data_1H4W
# 
_entry.id   1H4W 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   1H4W         pdb_00001h4w 10.2210/pdb1h4w/pdb 
PDBE  EBI-8047     ?            ?                   
WWPDB D_1290008047 ?            ?                   
# 
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 2002-02-11 
2 'Structure model' 1 1 2011-05-08 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2019-02-27 
5 'Structure model' 1 4 2023-12-13 
6 'Structure model' 1 5 2024-11-13 
# 
_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' 'Version format compliance' 
2  3 'Structure model' 'Version format compliance' 
3  4 'Structure model' Advisory                    
4  4 'Structure model' 'Data collection'           
5  4 'Structure model' 'Database references'       
6  4 'Structure model' 'Experimental preparation'  
7  4 'Structure model' Other                       
8  5 'Structure model' Advisory                    
9  5 'Structure model' 'Data collection'           
10 5 'Structure model' 'Database references'       
11 5 'Structure model' 'Derived calculations'      
12 5 'Structure model' Other                       
13 5 'Structure model' 'Refinement description'    
14 6 'Structure model' 'Structure summary'         
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  4 'Structure model' citation                      
2  4 'Structure model' exptl_crystal_grow            
3  4 'Structure model' pdbx_database_proc            
4  4 'Structure model' pdbx_database_status          
5  4 'Structure model' pdbx_unobs_or_zero_occ_atoms  
6  4 'Structure model' struct_biol                   
7  5 'Structure model' chem_comp_atom                
8  5 'Structure model' chem_comp_bond                
9  5 'Structure model' database_2                    
10 5 'Structure model' pdbx_database_status          
11 5 'Structure model' pdbx_initial_refinement_model 
12 5 'Structure model' pdbx_struct_conn_angle        
13 5 'Structure model' pdbx_unobs_or_zero_occ_atoms  
14 5 'Structure model' struct_conn                   
15 5 'Structure model' struct_site                   
16 6 'Structure model' pdbx_entry_details            
17 6 'Structure model' pdbx_modification_feature     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_citation.journal_abbrev'                     
2  4 'Structure model' '_citation.page_last'                          
3  4 'Structure model' '_citation.pdbx_database_id_DOI'               
4  4 'Structure model' '_citation.title'                              
5  4 'Structure model' '_exptl_crystal_grow.method'                   
6  4 'Structure model' '_exptl_crystal_grow.temp'                     
7  4 'Structure model' '_pdbx_database_status.recvd_author_approval'  
8  5 'Structure model' '_database_2.pdbx_DOI'                         
9  5 'Structure model' '_database_2.pdbx_database_accession'          
10 5 'Structure model' '_pdbx_database_status.status_code_sf'         
11 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'   
12 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'    
13 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id'  
14 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id'  
15 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id'  
16 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'   
17 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'   
18 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'    
19 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id'  
20 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id'  
21 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id'  
22 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'   
23 5 'Structure model' '_pdbx_struct_conn_angle.value'                
24 5 'Structure model' '_struct_conn.pdbx_dist_value'                 
25 5 'Structure model' '_struct_conn.ptnr1_auth_comp_id'              
26 5 'Structure model' '_struct_conn.ptnr1_auth_seq_id'               
27 5 'Structure model' '_struct_conn.ptnr1_label_asym_id'             
28 5 'Structure model' '_struct_conn.ptnr1_label_atom_id'             
29 5 'Structure model' '_struct_conn.ptnr1_label_comp_id'             
30 5 'Structure model' '_struct_conn.ptnr1_label_seq_id'              
31 5 'Structure model' '_struct_conn.ptnr2_auth_comp_id'              
32 5 'Structure model' '_struct_conn.ptnr2_auth_seq_id'               
33 5 'Structure model' '_struct_conn.ptnr2_label_asym_id'             
34 5 'Structure model' '_struct_conn.ptnr2_label_atom_id'             
35 5 'Structure model' '_struct_conn.ptnr2_label_comp_id'             
36 5 'Structure model' '_struct_conn.ptnr2_label_seq_id'              
37 5 'Structure model' '_struct_site.pdbx_auth_asym_id'               
38 5 'Structure model' '_struct_site.pdbx_auth_comp_id'               
39 5 'Structure model' '_struct_site.pdbx_auth_seq_id'                
40 6 'Structure model' '_pdbx_entry_details.has_protein_modification' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1H4W 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2001-05-15 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Katona, G.'     1 ? 
'Berglund, G.I.' 2 ? 
'Hajdu, J.'      3 ? 
'Graf, L.'       4 ? 
'Szilagyi, L.'   5 ? 
# 
_citation.id                        primary 
_citation.title                     'Crystal structure reveals basis for the inhibitor resistance of human brain trypsin.' 
_citation.journal_abbrev            'J. Mol. Biol.' 
_citation.journal_volume            315 
_citation.page_first                1209 
_citation.page_last                 1218 
_citation.year                      2002 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   11827488 
_citation.pdbx_database_id_DOI      10.1006/jmbi.2001.5305 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Katona, G.'     1 ? 
primary 'Berglund, G.I.' 2 ? 
primary 'Hajdu, J.'      3 ? 
primary 'Graf, L.'       4 ? 
primary 'Szilagyi, L.'   5 ? 
# 
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 'TRYPSIN IVA' 24301.510 1   3.4.21.4 ? ? BENZAMIDINE 
2 non-polymer syn BENZAMIDINE   120.152   1   ?        ? ? ?           
3 non-polymer syn 'CALCIUM ION' 40.078    1   ?        ? ? ?           
4 water       nat water         18.015    125 ?        ? ? ?           
# 
_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       
;IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAHCYKTRIQVRLGEHNIKVLEGNEQFINAVKIIRHPKYNRDT
LDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSM
FCVGFLEGGKDSCQRDSGGPVVCNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAHCYKTRIQVRLGEHNIKVLEGNEQFINAVKIIRHPKYNRDT
LDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSM
FCVGFLEGGKDSCQRDSGGPVVCNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS
;
_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 BENZAMIDINE   BEN 
3 'CALCIUM ION' CA  
4 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ILE n 
1 2   VAL n 
1 3   GLY n 
1 4   GLY n 
1 5   TYR n 
1 6   THR n 
1 7   CYS n 
1 8   GLU n 
1 9   GLU n 
1 10  ASN n 
1 11  SER n 
1 12  LEU n 
1 13  PRO n 
1 14  TYR n 
1 15  GLN n 
1 16  VAL n 
1 17  SER n 
1 18  LEU n 
1 19  ASN n 
1 20  SER n 
1 21  GLY n 
1 22  SER n 
1 23  HIS n 
1 24  PHE n 
1 25  CYS n 
1 26  GLY n 
1 27  GLY n 
1 28  SER n 
1 29  LEU n 
1 30  ILE n 
1 31  SER n 
1 32  GLU n 
1 33  GLN n 
1 34  TRP n 
1 35  VAL n 
1 36  VAL n 
1 37  SER n 
1 38  ALA n 
1 39  ALA n 
1 40  HIS n 
1 41  CYS n 
1 42  TYR n 
1 43  LYS n 
1 44  THR n 
1 45  ARG n 
1 46  ILE n 
1 47  GLN n 
1 48  VAL n 
1 49  ARG n 
1 50  LEU n 
1 51  GLY n 
1 52  GLU n 
1 53  HIS n 
1 54  ASN n 
1 55  ILE n 
1 56  LYS n 
1 57  VAL n 
1 58  LEU n 
1 59  GLU n 
1 60  GLY n 
1 61  ASN n 
1 62  GLU n 
1 63  GLN n 
1 64  PHE n 
1 65  ILE n 
1 66  ASN n 
1 67  ALA n 
1 68  VAL n 
1 69  LYS n 
1 70  ILE n 
1 71  ILE n 
1 72  ARG n 
1 73  HIS n 
1 74  PRO n 
1 75  LYS n 
1 76  TYR n 
1 77  ASN n 
1 78  ARG n 
1 79  ASP n 
1 80  THR n 
1 81  LEU n 
1 82  ASP n 
1 83  ASN n 
1 84  ASP n 
1 85  ILE n 
1 86  MET n 
1 87  LEU n 
1 88  ILE n 
1 89  LYS n 
1 90  LEU n 
1 91  SER n 
1 92  SER n 
1 93  PRO n 
1 94  ALA n 
1 95  VAL n 
1 96  ILE n 
1 97  ASN n 
1 98  ALA n 
1 99  ARG n 
1 100 VAL n 
1 101 SER n 
1 102 THR n 
1 103 ILE n 
1 104 SER n 
1 105 LEU n 
1 106 PRO n 
1 107 THR n 
1 108 ALA n 
1 109 PRO n 
1 110 PRO n 
1 111 ALA n 
1 112 ALA n 
1 113 GLY n 
1 114 THR n 
1 115 GLU n 
1 116 CYS n 
1 117 LEU n 
1 118 ILE n 
1 119 SER n 
1 120 GLY n 
1 121 TRP n 
1 122 GLY n 
1 123 ASN n 
1 124 THR n 
1 125 LEU n 
1 126 SER n 
1 127 PHE n 
1 128 GLY n 
1 129 ALA n 
1 130 ASP n 
1 131 TYR n 
1 132 PRO n 
1 133 ASP n 
1 134 GLU n 
1 135 LEU n 
1 136 LYS n 
1 137 CYS n 
1 138 LEU n 
1 139 ASP n 
1 140 ALA n 
1 141 PRO n 
1 142 VAL n 
1 143 LEU n 
1 144 THR n 
1 145 GLN n 
1 146 ALA n 
1 147 GLU n 
1 148 CYS n 
1 149 LYS n 
1 150 ALA n 
1 151 SER n 
1 152 TYR n 
1 153 PRO n 
1 154 GLY n 
1 155 LYS n 
1 156 ILE n 
1 157 THR n 
1 158 ASN n 
1 159 SER n 
1 160 MET n 
1 161 PHE n 
1 162 CYS n 
1 163 VAL n 
1 164 GLY n 
1 165 PHE n 
1 166 LEU n 
1 167 GLU n 
1 168 GLY n 
1 169 GLY n 
1 170 LYS n 
1 171 ASP n 
1 172 SER n 
1 173 CYS n 
1 174 GLN n 
1 175 ARG n 
1 176 ASP n 
1 177 SER n 
1 178 GLY n 
1 179 GLY n 
1 180 PRO n 
1 181 VAL n 
1 182 VAL n 
1 183 CYS n 
1 184 ASN n 
1 185 GLY n 
1 186 GLN n 
1 187 LEU n 
1 188 GLN n 
1 189 GLY n 
1 190 VAL n 
1 191 VAL n 
1 192 SER n 
1 193 TRP n 
1 194 GLY n 
1 195 HIS n 
1 196 GLY n 
1 197 CYS n 
1 198 ALA n 
1 199 TRP n 
1 200 LYS n 
1 201 ASN n 
1 202 ARG n 
1 203 PRO n 
1 204 GLY n 
1 205 VAL n 
1 206 TYR n 
1 207 THR n 
1 208 LYS n 
1 209 VAL n 
1 210 TYR n 
1 211 ASN n 
1 212 TYR n 
1 213 VAL n 
1 214 ASP n 
1 215 TRP n 
1 216 ILE n 
1 217 LYS n 
1 218 ASP n 
1 219 THR n 
1 220 ILE n 
1 221 ALA n 
1 222 ALA n 
1 223 ASN n 
1 224 SER 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               HUMAN 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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              'A FORM' 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                BRAIN 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'ESCHERICHIA COLI' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     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               'BL21(DE3)' 
_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                       PET17B 
_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 
BEN non-polymer         . BENZAMIDINE     ? 'C7 H8 N2'       120.152 
CA  non-polymer         . 'CALCIUM ION'   ? 'Ca 2'           40.078  
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 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
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   ILE 1   16  16  ILE ILE A . n 
A 1 2   VAL 2   17  17  VAL VAL A . n 
A 1 3   GLY 3   18  18  GLY GLY A . n 
A 1 4   GLY 4   19  19  GLY GLY A . n 
A 1 5   TYR 5   20  20  TYR TYR A . n 
A 1 6   THR 6   21  21  THR THR A . n 
A 1 7   CYS 7   22  22  CYS CYS A . n 
A 1 8   GLU 8   23  23  GLU GLU A . n 
A 1 9   GLU 9   24  24  GLU GLU A . n 
A 1 10  ASN 10  25  25  ASN ASN A . n 
A 1 11  SER 11  26  26  SER SER A . n 
A 1 12  LEU 12  27  27  LEU LEU A . n 
A 1 13  PRO 13  28  28  PRO PRO A . n 
A 1 14  TYR 14  29  29  TYR TYR A . n 
A 1 15  GLN 15  30  30  GLN GLN A . n 
A 1 16  VAL 16  31  31  VAL VAL A . n 
A 1 17  SER 17  32  32  SER SER A . n 
A 1 18  LEU 18  33  33  LEU LEU A . n 
A 1 19  ASN 19  34  34  ASN ASN A . n 
A 1 20  SER 20  37  37  SER SER A . n 
A 1 21  GLY 21  38  38  GLY GLY A . n 
A 1 22  SER 22  39  39  SER SER A . n 
A 1 23  HIS 23  40  40  HIS HIS A . n 
A 1 24  PHE 24  41  41  PHE PHE A . n 
A 1 25  CYS 25  42  42  CYS CYS A . n 
