data_6YHB
# 
_entry.id   6YHB 
# 
_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   6YHB         pdb_00006yhb 10.2210/pdb6yhb/pdb 
WWPDB D_1292106060 ?            ?                   
# 
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 2021-04-07 
2 'Structure model' 1 1 2021-06-02 
3 'Structure model' 1 2 2024-01-24 
# 
_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' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 3 '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 2 'Structure model' citation                      
2 2 'Structure model' citation_author               
3 3 'Structure model' chem_comp_atom                
4 3 'Structure model' chem_comp_bond                
5 3 'Structure model' database_2                    
6 3 '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  2 'Structure model' '_citation.country'                   
2  2 'Structure model' '_citation.journal_abbrev'            
3  2 'Structure model' '_citation.journal_id_CSD'            
4  2 'Structure model' '_citation.journal_id_ISSN'           
5  2 'Structure model' '_citation.journal_volume'            
6  2 'Structure model' '_citation.page_first'                
7  2 'Structure model' '_citation.page_last'                 
8  2 'Structure model' '_citation.pdbx_database_id_DOI'      
9  2 'Structure model' '_citation.pdbx_database_id_PubMed'   
10 2 'Structure model' '_citation.title'                     
11 2 'Structure model' '_citation.year'                      
12 3 'Structure model' '_database_2.pdbx_DOI'                
13 3 '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                        6YHB 
_pdbx_database_status.recvd_initial_deposition_date   2020-03-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 0000-0001-5080-9367 
'Manakova, E.' 2 0000-0002-6027-2265 
'Grazulis, S.' 3 0000-0002-7928-5218 
# 
_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            Chemistryopen 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2191-1363 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                567 
_citation.page_last                 580 
_citation.title                     'Switching the Inhibitor-Enzyme Recognition Profile via Chimeric Carbonic Anhydrase XII.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/open.202100042 
_citation.pdbx_database_id_PubMed   33945229 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnoviene, J.'   1  0000-0001-5503-4775 
primary 'Smirnov, A.'       2  ?                   
primary 'Zaksauskas, A.'    3  ?                   
primary 'Zubriene, A.'      4  0000-0001-5996-1883 
primary 'Petrauskas, V.'    5  0000-0001-7983-4128 
primary 'Mickeviciute, A.'  6  ?                   
primary 'Michailoviene, V.' 7  ?                   
primary 'Capkauskaite, E.'  8  ?                   
primary 'Manakova, E.'      9  0000-0002-6027-2265 
primary 'Grazulis, S.'      10 0000-0002-7928-5218 
primary 'Baranauskiene, L.' 11 0000-0002-9924-9177 
primary 'Chen, W.Y.'        12 ?                   
primary 'Ladbury, J.E.'     13 0000-0002-6328-7200 
primary 'Matulis, D.'       14 0000-0002-6178-6276 
# 
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'                                                       29220.879 1   4.2.1.1 
'A65S, N67K, I91T, F130A, V134S, L203N' ? ? 
2 non-polymer syn 'ZINC ION'                                                                   65.409    1   ?       ? ? ? 
3 non-polymer syn '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' 367.342   1   ?       ? ? ? 
4 water       nat water                                                                        18.015    116 ?       ? ? ? 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
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 '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' V50 
4 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  SER n 
1 66  PHE n 
1 67  LYS 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  THR 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 ALA n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 SER 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 ASN n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                      ? 'C3 H7 N O2'         
89.093  
ARG 'L-peptide linking' y ARGININE                                                                     ? 'C6 H15 N4 O2 1'     
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                   ? 'C4 H8 N2 O3'        
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                              ? 'C4 H7 N O4'         
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                     ? 'C3 H7 N O2 S'       
121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                    ? 'C5 H10 N2 O3'       
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                              ? 'C5 H9 N O4'         
147.129 
GLY 'peptide linking'   y GLYCINE                                                                      ? 'C2 H5 N O2'         
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                    ? 'C6 H10 N3 O2 1'     
156.162 
HOH non-polymer         . WATER                                                                        ? 'H2 O'               
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                   ? 'C6 H13 N O2'        
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                      ? 'C6 H13 N O2'        
131.173 
LYS 'L-peptide linking' y LYSINE                                                                       ? 'C6 H15 N2 O2 1'     
147.195 
MET 'L-peptide linking' y METHIONINE                                                                   ? 'C5 H11 N O2 S'      
149.211 
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 
V50 non-polymer         . '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' ? 'C12 H9 F4 N3 O2 S2' 
367.342 
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  SER 65  65  65  SER SER A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS 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  THR 91  91  91  THR THR 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 ALA 130 131 131 ALA ALA 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 SER 134 135 135 SER SER 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 ASN 203 204 204 ASN ASN 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 V50 1   302 1   V50 V50 A . 
D 4 HOH 1   401 67  HOH HOH A . 
D 4 HOH 2   402 71  HOH HOH A . 
D 4 HOH 3   403 66  HOH HOH A . 
D 4 HOH 4   404 11  HOH HOH A . 
D 4 HOH 5   405 4   HOH HOH A . 
D 4 HOH 6   406 79  HOH HOH A . 
D 4 HOH 7   407 64  HOH HOH A . 
D 4 HOH 8   408 110 HOH HOH A . 
D 4 HOH 9   409 76  HOH HOH A . 
D 4 HOH 10  410 44  HOH HOH A . 
D 4 HOH 11  411 83  HOH HOH A . 
D 4 HOH 12  412 48  HOH HOH A . 
D 4 HOH 13  413 31  HOH HOH A . 
D 4 HOH 14  414 100 HOH HOH A . 
D 4 HOH 15  415 116 HOH HOH A . 
D 4 HOH 16  416 58  HOH HOH A . 
D 4 HOH 17  417 54  HOH HOH A . 
D 4 HOH 18  418 21  HOH HOH A . 
D 4 HOH 19  419 3   HOH HOH A . 
D 4 HOH 20  420 30  HOH HOH A . 
D 4 HOH 21  421 46  HOH HOH A . 
D 4 HOH 22  422 47  HOH HOH A . 
D 4 HOH 23  423 61  HOH HOH A . 
D 4 HOH 24  424 16  HOH HOH A . 
D 4 HOH 25  425 56  HOH HOH A . 
D 4 HOH 26  426 45  HOH HOH A . 
D 4 HOH 27  427 86  HOH HOH A . 
D 4 HOH 28  428 33  HOH HOH A . 
D 4 HOH 29  429 112 HOH HOH A . 
D 4 HOH 30  430 15  HOH HOH A . 
D 4 HOH 31  431 41  HOH HOH A . 
D 4 HOH 32  432 27  HOH HOH A . 
D 4 HOH 33  433 36  HOH HOH A . 
D 4 HOH 34  434 6   HOH HOH A . 
D 4 HOH 35  435 63  HOH HOH A . 
D 4 HOH 36  436 37  HOH HOH A . 
D 4 HOH 37  437 29  HOH HOH A . 
D 4 HOH 38  438 85  HOH HOH A . 
D 4 HOH 39  439 65  HOH HOH A . 
D 4 HOH 40  440 106 HOH HOH A . 
D 4 HOH 41  441 13  HOH HOH A . 
D 4 HOH 42  442 59  HOH HOH A . 
D 4 HOH 43  443 26  HOH HOH A . 
D 4 HOH 44  444 89  HOH HOH A . 
D 4 HOH 45  445 14  HOH HOH A . 
D 4 HOH 46  446 92  HOH HOH A . 
D 4 HOH 47  447 7   HOH HOH A . 
D 4 HOH 48  448 5   HOH HOH A . 
D 4 HOH 49  449 20  HOH HOH A . 
D 4 HOH 50  450 49  HOH HOH A . 
D 4 HOH 51  451 24  HOH HOH A . 
D 4 HOH 52  452 38  HOH HOH A . 
D 4 HOH 53  453 25  HOH HOH A . 
D 4 HOH 54  454 40  HOH HOH A . 
D 4 HOH 55  455 10  HOH HOH A . 
D 4 HOH 56  456 42  HOH HOH A . 
D 4 HOH 57  457 8   HOH HOH A . 
D 4 HOH 58  458 52  HOH HOH A . 
D 4 HOH 59  459 1   HOH HOH A . 
D 4 HOH 60  460 9   HOH HOH A . 
D 4 HOH 61  461 94  HOH HOH A . 
D 4 HOH 62  462 78  HOH HOH A . 
D 4 HOH 63  463 93  HOH HOH A . 
D 4 HOH 64  464 84  HOH HOH A . 
D 4 HOH 65  465 43  HOH HOH A . 
D 4 HOH 66  466 80  HOH HOH A . 
D 4 HOH 67  467 101 HOH HOH A . 
D 4 HOH 68  468 62  HOH HOH A . 
D 4 HOH 69  469 39  HOH HOH A . 
D 4 HOH 70  470 88  HOH HOH A . 
D 4 HOH 71  471 19  HOH HOH A . 
D 4 HOH 72  472 108 HOH HOH A . 
D 4 HOH 73  473 68  HOH HOH A . 
D 4 HOH 74  474 35  HOH HOH A . 
D 4 HOH 75  475 22  HOH HOH A . 
D 4 HOH 76  476 69  HOH HOH A . 
D 4 HOH 77  477 57  HOH HOH A . 
D 4 HOH 78  478 51  HOH HOH A . 
D 4 HOH 79  479 2   HOH HOH A . 
D 4 HOH 80  480 72  HOH HOH A . 
D 4 HOH 81  481 102 HOH HOH A . 
D 4 HOH 82  482 96  HOH HOH A . 
D 4 HOH 83  483 23  HOH HOH A . 
D 4 HOH 84  484 60  HOH HOH A . 
D 4 HOH 85  485 77  HOH HOH A . 
D 4 HOH 86  486 70  HOH HOH A . 
D 4 HOH 87  487 28  HOH HOH A . 
D 4 HOH 88  488 12  HOH HOH A . 
D 4 HOH 89  489 81  HOH HOH A . 
D 4 HOH 90  490 99  HOH HOH A . 
D 4 HOH 91  491 32  HOH HOH A . 
D 4 HOH 92  492 91  HOH HOH A . 
D 4 HOH 93  493 103 HOH HOH A . 
D 4 HOH 94  494 50  HOH HOH A . 
D 4 HOH 95  495 98  HOH HOH A . 
D 4 HOH 96  496 53  HOH HOH A . 
D 4 HOH 97  497 18  HOH HOH A . 
D 4 HOH 98  498 34  HOH HOH A . 
D 4 HOH 99  499 113 HOH HOH A . 
D 4 HOH 100 500 109 HOH HOH A . 
D 4 HOH 101 501 107 HOH HOH A . 
D 4 HOH 102 502 55  HOH HOH A . 
D 4 HOH 103 503 104 HOH HOH A . 
D 4 HOH 104 504 105 HOH HOH A . 
D 4 HOH 105 505 87  HOH HOH A . 
D 4 HOH 106 506 73  HOH HOH A . 
D 4 HOH 107 507 17  HOH HOH A . 
D 4 HOH 108 508 115 HOH HOH A . 
D 4 HOH 109 509 111 HOH HOH A . 
D 4 HOH 110 510 75  HOH HOH A . 
D 4 HOH 111 511 95  HOH HOH A . 
D 4 HOH 112 512 90  HOH HOH A . 
D 4 HOH 113 513 82  HOH HOH A . 
D 4 HOH 114 514 114 HOH HOH A . 
D 4 HOH 115 515 97  HOH HOH A . 
D 4 HOH 116 516 74  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
3  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
4  1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
5  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
6  1 Y 1 A LYS 213 ? NZ  ? A LYS 212 NZ  
7  1 Y 1 A LEU 224 ? CD1 ? A LEU 223 CD1 
8  1 Y 1 A LEU 224 ? CD2 ? A LEU 223 CD2 
9  1 Y 1 A LYS 228 ? CE  ? A LYS 227 CE  
10 1 Y 1 A LYS 228 ? NZ  ? A LYS 227 NZ  
11 1 Y 1 A ASN 253 ? CG  ? A ASN 252 CG  
12 1 Y 1 A ASN 253 ? OD1 ? A ASN 252 OD1 
13 1 Y 1 A ASN 253 ? ND2 ? A ASN 252 ND2 
14 1 Y 1 A GLN 255 ? CD  ? A GLN 254 CD  
15 1 Y 1 A GLN 255 ? OE1 ? A GLN 254 OE1 
16 1 Y 1 A GLN 255 ? NE2 ? A GLN 254 NE2 
17 1 Y 1 A LYS 257 ? CE  ? A LYS 256 CE  
18 1 Y 1 A LYS 257 ? NZ  ? A LYS 256 NZ  
19 1 Y 1 A LYS 261 ? CG  ? A LYS 260 CG  
20 1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
21 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
22 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
# 
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       ? ? ? 3.2.19   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0189 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   103.500 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6YHB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.964 
_cell.length_a_esd                 ? 
_cell.length_b                     40.835 
_cell.length_b_esd                 ? 
_cell.length_c                     70.419 
_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                         6YHB 
_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                   6YHB 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.01 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         38.74 
_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              ? 
_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 was 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.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-11-30 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6YHB 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.650 
_reflns.d_resolution_low                 68.473 
_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                       27868 
_reflns.number_obs                       27868 
_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             99.000 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.800 
_reflns.pdbx_Rmerge_I_obs                0.058 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.058 
_reflns.pdbx_netI_over_av_sigmaI         8.300 
_reflns.pdbx_netI_over_sigmaI            18.300 
_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                  0.067 
_reflns.pdbx_Rpim_I_all                  0.025 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         189324 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_CC_star                     ? 
_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_CC_star 
_reflns_shell.pdbx_R_split 
1.650 1.740  ? 2.100  27973 ? ? ? 4057 99.100 ? ? ? ? 0.375 ? ? ? ? ? ? ? ? 6.900 0.375 ? ? 4.500  0.441 0.166 ? 1  1 ? ? ? 
1.740 1.840  ? 3.200  24676 ? ? ? 3778 98.500 ? ? ? ? 0.240 ? ? ? ? ? ? ? ? 6.500 0.240 ? ? 6.600  0.285 0.110 ? 2  1 ? ? ? 
1.840 1.970  ? 4.500  25205 ? ? ? 3615 99.400 ? ? ? ? 0.170 ? ? ? ? ? ? ? ? 7.000 0.170 ? ? 9.700  0.200 0.075 ? 3  1 ? ? ? 
1.970 2.130  ? 6.600  23207 ? ? ? 3380 99.500 ? ? ? ? 0.112 ? ? ? ? ? ? ? ? 6.900 0.112 ? ? 14.100 0.131 0.049 ? 4  1 ? ? ? 
2.130 2.330  ? 8.500  20527 ? ? ? 3089 98.400 ? ? ? ? 0.084 ? ? ? ? ? ? ? ? 6.600 0.084 ? ? 18.200 0.099 0.038 ? 5  1 ? ? ? 
2.330 2.610  ? 10.100 19589 ? ? ? 2794 99.100 ? ? ? ? 0.068 ? ? ? ? ? ? ? ? 7.000 0.068 ? ? 22.400 0.079 0.030 ? 6  1 ? ? ? 
2.610 3.010  ? 11.700 16302 ? ? ? 2464 98.800 ? ? ? ? 0.056 ? ? ? ? ? ? ? ? 6.600 0.056 ? ? 28.700 0.065 0.025 ? 7  1 ? ? ? 
3.010 3.690  ? 13.600 14972 ? ? ? 2117 99.200 ? ? ? ? 0.045 ? ? ? ? ? ? ? ? 7.100 0.045 ? ? 39.000 0.051 0.019 ? 8  1 ? ? ? 
3.690 5.220  ? 17.100 10855 ? ? ? 1639 98.700 ? ? ? ? 0.036 ? ? ? ? ? ? ? ? 6.600 0.036 ? ? 43.300 0.041 0.016 ? 9  1 ? ? ? 
5.220 68.473 ? 15.500 6018  ? ? ? 935  99.100 ? ? ? ? 0.035 ? ? ? ? ? ? ? ? 6.400 0.035 ? ? 44.100 0.040 0.016 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -2.1400 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.9600 
_refine.aniso_B[2][2]                            -2.6100 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            3.8500 
_refine.B_iso_max                                76.400 
_refine.B_iso_mean                               26.8540 
_refine.B_iso_min                                15.580 
_refine.correlation_coeff_Fo_to_Fc               0.9700 
_refine.correlation_coeff_Fo_to_Fc_free          0.9530 
_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                                 6YHB 
_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                            1.6500 
_refine.ls_d_res_low                             39.3200 
_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                     25088 
_refine.ls_number_reflns_R_free                  2762 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.7400 
_refine.ls_percent_reflns_R_free                 9.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1818 
_refine.ls_R_factor_R_free                       0.2228 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1773 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_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                      4Q09 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.1110 
_refine.pdbx_overall_ESU_R_Free                  0.1120 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_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             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.6500 
_refine_hist.d_res_low                        39.3200 
_refine_hist.number_atoms_solvent             116 
_refine_hist.number_atoms_total               2161 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       257 
_refine_hist.pdbx_B_iso_mean_ligand           41.74 
_refine_hist.pdbx_B_iso_mean_solvent          32.72 
_refine_hist.pdbx_number_atoms_protein        2021 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.019  2117 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.703  1.960  2883 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.464  5.000  259  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.912 24.688 96   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.983 15.000 338  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 18.155 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.119  0.200  299  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.021  1645 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.6500 
_refine_ls_shell.d_res_low                        1.6930 
_refine_ls_shell.number_reflns_all                2054 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             198 
_refine_ls_shell.number_reflns_R_work             1856 
_refine_ls_shell.percent_reflns_obs               98.8500 
_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                  0.3330 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.3040 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     6YHB 
_struct.title                        
;Crystal structure of chimeric carbonic anhydrase XII with 4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6YHB 
_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 ? 
# 
_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              6YHB 
_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 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 6YHB SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6YHB LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6YHB THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 6YHB ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 4 
1 6YHB SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 5 
1 6YHB ASN A 203 ? UNP P00918 LEU 203 'engineered mutation' 204 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   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)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  11340 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 HIS A 15  ? ASP A 19  ? HIS A 15  ASP A 19  5 ? 5 
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 ? SER A 134 ? ASP A 130 SER 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 ? ASP A 161 ? LEU A 157 ASP A 162 1 ? 6 
HELX_P HELX_P7 AA7 VAL A 162 ? LYS A 167 ? VAL A 163 LYS A 168 5 ? 6 
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 ? ? ? ? ? ? ? 1.943 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V50 . N23 ? ? A ZN  301 A V50 302 1_555 ? ? ? ? ? ? ? 1.942 ? ? 
# 
_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_555 100.9 ? 
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_555 118.4 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.6  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 ? C V50 .   ? A V50 302 ? 1_555 113.9 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 ? C V50 .   ? A V50 302 ? 1_555 111.7 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 ? C V50 .   ? A V50 302 ? 1_555 111.5 ? 
# 
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 3.52 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 9.60 
# 
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 ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 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 LYS A 148 ? N LYS A 149 O VAL A 217 ? O VAL A 218 
# 
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 V50 302 ? 11 'binding site for residue V50 A 302' 
# 
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  V50 C .   ? V50 A 302 . ? 1_555 ? 
5  AC2 11 GLN A 92  ? GLN A 92  . ? 1_555 ? 
6  AC2 11 HIS A 94  ? HIS A 94  . ? 1_555 ? 
7  AC2 11 HIS A 96  ? HIS A 96  . ? 1_555 ? 
8  AC2 11 HIS A 119 ? HIS A 119 . ? 1_555 ? 
9  AC2 11 VAL A 121 ? VAL A 121 . ? 1_555 ? 
10 AC2 11 LEU A 197 ? LEU A 198 . ? 1_555 ? 
11 AC2 11 THR A 198 ? THR A 199 . ? 1_555 ? 
12 AC2 11 THR A 199 ? THR A 200 . ? 1_555 ? 
13 AC2 11 PRO A 200 ? PRO A 201 . ? 1_555 ? 
14 AC2 11 TRP A 208 ? TRP A 209 . ? 1_555 ? 
15 AC2 11 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -141.62 17.81   
2 1 ARG A 27  ? ? -141.04 56.49   
3 1 LYS A 111 ? ? 79.46   -6.41   
4 1 PHE A 176 ? ? -150.79 79.48   
5 1 ASN A 244 ? ? -96.32  52.84   
6 1 LYS A 252 ? ? 55.72   -132.11 
# 
_pdbx_entry_details.entry_id                 6YHB 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
PHE N    N  N N 250 
PHE CA   C  N S 251 
PHE C    C  N N 252 
PHE O    O  N N 253 
PHE CB   C  N N 254 
PHE CG   C  Y N 255 
PHE CD1  C  Y N 256 
PHE CD2  C  Y N 257 
PHE CE1  C  Y N 258 
PHE CE2  C  Y N 259 
PHE CZ   C  Y N 260 
PHE OXT  O  N N 261 
PHE H    H  N N 262 
PHE H2   H  N N 263 
PHE HA   H  N N 264 
PHE HB2  H  N N 265 
PHE HB3  H  N N 266 
PHE HD1  H  N N 267 
PHE HD2  H  N N 268 
PHE HE1  H  N N 269 
PHE HE2  H  N N 270 
PHE HZ   H  N N 271 
PHE HXT  H  N N 272 
PRO N    N  N N 273 
PRO CA   C  N S 274 
PRO C    C  N N 275 
PRO O    O  N N 276 
PRO CB   C  N N 277 
PRO CG   C  N N 278 
PRO CD   C  N N 279 
PRO OXT  O  N N 280 
PRO H    H  N N 281 
PRO HA   H  N N 282 
PRO HB2  H  N N 283 
PRO HB3  H  N N 284 
PRO HG2  H  N N 285 
PRO HG3  H  N N 286 
PRO HD2  H  N N 287 
PRO HD3  H  N N 288 
PRO HXT  H  N N 289 
SER N    N  N N 290 
SER CA   C  N S 291 
SER C    C  N N 292 
SER O    O  N N 293 
SER CB   C  N N 294 
SER OG   O  N N 295 
SER OXT  O  N N 296 
SER H    H  N N 297 
SER H2   H  N N 298 
SER HA   H  N N 299 
SER HB2  H  N N 300 
SER HB3  H  N N 301 
SER HG   H  N N 302 
SER HXT  H  N N 303 
THR N    N  N N 304 
THR CA   C  N S 305 
THR C    C  N N 306 
THR O    O  N N 307 
THR CB   C  N R 308 
THR OG1  O  N N 309 
THR CG2  C  N N 310 
THR OXT  O  N N 311 
THR H    H  N N 312 
THR H2   H  N N 313 
THR HA   H  N N 314 
THR HB   H  N N 315 
THR HG1  H  N N 316 
THR HG21 H  N N 317 
THR HG22 H  N N 318 
THR HG23 H  N N 319 
THR HXT  H  N N 320 
TRP N    N  N N 321 
TRP CA   C  N S 322 
TRP C    C  N N 323 
TRP O    O  N N 324 
TRP CB   C  N N 325 
TRP CG   C  Y N 326 
TRP CD1  C  Y N 327 
TRP CD2  C  Y N 328 
TRP NE1  N  Y N 329 
TRP CE2  C  Y N 330 
TRP CE3  C  Y N 331 
TRP CZ2  C  Y N 332 
TRP CZ3  C  Y N 333 
TRP CH2  C  Y N 334 
TRP OXT  O  N N 335 
TRP H    H  N N 336 
TRP H2   H  N N 337 
TRP HA   H  N N 338 
TRP HB2  H  N N 339 
TRP HB3  H  N N 340 
TRP HD1  H  N N 341 
TRP HE1  H  N N 342 
TRP HE3  H  N N 343 
TRP HZ2  H  N N 344 
TRP HZ3  H  N N 345 
TRP HH2  H  N N 346 
TRP HXT  H  N N 347 
TYR N    N  N N 348 
TYR CA   C  N S 349 
TYR C    C  N N 350 
TYR O    O  N N 351 
TYR CB   C  N N 352 
TYR CG   C  Y N 353 
TYR CD1  C  Y N 354 
TYR CD2  C  Y N 355 
TYR CE1  C  Y N 356 
TYR CE2  C  Y N 357 
TYR CZ   C  Y N 358 
TYR OH   O  N N 359 
TYR OXT  O  N N 360 
TYR H    H  N N 361 
TYR H2   H  N N 362 
TYR HA   H  N N 363 
TYR HB2  H  N N 364 
TYR HB3  H  N N 365 
TYR HD1  H  N N 366 
TYR HD2  H  N N 367 
TYR HE1  H  N N 368 
TYR HE2  H  N N 369 
TYR HH   H  N N 370 
TYR HXT  H  N N 371 
V50 F13  F  N N 372 
V50 C4   C  Y N 373 
V50 C5   C  Y N 374 
V50 S7   S  N N 375 
V50 O9   O  N N 376 
V50 N23  N  N N 377 
V50 O8   O  N N 378 
V50 C6   C  Y N 379 
V50 F11  F  N N 380 
V50 C1   C  Y N 381 
V50 F10  F  N N 382 
V50 C3   C  Y N 383 
V50 F12  F  N N 384 
V50 C2   C  Y N 385 
V50 S14  S  N N 386 
V50 C15  C  Y N 387 
V50 N20  N  Y N 388 
V50 C19  C  Y N 389 
V50 C21  C  N N 390 
V50 C18  C  Y N 391 
V50 C17  C  Y N 392 
V50 N16  N  Y N 393 
V50 C22  C  N N 394 
V50 H1   H  N N 395 
V50 H2   H  N N 396 
V50 H3   H  N N 397 
V50 H4   H  N N 398 
V50 H5   H  N N 399 
V50 H6   H  N N 400 
V50 H7   H  N N 401 
V50 H8   H  N N 402 
V50 H9   H  N N 403 
VAL N    N  N N 404 
VAL CA   C  N S 405 
VAL C    C  N N 406 
VAL O    O  N N 407 
VAL CB   C  N N 408 
VAL CG1  C  N N 409 
VAL CG2  C  N N 410 
VAL OXT  O  N N 411 
VAL H    H  N N 412 
VAL H2   H  N N 413 
VAL HA   H  N N 414 
VAL HB   H  N N 415 
VAL HG11 H  N N 416 
VAL HG12 H  N N 417 
VAL HG13 H  N N 418 
VAL HG21 H  N N 419 
VAL HG22 H  N N 420 
VAL HG23 H  N N 421 
VAL HXT  H  N N 422 
ZN  ZN   ZN N N 423 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
V50 C21 C19  sing N N 358 
V50 C19 N20  doub Y N 359 
V50 C19 C18  sing Y N 360 
V50 N20 C15  sing Y N 361 
V50 C18 C17  doub Y N 362 
V50 S14 C15  sing N N 363 
V50 S14 C2   sing N N 364 
V50 C15 N16  doub Y N 365 
V50 F10 C1   sing N N 366 
V50 C17 N16  sing Y N 367 
V50 C17 C22  sing N N 368 
V50 C1  C2   doub Y N 369 
V50 C1  C6   sing Y N 370 
V50 C2  C3   sing Y N 371 
V50 F12 C3   sing N N 372 
V50 C3  C4   doub Y N 373 
V50 C6  F11  sing N N 374 
V50 C6  C5   doub Y N 375 
V50 C4  C5   sing Y N 376 
V50 C4  F13  sing N N 377 
V50 C5  S7   sing N N 378 
V50 N23 S7   sing N N 379 
V50 O8  S7   doub N N 380 
V50 S7  O9   doub N N 381 
V50 N23 H1   sing N N 382 
V50 N23 H2   sing N N 383 
V50 C21 H3   sing N N 384 
V50 C21 H4   sing N N 385 
V50 C21 H5   sing N N 386 
V50 C18 H6   sing N N 387 
V50 C22 H7   sing N N 388 
V50 C22 H8   sing N N 389 
V50 C22 H9   sing N N 390 
VAL N   CA   sing N N 391 
VAL N   H    sing N N 392 
VAL N   H2   sing N N 393 
VAL CA  C    sing N N 394 
VAL CA  CB   sing N N 395 
VAL CA  HA   sing N N 396 
VAL C   O    doub N N 397 
VAL C   OXT  sing N N 398 
VAL CB  CG1  sing N N 399 
VAL CB  CG2  sing N N 400 
VAL CB  HB   sing N N 401 
VAL CG1 HG11 sing N N 402 
VAL CG1 HG12 sing N N 403 
VAL CG1 HG13 sing N N 404 
VAL CG2 HG21 sing N N 405 
VAL CG2 HG22 sing N N 406 
VAL CG2 HG23 sing N N 407 
VAL OXT HXT  sing N N 408 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        V50 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   V50 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_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   4Q09 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6YHB 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.023830 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005722 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024489 
_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]   0.014604 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
