data_5DOG
# 
_entry.id   5DOG 
# 
_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   5DOG         pdb_00005dog 10.2210/pdb5dog/pdb 
WWPDB D_1000213517 ?            ?                   
# 
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 2016-09-28 
2 'Structure model' 1 1 2017-01-18 
3 'Structure model' 1 2 2017-02-01 
4 'Structure model' 1 3 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 4 'Structure model' 'Database references'    
5 4 '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' chem_comp_atom                
2 4 'Structure model' chem_comp_bond                
3 4 'Structure model' database_2                    
4 4 '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' '_database_2.pdbx_DOI'                
2 4 '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                        5DOG 
_pdbx_database_status.recvd_initial_deposition_date   2015-09-11 
_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            ? 
# 
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   ?       ? 
'2-[(2-Phenylethyl)amino]-3,5,6-trifluoro-4-[(2-phenylethyl)thio]-benzenesulfonamide' ? 
3 non-polymer syn BICINE                                                                          163.172   1   ?       ? Zn ? 
4 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                          195.237   1   ?       ? BICINE ? 
5 non-polymer syn '2-(benzylamino)-3,5,6-trifluoro-4-[(2-phenylethyl)sulfanyl]benzenesulfonamide' 452.513   1   ?       ? 
'N-(EHTYLSULFITE)MORPHOLINE'                                                          ? 
6 water       nat water                                                                           18.015    294 ?       ? ? ? 
# 
_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 BICINE                                                                          BCN 
4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                          MES 
5 '2-(benzylamino)-3,5,6-trifluoro-4-[(2-phenylethyl)sulfanyl]benzenesulfonamide' 5DT 
6 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 
5DT non-polymer         . '2-(benzylamino)-3,5,6-trifluoro-4-[(2-phenylethyl)sulfanyl]benzenesulfonamide' ? 'C21 H19 F3 N2 O2 S2' 
452.513 
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 
BCN non-polymer         . BICINE                                                                          ? 'C6 H13 N O4'         
163.172 
CYS 'L-peptide linking' y CYSTEINE                                                                        ? 'C3 H7 N O2 S'        
121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                       ? 'C5 H10 N2 O3'        
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                 ? 'C5 H9 N O4'          
147.129 
GLY 'peptide linking'   y GLYCINE                                                                         ? 'C2 H5 N O2'          
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                       ? 'C6 H10 N3 O2 1'      
156.162 
HOH non-polymer         . WATER                                                                           ? 'H2 O'                
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                      ? 'C6 H13 N O2'         
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                         ? 'C6 H13 N O2'         
131.173 
LYS 'L-peptide linking' y LYSINE                                                                          ? 'C6 H15 N2 O2 1'      
147.195 
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 
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 
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 BCN 1   302 1   BCN BCN A . 
D 4 MES 1   303 2   MES MES A . 
E 5 5DT 1   304 1   5DT XYX A . 
F 6 HOH 1   401 151 HOH HOH A . 
F 6 HOH 2   402 78  HOH HOH A . 
F 6 HOH 3   403 131 HOH HOH A . 
F 6 HOH 4   404 115 HOH HOH A . 
F 6 HOH 5   405 147 HOH HOH A . 
F 6 HOH 6   406 279 HOH HOH A . 
F 6 HOH 7   407 262 HOH HOH A . 
F 6 HOH 8   408 156 HOH HOH A . 
F 6 HOH 9   409 116 HOH HOH A . 
F 6 HOH 10  410 40  HOH HOH A . 
F 6 HOH 11  411 183 HOH HOH A . 
F 6 HOH 12  412 194 HOH HOH A . 
F 6 HOH 13  413 106 HOH HOH A . 
F 6 HOH 14  414 89  HOH HOH A . 
F 6 HOH 15  415 271 HOH HOH A . 
F 6 HOH 16  416 148 HOH HOH A . 
F 6 HOH 17  417 59  HOH HOH A . 
F 6 HOH 18  418 105 HOH HOH A . 
F 6 HOH 19  419 178 HOH HOH A . 
F 6 HOH 20  420 272 HOH HOH A . 
F 6 HOH 21  421 190 HOH HOH A . 
F 6 HOH 22  422 74  HOH HOH A . 
F 6 HOH 23  423 65  HOH HOH A . 
F 6 HOH 24  424 164 HOH HOH A . 
F 6 HOH 25  425 255 HOH HOH A . 
F 6 HOH 26  426 157 HOH HOH A . 
F 6 HOH 27  427 49  HOH HOH A . 
F 6 HOH 28  428 291 HOH HOH A . 
F 6 HOH 29  429 44  HOH HOH A . 
F 6 HOH 30  430 212 HOH HOH A . 
F 6 HOH 31  431 256 HOH HOH A . 
F 6 HOH 32  432 161 HOH HOH A . 
F 6 HOH 33  433 227 HOH HOH A . 
F 6 HOH 34  434 130 HOH HOH A . 
F 6 HOH 35  435 38  HOH HOH A . 
F 6 HOH 36  436 123 HOH HOH A . 
F 6 HOH 37  437 293 HOH HOH A . 
F 6 HOH 38  438 141 HOH HOH A . 
F 6 HOH 39  439 152 HOH HOH A . 
F 6 HOH 40  440 7   HOH HOH A . 
F 6 HOH 41  441 176 HOH HOH A . 
F 6 HOH 42  442 222 HOH HOH A . 
F 6 HOH 43  443 1   HOH HOH A . 
F 6 HOH 44  444 83  HOH HOH A . 
F 6 HOH 45  445 146 HOH HOH A . 
F 6 HOH 46  446 229 HOH HOH A . 
F 6 HOH 47  447 269 HOH HOH A . 
F 6 HOH 48  448 165 HOH HOH A . 
F 6 HOH 49  449 13  HOH HOH A . 
F 6 HOH 50  450 4   HOH HOH A . 
F 6 HOH 51  451 75  HOH HOH A . 
F 6 HOH 52  452 88  HOH HOH A . 
F 6 HOH 53  453 54  HOH HOH A . 
F 6 HOH 54  454 210 HOH HOH A . 
F 6 HOH 55  455 185 HOH HOH A . 
F 6 HOH 56  456 168 HOH HOH A . 
F 6 HOH 57  457 46  HOH HOH A . 
F 6 HOH 58  458 2   HOH HOH A . 
F 6 HOH 59  459 72  HOH HOH A . 
F 6 HOH 60  460 22  HOH HOH A . 
F 6 HOH 61  461 211 HOH HOH A . 
F 6 HOH 62  462 86  HOH HOH A . 
F 6 HOH 63  463 31  HOH HOH A . 
F 6 HOH 64  464 221 HOH HOH A . 
F 6 HOH 65  465 45  HOH HOH A . 
F 6 HOH 66  466 162 HOH HOH A . 
F 6 HOH 67  467 124 HOH HOH A . 
F 6 HOH 68  468 180 HOH HOH A . 
F 6 HOH 69  469 92  HOH HOH A . 
F 6 HOH 70  470 8   HOH HOH A . 
F 6 HOH 71  471 102 HOH HOH A . 
F 6 HOH 72  472 174 HOH HOH A . 
F 6 HOH 73  473 10  HOH HOH A . 
F 6 HOH 74  474 99  HOH HOH A . 
F 6 HOH 75  475 139 HOH HOH A . 
F 6 HOH 76  476 3   HOH HOH A . 
F 6 HOH 77  477 60  HOH HOH A . 
F 6 HOH 78  478 66  HOH HOH A . 
F 6 HOH 79  479 261 HOH HOH A . 
F 6 HOH 80  480 140 HOH HOH A . 
F 6 HOH 81  481 77  HOH HOH A . 
F 6 HOH 82  482 26  HOH HOH A . 
F 6 HOH 83  483 28  HOH HOH A . 
F 6 HOH 84  484 62  HOH HOH A . 
F 6 HOH 85  485 20  HOH HOH A . 
F 6 HOH 86  486 61  HOH HOH A . 
F 6 HOH 87  487 36  HOH HOH A . 
F 6 HOH 88  488 122 HOH HOH A . 
F 6 HOH 89  489 41  HOH HOH A . 
F 6 HOH 90  490 94  HOH HOH A . 
F 6 HOH 91  491 37  HOH HOH A . 
F 6 HOH 92  492 18  HOH HOH A . 
F 6 HOH 93  493 104 HOH HOH A . 
F 6 HOH 94  494 167 HOH HOH A . 
F 6 HOH 95  495 135 HOH HOH A . 
F 6 HOH 96  496 204 HOH HOH A . 
F 6 HOH 97  497 82  HOH HOH A . 
F 6 HOH 98  498 228 HOH HOH A . 
F 6 HOH 99  499 81  HOH HOH A . 
F 6 HOH 100 500 21  HOH HOH A . 
F 6 HOH 101 501 51  HOH HOH A . 
F 6 HOH 102 502 15  HOH HOH A . 
F 6 HOH 103 503 273 HOH HOH A . 
F 6 HOH 104 504 263 HOH HOH A . 
F 6 HOH 105 505 136 HOH HOH A . 
F 6 HOH 106 506 280 HOH HOH A . 
F 6 HOH 107 507 236 HOH HOH A . 
F 6 HOH 108 508 30  HOH HOH A . 
F 6 HOH 109 509 119 HOH HOH A . 
F 6 HOH 110 510 150 HOH HOH A . 
F 6 HOH 111 511 80  HOH HOH A . 
F 6 HOH 112 512 91  HOH HOH A . 
F 6 HOH 113 513 25  HOH HOH A . 
F 6 HOH 114 514 230 HOH HOH A . 
F 6 HOH 115 515 153 HOH HOH A . 
F 6 HOH 116 516 133 HOH HOH A . 
F 6 HOH 117 517 9   HOH HOH A . 
F 6 HOH 118 518 181 HOH HOH A . 
F 6 HOH 119 519 33  HOH HOH A . 
F 6 HOH 120 520 16  HOH HOH A . 
F 6 HOH 121 521 24  HOH HOH A . 
F 6 HOH 122 522 96  HOH HOH A . 
F 6 HOH 123 523 234 HOH HOH A . 
F 6 HOH 124 524 223 HOH HOH A . 
F 6 HOH 125 525 138 HOH HOH A . 
F 6 HOH 126 526 6   HOH HOH A . 
F 6 HOH 127 527 63  HOH HOH A . 
F 6 HOH 128 528 43  HOH HOH A . 
F 6 HOH 129 529 144 HOH HOH A . 
F 6 HOH 130 530 17  HOH HOH A . 
F 6 HOH 131 531 215 HOH HOH A . 
F 6 HOH 132 532 179 HOH HOH A . 
F 6 HOH 133 533 90  HOH HOH A . 
F 6 HOH 134 534 107 HOH HOH A . 
F 6 HOH 135 535 50  HOH HOH A . 
F 6 HOH 136 536 5   HOH HOH A . 
F 6 HOH 137 537 56  HOH HOH A . 
F 6 HOH 138 538 267 HOH HOH A . 
F 6 HOH 139 539 103 HOH HOH A . 
F 6 HOH 140 540 158 HOH HOH A . 
F 6 HOH 141 541 155 HOH HOH A . 
F 6 HOH 142 542 23  HOH HOH A . 
F 6 HOH 143 543 114 HOH HOH A . 
F 6 HOH 144 544 12  HOH HOH A . 
F 6 HOH 145 545 196 HOH HOH A . 
F 6 HOH 146 546 142 HOH HOH A . 
F 6 HOH 147 547 254 HOH HOH A . 
F 6 HOH 148 548 29  HOH HOH A . 
F 6 HOH 149 549 32  HOH HOH A . 
F 6 HOH 150 550 184 HOH HOH A . 
F 6 HOH 151 551 134 HOH HOH A . 
F 6 HOH 152 552 242 HOH HOH A . 
F 6 HOH 153 553 277 HOH HOH A . 
F 6 HOH 154 554 55  HOH HOH A . 
F 6 HOH 155 555 70  HOH HOH A . 
F 6 HOH 156 556 58  HOH HOH A . 
F 6 HOH 157 557 163 HOH HOH A . 
F 6 HOH 158 558 233 HOH HOH A . 
F 6 HOH 159 559 52  HOH HOH A . 
F 6 HOH 160 560 218 HOH HOH A . 
F 6 HOH 161 561 111 HOH HOH A . 
F 6 HOH 162 562 19  HOH HOH A . 
F 6 HOH 163 563 203 HOH HOH A . 
F 6 HOH 164 564 64  HOH HOH A . 
F 6 HOH 165 565 85  HOH HOH A . 
F 6 HOH 166 566 137 HOH HOH A . 
F 6 HOH 167 567 275 HOH HOH A . 
F 6 HOH 168 568 274 HOH HOH A . 
F 6 HOH 169 569 73  HOH HOH A . 
F 6 HOH 170 570 220 HOH HOH A . 
F 6 HOH 171 571 53  HOH HOH A . 
F 6 HOH 172 572 71  HOH HOH A . 
F 6 HOH 173 573 42  HOH HOH A . 
F 6 HOH 174 574 39  HOH HOH A . 
F 6 HOH 175 575 160 HOH HOH A . 
F 6 HOH 176 576 286 HOH HOH A . 
F 6 HOH 177 577 100 HOH HOH A . 
F 6 HOH 178 578 143 HOH HOH A . 
F 6 HOH 179 579 95  HOH HOH A . 
F 6 HOH 180 580 128 HOH HOH A . 
F 6 HOH 181 581 246 HOH HOH A . 
F 6 HOH 182 582 14  HOH HOH A . 
F 6 HOH 183 583 120 HOH HOH A . 
F 6 HOH 184 584 117 HOH HOH A . 
F 6 HOH 185 585 121 HOH HOH A . 
F 6 HOH 186 586 225 HOH HOH A . 
F 6 HOH 187 587 248 HOH HOH A . 
F 6 HOH 188 588 243 HOH HOH A . 
F 6 HOH 189 589 172 HOH HOH A . 
F 6 HOH 190 590 101 HOH HOH A . 
F 6 HOH 191 591 259 HOH HOH A . 
F 6 HOH 192 592 127 HOH HOH A . 
F 6 HOH 193 593 93  HOH HOH A . 
F 6 HOH 194 594 34  HOH HOH A . 
F 6 HOH 195 595 112 HOH HOH A . 
F 6 HOH 196 596 288 HOH HOH A . 
F 6 HOH 197 597 192 HOH HOH A . 
F 6 HOH 198 598 191 HOH HOH A . 
F 6 HOH 199 599 182 HOH HOH A . 
F 6 HOH 200 600 175 HOH HOH A . 
F 6 HOH 201 601 250 HOH HOH A . 
F 6 HOH 202 602 110 HOH HOH A . 
F 6 HOH 203 603 113 HOH HOH A . 
F 6 HOH 204 604 149 HOH HOH A . 
F 6 HOH 205 605 195 HOH HOH A . 
F 6 HOH 206 606 35  HOH HOH A . 
F 6 HOH 207 607 224 HOH HOH A . 
F 6 HOH 208 608 258 HOH HOH A . 
F 6 HOH 209 609 171 HOH HOH A . 
F 6 HOH 210 610 186 HOH HOH A . 
F 6 HOH 211 611 201 HOH HOH A . 
F 6 HOH 212 612 237 HOH HOH A . 
F 6 HOH 213 613 282 HOH HOH A . 
F 6 HOH 214 614 125 HOH HOH A . 
F 6 HOH 215 615 289 HOH HOH A . 
F 6 HOH 216 616 188 HOH HOH A . 
F 6 HOH 217 617 118 HOH HOH A . 
F 6 HOH 218 618 208 HOH HOH A . 
F 6 HOH 219 619 129 HOH HOH A . 
F 6 HOH 220 620 290 HOH HOH A . 
F 6 HOH 221 621 284 HOH HOH A . 
F 6 HOH 222 622 264 HOH HOH A . 
F 6 HOH 223 623 76  HOH HOH A . 
F 6 HOH 224 624 235 HOH HOH A . 
F 6 HOH 225 625 166 HOH HOH A . 
F 6 HOH 226 626 169 HOH HOH A . 
F 6 HOH 227 627 189 HOH HOH A . 
F 6 HOH 228 628 278 HOH HOH A . 
F 6 HOH 229 629 238 HOH HOH A . 
F 6 HOH 230 630 193 HOH HOH A . 
F 6 HOH 231 631 11  HOH HOH A . 
F 6 HOH 232 632 68  HOH HOH A . 
F 6 HOH 233 633 270 HOH HOH A . 
F 6 HOH 234 634 253 HOH HOH A . 
F 6 HOH 235 635 292 HOH HOH A . 
F 6 HOH 236 636 207 HOH HOH A . 
F 6 HOH 237 637 48  HOH HOH A . 
F 6 HOH 238 638 97  HOH HOH A . 
F 6 HOH 239 639 170 HOH HOH A . 
F 6 HOH 240 640 245 HOH HOH A . 
F 6 HOH 241 641 84  HOH HOH A . 
F 6 HOH 242 642 173 HOH HOH A . 
F 6 HOH 243 643 200 HOH HOH A . 
F 6 HOH 244 644 47  HOH HOH A . 
F 6 HOH 245 645 287 HOH HOH A . 
F 6 HOH 246 646 295 HOH HOH A . 
F 6 HOH 247 647 219 HOH HOH A . 
F 6 HOH 248 648 202 HOH HOH A . 
F 6 HOH 249 649 154 HOH HOH A . 
F 6 HOH 250 650 294 HOH HOH A . 
F 6 HOH 251 651 132 HOH HOH A . 
F 6 HOH 252 652 244 HOH HOH A . 
F 6 HOH 253 653 260 HOH HOH A . 
F 6 HOH 254 654 206 HOH HOH A . 
F 6 HOH 255 655 109 HOH HOH A . 
F 6 HOH 256 656 226 HOH HOH A . 
F 6 HOH 257 657 69  HOH HOH A . 
F 6 HOH 258 658 209 HOH HOH A . 
F 6 HOH 259 659 266 HOH HOH A . 
F 6 HOH 260 660 268 HOH HOH A . 
F 6 HOH 261 661 239 HOH HOH A . 
F 6 HOH 262 662 216 HOH HOH A . 
F 6 HOH 263 663 87  HOH HOH A . 
F 6 HOH 264 664 205 HOH HOH A . 
F 6 HOH 265 665 283 HOH HOH A . 
F 6 HOH 266 666 213 HOH HOH A . 
F 6 HOH 267 667 145 HOH HOH A . 
F 6 HOH 268 668 126 HOH HOH A . 
F 6 HOH 269 669 177 HOH HOH A . 
F 6 HOH 270 670 247 HOH HOH A . 
F 6 HOH 271 671 285 HOH HOH A . 
F 6 HOH 272 672 252 HOH HOH A . 
F 6 HOH 273 673 241 HOH HOH A . 
F 6 HOH 274 674 251 HOH HOH A . 
F 6 HOH 275 675 159 HOH HOH A . 
F 6 HOH 276 676 217 HOH HOH A . 
F 6 HOH 277 677 187 HOH HOH A . 
F 6 HOH 278 678 197 HOH HOH A . 
F 6 HOH 279 679 57  HOH HOH A . 
F 6 HOH 280 680 249 HOH HOH A . 
F 6 HOH 281 681 198 HOH HOH A . 
F 6 HOH 282 682 232 HOH HOH A . 
F 6 HOH 283 683 214 HOH HOH A . 
F 6 HOH 284 684 265 HOH HOH A . 
F 6 HOH 285 685 27  HOH HOH A . 
F 6 HOH 286 686 108 HOH HOH A . 
F 6 HOH 287 687 67  HOH HOH A . 
F 6 HOH 288 688 281 HOH HOH A . 
F 6 HOH 289 689 276 HOH HOH A . 
F 6 HOH 290 690 257 HOH HOH A . 
F 6 HOH 291 691 79  HOH HOH A . 
F 6 HOH 292 692 98  HOH HOH A . 
F 6 HOH 293 693 199 HOH HOH A . 
F 6 HOH 294 694 240 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   ? CB  ? A LYS 9  CB  
2  1 Y 1 A LYS 9   ? CG  ? A LYS 9  CG  
3  1 Y 1 A LYS 9   ? CD  ? A LYS 9  CD  
4  1 Y 1 A LYS 9   ? CE  ? A LYS 9  CE  
5  1 Y 1 A LYS 9   ? NZ  ? A LYS 9  NZ  
6  1 Y 1 A LYS 45  ? CE  ? A LYS 45 CE  
7  1 Y 1 A LYS 45  ? NZ  ? A LYS 45 NZ  
8  1 N 1 A MES 303 ? S   ? D MES 1  S   
9  1 N 1 A MES 303 ? O1S ? D MES 1  O1S 
10 1 N 1 A MES 303 ? O2S ? D MES 1  O2S 
11 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 scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.006    2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? .        3 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.290 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5DOG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.228 
_cell.length_a_esd                 ? 
_cell.length_b                     41.249 
_cell.length_b_esd                 ? 
_cell.length_c                     72.351 
_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                         5DOG 
_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                   5DOG 
_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            2.04 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.2 
_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              7.0 
_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: 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_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                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RIGAKU RAXIS IV++' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-08-08 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'VARIMAX-HF MIRROR' 
_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   1.5418 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate            17.023 
_reflns.entry_id                         5DOG 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.700 
_reflns.d_resolution_low                 22.871 
_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                       26789 
_reflns.number_obs                       26789 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.800 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.500 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.031 
_reflns.pdbx_netI_over_av_sigmaI         11.548 
_reflns.pdbx_netI_over_sigmaI            18.600 
_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                  0.049 
_reflns.pdbx_Rpim_I_all                  0.026 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         94591 
_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 
1.70 1.79  ? 3.6  13048 ? ? 3858 ? 99.20  ? ? ? 0.231 0.155 ? ? ? ? ? ? ? ? 3.40 0.155 ? ? 6.60  0.23 0.12 ? 1  1 ? ? 
1.79 1.90  ? 7.3  12864 ? ? 3679 ? 99.90  ? ? ? 0.118 0.083 ? ? ? ? ? ? ? ? 3.50 0.083 ? ? 10.10 0.12 0.06 ? 2  ? ? ? 
1.90 2.03  ? 11.1 12094 ? ? 3452 ? 100.00 ? ? ? 0.082 0.053 ? ? ? ? ? ? ? ? 3.50 0.053 ? ? 13.70 0.08 0.04 ? 3  ? ? ? 
2.03 2.19  ? 13.9 11540 ? ? 3243 ? 100.00 ? ? ? 0.065 0.039 ? ? ? ? ? ? ? ? 3.60 0.039 ? ? 17.60 0.06 0.03 ? 4  ? ? ? 
2.19 2.40  ? 16.4 10525 ? ? 2946 ? 100.00 ? ? ? 0.055 0.033 ? ? ? ? ? ? ? ? 3.60 0.033 ? ? 20.60 0.05 0.03 ? 5  ? ? ? 
2.40 2.69  ? 19.8 9788  ? ? 2710 ? 100.00 ? ? ? 0.047 0.028 ? ? ? ? ? ? ? ? 3.60 0.028 ? ? 22.50 0.05 0.03 ? 6  ? ? ? 
2.69 3.10  ? 22.5 8679  ? ? 2396 ? 100.00 ? ? ? 0.038 0.024 ? ? ? ? ? ? ? ? 3.60 0.024 ? ? 26.90 0.04 0.02 ? 7  ? ? ? 
3.10 3.80  ? 13.7 7344  ? ? 2023 ? 100.00 ? ? ? 0.043 0.028 ? ? ? ? ? ? ? ? 3.60 0.028 ? ? 31.40 0.04 0.02 ? 8  ? ? ? 
3.80 5.38  ? 21.1 5716  ? ? 1593 ? 100.00 ? ? ? 0.035 0.023 ? ? ? ? ? ? ? ? 3.60 0.023 ? ? 34.20 0.04 0.02 ? 9  ? ? ? 
5.38 22.87 ? 19.9 2993  ? ? 889  ? 98.60  ? ? ? 0.034 0.021 ? ? ? ? ? ? ? ? 3.40 0.021 ? ? 29.80 0.03 0.02 ? 10 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.290 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.070 
_refine.aniso_B[2][2]                            0.100 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.150 
_refine.B_iso_max                                67.71 
_refine.B_iso_mean                               16.753 
_refine.B_iso_min                                5.89 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.936 
_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                                 5DOG 
_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                            1.700 
_refine.ls_d_res_low                             22.870 
_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                     26778 
_refine.ls_number_reflns_R_free                  2737 
_refine.ls_number_reflns_R_work                  24041 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.810 
_refine.ls_percent_reflns_R_free                 10.200 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.167 
_refine.ls_R_factor_R_free                       0.214 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.162 
_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                      0.220 
_refine.ls_wR_factor_R_work                      0.169 
_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                       0.118 
_refine.pdbx_overall_ESU_R_Free                  0.121 
_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             0.119 
_refine.overall_SU_R_free                        0.121 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   0.887 
_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         50 
_refine_hist.number_atoms_solvent             294 
_refine_hist.number_atoms_total               2393 
_refine_hist.d_res_high                       1.700 
_refine_hist.d_res_low                        22.870 
# 
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' ? 0.021  0.020  2227 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.302  1.987  3028 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.993  5.000  265  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 34.319 24.800 100  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.162 15.000 355  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 24.140 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.161  0.200  306  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.021  1734 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.700 
_refine_ls_shell.d_res_low                        1.744 
_refine_ls_shell.number_reflns_all                1934 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             200 
_refine_ls_shell.number_reflns_R_work             1734 
_refine_ls_shell.percent_reflns_obs               99.030 
_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                  0.410 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.349 
_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                     5DOG 
_struct.title                        
;Crystal structure of human carbonic anhydrase isozyme II with 2-(Benzylamino)-3,5,6-trifluoro-4-[(2-phenylethyl)thio]benzene- sulfonamide
;
_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        5DOG 
_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 6 ? 
# 
_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              5DOG 
_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)' 640   ? 
1 MORE         8     ? 
1 'SSA (A^2)'  11420 ? 
# 
_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 
# 
_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 ? ? ? ? ? ? ? 1.987 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E 5DT . N10 A ? A ZN  301 A 5DT 304 1_555 ? ? ? ? ? ? ? 1.888 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E 5DT . N10 B ? A ZN  301 A 5DT 304 1_555 ? ? ? ? ? ? ? 1.882 ? ? 
metalc6 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E 5DT . S7  A ? A ZN  301 A 5DT 304 1_555 ? ? ? ? ? ? ? 2.834 ? ? 
metalc7 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E 5DT . S7  B ? A ZN  301 A 5DT 304 1_555 ? ? ? ? ? ? ? 2.931 ? ? 
# 
_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_555 107.8 ? 
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_555 114.0 ? 
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 97.3  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A E 5DT .   ? A 5DT 304 ? 1_555 110.1 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A E 5DT .   ? A 5DT 304 ? 1_555 103.5 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A E 5DT .   ? A 5DT 304 ? 1_555 121.7 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B E 5DT .   ? A 5DT 304 ? 1_555 108.0 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B E 5DT .   ? A 5DT 304 ? 1_555 107.1 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B E 5DT .   ? A 5DT 304 ? 1_555 121.3 ? 
10 N10 A E 5DT .   ? A 5DT 304 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B E 5DT .   ? A 5DT 304 ? 1_555 3.6   ? 
11 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  A E 5DT .   ? A 5DT 304 ? 1_555 99.0  ? 
12 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  A E 5DT .   ? A 5DT 304 ? 1_555 139.1 ? 
13 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  A E 5DT .   ? A 5DT 304 ? 1_555 99.3  ? 
14 N10 A E 5DT .   ? A 5DT 304 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  A E 5DT .   ? A 5DT 304 ? 1_555 36.9  ? 
15 N10 B E 5DT .   ? A 5DT 304 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  A E 5DT .   ? A 5DT 304 ? 1_555 33.6  ? 
16 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B E 5DT .   ? A 5DT 304 ? 1_555 95.8  ? 
17 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B E 5DT .   ? A 5DT 304 ? 1_555 140.9 ? 
18 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B E 5DT .   ? A 5DT 304 ? 1_555 100.9 ? 
19 N10 A E 5DT .   ? A 5DT 304 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B E 5DT .   ? A 5DT 304 ? 1_555 38.0  ? 
20 N10 B E 5DT .   ? A 5DT 304 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B E 5DT .   ? A 5DT 304 ? 1_555 34.6  ? 
21 S7  A E 5DT .   ? A 5DT 304 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B E 5DT .   ? A 5DT 304 ? 1_555 3.1   ? 
# 
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 -3.91 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 5.59  
# 
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  THR A 87  ? TRP A 97  ? THR A 87  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  THR A 87  ? TRP A 97  ? THR A 87  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 LEU A 211 ? O LEU A 212 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 ARG A 58  ? N ARG A 58  
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 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
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 BCN 302 ? 9  'binding site for residue BCN A 302' 
AC3 Software A MES 303 ? 6  'binding site for residue MES A 303' 
AC4 Software A 5DT 304 ? 25 'binding site for residue 5DT A 304' 
# 
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  5DT E .   ? 5DT A 304 . ? 1_555 ? 
5  AC2 9  LYS A 148 ? LYS A 149 . ? 1_555 ? 
6  AC2 9  LYS A 212 ? LYS A 213 . ? 1_555 ? 
7  AC2 9  GLU A 213 ? GLU A 214 . ? 1_555 ? 
8  AC2 9  PRO A 214 ? PRO A 215 . ? 1_555 ? 
9  AC2 9  HOH F .   ? HOH A 410 . ? 1_555 ? 
10 AC2 9  HOH F .   ? HOH A 464 . ? 1_555 ? 
11 AC2 9  HOH F .   ? HOH A 465 . ? 1_555 ? 
12 AC2 9  HOH F .   ? HOH A 576 . ? 1_555 ? 
13 AC2 9  HOH F .   ? HOH A 591 . ? 1_555 ? 
14 AC3 6  LEU A 163 ? LEU A 164 . ? 1_555 ? 
15 AC3 6  ASP A 164 ? ASP A 165 . ? 1_555 ? 
16 AC3 6  LYS A 167 ? LYS A 168 . ? 1_555 ? 
17 AC3 6  LYS A 224 ? LYS A 225 . ? 1_555 ? 
18 AC3 6  LEU A 228 ? LEU A 229 . ? 1_555 ? 
19 AC3 6  HOH F .   ? HOH A 532 . ? 1_555 ? 
20 AC4 25 TRP A 5   ? TRP A 5   . ? 1_555 ? 
21 AC4 25 TYR A 7   ? TYR A 7   . ? 1_555 ? 
22 AC4 25 HIS A 64  ? HIS A 64  . ? 1_555 ? 
23 AC4 25 ALA A 65  ? ALA A 65  . ? 1_555 ? 
24 AC4 25 GLN A 92  ? GLN A 92  . ? 1_555 ? 
25 AC4 25 HIS A 94  ? HIS A 94  . ? 1_555 ? 
26 AC4 25 HIS A 96  ? HIS A 96  . ? 1_555 ? 
27 AC4 25 HIS A 119 ? HIS A 119 . ? 1_555 ? 
28 AC4 25 VAL A 121 ? VAL A 121 . ? 1_555 ? 
29 AC4 25 PHE A 130 ? PHE A 131 . ? 1_555 ? 
30 AC4 25 LEU A 140 ? LEU A 141 . ? 1_555 ? 
31 AC4 25 VAL A 142 ? VAL A 143 . ? 1_555 ? 
32 AC4 25 LEU A 197 ? LEU A 198 . ? 1_555 ? 
33 AC4 25 THR A 198 ? THR A 199 . ? 1_555 ? 
34 AC4 25 THR A 199 ? THR A 200 . ? 1_555 ? 
35 AC4 25 PRO A 201 ? PRO A 202 . ? 1_555 ? 
36 AC4 25 TRP A 208 ? TRP A 209 . ? 1_555 ? 
37 AC4 25 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
38 AC4 25 HOH F .   ? HOH A 441 . ? 1_555 ? 
39 AC4 25 HOH F .   ? HOH A 472 . ? 1_555 ? 
40 AC4 25 HOH F .   ? HOH A 509 . ? 1_555 ? 
41 AC4 25 HOH F .   ? HOH A 511 . ? 1_555 ? 
42 AC4 25 HOH F .   ? HOH A 600 . ? 1_555 ? 
43 AC4 25 HOH F .   ? HOH A 646 . ? 1_555 ? 
44 AC4 25 HOH F .   ? HOH A 650 . ? 1_555 ? 
# 
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   ? ? 1.415 1.354 0.061 0.009 N 
2 1 CG A HIS 10  ? ? CD2 A HIS 10  ? ? 1.428 1.354 0.074 0.009 N 
3 1 CG A HIS 96  ? ? CD2 A HIS 96  ? ? 1.416 1.354 0.062 0.009 N 
4 1 CG A HIS 122 ? ? CD2 A HIS 122 ? ? 1.422 1.354 0.068 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  ? ? -140.97 21.07   
2 1 ARG A 27  ? ? -141.44 56.94   
3 1 LYS A 111 ? ? 77.07   -0.18   
4 1 ASN A 244 ? ? -98.83  52.67   
5 1 LYS A 252 ? ? 57.07   -137.81 
6 1 ASN A 253 ? ? -95.00  59.56   
# 
_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 
5DT F32  F  N N 1   
5DT C6   C  Y N 2   
5DT C1   C  Y N 3   
5DT S11  S  N N 4   
5DT C21  C  N N 5   
5DT C24  C  N N 6   
5DT C29  C  Y N 7   
5DT C28  C  Y N 8   
5DT C27  C  Y N 9   
5DT C31  C  Y N 10  
5DT C30  C  Y N 11  
5DT C26  C  Y N 12  
5DT C5   C  Y N 13  
5DT C4   C  Y N 14  
5DT S7   S  N N 15  
5DT O9   O  N N 16  
5DT N10  N  N N 17  
5DT O8   O  N N 18  
5DT C3   C  Y N 19  
5DT F12  F  N N 20  
5DT C2   C  Y N 21  
5DT F13  F  N N 22  
5DT N25  N  N N 23  
5DT C14  C  N N 24  
5DT C15  C  Y N 25  
5DT C20  C  Y N 26  
5DT C19  C  Y N 27  
5DT C18  C  Y N 28  
5DT C17  C  Y N 29  
5DT C16  C  Y N 30  
5DT H1   H  N N 31  
5DT H2   H  N N 32  
5DT H3   H  N N 33  
5DT H4   H  N N 34  
5DT H5   H  N N 35  
5DT H6   H  N N 36  
5DT H7   H  N N 37  
5DT H8   H  N N 38  
5DT H9   H  N N 39  
5DT H10  H  N N 40  
5DT H11  H  N N 41  
5DT H12  H  N N 42  
5DT H13  H  N N 43  
5DT H14  H  N N 44  
5DT H15  H  N N 45  
5DT H16  H  N N 46  
5DT H17  H  N N 47  
5DT H18  H  N N 48  
5DT H19  H  N N 49  
ALA N    N  N N 50  
ALA CA   C  N S 51  
ALA C    C  N N 52  
ALA O    O  N N 53  
ALA CB   C  N N 54  
ALA OXT  O  N N 55  
ALA H    H  N N 56  
ALA H2   H  N N 57  
ALA HA   H  N N 58  
ALA HB1  H  N N 59  
ALA HB2  H  N N 60  
ALA HB3  H  N N 61  
ALA HXT  H  N N 62  
ARG N    N  N N 63  
ARG CA   C  N S 64  
ARG C    C  N N 65  
ARG O    O  N N 66  
ARG CB   C  N N 67  
ARG CG   C  N N 68  
ARG CD   C  N N 69  
ARG NE   N  N N 70  
ARG CZ   C  N N 71  
ARG NH1  N  N N 72  
ARG NH2  N  N N 73  
ARG OXT  O  N N 74  
ARG H    H  N N 75  
ARG H2   H  N N 76  
ARG HA   H  N N 77  
ARG HB2  H  N N 78  
ARG HB3  H  N N 79  
ARG HG2  H  N N 80  
ARG HG3  H  N N 81  
ARG HD2  H  N N 82  
ARG HD3  H  N N 83  
ARG HE   H  N N 84  
ARG HH11 H  N N 85  
ARG HH12 H  N N 86  
ARG HH21 H  N N 87  
ARG HH22 H  N N 88  
ARG HXT  H  N N 89  
ASN N    N  N N 90  
ASN CA   C  N S 91  
ASN C    C  N N 92  
ASN O    O  N N 93  
ASN CB   C  N N 94  
ASN CG   C  N N 95  
ASN OD1  O  N N 96  
ASN ND2  N  N N 97  
ASN OXT  O  N N 98  
ASN H    H  N N 99  
ASN H2   H  N N 100 
ASN HA   H  N N 101 
ASN HB2  H  N N 102 
ASN HB3  H  N N 103 
ASN HD21 H  N N 104 
ASN HD22 H  N N 105 
ASN HXT  H  N N 106 
ASP N    N  N N 107 
ASP CA   C  N S 108 
ASP C    C  N N 109 
ASP O    O  N N 110 
ASP CB   C  N N 111 
ASP CG   C  N N 112 
ASP OD1  O  N N 113 
ASP OD2  O  N N 114 
ASP OXT  O  N N 115 
ASP H    H  N N 116 
ASP H2   H  N N 117 
ASP HA   H  N N 118 
ASP HB2  H  N N 119 
ASP HB3  H  N N 120 
ASP HD2  H  N N 121 
ASP HXT  H  N N 122 
BCN N1   N  N N 123 
BCN C1   C  N N 124 
BCN C2   C  N N 125 
BCN O21  O  N N 126 
BCN O22  O  N N 127 
BCN C3   C  N N 128 
BCN C4   C  N N 129 
BCN O4   O  N N 130 
BCN C5   C  N N 131 
BCN C6   C  N N 132 
BCN O6   O  N N 133 
BCN H11  H  N N 134 
BCN H12  H  N N 135 
BCN HO2  H  N N 136 
BCN H31  H  N N 137 
BCN H32  H  N N 138 
BCN H41  H  N N 139 
BCN H42  H  N N 140 
BCN HO4  H  N N 141 
BCN H51  H  N N 142 
BCN H52  H  N N 143 
BCN H61  H  N N 144 
BCN H62  H  N N 145 
BCN HO6  H  N N 146 
CYS N    N  N N 147 
CYS CA   C  N R 148 
CYS C    C  N N 149 
CYS O    O  N N 150 
CYS CB   C  N N 151 
CYS SG   S  N N 152 
CYS OXT  O  N N 153 
CYS H    H  N N 154 
CYS H2   H  N N 155 
CYS HA   H  N N 156 
CYS HB2  H  N N 157 
CYS HB3  H  N N 158 
CYS HG   H  N N 159 
CYS HXT  H  N N 160 
GLN N    N  N N 161 
GLN CA   C  N S 162 
GLN C    C  N N 163 
GLN O    O  N N 164 
GLN CB   C  N N 165 
GLN CG   C  N N 166 
GLN CD   C  N N 167 
GLN OE1  O  N N 168 
GLN NE2  N  N N 169 
GLN OXT  O  N N 170 
GLN H    H  N N 171 
GLN H2   H  N N 172 
GLN HA   H  N N 173 
GLN HB2  H  N N 174 
GLN HB3  H  N N 175 
GLN HG2  H  N N 176 
GLN HG3  H  N N 177 
GLN HE21 H  N N 178 
GLN HE22 H  N N 179 
GLN HXT  H  N N 180 
GLU N    N  N N 181 
GLU CA   C  N S 182 
GLU C    C  N N 183 
GLU O    O  N N 184 
GLU CB   C  N N 185 
GLU CG   C  N N 186 
GLU CD   C  N N 187 
GLU OE1  O  N N 188 
GLU OE2  O  N N 189 
GLU OXT  O  N N 190 
GLU H    H  N N 191 
GLU H2   H  N N 192 
GLU HA   H  N N 193 
GLU HB2  H  N N 194 
GLU HB3  H  N N 195 
GLU HG2  H  N N 196 
GLU HG3  H  N N 197 
GLU HE2  H  N N 198 
GLU HXT  H  N N 199 
GLY N    N  N N 200 
GLY CA   C  N N 201 
GLY C    C  N N 202 
GLY O    O  N N 203 
GLY OXT  O  N N 204 
GLY H    H  N N 205 
GLY H2   H  N N 206 
GLY HA2  H  N N 207 
GLY HA3  H  N N 208 
GLY HXT  H  N N 209 
HIS N    N  N N 210 
HIS CA   C  N S 211 
HIS C    C  N N 212 
HIS O    O  N N 213 
HIS CB   C  N N 214 
HIS CG   C  Y N 215 
HIS ND1  N  Y N 216 
HIS CD2  C  Y N 217 
HIS CE1  C  Y N 218 
HIS NE2  N  Y N 219 
HIS OXT  O  N N 220 
HIS H    H  N N 221 
HIS H2   H  N N 222 
HIS HA   H  N N 223 
HIS HB2  H  N N 224 
HIS HB3  H  N N 225 
HIS HD1  H  N N 226 
HIS HD2  H  N N 227 
HIS HE1  H  N N 228 
HIS HE2  H  N N 229 
HIS HXT  H  N N 230 
HOH O    O  N N 231 
HOH H1   H  N N 232 
HOH H2   H  N N 233 
ILE N    N  N N 234 
ILE CA   C  N S 235 
ILE C    C  N N 236 
ILE O    O  N N 237 
ILE CB   C  N S 238 
ILE CG1  C  N N 239 
ILE CG2  C  N N 240 
ILE CD1  C  N N 241 
ILE OXT  O  N N 242 
ILE H    H  N N 243 
ILE H2   H  N N 244 
ILE HA   H  N N 245 
ILE HB   H  N N 246 
ILE HG12 H  N N 247 
ILE HG13 H  N N 248 
ILE HG21 H  N N 249 
ILE HG22 H  N N 250 
ILE HG23 H  N N 251 
ILE HD11 H  N N 252 
ILE HD12 H  N N 253 
ILE HD13 H  N N 254 
ILE HXT  H  N N 255 
LEU N    N  N N 256 
LEU CA   C  N S 257 
LEU C    C  N N 258 
LEU O    O  N N 259 
LEU CB   C  N N 260 
LEU CG   C  N N 261 
LEU CD1  C  N N 262 
LEU CD2  C  N N 263 
LEU OXT  O  N N 264 
LEU H    H  N N 265 
LEU H2   H  N N 266 
LEU HA   H  N N 267 
LEU HB2  H  N N 268 
LEU HB3  H  N N 269 
LEU HG   H  N N 270 
LEU HD11 H  N N 271 
LEU HD12 H  N N 272 
LEU HD13 H  N N 273 
LEU HD21 H  N N 274 
LEU HD22 H  N N 275 
LEU HD23 H  N N 276 
LEU HXT  H  N N 277 
LYS N    N  N N 278 
LYS CA   C  N S 279 
LYS C    C  N N 280 
LYS O    O  N N 281 
LYS CB   C  N N 282 
LYS CG   C  N N 283 
LYS CD   C  N N 284 
LYS CE   C  N N 285 
LYS NZ   N  N N 286 
LYS OXT  O  N N 287 
LYS H    H  N N 288 
LYS H2   H  N N 289 
LYS HA   H  N N 290 
LYS HB2  H  N N 291 
LYS HB3  H  N N 292 
LYS HG2  H  N N 293 
LYS HG3  H  N N 294 
LYS HD2  H  N N 295 
LYS HD3  H  N N 296 
LYS HE2  H  N N 297 
LYS HE3  H  N N 298 
LYS HZ1  H  N N 299 
LYS HZ2  H  N N 300 
LYS HZ3  H  N N 301 
LYS HXT  H  N N 302 
MES O1   O  N N 303 
MES C2   C  N N 304 
MES C3   C  N N 305 