A 1 26  GLY 26  43  43  GLY GLY A . n 
A 1 27  GLY 27  44  44  GLY GLY A . n 
A 1 28  SER 28  45  45  SER SER A . n 
A 1 29  LEU 29  46  46  LEU LEU A . n 
A 1 30  ILE 30  47  47  ILE ILE A . n 
A 1 31  SER 31  48  48  SER SER A . n 
A 1 32  GLU 32  49  49  GLU GLU A . n 
A 1 33  GLN 33  50  50  GLN GLN A . n 
A 1 34  TRP 34  51  51  TRP TRP A . n 
A 1 35  VAL 35  52  52  VAL VAL A . n 
A 1 36  VAL 36  53  53  VAL VAL A . n 
A 1 37  SER 37  54  54  SER SER A . n 
A 1 38  ALA 38  55  55  ALA ALA A . n 
A 1 39  ALA 39  56  56  ALA ALA A . n 
A 1 40  HIS 40  57  57  HIS HIS A . n 
A 1 41  CYS 41  58  58  CYS CYS A . n 
A 1 42  TYR 42  59  59  TYR TYR A . n 
A 1 43  LYS 43  60  60  LYS LYS A . n 
A 1 44  THR 44  61  61  THR THR A . n 
A 1 45  ARG 45  62  62  ARG ARG A . n 
A 1 46  ILE 46  63  63  ILE ILE A . n 
A 1 47  GLN 47  64  64  GLN GLN A . n 
A 1 48  VAL 48  65  65  VAL VAL A . n 
A 1 49  ARG 49  66  66  ARG ARG A . n 
A 1 50  LEU 50  67  67  LEU LEU A . n 
A 1 51  GLY 51  69  69  GLY GLY A . n 
A 1 52  GLU 52  70  70  GLU GLU A . n 
A 1 53  HIS 53  71  71  HIS HIS A . n 
A 1 54  ASN 54  72  72  ASN ASN A . n 
A 1 55  ILE 55  73  73  ILE ILE A . n 
A 1 56  LYS 56  74  74  LYS LYS A . n 
A 1 57  VAL 57  75  75  VAL VAL A . n 
A 1 58  LEU 58  76  76  LEU LEU A . n 
A 1 59  GLU 59  77  77  GLU GLU A . n 
A 1 60  GLY 60  78  78  GLY GLY A . n 
A 1 61  ASN 61  79  79  ASN ASN A . n 
A 1 62  GLU 62  80  80  GLU GLU A . n 
A 1 63  GLN 63  81  81  GLN GLN A . n 
A 1 64  PHE 64  82  82  PHE PHE A . n 
A 1 65  ILE 65  83  83  ILE ILE A . n 
A 1 66  ASN 66  84  84  ASN ASN A . n 
A 1 67  ALA 67  85  85  ALA ALA A . n 
A 1 68  VAL 68  86  86  VAL VAL A . n 
A 1 69  LYS 69  87  87  LYS LYS A . n 
A 1 70  ILE 70  88  88  ILE ILE A . n 
A 1 71  ILE 71  89  89  ILE ILE A . n 
A 1 72  ARG 72  90  90  ARG ARG A . n 
A 1 73  HIS 73  91  91  HIS HIS A . n 
A 1 74  PRO 74  92  92  PRO PRO A . n 
A 1 75  LYS 75  93  93  LYS LYS A . n 
A 1 76  TYR 76  94  94  TYR TYR A . n 
A 1 77  ASN 77  95  95  ASN ASN A . n 
A 1 78  ARG 78  96  96  ARG ARG A . n 
A 1 79  ASP 79  97  97  ASP ASP A . n 
A 1 80  THR 80  98  98  THR THR A . n 
A 1 81  LEU 81  99  99  LEU LEU A . n 
A 1 82  ASP 82  100 100 ASP ASP A . n 
A 1 83  ASN 83  101 101 ASN ASN A . n 
A 1 84  ASP 84  102 102 ASP ASP A . n 
A 1 85  ILE 85  103 103 ILE ILE A . n 
A 1 86  MET 86  104 104 MET MET A . n 
A 1 87  LEU 87  105 105 LEU LEU A . n 
A 1 88  ILE 88  106 106 ILE ILE A . n 
A 1 89  LYS 89  107 107 LYS LYS A . n 
A 1 90  LEU 90  108 108 LEU LEU A . n 
A 1 91  SER 91  109 109 SER SER A . n 
A 1 92  SER 92  110 110 SER SER A . n 
A 1 93  PRO 93  111 111 PRO PRO A . n 
A 1 94  ALA 94  112 112 ALA ALA A . n 
A 1 95  VAL 95  113 113 VAL VAL A . n 
A 1 96  ILE 96  114 114 ILE ILE A . n 
A 1 97  ASN 97  115 115 ASN ASN A . n 
A 1 98  ALA 98  116 116 ALA ALA A . n 
A 1 99  ARG 99  117 117 ARG ARG A . n 
A 1 100 VAL 100 118 118 VAL VAL A . n 
A 1 101 SER 101 119 119 SER SER A . n 
A 1 102 THR 102 120 120 THR THR A . n 
A 1 103 ILE 103 121 121 ILE ILE A . n 
A 1 104 SER 104 122 122 SER SER A . n 
A 1 105 LEU 105 123 123 LEU LEU A . n 
A 1 106 PRO 106 124 124 PRO PRO A . n 
A 1 107 THR 107 125 125 THR THR A . n 
A 1 108 ALA 108 127 127 ALA ALA A . n 
A 1 109 PRO 109 128 128 PRO PRO A . n 
A 1 110 PRO 110 129 129 PRO PRO A . n 
A 1 111 ALA 111 130 130 ALA ALA A . n 
A 1 112 ALA 112 132 132 ALA ALA A . n 
A 1 113 GLY 113 133 133 GLY GLY A . n 
A 1 114 THR 114 134 134 THR THR A . n 
A 1 115 GLU 115 135 135 GLU GLU A . n 
A 1 116 CYS 116 136 136 CYS CYS A . n 
A 1 117 LEU 117 137 137 LEU LEU A . n 
A 1 118 ILE 118 138 138 ILE ILE A . n 
A 1 119 SER 119 139 139 SER SER A . n 
A 1 120 GLY 120 140 140 GLY GLY A . n 
A 1 121 TRP 121 141 141 TRP TRP A . n 
A 1 122 GLY 122 142 142 GLY GLY A . n 
A 1 123 ASN 123 143 143 ASN ASN A . n 
A 1 124 THR 124 144 144 THR THR A . n 
A 1 125 LEU 125 145 145 LEU LEU A . n 
A 1 126 SER 126 146 146 SER SER A . n 
A 1 127 PHE 127 147 147 PHE PHE A . n 
A 1 128 GLY 128 148 148 GLY GLY A . n 
A 1 129 ALA 129 149 149 ALA ALA A . n 
A 1 130 ASP 130 150 150 ASP ASP A . n 
A 1 131 TYR 131 151 151 TYR TYR A . n 
A 1 132 PRO 132 152 152 PRO PRO A . n 
A 1 133 ASP 133 153 153 ASP ASP A . n 
A 1 134 GLU 134 154 154 GLU GLU A . n 
A 1 135 LEU 135 155 155 LEU LEU A . n 
A 1 136 LYS 136 156 156 LYS LYS A . n 
A 1 137 CYS 137 157 157 CYS CYS A . n 
A 1 138 LEU 138 158 158 LEU LEU A . n 
A 1 139 ASP 139 159 159 ASP ASP A . n 
A 1 140 ALA 140 160 160 ALA ALA A . n 
A 1 141 PRO 141 161 161 PRO PRO A . n 
A 1 142 VAL 142 162 162 VAL VAL A . n 
A 1 143 LEU 143 163 163 LEU LEU A . n 
A 1 144 THR 144 164 164 THR THR A . n 
A 1 145 GLN 145 165 165 GLN GLN A . n 
A 1 146 ALA 146 166 166 ALA ALA A . n 
A 1 147 GLU 147 167 167 GLU GLU A . n 
A 1 148 CYS 148 168 168 CYS CYS A . n 
A 1 149 LYS 149 169 169 LYS LYS A . n 
A 1 150 ALA 150 170 170 ALA ALA A . n 
A 1 151 SER 151 171 171 SER SER A . n 
A 1 152 TYR 152 172 172 TYR TYR A . n 
A 1 153 PRO 153 173 173 PRO PRO A . n 
A 1 154 GLY 154 174 174 GLY GLY A . n 
A 1 155 LYS 155 175 175 LYS LYS A . n 
A 1 156 ILE 156 176 176 ILE ILE A . n 
A 1 157 THR 157 177 177 THR THR A . n 
A 1 158 ASN 158 178 178 ASN ASN A . n 
A 1 159 SER 159 179 179 SER SER A . n 
A 1 160 MET 160 180 180 MET MET A . n 
A 1 161 PHE 161 181 181 PHE PHE A . n 
A 1 162 CYS 162 182 182 CYS CYS A . n 
A 1 163 VAL 163 183 183 VAL VAL A . n 
A 1 164 GLY 164 184 184 GLY GLY A . n 
A 1 165 PHE 165 184 184 PHE PHE A A n 
A 1 166 LEU 166 185 185 LEU LEU A . n 
A 1 167 GLU 167 186 186 GLU GLU A . n 
A 1 168 GLY 168 187 187 GLY GLY A . n 
A 1 169 GLY 169 188 188 GLY GLY A . n 
A 1 170 LYS 170 188 188 LYS LYS A A n 
A 1 171 ASP 171 189 189 ASP ASP A . n 
A 1 172 SER 172 190 190 SER SER A . n 
A 1 173 CYS 173 191 191 CYS CYS A . n 
A 1 174 GLN 174 192 192 GLN GLN A . n 
A 1 175 ARG 175 193 193 ARG ARG A . n 
A 1 176 ASP 176 194 194 ASP ASP A . n 
A 1 177 SER 177 195 195 SER SER A . n 
A 1 178 GLY 178 196 196 GLY GLY A . n 
A 1 179 GLY 179 197 197 GLY GLY A . n 
A 1 180 PRO 180 198 198 PRO PRO A . n 
A 1 181 VAL 181 199 199 VAL VAL A . n 
A 1 182 VAL 182 200 200 VAL VAL A . n 
A 1 183 CYS 183 201 201 CYS CYS A . n 
A 1 184 ASN 184 202 202 ASN ASN A . n 
A 1 185 GLY 185 203 203 GLY GLY A . n 
A 1 186 GLN 186 204 204 GLN GLN A . n 
A 1 187 LEU 187 209 209 LEU LEU A . n 
A 1 188 GLN 188 210 210 GLN GLN A . n 
A 1 189 GLY 189 211 211 GLY GLY A . n 
A 1 190 VAL 190 212 212 VAL VAL A . n 
A 1 191 VAL 191 213 213 VAL VAL A . n 
A 1 192 SER 192 214 214 SER SER A . n 
A 1 193 TRP 193 215 215 TRP TRP A . n 
A 1 194 GLY 194 216 216 GLY GLY A . n 
A 1 195 HIS 195 217 217 HIS HIS A . n 
A 1 196 GLY 196 219 219 GLY GLY A . n 
A 1 197 CYS 197 220 220 CYS CYS A . n 
A 1 198 ALA 198 221 221 ALA ALA A . n 
A 1 199 TRP 199 221 221 TRP TRP A A n 
A 1 200 LYS 200 222 222 LYS LYS A . n 
A 1 201 ASN 201 223 223 ASN ASN A . n 
A 1 202 ARG 202 224 224 ARG ARG A . n 
A 1 203 PRO 203 225 225 PRO PRO A . n 
A 1 204 GLY 204 226 226 GLY GLY A . n 
A 1 205 VAL 205 227 227 VAL VAL A . n 
A 1 206 TYR 206 228 228 TYR TYR A . n 
A 1 207 THR 207 229 229 THR THR A . n 
A 1 208 LYS 208 230 230 LYS LYS A . n 
A 1 209 VAL 209 231 231 VAL VAL A . n 
A 1 210 TYR 210 232 232 TYR TYR A . n 
A 1 211 ASN 211 233 233 ASN ASN A . n 
A 1 212 TYR 212 234 234 TYR TYR A . n 
A 1 213 VAL 213 235 235 VAL VAL A . n 
A 1 214 ASP 214 236 236 ASP ASP A . n 
A 1 215 TRP 215 237 237 TRP TRP A . n 
A 1 216 ILE 216 238 238 ILE ILE A . n 
A 1 217 LYS 217 239 239 LYS LYS A . n 
A 1 218 ASP 218 240 240 ASP ASP A . n 
A 1 219 THR 219 241 241 THR THR A . n 
A 1 220 ILE 220 242 242 ILE ILE A . n 
A 1 221 ALA 221 243 243 ALA ALA A . n 
A 1 222 ALA 222 244 244 ALA ALA A . n 
A 1 223 ASN 223 245 245 ASN ASN A . n 
A 1 224 SER 224 246 246 SER SER 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 BEN 1   250  250  BEN BEN A . 
C 3 CA  1   260  260  CA  CA  A . 
D 4 HOH 1   2001 2001 HOH HOH A . 
D 4 HOH 2   2002 2002 HOH HOH A . 
D 4 HOH 3   2003 2003 HOH HOH A . 
D 4 HOH 4   2004 2004 HOH HOH A . 
D 4 HOH 5   2005 2005 HOH HOH A . 
D 4 HOH 6   2006 2006 HOH HOH A . 
D 4 HOH 7   2007 2007 HOH HOH A . 
D 4 HOH 8   2008 2008 HOH HOH A . 
D 4 HOH 9   2009 2009 HOH HOH A . 
D 4 HOH 10  2010 2010 HOH HOH A . 
D 4 HOH 11  2011 2011 HOH HOH A . 
D 4 HOH 12  2012 2012 HOH HOH A . 
D 4 HOH 13  2013 2013 HOH HOH A . 
D 4 HOH 14  2014 2014 HOH HOH A . 
D 4 HOH 15  2015 2015 HOH HOH A . 
D 4 HOH 16  2016 2016 HOH HOH A . 
D 4 HOH 17  2017 2017 HOH HOH A . 
D 4 HOH 18  2018 2018 HOH HOH A . 
D 4 HOH 19  2019 2019 HOH HOH A . 
D 4 HOH 20  2020 2020 HOH HOH A . 
D 4 HOH 21  2021 2021 HOH HOH A . 
D 4 HOH 22  2022 2022 HOH HOH A . 
D 4 HOH 23  2023 2023 HOH HOH A . 
D 4 HOH 24  2024 2024 HOH HOH A . 
D 4 HOH 25  2025 2025 HOH HOH A . 
D 4 HOH 26  2026 2026 HOH HOH A . 
D 4 HOH 27  2027 2027 HOH HOH A . 
D 4 HOH 28  2028 2028 HOH HOH A . 
D 4 HOH 29  2029 2029 HOH HOH A . 
D 4 HOH 30  2030 2030 HOH HOH A . 
D 4 HOH 31  2031 2031 HOH HOH A . 
D 4 HOH 32  2032 2032 HOH HOH A . 
D 4 HOH 33  2033 2033 HOH HOH A . 
D 4 HOH 34  2034 2034 HOH HOH A . 
D 4 HOH 35  2035 2035 HOH HOH A . 
D 4 HOH 36  2036 2036 HOH HOH A . 
D 4 HOH 37  2037 2037 HOH HOH A . 
D 4 HOH 38  2038 2038 HOH HOH A . 
D 4 HOH 39  2039 2039 HOH HOH A . 
D 4 HOH 40  2040 2040 HOH HOH A . 
D 4 HOH 41  2041 2041 HOH HOH A . 
D 4 HOH 42  2042 2042 HOH HOH A . 
D 4 HOH 43  2043 2043 HOH HOH A . 
D 4 HOH 44  2044 2044 HOH HOH A . 
D 4 HOH 45  2045 2045 HOH HOH A . 
D 4 HOH 46  2046 2046 HOH HOH A . 
D 4 HOH 47  2047 2047 HOH HOH A . 
D 4 HOH 48  2048 2048 HOH HOH A . 
D 4 HOH 49  2049 2049 HOH HOH A . 
D 4 HOH 50  2050 2050 HOH HOH A . 
D 4 HOH 51  2051 2051 HOH HOH A . 
D 4 HOH 52  2052 2052 HOH HOH A . 
D 4 HOH 53  2053 2053 HOH HOH A . 
D 4 HOH 54  2054 2054 HOH HOH A . 
D 4 HOH 55  2055 2055 HOH HOH A . 
D 4 HOH 56  2056 2056 HOH HOH A . 
D 4 HOH 57  2057 2057 HOH HOH A . 
D 4 HOH 58  2058 2058 HOH HOH A . 
D 4 HOH 59  2059 2059 HOH HOH A . 
D 4 HOH 60  2060 2060 HOH HOH A . 
D 4 HOH 61  2061 2061 HOH HOH A . 
D 4 HOH 62  2062 2062 HOH HOH A . 
D 4 HOH 63  2063 2063 HOH HOH A . 
D 4 HOH 64  2064 2064 HOH HOH A . 
D 4 HOH 65  2065 2065 HOH HOH A . 
D 4 HOH 66  2066 2066 HOH HOH A . 
D 4 HOH 67  2067 2067 HOH HOH A . 
D 4 HOH 68  2068 2068 HOH HOH A . 
D 4 HOH 69  2069 2069 HOH HOH A . 
D 4 HOH 70  2070 2070 HOH HOH A . 
D 4 HOH 71  2071 2071 HOH HOH A . 
D 4 HOH 72  2072 2072 HOH HOH A . 
D 4 HOH 73  2073 2073 HOH HOH A . 
D 4 HOH 74  2074 2074 HOH HOH A . 
D 4 HOH 75  2075 2075 HOH HOH A . 
D 4 HOH 76  2076 2076 HOH HOH A . 
D 4 HOH 77  2077 2077 HOH HOH A . 
D 4 HOH 78  2078 2078 HOH HOH A . 
D 4 HOH 79  2079 2079 HOH HOH A . 
D 4 HOH 80  2080 2080 HOH HOH A . 
D 4 HOH 81  2081 2081 HOH HOH A . 
D 4 HOH 82  2082 2082 HOH HOH A . 
D 4 HOH 83  2083 2083 HOH HOH A . 
D 4 HOH 84  2084 2084 HOH HOH A . 
D 4 HOH 85  2085 2085 HOH HOH A . 
D 4 HOH 86  2086 2086 HOH HOH A . 
D 4 HOH 87  2087 2087 HOH HOH A . 
D 4 HOH 88  2088 2088 HOH HOH A . 
D 4 HOH 89  2089 2089 HOH HOH A . 
D 4 HOH 90  2090 2090 HOH HOH A . 
D 4 HOH 91  2091 2091 HOH HOH A . 
D 4 HOH 92  2092 2092 HOH HOH A . 
D 4 HOH 93  2093 2093 HOH HOH A . 
D 4 HOH 94  2094 2094 HOH HOH A . 
D 4 HOH 95  2095 2095 HOH HOH A . 
D 4 HOH 96  2096 2096 HOH HOH A . 
D 4 HOH 97  2097 2097 HOH HOH A . 
D 4 HOH 98  2098 2098 HOH HOH A . 
D 4 HOH 99  2099 2099 HOH HOH A . 
D 4 HOH 100 2100 2100 HOH HOH A . 
D 4 HOH 101 2101 2101 HOH HOH A . 
D 4 HOH 102 2102 2102 HOH HOH A . 
D 4 HOH 103 2103 2103 HOH HOH A . 
D 4 HOH 104 2104 2104 HOH HOH A . 
D 4 HOH 105 2105 2105 HOH HOH A . 
D 4 HOH 106 2106 2106 HOH HOH A . 
D 4 HOH 107 2107 2107 HOH HOH A . 
D 4 HOH 108 2108 2108 HOH HOH A . 
D 4 HOH 109 2109 2109 HOH HOH A . 
D 4 HOH 110 2110 2110 HOH HOH A . 