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   ? 12.095  -0.448  7.701   1.00 44.30 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.791  0.067   8.143   1.00 39.40 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.995   -1.032  8.834   1.00 40.81 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 10.175  -2.203  8.507   1.00 40.73 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 9.970   0.551   6.948   1.00 40.26 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 9.152   1.710   7.370   1.00 33.91 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 9.537   2.464   8.437   1.00 31.57 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 8.015   2.250   6.868   1.00 41.79 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 8.677   3.455   8.603   1.00 45.47 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 7.717   3.338   7.647   1.00 47.50 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 9.050   -0.621  9.699   1.00 37.81 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 8.368   -1.539  10.602  1.00 30.19 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 7.340   -2.394  9.872   1.00 29.44 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.840   -2.019  8.811   1.00 30.96 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.750   -0.791  11.775  1.00 27.61 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 6.548   0.025   11.421  1.00 25.48 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 6.518   1.346   11.093  1.00 26.00 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 5.177   -0.431  11.409  1.00 27.14 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 5.222   1.750   10.883  1.00 26.63 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 4.378   0.681   11.067  1.00 26.82 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 4.554   -1.660  11.674  1.00 27.61 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.984   0.600   10.988  1.00 26.34 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 3.177   -1.748  11.568  1.00 25.91 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 2.410   -0.625  11.239  1.00 24.96 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 7.064   -3.561  10.463  1.00 26.03 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 6.073   -4.487  9.937   1.00 27.00 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.747   -5.573  10.946  1.00 24.63 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.748   -5.326  12.149  1.00 25.13 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 5.560   -6.800  10.447  1.00 24.73 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 5.113   -7.910  11.270  1.00 26.80 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 6.010   -9.131  11.074  1.00 29.90 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.758   -10.159 11.686  1.00 31.31 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.639   -8.212  10.959  1.00 24.84 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.706   -7.152  11.474  1.00 23.11 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 2.303   -7.152  12.810  1.00 22.36 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 2.278   -6.117  10.658  1.00 23.49 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 1.472   -6.141  13.283  1.00 21.94 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 1.426   -5.123  11.110  1.00 23.27 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 1.042   -5.130  12.444  1.00 23.42 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 0.210   -4.149  12.917  1.00 22.96 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 7.059   -9.004  10.238  1.00 31.56 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 8.031   -10.071 10.026  1.00 33.82 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.992   -10.311 11.198  1.00 34.26 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 9.054   -9.561  12.183  1.00 29.62 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.791   -11.371 11.047  1.00 35.54 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.789  -11.773 12.023  1.00 31.33 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.732  -10.606 12.297  1.00 27.52 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 12.212  -10.466 13.410  1.00 28.29 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.594  -12.957 11.469  1.00 35.36 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.754  -13.417 12.337  1.00 35.74 ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? 12.033  -9.816  11.266  1.00 27.13 ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? 13.125  -8.857  11.340  1.00 29.71 ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? 12.662  -7.438  11.683  1.00 29.23 ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? 13.501  -6.595  12.016  1.00 28.85 ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? 13.989  -8.944  10.070  1.00 30.34 ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? 14.737  -10.233 10.075  1.00 31.75 ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? 15.738  -10.487 10.996  1.00 34.32 ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? 14.545  -11.372 9.389   1.00 31.62 ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? 16.168  -11.719 10.836  1.00 36.06 ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? 15.450  -12.283 9.853   1.00 34.35 ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? 11.352  -7.159  11.580  1.00 27.27 ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? 10.889  -5.780  11.742  1.00 26.74 ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? 9.561   -5.739  12.506  1.00 25.08 ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? 8.845   -4.729  12.472  1.00 24.63 ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? 10.747  -5.073  10.390  1.00 26.33 ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? 9.666   -5.678  9.520   1.00 30.68 ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? 9.089   -6.695  9.866   1.00 32.85 ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? 9.408   -5.088  8.365   1.00 30.93 ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? 9.269   -6.851  13.189  1.00 25.71 ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? 7.966   -7.097  13.780  1.00 22.39 ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? 7.905   -6.563  15.201  1.00 23.40 ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? 8.804   -5.854  15.635  1.00 25.19 ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? 6.780   -6.818  15.909  1.00 22.94 ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? 6.538   -6.287  17.248  1.00 23.38 ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? 7.697   -6.255  18.227  1.00 24.37 ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? 7.775   -5.318  19.019  1.00 24.84 ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? 5.415   -7.203  17.734  1.00 23.76 ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? 4.570   -7.355  16.484  1.00 23.30 ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? 5.589   -7.479  15.359  1.00 23.02 ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? 8.578   -7.272  18.186  1.00 23.96 ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? 9.665   -7.318  19.153  1.00 24.69 ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? 10.744  -6.280  18.837  1.00 23.02 ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? 11.627  -6.036  19.656  1.00 20.74 ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? 10.279  -8.721  19.199  1.00 30.92 ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? 9.279   -9.804  19.614  1.00 39.06 ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? 8.458   -9.518  20.869  1.00 53.03 ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? 9.046   -9.032  21.865  1.00 56.18 ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? 7.216   -9.773  20.852  1.00 58.57 ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? 10.746  -5.758  17.607  1.00 21.60 ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? 11.722  -4.762  17.176  1.00 20.37 ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? 11.261  -3.319  17.377  1.00 22.14 ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? 12.086  -2.401  17.360  1.00 21.73 ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? 12.028  -4.988  15.696  1.00 20.54 ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? 12.809  -6.238  15.459  1.00 23.05 ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? 14.206  -6.266  15.486  1.00 24.30 ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? 12.410  -7.509  15.212  1.00 23.42 ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? 14.619  -7.505  15.241  1.00 24.04 ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? 13.543  -8.287  15.078  1.00 25.71 ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? 9.950   -3.104  17.588  1.00 23.96 ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? 9.372   -1.762  17.514  1.00 21.93 ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? 9.977   -0.790  18.524  1.00 20.59 ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? 10.021  0.421   18.279  1.00 21.05 ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? 7.844   -1.797  17.651  1.00 19.48 ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? 7.174   -2.472  16.503  1.00 19.88 ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? 7.725   -2.801  15.296  1.00 19.70 ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? 5.790   -2.851  16.435  1.00 20.48 ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? 6.797   -3.425  14.506  1.00 20.28 ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? 5.594   -3.440  15.168  1.00 20.14 ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? 4.713   -2.748  17.324  1.00 18.43 ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? 4.356   -3.929  14.760  1.00 18.80 ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? 3.490   -3.257  16.922  1.00 18.99 ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? 3.321   -3.822  15.657  1.00 20.48 ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? 10.395  -1.300  19.680  1.00 21.25 ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? 10.780  -0.396  20.745  1.00 21.11 ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? 12.020  0.409   20.351  1.00 21.32 ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? 12.322  1.423   20.967  1.00 19.17 ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? 11.035  -1.182  22.032  1.00 22.77 ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? 12.249  -2.035  21.925  1.00 24.63 ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? 13.452  -1.687  22.522  1.00 27.64 ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? 12.461  -3.200  21.272  1.00 24.16 ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? 14.353  -2.610  22.235  1.00 26.22 ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? 13.772  -3.548  21.489  1.00 24.72 ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? 12.740  -0.046  19.316  1.00 24.39 ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? 13.990  0.617   18.963  1.00 26.03 ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? 13.689  1.973   18.336  1.00 28.97 ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? 14.353  2.961   18.636  1.00 31.21 ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? 14.900  -0.271  18.104  1.00 24.11 ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? 15.547  -1.432  18.860  1.00 24.16 ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? 16.279  -2.350  17.884  1.00 24.25 ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? 15.394  -3.425  17.297  1.00 22.90 ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? 16.047  -4.097  16.141  1.00 26.31 ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 19  ? 12.668  2.023   17.486  1.00 25.73 ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 19  ? 12.256  3.299   16.946  1.00 27.32 ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 19  ? 11.230  3.980   17.841  1.00 26.42 ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 19  ? 11.143  5.201   17.798  1.00 25.67 ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 19  ? 11.663  3.142   15.557  1.00 31.17 ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 19  ? 12.746  3.017   14.516  1.00 37.56 ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 19  ? 13.562  3.944   14.420  1.00 38.88 ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 19  ? 12.793  1.961   13.870  1.00 45.68 ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 20  ? 10.502  3.206   18.674  1.00 23.53 ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 20  ? 9.367   3.750   19.403  1.00 21.28 ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 20  ? 9.470   3.247   20.830  1.00 22.45 ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 20  ? 8.858   2.243   21.193  1.00 23.25 ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 20  ? 8.052   3.376   18.703  1.00 23.73 ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 20  ? 7.988   3.808   17.252  1.00 24.44 ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 20  ? 7.691   5.121   16.915  1.00 28.68 ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 20  ? 8.272   2.920   16.232  1.00 26.51 ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 20  ? 7.661   5.519   15.580  1.00 27.86 ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 20  ? 8.239   3.310   14.899  1.00 28.77 ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 20  ? 7.940   4.618   14.581  1.00 28.36 ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 21  ? 10.351  3.864   21.637  1.00 22.45 ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 21  ? 10.630  3.379   22.984  1.00 23.59 ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 21  ? 9.399   3.241   23.879  1.00 23.61 ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 21  ? 9.460   2.509   24.855  1.00 22.62 ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 21  ? 11.535  4.464   23.619  1.00 25.97 ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 21  ? 12.025  5.316   22.476  1.00 25.81 ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 21  ? 11.179  5.022   21.259  1.00 24.80 ? 21  PRO A CD  1 
ATOM   158  N  N   . ILE A 1 22  ? 8.311   3.963   23.552  1.00 23.97 ? 22  ILE A N   1 
ATOM   159  C  CA  . ILE A 1 22  ? 7.076   3.866   24.318  1.00 23.94 ? 22  ILE A CA  1 
ATOM   160  C  C   . ILE A 1 22  ? 6.499   2.447   24.199  1.00 24.40 ? 22  ILE A C   1 
ATOM   161  O  O   . ILE A 1 22  ? 5.649   2.075   25.005  1.00 22.00 ? 22  ILE A O   1 
ATOM   162  C  CB  . ILE A 1 22  ? 6.072   4.960   23.897  1.00 24.09 ? 22  ILE A CB  1 
ATOM   163  C  CG1 . ILE A 1 22  ? 4.950   5.163   24.914  1.00 24.18 ? 22  ILE A CG1 1 
ATOM   164  C  CG2 . ILE A 1 22  ? 5.501   4.641   22.519  1.00 23.35 ? 22  ILE A CG2 1 
ATOM   165  C  CD1 . ILE A 1 22  ? 5.345   5.953   26.148  1.00 27.70 ? 22  ILE A CD1 1 
ATOM   166  N  N   . ALA A 1 23  ? 7.001   1.632   23.242  1.00 22.65 ? 23  ALA A N   1 
ATOM   167  C  CA  . ALA A 1 23  ? 6.591   0.227   23.110  1.00 24.42 ? 23  ALA A CA  1 
ATOM   168  C  C   . ALA A 1 23  ? 6.698   -0.512  24.438  1.00 26.77 ? 23  ALA A C   1 
ATOM   169  O  O   . ALA A 1 23  ? 6.024   -1.523  24.647  1.00 27.56 ? 23  ALA A O   1 
ATOM   170  C  CB  . ALA A 1 23  ? 7.392   -0.514  22.049  1.00 23.99 ? 23  ALA A CB  1 
ATOM   171  N  N   . LYS A 1 24  ? 7.584   -0.026  25.314  1.00 27.39 ? 24  LYS A N   1 
ATOM   172  C  CA  . LYS A 1 24  ? 7.798   -0.707  26.576  1.00 26.53 ? 24  LYS A CA  1 
ATOM   173  C  C   . LYS A 1 24  ? 7.212   0.134   27.709  1.00 27.39 ? 24  LYS A C   1 
ATOM   174  O  O   . LYS A 1 24  ? 7.600   -0.049  28.848  1.00 29.34 ? 24  LYS A O   1 
ATOM   175  C  CB  . LYS A 1 24  ? 9.297   -0.941  26.807  1.00 31.24 ? 24  LYS A CB  1 
ATOM   176  C  CG  . LYS A 1 24  ? 9.920   -2.030  25.942  1.00 30.27 ? 24  LYS A CG  1 
ATOM   177  C  CD  . LYS A 1 24  ? 11.431  -1.999  26.003  1.00 33.40 ? 24  LYS A CD  1 
ATOM   178  C  CE  . LYS A 1 24  ? 12.049  -3.253  25.415  1.00 35.55 ? 24  LYS A CE  1 
ATOM   179  N  NZ  . LYS A 1 24  ? 11.811  -4.437  26.274  1.00 36.85 ? 24  LYS A NZ  1 
ATOM   180  N  N   . GLY A 1 25  ? 6.253   1.020   27.402  1.00 27.18 ? 25  GLY A N   1 
ATOM   181  C  CA  . GLY A 1 25  ? 5.729   1.961   28.381  1.00 27.85 ? 25  GLY A CA  1 
ATOM   182  C  C   . GLY A 1 25  ? 4.623   1.361   29.253  1.00 27.37 ? 25  GLY A C   1 
ATOM   183  O  O   . GLY A 1 25  ? 4.389   0.149   29.236  1.00 27.38 ? 25  GLY A O   1 
ATOM   184  N  N   . GLU A 1 26  ? 3.948   2.236   30.009  1.00 26.86 ? 26  GLU A N   1 
ATOM   185  C  CA  . GLU A 1 26  ? 3.102   1.807   31.115  1.00 27.89 ? 26  GLU A CA  1 
ATOM   186  C  C   . GLU A 1 26  ? 1.658   1.559   30.672  1.00 25.60 ? 26  GLU A C   1 
ATOM   187  O  O   . GLU A 1 26  ? 0.852   1.087   31.480  1.00 24.97 ? 26  GLU A O   1 
ATOM   188  C  CB  . GLU A 1 26  ? 3.112   2.847   32.238  1.00 31.50 ? 26  GLU A CB  1 
ATOM   189  C  CG  . GLU A 1 26  ? 4.470   3.023   32.900  1.00 39.96 ? 26  GLU A CG  1 
ATOM   190  C  CD  . GLU A 1 26  ? 5.047   1.781   33.558  1.00 42.53 ? 26  GLU A CD  1 
ATOM   191  O  OE1 . GLU A 1 26  ? 4.466   1.323   34.566  1.00 50.36 ? 26  GLU A OE1 1 
ATOM   192  O  OE2 . GLU A 1 26  ? 6.073   1.268   33.061  1.00 50.83 ? 26  GLU A OE2 1 
ATOM   193  N  N   . ARG A 1 27  ? 1.295   1.905   29.427  1.00 20.98 ? 27  ARG A N   1 
ATOM   194  C  CA  . ARG A 1 27  ? -0.106  1.692   29.042  1.00 21.16 ? 27  ARG A CA  1 
ATOM   195  C  C   . ARG A 1 27  ? -0.188  1.193   27.590  1.00 21.13 ? 27  ARG A C   1 
ATOM   196  O  O   . ARG A 1 27  ? -0.906  1.762   26.779  1.00 19.89 ? 27  ARG A O   1 
ATOM   197  C  CB  . ARG A 1 27  ? -1.002  2.884   29.427  1.00 25.46 ? 27  ARG A CB  1 
ATOM   198  C  CG  . ARG A 1 27  ? -0.652  4.216   28.773  1.00 28.91 ? 27  ARG A CG  1 
ATOM   199  C  CD  . ARG A 1 27  ? -1.558  5.431   28.997  1.00 34.64 ? 27  ARG A CD  1 
ATOM   200  N  NE  . ARG A 1 27  ? -2.830  5.303   28.293  1.00 33.39 ? 27  ARG A NE  1 
ATOM   201  C  CZ  . ARG A 1 27  ? -3.606  6.329   27.958  1.00 30.87 ? 27  ARG A CZ  1 
ATOM   202  N  NH1 . ARG A 1 27  ? -3.239  7.566   28.264  1.00 27.51 ? 27  ARG A NH1 1 
ATOM   203  N  NH2 . ARG A 1 27  ? -4.748  6.120   27.318  1.00 27.97 ? 27  ARG A NH2 1 
ATOM   204  N  N   . GLN A 1 28  ? 0.493   0.078   27.295  1.00 20.63 ? 28  GLN A N   1 
ATOM   205  C  CA  . GLN A 1 28  ? 0.539   -0.422  25.920  1.00 21.25 ? 28  GLN A CA  1 
ATOM   206  C  C   . GLN A 1 28  ? -0.636  -1.365  25.653  1.00 21.05 ? 28  GLN A C   1 
ATOM   207  O  O   . GLN A 1 28  ? -1.153  -1.992  26.571  1.00 24.10 ? 28  GLN A O   1 
ATOM   208  C  CB  . GLN A 1 28  ? 1.889   -1.087  25.633  1.00 22.28 ? 28  GLN A CB  1 
ATOM   209  C  CG  . GLN A 1 28  ? 3.020   -0.072  25.528  1.00 20.22 ? 28  GLN A CG  1 
ATOM   210  C  CD  . GLN A 1 28  ? 2.878   0.757   24.283  1.00 21.19 ? 28  GLN A CD  1 
ATOM   211  O  OE1 . GLN A 1 28  ? 3.132   0.275   23.180  1.00 21.62 ? 28  GLN A OE1 1 
ATOM   212  N  NE2 . GLN A 1 28  ? 2.489   2.013   24.452  1.00 19.21 ? 28  GLN A NE2 1 
ATOM   213  N  N   . SER A 1 29  ? -1.026  -1.446  24.374  1.00 18.64 ? 29  SER A N   1 
ATOM   214  C  CA  . SER A 1 29  ? -2.101  -2.307  23.891  1.00 18.40 ? 29  SER A CA  1 
ATOM   215  C  C   . SER A 1 29  ? -1.592  -3.148  22.732  1.00 19.07 ? 29  SER A C   1 
ATOM   216  O  O   . SER A 1 29  ? -0.630  -2.742  22.063  1.00 17.63 ? 29  SER A O   1 
ATOM   217  C  CB  . SER A 1 29  ? -3.266  -1.439  23.431  1.00 18.65 ? 29  SER A CB  1 
ATOM   218  O  OG  . SER A 1 29  ? -3.787  -0.765  24.558  1.00 19.68 ? 29  SER A OG  1 
ATOM   219  N  N   . PRO A 1 30  ? -2.175  -4.349  22.473  1.00 19.52 ? 30  PRO A N   1 
ATOM   220  C  CA  . PRO A 1 30  ? -3.334  -4.854  23.215  1.00 20.91 ? 30  PRO A CA  1 
ATOM   221  C  C   . PRO A 1 30  ? -2.937  -5.550  24.509  1.00 21.11 ? 30  PRO A C   1 
ATOM   222  O  O   . PRO A 1 30  ? -1.740  -5.618  24.820  1.00 21.99 ? 30  PRO A O   1 
ATOM   223  C  CB  . PRO A 1 30  ? -3.903  -5.910  22.249  1.00 19.23 ? 30  PRO A CB  1 
ATOM   224  C  CG  . PRO A 1 30  ? -2.636  -6.470  21.592  1.00 21.35 ? 30  PRO A CG  1 
ATOM   225  C  CD  . PRO A 1 30  ? -1.734  -5.275  21.408  1.00 21.24 ? 30  PRO A CD  1 
ATOM   226  N  N   . VAL A 1 31  ? -3.950  -6.043  25.240  1.00 20.18 ? 31  VAL A N   1 
ATOM   227  C  CA  . VAL A 1 31  ? -3.788  -6.795  26.479  1.00 22.16 ? 31  VAL A CA  1 
ATOM   228  C  C   . VAL A 1 31  ? -4.667  -8.040  26.412  1.00 22.41 ? 31  VAL A C   1 
ATOM   229  O  O   . VAL A 1 31  ? -5.616  -8.132  25.626  1.00 19.88 ? 31  VAL A O   1 
ATOM   230  C  CB  . VAL A 1 31  ? -4.115  -5.998  27.761  1.00 22.47 ? 31  VAL A CB  1 
ATOM   231  C  CG1 . VAL A 1 31  ? -3.220  -4.776  27.904  1.00 24.26 ? 31  VAL A CG1 1 
ATOM   232  C  CG2 . VAL A 1 31  ? -5.604  -5.615  27.857  1.00 23.85 ? 31  VAL A CG2 1 
ATOM   233  N  N   . ASP A 1 32  ? -4.330  -9.009  27.270  1.00 22.57 ? 32  ASP A N   1 
ATOM   234  C  CA  . ASP A 1 32  ? -5.255  -10.102 27.482  1.00 22.48 ? 32  ASP A CA  1 
ATOM   235  C  C   . ASP A 1 32  ? -6.327  -9.591  28.436  1.00 22.12 ? 32  ASP A C   1 
ATOM   236  O  O   . ASP A 1 32  ? -6.019  -8.969  29.442  1.00 23.16 ? 32  ASP A O   1 
ATOM   237  C  CB  . ASP A 1 32  ? -4.555  -11.308 28.108  1.00 24.64 ? 32  ASP A CB  1 
ATOM   238  C  CG  . ASP A 1 32  ? -5.529  -12.449 28.367  1.00 28.04 ? 32  ASP A CG  1 
ATOM   239  O  OD1 . ASP A 1 32  ? -6.234  -12.873 27.408  1.00 25.80 ? 32  ASP A OD1 1 
ATOM   240  O  OD2 . ASP A 1 32  ? -5.615  -12.863 29.534  1.00 29.55 ? 32  ASP A OD2 1 
ATOM   241  N  N   . ILE A 1 33  ? -7.583  -9.864  28.107  1.00 23.46 ? 33  ILE A N   1 
ATOM   242  C  CA  . ILE A 1 33  ? -8.679  -9.488  28.981  1.00 24.07 ? 33  ILE A CA  1 
ATOM   243  C  C   . ILE A 1 33  ? -9.029  -10.702 29.836  1.00 24.74 ? 33  ILE A C   1 
ATOM   244  O  O   . ILE A 1 33  ? -9.575  -11.673 29.337  1.00 27.12 ? 33  ILE A O   1 
ATOM   245  C  CB  . ILE A 1 33  ? -9.878  -9.002  28.151  1.00 23.04 ? 33  ILE A CB  1 
ATOM   246  C  CG1 . ILE A 1 33  ? -9.493  -7.795  27.293  1.00 22.98 ? 33  ILE A CG1 1 
ATOM   247  C  CG2 . ILE A 1 33  ? -11.044 -8.690  29.075  1.00 24.17 ? 33  ILE A CG2 1 
ATOM   248  C  CD1 . ILE A 1 33  ? -10.562 -7.426  26.247  1.00 22.13 ? 33  ILE A CD1 1 
ATOM   249  N  N   . ASP A 1 34  ? -8.670  -10.629 31.119  1.00 27.35 ? 34  ASP A N   1 
ATOM   250  C  CA  . ASP A 1 34  ? -9.049  -11.641 32.088  1.00 29.46 ? 34  ASP A CA  1 
ATOM   251  C  C   . ASP A 1 34  ? -10.468 -11.323 32.567  1.00 28.34 ? 34  ASP A C   1 
ATOM   252  O  O   . ASP A 1 34  ? -10.681 -10.404 33.354  1.00 30.93 ? 34  ASP A O   1 
ATOM   253  C  CB  . ASP A 1 34  ? -8.016  -11.709 33.220  1.00 30.27 ? 34  ASP A CB  1 
ATOM   254  C  CG  . ASP A 1 34  ? -8.324  -12.777 34.266  1.00 39.54 ? 34  ASP A CG  1 
ATOM   255  O  OD1 . ASP A 1 34  ? -9.487  -13.235 34.349  1.00 39.35 ? 34  ASP A OD1 1 
ATOM   256  O  OD2 . ASP A 1 34  ? -7.400  -13.142 34.996  1.00 46.97 ? 34  ASP A OD2 1 
ATOM   257  N  N   . THR A 1 35  ? -11.431 -12.110 32.085  1.00 27.61 ? 35  THR A N   1 
ATOM   258  C  CA  . THR A 1 35  ? -12.852 -11.859 32.279  1.00 30.45 ? 35  THR A CA  1 
ATOM   259  C  C   . THR A 1 35  ? -13.233 -11.974 33.755  1.00 33.50 ? 35  THR A C   1 
ATOM   260  O  O   . THR A 1 35  ? -14.158 -11.302 34.207  1.00 32.12 ? 35  THR A O   1 
ATOM   261  C  CB  . THR A 1 35  ? -13.712 -12.796 31.418  1.00 33.22 ? 35  THR A CB  1 
ATOM   262  O  OG1 . THR A 1 35  ? -13.553 -14.145 31.861  1.00 31.63 ? 35  THR A OG1 1 
ATOM   263  C  CG2 . THR A 1 35  ? -13.391 -12.697 29.942  1.00 31.77 ? 35  THR A CG2 1 
ATOM   264  N  N   . HIS A 1 36  ? -12.519 -12.831 34.501  1.00 35.34 ? 36  HIS A N   1 
ATOM   265  C  CA  . HIS A 1 36  ? -12.856 -13.106 35.893  1.00 34.19 ? 36  HIS A CA  1 
ATOM   266  C  C   . HIS A 1 36  ? -12.232 -12.046 36.783  1.00 35.74 ? 36  HIS A C   1 
ATOM   267  O  O   . HIS A 1 36  ? -12.521 -11.945 37.977  1.00 41.46 ? 36  HIS A O   1 
ATOM   268  C  CB  . HIS A 1 36  ? -12.363 -14.499 36.291  1.00 31.87 ? 36  HIS A CB  1 
ATOM   269  C  CG  . HIS A 1 36  ? -12.904 -15.553 35.399  1.00 33.05 ? 36  HIS A CG  1 
ATOM   270  N  ND1 . HIS A 1 36  ? -14.208 -15.970 35.490  1.00 36.66 ? 36  HIS A ND1 1 
ATOM   271  C  CD2 . HIS A 1 36  ? -12.339 -16.231 34.374  1.00 33.84 ? 36  HIS A CD2 1 
ATOM   272  C  CE1 . HIS A 1 36  ? -14.444 -16.882 34.562  1.00 36.30 ? 36  HIS A CE1 1 
ATOM   273  N  NE2 . HIS A 1 36  ? -13.303 -17.059 33.866  1.00 40.35 ? 36  HIS A NE2 1 
ATOM   274  N  N   . THR A 1 37  ? -11.357 -11.255 36.182  1.00 32.45 ? 37  THR A N   1 
ATOM   275  C  CA  . THR A 1 37  ? -10.626 -10.266 36.945  1.00 32.67 ? 37  THR A CA  1 
ATOM   276  C  C   . THR A 1 37  ? -11.118 -8.852  36.589  1.00 29.44 ? 37  THR A C   1 
ATOM   277  O  O   . THR A 1 37  ? -10.849 -7.913  37.322  1.00 33.18 ? 37  THR A O   1 
ATOM   278  C  CB  . THR A 1 37  ? -9.146  -10.666 36.866  1.00 37.50 ? 37  THR A CB  1 
ATOM   279  O  OG1 . THR A 1 37  ? -8.716  -11.087 38.163  1.00 45.09 ? 37  THR A OG1 1 
ATOM   280  C  CG2 . THR A 1 37  ? -8.225  -9.626  36.286  1.00 35.44 ? 37  THR A CG2 1 
ATOM   281  N  N   . ALA A 1 38  ? -11.860 -8.689  35.488  1.00 29.56 ? 38  ALA A N   1 
ATOM   282  C  CA  . ALA A 1 38  ? -12.388 -7.369  35.132  1.00 28.30 ? 38  ALA A CA  1 
ATOM   283  C  C   . ALA A 1 38  ? -13.378 -6.868  36.191  1.00 29.16 ? 38  ALA A C   1 
ATOM   284  O  O   . ALA A 1 38  ? -14.149 -7.659  36.724  1.00 33.75 ? 38  ALA A O   1 
ATOM   285  C  CB  . ALA A 1 38  ? -13.040 -7.418  33.782  1.00 26.42 ? 38  ALA A CB  1 
ATOM   286  N  N   . LYS A 1 39  ? -13.351 -5.568  36.516  1.00 27.18 ? 39  LYS A N   1 
ATOM   287  C  CA  . LYS A 1 39  ? -14.264 -5.066  37.535  1.00 30.28 ? 39  LYS A CA  1 
ATOM   288  C  C   . LYS A 1 39  ? -15.541 -4.548  36.886  1.00 34.60 ? 39  LYS A C   1 
ATOM   289  O  O   . LYS A 1 39  ? -15.502 -3.639  36.044  1.00 31.54 ? 39  LYS A O   1 
ATOM   290  C  CB  . LYS A 1 39  ? -13.703 -4.014  38.494  1.00 32.10 ? 39  LYS A CB  1 
ATOM   291  C  CG  . LYS A 1 39  ? -14.421 -4.093  39.841  1.00 33.40 ? 39  LYS A CG  1 
ATOM   292  C  CD  . LYS A 1 39  ? -14.399 -2.891  40.734  1.00 39.95 ? 39  LYS A CD  1 
ATOM   293  C  CE  . LYS A 1 39  ? -15.678 -2.758  41.537  1.00 39.86 ? 39  LYS A CE  1 
ATOM   294  N  NZ  . LYS A 1 39  ? -15.754 -3.737  42.647  1.00 34.25 ? 39  LYS A NZ  1 
ATOM   295  N  N   . TYR A 1 40  ? -16.659 -5.150  37.310  1.00 34.30 ? 40  TYR A N   1 
ATOM   296  C  CA  . TYR A 1 40  ? -17.971 -4.658  36.930  1.00 39.17 ? 40  TYR A CA  1 
ATOM   297  C  C   . TYR A 1 40  ? -18.137 -3.274  37.527  1.00 37.54 ? 40  TYR A C   1 
ATOM   298  O  O   . TYR A 1 40  ? -18.073 -3.098  38.747  1.00 36.22 ? 40  TYR A O   1 
ATOM   299  C  CB  . TYR A 1 40  ? -19.106 -5.572  37.406  1.00 41.73 ? 40  TYR A CB  1 
ATOM   300  C  CG  . TYR A 1 40  ? -20.475 -4.957  37.243  1.00 43.80 ? 40  TYR A CG  1 
ATOM   301  C  CD1 . TYR A 1 40  ? -20.897 -4.475  36.012  1.00 41.15 ? 40  TYR A CD1 1 
ATOM   302  C  CD2 . TYR A 1 40  ? -21.350 -4.844  38.321  1.00 49.24 ? 40  TYR A CD2 1 
ATOM   303  C  CE1 . TYR A 1 40  ? -22.146 -3.900  35.846  1.00 44.97 ? 40  TYR A CE1 1 
ATOM   304  C  CE2 . TYR A 1 40  ? -22.609 -4.275  38.174  1.00 45.88 ? 40  TYR A CE2 1 
ATOM   305  C  CZ  . TYR A 1 40  ? -23.007 -3.801  36.929  1.00 49.73 ? 40  TYR A CZ  1 
ATOM   306  O  OH  . TYR A 1 40  ? -24.235 -3.230  36.750  1.00 48.38 ? 40  TYR A OH  1 
ATOM   307  N  N   . ASP A 1 41  ? -18.334 -2.302  36.642  1.00 34.28 ? 41  ASP A N   1 
ATOM   308  C  CA  . ASP A 1 41  ? -18.554 -0.952  37.108  1.00 38.29 ? 41  ASP A CA  1 
ATOM   309  C  C   . ASP A 1 41  ? -19.994 -0.518  36.792  1.00 43.91 ? 41  ASP A C   1 
ATOM   310  O  O   . ASP A 1 41  ? -20.274 -0.021  35.692  1.00 38.15 ? 41  ASP A O   1 
ATOM   311  C  CB  . ASP A 1 41  ? -17.428 -0.022  36.664  1.00 39.69 ? 41  ASP A CB  1 
ATOM   312  C  CG  . ASP A 1 41  ? -17.710 1.362   37.193  1.00 41.06 ? 41  ASP A CG  1 
ATOM   313  O  OD1 . ASP A 1 41  ? -18.810 1.522   37.748  1.00 38.67 ? 41  ASP A OD1 1 
ATOM   314  O  OD2 . ASP A 1 41  ? -16.846 2.246   37.045  1.00 44.07 ? 41  ASP A OD2 1 
ATOM   315  N  N   . PRO A 1 42  ? -20.942 -0.661  37.759  1.00 44.41 ? 42  PRO A N   1 
ATOM   316  C  CA  . PRO A 1 42  ? -22.353 -0.346  37.518  1.00 44.00 ? 42  PRO A CA  1 
ATOM   317  C  C   . PRO A 1 42  ? -22.540 1.144   37.237  1.00 42.14 ? 42  PRO A C   1 
