0.50 20.69 ? 173 SER A N   1 
ATOM   1386 N  N   B SER A 1 172 ? 14.982  4.423   -3.056  0.50 19.21 ? 173 SER A N   1 
ATOM   1387 C  CA  A SER A 1 172 ? 13.750  4.845   -2.553  0.50 20.85 ? 173 SER A CA  1 
ATOM   1388 C  CA  B SER A 1 172 ? 13.647  4.789   -2.544  0.50 19.24 ? 173 SER A CA  1 
ATOM   1389 C  C   A SER A 1 172 ? 12.570  4.892   -3.545  0.50 23.09 ? 173 SER A C   1 
ATOM   1390 C  C   B SER A 1 172 ? 12.536  4.676   -3.549  0.50 21.58 ? 173 SER A C   1 
ATOM   1391 O  O   A SER A 1 172 ? 12.773  4.965   -4.794  0.50 21.70 ? 173 SER A O   1 
ATOM   1392 O  O   B SER A 1 172 ? 12.729  4.519   -4.778  0.50 21.00 ? 173 SER A O   1 
ATOM   1393 C  CB  A SER A 1 172 ? 14.139  6.235   -2.009  0.50 22.52 ? 173 SER A CB  1 
ATOM   1394 C  CB  B SER A 1 172 ? 13.564  6.228   -1.952  0.50 19.50 ? 173 SER A CB  1 
ATOM   1395 O  OG  A SER A 1 172 ? 14.851  6.991   -2.979  0.50 19.66 ? 173 SER A OG  1 
ATOM   1396 O  OG  B SER A 1 172 ? 13.414  7.212   -2.982  0.50 15.71 ? 173 SER A OG  1 
ATOM   1397 N  N   . ALA A 1 173 ? 11.348  4.832   -3.030  1.00 20.85 ? 174 ALA A N   1 
ATOM   1398 C  CA  . ALA A 1 173 ? 10.154  4.852   -3.821  1.00 24.01 ? 174 ALA A CA  1 
ATOM   1399 C  C   . ALA A 1 173 ? 9.032   5.638   -3.169  1.00 28.76 ? 174 ALA A C   1 
ATOM   1400 O  O   . ALA A 1 173 ? 8.902   5.669   -1.925  1.00 23.37 ? 174 ALA A O   1 
ATOM   1401 C  CB  . ALA A 1 173 ? 9.700   3.445   -4.094  1.00 23.63 ? 174 ALA A CB  1 
ATOM   1402 N  N   . ASP A 1 174 ? 8.190   6.260   -3.991  1.00 27.78 ? 175 ASP A N   1 
ATOM   1403 C  CA  . ASP A 1 174 ? 7.018   6.928   -3.467  1.00 30.26 ? 175 ASP A CA  1 
ATOM   1404 C  C   . ASP A 1 174 ? 6.265   5.891   -2.722  1.00 27.57 ? 175 ASP A C   1 
ATOM   1405 O  O   . ASP A 1 174 ? 6.221   4.731   -3.148  1.00 26.89 ? 175 ASP A O   1 
ATOM   1406 C  CB  . ASP A 1 174 ? 6.086   7.484   -4.582  1.00 35.61 ? 175 ASP A CB  1 
ATOM   1407 C  CG  . ASP A 1 174 ? 6.824   8.387   -5.540  1.00 47.23 ? 175 ASP A CG  1 
ATOM   1408 O  OD1 . ASP A 1 174 ? 7.604   9.259   -5.048  1.00 42.14 ? 175 ASP A OD1 1 
ATOM   1409 O  OD2 . ASP A 1 174 ? 6.620   8.220   -6.783  1.00 52.73 ? 175 ASP A OD2 1 
ATOM   1410 N  N   . PHE A 1 175 ? 5.659   6.312   -1.606  1.00 21.48 ? 176 PHE A N   1 
ATOM   1411 C  CA  . PHE A 1 175 ? 4.826   5.402   -0.815  1.00 19.11 ? 176 PHE A CA  1 
ATOM   1412 C  C   . PHE A 1 175 ? 3.788   6.139   -0.071  1.00 20.65 ? 176 PHE A C   1 
ATOM   1413 O  O   . PHE A 1 175 ? 3.987   6.433   1.100   1.00 23.13 ? 176 PHE A O   1 
ATOM   1414 C  CB  . PHE A 1 175 ? 5.748   4.583   0.150   1.00 16.88 ? 176 PHE A CB  1 
ATOM   1415 C  CG  . PHE A 1 175 ? 5.129   3.307   0.650   1.00 17.89 ? 176 PHE A CG  1 
ATOM   1416 C  CD1 . PHE A 1 175 ? 4.857   2.241   -0.202  1.00 18.00 ? 176 PHE A CD1 1 
ATOM   1417 C  CD2 . PHE A 1 175 ? 4.880   3.130   1.998   1.00 16.26 ? 176 PHE A CD2 1 
ATOM   1418 C  CE1 . PHE A 1 175 ? 4.329   1.052   0.299   1.00 19.04 ? 176 PHE A CE1 1 
ATOM   1419 C  CE2 . PHE A 1 175 ? 4.297   2.002   2.503   1.00 16.99 ? 176 PHE A CE2 1 
ATOM   1420 C  CZ  . PHE A 1 175 ? 4.056   0.929   1.625   1.00 15.81 ? 176 PHE A CZ  1 
ATOM   1421 N  N   . THR A 1 176 ? 2.703   6.505   -0.755  1.00 17.39 ? 177 THR A N   1 
ATOM   1422 C  CA  . THR A 1 176 ? 1.569   7.266   -0.261  1.00 17.31 ? 177 THR A CA  1 
ATOM   1423 C  C   . THR A 1 176 ? 0.345   6.474   0.220   1.00 14.24 ? 177 THR A C   1 
ATOM   1424 O  O   . THR A 1 176 ? 0.130   5.297   -0.281  1.00 15.16 ? 177 THR A O   1 
ATOM   1425 C  CB  . THR A 1 176 ? 1.149   8.344   -1.303  1.00 18.84 ? 177 THR A CB  1 
ATOM   1426 O  OG1 . THR A 1 176 ? 0.762   7.666   -2.509  1.00 22.74 ? 177 THR A OG1 1 
ATOM   1427 C  CG2 . THR A 1 176 ? 2.360   9.244   -1.569  1.00 20.09 ? 177 THR A CG2 1 
ATOM   1428 N  N   . ASN A 1 177 ? -0.458  6.989   1.125   1.00 15.32 ? 178 ASN A N   1 
ATOM   1429 C  CA  . ASN A 1 177 ? -1.743  6.477   1.507   1.00 16.13 ? 178 ASN A CA  1 
ATOM   1430 C  C   . ASN A 1 177 ? -1.621  5.123   2.270   1.00 16.87 ? 178 ASN A C   1 
ATOM   1431 O  O   . ASN A 1 177 ? -2.561  4.331   2.256   1.00 16.23 ? 178 ASN A O   1 
ATOM   1432 C  CB  . ASN A 1 177 ? -2.686  6.307   0.274   1.00 16.26 ? 178 ASN A CB  1 
ATOM   1433 C  CG  . ASN A 1 177 ? -2.959  7.655   -0.405  1.00 18.01 ? 178 ASN A CG  1 
ATOM   1434 O  OD1 . ASN A 1 177 ? -3.677  8.491   0.163   1.00 20.26 ? 178 ASN A OD1 1 
ATOM   1435 N  ND2 . ASN A 1 177 ? -2.222  7.913   -1.504  1.00 15.02 ? 178 ASN A ND2 1 
ATOM   1436 N  N   . PHE A 1 178 ? -0.448  4.929   2.893   1.00 15.29 ? 179 PHE A N   1 
ATOM   1437 C  CA  . PHE A 1 178 ? -0.252  3.715   3.749   1.00 16.31 ? 179 PHE A CA  1 
ATOM   1438 C  C   . PHE A 1 178 ? -0.703  4.014   5.110   1.00 14.64 ? 179 PHE A C   1 
ATOM   1439 O  O   . PHE A 1 178 ? -0.249  5.022   5.704   1.00 14.59 ? 179 PHE A O   1 
ATOM   1440 C  CB  . PHE A 1 178 ? 1.139   3.288   3.855   1.00 13.89 ? 179 PHE A CB  1 
ATOM   1441 C  CG  . PHE A 1 178 ? 1.274   2.031   4.714   1.00 13.92 ? 179 PHE A CG  1 
ATOM   1442 C  CD1 . PHE A 1 178 ? 0.785   0.809   4.215   1.00 16.97 ? 179 PHE A CD1 1 
ATOM   1443 C  CD2 . PHE A 1 178 ? 1.814   2.095   6.003   1.00 14.42 ? 179 PHE A CD2 1 
ATOM   1444 C  CE1 . PHE A 1 178 ? 0.914   -0.332  4.981   1.00 17.93 ? 179 PHE A CE1 1 
ATOM   1445 C  CE2 . PHE A 1 178 ? 1.856   0.957   6.777   1.00 13.93 ? 179 PHE A CE2 1 
ATOM   1446 C  CZ  . PHE A 1 178 ? 1.433   -0.244  6.270   1.00 15.08 ? 179 PHE A CZ  1 
ATOM   1447 N  N   . ASP A 1 179 ? -1.590  3.171   5.614   1.00 15.20 ? 180 ASP A N   1 
ATOM   1448 C  CA  . ASP A 1 179 ? -2.190  3.335   6.893   1.00 14.31 ? 180 ASP A CA  1 
ATOM   1449 C  C   . ASP A 1 179 ? -1.563  2.495   8.000   1.00 13.54 ? 180 ASP A C   1 
ATOM   1450 O  O   . ASP A 1 179 ? -1.753  1.277   8.027   1.00 13.64 ? 180 ASP A O   1 
ATOM   1451 C  CB  . ASP A 1 179 ? -3.664  2.950   6.776   1.00 17.92 ? 180 ASP A CB  1 
ATOM   1452 C  CG  . ASP A 1 179 ? -4.476  3.349   7.983   1.00 19.57 ? 180 ASP A CG  1 
ATOM   1453 O  OD1 . ASP A 1 179 ? -3.890  3.610   9.057   1.00 16.73 ? 180 ASP A OD1 1 
ATOM   1454 O  OD2 . ASP A 1 179 ? -5.715  3.396   7.847   1.00 24.83 ? 180 ASP A OD2 1 
ATOM   1455 N  N   . PRO A 1 180 ? -0.848  3.147   8.929   1.00 10.81 ? 181 PRO A N   1 
ATOM   1456 C  CA  . PRO A 1 180 ? -0.087  2.316   9.927   1.00 10.75 ? 181 PRO A CA  1 
ATOM   1457 C  C   . PRO A 1 180 ? -0.984  1.692   10.941  1.00 11.66 ? 181 PRO A C   1 
ATOM   1458 O  O   . PRO A 1 180 ? -0.521  0.774   11.679  1.00 9.72  ? 181 PRO A O   1 
ATOM   1459 C  CB  . PRO A 1 180 ? 0.931   3.347   10.468  1.00 12.19 ? 181 PRO A CB  1 
ATOM   1460 C  CG  . PRO A 1 180 ? 0.147   4.637   10.456  1.00 12.33 ? 181 PRO A CG  1 
ATOM   1461 C  CD  . PRO A 1 180 ? -0.519  4.601   9.087   1.00 11.90 ? 181 PRO A CD  1 
ATOM   1462 N  N   . ARG A 1 181 ? -2.253  2.051   11.006  1.00 11.97 ? 182 ARG A N   1 
ATOM   1463 C  CA  . ARG A 1 181 ? -3.213  1.355   11.928  1.00 12.17 ? 182 ARG A CA  1 
ATOM   1464 C  C   . ARG A 1 181 ? -3.315  -0.164  11.588  1.00 12.60 ? 182 ARG A C   1 
ATOM   1465 O  O   . ARG A 1 181 ? -3.683  -0.947  12.452  1.00 13.99 ? 182 ARG A O   1 
ATOM   1466 C  CB  . ARG A 1 181 ? -4.611  2.033   11.854  1.00 13.49 ? 182 ARG A CB  1 
ATOM   1467 C  CG  . ARG A 1 181 ? -4.513  3.466   12.339  1.00 15.34 ? 182 ARG A CG  1 
ATOM   1468 C  CD  . ARG A 1 181 ? -5.826  4.221   12.202  1.00 19.09 ? 182 ARG A CD  1 
ATOM   1469 N  NE  . ARG A 1 181 ? -6.230  4.326   10.825  1.00 19.61 ? 182 ARG A NE  1 
ATOM   1470 C  CZ  . ARG A 1 181 ? -7.371  4.946   10.463  1.00 24.06 ? 182 ARG A CZ  1 
ATOM   1471 N  NH1 . ARG A 1 181 ? -8.150  5.452   11.412  1.00 25.97 ? 182 ARG A NH1 1 
ATOM   1472 N  NH2 . ARG A 1 181 ? -7.696  5.017   9.193   1.00 22.26 ? 182 ARG A NH2 1 
ATOM   1473 N  N   . GLY A 1 182 ? -3.055  -0.494  10.340  1.00 12.03 ? 183 GLY A N   1 
ATOM   1474 C  CA  . GLY A 1 182 ? -3.089  -1.910  9.883   1.00 12.61 ? 183 GLY A CA  1 
ATOM   1475 C  C   . GLY A 1 182 ? -2.006  -2.777  10.472  1.00 15.79 ? 183 GLY A C   1 
ATOM   1476 O  O   . GLY A 1 182 ? -1.970  -3.992  10.214  1.00 15.21 ? 183 GLY A O   1 
ATOM   1477 N  N   . LEU A 1 183 ? -1.075  -2.158  11.170  1.00 13.02 ? 184 LEU A N   1 
ATOM   1478 C  CA  . LEU A 1 183 ? 0.060   -2.928  11.760  1.00 12.04 ? 184 LEU A CA  1 
ATOM   1479 C  C   . LEU A 1 183 ? -0.104  -3.100  13.245  1.00 12.21 ? 184 LEU A C   1 
ATOM   1480 O  O   . LEU A 1 183 ? 0.817   -3.669  13.873  1.00 12.86 ? 184 LEU A O   1 
ATOM   1481 C  CB  . LEU A 1 183 ? 1.388   -2.194  11.476  1.00 12.64 ? 184 LEU A CB  1 
ATOM   1482 C  CG  . LEU A 1 183 ? 1.822   -1.976  9.995   1.00 11.99 ? 184 LEU A CG  1 
ATOM   1483 C  CD1 . LEU A 1 183 ? 3.037   -1.092  9.822   1.00 13.13 ? 184 LEU A CD1 1 
ATOM   1484 C  CD2 . LEU A 1 183 ? 2.077   -3.269  9.239   1.00 14.45 ? 184 LEU A CD2 1 
ATOM   1485 N  N   . LEU A 1 184 ? -1.188  -2.668  13.872  1.00 10.81 ? 185 LEU A N   1 
ATOM   1486 C  CA  . LEU A 1 184 ? -1.349  -2.681  15.358  1.00 10.88 ? 185 LEU A CA  1 
ATOM   1487 C  C   . LEU A 1 184 ? -2.107  -3.924  15.852  1.00 12.65 ? 185 LEU A C   1 
ATOM   1488 O  O   . LEU A 1 184 ? -3.258  -4.204  15.323  1.00 16.03 ? 185 LEU A O   1 
ATOM   1489 C  CB  . LEU A 1 184 ? -2.143  -1.433  15.829  1.00 9.59  ? 185 LEU A CB  1 
ATOM   1490 C  CG  . LEU A 1 184 ? -1.571  -0.079  15.465  1.00 10.60 ? 185 LEU A CG  1 
ATOM   1491 C  CD1 . LEU A 1 184 ? -2.462  1.049   15.947  1.00 12.50 ? 185 LEU A CD1 1 
ATOM   1492 C  CD2 . LEU A 1 184 ? -0.117  0.014   15.967  1.00 10.34 ? 185 LEU A CD2 1 
ATOM   1493 N  N   . PRO A 1 185 ? -1.694  -4.528  16.933  1.00 11.93 ? 186 PRO A N   1 
ATOM   1494 C  CA  . PRO A 1 185 ? -2.459  -5.639  17.473  1.00 11.80 ? 186 PRO A CA  1 
ATOM   1495 C  C   . PRO A 1 185 ? -3.728  -5.106  18.140  1.00 12.91 ? 186 PRO A C   1 
ATOM   1496 O  O   . PRO A 1 185 ? -3.908  -3.896  18.260  1.00 12.85 ? 186 PRO A O   1 
ATOM   1497 C  CB  . PRO A 1 185 ? -1.500  -6.247  18.537  1.00 11.09 ? 186 PRO A CB  1 
ATOM   1498 C  CG  . PRO A 1 185 ? -0.734  -5.048  19.064  1.00 9.44  ? 186 PRO A CG  1 
ATOM   1499 C  CD  . PRO A 1 185 ? -0.540  -4.134  17.784  1.00 10.06 ? 186 PRO A CD  1 
ATOM   1500 N  N   A GLU A 1 186 ? -4.602  -5.983  18.634  0.50 13.76 ? 187 GLU A N   1 
ATOM   1501 N  N   B GLU A 1 186 ? -4.599  -6.036  18.570  0.50 14.56 ? 187 GLU A N   1 
ATOM   1502 C  CA  A GLU A 1 186 ? -5.837  -5.550  19.286  0.50 13.57 ? 187 GLU A CA  1 
ATOM   1503 C  CA  B GLU A 1 186 ? -5.815  -5.713  19.313  0.50 14.96 ? 187 GLU A CA  1 
ATOM   1504 C  C   A GLU A 1 186 ? -5.616  -4.856  20.656  0.50 13.84 ? 187 GLU A C   1 
ATOM   1505 C  C   B GLU A 1 186 ? -5.525  -4.857  20.512  0.50 14.42 ? 187 GLU A C   1 
ATOM   1506 O  O   A GLU A 1 186 ? -6.248  -3.855  21.010  0.50 14.45 ? 187 GLU A O   1 
ATOM   1507 O  O   B GLU A 1 186 ? -6.015  -3.729  20.535  0.50 14.77 ? 187 GLU A O   1 
ATOM   1508 C  CB  A GLU A 1 186 ? -6.754  -6.782  19.383  0.50 14.51 ? 187 GLU A CB  1 
ATOM   1509 C  CB  B GLU A 1 186 ? -6.560  -6.997  19.739  0.50 17.23 ? 187 GLU A CB  1 
ATOM   1510 C  CG  A GLU A 1 186 ? -7.545  -6.784  20.666  0.50 15.41 ? 187 GLU A CG  1 
ATOM   1511 C  CG  B GLU A 1 186 ? -7.183  -7.773  18.602  0.50 20.50 ? 187 GLU A CG  1 
ATOM   1512 C  CD  A GLU A 1 186 ? -8.422  -8.037  20.820  0.50 15.93 ? 187 GLU A CD  1 