D 4 HOH 111 2111 2111 HOH HOH A . 
D 4 HOH 112 2112 2112 HOH HOH A . 
D 4 HOH 113 2113 2113 HOH HOH A . 
D 4 HOH 114 2114 2114 HOH HOH A . 
D 4 HOH 115 2115 2115 HOH HOH A . 
D 4 HOH 116 2116 2116 HOH HOH A . 
D 4 HOH 117 2117 2117 HOH HOH A . 
D 4 HOH 118 2118 2118 HOH HOH A . 
D 4 HOH 119 2119 2119 HOH HOH A . 
D 4 HOH 120 2120 2120 HOH HOH A . 
D 4 HOH 121 2121 2121 HOH HOH A . 
D 4 HOH 122 2122 2122 HOH HOH A . 
D 4 HOH 123 2123 2123 HOH HOH A . 
D 4 HOH 124 2124 2124 HOH HOH A . 
D 4 HOH 125 2125 2125 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 0 A GLU 24  ? CG  ? A GLU 9   CG  
2  1 Y 0 A GLU 24  ? CD  ? A GLU 9   CD  
3  1 Y 0 A GLU 24  ? OE1 ? A GLU 9   OE1 
4  1 Y 0 A GLU 24  ? OE2 ? A GLU 9   OE2 
5  1 Y 0 A ARG 62  ? CD  ? A ARG 45  CD  
6  1 Y 0 A ARG 62  ? NE  ? A ARG 45  NE  
7  1 Y 0 A ARG 62  ? CZ  ? A ARG 45  CZ  
8  1 Y 0 A ARG 62  ? NH1 ? A ARG 45  NH1 
9  1 Y 0 A ARG 62  ? NH2 ? A ARG 45  NH2 
10 1 Y 0 A LYS 74  ? CD  ? A LYS 56  CD  
11 1 Y 0 A LYS 74  ? CE  ? A LYS 56  CE  
12 1 Y 0 A LYS 74  ? NZ  ? A LYS 56  NZ  
13 1 Y 0 A ARG 96  ? CG  ? A ARG 78  CG  
14 1 Y 0 A ARG 96  ? CD  ? A ARG 78  CD  
15 1 Y 0 A ARG 96  ? NE  ? A ARG 78  NE  
16 1 Y 0 A ARG 96  ? CZ  ? A ARG 78  CZ  
17 1 Y 0 A ARG 96  ? NH1 ? A ARG 78  NH1 
18 1 Y 0 A ARG 96  ? NH2 ? A ARG 78  NH2 
19 1 Y 0 A GLU 135 ? CG  ? A GLU 115 CG  
20 1 Y 0 A GLU 135 ? CD  ? A GLU 115 CD  
21 1 Y 0 A GLU 135 ? OE1 ? A GLU 115 OE1 
22 1 Y 0 A GLU 135 ? OE2 ? A GLU 115 OE2 
23 1 Y 0 A GLN 165 ? CG  ? A GLN 145 CG  
24 1 Y 0 A GLN 165 ? CD  ? A GLN 145 CD  
25 1 Y 0 A GLN 165 ? OE1 ? A GLN 145 OE1 
26 1 Y 0 A GLN 165 ? NE2 ? A GLN 145 NE2 
27 1 Y 0 A LYS 169 ? CE  ? A LYS 149 CE  
28 1 Y 0 A LYS 169 ? NZ  ? A LYS 149 NZ  
29 1 Y 0 A LYS 175 ? CD  ? A LYS 155 CD  
30 1 Y 0 A LYS 175 ? CE  ? A LYS 155 CE  
31 1 Y 0 A LYS 175 ? NZ  ? A LYS 155 NZ  
32 1 Y 0 A ASN 178 ? CG  ? A ASN 158 CG  
33 1 Y 0 A ASN 178 ? OD1 ? A ASN 158 OD1 
34 1 Y 0 A ASN 178 ? ND2 ? A ASN 158 ND2 
35 1 Y 0 A LYS 222 ? CE  ? A LYS 200 CE  
36 1 Y 0 A LYS 222 ? NZ  ? A LYS 200 NZ  
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
CNS       refinement       1.0 ? 1 ? ? ? ? 
DENZO     'data reduction' .   ? 2 ? ? ? ? 
SCALEPACK 'data scaling'   .   ? 3 ? ? ? ? 
AMoRE     phasing          .   ? 4 ? ? ? ? 
# 
_cell.entry_id           1H4W 
_cell.length_a           56.683 
_cell.length_b           56.683 
_cell.length_c           143.210 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1H4W 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
# 
_exptl.entry_id          1H4W 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.3 
_exptl_crystal.density_percent_sol   46 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.70 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
;HANGING DROP VAPOUR DIFFUSION 3.3 MG/ML PROTEIN, 2% PEG 4000, 0.05M TRIS PH7.7, 2.5MM CACL2, 2.5 MG/ML BENZAMIDINE/HCL, 25 C, pH 7.70
;
# 
_diffrn.id                               1 
_diffrn.ambient_temp                     298.0 
_diffrn.ambient_temp_details             ? 
_diffrn.crystal_id                       1 
_diffrn.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2000-06-04 
_diffrn_detector.details                MIRRORS 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'SI 111 CHANNEL CUT' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.886 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE BM14' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   BM14 
_diffrn_source.pdbx_wavelength             0.886 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     1H4W 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             52.700 
_reflns.d_resolution_high            1.700 
_reflns.number_obs                   26174 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         94.9 
_reflns.pdbx_Rmerge_I_obs            0.04900 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        18.5000 
_reflns.B_iso_Wilson_estimate        15.8 
_reflns.pdbx_redundancy              4.300 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.70 
_reflns_shell.d_res_low              1.74 
_reflns_shell.percent_possible_all   92.0 
_reflns_shell.Rmerge_I_obs           0.32300 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.500 
_reflns_shell.pdbx_redundancy        ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 1H4W 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     26174 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             52.7 
_refine.ls_d_res_high                            1.7 
_refine.ls_percent_reflns_obs                    94.9 
_refine.ls_R_factor_obs                          0.188 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.188 
_refine.ls_R_factor_R_free                       0.203 
_refine.ls_R_factor_R_free_error                 0.006 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  1313 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               20.0 
_refine.aniso_B[1][1]                            -1.276 
_refine.aniso_B[2][2]                            -1.276 
_refine.aniso_B[3][3]                            2.552 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.359685 
_refine.solvent_model_param_bsol                 58.8756 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 1TRN' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        1H4W 
_refine_analyze.Luzzati_coordinate_error_obs    0.18 
_refine_analyze.Luzzati_sigma_a_obs             0.12 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.21 
_refine_analyze.Luzzati_sigma_a_free            0.15 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1704 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_refine_hist.number_atoms_solvent             125 
_refine_hist.number_atoms_total               1839 
_refine_hist.d_res_high                       1.7 
_refine_hist.d_res_low                        52.7 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d                0.004 ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             1.3   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      25.0  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      0.71  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             1.15  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            1.75  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             1.89  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            2.77  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   10 
_refine_ls_shell.d_res_high                       1.70 
_refine_ls_shell.d_res_low                        1.76 
_refine_ls_shell.number_reflns_R_work             2411 
_refine_ls_shell.R_factor_R_work                  0.230 
_refine_ls_shell.percent_reflns_obs               97.4 
_refine_ls_shell.R_factor_R_free                  0.234 
_refine_ls_shell.R_factor_R_free_error            0.021 
_refine_ls_shell.percent_reflns_R_free            5.0 
_refine_ls_shell.number_reflns_R_free             126 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
loop_
_pdbx_xplor_file.pdbx_refine_id 
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
'X-RAY DIFFRACTION' 1 PROTEIN_REP.PARAM PROTEIN.TOP 
'X-RAY DIFFRACTION' 2 WATER_REP.PARAM   WATER.TOP   
'X-RAY DIFFRACTION' 3 ION.PARAM         ION.TOP     
'X-RAY DIFFRACTION' 4 BEN.PAR           BEN.TOP     
# 
_database_PDB_matrix.entry_id          1H4W 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_struct.entry_id                  1H4W 
_struct.title                     'Structure of human trypsin IV (brain trypsin)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1H4W 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'SERINE PROTEASE, SIGNAL TRANSDUCTION, INHIBITOR RESISTANCE, ALZHEIMER DISEASE, HYDROLASE' 
# 
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                    TRY4_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          P35030 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              1H4W 
_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                 224 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P35030 
_struct_ref_seq.db_align_beg                  81 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  304 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       16 
_struct_ref_seq.pdbx_auth_seq_align_end       246 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             1H4W 
_struct_ref_seq_dif.mon_id                       VAL 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      68 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P35030 
_struct_ref_seq_dif.db_mon_id                    ALA 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          148 
_struct_ref_seq_dif.details                      'cloning artifact' 
_struct_ref_seq_dif.pdbx_auth_seq_num            86 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PQS 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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_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 1 ALA A 38  ? TYR A 42  ? ALA A 55  TYR A 59  5 ? 5  
HELX_P HELX_P2 2 THR A 144 ? TYR A 152 ? THR A 164 TYR A 172 1 ? 9  
HELX_P HELX_P3 3 TYR A 212 ? ASN A 223 ? TYR A 234 ASN A 245 1 ? 12 
# 
_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 
disulf1 disulf ? ? A CYS 7   SG  ? ? ? 1_555 A CYS 137 SG ? ? A CYS 22  A CYS 157  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf2 disulf ? ? A CYS 25  SG  ? ? ? 1_555 A CYS 41  SG ? ? A CYS 42  A CYS 58   1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf3 disulf ? ? A CYS 116 SG  ? ? ? 1_555 A CYS 183 SG ? ? A CYS 136 A CYS 201  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf4 disulf ? ? A CYS 148 SG  ? ? ? 1_555 A CYS 162 SG ? ? A CYS 168 A CYS 182  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf5 disulf ? ? A CYS 173 SG  ? ? ? 1_555 A CYS 197 SG ? ? A CYS 191 A CYS 220  1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc1 metalc ? ? A GLU 52  OE1 ? ? ? 1_555 C CA  .   CA ? ? A GLU 70  A CA  260  1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc2 metalc ? ? A ASN 54  O   ? ? ? 1_555 C CA  .   CA ? ? A ASN 72  A CA  260  1_555 ? ? ? ? ? ? ? 2.338 ? ? 
metalc3 metalc ? ? A VAL 57  O   ? ? ? 1_555 C CA  .   CA ? ? A VAL 75  A CA  260  1_555 ? ? ? ? ? ? ? 2.289 ? ? 
metalc4 metalc ? ? A GLU 59  OE1 ? ? ? 1_555 C CA  .   CA ? ? A GLU 77  A CA  260  1_555 ? ? ? ? ? ? ? 2.512 ? ? 
metalc5 metalc ? ? A GLU 62  OE2 ? ? ? 1_555 C CA  .   CA ? ? A GLU 80  A CA  260  1_555 ? ? ? ? ? ? ? 2.268 ? ? 
metalc6 metalc ? ? C CA  .   CA  ? ? ? 1_555 D HOH .   O  ? ? A CA  260 A HOH 2035 1_555 ? ? ? ? ? ? ? 2.353 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE1 ? A GLU 52 ? A GLU 70 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 O   ? A ASN 54 ? A ASN 72   ? 1_555 87.8  ? 
2  OE1 ? A GLU 52 ? A GLU 70 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 O   ? A VAL 57 ? A VAL 75   ? 1_555 164.1 ? 
3  O   ? A ASN 54 ? A ASN 72 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 O   ? A VAL 57 ? A VAL 75   ? 1_555 84.0  ? 
4  OE1 ? A GLU 52 ? A GLU 70 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 OE1 ? A GLU 59 ? A GLU 77   ? 1_555 94.6  ? 
5  O   ? A ASN 54 ? A ASN 72 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 OE1 ? A GLU 59 ? A GLU 77   ? 1_555 85.9  ? 
6  O   ? A VAL 57 ? A VAL 75 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 OE1 ? A GLU 59 ? A GLU 77   ? 1_555 98.4  ? 
7  OE1 ? A GLU 52 ? A GLU 70 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 OE2 ? A GLU 62 ? A GLU 80   ? 1_555 102.6 ? 
8  O   ? A ASN 54 ? A ASN 72 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 OE2 ? A GLU 62 ? A GLU 80   ? 1_555 167.7 ? 
9  O   ? A VAL 57 ? A VAL 75 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 OE2 ? A GLU 62 ? A GLU 80   ? 1_555 87.3  ? 
10 OE1 ? A GLU 59 ? A GLU 77 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 OE2 ? A GLU 62 ? A GLU 80   ? 1_555 86.8  ? 
11 OE1 ? A GLU 52 ? A GLU 70 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 O   ? D HOH .  ? A HOH 2035 ? 1_555 82.0  ? 
12 O   ? A ASN 54 ? A ASN 72 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 O   ? D HOH .  ? A HOH 2035 ? 1_555 100.9 ? 
13 O   ? A VAL 57 ? A VAL 75 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 O   ? D HOH .  ? A HOH 2035 ? 1_555 86.1  ? 
14 OE1 ? A GLU 59 ? A GLU 77 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 O   ? D HOH .  ? A HOH 2035 ? 1_555 172.3 ? 
15 OE2 ? A GLU 62 ? A GLU 80 ? 1_555 CA ? C CA . ? A CA 260 ? 1_555 O   ? D HOH .  ? A HOH 2035 ? 1_555 87.2  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 7   ? CYS A 137 ? CYS A 22  ? 1_555 CYS A 157 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 25  ? CYS A 41  ? CYS A 42  ? 1_555 CYS A 58  ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 116 ? CYS A 183 ? CYS A 136 ? 1_555 CYS A 201 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS A 148 ? CYS A 162 ? CYS A 168 ? 1_555 CYS A 182 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS A 173 ? CYS A 197 ? CYS A 191 ? 1_555 CYS A 220 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 7 ? 
AB ? 7 ? 
# 
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 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AA 5 6 ? anti-parallel 
AA 6 7 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
AB 4 5 ? anti-parallel 
AB 5 6 ? anti-parallel 
AB 6 7 ? anti-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 
AA 1 TYR A 5   ? THR A 6   ? TYR A 20  THR A 21  
AA 2 LYS A 136 ? PRO A 141 ? LYS A 156 PRO A 161 
AA 3 GLU A 115 ? GLY A 120 ? GLU A 135 GLY A 140 
AA 4 PRO A 180 ? CYS A 183 ? PRO A 198 CYS A 201 
AA 5 GLN A 186 ? TRP A 193 ? GLN A 204 TRP A 215 
AA 6 GLY A 204 ? LYS A 208 ? GLY A 226 LYS A 230 
AA 7 MET A 160 ? VAL A 163 ? MET A 180 VAL A 183 
AB 1 GLN A 15  ? ASN A 19  ? GLN A 30  ASN A 34  
AB 2 HIS A 23  ? SER A 31  ? HIS A 40  SER A 48  
AB 3 TRP A 34  ? SER A 37  ? TRP A 51  SER A 54  
AB 4 MET A 86  ? LEU A 90  ? MET A 104 LEU A 108 
AB 5 GLN A 63  ? ARG A 72  ? GLN A 81  ARG A 90  
AB 6 GLN A 47  ? LEU A 50  ? GLN A 64  LEU A 67  
AB 7 GLN A 15  ? ASN A 19  ? GLN A 30  ASN A 34  
# 
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 
AA 1 2 N TYR A 5   ? N TYR A 20  O CYS A 137 ? O CYS A 157 
AA 2 3 N ALA A 140 ? N ALA A 160 O CYS A 116 ? O CYS A 136 
AA 3 4 N SER A 119 ? N SER A 139 O PRO A 180 ? O PRO A 198 
AA 4 5 N CYS A 183 ? N CYS A 201 O GLN A 186 ? O GLN A 204 
AA 5 6 N TRP A 193 ? N TRP A 215 O VAL A 205 ? O VAL A 227 
AA 6 7 N TYR A 206 ? N TYR A 228 O PHE A 161 ? O PHE A 181 
AB 1 2 O LEU A 18  ? O LEU A 33  N PHE A 24  ? N PHE A 41  
AB 2 3 N ILE A 30  ? N ILE A 47  O TRP A 34  ? O TRP A 51  
AB 3 4 N SER A 37  ? N SER A 54  O MET A 86  ? O MET A 104 
AB 4 5 O LYS A 89  ? O LYS A 107 N VAL A 68  ? N VAL A 86  
AB 5 6 N ILE A 65  ? N ILE A 83  O VAL A 48  ? O VAL A 65  
AB 6 7 N ARG A 49  ? N ARG A 66  O SER A 17  ? O SER A 32  
# 
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 CA  260 ? 6 'BINDING SITE FOR RESIDUE CA A 260'  
AC2 Software A BEN 250 ? 8 'BINDING SITE FOR RESIDUE BEN A 250' 
# 
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 6 GLU A 52  ? GLU A 70   . ? 1_555 ? 