ATOM   318  O  O   . PRO A 1 42  ? -23.597 1.539   36.746  1.00 40.56 ? 42  PRO A O   1 
ATOM   319  C  CB  . PRO A 1 42  ? -23.033 -0.735  38.847  1.00 46.36 ? 42  PRO A CB  1 
ATOM   320  C  CG  . PRO A 1 42  ? -21.929 -0.576  39.882  1.00 47.69 ? 42  PRO A CG  1 
ATOM   321  C  CD  . PRO A 1 42  ? -20.698 -1.083  39.155  1.00 45.37 ? 42  PRO A CD  1 
ATOM   322  N  N   . SER A 1 43  ? -21.498 1.947   37.536  1.00 39.34 ? 43  SER A N   1 
ATOM   323  C  CA  . SER A 1 43  ? -21.470 3.378   37.252  1.00 41.59 ? 43  SER A CA  1 
ATOM   324  C  C   . SER A 1 43  ? -21.165 3.710   35.777  1.00 42.72 ? 43  SER A C   1 
ATOM   325  O  O   . SER A 1 43  ? -21.257 4.868   35.372  1.00 45.35 ? 43  SER A O   1 
ATOM   326  C  CB  . SER A 1 43  ? -20.510 4.082   38.183  1.00 46.51 ? 43  SER A CB  1 
ATOM   327  O  OG  . SER A 1 43  ? -19.181 4.093   37.669  1.00 43.49 ? 43  SER A OG  1 
ATOM   328  N  N   . LEU A 1 44  ? -20.790 2.723   34.950  1.00 38.83 ? 44  LEU A N   1 
ATOM   329  C  CA  . LEU A 1 44  ? -20.516 3.012   33.543  1.00 37.13 ? 44  LEU A CA  1 
ATOM   330  C  C   . LEU A 1 44  ? -21.823 3.218   32.789  1.00 41.91 ? 44  LEU A C   1 
ATOM   331  O  O   . LEU A 1 44  ? -22.788 2.490   33.004  1.00 45.01 ? 44  LEU A O   1 
ATOM   332  C  CB  . LEU A 1 44  ? -19.766 1.840   32.913  1.00 33.87 ? 44  LEU A CB  1 
ATOM   333  C  CG  . LEU A 1 44  ? -18.266 1.775   33.190  1.00 31.27 ? 44  LEU A CG  1 
ATOM   334  C  CD1 . LEU A 1 44  ? -17.767 0.394   32.823  1.00 28.34 ? 44  LEU A CD1 1 
ATOM   335  C  CD2 . LEU A 1 44  ? -17.519 2.835   32.385  1.00 30.94 ? 44  LEU A CD2 1 
ATOM   336  N  N   . LYS A 1 45  ? -21.835 4.185   31.867  1.00 45.69 ? 45  LYS A N   1 
ATOM   337  C  CA  . LYS A 1 45  ? -23.023 4.393   31.054  1.00 45.38 ? 45  LYS A CA  1 
ATOM   338  C  C   . LYS A 1 45  ? -23.059 3.385   29.910  1.00 43.27 ? 45  LYS A C   1 
ATOM   339  O  O   . LYS A 1 45  ? -22.049 2.753   29.584  1.00 44.86 ? 45  LYS A O   1 
ATOM   340  C  CB  . LYS A 1 45  ? -23.087 5.825   30.534  1.00 45.57 ? 45  LYS A CB  1 
ATOM   341  C  CG  . LYS A 1 45  ? -23.188 6.869   31.629  1.00 50.32 ? 45  LYS A CG  1 
ATOM   342  C  CD  . LYS A 1 45  ? -23.109 8.270   31.077  1.00 57.55 ? 45  LYS A CD  1 
ATOM   343  C  CE  . LYS A 1 45  ? -22.605 9.267   32.098  1.00 59.80 ? 45  LYS A CE  1 
ATOM   344  N  NZ  . LYS A 1 45  ? -21.311 8.835   32.679  1.00 62.70 ? 45  LYS A NZ  1 
ATOM   345  N  N   . PRO A 1 46  ? -24.247 3.133   29.311  1.00 35.15 ? 46  PRO A N   1 
ATOM   346  C  CA  . PRO A 1 46  ? -24.301 2.476   28.003  1.00 36.17 ? 46  PRO A CA  1 
ATOM   347  C  C   . PRO A 1 46  ? -23.461 3.250   26.993  1.00 28.64 ? 46  PRO A C   1 
ATOM   348  O  O   . PRO A 1 46  ? -23.360 4.472   27.057  1.00 29.37 ? 46  PRO A O   1 
ATOM   349  C  CB  . PRO A 1 46  ? -25.809 2.487   27.670  1.00 37.30 ? 46  PRO A CB  1 
ATOM   350  C  CG  . PRO A 1 46  ? -26.458 2.424   29.052  1.00 38.10 ? 46  PRO A CG  1 
ATOM   351  C  CD  . PRO A 1 46  ? -25.579 3.327   29.903  1.00 38.07 ? 46  PRO A CD  1 
ATOM   352  N  N   . LEU A 1 47  ? -22.837 2.489   26.093  1.00 31.98 ? 47  LEU A N   1 
ATOM   353  C  CA  . LEU A 1 47  ? -22.164 3.029   24.932  1.00 29.42 ? 47  LEU A CA  1 
ATOM   354  C  C   . LEU A 1 47  ? -23.233 3.632   24.029  1.00 31.17 ? 47  LEU A C   1 
ATOM   355  O  O   . LEU A 1 47  ? -24.276 3.021   23.819  1.00 29.78 ? 47  LEU A O   1 
ATOM   356  C  CB  . LEU A 1 47  ? -21.440 1.868   24.244  1.00 33.78 ? 47  LEU A CB  1 
ATOM   357  C  CG  . LEU A 1 47  ? -20.216 2.256   23.430  1.00 39.33 ? 47  LEU A CG  1 
ATOM   358  C  CD1 . LEU A 1 47  ? -19.251 3.088   24.273  1.00 38.79 ? 47  LEU A CD1 1 
ATOM   359  C  CD2 . LEU A 1 47  ? -19.539 1.028   22.864  1.00 34.63 ? 47  LEU A CD2 1 
ATOM   360  N  N   . SER A 1 48  ? -23.001 4.865   23.562  1.00 28.70 ? 48  SER A N   1 
ATOM   361  C  CA  . SER A 1 48  ? -23.825 5.462   22.530  1.00 27.44 ? 48  SER A CA  1 
ATOM   362  C  C   . SER A 1 48  ? -23.040 5.420   21.217  1.00 27.97 ? 48  SER A C   1 
ATOM   363  O  O   . SER A 1 48  ? -22.018 6.076   21.088  1.00 27.14 ? 48  SER A O   1 
ATOM   364  C  CB  . SER A 1 48  ? -24.166 6.867   22.928  1.00 28.71 ? 48  SER A CB  1 
ATOM   365  O  OG  . SER A 1 48  ? -24.862 7.540   21.893  1.00 30.65 ? 48  SER A OG  1 
ATOM   366  N  N   . VAL A 1 49  ? -23.513 4.618   20.264  1.00 27.23 ? 49  VAL A N   1 
ATOM   367  C  CA  . VAL A 1 49  ? -22.913 4.544   18.942  1.00 28.55 ? 49  VAL A CA  1 
ATOM   368  C  C   . VAL A 1 49  ? -23.936 5.148   17.998  1.00 30.47 ? 49  VAL A C   1 
ATOM   369  O  O   . VAL A 1 49  ? -24.982 4.537   17.783  1.00 30.94 ? 49  VAL A O   1 
ATOM   370  C  CB  . VAL A 1 49  ? -22.641 3.076   18.559  1.00 32.03 ? 49  VAL A CB  1 
ATOM   371  C  CG1 . VAL A 1 49  ? -22.010 2.953   17.177  1.00 32.27 ? 49  VAL A CG1 1 
ATOM   372  C  CG2 . VAL A 1 49  ? -21.818 2.343   19.612  1.00 30.32 ? 49  VAL A CG2 1 
ATOM   373  N  N   . SER A 1 50  ? -23.666 6.362   17.507  1.00 26.32 ? 50  SER A N   1 
ATOM   374  C  CA  . SER A 1 50  ? -24.582 7.029   16.595  1.00 27.61 ? 50  SER A CA  1 
ATOM   375  C  C   . SER A 1 50  ? -23.954 7.094   15.214  1.00 26.08 ? 50  SER A C   1 
ATOM   376  O  O   . SER A 1 50  ? -23.240 8.043   14.940  1.00 24.99 ? 50  SER A O   1 
ATOM   377  C  CB  . SER A 1 50  ? -24.905 8.428   17.051  1.00 30.06 ? 50  SER A CB  1 
ATOM   378  O  OG  . SER A 1 50  ? -25.494 8.409   18.337  1.00 39.20 ? 50  SER A OG  1 
ATOM   379  N  N   . TYR A 1 51  ? -24.248 6.107   14.371  1.00 27.08 ? 51  TYR A N   1 
ATOM   380  C  CA  . TYR A 1 51  ? -23.586 5.965   13.075  1.00 26.34 ? 51  TYR A CA  1 
ATOM   381  C  C   . TYR A 1 51  ? -24.541 6.217   11.907  1.00 27.70 ? 51  TYR A C   1 
ATOM   382  O  O   . TYR A 1 51  ? -24.163 6.049   10.736  1.00 23.79 ? 51  TYR A O   1 
ATOM   383  C  CB  . TYR A 1 51  ? -22.997 4.563   12.923  1.00 25.63 ? 51  TYR A CB  1 
ATOM   384  C  CG  . TYR A 1 51  ? -21.713 4.272   13.668  1.00 25.91 ? 51  TYR A CG  1 
ATOM   385  C  CD1 . TYR A 1 51  ? -21.017 5.253   14.359  1.00 23.36 ? 51  TYR A CD1 1 
ATOM   386  C  CD2 . TYR A 1 51  ? -21.177 2.994   13.628  1.00 24.40 ? 51  TYR A CD2 1 
ATOM   387  C  CE1 . TYR A 1 51  ? -19.818 4.963   15.001  1.00 22.52 ? 51  TYR A CE1 1 
ATOM   388  C  CE2 . TYR A 1 51  ? -19.993 2.678   14.267  1.00 23.80 ? 51  TYR A CE2 1 
ATOM   389  C  CZ  . TYR A 1 51  ? -19.325 3.669   14.967  1.00 23.40 ? 51  TYR A CZ  1 
ATOM   390  O  OH  . TYR A 1 51  ? -18.148 3.331   15.554  1.00 21.45 ? 51  TYR A OH  1 
ATOM   391  N  N   . ASP A 1 52  ? -25.769 6.671   12.201  1.00 30.88 ? 52  ASP A N   1 
ATOM   392  C  CA  . ASP A 1 52  ? -26.764 6.859   11.143  1.00 33.52 ? 52  ASP A CA  1 
ATOM   393  C  C   . ASP A 1 52  ? -26.296 7.807   10.034  1.00 33.04 ? 52  ASP A C   1 
ATOM   394  O  O   . ASP A 1 52  ? -26.666 7.612   8.875   1.00 32.40 ? 52  ASP A O   1 
ATOM   395  C  CB  . ASP A 1 52  ? -28.143 7.290   11.658  1.00 38.32 ? 52  ASP A CB  1 
ATOM   396  C  CG  . ASP A 1 52  ? -28.083 8.380   12.711  1.00 47.57 ? 52  ASP A CG  1 
ATOM   397  O  OD1 . ASP A 1 52  ? -27.404 8.160   13.750  1.00 51.94 ? 52  ASP A OD1 1 
ATOM   398  O  OD2 . ASP A 1 52  ? -28.720 9.444   12.490  1.00 55.73 ? 52  ASP A OD2 1 
ATOM   399  N  N   . GLN A 1 53  ? -25.512 8.836   10.356  1.00 29.85 ? 53  GLN A N   1 
ATOM   400  C  CA  . GLN A 1 53  ? -25.147 9.757   9.276   1.00 30.26 ? 53  GLN A CA  1 
ATOM   401  C  C   . GLN A 1 53  ? -23.717 9.521   8.764   1.00 25.85 ? 53  GLN A C   1 
ATOM   402  O  O   . GLN A 1 53  ? -23.125 10.392  8.126   1.00 24.33 ? 53  GLN A O   1 
ATOM   403  C  CB  . GLN A 1 53  ? -25.344 11.228  9.661   1.00 33.12 ? 53  GLN A CB  1 
ATOM   404  C  CG  . GLN A 1 53  ? -26.795 11.666  9.861   1.00 34.34 ? 53  GLN A CG  1 
ATOM   405  C  CD  . GLN A 1 53  ? -27.660 11.491  8.635   1.00 39.60 ? 53  GLN A CD  1 
ATOM   406  O  OE1 . GLN A 1 53  ? -28.675 10.799  8.679   1.00 44.69 ? 53  GLN A OE1 1 
ATOM   407  N  NE2 . GLN A 1 53  ? -27.266 12.088  7.517   1.00 38.27 ? 53  GLN A NE2 1 
ATOM   408  N  N   . ALA A 1 54  ? -23.176 8.326   8.982   1.00 22.91 ? 54  ALA A N   1 
ATOM   409  C  CA  . ALA A 1 54  ? -21.786 8.068   8.630   1.00 21.36 ? 54  ALA A CA  1 
ATOM   410  C  C   . ALA A 1 54  ? -21.615 8.193   7.113   1.00 21.72 ? 54  ALA A C   1 
ATOM   411  O  O   . ALA A 1 54  ? -22.485 7.762   6.350   1.00 22.04 ? 54  ALA A O   1 
ATOM   412  C  CB  . ALA A 1 54  ? -21.385 6.686   9.084   1.00 23.84 ? 54  ALA A CB  1 
ATOM   413  N  N   . THR A 1 55  ? -20.482 8.762   6.707   1.00 21.25 ? 55  THR A N   1 
ATOM   414  C  CA  . THR A 1 55  ? -20.147 8.931   5.290   1.00 21.12 ? 55  THR A CA  1 
ATOM   415  C  C   . THR A 1 55  ? -18.763 8.344   4.981   1.00 21.55 ? 55  THR A C   1 
ATOM   416  O  O   . THR A 1 55  ? -17.739 8.984   5.216   1.00 21.95 ? 55  THR A O   1 
ATOM   417  C  CB  . THR A 1 55  ? -20.094 10.417  4.910   1.00 22.30 ? 55  THR A CB  1 
ATOM   418  O  OG1 . THR A 1 55  ? -21.369 11.009  5.166   1.00 25.61 ? 55  THR A OG1 1 
ATOM   419  C  CG2 . THR A 1 55  ? -19.724 10.631  3.450   1.00 24.19 ? 55  THR A CG2 1 
ATOM   420  N  N   . SER A 1 56  ? -18.728 7.127   4.418   1.00 19.43 ? 56  SER A N   1 
ATOM   421  C  CA  . SER A 1 56  ? -17.444 6.549   4.074   1.00 19.92 ? 56  SER A CA  1 
ATOM   422  C  C   . SER A 1 56  ? -16.988 7.199   2.766   1.00 20.63 ? 56  SER A C   1 
ATOM   423  O  O   . SER A 1 56  ? -17.819 7.649   1.969   1.00 20.69 ? 56  SER A O   1 
ATOM   424  C  CB  . SER A 1 56  ? -17.503 5.044   3.934   1.00 20.20 ? 56  SER A CB  1 
ATOM   425  O  OG  . SER A 1 56  ? -18.483 4.699   2.965   1.00 20.87 ? 56  SER A OG  1 
ATOM   426  N  N   . LEU A 1 57  ? -15.667 7.292   2.608   1.00 20.17 ? 57  LEU A N   1 
ATOM   427  C  CA  . LEU A 1 57  ? -15.126 7.934   1.423   1.00 20.83 ? 57  LEU A CA  1 
ATOM   428  C  C   . LEU A 1 57  ? -14.289 6.991   0.573   1.00 20.72 ? 57  LEU A C   1 
ATOM   429  O  O   . LEU A 1 57  ? -14.492 6.954   -0.635  1.00 21.66 ? 57  LEU A O   1 
ATOM   430  C  CB  . LEU A 1 57  ? -14.308 9.145   1.844   1.00 21.49 ? 57  LEU A CB  1 
ATOM   431  C  CG  . LEU A 1 57  ? -15.107 10.258  2.522   1.00 25.58 ? 57  LEU A CG  1 
ATOM   432  C  CD1 . LEU A 1 57  ? -14.156 11.290  3.109   1.00 25.20 ? 57  LEU A CD1 1 
ATOM   433  C  CD2 . LEU A 1 57  ? -16.076 10.903  1.522   1.00 27.19 ? 57  LEU A CD2 1 
ATOM   434  N  N   . ARG A 1 58  ? -13.325 6.289   1.177   1.00 21.16 ? 58  ARG A N   1 
ATOM   435  C  CA  . ARG A 1 58  ? -12.314 5.575   0.401   1.00 23.12 ? 58  ARG A CA  1 
ATOM   436  C  C   . ARG A 1 58  ? -11.868 4.337   1.164   1.00 21.27 ? 58  ARG A C   1 
ATOM   437  O  O   . ARG A 1 58  ? -11.978 4.278   2.387   1.00 20.81 ? 58  ARG A O   1 
ATOM   438  C  CB  . ARG A 1 58  ? -11.049 6.432   0.211   1.00 24.74 ? 58  ARG A CB  1 
ATOM   439  C  CG  . ARG A 1 58  ? -11.246 7.678   -0.646  1.00 31.18 ? 58  ARG A CG  1 
ATOM   440  C  CD  . ARG A 1 58  ? -9.932  8.309   -1.109  1.00 32.28 ? 58  ARG A CD  1 
ATOM   441  N  NE  . ARG A 1 58  ? -9.214  7.430   -2.033  1.00 36.94 ? 58  ARG A NE  1 
ATOM   442  C  CZ  . ARG A 1 58  ? -9.452  7.360   -3.342  1.00 41.47 ? 58  ARG A CZ  1 
ATOM   443  N  NH1 . ARG A 1 58  ? -8.755  6.538   -4.106  1.00 42.37 ? 58  ARG A NH1 1 
ATOM   444  N  NH2 . ARG A 1 58  ? -10.383 8.121   -3.893  1.00 43.43 ? 58  ARG A NH2 1 
ATOM   445  N  N   . ILE A 1 59  ? -11.340 3.365   0.429   1.00 20.42 ? 59  ILE A N   1 
ATOM   446  C  CA  . ILE A 1 59  ? -10.670 2.245   1.067   1.00 19.54 ? 59  ILE A CA  1 
ATOM   447  C  C   . ILE A 1 59  ? -9.240  2.155   0.512   1.00 21.08 ? 59  ILE A C   1 
ATOM   448  O  O   . ILE A 1 59  ? -9.003  2.365   -0.678  1.00 21.20 ? 59  ILE A O   1 
ATOM   449  C  CB  . ILE A 1 59  ? -11.522 0.966   0.888   1.00 18.97 ? 59  ILE A CB  1 
ATOM   450  C  CG1 . ILE A 1 59  ? -11.014 -0.194  1.756   1.00 18.56 ? 59  ILE A CG1 1 
ATOM   451  C  CG2 . ILE A 1 59  ? -11.617 0.555   -0.582  1.00 18.33 ? 59  ILE A CG2 1 
ATOM   452  C  CD1 . ILE A 1 59  ? -11.844 -1.472  1.630   1.00 18.98 ? 59  ILE A CD1 1 
ATOM   453  N  N   . LEU A 1 60  ? -8.280  1.798   1.359   1.00 21.64 ? 60  LEU A N   1 
ATOM   454  C  CA  . LEU A 1 60  ? -6.901  1.760   0.876   1.00 22.50 ? 60  LEU A CA  1 
ATOM   455  C  C   . LEU A 1 60  ? -6.100  0.672   1.579   1.00 23.24 ? 60  LEU A C   1 
ATOM   456  O  O   . LEU A 1 60  ? -6.329  0.349   2.748   1.00 21.20 ? 60  LEU A O   1 
ATOM   457  C  CB  . LEU A 1 60  ? -6.230  3.118   1.121   1.00 25.69 ? 60  LEU A CB  1 
ATOM   458  C  CG  . LEU A 1 60  ? -5.789  3.315   2.570   1.00 30.98 ? 60  LEU A CG  1 
ATOM   459  C  CD1 . LEU A 1 60  ? -4.565  4.211   2.697   1.00 36.37 ? 60  LEU A CD1 1 
ATOM   460  C  CD2 . LEU A 1 60  ? -6.938  3.810   3.431   1.00 36.73 ? 60  LEU A CD2 1 
ATOM   461  N  N   . ASN A 1 61  ? -5.088  0.186   0.862   1.00 19.78 ? 61  ASN A N   1 
ATOM   462  C  CA  . ASN A 1 61  ? -4.091  -0.716  1.422   1.00 20.77 ? 61  ASN A CA  1 
ATOM   463  C  C   . ASN A 1 61  ? -2.857  0.119   1.779   1.00 20.20 ? 61  ASN A C   1 
ATOM   464  O  O   . ASN A 1 61  ? -2.242  0.700   0.893   1.00 21.61 ? 61  ASN A O   1 
ATOM   465  C  CB  . ASN A 1 61  ? -3.763  -1.815  0.401   1.00 20.01 ? 61  ASN A CB  1 
ATOM   466  C  CG  . ASN A 1 61  ? -2.700  -2.794  0.829   1.00 20.42 ? 61  ASN A CG  1 
ATOM   467  O  OD1 . ASN A 1 61  ? -1.796  -2.464  1.602   1.00 22.83 ? 61  ASN A OD1 1 
ATOM   468  N  ND2 . ASN A 1 61  ? -2.777  -4.010  0.309   1.00 21.28 ? 61  ASN A ND2 1 
ATOM   469  N  N   . ASN A 1 62  ? -2.545  0.212   3.075   1.00 21.35 ? 62  ASN A N   1 
ATOM   470  C  CA  . ASN A 1 62  ? -1.415  1.027   3.530   1.00 23.79 ? 62  ASN A CA  1 
ATOM   471  C  C   . ASN A 1 62  ? -0.162  0.174   3.776   1.00 22.59 ? 62  ASN A C   1 
ATOM   472  O  O   . ASN A 1 62  ? 0.834   0.674   4.289   1.00 24.25 ? 62  ASN A O   1 
ATOM   473  C  CB  . ASN A 1 62  ? -1.763  1.873   4.768   1.00 25.93 ? 62  ASN A CB  1 
ATOM   474  C  CG  . ASN A 1 62  ? -2.126  1.023   5.965   1.00 27.90 ? 62  ASN A CG  1 
ATOM   475  O  OD1 . ASN A 1 62  ? -1.911  -0.175  5.960   1.00 24.91 ? 62  ASN A OD1 1 
ATOM   476  N  ND2 . ASN A 1 62  ? -2.710  1.624   6.992   1.00 32.76 ? 62  ASN A ND2 1 
ATOM   477  N  N   . GLY A 1 63  ? -0.193  -1.111  3.418   1.00 23.39 ? 63  GLY A N   1 
ATOM   478  C  CA  . GLY A 1 63  ? 0.948   -2.010  3.562   1.00 23.92 ? 63  GLY A CA  1 
ATOM   479  C  C   . GLY A 1 63  ? 1.028   -2.680  4.936   1.00 24.51 ? 63  GLY A C   1 
ATOM   480  O  O   . GLY A 1 63  ? 1.883   -3.545  5.174   1.00 26.71 ? 63  GLY A O   1 
ATOM   481  N  N   . HIS A 1 64  ? 0.106   -2.300  5.829   1.00 25.96 ? 64  HIS A N   1 
ATOM   482  C  CA  . HIS A 1 64  ? 0.033   -2.864  7.171   1.00 26.88 ? 64  HIS A CA  1 
ATOM   483  C  C   . HIS A 1 64  ? -1.332  -3.513  7.370   1.00 26.25 ? 64  HIS A C   1 
ATOM   484  O  O   . HIS A 1 64  ? -1.430  -4.575  7.970   1.00 28.23 ? 64  HIS A O   1 
ATOM   485  C  CB  . HIS A 1 64  ? 0.272   -1.785  8.230   1.00 32.13 ? 64  HIS A CB  1 
ATOM   486  C  CG  . HIS A 1 64  ? 1.526   -1.006  7.994   1.00 38.71 ? 64  HIS A CG  1 
ATOM   487  N  ND1 . HIS A 1 64  ? 2.788   -1.581  8.083   1.00 41.02 ? 64  HIS A ND1 1 
ATOM   488  C  CD2 . HIS A 1 64  ? 1.724   0.287   7.663   1.00 40.50 ? 64  HIS A CD2 1 
ATOM   489  C  CE1 . HIS A 1 64  ? 3.709   -0.671  7.833   1.00 41.30 ? 64  HIS A CE1 1 
ATOM   490  N  NE2 . HIS A 1 64  ? 3.081   0.482   7.560   1.00 38.48 ? 64  HIS A NE2 1 
ATOM   491  N  N   . SER A 1 65  ? -2.363  -2.841  6.867   1.00 22.63 ? 65  SER A N   1 
ATOM   492  C  CA  . SER A 1 65  ? -3.729  -3.334  6.912   1.00 24.32 ? 65  SER A CA  1 
ATOM   493  C  C   . SER A 1 65  ? -4.478  -2.719  5.743   1.00 21.36 ? 65  SER A C   1 
ATOM   494  O  O   . SER A 1 65  ? -3.847  -2.168  4.827   1.00 22.33 ? 65  SER A O   1 
ATOM   495  C  CB  . SER A 1 65  ? -4.343  -2.975  8.243   1.00 23.33 ? 65  SER A CB  1 
ATOM   496  O  OG  . SER A 1 65  ? -5.666  -3.476  8.302   1.00 31.09 ? 65  SER A OG  1 
ATOM   497  N  N   . PHE A 1 66  ? -5.809  -2.857  5.729   1.00 21.81 ? 66  PHE A N   1 
ATOM   498  C  CA  . PHE A 1 66  ? -6.579  -1.998  4.845   1.00 22.40 ? 66  PHE A CA  1 
ATOM   499  C  C   . PHE A 1 66  ? -7.517  -1.162  5.697   1.00 21.42 ? 66  PHE A C   1 
ATOM   500  O  O   . PHE A 1 66  ? -7.905  -1.611  6.765   1.00 21.73 ? 66  PHE A O   1 
ATOM   501  C  CB  . PHE A 1 66  ? -7.347  -2.792  3.795   1.00 22.90 ? 66  PHE A CB  1 
ATOM   502  C  CG  . PHE A 1 66  ? -8.497  -3.604  4.314   1.00 21.07 ? 66  PHE A CG  1 
ATOM   503  C  CD1 . PHE A 1 66  ? -9.772  -3.058  4.440   1.00 21.91 ? 66  PHE A CD1 1 
ATOM   504  C  CD2 . PHE A 1 66  ? -8.309  -4.936  4.660   1.00 22.79 ? 66  PHE A CD2 1 
ATOM   505  C  CE1 . PHE A 1 66  ? -10.819 -3.832  4.925   1.00 19.88 ? 66  PHE A CE1 1 
ATOM   506  C  CE2 . PHE A 1 66  ? -9.370  -5.712  5.108   1.00 21.37 ? 66  PHE A CE2 1 
ATOM   507  C  CZ  . PHE A 1 66  ? -10.626 -5.163  5.227   1.00 20.14 ? 66  PHE A CZ  1 
ATOM   508  N  N   . LYS A 1 67  ? -7.854  0.023   5.197   1.00 21.98 ? 67  LYS A N   1 
ATOM   509  C  CA  . LYS A 1 67  ? -8.489  1.034   6.020   1.00 24.15 ? 67  LYS A CA  1 
ATOM   510  C  C   . LYS A 1 67  ? -9.633  1.650   5.219   1.00 23.72 ? 67  LYS A C   1 
ATOM   511  O  O   . LYS A 1 67  ? -9.449  2.007   4.052   1.00 21.99 ? 67  LYS A O   1 
ATOM   512  C  CB  . LYS A 1 67  ? -7.401  2.066   6.342   1.00 27.91 ? 67  LYS A CB  1 
ATOM   513  C  CG  . LYS A 1 67  ? -7.737  3.153   7.347   1.00 36.37 ? 67  LYS A CG  1 
ATOM   514  C  CD  . LYS A 1 67  ? -6.541  4.100   7.624   1.00 37.33 ? 67  LYS A CD  1 
ATOM   515  C  CE  . LYS A 1 67  ? -6.231  5.028   6.465   1.00 37.63 ? 67  LYS A CE  1 
ATOM   516  N  NZ  . LYS A 1 67  ? -5.309  6.147   6.793   1.00 34.99 ? 67  LYS A NZ  1 
ATOM   517  N  N   . VAL A 1 68  ? -10.812 1.778   5.851   1.00 19.87 ? 68  VAL A N   1 
ATOM   518  C  CA  . VAL A 1 68  ? -11.899 2.551   5.232   1.00 19.21 ? 68  VAL A CA  1 
ATOM   519  C  C   . VAL A 1 68  ? -11.937 3.890   5.949   1.00 20.04 ? 68  VAL A C   1 
ATOM   520  O  O   . VAL A 1 68  ? -12.079 3.905   7.169   1.00 19.84 ? 68  VAL A O   1 
ATOM   521  C  CB  . VAL A 1 68  ? -13.260 1.834   5.381   1.00 19.44 ? 68  VAL A CB  1 
ATOM   522  C  CG1 . VAL A 1 68  ? -14.467 2.712   4.968   1.00 18.36 ? 68  VAL A CG1 1 
ATOM   523  C  CG2 . VAL A 1 68  ? -13.262 0.512   4.628   1.00 19.18 ? 68  VAL A CG2 1 
ATOM   524  N  N   . GLU A 1 69  ? -11.812 4.986   5.191   1.00 20.42 ? 69  GLU A N   1 
ATOM   525  C  CA  . GLU A 1 69  ? -11.782 6.333   5.744   1.00 22.81 ? 69  GLU A CA  1 
ATOM   526  C  C   . GLU A 1 69  ? -13.147 7.003   5.600   1.00 20.57 ? 69  GLU A C   1 
ATOM   527  O  O   . GLU A 1 69  ? -13.821 6.857   4.589   1.00 21.41 ? 69  GLU A O   1 
ATOM   528  C  CB  . GLU A 1 69  ? -10.709 7.179   5.060   1.00 28.92 ? 69  GLU A CB  1 
ATOM   529  C  CG  . GLU A 1 69  ? -9.326  6.576   5.243   1.00 35.82 ? 69  GLU A CG  1 
ATOM   530  C  CD  . GLU A 1 69  ? -8.175  7.564   5.308   1.00 42.01 ? 69  GLU A CD  1 
ATOM   531  O  OE1 . GLU A 1 69  ? -7.593  7.821   4.254   1.00 55.06 ? 69  GLU A OE1 1 
ATOM   532  O  OE2 . GLU A 1 69  ? -7.854  8.055   6.409   1.00 44.43 ? 69  GLU A OE2 1 
ATOM   533  N  N   . PHE A 1 70  ? -13.517 7.739   6.647   1.00 19.53 ? 70  PHE A N   1 
ATOM   534  C  CA  . PHE A 1 70  ? -14.793 8.425   6.764   1.00 18.77 ? 70  PHE A CA  1 
ATOM   535  C  C   . PHE A 1 70  ? -14.602 9.940   6.701   1.00 18.81 ? 70  PHE A C   1 
ATOM   536  O  O   . PHE A 1 70  ? -13.525 10.450  6.995   1.00 19.64 ? 70  PHE A O   1 
ATOM   537  C  CB  . PHE A 1 70  ? -15.445 8.051   8.109   1.00 18.22 ? 70  PHE A CB  1 
ATOM   538  C  CG  . PHE A 1 70  ? -16.091 6.698   8.026   1.00 17.87 ? 70  PHE A CG  1 
ATOM   539  C  CD1 . PHE A 1 70  ? -15.340 5.547   8.231   1.00 20.22 ? 70  PHE A CD1 1 
ATOM   540  C  CD2 . PHE A 1 70  ? -17.440 6.568   7.733   1.00 17.98 ? 70  PHE A CD2 1 
ATOM   541  C  CE1 . PHE A 1 70  ? -15.913 4.289   8.110   1.00 19.78 ? 70  PHE A CE1 1 
ATOM   542  C  CE2 . PHE A 1 70  ? -18.012 5.306   7.583   1.00 17.11 ? 70  PHE A CE2 1 
ATOM   543  C  CZ  . PHE A 1 70  ? -17.246 4.170   7.772   1.00 18.33 ? 70  PHE A CZ  1 
ATOM   544  N  N   A ASP A 1 71  ? -15.659 10.663  6.307   0.50 20.69 ? 71  ASP A N   1 
ATOM   545  N  N   B ASP A 1 71  ? -15.677 10.631  6.286   0.50 20.36 ? 71  ASP A N   1 
ATOM   546  C  CA  A ASP A 1 71  ? -15.643 12.117  6.337   0.50 20.12 ? 71  ASP A CA  1 
ATOM   547  C  CA  B ASP A 1 71  ? -15.805 12.071  6.432   0.50 19.73 ? 71  ASP A CA  1 
ATOM   548  C  C   A ASP A 1 71  ? -15.949 12.556  7.770   0.50 20.74 ? 71  ASP A C   1 
ATOM   549  C  C   B ASP A 1 71  ? -15.946 12.370  7.921   0.50 19.69 ? 71  ASP A C   1 
ATOM   550  O  O   A ASP A 1 71  ? -17.103 12.535  8.189   0.50 24.41 ? 71  ASP A O   1 
ATOM   551  O  O   B ASP A 1 71  ? -16.966 12.066  8.534   0.50 21.88 ? 71  ASP A O   1 
ATOM   552  C  CB  A ASP A 1 71  ? -16.596 12.666  5.270   0.50 20.95 ? 71  ASP A CB  1 
ATOM   553  C  CB  B ASP A 1 71  ? -17.020 12.592  5.661   0.50 20.39 ? 71  ASP A CB  1 
ATOM   554  C  CG  A ASP A 1 71  ? -16.579 14.180  5.136   0.50 21.51 ? 71  ASP A CG  1 
ATOM   555  C  CG  B ASP A 1 71  ? -17.268 14.079  5.883   0.50 21.46 ? 71  ASP A CG  1 
ATOM   556  O  OD1 A ASP A 1 71  ? -15.813 14.826  5.871   0.50 22.07 ? 71  ASP A OD1 1 
ATOM   557  O  OD1 B ASP A 1 71  ? -16.375 14.739  6.457   0.50 21.59 ? 71  ASP A OD1 1 
ATOM   558  O  OD2 A ASP A 1 71  ? -17.355 14.699  4.310   0.50 22.52 ? 71  ASP A OD2 1 
ATOM   559  O  OD2 B ASP A 1 71  ? -18.353 14.562  5.489   0.50 20.15 ? 71  ASP A OD2 1 
ATOM   560  N  N   . ASP A 1 72  ? -14.899 12.938  8.504   1.00 19.47 ? 72  ASP A N   1 
ATOM   561  C  CA  . ASP A 1 72  ? -14.961 13.284  9.923   1.00 21.75 ? 72  ASP A CA  1 
ATOM   562  C  C   . ASP A 1 72  ? -14.896 14.805  10.092  1.00 20.96 ? 72  ASP A C   1 
ATOM   563  O  O   . ASP A 1 72  ? -14.477 15.270  11.140  1.00 21.65 ? 72  ASP A O   1 
ATOM   564  C  CB  . ASP A 1 72  ? -13.862 12.591  10.747  1.00 21.52 ? 72  ASP A CB  1 
ATOM   565  C  CG  . ASP A 1 72  ? -12.430 12.904  10.326  1.00 25.85 ? 72  ASP A CG  1 
ATOM   566  O  OD1 . ASP A 1 72  ? -12.239 13.621  9.303   1.00 26.05 ? 72  ASP A OD1 1 
ATOM   567  O  OD2 . ASP A 1 72  ? -11.498 12.426  11.006  1.00 26.79 ? 72  ASP A OD2 1 
ATOM   568  N  N   . SER A 1 73  ? -15.234 15.562  9.038   1.00 21.80 ? 73  SER A N   1 
ATOM   569  C  CA  . SER A 1 73  ? -15.281 17.030  9.055   1.00 23.69 ? 73  SER A CA  1 
ATOM   570  C  C   . SER A 1 73  ? -16.585 17.609  9.644   1.00 26.06 ? 73  SER A C   1 
ATOM   571  O  O   . SER A 1 73  ? -16.700 18.836  9.776   1.00 26.57 ? 73  SER A O   1 
ATOM   572  C  CB  . SER A 1 73  ? -15.028 17.592  7.655   1.00 24.09 ? 73  SER A CB  1 
ATOM   573  O  OG  . SER A 1 73  ? -16.157 17.398  6.825   1.00 25.34 ? 73  SER A OG  1 
ATOM   574  N  N   . GLN A 1 74  ? -17.569 16.770  9.996   1.00 26.64 ? 74  GLN A N   1 
ATOM   575  C  CA  . GLN A 1 74  ? -18.711 17.185  10.820  1.00 31.63 ? 74  GLN A CA  1 
ATOM   576  C  C   . GLN A 1 74  ? -19.084 16.056  11.773  1.00 31.31 ? 74  GLN A C   1 
ATOM   577  O  O   . GLN A 1 74  ? -18.581 14.949  11.614  1.00 27.47 ? 74  GLN A O   1 
ATOM   578  C  CB  . GLN A 1 74  ? -19.955 17.490  9.982   1.00 37.05 ? 74  GLN A CB  1 
ATOM   579  C  CG  . GLN A 1 74  ? -19.713 18.404  8.795   1.00 42.48 ? 74  GLN A CG  1 
ATOM   580  C  CD  . GLN A 1 74  ? -20.465 17.969  7.557   1.00 44.46 ? 74  GLN A CD  1 
ATOM   581  O  OE1 . GLN A 1 74  ? -21.693 18.002  7.511   1.00 39.23 ? 74  GLN A OE1 1 
ATOM   582  N  NE2 . GLN A 1 74  ? -19.725 17.557  6.536   1.00 49.88 ? 74  GLN A NE2 1 
ATOM   583  N  N   . ASP A 1 75  ? -20.014 16.316  12.710  1.00 33.29 ? 75  ASP A N   1 
ATOM   584  C  CA  . ASP A 1 75  ? -20.400 15.308  13.686  1.00 37.13 ? 75  ASP A CA  1 
ATOM   585  C  C   . ASP A 1 75  ? -21.352 14.264  13.088  1.00 40.28 ? 75  ASP A C   1 
ATOM   586  O  O   . ASP A 1 75  ? -22.524 14.216  13.439  1.00 45.55 ? 75  ASP A O   1 
ATOM   587  C  CB  . ASP A 1 75  ? -21.027 15.947  14.931  1.00 43.41 ? 75  ASP A CB  1 
ATOM   588  C  CG  . ASP A 1 75  ? -20.029 16.406  15.988  1.00 46.41 ? 75  ASP A CG  1 
ATOM   589  O  OD1 . ASP A 1 75  ? -18.819 16.111  15.832  1.00 43.44 ? 75  ASP A OD1 1 
ATOM   590  O  OD2 . ASP A 1 75  ? -20.475 17.042  16.984  1.00 45.35 ? 75  ASP A OD2 1 
ATOM   591  N  N   . LYS A 1 76  ? -20.845 13.369  12.243  1.00 33.34 ? 76  LYS A N   1 
ATOM   592  C  CA  . LYS A 1 76  ? -21.715 12.464  11.506  1.00 35.12 ? 76  LYS A CA  1 
ATOM   593  C  C   . LYS A 1 76  ? -21.812 11.090  12.172  1.00 37.53 ? 76  LYS A C   1 
ATOM   594  O  O   . LYS A 1 76  ? -22.857 10.449  12.149  1.00 44.95 ? 76  LYS A O   1 
ATOM   595  C  CB  . LYS A 1 76  ? -21.196 12.309  10.080  1.00 34.58 ? 76  LYS A CB  1 
ATOM   596  C  CG  . LYS A 1 76  ? -21.459 13.519  9.211   1.00 33.58 ? 76  LYS A CG  1 
ATOM   597  C  CD  . LYS A 1 76  ? -20.927 13.286  7.843   1.00 35.83 ? 76  LYS A CD  1 
ATOM   598  C  CE  . LYS A 1 76  ? -21.645 14.142  6.832   1.00 35.01 ? 76  LYS A CE  1 
ATOM   599  N  NZ  . LYS A 1 76  ? -21.201 13.769  5.478   1.00 37.55 ? 76  LYS A NZ  1 
ATOM   600  N  N   . ALA A 1 77  ? -20.706 10.606  12.713  1.00 32.79 ? 77  ALA A N   1 
ATOM   601  C  CA  . ALA A 1 77  ? -20.673 9.248   13.232  1.00 29.40 ? 77  ALA A CA  1 
ATOM   602  C  C   . ALA A 1 77  ? -19.869 9.322   14.511  1.00 26.75 ? 77  ALA A C   1 
ATOM   603  O  O   . ALA A 1 77  ? -18.658 9.484   14.467  1.00 30.37 ? 77  ALA A O   1 
ATOM   604  C  CB  . ALA A 1 77  ? -20.015 8.317   12.247  1.00 28.21 ? 77  ALA A CB  1 
ATOM   605  N  N   . VAL A 1 78  ? -20.558 9.300   15.640  1.00 26.51 ? 78  VAL A N   1 
ATOM   606  C  CA  . VAL A 1 78  ? -19.859 9.642   16.859  1.00 26.59 ? 78  VAL A CA  1 
ATOM   607  C  C   . VAL A 1 78  ? -20.132 8.555   17.894  1.00 25.05 ? 78  VAL A C   1 
ATOM   608  O  O   . VAL A 1 78  ? -21.155 7.871   17.866  1.00 25.76 ? 78  VAL A O   1 
ATOM   609  C  CB  . VAL A 1 78  ? -20.209 11.066  17.337  1.00 30.21 ? 78  VAL A CB  1 
ATOM   610  C  CG1 . VAL A 1 78  ? -20.124 12.094  16.206  1.00 31.55 ? 78  VAL A CG1 1 
ATOM   611  C  CG2 . VAL A 1 78  ? -21.566 11.129  18.012  1.00 33.12 ? 78  VAL A CG2 1 
ATOM   612  N  N   . LEU A 1 79  ? -19.166 8.404   18.787  1.00 24.45 ? 79  LEU A N   1 
ATOM   613  C  CA  . LEU A 1 79  ? -19.269 7.511   19.909  1.00 24.38 ? 79  LEU A CA  1 
ATOM   614  C  C   . LEU A 1 79  ? -19.288 8.408   21.138  1.00 25.83 ? 79  LEU A C   1 
ATOM   615  O  O   . LEU A 1 79  ? -18.469 9.328   21.249  1.00 25.77 ? 79  LEU A O   1 
ATOM   616  C  CB  . LEU A 1 79  ? -17.992 6.670   19.851  1.00 23.36 ? 79  LEU A CB  1 
ATOM   617  C  CG  . LEU A 1 79  ? -17.849 5.519   20.832  1.00 25.99 ? 79  LEU A CG  1 
ATOM   618  C  CD1 . LEU A 1 79  ? -18.927 4.468   20.611  1.00 26.14 ? 79  LEU A CD1 1 
ATOM   619  C  CD2 . LEU A 1 79  ? -16.464 4.902   20.689  1.00 25.63 ? 79  LEU A CD2 1 
ATOM   620  N  N   . LYS A 1 80  ? -20.229 8.156   22.046  1.00 25.96 ? 80  LYS A N   1 
ATOM   621  C  CA  . LYS A 1 80  ? -20.144 8.823   23.331  1.00 28.12 ? 80  LYS A CA  1 
ATOM   622  C  C   . LYS A 1 80  ? -20.629 7.890   24.430  1.00 26.52 ? 80  LYS A C   1 
ATOM   623  O  O   . LYS A 1 80  ? -20.987 6.743   24.173  1.00 24.95 ? 80  LYS A O   1 
ATOM   624  C  CB  . LYS A 1 80  ? -20.865 10.174  23.335  1.00 31.77 ? 80  LYS A CB  1 
ATOM   625  C  CG  . LYS A 1 80  ? -22.376 10.143  23.154  1.00 36.12 ? 80  LYS A CG  1 
ATOM   626  C  CD  . LYS A 1 80  ? -23.010 11.533  23.201  1.00 40.82 ? 80  LYS A CD  1 