ATOM   1513 C  CD  B GLU A 1 186 ? -8.023  -8.951  19.128  0.50 20.92 ? 187 GLU A CD  1 
ATOM   1514 O  OE1 A GLU A 1 186 ? -8.375  -8.916  19.948  0.50 16.77 ? 187 GLU A OE1 1 
ATOM   1515 O  OE1 B GLU A 1 186 ? -8.069  -9.181  20.376  0.50 21.75 ? 187 GLU A OE1 1 
ATOM   1516 O  OE2 A GLU A 1 186 ? -9.111  -8.123  21.871  0.50 18.04 ? 187 GLU A OE2 1 
ATOM   1517 O  OE2 B GLU A 1 186 ? -8.667  -9.618  18.311  0.50 26.25 ? 187 GLU A OE2 1 
ATOM   1518 N  N   . SER A 1 187 ? -4.687  -5.351  21.460  1.00 12.99 ? 188 SER A N   1 
ATOM   1519 C  CA  . SER A 1 187 ? -4.478  -4.719  22.719  1.00 13.91 ? 188 SER A CA  1 
ATOM   1520 C  C   . SER A 1 187 ? -3.347  -3.708  22.660  1.00 12.67 ? 188 SER A C   1 
ATOM   1521 O  O   . SER A 1 187 ? -2.327  -3.955  22.001  1.00 15.06 ? 188 SER A O   1 
ATOM   1522 C  CB  . SER A 1 187 ? -4.055  -5.775  23.744  1.00 12.75 ? 188 SER A CB  1 
ATOM   1523 O  OG  . SER A 1 187 ? -3.844  -5.185  24.973  1.00 14.96 ? 188 SER A OG  1 
ATOM   1524 N  N   . LEU A 1 188 ? -3.550  -2.596  23.375  1.00 11.29 ? 189 LEU A N   1 
ATOM   1525 C  CA  . LEU A 1 188 ? -2.493  -1.594  23.614  1.00 13.16 ? 189 LEU A CA  1 
ATOM   1526 C  C   . LEU A 1 188 ? -1.837  -1.747  24.989  1.00 11.55 ? 189 LEU A C   1 
ATOM   1527 O  O   . LEU A 1 188 ? -1.157  -0.810  25.440  1.00 13.00 ? 189 LEU A O   1 
ATOM   1528 C  CB  . LEU A 1 188 ? -3.006  -0.150  23.260  1.00 12.54 ? 189 LEU A CB  1 
ATOM   1529 C  CG  . LEU A 1 188 ? -3.451  0.112   21.808  1.00 14.84 ? 189 LEU A CG  1 
ATOM   1530 C  CD1 . LEU A 1 188 ? -3.923  1.529   21.717  1.00 17.56 ? 189 LEU A CD1 1 
ATOM   1531 C  CD2 . LEU A 1 188 ? -2.373  -0.120  20.738  1.00 16.14 ? 189 LEU A CD2 1 
ATOM   1532 N  N   . ASP A 1 189 ? -1.945  -2.882  25.658  1.00 13.77 ? 190 ASP A N   1 
ATOM   1533 C  CA  . ASP A 1 189 ? -1.230  -3.101  26.933  1.00 14.28 ? 190 ASP A CA  1 
ATOM   1534 C  C   . ASP A 1 189 ? 0.286   -3.035  26.650  1.00 11.99 ? 190 ASP A C   1 
ATOM   1535 O  O   . ASP A 1 189 ? 0.738   -3.529  25.572  1.00 12.26 ? 190 ASP A O   1 
ATOM   1536 C  CB  . ASP A 1 189 ? -1.552  -4.483  27.544  1.00 15.97 ? 190 ASP A CB  1 
ATOM   1537 C  CG  . ASP A 1 189 ? -2.920  -4.525  28.223  1.00 19.19 ? 190 ASP A CG  1 
ATOM   1538 O  OD1 . ASP A 1 189 ? -3.481  -3.454  28.555  1.00 22.59 ? 190 ASP A OD1 1 
ATOM   1539 O  OD2 . ASP A 1 189 ? -3.433  -5.647  28.424  1.00 21.69 ? 190 ASP A OD2 1 
ATOM   1540 N  N   . TYR A 1 190 ? 1.077   -2.409  27.539  1.00 9.43  ? 191 TYR A N   1 
ATOM   1541 C  CA  . TYR A 1 190 ? 2.491   -2.187  27.143  1.00 10.18 ? 191 TYR A CA  1 
ATOM   1542 C  C   . TYR A 1 190 ? 3.396   -2.301  28.385  1.00 10.73 ? 191 TYR A C   1 
ATOM   1543 O  O   . TYR A 1 190 ? 2.977   -2.134  29.551  1.00 9.60  ? 191 TYR A O   1 
ATOM   1544 C  CB  . TYR A 1 190 ? 2.607   -0.761  26.500  1.00 10.61 ? 191 TYR A CB  1 
ATOM   1545 C  CG  . TYR A 1 190 ? 2.213   0.352   27.431  1.00 9.80  ? 191 TYR A CG  1 
ATOM   1546 C  CD1 . TYR A 1 190 ? 3.122   0.926   28.356  1.00 10.43 ? 191 TYR A CD1 1 
ATOM   1547 C  CD2 . TYR A 1 190 ? 0.906   0.882   27.379  1.00 10.50 ? 191 TYR A CD2 1 
ATOM   1548 C  CE1 . TYR A 1 190 ? 2.718   1.976   29.219  1.00 10.32 ? 191 TYR A CE1 1 
ATOM   1549 C  CE2 . TYR A 1 190 ? 0.526   1.930   28.227  1.00 11.58 ? 191 TYR A CE2 1 
ATOM   1550 C  CZ  . TYR A 1 190 ? 1.420   2.472   29.135  1.00 11.68 ? 191 TYR A CZ  1 
ATOM   1551 O  OH  . TYR A 1 190 ? 1.027   3.497   29.982  1.00 13.35 ? 191 TYR A OH  1 
ATOM   1552 N  N   . TRP A 1 191 ? 4.697   -2.456  28.143  1.00 8.23  ? 192 TRP A N   1 
ATOM   1553 C  CA  . TRP A 1 191 ? 5.774   -2.230  29.079  1.00 8.50  ? 192 TRP A CA  1 
ATOM   1554 C  C   . TRP A 1 191 ? 6.464   -0.923  28.688  1.00 9.24  ? 192 TRP A C   1 
ATOM   1555 O  O   . TRP A 1 191 ? 6.452   -0.534  27.512  1.00 8.35  ? 192 TRP A O   1 
ATOM   1556 C  CB  . TRP A 1 191 ? 6.829   -3.315  29.006  1.00 8.91  ? 192 TRP A CB  1 
ATOM   1557 C  CG  . TRP A 1 191 ? 6.359   -4.682  29.427  1.00 9.10  ? 192 TRP A CG  1 
ATOM   1558 C  CD1 . TRP A 1 191 ? 6.112   -5.152  30.719  1.00 8.94  ? 192 TRP A CD1 1 
ATOM   1559 C  CD2 . TRP A 1 191 ? 6.087   -5.814  28.540  1.00 9.05  ? 192 TRP A CD2 1 
ATOM   1560 N  NE1 . TRP A 1 191 ? 5.700   -6.466  30.684  1.00 10.07 ? 192 TRP A NE1 1 
ATOM   1561 C  CE2 . TRP A 1 191 ? 5.665   -6.922  29.403  1.00 9.46  ? 192 TRP A CE2 1 
ATOM   1562 C  CE3 . TRP A 1 191 ? 6.154   -6.010  27.167  1.00 9.52  ? 192 TRP A CE3 1 
ATOM   1563 C  CZ2 . TRP A 1 191 ? 5.323   -8.161  28.882  1.00 9.61  ? 192 TRP A CZ2 1 
ATOM   1564 C  CZ3 . TRP A 1 191 ? 5.802   -7.262  26.654  1.00 10.17 ? 192 TRP A CZ3 1 
ATOM   1565 C  CH2 . TRP A 1 191 ? 5.406   -8.311  27.493  1.00 11.06 ? 192 TRP A CH2 1 
ATOM   1566 N  N   . THR A 1 192 ? 7.089   -0.234  29.621  1.00 8.01  ? 193 THR A N   1 
ATOM   1567 C  CA  . THR A 1 192 ? 7.734   1.043   29.326  1.00 8.31  ? 193 THR A CA  1 
ATOM   1568 C  C   . THR A 1 192 ? 8.975   1.256   30.197  1.00 8.04  ? 193 THR A C   1 
ATOM   1569 O  O   . THR A 1 192 ? 9.054   0.751   31.339  1.00 8.87  ? 193 THR A O   1 
ATOM   1570 C  CB  . THR A 1 192 ? 6.787   2.257   29.379  1.00 8.92  ? 193 THR A CB  1 
ATOM   1571 O  OG1 . THR A 1 192 ? 7.468   3.459   28.949  1.00 8.92  ? 193 THR A OG1 1 
ATOM   1572 C  CG2 . THR A 1 192 ? 6.302   2.484   30.813  1.00 9.12  ? 193 THR A CG2 1 
ATOM   1573 N  N   . TYR A 1 193 ? 10.041  1.774   29.563  1.00 7.85  ? 194 TYR A N   1 
ATOM   1574 C  CA  . TYR A 1 193 ? 11.262  2.087   30.293  1.00 8.16  ? 194 TYR A CA  1 
ATOM   1575 C  C   . TYR A 1 193 ? 12.072  3.100   29.522  1.00 8.94  ? 194 TYR A C   1 
ATOM   1576 O  O   . TYR A 1 193 ? 11.829  3.308   28.334  1.00 7.96  ? 194 TYR A O   1 
ATOM   1577 C  CB  . TYR A 1 193 ? 12.137  0.790   30.556  1.00 8.28  ? 194 TYR A CB  1 
ATOM   1578 C  CG  . TYR A 1 193 ? 12.859  0.312   29.280  1.00 7.55  ? 194 TYR A CG  1 
ATOM   1579 C  CD1 . TYR A 1 193 ? 12.180  -0.438  28.305  1.00 7.13  ? 194 TYR A CD1 1 
ATOM   1580 C  CD2 . TYR A 1 193 ? 14.194  0.635   29.032  1.00 7.88  ? 194 TYR A CD2 1 
ATOM   1581 C  CE1 . TYR A 1 193 ? 12.787  -0.803  27.121  1.00 6.84  ? 194 TYR A CE1 1 
ATOM   1582 C  CE2 . TYR A 1 193 ? 14.847  0.278   27.856  1.00 7.06  ? 194 TYR A CE2 1 
ATOM   1583 C  CZ  . TYR A 1 193 ? 14.154  -0.445  26.862  1.00 6.79  ? 194 TYR A CZ  1 
ATOM   1584 O  OH  . TYR A 1 193 ? 14.783  -0.726  25.718  1.00 6.57  ? 194 TYR A OH  1 
ATOM   1585 N  N   . PRO A 1 194 ? 13.036  3.838   30.188  1.00 7.50  ? 195 PRO A N   1 
ATOM   1586 C  CA  . PRO A 1 194 ? 13.871  4.781   29.507  1.00 8.19  ? 195 PRO A CA  1 
ATOM   1587 C  C   . PRO A 1 194 ? 15.090  4.157   28.858  1.00 7.55  ? 195 PRO A C   1 
ATOM   1588 O  O   . PRO A 1 194 ? 15.802  3.406   29.546  1.00 8.94  ? 195 PRO A O   1 
ATOM   1589 C  CB  . PRO A 1 194 ? 14.394  5.744   30.649  1.00 8.56  ? 195 PRO A CB  1 
ATOM   1590 C  CG  . PRO A 1 194 ? 14.289  4.863   31.867  1.00 9.18  ? 195 PRO A CG  1 
ATOM   1591 C  CD  . PRO A 1 194 ? 13.263  3.783   31.659  1.00 8.61  ? 195 PRO A CD  1 
ATOM   1592 N  N   . GLY A 1 195 ? 15.341  4.453   27.580  1.00 7.73  ? 196 GLY A N   1 
ATOM   1593 C  CA  . GLY A 1 195 ? 16.488  3.790   26.888  1.00 7.85  ? 196 GLY A CA  1 
ATOM   1594 C  C   . GLY A 1 195 ? 17.017  4.660   25.793  1.00 7.57  ? 196 GLY A C   1 
ATOM   1595 O  O   . GLY A 1 195 ? 17.070  5.914   25.890  1.00 7.65  ? 196 GLY A O   1 
ATOM   1596 N  N   . SER A 1 196 ? 17.380  3.995   24.691  1.00 7.08  ? 197 SER A N   1 
ATOM   1597 C  CA  . SER A 1 196 ? 18.161  4.675   23.620  1.00 7.07  ? 197 SER A CA  1 
ATOM   1598 C  C   . SER A 1 196 ? 17.717  4.291   22.206  1.00 6.44  ? 197 SER A C   1 
ATOM   1599 O  O   . SER A 1 196 ? 16.959  3.275   22.046  1.00 6.83  ? 197 SER A O   1 
ATOM   1600 C  CB  . SER A 1 196 ? 19.690  4.270   23.683  1.00 7.52  ? 197 SER A CB  1 
ATOM   1601 O  OG  . SER A 1 196 ? 19.897  2.861   23.349  1.00 6.59  ? 197 SER A OG  1 
ATOM   1602 N  N   . LEU A 1 197 ? 18.313  4.947   21.216  1.00 7.39  ? 198 LEU A N   1 
ATOM   1603 C  CA  . LEU A 1 197 ? 18.222  4.411   19.821  1.00 7.95  ? 198 LEU A CA  1 
ATOM   1604 C  C   . LEU A 1 197 ? 19.000  3.131   19.854  1.00 7.69  ? 198 LEU A C   1 
ATOM   1605 O  O   . LEU A 1 197 ? 20.019  2.958   20.601  1.00 7.26  ? 198 LEU A O   1 
ATOM   1606 C  CB  . LEU A 1 197 ? 18.876  5.395   18.848  1.00 10.47 ? 198 LEU A CB  1 
ATOM   1607 C  CG  . LEU A 1 197 ? 18.420  6.815   18.827  1.00 12.01 ? 198 LEU A CG  1 
ATOM   1608 C  CD1 . LEU A 1 197 ? 19.258  7.789   17.994  1.00 13.76 ? 198 LEU A CD1 1 
ATOM   1609 C  CD2 . LEU A 1 197 ? 16.996  6.861   18.423  1.00 16.70 ? 198 LEU A CD2 1 
ATOM   1610 N  N   . THR A 1 198 ? 18.574  2.136   19.099  1.00 6.99  ? 199 THR A N   1 
ATOM   1611 C  CA  . THR A 1 198 ? 19.241  0.854   19.052  1.00 8.05  ? 199 THR A CA  1 
ATOM   1612 C  C   . THR A 1 198 ? 20.225  0.776   17.866  1.00 9.05  ? 199 THR A C   1 
ATOM   1613 O  O   . THR A 1 198 ? 20.857  -0.273  17.729  1.00 9.50  ? 199 THR A O   1 
ATOM   1614 C  CB  . THR A 1 198 ? 18.222  -0.283  18.922  1.00 7.09  ? 199 THR A CB  1 
ATOM   1615 O  OG1 . THR A 1 198 ? 17.577  -0.217  17.614  1.00 7.02  ? 199 THR A OG1 1 
ATOM   1616 C  CG2 . THR A 1 198 ? 17.243  -0.365  20.125  1.00 7.62  ? 199 THR A CG2 1 
ATOM   1617 N  N   . THR A 1 199 ? 20.365  1.845   17.058  1.00 10.13 ? 200 THR A N   1 
ATOM   1618 C  CA  . THR A 1 199 ? 21.495  1.932   16.042  1.00 11.09 ? 200 THR A CA  1 
ATOM   1619 C  C   . THR A 1 199 ? 22.288  3.163   16.384  1.00 10.31 ? 200 THR A C   1 
ATOM   1620 O  O   . THR A 1 199 ? 21.793  4.103   16.974  1.00 10.89 ? 200 THR A O   1 
ATOM   1621 C  CB  . THR A 1 199 ? 20.982  2.110   14.580  1.00 13.39 ? 200 THR A CB  1 
ATOM   1622 O  OG1 . THR A 1 199 ? 20.121  3.214   14.491  1.00 18.53 ? 200 THR A OG1 1 
ATOM   1623 C  CG2 . THR A 1 199 ? 20.081  0.903   14.211  1.00 13.47 ? 200 THR A CG2 1 
ATOM   1624 N  N   . PRO A 1 200 ? 23.544  3.183   15.931  1.00 11.16 ? 201 PRO A N   1 
ATOM   1625 C  CA  . PRO A 1 200 ? 24.291  4.432   16.079  1.00 11.14 ? 201 PRO A CA  1 
ATOM   1626 C  C   . PRO A 1 200 ? 23.438  5.554   15.536  1.00 10.48 ? 201 PRO A C   1 
ATOM   1627 O  O   . PRO A 1 200 ? 22.819  5.467   14.433  1.00 12.09 ? 201 PRO A O   1 
ATOM   1628 C  CB  . PRO A 1 200 ? 25.515  4.132   15.141  1.00 10.67 ? 201 PRO A CB  1 
ATOM   1629 C  CG  . PRO A 1 200 ? 25.747  2.708   15.347  1.00 10.87 ? 201 PRO A CG  1 
ATOM   1630 C  CD  . PRO A 1 200 ? 24.302  2.139   15.222  1.00 12.34 ? 201 PRO A CD  1 
ATOM   1631 N  N   . PRO A 1 201 ? 23.439  6.722   16.195  1.00 9.75  ? 202 PRO A N   1 
ATOM   1632 C  CA  . PRO A 1 201 ? 24.376  7.148   17.251  1.00 10.69 ? 202 PRO A CA  1 
ATOM   1633 C  C   . PRO A 1 201 ? 24.062  6.699   18.707  1.00 9.77  ? 202 PRO A C   1 
ATOM   1634 O  O   . PRO A 1 201 ? 24.661  7.124   19.695  1.00 11.34 ? 202 PRO A O   1 
ATOM   1635 C  CB  . PRO A 1 201 ? 24.314  8.678   17.164  1.00 10.32 ? 202 PRO A CB  1 
ATOM   1636 C  CG  . PRO A 1 201 ? 22.972  9.000   16.611  1.00 11.80 ? 202 PRO A CG  1 
ATOM   1637 C  CD  . PRO A 1 201 ? 22.679  7.855   15.624  1.00 10.00 ? 202 PRO A CD  1 
ATOM   1638 N  N   . LEU A 1 202 ? 23.095  5.784   18.886  1.00 8.73  ? 203 LEU A N   1 
ATOM   1639 C  CA  . LEU A 1 202 ? 22.797  5.187   20.155  1.00 8.07  ? 203 LEU A CA  1 