MES N4   N  N N 306 
MES C5   C  N N 307 
MES C6   C  N N 308 
MES C7   C  N N 309 
MES C8   C  N N 310 
MES S    S  N N 311 
MES O1S  O  N N 312 
MES O2S  O  N N 313 
MES O3S  O  N N 314 
MES H21  H  N N 315 
MES H22  H  N N 316 
MES H31  H  N N 317 
MES H32  H  N N 318 
MES HN4  H  N N 319 
MES H51  H  N N 320 
MES H52  H  N N 321 
MES H61  H  N N 322 
MES H62  H  N N 323 
MES H71  H  N N 324 
MES H72  H  N N 325 
MES H81  H  N N 326 
MES H82  H  N N 327 
MET N    N  N N 328 
MET CA   C  N S 329 
MET C    C  N N 330 
MET O    O  N N 331 
MET CB   C  N N 332 
MET CG   C  N N 333 
MET SD   S  N N 334 
MET CE   C  N N 335 
MET OXT  O  N N 336 
MET H    H  N N 337 
MET H2   H  N N 338 
MET HA   H  N N 339 
MET HB2  H  N N 340 
MET HB3  H  N N 341 
MET HG2  H  N N 342 
MET HG3  H  N N 343 
MET HE1  H  N N 344 
MET HE2  H  N N 345 
MET HE3  H  N N 346 
MET HXT  H  N N 347 
PHE N    N  N N 348 
PHE CA   C  N S 349 
PHE C    C  N N 350 
PHE O    O  N N 351 
PHE CB   C  N N 352 
PHE CG   C  Y N 353 
PHE CD1  C  Y N 354 
PHE CD2  C  Y N 355 
PHE CE1  C  Y N 356 
PHE CE2  C  Y N 357 
PHE CZ   C  Y N 358 
PHE OXT  O  N N 359 
PHE H    H  N N 360 
PHE H2   H  N N 361 
PHE HA   H  N N 362 
PHE HB2  H  N N 363 
PHE HB3  H  N N 364 
PHE HD1  H  N N 365 
PHE HD2  H  N N 366 
PHE HE1  H  N N 367 
PHE HE2  H  N N 368 
PHE HZ   H  N N 369 
PHE HXT  H  N N 370 
PRO N    N  N N 371 
PRO CA   C  N S 372 
PRO C    C  N N 373 
PRO O    O  N N 374 
PRO CB   C  N N 375 
PRO CG   C  N N 376 
PRO CD   C  N N 377 
PRO OXT  O  N N 378 
PRO H    H  N N 379 
PRO HA   H  N N 380 
PRO HB2  H  N N 381 
PRO HB3  H  N N 382 
PRO HG2  H  N N 383 
PRO HG3  H  N N 384 
PRO HD2  H  N N 385 
PRO HD3  H  N N 386 
PRO HXT  H  N N 387 
SER N    N  N N 388 
SER CA   C  N S 389 
SER C    C  N N 390 
SER O    O  N N 391 
SER CB   C  N N 392 
SER OG   O  N N 393 
SER OXT  O  N N 394 
SER H    H  N N 395 
SER H2   H  N N 396 
SER HA   H  N N 397 
SER HB2  H  N N 398 
SER HB3  H  N N 399 
SER HG   H  N N 400 
SER HXT  H  N N 401 
THR N    N  N N 402 
THR CA   C  N S 403 
THR C    C  N N 404 
THR O    O  N N 405 
THR CB   C  N R 406 
THR OG1  O  N N 407 
THR CG2  C  N N 408 
THR OXT  O  N N 409 
THR H    H  N N 410 
THR H2   H  N N 411 
THR HA   H  N N 412 
THR HB   H  N N 413 
THR HG1  H  N N 414 
THR HG21 H  N N 415 
THR HG22 H  N N 416 
THR HG23 H  N N 417 
THR HXT  H  N N 418 
TRP N    N  N N 419 
TRP CA   C  N S 420 
TRP C    C  N N 421 
TRP O    O  N N 422 
TRP CB   C  N N 423 
TRP CG   C  Y N 424 
TRP CD1  C  Y N 425 
TRP CD2  C  Y N 426 
TRP NE1  N  Y N 427 
TRP CE2  C  Y N 428 
TRP CE3  C  Y N 429 
TRP CZ2  C  Y N 430 
TRP CZ3  C  Y N 431 
TRP CH2  C  Y N 432 
TRP OXT  O  N N 433 
TRP H    H  N N 434 
TRP H2   H  N N 435 
TRP HA   H  N N 436 
TRP HB2  H  N N 437 
TRP HB3  H  N N 438 
TRP HD1  H  N N 439 
TRP HE1  H  N N 440 
TRP HE3  H  N N 441 
TRP HZ2  H  N N 442 
TRP HZ3  H  N N 443 
TRP HH2  H  N N 444 
TRP HXT  H  N N 445 
TYR N    N  N N 446 
TYR CA   C  N S 447 
TYR C    C  N N 448 
TYR O    O  N N 449 
TYR CB   C  N N 450 
TYR CG   C  Y N 451 
TYR CD1  C  Y N 452 
TYR CD2  C  Y N 453 
TYR CE1  C  Y N 454 
TYR CE2  C  Y N 455 
TYR CZ   C  Y N 456 
TYR OH   O  N N 457 
TYR OXT  O  N N 458 
TYR H    H  N N 459 
TYR H2   H  N N 460 
TYR HA   H  N N 461 
TYR HB2  H  N N 462 
TYR HB3  H  N N 463 
TYR HD1  H  N N 464 
TYR HD2  H  N N 465 
TYR HE1  H  N N 466 
TYR HE2  H  N N 467 
TYR HH   H  N N 468 
TYR HXT  H  N N 469 
VAL N    N  N N 470 
VAL CA   C  N S 471 
VAL C    C  N N 472 
VAL O    O  N N 473 
VAL CB   C  N N 474 
VAL CG1  C  N N 475 
VAL CG2  C  N N 476 
VAL OXT  O  N N 477 
VAL H    H  N N 478 
VAL H2   H  N N 479 
VAL HA   H  N N 480 
VAL HB   H  N N 481 
VAL HG11 H  N N 482 
VAL HG12 H  N N 483 
VAL HG13 H  N N 484 
VAL HG21 H  N N 485 
VAL HG22 H  N N 486 
VAL HG23 H  N N 487 
VAL HXT  H  N N 488 
ZN  ZN   ZN N N 489 
# 
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 
5DT C17 C18  doub Y N 1   
5DT C17 C16  sing Y N 2   
5DT C18 C19  sing Y N 3   
5DT C16 C15  doub Y N 4   
5DT C19 C20  doub Y N 5   
5DT C15 C20  sing Y N 6   
5DT C15 C14  sing N N 7   
5DT C14 N25  sing N N 8   
5DT F32 C6   sing N N 9   
5DT C28 C27  doub Y N 10  
5DT C28 C29  sing Y N 11  
5DT C27 C26  sing Y N 12  
5DT S11 C1   sing N N 13  
5DT S11 C21  sing N N 14  
5DT C6  C1   doub Y N 15  
5DT C6  C5   sing Y N 16  
5DT C24 C29  sing N N 17  
5DT C24 C21  sing N N 18  
5DT N25 C5   sing N N 19  
5DT C29 C31  doub Y N 20  
5DT C26 C30  doub Y N 21  
5DT C1  C2   sing Y N 22  
5DT C5  C4   doub Y N 23  
5DT C31 C30  sing Y N 24  
5DT C2  F13  sing N N 25  
5DT C2  C3   doub Y N 26  
5DT C4  C3   sing Y N 27  
5DT C4  S7   sing N N 28  
5DT N10 S7   sing N N 29  
5DT C3  F12  sing N N 30  
5DT S7  O9   doub N N 31  
5DT S7  O8   doub N N 32  
5DT C21 H1   sing N N 33  
5DT C21 H2   sing N N 34  
5DT C24 H3   sing N N 35  
5DT C24 H4   sing N N 36  
5DT C28 H5   sing N N 37  
5DT C27 H6   sing N N 38  
5DT C31 H7   sing N N 39  
5DT C30 H8   sing N N 40  
5DT C26 H9   sing N N 41  
5DT N10 H10  sing N N 42  
5DT N10 H11  sing N N 43  
5DT N25 H12  sing N N 44  
5DT C14 H13  sing N N 45  
5DT C14 H14  sing N N 46  
5DT C20 H15  sing N N 47  
5DT C19 H16  sing N N 48  
5DT C18 H17  sing N N 49  
5DT C17 H18  sing N N 50  
5DT C16 H19  sing N N 51  
ALA N   CA   sing N N 52  
ALA N   H    sing N N 53  
ALA N   H2   sing N N 54  
ALA CA  C    sing N N 55  
ALA CA  CB   sing N N 56  
ALA CA  HA   sing N N 57  
ALA C   O    doub N N 58  
ALA C   OXT  sing N N 59  
ALA CB  HB1  sing N N 60  
ALA CB  HB2  sing N N 61  
ALA CB  HB3  sing N N 62  
ALA OXT HXT  sing N N 63  
ARG N   CA   sing N N 64  
ARG N   H    sing N N 65  
ARG N   H2   sing N N 66  
ARG CA  C    sing N N 67  
ARG CA  CB   sing N N 68  
ARG CA  HA   sing N N 69  
ARG C   O    doub N N 70  
ARG C   OXT  sing N N 71  
ARG CB  CG   sing N N 72  
ARG CB  HB2  sing N N 73  
ARG CB  HB3  sing N N 74  
ARG CG  CD   sing N N 75  
ARG CG  HG2  sing N N 76  
ARG CG  HG3  sing N N 77  
ARG CD  NE   sing N N 78  
ARG CD  HD2  sing N N 79  
ARG CD  HD3  sing N N 80  
ARG NE  CZ   sing N N 81  
ARG NE  HE   sing N N 82  
ARG CZ  NH1  sing N N 83  
ARG CZ  NH2  doub N N 84  
ARG NH1 HH11 sing N N 85  
ARG NH1 HH12 sing N N 86  
ARG NH2 HH21 sing N N 87  
ARG NH2 HH22 sing N N 88  
ARG OXT HXT  sing N N 89  
ASN N   CA   sing N N 90  
ASN N   H    sing N N 91  
ASN N   H2   sing N N 92  
ASN CA  C    sing N N 93  
ASN CA  CB   sing N N 94  
ASN CA  HA   sing N N 95  
ASN C   O    doub N N 96  
ASN C   OXT  sing N N 97  
ASN CB  CG   sing N N 98  
ASN CB  HB2  sing N N 99  
ASN CB  HB3  sing N N 100 
ASN CG  OD1  doub N N 101 
ASN CG  ND2  sing N N 102 
ASN ND2 HD21 sing N N 103 
ASN ND2 HD22 sing N N 104 
ASN OXT HXT  sing N N 105 
ASP N   CA   sing N N 106 
ASP N   H    sing N N 107 
ASP N   H2   sing N N 108 
ASP CA  C    sing N N 109 
ASP CA  CB   sing N N 110 
ASP CA  HA   sing N N 111 
ASP C   O    doub N N 112 
ASP C   OXT  sing N N 113 
ASP CB  CG   sing N N 114 
ASP CB  HB2  sing N N 115 
ASP CB  HB3  sing N N 116 
ASP CG  OD1  doub N N 117 
ASP CG  OD2  sing N N 118 
ASP OD2 HD2  sing N N 119 
ASP OXT HXT  sing N N 120 
BCN N1  C1   sing N N 121 
BCN N1  C3   sing N N 122 
BCN N1  C5   sing N N 123 
BCN C1  C2   sing N N 124 
BCN C1  H11  sing N N 125 
BCN C1  H12  sing N N 126 
BCN C2  O21  doub N N 127 
BCN C2  O22  sing N N 128 
BCN O22 HO2  sing N N 129 
BCN C3  C4   sing N N 130 
BCN C3  H31  sing N N 131 
BCN C3  H32  sing N N 132 
BCN C4  O4   sing N N 133 
BCN C4  H41  sing N N 134 
BCN C4  H42  sing N N 135 
BCN O4  HO4  sing N N 136 
BCN C5  C6   sing N N 137 
BCN C5  H51  sing N N 138 
BCN C5  H52  sing N N 139 
BCN C6  O6   sing N N 140 
BCN C6  H61  sing N N 141 
BCN C6  H62  sing N N 142 
BCN O6  HO6  sing N N 143 
CYS N   CA   sing N N 144 
CYS N   H    sing N N 145 
CYS N   H2   sing N N 146 
CYS CA  C    sing N N 147 
CYS CA  CB   sing N N 148 
CYS CA  HA   sing N N 149 
CYS C   O    doub N N 150 
CYS C   OXT  sing N N 151 
CYS CB  SG   sing N N 152 
CYS CB  HB2  sing N N 153 
CYS CB  HB3  sing N N 154 
CYS SG  HG   sing N N 155 
CYS OXT HXT  sing N N 156 
GLN N   CA   sing N N 157 
GLN N   H    sing N N 158 
GLN N   H2   sing N N 159 
GLN CA  C    sing N N 160 
GLN CA  CB   sing N N 161 
GLN CA  HA   sing N N 162 
GLN C   O    doub N N 163 
GLN C   OXT  sing N N 164 
GLN CB  CG   sing N N 165 
GLN CB  HB2  sing N N 166 
GLN CB  HB3  sing N N 167 
GLN CG  CD   sing N N 168 
GLN CG  HG2  sing N N 169 
GLN CG  HG3  sing N N 170 
GLN CD  OE1  doub N N 171 
GLN CD  NE2  sing N N 172 
GLN NE2 HE21 sing N N 173 
GLN NE2 HE22 sing N N 174 
GLN OXT HXT  sing N N 175 
GLU N   CA   sing N N 176 
GLU N   H    sing N N 177 
GLU N   H2   sing N N 178 
GLU CA  C    sing N N 179 
GLU CA  CB   sing N N 180 
GLU CA  HA   sing N N 181 
GLU C   O    doub N N 182 
GLU C   OXT  sing N N 183 
GLU CB  CG   sing N N 184 
GLU CB  HB2  sing N N 185 
GLU CB  HB3  sing N N 186 
GLU CG  CD   sing N N 187 
GLU CG  HG2  sing N N 188 
GLU CG  HG3  sing N N 189 
GLU CD  OE1  doub N N 190 
GLU CD  OE2  sing N N 191 
GLU OE2 HE2  sing N N 192 
GLU OXT HXT  sing N N 193 
GLY N   CA   sing N N 194 
GLY N   H    sing N N 195 
GLY N   H2   sing N N 196 
GLY CA  C    sing N N 197 
GLY CA  HA2  sing N N 198 
GLY CA  HA3  sing N N 199 
GLY C   O    doub N N 200 
GLY C   OXT  sing N N 201 
GLY OXT HXT  sing N N 202 
HIS N   CA   sing N N 203 
HIS N   H    sing N N 204 
HIS N   H2   sing N N 205 
HIS CA  C    sing N N 206 
HIS CA  CB   sing N N 207 
HIS CA  HA   sing N N 208 
HIS C   O    doub N N 209 
HIS C   OXT  sing N N 210 
HIS CB  CG   sing N N 211 
HIS CB  HB2  sing N N 212 
HIS CB  HB3  sing N N 213 
HIS CG  ND1  sing Y N 214 
HIS CG  CD2  doub Y N 215 
HIS ND1 CE1  doub Y N 216 
HIS ND1 HD1  sing N N 217 
HIS CD2 NE2  sing Y N 218 
HIS CD2 HD2  sing N N 219 
HIS CE1 NE2  sing Y N 220 
HIS CE1 HE1  sing N N 221 
HIS NE2 HE2  sing N N 222 
HIS OXT HXT  sing N N 223 
HOH O   H1   sing N N 224 
HOH O   H2   sing N N 225 
ILE N   CA   sing N N 226 
ILE N   H    sing N N 227 
ILE N   H2   sing N N 228 
ILE CA  C    sing N N 229 
ILE CA  CB   sing N N 230 
ILE CA  HA   sing N N 231 
ILE C   O    doub N N 232 
ILE C   OXT  sing N N 233 
ILE CB  CG1  sing N N 234 
ILE CB  CG2  sing N N 235 
ILE CB  HB   sing N N 236 
ILE CG1 CD1  sing N N 237 
ILE CG1 HG12 sing N N 238 
ILE CG1 HG13 sing N N 239 
ILE CG2 HG21 sing N N 240 
ILE CG2 HG22 sing N N 241 
ILE CG2 HG23 sing N N 242 
ILE CD1 HD11 sing N N 243 
ILE CD1 HD12 sing N N 244 
ILE CD1 HD13 sing N N 245 
ILE OXT HXT  sing N N 246 
LEU N   CA   sing N N 247 
LEU N   H    sing N N 248 
LEU N   H2   sing N N 249 
LEU CA  C    sing N N 250 
LEU CA  CB   sing N N 251 
LEU CA  HA   sing N N 252 
LEU C   O    doub N N 253 
LEU C   OXT  sing N N 254 
LEU CB  CG   sing N N 255 
LEU CB  HB2  sing N N 256 
LEU CB  HB3  sing N N 257 
LEU CG  CD1  sing N N 258 
LEU CG  CD2  sing N N 259 
LEU CG  HG   sing N N 260 
LEU CD1 HD11 sing N N 261 
LEU CD1 HD12 sing N N 262 
LEU CD1 HD13 sing N N 263 
LEU CD2 HD21 sing N N 264 
LEU CD2 HD22 sing N N 265 
LEU CD2 HD23 sing N N 266 
LEU OXT HXT  sing N N 267 
LYS N   CA   sing N N 268 
LYS N   H    sing N N 269 
LYS N   H2   sing N N 270 
LYS CA  C    sing N N 271 
LYS CA  CB   sing N N 272 
LYS CA  HA   sing N N 273 
LYS C   O    doub N N 274 
LYS C   OXT  sing N N 275 
LYS CB  CG   sing N N 276 
LYS CB  HB2  sing N N 277 
LYS CB  HB3  sing N N 278 
LYS CG  CD   sing N N 279 
LYS CG  HG2  sing N N 280 
LYS CG  HG3  sing N N 281 
LYS CD  CE   sing N N 282 
LYS CD  HD2  sing N N 283 
LYS CD  HD3  sing N N 284 
LYS CE  NZ   sing N N 285 
LYS CE  HE2  sing N N 286 
LYS CE  HE3  sing N N 287 
LYS NZ  HZ1  sing N N 288 
LYS NZ  HZ2  sing N N 289 
LYS NZ  HZ3  sing N N 290 
LYS OXT HXT  sing N N 291 
MES O1  C2   sing N N 292 
MES O1  C6   sing N N 293 
MES C2  C3   sing N N 294 
MES C2  H21  sing N N 295 
MES C2  H22  sing N N 296 
MES C3  N4   sing N N 297 
MES C3  H31  sing N N 298 
MES C3  H32  sing N N 299 
MES N4  C5   sing N N 300 
MES N4  C7   sing N N 301 
MES N4  HN4  sing N N 302 
MES C5  C6   sing N N 303 
MES C5  H51  sing N N 304 
MES C5  H52  sing N N 305 
MES C6  H61  sing N N 306 
MES C6  H62  sing N N 307 
MES C7  C8   sing N N 308 
MES C7  H71  sing N N 309 
MES C7  H72  sing N N 310 
MES C8  S    sing N N 311 
MES C8  H81  sing N N 312 
MES C8  H82  sing N N 313 
MES S   O1S  doub N N 314 
MES S   O2S  doub N N 315 
MES S   O3S  sing N N 316 
MET N   CA   sing N N 317 
MET N   H    sing N N 318 
MET N   H2   sing N N 319 
MET CA  C    sing N N 320 
MET CA  CB   sing N N 321 
MET CA  HA   sing N N 322 
MET C   O    doub N N 323 
MET C   OXT  sing N N 324 
MET CB  CG   sing N N 325 
MET CB  HB2  sing N N 326 
MET CB  HB3  sing N N 327 
MET CG  SD   sing N N 328 
MET CG  HG2  sing N N 329 
MET CG  HG3  sing N N 330 
MET SD  CE   sing N N 331 
MET CE  HE1  sing N N 332 
MET CE  HE2  sing N N 333 
MET CE  HE3  sing N N 334 
MET OXT HXT  sing N N 335 
PHE N   CA   sing N N 336 
PHE N   H    sing N N 337 
PHE N   H2   sing N N 338 
PHE CA  C    sing N N 339 
PHE CA  CB   sing N N 340 
PHE CA  HA   sing N N 341 
PHE C   O    doub N N 342 
PHE C   OXT  sing N N 343 
PHE CB  CG   sing N N 344 
PHE CB  HB2  sing N N 345 
PHE CB  HB3  sing N N 346 
PHE CG  CD1  doub Y N 347 
PHE CG  CD2  sing Y N 348 
PHE CD1 CE1  sing Y N 349 
PHE CD1 HD1  sing N N 350 
PHE CD2 CE2  doub Y N 351 
PHE CD2 HD2  sing N N 352 
PHE CE1 CZ   doub Y N 353 
PHE CE1 HE1  sing N N 354 
PHE CE2 CZ   sing Y N 355 
PHE CE2 HE2  sing N N 356 
PHE CZ  HZ   sing N N 357 
PHE OXT HXT  sing N N 358 
PRO N   CA   sing N N 359 
PRO N   CD   sing N N 360 
PRO N   H    sing N N 361 
PRO CA  C    sing N N 362 
PRO CA  CB   sing N N 363 
PRO CA  HA   sing N N 364 
PRO C   O    doub N N 365 
PRO C   OXT  sing N N 366 
PRO CB  CG   sing N N 367 
PRO CB  HB2  sing N N 368 
PRO CB  HB3  sing N N 369 
PRO CG  CD   sing N N 370 
PRO CG  HG2  sing N N 371 
PRO CG  HG3  sing N N 372 
PRO CD  HD2  sing N N 373 
PRO CD  HD3  sing N N 374 
PRO OXT HXT  sing N N 375 
SER N   CA   sing N N 376 
SER N   H    sing N N 377 
SER N   H2   sing N N 378 
SER CA  C    sing N N 379 
SER CA  CB   sing N N 380 
SER CA  HA   sing N N 381 
SER C   O    doub N N 382 
SER C   OXT  sing N N 383 
SER CB  OG   sing N N 384 
SER CB  HB2  sing N N 385 
SER CB  HB3  sing N N 386 
SER OG  HG   sing N N 387 
SER OXT HXT  sing N N 388 
THR N   CA   sing N N 389 
THR N   H    sing N N 390 
THR N   H2   sing N N 391 
THR CA  C    sing N N 392 
THR CA  CB   sing N N 393 
THR CA  HA   sing N N 394 
THR C   O    doub N N 395 
THR C   OXT  sing N N 396 
THR CB  OG1  sing N N 397 
THR CB  CG2  sing N N 398 
THR CB  HB   sing N N 399 
THR OG1 HG1  sing N N 400 
THR CG2 HG21 sing N N 401 
THR CG2 HG22 sing N N 402 
THR CG2 HG23 sing N N 403 
THR OXT HXT  sing N N 404 
TRP N   CA   sing N N 405 
TRP N   H    sing N N 406 
TRP N   H2   sing N N 407 
TRP CA  C    sing N N 408 
TRP CA  CB   sing N N 409 
TRP CA  HA   sing N N 410 
TRP C   O    doub N N 411 
TRP C   OXT  sing N N 412 
TRP CB  CG   sing N N 413 
TRP CB  HB2  sing N N 414 
TRP CB  HB3  sing N N 415 
TRP CG  CD1  doub Y N 416 
TRP CG  CD2  sing Y N 417 
TRP CD1 NE1  sing Y N 418 
TRP CD1 HD1  sing N N 419 
TRP CD2 CE2  doub Y N 420 
TRP CD2 CE3  sing Y N 421 
TRP NE1 CE2  sing Y N 422 
TRP NE1 HE1  sing N N 423 
TRP CE2 CZ2  sing Y N 424 
TRP CE3 CZ3  doub Y N 425 
TRP CE3 HE3  sing N N 426 
TRP CZ2 CH2  doub Y N 427 
TRP CZ2 HZ2  sing N N 428 
TRP CZ3 CH2  sing Y N 429 
TRP CZ3 HZ3  sing N N 430 
TRP CH2 HH2  sing N N 431 
TRP OXT HXT  sing N N 432 
TYR N   CA   sing N N 433 
TYR N   H    sing N N 434 
TYR N   H2   sing N N 435 
TYR CA  C    sing N N 436 
TYR CA  CB   sing N N 437 
TYR CA  HA   sing N N 438 
TYR C   O    doub N N 439 
TYR C   OXT  sing N N 440 
TYR CB  CG   sing N N 441 
TYR CB  HB2  sing N N 442 
TYR CB  HB3  sing N N 443 
TYR CG  CD1  doub Y N 444 
TYR CG  CD2  sing Y N 445 
TYR CD1 CE1  sing Y N 446 
TYR CD1 HD1  sing N N 447 
TYR CD2 CE2  doub Y N 448 
TYR CD2 HD2  sing N N 449 
TYR CE1 CZ   doub Y N 450 
TYR CE1 HE1  sing N N 451 
TYR CE2 CZ   sing Y N 452 
TYR CE2 HE2  sing N N 453 
TYR CZ  OH   sing N N 454 
TYR OH  HH   sing N N 455 
TYR OXT HXT  sing N N 456 
VAL N   CA   sing N N 457 
VAL N   H    sing N N 458 
VAL N   H2   sing N N 459 
VAL CA  C    sing N N 460 
VAL CA  CB   sing N N 461 
VAL CA  HA   sing N N 462 
VAL C   O    doub N N 463 
VAL C   OXT  sing N N 464 
VAL CB  CG1  sing N N 465 
VAL CB  CG2  sing N N 466 
VAL CB  HB   sing N N 467 
VAL CG1 HG11 sing N N 468 
VAL CG1 HG12 sing N N 469 
VAL CG1 HG13 sing N N 470 
VAL CG2 HG21 sing N N 471 
VAL CG2 HG22 sing N N 472 
VAL CG2 HG23 sing N N 473 
VAL OXT HXT  sing N N 474 
# 
_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                    5DOG 
_atom_sites.fract_transf_matrix[1][1]   0.023681 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006033 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024243 
_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]   0.014263 
_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   ? 29.949 2.914   7.938   1.00 31.36 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 30.863 1.882   8.502   1.00 31.69 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.214 0.926   9.468   1.00 25.42 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.438 -0.240  9.327   1.00 20.92 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 32.138 2.451   9.097   1.00 43.99 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 33.244 1.408   9.330   1.00 54.12 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 34.024 0.936   8.327   1.00 58.09 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 33.667 0.743   10.505  1.00 59.31 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 34.913 0.028   8.832   1.00 62.91 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 34.682 -0.095  10.160  1.00 60.72 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.407 1.380   10.430  1.00 20.95 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 28.784 0.423   11.386  1.00 15.59 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 27.813 -0.364  10.611  1.00 15.06 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.264 0.137   9.619   1.00 15.44 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.103 1.141   12.547  1.00 15.07 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 26.921 1.980   12.165  1.00 15.91 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 26.853 3.340   11.905  1.00 16.01 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.543 1.502   12.139  1.00 14.89 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.547 3.717   11.626  1.00 15.99 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.717 2.633   11.762  1.00 15.17 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 24.949 0.263   12.366  1.00 14.34 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.322 2.521   11.635  1.00 15.02 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.553 0.155   12.224  1.00 13.38 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 22.764 1.278   11.880  1.00 15.23 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.548 -1.584  11.059  1.00 13.13 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.544 -2.410  10.438  1.00 13.79 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.125 -3.559  11.317  1.00 14.51 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.070 -3.453  12.543  1.00 12.91 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 25.801 -4.674  10.683  1.00 15.31 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.415 -5.867  11.429  1.00 16.52 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.303 -7.065  11.177  1.00 23.14 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 26.233 -8.083  11.940  1.00 25.31 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 23.935 -6.181  11.162  1.00 14.76 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.034 -5.124  11.774  1.00 11.97 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.692 -5.174  13.135  1.00 11.07 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.555 -4.095  10.992  1.00 10.25 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 21.891 -4.151  13.686  1.00 9.76  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 21.734 -3.083  11.522  1.00 10.79 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.386 -3.163  12.872  1.00 9.56  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.558 -2.156  13.298  1.00 9.36  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.193 -6.877  10.198  1.00 22.36 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 27.922 -7.986  9.627   1.00 26.41 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 28.951 -8.527  10.601  1.00 27.83 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.130 -8.025  11.736  1.00 25.31 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 29.753 -9.478  10.095  1.00 33.55 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 30.839 -10.065 10.914  1.00 38.70 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 31.771 -9.075  11.646  1.00 36.16 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 32.162 -9.326  12.784  1.00 41.83 ? 9   LYS A O   1 
ATOM   49   N  N   . HIS A 1 10  ? 32.123 -7.954  10.999  1.00 26.17 ? 10  HIS A N   1 
ATOM   50   C  CA  . HIS A 1 10  ? 33.241 -7.092  11.432  1.00 23.27 ? 10  HIS A CA  1 
ATOM   51   C  C   . HIS A 1 10  ? 32.887 -5.682  11.886  1.00 19.64 ? 10  HIS A C   1 
ATOM   52   O  O   . HIS A 1 10  ? 33.723 -4.921  12.362  1.00 18.06 ? 10  HIS A O   1 
ATOM   53   C  CB  . HIS A 1 10  ? 34.271 -7.030  10.275  1.00 23.45 ? 10  HIS A CB  1 
ATOM   54   C  CG  . HIS A 1 10  ? 34.833 -8.407  9.918   1.00 25.50 ? 10  HIS A CG  1 
ATOM   55   N  ND1 . HIS A 1 10  ? 35.839 -8.993  10.637  1.00 25.14 ? 10  HIS A ND1 1 
ATOM   56   C  CD2 . HIS A 1 10  ? 34.482 -9.328  8.885   1.00 26.88 ? 10  HIS A CD2 1 
ATOM   57   C  CE1 . HIS A 1 10  ? 36.102 -10.232 10.120  1.00 26.09 ? 10  HIS A CE1 1 
ATOM   58   N  NE2 . HIS A 1 10  ? 35.292 -10.425 9.027   1.00 26.00 ? 10  HIS A NE2 1 
ATOM   59   N  N   . ASN A 1 11  ? 31.585 -5.342  11.820  1.00 16.47 ? 11  ASN A N   1 
ATOM   60   C  CA  . ASN A 1 11  ? 31.177 -3.996  12.102  1.00 15.15 ? 11  ASN A CA  1 
ATOM   61   C  C   . ASN A 1 11  ? 29.851 -4.013  12.896  1.00 13.81 ? 11  ASN A C   1 
ATOM   62   O  O   . ASN A 1 11  ? 29.189 -2.987  12.988  1.00 14.24 ? 11  ASN A O   1 
ATOM   63   C  CB  . ASN A 1 11  ? 30.958 -3.266  10.788  1.00 14.16 ? 11  ASN A CB  1 
ATOM   64   C  CG  . ASN A 1 11  ? 29.869 -3.864  9.925   1.00 16.20 ? 11  ASN A CG  1 
ATOM   65   O  OD1 . ASN A 1 11  ? 29.306 -4.908  10.232  1.00 17.76 ? 11  ASN A OD1 1 
ATOM   66   N  ND2 . ASN A 1 11  ? 29.569 -3.199  8.817   1.00 18.31 ? 11  ASN A ND2 1 
ATOM   67   N  N   . GLY A 1 12  ? 29.604 -5.174  13.526  1.00 13.12 ? 12  GLY A N   1 
ATOM   68   C  CA  . GLY A 1 12  ? 28.289 -5.424  14.175  1.00 13.13 ? 12  GLY A CA  1 
ATOM   69   C  C   . GLY A 1 12  ? 28.221 -4.795  15.568  1.00 12.73 ? 12  GLY A C   1 
ATOM   70   O  O   . GLY A 1 12  ? 29.080 -4.048  16.032  1.00 12.79 ? 12  GLY A O   1 
ATOM   71   N  N   . PRO A 1 13  ? 27.127 -5.075  16.281  1.00 12.01 ? 13  PRO A N   1 
ATOM   72   C  CA  . PRO A 1 13  ? 26.869 -4.430  17.565  1.00 12.19 ? 13  PRO A CA  1 
ATOM   73   C  C   . PRO A 1 13  ? 28.004 -4.478  18.589  1.00 11.92 ? 13  PRO A C   1 
ATOM   74   O  O   . PRO A 1 13  ? 28.163 -3.531  19.391  1.00 13.34 ? 13  PRO A O   1 
ATOM   75   C  CB  . PRO A 1 13  ? 25.667 -5.253  18.063  1.00 11.90 ? 13  PRO A CB  1 
ATOM   76   C  CG  . PRO A 1 13  ? 24.865 -5.443  16.806  1.00 12.07 ? 13  PRO A CG  1 
ATOM   77   C  CD  . PRO A 1 13  ? 25.968 -5.842  15.810  1.00 12.18 ? 13  PRO A CD  1 
ATOM   78   N  N   . GLU A 1 14  ? 28.804 -5.550  18.598  1.00 12.77 ? 14  GLU A N   1 
ATOM   79   C  CA  . GLU A 1 14  ? 29.893 -5.638  19.550  1.00 14.85 ? 14  GLU A CA  1 
ATOM   80   C  C   . GLU A 1 14  ? 31.046 -4.640  19.226  1.00 13.34 ? 14  GLU A C   1 
ATOM   81   O  O   . GLU A 1 14  ? 31.959 -4.412  20.051  1.00 14.88 ? 14  GLU A O   1 
ATOM   82   C  CB  . GLU A 1 14  ? 30.333 -7.112  19.556  1.00 20.58 ? 14  GLU A CB  1 
ATOM   83   C  CG  . GLU A 1 14  ? 31.072 -7.530  18.282  1.00 23.70 ? 14  GLU A CG  1 
ATOM   84   C  CD  . GLU A 1 14  ? 30.137 -8.065  17.212  1.00 30.14 ? 14  GLU A CD  1 
ATOM   85   O  OE1 . GLU A 1 14  ? 28.949 -7.689  17.220  1.00 25.37 ? 14  GLU A OE1 1 
ATOM   86   O  OE2 . GLU A 1 14  ? 30.595 -8.858  16.361  1.00 21.57 ? 14  GLU A OE2 1 
ATOM   87   N  N   . HIS A 1 15  ? 31.019 -4.033  18.035  1.00 11.52 ? 15  HIS A N   1 
ATOM   88   C  CA  . HIS A 1 15  ? 32.015 -3.035  17.620  1.00 12.41 ? 15  HIS A CA  1 
ATOM   89   C  C   . HIS A 1 15  ? 31.589 -1.587  17.779  1.00 13.05 ? 15  HIS A C   1 
ATOM   90   O  O   . HIS A 1 15  ? 32.432 -0.642  17.718  1.00 13.27 ? 15  HIS A O   1 
ATOM   91   C  CB  . HIS A 1 15  ? 32.445 -3.228  16.153  1.00 12.64 ? 15  HIS A CB  1 
ATOM   92   C  CG  . HIS A 1 15  ? 33.128 -4.566  15.892  1.00 17.35 ? 15  HIS A CG  1 
ATOM   93   N  ND1 . HIS A 1 15  ? 34.501 -4.739  15.995  1.00 19.03 ? 15  HIS A ND1 1 
ATOM   94   C  CD2 . HIS A 1 15  ? 32.609 -5.787  15.490  1.00 17.77 ? 15  HIS A CD2 1 
ATOM   95   C  CE1 . HIS A 1 15  ? 34.803 -6.041  15.730  1.00 19.73 ? 15  HIS A CE1 1 
ATOM   96   N  NE2 . HIS A 1 15  ? 33.661 -6.688  15.435  1.00 19.34 ? 15  HIS A NE2 1 
ATOM   97   N  N   . TRP A 1 16  ? 30.277 -1.367  17.938  1.00 10.70 ? 16  TRP A N   1 
ATOM   98   C  CA  . TRP A 1 16  ? 29.811 -0.018  17.932  1.00 11.12 ? 16  TRP A CA  1 
ATOM   99   C  C   . TRP A 1 16  ? 30.385 0.930   18.938  1.00 9.99  ? 16  TRP A C   1 
ATOM   100  O  O   . TRP A 1 16  ? 30.440 2.119   18.679  1.00 10.51 ? 16  TRP A O   1 
ATOM   101  C  CB  . TRP A 1 16  ? 28.282 0.019   18.009  1.00 9.89  ? 16  TRP A CB  1 
ATOM   102  C  CG  . TRP A 1 16  ? 27.562 -0.692  16.869  1.00 10.32 ? 16  TRP A CG  1 
ATOM   103  C  CD1 . TRP A 1 16  ? 28.088 -1.194  15.671  1.00 10.04 ? 16  TRP A CD1 1 
ATOM   104  C  CD2 . TRP A 1 16  ? 26.129 -0.993  16.803  1.00 9.86  ? 16  TRP A CD2 1 
ATOM   105  N  NE1 . TRP A 1 16  ? 27.095 -1.762  14.903  1.00 10.29 ? 16  TRP A NE1 1 
ATOM   106  C  CE2 . TRP A 1 16  ? 25.897 -1.675  15.528  1.00 9.97  ? 16  TRP A CE2 1 
ATOM   107  C  CE3 . TRP A 1 16  ? 25.058 -0.774  17.649  1.00 9.92  ? 16  TRP A CE3 1 
ATOM   108  C  CZ2 . TRP A 1 16  ? 24.638 -2.107  15.146  1.00 10.99 ? 16  TRP A CZ2 1 
ATOM   109  C  CZ3 . TRP A 1 16  ? 23.796 -1.205  17.254  1.00 8.70  ? 16  TRP A CZ3 1 
ATOM   110  C  CH2 . TRP A 1 16  ? 23.592 -1.860  16.036  1.00 9.30  ? 16  TRP A CH2 1 
ATOM   111  N  N   . HIS A 1 17  ? 30.804 0.408   20.090  1.00 11.55 ? 17  HIS A N   1 
ATOM   112  C  CA  . HIS A 1 17  ? 31.257 1.266   21.129  1.00 11.92 ? 17  HIS A CA  1 
ATOM   113  C  C   . HIS A 1 17  ? 32.494 2.063   20.753  1.00 12.91 ? 17  HIS A C   1 
ATOM   114  O  O   . HIS A 1 17  ? 32.738 3.061   21.355  1.00 11.19 ? 17  HIS A O   1 
ATOM   115  C  CB  . HIS A 1 17  ? 31.497 0.511   22.413  1.00 11.99 ? 17  HIS A CB  1 
ATOM   116  C  CG  . HIS A 1 17  ? 32.694 -0.391  22.346  1.00 13.43 ? 17  HIS A CG  1 
ATOM   117  N  ND1 . HIS A 1 17  ? 33.866 -0.023  22.855  1.00 15.16 ? 17  HIS A ND1 1 
ATOM   118  C  CD2 . HIS A 1 17  ? 32.905 -1.561  21.673  1.00 13.94 ? 17  HIS A CD2 1 
ATOM   119  C  CE1 . HIS A 1 17  ? 34.791 -0.949  22.575  1.00 12.78 ? 17  HIS A CE1 1 
ATOM   120  N  NE2 . HIS A 1 17  ? 34.211 -1.921  21.893  1.00 15.26 ? 17  HIS A NE2 1 
ATOM   121  N  N   . LYS A 1 18  ? 33.251 1.580   19.774  1.00 14.42 ? 18  LYS A N   1 
ATOM   122  C  CA  . LYS A 1 18  ? 34.505 2.261   19.424  1.00 15.99 ? 18  LYS A CA  1 
ATOM   123  C  C   . LYS A 1 18  ? 34.204 3.564   18.708  1.00 17.31 ? 18  LYS A C   1 
ATOM   124  O  O   . LYS A 1 18  ? 34.812 4.560   19.029  1.00 18.43 ? 18  LYS A O   1 
ATOM   125  C  CB  . LYS A 1 18  ? 35.379 1.361   18.541  1.00 15.37 ? 18  LYS A CB  1 
ATOM   126  C  CG  . LYS A 1 18  ? 35.984 0.159   19.236  1.00 16.15 ? 18  LYS A CG  1 
ATOM   127  C  CD  . LYS A 1 18  ? 36.604 -0.840  18.260  1.00 14.29 ? 18  LYS A CD  1 
ATOM   128  C  CE  . LYS A 1 18  ? 35.658 -1.777  17.555  1.00 13.04 ? 18  LYS A CE  1 
ATOM   129  N  NZ  . LYS A 1 18  ? 36.397 -2.619  16.567  1.00 14.86 ? 18  LYS A NZ  1 
ATOM   130  N  N   . ASP A 1 19  ? 33.184 3.610   17.839  1.00 15.03 ? 19  ASP A N   1 
ATOM   131  C  CA  . ASP A 1 19  ? 32.757 4.945   17.361  1.00 16.59 ? 19  ASP A CA  1 
ATOM   132  C  C   . ASP A 1 19  ? 31.721 5.695   18.220  1.00 15.91 ? 19  ASP A C   1 
ATOM   133  O  O   . ASP A 1 19  ? 31.615 6.940   18.117  1.00 15.51 ? 19  ASP A O   1 
ATOM   134  C  CB  . ASP A 1 19  ? 32.264 4.885   15.937  1.00 19.99 ? 19  ASP A CB  1 
ATOM   135  C  CG  . ASP A 1 19  ? 33.374 4.901   14.920  1.00 26.54 ? 19  ASP A CG  1 
ATOM   136  O  OD1 . ASP A 1 19  ? 34.514 5.232   15.262  1.00 30.34 ? 19  ASP A OD1 1 
ATOM   137  O  OD2 . ASP A 1 19  ? 33.094 4.566   13.767  1.00 35.69 ? 19  ASP A OD2 1 
ATOM   138  N  N   . PHE A 1 20  ? 30.956 4.925   19.027  1.00 13.62 ? 20  PHE A N   1 
ATOM   139  C  CA  . PHE A 1 20  ? 29.829 5.422   19.783  1.00 13.18 ? 20  PHE A CA  1 
ATOM   140  C  C   . PHE A 1 20  ? 29.902 4.981   21.194  1.00 12.35 ? 20  PHE A C   1 
ATOM   141  O  O   . PHE A 1 20  ? 29.284 4.032   21.569  1.00 10.72 ? 20  PHE A O   1 
ATOM   142  C  CB  . PHE A 1 20  ? 28.504 4.983   19.123  1.00 13.34 ? 20  PHE A CB  1 
ATOM   143  C  CG  . PHE A 1 20  ? 28.418 5.402   17.689  1.00 13.38 ? 20  PHE A CG  1 
ATOM   144  C  CD1 . PHE A 1 20  ? 28.070 6.725   17.339  1.00 15.43 ? 20  PHE A CD1 1 
ATOM   145  C  CD2 . PHE A 1 20  ? 28.736 4.465   16.690  1.00 16.07 ? 20  PHE A CD2 1 
ATOM   146  C  CE1 . PHE A 1 20  ? 28.038 7.077   16.005  1.00 13.85 ? 20  PHE A CE1 1 
ATOM   147  C  CE2 . PHE A 1 20  ? 28.743 4.826   15.342  1.00 15.28 ? 20  PHE A CE2 1 
ATOM   148  C  CZ  . PHE A 1 20  ? 28.392 6.130   15.027  1.00 15.13 ? 20  PHE A CZ  1 
ATOM   149  N  N   . PRO A 1 21  ? 30.760 5.628   21.999  1.00 13.46 ? 21  PRO A N   1 
ATOM   150  C  CA  . PRO A 1 21  ? 31.035 5.127   23.313  1.00 12.76 ? 21  PRO A CA  1 
ATOM   151  C  C   . PRO A 1 21  ? 29.784 4.972   24.207  1.00 13.43 ? 21  PRO A C   1 
ATOM   152  O  O   . PRO A 1 21  ? 29.805 4.243   25.186  1.00 13.32 ? 21  PRO A O   1 
ATOM   153  C  CB  . PRO A 1 21  ? 32.057 6.150   23.884  1.00 14.99 ? 21  PRO A CB  1 
ATOM   154  C  CG  . PRO A 1 21  ? 32.098 7.271   22.908  1.00 16.45 ? 21  PRO A CG  1 
ATOM   155  C  CD  . PRO A 1 21  ? 31.665 6.729   21.594  1.00 13.03 ? 21  PRO A CD  1 
ATOM   156  N  N   . ILE A 1 22  ? 28.725 5.755   23.918  1.00 10.71 ? 22  ILE A N   1 
ATOM   157  C  CA  . ILE A 1 22  ? 27.470 5.628   24.668  1.00 10.50 ? 22  ILE A CA  1 
ATOM   158  C  C   . ILE A 1 22  ? 26.862 4.232   24.521  1.00 9.71  ? 22  ILE A C   1 
ATOM   159  O  O   . ILE A 1 22  ? 25.957 3.895   25.309  1.00 9.27  ? 22  ILE A O   1 
ATOM   160  C  CB  . ILE A 1 22  ? 26.450 6.719   24.204  1.00 9.53  ? 22  ILE A CB  1 
ATOM   161  C  CG1 . ILE A 1 22  ? 25.433 7.059   25.256  1.00 10.82 ? 22  ILE A CG1 1 
ATOM   162  C  CG2 . ILE A 1 22  ? 25.843 6.346   22.851  1.00 11.27 ? 22  ILE A CG2 1 
ATOM   163  C  CD1 . ILE A 1 22  ? 24.547 8.232   24.845  1.00 12.63 ? 22  ILE A CD1 1 
ATOM   164  N  N   . ALA A 1 23  ? 27.379 3.440   23.585  1.00 10.22 ? 23  ALA A N   1 
ATOM   165  C  CA  . ALA A 1 23  ? 26.988 2.006   23.488  1.00 10.34 ? 23  ALA A CA  1 
ATOM   166  C  C   . ALA A 1 23  ? 27.031 1.272   24.821  1.00 11.18 ? 23  ALA A C   1 
ATOM   167  O  O   . ALA A 1 23  ? 26.300 0.270   25.049  1.00 10.99 ? 23  ALA A O   1 
ATOM   168  C  CB  . ALA A 1 23  ? 27.842 1.255   22.478  1.00 11.72 ? 23  ALA A CB  1 
ATOM   169  N  N   . LYS A 1 24  ? 27.960 1.700   25.702  1.00 12.78 ? 24  LYS A N   1 
ATOM   170  C  CA  . LYS A 1 24  ? 28.119 1.033   27.024  1.00 12.79 ? 24  LYS A CA  1 
ATOM   171  C  C   . LYS A 1 24  ? 27.519 1.932   28.084  1.00 13.26 ? 24  LYS A C   1 
ATOM   172  O  O   . LYS A 1 24  ? 27.983 1.888   29.278  1.00 14.84 ? 24  LYS A O   1 
ATOM   173  C  CB  . LYS A 1 24  ? 29.616 0.887   27.332  1.00 14.40 ? 24  LYS A CB  1 
ATOM   174  C  CG  . LYS A 1 24  ? 30.251 -0.115  26.419  1.00 16.14 ? 24  LYS A CG  1 
ATOM   175  C  CD  . LYS A 1 24  ? 31.734 -0.172  26.799  1.00 20.82 ? 24  LYS A CD  1 
ATOM   176  C  CE  . LYS A 1 24  ? 32.450 -0.941  25.726  1.00 21.80 ? 24  LYS A CE  1 
ATOM   177  N  NZ  . LYS A 1 24  ? 32.243 -2.385  25.886  1.00 24.21 ? 24  LYS A NZ  1 
ATOM   178  N  N   . GLY A 1 25  ? 26.537 2.780   27.731  1.00 11.74 ? 25  GLY A N   1 
ATOM   179  C  CA  . GLY A 1 25  ? 25.965 3.708   28.698  1.00 12.38 ? 25  GLY A CA  1 
ATOM   180  C  C   . GLY A 1 25  ? 24.964 3.163   29.705  1.00 11.48 ? 25  GLY A C   1 
ATOM   181  O  O   . GLY A 1 25  ? 24.738 1.947   29.789  1.00 14.65 ? 25  GLY A O   1 
ATOM   182  N  N   . GLU A 1 26  ? 24.348 4.092   30.418  1.00 12.99 ? 26  GLU A N   1 
ATOM   183  C  CA  . GLU A 1 26  ? 23.451 3.735   31.512  1.00 13.09 ? 26  GLU A CA  1 
ATOM   184  C  C   . GLU A 1 26  ? 22.005 3.477   31.136  1.00 11.74 ? 26  GLU A C   1 
ATOM   185  O  O   . GLU A 1 26  ? 21.238 2.931   31.932  1.00 12.60 ? 26  GLU A O   1 