ATOM   627  N  N   . GLY A 1 81  ? -20.641 8.437   25.645  1.00 29.75 ? 81  GLY A N   1 
ATOM   628  C  CA  . GLY A 1 81  ? -21.091 7.713   26.812  1.00 27.54 ? 81  GLY A CA  1 
ATOM   629  C  C   . GLY A 1 81  ? -20.069 6.637   27.149  1.00 28.40 ? 81  GLY A C   1 
ATOM   630  O  O   . GLY A 1 81  ? -18.882 6.826   26.926  1.00 27.87 ? 81  GLY A O   1 
ATOM   631  N  N   . GLY A 1 82  ? -20.559 5.483   27.604  1.00 30.72 ? 82  GLY A N   1 
ATOM   632  C  CA  . GLY A 1 82  ? -19.683 4.488   28.193  1.00 28.06 ? 82  GLY A CA  1 
ATOM   633  C  C   . GLY A 1 82  ? -18.757 5.155   29.189  1.00 31.53 ? 82  GLY A C   1 
ATOM   634  O  O   . GLY A 1 82  ? -19.212 5.961   30.005  1.00 34.10 ? 82  GLY A O   1 
ATOM   635  N  N   . PRO A 1 83  ? -17.432 4.886   29.099  1.00 28.13 ? 83  PRO A N   1 
ATOM   636  C  CA  . PRO A 1 83  ? -16.435 5.514   29.971  1.00 28.30 ? 83  PRO A CA  1 
ATOM   637  C  C   . PRO A 1 83  ? -15.983 6.886   29.474  1.00 30.36 ? 83  PRO A C   1 
ATOM   638  O  O   . PRO A 1 83  ? -15.102 7.501   30.069  1.00 30.83 ? 83  PRO A O   1 
ATOM   639  C  CB  . PRO A 1 83  ? -15.243 4.557   29.819  1.00 28.75 ? 83  PRO A CB  1 
ATOM   640  C  CG  . PRO A 1 83  ? -15.344 4.120   28.361  1.00 24.55 ? 83  PRO A CG  1 
ATOM   641  C  CD  . PRO A 1 83  ? -16.825 3.969   28.119  1.00 26.40 ? 83  PRO A CD  1 
ATOM   642  N  N   . LEU A 1 84  ? -16.597 7.373   28.388  1.00 30.43 ? 84  LEU A N   1 
ATOM   643  C  CA  . LEU A 1 84  ? -16.036 8.536   27.722  1.00 27.89 ? 84  LEU A CA  1 
ATOM   644  C  C   . LEU A 1 84  ? -16.718 9.771   28.292  1.00 31.16 ? 84  LEU A C   1 
ATOM   645  O  O   . LEU A 1 84  ? -17.877 9.704   28.679  1.00 31.22 ? 84  LEU A O   1 
ATOM   646  C  CB  . LEU A 1 84  ? -16.281 8.468   26.212  1.00 23.42 ? 84  LEU A CB  1 
ATOM   647  C  CG  . LEU A 1 84  ? -15.764 7.223   25.492  1.00 24.85 ? 84  LEU A CG  1 
ATOM   648  C  CD1 . LEU A 1 84  ? -16.135 7.318   24.007  1.00 22.29 ? 84  LEU A CD1 1 
ATOM   649  C  CD2 . LEU A 1 84  ? -14.246 7.067   25.660  1.00 22.56 ? 84  LEU A CD2 1 
ATOM   650  N  N   . ASP A 1 85  ? -15.946 10.860  28.333  1.00 37.29 ? 85  ASP A N   1 
ATOM   651  C  CA  . ASP A 1 85  ? -16.383 12.223  28.582  1.00 37.88 ? 85  ASP A CA  1 
ATOM   652  C  C   . ASP A 1 85  ? -16.355 12.920  27.234  1.00 39.64 ? 85  ASP A C   1 
ATOM   653  O  O   . ASP A 1 85  ? -15.381 12.796  26.488  1.00 46.86 ? 85  ASP A O   1 
ATOM   654  C  CB  . ASP A 1 85  ? -15.363 12.940  29.478  1.00 41.12 ? 85  ASP A CB  1 
ATOM   655  C  CG  . ASP A 1 85  ? -15.374 12.481  30.932  1.00 50.89 ? 85  ASP A CG  1 
ATOM   656  O  OD1 . ASP A 1 85  ? -16.482 12.175  31.444  1.00 53.83 ? 85  ASP A OD1 1 
ATOM   657  O  OD2 . ASP A 1 85  ? -14.274 12.433  31.555  1.00 50.82 ? 85  ASP A OD2 1 
ATOM   658  N  N   . GLY A 1 86  ? -17.423 13.632  26.899  1.00 38.83 ? 86  GLY A N   1 
ATOM   659  C  CA  . GLY A 1 86  ? -17.443 14.280  25.597  1.00 37.27 ? 86  GLY A CA  1 
ATOM   660  C  C   . GLY A 1 86  ? -17.742 13.323  24.439  1.00 38.83 ? 86  GLY A C   1 
ATOM   661  O  O   . GLY A 1 86  ? -18.292 12.233  24.631  1.00 38.62 ? 86  GLY A O   1 
ATOM   662  N  N   . THR A 1 87  ? -17.363 13.758  23.230  1.00 35.00 ? 87  THR A N   1 
ATOM   663  C  CA  . THR A 1 87  ? -17.831 13.184  21.975  1.00 31.02 ? 87  THR A CA  1 
ATOM   664  C  C   . THR A 1 87  ? -16.611 12.784  21.154  1.00 27.22 ? 87  THR A C   1 
ATOM   665  O  O   . THR A 1 87  ? -15.629 13.530  21.133  1.00 26.15 ? 87  THR A O   1 
ATOM   666  C  CB  . THR A 1 87  ? -18.629 14.244  21.204  1.00 36.13 ? 87  THR A CB  1 
ATOM   667  O  OG1 . THR A 1 87  ? -19.863 14.385  21.905  1.00 39.24 ? 87  THR A OG1 1 
ATOM   668  C  CG2 . THR A 1 87  ? -18.934 13.858  19.771  1.00 38.07 ? 87  THR A CG2 1 
ATOM   669  N  N   . TYR A 1 88  ? -16.663 11.594  20.529  1.00 23.58 ? 88  TYR A N   1 
ATOM   670  C  CA  . TYR A 1 88  ? -15.565 11.143  19.688  1.00 24.03 ? 88  TYR A CA  1 
ATOM   671  C  C   . TYR A 1 88  ? -16.063 10.857  18.277  1.00 24.40 ? 88  TYR A C   1 
ATOM   672  O  O   . TYR A 1 88  ? -17.074 10.189  18.098  1.00 27.58 ? 88  TYR A O   1 
ATOM   673  C  CB  . TYR A 1 88  ? -14.919 9.898   20.290  1.00 22.43 ? 88  TYR A CB  1 
ATOM   674  C  CG  . TYR A 1 88  ? -14.128 10.110  21.553  1.00 23.44 ? 88  TYR A CG  1 
ATOM   675  C  CD1 . TYR A 1 88  ? -14.778 10.396  22.747  1.00 22.01 ? 88  TYR A CD1 1 
ATOM   676  C  CD2 . TYR A 1 88  ? -12.744 9.943   21.571  1.00 20.91 ? 88  TYR A CD2 1 
ATOM   677  C  CE1 . TYR A 1 88  ? -14.051 10.594  23.908  1.00 23.96 ? 88  TYR A CE1 1 
ATOM   678  C  CE2 . TYR A 1 88  ? -12.010 10.117  22.733  1.00 22.44 ? 88  TYR A CE2 1 
ATOM   679  C  CZ  . TYR A 1 88  ? -12.675 10.438  23.906  1.00 22.37 ? 88  TYR A CZ  1 
ATOM   680  O  OH  . TYR A 1 88  ? -11.974 10.593  25.059  1.00 24.75 ? 88  TYR A OH  1 
ATOM   681  N  N   . ARG A 1 89  ? -15.340 11.333  17.259  1.00 23.72 ? 89  ARG A N   1 
ATOM   682  C  CA  . ARG A 1 89  ? -15.849 11.235  15.899  1.00 20.96 ? 89  ARG A CA  1 
ATOM   683  C  C   . ARG A 1 89  ? -15.179 10.068  15.159  1.00 19.53 ? 89  ARG A C   1 
ATOM   684  O  O   . ARG A 1 89  ? -13.958 9.943   15.227  1.00 16.60 ? 89  ARG A O   1 
ATOM   685  C  CB  . ARG A 1 89  ? -15.481 12.555  15.232  1.00 25.73 ? 89  ARG A CB  1 
ATOM   686  C  CG  . ARG A 1 89  ? -16.415 13.029  14.138  1.00 30.85 ? 89  ARG A CG  1 
ATOM   687  C  CD  . ARG A 1 89  ? -15.945 14.394  13.682  1.00 26.39 ? 89  ARG A CD  1 
ATOM   688  N  NE  . ARG A 1 89  ? -16.655 15.560  14.191  1.00 30.69 ? 89  ARG A NE  1 
ATOM   689  C  CZ  . ARG A 1 89  ? -16.349 16.813  13.865  1.00 31.01 ? 89  ARG A CZ  1 
ATOM   690  N  NH1 . ARG A 1 89  ? -15.379 17.066  13.004  1.00 27.08 ? 89  ARG A NH1 1 
ATOM   691  N  NH2 . ARG A 1 89  ? -17.041 17.824  14.358  1.00 36.36 ? 89  ARG A NH2 1 
ATOM   692  N  N   . LEU A 1 90  ? -15.960 9.240   14.425  1.00 20.40 ? 90  LEU A N   1 
ATOM   693  C  CA  . LEU A 1 90  ? -15.381 8.115   13.685  1.00 18.97 ? 90  LEU A CA  1 
ATOM   694  C  C   . LEU A 1 90  ? -14.566 8.626   12.498  1.00 19.17 ? 90  LEU A C   1 
ATOM   695  O  O   . LEU A 1 90  ? -15.080 9.392   11.692  1.00 19.84 ? 90  LEU A O   1 
ATOM   696  C  CB  . LEU A 1 90  ? -16.507 7.208   13.162  1.00 18.18 ? 90  LEU A CB  1 
ATOM   697  C  CG  . LEU A 1 90  ? -16.083 6.069   12.232  1.00 18.37 ? 90  LEU A CG  1 
ATOM   698  C  CD1 . LEU A 1 90  ? -15.258 5.040   12.976  1.00 19.71 ? 90  LEU A CD1 1 
ATOM   699  C  CD2 . LEU A 1 90  ? -17.306 5.378   11.610  1.00 18.74 ? 90  LEU A CD2 1 
ATOM   700  N  N   . THR A 1 91  ? -13.295 8.221   12.412  1.00 18.06 ? 91  THR A N   1 
ATOM   701  C  CA  . THR A 1 91  ? -12.424 8.647   11.308  1.00 19.39 ? 91  THR A CA  1 
ATOM   702  C  C   . THR A 1 91  ? -12.142 7.508   10.320  1.00 18.11 ? 91  THR A C   1 
ATOM   703  O  O   . THR A 1 91  ? -11.972 7.731   9.112   1.00 18.12 ? 91  THR A O   1 
ATOM   704  C  CB  . THR A 1 91  ? -11.160 9.327   11.882  1.00 20.19 ? 91  THR A CB  1 
ATOM   705  O  OG1 . THR A 1 91  ? -10.362 9.765   10.782  1.00 22.87 ? 91  THR A OG1 1 
ATOM   706  C  CG2 . THR A 1 91  ? -10.256 8.398   12.654  1.00 20.30 ? 91  THR A CG2 1 
ATOM   707  N  N   . GLN A 1 92  ? -11.989 6.270   10.814  1.00 18.78 ? 92  GLN A N   1 
ATOM   708  C  CA  . GLN A 1 92  ? -11.620 5.154   9.943   1.00 18.62 ? 92  GLN A CA  1 
ATOM   709  C  C   . GLN A 1 92  ? -11.863 3.835   10.670  1.00 18.79 ? 92  GLN A C   1 
ATOM   710  O  O   . GLN A 1 92  ? -11.991 3.809   11.896  1.00 17.05 ? 92  GLN A O   1 
ATOM   711  C  CB  . GLN A 1 92  ? -10.141 5.232   9.498   1.00 19.30 ? 92  GLN A CB  1 
ATOM   712  C  CG  . GLN A 1 92  ? -9.154  5.216   10.674  1.00 19.49 ? 92  GLN A CG  1 
ATOM   713  C  CD  . GLN A 1 92  ? -8.354  3.940   10.793  1.00 20.93 ? 92  GLN A CD  1 
ATOM   714  O  OE1 . GLN A 1 92  ? -8.883  2.834   10.717  1.00 23.04 ? 92  GLN A OE1 1 
ATOM   715  N  NE2 . GLN A 1 92  ? -7.056  4.087   10.994  1.00 21.38 ? 92  GLN A NE2 1 
ATOM   716  N  N   . PHE A 1 93  ? -12.015 2.740   9.905   1.00 18.20 ? 93  PHE A N   1 
ATOM   717  C  CA  . PHE A 1 93  ? -11.874 1.437   10.540  1.00 17.55 ? 93  PHE A CA  1 
ATOM   718  C  C   . PHE A 1 93  ? -10.895 0.578   9.740   1.00 18.35 ? 93  PHE A C   1 
ATOM   719  O  O   . PHE A 1 93  ? -10.692 0.764   8.529   1.00 18.80 ? 93  PHE A O   1 
ATOM   720  C  CB  . PHE A 1 93  ? -13.219 0.742   10.789  1.00 16.65 ? 93  PHE A CB  1 
ATOM   721  C  CG  . PHE A 1 93  ? -13.963 0.303   9.555   1.00 16.71 ? 93  PHE A CG  1 
ATOM   722  C  CD1 . PHE A 1 93  ? -13.552 -0.820  8.840   1.00 19.12 ? 93  PHE A CD1 1 
ATOM   723  C  CD2 . PHE A 1 93  ? -15.091 0.984   9.125   1.00 16.20 ? 93  PHE A CD2 1 
ATOM   724  C  CE1 . PHE A 1 93  ? -14.259 -1.247  7.726   1.00 17.99 ? 93  PHE A CE1 1 
ATOM   725  C  CE2 . PHE A 1 93  ? -15.795 0.569   7.995   1.00 17.15 ? 93  PHE A CE2 1 
ATOM   726  C  CZ  . PHE A 1 93  ? -15.364 -0.525  7.283   1.00 17.91 ? 93  PHE A CZ  1 
ATOM   727  N  N   . HIS A 1 94  ? -10.304 -0.389  10.438  1.00 18.07 ? 94  HIS A N   1 
ATOM   728  C  CA  . HIS A 1 94  ? -9.403  -1.321  9.787   1.00 19.85 ? 94  HIS A CA  1 
ATOM   729  C  C   . HIS A 1 94  ? -9.489  -2.629  10.564  1.00 20.48 ? 94  HIS A C   1 
ATOM   730  O  O   . HIS A 1 94  ? -10.173 -2.706  11.599  1.00 18.28 ? 94  HIS A O   1 
ATOM   731  C  CB  . HIS A 1 94  ? -7.984  -0.715  9.736   1.00 17.56 ? 94  HIS A CB  1 
ATOM   732  C  CG  . HIS A 1 94  ? -7.443  -0.591  11.117  1.00 19.89 ? 94  HIS A CG  1 
ATOM   733  N  ND1 . HIS A 1 94  ? -7.630  0.541   11.900  1.00 19.67 ? 94  HIS A ND1 1 
ATOM   734  C  CD2 . HIS A 1 94  ? -6.820  -1.504  11.886  1.00 21.93 ? 94  HIS A CD2 1 
ATOM   735  C  CE1 . HIS A 1 94  ? -7.080  0.323   13.087  1.00 21.55 ? 94  HIS A CE1 1 
ATOM   736  N  NE2 . HIS A 1 94  ? -6.557  -0.930  13.092  1.00 18.59 ? 94  HIS A NE2 1 
ATOM   737  N  N   . PHE A 1 95  ? -8.746  -3.636  10.093  1.00 19.01 ? 95  PHE A N   1 
ATOM   738  C  CA  . PHE A 1 95  ? -8.756  -4.939  10.747  1.00 18.87 ? 95  PHE A CA  1 
ATOM   739  C  C   . PHE A 1 95  ? -7.330  -5.452  10.970  1.00 18.98 ? 95  PHE A C   1 
ATOM   740  O  O   . PHE A 1 95  ? -6.348  -4.989  10.376  1.00 18.31 ? 95  PHE A O   1 
ATOM   741  C  CB  . PHE A 1 95  ? -9.483  -6.003  9.910   1.00 18.27 ? 95  PHE A CB  1 
ATOM   742  C  CG  . PHE A 1 95  ? -10.942 -5.743  9.625   1.00 20.09 ? 95  PHE A CG  1 
ATOM   743  C  CD1 . PHE A 1 95  ? -11.322 -4.906  8.571   1.00 21.41 ? 95  PHE A CD1 1 
ATOM   744  C  CD2 . PHE A 1 95  ? -11.936 -6.364  10.371  1.00 21.12 ? 95  PHE A CD2 1 
ATOM   745  C  CE1 . PHE A 1 95  ? -12.668 -4.700  8.273   1.00 22.53 ? 95  PHE A CE1 1 
ATOM   746  C  CE2 . PHE A 1 95  ? -13.283 -6.164  10.064  1.00 21.41 ? 95  PHE A CE2 1 
ATOM   747  C  CZ  . PHE A 1 95  ? -13.644 -5.333  9.018   1.00 20.79 ? 95  PHE A CZ  1 
ATOM   748  N  N   . HIS A 1 96  ? -7.240  -6.437  11.863  1.00 18.10 ? 96  HIS A N   1 
ATOM   749  C  CA  . HIS A 1 96  ? -6.038  -7.238  12.052  1.00 17.55 ? 96  HIS A CA  1 
ATOM   750  C  C   . HIS A 1 96  ? -6.474  -8.689  11.944  1.00 18.56 ? 96  HIS A C   1 
ATOM   751  O  O   . HIS A 1 96  ? -7.592  -8.997  12.369  1.00 18.23 ? 96  HIS A O   1 
ATOM   752  C  CB  . HIS A 1 96  ? -5.456  -7.027  13.463  1.00 18.19 ? 96  HIS A CB  1 
ATOM   753  C  CG  . HIS A 1 96  ? -5.127  -5.596  13.730  1.00 18.55 ? 96  HIS A CG  1 
ATOM   754  N  ND1 . HIS A 1 96  ? -3.900  -5.055  13.427  1.00 19.34 ? 96  HIS A ND1 1 
ATOM   755  C  CD2 . HIS A 1 96  ? -5.889  -4.583  14.190  1.00 19.57 ? 96  HIS A CD2 1 
ATOM   756  C  CE1 . HIS A 1 96  ? -3.907  -3.760  13.751  1.00 20.95 ? 96  HIS A CE1 1 
ATOM   757  N  NE2 . HIS A 1 96  ? -5.116  -3.451  14.226  1.00 21.06 ? 96  HIS A NE2 1 
ATOM   758  N  N   . TRP A 1 97  ? -5.643  -9.539  11.292  1.00 18.57 ? 97  TRP A N   1 
ATOM   759  C  CA  . TRP A 1 97  ? -6.064  -10.918 11.089  1.00 18.65 ? 97  TRP A CA  1 
ATOM   760  C  C   . TRP A 1 97  ? -4.886  -11.873 10.977  1.00 18.30 ? 97  TRP A C   1 
ATOM   761  O  O   . TRP A 1 97  ? -3.728  -11.450 10.923  1.00 19.41 ? 97  TRP A O   1 
ATOM   762  C  CB  . TRP A 1 97  ? -6.979  -11.058 9.869   1.00 19.65 ? 97  TRP A CB  1 
ATOM   763  C  CG  . TRP A 1 97  ? -6.297  -10.685 8.593   1.00 19.05 ? 97  TRP A CG  1 
ATOM   764  C  CD1 . TRP A 1 97  ? -5.658  -11.507 7.701   1.00 20.05 ? 97  TRP A CD1 1 
ATOM   765  C  CD2 . TRP A 1 97  ? -6.261  -9.369  8.031   1.00 20.83 ? 97  TRP A CD2 1 
ATOM   766  N  NE1 . TRP A 1 97  ? -5.178  -10.784 6.650   1.00 19.09 ? 97  TRP A NE1 1 
ATOM   767  C  CE2 . TRP A 1 97  ? -5.577  -9.477  6.798   1.00 20.26 ? 97  TRP A CE2 1 
ATOM   768  C  CE3 . TRP A 1 97  ? -6.758  -8.118  8.437   1.00 21.00 ? 97  TRP A CE3 1 
ATOM   769  C  CZ2 . TRP A 1 97  ? -5.327  -8.361  6.010   1.00 20.64 ? 97  TRP A CZ2 1 
ATOM   770  C  CZ3 . TRP A 1 97  ? -6.521  -7.021  7.640   1.00 20.50 ? 97  TRP A CZ3 1 
ATOM   771  C  CH2 . TRP A 1 97  ? -5.837  -7.150  6.427   1.00 20.12 ? 97  TRP A CH2 1 
ATOM   772  N  N   . GLY A 1 98  ? -5.232  -13.170 10.954  1.00 19.11 ? 98  GLY A N   1 
ATOM   773  C  CA  . GLY A 1 98  ? -4.254  -14.247 11.061  1.00 21.69 ? 98  GLY A CA  1 
ATOM   774  C  C   . GLY A 1 98  ? -3.999  -14.975 9.737   1.00 24.77 ? 98  GLY A C   1 
ATOM   775  O  O   . GLY A 1 98  ? -4.679  -14.733 8.739   1.00 23.56 ? 98  GLY A O   1 
ATOM   776  N  N   . SER A 1 99  ? -2.986  -15.854 9.756   1.00 25.47 ? 99  SER A N   1 
ATOM   777  C  CA  . SER A 1 99  ? -2.692  -16.718 8.618   1.00 26.62 ? 99  SER A CA  1 
ATOM   778  C  C   . SER A 1 99  ? -3.611  -17.934 8.664   1.00 26.26 ? 99  SER A C   1 
ATOM   779  O  O   . SER A 1 99  ? -3.671  -18.710 7.715   1.00 25.90 ? 99  SER A O   1 
ATOM   780  C  CB  . SER A 1 99  ? -1.258  -17.168 8.623   1.00 24.58 ? 99  SER A CB  1 
ATOM   781  O  OG  . SER A 1 99  ? -0.871  -17.580 9.939   1.00 24.49 ? 99  SER A OG  1 
ATOM   782  N  N   . LEU A 1 100 ? -4.236  -18.136 9.820   1.00 23.68 ? 100 LEU A N   1 
ATOM   783  C  CA  . LEU A 1 100 ? -5.237  -19.179 9.982   1.00 30.20 ? 100 LEU A CA  1 
ATOM   784  C  C   . LEU A 1 100 ? -6.193  -18.769 11.102  1.00 32.39 ? 100 LEU A C   1 
ATOM   785  O  O   . LEU A 1 100 ? -5.944  -17.774 11.780  1.00 26.02 ? 100 LEU A O   1 
ATOM   786  C  CB  . LEU A 1 100 ? -4.558  -20.520 10.280  1.00 32.37 ? 100 LEU A CB  1 
ATOM   787  C  CG  . LEU A 1 100 ? -3.827  -20.608 11.614  1.00 32.80 ? 100 LEU A CG  1 
ATOM   788  C  CD1 . LEU A 1 100 ? -3.690  -22.061 12.042  1.00 39.80 ? 100 LEU A CD1 1 
ATOM   789  C  CD2 . LEU A 1 100 ? -2.457  -19.961 11.503  1.00 34.48 ? 100 LEU A CD2 1 
ATOM   790  N  N   . ASP A 1 101 ? -7.273  -19.549 11.293  1.00 30.52 ? 101 ASP A N   1 
ATOM   791  C  CA  . ASP A 1 101 ? -8.451  -19.035 11.978  1.00 27.42 ? 101 ASP A CA  1 
ATOM   792  C  C   . ASP A 1 101 ? -8.179  -18.951 13.476  1.00 28.04 ? 101 ASP A C   1 
ATOM   793  O  O   . ASP A 1 101 ? -8.903  -18.262 14.194  1.00 28.55 ? 101 ASP A O   1 
ATOM   794  C  CB  . ASP A 1 101 ? -9.715  -19.875 11.693  1.00 30.72 ? 101 ASP A CB  1 
ATOM   795  C  CG  . ASP A 1 101 ? -10.232 -19.883 10.259  1.00 33.33 ? 101 ASP A CG  1 
ATOM   796  O  OD1 . ASP A 1 101 ? -9.823  -19.026 9.446   1.00 33.80 ? 101 ASP A OD1 1 
ATOM   797  O  OD2 . ASP A 1 101 ? -11.077 -20.760 9.949   1.00 41.83 ? 101 ASP A OD2 1 
ATOM   798  N  N   . GLY A 1 102 ? -7.157  -19.673 13.956  1.00 24.68 ? 102 GLY A N   1 
ATOM   799  C  CA  . GLY A 1 102 ? -6.921  -19.726 15.389  1.00 23.87 ? 102 GLY A CA  1 
ATOM   800  C  C   . GLY A 1 102 ? -6.075  -18.567 15.935  1.00 23.44 ? 102 GLY A C   1 
ATOM   801  O  O   . GLY A 1 102 ? -5.766  -18.518 17.126  1.00 27.11 ? 102 GLY A O   1 
ATOM   802  N  N   . GLN A 1 103 ? -5.709  -17.611 15.083  1.00 25.87 ? 103 GLN A N   1 
ATOM   803  C  CA  . GLN A 1 103 ? -5.044  -16.396 15.552  1.00 23.25 ? 103 GLN A CA  1 
ATOM   804  C  C   . GLN A 1 103 ? -5.446  -15.234 14.649  1.00 21.17 ? 103 GLN A C   1 
ATOM   805  O  O   . GLN A 1 103 ? -5.988  -15.470 13.579  1.00 22.45 ? 103 GLN A O   1 
ATOM   806  C  CB  . GLN A 1 103 ? -3.532  -16.596 15.523  1.00 22.95 ? 103 GLN A CB  1 
ATOM   807  C  CG  . GLN A 1 103 ? -3.010  -16.935 14.128  1.00 24.68 ? 103 GLN A CG  1 
ATOM   808  C  CD  . GLN A 1 103 ? -1.600  -17.473 14.254  1.00 29.85 ? 103 GLN A CD  1 
ATOM   809  O  OE1 . GLN A 1 103 ? -1.317  -18.340 15.075  1.00 32.09 ? 103 GLN A OE1 1 
ATOM   810  N  NE2 . GLN A 1 103 ? -0.701  -16.958 13.434  1.00 28.06 ? 103 GLN A NE2 1 
ATOM   811  N  N   . GLY A 1 104 ? -5.075  -14.008 15.031  1.00 21.35 ? 104 GLY A N   1 
ATOM   812  C  CA  . GLY A 1 104 ? -5.435  -12.827 14.261  1.00 19.10 ? 104 GLY A CA  1 
ATOM   813  C  C   . GLY A 1 104 ? -5.886  -11.645 15.104  1.00 19.37 ? 104 GLY A C   1 
ATOM   814  O  O   . GLY A 1 104 ? -5.661  -10.505 14.721  1.00 19.85 ? 104 GLY A O   1 
ATOM   815  N  N   . SER A 1 105 ? -6.526  -11.907 16.254  1.00 19.19 ? 105 SER A N   1 
ATOM   816  C  CA  . SER A 1 105 ? -6.916  -10.795 17.092  1.00 19.19 ? 105 SER A CA  1 
ATOM   817  C  C   . SER A 1 105 ? -5.684  -10.246 17.822  1.00 19.76 ? 105 SER A C   1 
ATOM   818  O  O   . SER A 1 105 ? -4.673  -10.917 18.040  1.00 19.76 ? 105 SER A O   1 
ATOM   819  C  CB  . SER A 1 105 ? -8.066  -11.138 18.054  1.00 18.80 ? 105 SER A CB  1 
ATOM   820  O  OG  . SER A 1 105 ? -7.642  -12.073 19.041  1.00 21.02 ? 105 SER A OG  1 
ATOM   821  N  N   . GLU A 1 106 ? -5.820  -8.994  18.229  1.00 19.09 ? 106 GLU A N   1 
ATOM   822  C  CA  . GLU A 1 106 ? -4.787  -8.336  19.007  1.00 17.60 ? 106 GLU A CA  1 
ATOM   823  C  C   . GLU A 1 106 ? -5.167  -8.502  20.468  1.00 17.80 ? 106 GLU A C   1 
ATOM   824  O  O   . GLU A 1 106 ? -4.373  -9.015  21.245  1.00 19.12 ? 106 GLU A O   1 
ATOM   825  C  CB  . GLU A 1 106 ? -4.748  -6.860  18.633  1.00 18.35 ? 106 GLU A CB  1 
ATOM   826  C  CG  . GLU A 1 106 ? -4.519  -6.647  17.138  1.00 19.39 ? 106 GLU A CG  1 
ATOM   827  C  CD  . GLU A 1 106 ? -3.715  -5.379  16.915  1.00 22.12 ? 106 GLU A CD  1 
ATOM   828  O  OE1 . GLU A 1 106 ? -4.262  -4.299  17.142  1.00 21.42 ? 106 GLU A OE1 1 
ATOM   829  O  OE2 . GLU A 1 106 ? -2.524  -5.480  16.535  1.00 23.68 ? 106 GLU A OE2 1 
ATOM   830  N  N   . HIS A 1 107 ? -6.369  -8.064  20.856  1.00 19.16 ? 107 HIS A N   1 
ATOM   831  C  CA  . HIS A 1 107 ? -6.757  -8.401  22.222  1.00 17.98 ? 107 HIS A CA  1 
ATOM   832  C  C   . HIS A 1 107 ? -7.061  -9.892  22.310  1.00 19.85 ? 107 HIS A C   1 
ATOM   833  O  O   . HIS A 1 107 ? -7.372  -10.532 21.315  1.00 18.27 ? 107 HIS A O   1 
ATOM   834  C  CB  . HIS A 1 107 ? -7.986  -7.625  22.686  1.00 17.44 ? 107 HIS A CB  1 
ATOM   835  C  CG  . HIS A 1 107 ? -7.695  -6.174  22.834  1.00 17.99 ? 107 HIS A CG  1 
ATOM   836  N  ND1 . HIS A 1 107 ? -7.735  -5.294  21.764  1.00 20.27 ? 107 HIS A ND1 1 
ATOM   837  C  CD2 . HIS A 1 107 ? -7.228  -5.481  23.885  1.00 19.01 ? 107 HIS A CD2 1 
ATOM   838  C  CE1 . HIS A 1 107 ? -7.377  -4.091  22.173  1.00 20.44 ? 107 HIS A CE1 1 
ATOM   839  N  NE2 . HIS A 1 107 ? -7.071  -4.178  23.485  1.00 19.12 ? 107 HIS A NE2 1 
ATOM   840  N  N   . THR A 1 108 ? -7.006  -10.450 23.518  1.00 19.73 ? 108 THR A N   1 
ATOM   841  C  CA  . THR A 1 108 ? -7.379  -11.847 23.659  1.00 21.06 ? 108 THR A CA  1 
ATOM   842  C  C   . THR A 1 108 ? -8.310  -11.890 24.864  1.00 21.96 ? 108 THR A C   1 
ATOM   843  O  O   . THR A 1 108 ? -8.324  -10.947 25.634  1.00 20.74 ? 108 THR A O   1 
ATOM   844  C  CB  . THR A 1 108 ? -6.158  -12.766 23.825  1.00 22.12 ? 108 THR A CB  1 
ATOM   845  O  OG1 . THR A 1 108 ? -5.415  -12.407 24.990  1.00 24.28 ? 108 THR A OG1 1 
ATOM   846  C  CG2 . THR A 1 108 ? -5.250  -12.781 22.616  1.00 19.57 ? 108 THR A CG2 1 
ATOM   847  N  N   . VAL A 1 109 ? -9.128  -12.932 24.972  1.00 22.81 ? 109 VAL A N   1 
ATOM   848  C  CA  . VAL A 1 109 ? -10.069 -13.022 26.083  1.00 23.22 ? 109 VAL A CA  1 
ATOM   849  C  C   . VAL A 1 109 ? -9.768  -14.316 26.841  1.00 24.53 ? 109 VAL A C   1 
ATOM   850  O  O   . VAL A 1 109 ? -9.914  -15.404 26.295  1.00 25.83 ? 109 VAL A O   1 
ATOM   851  C  CB  . VAL A 1 109 ? -11.522 -13.001 25.567  1.00 24.67 ? 109 VAL A CB  1 
ATOM   852  C  CG1 . VAL A 1 109 ? -12.501 -12.935 26.737  1.00 24.47 ? 109 VAL A CG1 1 
ATOM   853  C  CG2 . VAL A 1 109 ? -11.766 -11.831 24.632  1.00 23.92 ? 109 VAL A CG2 1 
ATOM   854  N  N   . ASP A 1 110 ? -9.331  -14.203 28.092  1.00 25.38 ? 110 ASP A N   1 
ATOM   855  C  CA  . ASP A 1 110 ? -8.868  -15.389 28.805  1.00 29.73 ? 110 ASP A CA  1 
ATOM   856  C  C   . ASP A 1 110 ? -7.913  -16.212 27.941  1.00 30.62 ? 110 ASP A C   1 
ATOM   857  O  O   . ASP A 1 110 ? -7.998  -17.446 27.924  1.00 27.25 ? 110 ASP A O   1 
ATOM   858  C  CB  . ASP A 1 110 ? -10.061 -16.226 29.284  1.00 31.98 ? 110 ASP A CB  1 
ATOM   859  C  CG  . ASP A 1 110 ? -10.933 -15.456 30.262  1.00 32.31 ? 110 ASP A CG  1 
ATOM   860  O  OD1 . ASP A 1 110 ? -10.381 -14.643 31.005  1.00 33.61 ? 110 ASP A OD1 1 
ATOM   861  O  OD2 . ASP A 1 110 ? -12.149 -15.699 30.282  1.00 35.12 ? 110 ASP A OD2 1 
ATOM   862  N  N   . LYS A 1 111 ? -7.020  -15.512 27.220  1.00 26.68 ? 111 LYS A N   1 
ATOM   863  C  CA  . LYS A 1 111 ? -5.982  -16.099 26.375  1.00 29.17 ? 111 LYS A CA  1 
ATOM   864  C  C   . LYS A 1 111 ? -6.510  -16.568 25.023  1.00 26.24 ? 111 LYS A C   1 
ATOM   865  O  O   . LYS A 1 111 ? -5.724  -16.957 24.167  1.00 23.25 ? 111 LYS A O   1 
ATOM   866  C  CB  . LYS A 1 111 ? -5.169  -17.183 27.109  1.00 34.06 ? 111 LYS A CB  1 
ATOM   867  C  CG  . LYS A 1 111 ? -4.386  -16.719 28.336  1.00 39.59 ? 111 LYS A CG  1 
ATOM   868  C  CD  . LYS A 1 111 ? -3.145  -15.901 27.993  1.00 45.51 ? 111 LYS A CD  1 
ATOM   869  C  CE  . LYS A 1 111 ? -2.479  -15.225 29.176  1.00 49.81 ? 111 LYS A CE  1 
ATOM   870  N  NZ  . LYS A 1 111 ? -1.962  -16.224 30.142  1.00 56.04 ? 111 LYS A NZ  1 
ATOM   871  N  N   . LYS A 1 112 ? -7.835  -16.526 24.799  1.00 27.11 ? 112 LYS A N   1 
ATOM   872  C  CA  . LYS A 1 112 ? -8.388  -16.980 23.525  1.00 27.33 ? 112 LYS A CA  1 
ATOM   873  C  C   . LYS A 1 112 ? -8.083  -15.970 22.412  1.00 24.48 ? 112 LYS A C   1 
ATOM   874  O  O   . LYS A 1 112 ? -8.283  -14.758 22.571  1.00 24.65 ? 112 LYS A O   1 
ATOM   875  C  CB  . LYS A 1 112 ? -9.904  -17.201 23.625  1.00 29.18 ? 112 LYS A CB  1 
ATOM   876  C  CG  . LYS A 1 112 ? -10.530 -17.659 22.316  1.00 30.94 ? 112 LYS A CG  1 
ATOM   877  C  CD  . LYS A 1 112 ? -12.055 -17.606 22.222  1.00 35.11 ? 112 LYS A CD  1 
ATOM   878  C  CE  . LYS A 1 112 ? -12.511 -18.100 20.863  1.00 35.39 ? 112 LYS A CE  1 
ATOM   879  N  NZ  . LYS A 1 112 ? -13.964 -18.396 20.860  1.00 41.52 ? 112 LYS A NZ  1 
ATOM   880  N  N   . LYS A 1 113 ? -7.596  -16.456 21.271  1.00 23.87 ? 113 LYS A N   1 
ATOM   881  C  CA  . LYS A 1 113 ? -7.379  -15.568 20.139  1.00 22.95 ? 113 LYS A CA  1 
ATOM   882  C  C   . LYS A 1 113 ? -8.497  -15.768 19.121  1.00 24.58 ? 113 LYS A C   1 
ATOM   883  O  O   . LYS A 1 113 ? -8.911  -16.899 18.848  1.00 25.14 ? 113 LYS A O   1 
ATOM   884  C  CB  . LYS A 1 113 ? -6.056  -15.861 19.433  1.00 24.53 ? 113 LYS A CB  1 
ATOM   885  C  CG  . LYS A 1 113 ? -4.781  -15.624 20.243  1.00 25.06 ? 113 LYS A CG  1 
ATOM   886  C  CD  . LYS A 1 113 ? -3.612  -16.269 19.532  1.00 25.85 ? 113 LYS A CD  1 
ATOM   887  C  CE  . LYS A 1 113 ? -2.243  -15.890 20.036  1.00 28.83 ? 113 LYS A CE  1 
ATOM   888  N  NZ  . LYS A 1 113 ? -2.025  -16.410 21.396  1.00 29.15 ? 113 LYS A NZ  1 
ATOM   889  N  N   . TYR A 1 114 ? -8.965  -14.660 18.541  1.00 21.20 ? 114 TYR A N   1 
ATOM   890  C  CA  . TYR A 1 114 ? -10.004 -14.718 17.543  1.00 21.08 ? 114 TYR A CA  1 
ATOM   891  C  C   . TYR A 1 114 ? -9.313  -14.682 16.197  1.00 22.64 ? 114 TYR A C   1 
ATOM   892  O  O   . TYR A 1 114 ? -8.113  -14.422 16.142  1.00 23.49 ? 114 TYR A O   1 
ATOM   893  C  CB  . TYR A 1 114 ? -11.050 -13.624 17.769  1.00 21.00 ? 114 TYR A CB  1 
ATOM   894  C  CG  . TYR A 1 114 ? -12.004 -13.913 18.909  1.00 21.27 ? 114 TYR A CG  1 
ATOM   895  C  CD1 . TYR A 1 114 ? -11.718 -13.497 20.197  1.00 24.27 ? 114 TYR A CD1 1 
ATOM   896  C  CD2 . TYR A 1 114 ? -13.198 -14.593 18.707  1.00 23.57 ? 114 TYR A CD2 1 
ATOM   897  C  CE1 . TYR A 1 114 ? -12.577 -13.735 21.255  1.00 24.67 ? 114 TYR A CE1 1 
ATOM   898  C  CE2 . TYR A 1 114 ? -14.073 -14.846 19.759  1.00 25.23 ? 114 TYR A CE2 1 
ATOM   899  C  CZ  . TYR A 1 114 ? -13.767 -14.405 21.034  1.00 26.18 ? 114 TYR A CZ  1 
ATOM   900  O  OH  . TYR A 1 114 ? -14.623 -14.620 22.087  1.00 33.51 ? 114 TYR A OH  1 
ATOM   901  N  N   . ALA A 1 115 ? -10.084 -14.935 15.140  1.00 23.31 ? 115 ALA A N   1 
ATOM   902  C  CA  . ALA A 1 115 ? -9.548  -14.983 13.791  1.00 24.34 ? 115 ALA A CA  1 
ATOM   903  C  C   . ALA A 1 115 ? -9.142  -13.588 13.323  1.00 24.17 ? 115 ALA A C   1 
ATOM   904  O  O   . ALA A 1 115 ? -8.364  -13.443 12.380  1.00 23.07 ? 115 ALA A O   1 
ATOM   905  C  CB  . ALA A 1 115 ? -10.594 -15.592 12.874  1.00 24.22 ? 115 ALA A CB  1 
ATOM   906  N  N   . ALA A 1 116 ? -9.794  -12.563 13.879  1.00 20.97 ? 116 ALA A N   1 
ATOM   907  C  CA  . ALA A 1 116 ? -9.545  -11.188 13.480  1.00 21.36 ? 116 ALA A CA  1 
ATOM   908  C  C   . ALA A 1 116 ? -10.128 -10.227 14.516  1.00 21.60 ? 116 ALA A C   1 
ATOM   909  O  O   . ALA A 1 116 ? -10.849 -10.645 15.425  1.00 20.39 ? 116 ALA A O   1 
ATOM   910  C  CB  . ALA A 1 116 ? -10.101 -10.902 12.102  1.00 21.73 ? 116 ALA A CB  1 
ATOM   911  N  N   . GLU A 1 117 ? -9.754  -8.938  14.384  1.00 21.59 ? 117 GLU A N   1 
ATOM   912  C  CA  . GLU A 1 117 ? -10.283 -7.880  15.228  1.00 20.31 ? 117 GLU A CA  1 
ATOM   913  C  C   . GLU A 1 117 ? -10.501 -6.657  14.347  1.00 20.46 ? 117 GLU A C   1 
ATOM   914  O  O   . GLU A 1 117 ? -9.643  -6.330  13.533  1.00 19.69 ? 117 GLU A O   1 
ATOM   915  C  CB  . GLU A 1 117 ? -9.292  -7.571  16.347  1.00 20.96 ? 117 GLU A CB  1 
ATOM   916  C  CG  . GLU A 1 117 ? -9.854  -6.673  17.449  1.00 21.47 ? 117 GLU A CG  1 
ATOM   917  C  CD  . GLU A 1 117 ? -8.929  -6.619  18.665  1.00 23.37 ? 117 GLU A CD  1 
ATOM   918  O  OE1 . GLU A 1 117 ? -8.249  -7.643  18.963  1.00 21.16 ? 117 GLU A OE1 1 
ATOM   919  O  OE2 . GLU A 1 117 ? -8.895  -5.563  19.324  1.00 24.47 ? 117 GLU A OE2 1 
ATOM   920  N  N   . LEU A 1 118 ? -11.701 -6.083  14.450  1.00 19.97 ? 118 LEU A N   1 
ATOM   921  C  CA  . LEU A 1 118 ? -12.064 -4.831  13.809  1.00 16.95 ? 118 LEU A CA  1 
ATOM   922  C  C   . LEU A 1 118 ? -11.795 -3.678  14.764  1.00 18.53 ? 118 LEU A C   1 
ATOM   923  O  O   . LEU A 1 118 ? -12.171 -3.741  15.957  1.00 16.50 ? 118 LEU A O   1 
ATOM   924  C  CB  . LEU A 1 118 ? -13.568 -4.942  13.504  1.00 18.78 ? 118 LEU A CB  1 
ATOM   925  C  CG  . LEU A 1 118 ? -14.277 -3.639  13.142  1.00 17.47 ? 118 LEU A CG  1 
ATOM   926  C  CD1 . LEU A 1 118 ? -13.671 -3.069  11.857  1.00 17.87 ? 118 LEU A CD1 1 
ATOM   927  C  CD2 . LEU A 1 118 ? -15.763 -3.912  12.944  1.00 18.49 ? 118 LEU A CD2 1 
ATOM   928  N  N   . HIS A 1 119 ? -11.182 -2.612  14.219  1.00 16.82 ? 119 HIS A N   1 
ATOM   929  C  CA  . HIS A 1 119 ? -10.908 -1.444  15.043  1.00 17.82 ? 119 HIS A CA  1 
ATOM   930  C  C   . HIS A 1 119 ? -11.651 -0.261  14.420  1.00 18.38 ? 119 HIS A C   1 
ATOM   931  O  O   . HIS A 1 119 ? -11.346 0.089   13.279  1.00 18.19 ? 119 HIS A O   1 
ATOM   932  C  CB  . HIS A 1 119 ? -9.392  -1.180  15.130  1.00 17.98 ? 119 HIS A CB  1 
ATOM   933  C  CG  . HIS A 1 119 ? -8.714  -2.147  16.051  1.00 19.16 ? 119 HIS A CG  1 
ATOM   934  N  ND1 . HIS A 1 119 ? -7.325  -2.293  16.137  1.00 18.54 ? 119 HIS A ND1 1 
ATOM   935  C  CD2 . HIS A 1 119 ? -9.245  -2.969  16.990  1.00 18.52 ? 119 HIS A CD2 1 