ATOM   1640 C  C   . LEU A 1 202 ? 22.406  6.199   21.248  1.00 7.61  ? 203 LEU A C   1 
ATOM   1641 O  O   . LEU A 1 202 ? 22.548  5.930   22.386  1.00 8.82  ? 203 LEU A O   1 
ATOM   1642 C  CB  . LEU A 1 202 ? 23.918  4.250   20.648  1.00 8.96  ? 203 LEU A CB  1 
ATOM   1643 C  CG  . LEU A 1 202 ? 24.253  3.143   19.571  1.00 8.34  ? 203 LEU A CG  1 
ATOM   1644 C  CD1 . LEU A 1 202 ? 25.536  2.509   20.102  1.00 12.30 ? 203 LEU A CD1 1 
ATOM   1645 C  CD2 . LEU A 1 202 ? 23.205  2.027   19.546  1.00 9.51  ? 203 LEU A CD2 1 
ATOM   1646 N  N   . LEU A 1 203 ? 21.798  7.321   20.815  1.00 7.61  ? 204 LEU A N   1 
ATOM   1647 C  CA  . LEU A 1 203 ? 21.586  8.414   21.792  1.00 8.10  ? 204 LEU A CA  1 
ATOM   1648 C  C   . LEU A 1 203 ? 20.490  8.046   22.801  1.00 8.11  ? 204 LEU A C   1 
ATOM   1649 O  O   . LEU A 1 203 ? 19.509  7.303   22.489  1.00 8.15  ? 204 LEU A O   1 
ATOM   1650 C  CB  . LEU A 1 203 ? 21.153  9.646   21.043  1.00 9.28  ? 204 LEU A CB  1 
ATOM   1651 C  CG  . LEU A 1 203 ? 22.226  10.238  20.082  1.00 10.87 ? 204 LEU A CG  1 
ATOM   1652 C  CD1 . LEU A 1 203 ? 21.635  11.366  19.206  1.00 12.50 ? 204 LEU A CD1 1 
ATOM   1653 C  CD2 . LEU A 1 203 ? 23.347  10.860  20.960  1.00 14.54 ? 204 LEU A CD2 1 
ATOM   1654 N  N   . GLU A 1 204 ? 20.666  8.445   24.022  1.00 9.58  ? 205 GLU A N   1 
ATOM   1655 C  CA  . GLU A 1 204 ? 19.865  8.100   25.182  1.00 9.21  ? 205 GLU A CA  1 
ATOM   1656 C  C   . GLU A 1 204 ? 18.657  9.049   25.300  1.00 10.18 ? 205 GLU A C   1 
ATOM   1657 O  O   . GLU A 1 204 ? 18.549  9.833   26.251  1.00 11.37 ? 205 GLU A O   1 
ATOM   1658 C  CB  . GLU A 1 204 ? 20.711  7.947   26.491  1.00 10.72 ? 205 GLU A CB  1 
ATOM   1659 C  CG  . GLU A 1 204 ? 21.581  6.696   26.339  1.00 11.23 ? 205 GLU A CG  1 
ATOM   1660 C  CD  . GLU A 1 204 ? 22.591  6.453   27.427  1.00 12.19 ? 205 GLU A CD  1 
ATOM   1661 O  OE1 . GLU A 1 204 ? 22.918  7.431   28.126  1.00 14.17 ? 205 GLU A OE1 1 
ATOM   1662 O  OE2 . GLU A 1 204 ? 22.979  5.294   27.611  1.00 12.12 ? 205 GLU A OE2 1 
ATOM   1663 N  N   . CYS A 1 205 ? 17.764  8.958   24.317  1.00 9.15  ? 206 CYS A N   1 
ATOM   1664 C  CA  . CYS A 1 205 ? 16.697  9.973   24.132  1.00 7.57  ? 206 CYS A CA  1 
ATOM   1665 C  C   . CYS A 1 205 ? 15.331  9.338   24.018  1.00 7.39  ? 206 CYS A C   1 
ATOM   1666 O  O   . CYS A 1 205 ? 14.381  10.075  23.685  1.00 8.27  ? 206 CYS A O   1 
ATOM   1667 C  CB  . CYS A 1 205 ? 16.954  10.834  22.886  1.00 8.20  ? 206 CYS A CB  1 
ATOM   1668 S  SG  . CYS A 1 205 ? 17.044  9.825   21.340  1.00 9.49  ? 206 CYS A SG  1 
ATOM   1669 N  N   . VAL A 1 206 ? 15.190  8.049   24.311  1.00 7.42  ? 207 VAL A N   1 
ATOM   1670 C  CA  . VAL A 1 206 ? 13.954  7.313   23.955  1.00 6.63  ? 207 VAL A CA  1 
ATOM   1671 C  C   . VAL A 1 206 ? 13.177  6.881   25.183  1.00 7.12  ? 207 VAL A C   1 
ATOM   1672 O  O   . VAL A 1 206 ? 13.728  6.238   26.065  1.00 7.65  ? 207 VAL A O   1 
ATOM   1673 C  CB  . VAL A 1 206 ? 14.257  6.021   23.160  1.00 6.39  ? 207 VAL A CB  1 
ATOM   1674 C  CG1 . VAL A 1 206 ? 12.933  5.330   22.795  1.00 5.89  ? 207 VAL A CG1 1 
ATOM   1675 C  CG2 . VAL A 1 206 ? 14.988  6.336   21.822  1.00 6.81  ? 207 VAL A CG2 1 
ATOM   1676 N  N   . THR A 1 207 ? 11.872  7.158   25.244  1.00 6.91  ? 208 THR A N   1 
ATOM   1677 C  CA  . THR A 1 207 ? 10.944  6.488   26.103  1.00 7.19  ? 208 THR A CA  1 
ATOM   1678 C  C   . THR A 1 207 ? 10.405  5.347   25.287  1.00 6.47  ? 208 THR A C   1 
ATOM   1679 O  O   . THR A 1 207 ? 9.724   5.521   24.236  1.00 7.60  ? 208 THR A O   1 
ATOM   1680 C  CB  . THR A 1 207 ? 9.772   7.414   26.518  1.00 8.10  ? 208 THR A CB  1 
ATOM   1681 O  OG1 . THR A 1 207 ? 10.308  8.486   27.330  1.00 8.00  ? 208 THR A OG1 1 
ATOM   1682 C  CG2 . THR A 1 207 ? 8.813   6.659   27.397  1.00 7.84  ? 208 THR A CG2 1 
ATOM   1683 N  N   . TRP A 1 208 ? 10.783  4.139   25.682  1.00 6.91  ? 209 TRP A N   1 
ATOM   1684 C  CA  . TRP A 1 208 ? 10.326  2.935   24.963  1.00 6.74  ? 209 TRP A CA  1 
ATOM   1685 C  C   . TRP A 1 208 ? 8.965   2.522   25.458  1.00 6.90  ? 209 TRP A C   1 
ATOM   1686 O  O   . TRP A 1 208 ? 8.758   2.439   26.690  1.00 7.53  ? 209 TRP A O   1 
ATOM   1687 C  CB  . TRP A 1 208 ? 11.361  1.740   25.232  1.00 7.20  ? 209 TRP A CB  1 
ATOM   1688 C  CG  . TRP A 1 208 ? 12.495  1.827   24.245  1.00 6.51  ? 209 TRP A CG  1 
ATOM   1689 C  CD1 . TRP A 1 208 ? 13.754  2.421   24.411  1.00 6.71  ? 209 TRP A CD1 1 
ATOM   1690 C  CD2 . TRP A 1 208 ? 12.407  1.439   22.862  1.00 6.89  ? 209 TRP A CD2 1 
ATOM   1691 N  NE1 . TRP A 1 208 ? 14.426  2.417   23.223  1.00 6.54  ? 209 TRP A NE1 1 
ATOM   1692 C  CE2 . TRP A 1 208 ? 13.696  1.768   22.253  1.00 6.38  ? 209 TRP A CE2 1 
ATOM   1693 C  CE3 . TRP A 1 208 ? 11.425  0.776   22.075  1.00 6.17  ? 209 TRP A CE3 1 
ATOM   1694 C  CZ2 . TRP A 1 208 ? 13.975  1.581   20.917  1.00 5.87  ? 209 TRP A CZ2 1 
ATOM   1695 C  CZ3 . TRP A 1 208 ? 11.732  0.522   20.742  1.00 5.95  ? 209 TRP A CZ3 1 
ATOM   1696 C  CH2 . TRP A 1 208 ? 12.994  0.900   20.152  1.00 5.66  ? 209 TRP A CH2 1 
ATOM   1697 N  N   . ILE A 1 209 ? 8.101   2.149   24.516  1.00 6.72  ? 210 ILE A N   1 
ATOM   1698 C  CA  . ILE A 1 209 ? 6.760   1.625   24.875  1.00 6.49  ? 210 ILE A CA  1 
ATOM   1699 C  C   . ILE A 1 209 ? 6.653   0.352   24.025  1.00 7.39  ? 210 ILE A C   1 
ATOM   1700 O  O   . ILE A 1 209 ? 6.573   0.448   22.804  1.00 7.30  ? 210 ILE A O   1 
ATOM   1701 C  CB  . ILE A 1 209 ? 5.675   2.695   24.511  1.00 7.41  ? 210 ILE A CB  1 
ATOM   1702 C  CG1 . ILE A 1 209 ? 5.909   3.973   25.281  1.00 8.40  ? 210 ILE A CG1 1 
ATOM   1703 C  CG2 . ILE A 1 209 ? 4.253   2.072   24.748  1.00 7.82  ? 210 ILE A CG2 1 
ATOM   1704 C  CD1 . ILE A 1 209 ? 5.057   5.164   24.830  1.00 9.55  ? 210 ILE A CD1 1 
ATOM   1705 N  N   . VAL A 1 210 ? 6.706   -0.810  24.647  1.00 7.21  ? 211 VAL A N   1 
ATOM   1706 C  CA  . VAL A 1 210 ? 6.727   -2.134  23.931  1.00 6.70  ? 211 VAL A CA  1 
ATOM   1707 C  C   . VAL A 1 210 ? 5.397   -2.827  24.194  1.00 7.70  ? 211 VAL A C   1 
ATOM   1708 O  O   . VAL A 1 210 ? 5.051   -3.023  25.362  1.00 8.25  ? 211 VAL A O   1 
ATOM   1709 C  CB  . VAL A 1 210 ? 7.934   -2.953  24.396  1.00 6.64  ? 211 VAL A CB  1 
ATOM   1710 C  CG1 . VAL A 1 210 ? 7.938   -4.321  23.707  1.00 6.25  ? 211 VAL A CG1 1 
ATOM   1711 C  CG2 . VAL A 1 210 ? 9.252   -2.208  24.066  1.00 6.71  ? 211 VAL A CG2 1 
ATOM   1712 N  N   . LEU A 1 211 ? 4.636   -3.116  23.141  1.00 7.93  ? 212 LEU A N   1 
ATOM   1713 C  CA  . LEU A 1 211 ? 3.305   -3.773  23.301  1.00 8.45  ? 212 LEU A CA  1 
ATOM   1714 C  C   . LEU A 1 211 ? 3.512   -5.203  23.726  1.00 8.10  ? 212 LEU A C   1 
ATOM   1715 O  O   . LEU A 1 211 ? 4.359   -5.929  23.209  1.00 8.73  ? 212 LEU A O   1 
ATOM   1716 C  CB  . LEU A 1 211 ? 2.560   -3.686  21.951  1.00 8.18  ? 212 LEU A CB  1 
ATOM   1717 C  CG  . LEU A 1 211 ? 2.161   -2.232  21.568  1.00 9.05  ? 212 LEU A CG  1 
ATOM   1718 C  CD1 . LEU A 1 211 ? 1.028   -2.329  20.450  1.00 10.31 ? 212 LEU A CD1 1 
ATOM   1719 C  CD2 . LEU A 1 211 ? 1.649   -1.382  22.788  1.00 9.20  ? 212 LEU A CD2 1 
ATOM   1720 N  N   . LYS A 1 212 ? 2.656   -5.653  24.686  1.00 9.19  ? 213 LYS A N   1 
ATOM   1721 C  CA  . LYS A 1 212 ? 2.717   -7.070  25.076  1.00 10.43 ? 213 LYS A CA  1 
ATOM   1722 C  C   . LYS A 1 212 ? 2.254   -8.037  24.011  1.00 9.83  ? 213 LYS A C   1 
ATOM   1723 O  O   . LYS A 1 212 ? 2.759   -9.146  23.882  1.00 11.16 ? 213 LYS A O   1 
ATOM   1724 C  CB  . LYS A 1 212 ? 1.877   -7.180  26.359  1.00 14.37 ? 213 LYS A CB  1 
ATOM   1725 C  CG  . LYS A 1 212 ? 1.295   -8.564  26.780  1.00 20.70 ? 213 LYS A CG  1 
ATOM   1726 C  CD  . LYS A 1 212 ? 0.048   -8.431  27.698  1.00 25.73 ? 213 LYS A CD  1 
ATOM   1727 C  CE  . LYS A 1 212 ? -1.325  -8.208  27.043  1.00 26.50 ? 213 LYS A CE  1 
ATOM   1728 N  NZ  . LYS A 1 212 ? -1.435  -7.732  25.604  1.00 28.97 ? 213 LYS A NZ  1 
ATOM   1729 N  N   . GLU A 1 213 ? 1.280   -7.614  23.189  1.00 8.35  ? 214 GLU A N   1 
ATOM   1730 C  CA  . GLU A 1 213 ? 0.749   -8.563  22.234  1.00 8.93  ? 214 GLU A CA  1 
ATOM   1731 C  C   . GLU A 1 213 ? 1.474   -8.431  20.885  1.00 8.41  ? 214 GLU A C   1 
ATOM   1732 O  O   . GLU A 1 213 ? 1.483   -7.338  20.305  1.00 8.12  ? 214 GLU A O   1 
ATOM   1733 C  CB  . GLU A 1 213 ? -0.749  -8.240  21.979  1.00 10.66 ? 214 GLU A CB  1 
ATOM   1734 C  CG  . GLU A 1 213 ? -1.451  -9.170  20.960  1.00 11.06 ? 214 GLU A CG  1 
ATOM   1735 C  CD  . GLU A 1 213 ? -2.994  -8.917  20.730  1.00 14.73 ? 214 GLU A CD  1 
ATOM   1736 O  OE1 . GLU A 1 213 ? -3.594  -8.087  21.367  1.00 14.17 ? 214 GLU A OE1 1 
ATOM   1737 O  OE2 . GLU A 1 213 ? -3.550  -9.761  19.961  1.00 22.68 ? 214 GLU A OE2 1 
ATOM   1738 N  N   . PRO A 1 214 ? 2.010   -9.532  20.366  1.00 8.76  ? 215 PRO A N   1 
ATOM   1739 C  CA  . PRO A 1 214 ? 2.628   -9.519  19.054  1.00 9.57  ? 215 PRO A CA  1 
ATOM   1740 C  C   . PRO A 1 214 ? 1.597   -9.504  17.948  1.00 10.86 ? 215 PRO A C   1 
ATOM   1741 O  O   . PRO A 1 214 ? 0.397   -9.888  18.177  1.00 11.54 ? 215 PRO A O   1 
ATOM   1742 C  CB  . PRO A 1 214 ? 3.475   -10.839 18.984  1.00 10.30 ? 215 PRO A CB  1 
ATOM   1743 C  CG  . PRO A 1 214 ? 3.232   -11.483 20.312  1.00 15.18 ? 215 PRO A CG  1 
ATOM   1744 C  CD  . PRO A 1 214 ? 2.068   -10.851 21.026  1.00 10.22 ? 215 PRO A CD  1 
ATOM   1745 N  N   . ILE A 1 215 ? 2.009   -9.042  16.767  1.00 9.39  ? 216 ILE A N   1 
ATOM   1746 C  CA  . ILE A 1 215 ? 1.170   -9.286  15.568  1.00 9.96  ? 216 ILE A CA  1 
ATOM   1747 C  C   . ILE A 1 215 ? 1.720   -10.525 14.888  1.00 10.19 ? 216 ILE A C   1 
ATOM   1748 O  O   . ILE A 1 215 ? 2.892   -10.899 15.108  1.00 10.54 ? 216 ILE A O   1 
ATOM   1749 C  CB  . ILE A 1 215 ? 1.159   -8.063  14.581  1.00 10.83 ? 216 ILE A CB  1 
ATOM   1750 C  CG1 . ILE A 1 215 ? 2.589   -7.702  14.094  1.00 10.65 ? 216 ILE A CG1 1 
ATOM   1751 C  CG2 . ILE A 1 215 ? 0.481   -6.833  15.286  1.00 12.18 ? 216 ILE A CG2 1 
ATOM   1752 C  CD1 . ILE A 1 215 ? 2.538   -6.686  12.881  1.00 10.26 ? 216 ILE A CD1 1 
ATOM   1753 N  N   A SER A 1 216 ? 0.874   -11.251 14.142  0.50 10.96 ? 217 SER A N   1 
ATOM   1754 N  N   B SER A 1 216 ? 0.884   -11.185 14.090  0.50 10.74 ? 217 SER A N   1 
ATOM   1755 C  CA  A SER A 1 216 ? 1.322   -12.400 13.320  0.50 10.49 ? 217 SER A CA  1 
ATOM   1756 C  CA  B SER A 1 216 ? 1.368   -12.265 13.262  0.50 10.05 ? 217 SER A CA  1 
ATOM   1757 C  C   A SER A 1 216 ? 1.464   -11.983 11.897  0.50 10.13 ? 217 SER A C   1 
ATOM   1758 C  C   B SER A 1 216 ? 1.506   -11.863 11.844  0.50 9.90  ? 217 SER A C   1 
ATOM   1759 O  O   A SER A 1 216 ? 0.525   -11.349 11.357  0.50 10.94 ? 217 SER A O   1 
ATOM   1760 O  O   B SER A 1 216 ? 0.669   -11.094 11.263  0.50 10.61 ? 217 SER A O   1 
ATOM   1761 C  CB  A SER A 1 216 ? 0.352   -13.567 13.362  0.50 13.28 ? 217 SER A CB  1 
ATOM   1762 C  CB  B SER A 1 216 ? 0.530   -13.494 13.383  0.50 11.95 ? 217 SER A CB  1 
ATOM   1763 O  OG  A SER A 1 216 ? 0.279   -14.146 14.659  0.50 14.59 ? 217 SER A OG  1 
ATOM   1764 O  OG  B SER A 1 216 ? -0.795  -13.171 13.028  0.50 12.89 ? 217 SER A OG  1 
ATOM   1765 N  N   . VAL A 1 217 ? 2.590   -12.355 11.283  1.00 9.42  ? 218 VAL A N   1 