ATOM   186  C  CB  . GLU A 1 26  ? 23.508 4.835   32.553  1.00 17.85 ? 26  GLU A CB  1 
ATOM   187  C  CG  . GLU A 1 26  ? 24.909 4.998   33.136  1.00 21.12 ? 26  GLU A CG  1 
ATOM   188  C  CD  . GLU A 1 26  ? 25.431 3.725   33.832  1.00 25.07 ? 26  GLU A CD  1 
ATOM   189  O  OE1 . GLU A 1 26  ? 24.707 3.121   34.662  1.00 28.34 ? 26  GLU A OE1 1 
ATOM   190  O  OE2 . GLU A 1 26  ? 26.561 3.282   33.503  1.00 30.28 ? 26  GLU A OE2 1 
ATOM   191  N  N   . ARG A 1 27  ? 21.617 3.822   29.921  1.00 10.72 ? 27  ARG A N   1 
ATOM   192  C  CA  . ARG A 1 27  ? 20.177 3.574   29.539  1.00 10.08 ? 27  ARG A CA  1 
ATOM   193  C  C   . ARG A 1 27  ? 20.129 3.108   28.088  1.00 9.26  ? 27  ARG A C   1 
ATOM   194  O  O   . ARG A 1 27  ? 19.353 3.701   27.245  1.00 9.29  ? 27  ARG A O   1 
ATOM   195  C  CB  . ARG A 1 27  ? 19.264 4.826   29.792  1.00 12.79 ? 27  ARG A CB  1 
ATOM   196  C  CG  . ARG A 1 27  ? 19.696 6.124   29.168  1.00 14.30 ? 27  ARG A CG  1 
ATOM   197  C  CD  . ARG A 1 27  ? 18.712 7.303   29.437  1.00 14.98 ? 27  ARG A CD  1 
ATOM   198  N  NE  . ARG A 1 27  ? 17.489 7.247   28.556  1.00 13.94 ? 27  ARG A NE  1 
ATOM   199  C  CZ  . ARG A 1 27  ? 16.546 8.140   28.552  1.00 13.21 ? 27  ARG A CZ  1 
ATOM   200  N  NH1 . ARG A 1 27  ? 16.648 9.256   29.358  1.00 12.62 ? 27  ARG A NH1 1 
ATOM   201  N  NH2 . ARG A 1 27  ? 15.548 8.001   27.723  1.00 14.38 ? 27  ARG A NH2 1 
ATOM   202  N  N   . GLN A 1 28  ? 20.859 2.008   27.813  1.00 8.36  ? 28  GLN A N   1 
ATOM   203  C  CA  . GLN A 1 28  ? 20.882 1.497   26.391  1.00 7.29  ? 28  GLN A CA  1 
ATOM   204  C  C   . GLN A 1 28  ? 19.727 0.550   26.136  1.00 7.05  ? 28  GLN A C   1 
ATOM   205  O  O   . GLN A 1 28  ? 19.216 -0.147  27.040  1.00 8.96  ? 28  GLN A O   1 
ATOM   206  C  CB  . GLN A 1 28  ? 22.223 0.783   26.117  1.00 8.19  ? 28  GLN A CB  1 
ATOM   207  C  CG  . GLN A 1 28  ? 23.315 1.868   26.012  1.00 8.50  ? 28  GLN A CG  1 
ATOM   208  C  CD  . GLN A 1 28  ? 23.193 2.687   24.709  1.00 8.31  ? 28  GLN A CD  1 
ATOM   209  O  OE1 . GLN A 1 28  ? 23.446 2.154   23.620  1.00 8.74  ? 28  GLN A OE1 1 
ATOM   210  N  NE2 . GLN A 1 28  ? 22.922 3.993   24.824  1.00 7.59  ? 28  GLN A NE2 1 
ATOM   211  N  N   . SER A 1 29  ? 19.361 0.497   24.856  1.00 6.74  ? 29  SER A N   1 
ATOM   212  C  CA  . SER A 1 29  ? 18.284 -0.412  24.378  1.00 6.36  ? 29  SER A CA  1 
ATOM   213  C  C   . SER A 1 29  ? 18.785 -1.295  23.238  1.00 6.46  ? 29  SER A C   1 
ATOM   214  O  O   . SER A 1 29  ? 19.737 -0.930  22.540  1.00 7.01  ? 29  SER A O   1 
ATOM   215  C  CB  . SER A 1 29  ? 17.137 0.432   23.809  1.00 6.09  ? 29  SER A CB  1 
ATOM   216  O  OG  . SER A 1 29  ? 16.506 1.133   24.925  1.00 6.51  ? 29  SER A OG  1 
ATOM   217  N  N   . PRO A 1 30  ? 18.130 -2.414  22.990  1.00 7.19  ? 30  PRO A N   1 
ATOM   218  C  CA  . PRO A 1 30  ? 17.009 -3.022  23.683  1.00 6.76  ? 30  PRO A CA  1 
ATOM   219  C  C   . PRO A 1 30  ? 17.407 -3.643  25.006  1.00 7.29  ? 30  PRO A C   1 
ATOM   220  O  O   . PRO A 1 30  ? 18.622 -3.645  25.385  1.00 7.03  ? 30  PRO A O   1 
ATOM   221  C  CB  . PRO A 1 30  ? 16.514 -4.017  22.653  1.00 7.03  ? 30  PRO A CB  1 
ATOM   222  C  CG  . PRO A 1 30  ? 17.839 -4.589  22.119  1.00 7.24  ? 30  PRO A CG  1 
ATOM   223  C  CD  . PRO A 1 30  ? 18.594 -3.275  21.889  1.00 7.02  ? 30  PRO A CD  1 
ATOM   224  N  N   . VAL A 1 31  ? 16.408 -4.180  25.697  1.00 8.09  ? 31  VAL A N   1 
ATOM   225  C  CA  . VAL A 1 31  ? 16.595 -4.927  26.950  1.00 7.97  ? 31  VAL A CA  1 
ATOM   226  C  C   . VAL A 1 31  ? 15.677 -6.133  26.954  1.00 9.08  ? 31  VAL A C   1 
ATOM   227  O  O   . VAL A 1 31  ? 14.698 -6.204  26.212  1.00 10.05 ? 31  VAL A O   1 
ATOM   228  C  CB  . VAL A 1 31  ? 16.303 -4.090  28.239  1.00 8.74  ? 31  VAL A CB  1 
ATOM   229  C  CG1 . VAL A 1 31  ? 17.188 -2.849  28.368  1.00 8.44  ? 31  VAL A CG1 1 
ATOM   230  C  CG2 . VAL A 1 31  ? 14.825 -3.701  28.338  1.00 9.20  ? 31  VAL A CG2 1 
ATOM   231  N  N   . ASP A 1 32  ? 16.078 -7.151  27.723  1.00 8.57  ? 32  ASP A N   1 
ATOM   232  C  CA  . ASP A 1 32  ? 15.165 -8.248  28.063  1.00 7.95  ? 32  ASP A CA  1 
ATOM   233  C  C   . ASP A 1 32  ? 14.121 -7.718  29.053  1.00 8.38  ? 32  ASP A C   1 
ATOM   234  O  O   . ASP A 1 32  ? 14.453 -7.021  30.023  1.00 9.37  ? 32  ASP A O   1 
ATOM   235  C  CB  . ASP A 1 32  ? 15.918 -9.431  28.667  1.00 8.87  ? 32  ASP A CB  1 
ATOM   236  C  CG  . ASP A 1 32  ? 14.968 -10.567 29.000  1.00 9.93  ? 32  ASP A CG  1 
ATOM   237  O  OD1 . ASP A 1 32  ? 14.242 -11.041 28.039  1.00 8.62  ? 32  ASP A OD1 1 
ATOM   238  O  OD2 . ASP A 1 32  ? 14.950 -11.062 30.215  1.00 12.06 ? 32  ASP A OD2 1 
ATOM   239  N  N   . ILE A 1 33  ? 12.856 -8.022  28.746  1.00 8.22  ? 33  ILE A N   1 
ATOM   240  C  CA  . ILE A 1 33  ? 11.731 -7.679  29.585  1.00 8.91  ? 33  ILE A CA  1 
ATOM   241  C  C   . ILE A 1 33  ? 11.466 -8.935  30.426  1.00 9.02  ? 33  ILE A C   1 
ATOM   242  O  O   . ILE A 1 33  ? 10.890 -9.927  29.995  1.00 10.98 ? 33  ILE A O   1 
ATOM   243  C  CB  . ILE A 1 33  ? 10.497 -7.230  28.797  1.00 8.33  ? 33  ILE A CB  1 
ATOM   244  C  CG1 . ILE A 1 33  ? 10.846 -5.953  28.012  1.00 9.66  ? 33  ILE A CG1 1 
ATOM   245  C  CG2 . ILE A 1 33  ? 9.368  -6.998  29.836  1.00 8.79  ? 33  ILE A CG2 1 
ATOM   246  C  CD1 . ILE A 1 33  ? 9.825  -5.618  26.851  1.00 9.80  ? 33  ILE A CD1 1 
ATOM   247  N  N   . ASP A 1 34  ? 11.849 -8.803  31.686  1.00 11.12 ? 34  ASP A N   1 
ATOM   248  C  CA  . ASP A 1 34  ? 11.565 -9.874  32.680  1.00 12.79 ? 34  ASP A CA  1 
ATOM   249  C  C   . ASP A 1 34  ? 10.159 -9.654  33.268  1.00 13.38 ? 34  ASP A C   1 
ATOM   250  O  O   . ASP A 1 34  ? 9.956  -8.681  34.062  1.00 13.75 ? 34  ASP A O   1 
ATOM   251  C  CB  . ASP A 1 34  ? 12.633 -9.886  33.771  1.00 14.96 ? 34  ASP A CB  1 
ATOM   252  C  CG  . ASP A 1 34  ? 12.507 -11.135 34.632  1.00 21.24 ? 34  ASP A CG  1 
ATOM   253  O  OD1 . ASP A 1 34  ? 11.723 -11.080 35.578  1.00 22.62 ? 34  ASP A OD1 1 
ATOM   254  O  OD2 . ASP A 1 34  ? 13.036 -12.225 34.248  1.00 21.61 ? 34  ASP A OD2 1 
ATOM   255  N  N   . THR A 1 35  ? 9.199  -10.483 32.855  1.00 13.45 ? 35  THR A N   1 
ATOM   256  C  CA  . THR A 1 35  ? 7.799  -10.168 33.020  1.00 14.49 ? 35  THR A CA  1 
ATOM   257  C  C   . THR A 1 35  ? 7.449  -10.307 34.484  1.00 17.38 ? 35  THR A C   1 
ATOM   258  O  O   . THR A 1 35  ? 6.513  -9.668  34.966  1.00 18.53 ? 35  THR A O   1 
ATOM   259  C  CB  . THR A 1 35  ? 6.889  -11.164 32.290  1.00 14.93 ? 35  THR A CB  1 
ATOM   260  O  OG1 . THR A 1 35  ? 7.094  -12.528 32.719  1.00 14.35 ? 35  THR A OG1 1 
ATOM   261  C  CG2 . THR A 1 35  ? 7.075  -11.064 30.748  1.00 13.29 ? 35  THR A CG2 1 
ATOM   262  N  N   . HIS A 1 36  ? 8.239  -11.112 35.217  1.00 17.09 ? 36  HIS A N   1 
ATOM   263  C  CA  . HIS A 1 36  ? 7.993  -11.233 36.663  1.00 19.29 ? 36  HIS A CA  1 
ATOM   264  C  C   . HIS A 1 36  ? 8.533  -10.079 37.495  1.00 22.41 ? 36  HIS A C   1 
ATOM   265  O  O   . HIS A 1 36  ? 8.007  -9.793  38.580  1.00 30.59 ? 36  HIS A O   1 
ATOM   266  C  CB  . HIS A 1 36  ? 8.390  -12.639 37.147  1.00 19.41 ? 36  HIS A CB  1 
ATOM   267  C  CG  . HIS A 1 36  ? 7.497  -13.725 36.562  1.00 18.90 ? 36  HIS A CG  1 
ATOM   268  N  ND1 . HIS A 1 36  ? 6.166  -13.841 36.899  1.00 20.61 ? 36  HIS A ND1 1 
ATOM   269  C  CD2 . HIS A 1 36  ? 7.744  -14.687 35.592  1.00 19.66 ? 36  HIS A CD2 1 
ATOM   270  C  CE1 . HIS A 1 36  ? 5.637  -14.855 36.178  1.00 25.30 ? 36  HIS A CE1 1 
ATOM   271  N  NE2 . HIS A 1 36  ? 6.606  -15.360 35.385  1.00 23.56 ? 36  HIS A NE2 1 
ATOM   272  N  N   . THR A 1 37  ? 9.544  -9.374  37.023  1.00 18.50 ? 37  THR A N   1 
ATOM   273  C  CA  . THR A 1 37  ? 10.051 -8.211  37.767  1.00 22.24 ? 37  THR A CA  1 
ATOM   274  C  C   . THR A 1 37  ? 9.482  -6.820  37.327  1.00 19.63 ? 37  THR A C   1 
ATOM   275  O  O   . THR A 1 37  ? 9.678  -5.807  38.033  1.00 17.73 ? 37  THR A O   1 
ATOM   276  C  CB  . THR A 1 37  ? 11.557 -8.270  38.018  1.00 30.26 ? 37  THR A CB  1 
ATOM   277  O  OG1 . THR A 1 37  ? 12.283 -7.859  36.894  1.00 36.05 ? 37  THR A OG1 1 
ATOM   278  C  CG2 . THR A 1 37  ? 11.992 -9.700  38.311  1.00 28.19 ? 37  THR A CG2 1 
ATOM   279  N  N   . ALA A 1 38  ? 8.825  -6.757  36.167  1.00 17.68 ? 38  ALA A N   1 
ATOM   280  C  CA  . ALA A 1 38  ? 8.186  -5.484  35.735  1.00 15.68 ? 38  ALA A CA  1 
ATOM   281  C  C   . ALA A 1 38  ? 7.028  -5.264  36.722  1.00 19.10 ? 38  ALA A C   1 
ATOM   282  O  O   . ALA A 1 38  ? 6.363  -6.166  37.143  1.00 21.19 ? 38  ALA A O   1 
ATOM   283  C  CB  . ALA A 1 38  ? 7.674  -5.558  34.313  1.00 17.99 ? 38  ALA A CB  1 
ATOM   284  N  N   . LYS A 1 39  ? 6.807  -4.038  37.063  1.00 18.45 ? 39  LYS A N   1 
ATOM   285  C  CA  . LYS A 1 39  ? 5.894  -3.739  38.145  1.00 18.90 ? 39  LYS A CA  1 
ATOM   286  C  C   . LYS A 1 39  ? 4.664  -3.118  37.468  1.00 16.69 ? 39  LYS A C   1 
ATOM   287  O  O   . LYS A 1 39  ? 4.761  -2.143  36.713  1.00 14.09 ? 39  LYS A O   1 
ATOM   288  C  CB  . LYS A 1 39  ? 6.687  -2.707  38.941  1.00 21.41 ? 39  LYS A CB  1 
ATOM   289  C  CG  . LYS A 1 39  ? 5.992  -1.751  39.860  1.00 26.65 ? 39  LYS A CG  1 
ATOM   290  C  CD  . LYS A 1 39  ? 5.790  -2.404  41.216  1.00 26.16 ? 39  LYS A CD  1 
ATOM   291  C  CE  . LYS A 1 39  ? 5.073  -1.487  42.213  1.00 27.80 ? 39  LYS A CE  1 
ATOM   292  N  NZ  . LYS A 1 39  ? 4.560  -2.381  43.267  1.00 27.40 ? 39  LYS A NZ  1 
ATOM   293  N  N   . TYR A 1 40  ? 3.477  -3.606  37.808  1.00 16.97 ? 40  TYR A N   1 
ATOM   294  C  CA  . TYR A 1 40  ? 2.276  -2.936  37.318  1.00 18.10 ? 40  TYR A CA  1 
ATOM   295  C  C   . TYR A 1 40  ? 2.183  -1.542  37.932  1.00 18.21 ? 40  TYR A C   1 
ATOM   296  O  O   . TYR A 1 40  ? 2.388  -1.371  39.166  1.00 18.73 ? 40  TYR A O   1 
ATOM   297  C  CB  . TYR A 1 40  ? 1.047  -3.791  37.688  1.00 19.52 ? 40  TYR A CB  1 
ATOM   298  C  CG  . TYR A 1 40  ? -0.203 -3.036  37.572  1.00 22.67 ? 40  TYR A CG  1 
ATOM   299  C  CD1 . TYR A 1 40  ? -0.626 -2.553  36.347  1.00 24.46 ? 40  TYR A CD1 1 
ATOM   300  C  CD2 . TYR A 1 40  ? -1.015 -2.809  38.682  1.00 28.96 ? 40  TYR A CD2 1 
ATOM   301  C  CE1 . TYR A 1 40  ? -1.803 -1.857  36.222  1.00 26.72 ? 40  TYR A CE1 1 
ATOM   302  C  CE2 . TYR A 1 40  ? -2.196 -2.079  38.579  1.00 29.25 ? 40  TYR A CE2 1 
ATOM   303  C  CZ  . TYR A 1 40  ? -2.584 -1.613  37.342  1.00 31.84 ? 40  TYR A CZ  1 
ATOM   304  O  OH  . TYR A 1 40  ? -3.741 -0.882  37.197  1.00 34.71 ? 40  TYR A OH  1 
ATOM   305  N  N   . ASP A 1 41  ? 1.896  -0.508  37.121  1.00 17.68 ? 41  ASP A N   1 
ATOM   306  C  CA  . ASP A 1 41  ? 1.920  0.884   37.626  1.00 18.78 ? 41  ASP A CA  1 
ATOM   307  C  C   . ASP A 1 41  ? 0.560  1.463   37.359  1.00 24.13 ? 41  ASP A C   1 
ATOM   308  O  O   . ASP A 1 41  ? 0.220  1.773   36.203  1.00 19.91 ? 41  ASP A O   1 
ATOM   309  C  CB  . ASP A 1 41  ? 2.939  1.722   36.893  1.00 22.64 ? 41  ASP A CB  1 
ATOM   310  C  CG  . ASP A 1 41  ? 3.019  3.126   37.423  1.00 25.11 ? 41  ASP A CG  1 
ATOM   311  O  OD1 . ASP A 1 41  ? 2.087  3.522   38.133  1.00 26.30 ? 41  ASP A OD1 1 
ATOM   312  O  OD2 . ASP A 1 41  ? 4.009  3.829   37.137  1.00 24.60 ? 41  ASP A OD2 1 
ATOM   313  N  N   . PRO A 1 42  ? -0.254 1.593   38.433  1.00 24.25 ? 42  PRO A N   1 
ATOM   314  C  CA  . PRO A 1 42  ? -1.650 1.898   38.118  1.00 25.61 ? 42  PRO A CA  1 
ATOM   315  C  C   . PRO A 1 42  ? -1.779 3.389   37.781  1.00 25.40 ? 42  PRO A C   1 
ATOM   316  O  O   . PRO A 1 42  ? -2.862 3.833   37.325  1.00 29.47 ? 42  PRO A O   1 
ATOM   317  C  CB  . PRO A 1 42  ? -2.381 1.485   39.435  1.00 26.75 ? 42  PRO A CB  1 
ATOM   318  C  CG  . PRO A 1 42  ? -1.380 1.873   40.482  1.00 25.59 ? 42  PRO A CG  1 
ATOM   319  C  CD  . PRO A 1 42  ? -0.038 1.406   39.892  1.00 26.04 ? 42  PRO A CD  1 
ATOM   320  N  N   . SER A 1 43  ? -0.719 4.171   37.997  1.00 25.98 ? 43  SER A N   1 
ATOM   321  C  CA  . SER A 1 43  ? -0.718 5.586   37.605  1.00 29.73 ? 43  SER A CA  1 
ATOM   322  C  C   . SER A 1 43  ? -0.468 5.801   36.093  1.00 30.12 ? 43  SER A C   1 
ATOM   323  O  O   . SER A 1 43  ? -0.620 6.920   35.571  1.00 31.14 ? 43  SER A O   1 
ATOM   324  C  CB  . SER A 1 43  ? 0.285  6.398   38.441  1.00 30.95 ? 43  SER A CB  1 
ATOM   325  O  OG  . SER A 1 43  ? 1.616  6.218   37.952  1.00 36.03 ? 43  SER A OG  1 
ATOM   326  N  N   . LEU A 1 44  ? -0.063 4.745   35.382  1.00 27.53 ? 44  LEU A N   1 
ATOM   327  C  CA  . LEU A 1 44  ? 0.054  4.855   33.906  1.00 24.63 ? 44  LEU A CA  1 
ATOM   328  C  C   . LEU A 1 44  ? -1.305 5.051   33.252  1.00 28.76 ? 44  LEU A C   1 
ATOM   329  O  O   . LEU A 1 44  ? -2.312 4.569   33.734  1.00 27.43 ? 44  LEU A O   1 
ATOM   330  C  CB  . LEU A 1 44  ? 0.713  3.629   33.316  1.00 19.96 ? 44  LEU A CB  1 
ATOM   331  C  CG  . LEU A 1 44  ? 2.228  3.520   33.550  1.00 17.50 ? 44  LEU A CG  1 
ATOM   332  C  CD1 . LEU A 1 44  ? 2.624  2.133   33.061  1.00 15.81 ? 44  LEU A CD1 1 
ATOM   333  C  CD2 . LEU A 1 44  ? 2.996  4.600   32.792  1.00 18.93 ? 44  LEU A CD2 1 
ATOM   334  N  N   . LYS A 1 45  ? -1.299 5.714   32.112  1.00 29.41 ? 45  LYS A N   1 
ATOM   335  C  CA  . LYS A 1 45  ? -2.534 5.981   31.374  1.00 29.70 ? 45  LYS A CA  1 
ATOM   336  C  C   . LYS A 1 45  ? -2.680 5.061   30.226  1.00 30.72 ? 45  LYS A C   1 
ATOM   337  O  O   . LYS A 1 45  ? -1.691 4.388   29.835  1.00 31.12 ? 45  LYS A O   1 
ATOM   338  C  CB  . LYS A 1 45  ? -2.513 7.397   30.892  1.00 31.37 ? 45  LYS A CB  1 
ATOM   339  C  CG  . LYS A 1 45  ? -2.737 8.361   32.024  1.00 31.96 ? 45  LYS A CG  1 
ATOM   340  C  CD  . LYS A 1 45  ? -2.999 9.767   31.499  1.00 41.86 ? 45  LYS A CD  1 
ATOM   341  N  N   . PRO A 1 46  ? -3.939 4.965   29.676  1.00 28.53 ? 46  PRO A N   1 
ATOM   342  C  CA  . PRO A 1 46  ? -3.997 4.183   28.466  1.00 28.16 ? 46  PRO A CA  1 
ATOM   343  C  C   . PRO A 1 46  ? -3.244 5.000   27.448  1.00 20.95 ? 46  PRO A C   1 
ATOM   344  O  O   . PRO A 1 46  ? -3.227 6.225   27.509  1.00 22.14 ? 46  PRO A O   1 
ATOM   345  C  CB  . PRO A 1 46  ? -5.504 4.152   28.127  1.00 24.46 ? 46  PRO A CB  1 
ATOM   346  C  CG  . PRO A 1 46  ? -6.188 4.431   29.421  1.00 30.86 ? 46  PRO A CG  1 
ATOM   347  C  CD  . PRO A 1 46  ? -5.282 5.455   30.061  1.00 31.98 ? 46  PRO A CD  1 
ATOM   348  N  N   . LEU A 1 47  ? -2.636 4.284   26.538  1.00 23.68 ? 47  LEU A N   1 
ATOM   349  C  CA  . LEU A 1 47  ? -1.898 4.908   25.504  1.00 19.09 ? 47  LEU A CA  1 
ATOM   350  C  C   . LEU A 1 47  ? -2.932 5.436   24.531  1.00 19.96 ? 47  LEU A C   1 
ATOM   351  O  O   . LEU A 1 47  ? -4.019 4.782   24.336  1.00 18.87 ? 47  LEU A O   1 
ATOM   352  C  CB  . LEU A 1 47  ? -1.147 3.823   24.831  1.00 21.61 ? 47  LEU A CB  1 
ATOM   353  C  CG  . LEU A 1 47  ? -0.020 4.020   23.896  1.00 22.69 ? 47  LEU A CG  1 
ATOM   354  C  CD1 . LEU A 1 47  ? 1.023  4.942   24.533  1.00 22.10 ? 47  LEU A CD1 1 
ATOM   355  C  CD2 . LEU A 1 47  ? 0.520  2.616   23.639  1.00 24.56 ? 47  LEU A CD2 1 
ATOM   356  N  N   . SER A 1 48  ? -2.596 6.551   23.914  1.00 14.74 ? 48  SER A N   1 
ATOM   357  C  CA  . SER A 1 48  ? -3.367 7.130   22.820  1.00 15.41 ? 48  SER A CA  1 
ATOM   358  C  C   . SER A 1 48  ? -2.607 7.149   21.527  1.00 15.49 ? 48  SER A C   1 
ATOM   359  O  O   . SER A 1 48  ? -1.653 7.894   21.348  1.00 14.77 ? 48  SER A O   1 
ATOM   360  C  CB  . SER A 1 48  ? -3.854 8.539   23.211  1.00 16.16 ? 48  SER A CB  1 
ATOM   361  O  OG  . SER A 1 48  ? -4.479 9.253   22.163  1.00 16.54 ? 48  SER A OG  1 
ATOM   362  N  N   . VAL A 1 49  ? -3.063 6.307   20.604  1.00 15.45 ? 49  VAL A N   1 
ATOM   363  C  CA  . VAL A 1 49  ? -2.472 6.236   19.297  1.00 18.71 ? 49  VAL A CA  1 
ATOM   364  C  C   . VAL A 1 49  ? -3.468 6.821   18.307  1.00 20.99 ? 49  VAL A C   1 
ATOM   365  O  O   . VAL A 1 49  ? -4.490 6.208   18.026  1.00 20.40 ? 49  VAL A O   1 
ATOM   366  C  CB  . VAL A 1 49  ? -2.183 4.808   18.861  1.00 20.81 ? 49  VAL A CB  1 
ATOM   367  C  CG1 . VAL A 1 49  ? -1.397 4.835   17.540  1.00 23.08 ? 49  VAL A CG1 1 
ATOM   368  C  CG2 . VAL A 1 49  ? -1.470 4.039   19.958  1.00 21.98 ? 49  VAL A CG2 1 
ATOM   369  N  N   . SER A 1 50  ? -3.174 7.986   17.787  1.00 16.79 ? 50  SER A N   1 
ATOM   370  C  CA  . SER A 1 50  ? -4.074 8.692   16.830  1.00 18.96 ? 50  SER A CA  1 
ATOM   371  C  C   . SER A 1 50  ? -3.456 8.788   15.478  1.00 17.18 ? 50  SER A C   1 
ATOM   372  O  O   . SER A 1 50  ? -2.755 9.732   15.177  1.00 17.63 ? 50  SER A O   1 
ATOM   373  C  CB  . SER A 1 50  ? -4.442 10.095  17.304  1.00 24.17 ? 50  SER A CB  1 
ATOM   374  O  OG  . SER A 1 50  ? -4.997 10.045  18.582  1.00 30.47 ? 50  SER A OG  1 
ATOM   375  N  N   . TYR A 1 51  ? -3.733 7.798   14.643  1.00 18.00 ? 51  TYR A N   1 
ATOM   376  C  CA  . TYR A 1 51  ? -3.139 7.735   13.336  1.00 15.64 ? 51  TYR A CA  1 
ATOM   377  C  C   . TYR A 1 51  ? -4.142 7.928   12.195  1.00 19.99 ? 51  TYR A C   1 
ATOM   378  O  O   . TYR A 1 51  ? -3.747 7.767   11.055  1.00 18.21 ? 51  TYR A O   1 
ATOM   379  C  CB  . TYR A 1 51  ? -2.490 6.380   13.111  1.00 13.80 ? 51  TYR A CB  1 
ATOM   380  C  CG  . TYR A 1 51  ? -1.203 6.023   13.931  1.00 12.95 ? 51  TYR A CG  1 
ATOM   381  C  CD1 . TYR A 1 51  ? -0.469 7.035   14.593  1.00 13.11 ? 51  TYR A CD1 1 
ATOM   382  C  CD2 . TYR A 1 51  ? -0.698 4.707   13.955  1.00 12.62 ? 51  TYR A CD2 1 
ATOM   383  C  CE1 . TYR A 1 51  ? 0.699  6.716   15.319  1.00 11.51 ? 51  TYR A CE1 1 
ATOM   384  C  CE2 . TYR A 1 51  ? 0.466  4.364   14.679  1.00 12.59 ? 51  TYR A CE2 1 
ATOM   385  C  CZ  . TYR A 1 51  ? 1.171  5.397   15.347  1.00 12.08 ? 51  TYR A CZ  1 
ATOM   386  O  OH  . TYR A 1 51  ? 2.316  5.049   16.009  1.00 11.02 ? 51  TYR A OH  1 
ATOM   387  N  N   . ASP A 1 52  ? -5.411 8.283   12.483  1.00 23.96 ? 52  ASP A N   1 
ATOM   388  C  CA  . ASP A 1 52  ? -6.440 8.498   11.394  1.00 26.01 ? 52  ASP A CA  1 
ATOM   389  C  C   . ASP A 1 52  ? -5.976 9.483   10.308  1.00 24.25 ? 52  ASP A C   1 
ATOM   390  O  O   . ASP A 1 52  ? -6.245 9.293   9.113   1.00 25.11 ? 52  ASP A O   1 
ATOM   391  C  CB  . ASP A 1 52  ? -7.804 8.913   11.978  1.00 30.82 ? 52  ASP A CB  1 
ATOM   392  C  CG  . ASP A 1 52  ? -7.674 9.962   13.086  1.00 36.41 ? 52  ASP A CG  1 
ATOM   393  O  OD1 . ASP A 1 52  ? -7.316 9.586   14.243  1.00 44.34 ? 52  ASP A OD1 1 
ATOM   394  O  OD2 . ASP A 1 52  ? -7.917 11.159  12.817  1.00 42.97 ? 52  ASP A OD2 1 
ATOM   395  N  N   . GLN A 1 53  ? -5.215 10.482  10.712  1.00 23.04 ? 53  GLN A N   1 
ATOM   396  C  CA  . GLN A 1 53  ? -4.713 11.479  9.768   1.00 25.46 ? 53  GLN A CA  1 
ATOM   397  C  C   . GLN A 1 53  ? -3.290 11.280  9.241   1.00 21.81 ? 53  GLN A C   1 
ATOM   398  O  O   . GLN A 1 53  ? -2.749 12.204  8.572   1.00 22.59 ? 53  GLN A O   1 
ATOM   399  C  CB  . GLN A 1 53  ? -4.887 12.870  10.379  1.00 31.90 ? 53  GLN A CB  1 
ATOM   400  C  CG  . GLN A 1 53  ? -6.361 13.223  10.577  1.00 37.39 ? 53  GLN A CG  1 
ATOM   401  C  CD  . GLN A 1 53  ? -7.050 13.437  9.236   1.00 41.45 ? 53  GLN A CD  1 
ATOM   402  O  OE1 . GLN A 1 53  ? -6.626 14.280  8.419   1.00 43.80 ? 53  GLN A OE1 1 
ATOM   403  N  NE2 . GLN A 1 53  ? -8.102 12.670  8.987   1.00 42.36 ? 53  GLN A NE2 1 
ATOM   404  N  N   . ALA A 1 54  ? -2.694 10.096  9.493   1.00 18.07 ? 54  ALA A N   1 
ATOM   405  C  CA  . ALA A 1 54  ? -1.323 9.804   9.034   1.00 17.13 ? 54  ALA A CA  1 
ATOM   406  C  C   . ALA A 1 54  ? -1.140 10.052  7.495   1.00 19.47 ? 54  ALA A C   1 
ATOM   407  O  O   . ALA A 1 54  ? -2.049 9.798   6.672   1.00 21.98 ? 54  ALA A O   1 
ATOM   408  C  CB  . ALA A 1 54  ? -0.855 8.393   9.507   1.00 16.51 ? 54  ALA A CB  1 
ATOM   409  N  N   . THR A 1 55  ? -0.031 10.669  7.113   1.00 15.48 ? 55  THR A N   1 
ATOM   410  C  CA  . THR A 1 55  ? 0.310  10.913  5.709   1.00 17.39 ? 55  THR A CA  1 
ATOM   411  C  C   . THR A 1 55  ? 1.652  10.311  5.445   1.00 14.30 ? 55  THR A C   1 
ATOM   412  O  O   . THR A 1 55  ? 2.711  10.931  5.719   1.00 14.50 ? 55  THR A O   1 
ATOM   413  C  CB  . THR A 1 55  ? 0.432  12.413  5.379   1.00 18.58 ? 55  THR A CB  1 
ATOM   414  O  OG1 . THR A 1 55  ? -0.843 13.007  5.511   1.00 23.85 ? 55  THR A OG1 1 
ATOM   415  C  CG2 . THR A 1 55  ? 0.835  12.582  3.971   1.00 20.53 ? 55  THR A CG2 1 
ATOM   416  N  N   . SER A 1 56  ? 1.632  9.108   4.922   1.00 14.33 ? 56  SER A N   1 
ATOM   417  C  CA  . SER A 1 56  ? 2.891  8.463   4.569   1.00 14.65 ? 56  SER A CA  1 
ATOM   418  C  C   . SER A 1 56  ? 3.377  9.096   3.256   1.00 16.34 ? 56  SER A C   1 
ATOM   419  O  O   . SER A 1 56  ? 2.558  9.589   2.434   1.00 17.90 ? 56  SER A O   1 
ATOM   420  C  CB  . SER A 1 56  ? 2.718  6.917   4.423   1.00 16.21 ? 56  SER A CB  1 
ATOM   421  O  OG  . SER A 1 56  ? 1.834  6.632   3.317   1.00 17.00 ? 56  SER A OG  1 
ATOM   422  N  N   . LEU A 1 57  ? 4.669  9.084   3.047   1.00 15.76 ? 57  LEU A N   1 
ATOM   423  C  CA  . LEU A 1 57  ? 5.195  9.696   1.832   1.00 18.58 ? 57  LEU A CA  1 
ATOM   424  C  C   . LEU A 1 57  ? 6.050  8.802   0.964   1.00 17.18 ? 57  LEU A C   1 
ATOM   425  O  O   . LEU A 1 57  ? 5.984  8.860   -0.282  1.00 18.25 ? 57  LEU A O   1 
ATOM   426  C  CB  . LEU A 1 57  ? 6.020  10.892  2.221   1.00 19.59 ? 57  LEU A CB  1 
ATOM   427  C  CG  . LEU A 1 57  ? 5.134  12.011  2.818   1.00 21.40 ? 57  LEU A CG  1 
ATOM   428  C  CD1 . LEU A 1 57  ? 6.084  13.102  3.226   1.00 24.56 ? 57  LEU A CD1 1 
ATOM   429  C  CD2 . LEU A 1 57  ? 4.046  12.518  1.870   1.00 24.44 ? 57  LEU A CD2 1 
ATOM   430  N  N   . ARG A 1 58  ? 6.921  8.008   1.587   1.00 15.55 ? 58  ARG A N   1 
ATOM   431  C  CA  . ARG A 1 58  ? 8.047  7.416   0.860   1.00 14.37 ? 58  ARG A CA  1 
ATOM   432  C  C   . ARG A 1 58  ? 8.548  6.259   1.674   1.00 13.72 ? 58  ARG A C   1 
ATOM   433  O  O   . ARG A 1 58  ? 8.408  6.249   2.890   1.00 13.52 ? 58  ARG A O   1 
ATOM   434  C  CB  . ARG A 1 58  ? 9.197  8.464   0.739   1.00 15.95 ? 58  ARG A CB  1 
ATOM   435  C  CG  . ARG A 1 58  ? 10.165 8.184   -0.359  1.00 18.82 ? 58  ARG A CG  1 
ATOM   436  C  CD  . ARG A 1 58  ? 11.127 9.339   -0.465  1.00 19.14 ? 58  ARG A CD  1 
ATOM   437  N  NE  . ARG A 1 58  ? 12.006 9.203   0.702   1.00 17.69 ? 58  ARG A NE  1 
ATOM   438  C  CZ  . ARG A 1 58  ? 13.333 9.319   0.640   1.00 17.72 ? 58  ARG A CZ  1 
ATOM   439  N  NH1 . ARG A 1 58  ? 13.931 9.592   -0.543  1.00 18.15 ? 58  ARG A NH1 1 
ATOM   440  N  NH2 . ARG A 1 58  ? 14.022 9.207   1.761   1.00 19.31 ? 58  ARG A NH2 1 
ATOM   441  N  N   . ILE A 1 59  ? 9.134  5.310   0.980   1.00 12.22 ? 59  ILE A N   1 
ATOM   442  C  CA  . ILE A 1 59  ? 9.787  4.183   1.639   1.00 11.09 ? 59  ILE A CA  1 
ATOM   443  C  C   . ILE A 1 59  ? 11.226 4.142   1.146   1.00 12.76 ? 59  ILE A C   1 
ATOM   444  O  O   . ILE A 1 59  ? 11.499 4.266   -0.046  1.00 12.41 ? 59  ILE A O   1 
ATOM   445  C  CB  . ILE A 1 59  ? 8.955  2.884   1.450   1.00 11.01 ? 59  ILE A CB  1 
ATOM   446  C  CG1 . ILE A 1 59  ? 9.550  1.709   2.278   1.00 10.73 ? 59  ILE A CG1 1 
ATOM   447  C  CG2 . ILE A 1 59  ? 8.911  2.481   -0.049  1.00 10.70 ? 59  ILE A CG2 1 
ATOM   448  C  CD1 . ILE A 1 59  ? 8.752  0.378   2.132   1.00 11.04 ? 59  ILE A CD1 1 
ATOM   449  N  N   . LEU A 1 60  ? 12.161 3.977   2.087   1.00 11.86 ? 60  LEU A N   1 
ATOM   450  C  CA  . LEU A 1 60  ? 13.580 4.085   1.785   1.00 11.58 ? 60  LEU A CA  1 
ATOM   451  C  C   . LEU A 1 60  ? 14.352 2.880   2.324   1.00 12.47 ? 60  LEU A C   1 
ATOM   452  O  O   . LEU A 1 60  ? 14.134 2.480   3.484   1.00 12.42 ? 60  LEU A O   1 
ATOM   453  C  CB  . LEU A 1 60  ? 14.118 5.392   2.430   1.00 11.27 ? 60  LEU A CB  1 
ATOM   454  C  CG  . LEU A 1 60  ? 15.670 5.487   2.419   1.00 11.54 ? 60  LEU A CG  1 
ATOM   455  C  CD1 . LEU A 1 60  ? 16.242 5.575   1.005   1.00 14.77 ? 60  LEU A CD1 1 
ATOM   456  C  CD2 . LEU A 1 60  ? 16.161 6.662   3.313   1.00 11.28 ? 60  LEU A CD2 1 
ATOM   457  N  N   . ASN A 1 61  ? 15.156 2.227   1.464   1.00 11.11 ? 61  ASN A N   1 
ATOM   458  C  CA  . ASN A 1 61  ? 16.181 1.322   1.950   1.00 11.68 ? 61  ASN A CA  1 
ATOM   459  C  C   . ASN A 1 61  ? 17.440 2.113   2.330   1.00 13.00 ? 61  ASN A C   1 
ATOM   460  O  O   . ASN A 1 61  ? 18.088 2.664   1.488   1.00 12.95 ? 61  ASN A O   1 
ATOM   461  C  CB  . ASN A 1 61  ? 16.490 0.297   0.853   1.00 11.81 ? 61  ASN A CB  1 
ATOM   462  C  CG  . ASN A 1 61  ? 17.515 -0.684  1.251   1.00 11.78 ? 61  ASN A CG  1 
ATOM   463  O  OD1 . ASN A 1 61  ? 18.399 -0.406  2.083   1.00 13.94 ? 61  ASN A OD1 1 
ATOM   464  N  ND2 . ASN A 1 61  ? 17.435 -1.878  0.677   1.00 11.87 ? 61  ASN A ND2 1 
ATOM   465  N  N   . ASN A 1 62  ? 17.765 2.185   3.617   1.00 13.13 ? 62  ASN A N   1 
ATOM   466  C  CA  . ASN A 1 62  ? 18.892 3.013   4.041   1.00 14.56 ? 62  ASN A CA  1 
ATOM   467  C  C   . ASN A 1 62  ? 20.137 2.205   4.311   1.00 14.37 ? 62  ASN A C   1 
ATOM   468  O  O   . ASN A 1 62  ? 21.140 2.735   4.903   1.00 16.59 ? 62  ASN A O   1 
ATOM   469  C  CB  . ASN A 1 62  ? 18.488 3.845   5.278   1.00 14.37 ? 62  ASN A CB  1 
ATOM   470  C  CG  . ASN A 1 62  ? 18.157 2.968   6.488   1.00 14.78 ? 62  ASN A CG  1 
ATOM   471  O  OD1 . ASN A 1 62  ? 18.583 1.810   6.605   1.00 13.74 ? 62  ASN A OD1 1 
ATOM   472  N  ND2 . ASN A 1 62  ? 17.445 3.551   7.418   1.00 19.69 ? 62  ASN A ND2 1 
ATOM   473  N  N   . GLY A 1 63  ? 20.146 0.927   3.888   1.00 12.73 ? 63  GLY A N   1 
ATOM   474  C  CA  . GLY A 1 63  ? 21.304 0.092   4.002   1.00 12.86 ? 63  GLY A CA  1 
ATOM   475  C  C   . GLY A 1 63  ? 21.366 -0.679  5.294   1.00 13.99 ? 63  GLY A C   1 
ATOM   476  O  O   . GLY A 1 63  ? 22.252 -1.506  5.462   1.00 14.63 ? 63  GLY A O   1 
ATOM   477  N  N   . HIS A 1 64  ? 20.419 -0.410  6.188   1.00 14.60 ? 64  HIS A N   1 
ATOM   478  C  CA  . HIS A 1 64  ? 20.383 -1.146  7.489   1.00 16.32 ? 64  HIS A CA  1 
ATOM   479  C  C   . HIS A 1 64  ? 19.013 -1.761  7.635   1.00 16.00 ? 64  HIS A C   1 
ATOM   480  O  O   . HIS A 1 64  ? 18.916 -2.913  8.109   1.00 18.15 ? 64  HIS A O   1 
ATOM   481  C  CB  . HIS A 1 64  ? 20.663 -0.226  8.663   1.00 19.26 ? 64  HIS A CB  1 
ATOM   482  C  CG  . HIS A 1 64  ? 21.892 0.672   8.477   1.00 24.36 ? 64  HIS A CG  1 
ATOM   483  N  ND1 . HIS A 1 64  ? 23.181 0.178   8.539   1.00 24.70 ? 64  HIS A ND1 1 
ATOM   484  C  CD2 . HIS A 1 64  ? 22.003 2.047   8.260   1.00 23.52 ? 64  HIS A CD2 1 
ATOM   485  C  CE1 . HIS A 1 64  ? 24.076 1.191   8.346   1.00 24.68 ? 64  HIS A CE1 1 
ATOM   486  N  NE2 . HIS A 1 64  ? 23.391 2.327   8.163   1.00 24.26 ? 64  HIS A NE2 1 
ATOM   487  N  N   . ALA A 1 65  ? 17.977 -1.022  7.235   1.00 13.07 ? 65  ALA A N   1 
ATOM   488  C  CA  . ALA A 1 65  ? 16.590 -1.463  7.332   1.00 12.01 ? 65  ALA A CA  1 
ATOM   489  C  C   . ALA A 1 65  ? 15.818 -0.714  6.234   1.00 10.58 ? 65  ALA A C   1 
ATOM   490  O  O   . ALA A 1 65  ? 16.483 -0.104  5.380   1.00 11.35 ? 65  ALA A O   1 
ATOM   491  C  CB  . ALA A 1 65  ? 16.012 -1.235  8.706   1.00 11.82 ? 65  ALA A CB  1 
ATOM   492  N  N   . PHE A 1 66  ? 14.501 -0.803  6.194   1.00 9.80  ? 66  PHE A N   1 
ATOM   493  C  CA  . PHE A 1 66  ? 13.737 0.185   5.385   1.00 9.93  ? 66  PHE A CA  1 
ATOM   494  C  C   . PHE A 1 66  ? 12.877 1.064   6.262   1.00 10.09 ? 66  PHE A C   1 
ATOM   495  O  O   . PHE A 1 66  ? 12.243 0.582   7.211   1.00 10.14 ? 66  PHE A O   1 
ATOM   496  C  CB  . PHE A 1 66  ? 12.895 -0.439  4.266   1.00 10.33 ? 66  PHE A CB  1 
ATOM   497  C  CG  . PHE A 1 66  ? 11.886 -1.409  4.773   1.00 11.02 ? 66  PHE A CG  1 
ATOM   498  C  CD1 . PHE A 1 66  ? 10.588 -0.973  5.091   1.00 10.91 ? 66  PHE A CD1 1 
ATOM   499  C  CD2 . PHE A 1 66  ? 12.212 -2.777  4.858   1.00 10.28 ? 66  PHE A CD2 1 
ATOM   500  C  CE1 . PHE A 1 66  ? 9.638  -1.874  5.578   1.00 11.88 ? 66  PHE A CE1 1 
ATOM   501  C  CE2 . PHE A 1 66  ? 11.267 -3.698  5.379   1.00 11.31 ? 66  PHE A CE2 1 
ATOM   502  C  CZ  . PHE A 1 66  ? 10.005 -3.247  5.719   1.00 11.16 ? 66  PHE A CZ  1 
ATOM   503  N  N   . ASN A 1 67  ? 12.820 2.369   5.940   1.00 10.68 ? 67  ASN A N   1 
ATOM   504  C  CA  . ASN A 1 67  ? 11.940 3.260   6.699   1.00 9.97  ? 67  ASN A CA  1 
ATOM   505  C  C   . ASN A 1 67  ? 10.761 3.651   5.844   1.00 11.03 ? 67  ASN A C   1 
ATOM   506  O  O   . ASN A 1 67  ? 10.970 4.043   4.674   1.00 11.12 ? 67  ASN A O   1 
ATOM   507  C  CB  . ASN A 1 67  ? 12.668 4.553   7.000   1.00 11.27 ? 67  ASN A CB  1 
ATOM   508  C  CG  . ASN A 1 67  ? 13.800 4.360   7.982   1.00 13.96 ? 67  ASN A CG  1 
ATOM   509  O  OD1 . ASN A 1 67  ? 13.837 3.350   8.654   1.00 14.67 ? 67  ASN A OD1 1 
ATOM   510  N  ND2 . ASN A 1 67  ? 14.747 5.331   8.062   1.00 17.73 ? 67  ASN A ND2 1 
ATOM   511  N  N   . VAL A 1 68  ? 9.577  3.563   6.413   1.00 9.94  ? 68  VAL A N   1 
ATOM   512  C  CA  . VAL A 1 68  ? 8.364  4.183   5.830   1.00 11.21 ? 68  VAL A CA  1 
ATOM   513  C  C   . VAL A 1 68  ? 8.232  5.546   6.502   1.00 13.88 ? 68  VAL A C   1 
ATOM   514  O  O   . VAL A 1 68  ? 8.085  5.660   7.751   1.00 11.66 ? 68  VAL A O   1 
ATOM   515  C  CB  . VAL A 1 68  ? 7.107  3.309   5.994   1.00 11.77 ? 68  VAL A CB  1 
ATOM   516  C  CG1 . VAL A 1 68  ? 5.825  4.084   5.560   1.00 12.05 ? 68  VAL A CG1 1 
ATOM   517  C  CG2 . VAL A 1 68  ? 7.252  2.016   5.221   1.00 11.64 ? 68  VAL A CG2 1 
ATOM   518  N  N   . GLU A 1 69  ? 8.245  6.608   5.682   1.00 12.58 ? 69  GLU A N   1 
ATOM   519  C  CA  . GLU A 1 69  ? 8.440  7.969   6.247   1.00 12.43 ? 69  GLU A CA  1 
ATOM   520  C  C   . GLU A 1 69  ? 7.125  8.702   6.171   1.00 13.32 ? 69  GLU A C   1 
ATOM   521  O  O   . GLU A 1 69  ? 6.350  8.495   5.228   1.00 13.27 ? 69  GLU A O   1 
ATOM   522  C  CB  . GLU A 1 69  ? 9.413  8.752   5.376   1.00 14.93 ? 69  GLU A CB  1 
ATOM   523  C  CG  . GLU A 1 69  ? 10.805 8.168   5.342   1.00 14.68 ? 69  GLU A CG  1 
ATOM   524  C  CD  . GLU A 1 69  ? 11.601 8.670   4.157   1.00 17.04 ? 69  GLU A CD  1 
ATOM   525  O  OE1 . GLU A 1 69  ? 11.022 9.407   3.300   1.00 19.33 ? 69  GLU A OE1 1 
ATOM   526  O  OE2 . GLU A 1 69  ? 12.792 8.302   4.053   1.00 18.96 ? 69  GLU A OE2 1 
ATOM   527  N  N   . PHE A 1 70  ? 6.875  9.566   7.143   1.00 11.81 ? 70  PHE A N   1 
ATOM   528  C  CA  . PHE A 1 70  ? 5.558  10.246  7.212   1.00 11.91 ? 70  PHE A CA  1 
ATOM   529  C  C   . PHE A 1 70  ? 5.767  11.740  7.126   1.00 13.59 ? 70  PHE A C   1 
ATOM   530  O  O   . PHE A 1 70  ? 6.856  12.220  7.485   1.00 14.33 ? 70  PHE A O   1 
ATOM   531  C  CB  . PHE A 1 70  ? 4.866  9.855   8.537   1.00 11.99 ? 70  PHE A CB  1 
ATOM   532  C  CG  . PHE A 1 70  ? 4.296  8.480   8.468   1.00 11.73 ? 70  PHE A CG  1 
ATOM   533  C  CD1 . PHE A 1 70  ? 5.095  7.353   8.660   1.00 10.64 ? 70  PHE A CD1 1 
ATOM   534  C  CD2 . PHE A 1 70  ? 2.935  8.288   8.208   1.00 10.69 ? 70  PHE A CD2 1 
ATOM   535  C  CE1 . PHE A 1 70  ? 4.518  6.044   8.552   1.00 10.38 ? 70  PHE A CE1 1 
ATOM   536  C  CE2 . PHE A 1 70  ? 2.387  7.032   8.031   1.00 11.04 ? 70  PHE A CE2 1 
ATOM   537  C  CZ  . PHE A 1 70  ? 3.196  5.896   8.188   1.00 11.13 ? 70  PHE A CZ  1 
ATOM   538  N  N   . ASP A 1 71  ? 4.753  12.495  6.684   1.00 14.97 ? 71  ASP A N   1 
ATOM   539  C  CA  . ASP A 1 71  ? 4.781  13.926  6.898   1.00 16.46 ? 71  ASP A CA  1 
ATOM   540  C  C   . ASP A 1 71  ? 4.524  14.330  8.365   1.00 16.80 ? 71  ASP A C   1 
ATOM   541  O  O   . ASP A 1 71  ? 3.430  14.055  8.943   1.00 19.21 ? 71  ASP A O   1 
ATOM   542  C  CB  . ASP A 1 71  ? 3.735  14.526  5.978   1.00 17.29 ? 71  ASP A CB  1 
ATOM   543  C  CG  . ASP A 1 71  ? 3.601  16.053  6.167   1.00 20.75 ? 71  ASP A CG  1 
ATOM   544  O  OD1 . ASP A 1 71  ? 4.477  16.691  6.815   1.00 19.18 ? 71  ASP A OD1 1 
ATOM   545  O  OD2 . ASP A 1 71  ? 2.569  16.579  5.736   1.00 22.84 ? 71  ASP A OD2 1 
ATOM   546  N  N   . ASP A 1 72  ? 5.547  14.925  9.006   1.00 16.81 ? 72  ASP A N   1 
ATOM   547  C  CA  . ASP A 1 72  ? 5.463  15.258  10.422  1.00 17.63 ? 72  ASP A CA  1 
ATOM   548  C  C   . ASP A 1 72  ? 5.533  16.775  10.588  1.00 24.05 ? 72  ASP A C   1 
ATOM   549  O  O   . ASP A 1 72  ? 5.977  17.248  11.636  1.00 21.51 ? 72  ASP A O   1 
ATOM   550  C  CB  . ASP A 1 72  ? 6.647  14.603  11.232  1.00 18.24 ? 72  ASP A CB  1 
ATOM   551  C  CG  . ASP A 1 72  ? 8.019  15.116  10.809  1.00 20.56 ? 72  ASP A CG  1 
ATOM   552  O  OD1 . ASP A 1 72  ? 8.116  15.829  9.787   1.00 17.96 ? 72  ASP A OD1 1 
ATOM   553  O  OD2 . ASP A 1 72  ? 9.023  14.835  11.518  1.00 16.74 ? 72  ASP A OD2 1 
ATOM   554  N  N   . SER A 1 73  ? 5.152  17.515  9.543   1.00 21.10 ? 73  SER A N   1 
ATOM   555  C  CA  . SER A 1 73  ? 5.164  19.003  9.614   1.00 25.35 ? 73  SER A CA  1 
ATOM   556  C  C   . SER A 1 73  ? 3.848  19.556  10.201  1.00 27.53 ? 73  SER A C   1 
ATOM   557  O  O   . SER A 1 73  ? 3.633  20.791  10.229  1.00 26.51 ? 73  SER A O   1 
ATOM   558  C  CB  . SER A 1 73  ? 5.457  19.592  8.236   1.00 23.28 ? 73  SER A CB  1 
ATOM   559  O  OG  . SER A 1 73  ? 4.347  19.351  7.363   1.00 23.41 ? 73  SER A OG  1 
ATOM   560  N  N   . GLN A 1 74  ? 2.983  18.659  10.701  1.00 26.16 ? 74  GLN A N   1 
ATOM   561  C  CA  . GLN A 1 74  ? 1.729  19.053  11.357  1.00 26.54 ? 74  GLN A CA  1 
ATOM   562  C  C   . GLN A 1 74  ? 1.298  17.956  12.264  1.00 27.11 ? 74  GLN A C   1 
ATOM   563  O  O   . GLN A 1 74  ? 1.821  16.902  12.074  1.00 26.14 ? 74  GLN A O   1 