2  AC1 6 ASN A 54  ? ASN A 72   . ? 1_555 ? 
3  AC1 6 VAL A 57  ? VAL A 75   . ? 1_555 ? 
4  AC1 6 GLU A 59  ? GLU A 77   . ? 1_555 ? 
5  AC1 6 GLU A 62  ? GLU A 80   . ? 1_555 ? 
6  AC1 6 HOH D .   ? HOH A 2035 . ? 1_555 ? 
7  AC2 8 ASP A 171 ? ASP A 189  . ? 1_555 ? 
8  AC2 8 SER A 172 ? SER A 190  . ? 1_555 ? 
9  AC2 8 CYS A 173 ? CYS A 191  . ? 1_555 ? 
10 AC2 8 GLN A 174 ? GLN A 192  . ? 1_555 ? 
11 AC2 8 SER A 177 ? SER A 195  . ? 1_555 ? 
12 AC2 8 GLY A 194 ? GLY A 216  . ? 1_555 ? 
13 AC2 8 GLY A 196 ? GLY A 219  . ? 1_555 ? 
14 AC2 8 GLY A 204 ? GLY A 226  . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   1H4W 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           'VAL A 86, CLONING ARTIFACT OR NATURAL POLYMORPHISM' 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    HIS 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     71 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -134.35 
_pdbx_validate_torsion.psi             -65.46 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;
SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET
RECORDS BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS
REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND
LAST STRANDS ARE IDENTICAL.
;
# 
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  
BEN C1   C  Y N 74  
BEN C2   C  Y N 75  
BEN C3   C  Y N 76  
BEN C4   C  Y N 77  
BEN C5   C  Y N 78  
BEN C6   C  Y N 79  
BEN C    C  N N 80  
BEN N1   N  N N 81  
BEN N2   N  N N 82  
BEN H2   H  N N 83  
BEN H3   H  N N 84  
BEN H4   H  N N 85  
BEN H5   H  N N 86  
BEN H6   H  N N 87  
BEN HN1  H  N N 88  
BEN HN21 H  N N 89  
BEN HN22 H  N N 90  
CA  CA   CA N N 91  
CYS N    N  N N 92  
CYS CA   C  N R 93  
CYS C    C  N N 94  
CYS O    O  N N 95  
CYS CB   C  N N 96  
CYS SG   S  N N 97  
CYS OXT  O  N N 98  
CYS H    H  N N 99  
CYS H2   H  N N 100 
CYS HA   H  N N 101 
CYS HB2  H  N N 102 
CYS HB3  H  N N 103 
CYS HG   H  N N 104 
CYS HXT  H  N N 105 
GLN N    N  N N 106 
GLN CA   C  N S 107 
GLN C    C  N N 108 
GLN O    O  N N 109 
GLN CB   C  N N 110 
GLN CG   C  N N 111 
GLN CD   C  N N 112 
GLN OE1  O  N N 113 
GLN NE2  N  N N 114 
GLN OXT  O  N N 115 
GLN H    H  N N 116 
GLN H2   H  N N 117 
GLN HA   H  N N 118 
GLN HB2  H  N N 119 
GLN HB3  H  N N 120 
GLN HG2  H  N N 121 
GLN HG3  H  N N 122 
GLN HE21 H  N N 123 
GLN HE22 H  N N 124 
GLN HXT  H  N N 125 
GLU N    N  N N 126 
GLU CA   C  N S 127 
GLU C    C  N N 128 
GLU O    O  N N 129 
GLU CB   C  N N 130 
GLU CG   C  N N 131 
GLU CD   C  N N 132 
GLU OE1  O  N N 133 
GLU OE2  O  N N 134 
GLU OXT  O  N N 135 
GLU H    H  N N 136 
GLU H2   H  N N 137 
GLU HA   H  N N 138 
GLU HB2  H  N N 139 
GLU HB3  H  N N 140 
GLU HG2  H  N N 141 
GLU HG3  H  N N 142 
GLU HE2  H  N N 143 
GLU HXT  H  N N 144 
GLY N    N  N N 145 
GLY CA   C  N N 146 
GLY C    C  N N 147 
GLY O    O  N N 148 
GLY OXT  O  N N 149 
GLY H    H  N N 150 
GLY H2   H  N N 151 
GLY HA2  H  N N 152 
GLY HA3  H  N N 153 
GLY HXT  H  N N 154 
HIS N    N  N N 155 
HIS CA   C  N S 156 
HIS C    C  N N 157 
HIS O    O  N N 158 
HIS CB   C  N N 159 
HIS CG   C  Y N 160 
HIS ND1  N  Y N 161 
HIS CD2  C  Y N 162 
HIS CE1  C  Y N 163 
HIS NE2  N  Y N 164 
HIS OXT  O  N N 165 
HIS H    H  N N 166 
HIS H2   H  N N 167 
HIS HA   H  N N 168 
HIS HB2  H  N N 169 
HIS HB3  H  N N 170 
HIS HD1  H  N N 171 
HIS HD2  H  N N 172 
HIS HE1  H  N N 173 
HIS HE2  H  N N 174 
HIS HXT  H  N N 175 
HOH O    O  N N 176 
HOH H1   H  N N 177 
HOH H2   H  N N 178 
ILE N    N  N N 179 
ILE CA   C  N S 180 
ILE C    C  N N 181 
ILE O    O  N N 182 
ILE CB   C  N S 183 
ILE CG1  C  N N 184 
ILE CG2  C  N N 185 
ILE CD1  C  N N 186 
ILE OXT  O  N N 187 
ILE H    H  N N 188 
ILE H2   H  N N 189 
ILE HA   H  N N 190 
ILE HB   H  N N 191 
ILE HG12 H  N N 192 
ILE HG13 H  N N 193 
ILE HG21 H  N N 194 
ILE HG22 H  N N 195 
ILE HG23 H  N N 196 
ILE HD11 H  N N 197 
ILE HD12 H  N N 198 
ILE HD13 H  N N 199 
ILE HXT  H  N N 200 
LEU N    N  N N 201 
LEU CA   C  N S 202 
LEU C    C  N N 203 
LEU O    O  N N 204 
LEU CB   C  N N 205 
LEU CG   C  N N 206 
LEU CD1  C  N N 207 
LEU CD2  C  N N 208 
LEU OXT  O  N N 209 
LEU H    H  N N 210 
LEU H2   H  N N 211 
LEU HA   H  N N 212 
LEU HB2  H  N N 213 
LEU HB3  H  N N 214 
LEU HG   H  N N 215 
LEU HD11 H  N N 216 
LEU HD12 H  N N 217 
LEU HD13 H  N N 218 
LEU HD21 H  N N 219 
LEU HD22 H  N N 220 
LEU HD23 H  N N 221 
LEU HXT  H  N N 222 
LYS N    N  N N 223 
LYS CA   C  N S 224 
LYS C    C  N N 225 
LYS O    O  N N 226 
LYS CB   C  N N 227 
LYS CG   C  N N 228 
LYS CD   C  N N 229 
LYS CE   C  N N 230 
LYS NZ   N  N N 231 
LYS OXT  O  N N 232 
LYS H    H  N N 233 
LYS H2   H  N N 234 
LYS HA   H  N N 235 
LYS HB2  H  N N 236 
LYS HB3  H  N N 237 
LYS HG2  H  N N 238 
LYS HG3  H  N N 239 
LYS HD2  H  N N 240 
LYS HD3  H  N N 241 
LYS HE2  H  N N 242 
LYS HE3  H  N N 243 
LYS HZ1  H  N N 244 
LYS HZ2  H  N N 245 
LYS HZ3  H  N N 246 
LYS HXT  H  N N 247 
MET N    N  N N 248 
MET CA   C  N S 249 
MET C    C  N N 250 
MET O    O  N N 251 
MET CB   C  N N 252 
MET CG   C  N N 253 
MET SD   S  N N 254 
MET CE   C  N N 255 
MET OXT  O  N N 256 
MET H    H  N N 257 
MET H2   H  N N 258 
MET HA   H  N N 259 
MET HB2  H  N N 260 
MET HB3  H  N N 261 
MET HG2  H  N N 262 
MET HG3  H  N N 263 
MET HE1  H  N N 264 
MET HE2  H  N N 265 
MET HE3  H  N N 266 
MET HXT  H  N N 267 
PHE N    N  N N 268 
PHE CA   C  N S 269 
PHE C    C  N N 270 
PHE O    O  N N 271 
PHE CB   C  N N 272 
PHE CG   C  Y N 273 
PHE CD1  C  Y N 274 
PHE CD2  C  Y N 275 
PHE CE1  C  Y N 276 
PHE CE2  C  Y N 277 
PHE CZ   C  Y N 278 
PHE OXT  O  N N 279 
PHE H    H  N N 280 
PHE H2   H  N N 281 
PHE HA   H  N N 282 
PHE HB2  H  N N 283 
PHE HB3  H  N N 284 
PHE HD1  H  N N 285 
PHE HD2  H  N N 286 
PHE HE1  H  N N 287 
PHE HE2  H  N N 288 
PHE HZ   H  N N 289 
PHE HXT  H  N N 290 
PRO N    N  N N 291 
PRO CA   C  N S 292 
PRO C    C  N N 293 
PRO O    O  N N 294 
PRO CB   C  N N 295 
PRO CG   C  N N 296 
PRO CD   C  N N 297 
PRO OXT  O  N N 298 
PRO H    H  N N 299 
PRO HA   H  N N 300 
PRO HB2  H  N N 301 
PRO HB3  H  N N 302 
PRO HG2  H  N N 303 
PRO HG3  H  N N 304 
PRO HD2  H  N N 305 
PRO HD3  H  N N 306 
PRO HXT  H  N N 307 
SER N    N  N N 308 
SER CA   C  N S 309 
SER C    C  N N 310 
SER O    O  N N 311 
SER CB   C  N N 312 
SER OG   O  N N 313 
SER OXT  O  N N 314 
SER H    H  N N 315 
SER H2   H  N N 316 
SER HA   H  N N 317 
SER HB2  H  N N 318 
SER HB3  H  N N 319 
SER HG   H  N N 320 
SER HXT  H  N N 321 
THR N    N  N N 322 
THR CA   C  N S 323 
THR C    C  N N 324 
THR O    O  N N 325 
THR CB   C  N R 326 
THR OG1  O  N N 327 
THR CG2  C  N N 328 
THR OXT  O  N N 329 
THR H    H  N N 330 
THR H2   H  N N 331 
THR HA   H  N N 332 
THR HB   H  N N 333 
THR HG1  H  N N 334 
THR HG21 H  N N 335 
THR HG22 H  N N 336 
THR HG23 H  N N 337 
THR HXT  H  N N 338 
TRP N    N  N N 339 
TRP CA   C  N S 340 
TRP C    C  N N 341 
TRP O    O  N N 342 
TRP CB   C  N N 343 
TRP CG   C  Y N 344 
TRP CD1  C  Y N 345 
TRP CD2  C  Y N 346 
TRP NE1  N  Y N 347 
TRP CE2  C  Y N 348 
TRP CE3  C  Y N 349 
TRP CZ2  C  Y N 350 
TRP CZ3  C  Y N 351 
TRP CH2  C  Y N 352 
TRP OXT  O  N N 353 
TRP H    H  N N 354 
TRP H2   H  N N 355 
TRP HA   H  N N 356 
TRP HB2  H  N N 357 
TRP HB3  H  N N 358 
TRP HD1  H  N N 359 
TRP HE1  H  N N 360 
TRP HE3  H  N N 361 
TRP HZ2  H  N N 362 
TRP HZ3  H  N N 363 
TRP HH2  H  N N 364 
TRP HXT  H  N N 365 
TYR N    N  N N 366 
TYR CA   C  N S 367 
TYR C    C  N N 368 
TYR O    O  N N 369 
TYR CB   C  N N 370 
TYR CG   C  Y N 371 
TYR CD1  C  Y N 372 
TYR CD2  C  Y N 373 
TYR CE1  C  Y N 374 
TYR CE2  C  Y N 375 
TYR CZ   C  Y N 376 
TYR OH   O  N N 377 
TYR OXT  O  N N 378 
TYR H    H  N N 379 
TYR H2   H  N N 380 
TYR HA   H  N N 381 
TYR HB2  H  N N 382 
TYR HB3  H  N N 383 
TYR HD1  H  N N 384 
TYR HD2  H  N N 385 
TYR HE1  H  N N 386 
TYR HE2  H  N N 387 
TYR HH   H  N N 388 
TYR HXT  H  N N 389 
VAL N    N  N N 390 
VAL CA   C  N S 391 
VAL C    C  N N 392 
VAL O    O  N N 393 
VAL CB   C  N N 394 
VAL CG1  C  N N 395 
VAL CG2  C  N N 396 
VAL OXT  O  N N 397 
VAL H    H  N N 398 
VAL H2   H  N N 399 
VAL HA   H  N N 400 
VAL HB   H  N N 401 
VAL HG11 H  N N 402 
VAL HG12 H  N N 403 
VAL HG13 H  N N 404 
VAL HG21 H  N N 405 
VAL HG22 H  N N 406 
VAL HG23 H  N N 407 
VAL HXT  H  N N 408 
# 
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  
BEN C1  C2   doub Y N 70  
BEN C1  C6   sing Y N 71  
BEN C1  C    sing N N 72  
BEN C2  C3   sing Y N 73  
BEN C2  H2   sing N N 74  
BEN C3  C4   doub Y N 75  
BEN C3  H3   sing N N 76  
BEN C4  C5   sing Y N 77  
BEN C4  H4   sing N N 78  
BEN C5  C6   doub Y N 79  
BEN C5  H5   sing N N 80  
BEN C6  H6   sing N N 81  
BEN C   N1   doub N E 82  
BEN C   N2   sing N N 83  
BEN N1  HN1  sing N N 84  
BEN N2  HN21 sing N N 85  
BEN N2  HN22 sing N N 86  
CYS N   CA   sing N N 87  
CYS N   H    sing N N 88  
CYS N   H2   sing N N 89  
CYS CA  C    sing N N 90  
CYS CA  CB   sing N N 91  
CYS CA  HA   sing N N 92  
CYS C   O    doub N N 93  
CYS C   OXT  sing N N 94  
CYS CB  SG   sing N N 95  
CYS CB  HB2  sing N N 96  
CYS CB  HB3  sing N N 97  
CYS SG  HG   sing N N 98  
CYS OXT HXT  sing N N 99  
GLN N   CA   sing N N 100 
GLN N   H    sing N N 101 
GLN N   H2   sing N N 102 
GLN CA  C    sing N N 103 
GLN CA  CB   sing N N 104 
GLN CA  HA   sing N N 105 
GLN C   O    doub N N 106 
GLN C   OXT  sing N N 107 
GLN CB  CG   sing N N 108 
GLN CB  HB2  sing N N 109 
GLN CB  HB3  sing N N 110 
GLN CG  CD   sing N N 111 
GLN CG  HG2  sing N N 112 
GLN CG  HG3  sing N N 113 
GLN CD  OE1  doub N N 114 
GLN CD  NE2  sing N N 115 
GLN NE2 HE21 sing N N 116 
GLN NE2 HE22 sing N N 117 
GLN OXT HXT  sing N N 118 
GLU N   CA   sing N N 119 
GLU N   H    sing N N 120 
GLU N   H2   sing N N 121 
GLU CA  C    sing N N 122 
GLU CA  CB   sing N N 123 
GLU CA  HA   sing N N 124 
GLU C   O    doub N N 125 
GLU C   OXT  sing N N 126 
GLU CB  CG   sing N N 127 
GLU CB  HB2  sing N N 128 
GLU CB  HB3  sing N N 129 
GLU CG  CD   sing N N 130 
GLU CG  HG2  sing N N 131 
GLU CG  HG3  sing N N 132 
GLU CD  OE1  doub N N 133 
GLU CD  OE2  sing N N 134 
GLU OE2 HE2  sing N N 135 
GLU OXT HXT  sing N N 136 
GLY N   CA   sing N N 137 
GLY N   H    sing N N 138 
GLY N   H2   sing N N 139 
GLY CA  C    sing N N 140 
GLY CA  HA2  sing N N 141 
GLY CA  HA3  sing N N 142 