ATOM   1766 C  CA  . VAL A 1 217 ? 2.826   -12.136 9.865   1.00 10.09 ? 218 VAL A CA  1 
ATOM   1767 C  C   . VAL A 1 217 ? 3.068   -13.518 9.188   1.00 9.24  ? 218 VAL A C   1 
ATOM   1768 O  O   . VAL A 1 217 ? 3.431   -14.504 9.926   1.00 9.64  ? 218 VAL A O   1 
ATOM   1769 C  CB  . VAL A 1 217 ? 4.030   -11.198 9.618   1.00 9.84  ? 218 VAL A CB  1 
ATOM   1770 C  CG1 . VAL A 1 217 ? 3.768   -9.823  10.237  1.00 12.05 ? 218 VAL A CG1 1 
ATOM   1771 C  CG2 . VAL A 1 217 ? 5.359   -11.811 10.060  1.00 10.99 ? 218 VAL A CG2 1 
ATOM   1772 N  N   . SER A 1 218 ? 2.873   -13.675 7.884   1.00 9.59  ? 219 SER A N   1 
ATOM   1773 C  CA  . SER A 1 218 ? 3.157   -14.990 7.321   1.00 10.59 ? 219 SER A CA  1 
ATOM   1774 C  C   . SER A 1 218 ? 4.622   -15.224 7.044   1.00 10.58 ? 219 SER A C   1 
ATOM   1775 O  O   . SER A 1 218 ? 5.462   -14.296 6.971   1.00 9.43  ? 219 SER A O   1 
ATOM   1776 C  CB  . SER A 1 218 ? 2.336   -15.159 6.070   1.00 10.97 ? 219 SER A CB  1 
ATOM   1777 O  OG  . SER A 1 218 ? 2.807   -14.277 5.038   1.00 11.65 ? 219 SER A OG  1 
ATOM   1778 N  N   A SER A 1 219 ? 4.975   -16.496 6.864   0.50 10.76 ? 220 SER A N   1 
ATOM   1779 N  N   B SER A 1 219 ? 4.946   -16.501 6.855   0.50 11.78 ? 220 SER A N   1 
ATOM   1780 C  CA  A SER A 1 219 ? 6.323   -16.823 6.499   0.50 11.09 ? 220 SER A CA  1 
ATOM   1781 C  CA  B SER A 1 219 ? 6.278   -16.852 6.497   0.50 12.79 ? 220 SER A CA  1 
ATOM   1782 C  C   A SER A 1 219 ? 6.689   -16.159 5.142   0.50 12.55 ? 220 SER A C   1 
ATOM   1783 C  C   B SER A 1 219 ? 6.671   -16.171 5.171   0.50 13.66 ? 220 SER A C   1 
ATOM   1784 O  O   A SER A 1 219 ? 7.803   -15.715 4.950   0.50 12.78 ? 220 SER A O   1 
ATOM   1785 O  O   B SER A 1 219 ? 7.792   -15.729 5.043   0.50 13.64 ? 220 SER A O   1 
ATOM   1786 C  CB  A SER A 1 219 ? 6.446   -18.363 6.454   0.50 11.24 ? 220 SER A CB  1 
ATOM   1787 C  CB  B SER A 1 219 ? 6.401   -18.387 6.426   0.50 14.65 ? 220 SER A CB  1 
ATOM   1788 O  OG  A SER A 1 219 ? 5.440   -18.894 5.613   0.50 10.02 ? 220 SER A OG  1 
ATOM   1789 O  OG  B SER A 1 219 ? 7.762   -18.757 6.387   0.50 17.55 ? 220 SER A OG  1 
ATOM   1790 N  N   . GLU A 1 220 ? 5.736   -16.042 4.218   1.00 12.33 ? 221 GLU A N   1 
ATOM   1791 C  CA  . GLU A 1 220 ? 6.070   -15.436 2.908   1.00 13.67 ? 221 GLU A CA  1 
ATOM   1792 C  C   . GLU A 1 220 ? 6.355   -13.903 3.106   1.00 12.40 ? 221 GLU A C   1 
ATOM   1793 O  O   . GLU A 1 220 ? 7.202   -13.354 2.425   1.00 12.99 ? 221 GLU A O   1 
ATOM   1794 C  CB  . GLU A 1 220 ? 4.955   -15.596 1.922   1.00 18.17 ? 221 GLU A CB  1 
ATOM   1795 C  CG  . GLU A 1 220 ? 4.722   -17.063 1.535   1.00 20.61 ? 221 GLU A CG  1 
ATOM   1796 C  CD  . GLU A 1 220 ? 3.543   -17.681 2.266   1.00 23.59 ? 221 GLU A CD  1 
ATOM   1797 O  OE1 . GLU A 1 220 ? 3.160   -17.282 3.383   1.00 21.05 ? 221 GLU A OE1 1 
ATOM   1798 O  OE2 . GLU A 1 220 ? 2.940   -18.664 1.730   1.00 30.81 ? 221 GLU A OE2 1 
ATOM   1799 N  N   . GLN A 1 221 ? 5.630   -13.252 4.048   1.00 11.78 ? 222 GLN A N   1 
ATOM   1800 C  CA  . GLN A 1 221 ? 5.860   -11.788 4.290   1.00 10.42 ? 222 GLN A CA  1 
ATOM   1801 C  C   . GLN A 1 221 ? 7.282   -11.605 4.836   1.00 11.39 ? 222 GLN A C   1 
ATOM   1802 O  O   . GLN A 1 221 ? 8.034   -10.747 4.318   1.00 10.77 ? 222 GLN A O   1 
ATOM   1803 C  CB  . GLN A 1 221 ? 4.806   -11.288 5.251   1.00 9.65  ? 222 GLN A CB  1 
ATOM   1804 C  CG  . GLN A 1 221 ? 3.447   -11.194 4.544   1.00 9.99  ? 222 GLN A CG  1 
ATOM   1805 C  CD  . GLN A 1 221 ? 2.317   -10.630 5.389   1.00 9.82  ? 222 GLN A CD  1 
ATOM   1806 O  OE1 . GLN A 1 221 ? 2.165   -10.989 6.567   1.00 10.20 ? 222 GLN A OE1 1 
ATOM   1807 N  NE2 . GLN A 1 221 ? 1.494   -9.736  4.818   1.00 10.81 ? 222 GLN A NE2 1 
ATOM   1808 N  N   . VAL A 1 222 ? 7.684   -12.391 5.848   1.00 12.18 ? 223 VAL A N   1 
ATOM   1809 C  CA  . VAL A 1 222 ? 9.021   -12.199 6.397   1.00 12.37 ? 223 VAL A CA  1 
ATOM   1810 C  C   . VAL A 1 222 ? 10.136  -12.658 5.415   1.00 13.88 ? 223 VAL A C   1 
ATOM   1811 O  O   . VAL A 1 222 ? 11.229  -12.081 5.344   1.00 13.46 ? 223 VAL A O   1 
ATOM   1812 C  CB  . VAL A 1 222 ? 9.144   -12.820 7.841   1.00 14.30 ? 223 VAL A CB  1 
ATOM   1813 C  CG1 . VAL A 1 222 ? 9.118   -14.321 7.770   1.00 17.67 ? 223 VAL A CG1 1 
ATOM   1814 C  CG2 . VAL A 1 222 ? 10.450  -12.287 8.510   1.00 15.82 ? 223 VAL A CG2 1 
ATOM   1815 N  N   . LEU A 1 223 ? 9.798   -13.663 4.589   1.00 14.30 ? 224 LEU A N   1 
ATOM   1816 C  CA  . LEU A 1 223 ? 10.770  -14.063 3.576   1.00 15.35 ? 224 LEU A CA  1 
ATOM   1817 C  C   . LEU A 1 223 ? 11.049  -12.933 2.657   1.00 15.98 ? 224 LEU A C   1 
ATOM   1818 O  O   . LEU A 1 223 ? 12.183  -12.824 2.208   1.00 17.47 ? 224 LEU A O   1 
ATOM   1819 C  CB  . LEU A 1 223 ? 10.280  -15.332 2.793   1.00 17.85 ? 224 LEU A CB  1 
ATOM   1820 C  CG  . LEU A 1 223 ? 10.593  -16.660 3.515   1.00 22.23 ? 224 LEU A CG  1 
ATOM   1821 C  CD1 . LEU A 1 223 ? 9.687   -17.833 3.009   1.00 23.62 ? 224 LEU A CD1 1 
ATOM   1822 C  CD2 . LEU A 1 223 ? 12.087  -17.014 3.382   1.00 24.39 ? 224 LEU A CD2 1 
ATOM   1823 N  N   . LYS A 1 224 ? 10.045  -12.126 2.335   1.00 14.25 ? 225 LYS A N   1 
ATOM   1824 C  CA  . LYS A 1 224 ? 10.321  -10.978 1.437   1.00 15.29 ? 225 LYS A CA  1 
ATOM   1825 C  C   . LYS A 1 224 ? 11.267  -9.925  2.094   1.00 14.48 ? 225 LYS A C   1 
ATOM   1826 O  O   . LYS A 1 224 ? 12.111  -9.372  1.429   1.00 14.36 ? 225 LYS A O   1 
ATOM   1827 C  CB  . LYS A 1 224 ? 9.051   -10.330 0.880   1.00 16.85 ? 225 LYS A CB  1 
ATOM   1828 C  CG  . LYS A 1 224 ? 8.094   -11.382 0.308   1.00 25.69 ? 225 LYS A CG  1 
ATOM   1829 C  CD  . LYS A 1 224 ? 8.152   -11.637 -1.145  1.00 31.16 ? 225 LYS A CD  1 
ATOM   1830 C  CE  . LYS A 1 224 ? 6.840   -11.226 -1.805  1.00 39.89 ? 225 LYS A CE  1 
ATOM   1831 N  NZ  . LYS A 1 224 ? 7.098   -10.419 -3.046  1.00 33.54 ? 225 LYS A NZ  1 
ATOM   1832 N  N   . PHE A 1 225 ? 11.156  -9.703  3.417   1.00 11.71 ? 226 PHE A N   1 
ATOM   1833 C  CA  . PHE A 1 225 ? 12.112  -8.795  4.066   1.00 10.83 ? 226 PHE A CA  1 
ATOM   1834 C  C   . PHE A 1 225 ? 13.575  -9.296  3.856   1.00 12.05 ? 226 PHE A C   1 
ATOM   1835 O  O   . PHE A 1 225 ? 14.501  -8.484  3.671   1.00 12.46 ? 226 PHE A O   1 
ATOM   1836 C  CB  . PHE A 1 225 ? 11.962  -8.786  5.658   1.00 10.87 ? 226 PHE A CB  1 
ATOM   1837 C  CG  . PHE A 1 225 ? 10.737  -8.092  6.221   1.00 11.73 ? 226 PHE A CG  1 
ATOM   1838 C  CD1 . PHE A 1 225 ? 9.680   -7.651  5.440   1.00 11.72 ? 226 PHE A CD1 1 
ATOM   1839 C  CD2 . PHE A 1 225 ? 10.658  -7.909  7.597   1.00 11.95 ? 226 PHE A CD2 1 
ATOM   1840 C  CE1 . PHE A 1 225 ? 8.582   -7.031  6.033   1.00 13.09 ? 226 PHE A CE1 1 
ATOM   1841 C  CE2 . PHE A 1 225 ? 9.573   -7.297  8.188   1.00 13.30 ? 226 PHE A CE2 1 
ATOM   1842 C  CZ  . PHE A 1 225 ? 8.528   -6.856  7.405   1.00 12.90 ? 226 PHE A CZ  1 
ATOM   1843 N  N   . ARG A 1 226 ? 13.772  -10.618 3.934   1.00 11.04 ? 227 ARG A N   1 
ATOM   1844 C  CA  . ARG A 1 226 ? 15.112  -11.235 3.816   1.00 11.78 ? 227 ARG A CA  1 
ATOM   1845 C  C   . ARG A 1 226 ? 15.630  -11.253 2.375   1.00 12.53 ? 227 ARG A C   1 
ATOM   1846 O  O   . ARG A 1 226 ? 16.764  -11.624 2.224   1.00 15.40 ? 227 ARG A O   1 
ATOM   1847 C  CB  . ARG A 1 226 ? 15.150  -12.694 4.326   1.00 11.97 ? 227 ARG A CB  1 
ATOM   1848 C  CG  . ARG A 1 226 ? 14.624  -12.925 5.775   1.00 12.41 ? 227 ARG A CG  1 
ATOM   1849 C  CD  . ARG A 1 226 ? 14.691  -14.387 6.230   1.00 12.85 ? 227 ARG A CD  1 
ATOM   1850 N  NE  . ARG A 1 226 ? 14.147  -14.501 7.576   1.00 12.73 ? 227 ARG A NE  1 
ATOM   1851 C  CZ  . ARG A 1 226 ? 13.152  -15.300 7.954   1.00 12.90 ? 227 ARG A CZ  1 
ATOM   1852 N  NH1 . ARG A 1 226 ? 12.691  -16.263 7.107   1.00 13.06 ? 227 ARG A NH1 1 
ATOM   1853 N  NH2 . ARG A 1 226 ? 12.712  -15.289 9.199   1.00 12.08 ? 227 ARG A NH2 1 
ATOM   1854 N  N   . LYS A 1 227 ? 14.882  -10.760 1.405   1.00 14.15 ? 228 LYS A N   1 
ATOM   1855 C  CA  . LYS A 1 227 ? 15.429  -10.630 0.036   1.00 15.20 ? 228 LYS A CA  1 
ATOM   1856 C  C   . LYS A 1 227 ? 16.059  -9.290  -0.235  1.00 17.04 ? 228 LYS A C   1 
ATOM   1857 O  O   . LYS A 1 227 ? 16.745  -9.059  -1.236  1.00 17.21 ? 228 LYS A O   1 
ATOM   1858 C  CB  . LYS A 1 227 ? 14.326  -10.986 -0.975  1.00 15.55 ? 228 LYS A CB  1 
ATOM   1859 C  CG  . LYS A 1 227 ? 14.032  -12.495 -0.990  1.00 18.62 ? 228 LYS A CG  1 
ATOM   1860 C  CD  . LYS A 1 227 ? 12.825  -12.830 -1.832  1.00 24.71 ? 228 LYS A CD  1 
ATOM   1861 C  CE  . LYS A 1 227 ? 12.923  -12.330 -3.277  1.00 32.58 ? 228 LYS A CE  1 
ATOM   1862 N  NZ  . LYS A 1 227 ? 13.146  -13.337 -4.364  1.00 36.11 ? 228 LYS A NZ  1 
ATOM   1863 N  N   . LEU A 1 228 ? 15.903  -8.367  0.725   1.00 13.88 ? 229 LEU A N   1 
ATOM   1864 C  CA  . LEU A 1 228 ? 16.627  -7.094  0.628   1.00 15.18 ? 229 LEU A CA  1 
ATOM   1865 C  C   . LEU A 1 228 ? 18.151  -7.302  0.838   1.00 13.62 ? 229 LEU A C   1 
ATOM   1866 O  O   . LEU A 1 228 ? 18.672  -8.307  1.337   1.00 15.25 ? 229 LEU A O   1 
ATOM   1867 C  CB  . LEU A 1 228 ? 16.029  -6.100  1.660   1.00 13.58 ? 229 LEU A CB  1 
ATOM   1868 C  CG  . LEU A 1 228 ? 14.566  -5.710  1.505   1.00 12.90 ? 229 LEU A CG  1 
ATOM   1869 C  CD1 . LEU A 1 228 ? 14.117  -5.082  2.816   1.00 13.78 ? 229 LEU A CD1 1 
ATOM   1870 C  CD2 . LEU A 1 228 ? 14.391  -4.624  0.431   1.00 13.53 ? 229 LEU A CD2 1 
ATOM   1871 N  N   . ASN A 1 229 ? 18.875  -6.222  0.480   1.00 17.51 ? 230 ASN A N   1 
ATOM   1872 C  CA  . ASN A 1 229 ? 20.291  -6.145  0.460   1.00 16.83 ? 230 ASN A CA  1 
ATOM   1873 C  C   . ASN A 1 229 ? 20.776  -4.948  1.302   1.00 16.77 ? 230 ASN A C   1 
ATOM   1874 O  O   . ASN A 1 229 ? 20.241  -3.838  1.190   1.00 18.12 ? 230 ASN A O   1 
ATOM   1875 C  CB  . ASN A 1 229 ? 20.715  -5.901  -1.016  1.00 18.56 ? 230 ASN A CB  1 
ATOM   1876 C  CG  . ASN A 1 229 ? 20.770  -7.181  -1.901  1.00 22.21 ? 230 ASN A CG  1 
ATOM   1877 O  OD1 . ASN A 1 229 ? 21.453  -7.120  -2.967  1.00 22.21 ? 230 ASN A OD1 1 
ATOM   1878 N  ND2 . ASN A 1 229 ? 20.095  -8.279  -1.545  1.00 17.87 ? 230 ASN A ND2 1 
ATOM   1879 N  N   . PHE A 1 230 ? 21.802  -5.252  2.059   1.00 20.34 ? 231 PHE A N   1 
ATOM   1880 C  CA  . PHE A 1 230 ? 22.521  -4.192  2.776   1.00 19.53 ? 231 PHE A CA  1 
ATOM   1881 C  C   . PHE A 1 230 ? 23.437  -3.420  1.797   1.00 24.05 ? 231 PHE A C   1 
ATOM   1882 O  O   . PHE A 1 230 ? 23.700  -2.241  2.035   1.00 22.58 ? 231 PHE A O   1 
ATOM   1883 C  CB  . PHE A 1 230 ? 23.499  -4.778  3.722   1.00 16.64 ? 231 PHE A CB  1 
ATOM   1884 C  CG  . PHE A 1 230 ? 22.933  -5.363  5.027   1.00 16.04 ? 231 PHE A CG  1 
ATOM   1885 C  CD1 . PHE A 1 230 ? 22.132  -4.606  5.900   1.00 14.96 ? 231 PHE A CD1 1 
ATOM   1886 C  CD2 . PHE A 1 230 ? 23.335  -6.671  5.398   1.00 15.83 ? 231 PHE A CD2 1 
ATOM   1887 C  CE1 . PHE A 1 230 ? 21.707  -5.178  7.130   1.00 16.38 ? 231 PHE A CE1 1 
ATOM   1888 C  CE2 . PHE A 1 230 ? 22.933  -7.244  6.654   1.00 17.14 ? 231 PHE A CE2 1 
ATOM   1889 C  CZ  . PHE A 1 230 ? 22.135  -6.457  7.502   1.00 14.46 ? 231 PHE A CZ  1 
ATOM   1890 N  N   . ASN A 1 231 ? 23.943  -4.102  0.770   1.00 23.97 ? 232 ASN A N   1 
ATOM   1891 C  CA  . ASN A 1 231 ? 24.820  -3.422  -0.242  1.00 24.82 ? 232 ASN A CA  1 
ATOM   1892 C  C   . ASN A 1 231 ? 24.093  -2.484  -1.218  1.00 22.48 ? 232 ASN A C   1 