ATOM   564  C  CB  . GLN A 1 74  ? 0.637  19.148  10.318  1.00 30.42 ? 74  GLN A CB  1 
ATOM   565  C  CG  . GLN A 1 74  ? 0.641  20.424  9.557   1.00 32.72 ? 74  GLN A CG  1 
ATOM   566  C  CD  . GLN A 1 74  ? -0.699 20.620  8.925   1.00 33.37 ? 74  GLN A CD  1 
ATOM   567  O  OE1 . GLN A 1 74  ? -1.625 21.164  9.566   1.00 39.58 ? 74  GLN A OE1 1 
ATOM   568  N  NE2 . GLN A 1 74  ? -0.841 20.141  7.694   1.00 26.20 ? 74  GLN A NE2 1 
ATOM   569  N  N   . ASP A 1 75  ? 0.391  18.185  13.229  1.00 30.20 ? 75  ASP A N   1 
ATOM   570  C  CA  . ASP A 1 75  ? -0.048 17.121  14.168  1.00 29.31 ? 75  ASP A CA  1 
ATOM   571  C  C   . ASP A 1 75  ? -1.046 16.231  13.457  1.00 29.45 ? 75  ASP A C   1 
ATOM   572  O  O   . ASP A 1 75  ? -2.243 16.560  13.439  1.00 35.36 ? 75  ASP A O   1 
ATOM   573  C  CB  . ASP A 1 75  ? -0.746 17.655  15.435  1.00 33.50 ? 75  ASP A CB  1 
ATOM   574  C  CG  . ASP A 1 75  ? 0.235  17.950  16.567  1.00 38.19 ? 75  ASP A CG  1 
ATOM   575  O  OD1 . ASP A 1 75  ? 1.430  17.620  16.440  1.00 39.37 ? 75  ASP A OD1 1 
ATOM   576  O  OD2 . ASP A 1 75  ? -0.189 18.518  17.590  1.00 42.85 ? 75  ASP A OD2 1 
ATOM   577  N  N   . LYS A 1 76  ? -0.571 15.154  12.858  1.00 24.23 ? 76  LYS A N   1 
ATOM   578  C  CA  . LYS A 1 76  ? -1.439 14.261  12.014  1.00 27.42 ? 76  LYS A CA  1 
ATOM   579  C  C   . LYS A 1 76  ? -1.486 12.798  12.476  1.00 29.17 ? 76  LYS A C   1 
ATOM   580  O  O   . LYS A 1 76  ? -2.486 12.079  12.276  1.00 33.28 ? 76  LYS A O   1 
ATOM   581  C  CB  . LYS A 1 76  ? -0.913 14.213  10.583  1.00 26.39 ? 76  LYS A CB  1 
ATOM   582  C  CG  . LYS A 1 76  ? -1.289 15.401  9.717   1.00 29.63 ? 76  LYS A CG  1 
ATOM   583  C  CD  . LYS A 1 76  ? -0.609 15.252  8.370   1.00 31.92 ? 76  LYS A CD  1 
ATOM   584  C  CE  . LYS A 1 76  ? -1.253 16.129  7.291   1.00 35.82 ? 76  LYS A CE  1 
ATOM   585  N  NZ  . LYS A 1 76  ? -0.521 15.975  6.011   1.00 29.63 ? 76  LYS A NZ  1 
ATOM   586  N  N   . ALA A 1 77  ? -0.372 12.324  13.003  1.00 24.90 ? 77  ALA A N   1 
ATOM   587  C  CA  . ALA A 1 77  ? -0.269 10.943  13.479  1.00 18.94 ? 77  ALA A CA  1 
ATOM   588  C  C   . ALA A 1 77  ? 0.519  11.156  14.794  1.00 19.08 ? 77  ALA A C   1 
ATOM   589  O  O   . ALA A 1 77  ? 1.713  11.446  14.736  1.00 19.99 ? 77  ALA A O   1 
ATOM   590  C  CB  . ALA A 1 77  ? 0.525  10.123  12.475  1.00 18.92 ? 77  ALA A CB  1 
ATOM   591  N  N   . VAL A 1 78  ? -0.153 11.111  15.932  1.00 16.87 ? 78  VAL A N   1 
ATOM   592  C  CA  . VAL A 1 78  ? 0.503  11.309  17.246  1.00 16.42 ? 78  VAL A CA  1 
ATOM   593  C  C   . VAL A 1 78  ? 0.219  10.207  18.274  1.00 15.30 ? 78  VAL A C   1 
ATOM   594  O  O   . VAL A 1 78  ? -0.800 9.497   18.320  1.00 16.01 ? 78  VAL A O   1 
ATOM   595  C  CB  . VAL A 1 78  ? 0.111  12.663  17.876  1.00 18.99 ? 78  VAL A CB  1 
ATOM   596  C  CG1 . VAL A 1 78  ? 0.356  13.792  16.895  1.00 19.46 ? 78  VAL A CG1 1 
ATOM   597  C  CG2 . VAL A 1 78  ? -1.328 12.617  18.261  1.00 19.13 ? 78  VAL A CG2 1 
ATOM   598  N  N   . LEU A 1 79  ? 1.222  10.090  19.117  1.00 12.70 ? 79  LEU A N   1 
ATOM   599  C  CA  . LEU A 1 79  ? 1.177  9.206   20.225  1.00 13.30 ? 79  LEU A CA  1 
ATOM   600  C  C   . LEU A 1 79  ? 1.205  10.095  21.440  1.00 13.53 ? 79  LEU A C   1 
ATOM   601  O  O   . LEU A 1 79  ? 2.011  11.050  21.539  1.00 13.55 ? 79  LEU A O   1 
ATOM   602  C  CB  . LEU A 1 79  ? 2.422  8.287   20.111  1.00 13.00 ? 79  LEU A CB  1 
ATOM   603  C  CG  . LEU A 1 79  ? 2.563  7.259   21.203  1.00 14.99 ? 79  LEU A CG  1 
ATOM   604  C  CD1 . LEU A 1 79  ? 1.494  6.155   21.146  1.00 17.64 ? 79  LEU A CD1 1 
ATOM   605  C  CD2 . LEU A 1 79  ? 3.955  6.654   21.068  1.00 11.97 ? 79  LEU A CD2 1 
ATOM   606  N  N   A LYS A 1 80  ? 0.334  9.796   22.385  0.50 13.60 ? 80  LYS A N   1 
ATOM   607  N  N   B LYS A 1 80  ? 0.311  9.808   22.374  0.50 13.69 ? 80  LYS A N   1 
ATOM   608  C  CA  A LYS A 1 80  ? 0.329  10.494  23.668  0.50 15.36 ? 80  LYS A CA  1 
ATOM   609  C  CA  B LYS A 1 80  ? 0.204  10.545  23.639  0.50 15.46 ? 80  LYS A CA  1 
ATOM   610  C  C   A LYS A 1 80  ? -0.254 9.596   24.760  0.50 14.73 ? 80  LYS A C   1 
ATOM   611  C  C   B LYS A 1 80  ? -0.255 9.594   24.755  0.50 14.81 ? 80  LYS A C   1 
ATOM   612  O  O   A LYS A 1 80  ? -0.632 8.464   24.497  0.50 13.85 ? 80  LYS A O   1 
ATOM   613  O  O   B LYS A 1 80  ? -0.586 8.444   24.497  0.50 13.80 ? 80  LYS A O   1 
ATOM   614  C  CB  A LYS A 1 80  ? -0.390 11.851  23.571  0.50 17.56 ? 80  LYS A CB  1 
ATOM   615  C  CB  B LYS A 1 80  ? -0.801 11.696  23.534  0.50 18.32 ? 80  LYS A CB  1 
ATOM   616  C  CG  A LYS A 1 80  ? -1.890 11.750  23.277  0.50 18.82 ? 80  LYS A CG  1 
ATOM   617  C  CG  B LYS A 1 80  ? -0.584 12.724  22.428  0.50 18.89 ? 80  LYS A CG  1 
ATOM   618  C  CD  A LYS A 1 80  ? -2.488 13.115  22.916  0.50 22.12 ? 80  LYS A CD  1 
ATOM   619  C  CD  B LYS A 1 80  ? -1.901 13.465  22.209  0.50 22.43 ? 80  LYS A CD  1 
ATOM   620  C  CE  A LYS A 1 80  ? -1.709 13.863  21.828  0.50 23.26 ? 80  LYS A CE  1 
ATOM   621  C  CE  B LYS A 1 80  ? -2.760 13.453  23.477  0.50 24.78 ? 80  LYS A CE  1 
ATOM   622  N  NZ  A LYS A 1 80  ? -2.489 14.940  21.128  0.50 26.88 ? 80  LYS A NZ  1 
ATOM   623  N  NZ  B LYS A 1 80  ? -4.215 13.448  23.100  0.50 26.78 ? 80  LYS A NZ  1 
ATOM   624  N  N   . GLY A 1 81  ? -0.237 10.070  26.008  1.00 14.97 ? 81  GLY A N   1 
ATOM   625  C  CA  . GLY A 1 81  ? -0.821 9.328   27.110  1.00 15.90 ? 81  GLY A CA  1 
ATOM   626  C  C   . GLY A 1 81  ? 0.109  8.234   27.464  1.00 18.24 ? 81  GLY A C   1 
ATOM   627  O  O   . GLY A 1 81  ? 1.316  8.355   27.208  1.00 17.34 ? 81  GLY A O   1 
ATOM   628  N  N   . GLY A 1 82  ? -0.398 7.150   28.043  1.00 17.49 ? 82  GLY A N   1 
ATOM   629  C  CA  . GLY A 1 82  ? 0.557  6.149   28.489  1.00 17.90 ? 82  GLY A CA  1 
ATOM   630  C  C   . GLY A 1 82  ? 1.530  6.761   29.520  1.00 16.14 ? 82  GLY A C   1 
ATOM   631  O  O   . GLY A 1 82  ? 1.134  7.541   30.440  1.00 17.69 ? 82  GLY A O   1 
ATOM   632  N  N   . PRO A 1 83  ? 2.875  6.511   29.375  1.00 12.99 ? 83  PRO A N   1 
ATOM   633  C  CA  . PRO A 1 83  ? 3.821  7.139   30.269  1.00 14.74 ? 83  PRO A CA  1 
ATOM   634  C  C   . PRO A 1 83  ? 4.241  8.563   29.805  1.00 14.54 ? 83  PRO A C   1 
ATOM   635  O  O   . PRO A 1 83  ? 5.079  9.195   30.429  1.00 17.35 ? 83  PRO A O   1 
ATOM   636  C  CB  . PRO A 1 83  ? 5.079  6.217   30.107  1.00 14.50 ? 83  PRO A CB  1 
ATOM   637  C  CG  . PRO A 1 83  ? 5.019  5.820   28.682  1.00 12.10 ? 83  PRO A CG  1 
ATOM   638  C  CD  . PRO A 1 83  ? 3.564  5.634   28.353  1.00 12.52 ? 83  PRO A CD  1 
ATOM   639  N  N   . LEU A 1 84  ? 3.710  9.040   28.700  1.00 13.61 ? 84  LEU A N   1 
ATOM   640  C  CA  . LEU A 1 84  ? 4.231  10.268  28.081  1.00 13.13 ? 84  LEU A CA  1 
ATOM   641  C  C   . LEU A 1 84  ? 3.548  11.504  28.641  1.00 15.73 ? 84  LEU A C   1 
ATOM   642  O  O   . LEU A 1 84  ? 2.373  11.455  29.011  1.00 17.75 ? 84  LEU A O   1 
ATOM   643  C  CB  . LEU A 1 84  ? 3.995  10.224  26.584  1.00 13.29 ? 84  LEU A CB  1 
ATOM   644  C  CG  . LEU A 1 84  ? 4.532  8.932   25.885  1.00 12.81 ? 84  LEU A CG  1 
ATOM   645  C  CD1 . LEU A 1 84  ? 4.061  8.875   24.446  1.00 13.22 ? 84  LEU A CD1 1 
ATOM   646  C  CD2 . LEU A 1 84  ? 6.086  8.838   26.010  1.00 12.81 ? 84  LEU A CD2 1 
ATOM   647  N  N   . ASP A 1 85  ? 4.317  12.584  28.694  1.00 16.73 ? 85  ASP A N   1 
ATOM   648  C  CA  . ASP A 1 85  ? 3.803  13.954  28.886  1.00 20.74 ? 85  ASP A CA  1 
ATOM   649  C  C   . ASP A 1 85  ? 3.843  14.599  27.542  1.00 22.26 ? 85  ASP A C   1 
ATOM   650  O  O   . ASP A 1 85  ? 4.841  14.503  26.817  1.00 24.29 ? 85  ASP A O   1 
ATOM   651  C  CB  . ASP A 1 85  ? 4.702  14.706  29.868  1.00 25.15 ? 85  ASP A CB  1 
ATOM   652  C  CG  . ASP A 1 85  ? 4.568  14.163  31.260  1.00 34.01 ? 85  ASP A CG  1 
ATOM   653  O  OD1 . ASP A 1 85  ? 3.471  13.632  31.594  1.00 35.48 ? 85  ASP A OD1 1 
ATOM   654  O  OD2 . ASP A 1 85  ? 5.549  14.264  32.036  1.00 38.60 ? 85  ASP A OD2 1 
ATOM   655  N  N   . GLY A 1 86  ? 2.782  15.276  27.169  1.00 25.07 ? 86  GLY A N   1 
ATOM   656  C  CA  . GLY A 1 86  ? 2.812  15.973  25.896  1.00 21.75 ? 86  GLY A CA  1 
ATOM   657  C  C   . GLY A 1 86  ? 2.557  15.050  24.672  1.00 21.71 ? 86  GLY A C   1 
ATOM   658  O  O   . GLY A 1 86  ? 1.954  13.968  24.781  1.00 20.86 ? 86  GLY A O   1 
ATOM   659  N  N   . THR A 1 87  ? 2.982  15.527  23.514  1.00 15.32 ? 87  THR A N   1 
ATOM   660  C  CA  . THR A 1 87  ? 2.519  14.966  22.259  1.00 16.67 ? 87  THR A CA  1 
ATOM   661  C  C   . THR A 1 87  ? 3.693  14.603  21.411  1.00 15.04 ? 87  THR A C   1 
ATOM   662  O  O   . THR A 1 87  ? 4.584  15.402  21.214  1.00 14.44 ? 87  THR A O   1 
ATOM   663  C  CB  . THR A 1 87  ? 1.707  16.020  21.472  1.00 20.37 ? 87  THR A CB  1 
ATOM   664  O  OG1 . THR A 1 87  ? 0.427  16.143  22.116  1.00 26.25 ? 87  THR A OG1 1 
ATOM   665  C  CG2 . THR A 1 87  ? 1.486  15.610  20.024  1.00 21.87 ? 87  THR A CG2 1 
ATOM   666  N  N   . TYR A 1 88  ? 3.669  13.382  20.903  1.00 12.69 ? 88  TYR A N   1 
ATOM   667  C  CA  . TYR A 1 88  ? 4.785  12.916  20.052  1.00 12.85 ? 88  TYR A CA  1 
ATOM   668  C  C   . TYR A 1 88  ? 4.281  12.630  18.656  1.00 12.45 ? 88  TYR A C   1 
ATOM   669  O  O   . TYR A 1 88  ? 3.327  11.866  18.501  1.00 15.75 ? 88  TYR A O   1 
ATOM   670  C  CB  . TYR A 1 88  ? 5.474  11.676  20.656  1.00 11.64 ? 88  TYR A CB  1 
ATOM   671  C  CG  . TYR A 1 88  ? 6.228  11.881  21.985  1.00 11.31 ? 88  TYR A CG  1 
ATOM   672  C  CD1 . TYR A 1 88  ? 5.545  12.229  23.162  1.00 10.36 ? 88  TYR A CD1 1 
ATOM   673  C  CD2 . TYR A 1 88  ? 7.623  11.721  22.049  1.00 11.19 ? 88  TYR A CD2 1 
ATOM   674  C  CE1 . TYR A 1 88  ? 6.232  12.409  24.379  1.00 10.60 ? 88  TYR A CE1 1 
ATOM   675  C  CE2 . TYR A 1 88  ? 8.308  11.913  23.235  1.00 10.00 ? 88  TYR A CE2 1 
ATOM   676  C  CZ  . TYR A 1 88  ? 7.611  12.244  24.381  1.00 9.91  ? 88  TYR A CZ  1 
ATOM   677  O  OH  . TYR A 1 88  ? 8.250  12.368  25.548  1.00 9.04  ? 88  TYR A OH  1 
ATOM   678  N  N   . ARG A 1 89  ? 4.928  13.215  17.636  1.00 11.54 ? 89  ARG A N   1 
ATOM   679  C  CA  . ARG A 1 89  ? 4.535  12.965  16.269  1.00 11.59 ? 89  ARG A CA  1 
ATOM   680  C  C   . ARG A 1 89  ? 5.201  11.733  15.716  1.00 10.34 ? 89  ARG A C   1 
ATOM   681  O  O   . ARG A 1 89  ? 6.335  11.397  16.071  1.00 8.83  ? 89  ARG A O   1 
ATOM   682  C  CB  . ARG A 1 89  ? 4.914  14.143  15.397  1.00 14.95 ? 89  ARG A CB  1 
ATOM   683  C  CG  . ARG A 1 89  ? 3.893  15.236  15.469  1.00 18.85 ? 89  ARG A CG  1 
ATOM   684  C  CD  . ARG A 1 89  ? 4.191  16.309  14.459  1.00 19.10 ? 89  ARG A CD  1 
ATOM   685  N  NE  . ARG A 1 89  ? 3.457  17.500  14.841  1.00 22.09 ? 89  ARG A NE  1 
ATOM   686  C  CZ  . ARG A 1 89  ? 3.777  18.732  14.472  1.00 23.17 ? 89  ARG A CZ  1 
ATOM   687  N  NH1 . ARG A 1 89  ? 4.832  18.948  13.697  1.00 20.80 ? 89  ARG A NH1 1 
ATOM   688  N  NH2 . ARG A 1 89  ? 3.037  19.752  14.879  1.00 21.75 ? 89  ARG A NH2 1 
ATOM   689  N  N   . LEU A 1 90  ? 4.488  11.063  14.827  1.00 9.86  ? 90  LEU A N   1 
ATOM   690  C  CA  . LEU A 1 90  ? 5.107  10.015  14.024  1.00 9.76  ? 90  LEU A CA  1 
ATOM   691  C  C   . LEU A 1 90  ? 5.964  10.537  12.884  1.00 10.29 ? 90  LEU A C   1 
ATOM   692  O  O   . LEU A 1 90  ? 5.507  11.296  12.037  1.00 12.22 ? 90  LEU A O   1 
ATOM   693  C  CB  . LEU A 1 90  ? 4.050  9.090   13.436  1.00 10.62 ? 90  LEU A CB  1 
ATOM   694  C  CG  . LEU A 1 90  ? 4.546  7.919   12.595  1.00 9.32  ? 90  LEU A CG  1 
ATOM   695  C  CD1 . LEU A 1 90  ? 5.311  6.842   13.382  1.00 11.14 ? 90  LEU A CD1 1 
ATOM   696  C  CD2 . LEU A 1 90  ? 3.305  7.250   11.952  1.00 9.23  ? 90  LEU A CD2 1 
ATOM   697  N  N   . ILE A 1 91  ? 7.176  10.017  12.823  1.00 9.01  ? 91  ILE A N   1 
ATOM   698  C  CA  . ILE A 1 91  ? 8.121  10.421  11.721  1.00 9.17  ? 91  ILE A CA  1 
ATOM   699  C  C   . ILE A 1 91  ? 8.417  9.262   10.764  1.00 9.72  ? 91  ILE A C   1 
ATOM   700  O  O   . ILE A 1 91  ? 8.510  9.473   9.562   1.00 9.80  ? 91  ILE A O   1 
ATOM   701  C  CB  . ILE A 1 91  ? 9.387  11.124  12.234  1.00 9.54  ? 91  ILE A CB  1 
ATOM   702  C  CG1 . ILE A 1 91  ? 10.330 11.419  11.022  1.00 10.02 ? 91  ILE A CG1 1 
ATOM   703  C  CG2 . ILE A 1 91  ? 10.160 10.255  13.276  1.00 8.35  ? 91  ILE A CG2 1 
ATOM   704  C  CD1 . ILE A 1 91  ? 11.425 12.416  11.423  1.00 11.17 ? 91  ILE A CD1 1 
ATOM   705  N  N   . GLN A 1 92  ? 8.606  8.027   11.284  1.00 9.49  ? 92  GLN A N   1 
ATOM   706  C  CA  . GLN A 1 92  ? 8.855  6.909   10.399  1.00 9.15  ? 92  GLN A CA  1 
ATOM   707  C  C   . GLN A 1 92  ? 8.596  5.620   11.173  1.00 9.83  ? 92  GLN A C   1 
ATOM   708  O  O   . GLN A 1 92  ? 8.564  5.657   12.402  1.00 9.19  ? 92  GLN A O   1 
ATOM   709  C  CB  . GLN A 1 92  ? 10.323 6.874   9.833   1.00 10.23 ? 92  GLN A CB  1 
ATOM   710  C  CG  . GLN A 1 92  ? 11.391 6.984   10.945  1.00 11.75 ? 92  GLN A CG  1 
ATOM   711  C  CD  . GLN A 1 92  ? 12.086 5.638   11.256  1.00 11.84 ? 92  GLN A CD  1 
ATOM   712  O  OE1 . GLN A 1 92  ? 11.480 4.631   11.243  1.00 11.29 ? 92  GLN A OE1 1 
ATOM   713  N  NE2 . GLN A 1 92  ? 13.371 5.669   11.489  1.00 16.69 ? 92  GLN A NE2 1 
ATOM   714  N  N   . PHE A 1 93  ? 8.311  4.531   10.447  1.00 8.41  ? 93  PHE A N   1 
ATOM   715  C  CA  . PHE A 1 93  ? 8.516  3.199   11.072  1.00 8.35  ? 93  PHE A CA  1 
ATOM   716  C  C   . PHE A 1 93  ? 9.474  2.299   10.311  1.00 8.51  ? 93  PHE A C   1 
ATOM   717  O  O   . PHE A 1 93  ? 9.729  2.500   9.095   1.00 8.90  ? 93  PHE A O   1 
ATOM   718  C  CB  . PHE A 1 93  ? 7.153  2.482   11.362  1.00 8.32  ? 93  PHE A CB  1 
ATOM   719  C  CG  . PHE A 1 93  ? 6.402  2.042   10.118  1.00 8.99  ? 93  PHE A CG  1 
ATOM   720  C  CD1 . PHE A 1 93  ? 6.796  0.939   9.412   1.00 10.04 ? 93  PHE A CD1 1 
ATOM   721  C  CD2 . PHE A 1 93  ? 5.245  2.800   9.694   1.00 8.91  ? 93  PHE A CD2 1 
ATOM   722  C  CE1 . PHE A 1 93  ? 6.142  0.500   8.245   1.00 9.36  ? 93  PHE A CE1 1 
ATOM   723  C  CE2 . PHE A 1 93  ? 4.564  2.319   8.540   1.00 9.06  ? 93  PHE A CE2 1 
ATOM   724  C  CZ  . PHE A 1 93  ? 5.020  1.228   7.825   1.00 9.64  ? 93  PHE A CZ  1 
ATOM   725  N  N   . HIS A 1 94  ? 10.021 1.286   10.985  1.00 7.26  ? 94  HIS A N   1 
ATOM   726  C  CA  . HIS A 1 94  ? 10.925 0.349   10.324  1.00 7.00  ? 94  HIS A CA  1 
ATOM   727  C  C   . HIS A 1 94  ? 10.805 -0.899  11.135  1.00 6.71  ? 94  HIS A C   1 
ATOM   728  O  O   . HIS A 1 94  ? 10.108 -0.940  12.181  1.00 7.20  ? 94  HIS A O   1 
ATOM   729  C  CB  . HIS A 1 94  ? 12.388 0.818   10.306  1.00 7.22  ? 94  HIS A CB  1 
ATOM   730  C  CG  . HIS A 1 94  ? 12.873 1.134   11.686  1.00 7.20  ? 94  HIS A CG  1 
ATOM   731  N  ND1 . HIS A 1 94  ? 12.656 2.325   12.274  1.00 7.73  ? 94  HIS A ND1 1 
ATOM   732  C  CD2 . HIS A 1 94  ? 13.465 0.303   12.651  1.00 7.98  ? 94  HIS A CD2 1 
ATOM   733  C  CE1 . HIS A 1 94  ? 13.105 2.294   13.534  1.00 7.50  ? 94  HIS A CE1 1 
ATOM   734  N  NE2 . HIS A 1 94  ? 13.619 1.044   13.767  1.00 6.89  ? 94  HIS A NE2 1 
ATOM   735  N  N   . PHE A 1 95  ? 11.480 -1.926  10.653  1.00 6.50  ? 95  PHE A N   1 
ATOM   736  C  CA  . PHE A 1 95  ? 11.535 -3.227  11.327  1.00 7.07  ? 95  PHE A CA  1 
ATOM   737  C  C   . PHE A 1 95  ? 12.958 -3.670  11.524  1.00 6.23  ? 95  PHE A C   1 
ATOM   738  O  O   . PHE A 1 95  ? 13.913 -3.211  10.883  1.00 7.03  ? 95  PHE A O   1 
ATOM   739  C  CB  . PHE A 1 95  ? 10.837 -4.320  10.502  1.00 6.71  ? 95  PHE A CB  1 
ATOM   740  C  CG  . PHE A 1 95  ? 9.378  -4.000  10.195  1.00 7.36  ? 95  PHE A CG  1 
ATOM   741  C  CD1 . PHE A 1 95  ? 9.030  -3.160  9.128   1.00 7.92  ? 95  PHE A CD1 1 
ATOM   742  C  CD2 . PHE A 1 95  ? 8.339  -4.680  10.873  1.00 7.86  ? 95  PHE A CD2 1 
ATOM   743  C  CE1 . PHE A 1 95  ? 7.712  -2.904  8.785   1.00 7.80  ? 95  PHE A CE1 1 
ATOM   744  C  CE2 . PHE A 1 95  ? 7.010  -4.449  10.538  1.00 8.09  ? 95  PHE A CE2 1 
ATOM   745  C  CZ  . PHE A 1 95  ? 6.700  -3.590  9.455   1.00 7.92  ? 95  PHE A CZ  1 
ATOM   746  N  N   . HIS A 1 96  ? 13.082 -4.574  12.482  1.00 7.06  ? 96  HIS A N   1 
ATOM   747  C  CA  . HIS A 1 96  ? 14.266 -5.447  12.615  1.00 7.23  ? 96  HIS A CA  1 
ATOM   748  C  C   . HIS A 1 96  ? 13.893 -6.917  12.476  1.00 7.45  ? 96  HIS A C   1 
ATOM   749  O  O   . HIS A 1 96  ? 12.851 -7.304  13.007  1.00 7.38  ? 96  HIS A O   1 
ATOM   750  C  CB  . HIS A 1 96  ? 14.941 -5.252  14.006  1.00 7.72  ? 96  HIS A CB  1 
ATOM   751  C  CG  . HIS A 1 96  ? 15.214 -3.814  14.328  1.00 8.51  ? 96  HIS A CG  1 
ATOM   752  N  ND1 . HIS A 1 96  ? 16.439 -3.248  14.117  1.00 8.54  ? 96  HIS A ND1 1 
ATOM   753  C  CD2 . HIS A 1 96  ? 14.362 -2.756  14.728  1.00 7.59  ? 96  HIS A CD2 1 
ATOM   754  C  CE1 . HIS A 1 96  ? 16.408 -1.951  14.540  1.00 8.57  ? 96  HIS A CE1 1 
ATOM   755  N  NE2 . HIS A 1 96  ? 15.144 -1.621  14.808  1.00 8.93  ? 96  HIS A NE2 1 
ATOM   756  N  N   . TRP A 1 97  ? 14.683 -7.713  11.756  1.00 7.45  ? 97  TRP A N   1 
ATOM   757  C  CA  . TRP A 1 97  ? 14.268 -9.107  11.597  1.00 8.42  ? 97  TRP A CA  1 
ATOM   758  C  C   . TRP A 1 97  ? 15.408 -10.044 11.507  1.00 8.52  ? 97  TRP A C   1 
ATOM   759  O  O   . TRP A 1 97  ? 16.583 -9.594  11.400  1.00 9.12  ? 97  TRP A O   1 
ATOM   760  C  CB  . TRP A 1 97  ? 13.297 -9.221  10.422  1.00 8.29  ? 97  TRP A CB  1 
ATOM   761  C  CG  . TRP A 1 97  ? 13.960 -8.797  9.113   1.00 8.24  ? 97  TRP A CG  1 
ATOM   762  C  CD1 . TRP A 1 97  ? 14.656 -9.627  8.215   1.00 9.79  ? 97  TRP A CD1 1 
ATOM   763  C  CD2 . TRP A 1 97  ? 14.020 -7.477  8.559   1.00 9.34  ? 97  TRP A CD2 1 
ATOM   764  N  NE1 . TRP A 1 97  ? 15.095 -8.893  7.122   1.00 9.53  ? 97  TRP A NE1 1 
ATOM   765  C  CE2 . TRP A 1 97  ? 14.718 -7.578  7.281   1.00 9.45  ? 97  TRP A CE2 1 
ATOM   766  C  CE3 . TRP A 1 97  ? 13.518 -6.221  8.964   1.00 7.82  ? 97  TRP A CE3 1 
ATOM   767  C  CZ2 . TRP A 1 97  ? 14.956 -6.441  6.507   1.00 8.32  ? 97  TRP A CZ2 1 
ATOM   768  C  CZ3 . TRP A 1 97  ? 13.745 -5.084  8.179   1.00 8.28  ? 97  TRP A CZ3 1 
ATOM   769  C  CH2 . TRP A 1 97  ? 14.420 -5.193  6.959   1.00 8.33  ? 97  TRP A CH2 1 
ATOM   770  N  N   . GLY A 1 98  ? 15.093 -11.349 11.536  1.00 8.87  ? 98  GLY A N   1 
ATOM   771  C  CA  . GLY A 1 98  ? 16.154 -12.379 11.595  1.00 8.95  ? 98  GLY A CA  1 
ATOM   772  C  C   . GLY A 1 98  ? 16.423 -13.033 10.239  1.00 10.22 ? 98  GLY A C   1 
ATOM   773  O  O   . GLY A 1 98  ? 15.703 -12.823 9.261   1.00 10.76 ? 98  GLY A O   1 
ATOM   774  N  N   . SER A 1 99  ? 17.438 -13.878 10.224  1.00 9.96  ? 99  SER A N   1 
ATOM   775  C  CA  . SER A 1 99  ? 17.646 -14.749 9.056   1.00 10.75 ? 99  SER A CA  1 
ATOM   776  C  C   . SER A 1 99  ? 16.752 -15.998 9.149   1.00 12.59 ? 99  SER A C   1 
ATOM   777  O  O   . SER A 1 99  ? 16.667 -16.766 8.176   1.00 14.18 ? 99  SER A O   1 
ATOM   778  C  CB  . SER A 1 99  ? 19.121 -15.192 9.041   1.00 11.23 ? 99  SER A CB  1 
ATOM   779  O  OG  . SER A 1 99  ? 19.550 -15.796 10.297  1.00 12.05 ? 99  SER A OG  1 
ATOM   780  N  N   . LEU A 1 100 ? 16.162 -16.226 10.329  1.00 11.99 ? 100 LEU A N   1 
ATOM   781  C  CA  . LEU A 1 100 ? 15.392 -17.416 10.644  1.00 13.24 ? 100 LEU A CA  1 
ATOM   782  C  C   . LEU A 1 100 ? 14.282 -16.954 11.591  1.00 12.47 ? 100 LEU A C   1 
ATOM   783  O  O   . LEU A 1 100 ? 14.399 -15.925 12.290  1.00 11.87 ? 100 LEU A O   1 
ATOM   784  C  CB  . LEU A 1 100 ? 16.240 -18.435 11.490  1.00 16.40 ? 100 LEU A CB  1 
ATOM   785  C  CG  . LEU A 1 100 ? 17.590 -18.856 10.912  1.00 18.85 ? 100 LEU A CG  1 
ATOM   786  C  CD1 . LEU A 1 100 ? 18.537 -19.245 12.031  1.00 23.24 ? 100 LEU A CD1 1 
ATOM   787  C  CD2 . LEU A 1 100 ? 17.339 -20.005 9.957   1.00 19.55 ? 100 LEU A CD2 1 
ATOM   788  N  N   . ASP A 1 101 ? 13.172 -17.702 11.636  1.00 11.48 ? 101 ASP A N   1 
ATOM   789  C  CA  . ASP A 1 101 ? 12.078 -17.223 12.464  1.00 12.04 ? 101 ASP A CA  1 
ATOM   790  C  C   . ASP A 1 101 ? 12.343 -17.181 13.934  1.00 12.33 ? 101 ASP A C   1 
ATOM   791  O  O   . ASP A 1 101 ? 11.680 -16.429 14.655  1.00 12.04 ? 101 ASP A O   1 
ATOM   792  C  CB  . ASP A 1 101 ? 10.796 -18.087 12.230  1.00 13.06 ? 101 ASP A CB  1 
ATOM   793  C  CG  . ASP A 1 101 ? 10.315 -18.126 10.780  1.00 15.78 ? 101 ASP A CG  1 
ATOM   794  O  OD1 . ASP A 1 101 ? 10.715 -17.277 9.960   1.00 15.57 ? 101 ASP A OD1 1 
ATOM   795  O  OD2 . ASP A 1 101 ? 9.446  -18.997 10.522  1.00 20.17 ? 101 ASP A OD2 1 
ATOM   796  N  N   . GLY A 1 102 ? 13.326 -18.009 14.396  1.00 11.77 ? 102 GLY A N   1 
ATOM   797  C  CA  . GLY A 1 102 ? 13.676 -18.028 15.827  1.00 11.50 ? 102 GLY A CA  1 
ATOM   798  C  C   . GLY A 1 102 ? 14.428 -16.806 16.364  1.00 10.85 ? 102 GLY A C   1 
ATOM   799  O  O   . GLY A 1 102 ? 14.763 -16.777 17.548  1.00 11.09 ? 102 GLY A O   1 
ATOM   800  N  N   . GLN A 1 103 ? 14.711 -15.795 15.522  1.00 10.41 ? 103 GLN A N   1 
ATOM   801  C  CA  . GLN A 1 103 ? 15.388 -14.616 16.016  1.00 9.51  ? 103 GLN A CA  1 
ATOM   802  C  C   . GLN A 1 103 ? 15.018 -13.395 15.177  1.00 8.99  ? 103 GLN A C   1 
ATOM   803  O  O   . GLN A 1 103 ? 14.433 -13.581 14.139  1.00 9.87  ? 103 GLN A O   1 
ATOM   804  C  CB  . GLN A 1 103 ? 16.884 -14.788 16.016  1.00 11.67 ? 103 GLN A CB  1 
ATOM   805  C  CG  . GLN A 1 103 ? 17.469 -15.092 14.624  1.00 12.85 ? 103 GLN A CG  1 
ATOM   806  C  CD  . GLN A 1 103 ? 18.944 -15.501 14.765  1.00 15.73 ? 103 GLN A CD  1 
ATOM   807  O  OE1 . GLN A 1 103 ? 19.336 -16.158 15.751  1.00 21.36 ? 103 GLN A OE1 1 
ATOM   808  N  NE2 . GLN A 1 103 ? 19.787 -15.042 13.848  1.00 14.68 ? 103 GLN A NE2 1 
ATOM   809  N  N   . GLY A 1 104 ? 15.319 -12.198 15.664  1.00 8.41  ? 104 GLY A N   1 
ATOM   810  C  CA  . GLY A 1 104 ? 15.023 -11.035 14.842  1.00 8.26  ? 104 GLY A CA  1 
ATOM   811  C  C   . GLY A 1 104 ? 14.578 -9.813  15.655  1.00 8.35  ? 104 GLY A C   1 
ATOM   812  O  O   . GLY A 1 104 ? 14.846 -8.662  15.314  1.00 10.45 ? 104 GLY A O   1 
ATOM   813  N  N   . SER A 1 105 ? 13.867 -10.096 16.762  1.00 8.19  ? 105 SER A N   1 
ATOM   814  C  CA  . SER A 1 105 ? 13.438 -8.972  17.640  1.00 7.59  ? 105 SER A CA  1 
ATOM   815  C  C   . SER A 1 105 ? 14.661 -8.464  18.456  1.00 7.13  ? 105 SER A C   1 
ATOM   816  O  O   . SER A 1 105 ? 15.686 -9.145  18.645  1.00 9.08  ? 105 SER A O   1 
ATOM   817  C  CB  . SER A 1 105 ? 12.335 -9.334  18.581  1.00 7.02  ? 105 SER A CB  1 
ATOM   818  O  OG  . SER A 1 105 ? 12.717 -10.351 19.587  1.00 7.64  ? 105 SER A OG  1 
ATOM   819  N  N   . GLU A 1 106 ? 14.507 -7.225  18.858  1.00 7.29  ? 106 GLU A N   1 
ATOM   820  C  CA  . GLU A 1 106 ? 15.565 -6.501  19.641  1.00 7.04  ? 106 GLU A CA  1 
ATOM   821  C  C   . GLU A 1 106 ? 15.223 -6.628  21.121  1.00 6.80  ? 106 GLU A C   1 
ATOM   822  O  O   . GLU A 1 106 ? 16.006 -7.198  21.882  1.00 7.63  ? 106 GLU A O   1 
ATOM   823  C  CB  . GLU A 1 106 ? 15.565 -5.057  19.238  1.00 7.17  ? 106 GLU A CB  1 
ATOM   824  C  CG  . GLU A 1 106 ? 16.171 -4.933  17.819  1.00 7.47  ? 106 GLU A CG  1 
ATOM   825  C  CD  . GLU A 1 106 ? 16.724 -3.595  17.511  1.00 7.76  ? 106 GLU A CD  1 
ATOM   826  O  OE1 . GLU A 1 106 ? 16.105 -2.491  17.791  1.00 7.27  ? 106 GLU A OE1 1 
ATOM   827  O  OE2 . GLU A 1 106 ? 17.880 -3.598  16.953  1.00 8.67  ? 106 GLU A OE2 1 
ATOM   828  N  N   . HIS A 1 107 ? 13.996 -6.281  21.540  1.00 7.10  ? 107 HIS A N   1 
ATOM   829  C  CA  . HIS A 1 107 ? 13.585 -6.594  22.878  1.00 6.95  ? 107 HIS A CA  1 
ATOM   830  C  C   . HIS A 1 107 ? 13.256 -8.055  22.909  1.00 7.25  ? 107 HIS A C   1 
ATOM   831  O  O   . HIS A 1 107 ? 12.927 -8.681  21.830  1.00 8.49  ? 107 HIS A O   1 
ATOM   832  C  CB  . HIS A 1 107 ? 12.324 -5.780  23.193  1.00 6.59  ? 107 HIS A CB  1 
ATOM   833  C  CG  . HIS A 1 107 ? 12.634 -4.319  23.358  1.00 6.88  ? 107 HIS A CG  1 
ATOM   834  N  ND1 . HIS A 1 107 ? 12.571 -3.431  22.320  1.00 6.77  ? 107 HIS A ND1 1 
ATOM   835  C  CD2 . HIS A 1 107 ? 13.161 -3.630  24.446  1.00 7.25  ? 107 HIS A CD2 1 
ATOM   836  C  CE1 . HIS A 1 107 ? 12.994 -2.203  22.774  1.00 7.00  ? 107 HIS A CE1 1 
ATOM   837  N  NE2 . HIS A 1 107 ? 13.358 -2.359  24.077  1.00 6.70  ? 107 HIS A NE2 1 
ATOM   838  N  N   . THR A 1 108 ? 13.402 -8.601  24.105  1.00 7.21  ? 108 THR A N   1 
ATOM   839  C  CA  . THR A 1 108 ? 13.039 -10.028 24.335  1.00 7.06  ? 108 THR A CA  1 
ATOM   840  C  C   . THR A 1 108 ? 12.096 -10.069 25.508  1.00 7.62  ? 108 THR A C   1 
ATOM   841  O  O   . THR A 1 108 ? 12.066 -9.080  26.277  1.00 7.77  ? 108 THR A O   1 
ATOM   842  C  CB  . THR A 1 108 ? 14.268 -10.918 24.527  1.00 7.40  ? 108 THR A CB  1 
ATOM   843  O  OG1 . THR A 1 108 ? 15.132 -10.468 25.596  1.00 8.33  ? 108 THR A OG1 1 
ATOM   844  C  CG2 . THR A 1 108 ? 15.080 -10.982 23.231  1.00 8.08  ? 108 THR A CG2 1 
ATOM   845  N  N   . VAL A 1 109 ? 11.338 -11.167 25.648  1.00 8.45  ? 109 VAL A N   1 
ATOM   846  C  CA  . VAL A 1 109 ? 10.338 -11.226 26.789  1.00 9.38  ? 109 VAL A CA  1 
ATOM   847  C  C   . VAL A 1 109 ? 10.657 -12.526 27.531  1.00 9.44  ? 109 VAL A C   1 
ATOM   848  O  O   . VAL A 1 109 ? 10.497 -13.614 26.957  1.00 9.36  ? 109 VAL A O   1 
ATOM   849  C  CB  . VAL A 1 109 ? 8.896  -11.291 26.228  1.00 10.14 ? 109 VAL A CB  1 
ATOM   850  C  CG1 . VAL A 1 109 ? 7.879  -11.411 27.332  1.00 11.05 ? 109 VAL A CG1 1 
ATOM   851  C  CG2 . VAL A 1 109 ? 8.580  -10.014 25.419  1.00 10.87 ? 109 VAL A CG2 1 
ATOM   852  N  N   . ASP A 1 110 ? 11.153 -12.429 28.752  1.00 9.60  ? 110 ASP A N   1 
ATOM   853  C  CA  . ASP A 1 110 ? 11.722 -13.603 29.438  1.00 11.40 ? 110 ASP A CA  1 
ATOM   854  C  C   . ASP A 1 110 ? 12.623 -14.449 28.547  1.00 10.68 ? 110 ASP A C   1 
ATOM   855  O  O   . ASP A 1 110 ? 12.508 -15.693 28.478  1.00 11.21 ? 110 ASP A O   1 
ATOM   856  C  CB  . ASP A 1 110 ? 10.555 -14.451 29.959  1.00 11.28 ? 110 ASP A CB  1 
ATOM   857  C  CG  . ASP A 1 110 ? 9.687  -13.666 30.989  1.00 11.29 ? 110 ASP A CG  1 
ATOM   858  O  OD1 . ASP A 1 110 ? 10.259 -12.812 31.658  1.00 11.73 ? 110 ASP A OD1 1 
ATOM   859  O  OD2 . ASP A 1 110 ? 8.520  -14.045 31.175  1.00 14.88 ? 110 ASP A OD2 1 
ATOM   860  N  N   . LYS A 1 111 ? 13.468 -13.710 27.817  1.00 9.97  ? 111 LYS A N   1 
ATOM   861  C  CA  . LYS A 1 111 ? 14.533 -14.255 26.919  1.00 11.21 ? 111 LYS A CA  1 
ATOM   862  C  C   . LYS A 1 111 ? 13.979 -14.777 25.601  1.00 10.09 ? 111 LYS A C   1 
ATOM   863  O  O   . LYS A 1 111 ? 14.755 -15.187 24.675  1.00 10.35 ? 111 LYS A O   1 
ATOM   864  C  CB  . LYS A 1 111 ? 15.475 -15.242 27.655  1.00 12.91 ? 111 LYS A CB  1 
ATOM   865  C  CG  . LYS A 1 111 ? 16.151 -14.633 28.897  1.00 15.10 ? 111 LYS A CG  1 
ATOM   866  C  CD  . LYS A 1 111 ? 17.121 -13.544 28.461  1.00 15.37 ? 111 LYS A CD  1 
ATOM   867  C  CE  . LYS A 1 111 ? 17.805 -12.942 29.684  1.00 18.05 ? 111 LYS A CE  1 
ATOM   868  N  NZ  . LYS A 1 111 ? 18.955 -13.816 30.066  1.00 21.26 ? 111 LYS A NZ  1 
ATOM   869  N  N   . LYS A 1 112 ? 12.659 -14.686 25.428  1.00 8.67  ? 112 LYS A N   1 
ATOM   870  C  CA  . LYS A 1 112 ? 12.075 -15.142 24.178  1.00 9.68  ? 112 LYS A CA  1 
ATOM   871  C  C   . LYS A 1 112 ? 12.372 -14.122 23.053  1.00 9.56  ? 112 LYS A C   1 
ATOM   872  O  O   . LYS A 1 112 ? 12.110 -12.906 23.207  1.00 8.79  ? 112 LYS A O   1 
ATOM   873  C  CB  . LYS A 1 112 ? 10.551 -15.251 24.284  1.00 10.21 ? 112 LYS A CB  1 
ATOM   874  C  CG  . LYS A 1 112 ? 9.901  -15.692 22.955  1.00 11.29 ? 112 LYS A CG  1 
ATOM   875  C  CD  . LYS A 1 112 ? 8.340  -15.575 23.055  1.00 13.78 ? 112 LYS A CD  1 
ATOM   876  C  CE  . LYS A 1 112 ? 7.686  -15.698 21.661  1.00 15.78 ? 112 LYS A CE  1 
ATOM   877  N  NZ  . LYS A 1 112 ? 7.839  -17.055 21.101  1.00 15.84 ? 112 LYS A NZ  1 
ATOM   878  N  N   . LYS A 1 113 ? 12.893 -14.645 21.923  1.00 9.45  ? 113 LYS A N   1 
ATOM   879  C  CA  . LYS A 1 113 ? 13.076 -13.787 20.701  1.00 9.68  ? 113 LYS A CA  1 
ATOM   880  C  C   . LYS A 1 113 ? 11.957 -13.982 19.723  1.00 8.85  ? 113 LYS A C   1 
ATOM   881  O  O   . LYS A 1 113 ? 11.526 -15.117 19.456  1.00 9.86  ? 113 LYS A O   1 
ATOM   882  C  CB  . LYS A 1 113 ? 14.410 -14.158 20.024  1.00 9.40  ? 113 LYS A CB  1 
ATOM   883  C  CG  . LYS A 1 113 ? 15.619 -13.761 20.892  1.00 10.36 ? 113 LYS A CG  1 
ATOM   884  C  CD  . LYS A 1 113 ? 16.787 -14.422 20.116  1.00 11.69 ? 113 LYS A CD  1 
ATOM   885  C  CE  . LYS A 1 113 ? 18.106 -13.805 20.568  1.00 12.04 ? 113 LYS A CE  1 
ATOM   886  N  NZ  . LYS A 1 113 ? 18.563 -14.664 21.649  1.00 18.32 ? 113 LYS A NZ  1 
ATOM   887  N  N   . TYR A 1 114 ? 11.405 -12.855 19.241  1.00 8.22  ? 114 TYR A N   1 
ATOM   888  C  CA  . TYR A 1 114 ? 10.385 -12.913 18.180  1.00 8.12  ? 114 TYR A CA  1 
ATOM   889  C  C   . TYR A 1 114 ? 11.023 -12.873 16.803  1.00 8.55  ? 114 TYR A C   1 
ATOM   890  O  O   . TYR A 1 114 ? 12.233 -12.578 16.686  1.00 7.81  ? 114 TYR A O   1 
ATOM   891  C  CB  . TYR A 1 114 ? 9.331  -11.741 18.324  1.00 8.15  ? 114 TYR A CB  1 
ATOM   892  C  CG  . TYR A 1 114 ? 8.367  -11.979 19.500  1.00 8.81  ? 114 TYR A CG  1 
ATOM   893  C  CD1 . TYR A 1 114 ? 8.684  -11.571 20.769  1.00 9.81  ? 114 TYR A CD1 1 
ATOM   894  C  CD2 . TYR A 1 114 ? 7.161  -12.660 19.304  1.00 10.08 ? 114 TYR A CD2 1 
ATOM   895  C  CE1 . TYR A 1 114 ? 7.787  -11.818 21.845  1.00 11.07 ? 114 TYR A CE1 1 
ATOM   896  C  CE2 . TYR A 1 114 ? 6.253  -12.835 20.342  1.00 11.29 ? 114 TYR A CE2 1 
ATOM   897  C  CZ  . TYR A 1 114 ? 6.585  -12.388 21.592  1.00 11.61 ? 114 TYR A CZ  1 
ATOM   898  O  OH  . TYR A 1 114 ? 5.683  -12.601 22.625  1.00 15.46 ? 114 TYR A OH  1 
ATOM   899  N  N   . ALA A 1 115 ? 10.262 -13.210 15.739  1.00 8.17  ? 115 ALA A N   1 
ATOM   900  C  CA  . ALA A 1 115 ? 10.845 -13.190 14.414  1.00 8.76  ? 115 ALA A CA  1 
ATOM   901  C  C   . ALA A 1 115 ? 11.218 -11.810 13.938  1.00 8.00  ? 115 ALA A C   1 
ATOM   902  O  O   . ALA A 1 115 ? 12.078 -11.657 13.044  1.00 7.93  ? 115 ALA A O   1 
ATOM   903  C  CB  . ALA A 1 115 ? 9.867  -13.832 13.404  1.00 9.60  ? 115 ALA A CB  1 
ATOM   904  N  N   . ALA A 1 116 ? 10.512 -10.802 14.424  1.00 7.66  ? 116 ALA A N   1 
ATOM   905  C  CA  . ALA A 1 116 ? 10.865 -9.465  14.037  1.00 6.94  ? 116 ALA A CA  1 
ATOM   906  C  C   . ALA A 1 116 ? 10.263 -8.478  15.027  1.00 6.85  ? 116 ALA A C   1 
ATOM   907  O  O   . ALA A 1 116 ? 9.515  -8.846  15.947  1.00 6.97  ? 116 ALA A O   1 
ATOM   908  C  CB  . ALA A 1 116 ? 10.307 -9.193  12.601  1.00 6.92  ? 116 ALA A CB  1 
ATOM   909  N  N   . GLU A 1 117 ? 10.622 -7.214  14.885  1.00 7.26  ? 117 GLU A N   1 
ATOM   910  C  CA  . GLU A 1 117 ? 10.042 -6.175  15.773  1.00 6.85  ? 117 GLU A CA  1 
ATOM   911  C  C   . GLU A 1 117 ? 9.877  -4.907  14.964  1.00 7.74  ? 117 GLU A C   1 
ATOM   912  O  O   . GLU A 1 117 ? 10.779 -4.471  14.242  1.00 8.47  ? 117 GLU A O   1 
ATOM   913  C  CB  . GLU A 1 117 ? 10.996 -5.954  16.969  1.00 6.99  ? 117 GLU A CB  1 
ATOM   914  C  CG  . GLU A 1 117 ? 10.521 -4.883  17.978  1.00 6.44  ? 117 GLU A CG  1 
ATOM   915  C  CD  . GLU A 1 117 ? 11.468 -4.864  19.173  1.00 7.13  ? 117 GLU A CD  1 
ATOM   916  O  OE1 . GLU A 1 117 ? 12.066 -5.882  19.507  1.00 7.90  ? 117 GLU A OE1 1 
ATOM   917  O  OE2 . GLU A 1 117 ? 11.487 -3.829  19.857  1.00 8.61  ? 117 GLU A OE2 1 
ATOM   918  N  N   . LEU A 1 118 ? 8.659  -4.362  15.014  1.00 7.17  ? 118 LEU A N   1 
ATOM   919  C  CA  . LEU A 1 118 ? 8.336  -3.072  14.382  1.00 6.71  ? 118 LEU A CA  1 
ATOM   920  C  C   . LEU A 1 118 ? 8.552  -1.891  15.371  1.00 6.66  ? 118 LEU A C   1 
ATOM   921  O  O   . LEU A 1 118 ? 8.146  -1.953  16.551  1.00 6.92  ? 118 LEU A O   1 
ATOM   922  C  CB  . LEU A 1 118 ? 6.831  -3.130  14.011  1.00 7.12  ? 118 LEU A CB  1 
ATOM   923  C  CG  . LEU A 1 118 ? 6.049  -1.809  13.642  1.00 7.82  ? 118 LEU A CG  1 
ATOM   924  C  CD1 . LEU A 1 118 ? 6.621  -1.273  12.354  1.00 8.37  ? 118 LEU A CD1 1 
ATOM   925  C  CD2 . LEU A 1 118 ? 4.577  -2.171  13.409  1.00 8.65  ? 118 LEU A CD2 1 
ATOM   926  N  N   . HIS A 1 119 ? 9.137  -0.825  14.851  1.00 5.89  ? 119 HIS A N   1 
ATOM   927  C  CA  . HIS A 1 119 ? 9.405  0.362   15.651  1.00 6.37  ? 119 HIS A CA  1 
ATOM   928  C  C   . HIS A 1 119 ? 8.742  1.526   14.979  1.00 6.28  ? 119 HIS A C   1 
ATOM   929  O  O   . HIS A 1 119 ? 9.148  1.893   13.840  1.00 7.31  ? 119 HIS A O   1 
ATOM   930  C  CB  . HIS A 1 119 ? 10.909 0.602   15.721  1.00 6.35  ? 119 HIS A CB  1 
ATOM   931  C  CG  . HIS A 1 119 ? 11.588 -0.331  16.660  1.00 6.67  ? 119 HIS A CG  1 
ATOM   932  N  ND1 . HIS A 1 119 ? 12.972 -0.552  16.684  1.00 7.01  ? 119 HIS A ND1 1 
ATOM   933  C  CD2 . HIS A 1 119 ? 11.059 -1.134  17.629  1.00 6.89  ? 119 HIS A CD2 1 
ATOM   934  C  CE1 . HIS A 1 119 ? 13.252 -1.451  17.617  1.00 6.60  ? 119 HIS A CE1 1 
ATOM   935  N  NE2 . HIS A 1 119 ? 12.106 -1.834  18.183  1.00 6.72  ? 119 HIS A NE2 1 
ATOM   936  N  N   . LEU A 1 120 ? 7.740  2.128   15.651  1.00 6.51  ? 120 LEU A N   1 
ATOM   937  C  CA  . LEU A 1 120 ? 7.100  3.360   15.134  1.00 7.53  ? 120 LEU A CA  1 
ATOM   938  C  C   . LEU A 1 120 ? 7.706  4.492   15.928  1.00 7.46  ? 120 LEU A C   1 
ATOM   939  O  O   . LEU A 1 120 ? 7.563  4.556   17.174  1.00 7.26  ? 120 LEU A O   1 
ATOM   940  C  CB  . LEU A 1 120 ? 5.598  3.336   15.379  1.00 7.56  ? 120 LEU A CB  1 
ATOM   941  C  CG  . LEU A 1 120 ? 4.967  2.236   14.476  1.00 7.85  ? 120 LEU A CG  1 