ATOM   936  C  CE1 . HIS A 1 119 ? -7.063  -3.238  17.027  1.00 19.13 ? 119 HIS A CE1 1 
ATOM   937  N  NE2 . HIS A 1 119 ? -8.207  -3.645  17.575  1.00 19.58 ? 119 HIS A NE2 1 
ATOM   938  N  N   . LEU A 1 120 ? -12.677 0.248   15.124  1.00 17.51 ? 120 LEU A N   1 
ATOM   939  C  CA  . LEU A 1 120 ? -13.346 1.490   14.715  1.00 17.99 ? 120 LEU A CA  1 
ATOM   940  C  C   . LEU A 1 120 ? -12.742 2.651   15.502  1.00 18.33 ? 120 LEU A C   1 
ATOM   941  O  O   . LEU A 1 120 ? -12.844 2.715   16.729  1.00 17.49 ? 120 LEU A O   1 
ATOM   942  C  CB  . LEU A 1 120 ? -14.863 1.372   14.923  1.00 18.82 ? 120 LEU A CB  1 
ATOM   943  C  CG  . LEU A 1 120 ? -15.556 0.363   14.003  1.00 19.90 ? 120 LEU A CG  1 
ATOM   944  C  CD1 . LEU A 1 120 ? -16.446 -0.534  14.849  1.00 22.15 ? 120 LEU A CD1 1 
ATOM   945  C  CD2 . LEU A 1 120 ? -16.406 1.100   12.973  1.00 20.64 ? 120 LEU A CD2 1 
ATOM   946  N  N   . VAL A 1 121 ? -12.056 3.539   14.790  1.00 18.00 ? 121 VAL A N   1 
ATOM   947  C  CA  . VAL A 1 121 ? -11.146 4.497   15.406  1.00 17.71 ? 121 VAL A CA  1 
ATOM   948  C  C   . VAL A 1 121 ? -11.823 5.869   15.459  1.00 18.30 ? 121 VAL A C   1 
ATOM   949  O  O   . VAL A 1 121 ? -12.207 6.394   14.430  1.00 17.44 ? 121 VAL A O   1 
ATOM   950  C  CB  . VAL A 1 121 ? -9.834  4.563   14.589  1.00 17.39 ? 121 VAL A CB  1 
ATOM   951  C  CG1 . VAL A 1 121 ? -8.861  5.578   15.158  1.00 18.36 ? 121 VAL A CG1 1 
ATOM   952  C  CG2 . VAL A 1 121 ? -9.167  3.202   14.511  1.00 16.94 ? 121 VAL A CG2 1 
ATOM   953  N  N   . HIS A 1 122 ? -11.921 6.466   16.664  1.00 15.92 ? 122 HIS A N   1 
ATOM   954  C  CA  . HIS A 1 122 ? -12.625 7.721   16.854  1.00 18.07 ? 122 HIS A CA  1 
ATOM   955  C  C   . HIS A 1 122 ? -11.706 8.724   17.550  1.00 18.60 ? 122 HIS A C   1 
ATOM   956  O  O   . HIS A 1 122 ? -10.873 8.336   18.357  1.00 19.64 ? 122 HIS A O   1 
ATOM   957  C  CB  . HIS A 1 122 ? -13.857 7.510   17.762  1.00 18.65 ? 122 HIS A CB  1 
ATOM   958  C  CG  . HIS A 1 122 ? -14.788 6.431   17.331  1.00 17.17 ? 122 HIS A CG  1 
ATOM   959  N  ND1 . HIS A 1 122 ? -14.504 5.085   17.520  1.00 17.21 ? 122 HIS A ND1 1 
ATOM   960  C  CD2 . HIS A 1 122 ? -16.028 6.486   16.795  1.00 18.92 ? 122 HIS A CD2 1 
ATOM   961  C  CE1 . HIS A 1 122 ? -15.513 4.357   17.076  1.00 16.98 ? 122 HIS A CE1 1 
ATOM   962  N  NE2 . HIS A 1 122 ? -16.485 5.193   16.657  1.00 18.13 ? 122 HIS A NE2 1 
ATOM   963  N  N   . TRP A 1 123 ? -11.859 10.024  17.263  1.00 18.36 ? 123 TRP A N   1 
ATOM   964  C  CA  . TRP A 1 123 ? -11.060 11.009  18.000  1.00 18.83 ? 123 TRP A CA  1 
ATOM   965  C  C   . TRP A 1 123 ? -11.949 12.002  18.746  1.00 19.14 ? 123 TRP A C   1 
ATOM   966  O  O   . TRP A 1 123 ? -13.036 12.355  18.283  1.00 18.03 ? 123 TRP A O   1 
ATOM   967  C  CB  . TRP A 1 123 ? -10.095 11.783  17.091  1.00 18.91 ? 123 TRP A CB  1 
ATOM   968  C  CG  . TRP A 1 123 ? -10.733 12.361  15.862  1.00 20.60 ? 123 TRP A CG  1 
ATOM   969  C  CD1 . TRP A 1 123 ? -10.937 11.712  14.673  1.00 22.03 ? 123 TRP A CD1 1 
ATOM   970  C  CD2 . TRP A 1 123 ? -11.201 13.705  15.670  1.00 20.55 ? 123 TRP A CD2 1 
ATOM   971  N  NE1 . TRP A 1 123 ? -11.490 12.560  13.758  1.00 23.62 ? 123 TRP A NE1 1 
ATOM   972  C  CE2 . TRP A 1 123 ? -11.640 13.795  14.329  1.00 20.91 ? 123 TRP A CE2 1 
ATOM   973  C  CE3 . TRP A 1 123 ? -11.259 14.846  16.476  1.00 20.54 ? 123 TRP A CE3 1 
ATOM   974  C  CZ2 . TRP A 1 123 ? -12.222 14.948  13.814  1.00 23.05 ? 123 TRP A CZ2 1 
ATOM   975  C  CZ3 . TRP A 1 123 ? -11.814 15.995  15.956  1.00 21.99 ? 123 TRP A CZ3 1 
ATOM   976  C  CH2 . TRP A 1 123 ? -12.282 16.046  14.637  1.00 23.02 ? 123 TRP A CH2 1 
ATOM   977  N  N   . ASN A 1 124 ? -11.413 12.487  19.871  1.00 19.62 ? 124 ASN A N   1 
ATOM   978  C  CA  . ASN A 1 124 ? -12.056 13.418  20.782  1.00 20.64 ? 124 ASN A CA  1 
ATOM   979  C  C   . ASN A 1 124 ? -12.199 14.778  20.089  1.00 21.65 ? 124 ASN A C   1 
ATOM   980  O  O   . ASN A 1 124 ? -11.197 15.425  19.763  1.00 20.98 ? 124 ASN A O   1 
ATOM   981  C  CB  . ASN A 1 124 ? -11.245 13.470  22.084  1.00 20.68 ? 124 ASN A CB  1 
ATOM   982  C  CG  . ASN A 1 124 ? -12.008 14.074  23.240  1.00 22.31 ? 124 ASN A CG  1 
ATOM   983  O  OD1 . ASN A 1 124 ? -12.791 14.993  23.053  1.00 24.63 ? 124 ASN A OD1 1 
ATOM   984  N  ND2 . ASN A 1 124 ? -11.808 13.544  24.437  1.00 26.01 ? 124 ASN A ND2 1 
ATOM   985  N  N   . THR A 1 125 ? -13.448 15.173  19.800  1.00 24.28 ? 125 THR A N   1 
ATOM   986  C  CA  . THR A 1 125 ? -13.728 16.406  19.073  1.00 25.24 ? 125 THR A CA  1 
ATOM   987  C  C   . THR A 1 125 ? -13.069 17.589  19.798  1.00 26.90 ? 125 THR A C   1 
ATOM   988  O  O   . THR A 1 125 ? -13.010 18.684  19.231  1.00 26.48 ? 125 THR A O   1 
ATOM   989  C  CB  . THR A 1 125 ? -15.242 16.614  18.901  1.00 28.73 ? 125 THR A CB  1 
ATOM   990  O  OG1 . THR A 1 125 ? -15.898 16.710  20.180  1.00 27.10 ? 125 THR A OG1 1 
ATOM   991  C  CG2 . THR A 1 125 ? -15.862 15.516  18.064  1.00 24.80 ? 125 THR A CG2 1 
ATOM   992  N  N   . LYS A 1 126 ? -12.691 17.511  21.175  1.00 26.73 ? 127 LYS A N   1 
ATOM   993  C  CA  . LYS A 1 126 ? -12.138 18.757  21.753  1.00 31.36 ? 127 LYS A CA  1 
ATOM   994  C  C   . LYS A 1 126 ? -10.756 19.063  21.181  1.00 30.51 ? 127 LYS A C   1 
ATOM   995  O  O   . LYS A 1 126 ? -10.300 20.202  21.266  1.00 30.46 ? 127 LYS A O   1 
ATOM   996  C  CB  . LYS A 1 126 ? -12.225 18.632  23.271  1.00 34.21 ? 127 LYS A CB  1 
ATOM   997  C  CG  . LYS A 1 126 ? -11.134 17.852  23.975  1.00 37.03 ? 127 LYS A CG  1 
ATOM   998  C  CD  . LYS A 1 126 ? -11.413 17.999  25.466  1.00 44.27 ? 127 LYS A CD  1 
ATOM   999  C  CE  . LYS A 1 126 ? -10.247 17.669  26.369  1.00 48.81 ? 127 LYS A CE  1 
ATOM   1000 N  NZ  . LYS A 1 126 ? -10.244 16.227  26.694  1.00 55.77 ? 127 LYS A NZ  1 
ATOM   1001 N  N   . TYR A 1 127 ? -10.146 18.079  20.503  1.00 25.11 ? 128 TYR A N   1 
ATOM   1002 C  CA  . TYR A 1 127 ? -8.825  18.258  19.926  1.00 25.37 ? 128 TYR A CA  1 
ATOM   1003 C  C   . TYR A 1 127 ? -8.855  18.609  18.446  1.00 24.90 ? 128 TYR A C   1 
ATOM   1004 O  O   . TYR A 1 127 ? -7.792  18.790  17.855  1.00 26.74 ? 128 TYR A O   1 
ATOM   1005 C  CB  . TYR A 1 127 ? -7.937  17.031  20.180  1.00 25.41 ? 128 TYR A CB  1 
ATOM   1006 C  CG  . TYR A 1 127 ? -7.819  16.774  21.656  1.00 27.21 ? 128 TYR A CG  1 
ATOM   1007 C  CD1 . TYR A 1 127 ? -7.397  17.796  22.503  1.00 31.27 ? 128 TYR A CD1 1 
ATOM   1008 C  CD2 . TYR A 1 127 ? -8.201  15.568  22.211  1.00 25.95 ? 128 TYR A CD2 1 
ATOM   1009 C  CE1 . TYR A 1 127 ? -7.318  17.602  23.870  1.00 32.39 ? 128 TYR A CE1 1 
ATOM   1010 C  CE2 . TYR A 1 127 ? -8.132  15.361  23.580  1.00 28.39 ? 128 TYR A CE2 1 
ATOM   1011 C  CZ  . TYR A 1 127 ? -7.678  16.380  24.407  1.00 32.34 ? 128 TYR A CZ  1 
ATOM   1012 O  OH  . TYR A 1 127 ? -7.605  16.186  25.759  1.00 31.07 ? 128 TYR A OH  1 
ATOM   1013 N  N   . GLY A 1 128 ? -10.037 18.647  17.823  1.00 25.77 ? 129 GLY A N   1 
ATOM   1014 C  CA  . GLY A 1 128 ? -10.122 19.287  16.515  1.00 26.61 ? 129 GLY A CA  1 
ATOM   1015 C  C   . GLY A 1 128 ? -9.717  18.409  15.329  1.00 32.73 ? 129 GLY A C   1 
ATOM   1016 O  O   . GLY A 1 128 ? -10.236 18.600  14.231  1.00 30.96 ? 129 GLY A O   1 
ATOM   1017 N  N   . ASP A 1 129 ? -8.791  17.465  15.529  1.00 27.33 ? 130 ASP A N   1 
ATOM   1018 C  CA  . ASP A 1 129 ? -8.304  16.636  14.439  1.00 31.80 ? 130 ASP A CA  1 
ATOM   1019 C  C   . ASP A 1 129 ? -7.700  15.356  15.027  1.00 27.70 ? 130 ASP A C   1 
ATOM   1020 O  O   . ASP A 1 129 ? -7.318  15.349  16.190  1.00 29.37 ? 130 ASP A O   1 
ATOM   1021 C  CB  . ASP A 1 129 ? -7.407  17.460  13.509  1.00 34.76 ? 130 ASP A CB  1 
ATOM   1022 C  CG  . ASP A 1 129 ? -6.225  16.727  12.904  1.00 46.42 ? 130 ASP A CG  1 
ATOM   1023 O  OD1 . ASP A 1 129 ? -5.210  16.543  13.634  1.00 47.92 ? 130 ASP A OD1 1 
ATOM   1024 O  OD2 . ASP A 1 129 ? -6.314  16.369  11.697  1.00 52.42 ? 130 ASP A OD2 1 
ATOM   1025 N  N   . ALA A 1 130 ? -7.685  14.276  14.237  1.00 27.82 ? 131 ALA A N   1 
ATOM   1026 C  CA  . ALA A 1 130 ? -7.184  12.971  14.650  1.00 30.45 ? 131 ALA A CA  1 
ATOM   1027 C  C   . ALA A 1 130 ? -5.689  13.052  14.963  1.00 28.55 ? 131 ALA A C   1 
ATOM   1028 O  O   . ALA A 1 130 ? -5.226  12.483  15.951  1.00 26.19 ? 131 ALA A O   1 
ATOM   1029 C  CB  . ALA A 1 130 ? -7.466  11.952  13.569  1.00 28.30 ? 131 ALA A CB  1 
ATOM   1030 N  N   . GLY A 1 131 ? -4.948  13.786  14.118  1.00 26.86 ? 132 GLY A N   1 
ATOM   1031 C  CA  . GLY A 1 131 ? -3.532  14.044  14.341  1.00 30.08 ? 132 GLY A CA  1 
ATOM   1032 C  C   . GLY A 1 131 ? -3.253  14.640  15.720  1.00 29.36 ? 132 GLY A C   1 
ATOM   1033 O  O   . GLY A 1 131 ? -2.475  14.075  16.485  1.00 29.93 ? 132 GLY A O   1 
ATOM   1034 N  N   . LYS A 1 132 ? -3.871  15.788  16.034  1.00 29.40 ? 133 LYS A N   1 
ATOM   1035 C  CA  . LYS A 1 132 ? -3.678  16.407  17.340  1.00 29.33 ? 133 LYS A CA  1 
ATOM   1036 C  C   . LYS A 1 132 ? -4.216  15.497  18.442  1.00 27.84 ? 133 LYS A C   1 
ATOM   1037 O  O   . LYS A 1 132 ? -3.631  15.431  19.515  1.00 25.88 ? 133 LYS A O   1 
ATOM   1038 C  CB  . LYS A 1 132 ? -4.327  17.794  17.446  1.00 36.06 ? 133 LYS A CB  1 
ATOM   1039 C  CG  . LYS A 1 132 ? -3.879  18.853  16.433  1.00 42.53 ? 133 LYS A CG  1 
ATOM   1040 C  CD  . LYS A 1 132 ? -2.433  19.375  16.501  1.00 46.23 ? 133 LYS A CD  1 
ATOM   1041 C  CE  . LYS A 1 132 ? -1.839  19.646  17.877  1.00 47.88 ? 133 LYS A CE  1 
ATOM   1042 N  NZ  . LYS A 1 132 ? -2.826  20.119  18.881  1.00 50.63 ? 133 LYS A NZ  1 
ATOM   1043 N  N   . ALA A 1 133 ? -5.339  14.813  18.198  1.00 24.21 ? 134 ALA A N   1 
ATOM   1044 C  CA  . ALA A 1 133 ? -5.917  13.949  19.229  1.00 26.59 ? 134 ALA A CA  1 
ATOM   1045 C  C   . ALA A 1 133 ? -4.891  12.894  19.667  1.00 23.92 ? 134 ALA A C   1 
ATOM   1046 O  O   . ALA A 1 133 ? -4.834  12.513  20.830  1.00 24.68 ? 134 ALA A O   1 
ATOM   1047 C  CB  . ALA A 1 133 ? -7.184  13.289  18.718  1.00 21.04 ? 134 ALA A CB  1 
ATOM   1048 N  N   . SER A 1 134 ? -4.077  12.417  18.724  1.00 24.90 ? 135 SER A N   1 
ATOM   1049 C  CA  . SER A 1 134 ? -3.190  11.292  19.001  1.00 27.29 ? 135 SER A CA  1 
ATOM   1050 C  C   . SER A 1 134 ? -2.043  11.716  19.925  1.00 29.41 ? 135 SER A C   1 
ATOM   1051 O  O   . SER A 1 134 ? -1.324  10.884  20.476  1.00 27.13 ? 135 SER A O   1 
ATOM   1052 C  CB  . SER A 1 134 ? -2.720  10.643  17.716  1.00 30.39 ? 135 SER A CB  1 
ATOM   1053 O  OG  . SER A 1 134 ? -1.770  11.461  17.041  1.00 32.65 ? 135 SER A OG  1 
ATOM   1054 N  N   . GLN A 1 135 ? -1.934  13.024  20.172  1.00 28.42 ? 136 GLN A N   1 
ATOM   1055 C  CA  . GLN A 1 135 ? -0.913  13.565  21.057  1.00 30.57 ? 136 GLN A CA  1 
ATOM   1056 C  C   . GLN A 1 135 ? -1.440  13.668  22.487  1.00 30.03 ? 136 GLN A C   1 
ATOM   1057 O  O   . GLN A 1 135 ? -0.758  14.180  23.367  1.00 33.18 ? 136 GLN A O   1 
ATOM   1058 C  CB  . GLN A 1 135 ? -0.485  14.946  20.551  1.00 33.27 ? 136 GLN A CB  1 
ATOM   1059 C  CG  . GLN A 1 135 ? 0.051   14.929  19.123  1.00 42.32 ? 136 GLN A CG  1 
ATOM   1060 C  CD  . GLN A 1 135 ? 1.153   13.912  18.944  1.00 51.14 ? 136 GLN A CD  1 
ATOM   1061 O  OE1 . GLN A 1 135 ? 1.902   13.596  19.869  1.00 58.49 ? 136 GLN A OE1 1 
ATOM   1062 N  NE2 . GLN A 1 135 ? 1.269   13.391  17.737  1.00 57.78 ? 136 GLN A NE2 1 
ATOM   1063 N  N   . GLN A 1 136 ? -2.650  13.174  22.735  1.00 27.83 ? 137 GLN A N   1 
ATOM   1064 C  CA  . GLN A 1 136 ? -3.284  13.450  24.020  1.00 27.70 ? 137 GLN A CA  1 
ATOM   1065 C  C   . GLN A 1 136 ? -3.631  12.142  24.712  1.00 26.03 ? 137 GLN A C   1 
ATOM   1066 O  O   . GLN A 1 136 ? -3.958  11.158  24.055  1.00 26.09 ? 137 GLN A O   1 
ATOM   1067 C  CB  . GLN A 1 136 ? -4.572  14.250  23.795  1.00 29.73 ? 137 GLN A CB  1 
ATOM   1068 C  CG  . GLN A 1 136 ? -4.346  15.535  22.999  1.00 33.52 ? 137 GLN A CG  1 
ATOM   1069 C  CD  . GLN A 1 136 ? -3.494  16.516  23.766  1.00 35.54 ? 137 GLN A CD  1 
ATOM   1070 O  OE1 . GLN A 1 136 ? -3.590  16.614  24.990  1.00 37.03 ? 137 GLN A OE1 1 
ATOM   1071 N  NE2 . GLN A 1 136 ? -2.652  17.244  23.049  1.00 36.56 ? 137 GLN A NE2 1 
ATOM   1072 N  N   . PRO A 1 137 ? -3.606  12.092  26.066  1.00 27.80 ? 138 PRO A N   1 
ATOM   1073 C  CA  . PRO A 1 137 ? -3.925  10.875  26.807  1.00 25.35 ? 138 PRO A CA  1 
ATOM   1074 C  C   . PRO A 1 137 ? -5.344  10.347  26.621  1.00 25.33 ? 138 PRO A C   1 
ATOM   1075 O  O   . PRO A 1 137 ? -5.556  9.138   26.688  1.00 26.82 ? 138 PRO A O   1 
ATOM   1076 C  CB  . PRO A 1 137 ? -3.753  11.274  28.290  1.00 28.69 ? 138 PRO A CB  1 
ATOM   1077 C  CG  . PRO A 1 137 ? -3.801  12.797  28.271  1.00 27.30 ? 138 PRO A CG  1 
ATOM   1078 C  CD  . PRO A 1 137 ? -3.197  13.204  26.943  1.00 29.24 ? 138 PRO A CD  1 
ATOM   1079 N  N   . ASP A 1 138 ? -6.297  11.263  26.390  1.00 23.00 ? 139 ASP A N   1 
ATOM   1080 C  CA  . ASP A 1 138 ? -7.688  10.908  26.151  1.00 25.28 ? 139 ASP A CA  1 
ATOM   1081 C  C   . ASP A 1 138 ? -8.076  11.268  24.712  1.00 22.69 ? 139 ASP A C   1 
ATOM   1082 O  O   . ASP A 1 138 ? -9.194  11.687  24.452  1.00 23.52 ? 139 ASP A O   1 
ATOM   1083 C  CB  . ASP A 1 138 ? -8.615  11.619  27.144  1.00 26.34 ? 139 ASP A CB  1 
ATOM   1084 C  CG  . ASP A 1 138 ? -8.490  13.132  27.131  1.00 30.74 ? 139 ASP A CG  1 
ATOM   1085 O  OD1 . ASP A 1 138 ? -7.489  13.658  26.556  1.00 35.10 ? 139 ASP A OD1 1 
ATOM   1086 O  OD2 . ASP A 1 138 ? -9.409  13.793  27.686  1.00 35.66 ? 139 ASP A OD2 1 
ATOM   1087 N  N   . GLY A 1 139 ? -7.129  11.156  23.789  1.00 22.62 ? 140 GLY A N   1 
ATOM   1088 C  CA  . GLY A 1 139 ? -7.323  11.623  22.420  1.00 19.86 ? 140 GLY A CA  1 
ATOM   1089 C  C   . GLY A 1 139 ? -8.212  10.739  21.543  1.00 21.27 ? 140 GLY A C   1 
ATOM   1090 O  O   . GLY A 1 139 ? -8.982  11.249  20.727  1.00 18.95 ? 140 GLY A O   1 
ATOM   1091 N  N   . LEU A 1 140 ? -8.085  9.412   21.701  1.00 19.07 ? 141 LEU A N   1 
ATOM   1092 C  CA  . LEU A 1 140 ? -8.743  8.468   20.816  1.00 19.97 ? 141 LEU A CA  1 
ATOM   1093 C  C   . LEU A 1 140 ? -9.582  7.495   21.641  1.00 19.29 ? 141 LEU A C   1 
ATOM   1094 O  O   . LEU A 1 140 ? -9.304  7.247   22.816  1.00 19.52 ? 141 LEU A O   1 
ATOM   1095 C  CB  . LEU A 1 140 ? -7.691  7.695   20.018  1.00 21.35 ? 141 LEU A CB  1 
ATOM   1096 C  CG  . LEU A 1 140 ? -6.803  8.486   19.060  1.00 25.44 ? 141 LEU A CG  1 
ATOM   1097 C  CD1 . LEU A 1 140 ? -6.039  7.517   18.161  1.00 27.11 ? 141 LEU A CD1 1 
ATOM   1098 C  CD2 . LEU A 1 140 ? -7.588  9.457   18.213  1.00 25.00 ? 141 LEU A CD2 1 
ATOM   1099 N  N   . ALA A 1 141 ? -10.665 7.024   21.026  1.00 19.53 ? 142 ALA A N   1 
ATOM   1100 C  CA  . ALA A 1 141 ? -11.437 5.899   21.524  1.00 20.87 ? 142 ALA A CA  1 
ATOM   1101 C  C   . ALA A 1 141 ? -11.509 4.910   20.373  1.00 20.79 ? 142 ALA A C   1 
ATOM   1102 O  O   . ALA A 1 141 ? -11.945 5.262   19.270  1.00 19.62 ? 142 ALA A O   1 
ATOM   1103 C  CB  . ALA A 1 141 ? -12.827 6.320   21.935  1.00 19.11 ? 142 ALA A CB  1 
ATOM   1104 N  N   . VAL A 1 142 ? -11.053 3.685   20.647  1.00 20.35 ? 143 VAL A N   1 
ATOM   1105 C  CA  . VAL A 1 142 ? -11.127 2.665   19.612  1.00 21.38 ? 143 VAL A CA  1 
ATOM   1106 C  C   . VAL A 1 142 ? -12.079 1.588   20.104  1.00 19.44 ? 143 VAL A C   1 
ATOM   1107 O  O   . VAL A 1 142 ? -11.942 1.135   21.241  1.00 20.12 ? 143 VAL A O   1 
ATOM   1108 C  CB  . VAL A 1 142 ? -9.744  2.093   19.227  1.00 20.89 ? 143 VAL A CB  1 
ATOM   1109 C  CG1 . VAL A 1 142 ? -9.892  1.054   18.123  1.00 20.97 ? 143 VAL A CG1 1 
ATOM   1110 C  CG2 . VAL A 1 142 ? -8.805  3.204   18.780  1.00 22.78 ? 143 VAL A CG2 1 
ATOM   1111 N  N   . LEU A 1 143 ? -13.105 1.328   19.278  1.00 18.94 ? 144 LEU A N   1 
ATOM   1112 C  CA  . LEU A 1 143 ? -14.095 0.306   19.548  1.00 19.43 ? 144 LEU A CA  1 
ATOM   1113 C  C   . LEU A 1 143 ? -13.578 -0.969  18.891  1.00 21.44 ? 144 LEU A C   1 
ATOM   1114 O  O   . LEU A 1 143 ? -13.409 -1.002  17.667  1.00 19.52 ? 144 LEU A O   1 
ATOM   1115 C  CB  . LEU A 1 143 ? -15.424 0.747   18.917  1.00 20.74 ? 144 LEU A CB  1 
ATOM   1116 C  CG  . LEU A 1 143 ? -16.611 -0.184  19.156  1.00 22.40 ? 144 LEU A CG  1 
ATOM   1117 C  CD1 . LEU A 1 143 ? -16.859 -0.348  20.652  1.00 22.09 ? 144 LEU A CD1 1 
ATOM   1118 C  CD2 . LEU A 1 143 ? -17.867 0.355   18.465  1.00 22.09 ? 144 LEU A CD2 1 
ATOM   1119 N  N   . GLY A 1 144 ? -13.267 -1.961  19.728  1.00 20.62 ? 145 GLY A N   1 
ATOM   1120 C  CA  . GLY A 1 144 ? -12.694 -3.232  19.291  1.00 18.64 ? 145 GLY A CA  1 
ATOM   1121 C  C   . GLY A 1 144 ? -13.783 -4.307  19.169  1.00 18.86 ? 145 GLY A C   1 
ATOM   1122 O  O   . GLY A 1 144 ? -14.575 -4.489  20.094  1.00 17.11 ? 145 GLY A O   1 
ATOM   1123 N  N   . ILE A 1 145 ? -13.829 -4.991  18.011  1.00 15.58 ? 146 ILE A N   1 
ATOM   1124 C  CA  . ILE A 1 145 ? -14.810 -6.046  17.802  1.00 18.03 ? 146 ILE A CA  1 
ATOM   1125 C  C   . ILE A 1 145 ? -14.109 -7.314  17.312  1.00 19.21 ? 146 ILE A C   1 
ATOM   1126 O  O   . ILE A 1 145 ? -13.432 -7.291  16.288  1.00 18.53 ? 146 ILE A O   1 
ATOM   1127 C  CB  . ILE A 1 145 ? -15.929 -5.589  16.831  1.00 18.44 ? 146 ILE A CB  1 
ATOM   1128 C  CG1 . ILE A 1 145 ? -16.579 -4.269  17.272  1.00 19.22 ? 146 ILE A CG1 1 
ATOM   1129 C  CG2 . ILE A 1 145 ? -16.950 -6.710  16.669  1.00 20.85 ? 146 ILE A CG2 1 
ATOM   1130 C  CD1 . ILE A 1 145 ? -17.715 -3.767  16.403  1.00 21.20 ? 146 ILE A CD1 1 
ATOM   1131 N  N   . PHE A 1 146 ? -14.331 -8.433  18.004  1.00 20.77 ? 147 PHE A N   1 
ATOM   1132 C  CA  . PHE A 1 146 ? -13.708 -9.698  17.616  1.00 21.11 ? 147 PHE A CA  1 
ATOM   1133 C  C   . PHE A 1 146 ? -14.477 -10.371 16.483  1.00 21.83 ? 147 PHE A C   1 
ATOM   1134 O  O   . PHE A 1 146 ? -15.704 -10.286 16.420  1.00 21.53 ? 147 PHE A O   1 
ATOM   1135 C  CB  . PHE A 1 146 ? -13.674 -10.651 18.812  1.00 20.67 ? 147 PHE A CB  1 
ATOM   1136 C  CG  . PHE A 1 146 ? -12.834 -10.182 19.969  1.00 19.77 ? 147 PHE A CG  1 
ATOM   1137 C  CD1 . PHE A 1 146 ? -11.457 -10.059 19.833  1.00 20.67 ? 147 PHE A CD1 1 
ATOM   1138 C  CD2 . PHE A 1 146 ? -13.404 -9.908  21.203  1.00 19.94 ? 147 PHE A CD2 1 
ATOM   1139 C  CE1 . PHE A 1 146 ? -10.667 -9.642  20.897  1.00 19.75 ? 147 PHE A CE1 1 
ATOM   1140 C  CE2 . PHE A 1 146 ? -12.609 -9.500  22.266  1.00 18.97 ? 147 PHE A CE2 1 
ATOM   1141 C  CZ  . PHE A 1 146 ? -11.248 -9.395  22.126  1.00 18.56 ? 147 PHE A CZ  1 
ATOM   1142 N  N   . LEU A 1 147 ? -13.743 -11.004 15.542  1.00 20.06 ? 148 LEU A N   1 
ATOM   1143 C  CA  . LEU A 1 147 ? -14.394 -11.799 14.520  1.00 19.25 ? 148 LEU A CA  1 
ATOM   1144 C  C   . LEU A 1 147 ? -14.091 -13.271 14.791  1.00 19.04 ? 148 LEU A C   1 
ATOM   1145 O  O   . LEU A 1 147 ? -12.916 -13.633 14.919  1.00 18.91 ? 148 LEU A O   1 
ATOM   1146 C  CB  . LEU A 1 147 ? -13.830 -11.432 13.138  1.00 18.01 ? 148 LEU A CB  1 
ATOM   1147 C  CG  . LEU A 1 147 ? -14.403 -10.190 12.453  1.00 17.90 ? 148 LEU A CG  1 
ATOM   1148 C  CD1 . LEU A 1 147 ? -14.060 -8.922  13.245  1.00 18.06 ? 148 LEU A CD1 1 
ATOM   1149 C  CD2 . LEU A 1 147 ? -13.773 -10.081 11.061  1.00 17.30 ? 148 LEU A CD2 1 
ATOM   1150 N  N   . LYS A 1 148 ? -15.150 -14.092 14.805  1.00 21.61 ? 149 LYS A N   1 
ATOM   1151 C  CA  . LYS A 1 148 ? -15.016 -15.541 14.803  1.00 24.20 ? 149 LYS A CA  1 
ATOM   1152 C  C   . LYS A 1 148 ? -15.517 -16.099 13.472  1.00 23.25 ? 149 LYS A C   1 
ATOM   1153 O  O   . LYS A 1 148 ? -16.382 -15.507 12.832  1.00 22.36 ? 149 LYS A O   1 
ATOM   1154 C  CB  . LYS A 1 148 ? -15.709 -16.191 16.002  1.00 28.33 ? 149 LYS A CB  1 
ATOM   1155 C  CG  . LYS A 1 148 ? -17.224 -16.304 15.936  1.00 33.85 ? 149 LYS A CG  1 
ATOM   1156 C  CD  . LYS A 1 148 ? -17.786 -16.884 17.227  1.00 38.89 ? 149 LYS A CD  1 
ATOM   1157 C  CE  . LYS A 1 148 ? -19.298 -16.969 17.216  1.00 45.08 ? 149 LYS A CE  1 
ATOM   1158 N  NZ  . LYS A 1 148 ? -19.867 -16.592 18.534  1.00 54.03 ? 149 LYS A NZ  1 
ATOM   1159 N  N   . VAL A 1 149 ? -14.987 -17.264 13.080  1.00 21.81 ? 150 VAL A N   1 
ATOM   1160 C  CA  . VAL A 1 149 ? -15.336 -17.816 11.781  1.00 25.24 ? 150 VAL A CA  1 
ATOM   1161 C  C   . VAL A 1 149 ? -16.510 -18.777 11.949  1.00 25.50 ? 150 VAL A C   1 
ATOM   1162 O  O   . VAL A 1 149 ? -16.460 -19.695 12.778  1.00 22.80 ? 150 VAL A O   1 
ATOM   1163 C  CB  . VAL A 1 149 ? -14.126 -18.473 11.087  1.00 25.79 ? 150 VAL A CB  1 
ATOM   1164 C  CG1 . VAL A 1 149 ? -14.528 -19.212 9.816   1.00 25.63 ? 150 VAL A CG1 1 
ATOM   1165 C  CG2 . VAL A 1 149 ? -13.060 -17.434 10.772  1.00 27.45 ? 150 VAL A CG2 1 
ATOM   1166 N  N   . GLY A 1 150 ? -17.567 -18.519 11.165  1.00 22.89 ? 151 GLY A N   1 
ATOM   1167 C  CA  . GLY A 1 150 ? -18.788 -19.306 11.202  1.00 22.88 ? 151 GLY A CA  1 
ATOM   1168 C  C   . GLY A 1 150 ? -19.735 -18.857 10.095  1.00 21.18 ? 151 GLY A C   1 
ATOM   1169 O  O   . GLY A 1 150 ? -19.374 -18.881 8.922   1.00 21.12 ? 151 GLY A O   1 
ATOM   1170 N  N   . SER A 1 151 ? -20.920 -18.381 10.470  1.00 22.63 ? 152 SER A N   1 
ATOM   1171 C  CA  . SER A 1 151 ? -21.784 -17.801 9.439   1.00 24.18 ? 152 SER A CA  1 
ATOM   1172 C  C   . SER A 1 151 ? -21.206 -16.476 8.948   1.00 24.53 ? 152 SER A C   1 
ATOM   1173 O  O   . SER A 1 151 ? -20.419 -15.832 9.638   1.00 21.68 ? 152 SER A O   1 
ATOM   1174 C  CB  . SER A 1 151 ? -23.182 -17.614 9.948   1.00 28.09 ? 152 SER A CB  1 
ATOM   1175 O  OG  . SER A 1 151 ? -23.136 -17.481 11.352  1.00 35.08 ? 152 SER A OG  1 
ATOM   1176 N  N   . ALA A 1 152 ? -21.605 -16.080 7.740   1.00 24.17 ? 153 ALA A N   1 
ATOM   1177 C  CA  . ALA A 1 152 ? -21.128 -14.840 7.159   1.00 24.23 ? 153 ALA A CA  1 
ATOM   1178 C  C   . ALA A 1 152 ? -21.803 -13.646 7.836   1.00 24.62 ? 153 ALA A C   1 
ATOM   1179 O  O   . ALA A 1 152 ? -22.905 -13.759 8.361   1.00 25.24 ? 153 ALA A O   1 
ATOM   1180 C  CB  . ALA A 1 152 ? -21.365 -14.861 5.670   1.00 26.64 ? 153 ALA A CB  1 
ATOM   1181 N  N   . LYS A 1 153 ? -21.086 -12.516 7.863   1.00 21.93 ? 154 LYS A N   1 
ATOM   1182 C  CA  . LYS A 1 153 ? -21.629 -11.232 8.242   1.00 22.49 ? 154 LYS A CA  1 
ATOM   1183 C  C   . LYS A 1 153 ? -22.035 -10.511 6.960   1.00 22.40 ? 154 LYS A C   1 
ATOM   1184 O  O   . LYS A 1 153 ? -21.180 -10.093 6.187   1.00 22.93 ? 154 LYS A O   1 
ATOM   1185 C  CB  . LYS A 1 153 ? -20.559 -10.445 9.012   1.00 20.95 ? 154 LYS A CB  1 
ATOM   1186 C  CG  . LYS A 1 153 ? -21.107 -9.210  9.702   1.00 22.14 ? 154 LYS A CG  1 
ATOM   1187 C  CD  . LYS A 1 153 ? -22.007 -9.606  10.859  1.00 23.44 ? 154 LYS A CD  1 
ATOM   1188 C  CE  . LYS A 1 153 ? -22.261 -8.449  11.807  1.00 28.96 ? 154 LYS A CE  1 
ATOM   1189 N  NZ  . LYS A 1 153 ? -23.301 -8.801  12.810  1.00 29.59 ? 154 LYS A NZ  1 
ATOM   1190 N  N   . PRO A 1 154 ? -23.345 -10.352 6.675   1.00 23.52 ? 155 PRO A N   1 
ATOM   1191 C  CA  . PRO A 1 154 ? -23.778 -9.771  5.401   1.00 22.63 ? 155 PRO A CA  1 
ATOM   1192 C  C   . PRO A 1 154 ? -23.310 -8.332  5.241   1.00 21.21 ? 155 PRO A C   1 
ATOM   1193 O  O   . PRO A 1 154 ? -23.002 -7.905  4.139   1.00 21.68 ? 155 PRO A O   1 
ATOM   1194 C  CB  . PRO A 1 154 ? -25.308 -9.869  5.450   1.00 24.71 ? 155 PRO A CB  1 
ATOM   1195 C  CG  . PRO A 1 154 ? -25.570 -10.912 6.532   1.00 27.00 ? 155 PRO A CG  1 
ATOM   1196 C  CD  . PRO A 1 154 ? -24.471 -10.699 7.558   1.00 23.89 ? 155 PRO A CD  1 
ATOM   1197 N  N   . GLY A 1 155 ? -23.168 -7.615  6.366   1.00 20.04 ? 156 GLY A N   1 
ATOM   1198 C  CA  . GLY A 1 155 ? -22.765 -6.218  6.328   1.00 21.90 ? 156 GLY A CA  1 
ATOM   1199 C  C   . GLY A 1 155 ? -21.276 -6.028  6.040   1.00 21.33 ? 156 GLY A C   1 
ATOM   1200 O  O   . GLY A 1 155 ? -20.867 -4.894  5.860   1.00 24.24 ? 156 GLY A O   1 
ATOM   1201 N  N   . LEU A 1 156 ? -20.466 -7.106  6.088   1.00 18.96 ? 157 LEU A N   1 
ATOM   1202 C  CA  . LEU A 1 156 ? -19.045 -7.057  5.770   1.00 19.10 ? 157 LEU A CA  1 
ATOM   1203 C  C   . LEU A 1 156 ? -18.821 -7.274  4.279   1.00 20.38 ? 157 LEU A C   1 
ATOM   1204 O  O   . LEU A 1 156 ? -17.744 -7.012  3.745   1.00 21.35 ? 157 LEU A O   1 
ATOM   1205 C  CB  . LEU A 1 156 ? -18.327 -8.158  6.568   1.00 19.49 ? 157 LEU A CB  1 
ATOM   1206 C  CG  . LEU A 1 156 ? -16.799 -8.198  6.457   1.00 21.62 ? 157 LEU A CG  1 
ATOM   1207 C  CD1 . LEU A 1 156 ? -16.183 -6.908  6.973   1.00 23.13 ? 157 LEU A CD1 1 
ATOM   1208 C  CD2 . LEU A 1 156 ? -16.268 -9.393  7.255   1.00 21.32 ? 157 LEU A CD2 1 
ATOM   1209 N  N   . GLN A 1 157 ? -19.848 -7.805  3.614   1.00 22.39 ? 158 GLN A N   1 
ATOM   1210 C  CA  . GLN A 1 157 ? -19.645 -8.291  2.260   1.00 21.29 ? 158 GLN A CA  1 
ATOM   1211 C  C   . GLN A 1 157 ? -19.183 -7.193  1.305   1.00 22.23 ? 158 GLN A C   1 
ATOM   1212 O  O   . GLN A 1 157 ? -18.379 -7.476  0.420   1.00 21.92 ? 158 GLN A O   1 
ATOM   1213 C  CB  . GLN A 1 157 ? -20.846 -9.109  1.773   1.00 22.30 ? 158 GLN A CB  1 
ATOM   1214 C  CG  . GLN A 1 157 ? -20.536 -9.899  0.488   1.00 23.40 ? 158 GLN A CG  1 
ATOM   1215 C  CD  . GLN A 1 157 ? -19.432 -10.913 0.683   1.00 21.86 ? 158 GLN A CD  1 
ATOM   1216 O  OE1 . GLN A 1 157 ? -19.231 -11.443 1.774   1.00 22.81 ? 158 GLN A OE1 1 
ATOM   1217 N  NE2 . GLN A 1 157 ? -18.694 -11.220 -0.374  1.00 23.31 ? 158 GLN A NE2 1 
ATOM   1218 N  N   . LYS A 1 158 ? -19.712 -5.967  1.436   1.00 23.10 ? 159 LYS A N   1 
ATOM   1219 C  CA  . LYS A 1 158 ? -19.347 -4.885  0.532   1.00 22.44 ? 159 LYS A CA  1 
ATOM   1220 C  C   . LYS A 1 158 ? -17.845 -4.619  0.641   1.00 23.21 ? 159 LYS A C   1 
ATOM   1221 O  O   . LYS A 1 158 ? -17.182 -4.337  -0.352  1.00 21.86 ? 159 LYS A O   1 
ATOM   1222 C  CB  . LYS A 1 158 ? -20.221 -3.641  0.782   1.00 26.73 ? 159 LYS A CB  1 
ATOM   1223 C  CG  . LYS A 1 158 ? -19.897 -2.385  -0.027  1.00 31.98 ? 159 LYS A CG  1 
ATOM   1224 C  CD  . LYS A 1 158 ? -20.872 -1.224  0.232   1.00 37.25 ? 159 LYS A CD  1 
ATOM   1225 C  CE  . LYS A 1 158 ? -20.455 0.112   -0.372  1.00 38.75 ? 159 LYS A CE  1 
ATOM   1226 N  NZ  . LYS A 1 158 ? -20.802 0.224   -1.817  1.00 34.15 ? 159 LYS A NZ  1 
ATOM   1227 N  N   . VAL A 1 159 ? -17.296 -4.750  1.854   1.00 20.42 ? 160 VAL A N   1 
ATOM   1228 C  CA  . VAL A 1 159 ? -15.857 -4.579  2.063   1.00 20.88 ? 160 VAL A CA  1 
ATOM   1229 C  C   . VAL A 1 159 ? -15.069 -5.688  1.359   1.00 19.94 ? 160 VAL A C   1 
ATOM   1230 O  O   . VAL A 1 159 ? -14.110 -5.436  0.630   1.00 22.46 ? 160 VAL A O   1 
ATOM   1231 C  CB  . VAL A 1 159 ? -15.527 -4.596  3.557   1.00 21.82 ? 160 VAL A CB  1 
ATOM   1232 C  CG1 . VAL A 1 159 ? -14.009 -4.647  3.763   1.00 22.11 ? 160 VAL A CG1 1 
ATOM   1233 C  CG2 . VAL A 1 159 ? -16.121 -3.390  4.254   1.00 22.06 ? 160 VAL A CG2 1 
ATOM   1234 N  N   . VAL A 1 160 ? -15.465 -6.944  1.577   1.00 19.44 ? 161 VAL A N   1 
ATOM   1235 C  CA  . VAL A 1 160 ? -14.699 -8.079  1.084   1.00 21.27 ? 161 VAL A CA  1 
ATOM   1236 C  C   . VAL A 1 160 ? -14.709 -8.095  -0.451  1.00 21.69 ? 161 VAL A C   1 
ATOM   1237 O  O   . VAL A 1 160 ? -13.711 -8.437  -1.097  1.00 22.89 ? 161 VAL A O   1 
ATOM   1238 C  CB  . VAL A 1 160 ? -15.271 -9.337  1.768   1.00 28.56 ? 161 VAL A CB  1 
ATOM   1239 C  CG1 . VAL A 1 160 ? -15.386 -10.574 0.900   1.00 31.31 ? 161 VAL A CG1 1 
ATOM   1240 C  CG2 . VAL A 1 160 ? -14.573 -9.571  3.096   1.00 28.66 ? 161 VAL A CG2 1 
ATOM   1241 N  N   . ASP A 1 161 ? -15.807 -7.633  -1.041  1.00 22.10 ? 162 ASP A N   1 
ATOM   1242 C  CA  . ASP A 1 161 ? -15.916 -7.678  -2.495  1.00 23.97 ? 162 ASP A CA  1 
ATOM   1243 C  C   . ASP A 1 161 ? -15.021 -6.683  -3.234  1.00 25.92 ? 162 ASP A C   1 
ATOM   1244 O  O   . ASP A 1 161 ? -14.881 -6.811  -4.458  1.00 23.81 ? 162 ASP A O   1 