ATOM   1893 O  O   . ASN A 1 231 ? 22.855  -2.541  -1.388  1.00 21.39 ? 232 ASN A O   1 
ATOM   1894 C  CB  . ASN A 1 231 ? 25.486  -4.497  -1.031  1.00 24.47 ? 232 ASN A CB  1 
ATOM   1895 C  CG  . ASN A 1 231 ? 24.476  -5.414  -1.673  1.00 25.10 ? 232 ASN A CG  1 
ATOM   1896 O  OD1 . ASN A 1 231 ? 24.109  -6.421  -1.068  1.00 27.87 ? 232 ASN A OD1 1 
ATOM   1897 N  ND2 . ASN A 1 231 ? 24.083  -5.128  -2.936  1.00 23.85 ? 232 ASN A ND2 1 
ATOM   1898 N  N   . GLY A 1 232 ? 24.820  -1.581  -1.922  1.00 25.19 ? 233 GLY A N   1 
ATOM   1899 C  CA  . GLY A 1 232 ? 24.181  -0.787  -3.008  1.00 25.75 ? 233 GLY A CA  1 
ATOM   1900 C  C   . GLY A 1 232 ? 24.145  -1.551  -4.332  1.00 23.04 ? 233 GLY A C   1 
ATOM   1901 O  O   . GLY A 1 232 ? 24.783  -2.540  -4.454  1.00 22.95 ? 233 GLY A O   1 
ATOM   1902 N  N   . GLU A 1 233 ? 23.315  -1.091  -5.272  1.00 23.60 ? 234 GLU A N   1 
ATOM   1903 C  CA  . GLU A 1 233 ? 23.269  -1.626  -6.632  1.00 25.19 ? 234 GLU A CA  1 
ATOM   1904 C  C   . GLU A 1 233 ? 24.665  -1.662  -7.259  1.00 22.87 ? 234 GLU A C   1 
ATOM   1905 O  O   . GLU A 1 233 ? 25.412  -0.668  -7.233  1.00 24.66 ? 234 GLU A O   1 
ATOM   1906 C  CB  . GLU A 1 233 ? 22.324  -0.799  -7.507  1.00 23.05 ? 234 GLU A CB  1 
ATOM   1907 C  CG  . GLU A 1 233 ? 21.999  -1.507  -8.814  1.00 26.05 ? 234 GLU A CG  1 
ATOM   1908 C  CD  . GLU A 1 233 ? 21.138  -0.685  -9.704  1.00 31.22 ? 234 GLU A CD  1 
ATOM   1909 O  OE1 . GLU A 1 233 ? 20.788  0.457   -9.297  1.00 34.72 ? 234 GLU A OE1 1 
ATOM   1910 O  OE2 . GLU A 1 233 ? 20.843  -1.179  -10.820 1.00 34.19 ? 234 GLU A OE2 1 
ATOM   1911 N  N   . GLY A 1 234 ? 25.009  -2.858  -7.737  1.00 25.65 ? 235 GLY A N   1 
ATOM   1912 C  CA  . GLY A 1 234 ? 26.251  -3.068  -8.450  1.00 32.49 ? 235 GLY A CA  1 
ATOM   1913 C  C   . GLY A 1 234 ? 27.419  -3.288  -7.529  1.00 34.72 ? 235 GLY A C   1 
ATOM   1914 O  O   . GLY A 1 234 ? 28.572  -3.079  -7.915  1.00 31.23 ? 235 GLY A O   1 
ATOM   1915 N  N   . GLU A 1 235 ? 27.102  -3.674  -6.296  1.00 37.71 ? 236 GLU A N   1 
ATOM   1916 C  CA  . GLU A 1 235 ? 28.086  -4.117  -5.322  1.00 37.30 ? 236 GLU A CA  1 
ATOM   1917 C  C   . GLU A 1 235 ? 27.682  -5.544  -5.013  1.00 38.34 ? 236 GLU A C   1 
ATOM   1918 O  O   . GLU A 1 235 ? 26.548  -5.967  -5.320  1.00 38.24 ? 236 GLU A O   1 
ATOM   1919 C  CB  . GLU A 1 235 ? 27.998  -3.294  -4.049  1.00 45.83 ? 236 GLU A CB  1 
ATOM   1920 C  CG  . GLU A 1 235 ? 29.001  -2.184  -3.904  1.00 50.74 ? 236 GLU A CG  1 
ATOM   1921 C  CD  . GLU A 1 235 ? 28.662  -1.326  -2.704  1.00 61.01 ? 236 GLU A CD  1 
ATOM   1922 O  OE1 . GLU A 1 235 ? 28.398  -1.891  -1.601  1.00 62.02 ? 236 GLU A OE1 1 
ATOM   1923 O  OE2 . GLU A 1 235 ? 28.634  -0.085  -2.867  1.00 62.54 ? 236 GLU A OE2 1 
ATOM   1924 N  N   . PRO A 1 236 ? 28.592  -6.305  -4.402  1.00 33.41 ? 237 PRO A N   1 
ATOM   1925 C  CA  . PRO A 1 236 ? 28.385  -7.722  -4.152  1.00 30.62 ? 237 PRO A CA  1 
ATOM   1926 C  C   . PRO A 1 236 ? 27.207  -7.935  -3.160  1.00 30.62 ? 237 PRO A C   1 
ATOM   1927 O  O   . PRO A 1 236 ? 27.086  -7.149  -2.215  1.00 27.65 ? 237 PRO A O   1 
ATOM   1928 C  CB  . PRO A 1 236 ? 29.705  -8.158  -3.543  1.00 32.14 ? 237 PRO A CB  1 
ATOM   1929 C  CG  . PRO A 1 236 ? 30.709  -7.082  -3.848  1.00 31.28 ? 237 PRO A CG  1 
ATOM   1930 C  CD  . PRO A 1 236 ? 29.934  -5.824  -3.998  1.00 36.35 ? 237 PRO A CD  1 
ATOM   1931 N  N   . GLU A 1 237 ? 26.376  -8.961  -3.394  1.00 29.34 ? 238 GLU A N   1 
ATOM   1932 C  CA  . GLU A 1 237 ? 25.101  -9.155  -2.644  1.00 26.21 ? 238 GLU A CA  1 
ATOM   1933 C  C   . GLU A 1 237 ? 25.327  -9.652  -1.221  1.00 22.60 ? 238 GLU A C   1 
ATOM   1934 O  O   . GLU A 1 237 ? 25.798  -10.721 -1.018  1.00 20.81 ? 238 GLU A O   1 
ATOM   1935 C  CB  . GLU A 1 237 ? 24.100  -10.107 -3.361  1.00 27.65 ? 238 GLU A CB  1 
ATOM   1936 C  CG  . GLU A 1 237 ? 22.756  -10.227 -2.618  1.00 26.53 ? 238 GLU A CG  1 
ATOM   1937 C  CD  . GLU A 1 237 ? 21.636  -10.974 -3.321  1.00 26.39 ? 238 GLU A CD  1 
ATOM   1938 O  OE1 . GLU A 1 237 ? 21.943  -12.062 -3.894  1.00 28.13 ? 238 GLU A OE1 1 
ATOM   1939 O  OE2 . GLU A 1 237 ? 20.466  -10.439 -3.328  1.00 21.72 ? 238 GLU A OE2 1 
ATOM   1940 N  N   . GLU A 1 238 ? 24.812  -8.895  -0.245  1.00 22.28 ? 239 GLU A N   1 
ATOM   1941 C  CA  . GLU A 1 238 ? 24.835  -9.327  1.138   1.00 23.27 ? 239 GLU A CA  1 
ATOM   1942 C  C   . GLU A 1 238 ? 23.380  -9.172  1.632   1.00 17.36 ? 239 GLU A C   1 
ATOM   1943 O  O   . GLU A 1 238 ? 22.809  -8.086  1.603   1.00 18.94 ? 239 GLU A O   1 
ATOM   1944 C  CB  . GLU A 1 238 ? 25.711  -8.402  1.969   1.00 24.98 ? 239 GLU A CB  1 
ATOM   1945 C  CG  . GLU A 1 238 ? 26.301  -9.163  3.150   1.00 29.38 ? 239 GLU A CG  1 
ATOM   1946 C  CD  . GLU A 1 238 ? 27.813  -8.946  3.280   1.00 34.81 ? 239 GLU A CD  1 
ATOM   1947 O  OE1 . GLU A 1 238 ? 28.337  -8.758  4.428   1.00 34.96 ? 239 GLU A OE1 1 
ATOM   1948 O  OE2 . GLU A 1 238 ? 28.476  -8.910  2.219   1.00 48.54 ? 239 GLU A OE2 1 
ATOM   1949 N  N   . LEU A 1 239 ? 22.776  -10.309 1.987   1.00 17.55 ? 240 LEU A N   1 
ATOM   1950 C  CA  . LEU A 1 239 ? 21.287  -10.191 2.287   1.00 15.86 ? 240 LEU A CA  1 
ATOM   1951 C  C   . LEU A 1 239 ? 21.107  -9.362  3.594   1.00 13.14 ? 240 LEU A C   1 
ATOM   1952 O  O   . LEU A 1 239 ? 21.867  -9.574  4.595   1.00 16.32 ? 240 LEU A O   1 
ATOM   1953 C  CB  . LEU A 1 239 ? 20.719  -11.573 2.513   1.00 13.76 ? 240 LEU A CB  1 
ATOM   1954 C  CG  . LEU A 1 239 ? 20.554  -12.448 1.246   1.00 13.51 ? 240 LEU A CG  1 
ATOM   1955 C  CD1 . LEU A 1 239 ? 19.886  -13.779 1.589   1.00 16.95 ? 240 LEU A CD1 1 
ATOM   1956 C  CD2 . LEU A 1 239 ? 19.710  -11.730 0.201   1.00 15.35 ? 240 LEU A CD2 1 
ATOM   1957 N  N   . MET A 1 240 ? 20.090  -8.544  3.574   1.00 14.04 ? 241 MET A N   1 
ATOM   1958 C  CA  . MET A 1 240 ? 19.716  -7.735  4.786   1.00 12.56 ? 241 MET A CA  1 
ATOM   1959 C  C   . MET A 1 240 ? 18.916  -8.683  5.717   1.00 11.66 ? 241 MET A C   1 
ATOM   1960 O  O   . MET A 1 240 ? 17.675  -8.848  5.552   1.00 12.79 ? 241 MET A O   1 
ATOM   1961 C  CB  . MET A 1 240 ? 18.945  -6.486  4.367   1.00 13.92 ? 241 MET A CB  1 
ATOM   1962 C  CG  . MET A 1 240 ? 18.556  -5.563  5.578   1.00 13.88 ? 241 MET A CG  1 
ATOM   1963 S  SD  . MET A 1 240 ? 17.676  -4.173  5.071   1.00 16.00 ? 241 MET A SD  1 
ATOM   1964 C  CE  . MET A 1 240 ? 18.973  -3.042  4.456   1.00 13.56 ? 241 MET A CE  1 
ATOM   1965 N  N   . VAL A 1 241 ? 19.680  -9.328  6.550   1.00 12.54 ? 242 VAL A N   1 
ATOM   1966 C  CA  . VAL A 1 241 ? 19.115  -10.194 7.606   1.00 11.19 ? 242 VAL A CA  1 
ATOM   1967 C  C   . VAL A 1 241 ? 19.922  -9.976  8.921   1.00 12.65 ? 242 VAL A C   1 
ATOM   1968 O  O   . VAL A 1 241 ? 21.122  -9.606  8.934   1.00 12.86 ? 242 VAL A O   1 
ATOM   1969 C  CB  . VAL A 1 241 ? 19.147  -11.704 7.262   1.00 10.91 ? 242 VAL A CB  1 
ATOM   1970 C  CG1 . VAL A 1 241 ? 18.208  -11.985 6.052   1.00 11.33 ? 242 VAL A CG1 1 
ATOM   1971 C  CG2 . VAL A 1 241 ? 20.621  -12.192 7.100   1.00 12.94 ? 242 VAL A CG2 1 
ATOM   1972 N  N   . ASP A 1 242 ? 19.284  -10.262 10.058  1.00 10.86 ? 243 ASP A N   1 
ATOM   1973 C  CA  . ASP A 1 242 ? 19.967  -10.094 11.326  1.00 11.03 ? 243 ASP A CA  1 
ATOM   1974 C  C   . ASP A 1 242 ? 20.426  -8.676  11.561  1.00 10.38 ? 243 ASP A C   1 
ATOM   1975 O  O   . ASP A 1 242 ? 21.563  -8.482  12.055  1.00 11.73 ? 243 ASP A O   1 
ATOM   1976 C  CB  . ASP A 1 242 ? 21.062  -11.161 11.638  1.00 10.08 ? 243 ASP A CB  1 
ATOM   1977 C  CG  . ASP A 1 242 ? 20.481  -12.555 11.703  1.00 12.22 ? 243 ASP A CG  1 
ATOM   1978 O  OD1 . ASP A 1 242 ? 19.412  -12.787 12.324  1.00 10.71 ? 243 ASP A OD1 1 
ATOM   1979 O  OD2 . ASP A 1 242 ? 21.069  -13.489 11.072  1.00 13.87 ? 243 ASP A OD2 1 
ATOM   1980 N  N   . ASN A 1 243 ? 19.549  -7.725  11.287  1.00 8.86  ? 244 ASN A N   1 
ATOM   1981 C  CA  . ASN A 1 243 ? 19.906  -6.307  11.563  1.00 8.40  ? 244 ASN A CA  1 
ATOM   1982 C  C   . ASN A 1 243 ? 19.290  -5.891  12.938  1.00 8.66  ? 244 ASN A C   1 
ATOM   1983 O  O   . ASN A 1 243 ? 18.607  -4.845  12.989  1.00 8.80  ? 244 ASN A O   1 
ATOM   1984 C  CB  . ASN A 1 243 ? 19.378  -5.422  10.421  1.00 10.13 ? 244 ASN A CB  1 
ATOM   1985 C  CG  . ASN A 1 243 ? 17.867  -5.598  10.155  1.00 11.77 ? 244 ASN A CG  1 
ATOM   1986 O  OD1 . ASN A 1 243 ? 17.200  -6.464  10.742  1.00 11.55 ? 244 ASN A OD1 1 
ATOM   1987 N  ND2 . ASN A 1 243 ? 17.283  -4.646  9.378   1.00 14.53 ? 244 ASN A ND2 1 
ATOM   1988 N  N   . TRP A 1 244 ? 19.558  -6.695  13.919  1.00 7.53  ? 245 TRP A N   1 
ATOM   1989 C  CA  . TRP A 1 244 ? 19.099  -6.442  15.287  1.00 7.85  ? 245 TRP A CA  1 
ATOM   1990 C  C   . TRP A 1 244 ? 20.289  -6.294  16.176  1.00 9.20  ? 245 TRP A C   1 
ATOM   1991 O  O   . TRP A 1 244 ? 21.303  -6.990  16.046  1.00 9.97  ? 245 TRP A O   1 
ATOM   1992 C  CB  . TRP A 1 244 ? 18.126  -7.560  15.781  1.00 9.28  ? 245 TRP A CB  1 
ATOM   1993 C  CG  . TRP A 1 244 ? 18.609  -8.947  15.602  1.00 7.82  ? 245 TRP A CG  1 
ATOM   1994 C  CD1 . TRP A 1 244 ? 18.452  -9.723  14.449  1.00 9.39  ? 245 TRP A CD1 1 
ATOM   1995 C  CD2 . TRP A 1 244 ? 19.208  -9.803  16.601  1.00 9.15  ? 245 TRP A CD2 1 
ATOM   1996 N  NE1 . TRP A 1 244 ? 18.987  -10.980 14.674  1.00 8.97  ? 245 TRP A NE1 1 
ATOM   1997 C  CE2 . TRP A 1 244 ? 19.421  -11.097 15.959  1.00 9.37  ? 245 TRP A CE2 1 
ATOM   1998 C  CE3 . TRP A 1 244 ? 19.538  -9.665  17.984  1.00 9.67  ? 245 TRP A CE3 1 
ATOM   1999 C  CZ2 . TRP A 1 244 ? 20.041  -12.168 16.649  1.00 9.97  ? 245 TRP A CZ2 1 
ATOM   2000 C  CZ3 . TRP A 1 244 ? 20.170  -10.757 18.634  1.00 10.25 ? 245 TRP A CZ3 1 
ATOM   2001 C  CH2 . TRP A 1 244 ? 20.356  -11.994 17.967  1.00 10.83 ? 245 TRP A CH2 1 
ATOM   2002 N  N   . ARG A 1 245 ? 20.160  -5.410  17.159  1.00 8.19  ? 246 ARG A N   1 
ATOM   2003 C  CA  . ARG A 1 245 ? 21.128  -5.329  18.280  1.00 8.49  ? 246 ARG A CA  1 
ATOM   2004 C  C   . ARG A 1 245 ? 20.676  -6.199  19.437  1.00 8.57  ? 246 ARG A C   1 
ATOM   2005 O  O   . ARG A 1 245 ? 19.494  -6.213  19.759  1.00 9.39  ? 246 ARG A O   1 
ATOM   2006 C  CB  . ARG A 1 245 ? 21.114  -3.841  18.799  1.00 8.48  ? 246 ARG A CB  1 
ATOM   2007 C  CG  . ARG A 1 245 ? 22.245  -3.596  19.797  1.00 9.48  ? 246 ARG A CG  1 
ATOM   2008 C  CD  . ARG A 1 245 ? 22.181  -2.221  20.459  1.00 10.52 ? 246 ARG A CD  1 
ATOM   2009 N  NE  . ARG A 1 245 ? 23.471  -1.996  21.216  1.00 10.89 ? 246 ARG A NE  1 
ATOM   2010 C  CZ  . ARG A 1 245 ? 23.671  -0.957  22.030  1.00 11.00 ? 246 ARG A CZ  1 
ATOM   2011 N  NH1 . ARG A 1 245 ? 22.681  -0.085  22.348  1.00 10.51 ? 246 ARG A NH1 1 
ATOM   2012 N  NH2 . ARG A 1 245 ? 24.898  -0.726  22.543  1.00 10.99 ? 246 ARG A NH2 1 
ATOM   2013 N  N   . PRO A 1 246 ? 21.492  -7.041  20.069  1.00 9.95  ? 247 PRO A N   1 
ATOM   2014 C  CA  . PRO A 1 246 ? 21.072  -7.852  21.187  1.00 9.54  ? 247 PRO A CA  1 
ATOM   2015 C  C   . PRO A 1 246 ? 20.774  -7.060  22.489  1.00 8.84  ? 247 PRO A C   1 
ATOM   2016 O  O   . PRO A 1 246 ? 21.186  -5.856  22.635  1.00 9.24  ? 247 PRO A O   1 
ATOM   2017 C  CB  . PRO A 1 246 ? 22.340  -8.738  21.480  1.00 12.33 ? 247 PRO A CB  1 
ATOM   2018 C  CG  . PRO A 1 246 ? 23.221  -8.555  20.280  1.00 13.25 ? 247 PRO A CG  1 
ATOM   2019 C  CD  . PRO A 1 246 ? 22.925  -7.192  19.702  1.00 11.03 ? 247 PRO A CD  1 