ATOM   942  C  CD1 . LEU A 1 120 ? 4.196  1.232   15.317  1.00 8.51  ? 120 LEU A CD1 1 
ATOM   943  C  CD2 . LEU A 1 120 ? 4.060  2.830   13.372  1.00 8.60  ? 120 LEU A CD2 1 
ATOM   944  N  N   . VAL A 1 121 ? 8.439  5.334   15.192  1.00 7.12  ? 121 VAL A N   1 
ATOM   945  C  CA  . VAL A 1 121 ? 9.285  6.382   15.878  1.00 7.33  ? 121 VAL A CA  1 
ATOM   946  C  C   . VAL A 1 121 ? 8.572  7.721   15.937  1.00 7.44  ? 121 VAL A C   1 
ATOM   947  O  O   . VAL A 1 121 ? 8.116  8.210   14.896  1.00 7.86  ? 121 VAL A O   1 
ATOM   948  C  CB  . VAL A 1 121 ? 10.628 6.496   15.144  1.00 7.45  ? 121 VAL A CB  1 
ATOM   949  C  CG1 . VAL A 1 121 ? 11.507 7.596   15.798  1.00 6.93  ? 121 VAL A CG1 1 
ATOM   950  C  CG2 . VAL A 1 121 ? 11.355 5.152   15.071  1.00 8.41  ? 121 VAL A CG2 1 
ATOM   951  N  N   . HIS A 1 122 ? 8.513  8.347   17.126  1.00 7.76  ? 122 HIS A N   1 
ATOM   952  C  CA  . HIS A 1 122 ? 7.794  9.635   17.277  1.00 8.12  ? 122 HIS A CA  1 
ATOM   953  C  C   . HIS A 1 122 ? 8.653  10.603  18.041  1.00 8.46  ? 122 HIS A C   1 
ATOM   954  O  O   . HIS A 1 122 ? 9.445  10.186  18.934  1.00 8.35  ? 122 HIS A O   1 
ATOM   955  C  CB  . HIS A 1 122 ? 6.543  9.426   18.099  1.00 9.21  ? 122 HIS A CB  1 
ATOM   956  C  CG  . HIS A 1 122 ? 5.656  8.269   17.677  1.00 9.52  ? 122 HIS A CG  1 
ATOM   957  N  ND1 . HIS A 1 122 ? 5.951  6.970   17.981  1.00 8.31  ? 122 HIS A ND1 1 
ATOM   958  C  CD2 . HIS A 1 122 ? 4.408  8.251   16.995  1.00 9.51  ? 122 HIS A CD2 1 
ATOM   959  C  CE1 . HIS A 1 122 ? 4.949  6.158   17.528  1.00 10.50 ? 122 HIS A CE1 1 
ATOM   960  N  NE2 . HIS A 1 122 ? 3.995  6.947   16.946  1.00 9.04  ? 122 HIS A NE2 1 
ATOM   961  N  N   . TRP A 1 123 ? 8.543  11.875  17.689  1.00 9.55  ? 123 TRP A N   1 
ATOM   962  C  CA  . TRP A 1 123 ? 9.388  12.899  18.419  1.00 9.08  ? 123 TRP A CA  1 
ATOM   963  C  C   . TRP A 1 123 ? 8.518  13.889  19.133  1.00 10.50 ? 123 TRP A C   1 
ATOM   964  O  O   . TRP A 1 123 ? 7.396  14.247  18.687  1.00 9.96  ? 123 TRP A O   1 
ATOM   965  C  CB  . TRP A 1 123 ? 10.384 13.555  17.478  1.00 10.05 ? 123 TRP A CB  1 
ATOM   966  C  CG  . TRP A 1 123 ? 9.749  14.219  16.280  1.00 11.74 ? 123 TRP A CG  1 
ATOM   967  C  CD1 . TRP A 1 123 ? 9.515  13.662  15.024  1.00 12.49 ? 123 TRP A CD1 1 
ATOM   968  C  CD2 . TRP A 1 123 ? 9.249  15.596  16.184  1.00 13.85 ? 123 TRP A CD2 1 
ATOM   969  N  NE1 . TRP A 1 123 ? 8.920  14.573  14.190  1.00 14.14 ? 123 TRP A NE1 1 
ATOM   970  C  CE2 . TRP A 1 123 ? 8.734  15.752  14.822  1.00 13.62 ? 123 TRP A CE2 1 
ATOM   971  C  CE3 . TRP A 1 123 ? 9.179  16.671  17.056  1.00 13.28 ? 123 TRP A CE3 1 
ATOM   972  C  CZ2 . TRP A 1 123 ? 8.179  16.940  14.381  1.00 15.25 ? 123 TRP A CZ2 1 
ATOM   973  C  CZ3 . TRP A 1 123 ? 8.617  17.863  16.597  1.00 14.11 ? 123 TRP A CZ3 1 
ATOM   974  C  CH2 . TRP A 1 123 ? 8.130  17.993  15.292  1.00 14.42 ? 123 TRP A CH2 1 
ATOM   975  N  N   . ASN A 1 124 ? 9.016  14.359  20.282  1.00 10.04 ? 124 ASN A N   1 
ATOM   976  C  CA  . ASN A 1 124 ? 8.286  15.258  21.188  1.00 10.51 ? 124 ASN A CA  1 
ATOM   977  C  C   . ASN A 1 124 ? 8.117  16.646  20.559  1.00 10.64 ? 124 ASN A C   1 
ATOM   978  O  O   . ASN A 1 124 ? 9.096  17.293  20.259  1.00 9.76  ? 124 ASN A O   1 
ATOM   979  C  CB  . ASN A 1 124 ? 9.100  15.317  22.512  1.00 10.62 ? 124 ASN A CB  1 
ATOM   980  C  CG  . ASN A 1 124 ? 8.299  15.903  23.644  1.00 11.33 ? 124 ASN A CG  1 
ATOM   981  O  OD1 . ASN A 1 124 ? 7.447  16.762  23.394  1.00 11.75 ? 124 ASN A OD1 1 
ATOM   982  N  ND2 . ASN A 1 124 ? 8.559  15.473  24.896  1.00 13.38 ? 124 ASN A ND2 1 
ATOM   983  N  N   . THR A 1 125 ? 6.867  17.088  20.350  1.00 11.44 ? 125 THR A N   1 
ATOM   984  C  CA  . THR A 1 125 ? 6.653  18.363  19.672  1.00 14.37 ? 125 THR A CA  1 
ATOM   985  C  C   . THR A 1 125 ? 7.213  19.566  20.445  1.00 14.82 ? 125 THR A C   1 
ATOM   986  O  O   . THR A 1 125 ? 7.416  20.626  19.849  1.00 13.99 ? 125 THR A O   1 
ATOM   987  C  CB  . THR A 1 125 ? 5.176  18.542  19.332  1.00 15.22 ? 125 THR A CB  1 
ATOM   988  O  OG1 . THR A 1 125 ? 4.463  18.518  20.570  1.00 18.19 ? 125 THR A OG1 1 
ATOM   989  C  CG2 . THR A 1 125 ? 4.692  17.407  18.446  1.00 16.32 ? 125 THR A CG2 1 
ATOM   990  N  N   . LYS A 1 126 ? 7.479  19.412  21.749  1.00 12.43 ? 127 LYS A N   1 
ATOM   991  C  CA  . LYS A 1 126 ? 8.042  20.533  22.529  1.00 12.81 ? 127 LYS A CA  1 
ATOM   992  C  C   . LYS A 1 126 ? 9.434  20.919  22.049  1.00 13.38 ? 127 LYS A C   1 
ATOM   993  O  O   . LYS A 1 126 ? 9.893  21.995  22.363  1.00 14.75 ? 127 LYS A O   1 
ATOM   994  C  CB  . LYS A 1 126 ? 7.998  20.357  23.997  1.00 14.93 ? 127 LYS A CB  1 
ATOM   995  C  CG  . LYS A 1 126 ? 8.992  19.433  24.543  1.00 16.33 ? 127 LYS A CG  1 
ATOM   996  C  CD  . LYS A 1 126 ? 8.604  19.347  26.012  1.00 21.33 ? 127 LYS A CD  1 
ATOM   997  C  CE  . LYS A 1 126 ? 9.570  18.467  26.654  1.00 21.28 ? 127 LYS A CE  1 
ATOM   998  N  NZ  . LYS A 1 126 ? 9.386  18.513  28.135  1.00 33.48 ? 127 LYS A NZ  1 
ATOM   999  N  N   . TYR A 1 127 ? 10.084 20.063  21.273  1.00 11.02 ? 128 TYR A N   1 
ATOM   1000 C  CA  . TYR A 1 127 ? 11.443 20.360  20.811  1.00 11.74 ? 128 TYR A CA  1 
ATOM   1001 C  C   . TYR A 1 127 ? 11.455 20.782  19.359  1.00 14.18 ? 128 TYR A C   1 
ATOM   1002 O  O   . TYR A 1 127 ? 12.520 21.062  18.798  1.00 14.58 ? 128 TYR A O   1 
ATOM   1003 C  CB  . TYR A 1 127 ? 12.358 19.102  21.057  1.00 10.67 ? 128 TYR A CB  1 
ATOM   1004 C  CG  . TYR A 1 127 ? 12.463 18.819  22.512  1.00 9.69  ? 128 TYR A CG  1 
ATOM   1005 C  CD1 . TYR A 1 127 ? 12.911 19.796  23.394  1.00 13.22 ? 128 TYR A CD1 1 
ATOM   1006 C  CD2 . TYR A 1 127 ? 12.117 17.573  23.046  1.00 9.74  ? 128 TYR A CD2 1 
ATOM   1007 C  CE1 . TYR A 1 127 ? 12.967 19.517  24.767  1.00 11.17 ? 128 TYR A CE1 1 
ATOM   1008 C  CE2 . TYR A 1 127 ? 12.196 17.280  24.394  1.00 10.87 ? 128 TYR A CE2 1 
ATOM   1009 C  CZ  . TYR A 1 127 ? 12.647 18.284  25.243  1.00 11.78 ? 128 TYR A CZ  1 
ATOM   1010 O  OH  . TYR A 1 127 ? 12.692 17.975  26.591  1.00 12.15 ? 128 TYR A OH  1 
ATOM   1011 N  N   . GLY A 1 128 ? 10.284 20.865  18.712  1.00 12.57 ? 129 GLY A N   1 
ATOM   1012 C  CA  . GLY A 1 128 ? 10.237 21.552  17.378  1.00 12.80 ? 129 GLY A CA  1 
ATOM   1013 C  C   . GLY A 1 128 ? 10.612 20.683  16.163  1.00 13.40 ? 129 GLY A C   1 
ATOM   1014 O  O   . GLY A 1 128 ? 9.954  20.785  15.100  1.00 14.52 ? 129 GLY A O   1 
ATOM   1015 N  N   . ASP A 1 129 ? 11.650 19.840  16.255  1.00 12.29 ? 130 ASP A N   1 
ATOM   1016 C  CA  . ASP A 1 129 ? 11.917 18.876  15.185  1.00 14.07 ? 130 ASP A CA  1 
ATOM   1017 C  C   . ASP A 1 129 ? 12.607 17.640  15.707  1.00 14.43 ? 130 ASP A C   1 
ATOM   1018 O  O   . ASP A 1 129 ? 13.042 17.619  16.873  1.00 13.28 ? 130 ASP A O   1 
ATOM   1019 C  CB  . ASP A 1 129 ? 12.612 19.470  13.950  1.00 17.30 ? 130 ASP A CB  1 
ATOM   1020 C  CG  . ASP A 1 129 ? 14.043 19.955  14.206  1.00 20.96 ? 130 ASP A CG  1 
ATOM   1021 O  OD1 . ASP A 1 129 ? 14.712 19.528  15.172  1.00 23.85 ? 130 ASP A OD1 1 
ATOM   1022 O  OD2 . ASP A 1 129 ? 14.500 20.782  13.389  1.00 23.04 ? 130 ASP A OD2 1 
ATOM   1023 N  N   . PHE A 1 130 ? 12.742 16.627  14.835  1.00 12.25 ? 131 PHE A N   1 
ATOM   1024 C  CA  . PHE A 1 130 ? 13.436 15.375  15.214  1.00 12.26 ? 131 PHE A CA  1 
ATOM   1025 C  C   . PHE A 1 130 ? 14.888 15.613  15.623  1.00 11.90 ? 131 PHE A C   1 
ATOM   1026 O  O   . PHE A 1 130 ? 15.313 15.037  16.616  1.00 10.84 ? 131 PHE A O   1 
ATOM   1027 C  CB  . PHE A 1 130 ? 13.390 14.351  14.047  1.00 11.36 ? 131 PHE A CB  1 
ATOM   1028 C  CG  . PHE A 1 130 ? 14.043 13.066  14.358  1.00 12.85 ? 131 PHE A CG  1 
ATOM   1029 C  CD1 . PHE A 1 130 ? 13.284 12.042  14.986  1.00 11.37 ? 131 PHE A CD1 1 
ATOM   1030 C  CD2 . PHE A 1 130 ? 15.364 12.807  13.996  1.00 13.50 ? 131 PHE A CD2 1 
ATOM   1031 C  CE1 . PHE A 1 130 ? 13.846 10.826  15.300  1.00 14.36 ? 131 PHE A CE1 1 
ATOM   1032 C  CE2 . PHE A 1 130 ? 15.929 11.609  14.290  1.00 14.36 ? 131 PHE A CE2 1 
ATOM   1033 C  CZ  . PHE A 1 130 ? 15.176 10.598  14.949  1.00 16.35 ? 131 PHE A CZ  1 
ATOM   1034 N  N   . GLY A 1 131 ? 15.651 16.436  14.868  1.00 12.20 ? 132 GLY A N   1 
ATOM   1035 C  CA  . GLY A 1 131 ? 17.071 16.556  15.148  1.00 12.48 ? 132 GLY A CA  1 
ATOM   1036 C  C   . GLY A 1 131 ? 17.310 17.191  16.518  1.00 12.95 ? 132 GLY A C   1 
ATOM   1037 O  O   . GLY A 1 131 ? 18.289 16.850  17.204  1.00 13.74 ? 132 GLY A O   1 
ATOM   1038 N  N   . LYS A 1 132 ? 16.408 18.074  16.931  1.00 11.93 ? 133 LYS A N   1 
ATOM   1039 C  CA  . LYS A 1 132 ? 16.551 18.664  18.266  1.00 12.08 ? 133 LYS A CA  1 
ATOM   1040 C  C   . LYS A 1 132 ? 16.057 17.697  19.367  1.00 12.55 ? 133 LYS A C   1 
ATOM   1041 O  O   . LYS A 1 132 ? 16.580 17.617  20.465  1.00 11.16 ? 133 LYS A O   1 
ATOM   1042 C  CB  . LYS A 1 132 ? 15.783 19.971  18.352  1.00 12.80 ? 133 LYS A CB  1 
ATOM   1043 C  CG  . LYS A 1 132 ? 16.467 21.147  17.612  1.00 15.66 ? 133 LYS A CG  1 
ATOM   1044 C  CD  . LYS A 1 132 ? 17.848 21.473  18.217  1.00 19.48 ? 133 LYS A CD  1 
ATOM   1045 C  CE  . LYS A 1 132 ? 18.279 22.918  17.853  1.00 22.57 ? 133 LYS A CE  1 
ATOM   1046 N  NZ  . LYS A 1 132 ? 19.445 23.324  18.721  1.00 26.71 ? 133 LYS A NZ  1 
ATOM   1047 N  N   . ALA A 1 133 ? 14.998 17.009  19.040  1.00 11.14 ? 134 ALA A N   1 
ATOM   1048 C  CA  . ALA A 1 133 ? 14.398 16.039  20.018  1.00 9.84  ? 134 ALA A CA  1 
ATOM   1049 C  C   . ALA A 1 133 ? 15.409 14.982  20.422  1.00 9.44  ? 134 ALA A C   1 
ATOM   1050 O  O   . ALA A 1 133 ? 15.475 14.594  21.593  1.00 9.78  ? 134 ALA A O   1 
ATOM   1051 C  CB  . ALA A 1 133 ? 13.137 15.411  19.402  1.00 10.04 ? 134 ALA A CB  1 
ATOM   1052 N  N   . VAL A 1 134 ? 16.219 14.476  19.480  1.00 9.24  ? 135 VAL A N   1 
ATOM   1053 C  CA  . VAL A 1 134 ? 17.122 13.323  19.836  1.00 10.32 ? 135 VAL A CA  1 
ATOM   1054 C  C   . VAL A 1 134 ? 18.225 13.749  20.815  1.00 11.23 ? 135 VAL A C   1 
ATOM   1055 O  O   . VAL A 1 134 ? 18.909 12.916  21.406  1.00 10.86 ? 135 VAL A O   1 
ATOM   1056 C  CB  . VAL A 1 134 ? 17.749 12.624  18.602  1.00 10.40 ? 135 VAL A CB  1 
ATOM   1057 C  CG1 . VAL A 1 134 ? 16.648 12.046  17.721  1.00 11.25 ? 135 VAL A CG1 1 
ATOM   1058 C  CG2 . VAL A 1 134 ? 18.641 13.547  17.828  1.00 11.26 ? 135 VAL A CG2 1 
ATOM   1059 N  N   . GLN A 1 135 ? 18.355 15.065  21.028  1.00 11.81 ? 136 GLN A N   1 
ATOM   1060 C  CA  . GLN A 1 135 ? 19.376 15.569  21.983  1.00 12.57 ? 136 GLN A CA  1 
ATOM   1061 C  C   . GLN A 1 135 ? 18.807 15.683  23.391  1.00 12.15 ? 136 GLN A C   1 
ATOM   1062 O  O   . GLN A 1 135 ? 19.468 16.223  24.311  1.00 12.93 ? 136 GLN A O   1 
ATOM   1063 C  CB  . GLN A 1 135 ? 19.836 16.961  21.490  1.00 14.61 ? 136 GLN A CB  1 
ATOM   1064 C  CG  . GLN A 1 135 ? 20.381 16.904  20.089  1.00 16.16 ? 136 GLN A CG  1 
ATOM   1065 C  CD  . GLN A 1 135 ? 20.884 18.225  19.534  1.00 23.64 ? 136 GLN A CD  1 
ATOM   1066 O  OE1 . GLN A 1 135 ? 20.511 18.608  18.414  1.00 26.38 ? 136 GLN A OE1 1 
ATOM   1067 N  NE2 . GLN A 1 135 ? 21.752 18.909  20.272  1.00 21.23 ? 136 GLN A NE2 1 
ATOM   1068 N  N   . GLN A 1 136 ? 17.576 15.238  23.576  1.00 10.86 ? 137 GLN A N   1 
ATOM   1069 C  CA  . GLN A 1 136 ? 16.874 15.405  24.870  1.00 11.13 ? 137 GLN A CA  1 
ATOM   1070 C  C   . GLN A 1 136 ? 16.481 14.031  25.458  1.00 10.48 ? 137 GLN A C   1 
ATOM   1071 O  O   . GLN A 1 136 ? 16.128 13.106  24.740  1.00 9.22  ? 137 GLN A O   1 
ATOM   1072 C  CB  . GLN A 1 136 ? 15.607 16.218  24.684  1.00 11.12 ? 137 GLN A CB  1 
ATOM   1073 C  CG  . GLN A 1 136 ? 15.911 17.598  24.047  1.00 14.78 ? 137 GLN A CG  1 
ATOM   1074 C  CD  . GLN A 1 136 ? 16.805 18.499  24.924  1.00 16.22 ? 137 GLN A CD  1 
ATOM   1075 O  OE1 . GLN A 1 136 ? 16.831 18.379  26.125  1.00 22.34 ? 137 GLN A OE1 1 
ATOM   1076 N  NE2 . GLN A 1 136 ? 17.575 19.325  24.298  1.00 23.27 ? 137 GLN A NE2 1 
ATOM   1077 N  N   . PRO A 1 137 ? 16.505 13.890  26.808  1.00 11.34 ? 138 PRO A N   1 
ATOM   1078 C  CA  . PRO A 1 137 ? 16.234 12.585  27.420  1.00 11.18 ? 138 PRO A CA  1 
ATOM   1079 C  C   . PRO A 1 137 ? 14.786 12.142  27.212  1.00 10.92 ? 138 PRO A C   1 
ATOM   1080 O  O   . PRO A 1 137 ? 14.507 10.910  27.261  1.00 10.51 ? 138 PRO A O   1 
ATOM   1081 C  CB  . PRO A 1 137 ? 16.523 12.778  28.924  1.00 13.28 ? 138 PRO A CB  1 
ATOM   1082 C  CG  . PRO A 1 137 ? 16.652 14.260  29.116  1.00 15.01 ? 138 PRO A CG  1 
ATOM   1083 C  CD  . PRO A 1 137 ? 16.989 14.891  27.780  1.00 12.66 ? 138 PRO A CD  1 
ATOM   1084 N  N   . ASP A 1 138 ? 13.884 13.100  26.977  1.00 9.67  ? 139 ASP A N   1 
ATOM   1085 C  CA  . ASP A 1 138 ? 12.467 12.767  26.707  1.00 9.92  ? 139 ASP A CA  1 
ATOM   1086 C  C   . ASP A 1 138 ? 12.124 13.141  25.252  1.00 8.52  ? 139 ASP A C   1 
ATOM   1087 O  O   . ASP A 1 138 ? 10.999 13.537  24.935  1.00 8.06  ? 139 ASP A O   1 
ATOM   1088 C  CB  . ASP A 1 138 ? 11.501 13.439  27.719  1.00 11.42 ? 139 ASP A CB  1 
ATOM   1089 C  CG  . ASP A 1 138 ? 11.621 14.915  27.769  1.00 13.20 ? 139 ASP A CG  1 
ATOM   1090 O  OD1 . ASP A 1 138 ? 12.552 15.450  27.159  1.00 12.92 ? 139 ASP A OD1 1 
ATOM   1091 O  OD2 . ASP A 1 138 ? 10.730 15.558  28.410  1.00 15.07 ? 139 ASP A OD2 1 
ATOM   1092 N  N   . GLY A 1 139 ? 13.105 13.005  24.356  1.00 7.60  ? 140 GLY A N   1 
ATOM   1093 C  CA  . GLY A 1 139 ? 12.864 13.573  23.007  1.00 6.94  ? 140 GLY A CA  1 
ATOM   1094 C  C   . GLY A 1 139 ? 12.048 12.640  22.108  1.00 8.31  ? 140 GLY A C   1 
ATOM   1095 O  O   . GLY A 1 139 ? 11.331 13.151  21.232  1.00 7.81  ? 140 GLY A O   1 
ATOM   1096 N  N   . LEU A 1 140 ? 12.159 11.319  22.317  1.00 7.78  ? 141 LEU A N   1 
ATOM   1097 C  CA  . LEU A 1 140 ? 11.498 10.390  21.378  1.00 7.84  ? 141 LEU A CA  1 
ATOM   1098 C  C   . LEU A 1 140 ? 10.596 9.445   22.178  1.00 7.84  ? 141 LEU A C   1 
ATOM   1099 O  O   . LEU A 1 140 ? 10.833 9.167   23.371  1.00 8.44  ? 141 LEU A O   1 
ATOM   1100 C  CB  . LEU A 1 140 ? 12.530 9.565   20.628  1.00 8.73  ? 141 LEU A CB  1 
ATOM   1101 C  CG  . LEU A 1 140 ? 13.471 10.221  19.615  1.00 10.96 ? 141 LEU A CG  1 
ATOM   1102 C  CD1 . LEU A 1 140 ? 14.076 9.124   18.732  1.00 9.03  ? 141 LEU A CD1 1 
ATOM   1103 C  CD2 . LEU A 1 140 ? 12.808 11.154  18.649  1.00 11.90 ? 141 LEU A CD2 1 
ATOM   1104 N  N   . ALA A 1 141 ? 9.573  8.918   21.515  1.00 8.04  ? 142 ALA A N   1 
ATOM   1105 C  CA  . ALA A 1 141 ? 8.757  7.813   22.036  1.00 7.32  ? 142 ALA A CA  1 
ATOM   1106 C  C   . ALA A 1 141 ? 8.744  6.798   20.901  1.00 7.70  ? 142 ALA A C   1 
ATOM   1107 O  O   . ALA A 1 141 ? 8.339  7.164   19.774  1.00 7.88  ? 142 ALA A O   1 
ATOM   1108 C  CB  . ALA A 1 141 ? 7.326  8.311   22.361  1.00 7.29  ? 142 ALA A CB  1 
ATOM   1109 N  N   . VAL A 1 142 ? 9.222  5.574   21.154  1.00 7.28  ? 143 VAL A N   1 
ATOM   1110 C  CA  . VAL A 1 142 ? 9.191  4.525   20.134  1.00 7.88  ? 143 VAL A CA  1 
ATOM   1111 C  C   . VAL A 1 142 ? 8.197  3.482   20.610  1.00 8.15  ? 143 VAL A C   1 
ATOM   1112 O  O   . VAL A 1 142 ? 8.347  2.919   21.737  1.00 7.57  ? 143 VAL A O   1 
ATOM   1113 C  CB  . VAL A 1 142 ? 10.576 3.947   19.783  1.00 8.01  ? 143 VAL A CB  1 
ATOM   1114 C  CG1 . VAL A 1 142 ? 10.482 2.910   18.630  1.00 8.25  ? 143 VAL A CG1 1 
ATOM   1115 C  CG2 . VAL A 1 142 ? 11.500 5.067   19.372  1.00 8.32  ? 143 VAL A CG2 1 
ATOM   1116 N  N   . LEU A 1 143 ? 7.227  3.163   19.744  1.00 7.39  ? 144 LEU A N   1 
ATOM   1117 C  CA  . LEU A 1 143 ? 6.278  2.102   20.031  1.00 7.90  ? 144 LEU A CA  1 
ATOM   1118 C  C   . LEU A 1 143 ? 6.810  0.863   19.355  1.00 8.63  ? 144 LEU A C   1 
ATOM   1119 O  O   . LEU A 1 143 ? 6.983  0.878   18.106  1.00 8.98  ? 144 LEU A O   1 
ATOM   1120 C  CB  . LEU A 1 143 ? 4.904  2.536   19.427  1.00 9.20  ? 144 LEU A CB  1 
ATOM   1121 C  CG  . LEU A 1 143 ? 3.783  1.565   19.553  1.00 9.66  ? 144 LEU A CG  1 
ATOM   1122 C  CD1 . LEU A 1 143 ? 3.520  1.328   21.025  1.00 10.80 ? 144 LEU A CD1 1 
ATOM   1123 C  CD2 . LEU A 1 143 ? 2.537  2.177   18.929  1.00 8.76  ? 144 LEU A CD2 1 
ATOM   1124 N  N   . GLY A 1 144 ? 7.083  -0.165  20.158  1.00 8.65  ? 145 GLY A N   1 
ATOM   1125 C  CA  . GLY A 1 144 ? 7.691  -1.397  19.674  1.00 8.12  ? 145 GLY A CA  1 
ATOM   1126 C  C   . GLY A 1 144 ? 6.614  -2.484  19.649  1.00 8.65  ? 145 GLY A C   1 
ATOM   1127 O  O   . GLY A 1 144 ? 5.853  -2.630  20.629  1.00 9.15  ? 145 GLY A O   1 
ATOM   1128 N  N   . ILE A 1 145 ? 6.531  -3.236  18.548  1.00 7.83  ? 146 ILE A N   1 
ATOM   1129 C  CA  . ILE A 1 145 ? 5.470  -4.281  18.372  1.00 7.32  ? 146 ILE A CA  1 
ATOM   1130 C  C   . ILE A 1 145 ? 6.185  -5.544  17.890  1.00 7.83  ? 146 ILE A C   1 
ATOM   1131 O  O   . ILE A 1 145 ? 6.893  -5.536  16.863  1.00 8.43  ? 146 ILE A O   1 
ATOM   1132 C  CB  . ILE A 1 145 ? 4.417  -3.786  17.353  1.00 7.43  ? 146 ILE A CB  1 
ATOM   1133 C  CG1 . ILE A 1 145 ? 3.763  -2.494  17.934  1.00 8.22  ? 146 ILE A CG1 1 
ATOM   1134 C  CG2 . ILE A 1 145 ? 3.377  -4.918  17.160  1.00 8.75  ? 146 ILE A CG2 1 
ATOM   1135 C  CD1 . ILE A 1 145 ? 2.659  -1.932  17.039  1.00 7.92  ? 146 ILE A CD1 1 
ATOM   1136 N  N   . PHE A 1 146 ? 5.997  -6.642  18.601  1.00 8.44  ? 147 PHE A N   1 
ATOM   1137 C  CA  . PHE A 1 146 ? 6.668  -7.912  18.140  1.00 7.06  ? 147 PHE A CA  1 
ATOM   1138 C  C   . PHE A 1 146 ? 5.907  -8.539  16.988  1.00 7.80  ? 147 PHE A C   1 
ATOM   1139 O  O   . PHE A 1 146 ? 4.682  -8.387  16.902  1.00 7.53  ? 147 PHE A O   1 
ATOM   1140 C  CB  . PHE A 1 146 ? 6.675  -8.896  19.308  1.00 7.45  ? 147 PHE A CB  1 
ATOM   1141 C  CG  . PHE A 1 146 ? 7.516  -8.423  20.428  1.00 7.07  ? 147 PHE A CG  1 
ATOM   1142 C  CD1 . PHE A 1 146 ? 8.872  -8.272  20.221  1.00 6.85  ? 147 PHE A CD1 1 
ATOM   1143 C  CD2 . PHE A 1 146 ? 6.988  -8.219  21.697  1.00 7.84  ? 147 PHE A CD2 1 
ATOM   1144 C  CE1 . PHE A 1 146 ? 9.688  -7.822  21.296  1.00 7.43  ? 147 PHE A CE1 1 
ATOM   1145 C  CE2 . PHE A 1 146 ? 7.731  -7.757  22.781  1.00 8.93  ? 147 PHE A CE2 1 
ATOM   1146 C  CZ  . PHE A 1 146 ? 9.093  -7.578  22.579  1.00 7.83  ? 147 PHE A CZ  1 
ATOM   1147 N  N   . LEU A 1 147 ? 6.632  -9.216  16.093  1.00 7.63  ? 148 LEU A N   1 
ATOM   1148 C  CA  . LEU A 1 147 ? 6.022  -10.007 15.011  1.00 7.42  ? 148 LEU A CA  1 
ATOM   1149 C  C   . LEU A 1 147 ? 6.343  -11.483 15.244  1.00 9.02  ? 148 LEU A C   1 
ATOM   1150 O  O   . LEU A 1 147 ? 7.522  -11.818 15.475  1.00 7.87  ? 148 LEU A O   1 
ATOM   1151 C  CB  . LEU A 1 147 ? 6.638  -9.614  13.641  1.00 8.05  ? 148 LEU A CB  1 
ATOM   1152 C  CG  . LEU A 1 147 ? 6.031  -8.360  12.968  1.00 8.00  ? 148 LEU A CG  1 
ATOM   1153 C  CD1 . LEU A 1 147 ? 6.293  -7.078  13.841  1.00 8.60  ? 148 LEU A CD1 1 
ATOM   1154 C  CD2 . LEU A 1 147 ? 6.656  -8.139  11.576  1.00 9.26  ? 148 LEU A CD2 1 
ATOM   1155 N  N   . LYS A 1 148 ? 5.305  -12.350 15.157  1.00 9.96  ? 149 LYS A N   1 
ATOM   1156 C  CA  . LYS A 1 148 ? 5.550  -13.773 15.117  1.00 10.47 ? 149 LYS A CA  1 
ATOM   1157 C  C   . LYS A 1 148 ? 5.035  -14.264 13.773  1.00 11.46 ? 149 LYS A C   1 
ATOM   1158 O  O   . LYS A 1 148 ? 4.221  -13.581 13.138  1.00 10.48 ? 149 LYS A O   1 
ATOM   1159 C  CB  . LYS A 1 148 ? 4.830  -14.505 16.261  1.00 12.02 ? 149 LYS A CB  1 
ATOM   1160 C  CG  . LYS A 1 148 ? 3.308  -14.220 16.285  1.00 16.25 ? 149 LYS A CG  1 
ATOM   1161 C  CD  . LYS A 1 148 ? 2.706  -15.009 17.441  1.00 20.79 ? 149 LYS A CD  1 
ATOM   1162 C  CE  . LYS A 1 148 ? 1.214  -15.244 17.221  1.00 26.47 ? 149 LYS A CE  1 
ATOM   1163 N  NZ  . LYS A 1 148 ? 0.549  -15.859 18.443  1.00 31.23 ? 149 LYS A NZ  1 
ATOM   1164 N  N   . VAL A 1 149 ? 5.535  -15.439 13.347  1.00 9.99  ? 150 VAL A N   1 
ATOM   1165 C  CA  . VAL A 1 149 ? 5.141  -15.981 12.029  1.00 11.72 ? 150 VAL A CA  1 
ATOM   1166 C  C   . VAL A 1 149 ? 3.915  -16.875 12.252  1.00 12.91 ? 150 VAL A C   1 
ATOM   1167 O  O   . VAL A 1 149 ? 3.945  -17.801 13.081  1.00 14.21 ? 150 VAL A O   1 
ATOM   1168 C  CB  . VAL A 1 149 ? 6.296  -16.809 11.478  1.00 12.03 ? 150 VAL A CB  1 
ATOM   1169 C  CG1 . VAL A 1 149 ? 5.896  -17.614 10.240  1.00 12.15 ? 150 VAL A CG1 1 
ATOM   1170 C  CG2 . VAL A 1 149 ? 7.450  -15.876 11.104  1.00 13.74 ? 150 VAL A CG2 1 
ATOM   1171 N  N   . GLY A 1 150 ? 2.852  -16.605 11.507  1.00 11.99 ? 151 GLY A N   1 
ATOM   1172 C  CA  . GLY A 1 150 ? 1.649  -17.447 11.567  1.00 14.47 ? 151 GLY A CA  1 
ATOM   1173 C  C   . GLY A 1 150 ? 0.764  -16.980 10.434  1.00 13.26 ? 151 GLY A C   1 
ATOM   1174 O  O   . GLY A 1 150 ? 1.160  -17.116 9.282   1.00 12.52 ? 151 GLY A O   1 
ATOM   1175 N  N   A SER A 1 151 ? -0.430 -16.446 10.742  0.50 13.75 ? 152 SER A N   1 
ATOM   1176 N  N   B SER A 1 151 ? -0.399 -16.414 10.771  0.50 13.62 ? 152 SER A N   1 
ATOM   1177 C  CA  A SER A 1 151 ? -1.312 -15.942 9.664   0.50 14.43 ? 152 SER A CA  1 
ATOM   1178 C  CA  B SER A 1 151 ? -1.301 -15.856 9.760   0.50 14.28 ? 152 SER A CA  1 
ATOM   1179 C  C   A SER A 1 151 ? -0.747 -14.643 9.106   0.50 14.39 ? 152 SER A C   1 
ATOM   1180 C  C   B SER A 1 151 ? -0.698 -14.616 9.107   0.50 14.28 ? 152 SER A C   1 
ATOM   1181 O  O   A SER A 1 151 ? -0.028 -13.937 9.806   0.50 13.77 ? 152 SER A O   1 
ATOM   1182 O  O   B SER A 1 151 ? 0.093  -13.919 9.746   0.50 13.67 ? 152 SER A O   1 
ATOM   1183 C  CB  A SER A 1 151 ? -2.754 -15.721 10.123  0.50 15.79 ? 152 SER A CB  1 
ATOM   1184 C  CB  B SER A 1 151 ? -2.617 -15.484 10.403  0.50 15.45 ? 152 SER A CB  1 
ATOM   1185 O  OG  A SER A 1 151 ? -2.838 -14.806 11.213  0.50 15.21 ? 152 SER A OG  1 
ATOM   1186 O  OG  B SER A 1 151 ? -3.268 -16.659 10.848  0.50 14.89 ? 152 SER A OG  1 
ATOM   1187 N  N   . ALA A 1 152 ? -1.026 -14.363 7.838   1.00 12.94 ? 153 ALA A N   1 
ATOM   1188 C  CA  . ALA A 1 152 ? -0.656 -13.079 7.243   1.00 12.36 ? 153 ALA A CA  1 
ATOM   1189 C  C   . ALA A 1 152 ? -1.291 -11.835 7.958   1.00 12.19 ? 153 ALA A C   1 
ATOM   1190 O  O   . ALA A 1 152 ? -2.373 -11.902 8.546   1.00 12.93 ? 153 ALA A O   1 
ATOM   1191 C  CB  . ALA A 1 152 ? -1.016 -13.020 5.742   1.00 13.03 ? 153 ALA A CB  1 
ATOM   1192 N  N   . LYS A 1 153 ? -0.569 -10.735 7.912   1.00 11.95 ? 154 LYS A N   1 
ATOM   1193 C  CA  . LYS A 1 153 ? -1.078 -9.470  8.379   1.00 13.12 ? 154 LYS A CA  1 
ATOM   1194 C  C   . LYS A 1 153 ? -1.490 -8.670  7.141   1.00 13.69 ? 154 LYS A C   1 
ATOM   1195 O  O   . LYS A 1 153 ? -0.673 -8.163  6.353   1.00 12.90 ? 154 LYS A O   1 
ATOM   1196 C  CB  . LYS A 1 153 ? 0.031  -8.712  9.178   1.00 13.91 ? 154 LYS A CB  1 
ATOM   1197 C  CG  . LYS A 1 153 ? -0.508 -7.490  9.919   1.00 15.56 ? 154 LYS A CG  1 
ATOM   1198 C  CD  . LYS A 1 153 ? -1.290 -7.938  11.165  1.00 15.94 ? 154 LYS A CD  1 
ATOM   1199 C  CE  . LYS A 1 153 ? -1.661 -6.769  12.048  1.00 18.63 ? 154 LYS A CE  1 
ATOM   1200 N  NZ  . LYS A 1 153 ? -2.597 -7.231  13.127  1.00 20.05 ? 154 LYS A NZ  1 
ATOM   1201 N  N   . PRO A 1 154 ? -2.816 -8.611  6.900   1.00 15.82 ? 155 PRO A N   1 
ATOM   1202 C  CA  . PRO A 1 154 ? -3.266 -7.923  5.650   1.00 16.30 ? 155 PRO A CA  1 
ATOM   1203 C  C   . PRO A 1 154 ? -2.723 -6.503  5.539   1.00 15.77 ? 155 PRO A C   1 
ATOM   1204 O  O   . PRO A 1 154 ? -2.283 -6.113  4.458   1.00 18.11 ? 155 PRO A O   1 
ATOM   1205 C  CB  . PRO A 1 154 ? -4.814 -7.958  5.773   1.00 16.85 ? 155 PRO A CB  1 
ATOM   1206 C  CG  . PRO A 1 154 ? -5.092 -9.039  6.771   1.00 20.05 ? 155 PRO A CG  1 
ATOM   1207 C  CD  . PRO A 1 154 ? -3.940 -9.075  7.725   1.00 17.61 ? 155 PRO A CD  1 
ATOM   1208 N  N   . GLY A 1 155 ? -2.614 -5.783  6.641   1.00 15.75 ? 156 GLY A N   1 
ATOM   1209 C  CA  . GLY A 1 155 ? -2.188 -4.385  6.602   1.00 14.65 ? 156 GLY A CA  1 
ATOM   1210 C  C   . GLY A 1 155 ? -0.723 -4.196  6.357   1.00 16.30 ? 156 GLY A C   1 
ATOM   1211 O  O   . GLY A 1 155 ? -0.282 -3.061  6.152   1.00 17.15 ? 156 GLY A O   1 
ATOM   1212 N  N   . LEU A 1 156 ? 0.030  -5.304  6.355   1.00 14.54 ? 157 LEU A N   1 
ATOM   1213 C  CA  . LEU A 1 156 ? 1.451  -5.268  5.986   1.00 12.83 ? 157 LEU A CA  1 
ATOM   1214 C  C   . LEU A 1 156 ? 1.702  -5.516  4.538   1.00 13.27 ? 157 LEU A C   1 
ATOM   1215 O  O   . LEU A 1 156 ? 2.797  -5.264  4.027   1.00 14.03 ? 157 LEU A O   1 
ATOM   1216 C  CB  . LEU A 1 156 ? 2.257  -6.269  6.854   1.00 11.34 ? 157 LEU A CB  1 
ATOM   1217 C  CG  . LEU A 1 156 ? 3.756  -6.481  6.653   1.00 10.86 ? 157 LEU A CG  1 
ATOM   1218 C  CD1 . LEU A 1 156 ? 4.433  -5.166  7.109   1.00 11.89 ? 157 LEU A CD1 1 
ATOM   1219 C  CD2 . LEU A 1 156 ? 4.237  -7.759  7.390   1.00 11.99 ? 157 LEU A CD2 1 
ATOM   1220 N  N   . GLN A 1 157 ? 0.715  -6.081  3.844   1.00 13.84 ? 158 GLN A N   1 
ATOM   1221 C  CA  . GLN A 1 157 ? 1.016  -6.473  2.491   1.00 14.35 ? 158 GLN A CA  1 
ATOM   1222 C  C   . GLN A 1 157 ? 1.459  -5.331  1.568   1.00 12.89 ? 158 GLN A C   1 
ATOM   1223 O  O   . GLN A 1 157 ? 2.312  -5.585  0.754   1.00 14.61 ? 158 GLN A O   1 
ATOM   1224 C  CB  . GLN A 1 157 ? -0.095 -7.362  1.874   1.00 15.08 ? 158 GLN A CB  1 
ATOM   1225 C  CG  . GLN A 1 157 ? 0.356  -8.080  0.573   1.00 16.33 ? 158 GLN A CG  1 
ATOM   1226 C  CD  . GLN A 1 157 ? 1.468  -9.123  0.846   1.00 17.45 ? 158 GLN A CD  1 
ATOM   1227 O  OE1 . GLN A 1 157 ? 1.494  -9.750  1.914   1.00 17.46 ? 158 GLN A OE1 1 
ATOM   1228 N  NE2 . GLN A 1 157 ? 2.350  -9.333  -0.111  1.00 18.91 ? 158 GLN A NE2 1 
ATOM   1229 N  N   . LYS A 1 158 ? 0.940  -4.105  1.682   1.00 15.39 ? 159 LYS A N   1 
ATOM   1230 C  CA  . LYS A 1 158 ? 1.307  -3.097  0.748   1.00 14.47 ? 159 LYS A CA  1 
ATOM   1231 C  C   . LYS A 1 158 ? 2.813  -2.781  0.936   1.00 14.52 ? 159 LYS A C   1 
ATOM   1232 O  O   . LYS A 1 158 ? 3.508  -2.409  0.001   1.00 15.65 ? 159 LYS A O   1 
ATOM   1233 C  CB  . LYS A 1 158 ? 0.424  -1.837  0.963   1.00 18.27 ? 159 LYS A CB  1 
ATOM   1234 C  CG  . LYS A 1 158 ? 0.854  -0.544  0.252   1.00 25.76 ? 159 LYS A CG  1 
ATOM   1235 C  CD  . LYS A 1 158 ? -0.100 0.634   0.599   1.00 27.44 ? 159 LYS A CD  1 
ATOM   1236 C  CE  . LYS A 1 158 ? 0.314  2.001   -0.002  1.00 29.04 ? 159 LYS A CE  1 
ATOM   1237 N  NZ  . LYS A 1 158 ? 0.253  1.891   -1.519  1.00 34.79 ? 159 LYS A NZ  1 
ATOM   1238 N  N   . VAL A 1 159 ? 3.292  -2.919  2.191   1.00 14.07 ? 160 VAL A N   1 
ATOM   1239 C  CA  . VAL A 1 159 ? 4.746  -2.749  2.447   1.00 13.09 ? 160 VAL A CA  1 
ATOM   1240 C  C   . VAL A 1 159 ? 5.584  -3.851  1.774   1.00 12.88 ? 160 VAL A C   1 
ATOM   1241 O  O   . VAL A 1 159 ? 6.575  -3.570  1.093   1.00 13.47 ? 160 VAL A O   1 
ATOM   1242 C  CB  . VAL A 1 159 ? 5.042  -2.725  3.955   1.00 13.47 ? 160 VAL A CB  1 
ATOM   1243 C  CG1 . VAL A 1 159 ? 6.559  -2.683  4.162   1.00 13.48 ? 160 VAL A CG1 1 
ATOM   1244 C  CG2 . VAL A 1 159 ? 4.328  -1.559  4.675   1.00 14.27 ? 160 VAL A CG2 1 
ATOM   1245 N  N   . VAL A 1 160 ? 5.180  -5.117  1.949   1.00 13.03 ? 161 VAL A N   1 
ATOM   1246 C  CA  . VAL A 1 160 ? 5.915  -6.281  1.401   1.00 15.57 ? 161 VAL A CA  1 
ATOM   1247 C  C   . VAL A 1 160 ? 5.944  -6.153  -0.112  1.00 14.72 ? 161 VAL A C   1 
ATOM   1248 O  O   . VAL A 1 160 ? 6.937  -6.390  -0.743  1.00 15.34 ? 161 VAL A O   1 
ATOM   1249 C  CB  . VAL A 1 160 ? 5.181  -7.590  1.862   1.00 17.67 ? 161 VAL A CB  1 
ATOM   1250 C  CG1 . VAL A 1 160 ? 5.635  -8.801  1.065   1.00 19.62 ? 161 VAL A CG1 1 
ATOM   1251 C  CG2 . VAL A 1 160 ? 5.436  -7.756  3.365   1.00 17.69 ? 161 VAL A CG2 1 
ATOM   1252 N  N   . ASP A 1 161 ? 4.863  -5.656  -0.671  1.00 16.66 ? 162 ASP A N   1 
ATOM   1253 C  CA  . ASP A 1 161 ? 4.797  -5.660  -2.117  1.00 17.72 ? 162 ASP A CA  1 
ATOM   1254 C  C   . ASP A 1 161 ? 5.635  -4.582  -2.808  1.00 18.84 ? 162 ASP A C   1 
ATOM   1255 O  O   . ASP A 1 161 ? 5.880  -4.704  -4.001  1.00 21.16 ? 162 ASP A O   1 
ATOM   1256 C  CB  . ASP A 1 161 ? 3.385  -5.643  -2.592  1.00 20.32 ? 162 ASP A CB  1 
ATOM   1257 C  CG  . ASP A 1 161 ? 2.762  -7.045  -2.631  1.00 22.65 ? 162 ASP A CG  1 
ATOM   1258 O  OD1 . ASP A 1 161 ? 3.507  -8.070  -2.742  1.00 25.30 ? 162 ASP A OD1 1 
ATOM   1259 O  OD2 . ASP A 1 161 ? 1.528  -7.094  -2.531  1.00 26.56 ? 162 ASP A OD2 1 
ATOM   1260 N  N   . VAL A 1 162 ? 6.051  -3.511  -2.102  1.00 14.61 ? 163 VAL A N   1 
ATOM   1261 C  CA  . VAL A 1 162 ? 6.915  -2.500  -2.694  1.00 15.27 ? 163 VAL A CA  1 
ATOM   1262 C  C   . VAL A 1 162 ? 8.418  -2.842  -2.489  1.00 14.91 ? 163 VAL A C   1 
ATOM   1263 O  O   . VAL A 1 162 ? 9.297  -2.185  -3.071  1.00 13.43 ? 163 VAL A O   1 
ATOM   1264 C  CB  . VAL A 1 162 ? 6.553  -1.106  -2.092  1.00 16.92 ? 163 VAL A CB  1 
ATOM   1265 C  CG1 . VAL A 1 162 ? 7.183  -0.902  -0.738  1.00 17.02 ? 163 VAL A CG1 1 
ATOM   1266 C  CG2 . VAL A 1 162 ? 6.868  -0.006  -3.055  1.00 18.10 ? 163 VAL A CG2 1 
ATOM   1267 N  N   . LEU A 1 163 ? 8.739  -3.833  -1.631  1.00 14.59 ? 164 LEU A N   1 
ATOM   1268 C  CA  . LEU A 1 163 ? 10.179 -4.102  -1.327  1.00 13.89 ? 164 LEU A CA  1 
ATOM   1269 C  C   . LEU A 1 163 ? 11.084 -4.448  -2.526  1.00 15.76 ? 164 LEU A C   1 
ATOM   1270 O  O   . LEU A 1 163 ? 12.256 -4.095  -2.545  1.00 15.21 ? 164 LEU A O   1 
ATOM   1271 C  CB  . LEU A 1 163 ? 10.360 -5.167  -0.240  1.00 13.41 ? 164 LEU A CB  1 
ATOM   1272 C  CG  . LEU A 1 163 ? 9.655  -4.828  1.064   1.00 14.04 ? 164 LEU A CG  1 
ATOM   1273 C  CD1 . LEU A 1 163 ? 9.936  -5.988  2.024   1.00 13.82 ? 164 LEU A CD1 1 
ATOM   1274 C  CD2 . LEU A 1 163 ? 10.143 -3.545  1.714   1.00 13.10 ? 164 LEU A CD2 1 
ATOM   1275 N  N   . ASP A 1 164 ? 10.524 -5.098  -3.549  1.00 15.99 ? 165 ASP A N   1 
ATOM   1276 C  CA  . ASP A 1 164 ? 11.357 -5.439  -4.671  1.00 20.20 ? 165 ASP A CA  1 
ATOM   1277 C  C   . ASP A 1 164 ? 11.780 -4.137  -5.391  1.00 19.94 ? 165 ASP A C   1 
ATOM   1278 O  O   . ASP A 1 164 ? 12.812 -4.142  -6.079  1.00 24.21 ? 165 ASP A O   1 
ATOM   1279 C  CB  . ASP A 1 164 ? 10.576 -6.387  -5.623  1.00 23.18 ? 165 ASP A CB  1 
ATOM   1280 C  CG  . ASP A 1 164 ? 9.679  -5.611  -6.529  1.00 31.46 ? 165 ASP A CG  1 
ATOM   1281 O  OD1 . ASP A 1 164 ? 8.656  -5.065  -6.028  1.00 36.09 ? 165 ASP A OD1 1 
ATOM   1282 O  OD2 . ASP A 1 164 ? 10.018 -5.479  -7.741  1.00 34.23 ? 165 ASP A OD2 1 
ATOM   1283 N  N   . SER A 1 165 ? 11.061 -3.029  -5.179  1.00 16.88 ? 166 SER A N   1 
ATOM   1284 C  CA  . SER A 1 165 ? 11.430 -1.780  -5.818  1.00 16.61 ? 166 SER A CA  1 
ATOM   1285 C  C   . SER A 1 165 ? 12.469 -0.995  -5.066  1.00 16.31 ? 166 SER A C   1 
ATOM   1286 O  O   . SER A 1 165 ? 13.062 -0.015  -5.600  1.00 15.92 ? 166 SER A O   1 
ATOM   1287 C  CB  . SER A 1 165 ? 10.206 -0.930  -6.128  1.00 17.35 ? 166 SER A CB  1 
ATOM   1288 O  OG  . SER A 1 165 ? 9.734  -0.229  -5.008  1.00 19.72 ? 166 SER A OG  1 
ATOM   1289 N  N   . ILE A 1 166 ? 12.768 -1.448  -3.833  1.00 14.19 ? 167 ILE A N   1 
ATOM   1290 C  CA  . ILE A 1 166 ? 13.827 -0.798  -3.041  1.00 12.99 ? 167 ILE A CA  1 
ATOM   1291 C  C   . ILE A 1 166 ? 14.848 -1.803  -2.528  1.00 13.74 ? 167 ILE A C   1 
ATOM   1292 O  O   . ILE A 1 166 ? 15.256 -1.776  -1.363  1.00 13.14 ? 167 ILE A O   1 
ATOM   1293 C  CB  . ILE A 1 166 ? 13.237 0.055   -1.856  1.00 12.46 ? 167 ILE A CB  1 
ATOM   1294 C  CG1 . ILE A 1 166 ? 12.333 -0.765  -0.959  1.00 12.24 ? 167 ILE A CG1 1 
ATOM   1295 C  CG2 . ILE A 1 166 ? 12.391 1.252   -2.349  1.00 13.95 ? 167 ILE A CG2 1 
ATOM   1296 C  CD1 . ILE A 1 166 ? 12.413 -0.214  0.464   1.00 14.30 ? 167 ILE A CD1 1 
ATOM   1297 N  N   . LYS A 1 167 ? 15.258 -2.712  -3.407  1.00 14.68 ? 168 LYS A N   1 
ATOM   1298 C  CA  . LYS A 1 167 ? 16.015 -3.847  -2.997  1.00 13.76 ? 168 LYS A CA  1 
ATOM   1299 C  C   . LYS A 1 167 ? 17.348 -3.479  -2.357  1.00 14.29 ? 168 LYS A C   1 
ATOM   1300 O  O   . LYS A 1 167 ? 17.746 -4.156  -1.385  1.00 12.41 ? 168 LYS A O   1 
ATOM   1301 C  CB  . LYS A 1 167 ? 16.266 -4.769  -4.194  1.00 14.26 ? 168 LYS A CB  1 
ATOM   1302 C  CG  . LYS A 1 167 ? 17.038 -6.008  -3.784  1.00 17.56 ? 168 LYS A CG  1 
ATOM   1303 C  CD  . LYS A 1 167 ? 17.225 -6.895  -5.041  1.00 22.57 ? 168 LYS A CD  1 
ATOM   1304 C  CE  . LYS A 1 167 ? 18.101 -8.102  -4.726  1.00 27.41 ? 168 LYS A CE  1 
ATOM   1305 N  NZ  . LYS A 1 167 ? 18.135 -9.097  -5.853  1.00 33.17 ? 168 LYS A NZ  1 
ATOM   1306 N  N   . THR A 1 168 ? 18.038 -2.474  -2.923  1.00 12.17 ? 169 THR A N   1 
ATOM   1307 C  CA  . THR A 1 168 ? 19.379 -2.126  -2.514  1.00 12.37 ? 169 THR A CA  1 
ATOM   1308 C  C   . THR A 1 168 ? 19.453 -0.751  -1.790  1.00 12.11 ? 169 THR A C   1 
ATOM   1309 O  O   . THR A 1 168 ? 18.572 0.114   -1.927  1.00 12.32 ? 169 THR A O   1 
ATOM   1310 C  CB  . THR A 1 168 ? 20.337 -2.193  -3.722  1.00 15.01 ? 169 THR A CB  1 
ATOM   1311 O  OG1 . THR A 1 168 ? 19.770 -1.396  -4.783  1.00 13.88 ? 169 THR A OG1 1 
ATOM   1312 C  CG2 . THR A 1 168 ? 20.377 -3.636  -4.172  1.00 15.53 ? 169 THR A CG2 1 
ATOM   1313 N  N   . LYS A 1 169 ? 20.515 -0.600  -1.021  1.00 13.35 ? 170 LYS A N   1 
ATOM   1314 C  CA  . LYS A 1 169 ? 20.848 0.616   -0.293  1.00 14.81 ? 170 LYS A CA  1 
ATOM   1315 C  C   . LYS A 1 169 ? 20.703 1.883   -1.086  1.00 15.75 ? 170 LYS A C   1 
ATOM   1316 O  O   . LYS A 1 169 ? 21.222 1.969   -2.196  1.00 17.04 ? 170 LYS A O   1 
ATOM   1317 C  CB  . LYS A 1 169 ? 22.258 0.462   0.270   1.00 15.90 ? 170 LYS A CB  1 
ATOM   1318 C  CG  . LYS A 1 169 ? 22.746 1.666   1.070   1.00 17.50 ? 170 LYS A CG  1 
ATOM   1319 C  CD  . LYS A 1 169 ? 24.188 1.406   1.487   1.00 23.03 ? 170 LYS A CD  1 
ATOM   1320 C  CE  . LYS A 1 169 ? 24.602 2.421   2.530   1.00 29.90 ? 170 LYS A CE  1 