GLY C   O    doub N N 143 
GLY C   OXT  sing N N 144 
GLY OXT HXT  sing N N 145 
HIS N   CA   sing N N 146 
HIS N   H    sing N N 147 
HIS N   H2   sing N N 148 
HIS CA  C    sing N N 149 
HIS CA  CB   sing N N 150 
HIS CA  HA   sing N N 151 
HIS C   O    doub N N 152 
HIS C   OXT  sing N N 153 
HIS CB  CG   sing N N 154 
HIS CB  HB2  sing N N 155 
HIS CB  HB3  sing N N 156 
HIS CG  ND1  sing Y N 157 
HIS CG  CD2  doub Y N 158 
HIS ND1 CE1  doub Y N 159 
HIS ND1 HD1  sing N N 160 
HIS CD2 NE2  sing Y N 161 
HIS CD2 HD2  sing N N 162 
HIS CE1 NE2  sing Y N 163 
HIS CE1 HE1  sing N N 164 
HIS NE2 HE2  sing N N 165 
HIS OXT HXT  sing N N 166 
HOH O   H1   sing N N 167 
HOH O   H2   sing N N 168 
ILE N   CA   sing N N 169 
ILE N   H    sing N N 170 
ILE N   H2   sing N N 171 
ILE CA  C    sing N N 172 
ILE CA  CB   sing N N 173 
ILE CA  HA   sing N N 174 
ILE C   O    doub N N 175 
ILE C   OXT  sing N N 176 
ILE CB  CG1  sing N N 177 
ILE CB  CG2  sing N N 178 
ILE CB  HB   sing N N 179 
ILE CG1 CD1  sing N N 180 
ILE CG1 HG12 sing N N 181 
ILE CG1 HG13 sing N N 182 
ILE CG2 HG21 sing N N 183 
ILE CG2 HG22 sing N N 184 
ILE CG2 HG23 sing N N 185 
ILE CD1 HD11 sing N N 186 
ILE CD1 HD12 sing N N 187 
ILE CD1 HD13 sing N N 188 
ILE OXT HXT  sing N N 189 
LEU N   CA   sing N N 190 
LEU N   H    sing N N 191 
LEU N   H2   sing N N 192 
LEU CA  C    sing N N 193 
LEU CA  CB   sing N N 194 
LEU CA  HA   sing N N 195 
LEU C   O    doub N N 196 
LEU C   OXT  sing N N 197 
LEU CB  CG   sing N N 198 
LEU CB  HB2  sing N N 199 
LEU CB  HB3  sing N N 200 
LEU CG  CD1  sing N N 201 
LEU CG  CD2  sing N N 202 
LEU CG  HG   sing N N 203 
LEU CD1 HD11 sing N N 204 
LEU CD1 HD12 sing N N 205 
LEU CD1 HD13 sing N N 206 
LEU CD2 HD21 sing N N 207 
LEU CD2 HD22 sing N N 208 
LEU CD2 HD23 sing N N 209 
LEU OXT HXT  sing N N 210 
LYS N   CA   sing N N 211 
LYS N   H    sing N N 212 
LYS N   H2   sing N N 213 
LYS CA  C    sing N N 214 
LYS CA  CB   sing N N 215 
LYS CA  HA   sing N N 216 
LYS C   O    doub N N 217 
LYS C   OXT  sing N N 218 
LYS CB  CG   sing N N 219 
LYS CB  HB2  sing N N 220 
LYS CB  HB3  sing N N 221 
LYS CG  CD   sing N N 222 
LYS CG  HG2  sing N N 223 
LYS CG  HG3  sing N N 224 
LYS CD  CE   sing N N 225 
LYS CD  HD2  sing N N 226 
LYS CD  HD3  sing N N 227 
LYS CE  NZ   sing N N 228 
LYS CE  HE2  sing N N 229 
LYS CE  HE3  sing N N 230 
LYS NZ  HZ1  sing N N 231 
LYS NZ  HZ2  sing N N 232 
LYS NZ  HZ3  sing N N 233 
LYS OXT HXT  sing N N 234 
MET N   CA   sing N N 235 
MET N   H    sing N N 236 
MET N   H2   sing N N 237 
MET CA  C    sing N N 238 
MET CA  CB   sing N N 239 
MET CA  HA   sing N N 240 
MET C   O    doub N N 241 
MET C   OXT  sing N N 242 
MET CB  CG   sing N N 243 
MET CB  HB2  sing N N 244 
MET CB  HB3  sing N N 245 
MET CG  SD   sing N N 246 
MET CG  HG2  sing N N 247 
MET CG  HG3  sing N N 248 
MET SD  CE   sing N N 249 
MET CE  HE1  sing N N 250 
MET CE  HE2  sing N N 251 
MET CE  HE3  sing N N 252 
MET OXT HXT  sing N N 253 
PHE N   CA   sing N N 254 
PHE N   H    sing N N 255 
PHE N   H2   sing N N 256 
PHE CA  C    sing N N 257 
PHE CA  CB   sing N N 258 
PHE CA  HA   sing N N 259 
PHE C   O    doub N N 260 
PHE C   OXT  sing N N 261 
PHE CB  CG   sing N N 262 
PHE CB  HB2  sing N N 263 
PHE CB  HB3  sing N N 264 
PHE CG  CD1  doub Y N 265 
PHE CG  CD2  sing Y N 266 
PHE CD1 CE1  sing Y N 267 
PHE CD1 HD1  sing N N 268 
PHE CD2 CE2  doub Y N 269 
PHE CD2 HD2  sing N N 270 
PHE CE1 CZ   doub Y N 271 
PHE CE1 HE1  sing N N 272 
PHE CE2 CZ   sing Y N 273 
PHE CE2 HE2  sing N N 274 
PHE CZ  HZ   sing N N 275 
PHE OXT HXT  sing N N 276 
PRO N   CA   sing N N 277 
PRO N   CD   sing N N 278 
PRO N   H    sing N N 279 
PRO CA  C    sing N N 280 
PRO CA  CB   sing N N 281 
PRO CA  HA   sing N N 282 
PRO C   O    doub N N 283 
PRO C   OXT  sing N N 284 
PRO CB  CG   sing N N 285 
PRO CB  HB2  sing N N 286 
PRO CB  HB3  sing N N 287 
PRO CG  CD   sing N N 288 
PRO CG  HG2  sing N N 289 
PRO CG  HG3  sing N N 290 
PRO CD  HD2  sing N N 291 
PRO CD  HD3  sing N N 292 
PRO OXT HXT  sing N N 293 
SER N   CA   sing N N 294 
SER N   H    sing N N 295 
SER N   H2   sing N N 296 
SER CA  C    sing N N 297 
SER CA  CB   sing N N 298 
SER CA  HA   sing N N 299 
SER C   O    doub N N 300 
SER C   OXT  sing N N 301 
SER CB  OG   sing N N 302 
SER CB  HB2  sing N N 303 
SER CB  HB3  sing N N 304 
SER OG  HG   sing N N 305 
SER OXT HXT  sing N N 306 
THR N   CA   sing N N 307 
THR N   H    sing N N 308 
THR N   H2   sing N N 309 
THR CA  C    sing N N 310 
THR CA  CB   sing N N 311 
THR CA  HA   sing N N 312 
THR C   O    doub N N 313 
THR C   OXT  sing N N 314 
THR CB  OG1  sing N N 315 
THR CB  CG2  sing N N 316 
THR CB  HB   sing N N 317 
THR OG1 HG1  sing N N 318 
THR CG2 HG21 sing N N 319 
THR CG2 HG22 sing N N 320 
THR CG2 HG23 sing N N 321 
THR OXT HXT  sing N N 322 
TRP N   CA   sing N N 323 
TRP N   H    sing N N 324 
TRP N   H2   sing N N 325 
TRP CA  C    sing N N 326 
TRP CA  CB   sing N N 327 
TRP CA  HA   sing N N 328 
TRP C   O    doub N N 329 
TRP C   OXT  sing N N 330 
TRP CB  CG   sing N N 331 
TRP CB  HB2  sing N N 332 
TRP CB  HB3  sing N N 333 
TRP CG  CD1  doub Y N 334 
TRP CG  CD2  sing Y N 335 
TRP CD1 NE1  sing Y N 336 
TRP CD1 HD1  sing N N 337 
TRP CD2 CE2  doub Y N 338 
TRP CD2 CE3  sing Y N 339 
TRP NE1 CE2  sing Y N 340 
TRP NE1 HE1  sing N N 341 
TRP CE2 CZ2  sing Y N 342 
TRP CE3 CZ3  doub Y N 343 
TRP CE3 HE3  sing N N 344 
TRP CZ2 CH2  doub Y N 345 
TRP CZ2 HZ2  sing N N 346 
TRP CZ3 CH2  sing Y N 347 
TRP CZ3 HZ3  sing N N 348 
TRP CH2 HH2  sing N N 349 
TRP OXT HXT  sing N N 350 
TYR N   CA   sing N N 351 
TYR N   H    sing N N 352 
TYR N   H2   sing N N 353 
TYR CA  C    sing N N 354 
TYR CA  CB   sing N N 355 
TYR CA  HA   sing N N 356 
TYR C   O    doub N N 357 
TYR C   OXT  sing N N 358 
TYR CB  CG   sing N N 359 
TYR CB  HB2  sing N N 360 
TYR CB  HB3  sing N N 361 
TYR CG  CD1  doub Y N 362 
TYR CG  CD2  sing Y N 363 
TYR CD1 CE1  sing Y N 364 
TYR CD1 HD1  sing N N 365 
TYR CD2 CE2  doub Y N 366 
TYR CD2 HD2  sing N N 367 
TYR CE1 CZ   doub Y N 368 
TYR CE1 HE1  sing N N 369 
TYR CE2 CZ   sing Y N 370 
TYR CE2 HE2  sing N N 371 
TYR CZ  OH   sing N N 372 
TYR OH  HH   sing N N 373 
TYR OXT HXT  sing N N 374 
VAL N   CA   sing N N 375 
VAL N   H    sing N N 376 
VAL N   H2   sing N N 377 
VAL CA  C    sing N N 378 
VAL CA  CB   sing N N 379 
VAL CA  HA   sing N N 380 
VAL C   O    doub N N 381 
VAL C   OXT  sing N N 382 
VAL CB  CG1  sing N N 383 
VAL CB  CG2  sing N N 384 
VAL CB  HB   sing N N 385 
VAL CG1 HG11 sing N N 386 
VAL CG1 HG12 sing N N 387 
VAL CG1 HG13 sing N N 388 
VAL CG2 HG21 sing N N 389 
VAL CG2 HG22 sing N N 390 
VAL CG2 HG23 sing N N 391 
VAL OXT HXT  sing N N 392 
# 
_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   1TRN 
_pdbx_initial_refinement_model.details          'PDB ENTRY 1TRN' 
# 
_atom_sites.entry_id                    1H4W 
_atom_sites.fract_transf_matrix[1][1]   0.017642 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017642 
_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]   0.006983 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ILE A 1 1   ? 58.409 34.673 41.445 1.00   9.57  ? 16   ILE A N   1 
ATOM   2    C  CA  . ILE A 1 1   ? 58.734 36.059 41.899 1.00   9.85  ? 16   ILE A CA  1 
ATOM   3    C  C   . ILE A 1 1   ? 59.613 36.749 40.864 1.00   10.19 ? 16   ILE A C   1 
ATOM   4    O  O   . ILE A 1 1   ? 60.663 36.222 40.480 1.00   10.86 ? 16   ILE A O   1 
ATOM   5    C  CB  . ILE A 1 1   ? 59.504 36.046 43.245 1.00   9.17  ? 16   ILE A CB  1 
ATOM   6    C  CG1 . ILE A 1 1   ? 58.686 35.324 44.324 1.00   12.74 ? 16   ILE A CG1 1 
ATOM   7    C  CG2 . ILE A 1 1   ? 59.819 37.483 43.676 1.00   11.18 ? 16   ILE A CG2 1 
ATOM   8    C  CD1 . ILE A 1 1   ? 57.442 36.071 44.783 1.00   13.77 ? 16   ILE A CD1 1 
ATOM   9    N  N   . VAL A 1 2   ? 59.173 37.920 40.413 1.00   9.87  ? 17   VAL A N   1 
ATOM   10   C  CA  . VAL A 1 2   ? 59.915 38.711 39.438 1.00   11.20 ? 17   VAL A CA  1 
ATOM   11   C  C   . VAL A 1 2   ? 60.558 39.898 40.153 1.00   11.28 ? 17   VAL A C   1 
ATOM   12   O  O   . VAL A 1 2   ? 59.891 40.607 40.902 1.00   12.43 ? 17   VAL A O   1 
ATOM   13   C  CB  . VAL A 1 2   ? 58.985 39.263 38.334 1.00   11.72 ? 17   VAL A CB  1 
ATOM   14   C  CG1 . VAL A 1 2   ? 59.795 40.089 37.333 1.00   14.74 ? 17   VAL A CG1 1 
ATOM   15   C  CG2 . VAL A 1 2   ? 58.272 38.119 37.634 1.00   11.71 ? 17   VAL A CG2 1 
ATOM   16   N  N   . GLY A 1 3   ? 61.853 40.101 39.923 1.00   13.18 ? 18   GLY A N   1 
ATOM   17   C  CA  . GLY A 1 3   ? 62.557 41.214 40.537 1.00   13.33 ? 18   GLY A CA  1 
ATOM   18   C  C   . GLY A 1 3   ? 62.862 41.081 42.019 1.00   14.79 ? 18   GLY A C   1 
ATOM   19   O  O   . GLY A 1 3   ? 63.148 42.078 42.687 1.00   15.91 ? 18   GLY A O   1 
ATOM   20   N  N   . GLY A 1 4   ? 62.810 39.859 42.537 1.00   13.76 ? 19   GLY A N   1 
ATOM   21   C  CA  . GLY A 1 4   ? 63.089 39.657 43.947 1.00   14.86 ? 19   GLY A CA  1 
ATOM   22   C  C   . GLY A 1 4   ? 64.517 39.212 44.187 1.00   14.42 ? 19   GLY A C   1 
ATOM   23   O  O   . GLY A 1 4   ? 65.395 39.430 43.354 1.00   15.42 ? 19   GLY A O   1 
ATOM   24   N  N   . TYR A 1 5   ? 64.748 38.589 45.335 1.00   13.40 ? 20   TYR A N   1 
ATOM   25   C  CA  . TYR A 1 5   ? 66.070 38.094 45.692 1.00   13.83 ? 20   TYR A CA  1 
ATOM   26   C  C   . TYR A 1 5   ? 65.933 36.694 46.275 1.00   14.36 ? 20   TYR A C   1 
ATOM   27   O  O   . TYR A 1 5   ? 64.853 36.292 46.706 1.00   12.91 ? 20   TYR A O   1 
ATOM   28   C  CB  . TYR A 1 5   ? 66.732 39.020 46.719 1.00   14.69 ? 20   TYR A CB  1 
ATOM   29   C  CG  . TYR A 1 5   ? 65.902 39.257 47.960 1.00   14.54 ? 20   TYR A CG  1 
ATOM   30   C  CD1 . TYR A 1 5   ? 64.915 40.242 47.986 1.00   15.11 ? 20   TYR A CD1 1 
ATOM   31   C  CD2 . TYR A 1 5   ? 66.101 38.492 49.110 1.00   14.19 ? 20   TYR A CD2 1 
ATOM   32   C  CE1 . TYR A 1 5   ? 64.148 40.463 49.125 1.00   16.03 ? 20   TYR A CE1 1 
ATOM   33   C  CE2 . TYR A 1 5   ? 65.338 38.704 50.254 1.00   15.37 ? 20   TYR A CE2 1 
ATOM   34   C  CZ  . TYR A 1 5   ? 64.366 39.690 50.254 1.00   16.23 ? 20   TYR A CZ  1 
ATOM   35   O  OH  . TYR A 1 5   ? 63.611 39.901 51.383 1.00   17.78 ? 20   TYR A OH  1 
ATOM   36   N  N   . THR A 1 6   ? 67.027 35.945 46.281 1.00   14.42 ? 21   THR A N   1 