ATOM   1245 C  CB  . ASP A 1 161 ? -17.357 -7.567  -2.989  1.00 25.44 ? 162 ASP A CB  1 
ATOM   1246 C  CG  . ASP A 1 161 ? -18.089 -8.896  -2.891  1.00 30.76 ? 162 ASP A CG  1 
ATOM   1247 O  OD1 . ASP A 1 161 ? -17.414 -9.968  -2.819  1.00 29.91 ? 162 ASP A OD1 1 
ATOM   1248 O  OD2 . ASP A 1 161 ? -19.330 -8.852  -2.872  1.00 33.68 ? 162 ASP A OD2 1 
ATOM   1249 N  N   . VAL A 1 162 ? -14.433 -5.695  -2.554  1.00 22.37 ? 163 VAL A N   1 
ATOM   1250 C  CA  . VAL A 1 162 ? -13.584 -4.736  -3.277  1.00 22.75 ? 163 VAL A CA  1 
ATOM   1251 C  C   . VAL A 1 162 ? -12.097 -4.943  -3.000  1.00 21.85 ? 163 VAL A C   1 
ATOM   1252 O  O   . VAL A 1 162 ? -11.282 -4.221  -3.573  1.00 21.70 ? 163 VAL A O   1 
ATOM   1253 C  CB  . VAL A 1 162 ? -13.964 -3.253  -3.052  1.00 23.89 ? 163 VAL A CB  1 
ATOM   1254 C  CG1 . VAL A 1 162 ? -15.357 -2.942  -3.570  1.00 27.75 ? 163 VAL A CG1 1 
ATOM   1255 C  CG2 . VAL A 1 162 ? -13.818 -2.824  -1.593  1.00 23.76 ? 163 VAL A CG2 1 
ATOM   1256 N  N   . LEU A 1 163 ? -11.739 -5.923  -2.156  1.00 21.18 ? 164 LEU A N   1 
ATOM   1257 C  CA  . LEU A 1 163 ? -10.351 -6.061  -1.740  1.00 20.45 ? 164 LEU A CA  1 
ATOM   1258 C  C   . LEU A 1 163 ? -9.450  -6.425  -2.920  1.00 21.47 ? 164 LEU A C   1 
ATOM   1259 O  O   . LEU A 1 163 ? -8.270  -6.072  -2.899  1.00 20.73 ? 164 LEU A O   1 
ATOM   1260 C  CB  . LEU A 1 163 ? -10.221 -7.061  -0.596  1.00 21.43 ? 164 LEU A CB  1 
ATOM   1261 C  CG  . LEU A 1 163 ? -10.889 -6.610  0.703   1.00 22.58 ? 164 LEU A CG  1 
ATOM   1262 C  CD1 . LEU A 1 163 ? -10.829 -7.724  1.736   1.00 21.83 ? 164 LEU A CD1 1 
ATOM   1263 C  CD2 . LEU A 1 163 ? -10.269 -5.323  1.231   1.00 20.05 ? 164 LEU A CD2 1 
ATOM   1264 N  N   . ASP A 1 164 ? -10.006 -7.128  -3.913  1.00 23.35 ? 165 ASP A N   1 
ATOM   1265 C  CA  . ASP A 1 164 ? -9.238  -7.518  -5.092  1.00 27.71 ? 165 ASP A CA  1 
ATOM   1266 C  C   . ASP A 1 164 ? -8.711  -6.276  -5.819  1.00 28.26 ? 165 ASP A C   1 
ATOM   1267 O  O   . ASP A 1 164 ? -7.760  -6.372  -6.604  1.00 28.63 ? 165 ASP A O   1 
ATOM   1268 C  CB  . ASP A 1 164 ? -10.093 -8.346  -6.067  1.00 30.91 ? 165 ASP A CB  1 
ATOM   1269 C  CG  . ASP A 1 164 ? -11.104 -7.492  -6.823  1.00 35.13 ? 165 ASP A CG  1 
ATOM   1270 O  OD1 . ASP A 1 164 ? -12.073 -7.009  -6.181  1.00 39.90 ? 165 ASP A OD1 1 
ATOM   1271 O  OD2 . ASP A 1 164 ? -10.898 -7.246  -8.045  1.00 36.55 ? 165 ASP A OD2 1 
ATOM   1272 N  N   . SER A 1 165 ? -9.355  -5.119  -5.603  1.00 26.05 ? 166 SER A N   1 
ATOM   1273 C  CA  . SER A 1 165 ? -8.965  -3.890  -6.283  1.00 27.57 ? 166 SER A CA  1 
ATOM   1274 C  C   . SER A 1 165 ? -7.901  -3.096  -5.502  1.00 25.65 ? 166 SER A C   1 
ATOM   1275 O  O   . SER A 1 165 ? -7.398  -2.084  -5.995  1.00 24.27 ? 166 SER A O   1 
ATOM   1276 C  CB  . SER A 1 165 ? -10.198 -3.068  -6.562  1.00 31.64 ? 166 SER A CB  1 
ATOM   1277 O  OG  . SER A 1 165 ? -10.674 -2.499  -5.346  1.00 29.36 ? 166 SER A OG  1 
ATOM   1278 N  N   . ILE A 1 166 ? -7.588  -3.500  -4.259  1.00 22.42 ? 167 ILE A N   1 
ATOM   1279 C  CA  . ILE A 1 166 ? -6.537  -2.845  -3.479  1.00 21.81 ? 167 ILE A CA  1 
ATOM   1280 C  C   . ILE A 1 166 ? -5.544  -3.901  -2.994  1.00 22.50 ? 167 ILE A C   1 
ATOM   1281 O  O   . ILE A 1 166 ? -5.173  -3.925  -1.828  1.00 20.97 ? 167 ILE A O   1 
ATOM   1282 C  CB  . ILE A 1 166 ? -7.113  -2.024  -2.290  1.00 20.36 ? 167 ILE A CB  1 
ATOM   1283 C  CG1 . ILE A 1 166 ? -7.981  -2.875  -1.360  1.00 20.48 ? 167 ILE A CG1 1 
ATOM   1284 C  CG2 . ILE A 1 166 ? -7.846  -0.783  -2.804  1.00 21.98 ? 167 ILE A CG2 1 
ATOM   1285 C  CD1 . ILE A 1 166 ? -8.137  -2.302  0.064   1.00 19.10 ? 167 ILE A CD1 1 
ATOM   1286 N  N   . LYS A 1 167 ? -5.141  -4.816  -3.890  1.00 21.29 ? 168 LYS A N   1 
ATOM   1287 C  CA  . LYS A 1 167 ? -4.322  -5.942  -3.469  1.00 24.10 ? 168 LYS A CA  1 
ATOM   1288 C  C   . LYS A 1 167 ? -2.995  -5.509  -2.823  1.00 23.27 ? 168 LYS A C   1 
ATOM   1289 O  O   . LYS A 1 167 ? -2.586  -6.119  -1.835  1.00 22.37 ? 168 LYS A O   1 
ATOM   1290 C  CB  . LYS A 1 167 ? -4.000  -6.823  -4.671  1.00 25.13 ? 168 LYS A CB  1 
ATOM   1291 C  CG  . LYS A 1 167 ? -3.393  -8.166  -4.299  1.00 30.94 ? 168 LYS A CG  1 
ATOM   1292 C  CD  . LYS A 1 167 ? -2.836  -8.842  -5.545  1.00 35.58 ? 168 LYS A CD  1 
ATOM   1293 C  CE  . LYS A 1 167 ? -2.080  -10.116 -5.249  1.00 40.81 ? 168 LYS A CE  1 
ATOM   1294 N  NZ  . LYS A 1 167 ? -0.897  -10.240 -6.137  1.00 46.29 ? 168 LYS A NZ  1 
ATOM   1295 N  N   . THR A 1 168 ? -2.338  -4.460  -3.355  1.00 23.29 ? 169 THR A N   1 
ATOM   1296 C  CA  . THR A 1 168 ? -0.964  -4.174  -2.947  1.00 23.29 ? 169 THR A CA  1 
ATOM   1297 C  C   . THR A 1 168 ? -0.843  -2.809  -2.276  1.00 23.96 ? 169 THR A C   1 
ATOM   1298 O  O   . THR A 1 168 ? -1.685  -1.927  -2.441  1.00 23.44 ? 169 THR A O   1 
ATOM   1299 C  CB  . THR A 1 168 ? 0.026   -4.335  -4.112  1.00 24.15 ? 169 THR A CB  1 
ATOM   1300 O  OG1 . THR A 1 168 ? -0.553  -3.590  -5.182  1.00 26.08 ? 169 THR A OG1 1 
ATOM   1301 C  CG2 . THR A 1 168 ? 0.253   -5.788  -4.496  1.00 24.01 ? 169 THR A CG2 1 
ATOM   1302 N  N   . LYS A 1 169 ? 0.248   -2.653  -1.524  1.00 23.93 ? 170 LYS A N   1 
ATOM   1303 C  CA  . LYS A 1 169 ? 0.513   -1.438  -0.766  1.00 25.65 ? 170 LYS A CA  1 
ATOM   1304 C  C   . LYS A 1 169 ? 0.350   -0.216  -1.664  1.00 28.24 ? 170 LYS A C   1 
ATOM   1305 O  O   . LYS A 1 169 ? 0.848   -0.196  -2.795  1.00 29.08 ? 170 LYS A O   1 
ATOM   1306 C  CB  . LYS A 1 169 ? 1.910   -1.513  -0.147  1.00 25.35 ? 170 LYS A CB  1 
ATOM   1307 C  CG  . LYS A 1 169 ? 2.349   -0.239  0.566   1.00 29.69 ? 170 LYS A CG  1 
ATOM   1308 C  CD  . LYS A 1 169 ? 3.773   -0.269  1.028   1.00 31.97 ? 170 LYS A CD  1 
ATOM   1309 C  CE  . LYS A 1 169 ? 4.134   0.955   1.841   1.00 36.24 ? 170 LYS A CE  1 
ATOM   1310 N  NZ  . LYS A 1 169 ? 3.719   0.770   3.255   1.00 39.51 ? 170 LYS A NZ  1 
ATOM   1311 N  N   . GLY A 1 170 ? -0.425  0.756   -1.172  1.00 27.27 ? 171 GLY A N   1 
ATOM   1312 C  CA  . GLY A 1 170 ? -0.609  2.047   -1.811  1.00 27.76 ? 171 GLY A CA  1 
ATOM   1313 C  C   . GLY A 1 170 ? -1.735  2.105   -2.834  1.00 28.25 ? 171 GLY A C   1 
ATOM   1314 O  O   . GLY A 1 170 ? -1.927  3.144   -3.474  1.00 31.19 ? 171 GLY A O   1 
ATOM   1315 N  N   . LYS A 1 171 ? -2.448  0.983   -3.023  1.00 25.31 ? 172 LYS A N   1 
ATOM   1316 C  CA  . LYS A 1 171 ? -3.640  1.021   -3.851  1.00 23.76 ? 172 LYS A CA  1 
ATOM   1317 C  C   . LYS A 1 171 ? -4.832  1.466   -3.009  1.00 23.75 ? 172 LYS A C   1 
ATOM   1318 O  O   . LYS A 1 171 ? -4.920  1.179   -1.810  1.00 24.32 ? 172 LYS A O   1 
ATOM   1319 C  CB  . LYS A 1 171 ? -3.882  -0.315  -4.559  1.00 24.75 ? 172 LYS A CB  1 
ATOM   1320 C  CG  . LYS A 1 171 ? -2.822  -0.689  -5.590  1.00 27.01 ? 172 LYS A CG  1 
ATOM   1321 C  CD  . LYS A 1 171 ? -3.231  -1.823  -6.515  1.00 33.78 ? 172 LYS A CD  1 
ATOM   1322 C  CE  . LYS A 1 171 ? -4.399  -1.452  -7.412  1.00 36.23 ? 172 LYS A CE  1 
ATOM   1323 N  NZ  . LYS A 1 171 ? -4.885  -2.587  -8.242  1.00 40.65 ? 172 LYS A NZ  1 
ATOM   1324 N  N   . SER A 1 172 ? -5.730  2.204   -3.657  1.00 23.56 ? 173 SER A N   1 
ATOM   1325 C  CA  . SER A 1 172 ? -6.925  2.720   -3.000  1.00 24.33 ? 173 SER A CA  1 
ATOM   1326 C  C   . SER A 1 172 ? -8.085  2.777   -3.988  1.00 26.54 ? 173 SER A C   1 
ATOM   1327 O  O   . SER A 1 172 ? -7.900  2.723   -5.215  1.00 24.18 ? 173 SER A O   1 
ATOM   1328 C  CB  . SER A 1 172 ? -6.674  4.080   -2.355  1.00 28.70 ? 173 SER A CB  1 
ATOM   1329 O  OG  . SER A 1 172 ? -6.406  5.074   -3.329  1.00 27.25 ? 173 SER A OG  1 
ATOM   1330 N  N   . ALA A 1 173 ? -9.296  2.930   -3.447  1.00 24.83 ? 174 ALA A N   1 
ATOM   1331 C  CA  . ALA A 1 173 ? -10.473 3.076   -4.290  1.00 24.35 ? 174 ALA A CA  1 
ATOM   1332 C  C   . ALA A 1 173 ? -11.551 3.895   -3.584  1.00 27.30 ? 174 ALA A C   1 
ATOM   1333 O  O   . ALA A 1 173 ? -11.635 3.913   -2.345  1.00 23.76 ? 174 ALA A O   1 
ATOM   1334 C  CB  . ALA A 1 173 ? -11.008 1.709   -4.624  1.00 27.92 ? 174 ALA A CB  1 
ATOM   1335 N  N   . ASP A 1 174 ? -12.440 4.488   -4.391  1.00 27.74 ? 175 ASP A N   1 
ATOM   1336 C  CA  . ASP A 1 174 ? -13.602 5.149   -3.824  1.00 31.77 ? 175 ASP A CA  1 
ATOM   1337 C  C   . ASP A 1 174 ? -14.411 4.094   -3.085  1.00 26.38 ? 175 ASP A C   1 
ATOM   1338 O  O   . ASP A 1 174 ? -14.519 2.948   -3.523  1.00 22.85 ? 175 ASP A O   1 
ATOM   1339 C  CB  . ASP A 1 174 ? -14.456 5.843   -4.894  1.00 38.09 ? 175 ASP A CB  1 
ATOM   1340 C  CG  . ASP A 1 174 ? -13.688 6.855   -5.736  1.00 50.68 ? 175 ASP A CG  1 
ATOM   1341 O  OD1 . ASP A 1 174 ? -13.069 7.777   -5.139  1.00 45.31 ? 175 ASP A OD1 1 
ATOM   1342 O  OD2 . ASP A 1 174 ? -13.711 6.717   -6.992  1.00 56.72 ? 175 ASP A OD2 1 
ATOM   1343 N  N   . PHE A 1 175 ? -14.989 4.492   -1.948  1.00 24.51 ? 176 PHE A N   1 
ATOM   1344 C  CA  . PHE A 1 175 ? -15.770 3.541   -1.180  1.00 21.61 ? 176 PHE A CA  1 
ATOM   1345 C  C   . PHE A 1 175 ? -16.868 4.274   -0.411  1.00 23.79 ? 176 PHE A C   1 
ATOM   1346 O  O   . PHE A 1 175 ? -16.752 4.484   0.810   1.00 23.26 ? 176 PHE A O   1 
ATOM   1347 C  CB  . PHE A 1 175 ? -14.838 2.713   -0.274  1.00 21.20 ? 176 PHE A CB  1 
ATOM   1348 C  CG  . PHE A 1 175 ? -15.470 1.458   0.281   1.00 20.99 ? 176 PHE A CG  1 
ATOM   1349 C  CD1 . PHE A 1 175 ? -15.815 0.405   -0.550  1.00 21.99 ? 176 PHE A CD1 1 
ATOM   1350 C  CD2 . PHE A 1 175 ? -15.740 1.332   1.638   1.00 18.17 ? 176 PHE A CD2 1 
ATOM   1351 C  CE1 . PHE A 1 175 ? -16.358 -0.771  -0.038  1.00 22.08 ? 176 PHE A CE1 1 
ATOM   1352 C  CE2 . PHE A 1 175 ? -16.289 0.165   2.150   1.00 19.89 ? 176 PHE A CE2 1 
ATOM   1353 C  CZ  . PHE A 1 175 ? -16.600 -0.890  1.318   1.00 19.46 ? 176 PHE A CZ  1 
ATOM   1354 N  N   . THR A 1 176 ? -17.961 4.613   -1.112  1.00 24.47 ? 177 THR A N   1 
ATOM   1355 C  CA  . THR A 1 176 ? -19.026 5.379   -0.481  1.00 23.77 ? 177 THR A CA  1 
ATOM   1356 C  C   . THR A 1 176 ? -20.215 4.523   -0.065  1.00 23.36 ? 177 THR A C   1 
ATOM   1357 O  O   . THR A 1 176 ? -20.383 3.394   -0.521  1.00 25.13 ? 177 THR A O   1 
ATOM   1358 C  CB  . THR A 1 176 ? -19.497 6.514   -1.388  1.00 26.89 ? 177 THR A CB  1 
ATOM   1359 O  OG1 . THR A 1 176 ? -19.896 5.898   -2.615  1.00 27.13 ? 177 THR A OG1 1 
ATOM   1360 C  CG2 . THR A 1 176 ? -18.414 7.554   -1.598  1.00 27.72 ? 177 THR A CG2 1 
ATOM   1361 N  N   . ASN A 1 177 ? -21.021 5.101   0.833   1.00 22.66 ? 178 ASN A N   1 
ATOM   1362 C  CA  . ASN A 1 177 ? -22.279 4.543   1.293   1.00 23.63 ? 178 ASN A CA  1 
ATOM   1363 C  C   . ASN A 1 177 ? -22.082 3.190   1.976   1.00 24.83 ? 178 ASN A C   1 
ATOM   1364 O  O   . ASN A 1 177 ? -22.980 2.340   1.936   1.00 24.14 ? 178 ASN A O   1 
ATOM   1365 C  CB  . ASN A 1 177 ? -23.269 4.378   0.147   1.00 23.40 ? 178 ASN A CB  1 
ATOM   1366 C  CG  . ASN A 1 177 ? -23.612 5.734   -0.427  1.00 24.92 ? 178 ASN A CG  1 
ATOM   1367 O  OD1 . ASN A 1 177 ? -24.309 6.509   0.218   1.00 24.11 ? 178 ASN A OD1 1 
ATOM   1368 N  ND2 . ASN A 1 177 ? -23.052 6.034   -1.587  1.00 20.81 ? 178 ASN A ND2 1 
ATOM   1369 N  N   . PHE A 1 178 ? -20.934 3.014   2.617   1.00 22.02 ? 179 PHE A N   1 
ATOM   1370 C  CA  . PHE A 1 178 ? -20.772 1.822   3.427   1.00 20.77 ? 179 PHE A CA  1 
ATOM   1371 C  C   . PHE A 1 178 ? -21.277 2.137   4.830   1.00 20.47 ? 179 PHE A C   1 
ATOM   1372 O  O   . PHE A 1 178 ? -20.824 3.102   5.439   1.00 23.39 ? 179 PHE A O   1 
ATOM   1373 C  CB  . PHE A 1 178 ? -19.311 1.363   3.452   1.00 21.71 ? 179 PHE A CB  1 
ATOM   1374 C  CG  . PHE A 1 178 ? -19.173 0.166   4.351   1.00 21.17 ? 179 PHE A CG  1 
ATOM   1375 C  CD1 . PHE A 1 178 ? -19.565 -1.084  3.897   1.00 22.30 ? 179 PHE A CD1 1 
ATOM   1376 C  CD2 . PHE A 1 178 ? -18.852 0.328   5.697   1.00 21.53 ? 179 PHE A CD2 1 
ATOM   1377 C  CE1 . PHE A 1 178 ? -19.543 -2.174  4.755   1.00 23.19 ? 179 PHE A CE1 1 
ATOM   1378 C  CE2 . PHE A 1 178 ? -18.841 -0.760  6.555   1.00 21.58 ? 179 PHE A CE2 1 
ATOM   1379 C  CZ  . PHE A 1 178 ? -19.188 -2.009  6.083   1.00 22.75 ? 179 PHE A CZ  1 
ATOM   1380 N  N   . ASP A 1 179 ? -22.180 1.297   5.340   1.00 20.06 ? 180 ASP A N   1 
ATOM   1381 C  CA  . ASP A 1 179 ? -22.759 1.523   6.658   1.00 20.64 ? 180 ASP A CA  1 
ATOM   1382 C  C   . ASP A 1 179 ? -22.035 0.703   7.722   1.00 19.96 ? 180 ASP A C   1 
ATOM   1383 O  O   . ASP A 1 179 ? -22.228 -0.517  7.806   1.00 19.28 ? 180 ASP A O   1 
ATOM   1384 C  CB  . ASP A 1 179 ? -24.224 1.099   6.657   1.00 24.62 ? 180 ASP A CB  1 
ATOM   1385 C  CG  . ASP A 1 179 ? -24.968 1.543   7.904   1.00 24.67 ? 180 ASP A CG  1 
ATOM   1386 O  OD1 . ASP A 1 179 ? -24.326 1.856   8.896   1.00 23.05 ? 180 ASP A OD1 1 
ATOM   1387 O  OD2 . ASP A 1 179 ? -26.195 1.555   7.847   1.00 32.56 ? 180 ASP A OD2 1 
ATOM   1388 N  N   . PRO A 1 180 ? -21.248 1.327   8.629   1.00 19.40 ? 181 PRO A N   1 
ATOM   1389 C  CA  . PRO A 1 180 ? -20.529 0.566   9.652   1.00 21.25 ? 181 PRO A CA  1 
ATOM   1390 C  C   . PRO A 1 180 ? -21.473 -0.038  10.686  1.00 20.55 ? 181 PRO A C   1 
ATOM   1391 O  O   . PRO A 1 180 ? -21.066 -0.897  11.471  1.00 22.23 ? 181 PRO A O   1 
ATOM   1392 C  CB  . PRO A 1 180 ? -19.577 1.591   10.288  1.00 21.44 ? 181 PRO A CB  1 
ATOM   1393 C  CG  . PRO A 1 180 ? -20.250 2.939   10.030  1.00 22.40 ? 181 PRO A CG  1 
ATOM   1394 C  CD  . PRO A 1 180 ? -20.987 2.771   8.722   1.00 20.11 ? 181 PRO A CD  1 
ATOM   1395 N  N   . ARG A 1 181 ? -22.761 0.319   10.647  1.00 22.28 ? 182 ARG A N   1 
ATOM   1396 C  CA  . ARG A 1 181 ? -23.673 -0.311  11.602  1.00 21.87 ? 182 ARG A CA  1 
ATOM   1397 C  C   . ARG A 1 181 ? -23.796 -1.806  11.307  1.00 21.79 ? 182 ARG A C   1 
ATOM   1398 O  O   . ARG A 1 181 ? -24.182 -2.599  12.170  1.00 22.22 ? 182 ARG A O   1 
ATOM   1399 C  CB  . ARG A 1 181 ? -25.050 0.363   11.552  1.00 22.91 ? 182 ARG A CB  1 
ATOM   1400 C  CG  . ARG A 1 181 ? -25.074 1.757   12.159  1.00 25.64 ? 182 ARG A CG  1 
ATOM   1401 C  CD  . ARG A 1 181 ? -26.418 2.425   11.985  1.00 26.11 ? 182 ARG A CD  1 
ATOM   1402 N  NE  . ARG A 1 181 ? -26.797 2.581   10.577  1.00 25.18 ? 182 ARG A NE  1 
ATOM   1403 C  CZ  . ARG A 1 181 ? -27.837 3.300   10.144  1.00 30.59 ? 182 ARG A CZ  1 
ATOM   1404 N  NH1 . ARG A 1 181 ? -28.621 3.929   11.008  1.00 30.12 ? 182 ARG A NH1 1 
ATOM   1405 N  NH2 . ARG A 1 181 ? -28.103 3.366   8.848   1.00 28.84 ? 182 ARG A NH2 1 
ATOM   1406 N  N   . GLY A 1 182 ? -23.524 -2.179  10.048  1.00 19.80 ? 183 GLY A N   1 
ATOM   1407 C  CA  . GLY A 1 182 ? -23.612 -3.571  9.631   1.00 20.76 ? 183 GLY A CA  1 
ATOM   1408 C  C   . GLY A 1 182 ? -22.457 -4.442  10.120  1.00 21.91 ? 183 GLY A C   1 
ATOM   1409 O  O   . GLY A 1 182 ? -22.443 -5.648  9.836   1.00 23.81 ? 183 GLY A O   1 
ATOM   1410 N  N   . LEU A 1 183 ? -21.549 -3.868  10.925  1.00 21.14 ? 184 LEU A N   1 
ATOM   1411 C  CA  . LEU A 1 183 ? -20.425 -4.639  11.453  1.00 19.76 ? 184 LEU A CA  1 
ATOM   1412 C  C   . LEU A 1 183 ? -20.560 -4.843  12.961  1.00 21.21 ? 184 LEU A C   1 
ATOM   1413 O  O   . LEU A 1 183 ? -19.674 -5.409  13.586  1.00 24.94 ? 184 LEU A O   1 
ATOM   1414 C  CB  . LEU A 1 183 ? -19.123 -3.890  11.155  1.00 20.25 ? 184 LEU A CB  1 
ATOM   1415 C  CG  . LEU A 1 183 ? -18.767 -3.699  9.683   1.00 22.24 ? 184 LEU A CG  1 
ATOM   1416 C  CD1 . LEU A 1 183 ? -17.527 -2.831  9.566   1.00 22.42 ? 184 LEU A CD1 1 
ATOM   1417 C  CD2 . LEU A 1 183 ? -18.580 -5.037  8.981   1.00 23.37 ? 184 LEU A CD2 1 
ATOM   1418 N  N   . LEU A 1 184 ? -21.667 -4.408  13.551  1.00 19.33 ? 185 LEU A N   1 
ATOM   1419 C  CA  . LEU A 1 184 ? -21.777 -4.442  15.004  1.00 22.38 ? 185 LEU A CA  1 
ATOM   1420 C  C   . LEU A 1 184 ? -22.508 -5.710  15.412  1.00 22.37 ? 185 LEU A C   1 
ATOM   1421 O  O   . LEU A 1 184 ? -23.375 -6.165  14.673  1.00 25.90 ? 185 LEU A O   1 
ATOM   1422 C  CB  . LEU A 1 184 ? -22.557 -3.215  15.488  1.00 20.55 ? 185 LEU A CB  1 
ATOM   1423 C  CG  . LEU A 1 184 ? -21.919 -1.867  15.152  1.00 23.70 ? 185 LEU A CG  1 
ATOM   1424 C  CD1 . LEU A 1 184 ? -22.761 -0.714  15.675  1.00 23.03 ? 185 LEU A CD1 1 
ATOM   1425 C  CD2 . LEU A 1 184 ? -20.499 -1.777  15.694  1.00 23.96 ? 185 LEU A CD2 1 
ATOM   1426 N  N   . PRO A 1 185 ? -22.169 -6.305  16.576  1.00 21.69 ? 186 PRO A N   1 
ATOM   1427 C  CA  . PRO A 1 185 ? -22.946 -7.427  17.114  1.00 22.76 ? 186 PRO A CA  1 
ATOM   1428 C  C   . PRO A 1 185 ? -24.196 -6.870  17.816  1.00 23.09 ? 186 PRO A C   1 
ATOM   1429 O  O   . PRO A 1 185 ? -24.367 -5.658  17.947  1.00 21.68 ? 186 PRO A O   1 
ATOM   1430 C  CB  . PRO A 1 185 ? -21.957 -8.022  18.137  1.00 21.43 ? 186 PRO A CB  1 
ATOM   1431 C  CG  . PRO A 1 185 ? -21.258 -6.782  18.690  1.00 19.72 ? 186 PRO A CG  1 
ATOM   1432 C  CD  . PRO A 1 185 ? -21.052 -5.910  17.452  1.00 20.14 ? 186 PRO A CD  1 
ATOM   1433 N  N   . GLU A 1 186 ? -25.067 -7.764  18.287  1.00 25.95 ? 187 GLU A N   1 
ATOM   1434 C  CA  . GLU A 1 186 ? -26.331 -7.348  18.887  1.00 26.93 ? 187 GLU A CA  1 
ATOM   1435 C  C   . GLU A 1 186 ? -26.045 -6.544  20.149  1.00 27.03 ? 187 GLU A C   1 
ATOM   1436 O  O   . GLU A 1 186 ? -26.656 -5.511  20.387  1.00 27.01 ? 187 GLU A O   1 
ATOM   1437 C  CB  . GLU A 1 186 ? -27.163 -8.558  19.306  1.00 29.17 ? 187 GLU A CB  1 
ATOM   1438 C  CG  . GLU A 1 186 ? -27.613 -9.439  18.158  1.00 35.47 ? 187 GLU A CG  1 
ATOM   1439 C  CD  . GLU A 1 186 ? -28.501 -10.602 18.600  1.00 38.63 ? 187 GLU A CD  1 
ATOM   1440 O  OE1 . GLU A 1 186 ? -28.582 -10.866 19.813  1.00 35.81 ? 187 GLU A OE1 1 
ATOM   1441 O  OE2 . GLU A 1 186 ? -29.114 -11.239 17.730  1.00 44.96 ? 187 GLU A OE2 1 
ATOM   1442 N  N   . SER A 1 187 ? -25.119 -7.046  20.966  1.00 24.10 ? 188 SER A N   1 
ATOM   1443 C  CA  . SER A 1 187 ? -24.897 -6.479  22.289  1.00 24.85 ? 188 SER A CA  1 
ATOM   1444 C  C   . SER A 1 187 ? -23.804 -5.412  22.234  1.00 25.46 ? 188 SER A C   1 
ATOM   1445 O  O   . SER A 1 187 ? -22.827 -5.579  21.499  1.00 27.01 ? 188 SER A O   1 
ATOM   1446 C  CB  . SER A 1 187 ? -24.500 -7.556  23.273  1.00 28.18 ? 188 SER A CB  1 
ATOM   1447 O  OG  . SER A 1 187 ? -24.401 -7.006  24.577  1.00 24.91 ? 188 SER A OG  1 
ATOM   1448 N  N   . LEU A 1 188 ? -23.949 -4.361  23.056  1.00 23.38 ? 189 LEU A N   1 
ATOM   1449 C  CA  . LEU A 1 188 ? -22.876 -3.389  23.259  1.00 23.76 ? 189 LEU A CA  1 
ATOM   1450 C  C   . LEU A 1 188 ? -22.244 -3.539  24.643  1.00 24.22 ? 189 LEU A C   1 
ATOM   1451 O  O   . LEU A 1 188 ? -21.659 -2.586  25.129  1.00 26.83 ? 189 LEU A O   1 
ATOM   1452 C  CB  . LEU A 1 188 ? -23.386 -1.946  23.083  1.00 24.37 ? 189 LEU A CB  1 
ATOM   1453 C  CG  . LEU A 1 188 ? -23.816 -1.522  21.684  1.00 25.60 ? 189 LEU A CG  1 
ATOM   1454 C  CD1 . LEU A 1 188 ? -24.320 -0.087  21.670  1.00 27.22 ? 189 LEU A CD1 1 
ATOM   1455 C  CD2 . LEU A 1 188 ? -22.710 -1.725  20.646  1.00 28.51 ? 189 LEU A CD2 1 
ATOM   1456 N  N   . ASP A 1 189 ? -22.389 -4.686  25.313  1.00 24.39 ? 190 ASP A N   1 
ATOM   1457 C  CA  . ASP A 1 189 ? -21.641 -4.877  26.547  1.00 24.96 ? 190 ASP A CA  1 
ATOM   1458 C  C   . ASP A 1 189 ? -20.156 -4.876  26.177  1.00 24.29 ? 190 ASP A C   1 
ATOM   1459 O  O   . ASP A 1 189 ? -19.797 -5.328  25.081  1.00 23.93 ? 190 ASP A O   1 
ATOM   1460 C  CB  . ASP A 1 189 ? -21.972 -6.205  27.223  1.00 26.44 ? 190 ASP A CB  1 
ATOM   1461 C  CG  . ASP A 1 189 ? -23.394 -6.308  27.772  1.00 30.85 ? 190 ASP A CG  1 
ATOM   1462 O  OD1 . ASP A 1 189 ? -24.059 -5.266  27.896  1.00 32.16 ? 190 ASP A OD1 1 
ATOM   1463 O  OD2 . ASP A 1 189 ? -23.815 -7.431  28.043  1.00 30.42 ? 190 ASP A OD2 1 
ATOM   1464 N  N   . TYR A 1 190 ? -19.333 -4.309  27.066  1.00 22.67 ? 191 TYR A N   1 
ATOM   1465 C  CA  . TYR A 1 190 ? -17.945 -3.993  26.755  1.00 23.07 ? 191 TYR A CA  1 
ATOM   1466 C  C   . TYR A 1 190 ? -17.056 -4.071  27.987  1.00 21.20 ? 191 TYR A C   1 
ATOM   1467 O  O   . TYR A 1 190 ? -17.501 -3.956  29.128  1.00 21.58 ? 191 TYR A O   1 
ATOM   1468 C  CB  . TYR A 1 190 ? -17.828 -2.610  26.089  1.00 21.81 ? 191 TYR A CB  1 
ATOM   1469 C  CG  . TYR A 1 190 ? -18.204 -1.451  26.984  1.00 24.29 ? 191 TYR A CG  1 
ATOM   1470 C  CD1 . TYR A 1 190 ? -17.290 -0.887  27.876  1.00 23.33 ? 191 TYR A CD1 1 
ATOM   1471 C  CD2 . TYR A 1 190 ? -19.487 -0.919  26.947  1.00 23.52 ? 191 TYR A CD2 1 
ATOM   1472 C  CE1 . TYR A 1 190 ? -17.648 0.184   28.688  1.00 23.76 ? 191 TYR A CE1 1 
ATOM   1473 C  CE2 . TYR A 1 190 ? -19.864 0.153   27.741  1.00 24.57 ? 191 TYR A CE2 1 
ATOM   1474 C  CZ  . TYR A 1 190 ? -18.936 0.705   28.615  1.00 26.48 ? 191 TYR A CZ  1 
ATOM   1475 O  OH  . TYR A 1 190 ? -19.335 1.725   29.420  1.00 23.86 ? 191 TYR A OH  1 
ATOM   1476 N  N   . TRP A 1 191 ? -15.773 -4.296  27.715  1.00 22.11 ? 192 TRP A N   1 
ATOM   1477 C  CA  . TRP A 1 191 ? -14.700 -4.033  28.653  1.00 21.24 ? 192 TRP A CA  1 
ATOM   1478 C  C   . TRP A 1 191 ? -14.018 -2.748  28.223  1.00 23.55 ? 192 TRP A C   1 
ATOM   1479 O  O   . TRP A 1 191 ? -13.942 -2.462  27.023  1.00 21.27 ? 192 TRP A O   1 
ATOM   1480 C  CB  . TRP A 1 191 ? -13.681 -5.172  28.631  1.00 21.94 ? 192 TRP A CB  1 
ATOM   1481 C  CG  . TRP A 1 191 ? -14.254 -6.503  29.000  1.00 21.93 ? 192 TRP A CG  1 
ATOM   1482 C  CD1 . TRP A 1 191 ? -14.583 -6.926  30.264  1.00 19.99 ? 192 TRP A CD1 1 
ATOM   1483 C  CD2 . TRP A 1 191 ? -14.465 -7.616  28.118  1.00 20.26 ? 192 TRP A CD2 1 
ATOM   1484 N  NE1 . TRP A 1 191 ? -15.022 -8.229  30.209  1.00 21.74 ? 192 TRP A NE1 1 
ATOM   1485 C  CE2 . TRP A 1 191 ? -14.987 -8.666  28.903  1.00 21.73 ? 192 TRP A CE2 1 
ATOM   1486 C  CE3 . TRP A 1 191 ? -14.292 -7.817  26.738  1.00 19.85 ? 192 TRP A CE3 1 
ATOM   1487 C  CZ2 . TRP A 1 191 ? -15.311 -9.913  28.359  1.00 21.30 ? 192 TRP A CZ2 1 
ATOM   1488 C  CZ3 . TRP A 1 191 ? -14.633 -9.043  26.201  1.00 24.00 ? 192 TRP A CZ3 1 
ATOM   1489 C  CH2 . TRP A 1 191 ? -15.113 -10.083 26.999  1.00 23.48 ? 192 TRP A CH2 1 
ATOM   1490 N  N   . THR A 1 192 ? -13.425 -2.048  29.195  1.00 20.04 ? 193 THR A N   1 
ATOM   1491 C  CA  . THR A 1 192 ? -12.716 -0.817  28.880  1.00 20.59 ? 193 THR A CA  1 
ATOM   1492 C  C   . THR A 1 192 ? -11.455 -0.687  29.732  1.00 19.56 ? 193 THR A C   1 
ATOM   1493 O  O   . THR A 1 192 ? -11.416 -1.090  30.902  1.00 21.32 ? 193 THR A O   1 
ATOM   1494 C  CB  . THR A 1 192 ? -13.655 0.402   28.914  1.00 20.76 ? 193 THR A CB  1 
ATOM   1495 O  OG1 . THR A 1 192 ? -12.932 1.527   28.403  1.00 21.07 ? 193 THR A OG1 1 
ATOM   1496 C  CG2 . THR A 1 192 ? -14.161 0.744   30.314  1.00 21.05 ? 193 THR A CG2 1 
ATOM   1497 N  N   . TYR A 1 193 ? -10.419 -0.089  29.130  1.00 19.11 ? 194 TYR A N   1 
ATOM   1498 C  CA  . TYR A 1 193 ? -9.153  0.130   29.819  1.00 18.84 ? 194 TYR A CA  1 
ATOM   1499 C  C   . TYR A 1 193 ? -8.340  1.165   29.056  1.00 20.60 ? 194 TYR A C   1 
ATOM   1500 O  O   . TYR A 1 193 ? -8.580  1.355   27.846  1.00 19.02 ? 194 TYR A O   1 
ATOM   1501 C  CB  . TYR A 1 193 ? -8.358  -1.178  29.950  1.00 17.93 ? 194 TYR A CB  1 
ATOM   1502 C  CG  . TYR A 1 193 ? -7.664  -1.587  28.673  1.00 19.88 ? 194 TYR A CG  1 
ATOM   1503 C  CD1 . TYR A 1 193 ? -8.320  -2.348  27.712  1.00 18.70 ? 194 TYR A CD1 1 
ATOM   1504 C  CD2 . TYR A 1 193 ? -6.344  -1.220  28.448  1.00 19.76 ? 194 TYR A CD2 1 
ATOM   1505 C  CE1 . TYR A 1 193 ? -7.684  -2.696  26.520  1.00 19.16 ? 194 TYR A CE1 1 
ATOM   1506 C  CE2 . TYR A 1 193 ? -5.695  -1.574  27.271  1.00 20.62 ? 194 TYR A CE2 1 
ATOM   1507 C  CZ  . TYR A 1 193 ? -6.357  -2.326  26.321  1.00 19.39 ? 194 TYR A CZ  1 
ATOM   1508 O  OH  . TYR A 1 193 ? -5.698  -2.617  25.149  1.00 18.74 ? 194 TYR A OH  1 
ATOM   1509 N  N   . PRO A 1 194 ? -7.417  1.887   29.744  1.00 19.35 ? 195 PRO A N   1 
ATOM   1510 C  CA  . PRO A 1 194 ? -6.561  2.873   29.097  1.00 21.23 ? 195 PRO A CA  1 
ATOM   1511 C  C   . PRO A 1 194 ? -5.355  2.215   28.419  1.00 20.88 ? 195 PRO A C   1 
ATOM   1512 O  O   . PRO A 1 194 ? -4.635  1.441   29.025  1.00 20.11 ? 195 PRO A O   1 
ATOM   1513 C  CB  . PRO A 1 194 ? -6.159  3.819   30.245  1.00 22.50 ? 195 PRO A CB  1 
ATOM   1514 C  CG  . PRO A 1 194 ? -6.225  2.969   31.509  1.00 24.03 ? 195 PRO A CG  1 
ATOM   1515 C  CD  . PRO A 1 194 ? -7.231  1.866   31.215  1.00 23.07 ? 195 PRO A CD  1 
ATOM   1516 N  N   . GLY A 1 195 ? -5.144  2.503   27.130  1.00 18.93 ? 196 GLY A N   1 
ATOM   1517 C  CA  . GLY A 1 195 ? -4.032  1.872   26.433  1.00 18.14 ? 196 GLY A CA  1 
ATOM   1518 C  C   . GLY A 1 195 ? -3.494  2.736   25.291  1.00 17.68 ? 196 GLY A C   1 
ATOM   1519 O  O   . GLY A 1 195 ? -3.405  3.970   25.425  1.00 16.67 ? 196 GLY A O   1 
ATOM   1520 N  N   . SER A 1 196 ? -3.096  2.076   24.191  1.00 18.13 ? 197 SER A N   1 
ATOM   1521 C  CA  . SER A 1 196 ? -2.256  2.722   23.199  1.00 18.79 ? 197 SER A CA  1 
ATOM   1522 C  C   . SER A 1 196 ? -2.710  2.326   21.806  1.00 19.71 ? 197 SER A C   1 
ATOM   1523 O  O   . SER A 1 196 ? -3.458  1.356   21.643  1.00 17.32 ? 197 SER A O   1 
ATOM   1524 C  CB  . SER A 1 196 ? -0.788  2.306   23.356  1.00 19.94 ? 197 SER A CB  1 
ATOM   1525 O  OG  . SER A 1 196 ? -0.552  0.973   22.865  1.00 19.45 ? 197 SER A OG  1 
ATOM   1526 N  N   . LEU A 1 197 ? -2.198  3.061   20.809  1.00 18.32 ? 198 LEU A N   1 
ATOM   1527 C  CA  . LEU A 1 197 ? -2.173  2.520   19.459  1.00 18.78 ? 198 LEU A CA  1 
ATOM   1528 C  C   . LEU A 1 197 ? -1.402  1.192   19.486  1.00 19.61 ? 198 LEU A C   1 
ATOM   1529 O  O   . LEU A 1 197 ? -0.440  1.054   20.254  1.00 20.57 ? 198 LEU A O   1 
ATOM   1530 C  CB  . LEU A 1 197 ? -1.459  3.569   18.599  1.00 20.75 ? 198 LEU A CB  1 
ATOM   1531 C  CG  . LEU A 1 197 ? -2.123  4.954   18.541  1.00 22.64 ? 198 LEU A CG  1 
ATOM   1532 C  CD1 . LEU A 1 197 ? -1.224  5.930   17.791  1.00 23.63 ? 198 LEU A CD1 1 
ATOM   1533 C  CD2 . LEU A 1 197 ? -3.487  4.896   17.877  1.00 23.21 ? 198 LEU A CD2 1 
ATOM   1534 N  N   . THR A 1 198 ? -1.775  0.231   18.608  1.00 19.39 ? 199 THR A N   1 
ATOM   1535 C  CA  . THR A 1 198 ? -1.168  -1.098  18.626  1.00 19.12 ? 199 THR A CA  1 
ATOM   1536 C  C   . THR A 1 198 ? -0.183  -1.264  17.458  1.00 19.65 ? 199 THR A C   1 
ATOM   1537 O  O   . THR A 1 198 ? 0.355   -2.358  17.254  1.00 19.17 ? 199 THR A O   1 
ATOM   1538 C  CB  . THR A 1 198 ? -2.225  -2.215  18.488  1.00 18.44 ? 199 THR A CB  1 
ATOM   1539 O  OG1 . THR A 1 198 ? -2.832  -2.113  17.205  1.00 17.42 ? 199 THR A OG1 1 
ATOM   1540 C  CG2 . THR A 1 198 ? -3.350  -2.136  19.501  1.00 15.75 ? 199 THR A CG2 1 
ATOM   1541 N  N   . THR A 1 199 ? -0.017  -0.222  16.644  1.00 20.80 ? 200 THR A N   1 
ATOM   1542 C  CA  . THR A 1 199 ? 1.118   -0.193  15.735  1.00 21.96 ? 200 THR A CA  1 
ATOM   1543 C  C   . THR A 1 199 ? 1.931   1.069   16.015  1.00 22.00 ? 200 THR A C   1 
ATOM   1544 O  O   . THR A 1 199 ? 1.422   1.995   16.626  1.00 20.73 ? 200 THR A O   1 
ATOM   1545 C  CB  . THR A 1 199 ? 0.694   -0.192  14.261  1.00 23.27 ? 200 THR A CB  1 
ATOM   1546 O  OG1 . THR A 1 199 ? 0.225   1.124   13.978  1.00 26.61 ? 200 THR A OG1 1 
ATOM   1547 C  CG2 . THR A 1 199 ? -0.408  -1.177  13.939  1.00 23.49 ? 200 THR A CG2 1 
ATOM   1548 N  N   . PRO A 1 200 ? 3.191   1.166   15.540  1.00 23.34 ? 201 PRO A N   1 
ATOM   1549 C  CA  . PRO A 1 200 ? 3.937   2.422   15.607  1.00 22.52 ? 201 PRO A CA  1 
ATOM   1550 C  C   . PRO A 1 200 ? 3.033   3.529   15.089  1.00 23.94 ? 201 PRO A C   1 
ATOM   1551 O  O   . PRO A 1 200 ? 2.311   3.332   14.124  1.00 26.56 ? 201 PRO A O   1 
ATOM   1552 C  CB  . PRO A 1 200 ? 5.068   2.150   14.606  1.00 21.82 ? 201 PRO A CB  1 
ATOM   1553 C  CG  . PRO A 1 200 ? 5.385   0.699   14.861  1.00 22.61 ? 201 PRO A CG  1 
ATOM   1554 C  CD  . PRO A 1 200 ? 4.029   0.046   15.076  1.00 23.50 ? 201 PRO A CD  1 