ATOM   1321 N  NZ  . LYS A 1 169 ? 26.103 2.450   2.529   1.00 33.92 ? 170 LYS A NZ  1 
ATOM   1322 N  N   . GLY A 1 170 ? 19.935 2.834   -0.570  1.00 16.27 ? 171 GLY A N   1 
ATOM   1323 C  CA  . GLY A 1 170 ? 19.768 4.139   -1.235  1.00 15.39 ? 171 GLY A CA  1 
ATOM   1324 C  C   . GLY A 1 170 ? 18.580 4.226   -2.167  1.00 17.27 ? 171 GLY A C   1 
ATOM   1325 O  O   . GLY A 1 170 ? 18.230 5.357   -2.611  1.00 21.21 ? 171 GLY A O   1 
ATOM   1326 N  N   . LYS A 1 171 ? 17.938 3.097   -2.469  1.00 14.64 ? 172 LYS A N   1 
ATOM   1327 C  CA  . LYS A 1 171 ? 16.718 3.149   -3.272  1.00 15.68 ? 172 LYS A CA  1 
ATOM   1328 C  C   . LYS A 1 171 ? 15.483 3.560   -2.470  1.00 15.45 ? 172 LYS A C   1 
ATOM   1329 O  O   . LYS A 1 171 ? 15.326 3.150   -1.321  1.00 14.84 ? 172 LYS A O   1 
ATOM   1330 C  CB  . LYS A 1 171 ? 16.431 1.804   -3.940  1.00 17.12 ? 172 LYS A CB  1 
ATOM   1331 C  CG  . LYS A 1 171 ? 17.450 1.536   -5.036  1.00 19.55 ? 172 LYS A CG  1 
ATOM   1332 C  CD  . LYS A 1 171 ? 17.017 0.404   -6.003  1.00 28.32 ? 172 LYS A CD  1 
ATOM   1333 C  CE  . LYS A 1 171 ? 16.030 0.850   -7.102  1.00 32.19 ? 172 LYS A CE  1 
ATOM   1334 N  NZ  . LYS A 1 171 ? 15.443 -0.292  -7.921  1.00 31.02 ? 172 LYS A NZ  1 
ATOM   1335 N  N   . SER A 1 172 ? 14.602 4.328   -3.091  1.00 15.65 ? 173 SER A N   1 
ATOM   1336 C  CA  . SER A 1 172 ? 13.410 4.788   -2.455  1.00 15.81 ? 173 SER A CA  1 
ATOM   1337 C  C   . SER A 1 172 ? 12.262 4.724   -3.455  1.00 16.10 ? 173 SER A C   1 
ATOM   1338 O  O   . SER A 1 172 ? 12.486 4.577   -4.732  1.00 17.12 ? 173 SER A O   1 
ATOM   1339 C  CB  . SER A 1 172 ? 13.556 6.214   -1.909  1.00 15.84 ? 173 SER A CB  1 
ATOM   1340 O  OG  . SER A 1 172 ? 13.684 7.199   -2.933  1.00 16.17 ? 173 SER A OG  1 
ATOM   1341 N  N   . ALA A 1 173 ? 11.039 4.756   -2.910  1.00 16.29 ? 174 ALA A N   1 
ATOM   1342 C  CA  . ALA A 1 173 ? 9.837  4.625   -3.732  1.00 15.73 ? 174 ALA A CA  1 
ATOM   1343 C  C   . ALA A 1 173 ? 8.721  5.416   -3.090  1.00 18.73 ? 174 ALA A C   1 
ATOM   1344 O  O   . ALA A 1 173 ? 8.622  5.482   -1.844  1.00 15.04 ? 174 ALA A O   1 
ATOM   1345 C  CB  . ALA A 1 173 ? 9.443  3.191   -3.960  1.00 17.03 ? 174 ALA A CB  1 
ATOM   1346 N  N   A ASP A 1 174 ? 7.910  6.060   -3.923  0.50 16.74 ? 175 ASP A N   1 
ATOM   1347 N  N   B ASP A 1 174 ? 7.893  6.068   -3.918  0.50 17.27 ? 175 ASP A N   1 
ATOM   1348 C  CA  A ASP A 1 174 ? 6.699  6.712   -3.446  0.50 18.71 ? 175 ASP A CA  1 
ATOM   1349 C  CA  B ASP A 1 174 ? 6.677  6.737   -3.416  0.50 19.72 ? 175 ASP A CA  1 
ATOM   1350 C  C   A ASP A 1 174 ? 5.822  5.723   -2.627  0.50 18.59 ? 175 ASP A C   1 
ATOM   1351 C  C   B ASP A 1 174 ? 5.849  5.723   -2.609  0.50 19.25 ? 175 ASP A C   1 
ATOM   1352 O  O   A ASP A 1 174 ? 5.607  4.560   -3.018  0.50 18.38 ? 175 ASP A O   1 
ATOM   1353 O  O   B ASP A 1 174 ? 5.682  4.550   -2.996  0.50 19.05 ? 175 ASP A O   1 
ATOM   1354 C  CB  A ASP A 1 174 ? 5.932  7.329   -4.641  0.50 20.16 ? 175 ASP A CB  1 
ATOM   1355 C  CB  B ASP A 1 174 ? 5.812  7.349   -4.559  0.50 22.38 ? 175 ASP A CB  1 
ATOM   1356 C  CG  A ASP A 1 174 ? 6.772  8.365   -5.399  0.50 21.49 ? 175 ASP A CG  1 
ATOM   1357 C  CG  B ASP A 1 174 ? 4.965  8.559   -4.098  0.50 23.87 ? 175 ASP A CG  1 
ATOM   1358 O  OD1 A ASP A 1 174 ? 7.440  9.194   -4.748  0.50 24.80 ? 175 ASP A OD1 1 
ATOM   1359 O  OD1 B ASP A 1 174 ? 4.948  8.890   -2.915  0.50 29.95 ? 175 ASP A OD1 1 
ATOM   1360 O  OD2 A ASP A 1 174 ? 6.758  8.385   -6.653  0.50 21.75 ? 175 ASP A OD2 1 
ATOM   1361 O  OD2 B ASP A 1 174 ? 4.304  9.204   -4.917  0.50 29.94 ? 175 ASP A OD2 1 
ATOM   1362 N  N   . PHE A 1 175 ? 5.352  6.183   -1.467  1.00 16.95 ? 176 PHE A N   1 
ATOM   1363 C  CA  . PHE A 1 175 ? 4.603  5.307   -0.573  1.00 14.87 ? 176 PHE A CA  1 
ATOM   1364 C  C   . PHE A 1 175 ? 3.563  6.111   0.128   1.00 17.23 ? 176 PHE A C   1 
ATOM   1365 O  O   . PHE A 1 175 ? 3.582  6.281   1.365   1.00 20.87 ? 176 PHE A O   1 
ATOM   1366 C  CB  . PHE A 1 175 ? 5.565  4.551   0.411   1.00 14.95 ? 176 PHE A CB  1 
ATOM   1367 C  CG  . PHE A 1 175 ? 4.972  3.259   0.916   1.00 14.36 ? 176 PHE A CG  1 
ATOM   1368 C  CD1 . PHE A 1 175 ? 4.716  2.217   0.038   1.00 15.82 ? 176 PHE A CD1 1 
ATOM   1369 C  CD2 . PHE A 1 175 ? 4.614  3.111   2.281   1.00 14.01 ? 176 PHE A CD2 1 
ATOM   1370 C  CE1 . PHE A 1 175 ? 4.139  1.035   0.484   1.00 16.66 ? 176 PHE A CE1 1 
ATOM   1371 C  CE2 . PHE A 1 175 ? 4.046  1.929   2.724   1.00 14.33 ? 176 PHE A CE2 1 
ATOM   1372 C  CZ  . PHE A 1 175 ? 3.787  0.902   1.829   1.00 15.65 ? 176 PHE A CZ  1 
ATOM   1373 N  N   . THR A 1 176 ? 2.598  6.595   -0.652  1.00 13.74 ? 177 THR A N   1 
ATOM   1374 C  CA  . THR A 1 176 ? 1.543  7.388   -0.041  1.00 15.36 ? 177 THR A CA  1 
ATOM   1375 C  C   . THR A 1 176 ? 0.357  6.555   0.374   1.00 14.26 ? 177 THR A C   1 
ATOM   1376 O  O   . THR A 1 176 ? 0.182  5.408   -0.110  1.00 15.42 ? 177 THR A O   1 
ATOM   1377 C  CB  . THR A 1 176 ? 1.113  8.516   -1.019  1.00 18.00 ? 177 THR A CB  1 
ATOM   1378 O  OG1 . THR A 1 176 ? 0.959  7.960   -2.311  1.00 20.70 ? 177 THR A OG1 1 
ATOM   1379 C  CG2 . THR A 1 176 ? 2.164  9.559   -1.090  1.00 20.49 ? 177 THR A CG2 1 
ATOM   1380 N  N   . ASN A 1 177 ? -0.480 7.177   1.205   1.00 13.40 ? 178 ASN A N   1 
ATOM   1381 C  CA  . ASN A 1 177 ? -1.770 6.614   1.616   1.00 13.44 ? 178 ASN A CA  1 
ATOM   1382 C  C   . ASN A 1 177 ? -1.620 5.284   2.319   1.00 13.75 ? 178 ASN A C   1 
ATOM   1383 O  O   . ASN A 1 177 ? -2.510 4.412   2.257   1.00 17.36 ? 178 ASN A O   1 
ATOM   1384 C  CB  . ASN A 1 177 ? -2.683 6.485   0.399   1.00 13.30 ? 178 ASN A CB  1 
ATOM   1385 C  CG  . ASN A 1 177 ? -2.926 7.858   -0.234  1.00 16.06 ? 178 ASN A CG  1 
ATOM   1386 O  OD1 . ASN A 1 177 ? -3.591 8.718   0.360   1.00 17.45 ? 178 ASN A OD1 1 
ATOM   1387 N  ND2 . ASN A 1 177 ? -2.298 8.096   -1.381  1.00 14.67 ? 178 ASN A ND2 1 
ATOM   1388 N  N   . PHE A 1 178 ? -0.496 5.110   3.016   1.00 12.73 ? 179 PHE A N   1 
ATOM   1389 C  CA  . PHE A 1 178 ? -0.364 3.869   3.818   1.00 13.17 ? 179 PHE A CA  1 
ATOM   1390 C  C   . PHE A 1 178 ? -0.895 4.145   5.207   1.00 12.60 ? 179 PHE A C   1 
ATOM   1391 O  O   . PHE A 1 178 ? -0.452 5.087   5.865   1.00 14.24 ? 179 PHE A O   1 
ATOM   1392 C  CB  . PHE A 1 178 ? 1.057  3.346   3.862   1.00 12.61 ? 179 PHE A CB  1 
ATOM   1393 C  CG  . PHE A 1 178 ? 1.201  2.090   4.693   1.00 12.93 ? 179 PHE A CG  1 
ATOM   1394 C  CD1 . PHE A 1 178 ? 0.839  0.836   4.188   1.00 13.26 ? 179 PHE A CD1 1 
ATOM   1395 C  CD2 . PHE A 1 178 ? 1.565  2.192   6.021   1.00 13.50 ? 179 PHE A CD2 1 
ATOM   1396 C  CE1 . PHE A 1 178 ? 0.877  -0.325  4.991   1.00 14.81 ? 179 PHE A CE1 1 
ATOM   1397 C  CE2 . PHE A 1 178 ? 1.614  1.020   6.816   1.00 12.11 ? 179 PHE A CE2 1 
ATOM   1398 C  CZ  . PHE A 1 178 ? 1.270  -0.229  6.327   1.00 14.26 ? 179 PHE A CZ  1 
ATOM   1399 N  N   . ASP A 1 179 ? -1.779 3.266   5.686   1.00 11.98 ? 180 ASP A N   1 
ATOM   1400 C  CA  . ASP A 1 179 ? -2.358 3.453   7.018   1.00 12.61 ? 180 ASP A CA  1 
ATOM   1401 C  C   . ASP A 1 179 ? -1.660 2.583   8.059   1.00 11.89 ? 180 ASP A C   1 
ATOM   1402 O  O   . ASP A 1 179 ? -1.881 1.354   8.097   1.00 10.96 ? 180 ASP A O   1 
ATOM   1403 C  CB  . ASP A 1 179 ? -3.817 3.055   6.942   1.00 15.95 ? 180 ASP A CB  1 
ATOM   1404 C  CG  . ASP A 1 179 ? -4.589 3.419   8.180   1.00 19.19 ? 180 ASP A CG  1 
ATOM   1405 O  OD1 . ASP A 1 179 ? -4.012 3.712   9.238   1.00 15.71 ? 180 ASP A OD1 1 
ATOM   1406 O  OD2 . ASP A 1 179 ? -5.842 3.429   8.114   1.00 24.75 ? 180 ASP A OD2 1 
ATOM   1407 N  N   . PRO A 1 180 ? -0.880 3.225   8.973   1.00 11.68 ? 181 PRO A N   1 
ATOM   1408 C  CA  . PRO A 1 180 ? -0.177 2.373   9.950   1.00 12.33 ? 181 PRO A CA  1 
ATOM   1409 C  C   . PRO A 1 180 ? -1.091 1.740   11.024  1.00 12.42 ? 181 PRO A C   1 
ATOM   1410 O  O   . PRO A 1 180 ? -0.641 0.774   11.767  1.00 10.34 ? 181 PRO A O   1 
ATOM   1411 C  CB  . PRO A 1 180 ? 0.847  3.329   10.518  1.00 13.21 ? 181 PRO A CB  1 
ATOM   1412 C  CG  . PRO A 1 180 ? 0.124  4.683   10.512  1.00 12.79 ? 181 PRO A CG  1 
ATOM   1413 C  CD  . PRO A 1 180 ? -0.503 4.641   9.115   1.00 13.05 ? 181 PRO A CD  1 
ATOM   1414 N  N   . ARG A 1 181 ? -2.375 2.123   11.052  1.00 10.43 ? 182 ARG A N   1 
ATOM   1415 C  CA  . ARG A 1 181 ? -3.264 1.371   11.999  1.00 11.73 ? 182 ARG A CA  1 
ATOM   1416 C  C   . ARG A 1 181 ? -3.368 -0.146  11.693  1.00 12.51 ? 182 ARG A C   1 
ATOM   1417 O  O   . ARG A 1 181 ? -3.769 -0.933  12.558  1.00 13.03 ? 182 ARG A O   1 
ATOM   1418 C  CB  . ARG A 1 181 ? -4.654 2.014   11.993  1.00 12.36 ? 182 ARG A CB  1 
ATOM   1419 C  CG  . ARG A 1 181 ? -4.625 3.475   12.500  1.00 14.77 ? 182 ARG A CG  1 
ATOM   1420 C  CD  . ARG A 1 181 ? -5.973 4.164   12.403  1.00 17.93 ? 182 ARG A CD  1 
ATOM   1421 N  NE  . ARG A 1 181 ? -6.330 4.314   11.007  1.00 20.19 ? 182 ARG A NE  1 
ATOM   1422 C  CZ  . ARG A 1 181 ? -7.426 4.948   10.614  1.00 24.41 ? 182 ARG A CZ  1 
ATOM   1423 N  NH1 . ARG A 1 181 ? -8.287 5.447   11.498  1.00 24.19 ? 182 ARG A NH1 1 
ATOM   1424 N  NH2 . ARG A 1 181 ? -7.677 5.040   9.344   1.00 26.08 ? 182 ARG A NH2 1 
ATOM   1425 N  N   . GLY A 1 182 ? -3.128 -0.525  10.422  1.00 11.56 ? 183 GLY A N   1 
ATOM   1426 C  CA  . GLY A 1 182 ? -3.231 -1.918  10.026  1.00 12.49 ? 183 GLY A CA  1 
ATOM   1427 C  C   . GLY A 1 182 ? -2.056 -2.735  10.476  1.00 12.10 ? 183 GLY A C   1 
ATOM   1428 O  O   . GLY A 1 182 ? -1.994 -3.914  10.157  1.00 14.87 ? 183 GLY A O   1 
ATOM   1429 N  N   . LEU A 1 183 ? -1.137 -2.124  11.251  1.00 11.77 ? 184 LEU A N   1 
ATOM   1430 C  CA  . LEU A 1 183 ? 0.011  -2.911  11.791  1.00 11.85 ? 184 LEU A CA  1 
ATOM   1431 C  C   . LEU A 1 183 ? -0.113 -3.105  13.299  1.00 12.77 ? 184 LEU A C   1 
ATOM   1432 O  O   . LEU A 1 183 ? 0.805  -3.688  13.920  1.00 13.17 ? 184 LEU A O   1 
ATOM   1433 C  CB  . LEU A 1 183 ? 1.314  -2.102  11.558  1.00 11.72 ? 184 LEU A CB  1 
ATOM   1434 C  CG  . LEU A 1 183 ? 1.615  -1.973  10.053  1.00 12.79 ? 184 LEU A CG  1 
ATOM   1435 C  CD1 . LEU A 1 183 ? 2.829  -1.079  9.913   1.00 13.31 ? 184 LEU A CD1 1 
ATOM   1436 C  CD2 . LEU A 1 183 ? 1.810  -3.294  9.300   1.00 14.56 ? 184 LEU A CD2 1 
ATOM   1437 N  N   . LEU A 1 184 ? -1.211 -2.622  13.909  1.00 11.96 ? 185 LEU A N   1 
ATOM   1438 C  CA  . LEU A 1 184 ? -1.376 -2.682  15.385  1.00 10.64 ? 185 LEU A CA  1 
ATOM   1439 C  C   . LEU A 1 184 ? -2.071 -4.006  15.788  1.00 14.36 ? 185 LEU A C   1 
ATOM   1440 O  O   . LEU A 1 184 ? -2.969 -4.517  15.076  1.00 17.22 ? 185 LEU A O   1 
ATOM   1441 C  CB  . LEU A 1 184 ? -2.233 -1.510  15.925  1.00 10.40 ? 185 LEU A CB  1 
ATOM   1442 C  CG  . LEU A 1 184 ? -1.624 -0.127  15.605  1.00 9.50  ? 185 LEU A CG  1 
ATOM   1443 C  CD1 . LEU A 1 184 ? -2.461 1.137   15.918  1.00 10.79 ? 185 LEU A CD1 1 
ATOM   1444 C  CD2 . LEU A 1 184 ? -0.202 0.008   16.185  1.00 10.58 ? 185 LEU A CD2 1 
ATOM   1445 N  N   . PRO A 1 185 ? -1.727 -4.512  16.955  1.00 13.43 ? 186 PRO A N   1 
ATOM   1446 C  CA  . PRO A 1 185 ? -2.473 -5.613  17.465  1.00 13.57 ? 186 PRO A CA  1 
ATOM   1447 C  C   . PRO A 1 185 ? -3.792 -5.093  18.119  1.00 12.93 ? 186 PRO A C   1 
ATOM   1448 O  O   . PRO A 1 185 ? -4.035 -3.885  18.206  1.00 13.70 ? 186 PRO A O   1 
ATOM   1449 C  CB  . PRO A 1 185 ? -1.537 -6.191  18.530  1.00 13.35 ? 186 PRO A CB  1 
ATOM   1450 C  CG  . PRO A 1 185 ? -0.842 -4.978  19.086  1.00 11.83 ? 186 PRO A CG  1 
ATOM   1451 C  CD  . PRO A 1 185 ? -0.598 -4.108  17.826  1.00 11.91 ? 186 PRO A CD  1 
ATOM   1452 N  N   A GLU A 1 186 ? -4.592 -6.021  18.608  0.50 13.31 ? 187 GLU A N   1 
ATOM   1453 N  N   B GLU A 1 186 ? -4.632 -6.010  18.615  0.50 13.70 ? 187 GLU A N   1 
ATOM   1454 C  CA  A GLU A 1 186 ? -5.850 -5.640  19.168  0.50 13.96 ? 187 GLU A CA  1 
ATOM   1455 C  CA  B GLU A 1 186 ? -5.890 -5.611  19.271  0.50 14.61 ? 187 GLU A CA  1 
ATOM   1456 C  C   A GLU A 1 186 ? -5.698 -4.907  20.494  0.50 13.35 ? 187 GLU A C   1 
ATOM   1457 C  C   B GLU A 1 186 ? -5.659 -4.829  20.514  0.50 13.78 ? 187 GLU A C   1 
ATOM   1458 O  O   A GLU A 1 186 ? -6.377 -3.925  20.712  0.50 14.23 ? 187 GLU A O   1 
ATOM   1459 O  O   B GLU A 1 186 ? -6.282 -3.796  20.736  0.50 14.62 ? 187 GLU A O   1 
ATOM   1460 C  CB  A GLU A 1 186 ? -6.718 -6.879  19.301  0.50 14.81 ? 187 GLU A CB  1 
ATOM   1461 C  CB  B GLU A 1 186 ? -6.715 -6.825  19.698  0.50 15.96 ? 187 GLU A CB  1 
ATOM   1462 C  CG  A GLU A 1 186 ? -7.817 -6.746  20.312  0.50 15.39 ? 187 GLU A CG  1 
ATOM   1463 C  CG  B GLU A 1 186 ? -7.477 -7.480  18.563  0.50 18.38 ? 187 GLU A CG  1 
ATOM   1464 C  CD  A GLU A 1 186 ? -8.452 -8.087  20.659  0.50 14.68 ? 187 GLU A CD  1 
ATOM   1465 C  CD  B GLU A 1 186 ? -8.255 -8.723  19.002  0.50 18.86 ? 187 GLU A CD  1 
ATOM   1466 O  OE1 A GLU A 1 186 ? -8.334 -9.072  19.864  0.50 15.65 ? 187 GLU A OE1 1 
ATOM   1467 O  OE1 B GLU A 1 186 ? -8.335 -9.031  20.216  0.50 19.85 ? 187 GLU A OE1 1 
ATOM   1468 O  OE2 A GLU A 1 186 ? -9.073 -8.151  21.742  0.50 14.74 ? 187 GLU A OE2 1 
ATOM   1469 O  OE2 B GLU A 1 186 ? -8.771 -9.413  18.113  0.50 22.75 ? 187 GLU A OE2 1 
ATOM   1470 N  N   . SER A 1 187 ? -4.789 -5.360  21.372  1.00 12.56 ? 188 SER A N   1 
ATOM   1471 C  CA  . SER A 1 187 ? -4.605 -4.774  22.708  1.00 12.20 ? 188 SER A CA  1 
ATOM   1472 C  C   . SER A 1 187 ? -3.459 -3.779  22.665  1.00 13.12 ? 188 SER A C   1 
ATOM   1473 O  O   . SER A 1 187 ? -2.436 -4.090  22.008  1.00 13.19 ? 188 SER A O   1 
ATOM   1474 C  CB  . SER A 1 187 ? -4.242 -5.883  23.692  1.00 13.67 ? 188 SER A CB  1 
ATOM   1475 O  OG  . SER A 1 187 ? -4.055 -5.329  25.003  1.00 13.45 ? 188 SER A OG  1 
ATOM   1476 N  N   . LEU A 1 188 ? -3.633 -2.700  23.403  1.00 10.00 ? 189 LEU A N   1 
ATOM   1477 C  CA  . LEU A 1 188 ? -2.534 -1.749  23.647  1.00 12.38 ? 189 LEU A CA  1 
ATOM   1478 C  C   . LEU A 1 188 ? -1.915 -1.892  25.067  1.00 11.82 ? 189 LEU A C   1 
ATOM   1479 O  O   . LEU A 1 188 ? -1.210 -0.969  25.460  1.00 14.59 ? 189 LEU A O   1 
ATOM   1480 C  CB  . LEU A 1 188 ? -3.042 -0.306  23.411  1.00 14.67 ? 189 LEU A CB  1 
ATOM   1481 C  CG  . LEU A 1 188 ? -3.561 0.076   22.024  1.00 15.77 ? 189 LEU A CG  1 
ATOM   1482 C  CD1 . LEU A 1 188 ? -4.018 1.550   22.089  1.00 18.49 ? 189 LEU A CD1 1 
ATOM   1483 C  CD2 . LEU A 1 188 ? -2.530 -0.184  20.912  1.00 17.42 ? 189 LEU A CD2 1 
ATOM   1484 N  N   . ASP A 1 189 ? -2.056 -3.033  25.763  1.00 12.98 ? 190 ASP A N   1 
ATOM   1485 C  CA  . ASP A 1 189 ? -1.265 -3.275  27.009  1.00 12.00 ? 190 ASP A CA  1 
ATOM   1486 C  C   . ASP A 1 189 ? 0.234  -3.220  26.643  1.00 11.48 ? 190 ASP A C   1 
ATOM   1487 O  O   . ASP A 1 189 ? 0.617  -3.672  25.563  1.00 10.30 ? 190 ASP A O   1 
ATOM   1488 C  CB  . ASP A 1 189 ? -1.535 -4.603  27.657  1.00 12.98 ? 190 ASP A CB  1 
ATOM   1489 C  CG  . ASP A 1 189 ? -2.976 -4.737  28.221  1.00 15.57 ? 190 ASP A CG  1 
ATOM   1490 O  OD1 . ASP A 1 189 ? -3.662 -3.741  28.415  1.00 17.87 ? 190 ASP A OD1 1 
ATOM   1491 O  OD2 . ASP A 1 189 ? -3.396 -5.872  28.342  1.00 19.36 ? 190 ASP A OD2 1 
ATOM   1492 N  N   . TYR A 1 190 ? 1.019  -2.561  27.513  1.00 10.38 ? 191 TYR A N   1 
ATOM   1493 C  CA  . TYR A 1 190 ? 2.428  -2.315  27.172  1.00 9.61  ? 191 TYR A CA  1 
ATOM   1494 C  C   . TYR A 1 190 ? 3.337  -2.398  28.394  1.00 9.51  ? 191 TYR A C   1 
ATOM   1495 O  O   . TYR A 1 190 ? 2.892  -2.292  29.532  1.00 9.51  ? 191 TYR A O   1 
ATOM   1496 C  CB  . TYR A 1 190 ? 2.573  -0.895  26.524  1.00 10.19 ? 191 TYR A CB  1 
ATOM   1497 C  CG  . TYR A 1 190 ? 2.170  0.249   27.424  1.00 10.20 ? 191 TYR A CG  1 
ATOM   1498 C  CD1 . TYR A 1 190 ? 3.078  0.842   28.298  1.00 9.40  ? 191 TYR A CD1 1 
ATOM   1499 C  CD2 . TYR A 1 190 ? 0.874  0.742   27.393  1.00 9.64  ? 191 TYR A CD2 1 
ATOM   1500 C  CE1 . TYR A 1 190 ? 2.700  1.889   29.114  1.00 10.23 ? 191 TYR A CE1 1 
ATOM   1501 C  CE2 . TYR A 1 190 ? 0.487  1.786   28.203  1.00 10.53 ? 191 TYR A CE2 1 
ATOM   1502 C  CZ  . TYR A 1 190 ? 1.401  2.354   29.060  1.00 11.78 ? 191 TYR A CZ  1 
ATOM   1503 O  OH  . TYR A 1 190 ? 0.999  3.394   29.861  1.00 12.66 ? 191 TYR A OH  1 
ATOM   1504 N  N   . TRP A 1 191 ? 4.636  -2.561  28.121  1.00 8.77  ? 192 TRP A N   1 
ATOM   1505 C  CA  . TRP A 1 191 ? 5.687  -2.279  29.121  1.00 8.12  ? 192 TRP A CA  1 
ATOM   1506 C  C   . TRP A 1 191 ? 6.402  -1.028  28.698  1.00 7.98  ? 192 TRP A C   1 
ATOM   1507 O  O   . TRP A 1 191 ? 6.399  -0.643  27.545  1.00 8.02  ? 192 TRP A O   1 
ATOM   1508 C  CB  . TRP A 1 191 ? 6.736  -3.391  29.071  1.00 8.71  ? 192 TRP A CB  1 
ATOM   1509 C  CG  . TRP A 1 191 ? 6.205  -4.698  29.485  1.00 9.18  ? 192 TRP A CG  1 
ATOM   1510 C  CD1 . TRP A 1 191 ? 5.977  -5.162  30.801  1.00 9.81  ? 192 TRP A CD1 1 
ATOM   1511 C  CD2 . TRP A 1 191 ? 5.979  -5.838  28.620  1.00 9.76  ? 192 TRP A CD2 1 
ATOM   1512 N  NE1 . TRP A 1 191 ? 5.608  -6.496  30.768  1.00 10.39 ? 192 TRP A NE1 1 
ATOM   1513 C  CE2 . TRP A 1 191 ? 5.534  -6.939  29.477  1.00 10.27 ? 192 TRP A CE2 1 
ATOM   1514 C  CE3 . TRP A 1 191 ? 6.046  -6.028  27.256  1.00 9.50  ? 192 TRP A CE3 1 
ATOM   1515 C  CZ2 . TRP A 1 191 ? 5.212  -8.202  28.957  1.00 11.10 ? 192 TRP A CZ2 1 
ATOM   1516 C  CZ3 . TRP A 1 191 ? 5.735  -7.300  26.742  1.00 9.45  ? 192 TRP A CZ3 1 
ATOM   1517 C  CH2 . TRP A 1 191 ? 5.374  -8.374  27.588  1.00 10.87 ? 192 TRP A CH2 1 
ATOM   1518 N  N   . THR A 1 192 ? 6.901  -0.281  29.685  1.00 7.40  ? 193 THR A N   1 
ATOM   1519 C  CA  . THR A 1 192 ? 7.618  0.944   29.345  1.00 8.15  ? 193 THR A CA  1 
ATOM   1520 C  C   . THR A 1 192 ? 8.881  1.126   30.175  1.00 8.57  ? 193 THR A C   1 
ATOM   1521 O  O   . THR A 1 192 ? 8.903  0.768   31.332  1.00 9.90  ? 193 THR A O   1 
ATOM   1522 C  CB  . THR A 1 192 ? 6.722  2.191   29.401  1.00 7.79  ? 193 THR A CB  1 
ATOM   1523 O  OG1 . THR A 1 192 ? 7.427  3.407   29.035  1.00 8.20  ? 193 THR A OG1 1 
ATOM   1524 C  CG2 . THR A 1 192 ? 6.118  2.452   30.814  1.00 8.41  ? 193 THR A CG2 1 
ATOM   1525 N  N   . TYR A 1 193 ? 9.948  1.706   29.561  1.00 8.43  ? 194 TYR A N   1 
ATOM   1526 C  CA  . TYR A 1 193 ? 11.149 1.990   30.334  1.00 8.10  ? 194 TYR A CA  1 
ATOM   1527 C  C   . TYR A 1 193 ? 11.935 3.069   29.550  1.00 7.65  ? 194 TYR A C   1 
ATOM   1528 O  O   . TYR A 1 193 ? 11.657 3.280   28.340  1.00 6.71  ? 194 TYR A O   1 
ATOM   1529 C  CB  . TYR A 1 193 ? 12.049 0.731   30.491  1.00 8.29  ? 194 TYR A CB  1 
ATOM   1530 C  CG  . TYR A 1 193 ? 12.717 0.283   29.253  1.00 8.45  ? 194 TYR A CG  1 
ATOM   1531 C  CD1 . TYR A 1 193 ? 12.012 -0.444  28.253  1.00 7.81  ? 194 TYR A CD1 1 
ATOM   1532 C  CD2 . TYR A 1 193 ? 14.036 0.656   29.000  1.00 8.57  ? 194 TYR A CD2 1 
ATOM   1533 C  CE1 . TYR A 1 193 ? 12.680 -0.881  27.086  1.00 8.55  ? 194 TYR A CE1 1 
ATOM   1534 C  CE2 . TYR A 1 193 ? 14.699 0.291   27.782  1.00 9.57  ? 194 TYR A CE2 1 
ATOM   1535 C  CZ  . TYR A 1 193 ? 13.998 -0.404  26.833  1.00 9.33  ? 194 TYR A CZ  1 
ATOM   1536 O  OH  . TYR A 1 193 ? 14.671 -0.748  25.674  1.00 9.31  ? 194 TYR A OH  1 
ATOM   1537 N  N   . PRO A 1 194 ? 12.876 3.745   30.226  1.00 8.04  ? 195 PRO A N   1 
ATOM   1538 C  CA  . PRO A 1 194 ? 13.705 4.739   29.557  1.00 7.57  ? 195 PRO A CA  1 
ATOM   1539 C  C   . PRO A 1 194 ? 14.923 4.118   28.877  1.00 8.36  ? 195 PRO A C   1 
ATOM   1540 O  O   . PRO A 1 194 ? 15.635 3.319   29.518  1.00 8.66  ? 195 PRO A O   1 
ATOM   1541 C  CB  . PRO A 1 194 ? 14.203 5.632   30.743  1.00 8.79  ? 195 PRO A CB  1 
ATOM   1542 C  CG  . PRO A 1 194 ? 14.241 4.665   31.899  1.00 9.32  ? 195 PRO A CG  1 
ATOM   1543 C  CD  . PRO A 1 194 ? 12.961 3.905   31.694  1.00 8.22  ? 195 PRO A CD  1 
ATOM   1544 N  N   . GLY A 1 195 ? 15.120 4.457   27.602  1.00 7.57  ? 196 GLY A N   1 
ATOM   1545 C  CA  . GLY A 1 195 ? 16.216 3.773   26.860  1.00 6.92  ? 196 GLY A CA  1 
ATOM   1546 C  C   . GLY A 1 195 ? 16.788 4.652   25.800  1.00 6.94  ? 196 GLY A C   1 
ATOM   1547 O  O   . GLY A 1 195 ? 16.883 5.885   25.934  1.00 7.15  ? 196 GLY A O   1 
ATOM   1548 N  N   . SER A 1 196 ? 17.222 3.994   24.731  1.00 7.65  ? 197 SER A N   1 
ATOM   1549 C  CA  . SER A 1 196 ? 17.977 4.681   23.677  1.00 7.89  ? 197 SER A CA  1 
ATOM   1550 C  C   . SER A 1 196 ? 17.527 4.284   22.267  1.00 7.66  ? 197 SER A C   1 
ATOM   1551 O  O   . SER A 1 196 ? 16.807 3.291   22.128  1.00 7.91  ? 197 SER A O   1 
ATOM   1552 C  CB  . SER A 1 196 ? 19.478 4.244   23.838  1.00 7.56  ? 197 SER A CB  1 
ATOM   1553 O  OG  . SER A 1 196 ? 19.678 2.893   23.386  1.00 7.90  ? 197 SER A OG  1 
ATOM   1554 N  N   . LEU A 1 197 ? 18.088 4.934   21.251  1.00 8.25  ? 198 LEU A N   1 
ATOM   1555 C  CA  . LEU A 1 197 ? 17.939 4.449   19.890  1.00 9.34  ? 198 LEU A CA  1 
ATOM   1556 C  C   . LEU A 1 197 ? 18.772 3.104   19.930  1.00 8.85  ? 198 LEU A C   1 
ATOM   1557 O  O   . LEU A 1 197 ? 19.831 2.927   20.647  1.00 8.99  ? 198 LEU A O   1 
ATOM   1558 C  CB  . LEU A 1 197 ? 18.657 5.295   18.848  1.00 11.87 ? 198 LEU A CB  1 
ATOM   1559 C  CG  . LEU A 1 197 ? 18.276 6.763   18.813  1.00 16.71 ? 198 LEU A CG  1 
ATOM   1560 C  CD1 . LEU A 1 197 ? 19.065 7.633   17.843  1.00 18.14 ? 198 LEU A CD1 1 
ATOM   1561 C  CD2 . LEU A 1 197 ? 16.785 6.902   18.583  1.00 19.55 ? 198 LEU A CD2 1 
ATOM   1562 N  N   . THR A 1 198 ? 18.297 2.133   19.152  1.00 6.87  ? 199 THR A N   1 
ATOM   1563 C  CA  . THR A 1 198 ? 19.027 0.802   19.100  1.00 6.70  ? 199 THR A CA  1 
ATOM   1564 C  C   . THR A 1 198 ? 20.038 0.762   17.916  1.00 7.10  ? 199 THR A C   1 
ATOM   1565 O  O   . THR A 1 198 ? 20.678 -0.321  17.737  1.00 8.37  ? 199 THR A O   1 
ATOM   1566 C  CB  . THR A 1 198 ? 18.060 -0.368  19.010  1.00 6.21  ? 199 THR A CB  1 
ATOM   1567 O  OG1 . THR A 1 198 ? 17.454 -0.299  17.709  1.00 6.79  ? 199 THR A OG1 1 
ATOM   1568 C  CG2 . THR A 1 198 ? 17.051 -0.314  20.171  1.00 6.38  ? 199 THR A CG2 1 
ATOM   1569 N  N   . THR A 1 199 ? 20.113 1.840   17.129  1.00 7.57  ? 200 THR A N   1 
ATOM   1570 C  CA  . THR A 1 199 ? 21.143 2.016   16.081  1.00 9.11  ? 200 THR A CA  1 
ATOM   1571 C  C   . THR A 1 199 ? 22.022 3.217   16.413  1.00 8.63  ? 200 THR A C   1 
ATOM   1572 O  O   . THR A 1 199 ? 21.570 4.206   16.989  1.00 9.28  ? 200 THR A O   1 
ATOM   1573 C  CB  . THR A 1 199 ? 20.504 2.240   14.715  1.00 10.08 ? 200 THR A CB  1 
ATOM   1574 O  OG1 . THR A 1 199 ? 19.513 3.296   14.811  1.00 11.18 ? 200 THR A OG1 1 
ATOM   1575 C  CG2 . THR A 1 199 ? 19.931 0.902   14.272  1.00 10.18 ? 200 THR A CG2 1 
ATOM   1576 N  N   . PRO A 1 200 ? 23.307 3.150   15.946  1.00 9.30  ? 201 PRO A N   1 
ATOM   1577 C  CA  . PRO A 1 200 ? 24.104 4.394   16.089  1.00 9.64  ? 201 PRO A CA  1 
ATOM   1578 C  C   . PRO A 1 200 ? 23.314 5.582   15.567  1.00 10.78 ? 201 PRO A C   1 
ATOM   1579 O  O   . PRO A 1 200 ? 22.721 5.455   14.461  1.00 12.85 ? 201 PRO A O   1 
ATOM   1580 C  CB  . PRO A 1 200 ? 25.298 4.082   15.183  1.00 8.71  ? 201 PRO A CB  1 
ATOM   1581 C  CG  . PRO A 1 200 ? 25.533 2.630   15.414  1.00 8.46  ? 201 PRO A CG  1 
ATOM   1582 C  CD  . PRO A 1 200 ? 24.101 2.040   15.404  1.00 8.88  ? 201 PRO A CD  1 
ATOM   1583 N  N   . PRO A 1 201 ? 23.399 6.772   16.213  1.00 11.14 ? 202 PRO A N   1 
ATOM   1584 C  CA  . PRO A 1 201 ? 24.273 7.141   17.349  1.00 10.43 ? 202 PRO A CA  1 
ATOM   1585 C  C   . PRO A 1 201 ? 23.904 6.689   18.759  1.00 10.23 ? 202 PRO A C   1 
ATOM   1586 O  O   . PRO A 1 201 ? 24.582 7.122   19.727  1.00 10.57 ? 202 PRO A O   1 
ATOM   1587 C  CB  . PRO A 1 201 ? 24.335 8.673   17.232  1.00 11.29 ? 202 PRO A CB  1 
ATOM   1588 C  CG  . PRO A 1 201 ? 22.974 9.012   16.743  1.00 11.83 ? 202 PRO A CG  1 
ATOM   1589 C  CD  . PRO A 1 201 ? 22.728 7.991   15.653  1.00 11.09 ? 202 PRO A CD  1 
ATOM   1590 N  N   . LEU A 1 202 ? 22.896 5.790   18.884  1.00 8.98  ? 203 LEU A N   1 
ATOM   1591 C  CA  . LEU A 1 202 ? 22.595 5.114   20.175  1.00 7.98  ? 203 LEU A CA  1 
ATOM   1592 C  C   . LEU A 1 202 ? 22.207 6.132   21.262  1.00 8.96  ? 203 LEU A C   1 
ATOM   1593 O  O   . LEU A 1 202 ? 22.383 5.918   22.461  1.00 7.45  ? 203 LEU A O   1 
ATOM   1594 C  CB  . LEU A 1 202 ? 23.747 4.179   20.662  1.00 7.85  ? 203 LEU A CB  1 
ATOM   1595 C  CG  . LEU A 1 202 ? 24.064 3.082   19.646  1.00 7.62  ? 203 LEU A CG  1 
ATOM   1596 C  CD1 . LEU A 1 202 ? 25.346 2.434   20.182  1.00 8.62  ? 203 LEU A CD1 1 
ATOM   1597 C  CD2 . LEU A 1 202 ? 22.945 2.015   19.605  1.00 9.09  ? 203 LEU A CD2 1 
ATOM   1598 N  N   . LEU A 1 203 ? 21.630 7.241   20.811  1.00 8.35  ? 204 LEU A N   1 
ATOM   1599 C  CA  . LEU A 1 203 ? 21.365 8.329   21.740  1.00 9.60  ? 204 LEU A CA  1 
ATOM   1600 C  C   . LEU A 1 203 ? 20.341 7.940   22.805  1.00 9.72  ? 204 LEU A C   1 
ATOM   1601 O  O   . LEU A 1 203 ? 19.350 7.274   22.509  1.00 9.22  ? 204 LEU A O   1 
ATOM   1602 C  CB  . LEU A 1 203 ? 20.866 9.601   20.997  1.00 10.08 ? 204 LEU A CB  1 
ATOM   1603 C  CG  . LEU A 1 203 ? 21.935 10.192  19.997  1.00 11.02 ? 204 LEU A CG  1 
ATOM   1604 C  CD1 . LEU A 1 203 ? 21.294 11.209  19.076  1.00 13.96 ? 204 LEU A CD1 1 
ATOM   1605 C  CD2 . LEU A 1 203 ? 23.007 10.831  20.882  1.00 12.72 ? 204 LEU A CD2 1 
ATOM   1606 N  N   . GLU A 1 204 ? 20.540 8.440   24.033  1.00 9.58  ? 205 GLU A N   1 
ATOM   1607 C  CA  . GLU A 1 204 ? 19.681 8.069   25.174  1.00 9.41  ? 205 GLU A CA  1 
ATOM   1608 C  C   . GLU A 1 204 ? 18.515 8.995   25.302  1.00 9.78  ? 205 GLU A C   1 
ATOM   1609 O  O   . GLU A 1 204 ? 18.382 9.787   26.277  1.00 10.15 ? 205 GLU A O   1 
ATOM   1610 C  CB  . GLU A 1 204 ? 20.565 7.993   26.443  1.00 9.75  ? 205 GLU A CB  1 
ATOM   1611 C  CG  . GLU A 1 204 ? 21.427 6.707   26.246  1.00 9.65  ? 205 GLU A CG  1 
ATOM   1612 C  CD  . GLU A 1 204 ? 22.386 6.415   27.433  1.00 10.89 ? 205 GLU A CD  1 
ATOM   1613 O  OE1 . GLU A 1 204 ? 22.655 7.408   28.161  1.00 10.59 ? 205 GLU A OE1 1 
ATOM   1614 O  OE2 . GLU A 1 204 ? 22.809 5.251   27.557  1.00 10.37 ? 205 GLU A OE2 1 
ATOM   1615 N  N   . CYS A 1 205 ? 17.638 8.899   24.310  1.00 8.41  ? 206 CYS A N   1 
ATOM   1616 C  CA  . CYS A 1 205 ? 16.579 9.923   24.124  1.00 7.96  ? 206 CYS A CA  1 
ATOM   1617 C  C   . CYS A 1 205 ? 15.172 9.359   24.020  1.00 7.73  ? 206 CYS A C   1 
ATOM   1618 O  O   . CYS A 1 205 ? 14.272 10.073  23.624  1.00 8.41  ? 206 CYS A O   1 
ATOM   1619 C  CB  . CYS A 1 205 ? 16.837 10.744  22.899  1.00 8.65  ? 206 CYS A CB  1 
ATOM   1620 S  SG  . CYS A 1 205 ? 16.880 9.826   21.369  1.00 9.88  ? 206 CYS A SG  1 
ATOM   1621 N  N   . VAL A 1 206 ? 15.034 8.075   24.376  1.00 6.97  ? 207 VAL A N   1 
ATOM   1622 C  CA  . VAL A 1 206 ? 13.810 7.290   23.991  1.00 6.83  ? 207 VAL A CA  1 
ATOM   1623 C  C   . VAL A 1 206 ? 13.020 6.834   25.230  1.00 6.56  ? 207 VAL A C   1 
ATOM   1624 O  O   . VAL A 1 206 ? 13.547 6.194   26.144  1.00 7.94  ? 207 VAL A O   1 
ATOM   1625 C  CB  . VAL A 1 206 ? 14.106 6.032   23.116  1.00 7.91  ? 207 VAL A CB  1 
ATOM   1626 C  CG1 . VAL A 1 206 ? 12.753 5.349   22.789  1.00 7.60  ? 207 VAL A CG1 1 
ATOM   1627 C  CG2 . VAL A 1 206 ? 14.873 6.448   21.824  1.00 8.50  ? 207 VAL A CG2 1 
ATOM   1628 N  N   . THR A 1 207 ? 11.719 7.157   25.257  1.00 7.47  ? 208 THR A N   1 
ATOM   1629 C  CA  . THR A 1 207 ? 10.778 6.410   26.126  1.00 7.11  ? 208 THR A CA  1 
ATOM   1630 C  C   . THR A 1 207 ? 10.299 5.287   25.309  1.00 7.18  ? 208 THR A C   1 
ATOM   1631 O  O   . THR A 1 207 ? 9.603  5.509   24.290  1.00 7.04  ? 208 THR A O   1 
ATOM   1632 C  CB  . THR A 1 207 ? 9.589  7.344   26.587  1.00 7.85  ? 208 THR A CB  1 
ATOM   1633 O  OG1 . THR A 1 207 ? 10.160 8.431   27.354  1.00 7.48  ? 208 THR A OG1 1 
ATOM   1634 C  CG2 . THR A 1 207 ? 8.638  6.561   27.465  1.00 8.01  ? 208 THR A CG2 1 
ATOM   1635 N  N   . TRP A 1 208 ? 10.630 4.091   25.760  1.00 7.16  ? 209 TRP A N   1 
ATOM   1636 C  CA  . TRP A 1 208 ? 10.200 2.853   25.025  1.00 7.04  ? 209 TRP A CA  1 
ATOM   1637 C  C   . TRP A 1 208 ? 8.835  2.436   25.494  1.00 7.31  ? 209 TRP A C   1 
ATOM   1638 O  O   . TRP A 1 208 ? 8.596  2.366   26.688  1.00 8.09  ? 209 TRP A O   1 
ATOM   1639 C  CB  . TRP A 1 208 ? 11.205 1.687   25.284  1.00 7.94  ? 209 TRP A CB  1 
ATOM   1640 C  CG  . TRP A 1 208 ? 12.325 1.831   24.302  1.00 7.49  ? 209 TRP A CG  1 
ATOM   1641 C  CD1 . TRP A 1 208 ? 13.581 2.428   24.456  1.00 7.59  ? 209 TRP A CD1 1 
ATOM   1642 C  CD2 . TRP A 1 208 ? 12.244 1.433   22.915  1.00 7.54  ? 209 TRP A CD2 1 
ATOM   1643 N  NE1 . TRP A 1 208 ? 14.258 2.417   23.263  1.00 7.76  ? 209 TRP A NE1 1 
ATOM   1644 C  CE2 . TRP A 1 208 ? 13.504 1.778   22.307  1.00 7.37  ? 209 TRP A CE2 1 
ATOM   1645 C  CE3 . TRP A 1 208 ? 11.252 0.794   22.145  1.00 7.67  ? 209 TRP A CE3 1 
ATOM   1646 C  CZ2 . TRP A 1 208 ? 13.780 1.534   20.982  1.00 7.69  ? 209 TRP A CZ2 1 
ATOM   1647 C  CZ3 . TRP A 1 208 ? 11.539 0.491   20.817  1.00 8.23  ? 209 TRP A CZ3 1 
ATOM   1648 C  CH2 . TRP A 1 208 ? 12.774 0.844   20.240  1.00 7.68  ? 209 TRP A CH2 1 
ATOM   1649 N  N   . ILE A 1 209 ? 7.959  2.158   24.543  1.00 7.37  ? 210 ILE A N   1 
ATOM   1650 C  CA  . ILE A 1 209 ? 6.633  1.602   24.914  1.00 7.31  ? 210 ILE A CA  1 
ATOM   1651 C  C   . ILE A 1 209 ? 6.519  0.324   24.081  1.00 7.90  ? 210 ILE A C   1 
ATOM   1652 O  O   . ILE A 1 209 ? 6.384  0.404   22.844  1.00 7.78  ? 210 ILE A O   1 
ATOM   1653 C  CB  . ILE A 1 209 ? 5.533  2.633   24.557  1.00 8.10  ? 210 ILE A CB  1 
ATOM   1654 C  CG1 . ILE A 1 209 ? 5.782  3.939   25.348  1.00 9.11  ? 210 ILE A CG1 1 
ATOM   1655 C  CG2 . ILE A 1 209 ? 4.101  1.987   24.711  1.00 8.52  ? 210 ILE A CG2 1 
ATOM   1656 C  CD1 . ILE A 1 209 ? 4.833  5.004   24.855  1.00 10.57 ? 210 ILE A CD1 1 
ATOM   1657 N  N   . VAL A 1 210 ? 6.593  -0.842  24.725  1.00 7.55  ? 211 VAL A N   1 
ATOM   1658 C  CA  . VAL A 1 210 ? 6.611  -2.085  23.950  1.00 7.50  ? 211 VAL A CA  1 
ATOM   1659 C  C   . VAL A 1 210 ? 5.323  -2.825  24.207  1.00 7.52  ? 211 VAL A C   1 
ATOM   1660 O  O   . VAL A 1 210 ? 4.990  -3.143  25.375  1.00 8.24  ? 211 VAL A O   1 
ATOM   1661 C  CB  . VAL A 1 210 ? 7.789  -2.999  24.407  1.00 6.65  ? 211 VAL A CB  1 
ATOM   1662 C  CG1 . VAL A 1 210 ? 7.804  -4.349  23.698  1.00 6.21  ? 211 VAL A CG1 1 
ATOM   1663 C  CG2 . VAL A 1 210 ? 9.119  -2.249  24.161  1.00 6.70  ? 211 VAL A CG2 1 
ATOM   1664 N  N   . LEU A 1 211 ? 4.562  -3.036  23.134  1.00 8.38  ? 212 LEU A N   1 
ATOM   1665 C  CA  . LEU A 1 211 ? 3.286  -3.749  23.318  1.00 8.71  ? 212 LEU A CA  1 
ATOM   1666 C  C   . LEU A 1 211 ? 3.487  -5.204  23.667  1.00 8.92  ? 212 LEU A C   1 
ATOM   1667 O  O   . LEU A 1 211 ? 4.341  -5.965  23.091  1.00 9.30  ? 212 LEU A O   1 
ATOM   1668 C  CB  . LEU A 1 211 ? 2.464  -3.599  22.014  1.00 8.49  ? 212 LEU A CB  1 
ATOM   1669 C  CG  . LEU A 1 211 ? 2.053  -2.219  21.536  1.00 8.45  ? 212 LEU A CG  1 
ATOM   1670 C  CD1 . LEU A 1 211 ? 0.974  -2.286  20.415  1.00 8.34  ? 212 LEU A CD1 1 
ATOM   1671 C  CD2 . LEU A 1 211 ? 1.558  -1.370  22.716  1.00 8.41  ? 212 LEU A CD2 1 
ATOM   1672 N  N   . LYS A 1 212 ? 2.619  -5.686  24.567  1.00 9.45  ? 213 LYS A N   1 
ATOM   1673 C  CA  . LYS A 1 212 ? 2.611  -7.102  24.948  1.00 9.99  ? 213 LYS A CA  1 
ATOM   1674 C  C   . LYS A 1 212 ? 2.113  -8.085  23.877  1.00 9.50  ? 213 LYS A C   1 
ATOM   1675 O  O   . LYS A 1 212 ? 2.658  -9.171  23.738  1.00 10.60 ? 213 LYS A O   1 
ATOM   1676 C  CB  . LYS A 1 212 ? 1.808  -7.273  26.238  1.00 12.04 ? 213 LYS A CB  1 
ATOM   1677 C  CG  . LYS A 1 212 ? 1.545  -8.782  26.561  1.00 16.84 ? 213 LYS A CG  1 
ATOM   1678 C  CD  . LYS A 1 212 ? 0.830  -8.862  27.898  1.00 20.00 ? 213 LYS A CD  1 
ATOM   1679 C  CE  . LYS A 1 212 ? 0.666  -10.286 28.395  1.00 25.64 ? 213 LYS A CE  1 
ATOM   1680 N  NZ  . LYS A 1 212 ? -0.454 -10.370 29.417  1.00 34.78 ? 213 LYS A NZ  1 
ATOM   1681 N  N   . GLU A 1 213 ? 1.079  -7.688  23.153  1.00 8.39  ? 214 GLU A N   1 
ATOM   1682 C  CA  . GLU A 1 213 ? 0.498  -8.570  22.158  1.00 10.75 ? 214 GLU A CA  1 
ATOM   1683 C  C   . GLU A 1 213 ? 1.262  -8.484  20.837  1.00 9.49  ? 214 GLU A C   1 
ATOM   1684 O  O   . GLU A 1 213 ? 1.334  -7.369  20.282  1.00 9.53  ? 214 GLU A O   1 
ATOM   1685 C  CB  . GLU A 1 213 ? -0.916 -8.145  21.841  1.00 11.86 ? 214 GLU A CB  1 
ATOM   1686 C  CG  . GLU A 1 213 ? -1.548 -9.241  20.993  1.00 14.07 ? 214 GLU A CG  1 
ATOM   1687 C  CD  . GLU A 1 213 ? -3.039 -9.044  20.768  1.00 18.84 ? 214 GLU A CD  1 
ATOM   1688 O  OE1 . GLU A 1 213 ? -3.673 -8.140  21.327  1.00 14.75 ? 214 GLU A OE1 1 
ATOM   1689 O  OE2 . GLU A 1 213 ? -3.581 -9.947  20.076  1.00 26.60 ? 214 GLU A OE2 1 
ATOM   1690 N  N   . PRO A 1 214 ? 1.816  -9.575  20.346  1.00 10.04 ? 215 PRO A N   1 
ATOM   1691 C  CA  . PRO A 1 214 ? 2.517  -9.530  19.044  1.00 9.83  ? 215 PRO A CA  1 
ATOM   1692 C  C   . PRO A 1 214 ? 1.501  -9.544  17.906  1.00 11.39 ? 215 PRO A C   1 
ATOM   1693 O  O   . PRO A 1 214 ? 0.329  -9.932  18.130  1.00 12.82 ? 215 PRO A O   1 
ATOM   1694 C  CB  . PRO A 1 214 ? 3.300  -10.831 18.964  1.00 10.63 ? 215 PRO A CB  1 
ATOM   1695 C  CG  . PRO A 1 214 ? 2.620  -11.765 19.896  1.00 13.64 ? 215 PRO A CG  1 
ATOM   1696 C  CD  . PRO A 1 214 ? 1.962  -10.903 20.989  1.00 11.47 ? 215 PRO A CD  1 
ATOM   1697 N  N   . ILE A 1 215 ? 1.896  -9.054  16.747  1.00 10.16 ? 216 ILE A N   1 
ATOM   1698 C  CA  . ILE A 1 215 ? 1.046  -9.260  15.569  1.00 10.50 ? 216 ILE A CA  1 