ATOM   2020 N  N   . ALA A 1 247 ? 20.117  -7.717  23.449  1.00 10.05 ? 248 ALA A N   1 
ATOM   2021 C  CA  . ALA A 1 247 ? 19.798  -7.118  24.707  1.00 9.45  ? 248 ALA A CA  1 
ATOM   2022 C  C   . ALA A 1 247 ? 21.021  -6.539  25.414  1.00 10.00 ? 248 ALA A C   1 
ATOM   2023 O  O   . ALA A 1 247 ? 22.134  -7.189  25.431  1.00 11.60 ? 248 ALA A O   1 
ATOM   2024 C  CB  . ALA A 1 247 ? 19.041  -8.133  25.581  1.00 10.41 ? 248 ALA A CB  1 
ATOM   2025 N  N   . GLN A 1 248 ? 20.860  -5.369  26.025  1.00 9.42  ? 249 GLN A N   1 
ATOM   2026 C  CA  . GLN A 1 248 ? 21.946  -4.648  26.750  1.00 10.26 ? 249 GLN A CA  1 
ATOM   2027 C  C   . GLN A 1 248 ? 21.612  -4.686  28.225  1.00 10.93 ? 249 GLN A C   1 
ATOM   2028 O  O   . GLN A 1 248 ? 20.444  -4.916  28.636  1.00 11.00 ? 249 GLN A O   1 
ATOM   2029 C  CB  . GLN A 1 248 ? 22.002  -3.245  26.242  1.00 11.19 ? 249 GLN A CB  1 
ATOM   2030 C  CG  . GLN A 1 248 ? 22.332  -3.141  24.732  1.00 11.23 ? 249 GLN A CG  1 
ATOM   2031 C  CD  . GLN A 1 248 ? 23.665  -3.794  24.352  1.00 13.24 ? 249 GLN A CD  1 
ATOM   2032 O  OE1 . GLN A 1 248 ? 24.712  -3.491  25.014  1.00 15.19 ? 249 GLN A OE1 1 
ATOM   2033 N  NE2 . GLN A 1 248 ? 23.668  -4.719  23.380  1.00 13.27 ? 249 GLN A NE2 1 
ATOM   2034 N  N   . PRO A 1 249 ? 22.631  -4.423  29.098  1.00 13.65 ? 250 PRO A N   1 
ATOM   2035 C  CA  . PRO A 1 249 ? 22.345  -4.516  30.539  1.00 13.90 ? 250 PRO A CA  1 
ATOM   2036 C  C   . PRO A 1 249 ? 21.319  -3.456  30.999  1.00 12.37 ? 250 PRO A C   1 
ATOM   2037 O  O   . PRO A 1 249 ? 21.334  -2.290  30.548  1.00 15.31 ? 250 PRO A O   1 
ATOM   2038 C  CB  . PRO A 1 249 ? 23.716  -4.201  31.167  1.00 14.38 ? 250 PRO A CB  1 
ATOM   2039 C  CG  . PRO A 1 249 ? 24.681  -4.621  30.144  1.00 15.23 ? 250 PRO A CG  1 
ATOM   2040 C  CD  . PRO A 1 249 ? 24.045  -4.171  28.812  1.00 12.86 ? 250 PRO A CD  1 
ATOM   2041 N  N   . LEU A 1 250 ? 20.409  -3.896  31.854  1.00 14.30 ? 251 LEU A N   1 
ATOM   2042 C  CA  . LEU A 1 250 ? 19.360  -3.051  32.389  1.00 13.58 ? 251 LEU A CA  1 
ATOM   2043 C  C   . LEU A 1 250 ? 19.912  -1.965  33.306  1.00 14.09 ? 251 LEU A C   1 
ATOM   2044 O  O   . LEU A 1 250 ? 19.381  -0.815  33.347  1.00 12.01 ? 251 LEU A O   1 
ATOM   2045 C  CB  . LEU A 1 250 ? 18.305  -3.862  33.141  1.00 15.49 ? 251 LEU A CB  1 
ATOM   2046 C  CG  . LEU A 1 250 ? 16.936  -3.216  33.451  1.00 15.95 ? 251 LEU A CG  1 
ATOM   2047 C  CD1 . LEU A 1 250 ? 16.236  -2.603  32.229  1.00 15.46 ? 251 LEU A CD1 1 
ATOM   2048 C  CD2 . LEU A 1 250 ? 16.063  -4.255  34.128  1.00 20.61 ? 251 LEU A CD2 1 
ATOM   2049 N  N   . LYS A 1 251 ? 20.984  -2.303  34.046  1.00 15.20 ? 252 LYS A N   1 
ATOM   2050 C  CA  . LYS A 1 251 ? 21.681  -1.252  34.888  1.00 14.78 ? 252 LYS A CA  1 
ATOM   2051 C  C   . LYS A 1 251 ? 20.676  -0.753  35.917  1.00 16.47 ? 252 LYS A C   1 
ATOM   2052 O  O   . LYS A 1 251 ? 19.852  -1.542  36.434  1.00 18.54 ? 252 LYS A O   1 
ATOM   2053 C  CB  . LYS A 1 251 ? 22.390  -0.178  34.049  1.00 16.66 ? 252 LYS A CB  1 
ATOM   2054 C  CG  . LYS A 1 251 ? 23.558  -0.837  33.308  1.00 17.67 ? 252 LYS A CG  1 
ATOM   2055 C  CD  . LYS A 1 251 ? 24.445  0.124   32.601  1.00 20.07 ? 252 LYS A CD  1 
ATOM   2056 C  CE  . LYS A 1 251 ? 25.715  -0.580  32.192  1.00 22.32 ? 252 LYS A CE  1 
ATOM   2057 N  NZ  . LYS A 1 251 ? 26.600  0.332   31.442  1.00 23.86 ? 252 LYS A NZ  1 
ATOM   2058 N  N   . ASN A 1 252 ? 20.679  0.541   36.160  1.00 17.19 ? 253 ASN A N   1 
ATOM   2059 C  CA  . ASN A 1 252 ? 19.813  0.992   37.213  1.00 22.64 ? 253 ASN A CA  1 
ATOM   2060 C  C   . ASN A 1 252 ? 18.436  1.449   36.640  1.00 21.45 ? 253 ASN A C   1 
ATOM   2061 O  O   . ASN A 1 252 ? 18.181  2.729   36.625  1.00 24.29 ? 253 ASN A O   1 
ATOM   2062 C  CB  . ASN A 1 252 ? 20.517  2.146   37.938  1.00 28.29 ? 253 ASN A CB  1 
ATOM   2063 C  CG  . ASN A 1 252 ? 19.739  2.643   39.148  1.00 34.74 ? 253 ASN A CG  1 
ATOM   2064 O  OD1 . ASN A 1 252 ? 19.147  1.852   39.908  1.00 40.49 ? 253 ASN A OD1 1 
ATOM   2065 N  ND2 . ASN A 1 252 ? 19.706  3.975   39.311  1.00 35.71 ? 253 ASN A ND2 1 
ATOM   2066 N  N   . ARG A 1 253 ? 17.672  0.461   36.063  1.00 14.64 ? 254 ARG A N   1 
ATOM   2067 C  CA  . ARG A 1 253 ? 16.335  0.751   35.503  1.00 14.54 ? 254 ARG A CA  1 
ATOM   2068 C  C   . ARG A 1 253 ? 15.305  -0.241  35.939  1.00 16.04 ? 254 ARG A C   1 
ATOM   2069 O  O   . ARG A 1 253 ? 15.610  -1.403  36.089  1.00 18.02 ? 254 ARG A O   1 
ATOM   2070 C  CB  . ARG A 1 253 ? 16.291  0.865   33.913  1.00 13.00 ? 254 ARG A CB  1 
ATOM   2071 C  CG  . ARG A 1 253 ? 17.166  2.036   33.412  1.00 10.75 ? 254 ARG A CG  1 
ATOM   2072 C  CD  . ARG A 1 253 ? 17.327  2.039   31.915  1.00 12.27 ? 254 ARG A CD  1 
ATOM   2073 N  NE  . ARG A 1 253 ? 18.212  0.947   31.453  1.00 10.45 ? 254 ARG A NE  1 
ATOM   2074 C  CZ  . ARG A 1 253 ? 18.478  0.678   30.156  1.00 9.39  ? 254 ARG A CZ  1 
ATOM   2075 N  NH1 . ARG A 1 253 ? 17.848  1.376   29.162  1.00 8.86  ? 254 ARG A NH1 1 
ATOM   2076 N  NH2 . ARG A 1 253 ? 19.301  -0.297  29.828  1.00 9.53  ? 254 ARG A NH2 1 
ATOM   2077 N  N   . GLN A 1 254 ? 14.055  0.233   36.109  1.00 16.23 ? 255 GLN A N   1 
ATOM   2078 C  CA  . GLN A 1 254 ? 12.886  -0.674  36.328  1.00 18.52 ? 255 GLN A CA  1 
ATOM   2079 C  C   . GLN A 1 254 ? 11.919  -0.583  35.150  1.00 17.08 ? 255 GLN A C   1 
ATOM   2080 O  O   . GLN A 1 254 ? 11.576  0.503   34.699  1.00 21.87 ? 255 GLN A O   1 
ATOM   2081 C  CB  . GLN A 1 254 ? 12.107  -0.354  37.614  1.00 25.23 ? 255 GLN A CB  1 
ATOM   2082 C  CG  . GLN A 1 254 ? 11.376  -1.612  38.137  1.00 31.60 ? 255 GLN A CG  1 
ATOM   2083 C  CD  . GLN A 1 254 ? 10.542  -1.419  39.406  1.00 38.05 ? 255 GLN A CD  1 
ATOM   2084 O  OE1 . GLN A 1 254 ? 9.791   -0.448  39.532  1.00 40.98 ? 255 GLN A OE1 1 
ATOM   2085 N  NE2 . GLN A 1 254 ? 10.647  -2.386  40.345  1.00 37.49 ? 255 GLN A NE2 1 
ATOM   2086 N  N   . ILE A 1 255 ? 11.555  -1.739  34.616  1.00 13.82 ? 256 ILE A N   1 
ATOM   2087 C  CA  . ILE A 1 255 ? 10.568  -1.757  33.560  1.00 12.76 ? 256 ILE A CA  1 
ATOM   2088 C  C   . ILE A 1 255 ? 9.176   -1.751  34.217  1.00 11.49 ? 256 ILE A C   1 
ATOM   2089 O  O   . ILE A 1 255 ? 8.960   -2.399  35.236  1.00 13.13 ? 256 ILE A O   1 
ATOM   2090 C  CB  . ILE A 1 255 ? 10.788  -2.967  32.674  1.00 12.22 ? 256 ILE A CB  1 
ATOM   2091 C  CG1 . ILE A 1 255 ? 12.206  -2.913  32.034  1.00 14.97 ? 256 ILE A CG1 1 
ATOM   2092 C  CG2 . ILE A 1 255 ? 9.655   -3.085  31.621  1.00 13.00 ? 256 ILE A CG2 1 
ATOM   2093 C  CD1 . ILE A 1 255 ? 12.495  -4.200  31.256  1.00 14.61 ? 256 ILE A CD1 1 
ATOM   2094 N  N   . LYS A 1 256 ? 8.283   -0.869  33.709  1.00 11.26 ? 257 LYS A N   1 
ATOM   2095 C  CA  . LYS A 1 256 ? 6.907   -0.678  34.244  1.00 12.10 ? 257 LYS A CA  1 
ATOM   2096 C  C   . LYS A 1 256 ? 5.938   -1.326  33.292  1.00 11.57 ? 257 LYS A C   1 
ATOM   2097 O  O   . LYS A 1 256 ? 6.172   -1.339  32.073  1.00 12.46 ? 257 LYS A O   1 
ATOM   2098 C  CB  . LYS A 1 256 ? 6.598   0.829   34.471  1.00 14.21 ? 257 LYS A CB  1 
ATOM   2099 C  CG  . LYS A 1 256 ? 7.545   1.564   35.458  1.00 20.54 ? 257 LYS A CG  1 
ATOM   2100 C  CD  . LYS A 1 256 ? 7.275   1.232   36.940  1.00 28.33 ? 257 LYS A CD  1 
ATOM   2101 C  CE  . LYS A 1 256 ? 7.107   2.531   37.820  1.00 31.76 ? 257 LYS A CE  1 
ATOM   2102 N  NZ  . LYS A 1 256 ? 6.730   2.491   39.308  1.00 28.57 ? 257 LYS A NZ  1 
ATOM   2103 N  N   . ALA A 1 257 ? 4.877   -1.951  33.794  1.00 12.13 ? 258 ALA A N   1 
ATOM   2104 C  CA  . ALA A 1 257 ? 3.784   -2.569  33.034  1.00 11.26 ? 258 ALA A CA  1 
ATOM   2105 C  C   . ALA A 1 257 ? 2.488   -1.826  33.218  1.00 13.16 ? 258 ALA A C   1 
ATOM   2106 O  O   . ALA A 1 257 ? 2.149   -1.388  34.373  1.00 14.23 ? 258 ALA A O   1 
ATOM   2107 C  CB  . ALA A 1 257 ? 3.657   -4.092  33.371  1.00 10.20 ? 258 ALA A CB  1 
ATOM   2108 N  N   . SER A 1 258 ? 1.751   -1.628  32.150  1.00 11.61 ? 259 SER A N   1 
ATOM   2109 C  CA  . SER A 1 258 ? 0.432   -0.976  32.203  1.00 13.29 ? 259 SER A CA  1 
ATOM   2110 C  C   . SER A 1 258 ? -0.650  -1.965  32.582  1.00 15.61 ? 259 SER A C   1 
ATOM   2111 O  O   . SER A 1 258 ? -1.802  -1.549  32.761  1.00 18.21 ? 259 SER A O   1 
ATOM   2112 C  CB  . SER A 1 258 ? 0.141   -0.325  30.867  1.00 13.30 ? 259 SER A CB  1 
ATOM   2113 O  OG  . SER A 1 258 ? -0.314  -1.309  29.926  1.00 13.04 ? 259 SER A OG  1 
ATOM   2114 N  N   . PHE A 1 259 ? -0.336  -3.241  32.771  1.00 15.91 ? 260 PHE A N   1 
ATOM   2115 C  CA  . PHE A 1 259 ? -1.337  -4.286  32.863  1.00 17.24 ? 260 PHE A CA  1 
ATOM   2116 C  C   . PHE A 1 259 ? -0.874  -5.272  33.917  1.00 21.10 ? 260 PHE A C   1 
ATOM   2117 O  O   . PHE A 1 259 ? 0.317   -5.337  34.281  1.00 19.27 ? 260 PHE A O   1 
ATOM   2118 C  CB  . PHE A 1 259 ? -1.546  -5.025  31.557  1.00 20.36 ? 260 PHE A CB  1 
ATOM   2119 C  CG  . PHE A 1 259 ? -0.277  -5.742  31.067  1.00 19.15 ? 260 PHE A CG  1 
ATOM   2120 C  CD1 . PHE A 1 259 ? 0.736   -5.025  30.386  1.00 18.90 ? 260 PHE A CD1 1 
ATOM   2121 C  CD2 . PHE A 1 259 ? -0.046  -7.093  31.376  1.00 19.66 ? 260 PHE A CD2 1 
ATOM   2122 C  CE1 . PHE A 1 259 ? 1.915   -5.648  29.970  1.00 19.92 ? 260 PHE A CE1 1 
ATOM   2123 C  CE2 . PHE A 1 259 ? 1.156   -7.699  30.985  1.00 20.04 ? 260 PHE A CE2 1 
ATOM   2124 C  CZ  . PHE A 1 259 ? 2.152   -6.979  30.255  1.00 18.33 ? 260 PHE A CZ  1 
ATOM   2125 N  N   . LYS A 1 260 ? -1.902  -5.996  34.406  1.00 28.87 ? 261 LYS A N   1 
ATOM   2126 C  CA  . LYS A 1 260 ? -1.924  -7.176  35.317  1.00 40.02 ? 261 LYS A CA  1 
ATOM   2127 C  C   . LYS A 1 260 ? -1.620  -7.049  36.815  1.00 47.36 ? 261 LYS A C   1 
ATOM   2128 O  O   . LYS A 1 260 ? -2.334  -6.331  37.544  1.00 54.05 ? 261 LYS A O   1 
ATOM   2129 C  CB  . LYS A 1 260 ? -1.353  -8.447  34.673  1.00 38.51 ? 261 LYS A CB  1 
ATOM   2130 C  CG  . LYS A 1 260 ? -2.279  -8.961  33.572  1.00 39.48 ? 261 LYS A CG  1 
ATOM   2131 O  OXT . LYS A 1 260 ? -0.690  -7.645  37.338  1.00 61.42 ? 261 LYS A OXT 1 
HETATM 2132 ZN ZN  . ZN  B 2 .   ? 14.601  0.213   15.307  1.00 7.04  ? 301 ZN  A ZN  1 
HETATM 2133 S  S   . DMS C 3 .   ? 22.614  -9.794  15.014  1.00 30.95 ? 302 DMS A S   1 
HETATM 2134 O  O   . DMS C 3 .   ? 23.421  -8.734  14.256  1.00 38.08 ? 302 DMS A O   1 
HETATM 2135 C  C1  . DMS C 3 .   ? 23.240  -11.338 14.544  1.00 27.76 ? 302 DMS A C1  1 
HETATM 2136 C  C2  . DMS C 3 .   ? 23.069  -9.770  16.658  1.00 25.74 ? 302 DMS A C2  1 
HETATM 2137 O  O1  . MES D 4 .   ? 13.732  -7.272  -2.498  1.00 32.09 ? 303 MES A O1  1 
HETATM 2138 C  C2  . MES D 4 .   ? 14.019  -8.045  -3.699  1.00 32.39 ? 303 MES A C2  1 
HETATM 2139 C  C3  . MES D 4 .   ? 12.846  -8.793  -4.291  1.00 30.63 ? 303 MES A C3  1 
HETATM 2140 N  N4  . MES D 4 .   ? 11.895  -9.351  -3.299  1.00 32.36 ? 303 MES A N4  1 
HETATM 2141 C  C5  . MES D 4 .   ? 11.509  -8.329  -2.276  1.00 31.47 ? 303 MES A C5  1 
HETATM 2142 C  C6  . MES D 4 .   ? 12.765  -7.851  -1.585  1.00 28.56 ? 303 MES A C6  1 
HETATM 2143 C  C7  . MES D 4 .   ? 10.706  -9.963  -3.969  1.00 35.45 ? 303 MES A C7  1 
HETATM 2144 C  C8  . MES D 4 .   ? 9.503   -9.525  -3.164  1.00 25.90 ? 303 MES A C8  1 
HETATM 2145 C  C1  . PEG E 5 .   ? 29.827  -2.974  22.180  1.00 26.09 ? 304 PEG A C1  1 
HETATM 2146 O  O1  . PEG E 5 .   ? 29.792  -1.879  21.238  1.00 14.30 ? 304 PEG A O1  1 