ATOM   37   C  CA  . THR A 1 6   ? 66.993 34.600 46.829 1.00   15.61 ? 21   THR A CA  1 
ATOM   38   C  C   . THR A 1 6   ? 66.910 34.697 48.345 1.00   15.46 ? 21   THR A C   1 
ATOM   39   O  O   . THR A 1 6   ? 67.751 35.337 48.979 1.00   16.49 ? 21   THR A O   1 
ATOM   40   C  CB  . THR A 1 6   ? 68.254 33.813 46.449 1.00   16.36 ? 21   THR A CB  1 
ATOM   41   O  OG1 . THR A 1 6   ? 68.359 33.750 45.023 1.00   19.03 ? 21   THR A OG1 1 
ATOM   42   C  CG2 . THR A 1 6   ? 68.191 32.398 47.014 1.00   18.79 ? 21   THR A CG2 1 
ATOM   43   N  N   . CYS A 1 7   ? 65.889 34.077 48.927 1.00   13.60 ? 22   CYS A N   1 
ATOM   44   C  CA  . CYS A 1 7   ? 65.732 34.103 50.375 1.00   14.63 ? 22   CYS A CA  1 
ATOM   45   C  C   . CYS A 1 7   ? 66.865 33.310 51.015 1.00   15.82 ? 22   CYS A C   1 
ATOM   46   O  O   . CYS A 1 7   ? 67.422 32.404 50.398 1.00   16.44 ? 22   CYS A O   1 
ATOM   47   C  CB  . CYS A 1 7   ? 64.435 33.430 50.810 1.00   13.03 ? 22   CYS A CB  1 
ATOM   48   S  SG  . CYS A 1 7   ? 62.880 33.817 49.948 1.00   12.89 ? 22   CYS A SG  1 
ATOM   49   N  N   . GLU A 1 8   ? 67.193 33.633 52.259 1.00   16.88 ? 23   GLU A N   1 
ATOM   50   C  CA  . GLU A 1 8   ? 68.235 32.889 52.950 1.00   17.81 ? 23   GLU A CA  1 
ATOM   51   C  C   . GLU A 1 8   ? 67.642 31.516 53.255 1.00   16.76 ? 23   GLU A C   1 
ATOM   52   O  O   . GLU A 1 8   ? 66.466 31.413 53.609 1.00   16.68 ? 23   GLU A O   1 
ATOM   53   C  CB  . GLU A 1 8   ? 68.629 33.590 54.248 1.00   19.29 ? 23   GLU A CB  1 
ATOM   54   C  CG  . GLU A 1 8   ? 69.937 33.090 54.826 1.00   24.34 ? 23   GLU A CG  1 
ATOM   55   C  CD  . GLU A 1 8   ? 70.414 33.939 55.983 1.00   25.84 ? 23   GLU A CD  1 
ATOM   56   O  OE1 . GLU A 1 8   ? 69.892 33.772 57.102 1.00   30.29 ? 23   GLU A OE1 1 
ATOM   57   O  OE2 . GLU A 1 8   ? 71.301 34.785 55.762 1.00   30.38 ? 23   GLU A OE2 1 
ATOM   58   N  N   . GLU A 1 9   ? 68.448 30.469 53.111 1.00   17.35 ? 24   GLU A N   1 
ATOM   59   C  CA  . GLU A 1 9   ? 67.988 29.101 53.353 1.00   18.03 ? 24   GLU A CA  1 
ATOM   60   C  C   . GLU A 1 9   ? 67.190 28.895 54.642 1.00   18.64 ? 24   GLU A C   1 
ATOM   61   O  O   . GLU A 1 9   ? 67.665 29.188 55.740 1.00   18.37 ? 24   GLU A O   1 
ATOM   62   C  CB  . GLU A 1 9   ? 69.180 28.129 53.320 1.00   19.83 ? 24   GLU A CB  1 
ATOM   63   C  CG  . GLU A 1 9   ? 70.456 28.658 53.956 0.0000 19.31 ? 24   GLU A CG  1 
ATOM   64   C  CD  . GLU A 1 9   ? 71.151 29.692 53.091 0.0000 19.50 ? 24   GLU A CD  1 
ATOM   65   O  OE1 . GLU A 1 9   ? 71.499 29.364 51.936 0.0000 19.46 ? 24   GLU A OE1 1 
ATOM   66   O  OE2 . GLU A 1 9   ? 71.352 30.829 53.563 0.0000 19.46 ? 24   GLU A OE2 1 
ATOM   67   N  N   . ASN A 1 10  ? 65.967 28.392 54.484 1.00   17.76 ? 25   ASN A N   1 
ATOM   68   C  CA  . ASN A 1 10  ? 65.061 28.108 55.595 1.00   18.30 ? 25   ASN A CA  1 
ATOM   69   C  C   . ASN A 1 10  ? 64.721 29.298 56.489 1.00   17.44 ? 25   ASN A C   1 
ATOM   70   O  O   . ASN A 1 10  ? 64.386 29.121 57.664 1.00   18.59 ? 25   ASN A O   1 
ATOM   71   C  CB  . ASN A 1 10  ? 65.627 26.972 56.452 1.00   20.83 ? 25   ASN A CB  1 
ATOM   72   C  CG  . ASN A 1 10  ? 65.852 25.704 55.659 1.00   22.43 ? 25   ASN A CG  1 
ATOM   73   O  OD1 . ASN A 1 10  ? 64.915 25.135 55.094 1.00   24.65 ? 25   ASN A OD1 1 
ATOM   74   N  ND2 . ASN A 1 10  ? 67.100 25.256 55.604 1.00   22.28 ? 25   ASN A ND2 1 
ATOM   75   N  N   . SER A 1 11  ? 64.787 30.506 55.938 1.00   15.72 ? 26   SER A N   1 
ATOM   76   C  CA  . SER A 1 11  ? 64.471 31.698 56.717 1.00   14.88 ? 26   SER A CA  1 
ATOM   77   C  C   . SER A 1 11  ? 62.958 31.943 56.798 1.00   13.99 ? 26   SER A C   1 
ATOM   78   O  O   . SER A 1 11  ? 62.496 32.783 57.571 1.00   14.63 ? 26   SER A O   1 
ATOM   79   C  CB  . SER A 1 11  ? 65.182 32.922 56.135 1.00   15.99 ? 26   SER A CB  1 
ATOM   80   O  OG  . SER A 1 11  ? 64.827 33.120 54.785 1.00   17.06 ? 26   SER A OG  1 
ATOM   81   N  N   A LEU A 1 12  ? 62.201 31.206 55.988 0.50   13.53 ? 27   LEU A N   1 
ATOM   82   N  N   B LEU A 1 12  ? 62.198 31.212 55.987 0.50   12.96 ? 27   LEU A N   1 
ATOM   83   C  CA  A LEU A 1 12  ? 60.743 31.305 55.968 0.50   13.95 ? 27   LEU A CA  1 
ATOM   84   C  CA  B LEU A 1 12  ? 60.739 31.306 55.983 0.50   12.93 ? 27   LEU A CA  1 
ATOM   85   C  C   A LEU A 1 12  ? 60.209 29.898 56.231 0.50   13.95 ? 27   LEU A C   1 
ATOM   86   C  C   B LEU A 1 12  ? 60.239 29.889 56.257 0.50   12.43 ? 27   LEU A C   1 
ATOM   87   O  O   A LEU A 1 12  ? 59.675 29.247 55.334 0.50   12.80 ? 27   LEU A O   1 
ATOM   88   O  O   B LEU A 1 12  ? 59.772 29.199 55.352 0.50   11.49 ? 27   LEU A O   1 
ATOM   89   C  CB  A LEU A 1 12  ? 60.257 31.796 54.600 0.50   14.51 ? 27   LEU A CB  1 
ATOM   90   C  CB  B LEU A 1 12  ? 60.221 31.790 54.623 0.50   13.63 ? 27   LEU A CB  1 
ATOM   91   C  CG  A LEU A 1 12  ? 60.821 33.129 54.102 0.50   15.18 ? 27   LEU A CG  1 
ATOM   92   C  CG  B LEU A 1 12  ? 60.464 33.256 54.253 0.50   14.57 ? 27   LEU A CG  1 
ATOM   93   C  CD1 A LEU A 1 12  ? 60.155 33.496 52.782 0.50   15.24 ? 27   LEU A CD1 1 
ATOM   94   C  CD1 B LEU A 1 12  ? 61.943 33.501 54.016 0.50   14.80 ? 27   LEU A CD1 1 
ATOM   95   C  CD2 A LEU A 1 12  ? 60.577 34.215 55.137 0.50   14.96 ? 27   LEU A CD2 1 
ATOM   96   C  CD2 B LEU A 1 12  ? 59.663 33.598 53.005 0.50   13.56 ? 27   LEU A CD2 1 
ATOM   97   N  N   A PRO A 1 13  ? 60.345 29.416 57.479 0.50   14.24 ? 28   PRO A N   1 
ATOM   98   N  N   B PRO A 1 13  ? 60.321 29.446 57.524 0.50   12.05 ? 28   PRO A N   1 
ATOM   99   C  CA  A PRO A 1 13  ? 59.904 28.084 57.913 0.50   12.88 ? 28   PRO A CA  1 
ATOM   100  C  CA  B PRO A 1 13  ? 59.900 28.107 57.956 0.50   10.95 ? 28   PRO A CA  1 
ATOM   101  C  C   A PRO A 1 13  ? 58.462 27.696 57.595 0.50   12.17 ? 28   PRO A C   1 
ATOM   102  C  C   B PRO A 1 13  ? 58.449 27.708 57.696 0.50   10.96 ? 28   PRO A C   1 
ATOM   103  O  O   A PRO A 1 13  ? 58.146 26.509 57.510 0.50   12.31 ? 28   PRO A O   1 
ATOM   104  O  O   B PRO A 1 13  ? 58.113 26.525 57.749 0.50   11.70 ? 28   PRO A O   1 
ATOM   105  C  CB  A PRO A 1 13  ? 60.163 28.110 59.419 0.50   13.54 ? 28   PRO A CB  1 
ATOM   106  C  CB  B PRO A 1 13  ? 60.254 28.103 59.443 0.50   10.57 ? 28   PRO A CB  1 
ATOM   107  C  CG  A PRO A 1 13  ? 61.306 29.056 59.554 0.50   15.05 ? 28   PRO A CG  1 
ATOM   108  C  CG  B PRO A 1 13  ? 60.047 29.529 59.834 0.50   10.44 ? 28   PRO A CG  1 
ATOM   109  C  CD  A PRO A 1 13  ? 60.911 30.165 58.614 0.50   15.10 ? 28   PRO A CD  1 
ATOM   110  C  CD  B PRO A 1 13  ? 60.686 30.277 58.687 0.50   11.92 ? 28   PRO A CD  1 
ATOM   111  N  N   . TYR A 1 14  ? 57.598 28.689 57.412 1.00   10.20 ? 29   TYR A N   1 
ATOM   112  C  CA  . TYR A 1 14  ? 56.186 28.436 57.138 1.00   10.10 ? 29   TYR A CA  1 
ATOM   113  C  C   . TYR A 1 14  ? 55.858 28.224 55.662 1.00   9.95  ? 29   TYR A C   1 
ATOM   114  O  O   . TYR A 1 14  ? 54.738 27.831 55.331 1.00   9.45  ? 29   TYR A O   1 
ATOM   115  C  CB  . TYR A 1 14  ? 55.353 29.602 57.673 1.00   9.84  ? 29   TYR A CB  1 
ATOM   116  C  CG  . TYR A 1 14  ? 55.814 30.931 57.121 1.00   10.08 ? 29   TYR A CG  1 
ATOM   117  C  CD1 . TYR A 1 14  ? 55.389 31.375 55.870 1.00   10.72 ? 29   TYR A CD1 1 
ATOM   118  C  CD2 . TYR A 1 14  ? 56.727 31.716 57.826 1.00   11.11 ? 29   TYR A CD2 1 
ATOM   119  C  CE1 . TYR A 1 14  ? 55.864 32.576 55.331 1.00   10.65 ? 29   TYR A CE1 1 
ATOM   120  C  CE2 . TYR A 1 14  ? 57.209 32.911 57.298 1.00   10.23 ? 29   TYR A CE2 1 
ATOM   121  C  CZ  . TYR A 1 14  ? 56.773 33.336 56.054 1.00   12.07 ? 29   TYR A CZ  1 
ATOM   122  O  OH  . TYR A 1 14  ? 57.234 34.527 55.543 1.00   13.18 ? 29   TYR A OH  1 
ATOM   123  N  N   . GLN A 1 15  ? 56.825 28.487 54.784 1.00   9.41  ? 30   GLN A N   1 
ATOM   124  C  CA  . GLN A 1 15  ? 56.610 28.332 53.344 1.00   10.28 ? 30   GLN A CA  1 
ATOM   125  C  C   . GLN A 1 15  ? 56.645 26.870 52.941 1.00   10.24 ? 30   GLN A C   1 
ATOM   126  O  O   . GLN A 1 15  ? 57.580 26.153 53.289 1.00   12.48 ? 30   GLN A O   1 
ATOM   127  C  CB  . GLN A 1 15  ? 57.690 29.074 52.553 1.00   10.73 ? 30   GLN A CB  1 
ATOM   128  C  CG  . GLN A 1 15  ? 57.682 28.765 51.046 1.00   11.03 ? 30   GLN A CG  1 
ATOM   129  C  CD  . GLN A 1 15  ? 56.662 29.585 50.278 1.00   14.20 ? 30   GLN A CD  1 
ATOM   130  O  OE1 . GLN A 1 15  ? 55.902 29.058 49.460 1.00   15.67 ? 30   GLN A OE1 1 
ATOM   131  N  NE2 . GLN A 1 15  ? 56.646 30.883 50.531 1.00   13.45 ? 30   GLN A NE2 1 
ATOM   132  N  N   . VAL A 1 16  ? 55.630 26.436 52.199 1.00   11.22 ? 31   VAL A N   1 
ATOM   133  C  CA  . VAL A 1 16  ? 55.589 25.059 51.732 1.00   12.13 ? 31   VAL A CA  1 
ATOM   134  C  C   . VAL A 1 16  ? 55.433 25.028 50.218 1.00   12.95 ? 31   VAL A C   1 
ATOM   135  O  O   . VAL A 1 16  ? 55.021 26.013 49.594 1.00   11.18 ? 31   VAL A O   1 
ATOM   136  C  CB  . VAL A 1 16  ? 54.416 24.263 52.364 1.00   14.84 ? 31   VAL A CB  1 
ATOM   137  C  CG1 . VAL A 1 16  ? 54.425 24.426 53.873 1.00   16.84 ? 31   VAL A CG1 1 
ATOM   138  C  CG2 . VAL A 1 16  ? 53.096 24.719 51.778 1.00   14.46 ? 31   VAL A CG2 1 
ATOM   139  N  N   . SER A 1 17  ? 55.781 23.889 49.636 1.00   12.57 ? 32   SER A N   1 
ATOM   140  C  CA  . SER A 1 17  ? 55.652 23.679 48.204 1.00   12.92 ? 32   SER A CA  1 
ATOM   141  C  C   . SER A 1 17  ? 54.602 22.590 48.012 1.00   13.80 ? 32   SER A C   1 
ATOM   142  O  O   . SER A 1 17  ? 54.640 21.568 48.694 1.00   16.15 ? 32   SER A O   1 
ATOM   143  C  CB  . SER A 1 17  ? 56.988 23.215 47.612 1.00   13.38 ? 32   SER A CB  1 
ATOM   144  O  OG  . SER A 1 17  ? 56.820 22.700 46.295 1.00   14.77 ? 32   SER A OG  1 
ATOM   145  N  N   . LEU A 1 18  ? 53.643 22.829 47.121 1.00   13.30 ? 33   LEU A N   1 
ATOM   146  C  CA  . LEU A 1 18  ? 52.622 21.830 46.827 1.00   14.10 ? 33   LEU A CA  1 
ATOM   147  C  C   . LEU A 1 18  ? 53.169 21.110 45.605 1.00   14.73 ? 33   LEU A C   1 
ATOM   148  O  O   . LEU A 1 18  ? 53.456 21.735 44.583 1.00   14.12 ? 33   LEU A O   1 
ATOM   149  C  CB  . LEU A 1 18  ? 51.276 22.488 46.517 1.00   15.72 ? 33   LEU A CB  1 
ATOM   150  C  CG  . LEU A 1 18  ? 50.686 23.353 47.638 1.00   15.64 ? 33   LEU A CG  1 
ATOM   151  C  CD1 . LEU A 1 18  ? 49.242 23.687 47.310 1.00   16.96 ? 33   LEU A CD1 1 
ATOM   152  C  CD2 . LEU A 1 18  ? 50.761 22.613 48.972 1.00   17.42 ? 33   LEU A CD2 1 