ATOM   1699 C  C   . ILE A 1 215 ? 1.552  -10.496 14.845  1.00 10.82 ? 216 ILE A C   1 
ATOM   1700 O  O   . ILE A 1 215 ? 2.720  -10.877 14.986  1.00 10.97 ? 216 ILE A O   1 
ATOM   1701 C  CB  . ILE A 1 215 ? 1.046  -8.043  14.585  1.00 10.06 ? 216 ILE A CB  1 
ATOM   1702 C  CG1 . ILE A 1 215 ? 2.491  -7.705  14.109  1.00 10.18 ? 216 ILE A CG1 1 
ATOM   1703 C  CG2 . ILE A 1 215 ? 0.370  -6.744  15.253  1.00 12.08 ? 216 ILE A CG2 1 
ATOM   1704 C  CD1 . ILE A 1 215 ? 2.563  -6.739  12.876  1.00 10.14 ? 216 ILE A CD1 1 
ATOM   1705 N  N   A SER A 1 216 ? 0.674  -11.138 14.063  0.50 10.85 ? 217 SER A N   1 
ATOM   1706 N  N   B SER A 1 216 ? 0.689  -11.172 14.085  0.50 11.21 ? 217 SER A N   1 
ATOM   1707 C  CA  A SER A 1 216 ? 1.113  -12.284 13.250  0.50 11.09 ? 217 SER A CA  1 
ATOM   1708 C  CA  B SER A 1 216 ? 1.197  -12.298 13.289  0.50 11.57 ? 217 SER A CA  1 
ATOM   1709 C  C   A SER A 1 216 ? 1.322  -11.864 11.806  0.50 11.13 ? 217 SER A C   1 
ATOM   1710 C  C   B SER A 1 216 ? 1.333  -11.883 11.837  0.50 11.43 ? 217 SER A C   1 
ATOM   1711 O  O   A SER A 1 216 ? 0.512  -11.112 11.260  0.50 12.68 ? 217 SER A O   1 
ATOM   1712 O  O   B SER A 1 216 ? 0.486  -11.152 11.324  0.50 12.87 ? 217 SER A O   1 
ATOM   1713 C  CB  A SER A 1 216 ? 0.101  -13.430 13.271  0.50 11.42 ? 217 SER A CB  1 
ATOM   1714 C  CB  B SER A 1 216 ? 0.299  -13.527 13.372  0.50 12.47 ? 217 SER A CB  1 
ATOM   1715 O  OG  A SER A 1 216 ? -0.010 -13.967 14.574  0.50 12.22 ? 217 SER A OG  1 
ATOM   1716 O  OG  B SER A 1 216 ? -1.043 -13.127 13.327  0.50 14.65 ? 217 SER A OG  1 
ATOM   1717 N  N   . VAL A 1 217 ? 2.420  -12.331 11.222  1.00 11.16 ? 218 VAL A N   1 
ATOM   1718 C  CA  . VAL A 1 217 ? 2.723  -12.104 9.802   1.00 11.40 ? 218 VAL A CA  1 
ATOM   1719 C  C   . VAL A 1 217 ? 2.985  -13.474 9.187   1.00 10.89 ? 218 VAL A C   1 
ATOM   1720 O  O   . VAL A 1 217 ? 3.383  -14.427 9.888   1.00 11.89 ? 218 VAL A O   1 
ATOM   1721 C  CB  . VAL A 1 217 ? 3.938  -11.179 9.548   1.00 10.77 ? 218 VAL A CB  1 
ATOM   1722 C  CG1 . VAL A 1 217 ? 3.697  -9.848  10.203  1.00 10.56 ? 218 VAL A CG1 1 
ATOM   1723 C  CG2 . VAL A 1 217 ? 5.248  -11.827 9.991   1.00 13.37 ? 218 VAL A CG2 1 
ATOM   1724 N  N   . SER A 1 218 ? 2.797  -13.638 7.879   1.00 11.57 ? 219 SER A N   1 
ATOM   1725 C  CA  . SER A 1 218 ? 2.967  -14.996 7.284   1.00 11.25 ? 219 SER A CA  1 
ATOM   1726 C  C   . SER A 1 218 ? 4.440  -15.237 6.986   1.00 12.27 ? 219 SER A C   1 
ATOM   1727 O  O   . SER A 1 218 ? 5.276  -14.297 6.941   1.00 11.05 ? 219 SER A O   1 
ATOM   1728 C  CB  . SER A 1 218 ? 2.131  -15.150 6.002   1.00 11.49 ? 219 SER A CB  1 
ATOM   1729 O  OG  . SER A 1 218 ? 2.623  -14.211 5.038   1.00 11.30 ? 219 SER A OG  1 
ATOM   1730 N  N   . SER A 1 219 ? 4.763  -16.514 6.849   1.00 12.37 ? 220 SER A N   1 
ATOM   1731 C  CA  . SER A 1 219 ? 6.101  -16.909 6.482   1.00 12.68 ? 220 SER A CA  1 
ATOM   1732 C  C   . SER A 1 219 ? 6.462  -16.233 5.139   1.00 13.74 ? 220 SER A C   1 
ATOM   1733 O  O   . SER A 1 219 ? 7.612  -15.731 4.999   1.00 12.91 ? 220 SER A O   1 
ATOM   1734 C  CB  . SER A 1 219 ? 6.246  -18.442 6.486   1.00 17.07 ? 220 SER A CB  1 
ATOM   1735 O  OG  . SER A 1 219 ? 5.388  -18.891 5.510   1.00 23.93 ? 220 SER A OG  1 
ATOM   1736 N  N   . GLU A 1 220 ? 5.516  -16.146 4.175   1.00 13.07 ? 221 GLU A N   1 
ATOM   1737 C  CA  . GLU A 1 220 ? 5.800  -15.479 2.893   1.00 14.46 ? 221 GLU A CA  1 
ATOM   1738 C  C   . GLU A 1 220 ? 6.118  -13.969 3.093   1.00 14.38 ? 221 GLU A C   1 
ATOM   1739 O  O   . GLU A 1 220 ? 7.002  -13.442 2.414   1.00 14.24 ? 221 GLU A O   1 
ATOM   1740 C  CB  . GLU A 1 220 ? 4.638  -15.609 1.921   1.00 17.58 ? 221 GLU A CB  1 
ATOM   1741 C  CG  . GLU A 1 220 ? 4.415  -17.062 1.489   1.00 21.23 ? 221 GLU A CG  1 
ATOM   1742 C  CD  . GLU A 1 220 ? 3.505  -17.827 2.425   1.00 26.74 ? 221 GLU A CD  1 
ATOM   1743 O  OE1 . GLU A 1 220 ? 3.054  -17.296 3.468   1.00 23.20 ? 221 GLU A OE1 1 
ATOM   1744 O  OE2 . GLU A 1 220 ? 3.186  -18.997 2.105   1.00 30.54 ? 221 GLU A OE2 1 
ATOM   1745 N  N   . GLN A 1 221 ? 5.403  -13.287 3.997   1.00 11.82 ? 222 GLN A N   1 
ATOM   1746 C  CA  . GLN A 1 221 ? 5.655  -11.871 4.276   1.00 11.58 ? 222 GLN A CA  1 
ATOM   1747 C  C   . GLN A 1 221 ? 7.093  -11.652 4.802   1.00 11.90 ? 222 GLN A C   1 
ATOM   1748 O  O   . GLN A 1 221 ? 7.884  -10.906 4.223   1.00 11.15 ? 222 GLN A O   1 
ATOM   1749 C  CB  . GLN A 1 221 ? 4.589  -11.359 5.264   1.00 12.35 ? 222 GLN A CB  1 
ATOM   1750 C  CG  . GLN A 1 221 ? 3.253  -11.139 4.515   1.00 12.68 ? 222 GLN A CG  1 
ATOM   1751 C  CD  . GLN A 1 221 ? 2.139  -10.617 5.388   1.00 13.07 ? 222 GLN A CD  1 
ATOM   1752 O  OE1 . GLN A 1 221 ? 2.071  -10.954 6.546   1.00 13.43 ? 222 GLN A OE1 1 
ATOM   1753 N  NE2 . GLN A 1 221 ? 1.315  -9.711  4.845   1.00 11.56 ? 222 GLN A NE2 1 
ATOM   1754 N  N   . VAL A 1 222 ? 7.468  -12.361 5.864   1.00 12.35 ? 223 VAL A N   1 
ATOM   1755 C  CA  . VAL A 1 222 ? 8.852  -12.223 6.417   1.00 12.86 ? 223 VAL A CA  1 
ATOM   1756 C  C   . VAL A 1 222 ? 9.981  -12.694 5.391   1.00 14.76 ? 223 VAL A C   1 
ATOM   1757 O  O   . VAL A 1 222 ? 11.066 -12.132 5.358   1.00 14.72 ? 223 VAL A O   1 
ATOM   1758 C  CB  . VAL A 1 222 ? 8.968  -12.896 7.834   1.00 15.48 ? 223 VAL A CB  1 
ATOM   1759 C  CG1 . VAL A 1 222 ? 9.062  -14.380 7.700   1.00 16.96 ? 223 VAL A CG1 1 
ATOM   1760 C  CG2 . VAL A 1 222 ? 10.251 -12.416 8.556   1.00 17.46 ? 223 VAL A CG2 1 
ATOM   1761 N  N   . LEU A 1 223 ? 9.678  -13.683 4.535   1.00 13.55 ? 224 LEU A N   1 
ATOM   1762 C  CA  . LEU A 1 223 ? 10.645 -14.133 3.539   1.00 15.99 ? 224 LEU A CA  1 
ATOM   1763 C  C   . LEU A 1 223 ? 10.958 -13.027 2.603   1.00 14.59 ? 224 LEU A C   1 
ATOM   1764 O  O   . LEU A 1 223 ? 12.137 -12.874 2.246   1.00 15.36 ? 224 LEU A O   1 
ATOM   1765 C  CB  . LEU A 1 223 ? 10.138 -15.356 2.765   1.00 18.22 ? 224 LEU A CB  1 
ATOM   1766 C  CG  . LEU A 1 223 ? 10.372 -16.616 3.612   1.00 19.64 ? 224 LEU A CG  1 
ATOM   1767 C  CD1 . LEU A 1 223 ? 9.437  -17.753 3.159   1.00 24.26 ? 224 LEU A CD1 1 
ATOM   1768 C  CD2 . LEU A 1 223 ? 11.865 -16.981 3.531   1.00 21.83 ? 224 LEU A CD2 1 
ATOM   1769 N  N   . LYS A 1 224 ? 9.956  -12.212 2.265   1.00 14.34 ? 225 LYS A N   1 
ATOM   1770 C  CA  . LYS A 1 224 ? 10.186 -11.041 1.424   1.00 14.59 ? 225 LYS A CA  1 
ATOM   1771 C  C   . LYS A 1 224 ? 11.039 -9.971  2.091   1.00 13.82 ? 225 LYS A C   1 
ATOM   1772 O  O   . LYS A 1 224 ? 11.817 -9.351  1.392   1.00 14.48 ? 225 LYS A O   1 
ATOM   1773 C  CB  . LYS A 1 224 ? 8.874  -10.510 0.862   1.00 16.48 ? 225 LYS A CB  1 
ATOM   1774 C  CG  . LYS A 1 224 ? 8.394  -11.521 -0.218  1.00 19.84 ? 225 LYS A CG  1 
ATOM   1775 C  CD  . LYS A 1 224 ? 6.960  -11.316 -0.684  1.00 25.08 ? 225 LYS A CD  1 
ATOM   1776 C  CE  . LYS A 1 224 ? 6.486  -12.416 -1.652  1.00 29.77 ? 225 LYS A CE  1 
ATOM   1777 N  NZ  . LYS A 1 224 ? 5.286  -11.982 -2.469  1.00 30.43 ? 225 LYS A NZ  1 
ATOM   1778 N  N   . PHE A 1 225 ? 10.950 -9.786  3.437   1.00 11.99 ? 226 PHE A N   1 
ATOM   1779 C  CA  . PHE A 1 225 ? 11.857 -8.891  4.132   1.00 10.97 ? 226 PHE A CA  1 
ATOM   1780 C  C   . PHE A 1 225 ? 13.301 -9.396  3.899   1.00 10.65 ? 226 PHE A C   1 
ATOM   1781 O  O   . PHE A 1 225 ? 14.210 -8.604  3.701   1.00 9.58  ? 226 PHE A O   1 
ATOM   1782 C  CB  . PHE A 1 225 ? 11.647 -8.960  5.653   1.00 11.62 ? 226 PHE A CB  1 
ATOM   1783 C  CG  . PHE A 1 225 ? 10.511 -8.120  6.187   1.00 12.46 ? 226 PHE A CG  1 
ATOM   1784 C  CD1 . PHE A 1 225 ? 9.488  -7.618  5.383   1.00 14.53 ? 226 PHE A CD1 1 
ATOM   1785 C  CD2 . PHE A 1 225 ? 10.474 -7.854  7.542   1.00 14.78 ? 226 PHE A CD2 1 
ATOM   1786 C  CE1 . PHE A 1 225 ? 8.464  -6.860  5.943   1.00 14.24 ? 226 PHE A CE1 1 
ATOM   1787 C  CE2 . PHE A 1 225 ? 9.463  -7.105  8.100   1.00 15.04 ? 226 PHE A CE2 1 
ATOM   1788 C  CZ  . PHE A 1 225 ? 8.456  -6.606  7.303   1.00 15.09 ? 226 PHE A CZ  1 
ATOM   1789 N  N   . ARG A 1 226 ? 13.514 -10.701 3.980   1.00 9.58  ? 227 ARG A N   1 
ATOM   1790 C  CA  . ARG A 1 226 ? 14.886 -11.246 3.886   1.00 11.40 ? 227 ARG A CA  1 
ATOM   1791 C  C   . ARG A 1 226 ? 15.456 -11.271 2.467   1.00 11.74 ? 227 ARG A C   1 
ATOM   1792 O  O   . ARG A 1 226 ? 16.627 -11.686 2.292   1.00 13.56 ? 227 ARG A O   1 
ATOM   1793 C  CB  . ARG A 1 226 ? 14.901 -12.673 4.430   1.00 10.52 ? 227 ARG A CB  1 
ATOM   1794 C  CG  . ARG A 1 226 ? 14.291 -12.875 5.821   1.00 11.16 ? 227 ARG A CG  1 
ATOM   1795 C  CD  . ARG A 1 226 ? 14.401 -14.339 6.283   1.00 11.27 ? 227 ARG A CD  1 
ATOM   1796 N  NE  . ARG A 1 226 ? 13.871 -14.428 7.665   1.00 11.73 ? 227 ARG A NE  1 
ATOM   1797 C  CZ  . ARG A 1 226 ? 12.936 -15.315 8.070   1.00 12.14 ? 227 ARG A CZ  1 
ATOM   1798 N  NH1 . ARG A 1 226 ? 12.492 -16.253 7.206   1.00 13.75 ? 227 ARG A NH1 1 
ATOM   1799 N  NH2 . ARG A 1 226 ? 12.479 -15.291 9.313   1.00 11.80 ? 227 ARG A NH2 1 
ATOM   1800 N  N   . LYS A 1 227 ? 14.683 -10.832 1.476   1.00 12.67 ? 228 LYS A N   1 
ATOM   1801 C  CA  . LYS A 1 227 ? 15.251 -10.665 0.116   1.00 13.80 ? 228 LYS A CA  1 
ATOM   1802 C  C   . LYS A 1 227 ? 15.849 -9.303  -0.119  1.00 13.25 ? 228 LYS A C   1 
ATOM   1803 O  O   . LYS A 1 227 ? 16.537 -9.088  -1.147  1.00 13.21 ? 228 LYS A O   1 
ATOM   1804 C  CB  . LYS A 1 227 ? 14.155 -10.887 -0.929  1.00 15.40 ? 228 LYS A CB  1 
ATOM   1805 C  CG  . LYS A 1 227 ? 13.842 -12.365 -1.007  1.00 17.93 ? 228 LYS A CG  1 
ATOM   1806 C  CD  . LYS A 1 227 ? 12.727 -12.663 -2.008  1.00 25.23 ? 228 LYS A CD  1 
ATOM   1807 C  CE  . LYS A 1 227 ? 13.379 -12.866 -3.382  1.00 30.22 ? 228 LYS A CE  1 
ATOM   1808 N  NZ  . LYS A 1 227 ? 12.446 -13.134 -4.528  1.00 35.48 ? 228 LYS A NZ  1 
ATOM   1809 N  N   . LEU A 1 228 ? 15.646 -8.372  0.835   1.00 10.77 ? 229 LEU A N   1 
ATOM   1810 C  CA  . LEU A 1 228 ? 16.293 -7.055  0.698   1.00 10.67 ? 229 LEU A CA  1 
ATOM   1811 C  C   . LEU A 1 228 ? 17.804 -7.212  0.804   1.00 10.97 ? 229 LEU A C   1 
ATOM   1812 O  O   . LEU A 1 228 ? 18.314 -8.241  1.267   1.00 11.43 ? 229 LEU A O   1 
ATOM   1813 C  CB  . LEU A 1 228 ? 15.763 -6.103  1.797   1.00 9.41  ? 229 LEU A CB  1 
ATOM   1814 C  CG  . LEU A 1 228 ? 14.330 -5.694  1.600   1.00 9.27  ? 229 LEU A CG  1 
ATOM   1815 C  CD1 . LEU A 1 228 ? 13.831 -5.157  2.921   1.00 9.52  ? 229 LEU A CD1 1 
ATOM   1816 C  CD2 . LEU A 1 228 ? 14.326 -4.632  0.482   1.00 10.99 ? 229 LEU A CD2 1 
ATOM   1817 N  N   . ASN A 1 229 ? 18.504 -6.155  0.421   1.00 12.46 ? 230 ASN A N   1 
ATOM   1818 C  CA  . ASN A 1 229 ? 19.950 -6.172  0.444   1.00 12.77 ? 230 ASN A CA  1 
ATOM   1819 C  C   . ASN A 1 229 ? 20.506 -5.010  1.314   1.00 12.35 ? 230 ASN A C   1 
ATOM   1820 O  O   . ASN A 1 229 ? 20.032 -3.889  1.241   1.00 11.97 ? 230 ASN A O   1 
ATOM   1821 C  CB  . ASN A 1 229 ? 20.504 -5.939  -0.975  1.00 14.26 ? 230 ASN A CB  1 
ATOM   1822 C  CG  . ASN A 1 229 ? 20.458 -7.153  -1.903  1.00 16.24 ? 230 ASN A CG  1 
ATOM   1823 O  OD1 . ASN A 1 229 ? 20.940 -6.984  -3.061  1.00 17.16 ? 230 ASN A OD1 1 
ATOM   1824 N  ND2 . ASN A 1 229 ? 19.850 -8.301  -1.518  1.00 14.22 ? 230 ASN A ND2 1 
ATOM   1825 N  N   . PHE A 1 230 ? 21.575 -5.285  2.055   1.00 12.05 ? 231 PHE A N   1 
ATOM   1826 C  CA  . PHE A 1 230 ? 22.330 -4.246  2.767   1.00 12.48 ? 231 PHE A CA  1 
ATOM   1827 C  C   . PHE A 1 230 ? 23.193 -3.448  1.796   1.00 13.87 ? 231 PHE A C   1 
ATOM   1828 O  O   . PHE A 1 230 ? 23.456 -2.265  2.038   1.00 14.57 ? 231 PHE A O   1 
ATOM   1829 C  CB  . PHE A 1 230 ? 23.335 -4.892  3.716   1.00 13.39 ? 231 PHE A CB  1 
ATOM   1830 C  CG  . PHE A 1 230 ? 22.755 -5.466  5.029   1.00 13.27 ? 231 PHE A CG  1 
ATOM   1831 C  CD1 . PHE A 1 230 ? 21.992 -4.666  5.906   1.00 13.01 ? 231 PHE A CD1 1 
ATOM   1832 C  CD2 . PHE A 1 230 ? 23.077 -6.777  5.441   1.00 12.92 ? 231 PHE A CD2 1 
ATOM   1833 C  CE1 . PHE A 1 230 ? 21.488 -5.130  7.155   1.00 12.23 ? 231 PHE A CE1 1 
ATOM   1834 C  CE2 . PHE A 1 230 ? 22.626 -7.254  6.697   1.00 12.40 ? 231 PHE A CE2 1 
ATOM   1835 C  CZ  . PHE A 1 230 ? 21.837 -6.445  7.537   1.00 12.15 ? 231 PHE A CZ  1 
ATOM   1836 N  N   . ASN A 1 231 ? 23.615 -4.122  0.731   1.00 14.64 ? 232 ASN A N   1 
ATOM   1837 C  CA  . ASN A 1 231 ? 24.547 -3.508  -0.251  1.00 15.16 ? 232 ASN A CA  1 
ATOM   1838 C  C   . ASN A 1 231 ? 23.815 -2.631  -1.251  1.00 15.99 ? 232 ASN A C   1 
ATOM   1839 O  O   . ASN A 1 231 ? 22.591 -2.729  -1.408  1.00 15.76 ? 232 ASN A O   1 
ATOM   1840 C  CB  . ASN A 1 231 ? 25.240 -4.644  -1.029  1.00 15.62 ? 232 ASN A CB  1 
ATOM   1841 C  CG  . ASN A 1 231 ? 24.244 -5.553  -1.665  1.00 16.32 ? 232 ASN A CG  1 
ATOM   1842 O  OD1 . ASN A 1 231 ? 23.658 -6.387  -0.995  1.00 16.69 ? 232 ASN A OD1 1 
ATOM   1843 N  ND2 . ASN A 1 231 ? 23.986 -5.369  -2.962  1.00 17.95 ? 232 ASN A ND2 1 
ATOM   1844 N  N   . GLY A 1 232 ? 24.570 -1.750  -1.942  1.00 15.14 ? 233 GLY A N   1 
ATOM   1845 C  CA  . GLY A 1 232 ? 23.980 -0.925  -3.038  1.00 16.03 ? 233 GLY A CA  1 
ATOM   1846 C  C   . GLY A 1 232 ? 23.904 -1.681  -4.331  1.00 17.63 ? 233 GLY A C   1 
ATOM   1847 O  O   . GLY A 1 232 ? 24.549 -2.697  -4.499  1.00 19.81 ? 233 GLY A O   1 
ATOM   1848 N  N   . GLU A 1 233 ? 23.173 -1.112  -5.281  1.00 17.80 ? 234 GLU A N   1 
ATOM   1849 C  CA  . GLU A 1 233 ? 23.091 -1.654  -6.612  1.00 18.79 ? 234 GLU A CA  1 
ATOM   1850 C  C   . GLU A 1 233 ? 24.477 -1.862  -7.240  1.00 20.43 ? 234 GLU A C   1 
ATOM   1851 O  O   . GLU A 1 233 ? 25.325 -1.011  -7.183  1.00 21.82 ? 234 GLU A O   1 
ATOM   1852 C  CB  . GLU A 1 233 ? 22.214 -0.792  -7.490  1.00 18.86 ? 234 GLU A CB  1 
ATOM   1853 C  CG  . GLU A 1 233 ? 21.923 -1.346  -8.892  1.00 18.61 ? 234 GLU A CG  1 
ATOM   1854 C  CD  . GLU A 1 233 ? 21.069 -0.400  -9.697  1.00 25.24 ? 234 GLU A CD  1 
ATOM   1855 O  OE1 . GLU A 1 233 ? 20.782 0.766   -9.239  1.00 20.73 ? 234 GLU A OE1 1 
ATOM   1856 O  OE2 . GLU A 1 233 ? 20.717 -0.794  -10.841 1.00 25.23 ? 234 GLU A OE2 1 
ATOM   1857 N  N   . GLY A 1 234 ? 24.644 -3.014  -7.851  1.00 22.29 ? 235 GLY A N   1 
ATOM   1858 C  CA  . GLY A 1 234 ? 25.892 -3.342  -8.485  1.00 29.22 ? 235 GLY A CA  1 
ATOM   1859 C  C   . GLY A 1 234 ? 27.004 -3.570  -7.485  1.00 30.60 ? 235 GLY A C   1 
ATOM   1860 O  O   . GLY A 1 234 ? 28.197 -3.355  -7.794  1.00 34.17 ? 235 GLY A O   1 
ATOM   1861 N  N   . GLU A 1 235 ? 26.628 -4.006  -6.283  1.00 26.25 ? 236 GLU A N   1 
ATOM   1862 C  CA  . GLU A 1 235 ? 27.595 -4.603  -5.342  1.00 25.36 ? 236 GLU A CA  1 
ATOM   1863 C  C   . GLU A 1 235 ? 27.243 -6.025  -5.042  1.00 25.03 ? 236 GLU A C   1 
ATOM   1864 O  O   . GLU A 1 235 ? 26.147 -6.483  -5.412  1.00 25.44 ? 236 GLU A O   1 
ATOM   1865 C  CB  . GLU A 1 235 ? 27.667 -3.831  -4.041  1.00 25.39 ? 236 GLU A CB  1 
ATOM   1866 C  CG  . GLU A 1 235 ? 28.029 -2.388  -4.280  1.00 27.07 ? 236 GLU A CG  1 
ATOM   1867 C  CD  . GLU A 1 235 ? 28.153 -1.609  -2.979  1.00 34.74 ? 236 GLU A CD  1 
ATOM   1868 O  OE1 . GLU A 1 235 ? 27.408 -1.865  -1.984  1.00 28.93 ? 236 GLU A OE1 1 
ATOM   1869 O  OE2 . GLU A 1 235 ? 29.012 -0.721  -2.938  1.00 35.08 ? 236 GLU A OE2 1 
ATOM   1870 N  N   . PRO A 1 236 ? 28.213 -6.781  -4.492  1.00 25.17 ? 237 PRO A N   1 
ATOM   1871 C  CA  . PRO A 1 236 ? 27.943 -8.177  -4.190  1.00 24.98 ? 237 PRO A CA  1 
ATOM   1872 C  C   . PRO A 1 236 ? 26.797 -8.287  -3.167  1.00 21.38 ? 237 PRO A C   1 
ATOM   1873 O  O   . PRO A 1 236 ? 26.769 -7.519  -2.229  1.00 20.02 ? 237 PRO A O   1 
ATOM   1874 C  CB  . PRO A 1 236 ? 29.252 -8.681  -3.573  1.00 27.69 ? 237 PRO A CB  1 
ATOM   1875 C  CG  . PRO A 1 236 ? 30.305 -7.662  -3.933  1.00 29.31 ? 237 PRO A CG  1 
ATOM   1876 C  CD  . PRO A 1 236 ? 29.570 -6.359  -4.069  1.00 27.72 ? 237 PRO A CD  1 
ATOM   1877 N  N   . GLU A 1 237 ? 25.910 -9.254  -3.378  1.00 20.97 ? 238 GLU A N   1 
ATOM   1878 C  CA  . GLU A 1 237 ? 24.712 -9.308  -2.586  1.00 19.27 ? 238 GLU A CA  1 
ATOM   1879 C  C   . GLU A 1 237 ? 24.984 -9.719  -1.166  1.00 19.88 ? 238 GLU A C   1 
ATOM   1880 O  O   . GLU A 1 237 ? 25.606 -10.741 -0.926  1.00 18.64 ? 238 GLU A O   1 
ATOM   1881 C  CB  . GLU A 1 237 ? 23.668 -10.192 -3.229  1.00 19.96 ? 238 GLU A CB  1 
ATOM   1882 C  CG  . GLU A 1 237 ? 22.386 -10.268 -2.397  1.00 20.40 ? 238 GLU A CG  1 
ATOM   1883 C  CD  . GLU A 1 237 ? 21.296 -10.994 -3.139  1.00 21.94 ? 238 GLU A CD  1 
ATOM   1884 O  OE1 . GLU A 1 237 ? 21.604 -12.074 -3.716  1.00 27.73 ? 238 GLU A OE1 1 
ATOM   1885 O  OE2 . GLU A 1 237 ? 20.167 -10.489 -3.227  1.00 17.92 ? 238 GLU A OE2 1 
ATOM   1886 N  N   . GLU A 1 238 ? 24.479 -8.906  -0.225  1.00 17.45 ? 239 GLU A N   1 
ATOM   1887 C  CA  . GLU A 1 238 ? 24.543 -9.254  1.194   1.00 20.69 ? 239 GLU A CA  1 
ATOM   1888 C  C   . GLU A 1 238 ? 23.086 -9.146  1.641   1.00 16.36 ? 239 GLU A C   1 
ATOM   1889 O  O   . GLU A 1 238 ? 22.548 -8.060  1.597   1.00 14.63 ? 239 GLU A O   1 
ATOM   1890 C  CB  . GLU A 1 238 ? 25.363 -8.298  2.051   1.00 23.33 ? 239 GLU A CB  1 
ATOM   1891 C  CG  . GLU A 1 238 ? 26.677 -7.760  1.521   1.00 35.08 ? 239 GLU A CG  1 
ATOM   1892 C  CD  . GLU A 1 238 ? 27.104 -6.462  2.245   1.00 41.40 ? 239 GLU A CD  1 
ATOM   1893 O  OE1 . GLU A 1 238 ? 27.310 -6.495  3.487   1.00 47.97 ? 239 GLU A OE1 1 
ATOM   1894 O  OE2 . GLU A 1 238 ? 27.210 -5.398  1.582   1.00 44.19 ? 239 GLU A OE2 1 
ATOM   1895 N  N   . LEU A 1 239 ? 22.415 -10.272 1.946   1.00 13.47 ? 240 LEU A N   1 
ATOM   1896 C  CA  . LEU A 1 239 ? 21.028 -10.175 2.250   1.00 11.35 ? 240 LEU A CA  1 
ATOM   1897 C  C   . LEU A 1 239 ? 20.860 -9.351  3.554   1.00 11.86 ? 240 LEU A C   1 
ATOM   1898 O  O   . LEU A 1 239 ? 21.633 -9.542  4.541   1.00 13.42 ? 240 LEU A O   1 
ATOM   1899 C  CB  . LEU A 1 239 ? 20.456 -11.606 2.458   1.00 13.15 ? 240 LEU A CB  1 
ATOM   1900 C  CG  . LEU A 1 239 ? 20.462 -12.527 1.225   1.00 13.12 ? 240 LEU A CG  1 
ATOM   1901 C  CD1 . LEU A 1 239 ? 19.888 -13.807 1.755   1.00 15.67 ? 240 LEU A CD1 1 
ATOM   1902 C  CD2 . LEU A 1 239 ? 19.595 -11.862 0.166   1.00 13.95 ? 240 LEU A CD2 1 
ATOM   1903 N  N   . MET A 1 240 ? 19.778 -8.557  3.588   1.00 11.08 ? 241 MET A N   1 
ATOM   1904 C  CA  . MET A 1 240 ? 19.427 -7.733  4.753   1.00 10.84 ? 241 MET A CA  1 
ATOM   1905 C  C   . MET A 1 240 ? 18.701 -8.652  5.717   1.00 10.35 ? 241 MET A C   1 
ATOM   1906 O  O   . MET A 1 240 ? 17.467 -8.833  5.616   1.00 11.74 ? 241 MET A O   1 
ATOM   1907 C  CB  . MET A 1 240 ? 18.579 -6.489  4.371   1.00 11.41 ? 241 MET A CB  1 
ATOM   1908 C  CG  . MET A 1 240 ? 18.308 -5.485  5.589   1.00 10.99 ? 241 MET A CG  1 
ATOM   1909 S  SD  . MET A 1 240 ? 17.281 -4.165  4.987   1.00 13.10 ? 241 MET A SD  1 
ATOM   1910 C  CE  . MET A 1 240 ? 18.542 -3.028  4.282   1.00 13.39 ? 241 MET A CE  1 
ATOM   1911 N  N   . VAL A 1 241 ? 19.481 -9.258  6.623   1.00 10.29 ? 242 VAL A N   1 
ATOM   1912 C  CA  . VAL A 1 241 ? 18.854 -10.146 7.667   1.00 9.87  ? 242 VAL A CA  1 
ATOM   1913 C  C   . VAL A 1 241 ? 19.640 -9.890  8.938   1.00 10.37 ? 242 VAL A C   1 
ATOM   1914 O  O   . VAL A 1 241 ? 20.850 -9.495  8.881   1.00 10.54 ? 242 VAL A O   1 
ATOM   1915 C  CB  . VAL A 1 241 ? 18.942 -11.666 7.329   1.00 9.79  ? 242 VAL A CB  1 
ATOM   1916 C  CG1 . VAL A 1 241 ? 18.080 -11.927 6.078   1.00 10.84 ? 242 VAL A CG1 1 
ATOM   1917 C  CG2 . VAL A 1 241 ? 20.422 -12.126 7.163   1.00 11.61 ? 242 VAL A CG2 1 
ATOM   1918 N  N   . ASP A 1 242 ? 19.035 -10.252 10.079  1.00 8.97  ? 243 ASP A N   1 
ATOM   1919 C  CA  . ASP A 1 242 ? 19.778 -10.095 11.300  1.00 9.71  ? 243 ASP A CA  1 
ATOM   1920 C  C   . ASP A 1 242 ? 20.241 -8.677  11.582  1.00 9.45  ? 243 ASP A C   1 
ATOM   1921 O  O   . ASP A 1 242 ? 21.358 -8.462  12.175  1.00 10.49 ? 243 ASP A O   1 
ATOM   1922 C  CB  . ASP A 1 242 ? 20.889 -11.161 11.499  1.00 9.91  ? 243 ASP A CB  1 
ATOM   1923 C  CG  . ASP A 1 242 ? 20.333 -12.574 11.625  1.00 10.17 ? 243 ASP A CG  1 
ATOM   1924 O  OD1 . ASP A 1 242 ? 19.315 -12.748 12.325  1.00 10.74 ? 243 ASP A OD1 1 
ATOM   1925 O  OD2 . ASP A 1 242 ? 20.929 -13.531 11.000  1.00 10.47 ? 243 ASP A OD2 1 
ATOM   1926 N  N   . ASN A 1 243 ? 19.305 -7.717  11.329  1.00 9.36  ? 244 ASN A N   1 
ATOM   1927 C  CA  . ASN A 1 243 ? 19.654 -6.291  11.615  1.00 9.48  ? 244 ASN A CA  1 
ATOM   1928 C  C   . ASN A 1 243 ? 19.059 -5.905  12.972  1.00 9.25  ? 244 ASN A C   1 
ATOM   1929 O  O   . ASN A 1 243 ? 18.357 -4.874  13.064  1.00 9.25  ? 244 ASN A O   1 
ATOM   1930 C  CB  . ASN A 1 243 ? 19.088 -5.401  10.506  1.00 9.53  ? 244 ASN A CB  1 
ATOM   1931 C  CG  . ASN A 1 243 ? 17.627 -5.645  10.227  1.00 9.39  ? 244 ASN A CG  1 
ATOM   1932 O  OD1 . ASN A 1 243 ? 16.959 -6.539  10.821  1.00 9.77  ? 244 ASN A OD1 1 
ATOM   1933 N  ND2 . ASN A 1 243 ? 17.080 -4.789  9.343   1.00 12.36 ? 244 ASN A ND2 1 
ATOM   1934 N  N   . TRP A 1 244 ? 19.358 -6.710  13.997  1.00 8.35  ? 245 TRP A N   1 
ATOM   1935 C  CA  . TRP A 1 244 ? 18.871 -6.429  15.353  1.00 7.83  ? 245 TRP A CA  1 
ATOM   1936 C  C   . TRP A 1 244 ? 20.091 -6.344  16.249  1.00 8.55  ? 245 TRP A C   1 
ATOM   1937 O  O   . TRP A 1 244 ? 21.092 -7.056  16.113  1.00 9.21  ? 245 TRP A O   1 
ATOM   1938 C  CB  . TRP A 1 244 ? 17.841 -7.505  15.814  1.00 7.93  ? 245 TRP A CB  1 
ATOM   1939 C  CG  . TRP A 1 244 ? 18.379 -8.915  15.611  1.00 7.86  ? 245 TRP A CG  1 
ATOM   1940 C  CD1 . TRP A 1 244 ? 18.289 -9.669  14.464  1.00 8.12  ? 245 TRP A CD1 1 
ATOM   1941 C  CD2 . TRP A 1 244 ? 18.966 -9.773  16.626  1.00 8.24  ? 245 TRP A CD2 1 
ATOM   1942 N  NE1 . TRP A 1 244 ? 18.817 -10.913 14.664  1.00 8.80  ? 245 TRP A NE1 1 
ATOM   1943 C  CE2 . TRP A 1 244 ? 19.220 -11.035 15.981  1.00 8.59  ? 245 TRP A CE2 1 
ATOM   1944 C  CE3 . TRP A 1 244 ? 19.259 -9.606  18.006  1.00 8.48  ? 245 TRP A CE3 1 
ATOM   1945 C  CZ2 . TRP A 1 244 ? 19.838 -12.093 16.648  1.00 8.86  ? 245 TRP A CZ2 1 
ATOM   1946 C  CZ3 . TRP A 1 244 ? 19.834 -10.716 18.690  1.00 8.93  ? 245 TRP A CZ3 1 
ATOM   1947 C  CH2 . TRP A 1 244 ? 20.142 -11.891 18.001  1.00 9.02  ? 245 TRP A CH2 1 
ATOM   1948 N  N   . ARG A 1 245 ? 19.966 -5.465  17.258  1.00 7.85  ? 246 ARG A N   1 
ATOM   1949 C  CA  . ARG A 1 245 ? 20.957 -5.338  18.355  1.00 8.32  ? 246 ARG A CA  1 
ATOM   1950 C  C   . ARG A 1 245 ? 20.438 -6.215  19.482  1.00 8.81  ? 246 ARG A C   1 
ATOM   1951 O  O   . ARG A 1 245 ? 19.254 -6.228  19.767  1.00 9.92  ? 246 ARG A O   1 
ATOM   1952 C  CB  . ARG A 1 245 ? 21.001 -3.871  18.817  1.00 8.32  ? 246 ARG A CB  1 
ATOM   1953 C  CG  . ARG A 1 245 ? 22.136 -3.708  19.837  1.00 7.89  ? 246 ARG A CG  1 
ATOM   1954 C  CD  . ARG A 1 245 ? 22.045 -2.311  20.476  1.00 8.68  ? 246 ARG A CD  1 
ATOM   1955 N  NE  . ARG A 1 245 ? 23.317 -2.030  21.245  1.00 8.66  ? 246 ARG A NE  1 
ATOM   1956 C  CZ  . ARG A 1 245 ? 23.513 -0.990  22.068  1.00 10.04 ? 246 ARG A CZ  1 
ATOM   1957 N  NH1 . ARG A 1 245 ? 22.498 -0.176  22.451  1.00 8.75  ? 246 ARG A NH1 1 
ATOM   1958 N  NH2 . ARG A 1 245 ? 24.733 -0.796  22.583  1.00 9.48  ? 246 ARG A NH2 1 
ATOM   1959 N  N   . PRO A 1 246 ? 21.293 -6.997  20.113  1.00 9.06  ? 247 PRO A N   1 
ATOM   1960 C  CA  . PRO A 1 246 ? 20.896 -7.876  21.232  1.00 9.20  ? 247 PRO A CA  1 
ATOM   1961 C  C   . PRO A 1 246 ? 20.632 -7.055  22.472  1.00 8.23  ? 247 PRO A C   1 
ATOM   1962 O  O   . PRO A 1 246 ? 21.029 -5.922  22.577  1.00 8.74  ? 247 PRO A O   1 
ATOM   1963 C  CB  . PRO A 1 246 ? 22.102 -8.762  21.484  1.00 9.20  ? 247 PRO A CB  1 
ATOM   1964 C  CG  . PRO A 1 246 ? 23.170 -8.245  20.587  1.00 11.14 ? 247 PRO A CG  1 
ATOM   1965 C  CD  . PRO A 1 246 ? 22.731 -7.047  19.812  1.00 9.89  ? 247 PRO A CD  1 
ATOM   1966 N  N   . ALA A 1 247 ? 19.901 -7.701  23.373  1.00 8.16  ? 248 ALA A N   1 
ATOM   1967 C  CA  . ALA A 1 247 ? 19.611 -7.114  24.668  1.00 8.05  ? 248 ALA A CA  1 
ATOM   1968 C  C   . ALA A 1 247 ? 20.867 -6.580  25.389  1.00 9.26  ? 248 ALA A C   1 
ATOM   1969 O  O   . ALA A 1 247 ? 21.924 -7.264  25.486  1.00 10.17 ? 248 ALA A O   1 
ATOM   1970 C  CB  . ALA A 1 247 ? 18.835 -8.168  25.517  1.00 8.97  ? 248 ALA A CB  1 
ATOM   1971 N  N   . GLN A 1 248 ? 20.696 -5.409  26.008  1.00 8.36  ? 249 GLN A N   1 
ATOM   1972 C  CA  . GLN A 1 248 ? 21.748 -4.680  26.722  1.00 10.16 ? 249 GLN A CA  1 
ATOM   1973 C  C   . GLN A 1 248 ? 21.424 -4.669  28.221  1.00 10.39 ? 249 GLN A C   1 
ATOM   1974 O  O   . GLN A 1 248 ? 20.288 -4.832  28.643  1.00 9.90  ? 249 GLN A O   1 
ATOM   1975 C  CB  . GLN A 1 248 ? 21.808 -3.283  26.200  1.00 10.61 ? 249 GLN A CB  1 
ATOM   1976 C  CG  . GLN A 1 248 ? 22.125 -3.161  24.685  1.00 10.88 ? 249 GLN A CG  1 
ATOM   1977 C  CD  . GLN A 1 248 ? 23.453 -3.825  24.359  1.00 11.61 ? 249 GLN A CD  1 
ATOM   1978 O  OE1 . GLN A 1 248 ? 24.511 -3.427  24.926  1.00 13.59 ? 249 GLN A OE1 1 
ATOM   1979 N  NE2 . GLN A 1 248 ? 23.431 -4.811  23.480  1.00 12.31 ? 249 GLN A NE2 1 
ATOM   1980 N  N   . PRO A 1 249 ? 22.408 -4.390  29.072  1.00 11.38 ? 250 PRO A N   1 
ATOM   1981 C  CA  . PRO A 1 249 ? 22.133 -4.497  30.509  1.00 12.10 ? 250 PRO A CA  1 
ATOM   1982 C  C   . PRO A 1 249 ? 21.158 -3.442  31.005  1.00 11.68 ? 250 PRO A C   1 
ATOM   1983 O  O   . PRO A 1 249 ? 21.249 -2.268  30.602  1.00 11.91 ? 250 PRO A O   1 
ATOM   1984 C  CB  . PRO A 1 249 ? 23.505 -4.191  31.142  1.00 12.79 ? 250 PRO A CB  1 
ATOM   1985 C  CG  . PRO A 1 249 ? 24.488 -4.405  30.091  1.00 14.99 ? 250 PRO A CG  1 
ATOM   1986 C  CD  . PRO A 1 249 ? 23.820 -4.119  28.766  1.00 12.82 ? 250 PRO A CD  1 
ATOM   1987 N  N   . LEU A 1 250 ? 20.228 -3.891  31.878  1.00 12.67 ? 251 LEU A N   1 
ATOM   1988 C  CA  . LEU A 1 250 ? 19.152 -3.031  32.339  1.00 12.10 ? 251 LEU A CA  1 
ATOM   1989 C  C   . LEU A 1 250 ? 19.722 -1.948  33.278  1.00 12.78 ? 251 LEU A C   1 
ATOM   1990 O  O   . LEU A 1 250 ? 19.226 -0.825  33.309  1.00 11.28 ? 251 LEU A O   1 
ATOM   1991 C  CB  . LEU A 1 250 ? 18.069 -3.868  33.001  1.00 11.90 ? 251 LEU A CB  1 
ATOM   1992 C  CG  . LEU A 1 250 ? 16.807 -3.180  33.511  1.00 12.98 ? 251 LEU A CG  1 
ATOM   1993 C  CD1 . LEU A 1 250 ? 16.113 -2.515  32.323  1.00 14.25 ? 251 LEU A CD1 1 
ATOM   1994 C  CD2 . LEU A 1 250 ? 15.864 -4.114  34.284  1.00 15.33 ? 251 LEU A CD2 1 
ATOM   1995 N  N   . LYS A 1 251 ? 20.780 -2.291  34.036  1.00 13.42 ? 252 LYS A N   1 
ATOM   1996 C  CA  . LYS A 1 251 ? 21.374 -1.253  34.955  1.00 15.23 ? 252 LYS A CA  1 
ATOM   1997 C  C   . LYS A 1 251 ? 20.324 -0.716  35.917  1.00 15.47 ? 252 LYS A C   1 
ATOM   1998 O  O   . LYS A 1 251 ? 19.541 -1.524  36.459  1.00 17.63 ? 252 LYS A O   1 
ATOM   1999 C  CB  . LYS A 1 251 ? 22.135 -0.182  34.153  1.00 16.32 ? 252 LYS A CB  1 
ATOM   2000 C  CG  . LYS A 1 251 ? 23.239 -0.906  33.360  1.00 18.99 ? 252 LYS A CG  1 
ATOM   2001 C  CD  . LYS A 1 251 ? 24.291 0.102   32.954  1.00 19.56 ? 252 LYS A CD  1 
ATOM   2002 C  CE  . LYS A 1 251 ? 25.610 -0.565  32.612  1.00 25.19 ? 252 LYS A CE  1 
ATOM   2003 N  NZ  . LYS A 1 251 ? 26.242 0.121   31.452  1.00 24.45 ? 252 LYS A NZ  1 
ATOM   2004 N  N   . ASN A 1 252 ? 20.317 0.565   36.135  1.00 15.56 ? 253 ASN A N   1 
ATOM   2005 C  CA  . ASN A 1 252 ? 19.535 1.121   37.220  1.00 22.73 ? 253 ASN A CA  1 
ATOM   2006 C  C   . ASN A 1 252 ? 18.207 1.559   36.668  1.00 21.04 ? 253 ASN A C   1 
ATOM   2007 O  O   . ASN A 1 252 ? 17.949 2.800   36.702  1.00 22.85 ? 253 ASN A O   1 
ATOM   2008 C  CB  . ASN A 1 252 ? 20.239 2.346   37.857  1.00 27.12 ? 253 ASN A CB  1 
ATOM   2009 C  CG  . ASN A 1 252 ? 19.477 2.872   39.066  1.00 30.11 ? 253 ASN A CG  1 
ATOM   2010 O  OD1 . ASN A 1 252 ? 18.829 2.095   39.774  1.00 34.90 ? 253 ASN A OD1 1 
ATOM   2011 N  ND2 . ASN A 1 252 ? 19.501 4.182   39.275  1.00 31.85 ? 253 ASN A ND2 1 
ATOM   2012 N  N   . ARG A 1 253 ? 17.441 0.591   36.082  1.00 16.12 ? 254 ARG A N   1 
ATOM   2013 C  CA  . ARG A 1 253 ? 16.157 0.940   35.451  1.00 13.86 ? 254 ARG A CA  1 
ATOM   2014 C  C   . ARG A 1 253 ? 15.045 0.034   35.843  1.00 15.16 ? 254 ARG A C   1 
ATOM   2015 O  O   . ARG A 1 253 ? 15.275 -1.151  36.079  1.00 15.67 ? 254 ARG A O   1 
ATOM   2016 C  CB  . ARG A 1 253 ? 16.252 0.943   33.884  1.00 11.49 ? 254 ARG A CB  1 
ATOM   2017 C  CG  . ARG A 1 253 ? 17.124 2.105   33.366  1.00 11.77 ? 254 ARG A CG  1 
ATOM   2018 C  CD  . ARG A 1 253 ? 17.197 2.027   31.854  1.00 10.50 ? 254 ARG A CD  1 
ATOM   2019 N  NE  . ARG A 1 253 ? 18.114 0.902   31.441  1.00 9.28  ? 254 ARG A NE  1 
ATOM   2020 C  CZ  . ARG A 1 253 ? 18.351 0.617   30.162  1.00 9.07  ? 254 ARG A CZ  1 
ATOM   2021 N  NH1 . ARG A 1 253 ? 17.729 1.353   29.201  1.00 9.17  ? 254 ARG A NH1 1 
ATOM   2022 N  NH2 . ARG A 1 253 ? 19.188 -0.338  29.833  1.00 8.64  ? 254 ARG A NH2 1 
ATOM   2023 N  N   . GLN A 1 254 ? 13.819 0.598   35.861  1.00 13.88 ? 255 GLN A N   1 
ATOM   2024 C  CA  . GLN A 1 254 ? 12.662 -0.169  36.188  1.00 17.20 ? 255 GLN A CA  1 
ATOM   2025 C  C   . GLN A 1 254 ? 11.783 -0.279  34.937  1.00 13.60 ? 255 GLN A C   1 
ATOM   2026 O  O   . GLN A 1 254 ? 11.499 0.737   34.320  1.00 15.63 ? 255 GLN A O   1 
ATOM   2027 C  CB  . GLN A 1 254 ? 11.903 0.611   37.258  1.00 23.95 ? 255 GLN A CB  1 
ATOM   2028 C  CG  . GLN A 1 254 ? 12.212 0.077   38.634  1.00 33.05 ? 255 GLN A CG  1 
ATOM   2029 C  CD  . GLN A 1 254 ? 11.326 -1.130  38.976  1.00 43.71 ? 255 GLN A CD  1 
ATOM   2030 O  OE1 . GLN A 1 254 ? 10.639 -1.717  38.101  1.00 50.54 ? 255 GLN A OE1 1 
ATOM   2031 N  NE2 . GLN A 1 254 ? 11.326 -1.510  40.268  1.00 49.48 ? 255 GLN A NE2 1 
ATOM   2032 N  N   . ILE A 1 255 ? 11.384 -1.493  34.561  1.00 11.37 ? 256 ILE A N   1 
ATOM   2033 C  CA  . ILE A 1 255 ? 10.404 -1.581  33.478  1.00 10.80 ? 256 ILE A CA  1 
ATOM   2034 C  C   . ILE A 1 255 ? 9.003  -1.660  34.158  1.00 10.28 ? 256 ILE A C   1 
ATOM   2035 O  O   . ILE A 1 255 ? 8.816  -2.416  35.148  1.00 11.17 ? 256 ILE A O   1 
ATOM   2036 C  CB  . ILE A 1 255 ? 10.635 -2.837  32.658  1.00 11.00 ? 256 ILE A CB  1 
ATOM   2037 C  CG1 . ILE A 1 255 ? 12.038 -2.821  31.988  1.00 11.57 ? 256 ILE A CG1 1 
ATOM   2038 C  CG2 . ILE A 1 255 ? 9.485  -3.030  31.640  1.00 11.05 ? 256 ILE A CG2 1 
ATOM   2039 C  CD1 . ILE A 1 255 ? 12.346 -4.113  31.198  1.00 13.74 ? 256 ILE A CD1 1 
ATOM   2040 N  N   . LYS A 1 256 ? 8.099  -0.769  33.702  1.00 10.64 ? 257 LYS A N   1 
ATOM   2041 C  CA  . LYS A 1 256 ? 6.711  -0.705  34.282  1.00 10.90 ? 257 LYS A CA  1 
ATOM   2042 C  C   . LYS A 1 256 ? 5.721  -1.314  33.326  1.00 12.01 ? 257 LYS A C   1 
ATOM   2043 O  O   . LYS A 1 256 ? 5.901  -1.216  32.118  1.00 11.56 ? 257 LYS A O   1 
ATOM   2044 C  CB  . LYS A 1 256 ? 6.344  0.747   34.547  1.00 12.97 ? 257 LYS A CB  1 
ATOM   2045 C  CG  . LYS A 1 256 ? 7.214  1.310   35.651  1.00 16.42 ? 257 LYS A CG  1 
ATOM   2046 C  CD  . LYS A 1 256 ? 7.045  2.806   35.752  1.00 24.27 ? 257 LYS A CD  1 
ATOM   2047 C  CE  . LYS A 1 256 ? 7.990  3.313   36.841  1.00 29.54 ? 257 LYS A CE  1 
ATOM   2048 N  NZ  . LYS A 1 256 ? 8.230  4.781   36.676  1.00 33.90 ? 257 LYS A NZ  1 
ATOM   2049 N  N   . ALA A 1 257 ? 4.702  -1.986  33.863  1.00 10.65 ? 258 ALA A N   1 
ATOM   2050 C  CA  . ALA A 1 257 ? 3.614  -2.600  33.051  1.00 11.92 ? 258 ALA A CA  1 
ATOM   2051 C  C   . ALA A 1 257 ? 2.371  -1.790  33.198  1.00 11.73 ? 258 ALA A C   1 
ATOM   2052 O  O   . ALA A 1 257 ? 2.023  -1.329  34.323  1.00 11.66 ? 258 ALA A O   1 
ATOM   2053 C  CB  . ALA A 1 257 ? 3.343  -4.060  33.456  1.00 13.37 ? 258 ALA A CB  1 
ATOM   2054 N  N   . SER A 1 258 ? 1.631  -1.712  32.093  1.00 10.23 ? 259 SER A N   1 
ATOM   2055 C  CA  . SER A 1 258 ? 0.389  -0.995  32.104  1.00 12.28 ? 259 SER A CA  1 
ATOM   2056 C  C   . SER A 1 258 ? -0.727 -1.885  32.547  1.00 12.08 ? 259 SER A C   1 
ATOM   2057 O  O   . SER A 1 258 ? -1.852 -1.356  32.659  1.00 15.02 ? 259 SER A O   1 
ATOM   2058 C  CB  . SER A 1 258 ? 0.056  -0.434  30.724  1.00 11.93 ? 259 SER A CB  1 
ATOM   2059 O  OG  . SER A 1 258 ? -0.396 -1.443  29.786  1.00 11.78 ? 259 SER A OG  1 
ATOM   2060 N  N   . PHE A 1 259 ? -0.461 -3.151  32.761  1.00 13.32 ? 260 PHE A N   1 
ATOM   2061 C  CA  . PHE A 1 259 ? -1.545 -4.093  33.005  1.00 16.54 ? 260 PHE A CA  1 
ATOM   2062 C  C   . PHE A 1 259 ? -1.206 -4.994  34.161  1.00 21.44 ? 260 PHE A C   1 
ATOM   2063 O  O   . PHE A 1 259 ? -0.018 -5.234  34.482  1.00 20.00 ? 260 PHE A O   1 
ATOM   2064 C  CB  . PHE A 1 259 ? -1.736 -4.957  31.767  1.00 15.98 ? 260 PHE A CB  1 
ATOM   2065 C  CG  . PHE A 1 259 ? -0.459 -5.677  31.363  1.00 16.58 ? 260 PHE A CG  1 
ATOM   2066 C  CD1 . PHE A 1 259 ? 0.472  -5.003  30.554  1.00 14.97 ? 260 PHE A CD1 1 
ATOM   2067 C  CD2 . PHE A 1 259 ? -0.166 -6.953  31.832  1.00 19.19 ? 260 PHE A CD2 1 
ATOM   2068 C  CE1 . PHE A 1 259 ? 1.669  -5.595  30.202  1.00 16.48 ? 260 PHE A CE1 1 
ATOM   2069 C  CE2 . PHE A 1 259 ? 1.040  -7.566  31.477  1.00 18.81 ? 260 PHE A CE2 1 
ATOM   2070 C  CZ  . PHE A 1 259 ? 1.984  -6.854  30.690  1.00 17.02 ? 260 PHE A CZ  1 
ATOM   2071 N  N   . LYS A 1 260 ? -2.305 -5.489  34.752  1.00 29.14 ? 261 LYS A N   1 
ATOM   2072 C  CA  . LYS A 1 260 ? -2.432 -6.711  35.602  1.00 37.20 ? 261 LYS A CA  1 
ATOM   2073 C  C   . LYS A 1 260 ? -2.069 -6.701  37.085  1.00 45.88 ? 261 LYS A C   1 
ATOM   2074 O  O   . LYS A 1 260 ? -1.063 -7.263  37.516  1.00 52.72 ? 261 LYS A O   1 
ATOM   2075 C  CB  . LYS A 1 260 ? -1.954 -7.974  34.864  1.00 40.40 ? 261 LYS A CB  1 
ATOM   2076 C  CG  . LYS A 1 260 ? -2.989 -8.382  33.815  1.00 43.53 ? 261 LYS A CG  1 