ATOM   1555 N  N   . PRO A 1 201 ? 3.019   4.734   15.695  1.00 24.37 ? 202 PRO A N   1 
ATOM   1556 C  CA  . PRO A 1 201 ? 3.990   5.117   16.725  1.00 21.78 ? 202 PRO A CA  1 
ATOM   1557 C  C   . PRO A 1 201 ? 3.681   4.734   18.174  1.00 21.93 ? 202 PRO A C   1 
ATOM   1558 O  O   . PRO A 1 201 ? 4.369   5.192   19.082  1.00 23.28 ? 202 PRO A O   1 
ATOM   1559 C  CB  . PRO A 1 201 ? 3.982   6.647   16.561  1.00 24.15 ? 202 PRO A CB  1 
ATOM   1560 C  CG  . PRO A 1 201 ? 2.584   7.010   16.089  1.00 25.17 ? 202 PRO A CG  1 
ATOM   1561 C  CD  . PRO A 1 201 ? 2.100   5.818   15.303  1.00 24.39 ? 202 PRO A CD  1 
ATOM   1562 N  N   . LEU A 1 202 ? 2.637   3.921   18.376  1.00 20.22 ? 203 LEU A N   1 
ATOM   1563 C  CA  . LEU A 1 202 ? 2.332   3.308   19.667  1.00 20.57 ? 203 LEU A CA  1 
ATOM   1564 C  C   . LEU A 1 202 ? 1.944   4.330   20.735  1.00 18.90 ? 203 LEU A C   1 
ATOM   1565 O  O   . LEU A 1 202 ? 2.009   4.002   21.931  1.00 21.93 ? 203 LEU A O   1 
ATOM   1566 C  CB  . LEU A 1 202 ? 3.510   2.425   20.124  1.00 20.20 ? 203 LEU A CB  1 
ATOM   1567 C  CG  . LEU A 1 202 ? 3.832   1.222   19.232  1.00 20.83 ? 203 LEU A CG  1 
ATOM   1568 C  CD1 . LEU A 1 202 ? 5.168   0.604   19.619  1.00 20.79 ? 203 LEU A CD1 1 
ATOM   1569 C  CD2 . LEU A 1 202 ? 2.709   0.181   19.310  1.00 19.83 ? 203 LEU A CD2 1 
ATOM   1570 N  N   . ASN A 1 203 ? 1.449   5.529   20.337  1.00 21.11 ? 204 ASN A N   1 
ATOM   1571 C  CA  . ASN A 1 203 ? 1.126   6.575   21.305  1.00 20.86 ? 204 ASN A CA  1 
ATOM   1572 C  C   . ASN A 1 203 ? 0.133   6.068   22.349  1.00 21.12 ? 204 ASN A C   1 
ATOM   1573 O  O   . ASN A 1 203 ? -0.783  5.302   22.041  1.00 20.90 ? 204 ASN A O   1 
ATOM   1574 C  CB  . ASN A 1 203 ? 0.491   7.813   20.665  1.00 23.98 ? 204 ASN A CB  1 
ATOM   1575 C  CG  . ASN A 1 203 ? 1.291   8.394   19.521  1.00 27.45 ? 204 ASN A CG  1 
ATOM   1576 O  OD1 . ASN A 1 203 ? 2.348   7.890   19.154  1.00 31.14 ? 204 ASN A OD1 1 
ATOM   1577 N  ND2 . ASN A 1 203 ? 0.817   9.497   18.971  1.00 30.96 ? 204 ASN A ND2 1 
ATOM   1578 N  N   . GLU A 1 204 ? 0.283   6.554   23.579  1.00 21.66 ? 205 GLU A N   1 
ATOM   1579 C  CA  . GLU A 1 204 ? -0.591  6.133   24.666  1.00 22.95 ? 205 GLU A CA  1 
ATOM   1580 C  C   . GLU A 1 204 ? -1.765  7.110   24.768  1.00 24.95 ? 205 GLU A C   1 
ATOM   1581 O  O   . GLU A 1 204 ? -1.908  7.868   25.732  1.00 25.37 ? 205 GLU A O   1 
ATOM   1582 C  CB  . GLU A 1 204 ? 0.219   5.967   25.955  1.00 23.81 ? 205 GLU A CB  1 
ATOM   1583 C  CG  . GLU A 1 204 ? 1.181   4.780   25.864  1.00 24.31 ? 205 GLU A CG  1 
ATOM   1584 C  CD  . GLU A 1 204 ? 2.047   4.438   27.071  1.00 26.85 ? 205 GLU A CD  1 
ATOM   1585 O  OE1 . GLU A 1 204 ? 2.387   5.368   27.874  1.00 29.99 ? 205 GLU A OE1 1 
ATOM   1586 O  OE2 . GLU A 1 204 ? 2.363   3.246   27.238  1.00 25.06 ? 205 GLU A OE2 1 
ATOM   1587 N  N   . CYS A 1 205 ? -2.651  7.026   23.776  1.00 20.45 ? 206 CYS A N   1 
ATOM   1588 C  CA  . CYS A 1 205 ? -3.677  8.032   23.565  1.00 21.26 ? 206 CYS A CA  1 
ATOM   1589 C  C   . CYS A 1 205 ? -5.069  7.407   23.447  1.00 21.93 ? 206 CYS A C   1 
ATOM   1590 O  O   . CYS A 1 205 ? -6.026  8.122   23.133  1.00 23.13 ? 206 CYS A O   1 
ATOM   1591 C  CB  . CYS A 1 205 ? -3.323  8.836   22.315  1.00 21.80 ? 206 CYS A CB  1 
ATOM   1592 S  SG  . CYS A 1 205 ? -3.309  7.824   20.806  1.00 24.98 ? 206 CYS A SG  1 
ATOM   1593 N  N   . VAL A 1 206 ? -5.191  6.088   23.698  1.00 18.54 ? 207 VAL A N   1 
ATOM   1594 C  CA  . VAL A 1 206 ? -6.403  5.331   23.387  1.00 17.89 ? 207 VAL A CA  1 
ATOM   1595 C  C   . VAL A 1 206 ? -7.186  4.959   24.659  1.00 18.24 ? 207 VAL A C   1 
ATOM   1596 O  O   . VAL A 1 206 ? -6.625  4.433   25.613  1.00 22.50 ? 207 VAL A O   1 
ATOM   1597 C  CB  . VAL A 1 206 ? -6.126  4.092   22.511  1.00 17.87 ? 207 VAL A CB  1 
ATOM   1598 C  CG1 . VAL A 1 206 ? -7.442  3.394   22.145  1.00 16.71 ? 207 VAL A CG1 1 
ATOM   1599 C  CG2 . VAL A 1 206 ? -5.370  4.469   21.225  1.00 18.71 ? 207 VAL A CG2 1 
ATOM   1600 N  N   . THR A 1 207 ? -8.488  5.262   24.675  1.00 19.16 ? 208 THR A N   1 
ATOM   1601 C  CA  . THR A 1 207 ? -9.413  4.577   25.563  1.00 19.96 ? 208 THR A CA  1 
ATOM   1602 C  C   . THR A 1 207 ? -9.948  3.393   24.763  1.00 20.56 ? 208 THR A C   1 
ATOM   1603 O  O   . THR A 1 207 ? -10.667 3.566   23.778  1.00 19.52 ? 208 THR A O   1 
ATOM   1604 C  CB  . THR A 1 207 ? -10.552 5.485   26.080  1.00 22.34 ? 208 THR A CB  1 
ATOM   1605 O  OG1 . THR A 1 207 ? -10.069 6.593   26.851  1.00 20.16 ? 208 THR A OG1 1 
ATOM   1606 C  CG2 . THR A 1 207 ? -11.599 4.726   26.872  1.00 21.09 ? 208 THR A CG2 1 
ATOM   1607 N  N   . TRP A 1 208 ? -9.556  2.188   25.170  1.00 18.38 ? 209 TRP A N   1 
ATOM   1608 C  CA  . TRP A 1 208 ? -10.078 0.969   24.555  1.00 19.69 ? 209 TRP A CA  1 
ATOM   1609 C  C   . TRP A 1 208 ? -11.466 0.609   25.063  1.00 18.25 ? 209 TRP A C   1 
ATOM   1610 O  O   . TRP A 1 208 ? -11.750 0.638   26.262  1.00 19.16 ? 209 TRP A O   1 
ATOM   1611 C  CB  . TRP A 1 208 ? -9.091  -0.199  24.713  1.00 18.51 ? 209 TRP A CB  1 
ATOM   1612 C  CG  . TRP A 1 208 ? -7.974  -0.066  23.713  1.00 18.74 ? 209 TRP A CG  1 
ATOM   1613 C  CD1 . TRP A 1 208 ? -6.735  0.475   23.924  1.00 19.03 ? 209 TRP A CD1 1 
ATOM   1614 C  CD2 . TRP A 1 208 ? -8.025  -0.423  22.317  1.00 19.52 ? 209 TRP A CD2 1 
ATOM   1615 N  NE1 . TRP A 1 208 ? -6.012  0.474   22.752  1.00 19.55 ? 209 TRP A NE1 1 
ATOM   1616 C  CE2 . TRP A 1 208 ? -6.780  -0.060  21.751  1.00 18.12 ? 209 TRP A CE2 1 
ATOM   1617 C  CE3 . TRP A 1 208 ? -9.000  -1.026  21.503  1.00 18.01 ? 209 TRP A CE3 1 
ATOM   1618 C  CZ2 . TRP A 1 208 ? -6.486  -0.266  20.399  1.00 18.07 ? 209 TRP A CZ2 1 
ATOM   1619 C  CZ3 . TRP A 1 208 ? -8.689  -1.269  20.180  1.00 18.09 ? 209 TRP A CZ3 1 
ATOM   1620 C  CH2 . TRP A 1 208 ? -7.452  -0.892  19.647  1.00 20.09 ? 209 TRP A CH2 1 
ATOM   1621 N  N   . ILE A 1 209 ? -12.328 0.253   24.114  1.00 20.33 ? 210 ILE A N   1 
ATOM   1622 C  CA  . ILE A 1 209 ? -13.683 -0.229  24.365  1.00 19.85 ? 210 ILE A CA  1 
ATOM   1623 C  C   . ILE A 1 209 ? -13.841 -1.479  23.495  1.00 20.41 ? 210 ILE A C   1 
ATOM   1624 O  O   . ILE A 1 209 ? -13.842 -1.421  22.249  1.00 18.70 ? 210 ILE A O   1 
ATOM   1625 C  CB  . ILE A 1 209 ? -14.749 0.863   24.079  1.00 19.25 ? 210 ILE A CB  1 
ATOM   1626 C  CG1 . ILE A 1 209 ? -14.564 2.105   24.955  1.00 18.96 ? 210 ILE A CG1 1 
ATOM   1627 C  CG2 . ILE A 1 209 ? -16.163 0.294   24.215  1.00 19.38 ? 210 ILE A CG2 1 
ATOM   1628 C  CD1 . ILE A 1 209 ? -15.285 3.324   24.440  1.00 21.13 ? 210 ILE A CD1 1 
ATOM   1629 N  N   . VAL A 1 210 ? -13.809 -2.634  24.165  1.00 20.47 ? 211 VAL A N   1 
ATOM   1630 C  CA  . VAL A 1 210 ? -13.782 -3.894  23.433  1.00 19.48 ? 211 VAL A CA  1 
ATOM   1631 C  C   . VAL A 1 210 ? -15.087 -4.611  23.746  1.00 20.31 ? 211 VAL A C   1 
ATOM   1632 O  O   . VAL A 1 210 ? -15.420 -4.817  24.917  1.00 19.25 ? 211 VAL A O   1 
ATOM   1633 C  CB  . VAL A 1 210 ? -12.552 -4.756  23.791  1.00 20.33 ? 211 VAL A CB  1 
ATOM   1634 C  CG1 . VAL A 1 210 ? -12.622 -6.152  23.165  1.00 18.41 ? 211 VAL A CG1 1 
ATOM   1635 C  CG2 . VAL A 1 210 ? -11.231 -4.070  23.442  1.00 21.64 ? 211 VAL A CG2 1 
ATOM   1636 N  N   . LEU A 1 211 ? -15.836 -4.905  22.686  1.00 20.22 ? 212 LEU A N   1 
ATOM   1637 C  CA  . LEU A 1 211 ? -17.142 -5.529  22.804  1.00 22.37 ? 212 LEU A CA  1 
ATOM   1638 C  C   . LEU A 1 211 ? -16.979 -7.001  23.201  1.00 22.63 ? 212 LEU A C   1 
ATOM   1639 O  O   . LEU A 1 211 ? -16.155 -7.722  22.639  1.00 22.45 ? 212 LEU A O   1 
ATOM   1640 C  CB  . LEU A 1 211 ? -17.882 -5.391  21.472  1.00 22.38 ? 212 LEU A CB  1 
ATOM   1641 C  CG  . LEU A 1 211 ? -18.265 -3.961  21.066  1.00 20.44 ? 212 LEU A CG  1 
ATOM   1642 C  CD1 . LEU A 1 211 ? -19.310 -4.055  19.962  1.00 23.96 ? 212 LEU A CD1 1 
ATOM   1643 C  CD2 . LEU A 1 211 ? -18.804 -3.181  22.293  1.00 20.01 ? 212 LEU A CD2 1 
ATOM   1644 N  N   . LYS A 1 212 ? -17.789 -7.419  24.187  1.00 21.73 ? 213 LYS A N   1 
ATOM   1645 C  CA  . LYS A 1 212 ? -17.861 -8.798  24.656  1.00 22.35 ? 213 LYS A CA  1 
ATOM   1646 C  C   . LYS A 1 212 ? -18.336 -9.760  23.564  1.00 21.22 ? 213 LYS A C   1 
ATOM   1647 O  O   . LYS A 1 212 ? -17.829 -10.873 23.455  1.00 23.43 ? 213 LYS A O   1 
ATOM   1648 C  CB  . LYS A 1 212 ? -18.748 -8.866  25.910  1.00 25.56 ? 213 LYS A CB  1 
ATOM   1649 C  CG  . LYS A 1 212 ? -19.472 -10.193 26.121  1.00 36.20 ? 213 LYS A CG  1 
ATOM   1650 C  CD  . LYS A 1 212 ? -20.724 -10.099 26.995  1.00 37.33 ? 213 LYS A CD  1 
ATOM   1651 C  CE  . LYS A 1 212 ? -20.914 -11.318 27.887  1.00 46.70 ? 213 LYS A CE  1 
ATOM   1652 N  N   . GLU A 1 213 ? -19.302 -9.363  22.739  1.00 24.12 ? 214 GLU A N   1 
ATOM   1653 C  CA  . GLU A 1 213 ? -19.871 -10.308 21.787  1.00 21.76 ? 214 GLU A CA  1 
ATOM   1654 C  C   . GLU A 1 213 ? -19.113 -10.220 20.458  1.00 21.93 ? 214 GLU A C   1 
ATOM   1655 O  O   . GLU A 1 213 ? -19.074 -9.159  19.849  1.00 18.60 ? 214 GLU A O   1 
ATOM   1656 C  CB  . GLU A 1 213 ? -21.337 -9.947  21.540  1.00 24.99 ? 214 GLU A CB  1 
ATOM   1657 C  CG  . GLU A 1 213 ? -22.051 -10.867 20.550  1.00 28.61 ? 214 GLU A CG  1 
ATOM   1658 C  CD  . GLU A 1 213 ? -23.501 -10.480 20.248  1.00 36.39 ? 214 GLU A CD  1 
ATOM   1659 O  OE1 . GLU A 1 213 ? -24.123 -9.827  21.122  1.00 27.50 ? 214 GLU A OE1 1 
ATOM   1660 O  OE2 . GLU A 1 213 ? -24.001 -10.812 19.133  1.00 38.13 ? 214 GLU A OE2 1 
ATOM   1661 N  N   . PRO A 1 214 ? -18.508 -11.321 19.952  1.00 21.35 ? 215 PRO A N   1 
ATOM   1662 C  CA  . PRO A 1 214 ? -17.876 -11.311 18.637  1.00 21.33 ? 215 PRO A CA  1 
ATOM   1663 C  C   . PRO A 1 214 ? -18.932 -11.217 17.549  1.00 22.94 ? 215 PRO A C   1 
ATOM   1664 O  O   . PRO A 1 214 ? -20.100 -11.544 17.765  1.00 23.11 ? 215 PRO A O   1 
ATOM   1665 C  CB  . PRO A 1 214 ? -17.214 -12.704 18.517  1.00 23.56 ? 215 PRO A CB  1 
ATOM   1666 C  CG  . PRO A 1 214 ? -17.194 -13.244 19.928  1.00 27.98 ? 215 PRO A CG  1 
ATOM   1667 C  CD  . PRO A 1 214 ? -18.408 -12.638 20.608  1.00 25.96 ? 215 PRO A CD  1 
ATOM   1668 N  N   . ILE A 1 215 ? -18.504 -10.817 16.350  1.00 20.20 ? 216 ILE A N   1 
ATOM   1669 C  CA  . ILE A 1 215 ? -19.334 -11.048 15.193  1.00 21.28 ? 216 ILE A CA  1 
ATOM   1670 C  C   . ILE A 1 215 ? -18.837 -12.316 14.512  1.00 21.50 ? 216 ILE A C   1 
ATOM   1671 O  O   . ILE A 1 215 ? -17.659 -12.659 14.598  1.00 21.97 ? 216 ILE A O   1 
ATOM   1672 C  CB  . ILE A 1 215 ? -19.347 -9.847  14.235  1.00 20.61 ? 216 ILE A CB  1 
ATOM   1673 C  CG1 . ILE A 1 215 ? -17.944 -9.493  13.728  1.00 20.40 ? 216 ILE A CG1 1 
ATOM   1674 C  CG2 . ILE A 1 215 ? -20.022 -8.611  14.845  1.00 21.74 ? 216 ILE A CG2 1 
ATOM   1675 C  CD1 . ILE A 1 215 ? -18.020 -8.500  12.573  1.00 21.88 ? 216 ILE A CD1 1 
ATOM   1676 N  N   . SER A 1 216 ? -19.748 -13.004 13.826  1.00 20.88 ? 217 SER A N   1 
ATOM   1677 C  CA  A SER A 1 216 ? -19.386 -14.165 13.025  0.50 21.18 ? 217 SER A CA  1 
ATOM   1678 C  CA  B SER A 1 216 ? -19.362 -14.157 13.035  0.50 21.34 ? 217 SER A CA  1 
ATOM   1679 C  C   . SER A 1 216 ? -19.145 -13.730 11.586  1.00 19.52 ? 217 SER A C   1 
ATOM   1680 O  O   . SER A 1 216 ? -19.941 -12.992 11.011  1.00 23.61 ? 217 SER A O   1 
ATOM   1681 C  CB  A SER A 1 216 ? -20.449 -15.237 13.070  0.50 21.28 ? 217 SER A CB  1 
ATOM   1682 C  CB  B SER A 1 216 ? -20.383 -15.262 13.159  0.50 21.72 ? 217 SER A CB  1 
ATOM   1683 O  OG  A SER A 1 216 ? -20.612 -15.724 14.385  0.50 21.94 ? 217 SER A OG  1 
ATOM   1684 O  OG  B SER A 1 216 ? -20.066 -16.322 12.280  0.50 23.15 ? 217 SER A OG  1 
ATOM   1685 N  N   . VAL A 1 217 ? -18.033 -14.167 11.023  1.00 19.25 ? 218 VAL A N   1 
ATOM   1686 C  CA  . VAL A 1 217 ? -17.796 -13.976 9.600   1.00 19.68 ? 218 VAL A CA  1 
ATOM   1687 C  C   . VAL A 1 217 ? -17.550 -15.352 8.989   1.00 20.66 ? 218 VAL A C   1 
ATOM   1688 O  O   . VAL A 1 217 ? -17.253 -16.307 9.696   1.00 23.19 ? 218 VAL A O   1 
ATOM   1689 C  CB  . VAL A 1 217 ? -16.630 -13.009 9.333   1.00 20.43 ? 218 VAL A CB  1 
ATOM   1690 C  CG1 . VAL A 1 217 ? -16.891 -11.657 10.010  1.00 20.06 ? 218 VAL A CG1 1 
ATOM   1691 C  CG2 . VAL A 1 217 ? -15.291 -13.592 9.826   1.00 21.10 ? 218 VAL A CG2 1 
ATOM   1692 N  N   . SER A 1 218 ? -17.660 -15.467 7.664   1.00 21.85 ? 219 SER A N   1 
ATOM   1693 C  CA  . SER A 1 218 ? -17.468 -16.786 7.084   1.00 21.31 ? 219 SER A CA  1 
ATOM   1694 C  C   . SER A 1 218 ? -15.997 -17.005 6.743   1.00 22.06 ? 219 SER A C   1 
ATOM   1695 O  O   . SER A 1 218 ? -15.205 -16.070 6.751   1.00 20.64 ? 219 SER A O   1 
ATOM   1696 C  CB  . SER A 1 218 ? -18.371 -17.004 5.901   1.00 21.29 ? 219 SER A CB  1 
ATOM   1697 O  OG  . SER A 1 218 ? -18.022 -16.119 4.871   1.00 21.12 ? 219 SER A OG  1 
ATOM   1698 N  N   . SER A 1 219 ? -15.615 -18.269 6.515   1.00 21.59 ? 220 SER A N   1 
ATOM   1699 C  CA  . SER A 1 219 ? -14.266 -18.580 6.069   1.00 22.65 ? 220 SER A CA  1 
ATOM   1700 C  C   . SER A 1 219 ? -13.982 -17.861 4.754   1.00 23.02 ? 220 SER A C   1 
ATOM   1701 O  O   . SER A 1 219 ? -12.870 -17.372 4.565   1.00 23.78 ? 220 SER A O   1 
ATOM   1702 C  CB  . SER A 1 219 ? -14.073 -20.087 5.927   1.00 25.32 ? 220 SER A CB  1 
ATOM   1703 O  OG  . SER A 1 219 ? -15.092 -20.615 5.082   1.00 28.63 ? 220 SER A OG  1 
ATOM   1704 N  N   . GLU A 1 220 ? -14.998 -17.760 3.872   1.00 23.36 ? 221 GLU A N   1 
ATOM   1705 C  CA  . GLU A 1 220 ? -14.797 -17.156 2.555   1.00 23.52 ? 221 GLU A CA  1 
ATOM   1706 C  C   . GLU A 1 220 ? -14.474 -15.667 2.706   1.00 22.81 ? 221 GLU A C   1 
ATOM   1707 O  O   . GLU A 1 220 ? -13.646 -15.114 1.980   1.00 22.49 ? 221 GLU A O   1 
ATOM   1708 C  CB  . GLU A 1 220 ? -16.040 -17.260 1.668   1.00 26.25 ? 221 GLU A CB  1 
ATOM   1709 C  CG  . GLU A 1 220 ? -16.337 -18.665 1.171   1.00 28.52 ? 221 GLU A CG  1 
ATOM   1710 C  CD  . GLU A 1 220 ? -17.256 -19.454 2.084   1.00 32.70 ? 221 GLU A CD  1 
ATOM   1711 O  OE1 . GLU A 1 220 ? -17.563 -18.975 3.199   1.00 33.18 ? 221 GLU A OE1 1 
ATOM   1712 O  OE2 . GLU A 1 220 ? -17.688 -20.545 1.668   1.00 39.17 ? 221 GLU A OE2 1 
ATOM   1713 N  N   . GLN A 1 221 ? -15.137 -15.018 3.667   1.00 20.76 ? 222 GLN A N   1 
ATOM   1714 C  CA  . GLN A 1 221 ? -14.876 -13.605 3.950   1.00 20.20 ? 222 GLN A CA  1 
ATOM   1715 C  C   . GLN A 1 221 ? -13.434 -13.408 4.431   1.00 22.61 ? 222 GLN A C   1 
ATOM   1716 O  O   . GLN A 1 221 ? -12.706 -12.564 3.901   1.00 22.43 ? 222 GLN A O   1 
ATOM   1717 C  CB  . GLN A 1 221 ? -15.891 -13.096 4.975   1.00 20.79 ? 222 GLN A CB  1 
ATOM   1718 C  CG  . GLN A 1 221 ? -17.282 -12.977 4.344   1.00 19.34 ? 222 GLN A CG  1 
ATOM   1719 C  CD  . GLN A 1 221 ? -18.352 -12.412 5.234   1.00 18.86 ? 222 GLN A CD  1 
ATOM   1720 O  OE1 . GLN A 1 221 ? -18.470 -12.774 6.409   1.00 20.28 ? 222 GLN A OE1 1 
ATOM   1721 N  NE2 . GLN A 1 221 ? -19.188 -11.568 4.641   1.00 18.83 ? 222 GLN A NE2 1 
ATOM   1722 N  N   . VAL A 1 222 ? -13.008 -14.158 5.462   1.00 21.53 ? 223 VAL A N   1 
ATOM   1723 C  CA  . VAL A 1 222 ? -11.660 -13.955 5.968   1.00 23.66 ? 223 VAL A CA  1 
ATOM   1724 C  C   . VAL A 1 222 ? -10.595 -14.365 4.943   1.00 27.50 ? 223 VAL A C   1 
ATOM   1725 O  O   . VAL A 1 222 ? -9.511  -13.786 4.917   1.00 28.30 ? 223 VAL A O   1 
ATOM   1726 C  CB  . VAL A 1 222 ? -11.443 -14.568 7.366   1.00 27.69 ? 223 VAL A CB  1 
ATOM   1727 C  CG1 . VAL A 1 222 ? -11.362 -16.092 7.346   1.00 28.96 ? 223 VAL A CG1 1 
ATOM   1728 C  CG2 . VAL A 1 222 ? -10.215 -13.963 8.033   1.00 28.06 ? 223 VAL A CG2 1 
ATOM   1729 N  N   . LEU A 1 223 ? -10.890 -15.354 4.089   1.00 25.51 ? 224 LEU A N   1 
ATOM   1730 C  CA  . LEU A 1 223 ? -9.913  -15.776 3.101   1.00 27.38 ? 224 LEU A CA  1 
ATOM   1731 C  C   . LEU A 1 223 ? -9.578  -14.630 2.149   1.00 25.32 ? 224 LEU A C   1 
ATOM   1732 O  O   . LEU A 1 223 ? -8.427  -14.518 1.722   1.00 24.71 ? 224 LEU A O   1 
ATOM   1733 C  CB  . LEU A 1 223 ? -10.397 -17.019 2.345   1.00 30.21 ? 224 LEU A CB  1 
ATOM   1734 C  CG  . LEU A 1 223 ? -9.280  -17.818 1.676   1.00 38.62 ? 224 LEU A CG  1 
ATOM   1735 N  N   . LYS A 1 224 ? -10.571 -13.780 1.837   1.00 22.82 ? 225 LYS A N   1 
ATOM   1736 C  CA  . LYS A 1 224 ? -10.346 -12.601 1.027   1.00 24.61 ? 225 LYS A CA  1 
ATOM   1737 C  C   . LYS A 1 224 ? -9.416  -11.599 1.715   1.00 22.64 ? 225 LYS A C   1 
ATOM   1738 O  O   . LYS A 1 224 ? -8.620  -10.971 1.047   1.00 21.08 ? 225 LYS A O   1 
ATOM   1739 C  CB  . LYS A 1 224 ? -11.666 -11.994 0.543   1.00 29.49 ? 225 LYS A CB  1 
ATOM   1740 C  CG  . LYS A 1 224 ? -12.377 -12.815 -0.528  1.00 33.69 ? 225 LYS A CG  1 
ATOM   1741 C  CD  . LYS A 1 224 ? -13.492 -12.059 -1.203  1.00 43.68 ? 225 LYS A CD  1 
ATOM   1742 C  CE  . LYS A 1 224 ? -13.689 -12.480 -2.646  1.00 47.92 ? 225 LYS A CE  1 
ATOM   1743 N  NZ  . LYS A 1 224 ? -14.301 -13.824 -2.718  1.00 51.89 ? 225 LYS A NZ  1 
ATOM   1744 N  N   . PHE A 1 225 ? -9.493  -11.429 3.045   1.00 19.96 ? 226 PHE A N   1 
ATOM   1745 C  CA  . PHE A 1 225 ? -8.481  -10.604 3.695   1.00 21.02 ? 226 PHE A CA  1 
ATOM   1746 C  C   . PHE A 1 225 ? -7.069  -11.153 3.414   1.00 21.11 ? 226 PHE A C   1 
ATOM   1747 O  O   . PHE A 1 225 ? -6.115  -10.393 3.261   1.00 22.07 ? 226 PHE A O   1 
ATOM   1748 C  CB  . PHE A 1 225 ? -8.650  -10.633 5.223   1.00 19.68 ? 226 PHE A CB  1 
ATOM   1749 C  CG  . PHE A 1 225 ? -9.837  -9.904  5.813   1.00 23.06 ? 226 PHE A CG  1 
ATOM   1750 C  CD1 . PHE A 1 225 ? -10.879 -9.428  5.033   1.00 23.44 ? 226 PHE A CD1 1 
ATOM   1751 C  CD2 . PHE A 1 225 ? -9.946  -9.779  7.194   1.00 25.51 ? 226 PHE A CD2 1 
ATOM   1752 C  CE1 . PHE A 1 225 ? -11.958 -8.777  5.615   1.00 26.81 ? 226 PHE A CE1 1 
ATOM   1753 C  CE2 . PHE A 1 225 ? -11.030 -9.148  7.783   1.00 28.03 ? 226 PHE A CE2 1 
ATOM   1754 C  CZ  . PHE A 1 225 ? -12.039 -8.648  6.988   1.00 26.64 ? 226 PHE A CZ  1 
ATOM   1755 N  N   . ARG A 1 226 ? -6.923  -12.484 3.413   1.00 21.20 ? 227 ARG A N   1 
ATOM   1756 C  CA  . ARG A 1 226 ? -5.604  -13.110 3.428   1.00 21.51 ? 227 ARG A CA  1 
ATOM   1757 C  C   . ARG A 1 226 ? -4.995  -13.103 2.018   1.00 23.39 ? 227 ARG A C   1 
ATOM   1758 O  O   . ARG A 1 226 ? -3.850  -13.517 1.842   1.00 25.52 ? 227 ARG A O   1 
ATOM   1759 C  CB  . ARG A 1 226 ? -5.723  -14.550 3.935   1.00 21.09 ? 227 ARG A CB  1 
ATOM   1760 C  CG  . ARG A 1 226 ? -6.088  -14.708 5.410   1.00 19.38 ? 227 ARG A CG  1 
ATOM   1761 C  CD  . ARG A 1 226 ? -6.113  -16.182 5.830   1.00 22.26 ? 227 ARG A CD  1 
ATOM   1762 N  NE  . ARG A 1 226 ? -6.633  -16.288 7.191   1.00 22.92 ? 227 ARG A NE  1 
ATOM   1763 C  CZ  . ARG A 1 226 ? -7.469  -17.205 7.659   1.00 27.48 ? 227 ARG A CZ  1 
ATOM   1764 N  NH1 . ARG A 1 226 ? -7.920  -18.175 6.875   1.00 30.58 ? 227 ARG A NH1 1 
ATOM   1765 N  NH2 . ARG A 1 226 ? -7.874  -17.153 8.917   1.00 26.52 ? 227 ARG A NH2 1 
ATOM   1766 N  N   . LYS A 1 227 ? -5.760  -12.619 1.035   1.00 23.05 ? 228 LYS A N   1 
ATOM   1767 C  CA  . LYS A 1 227 ? -5.267  -12.473 -0.334  1.00 25.42 ? 228 LYS A CA  1 
ATOM   1768 C  C   . LYS A 1 227 ? -4.558  -11.138 -0.536  1.00 23.65 ? 228 LYS A C   1 
ATOM   1769 O  O   . LYS A 1 227 ? -3.894  -10.942 -1.548  1.00 21.33 ? 228 LYS A O   1 
ATOM   1770 C  CB  . LYS A 1 227 ? -6.424  -12.636 -1.331  1.00 26.62 ? 228 LYS A CB  1 
ATOM   1771 C  CG  . LYS A 1 227 ? -6.967  -14.054 -1.443  1.00 30.21 ? 228 LYS A CG  1 
ATOM   1772 C  CD  . LYS A 1 227 ? -7.939  -14.245 -2.600  1.00 36.47 ? 228 LYS A CD  1 
ATOM   1773 N  N   . LEU A 1 228 ? -4.710  -10.192 0.406   1.00 23.36 ? 229 LEU A N   1 
ATOM   1774 C  CA  . LEU A 1 228 ? -3.998  -8.919  0.317   1.00 22.45 ? 229 LEU A CA  1 
ATOM   1775 C  C   . LEU A 1 228 ? -2.491  -9.140  0.477   1.00 24.27 ? 229 LEU A C   1 
ATOM   1776 O  O   . LEU A 1 228 ? -2.081  -10.170 0.986   1.00 24.01 ? 229 LEU A O   1 
ATOM   1777 C  CB  . LEU A 1 228 ? -4.517  -7.983  1.411   1.00 21.70 ? 229 LEU A CB  1 
ATOM   1778 C  CG  . LEU A 1 228 ? -5.988  -7.578  1.253   1.00 21.13 ? 229 LEU A CG  1 
ATOM   1779 C  CD1 . LEU A 1 228 ? -6.516  -6.942  2.532   1.00 20.69 ? 229 LEU A CD1 1 
ATOM   1780 C  CD2 . LEU A 1 228 ? -6.130  -6.615  0.085   1.00 21.66 ? 229 LEU A CD2 1 
ATOM   1781 N  N   . ASN A 1 229 ? -1.691  -8.176  -0.008  1.00 24.95 ? 230 ASN A N   1 
ATOM   1782 C  CA  . ASN A 1 229 ? -0.240  -8.198  0.049   1.00 23.72 ? 230 ASN A CA  1 
ATOM   1783 C  C   . ASN A 1 229 ? 0.279   -7.044  0.908   1.00 25.70 ? 230 ASN A C   1 
ATOM   1784 O  O   . ASN A 1 229 ? -0.251  -5.929  0.856   1.00 27.51 ? 230 ASN A O   1 
ATOM   1785 C  CB  . ASN A 1 229 ? 0.359   -7.963  -1.337  1.00 25.84 ? 230 ASN A CB  1 
ATOM   1786 C  CG  . ASN A 1 229 ? 0.293   -9.166  -2.254  1.00 26.70 ? 230 ASN A CG  1 
ATOM   1787 O  OD1 . ASN A 1 229 ? 0.886   -9.140  -3.323  1.00 30.99 ? 230 ASN A OD1 1 
ATOM   1788 N  ND2 . ASN A 1 229 ? -0.418  -10.207 -1.863  1.00 26.11 ? 230 ASN A ND2 1 
ATOM   1789 N  N   . PHE A 1 230 ? 1.369   -7.301  1.636   1.00 24.40 ? 231 PHE A N   1 
ATOM   1790 C  CA  . PHE A 1 230 ? 2.054   -6.271  2.411   1.00 25.28 ? 231 PHE A CA  1 
ATOM   1791 C  C   . PHE A 1 230 ? 2.875   -5.393  1.474   1.00 28.80 ? 231 PHE A C   1 
ATOM   1792 O  O   . PHE A 1 230 ? 3.041   -4.195  1.706   1.00 27.10 ? 231 PHE A O   1 
ATOM   1793 C  CB  . PHE A 1 230 ? 3.018   -6.873  3.439   1.00 26.12 ? 231 PHE A CB  1 
ATOM   1794 C  CG  . PHE A 1 230 ? 2.485   -7.467  4.728   1.00 25.73 ? 231 PHE A CG  1 
ATOM   1795 C  CD1 . PHE A 1 230 ? 1.819   -6.685  5.663   1.00 26.48 ? 231 PHE A CD1 1 
ATOM   1796 C  CD2 . PHE A 1 230 ? 2.735   -8.796  5.057   1.00 22.84 ? 231 PHE A CD2 1 
ATOM   1797 C  CE1 . PHE A 1 230 ? 1.393   -7.224  6.870   1.00 24.01 ? 231 PHE A CE1 1 
ATOM   1798 C  CE2 . PHE A 1 230 ? 2.285   -9.343  6.256   1.00 25.07 ? 231 PHE A CE2 1 
ATOM   1799 C  CZ  . PHE A 1 230 ? 1.603   -8.559  7.166   1.00 23.73 ? 231 PHE A CZ  1 
ATOM   1800 N  N   . ASN A 1 231 ? 3.376   -6.012  0.400   1.00 28.20 ? 232 ASN A N   1 
ATOM   1801 C  CA  . ASN A 1 231 ? 4.325   -5.393  -0.505  1.00 30.23 ? 232 ASN A CA  1 
ATOM   1802 C  C   . ASN A 1 231 ? 3.595   -4.506  -1.499  1.00 30.00 ? 232 ASN A C   1 
ATOM   1803 O  O   . ASN A 1 231 ? 2.401   -4.679  -1.717  1.00 27.47 ? 232 ASN A O   1 
ATOM   1804 C  CB  . ASN A 1 231 ? 5.032   -6.474  -1.328  1.00 29.24 ? 232 ASN A CB  1 
ATOM   1805 C  CG  . ASN A 1 231 ? 4.064   -7.413  -2.015  1.00 29.84 ? 232 ASN A CG  1 
ATOM   1806 O  OD1 . ASN A 1 231 ? 3.517   -8.321  -1.382  1.00 30.54 ? 232 ASN A OD1 1 
ATOM   1807 N  ND2 . ASN A 1 231 ? 3.866   -7.219  -3.317  1.00 28.85 ? 232 ASN A ND2 1 
ATOM   1808 N  N   . GLY A 1 232 ? 4.340   -3.580  -2.123  1.00 26.74 ? 233 GLY A N   1 
ATOM   1809 C  CA  . GLY A 1 232 ? 3.817   -2.832  -3.252  1.00 29.51 ? 233 GLY A CA  1 
ATOM   1810 C  C   . GLY A 1 232 ? 3.949   -3.645  -4.536  1.00 35.22 ? 233 GLY A C   1 
ATOM   1811 O  O   . GLY A 1 232 ? 4.682   -4.639  -4.586  1.00 34.81 ? 233 GLY A O   1 
ATOM   1812 N  N   . GLU A 1 233 ? 3.228   -3.212  -5.566  1.00 34.45 ? 234 GLU A N   1 
ATOM   1813 C  CA  . GLU A 1 233 ? 3.181   -3.955  -6.812  1.00 42.67 ? 234 GLU A CA  1 
ATOM   1814 C  C   . GLU A 1 233 ? 4.565   -3.932  -7.455  1.00 41.86 ? 234 GLU A C   1 
ATOM   1815 O  O   . GLU A 1 233 ? 5.165   -2.870  -7.575  1.00 36.87 ? 234 GLU A O   1 
ATOM   1816 C  CB  . GLU A 1 233 ? 2.125   -3.359  -7.734  1.00 46.57 ? 234 GLU A CB  1 
ATOM   1817 C  CG  . GLU A 1 233 ? 1.985   -4.113  -9.040  1.00 51.75 ? 234 GLU A CG  1 
ATOM   1818 C  CD  . GLU A 1 233 ? 0.957   -3.486  -9.961  1.00 57.74 ? 234 GLU A CD  1 
ATOM   1819 O  OE1 . GLU A 1 233 ? 0.111   -2.706  -9.467  1.00 57.48 ? 234 GLU A OE1 1 
ATOM   1820 O  OE2 . GLU A 1 233 ? 1.011   -3.770  -11.171 1.00 67.57 ? 234 GLU A OE2 1 
ATOM   1821 N  N   . GLY A 1 234 ? 5.073   -5.118  -7.806  1.00 43.79 ? 235 GLY A N   1 
ATOM   1822 C  CA  . GLY A 1 234 ? 6.379   -5.243  -8.430  1.00 45.18 ? 235 GLY A CA  1 
ATOM   1823 C  C   . GLY A 1 234 ? 7.523   -5.326  -7.419  1.00 50.02 ? 235 GLY A C   1 
ATOM   1824 O  O   . GLY A 1 234 ? 8.689   -5.243  -7.815  1.00 46.52 ? 235 GLY A O   1 
ATOM   1825 N  N   . GLU A 1 235 ? 7.182   -5.437  -6.122  1.00 42.00 ? 236 GLU A N   1 
ATOM   1826 C  CA  . GLU A 1 235 ? 8.103   -5.886  -5.088  1.00 42.52 ? 236 GLU A CA  1 
ATOM   1827 C  C   . GLU A 1 235 ? 7.816   -7.363  -4.840  1.00 41.75 ? 236 GLU A C   1 
ATOM   1828 O  O   . GLU A 1 235 ? 6.790   -7.863  -5.288  1.00 43.00 ? 236 GLU A O   1 
ATOM   1829 C  CB  . GLU A 1 235 ? 7.894   -5.163  -3.750  1.00 50.42 ? 236 GLU A CB  1 
ATOM   1830 C  CG  . GLU A 1 235 ? 7.992   -3.646  -3.785  1.00 56.09 ? 236 GLU A CG  1 
ATOM   1831 C  CD  . GLU A 1 235 ? 7.547   -2.959  -2.497  1.00 58.36 ? 236 GLU A CD  1 
ATOM   1832 O  OE1 . GLU A 1 235 ? 7.420   -3.644  -1.456  1.00 55.01 ? 236 GLU A OE1 1 
ATOM   1833 O  OE2 . GLU A 1 235 ? 7.322   -1.734  -2.527  1.00 67.62 ? 236 GLU A OE2 1 
ATOM   1834 N  N   . PRO A 1 236 ? 8.696   -8.121  -4.141  1.00 43.95 ? 237 PRO A N   1 
ATOM   1835 C  CA  . PRO A 1 236 ? 8.408   -9.514  -3.782  1.00 42.39 ? 237 PRO A CA  1 
ATOM   1836 C  C   . PRO A 1 236 ? 7.092   -9.728  -3.035  1.00 39.88 ? 237 PRO A C   1 
ATOM   1837 O  O   . PRO A 1 236 ? 6.811   -9.014  -2.076  1.00 39.56 ? 237 PRO A O   1 
ATOM   1838 C  CB  . PRO A 1 236 ? 9.576   -9.883  -2.850  1.00 45.06 ? 237 PRO A CB  1 
ATOM   1839 C  CG  . PRO A 1 236 ? 10.708  -9.005  -3.332  1.00 42.89 ? 237 PRO A CG  1 
ATOM   1840 C  CD  . PRO A 1 236 ? 10.048  -7.703  -3.729  1.00 48.31 ? 237 PRO A CD  1 
ATOM   1841 N  N   . GLU A 1 237 ? 6.330   -10.747 -3.463  1.00 34.33 ? 238 GLU A N   1 
ATOM   1842 C  CA  . GLU A 1 237 ? 5.028   -11.089 -2.905  1.00 35.80 ? 238 GLU A CA  1 
ATOM   1843 C  C   . GLU A 1 237 ? 5.159   -11.549 -1.454  1.00 37.52 ? 238 GLU A C   1 
ATOM   1844 O  O   . GLU A 1 237 ? 5.903   -12.476 -1.152  1.00 44.81 ? 238 GLU A O   1 
ATOM   1845 C  CB  . GLU A 1 237 ? 4.360   -12.173 -3.760  1.00 36.06 ? 238 GLU A CB  1 
ATOM   1846 C  CG  . GLU A 1 237 ? 2.982   -12.595 -3.274  1.00 39.01 ? 238 GLU A CG  1 
ATOM   1847 C  CD  . GLU A 1 237 ? 2.238   -13.548 -4.199  1.00 43.74 ? 238 GLU A CD  1 
ATOM   1848 O  OE1 . GLU A 1 237 ? 2.737   -13.827 -5.299  1.00 46.36 ? 238 GLU A OE1 1 
ATOM   1849 O  OE2 . GLU A 1 237 ? 1.164   -14.032 -3.810  1.00 48.23 ? 238 GLU A OE2 1 
ATOM   1850 N  N   . GLU A 1 238 ? 4.413   -10.890 -0.560  1.00 36.70 ? 239 GLU A N   1 
ATOM   1851 C  CA  . GLU A 1 238 ? 4.334   -11.265 0.839   1.00 32.76 ? 239 GLU A CA  1 
ATOM   1852 C  C   . GLU A 1 238 ? 2.884   -11.056 1.276   1.00 32.94 ? 239 GLU A C   1 
ATOM   1853 O  O   . GLU A 1 238 ? 2.415   -9.918  1.264   1.00 33.26 ? 239 GLU A O   1 
ATOM   1854 C  CB  . GLU A 1 238 ? 5.261   -10.341 1.628   1.00 42.12 ? 239 GLU A CB  1 
ATOM   1855 C  CG  . GLU A 1 238 ? 5.948   -11.015 2.806   1.00 54.45 ? 239 GLU A CG  1 
ATOM   1856 C  CD  . GLU A 1 238 ? 7.127   -10.250 3.414   1.00 60.96 ? 239 GLU A CD  1 
ATOM   1857 O  OE1 . GLU A 1 238 ? 7.406   -10.455 4.621   1.00 56.51 ? 239 GLU A OE1 1 
ATOM   1858 O  OE2 . GLU A 1 238 ? 7.772   -9.449  2.684   1.00 63.96 ? 239 GLU A OE2 1 
ATOM   1859 N  N   . LEU A 1 239 ? 2.167   -12.154 1.571   1.00 29.69 ? 240 LEU A N   1 
ATOM   1860 C  CA  . LEU A 1 239 ? 0.753   -12.060 1.895   1.00 28.16 ? 240 LEU A CA  1 
ATOM   1861 C  C   . LEU A 1 239 ? 0.611   -11.238 3.168   1.00 27.67 ? 240 LEU A C   1 
ATOM   1862 O  O   . LEU A 1 239 ? 1.331   -11.485 4.127   1.00 24.42 ? 240 LEU A O   1 
ATOM   1863 C  CB  . LEU A 1 239 ? 0.158   -13.449 2.127   1.00 30.03 ? 240 LEU A CB  1 