HETATM 2147 C  C2  . PEG E 5 .   ? 30.216  -2.682  23.648  1.00 20.43 ? 304 PEG A C2  1 
HETATM 2148 O  O2  . PEG E 5 .   ? 29.439  -3.286  24.680  1.00 28.53 ? 304 PEG A O2  1 
HETATM 2149 C  C3  . PEG E 5 .   ? 28.084  -3.536  24.163  1.00 31.67 ? 304 PEG A C3  1 
HETATM 2150 C  C4  . PEG E 5 .   ? 27.910  -4.960  23.626  1.00 30.54 ? 304 PEG A C4  1 
HETATM 2151 O  O4  . PEG E 5 .   ? 26.872  -4.983  22.609  1.00 27.68 ? 304 PEG A O4  1 
HETATM 2152 S  S   . DMS F 3 .   ? -2.341  -10.039 15.453  1.00 47.24 ? 305 DMS A S   1 
HETATM 2153 O  O   . DMS F 3 .   ? -3.225  -8.802  15.557  1.00 35.07 ? 305 DMS A O   1 
HETATM 2154 C  C1  . DMS F 3 .   ? -3.078  -11.625 15.453  1.00 41.16 ? 305 DMS A C1  1 
HETATM 2155 C  C2  . DMS F 3 .   ? -1.796  -9.817  13.903  1.00 18.74 ? 305 DMS A C2  1 
HETATM 2156 F  F27 . WWO G 6 .   ? 14.313  5.138   15.060  1.00 32.90 ? 306 WWO A F27 1 
HETATM 2157 C  C5  . WWO G 6 .   ? 15.628  5.330   15.094  1.00 30.23 ? 306 WWO A C5  1 
HETATM 2158 C  C4  . WWO G 6 .   ? 16.349  4.349   15.839  1.00 27.40 ? 306 WWO A C4  1 
HETATM 2159 S  S7  . WWO G 6 .   ? 15.474  2.991   16.699  1.00 27.78 ? 306 WWO A S7  1 
HETATM 2160 O  O9  . WWO G 6 .   ? 13.906  2.974   16.609  1.00 20.90 ? 306 WWO A O9  1 
HETATM 2161 N  N10 . WWO G 6 .   ? 15.701  1.508   15.943  1.00 15.06 ? 306 WWO A N10 1 
HETATM 2162 O  O8  . WWO G 6 .   ? 15.760  2.713   18.156  1.00 20.11 ? 306 WWO A O8  1 
HETATM 2163 C  C3  . WWO G 6 .   ? 17.756  4.458   15.879  1.00 29.91 ? 306 WWO A C3  1 
HETATM 2164 F  F12 . WWO G 6 .   ? 18.485  3.514   16.548  1.00 30.07 ? 306 WWO A F12 1 
HETATM 2165 C  C2  . WWO G 6 .   ? 18.407  5.530   15.234  1.00 32.72 ? 306 WWO A C2  1 
HETATM 2166 F  F13 . WWO G 6 .   ? 19.791  5.653   15.281  1.00 28.67 ? 306 WWO A F13 1 
HETATM 2167 C  C6  . WWO G 6 .   ? 16.257  6.436   14.439  1.00 32.49 ? 306 WWO A C6  1 
HETATM 2168 C  C1  . WWO G 6 .   ? 17.687  6.501   14.509  1.00 31.26 ? 306 WWO A C1  1 
HETATM 2169 S  S11 . WWO G 6 .   ? 18.694  7.839   13.806  1.00 37.74 ? 306 WWO A S11 1 
HETATM 2170 O  O22 . WWO G 6 .   ? 17.749  8.711   12.939  1.00 41.84 ? 306 WWO A O22 1 
HETATM 2171 O  O23 . WWO G 6 .   ? 19.531  7.198   12.648  1.00 49.02 ? 306 WWO A O23 1 
HETATM 2172 C  C21 . WWO G 6 .   ? 19.646  9.069   14.756  1.00 39.32 ? 306 WWO A C21 1 
HETATM 2173 C  C24 . WWO G 6 .   ? 20.413  10.089  13.918  1.00 45.65 ? 306 WWO A C24 1 
HETATM 2174 O  O25 . WWO G 6 .   ? 20.263  11.371  14.451  1.00 46.93 ? 306 WWO A O25 1 
HETATM 2175 N  N26 . WWO G 6 .   ? 15.555  7.423   13.692  1.00 32.74 ? 306 WWO A N26 1 
HETATM 2176 C  C14 . WWO G 6 .   ? 14.890  7.251   12.404  1.00 38.20 ? 306 WWO A C14 1 
HETATM 2177 C  C15 . WWO G 6 .   ? 15.089  8.272   11.312  1.00 48.95 ? 306 WWO A C15 1 
HETATM 2178 C  C20 . WWO G 6 .   ? 16.183  8.158   10.408  1.00 56.63 ? 306 WWO A C20 1 
HETATM 2179 C  C19 . WWO G 6 .   ? 16.396  9.090   9.368   1.00 61.04 ? 306 WWO A C19 1 
HETATM 2180 C  C18 . WWO G 6 .   ? 15.487  10.155  9.211   1.00 60.73 ? 306 WWO A C18 1 
HETATM 2181 C  C17 . WWO G 6 .   ? 14.388  10.262  10.088  1.00 55.23 ? 306 WWO A C17 1 
HETATM 2182 C  C16 . WWO G 6 .   ? 14.184  9.337   11.141  1.00 47.98 ? 306 WWO A C16 1 
HETATM 2183 O  O   . HOH H 7 .   ? 20.674  -15.126 29.556  1.00 34.73 ? 401 HOH A O   1 
HETATM 2184 O  O   . HOH H 7 .   ? -1.567  -12.475 11.096  1.00 24.21 ? 402 HOH A O   1 
HETATM 2185 O  O   . HOH H 7 .   ? 22.926  14.371  22.909  1.00 27.36 ? 403 HOH A O   1 
HETATM 2186 O  O   . HOH H 7 .   ? 3.274   20.913  6.078   1.00 11.85 ? 404 HOH A O   1 
HETATM 2187 O  O   . HOH H 7 .   ? 7.590   -7.028  -5.292  1.00 18.38 ? 405 HOH A O   1 
HETATM 2188 O  O   . HOH H 7 .   ? 11.688  8.669   -3.614  1.00 35.36 ? 406 HOH A O   1 
HETATM 2189 O  O   . HOH H 7 .   ? 17.652  7.559   -2.521  1.00 33.85 ? 407 HOH A O   1 
HETATM 2190 O  O   . HOH H 7 .   ? 34.957  1.516   6.570   1.00 27.32 ? 408 HOH A O   1 
HETATM 2191 O  O   . HOH H 7 .   ? 4.043   -4.286  42.829  1.00 36.86 ? 409 HOH A O   1 
HETATM 2192 O  O   . HOH H 7 .   ? 6.658   -16.717 19.059  1.00 26.29 ? 410 HOH A O   1 
HETATM 2193 O  O   . HOH H 7 .   ? -2.956  10.586  20.176  1.00 26.23 ? 411 HOH A O   1 
HETATM 2194 O  O   . HOH H 7 .   ? 2.317   -10.145 -3.383  1.00 23.54 ? 412 HOH A O   1 
HETATM 2195 O  O   . HOH H 7 .   ? 9.033   12.770  5.954   1.00 29.90 ? 413 HOH A O   1 
HETATM 2196 O  O   . HOH H 7 .   ? 30.990  -2.387  -7.726  1.00 25.45 ? 414 HOH A O   1 
HETATM 2197 O  O   . HOH H 7 .   ? -4.461  -8.693  17.864  1.00 21.50 ? 415 HOH A O   1 
HETATM 2198 O  O   . HOH H 7 .   ? -4.125  -1.213  31.822  1.00 31.80 ? 416 HOH A O   1 
HETATM 2199 O  O   . HOH H 7 .   ? 10.195  -13.589 34.102  1.00 25.58 ? 417 HOH A O   1 
HETATM 2200 O  O   . HOH H 7 .   ? 1.333   -14.971 3.094   1.00 26.08 ? 418 HOH A O   1 
HETATM 2201 O  O   . HOH H 7 .   ? 8.258   -20.294 8.558   1.00 31.86 ? 419 HOH A O   1 
HETATM 2202 O  O   . HOH H 7 .   ? 31.950  -7.441  9.581   1.00 31.28 ? 420 HOH A O   1 
HETATM 2203 O  O   . HOH H 7 .   ? 12.520  -1.979  7.880   1.00 11.91 ? 421 HOH A O   1 
HETATM 2204 O  O   . HOH H 7 .   ? 14.543  -18.304 19.543  1.00 17.41 ? 422 HOH A O   1 
HETATM 2205 O  O   . HOH H 7 .   ? 4.715   -13.426 32.805  1.00 29.29 ? 423 HOH A O   1 
HETATM 2206 O  O   . HOH H 7 .   ? 14.286  -13.021 31.699  1.00 24.05 ? 424 HOH A O   1 
HETATM 2207 O  O   . HOH H 7 .   ? 26.124  -3.049  21.091  1.00 12.75 ? 425 HOH A O   1 
HETATM 2208 O  O   . HOH H 7 .   ? 5.252   -8.198  38.008  1.00 36.66 ? 426 HOH A O   1 
HETATM 2209 O  O   . HOH H 7 .   ? 12.832  -13.294 37.191  1.00 25.35 ? 427 HOH A O   1 
HETATM 2210 O  O   . HOH H 7 .   ? 4.576   7.084   -7.883  1.00 26.12 ? 428 HOH A O   1 
HETATM 2211 O  O   . HOH H 7 .   ? 18.861  -1.344  11.600  1.00 18.54 ? 429 HOH A O   1 
HETATM 2212 O  O   . HOH H 7 .   ? 6.835   -14.772 28.881  1.00 23.92 ? 430 HOH A O   1 
HETATM 2213 O  O   . HOH H 7 .   ? 1.935   -2.496  41.523  1.00 34.27 ? 431 HOH A O   1 
HETATM 2214 O  O   . HOH H 7 .   ? 32.421  -4.994  22.579  1.00 28.22 ? 432 HOH A O   1 
HETATM 2215 O  O   . HOH H 7 .   ? 25.734  -1.611  26.490  1.00 16.81 ? 433 HOH A O   1 
HETATM 2216 O  O   . HOH H 7 .   ? 24.019  -2.391  7.939   1.00 24.43 ? 434 HOH A O   1 
HETATM 2217 O  O   . HOH H 7 .   ? 0.222   7.750   32.627  1.00 23.73 ? 435 HOH A O   1 
HETATM 2218 O  O   . HOH H 7 .   ? 21.462  -17.662 11.096  1.00 27.84 ? 436 HOH A O   1 
HETATM 2219 O  O   . HOH H 7 .   ? 6.343   21.793  17.549  1.00 30.11 ? 437 HOH A O   1 
HETATM 2220 O  O   . HOH H 7 .   ? 25.046  7.065   29.635  1.00 19.10 ? 438 HOH A O   1 
HETATM 2221 O  O   . HOH H 7 .   ? 37.032  5.427   15.450  1.00 26.63 ? 439 HOH A O   1 
HETATM 2222 O  O   . HOH H 7 .   ? -5.764  -8.637  14.869  1.00 33.67 ? 440 HOH A O   1 
HETATM 2223 O  O   . HOH H 7 .   ? 10.916  -16.392 17.120  1.00 17.68 ? 441 HOH A O   1 
HETATM 2224 O  O   . HOH H 7 .   ? 13.248  -13.574 11.390  1.00 9.61  ? 442 HOH A O   1 
HETATM 2225 O  O   . HOH H 7 .   ? -4.811  7.979   26.897  1.00 25.27 ? 443 HOH A O   1 
HETATM 2226 O  O   . HOH H 7 .   ? 13.202  9.016   27.892  1.00 24.64 ? 444 HOH A O   1 
HETATM 2227 O  O   . HOH H 7 .   ? 36.420  5.516   20.974  1.00 35.87 ? 445 HOH A O   1 
HETATM 2228 O  O   . HOH H 7 .   ? 15.035  19.436  27.312  1.00 34.62 ? 446 HOH A O   1 
HETATM 2229 O  O   . HOH H 7 .   ? 20.016  -2.185  15.750  1.00 8.58  ? 447 HOH A O   1 
HETATM 2230 O  O   . HOH H 7 .   ? 1.669   -18.826 4.961   1.00 20.72 ? 448 HOH A O   1 
HETATM 2231 O  O   . HOH H 7 .   ? 20.855  15.964  16.234  1.00 28.09 ? 449 HOH A O   1 
HETATM 2232 O  O   . HOH H 7 .   ? 23.590  9.969   27.659  1.00 31.20 ? 450 HOH A O   1 
HETATM 2233 O  O   . HOH H 7 .   ? 10.055  -17.610 7.129   1.00 29.59 ? 451 HOH A O   1 
HETATM 2234 O  O   . HOH H 7 .   ? 5.083   17.784  23.657  1.00 18.92 ? 452 HOH A O   1 
HETATM 2235 O  O   . HOH H 7 .   ? 29.574  5.075   27.713  1.00 25.61 ? 453 HOH A O   1 
HETATM 2236 O  O   . HOH H 7 .   ? 18.743  -6.900  29.272  1.00 12.24 ? 454 HOH A O   1 
HETATM 2237 O  O   . HOH H 7 .   ? 21.561  3.030   34.627  1.00 28.22 ? 455 HOH A O   1 
HETATM 2238 O  O   . HOH H 7 .   ? 0.347   10.179  30.186  1.00 27.84 ? 456 HOH A O   1 
HETATM 2239 O  O   . HOH H 7 .   ? 7.052   12.457  27.817  1.00 21.13 ? 457 HOH A O   1 
HETATM 2240 O  O   . HOH H 7 .   ? 10.553  10.620  25.707  1.00 11.02 ? 458 HOH A O   1 
HETATM 2241 O  O   . HOH H 7 .   ? 16.224  2.726   10.064  1.00 23.94 ? 459 HOH A O   1 
HETATM 2242 O  O   . HOH H 7 .   ? 23.937  -11.186 5.214   1.00 29.03 ? 460 HOH A O   1 
HETATM 2243 O  O   . HOH H 7 .   ? 22.304  16.822  24.466  1.00 30.20 ? 461 HOH A O   1 
HETATM 2244 O  O   . HOH H 7 .   ? -0.479  17.739  3.731   1.00 35.96 ? 462 HOH A O   1 
HETATM 2245 O  O   . HOH H 7 .   ? 21.213  0.974   -4.826  1.00 26.08 ? 463 HOH A O   1 
HETATM 2246 O  O   . HOH H 7 .   ? 3.113   12.274  11.412  1.00 18.28 ? 464 HOH A O   1 
HETATM 2247 O  O   . HOH H 7 .   ? -4.597  11.639  13.633  1.00 30.19 ? 465 HOH A O   1 
HETATM 2248 O  O   . HOH H 7 .   ? 15.316  -2.780  -6.506  1.00 27.87 ? 466 HOH A O   1 
HETATM 2249 O  O   . HOH H 7 .   ? -0.464  7.530   4.680   1.00 14.86 ? 467 HOH A O   1 
HETATM 2250 O  O   . HOH H 7 .   ? 16.520  -10.086 32.121  1.00 22.70 ? 468 HOH A O   1 
HETATM 2251 O  O   . HOH H 7 .   ? 7.923   -20.520 11.678  1.00 28.82 ? 469 HOH A O   1 
HETATM 2252 O  O   . HOH H 7 .   ? 16.707  -11.686 18.031  1.00 8.38  ? 470 HOH A O   1 
HETATM 2253 O  O   . HOH H 7 .   ? 17.713  -9.292  20.909  1.00 11.53 ? 471 HOH A O   1 
HETATM 2254 O  O   . HOH H 7 .   ? 3.204   -18.654 8.035   1.00 11.68 ? 472 HOH A O   1 
HETATM 2255 O  O   . HOH H 7 .   ? 34.618  2.199   24.580  1.00 18.93 ? 473 HOH A O   1 
HETATM 2256 O  O   . HOH H 7 .   ? 10.989  15.558  8.928   1.00 30.22 ? 474 HOH A O   1 
HETATM 2257 O  O   . HOH H 7 .   ? 12.495  2.555   -6.674  1.00 25.15 ? 475 HOH A O   1 
HETATM 2258 O  O   . HOH H 7 .   ? 4.188   -6.524  20.537  1.00 7.56  ? 476 HOH A O   1 
HETATM 2259 O  O   . HOH H 7 .   ? -4.988  -4.594  13.218  1.00 23.89 ? 477 HOH A O   1 
HETATM 2260 O  O   . HOH H 7 .   ? -1.507  -3.933  2.767   1.00 23.38 ? 478 HOH A O   1 
HETATM 2261 O  O   . HOH H 7 .   ? -5.988  -11.021 20.231  1.00 28.44 ? 479 HOH A O   1 
HETATM 2262 O  O   . HOH H 7 .   ? 22.531  -9.907  25.133  1.00 22.12 ? 480 HOH A O   1 
HETATM 2263 O  O   . HOH H 7 .   ? 23.160  -13.801 9.293   1.00 24.46 ? 481 HOH A O   1 
HETATM 2264 O  O   . HOH H 7 .   ? 36.566  -0.762  14.435  1.00 17.95 ? 482 HOH A O   1 
HETATM 2265 O  O   . HOH H 7 .   ? 17.795  -11.412 25.310  1.00 11.52 ? 483 HOH A O   1 
HETATM 2266 O  O   . HOH H 7 .   ? 27.994  -9.098  14.685  1.00 38.48 ? 484 HOH A O   1 
HETATM 2267 O  O   . HOH H 7 .   ? 15.154  5.744   -5.974  1.00 34.30 ? 485 HOH A O   1 
HETATM 2268 O  O   . HOH H 7 .   ? 26.661  8.995   20.108  1.00 20.92 ? 486 HOH A O   1 
HETATM 2269 O  O   . HOH H 7 .   ? -2.833  -0.484  29.106  1.00 29.29 ? 487 HOH A O   1 
HETATM 2270 O  O   . HOH H 7 .   ? -2.046  -1.094  6.614   1.00 20.02 ? 488 HOH A O   1 
HETATM 2271 O  O   . HOH H 7 .   ? 17.496  -14.026 24.443  1.00 11.76 ? 489 HOH A O   1 
HETATM 2272 O  O   . HOH H 7 .   ? 32.486  3.536   26.053  1.00 22.39 ? 490 HOH A O   1 
HETATM 2273 O  O   . HOH H 7 .   ? 4.835   -8.135  32.972  1.00 15.93 ? 491 HOH A O   1 