ATOM   153  N  N   . ASN A 1 19  ? 53.322 19.795 45.719 1.00   16.72 ? 34   ASN A N   1 
ATOM   154  C  CA  . ASN A 1 19  ? 53.901 18.996 44.646 1.00   19.72 ? 34   ASN A CA  1 
ATOM   155  C  C   . ASN A 1 19  ? 52.961 17.916 44.121 1.00   21.11 ? 34   ASN A C   1 
ATOM   156  O  O   . ASN A 1 19  ? 52.317 17.205 44.890 1.00   20.89 ? 34   ASN A O   1 
ATOM   157  C  CB  . ASN A 1 19  ? 55.201 18.364 45.161 1.00   19.59 ? 34   ASN A CB  1 
ATOM   158  C  CG  . ASN A 1 19  ? 55.954 17.597 44.092 1.00   21.97 ? 34   ASN A CG  1 
ATOM   159  O  OD1 . ASN A 1 19  ? 55.507 16.547 43.628 1.00   23.13 ? 34   ASN A OD1 1 
ATOM   160  N  ND2 . ASN A 1 19  ? 57.111 18.119 43.700 1.00   19.81 ? 34   ASN A ND2 1 
ATOM   161  N  N   . SER A 1 20  ? 52.888 17.812 42.799 1.00   24.09 ? 37   SER A N   1 
ATOM   162  C  CA  . SER A 1 20  ? 52.051 16.819 42.136 1.00   28.76 ? 37   SER A CA  1 
ATOM   163  C  C   . SER A 1 20  ? 52.890 16.288 40.982 1.00   29.50 ? 37   SER A C   1 
ATOM   164  O  O   . SER A 1 20  ? 52.482 16.340 39.823 1.00   33.17 ? 37   SER A O   1 
ATOM   165  C  CB  . SER A 1 20  ? 50.776 17.476 41.602 1.00   30.13 ? 37   SER A CB  1 
ATOM   166  O  OG  . SER A 1 20  ? 49.909 16.514 41.029 1.00   37.00 ? 37   SER A OG  1 
ATOM   167  N  N   . GLY A 1 21  ? 54.070 15.779 41.316 1.00   28.61 ? 38   GLY A N   1 
ATOM   168  C  CA  . GLY A 1 21  ? 54.986 15.287 40.305 1.00   28.80 ? 38   GLY A CA  1 
ATOM   169  C  C   . GLY A 1 21  ? 56.079 16.331 40.204 1.00   27.82 ? 38   GLY A C   1 
ATOM   170  O  O   . GLY A 1 21  ? 57.253 16.026 40.004 1.00   30.86 ? 38   GLY A O   1 
ATOM   171  N  N   . SER A 1 22  ? 55.670 17.585 40.355 1.00   25.96 ? 39   SER A N   1 
ATOM   172  C  CA  . SER A 1 22  ? 56.577 18.723 40.319 1.00   23.56 ? 39   SER A CA  1 
ATOM   173  C  C   . SER A 1 22  ? 55.899 19.851 41.089 1.00   20.64 ? 39   SER A C   1 
ATOM   174  O  O   . SER A 1 22  ? 54.706 19.779 41.384 1.00   19.56 ? 39   SER A O   1 
ATOM   175  C  CB  . SER A 1 22  ? 56.839 19.168 38.880 1.00   25.85 ? 39   SER A CB  1 
ATOM   176  O  OG  . SER A 1 22  ? 55.660 19.683 38.287 1.00   29.75 ? 39   SER A OG  1 
ATOM   177  N  N   . HIS A 1 23  ? 56.662 20.884 41.422 1.00   18.55 ? 40   HIS A N   1 
ATOM   178  C  CA  . HIS A 1 23  ? 56.110 22.017 42.153 1.00   15.78 ? 40   HIS A CA  1 
ATOM   179  C  C   . HIS A 1 23  ? 55.110 22.768 41.283 1.00   14.72 ? 40   HIS A C   1 
ATOM   180  O  O   . HIS A 1 23  ? 55.399 23.063 40.121 1.00   14.35 ? 40   HIS A O   1 
ATOM   181  C  CB  . HIS A 1 23  ? 57.233 22.965 42.573 1.00   15.29 ? 40   HIS A CB  1 
ATOM   182  C  CG  . HIS A 1 23  ? 56.743 24.273 43.112 1.00   14.50 ? 40   HIS A CG  1 
ATOM   183  N  ND1 . HIS A 1 23  ? 56.476 25.359 42.306 1.00   16.92 ? 40   HIS A ND1 1 
ATOM   184  C  CD2 . HIS A 1 23  ? 56.414 24.648 44.370 1.00   12.35 ? 40   HIS A CD2 1 
ATOM   185  C  CE1 . HIS A 1 23  ? 56.003 26.347 43.046 1.00   12.75 ? 40   HIS A CE1 1 
ATOM   186  N  NE2 . HIS A 1 23  ? 55.955 25.940 44.301 1.00   15.59 ? 40   HIS A NE2 1 
ATOM   187  N  N   . PHE A 1 24  ? 53.943 23.090 41.839 1.00   13.10 ? 41   PHE A N   1 
ATOM   188  C  CA  . PHE A 1 24  ? 52.941 23.810 41.062 1.00   13.39 ? 41   PHE A CA  1 
ATOM   189  C  C   . PHE A 1 24  ? 52.283 24.970 41.809 1.00   12.88 ? 41   PHE A C   1 
ATOM   190  O  O   . PHE A 1 24  ? 51.667 25.832 41.192 1.00   15.45 ? 41   PHE A O   1 
ATOM   191  C  CB  . PHE A 1 24  ? 51.874 22.836 40.542 1.00   14.00 ? 41   PHE A CB  1 
ATOM   192  C  CG  . PHE A 1 24  ? 50.935 22.328 41.601 1.00   14.77 ? 41   PHE A CG  1 
ATOM   193  C  CD1 . PHE A 1 24  ? 49.753 23.008 41.887 1.00   16.21 ? 41   PHE A CD1 1 
ATOM   194  C  CD2 . PHE A 1 24  ? 51.229 21.171 42.314 1.00   16.30 ? 41   PHE A CD2 1 
ATOM   195  C  CE1 . PHE A 1 24  ? 48.879 22.543 42.867 1.00   15.75 ? 41   PHE A CE1 1 
ATOM   196  C  CE2 . PHE A 1 24  ? 50.361 20.696 43.297 1.00   16.22 ? 41   PHE A CE2 1 
ATOM   197  C  CZ  . PHE A 1 24  ? 49.184 21.383 43.574 1.00   16.66 ? 41   PHE A CZ  1 
ATOM   198  N  N   . CYS A 1 25  ? 52.422 24.997 43.131 1.00   12.66 ? 42   CYS A N   1 
ATOM   199  C  CA  . CYS A 1 25  ? 51.840 26.067 43.938 1.00   11.34 ? 42   CYS A CA  1 
ATOM   200  C  C   . CYS A 1 25  ? 52.521 26.159 45.293 1.00   11.73 ? 42   CYS A C   1 
ATOM   201  O  O   . CYS A 1 25  ? 53.201 25.232 45.730 1.00   10.92 ? 42   CYS A O   1 
ATOM   202  C  CB  . CYS A 1 25  ? 50.345 25.831 44.181 1.00   13.35 ? 42   CYS A CB  1 
ATOM   203  S  SG  . CYS A 1 25  ? 49.182 26.414 42.903 1.00   14.08 ? 42   CYS A SG  1 
ATOM   204  N  N   . GLY A 1 26  ? 52.325 27.290 45.956 1.00   10.15 ? 43   GLY A N   1 
ATOM   205  C  CA  . GLY A 1 26  ? 52.897 27.466 47.274 1.00   9.82  ? 43   GLY A CA  1 
ATOM   206  C  C   . GLY A 1 26  ? 51.798 27.333 48.311 1.00   11.40 ? 43   GLY A C   1 
ATOM   207  O  O   . GLY A 1 26  ? 50.630 27.108 47.972 1.00   11.41 ? 43   GLY A O   1 
ATOM   208  N  N   . GLY A 1 27  ? 52.174 27.464 49.578 1.00   11.20 ? 44   GLY A N   1 
ATOM   209  C  CA  . GLY A 1 27  ? 51.213 27.371 50.662 1.00   10.84 ? 44   GLY A CA  1 
ATOM   210  C  C   . GLY A 1 27  ? 51.871 27.835 51.948 1.00   10.74 ? 44   GLY A C   1 
ATOM   211  O  O   . GLY A 1 27  ? 53.079 28.084 51.967 1.00   10.78 ? 44   GLY A O   1 
ATOM   212  N  N   . SER A 1 28  ? 51.085 27.939 53.016 1.00   10.47 ? 45   SER A N   1 
ATOM   213  C  CA  . SER A 1 28  ? 51.597 28.381 54.314 1.00   11.64 ? 45   SER A CA  1 
ATOM   214  C  C   . SER A 1 28  ? 51.143 27.449 55.431 1.00   11.75 ? 45   SER A C   1 
ATOM   215  O  O   . SER A 1 28  ? 49.964 27.109 55.518 1.00   11.51 ? 45   SER A O   1 
ATOM   216  C  CB  . SER A 1 28  ? 51.099 29.798 54.624 1.00   11.61 ? 45   SER A CB  1 
ATOM   217  O  OG  . SER A 1 28  ? 51.499 30.714 53.619 1.00   14.45 ? 45   SER A OG  1 
ATOM   218  N  N   . LEU A 1 29  ? 52.076 27.051 56.292 1.00   11.38 ? 46   LEU A N   1 
ATOM   219  C  CA  . LEU A 1 29  ? 51.745 26.173 57.411 1.00   10.89 ? 46   LEU A CA  1 
ATOM   220  C  C   . LEU A 1 29  ? 51.251 27.039 58.574 1.00   11.12 ? 46   LEU A C   1 
ATOM   221  O  O   . LEU A 1 29  ? 52.002 27.870 59.087 1.00   11.43 ? 46   LEU A O   1 
ATOM   222  C  CB  . LEU A 1 29  ? 52.987 25.383 57.845 1.00   11.39 ? 46   LEU A CB  1 
ATOM   223  C  CG  . LEU A 1 29  ? 52.763 24.262 58.867 1.00   12.93 ? 46   LEU A CG  1 
ATOM   224  C  CD1 . LEU A 1 29  ? 52.052 23.091 58.193 1.00   12.06 ? 46   LEU A CD1 1 
ATOM   225  C  CD2 . LEU A 1 29  ? 54.097 23.816 59.439 1.00   12.22 ? 46   LEU A CD2 1 
ATOM   226  N  N   . ILE A 1 30  ? 49.998 26.859 58.991 1.00   12.11 ? 47   ILE A N   1 
ATOM   227  C  CA  . ILE A 1 30  ? 49.463 27.654 60.099 1.00   12.19 ? 47   ILE A CA  1 
ATOM   228  C  C   . ILE A 1 30  ? 49.281 26.838 61.378 1.00   13.95 ? 47   ILE A C   1 
ATOM   229  O  O   . ILE A 1 30  ? 49.042 27.392 62.449 1.00   15.12 ? 47   ILE A O   1 
ATOM   230  C  CB  . ILE A 1 30  ? 48.109 28.317 59.742 1.00   12.85 ? 47   ILE A CB  1 
ATOM   231  C  CG1 . ILE A 1 30  ? 47.069 27.248 59.397 1.00   11.90 ? 47   ILE A CG1 1 
ATOM   232  C  CG2 . ILE A 1 30  ? 48.299 29.290 58.587 1.00   12.45 ? 47   ILE A CG2 1 
ATOM   233  C  CD1 . ILE A 1 30  ? 45.659 27.798 59.248 1.00   17.07 ? 47   ILE A CD1 1 
ATOM   234  N  N   . SER A 1 31  ? 49.392 25.521 61.250 1.00   15.09 ? 48   SER A N   1 
ATOM   235  C  CA  . SER A 1 31  ? 49.279 24.613 62.386 1.00   16.72 ? 48   SER A CA  1 
ATOM   236  C  C   . SER A 1 31  ? 50.069 23.372 61.991 1.00   16.42 ? 48   SER A C   1 
ATOM   237  O  O   . SER A 1 31  ? 50.354 23.172 60.812 1.00   15.70 ? 48   SER A O   1 
ATOM   238  C  CB  . SER A 1 31  ? 47.815 24.256 62.655 1.00   18.97 ? 48   SER A CB  1 
ATOM   239  O  OG  . SER A 1 31  ? 47.688 23.609 63.911 1.00   23.45 ? 48   SER A OG  1 
ATOM   240  N  N   . GLU A 1 32  ? 50.431 22.538 62.961 1.00   17.40 ? 49   GLU A N   1 
ATOM   241  C  CA  . GLU A 1 32  ? 51.218 21.349 62.649 1.00   19.55 ? 49   GLU A CA  1 
ATOM   242  C  C   . GLU A 1 32  ? 50.632 20.461 61.560 1.00   18.88 ? 49   GLU A C   1 
ATOM   243  O  O   . GLU A 1 32  ? 51.376 19.807 60.833 1.00   19.46 ? 49   GLU A O   1 
ATOM   244  C  CB  . GLU A 1 32  ? 51.457 20.508 63.911 1.00   22.78 ? 49   GLU A CB  1 
ATOM   245  C  CG  . GLU A 1 32  ? 52.314 21.198 64.958 1.00   28.77 ? 49   GLU A CG  1 
ATOM   246  C  CD  . GLU A 1 32  ? 51.492 21.845 66.058 1.00   31.75 ? 49   GLU A CD  1 
ATOM   247  O  OE1 . GLU A 1 32  ? 50.509 22.546 65.740 1.00   32.80 ? 49   GLU A OE1 1 
ATOM   248  O  OE2 . GLU A 1 32  ? 51.837 21.653 67.244 1.00   35.20 ? 49   GLU A OE2 1 
ATOM   249  N  N   . GLN A 1 33  ? 49.310 20.450 61.423 1.00   18.45 ? 50   GLN A N   1 
ATOM   250  C  CA  . GLN A 1 33  ? 48.682 19.591 60.428 1.00   19.04 ? 50   GLN A CA  1 
ATOM   251  C  C   . GLN A 1 33  ? 47.843 20.331 59.382 1.00   18.32 ? 50   GLN A C   1 
ATOM   252  O  O   . GLN A 1 33  ? 47.149 19.703 58.583 1.00   17.08 ? 50   GLN A O   1 
ATOM   253  C  CB  . GLN A 1 33  ? 47.822 18.546 61.155 1.00   21.45 ? 50   GLN A CB  1 
ATOM   254  C  CG  . GLN A 1 33  ? 47.459 17.327 60.330 1.00   24.75 ? 50   GLN A CG  1 
ATOM   255  C  CD  . GLN A 1 33  ? 46.926 16.184 61.182 1.00   27.20 ? 50   GLN A CD  1 
ATOM   256  O  OE1 . GLN A 1 33  ? 46.628 15.102 60.671 1.00   29.97 ? 50   GLN A OE1 1 
ATOM   257  N  NE2 . GLN A 1 33  ? 46.806 16.418 62.485 1.00   25.34 ? 50   GLN A NE2 1 
ATOM   258  N  N   . TRP A 1 34  ? 47.926 21.659 59.367 1.00   16.23 ? 51   TRP A N   1 
ATOM   259  C  CA  . TRP A 1 34  ? 47.138 22.440 58.424 1.00   14.62 ? 51   TRP A CA  1 
ATOM   260  C  C   . TRP A 1 34  ? 47.903 23.475 57.603 1.00   15.41 ? 51   TRP A C   1 
ATOM   261  O  O   . TRP A 1 34  ? 48.727 24.225 58.131 1.00   13.35 ? 51   TRP A O   1 
ATOM   262  C  CB  . TRP A 1 34  ? 45.986 23.124 59.164 1.00   17.05 ? 51   TRP A CB  1 
ATOM   263  C  CG  . TRP A 1 34  ? 44.959 22.159 59.673 1.00   17.57 ? 51   TRP A CG  1 
ATOM   264  C  CD1 . TRP A 1 34  ? 44.971 21.488 60.869 1.00   19.60 ? 51   TRP A CD1 1 
ATOM   265  C  CD2 . TRP A 1 34  ? 43.781 21.731 58.983 1.00   18.65 ? 51   TRP A CD2 1 
ATOM   266  N  NE1 . TRP A 1 34  ? 43.865 20.670 60.962 1.00   19.28 ? 51   TRP A NE1 1 
ATOM   267  C  CE2 . TRP A 1 34  ? 43.120 20.800 59.819 1.00   20.62 ? 51   TRP A CE2 1 
ATOM   268  C  CE3 . TRP A 1 34  ? 43.217 22.044 57.738 1.00   19.10 ? 51   TRP A CE3 1 
ATOM   269  C  CZ2 . TRP A 1 34  ? 41.921 20.178 59.447 1.00   19.94 ? 51   TRP A CZ2 1 