ATOM   1864 C  CG  . LEU A 1 239 ? -0.075  -14.307 0.884   1.00 33.21 ? 240 LEU A CG  1 
ATOM   1865 C  CD1 . LEU A 1 239 ? -1.007  -15.452 1.249   1.00 33.22 ? 240 LEU A CD1 1 
ATOM   1866 C  CD2 . LEU A 1 239 ? -0.695  -13.475 -0.241  1.00 33.07 ? 240 LEU A CD2 1 
ATOM   1867 N  N   . MET A 1 240 ? -0.357  -10.309 3.167   1.00 23.81 ? 241 MET A N   1 
ATOM   1868 C  CA  . MET A 1 240 ? -0.750  -9.612  4.387   1.00 23.62 ? 241 MET A CA  1 
ATOM   1869 C  C   . MET A 1 240 ? -1.565  -10.552 5.270   1.00 20.45 ? 241 MET A C   1 
ATOM   1870 O  O   . MET A 1 240 ? -2.780  -10.696 5.100   1.00 22.92 ? 241 MET A O   1 
ATOM   1871 C  CB  . MET A 1 240 ? -1.609  -8.398  4.024   1.00 22.85 ? 241 MET A CB  1 
ATOM   1872 C  CG  . MET A 1 240 ? -1.859  -7.461  5.208   1.00 21.78 ? 241 MET A CG  1 
ATOM   1873 S  SD  . MET A 1 240 ? -2.899  -6.121  4.632   1.00 23.77 ? 241 MET A SD  1 
ATOM   1874 C  CE  . MET A 1 240 ? -1.702  -5.036  3.847   1.00 23.42 ? 241 MET A CE  1 
ATOM   1875 N  N   . VAL A 1 241 ? -0.869  -11.215 6.204   1.00 24.17 ? 242 VAL A N   1 
ATOM   1876 C  CA  . VAL A 1 241 ? -1.474  -12.047 7.227   1.00 22.58 ? 242 VAL A CA  1 
ATOM   1877 C  C   . VAL A 1 241 ? -0.655  -11.851 8.497   1.00 23.02 ? 242 VAL A C   1 
ATOM   1878 O  O   . VAL A 1 241 ? 0.495   -11.446 8.423   1.00 23.70 ? 242 VAL A O   1 
ATOM   1879 C  CB  . VAL A 1 241 ? -1.492  -13.544 6.823   1.00 23.40 ? 242 VAL A CB  1 
ATOM   1880 C  CG1 . VAL A 1 241 ? -2.452  -13.810 5.674   1.00 22.38 ? 242 VAL A CG1 1 
ATOM   1881 C  CG2 . VAL A 1 241 ? -0.103  -14.071 6.500   1.00 24.56 ? 242 VAL A CG2 1 
ATOM   1882 N  N   . ASP A 1 242 ? -1.253  -12.173 9.640   1.00 21.26 ? 243 ASP A N   1 
ATOM   1883 C  CA  . ASP A 1 242 ? -0.632  -12.026 10.943  1.00 22.24 ? 243 ASP A CA  1 
ATOM   1884 C  C   . ASP A 1 242 ? -0.166  -10.586 11.163  1.00 21.97 ? 243 ASP A C   1 
ATOM   1885 O  O   . ASP A 1 242 ? 0.951   -10.340 11.633  1.00 21.72 ? 243 ASP A O   1 
ATOM   1886 C  CB  . ASP A 1 242 ? 0.438   -13.095 11.203  1.00 22.05 ? 243 ASP A CB  1 
ATOM   1887 C  CG  . ASP A 1 242 ? -0.130  -14.502 11.300  1.00 25.56 ? 243 ASP A CG  1 
ATOM   1888 O  OD1 . ASP A 1 242 ? -1.104  -14.720 12.067  1.00 24.17 ? 243 ASP A OD1 1 
ATOM   1889 O  OD2 . ASP A 1 242 ? 0.420   -15.387 10.625  1.00 26.80 ? 243 ASP A OD2 1 
ATOM   1890 N  N   . ASN A 1 243 ? -1.055  -9.646  10.871  1.00 18.85 ? 244 ASN A N   1 
ATOM   1891 C  CA  . ASN A 1 243 ? -0.735  -8.250  11.119  1.00 21.05 ? 244 ASN A CA  1 
ATOM   1892 C  C   . ASN A 1 243 ? -1.318  -7.837  12.472  1.00 20.38 ? 244 ASN A C   1 
ATOM   1893 O  O   . ASN A 1 243 ? -2.002  -6.823  12.567  1.00 21.84 ? 244 ASN A O   1 
ATOM   1894 C  CB  . ASN A 1 243 ? -1.246  -7.320  10.023  1.00 21.28 ? 244 ASN A CB  1 
ATOM   1895 C  CG  . ASN A 1 243 ? -2.721  -7.483  9.727   1.00 22.34 ? 244 ASN A CG  1 
ATOM   1896 O  OD1 . ASN A 1 243 ? -3.370  -8.395  10.248  1.00 22.82 ? 244 ASN A OD1 1 
ATOM   1897 N  ND2 . ASN A 1 243 ? -3.253  -6.582  8.906   1.00 20.53 ? 244 ASN A ND2 1 
ATOM   1898 N  N   . TRP A 1 244 ? -0.993  -8.607  13.500  1.00 20.02 ? 245 TRP A N   1 
ATOM   1899 C  CA  . TRP A 1 244 ? -1.427  -8.321  14.860  1.00 19.88 ? 245 TRP A CA  1 
ATOM   1900 C  C   . TRP A 1 244 ? -0.217  -8.207  15.783  1.00 21.30 ? 245 TRP A C   1 
ATOM   1901 O  O   . TRP A 1 244 ? 0.779   -8.920  15.617  1.00 19.23 ? 245 TRP A O   1 
ATOM   1902 C  CB  . TRP A 1 244 ? -2.416  -9.386  15.367  1.00 21.51 ? 245 TRP A CB  1 
ATOM   1903 C  CG  . TRP A 1 244 ? -1.987  -10.811 15.176  1.00 22.45 ? 245 TRP A CG  1 
ATOM   1904 C  CD1 . TRP A 1 244 ? -2.098  -11.569 14.035  1.00 20.32 ? 245 TRP A CD1 1 
ATOM   1905 C  CD2 . TRP A 1 244 ? -1.400  -11.666 16.173  1.00 20.16 ? 245 TRP A CD2 1 
ATOM   1906 N  NE1 . TRP A 1 244 ? -1.592  -12.827 14.254  1.00 19.45 ? 245 TRP A NE1 1 
ATOM   1907 C  CE2 . TRP A 1 244 ? -1.166  -12.912 15.556  1.00 21.49 ? 245 TRP A CE2 1 
ATOM   1908 C  CE3 . TRP A 1 244 ? -1.057  -11.498 17.521  1.00 21.56 ? 245 TRP A CE3 1 
ATOM   1909 C  CZ2 . TRP A 1 244 ? -0.601  -13.984 16.249  1.00 21.13 ? 245 TRP A CZ2 1 
ATOM   1910 C  CZ3 . TRP A 1 244 ? -0.497  -12.552 18.202  1.00 21.79 ? 245 TRP A CZ3 1 
ATOM   1911 C  CH2 . TRP A 1 244 ? -0.294  -13.776 17.574  1.00 22.40 ? 245 TRP A CH2 1 
ATOM   1912 N  N   . ARG A 1 245 ? -0.348  -7.339  16.796  1.00 20.03 ? 246 ARG A N   1 
ATOM   1913 C  CA  . ARG A 1 245 ? 0.595   -7.236  17.901  1.00 18.96 ? 246 ARG A CA  1 
ATOM   1914 C  C   . ARG A 1 245 ? 0.106   -8.124  19.033  1.00 22.20 ? 246 ARG A C   1 
ATOM   1915 O  O   . ARG A 1 245 ? -1.096  -8.158  19.319  1.00 24.68 ? 246 ARG A O   1 
ATOM   1916 C  CB  . ARG A 1 245 ? 0.683   -5.794  18.417  1.00 19.73 ? 246 ARG A CB  1 
ATOM   1917 C  CG  . ARG A 1 245 ? 1.849   -5.551  19.370  1.00 22.11 ? 246 ARG A CG  1 
ATOM   1918 C  CD  . ARG A 1 245 ? 1.735   -4.222  20.109  1.00 21.30 ? 246 ARG A CD  1 
ATOM   1919 N  NE  . ARG A 1 245 ? 2.981   -3.837  20.774  1.00 21.17 ? 246 ARG A NE  1 
ATOM   1920 C  CZ  . ARG A 1 245 ? 3.135   -2.783  21.583  1.00 24.14 ? 246 ARG A CZ  1 
ATOM   1921 N  NH1 . ARG A 1 245 ? 2.119   -1.974  21.893  1.00 22.36 ? 246 ARG A NH1 1 
ATOM   1922 N  NH2 . ARG A 1 245 ? 4.330   -2.544  22.093  1.00 24.26 ? 246 ARG A NH2 1 
ATOM   1923 N  N   . PRO A 1 246 ? 1.000   -8.918  19.665  1.00 22.91 ? 247 PRO A N   1 
ATOM   1924 C  CA  . PRO A 1 246 ? 0.607   -9.744  20.807  1.00 21.78 ? 247 PRO A CA  1 
ATOM   1925 C  C   . PRO A 1 246 ? 0.235   -8.901  22.017  1.00 21.92 ? 247 PRO A C   1 
ATOM   1926 O  O   . PRO A 1 246 ? 0.598   -7.716  22.118  1.00 22.51 ? 247 PRO A O   1 
ATOM   1927 C  CB  . PRO A 1 246 ? 1.882   -10.526 21.152  1.00 22.76 ? 247 PRO A CB  1 
ATOM   1928 C  CG  . PRO A 1 246 ? 2.701   -10.484 19.870  1.00 23.42 ? 247 PRO A CG  1 
ATOM   1929 C  CD  . PRO A 1 246 ? 2.410   -9.116  19.292  1.00 22.74 ? 247 PRO A CD  1 
ATOM   1930 N  N   . ALA A 1 247 ? -0.460  -9.569  22.944  1.00 20.85 ? 248 ALA A N   1 
ATOM   1931 C  CA  . ALA A 1 247 ? -0.772  -9.010  24.251  1.00 21.15 ? 248 ALA A CA  1 
ATOM   1932 C  C   . ALA A 1 247 ? 0.482   -8.485  24.967  1.00 24.03 ? 248 ALA A C   1 
ATOM   1933 O  O   . ALA A 1 247 ? 1.545   -9.122  25.015  1.00 23.55 ? 248 ALA A O   1 
ATOM   1934 C  CB  . ALA A 1 247 ? -1.473  -10.062 25.061  1.00 22.48 ? 248 ALA A CB  1 
ATOM   1935 N  N   . GLN A 1 248 ? 0.309   -7.320  25.595  1.00 23.78 ? 249 GLN A N   1 
ATOM   1936 C  CA  . GLN A 1 248 ? 1.355   -6.582  26.270  1.00 21.26 ? 249 GLN A CA  1 
ATOM   1937 C  C   . GLN A 1 248 ? 1.025   -6.591  27.758  1.00 23.96 ? 249 GLN A C   1 
ATOM   1938 O  O   . GLN A 1 248 ? -0.135  -6.773  28.123  1.00 24.71 ? 249 GLN A O   1 
ATOM   1939 C  CB  . GLN A 1 248 ? 1.356   -5.153  25.725  1.00 22.96 ? 249 GLN A CB  1 
ATOM   1940 C  CG  . GLN A 1 248 ? 1.705   -5.080  24.236  1.00 23.11 ? 249 GLN A CG  1 
ATOM   1941 C  CD  . GLN A 1 248 ? 3.055   -5.680  23.901  1.00 25.84 ? 249 GLN A CD  1 
ATOM   1942 O  OE1 . GLN A 1 248 ? 4.076   -5.312  24.479  1.00 25.63 ? 249 GLN A OE1 1 
ATOM   1943 N  NE2 . GLN A 1 248 ? 3.085   -6.592  22.938  1.00 25.02 ? 249 GLN A NE2 1 
ATOM   1944 N  N   . PRO A 1 249 ? 2.017   -6.457  28.658  1.00 26.93 ? 250 PRO A N   1 
ATOM   1945 C  CA  . PRO A 1 249 ? 1.732   -6.606  30.083  1.00 27.54 ? 250 PRO A CA  1 
ATOM   1946 C  C   . PRO A 1 249 ? 0.768   -5.514  30.543  1.00 28.71 ? 250 PRO A C   1 
ATOM   1947 O  O   . PRO A 1 249 ? 0.824   -4.382  30.068  1.00 30.02 ? 250 PRO A O   1 
ATOM   1948 C  CB  . PRO A 1 249 ? 3.109   -6.521  30.744  1.00 27.40 ? 250 PRO A CB  1 
ATOM   1949 C  CG  . PRO A 1 249 ? 3.996   -5.832  29.721  1.00 28.93 ? 250 PRO A CG  1 
ATOM   1950 C  CD  . PRO A 1 249 ? 3.449   -6.219  28.368  1.00 24.97 ? 250 PRO A CD  1 
ATOM   1951 N  N   . LEU A 1 250 ? -0.101  -5.877  31.488  1.00 27.81 ? 251 LEU A N   1 
ATOM   1952 C  CA  . LEU A 1 250 ? -1.157  -4.979  31.936  1.00 29.24 ? 251 LEU A CA  1 
ATOM   1953 C  C   . LEU A 1 250 ? -0.579  -3.868  32.822  1.00 28.94 ? 251 LEU A C   1 
ATOM   1954 O  O   . LEU A 1 250 ? -1.121  -2.758  32.872  1.00 28.08 ? 251 LEU A O   1 
ATOM   1955 C  CB  . LEU A 1 250 ? -2.196  -5.826  32.690  1.00 29.59 ? 251 LEU A CB  1 
ATOM   1956 C  CG  . LEU A 1 250 ? -3.513  -5.153  33.064  1.00 28.45 ? 251 LEU A CG  1 
ATOM   1957 C  CD1 . LEU A 1 250 ? -4.182  -4.536  31.841  1.00 29.30 ? 251 LEU A CD1 1 
ATOM   1958 C  CD2 . LEU A 1 250 ? -4.436  -6.189  33.688  1.00 29.90 ? 251 LEU A CD2 1 
ATOM   1959 N  N   . LYS A 1 251 ? 0.501   -4.183  33.547  1.00 29.41 ? 252 LYS A N   1 
ATOM   1960 C  CA  . LYS A 1 251 ? 1.125   -3.277  34.506  1.00 31.09 ? 252 LYS A CA  1 
ATOM   1961 C  C   . LYS A 1 251 ? 0.078   -2.828  35.524  1.00 30.79 ? 252 LYS A C   1 
ATOM   1962 O  O   . LYS A 1 251 ? -0.669  -3.655  36.030  1.00 35.60 ? 252 LYS A O   1 
ATOM   1963 C  CB  . LYS A 1 251 ? 1.935   -2.186  33.804  1.00 31.47 ? 252 LYS A CB  1 
ATOM   1964 C  CG  . LYS A 1 251 ? 2.955   -2.760  32.833  1.00 32.86 ? 252 LYS A CG  1 
ATOM   1965 C  CD  . LYS A 1 251 ? 4.113   -1.886  32.487  1.00 37.44 ? 252 LYS A CD  1 
ATOM   1966 C  CE  . LYS A 1 251 ? 5.198   -2.693  31.796  1.00 38.45 ? 252 LYS A CE  1 
ATOM   1967 N  NZ  . LYS A 1 251 ? 5.918   -1.880  30.782  1.00 37.15 ? 252 LYS A NZ  1 
ATOM   1968 N  N   . ASN A 1 252 ? -0.022  -1.534  35.808  1.00 33.10 ? 253 ASN A N   1 
ATOM   1969 C  CA  . ASN A 1 252 ? -0.839  -1.174  36.972  1.00 40.33 ? 253 ASN A CA  1 
ATOM   1970 C  C   . ASN A 1 252 ? -2.352  -1.099  36.671  1.00 39.65 ? 253 ASN A C   1 
ATOM   1971 O  O   . ASN A 1 252 ? -3.126  -0.839  37.586  1.00 46.49 ? 253 ASN A O   1 
ATOM   1972 C  CB  . ASN A 1 252 ? -0.270  0.046   37.712  1.00 41.97 ? 253 ASN A CB  1 
ATOM   1973 N  N   . ARG A 1 253 ? -2.799  -1.398  35.438  1.00 28.20 ? 254 ARG A N   1 
ATOM   1974 C  CA  . ARG A 1 253 ? -4.144  -1.030  35.001  1.00 27.85 ? 254 ARG A CA  1 
ATOM   1975 C  C   . ARG A 1 253 ? -5.227  -2.025  35.431  1.00 28.81 ? 254 ARG A C   1 
ATOM   1976 O  O   . ARG A 1 253 ? -4.985  -3.228  35.561  1.00 29.49 ? 254 ARG A O   1 
ATOM   1977 C  CB  . ARG A 1 253 ? -4.141  -0.910  33.478  1.00 24.28 ? 254 ARG A CB  1 
ATOM   1978 C  CG  . ARG A 1 253 ? -3.215  0.174   32.968  1.00 25.25 ? 254 ARG A CG  1 
ATOM   1979 C  CD  . ARG A 1 253 ? -3.111  0.098   31.462  1.00 22.30 ? 254 ARG A CD  1 
ATOM   1980 N  NE  . ARG A 1 253 ? -2.268  -1.015  31.022  1.00 21.87 ? 254 ARG A NE  1 
ATOM   1981 C  CZ  . ARG A 1 253 ? -2.020  -1.249  29.735  1.00 22.49 ? 254 ARG A CZ  1 
ATOM   1982 N  NH1 . ARG A 1 253 ? -2.636  -0.521  28.822  1.00 19.98 ? 254 ARG A NH1 1 
ATOM   1983 N  NH2 . ARG A 1 253 ? -1.230  -2.244  29.360  1.00 22.41 ? 254 ARG A NH2 1 
ATOM   1984 N  N   . GLN A 1 254 ? -6.446  -1.503  35.604  1.00 27.90 ? 255 GLN A N   1 
ATOM   1985 C  CA  . GLN A 1 254 ? -7.631  -2.306  35.846  1.00 30.08 ? 255 GLN A CA  1 
ATOM   1986 C  C   . GLN A 1 254 ? -8.493  -2.265  34.582  1.00 30.07 ? 255 GLN A C   1 
ATOM   1987 O  O   . GLN A 1 254 ? -8.640  -1.218  33.958  1.00 29.39 ? 255 GLN A O   1 
ATOM   1988 C  CB  . GLN A 1 254 ? -8.354  -1.758  37.086  1.00 33.59 ? 255 GLN A CB  1 
ATOM   1989 C  CG  . GLN A 1 254 ? -9.538  -2.607  37.547  1.00 41.96 ? 255 GLN A CG  1 
ATOM   1990 N  N   . ILE A 1 255 ? -9.031  -3.420  34.191  1.00 26.97 ? 256 ILE A N   1 
ATOM   1991 C  CA  . ILE A 1 255 ? -9.999  -3.478  33.110  1.00 25.98 ? 256 ILE A CA  1 
ATOM   1992 C  C   . ILE A 1 255 ? -11.379 -3.445  33.753  1.00 26.28 ? 256 ILE A C   1 
ATOM   1993 O  O   . ILE A 1 255 ? -11.649 -4.178  34.700  1.00 25.85 ? 256 ILE A O   1 
ATOM   1994 C  CB  . ILE A 1 255 ? -9.795  -4.736  32.249  1.00 25.82 ? 256 ILE A CB  1 
ATOM   1995 C  CG1 . ILE A 1 255 ? -8.360  -4.820  31.724  1.00 26.32 ? 256 ILE A CG1 1 
ATOM   1996 C  CG2 . ILE A 1 255 ? -10.825 -4.813  31.120  1.00 25.01 ? 256 ILE A CG2 1 
ATOM   1997 C  CD1 . ILE A 1 255 ? -8.126  -6.050  30.870  1.00 26.36 ? 256 ILE A CD1 1 
ATOM   1998 N  N   . LYS A 1 256 ? -12.225 -2.547  33.258  1.00 25.56 ? 257 LYS A N   1 
ATOM   1999 C  CA  . LYS A 1 256 ? -13.575 -2.420  33.770  1.00 25.80 ? 257 LYS A CA  1 
ATOM   2000 C  C   . LYS A 1 256 ? -14.547 -3.085  32.794  1.00 26.53 ? 257 LYS A C   1 
ATOM   2001 O  O   . LYS A 1 256 ? -14.306 -3.135  31.576  1.00 26.07 ? 257 LYS A O   1 
ATOM   2002 C  CB  . LYS A 1 256 ? -13.816 -0.947  34.136  1.00 30.44 ? 257 LYS A CB  1 
ATOM   2003 C  CG  . LYS A 1 256 ? -12.733 -0.374  35.064  1.00 34.48 ? 257 LYS A CG  1 
ATOM   2004 C  CD  . LYS A 1 256 ? -13.000 1.000   35.656  1.00 47.01 ? 257 LYS A CD  1 
ATOM   2005 N  N   . ALA A 1 257 ? -15.610 -3.663  33.355  1.00 23.78 ? 258 ALA A N   1 
ATOM   2006 C  CA  . ALA A 1 257 ? -16.677 -4.247  32.557  1.00 23.62 ? 258 ALA A CA  1 
ATOM   2007 C  C   . ALA A 1 257 ? -17.956 -3.438  32.754  1.00 25.89 ? 258 ALA A C   1 
ATOM   2008 O  O   . ALA A 1 257 ? -18.227 -2.947  33.863  1.00 23.09 ? 258 ALA A O   1 
ATOM   2009 C  CB  . ALA A 1 257 ? -16.908 -5.689  32.935  1.00 25.40 ? 258 ALA A CB  1 
ATOM   2010 N  N   . SER A 1 258 ? -18.740 -3.333  31.672  1.00 24.41 ? 259 SER A N   1 
ATOM   2011 C  CA  . SER A 1 258 ? -20.027 -2.646  31.679  1.00 25.99 ? 259 SER A CA  1 
ATOM   2012 C  C   . SER A 1 258 ? -21.148 -3.602  32.085  1.00 27.58 ? 259 SER A C   1 
ATOM   2013 O  O   . SER A 1 258 ? -22.316 -3.217  32.082  1.00 27.78 ? 259 SER A O   1 
ATOM   2014 C  CB  . SER A 1 258 ? -20.337 -2.087  30.315  1.00 26.21 ? 259 SER A CB  1 
ATOM   2015 O  OG  . SER A 1 258 ? -20.698 -3.153  29.444  1.00 26.11 ? 259 SER A OG  1 
ATOM   2016 N  N   . PHE A 1 259 ? -20.806 -4.865  32.370  1.00 27.37 ? 260 PHE A N   1 
ATOM   2017 C  CA  . PHE A 1 259 ? -21.823 -5.900  32.490  1.00 31.13 ? 260 PHE A CA  1 
ATOM   2018 C  C   . PHE A 1 259 ? -21.390 -6.954  33.505  1.00 37.90 ? 260 PHE A C   1 
ATOM   2019 O  O   . PHE A 1 259 ? -20.235 -6.962  33.953  1.00 34.58 ? 260 PHE A O   1 
ATOM   2020 C  CB  . PHE A 1 259 ? -22.033 -6.622  31.157  1.00 29.13 ? 260 PHE A CB  1 
ATOM   2021 C  CG  . PHE A 1 259 ? -20.803 -7.356  30.689  1.00 32.17 ? 260 PHE A CG  1 
ATOM   2022 C  CD1 . PHE A 1 259 ? -19.815 -6.696  29.967  1.00 30.07 ? 260 PHE A CD1 1 
ATOM   2023 C  CD2 . PHE A 1 259 ? -20.601 -8.693  31.029  1.00 33.38 ? 260 PHE A CD2 1 
ATOM   2024 C  CE1 . PHE A 1 259 ? -18.660 -7.369  29.586  1.00 27.95 ? 260 PHE A CE1 1 
ATOM   2025 C  CE2 . PHE A 1 259 ? -19.448 -9.360  30.640  1.00 33.03 ? 260 PHE A CE2 1 
ATOM   2026 C  CZ  . PHE A 1 259 ? -18.493 -8.700  29.903  1.00 31.37 ? 260 PHE A CZ  1 
ATOM   2027 N  N   . LYS A 1 260 ? -22.356 -7.848  33.770  1.00 46.07 ? 261 LYS A N   1 
ATOM   2028 C  CA  . LYS A 1 260 ? -22.355 -8.985  34.684  1.00 61.44 ? 261 LYS A CA  1 
ATOM   2029 C  C   . LYS A 1 260 ? -22.325 -8.496  36.143  1.00 68.75 ? 261 LYS A C   1 
ATOM   2030 O  O   . LYS A 1 260 ? -22.541 -7.312  36.447  1.00 75.71 ? 261 LYS A O   1 
ATOM   2031 C  CB  . LYS A 1 260 ? -21.342 -10.073 34.294  1.00 65.48 ? 261 LYS A CB  1 
ATOM   2032 O  OXT . LYS A 1 260 ? -22.111 -9.275  37.071  1.00 76.40 ? 261 LYS A OXT 1 
HETATM 2033 ZN ZN  . ZN  B 2 .   ? -5.937  -1.607  14.804  1.00 19.01 ? 301 ZN  A ZN  1 
HETATM 2034 F  F13 . V50 C 3 .   ? -2.123  1.462   16.009  1.00 29.13 ? 302 V50 A F13 1 
HETATM 2035 C  C4  . V50 C 3 .   ? -2.858  2.352   15.343  1.00 27.88 ? 302 V50 A C4  1 
HETATM 2036 C  C5  . V50 C 3 .   ? -4.269  2.261   15.344  1.00 26.78 ? 302 V50 A C5  1 
HETATM 2037 S  S7  . V50 C 3 .   ? -5.086  0.972   16.283  1.00 22.86 ? 302 V50 A S7  1 
HETATM 2038 O  O9  . V50 C 3 .   ? -6.528  1.033   16.089  1.00 19.28 ? 302 V50 A O9  1 
HETATM 2039 N  N23 . V50 C 3 .   ? -4.619  -0.472  15.668  1.00 21.54 ? 302 V50 A N23 1 
HETATM 2040 O  O8  . V50 C 3 .   ? -4.566  1.038   17.642  1.00 20.41 ? 302 V50 A O8  1 
HETATM 2041 C  C6  . V50 C 3 .   ? -4.886  3.275   14.616  1.00 30.90 ? 302 V50 A C6  1 
HETATM 2042 F  F11 . V50 C 3 .   ? -6.199  3.293   14.557  1.00 35.32 ? 302 V50 A F11 1 
HETATM 2043 C  C1  . V50 C 3 .   ? -4.201  4.301   13.915  1.00 32.68 ? 302 V50 A C1  1 
HETATM 2044 F  F10 . V50 C 3 .   ? -4.921  5.202   13.216  1.00 35.34 ? 302 V50 A F10 1 
HETATM 2045 C  C3  . V50 C 3 .   ? -2.154  3.370   14.661  1.00 32.21 ? 302 V50 A C3  1 
HETATM 2046 F  F12 . V50 C 3 .   ? -0.807  3.437   14.742  1.00 32.46 ? 302 V50 A F12 1 
HETATM 2047 C  C2  . V50 C 3 .   ? -2.799  4.376   13.932  1.00 36.18 ? 302 V50 A C2  1 
HETATM 2048 S  S14 . V50 C 3 .   ? -1.752  5.586   13.069  1.00 42.05 ? 302 V50 A S14 1 
HETATM 2049 C  C15 . V50 C 3 .   ? -2.401  7.196   13.443  1.00 56.18 ? 302 V50 A C15 1 
HETATM 2050 N  N20 . V50 C 3 .   ? -3.636  7.363   13.913  1.00 61.15 ? 302 V50 A N20 1 
HETATM 2051 C  C19 . V50 C 3 .   ? -4.003  8.647   14.136  1.00 66.68 ? 302 V50 A C19 1 
HETATM 2052 C  C21 . V50 C 3 .   ? -5.395  8.863   14.662  1.00 64.85 ? 302 V50 A C21 1 
HETATM 2053 C  C18 . V50 C 3 .   ? -3.224  9.752   13.931  1.00 73.15 ? 302 V50 A C18 1 
HETATM 2054 C  C17 . V50 C 3 .   ? -1.972  9.438   13.452  1.00 75.03 ? 302 V50 A C17 1 
HETATM 2055 N  N16 . V50 C 3 .   ? -1.553  8.188   13.199  1.00 67.13 ? 302 V50 A N16 1 
HETATM 2056 C  C22 . V50 C 3 .   ? -0.971  10.538  13.170  1.00 73.61 ? 302 V50 A C22 1 
HETATM 2057 O  O   . HOH D 4 .   ? -28.260 11.376  5.560   1.00 30.18 ? 401 HOH A O   1 
HETATM 2058 O  O   . HOH D 4 .   ? -9.770  -18.168 16.338  1.00 33.02 ? 402 HOH A O   1 
HETATM 2059 O  O   . HOH D 4 .   ? -24.831 9.854   13.237  1.00 31.52 ? 403 HOH A O   1 
HETATM 2060 O  O   . HOH D 4 .   ? -17.291 19.177  5.722   1.00 20.49 ? 404 HOH A O   1 
HETATM 2061 O  O   . HOH D 4 .   ? -0.462  -4.231  15.210  1.00 20.21 ? 405 HOH A O   1 
HETATM 2062 O  O   . HOH D 4 .   ? -13.633 -5.302  -6.883  1.00 36.11 ? 406 HOH A O   1 
HETATM 2063 O  O   . HOH D 4 .   ? -9.856  -5.831  38.079  1.00 51.05 ? 407 HOH A O   1 
HETATM 2064 O  O   . HOH D 4 .   ? -17.918 6.173   38.050  1.00 46.63 ? 408 HOH A O   1 
HETATM 2065 O  O   . HOH D 4 .   ? -13.893 -16.174 28.604  1.00 44.82 ? 409 HOH A O   1 
HETATM 2066 O  O   . HOH D 4 .   ? -5.913  -20.412 18.710  1.00 33.68 ? 410 HOH A O   1 
HETATM 2067 O  O   . HOH D 4 .   ? -0.711  -12.395 -3.891  1.00 41.92 ? 411 HOH A O   1 
HETATM 2068 O  O   . HOH D 4 .   ? -24.426 4.940   8.516   1.00 47.37 ? 412 HOH A O   1 
HETATM 2069 O  O   . HOH D 4 .   ? -19.497 10.968  26.419  1.00 29.73 ? 413 HOH A O   1 
HETATM 2070 O  O   . HOH D 4 .   ? -15.943 -10.404 -4.843  1.00 33.02 ? 414 HOH A O   1 
HETATM 2071 O  O   . HOH D 4 .   ? -18.694 -12.098 -3.392  1.00 32.93 ? 415 HOH A O   1 
HETATM 2072 O  O   . HOH D 4 .   ? 5.032   -2.468  28.436  1.00 36.20 ? 416 HOH A O   1 
HETATM 2073 O  O   . HOH D 4 .   ? -30.907 -10.966 15.888  1.00 30.30 ? 417 HOH A O   1 
HETATM 2074 O  O   . HOH D 4 .   ? 4.245   4.829   29.604  1.00 33.55 ? 418 HOH A O   1 
HETATM 2075 O  O   . HOH D 4 .   ? -16.277 -8.275  20.099  1.00 19.77 ? 419 HOH A O   1 
HETATM 2076 O  O   . HOH D 4 .   ? -13.191 10.604  27.368  1.00 31.32 ? 420 HOH A O   1 
HETATM 2077 O  O   . HOH D 4 .   ? -9.670  8.532   25.063  1.00 26.11 ? 421 HOH A O   1 
HETATM 2078 O  O   . HOH D 4 .   ? 15.982  -2.326  14.211  1.00 26.41 ? 422 HOH A O   1 
HETATM 2079 O  O   . HOH D 4 .   ? -6.446  -14.742 31.163  1.00 37.12 ? 423 HOH A O   1 
HETATM 2080 O  O   . HOH D 4 .   ? -7.360  -15.403 10.951  1.00 22.22 ? 424 HOH A O   1 
HETATM 2081 O  O   . HOH D 4 .   ? 5.835   7.123   20.104  1.00 27.83 ? 425 HOH A O   1 
HETATM 2082 O  O   . HOH D 4 .   ? 15.902  3.277   20.752  1.00 36.22 ? 426 HOH A O   1 
HETATM 2083 O  O   . HOH D 4 .   ? 3.417   -12.832 5.028   1.00 28.37 ? 427 HOH A O   1 
HETATM 2084 O  O   . HOH D 4 .   ? -17.350 20.447  7.786   1.00 21.48 ? 428 HOH A O   1 
HETATM 2085 O  O   . HOH D 4 .   ? -23.296 -0.767  26.143  1.00 33.61 ? 429 HOH A O   1 
HETATM 2086 O  O   . HOH D 4 .   ? -18.642 10.016  8.642   1.00 22.45 ? 430 HOH A O   1 
HETATM 2087 O  O   . HOH D 4 .   ? -15.267 15.947  23.282  1.00 36.63 ? 431 HOH A O   1 
HETATM 2088 O  O   . HOH D 4 .   ? -17.449 10.469  11.072  1.00 25.38 ? 432 HOH A O   1 
HETATM 2089 O  O   . HOH D 4 .   ? -3.379  -12.892 -3.308  1.00 30.81 ? 433 HOH A O   1 
HETATM 2090 O  O   . HOH D 4 .   ? 1.143   -1.235  -5.247  1.00 30.90 ? 434 HOH A O   1 
HETATM 2091 O  O   . HOH D 4 .   ? -15.113 -10.155 36.867  1.00 41.27 ? 435 HOH A O   1 
HETATM 2092 O  O   . HOH D 4 .   ? -12.584 -8.926  -3.484  1.00 29.21 ? 436 HOH A O   1 
HETATM 2093 O  O   . HOH D 4 .   ? -13.165 -16.139 -0.457  1.00 35.91 ? 437 HOH A O   1 
HETATM 2094 O  O   . HOH D 4 .   ? -25.183 -5.771  12.713  1.00 37.53 ? 438 HOH A O   1 
HETATM 2095 O  O   . HOH D 4 .   ? -23.364 8.928   19.921  1.00 34.49 ? 439 HOH A O   1 
HETATM 2096 O  O   . HOH D 4 .   ? 4.428   -3.400  4.232   1.00 43.12 ? 440 HOH A O   1 
HETATM 2097 O  O   . HOH D 4 .   ? -22.668 -2.774  6.356   1.00 24.42 ? 441 HOH A O   1 
HETATM 2098 O  O   . HOH D 4 .   ? 0.665   1.131   34.194  1.00 37.45 ? 442 HOH A O   1 
HETATM 2099 O  O   . HOH D 4 .   ? 9.246   -3.820  20.751  1.00 25.76 ? 443 HOH A O   1 
HETATM 2100 O  O   . HOH D 4 .   ? -3.716  5.503   -3.302  1.00 34.53 ? 444 HOH A O   1 
HETATM 2101 O  O   . HOH D 4 .   ? -1.767  -3.442  11.178  1.00 28.53 ? 445 HOH A O   1 
HETATM 2102 O  O   . HOH D 4 .   ? -12.311 -16.706 26.333  1.00 32.05 ? 446 HOH A O   1 
HETATM 2103 O  O   . HOH D 4 .   ? -20.901 -6.992  23.211  1.00 22.25 ? 447 HOH A O   1 
HETATM 2104 O  O   . HOH D 4 .   ? -21.300 5.648   4.549   1.00 22.14 ? 448 HOH A O   1 
HETATM 2105 O  O   . HOH D 4 .   ? -1.872  -8.806  28.744  1.00 21.72 ? 449 HOH A O   1 
HETATM 2106 O  O   . HOH D 4 .   ? -21.248 -18.527 13.421  1.00 38.92 ? 450 HOH A O   1 
HETATM 2107 O  O   . HOH D 4 .   ? -2.836  -11.158 20.462  1.00 23.89 ? 451 HOH A O   1 
HETATM 2108 O  O   . HOH D 4 .   ? 2.680   -15.549 9.059   1.00 29.40 ? 452 HOH A O   1 
HETATM 2109 O  O   . HOH D 4 .   ? 5.540   -4.862  20.670  1.00 22.68 ? 453 HOH A O   1 
HETATM 2110 O  O   . HOH D 4 .   ? -5.436  -4.893  -6.775  1.00 30.42 ? 454 HOH A O   1 
HETATM 2111 O  O   . HOH D 4 .   ? -20.557 7.836   1.671   1.00 25.19 ? 455 HOH A O   1 
HETATM 2112 O  O   . HOH D 4 .   ? -24.308 12.002  6.214   1.00 26.48 ? 456 HOH A O   1 
HETATM 2113 O  O   . HOH D 4 .   ? -3.182  -15.882 23.974  1.00 25.63 ? 457 HOH A O   1 
HETATM 2114 O  O   . HOH D 4 .   ? 13.908  0.499   24.158  1.00 29.52 ? 458 HOH A O   1 
HETATM 2115 O  O   . HOH D 4 .   ? -3.924  -13.550 17.601  1.00 19.95 ? 459 HOH A O   1 
HETATM 2116 O  O   . HOH D 4 .   ? -2.761  -13.232 24.937  1.00 25.39 ? 460 HOH A O   1 
HETATM 2117 O  O   . HOH D 4 .   ? 5.226   -6.915  7.688   1.00 34.45 ? 461 HOH A O   1 
HETATM 2118 O  O   . HOH D 4 .   ? -18.314 -4.021  -2.875  1.00 31.95 ? 462 HOH A O   1 
HETATM 2119 O  O   . HOH D 4 .   ? -25.405 -14.954 8.089   1.00 38.32 ? 463 HOH A O   1 
HETATM 2120 O  O   . HOH D 4 .   ? -18.095 4.158   -3.857  1.00 35.75 ? 464 HOH A O   1 
HETATM 2121 O  O   . HOH D 4 .   ? -24.397 -7.557  8.866   1.00 25.60 ? 465 HOH A O   1 
HETATM 2122 O  O   . HOH D 4 .   ? -6.445  -8.586  -7.670  1.00 41.29 ? 466 HOH A O   1 
HETATM 2123 O  O   . HOH D 4 .   ? -12.758 -0.834  -6.157  1.00 32.39 ? 467 HOH A O   1 
HETATM 2124 O  O   . HOH D 4 .   ? -8.976  -8.205  33.551  1.00 39.82 ? 468 HOH A O   1 
HETATM 2125 O  O   . HOH D 4 .   ? -1.377  -5.216  -7.305  1.00 37.84 ? 469 HOH A O   1 
HETATM 2126 O  O   . HOH D 4 .   ? 0.059   -8.563  32.274  1.00 38.07 ? 470 HOH A O   1 
HETATM 2127 O  O   . HOH D 4 .   ? -22.288 -5.703  2.517   1.00 27.12 ? 471 HOH A O   1 
HETATM 2128 O  O   . HOH D 4 .   ? 11.966  1.462   25.574  1.00 35.71 ? 472 HOH A O   1 
HETATM 2129 O  O   . HOH D 4 .   ? -10.871 10.028  7.821   1.00 30.56 ? 473 HOH A O   1 
HETATM 2130 O  O   . HOH D 4 .   ? -7.551  -19.267 21.048  1.00 33.59 ? 474 HOH A O   1 
HETATM 2131 O  O   . HOH D 4 .   ? -15.879 -9.786  32.560  1.00 28.35 ? 475 HOH A O   1 
HETATM 2132 O  O   . HOH D 4 .   ? -19.131 -20.738 4.760   1.00 29.17 ? 476 HOH A O   1 
HETATM 2133 O  O   . HOH D 4 .   ? 2.205   8.605   23.906  1.00 30.05 ? 477 HOH A O   1 
HETATM 2134 O  O   . HOH D 4 .   ? -15.307 8.951   -2.467  1.00 33.17 ? 478 HOH A O   1 
HETATM 2135 O  O   . HOH D 4 .   ? 1.947   -1.689  28.975  1.00 25.90 ? 479 HOH A O   1 
HETATM 2136 O  O   . HOH D 4 .   ? -12.768 -18.430 14.425  1.00 28.61 ? 480 HOH A O   1 
HETATM 2137 O  O   . HOH D 4 .   ? -26.008 -3.869  24.958  1.00 32.30 ? 481 HOH A O   1 
HETATM 2138 O  O   . HOH D 4 .   ? -16.286 -7.048  39.423  1.00 36.34 ? 482 HOH A O   1 
HETATM 2139 O  O   . HOH D 4 .   ? -15.372 -12.190 24.125  1.00 31.64 ? 483 HOH A O   1 
HETATM 2140 O  O   . HOH D 4 .   ? -6.818  -8.701  32.223  1.00 30.64 ? 484 HOH A O   1 
HETATM 2141 O  O   . HOH D 4 .   ? -22.845 -13.244 11.218  1.00 32.97 ? 485 HOH A O   1 
HETATM 2142 O  O   . HOH D 4 .   ? -8.629  14.622  11.467  1.00 32.11 ? 486 HOH A O   1 
HETATM 2143 O  O   . HOH D 4 .   ? -11.249 2.965   30.302  1.00 31.74 ? 487 HOH A O   1 
HETATM 2144 O  O   . HOH D 4 .   ? -23.205 -0.937  3.739   1.00 26.58 ? 488 HOH A O   1 
HETATM 2145 O  O   . HOH D 4 .   ? -8.795  -10.017 -1.730  1.00 36.29 ? 489 HOH A O   1 
HETATM 2146 O  O   . HOH D 4 .   ? -24.469 -9.266  1.983   1.00 30.67 ? 490 HOH A O   1 
HETATM 2147 O  O   . HOH D 4 .   ? 3.256   -11.464 9.482   1.00 34.49 ? 491 HOH A O   1 
HETATM 2148 O  O   . HOH D 4 .   ? -27.095 2.667   22.912  1.00 35.59 ? 492 HOH A O   1 
HETATM 2149 O  O   . HOH D 4 .   ? -8.391  -6.010  35.546  1.00 35.57 ? 493 HOH A O   1 
HETATM 2150 O  O   . HOH D 4 .   ? -22.366 -11.538 13.865  1.00 32.86 ? 494 HOH A O   1 
HETATM 2151 O  O   . HOH D 4 .   ? -13.018 19.821  14.292  1.00 43.48 ? 495 HOH A O   1 
HETATM 2152 O  O   . HOH D 4 .   ? -5.113  2.738   -6.593  1.00 31.85 ? 496 HOH A O   1 
HETATM 2153 O  O   . HOH D 4 .   ? -1.426  -12.426 22.462  1.00 23.54 ? 497 HOH A O   1 
HETATM 2154 O  O   . HOH D 4 .   ? 14.456  5.990   19.090  1.00 40.78 ? 498 HOH A O   1 
HETATM 2155 O  O   . HOH D 4 .   ? -23.498 -2.193  28.601  1.00 40.19 ? 499 HOH A O   1 
HETATM 2156 O  O   . HOH D 4 .   ? -16.318 -14.078 36.726  1.00 39.52 ? 500 HOH A O   1 
HETATM 2157 O  O   . HOH D 4 .   ? 5.393   -10.309 7.976   1.00 46.54 ? 501 HOH A O   1 
HETATM 2158 O  O   . HOH D 4 .   ? 8.123   6.271   21.465  1.00 25.23 ? 502 HOH A O   1 
HETATM 2159 O  O   . HOH D 4 .   ? 10.884  -2.471  13.183  1.00 34.89 ? 503 HOH A O   1 
HETATM 2160 O  O   . HOH D 4 .   ? 13.513  -3.494  12.966  1.00 34.36 ? 504 HOH A O   1 
HETATM 2161 O  O   . HOH D 4 .   ? 1.837   -9.915  28.180  1.00 43.16 ? 505 HOH A O   1 
HETATM 2162 O  O   . HOH D 4 .   ? 0.467   -14.294 22.005  1.00 32.76 ? 506 HOH A O   1 
HETATM 2163 O  O   . HOH D 4 .   ? 2.174   -11.751 14.493  1.00 34.42 ? 507 HOH A O   1 
HETATM 2164 O  O   . HOH D 4 .   ? -6.659  -9.033  -2.785  1.00 35.16 ? 508 HOH A O   1 
HETATM 2165 O  O   . HOH D 4 .   ? -24.394 11.431  19.733  1.00 38.58 ? 509 HOH A O   1 
HETATM 2166 O  O   . HOH D 4 .   ? -1.305  -17.466 24.786  1.00 47.60 ? 510 HOH A O   1 
HETATM 2167 O  O   . HOH D 4 .   ? -3.077  4.100   9.772   1.00 36.63 ? 511 HOH A O   1 
HETATM 2168 O  O   . HOH D 4 .   ? 3.569   4.786   2.298   1.00 31.97 ? 512 HOH A O   1 
HETATM 2169 O  O   . HOH D 4 .   ? -11.026 -11.277 -3.692  1.00 39.21 ? 513 HOH A O   1 
HETATM 2170 O  O   . HOH D 4 .   ? -0.701  3.560   10.277  1.00 42.42 ? 514 HOH A O   1 
HETATM 2171 O  O   . HOH D 4 .   ? -1.095  -13.195 26.869  1.00 34.27 ? 515 HOH A O   1 
HETATM 2172 O  O   . HOH D 4 .   ? 2.931   -14.294 20.249  1.00 44.02 ? 516 HOH A O   1 
# 