HETATM 2274 O  O   . HOH H 7 .   ? 5.448   10.993  -1.948  1.00 22.85 ? 492 HOH A O   1 
HETATM 2275 O  O   . HOH H 7 .   ? -0.433  -5.199  23.617  1.00 11.74 ? 493 HOH A O   1 
HETATM 2276 O  O   . HOH H 7 .   ? 0.069   9.735   1.767   1.00 17.91 ? 494 HOH A O   1 
HETATM 2277 O  O   . HOH H 7 .   ? 17.615  -11.151 -2.854  1.00 27.95 ? 495 HOH A O   1 
HETATM 2278 O  O   . HOH H 7 .   ? 20.068  11.216  28.132  1.00 27.76 ? 496 HOH A O   1 
HETATM 2279 O  O   . HOH H 7 .   ? 1.518   19.247  6.212   1.00 20.59 ? 497 HOH A O   1 
HETATM 2280 O  O   . HOH H 7 .   ? 5.111   -10.500 24.514  1.00 15.75 ? 498 HOH A O   1 
HETATM 2281 O  O   . HOH H 7 .   ? 11.216  16.496  12.129  1.00 20.41 ? 499 HOH A O   1 
HETATM 2282 O  O   . HOH H 7 .   ? 20.760  12.764  23.580  1.00 17.34 ? 500 HOH A O   1 
HETATM 2283 O  O   . HOH H 7 .   ? 7.620   21.800  14.860  1.00 24.07 ? 501 HOH A O   1 
HETATM 2284 O  O   . HOH H 7 .   ? 22.670  -4.475  34.605  1.00 22.49 ? 502 HOH A O   1 
HETATM 2285 O  O   . HOH H 7 .   ? 0.710   12.816  26.624  1.00 16.76 ? 503 HOH A O   1 
HETATM 2286 O  O   . HOH H 7 .   ? 8.387   -7.121  -3.168  1.00 23.65 ? 504 HOH A O   1 
HETATM 2287 O  O   . HOH H 7 .   ? -0.380  -4.989  -1.607  1.00 32.93 ? 505 HOH A O   1 
HETATM 2288 O  O   . HOH H 7 .   ? 23.861  -9.413  9.543   1.00 24.33 ? 506 HOH A O   1 
HETATM 2289 O  O   . HOH H 7 .   ? 6.318   11.180  31.892  1.00 35.28 ? 507 HOH A O   1 
HETATM 2290 O  O   . HOH H 7 .   ? -3.684  14.074  6.391   1.00 30.28 ? 508 HOH A O   1 
HETATM 2291 O  O   . HOH H 7 .   ? -3.779  -5.877  9.139   1.00 16.17 ? 509 HOH A O   1 
HETATM 2292 O  O   . HOH H 7 .   ? 17.176  2.643   13.816  1.00 20.87 ? 510 HOH A O   1 
HETATM 2293 O  O   . HOH H 7 .   ? 12.523  -18.130 26.846  1.00 28.88 ? 511 HOH A O   1 
HETATM 2294 O  O   . HOH H 7 .   ? 1.810   11.918  8.968   1.00 15.05 ? 512 HOH A O   1 
HETATM 2295 O  O   . HOH H 7 .   ? -2.898  1.160   26.486  1.00 17.45 ? 513 HOH A O   1 
HETATM 2296 O  O   . HOH H 7 .   ? 15.254  -9.642  36.540  1.00 32.59 ? 514 HOH A O   1 
HETATM 2297 O  O   . HOH H 7 .   ? 29.107  -3.882  -10.594 1.00 24.28 ? 515 HOH A O   1 
HETATM 2298 O  O   . HOH H 7 .   ? -2.124  1.101   34.478  1.00 26.81 ? 516 HOH A O   1 
HETATM 2299 O  O   . HOH H 7 .   ? -0.842  -12.380 18.828  1.00 28.91 ? 517 HOH A O   1 
HETATM 2300 O  O   . HOH H 7 .   ? 2.313   13.994  12.967  1.00 23.06 ? 518 HOH A O   1 
HETATM 2301 O  O   . HOH H 7 .   ? 2.535   -1.844  -2.639  1.00 29.15 ? 519 HOH A O   1 
HETATM 2302 O  O   . HOH H 7 .   ? 17.005  -6.846  31.390  1.00 23.44 ? 520 HOH A O   1 
HETATM 2303 O  O   . HOH H 7 .   ? 13.948  -6.934  32.779  1.00 17.07 ? 521 HOH A O   1 
HETATM 2304 O  O   . HOH H 7 .   ? -6.595  4.501   23.486  1.00 31.66 ? 522 HOH A O   1 
HETATM 2305 O  O   . HOH H 7 .   ? 8.516   14.735  29.120  1.00 30.41 ? 523 HOH A O   1 
HETATM 2306 O  O   . HOH H 7 .   ? -5.728  -2.148  25.211  1.00 22.87 ? 524 HOH A O   1 
HETATM 2307 O  O   . HOH H 7 .   ? 15.350  17.182  11.942  1.00 27.66 ? 525 HOH A O   1 
HETATM 2308 O  O   . HOH H 7 .   ? 8.101   -15.069 26.516  1.00 22.34 ? 526 HOH A O   1 
HETATM 2309 O  O   . HOH H 7 .   ? 12.114  -4.227  35.982  1.00 18.48 ? 527 HOH A O   1 
HETATM 2310 O  O   . HOH H 7 .   ? 22.417  0.213   29.583  1.00 13.21 ? 528 HOH A O   1 
HETATM 2311 O  O   . HOH H 7 .   ? 6.987   16.412  27.030  1.00 29.12 ? 529 HOH A O   1 
HETATM 2312 O  O   . HOH H 7 .   ? 15.013  -17.909 23.956  1.00 29.32 ? 530 HOH A O   1 
HETATM 2313 O  O   . HOH H 7 .   ? 0.985   4.126   -3.154  1.00 43.30 ? 531 HOH A O   1 
HETATM 2314 O  O   . HOH H 7 .   ? 11.436  -6.302  34.015  1.00 24.40 ? 532 HOH A O   1 
HETATM 2315 O  O   . HOH H 7 .   ? 8.493   10.103  28.924  1.00 31.73 ? 533 HOH A O   1 
HETATM 2316 O  O   . HOH H 7 .   ? 7.822   -16.756 14.812  1.00 26.41 ? 534 HOH A O   1 
HETATM 2317 O  O   . HOH H 7 .   ? 13.885  7.958   6.862   1.00 27.14 ? 535 HOH A O   1 
HETATM 2318 O  O   . HOH H 7 .   ? 25.928  -4.589  7.883   1.00 32.99 ? 536 HOH A O   1 
HETATM 2319 O  O   . HOH H 7 .   ? 3.815   -14.687 21.863  1.00 31.09 ? 537 HOH A O   1 
HETATM 2320 O  O   . HOH H 7 .   ? 2.517   -7.257  34.496  1.00 24.57 ? 538 HOH A O   1 
HETATM 2321 O  O   . HOH H 7 .   ? 30.769  3.898   12.143  1.00 34.58 ? 539 HOH A O   1 
HETATM 2322 O  O   . HOH H 7 .   ? 22.426  10.739  24.504  1.00 16.96 ? 540 HOH A O   1 
HETATM 2323 O  O   . HOH H 7 .   ? 10.196  19.310  12.111  1.00 38.06 ? 541 HOH A O   1 
HETATM 2324 O  O   . HOH H 7 .   ? -4.052  6.457   8.311   1.00 29.51 ? 542 HOH A O   1 
HETATM 2325 O  O   . HOH H 7 .   ? 35.287  7.585   19.148  1.00 37.40 ? 543 HOH A O   1 
HETATM 2326 O  O   . HOH H 7 .   ? 25.340  -0.586  28.804  1.00 24.47 ? 544 HOH A O   1 
HETATM 2327 O  O   . HOH H 7 .   ? 20.031  -15.901 18.046  1.00 25.47 ? 545 HOH A O   1 
HETATM 2328 O  O   . HOH H 7 .   ? 16.504  -14.075 0.612   1.00 25.18 ? 546 HOH A O   1 
HETATM 2329 O  O   . HOH H 7 .   ? 34.332  -1.914  13.587  1.00 22.99 ? 547 HOH A O   1 
HETATM 2330 O  O   . HOH H 7 .   ? -0.931  -16.671 13.734  1.00 22.85 ? 548 HOH A O   1 
HETATM 2331 O  O   . HOH H 7 .   ? 13.177  -20.396 10.307  1.00 21.51 ? 549 HOH A O   1 
HETATM 2332 O  O   . HOH H 7 .   ? 20.818  -6.776  32.417  1.00 28.84 ? 550 HOH A O   1 
HETATM 2333 O  O   . HOH H 7 .   ? 34.364  -3.951  24.714  1.00 25.09 ? 551 HOH A O   1 
HETATM 2334 O  O   . HOH H 7 .   ? -2.447  1.013   3.773   1.00 22.33 ? 552 HOH A O   1 
HETATM 2335 O  O   . HOH H 7 .   ? 4.253   -5.475  40.092  1.00 30.28 ? 553 HOH A O   1 
HETATM 2336 O  O   . HOH H 7 .   ? -0.015  20.831  13.834  1.00 31.49 ? 554 HOH A O   1 
HETATM 2337 O  O   . HOH H 7 .   ? 28.846  8.057   21.818  1.00 17.25 ? 555 HOH A O   1 
HETATM 2338 O  O   . HOH H 7 .   ? 19.193  -10.512 23.015  1.00 12.22 ? 556 HOH A O   1 
HETATM 2339 O  O   . HOH H 7 .   ? 23.037  -2.483  -12.355 1.00 32.47 ? 557 HOH A O   1 
HETATM 2340 O  O   . HOH H 7 .   ? -3.570  -7.586  2.058   1.00 24.78 ? 558 HOH A O   1 
HETATM 2341 O  O   . HOH H 7 .   ? 24.078  -12.332 -5.970  1.00 42.11 ? 559 HOH A O   1 
HETATM 2342 O  O   . HOH H 7 .   ? 21.834  -12.451 30.256  1.00 30.73 ? 560 HOH A O   1 
HETATM 2343 O  O   . HOH H 7 .   ? 13.087  -17.549 21.743  1.00 19.77 ? 561 HOH A O   1 
HETATM 2344 O  O   . HOH H 7 .   ? -3.163  -15.931 6.583   1.00 30.05 ? 562 HOH A O   1 
HETATM 2345 O  O   . HOH H 7 .   ? 14.035  -15.055 1.401   1.00 25.59 ? 563 HOH A O   1 
HETATM 2346 O  O   . HOH H 7 .   ? 21.115  -12.500 22.395  1.00 27.25 ? 564 HOH A O   1 
HETATM 2347 O  O   . HOH H 7 .   ? -0.059  -17.693 6.565   1.00 24.46 ? 565 HOH A O   1 
HETATM 2348 O  O   . HOH H 7 .   ? 19.315  -11.448 27.705  1.00 24.50 ? 566 HOH A O   1 
HETATM 2349 O  O   . HOH H 7 .   ? 9.345   4.834   30.964  1.00 24.91 ? 567 HOH A O   1 
HETATM 2350 O  O   . HOH H 7 .   ? 14.912  -17.454 5.315   1.00 26.74 ? 568 HOH A O   1 
HETATM 2351 O  O   . HOH H 7 .   ? 6.739   -2.939  -6.498  1.00 27.59 ? 569 HOH A O   1 
HETATM 2352 O  O   . HOH H 7 .   ? 12.671  -15.413 34.915  1.00 30.52 ? 570 HOH A O   1 
HETATM 2353 O  O   . HOH H 7 .   ? 8.466   -15.409 16.897  1.00 20.64 ? 571 HOH A O   1 
HETATM 2354 O  O   . HOH H 7 .   ? 3.247   5.950   -3.862  1.00 28.88 ? 572 HOH A O   1 
HETATM 2355 O  O   . HOH H 7 .   ? 17.363  1.136   11.706  1.00 26.52 ? 573 HOH A O   1 
HETATM 2356 O  O   . HOH H 7 .   ? 16.119  4.360   12.080  1.00 36.07 ? 574 HOH A O   1 
HETATM 2357 O  O   . HOH H 7 .   ? 31.491  -0.651  13.837  1.00 34.14 ? 575 HOH A O   1 
HETATM 2358 O  O   . HOH H 7 .   ? 2.465   16.377  2.717   1.00 38.46 ? 576 HOH A O   1 
HETATM 2359 O  O   . HOH H 7 .   ? 19.834  13.331  26.023  1.00 24.04 ? 577 HOH A O   1 
HETATM 2360 O  O   . HOH H 7 .   ? 3.734   -21.319 4.111   1.00 27.03 ? 578 HOH A O   1 
HETATM 2361 O  O   . HOH H 7 .   ? 17.331  5.600   10.296  1.00 38.45 ? 579 HOH A O   1 
HETATM 2362 O  O   . HOH H 7 .   ? -1.165  -10.960 24.371  1.00 35.66 ? 580 HOH A O   1 
HETATM 2363 O  O   . HOH H 7 .   ? 12.599  0.367   41.420  1.00 31.02 ? 581 HOH A O   1 
HETATM 2364 O  O   . HOH H 7 .   ? -0.851  -0.611  -3.846  1.00 32.03 ? 582 HOH A O   1 
HETATM 2365 O  O   . HOH H 7 .   ? 18.408  -15.818 5.205   1.00 32.25 ? 583 HOH A O   1 
HETATM 2366 O  O   . HOH H 7 .   ? 24.090  -11.315 8.171   1.00 32.61 ? 584 HOH A O   1 
HETATM 2367 O  O   . HOH H 7 .   ? 3.840   2.197   -3.737  1.00 32.12 ? 585 HOH A O   1 
HETATM 2368 O  O   . HOH H 7 .   ? 3.455   21.650  17.691  1.00 30.68 ? 586 HOH A O   1 
HETATM 2369 O  O   . HOH H 7 .   ? -5.414  -4.321  5.053   1.00 38.99 ? 587 HOH A O   1 
HETATM 2370 O  O   . HOH H 7 .   ? -10.528 7.505   13.113  1.00 36.97 ? 588 HOH A O   1 
HETATM 2371 O  O   . HOH H 7 .   ? 21.414  2.806   -6.674  1.00 33.01 ? 589 HOH A O   1 
HETATM 2372 O  O   . HOH H 7 .   ? 3.920   -12.223 37.450  1.00 30.31 ? 590 HOH A O   1 
HETATM 2373 O  O   . HOH H 7 .   ? 21.787  5.416   2.372   1.00 35.93 ? 591 HOH A O   1 
HETATM 2374 O  O   . HOH H 7 .   ? 4.937   17.216  3.238   1.00 39.35 ? 592 HOH A O   1 
HETATM 2375 O  O   . HOH H 7 .   ? 35.818  1.803   15.024  1.00 29.02 ? 593 HOH A O   1 
HETATM 2376 O  O   . HOH H 7 .   ? 19.406  -15.516 25.295  1.00 28.14 ? 594 HOH A O   1 
HETATM 2377 O  O   . HOH H 7 .   ? 16.346  22.118  21.491  1.00 27.89 ? 595 HOH A O   1 
HETATM 2378 O  O   . HOH H 7 .   ? 19.224  -10.288 31.455  1.00 29.40 ? 596 HOH A O   1 
HETATM 2379 O  O   . HOH H 7 .   ? -6.686  6.706   25.319  1.00 27.07 ? 597 HOH A O   1 
HETATM 2380 O  O   . HOH H 7 .   ? 33.431  -4.706  8.151   1.00 30.41 ? 598 HOH A O   1 
HETATM 2381 O  O   . HOH H 7 .   ? -11.992 6.321   11.400  1.00 36.02 ? 599 HOH A O   1 
HETATM 2382 O  O   . HOH H 7 .   ? 23.260  -8.021  30.623  1.00 33.66 ? 600 HOH A O   1 
HETATM 2383 O  O   . HOH H 7 .   ? -6.010  -4.658  8.074   1.00 40.87 ? 601 HOH A O   1 
HETATM 2384 O  O   . HOH H 7 .   ? 36.581  0.526   26.005  1.00 27.10 ? 602 HOH A O   1 
HETATM 2385 O  O   . HOH H 7 .   ? 9.525   12.631  0.764   1.00 33.06 ? 603 HOH A O   1 
HETATM 2386 O  O   . HOH H 7 .   ? -2.788  -5.026  0.133   1.00 34.94 ? 604 HOH A O   1 
HETATM 2387 O  O   . HOH H 7 .   ? -1.304  14.223  27.185  1.00 35.75 ? 605 HOH A O   1 
HETATM 2388 O  O   . HOH H 7 .   ? 23.272  -12.523 20.603  1.00 31.20 ? 606 HOH A O   1 
HETATM 2389 O  O   . HOH H 7 .   ? 15.397  -8.611  39.449  1.00 30.69 ? 607 HOH A O   1 
HETATM 2390 O  O   . HOH H 7 .   ? 22.747  -15.595 7.176   1.00 33.02 ? 608 HOH A O   1 
HETATM 2391 O  O   . HOH H 7 .   ? 16.726  -7.970  33.636  1.00 43.38 ? 609 HOH A O   1 
HETATM 2392 O  O   . HOH H 7 .   ? 4.301   -12.135 26.673  1.00 28.01 ? 610 HOH A O   1 
HETATM 2393 O  O   . HOH H 7 .   ? 16.660  2.999   43.360  1.00 33.90 ? 611 HOH A O   1 
HETATM 2394 O  O   . HOH H 7 .   ? 3.143   -10.586 31.650  1.00 27.69 ? 612 HOH A O   1 
HETATM 2395 O  O   . HOH H 7 .   ? 20.171  -9.338  29.030  1.00 18.62 ? 613 HOH A O   1 
HETATM 2396 O  O   . HOH H 7 .   ? 27.634  7.156   28.746  1.00 29.38 ? 614 HOH A O   1 
HETATM 2397 O  O   . HOH H 7 .   ? 35.347  0.428   28.524  1.00 33.46 ? 615 HOH A O   1 
HETATM 2398 O  O   . HOH H 7 .   ? 27.695  10.473  17.850  1.00 30.50 ? 616 HOH A O   1 
HETATM 2399 O  O   . HOH H 7 .   ? 26.726  11.078  21.937  1.00 31.55 ? 617 HOH A O   1 
HETATM 2400 O  O   . HOH H 7 .   ? 24.991  11.804  23.801  1.00 22.73 ? 618 HOH A O   1 
# 