ATOM   2077 C  CD  . LYS A 1 260 ? -2.868 -9.843  33.455  1.00 46.65 ? 261 LYS A CD  1 
ATOM   2078 C  CE  . LYS A 1 260 ? -2.022 -10.037 32.219  1.00 47.07 ? 261 LYS A CE  1 
ATOM   2079 N  NZ  . LYS A 1 260 ? -0.913 -10.999 32.491  1.00 44.15 ? 261 LYS A NZ  1 
ATOM   2080 O  OXT . LYS A 1 260 ? -2.831 -6.121  37.880  1.00 53.41 ? 261 LYS A OXT 1 
HETATM 2081 ZN ZN  . ZN  B 2 .   ? 14.382 0.168   15.379  1.00 8.36  ? 301 ZN  A ZN  1 
HETATM 2082 N  N1  . BCN C 3 .   ? 0.594  -12.746 23.260  1.00 34.32 ? 302 BCN A N1  1 
HETATM 2083 C  C1  . BCN C 3 .   ? 1.197  -12.262 24.471  1.00 30.83 ? 302 BCN A C1  1 
HETATM 2084 C  C2  . BCN C 3 .   ? 1.126  -13.210 25.591  1.00 36.12 ? 302 BCN A C2  1 
HETATM 2085 O  O21 . BCN C 3 .   ? 0.277  -14.092 25.510  1.00 36.94 ? 302 BCN A O21 1 
HETATM 2086 O  O22 . BCN C 3 .   ? 1.948  -13.088 26.582  1.00 33.36 ? 302 BCN A O22 1 
HETATM 2087 C  C3  . BCN C 3 .   ? 1.041  -13.767 22.445  1.00 25.52 ? 302 BCN A C3  1 
HETATM 2088 C  C4  . BCN C 3 .   ? 0.957  -14.599 21.257  1.00 33.40 ? 302 BCN A C4  1 
HETATM 2089 O  O4  . BCN C 3 .   ? -0.226 -14.199 20.592  1.00 38.15 ? 302 BCN A O4  1 
HETATM 2090 C  C5  . BCN C 3 .   ? -0.632 -12.079 22.929  1.00 26.95 ? 302 BCN A C5  1 
HETATM 2091 C  C6  . BCN C 3 .   ? -0.501 -11.186 24.165  1.00 34.99 ? 302 BCN A C6  1 
HETATM 2092 O  O6  . BCN C 3 .   ? -1.519 -10.489 24.739  1.00 29.12 ? 302 BCN A O6  1 
HETATM 2093 O  O1  . MES D 4 .   ? 13.745 -7.389  -3.134  1.00 40.16 ? 303 MES A O1  1 
HETATM 2094 C  C2  . MES D 4 .   ? 13.098 -7.226  -1.853  1.00 32.35 ? 303 MES A C2  1 
HETATM 2095 C  C3  . MES D 4 .   ? 11.810 -8.056  -1.494  1.00 25.67 ? 303 MES A C3  1 
HETATM 2096 N  N4  . MES D 4 .   ? 11.129 -8.549  -2.762  1.00 36.53 ? 303 MES A N4  1 
HETATM 2097 C  C5  . MES D 4 .   ? 12.093 -9.279  -3.683  1.00 35.88 ? 303 MES A C5  1 
HETATM 2098 C  C6  . MES D 4 .   ? 13.328 -8.406  -4.112  1.00 32.86 ? 303 MES A C6  1 
HETATM 2099 C  C7  . MES D 4 .   ? 9.892  -9.301  -2.397  1.00 36.51 ? 303 MES A C7  1 
HETATM 2100 C  C8  . MES D 4 .   ? 8.899  -9.635  -3.503  1.00 39.66 ? 303 MES A C8  1 
HETATM 2101 F  F32 A 5DT E 5 .   ? 17.276 5.072   12.777  0.50 39.25 ? 304 5DT A F32 1 
HETATM 2102 F  F32 B 5DT E 5 .   ? 17.245 5.018   12.566  0.50 43.24 ? 304 5DT A F32 1 
HETATM 2103 C  C6  A 5DT E 5 .   ? 16.529 5.069   13.910  0.50 33.22 ? 304 5DT A C6  1 
HETATM 2104 C  C6  B 5DT E 5 .   ? 16.490 5.102   13.691  0.50 35.32 ? 304 5DT A C6  1 
HETATM 2105 C  C1  A 5DT E 5 .   ? 16.018 6.277   14.383  0.50 31.67 ? 304 5DT A C1  1 
HETATM 2106 C  C1  B 5DT E 5 .   ? 15.965 6.348   14.061  0.50 34.64 ? 304 5DT A C1  1 
HETATM 2107 S  S11 A 5DT E 5 .   ? 16.344 7.750   13.436  0.50 34.06 ? 304 5DT A S11 1 
HETATM 2108 S  S11 B 5DT E 5 .   ? 16.316 7.760   12.990  0.50 39.02 ? 304 5DT A S11 1 
HETATM 2109 C  C21 A 5DT E 5 .   ? 17.606 8.383   14.586  0.50 27.49 ? 304 5DT A C21 1 
HETATM 2110 C  C21 B 5DT E 5 .   ? 14.730 7.973   12.112  0.50 30.06 ? 304 5DT A C21 1 
HETATM 2111 C  C24 A 5DT E 5 .   ? 18.947 8.208   13.939  0.50 22.47 ? 304 5DT A C24 1 
HETATM 2112 C  C24 B 5DT E 5 .   ? 14.387 9.416   11.859  0.50 28.80 ? 304 5DT A C24 1 
HETATM 2113 C  C29 A 5DT E 5 .   ? 19.873 9.354   14.070  0.50 22.00 ? 304 5DT A C29 1 
HETATM 2114 C  C29 B 5DT E 5 .   ? 14.198 9.857   10.444  0.50 28.75 ? 304 5DT A C29 1 
HETATM 2115 C  C28 A 5DT E 5 .   ? 20.919 9.400   13.136  0.50 21.83 ? 304 5DT A C28 1 
HETATM 2116 C  C28 B 5DT E 5 .   ? 14.800 11.054  10.019  0.50 29.83 ? 304 5DT A C28 1 
HETATM 2117 C  C27 A 5DT E 5 .   ? 21.883 10.399  13.164  0.50 21.17 ? 304 5DT A C27 1 
HETATM 2118 C  C27 B 5DT E 5 .   ? 14.592 11.502  8.687   0.50 28.82 ? 304 5DT A C27 1 
HETATM 2119 C  C31 A 5DT E 5 .   ? 19.793 10.336  15.072  0.50 20.07 ? 304 5DT A C31 1 
HETATM 2120 C  C31 B 5DT E 5 .   ? 13.384 9.147   9.545   0.50 28.86 ? 304 5DT A C31 1 
HETATM 2121 C  C30 A 5DT E 5 .   ? 20.753 11.366  15.093  0.50 20.07 ? 304 5DT A C30 1 
HETATM 2122 C  C30 B 5DT E 5 .   ? 13.147 9.581   8.239   0.50 22.02 ? 304 5DT A C30 1 
HETATM 2123 C  C26 A 5DT E 5 .   ? 21.783 11.401  14.148  0.50 21.14 ? 304 5DT A C26 1 
HETATM 2124 C  C26 B 5DT E 5 .   ? 13.778 10.761  7.808   0.50 29.90 ? 304 5DT A C26 1 
HETATM 2125 C  C5  A 5DT E 5 .   ? 16.347 3.872   14.601  0.50 29.01 ? 304 5DT A C5  1 
HETATM 2126 C  C5  B 5DT E 5 .   ? 16.315 3.947   14.463  0.50 30.79 ? 304 5DT A C5  1 
HETATM 2127 C  C4  A 5DT E 5 .   ? 15.566 3.938   15.802  0.50 28.10 ? 304 5DT A C4  1 
HETATM 2128 C  C4  B 5DT E 5 .   ? 15.532 4.066   15.652  0.50 28.55 ? 304 5DT A C4  1 
HETATM 2129 S  S7  A 5DT E 5 .   ? 15.185 2.484   16.802  0.50 27.09 ? 304 5DT A S7  1 
HETATM 2130 S  S7  B 5DT E 5 .   ? 15.166 2.651   16.725  0.50 27.73 ? 304 5DT A S7  1 
HETATM 2131 O  O9  A 5DT E 5 .   ? 13.632 2.422   16.836  0.50 24.73 ? 304 5DT A O9  1 
HETATM 2132 O  O9  B 5DT E 5 .   ? 13.605 2.601   16.738  0.50 21.99 ? 304 5DT A O9  1 
HETATM 2133 N  N10 A 5DT E 5 .   ? 15.897 1.121   15.981  0.50 19.63 ? 304 5DT A N10 1 
HETATM 2134 N  N10 B 5DT E 5 .   ? 15.825 1.216   15.981  0.50 18.63 ? 304 5DT A N10 1 
HETATM 2135 O  O8  A 5DT E 5 .   ? 15.660 2.623   18.249  0.50 20.21 ? 304 5DT A O8  1 
HETATM 2136 O  O8  B 5DT E 5 .   ? 15.640 2.778   18.179  0.50 19.62 ? 304 5DT A O8  1 
HETATM 2137 C  C3  A 5DT E 5 .   ? 15.031 5.159   16.247  0.50 30.43 ? 304 5DT A C3  1 
HETATM 2138 C  C3  B 5DT E 5 .   ? 14.984 5.308   16.006  0.50 31.24 ? 304 5DT A C3  1 
HETATM 2139 F  F12 A 5DT E 5 .   ? 14.303 5.185   17.396  0.50 30.14 ? 304 5DT A F12 1 
HETATM 2140 F  F12 B 5DT E 5 .   ? 14.247 5.391   17.149  0.50 30.43 ? 304 5DT A F12 1 
HETATM 2141 C  C2  A 5DT E 5 .   ? 15.260 6.338   15.541  0.50 31.36 ? 304 5DT A C2  1 
HETATM 2142 C  C2  B 5DT E 5 .   ? 15.205 6.450   15.228  0.50 32.93 ? 304 5DT A C2  1 
HETATM 2143 F  F13 A 5DT E 5 .   ? 14.747 7.530   15.984  0.50 32.86 ? 304 5DT A F13 1 
HETATM 2144 F  F13 B 5DT E 5 .   ? 14.659 7.640   15.624  0.50 34.94 ? 304 5DT A F13 1 
HETATM 2145 N  N25 A 5DT E 5 .   ? 16.910 2.699   14.003  0.50 21.62 ? 304 5DT A N25 1 
HETATM 2146 N  N25 B 5DT E 5 .   ? 16.892 2.735   13.965  0.50 22.74 ? 304 5DT A N25 1 
HETATM 2147 C  C14 A 5DT E 5 .   ? 16.399 2.213   12.723  0.50 25.37 ? 304 5DT A C14 1 
HETATM 2148 C  C14 B 5DT E 5 .   ? 16.354 2.152   12.746  0.50 26.00 ? 304 5DT A C14 1 
HETATM 2149 C  C15 A 5DT E 5 .   ? 17.261 1.144   12.118  0.50 23.68 ? 304 5DT A C15 1 
HETATM 2150 C  C15 B 5DT E 5 .   ? 17.246 1.166   12.050  0.50 23.92 ? 304 5DT A C15 1 
HETATM 2151 C  C20 A 5DT E 5 .   ? 16.908 -0.210  12.215  0.50 27.83 ? 304 5DT A C20 1 
HETATM 2152 C  C20 B 5DT E 5 .   ? 17.180 -0.190  12.401  0.50 28.52 ? 304 5DT A C20 1 
HETATM 2153 C  C19 A 5DT E 5 .   ? 17.743 -1.243  11.707  0.50 24.23 ? 304 5DT A C19 1 
HETATM 2154 C  C19 B 5DT E 5 .   ? 18.016 -1.174  11.816  0.50 24.20 ? 304 5DT A C19 1 
HETATM 2155 C  C18 A 5DT E 5 .   ? 18.922 -0.891  11.122  0.50 24.25 ? 304 5DT A C18 1 
HETATM 2156 C  C18 B 5DT E 5 .   ? 18.924 -0.757  10.894  0.50 25.54 ? 304 5DT A C18 1 
HETATM 2157 C  C17 A 5DT E 5 .   ? 19.302 0.461   11.028  0.50 27.84 ? 304 5DT A C17 1 
HETATM 2158 C  C17 B 5DT E 5 .   ? 19.018 0.604   10.526  0.50 29.00 ? 304 5DT A C17 1 
HETATM 2159 C  C16 A 5DT E 5 .   ? 18.476 1.486   11.520  0.50 26.90 ? 304 5DT A C16 1 
HETATM 2160 C  C16 B 5DT E 5 .   ? 18.187 1.579   11.101  0.50 26.41 ? 304 5DT A C16 1 
HETATM 2161 O  O   . HOH F 6 .   ? 3.318  20.988  6.164   1.00 18.37 ? 401 HOH A O   1 
HETATM 2162 O  O   . HOH F 6 .   ? 5.337  11.001  -1.998  1.00 22.18 ? 402 HOH A O   1 
HETATM 2163 O  O   . HOH F 6 .   ? 34.883 1.911   6.292   1.00 33.93 ? 403 HOH A O   1 
HETATM 2164 O  O   . HOH F 6 .   ? -4.571 11.608  13.446  1.00 28.83 ? 404 HOH A O   1 
HETATM 2165 O  O   . HOH F 6 .   ? 5.717  -8.522  37.601  1.00 31.37 ? 405 HOH A O   1 
HETATM 2166 O  O   . HOH F 6 .   ? 21.368 -7.867  -5.353  1.00 28.70 ? 406 HOH A O   1 
HETATM 2167 O  O   . HOH F 6 .   ? 8.371  20.420  29.406  1.00 37.71 ? 407 HOH A O   1 
HETATM 2168 O  O   . HOH F 6 .   ? 18.505 -17.179 21.579  1.00 32.96 ? 408 HOH A O   1 
HETATM 2169 O  O   . HOH F 6 .   ? 0.195  -5.060  -1.842  1.00 33.55 ? 409 HOH A O   1 
HETATM 2170 O  O   . HOH F 6 .   ? 4.247  -12.040 26.468  1.00 19.76 ? 410 HOH A O   1 
HETATM 2171 O  O   . HOH F 6 .   ? 11.044 17.523  29.988  1.00 29.08 ? 411 HOH A O   1 
HETATM 2172 O  O   . HOH F 6 .   ? 2.410  22.221  14.858  1.00 29.03 ? 412 HOH A O   1 
HETATM 2173 O  O   . HOH F 6 .   ? 8.675  14.435  29.423  1.00 23.88 ? 413 HOH A O   1 
HETATM 2174 O  O   . HOH F 6 .   ? 15.875 4.055   37.500  1.00 25.28 ? 414 HOH A O   1 
HETATM 2175 O  O   . HOH F 6 .   ? 23.187 9.898   27.967  1.00 33.58 ? 415 HOH A O   1 
HETATM 2176 O  O   . HOH F 6 .   ? -4.872 8.160   27.187  1.00 31.92 ? 416 HOH A O   1 
HETATM 2177 O  O   . HOH F 6 .   ? 32.182 -5.184  22.485  1.00 23.20 ? 417 HOH A O   1 
HETATM 2178 O  O   . HOH F 6 .   ? 37.069 5.323   15.495  1.00 27.06 ? 418 HOH A O   1 
HETATM 2179 O  O   . HOH F 6 .   ? 7.904  15.276  31.890  1.00 25.22 ? 419 HOH A O   1 
HETATM 2180 O  O   . HOH F 6 .   ? 27.800 -1.700  30.528  1.00 29.96 ? 420 HOH A O   1 
HETATM 2181 O  O   . HOH F 6 .   ? 18.967 -2.553  -6.934  1.00 25.36 ? 421 HOH A O   1 
HETATM 2182 O  O   . HOH F 6 .   ? 22.318 -9.792  25.232  1.00 21.95 ? 422 HOH A O   1 
HETATM 2183 O  O   . HOH F 6 .   ? 14.201 -13.079 31.630  1.00 18.28 ? 423 HOH A O   1 
HETATM 2184 O  O   . HOH F 6 .   ? 1.884  -18.839 5.167   1.00 26.04 ? 424 HOH A O   1 
HETATM 2185 O  O   . HOH F 6 .   ? -1.776 -13.014 16.192  1.00 31.48 ? 425 HOH A O   1 
HETATM 2186 O  O   . HOH F 6 .   ? 20.294 25.700  18.189  1.00 24.61 ? 426 HOH A O   1 
HETATM 2187 O  O   . HOH F 6 .   ? 16.277 -10.115 32.216  1.00 20.05 ? 427 HOH A O   1 
HETATM 2188 O  O   . HOH F 6 .   ? 10.652 4.910   37.563  1.00 38.34 ? 428 HOH A O   1 
HETATM 2189 O  O   . HOH F 6 .   ? -3.095 10.529  20.393  1.00 21.54 ? 429 HOH A O   1 
HETATM 2190 O  O   . HOH F 6 .   ? 12.426 0.477   41.501  1.00 39.27 ? 430 HOH A O   1 
HETATM 2191 O  O   . HOH F 6 .   ? 30.752 -2.958  -7.876  1.00 28.54 ? 431 HOH A O   1 
HETATM 2192 O  O   . HOH F 6 .   ? 20.602 16.054  16.321  1.00 23.68 ? 432 HOH A O   1 
HETATM 2193 O  O   . HOH F 6 .   ? -4.852 -4.328  13.274  1.00 33.45 ? 433 HOH A O   1 
HETATM 2194 O  O   . HOH F 6 .   ? 31.559 -6.773  8.736   1.00 32.21 ? 434 HOH A O   1 
HETATM 2195 O  O   . HOH F 6 .   ? 3.153  12.273  11.446  1.00 17.22 ? 435 HOH A O   1 
HETATM 2196 O  O   . HOH F 6 .   ? 0.404  10.202  30.197  1.00 21.49 ? 436 HOH A O   1 
HETATM 2197 O  O   . HOH F 6 .   ? 22.062 16.605  24.397  1.00 32.63 ? 437 HOH A O   1 
HETATM 2198 O  O   . HOH F 6 .   ? 6.873  -14.799 29.275  1.00 17.12 ? 438 HOH A O   1 
HETATM 2199 O  O   . HOH F 6 .   ? 6.231  21.811  17.827  1.00 18.99 ? 439 HOH A O   1 
HETATM 2200 O  O   . HOH F 6 .   ? 14.361 -18.311 19.645  1.00 14.03 ? 440 HOH A O   1 
HETATM 2201 O  O   . HOH F 6 .   ? 16.023 2.756   10.008  1.00 27.29 ? 441 HOH A O   1 
HETATM 2202 O  O   . HOH F 6 .   ? -4.642 -7.056  11.462  1.00 26.87 ? 442 HOH A O   1 
HETATM 2203 O  O   . HOH F 6 .   ? 19.838 -2.168  15.841  1.00 7.66  ? 443 HOH A O   1 
HETATM 2204 O  O   . HOH F 6 .   ? 5.790  21.371  13.243  1.00 21.35 ? 444 HOH A O   1 
HETATM 2205 O  O   . HOH F 6 .   ? 11.815 7.869   29.339  1.00 16.69 ? 445 HOH A O   1 
HETATM 2206 O  O   . HOH F 6 .   ? 19.731 -4.160  36.565  1.00 31.04 ? 446 HOH A O   1 
HETATM 2207 O  O   . HOH F 6 .   ? 2.016  19.462  18.708  1.00 37.02 ? 447 HOH A O   1 
HETATM 2208 O  O   . HOH F 6 .   ? 0.999  -14.747 3.013   1.00 19.58 ? 448 HOH A O   1 
HETATM 2209 O  O   . HOH F 6 .   ? 21.176 0.852   -4.722  1.00 14.59 ? 449 HOH A O   1 
HETATM 2210 O  O   . HOH F 6 .   ? 12.415 -1.972  7.921   1.00 10.19 ? 450 HOH A O   1 
HETATM 2211 O  O   . HOH F 6 .   ? 6.915  16.115  27.237  1.00 22.30 ? 451 HOH A O   1 
HETATM 2212 O  O   . HOH F 6 .   ? 16.810 -6.640  31.198  1.00 18.18 ? 452 HOH A O   1 
HETATM 2213 O  O   . HOH F 6 .   ? 25.359 -1.602  26.691  1.00 15.74 ? 453 HOH A O   1 
HETATM 2214 O  O   . HOH F 6 .   ? 23.209 -12.899 -5.675  1.00 32.49 ? 454 HOH A O   1 
HETATM 2215 O  O   . HOH F 6 .   ? 2.541  -10.420 -3.560  1.00 23.33 ? 455 HOH A O   1 
HETATM 2216 O  O   . HOH F 6 .   ? 7.040  -7.074  -5.333  1.00 28.21 ? 456 HOH A O   1 
HETATM 2217 O  O   . HOH F 6 .   ? 14.966 -2.597  -6.403  1.00 22.62 ? 457 HOH A O   1 
HETATM 2218 O  O   . HOH F 6 .   ? 4.038  -6.557  20.504  1.00 11.01 ? 458 HOH A O   1 
HETATM 2219 O  O   . HOH F 6 .   ? 12.353 2.565   -6.486  1.00 25.72 ? 459 HOH A O   1 
HETATM 2220 O  O   . HOH F 6 .   ? 10.741 -16.342 17.157  1.00 16.88 ? 460 HOH A O   1 
HETATM 2221 O  O   . HOH F 6 .   ? -6.439 -5.246  26.211  1.00 34.72 ? 461 HOH A O   1 
HETATM 2222 O  O   . HOH F 6 .   ? 25.436 -0.784  29.067  1.00 22.74 ? 462 HOH A O   1 
HETATM 2223 O  O   . HOH F 6 .   ? 1.743  11.981  9.075   1.00 15.78 ? 463 HOH A O   1 
HETATM 2224 O  O   . HOH F 6 .   ? -0.780 -12.335 18.548  1.00 29.68 ? 464 HOH A O   1 
HETATM 2225 O  O   . HOH F 6 .   ? 3.740  -14.390 22.170  1.00 20.65 ? 465 HOH A O   1 
HETATM 2226 O  O   . HOH F 6 .   ? 17.626 19.859  21.671  1.00 22.98 ? 466 HOH A O   1 
HETATM 2227 O  O   . HOH F 6 .   ? 4.719  -13.754 32.954  1.00 25.05 ? 467 HOH A O   1 
HETATM 2228 O  O   . HOH F 6 .   ? 7.957  -20.142 8.602   1.00 23.80 ? 468 HOH A O   1 
HETATM 2229 O  O   . HOH F 6 .   ? 22.850 -13.631 9.118   1.00 21.44 ? 469 HOH A O   1 
HETATM 2230 O  O   . HOH F 6 .   ? 17.519 -9.237  20.989  1.00 11.97 ? 470 HOH A O   1 
HETATM 2231 O  O   . HOH F 6 .   ? 7.790  -20.727 11.751  1.00 36.78 ? 471 HOH A O   1 
HETATM 2232 O  O   . HOH F 6 .   ? 20.146 5.712   13.714  1.00 21.98 ? 472 HOH A O   1 
HETATM 2233 O  O   . HOH F 6 .   ? 13.051 -13.612 11.463  1.00 9.78  ? 473 HOH A O   1 
HETATM 2234 O  O   . HOH F 6 .   ? -4.507 -13.400 7.856   1.00 26.80 ? 474 HOH A O   1 
HETATM 2235 O  O   . HOH F 6 .   ? 19.775 11.061  28.215  1.00 22.33 ? 475 HOH A O   1 
HETATM 2236 O  O   . HOH F 6 .   ? 16.537 -11.673 18.187  1.00 9.63  ? 476 HOH A O   1 
HETATM 2237 O  O   . HOH F 6 .   ? 10.188 -13.407 34.298  1.00 22.46 ? 477 HOH A O   1 
HETATM 2238 O  O   . HOH F 6 .   ? 4.958  17.738  23.863  1.00 21.53 ? 478 HOH A O   1 
HETATM 2239 O  O   . HOH F 6 .   ? 28.446 -3.275  0.091   1.00 43.64 ? 479 HOH A O   1 
HETATM 2240 O  O   . HOH F 6 .   ? 21.032 3.155   34.630  1.00 26.38 ? 480 HOH A O   1 
HETATM 2241 O  O   . HOH F 6 .   ? 36.722 4.550   20.961  1.00 21.79 ? 481 HOH A O   1 
HETATM 2242 O  O   . HOH F 6 .   ? 24.712 6.949   29.876  1.00 16.80 ? 482 HOH A O   1 
HETATM 2243 O  O   . HOH F 6 .   ? 6.416  -16.746 18.806  1.00 16.59 ? 483 HOH A O   1 
HETATM 2244 O  O   . HOH F 6 .   ? -1.688 -3.945  2.930   1.00 19.47 ? 484 HOH A O   1 
HETATM 2245 O  O   . HOH F 6 .   ? 4.922  -10.462 24.515  1.00 12.10 ? 485 HOH A O   1 
HETATM 2246 O  O   . HOH F 6 .   ? 0.615  12.612  26.722  1.00 14.53 ? 486 HOH A O   1 
HETATM 2247 O  O   . HOH F 6 .   ? 7.253  12.310  28.082  1.00 14.73 ? 487 HOH A O   1 
HETATM 2248 O  O   . HOH F 6 .   ? 0.719  15.629  28.912  1.00 35.46 ? 488 HOH A O   1 
HETATM 2249 O  O   . HOH F 6 .   ? 3.059  -18.655 8.080   1.00 15.64 ? 489 HOH A O   1 
HETATM 2250 O  O   . HOH F 6 .   ? -2.005 1.635   34.637  1.00 27.19 ? 490 HOH A O   1 
HETATM 2251 O  O   . HOH F 6 .   ? -0.177 9.774   1.972   1.00 16.38 ? 491 HOH A O   1 
HETATM 2252 O  O   . HOH F 6 .   ? 17.673 -11.415 25.327  1.00 13.68 ? 492 HOH A O   1 
HETATM 2253 O  O   . HOH F 6 .   ? -4.637 -8.864  17.809  1.00 26.39 ? 493 HOH A O   1 
HETATM 2254 O  O   . HOH F 6 .   ? 2.610  -1.845  -2.510  1.00 25.02 ? 494 HOH A O   1 
HETATM 2255 O  O   . HOH F 6 .   ? 32.654 1.506   16.054  1.00 26.58 ? 495 HOH A O   1 
HETATM 2256 O  O   . HOH F 6 .   ? 7.579  1.067   -6.066  1.00 27.85 ? 496 HOH A O   1 
HETATM 2257 O  O   . HOH F 6 .   ? -2.102 -1.189  6.952   1.00 18.59 ? 497 HOH A O   1 
HETATM 2258 O  O   . HOH F 6 .   ? 8.989  11.230  3.173   1.00 31.95 ? 498 HOH A O   1 
HETATM 2259 O  O   . HOH F 6 .   ? 17.369 -11.062 -2.850  1.00 19.02 ? 499 HOH A O   1 
HETATM 2260 O  O   . HOH F 6 .   ? 26.435 8.976   20.515  1.00 14.31 ? 500 HOH A O   1 
HETATM 2261 O  O   . HOH F 6 .   ? 10.489 -17.587 20.036  1.00 16.20 ? 501 HOH A O   1 
HETATM 2262 O  O   . HOH F 6 .   ? 10.350 10.590  25.675  1.00 9.98  ? 502 HOH A O   1 
HETATM 2263 O  O   . HOH F 6 .   ? 5.981  4.338   38.973  1.00 32.19 ? 503 HOH A O   1 
HETATM 2264 O  O   . HOH F 6 .   ? 34.941 3.755   22.834  1.00 30.94 ? 504 HOH A O   1 
HETATM 2265 O  O   . HOH F 6 .   ? 34.480 2.044   24.566  1.00 21.98 ? 505 HOH A O   1 
HETATM 2266 O  O   . HOH F 6 .   ? 26.793 2.613   8.505   1.00 28.74 ? 506 HOH A O   1 
HETATM 2267 O  O   . HOH F 6 .   ? 27.324 -9.381  15.770  1.00 28.88 ? 507 HOH A O   1 
HETATM 2268 O  O   . HOH F 6 .   ? 25.488 -4.716  7.942   1.00 20.42 ? 508 HOH A O   1 
HETATM 2269 O  O   . HOH F 6 .   ? 10.483 10.291  7.815   1.00 17.82 ? 509 HOH A O   1 
HETATM 2270 O  O   . HOH F 6 .   ? 8.996  12.664  5.797   1.00 25.55 ? 510 HOH A O   1 
HETATM 2271 O  O   . HOH F 6 .   ? 14.163 7.790   6.401   1.00 19.31 ? 511 HOH A O   1 
HETATM 2272 O  O   . HOH F 6 .   ? 23.805 -2.445  7.915   1.00 22.26 ? 512 HOH A O   1 
HETATM 2273 O  O   . HOH F 6 .   ? 29.687 -2.077  21.190  1.00 15.18 ? 513 HOH A O   1 
HETATM 2274 O  O   . HOH F 6 .   ? 4.051  0.568   40.240  1.00 33.27 ? 514 HOH A O   1 
HETATM 2275 O  O   . HOH F 6 .   ? 7.426  21.918  15.171  1.00 19.56 ? 515 HOH A O   1 
HETATM 2276 O  O   . HOH F 6 .   ? 23.574 -11.371 5.295   1.00 20.76 ? 516 HOH A O   1 
HETATM 2277 O  O   . HOH F 6 .   ? -0.780 7.650   4.860   1.00 14.69 ? 517 HOH A O   1 
HETATM 2278 O  O   . HOH F 6 .   ? 15.063 19.674  27.829  1.00 31.12 ? 518 HOH A O   1 
HETATM 2279 O  O   . HOH F 6 .   ? -3.844 -5.835  9.132   1.00 18.07 ? 519 HOH A O   1 
HETATM 2280 O  O   . HOH F 6 .   ? 22.291 0.440   29.606  1.00 12.84 ? 520 HOH A O   1 
HETATM 2281 O  O   . HOH F 6 .   ? -0.611 -5.402  23.765  1.00 12.77 ? 521 HOH A O   1 
HETATM 2282 O  O   . HOH F 6 .   ? 36.396 -0.805  14.453  1.00 21.38 ? 522 HOH A O   1 
HETATM 2283 O  O   . HOH F 6 .   ? 3.924  -12.452 37.797  1.00 31.04 ? 523 HOH A O   1 
HETATM 2284 O  O   . HOH F 6 .   ? 19.442 6.444   -4.885  1.00 27.42 ? 524 HOH A O   1 
HETATM 2285 O  O   . HOH F 6 .   ? 29.387 4.757   27.904  1.00 27.35 ? 525 HOH A O   1 
HETATM 2286 O  O   . HOH F 6 .   ? 25.926 -3.090  21.016  1.00 11.28 ? 526 HOH A O   1 
HETATM 2287 O  O   . HOH F 6 .   ? 12.872 -17.443 21.775  1.00 16.33 ? 527 HOH A O   1 
HETATM 2288 O  O   . HOH F 6 .   ? 7.557  -16.793 14.741  1.00 18.36 ? 528 HOH A O   1 
HETATM 2289 O  O   . HOH F 6 .   ? 9.903  2.921   33.570  1.00 18.49 ? 529 HOH A O   1 
HETATM 2290 O  O   . HOH F 6 .   ? 8.094  -15.057 26.796  1.00 12.22 ? 530 HOH A O   1 
HETATM 2291 O  O   . HOH F 6 .   ? 28.642 -6.022  -0.762  1.00 36.29 ? 531 HOH A O   1 
HETATM 2292 O  O   . HOH F 6 .   ? 8.179  -6.928  -3.207  1.00 23.78 ? 532 HOH A O   1 
HETATM 2293 O  O   . HOH F 6 .   ? 9.990  -17.968 7.330   1.00 27.59 ? 533 HOH A O   1 
HETATM 2294 O  O   . HOH F 6 .   ? -2.324 -11.335 11.343  1.00 23.73 ? 534 HOH A O   1 
HETATM 2295 O  O   . HOH F 6 .   ? 20.594 12.759  23.659  1.00 16.17 ? 535 HOH A O   1 
HETATM 2296 O  O   . HOH F 6 .   ? 17.339 -14.089 24.435  1.00 10.89 ? 536 HOH A O   1 
HETATM 2297 O  O   . HOH F 6 .   ? 1.209  -2.520  41.453  1.00 24.34 ? 537 HOH A O   1 
HETATM 2298 O  O   . HOH F 6 .   ? 2.823  4.478   40.681  1.00 41.49 ? 538 HOH A O   1 
HETATM 2299 O  O   . HOH F 6 .   ? -3.865 6.547   8.508   1.00 25.04 ? 539 HOH A O   1 
HETATM 2300 O  O   . HOH F 6 .   ? 13.161 -17.283 30.728  1.00 26.12 ? 540 HOH A O   1 
HETATM 2301 O  O   . HOH F 6 .   ? 16.349 -14.110 0.844   1.00 23.19 ? 541 HOH A O   1 
HETATM 2302 O  O   . HOH F 6 .   ? 13.798 -6.840  32.779  1.00 18.53 ? 542 HOH A O   1 
HETATM 2303 O  O   . HOH F 6 .   ? 22.636 -4.370  34.582  1.00 20.33 ? 543 HOH A O   1 
HETATM 2304 O  O   . HOH F 6 .   ? 18.536 -6.981  29.272  1.00 11.48 ? 544 HOH A O   1 
HETATM 2305 O  O   . HOH F 6 .   ? -2.968 -0.441  29.094  1.00 31.33 ? 545 HOH A O   1 
HETATM 2306 O  O   . HOH F 6 .   ? 14.320 -3.406  37.529  1.00 19.34 ? 546 HOH A O   1 
HETATM 2307 O  O   . HOH F 6 .   ? 4.079  2.214   -3.530  1.00 36.03 ? 547 HOH A O   1 
HETATM 2308 O  O   . HOH F 6 .   ? -1.907 -9.810  14.119  1.00 17.52 ? 548 HOH A O   1 
HETATM 2309 O  O   . HOH F 6 .   ? 4.868  -8.119  33.232  1.00 16.38 ? 549 HOH A O   1 
HETATM 2310 O  O   . HOH F 6 .   ? 1.592  19.321  6.455   1.00 31.71 ? 550 HOH A O   1 
HETATM 2311 O  O   . HOH F 6 .   ? 18.212 7.891   -1.303  1.00 21.97 ? 551 HOH A O   1 
HETATM 2312 O  O   . HOH F 6 .   ? 3.639  -4.992  42.573  1.00 28.70 ? 552 HOH A O   1 
HETATM 2313 O  O   . HOH F 6 .   ? -4.440 -7.788  15.235  1.00 28.90 ? 553 HOH A O   1 
HETATM 2314 O  O   . HOH F 6 .   ? 22.344 10.605  24.512  1.00 16.91 ? 554 HOH A O   1 
HETATM 2315 O  O   . HOH F 6 .   ? -5.867 -2.213  25.128  1.00 21.01 ? 555 HOH A O   1 
HETATM 2316 O  O   . HOH F 6 .   ? 8.257  9.849   28.967  1.00 20.62 ? 556 HOH A O   1 
HETATM 2317 O  O   . HOH F 6 .   ? -3.185 -15.763 6.560   1.00 32.34 ? 557 HOH A O   1 
HETATM 2318 O  O   . HOH F 6 .   ? -5.210 -5.534  30.548  1.00 26.64 ? 558 HOH A O   1 
HETATM 2319 O  O   . HOH F 6 .   ? -1.193 -16.505 13.536  1.00 20.67 ? 559 HOH A O   1 
HETATM 2320 O  O   . HOH F 6 .   ? 27.545 1.349   -1.569  1.00 30.76 ? 560 HOH A O   1 
HETATM 2321 O  O   . HOH F 6 .   ? 14.631 -17.988 24.002  1.00 21.60 ? 561 HOH A O   1 
HETATM 2322 O  O   . HOH F 6 .   ? 9.045  4.570   31.120  1.00 16.13 ? 562 HOH A O   1 
HETATM 2323 O  O   . HOH F 6 .   ? 3.800  -5.740  39.721  1.00 31.59 ? 563 HOH A O   1 
HETATM 2324 O  O   . HOH F 6 .   ? 13.910 -15.010 1.461   1.00 20.93 ? 564 HOH A O   1 
HETATM 2325 O  O   . HOH F 6 .   ? 12.455 -18.077 26.852  1.00 19.46 ? 565 HOH A O   1 
HETATM 2326 O  O   . HOH F 6 .   ? 32.297 3.059   26.034  1.00 20.73 ? 566 HOH A O   1 
HETATM 2327 O  O   . HOH F 6 .   ? 7.293  16.773  6.173   1.00 33.78 ? 567 HOH A O   1 
HETATM 2328 O  O   . HOH F 6 .   ? -4.904 9.793   6.201   1.00 31.31 ? 568 HOH A O   1 
HETATM 2329 O  O   . HOH F 6 .   ? -2.856 1.133   4.051   1.00 18.10 ? 569 HOH A O   1 
HETATM 2330 O  O   . HOH F 6 .   ? 10.689 14.972  8.772   1.00 28.88 ? 570 HOH A O   1 
HETATM 2331 O  O   . HOH F 6 .   ? 11.088 16.709  12.344  1.00 20.13 ? 571 HOH A O   1 
HETATM 2332 O  O   . HOH F 6 .   ? 23.677 -9.490  9.576   1.00 18.25 ? 572 HOH A O   1 
HETATM 2333 O  O   . HOH F 6 .   ? 12.049 -3.882  36.100  1.00 19.62 ? 573 HOH A O   1 
HETATM 2334 O  O   . HOH F 6 .   ? 34.106 -4.132  24.468  1.00 23.80 ? 574 HOH A O   1 
HETATM 2335 O  O   . HOH F 6 .   ? 13.042 -20.361 10.428  1.00 25.04 ? 575 HOH A O   1 
HETATM 2336 O  O   . HOH F 6 .   ? -1.632 -7.647  25.439  1.00 23.15 ? 576 HOH A O   1 
HETATM 2337 O  O   . HOH F 6 .   ? -2.929 1.066   26.688  1.00 23.87 ? 577 HOH A O   1 
HETATM 2338 O  O   . HOH F 6 .   ? 14.017 3.498   35.464  1.00 22.42 ? 578 HOH A O   1 
HETATM 2339 O  O   . HOH F 6 .   ? 12.365 -13.550 37.038  1.00 20.57 ? 579 HOH A O   1 
HETATM 2340 O  O   . HOH F 6 .   ? 10.450 22.590  25.191  1.00 23.88 ? 580 HOH A O   1 
HETATM 2341 O  O   . HOH F 6 .   ? 26.924 -1.021  6.934   1.00 35.07 ? 581 HOH A O   1 
HETATM 2342 O  O   . HOH F 6 .   ? 19.069 -10.496 22.938  1.00 10.49 ? 582 HOH A O   1 
HETATM 2343 O  O   . HOH F 6 .   ? 8.369  5.363   -6.753  1.00 27.30 ? 583 HOH A O   1 
HETATM 2344 O  O   . HOH F 6 .   ? 35.233 7.496   19.135  1.00 28.01 ? 584 HOH A O   1 
HETATM 2345 O  O   . HOH F 6 .   ? -2.335 -9.136  17.088  1.00 26.32 ? 585 HOH A O   1 
HETATM 2346 O  O   . HOH F 6 .   ? -4.923 -4.615  33.654  1.00 33.25 ? 586 HOH A O   1 
HETATM 2347 O  O   . HOH F 6 .   ? 3.003  -1.138  45.476  1.00 38.01 ? 587 HOH A O   1 
HETATM 2348 O  O   . HOH F 6 .   ? 27.405 -3.564  4.006   1.00 34.21 ? 588 HOH A O   1 
HETATM 2349 O  O   . HOH F 6 .   ? 15.280 17.101  11.985  1.00 25.82 ? 589 HOH A O   1 
HETATM 2350 O  O   . HOH F 6 .   ? 26.078 -5.636  22.380  1.00 24.47 ? 590 HOH A O   1 
HETATM 2351 O  O   . HOH F 6 .   ? -2.609 -11.204 27.425  1.00 41.61 ? 591 HOH A O   1 
HETATM 2352 O  O   . HOH F 6 .   ? -4.225 13.016  19.644  1.00 33.21 ? 592 HOH A O   1 
HETATM 2353 O  O   . HOH F 6 .   ? 22.514 -9.635  15.596  1.00 25.98 ? 593 HOH A O   1 
HETATM 2354 O  O   . HOH F 6 .   ? 28.722 7.979   21.906  1.00 15.57 ? 594 HOH A O   1 
HETATM 2355 O  O   . HOH F 6 .   ? 20.410 -6.755  32.768  1.00 25.30 ? 595 HOH A O   1 
HETATM 2356 O  O   . HOH F 6 .   ? 28.878 0.424   -5.721  1.00 44.64 ? 596 HOH A O   1 
HETATM 2357 O  O   . HOH F 6 .   ? 14.131 -6.660  -7.092  1.00 29.92 ? 597 HOH A O   1 
HETATM 2358 O  O   . HOH F 6 .   ? -2.999 1.611   1.178   1.00 27.86 ? 598 HOH A O   1 
HETATM 2359 O  O   . HOH F 6 .   ? 5.817  -18.147 23.093  1.00 28.31 ? 599 HOH A O   1 
HETATM 2360 O  O   . HOH F 6 .   ? 16.717 5.332   10.385  1.00 31.54 ? 600 HOH A O   1 
HETATM 2361 O  O   . HOH F 6 .   ? 6.317  7.911   32.906  1.00 30.50 ? 601 HOH A O   1 
HETATM 2362 O  O   . HOH F 6 .   ? -3.558 -7.628  2.130   1.00 25.94 ? 602 HOH A O   1 
HETATM 2363 O  O   . HOH F 6 .   ? 15.521 5.492   -5.769  1.00 23.94 ? 603 HOH A O   1 
HETATM 2364 O  O   . HOH F 6 .   ? 4.280  -14.182 -4.358  1.00 36.86 ? 604 HOH A O   1 
HETATM 2365 O  O   . HOH F 6 .   ? 17.622 6.596   7.050   1.00 31.47 ? 605 HOH A O   1 
HETATM 2366 O  O   . HOH F 6 .   ? 11.602 -6.087  34.246  1.00 15.89 ? 606 HOH A O   1 
HETATM 2367 O  O   . HOH F 6 .   ? 32.089 -1.946  7.345   1.00 34.19 ? 607 HOH A O   1 
HETATM 2368 O  O   . HOH F 6 .   ? 19.295 9.866   30.849  1.00 35.81 ? 608 HOH A O   1 
HETATM 2369 O  O   . HOH F 6 .   ? 29.137 -4.069  -10.663 1.00 34.04 ? 609 HOH A O   1 
HETATM 2370 O  O   . HOH F 6 .   ? 27.382 -4.089  6.802   1.00 30.20 ? 610 HOH A O   1 
HETATM 2371 O  O   . HOH F 6 .   ? 30.396 3.830   12.416  1.00 29.76 ? 611 HOH A O   1 
HETATM 2372 O  O   . HOH F 6 .   ? 2.578  -6.899  34.863  1.00 36.22 ? 612 HOH A O   1 
HETATM 2373 O  O   . HOH F 6 .   ? -2.702 1.595   32.168  1.00 32.29 ? 613 HOH A O   1 
HETATM 2374 O  O   . HOH F 6 .   ? -0.202 -17.957 6.586   1.00 28.90 ? 614 HOH A O   1 
HETATM 2375 O  O   . HOH F 6 .   ? 22.655 -14.051 -1.498  1.00 52.53 ? 615 HOH A O   1 
HETATM 2376 O  O   . HOH F 6 .   ? 20.703 -13.831 27.405  1.00 31.68 ? 616 HOH A O   1 
HETATM 2377 O  O   . HOH F 6 .   ? 14.947 -9.585  36.641  1.00 25.35 ? 617 HOH A O   1 
HETATM 2378 O  O   . HOH F 6 .   ? 3.767  -21.369 4.155   1.00 32.22 ? 618 HOH A O   1 
HETATM 2379 O  O   . HOH F 6 .   ? 25.712 -11.407 -5.724  1.00 30.14 ? 619 HOH A O   1 
HETATM 2380 O  O   . HOH F 6 .   ? 19.416 -13.778 -5.295  1.00 37.06 ? 620 HOH A O   1 
HETATM 2381 O  O   . HOH F 6 .   ? 9.994  19.406  12.206  1.00 33.33 ? 621 HOH A O   1 
HETATM 2382 O  O   . HOH F 6 .   ? -6.714 6.447   23.809  1.00 31.80 ? 622 HOH A O   1 
HETATM 2383 O  O   . HOH F 6 .   ? 21.410 2.582   -6.661  1.00 24.75 ? 623 HOH A O   1 
HETATM 2384 O  O   . HOH F 6 .   ? -0.687 21.698  17.510  1.00 42.83 ? 624 HOH A O   1 
HETATM 2385 O  O   . HOH F 6 .   ? 2.471  5.279   -3.589  1.00 28.75 ? 625 HOH A O   1 
HETATM 2386 O  O   . HOH F 6 .   ? 24.326 2.761   -1.839  1.00 34.31 ? 626 HOH A O   1 
HETATM 2387 O  O   . HOH F 6 .   ? 10.798 7.778   -4.255  1.00 33.51 ? 627 HOH A O   1 
HETATM 2388 O  O   . HOH F 6 .   ? 15.474 -10.797 -5.175  1.00 36.53 ? 628 HOH A O   1 
HETATM 2389 O  O   . HOH F 6 .   ? 15.698 2.176   40.586  1.00 37.44 ? 629 HOH A O   1 
HETATM 2390 O  O   . HOH F 6 .   ? 31.178 -0.537  13.745  1.00 32.73 ? 630 HOH A O   1 
HETATM 2391 O  O   . HOH F 6 .   ? 8.208  -15.397 16.977  1.00 14.36 ? 631 HOH A O   1 
HETATM 2392 O  O   . HOH F 6 .   ? 20.788 -12.376 22.268  1.00 17.08 ? 632 HOH A O   1 
HETATM 2393 O  O   . HOH F 6 .   ? 33.899 -1.883  13.512  1.00 31.52 ? 633 HOH A O   1 
HETATM 2394 O  O   . HOH F 6 .   ? 13.970 18.775  10.815  1.00 40.34 ? 634 HOH A O   1 
HETATM 2395 O  O   . HOH F 6 .   ? 3.311  -7.540  37.369  1.00 45.34 ? 635 HOH A O   1 
HETATM 2396 O  O   . HOH F 6 .   ? 5.702  13.602  35.340  1.00 39.18 ? 636 HOH A O   1 
HETATM 2397 O  O   . HOH F 6 .   ? 29.669 -2.813  23.737  1.00 24.03 ? 637 HOH A O   1 
HETATM 2398 O  O   . HOH F 6 .   ? 19.699 13.098  25.963  1.00 29.13 ? 638 HOH A O   1 
HETATM 2399 O  O   . HOH F 6 .   ? 7.184  5.396   33.466  1.00 32.16 ? 639 HOH A O   1 
HETATM 2400 O  O   . HOH F 6 .   ? 25.972 -8.889  18.637  1.00 38.04 ? 640 HOH A O   1 
HETATM 2401 O  O   . HOH F 6 .   ? 12.715 -15.675 35.116  1.00 18.81 ? 641 HOH A O   1 
HETATM 2402 O  O   . HOH F 6 .   ? 5.666  -14.513 25.644  1.00 23.51 ? 642 HOH A O   1 
HETATM 2403 O  O   . HOH F 6 .   ? 4.557  -12.716 29.018  1.00 29.57 ? 643 HOH A O   1 
HETATM 2404 O  O   . HOH F 6 .   ? 3.340  21.938  17.718  1.00 21.66 ? 644 HOH A O   1 
HETATM 2405 O  O   . HOH F 6 .   ? 16.122 9.668   -3.967  1.00 33.12 ? 645 HOH A O   1 
HETATM 2406 O  O   . HOH F 6 .   ? 19.867 3.330   10.120  1.00 32.71 ? 646 HOH A O   1 
HETATM 2407 O  O   . HOH F 6 .   ? 8.547  8.696   31.409  1.00 35.61 ? 647 HOH A O   1 
HETATM 2408 O  O   . HOH F 6 .   ? 31.316 7.712   13.134  1.00 39.48 ? 648 HOH A O   1 
HETATM 2409 O  O   . HOH F 6 .   ? 18.325 -15.866 4.968   1.00 39.74 ? 649 HOH A O   1 
HETATM 2410 O  O   . HOH F 6 .   ? 16.722 8.023   9.748   1.00 40.08 ? 650 HOH A O   1 
HETATM 2411 O  O   . HOH F 6 .   ? 27.011 -12.202 8.698   1.00 35.00 ? 651 HOH A O   1 
HETATM 2412 O  O   . HOH F 6 .   ? 8.401  12.786  -5.227  1.00 31.15 ? 652 HOH A O   1 
HETATM 2413 O  O   . HOH F 6 .   ? 24.316 4.582   -0.052  1.00 34.51 ? 653 HOH A O   1 
HETATM 2414 O  O   . HOH F 6 .   ? 22.117 5.016   1.774   1.00 32.63 ? 654 HOH A O   1 
HETATM 2415 O  O   . HOH F 6 .   ? 19.735 -11.290 27.198  1.00 19.19 ? 655 HOH A O   1 
HETATM 2416 O  O   . HOH F 6 .   ? -5.887 -4.570  8.445   1.00 40.98 ? 656 HOH A O   1 
HETATM 2417 O  O   . HOH F 6 .   ? 4.129  -16.065 20.267  1.00 21.36 ? 657 HOH A O   1 
HETATM 2418 O  O   . HOH F 6 .   ? 32.983 -4.900  7.850   1.00 30.72 ? 658 HOH A O   1 
HETATM 2419 O  O   . HOH F 6 .   ? -4.093 10.880  26.147  1.00 38.93 ? 659 HOH A O   1 
HETATM 2420 O  O   . HOH F 6 .   ? 4.126  -15.906 24.121  1.00 38.84 ? 660 HOH A O   1 
HETATM 2421 O  O   . HOH F 6 .   ? 23.054 -7.767  31.033  1.00 37.98 ? 661 HOH A O   1 
HETATM 2422 O  O   . HOH F 6 .   ? 27.531 -3.549  27.492  1.00 31.17 ? 662 HOH A O   1 
HETATM 2423 O  O   . HOH F 6 .   ? 24.043 -11.721 8.090   1.00 23.09 ? 663 HOH A O   1 
HETATM 2424 O  O   . HOH F 6 .   ? 9.714  2.774   -7.643  1.00 33.84 ? 664 HOH A O   1 
HETATM 2425 O  O   . HOH F 6 .   ? 20.205 3.759   43.200  1.00 34.06 ? 665 HOH A O   1 
HETATM 2426 O  O   . HOH F 6 .   ? 22.808 14.365  22.951  1.00 30.61 ? 666 HOH A O   1 
HETATM 2427 O  O   . HOH F 6 .   ? 10.409 6.849   31.258  1.00 19.39 ? 667 HOH A O   1 
HETATM 2428 O  O   . HOH F 6 .   ? 18.901 -10.064 31.733  1.00 27.59 ? 668 HOH A O   1 
HETATM 2429 O  O   . HOH F 6 .   ? 15.182 -18.992 26.188  1.00 25.92 ? 669 HOH A O   1 
HETATM 2430 O  O   . HOH F 6 .   ? 24.598 -11.840 12.393  1.00 29.63 ? 670 HOH A O   1 
HETATM 2431 O  O   . HOH F 6 .   ? 20.985 -4.983  -7.391  1.00 35.64 ? 671 HOH A O   1 
HETATM 2432 O  O   . HOH F 6 .   ? 3.200  -10.187 31.948  1.00 28.74 ? 672 HOH A O   1 
HETATM 2433 O  O   . HOH F 6 .   ? -2.678 -5.584  0.030   1.00 35.48 ? 673 HOH A O   1 
HETATM 2434 O  O   . HOH F 6 .   ? 4.826  18.953  26.517  1.00 30.24 ? 674 HOH A O   1 
HETATM 2435 O  O   . HOH F 6 .   ? 19.155 -15.574 25.770  1.00 23.10 ? 675 HOH A O   1 
HETATM 2436 O  O   . HOH F 6 .   ? 15.995 -7.811  33.927  1.00 32.70 ? 676 HOH A O   1 
HETATM 2437 O  O   . HOH F 6 .   ? 9.378  12.587  0.870   1.00 26.92 ? 677 HOH A O   1 
HETATM 2438 O  O   . HOH F 6 .   ? 8.802  15.286  5.080   1.00 29.32 ? 678 HOH A O   1 
HETATM 2439 O  O   . HOH F 6 .   ? 16.158 22.340  21.469  1.00 21.57 ? 679 HOH A O   1 
HETATM 2440 O  O   . HOH F 6 .   ? -0.317 -18.427 14.965  1.00 45.57 ? 680 HOH A O   1 
HETATM 2441 O  O   . HOH F 6 .   ? 22.617 -15.700 7.072   1.00 32.66 ? 681 HOH A O   1 
HETATM 2442 O  O   . HOH F 6 .   ? 33.330 5.847   27.408  1.00 29.17 ? 682 HOH A O   1 
HETATM 2443 O  O   . HOH F 6 .   ? 27.426 7.182   29.379  1.00 33.26 ? 683 HOH A O   1 
HETATM 2444 O  O   . HOH F 6 .   ? -7.330 7.412   26.040  1.00 34.34 ? 684 HOH A O   1 
HETATM 2445 O  O   . HOH F 6 .   ? 8.238  23.518  26.321  1.00 18.16 ? 685 HOH A O   1 
HETATM 2446 O  O   . HOH F 6 .   ? 25.208 6.904   2.214   1.00 21.84 ? 686 HOH A O   1 
HETATM 2447 O  O   . HOH F 6 .   ? 19.913 -9.375  29.145  1.00 16.77 ? 687 HOH A O   1 
HETATM 2448 O  O   . HOH F 6 .   ? 27.700 10.271  18.443  1.00 31.29 ? 688 HOH A O   1 
HETATM 2449 O  O   . HOH F 6 .   ? 17.746 22.980  27.237  1.00 36.93 ? 689 HOH A O   1 
HETATM 2450 O  O   . HOH F 6 .   ? 26.582 10.893  21.944  1.00 34.49 ? 690 HOH A O   1 
HETATM 2451 O  O   . HOH F 6 .   ? 25.079 -10.239 23.071  1.00 38.64 ? 691 HOH A O   1 
HETATM 2452 O  O   . HOH F 6 .   ? 23.035 -12.238 20.629  1.00 25.33 ? 692 HOH A O   1 
HETATM 2453 O  O   . HOH F 6 .   ? 24.853 11.498  23.836  1.00 33.57 ? 693 HOH A O   1 
HETATM 2454 O  O   . HOH F 6 .   ? 33.175 -5.214  -2.103  1.00 37.58 ? 694 HOH A O   1 
# 