ATOM   270  C  CZ3 . TRP A 1 34  ? 42.024 21.427 57.369 1.00   20.80 ? 51   TRP A CZ3 1 
ATOM   271  C  CH2 . TRP A 1 34  ? 41.391 20.503 58.225 1.00   20.58 ? 51   TRP A CH2 1 
ATOM   272  N  N   . VAL A 1 35  ? 47.602 23.503 56.306 1.00   13.67 ? 52   VAL A N   1 
ATOM   273  C  CA  . VAL A 1 35  ? 48.219 24.427 55.355 1.00   13.26 ? 52   VAL A CA  1 
ATOM   274  C  C   . VAL A 1 35  ? 47.150 25.270 54.658 1.00   13.32 ? 52   VAL A C   1 
ATOM   275  O  O   . VAL A 1 35  ? 46.072 24.771 54.326 1.00   13.52 ? 52   VAL A O   1 
ATOM   276  C  CB  . VAL A 1 35  ? 49.010 23.654 54.266 1.00   14.26 ? 52   VAL A CB  1 
ATOM   277  C  CG1 . VAL A 1 35  ? 49.384 24.588 53.111 1.00   14.99 ? 52   VAL A CG1 1 
ATOM   278  C  CG2 . VAL A 1 35  ? 50.256 23.033 54.873 1.00   15.29 ? 52   VAL A CG2 1 
ATOM   279  N  N   . VAL A 1 36  ? 47.448 26.551 54.451 1.00   11.88 ? 53   VAL A N   1 
ATOM   280  C  CA  . VAL A 1 36  ? 46.531 27.453 53.755 1.00   12.67 ? 53   VAL A CA  1 
ATOM   281  C  C   . VAL A 1 36  ? 47.111 27.698 52.366 1.00   11.69 ? 53   VAL A C   1 
ATOM   282  O  O   . VAL A 1 36  ? 48.318 27.901 52.225 1.00   11.78 ? 53   VAL A O   1 
ATOM   283  C  CB  . VAL A 1 36  ? 46.409 28.822 54.467 1.00   12.76 ? 53   VAL A CB  1 
ATOM   284  C  CG1 . VAL A 1 36  ? 45.602 29.792 53.602 1.00   14.97 ? 53   VAL A CG1 1 
ATOM   285  C  CG2 . VAL A 1 36  ? 45.743 28.649 55.825 1.00   14.99 ? 53   VAL A CG2 1 
ATOM   286  N  N   . SER A 1 37  ? 46.261 27.669 51.344 1.00   11.50 ? 54   SER A N   1 
ATOM   287  C  CA  . SER A 1 37  ? 46.709 27.911 49.975 1.00   11.57 ? 54   SER A CA  1 
ATOM   288  C  C   . SER A 1 37  ? 45.550 28.534 49.195 1.00   12.29 ? 54   SER A C   1 
ATOM   289  O  O   . SER A 1 37  ? 44.562 28.965 49.792 1.00   12.88 ? 54   SER A O   1 
ATOM   290  C  CB  . SER A 1 37  ? 47.164 26.594 49.321 1.00   12.12 ? 54   SER A CB  1 
ATOM   291  O  OG  . SER A 1 37  ? 47.766 26.807 48.053 1.00   12.34 ? 54   SER A OG  1 
ATOM   292  N  N   . ALA A 1 38  ? 45.677 28.596 47.874 1.00   11.74 ? 55   ALA A N   1 
ATOM   293  C  CA  . ALA A 1 38  ? 44.631 29.168 47.033 1.00   12.75 ? 55   ALA A CA  1 
ATOM   294  C  C   . ALA A 1 38  ? 43.755 28.052 46.488 1.00   14.67 ? 55   ALA A C   1 
ATOM   295  O  O   . ALA A 1 38  ? 44.249 26.970 46.174 1.00   14.88 ? 55   ALA A O   1 
ATOM   296  C  CB  . ALA A 1 38  ? 45.253 29.950 45.882 1.00   11.19 ? 55   ALA A CB  1 
ATOM   297  N  N   . ALA A 1 39  ? 42.456 28.317 46.376 1.00   15.26 ? 56   ALA A N   1 
ATOM   298  C  CA  . ALA A 1 39  ? 41.528 27.318 45.864 1.00   17.12 ? 56   ALA A CA  1 
ATOM   299  C  C   . ALA A 1 39  ? 41.829 26.952 44.409 1.00   17.65 ? 56   ALA A C   1 
ATOM   300  O  O   . ALA A 1 39  ? 41.559 25.826 43.985 1.00   17.80 ? 56   ALA A O   1 
ATOM   301  C  CB  . ALA A 1 39  ? 40.088 27.823 45.996 1.00   17.16 ? 56   ALA A CB  1 
ATOM   302  N  N   . HIS A 1 40  ? 42.391 27.880 43.637 1.00   16.97 ? 57   HIS A N   1 
ATOM   303  C  CA  . HIS A 1 40  ? 42.677 27.553 42.247 1.00   18.32 ? 57   HIS A CA  1 
ATOM   304  C  C   . HIS A 1 40  ? 43.861 26.599 42.113 1.00   18.88 ? 57   HIS A C   1 
ATOM   305  O  O   . HIS A 1 40  ? 44.190 26.157 41.014 1.00   20.75 ? 57   HIS A O   1 
ATOM   306  C  CB  . HIS A 1 40  ? 42.876 28.821 41.394 1.00   18.45 ? 57   HIS A CB  1 
ATOM   307  C  CG  . HIS A 1 40  ? 44.219 29.469 41.534 1.00   21.01 ? 57   HIS A CG  1 
ATOM   308  N  ND1 . HIS A 1 40  ? 44.456 30.518 42.397 1.00   20.68 ? 57   HIS A ND1 1 
ATOM   309  C  CD2 . HIS A 1 40  ? 45.382 29.255 40.874 1.00   20.63 ? 57   HIS A CD2 1 
ATOM   310  C  CE1 . HIS A 1 40  ? 45.706 30.924 42.261 1.00   20.88 ? 57   HIS A CE1 1 
ATOM   311  N  NE2 . HIS A 1 40  ? 46.289 30.175 41.343 1.00   22.31 ? 57   HIS A NE2 1 
ATOM   312  N  N   . CYS A 1 41  ? 44.485 26.270 43.242 1.00   18.08 ? 58   CYS A N   1 
ATOM   313  C  CA  . CYS A 1 41  ? 45.612 25.339 43.263 1.00   17.88 ? 58   CYS A CA  1 
ATOM   314  C  C   . CYS A 1 41  ? 45.112 23.931 43.567 1.00   19.29 ? 58   CYS A C   1 
ATOM   315  O  O   . CYS A 1 41  ? 45.902 23.013 43.784 1.00   19.42 ? 58   CYS A O   1 
ATOM   316  C  CB  . CYS A 1 41  ? 46.615 25.729 44.344 1.00   17.29 ? 58   CYS A CB  1 
ATOM   317  S  SG  . CYS A 1 41  ? 47.638 27.184 43.975 1.00   16.29 ? 58   CYS A SG  1 
ATOM   318  N  N   . TYR A 1 42  ? 43.796 23.769 43.599 1.00   19.93 ? 59   TYR A N   1 
ATOM   319  C  CA  . TYR A 1 42  ? 43.206 22.475 43.906 1.00   22.63 ? 59   TYR A CA  1 
ATOM   320  C  C   . TYR A 1 42  ? 43.585 21.357 42.938 1.00   22.62 ? 59   TYR A C   1 
ATOM   321  O  O   . TYR A 1 42  ? 43.655 21.557 41.727 1.00   22.66 ? 59   TYR A O   1 
ATOM   322  C  CB  . TYR A 1 42  ? 41.680 22.588 43.956 1.00   23.93 ? 59   TYR A CB  1 
ATOM   323  C  CG  . TYR A 1 42  ? 40.999 21.278 44.275 1.00   27.27 ? 59   TYR A CG  1 
ATOM   324  C  CD1 . TYR A 1 42  ? 40.958 20.793 45.580 1.00   27.79 ? 59   TYR A CD1 1 
ATOM   325  C  CD2 . TYR A 1 42  ? 40.429 20.503 43.265 1.00   28.28 ? 59   TYR A CD2 1 
ATOM   326  C  CE1 . TYR A 1 42  ? 40.365 19.566 45.875 1.00   30.04 ? 59   TYR A CE1 1 
ATOM   327  C  CE2 . TYR A 1 42  ? 39.835 19.276 43.547 1.00   29.34 ? 59   TYR A CE2 1 
ATOM   328  C  CZ  . TYR A 1 42  ? 39.807 18.813 44.852 1.00   30.54 ? 59   TYR A CZ  1 
ATOM   329  O  OH  . TYR A 1 42  ? 39.225 17.598 45.135 1.00   31.78 ? 59   TYR A OH  1 
ATOM   330  N  N   . LYS A 1 43  ? 43.838 20.183 43.506 1.00   24.47 ? 60   LYS A N   1 
ATOM   331  C  CA  . LYS A 1 43  ? 44.167 18.974 42.760 1.00   26.17 ? 60   LYS A CA  1 
ATOM   332  C  C   . LYS A 1 43  ? 43.748 17.799 43.634 1.00   27.94 ? 60   LYS A C   1 
ATOM   333  O  O   . LYS A 1 43  ? 43.835 17.871 44.859 1.00   27.28 ? 60   LYS A O   1 
ATOM   334  C  CB  . LYS A 1 43  ? 45.662 18.887 42.453 1.00   26.83 ? 60   LYS A CB  1 
ATOM   335  C  CG  . LYS A 1 43  ? 46.104 19.776 41.311 1.00   27.37 ? 60   LYS A CG  1 
ATOM   336  C  CD  . LYS A 1 43  ? 47.498 19.414 40.838 1.00   30.41 ? 60   LYS A CD  1 
ATOM   337  C  CE  . LYS A 1 43  ? 47.888 20.239 39.625 1.00   31.18 ? 60   LYS A CE  1 
ATOM   338  N  NZ  . LYS A 1 43  ? 49.225 19.847 39.098 1.00   34.90 ? 60   LYS A NZ  1 
ATOM   339  N  N   . THR A 1 44  ? 43.286 16.725 43.002 1.00   29.04 ? 61   THR A N   1 
ATOM   340  C  CA  . THR A 1 44  ? 42.834 15.541 43.726 1.00   31.15 ? 61   THR A CA  1 
ATOM   341  C  C   . THR A 1 44  ? 43.890 14.981 44.674 1.00   29.85 ? 61   THR A C   1 
ATOM   342  O  O   . THR A 1 44  ? 43.586 14.612 45.811 1.00   30.58 ? 61   THR A O   1 
ATOM   343  C  CB  . THR A 1 44  ? 42.419 14.429 42.744 1.00   32.25 ? 61   THR A CB  1 
ATOM   344  O  OG1 . THR A 1 44  ? 41.408 14.929 41.859 1.00   35.97 ? 61   THR A OG1 1 
ATOM   345  C  CG2 . THR A 1 44  ? 41.878 13.227 43.502 1.00   34.60 ? 61   THR A CG2 1 
ATOM   346  N  N   . ARG A 1 45  ? 45.129 14.909 44.200 1.00   28.85 ? 62   ARG A N   1 
ATOM   347  C  CA  . ARG A 1 45  ? 46.226 14.388 45.005 1.00   28.54 ? 62   ARG A CA  1 
ATOM   348  C  C   . ARG A 1 45  ? 47.307 15.457 45.141 1.00   27.25 ? 62   ARG A C   1 
ATOM   349  O  O   . ARG A 1 45  ? 47.748 16.031 44.145 1.00   26.98 ? 62   ARG A O   1 
ATOM   350  C  CB  . ARG A 1 45  ? 46.810 13.137 44.340 1.00   30.58 ? 62   ARG A CB  1 
ATOM   351  C  CG  . ARG A 1 45  ? 47.778 12.353 45.211 1.00   33.08 ? 62   ARG A CG  1 
ATOM   352  C  CD  . ARG A 1 45  ? 47.076 11.661 46.377 0.0000 32.82 ? 62   ARG A CD  1 
ATOM   353  N  NE  . ARG A 1 45  ? 46.199 10.573 45.947 0.0000 33.36 ? 62   ARG A NE  1 
ATOM   354  C  CZ  . ARG A 1 45  ? 44.963 10.733 45.482 0.0000 33.49 ? 62   ARG A CZ  1 
ATOM   355  N  NH1 . ARG A 1 45  ? 44.434 11.944 45.381 0.0000 33.64 ? 62   ARG A NH1 1 
ATOM   356  N  NH2 . ARG A 1 45  ? 44.252 9.675  45.114 0.0000 33.64 ? 62   ARG A NH2 1 
ATOM   357  N  N   . ILE A 1 46  ? 47.731 15.724 46.374 1.00   25.24 ? 63   ILE A N   1 
ATOM   358  C  CA  . ILE A 1 46  ? 48.758 16.732 46.620 1.00   22.74 ? 63   ILE A CA  1 
ATOM   359  C  C   . ILE A 1 46  ? 49.745 16.314 47.699 1.00   21.11 ? 63   ILE A C   1 
ATOM   360  O  O   . ILE A 1 46  ? 49.347 15.879 48.779 1.00   22.57 ? 63   ILE A O   1 
ATOM   361  C  CB  . ILE A 1 46  ? 48.137 18.081 47.077 1.00   22.83 ? 63   ILE A CB  1 
ATOM   362  C  CG1 . ILE A 1 46  ? 47.229 18.644 45.985 1.00   22.07 ? 63   ILE A CG1 1 
ATOM   363  C  CG2 . ILE A 1 46  ? 49.241 19.074 47.425 1.00   22.45 ? 63   ILE A CG2 1 
ATOM   364  C  CD1 . ILE A 1 46  ? 46.549 19.939 46.367 1.00   23.10 ? 63   ILE A CD1 1 
ATOM   365  N  N   . GLN A 1 47  ? 51.033 16.439 47.402 1.00   19.04 ? 64   GLN A N   1 
ATOM   366  C  CA  . GLN A 1 47  ? 52.055 16.130 48.394 1.00   20.02 ? 64   GLN A CA  1 
ATOM   367  C  C   . GLN A 1 47  ? 52.589 17.478 48.863 1.00   19.14 ? 64   GLN A C   1 
ATOM   368  O  O   . GLN A 1 47  ? 52.970 18.314 48.044 1.00   19.22 ? 64   GLN A O   1 
ATOM   369  C  CB  . GLN A 1 47  ? 53.203 15.314 47.794 1.00   21.18 ? 64   GLN A CB  1 
ATOM   370  C  CG  . GLN A 1 47  ? 54.270 14.949 48.828 1.00   24.04 ? 64   GLN A CG  1 
ATOM   371  C  CD  . GLN A 1 47  ? 55.423 14.149 48.249 1.00   24.94 ? 64   GLN A CD  1 
ATOM   372  O  OE1 . GLN A 1 47  ? 56.179 14.641 47.413 1.00   27.94 ? 64   GLN A OE1 1 
ATOM   373  N  NE2 . GLN A 1 47  ? 55.563 12.905 48.696 1.00   28.78 ? 64   GLN A NE2 1 
ATOM   374  N  N   . VAL A 1 48  ? 52.601 17.689 50.172 1.00   18.25 ? 65   VAL A N   1 
ATOM   375  C  CA  . VAL A 1 48  ? 53.092 18.939 50.739 1.00   16.79 ? 65   VAL A CA  1 
ATOM   376  C  C   . VAL A 1 48  ? 54.554 18.771 51.123 1.00   17.17 ? 65   VAL A C   1 
ATOM   377  O  O   . VAL A 1 48  ? 54.915 17.843 51.846 1.00   17.93 ? 65   VAL A O   1 
ATOM   378  C  CB  . VAL A 1 48  ? 52.274 19.340 51.990 1.00   17.66 ? 65   VAL A CB  1 
ATOM   379  C  CG1 . VAL A 1 48  ? 52.837 20.618 52.599 1.00   18.92 ? 65   VAL A CG1 1 
ATOM   380  C  CG2 . VAL A 1 48  ? 50.812 19.530 51.614 1.00   18.12 ? 65   VAL A CG2 1 
ATOM   381  N  N   . ARG A 1 49  ? 55.400 19.667 50.627 1.00   15.31 ? 66   ARG A N   1 
ATOM   382  C  CA  . ARG A 1 49  ? 56.824 19.599 50.922 1.00   13.97 ? 66   ARG A CA  1 
ATOM   383  C  C   . ARG A 1 49  ? 57.258 20.765 51.800 1.00   15.68 ? 66   ARG A C   1 
ATOM   384  O  O   . ARG A 1 49  ? 57.237 21.925 51.380 1.00   16.23 ? 66   ARG A O   1 
ATOM   385  C  CB  . ARG A 1 49  ? 57.622 19.559 49.617 1.00   14.33 ? 66   ARG A CB  1 
ATOM   386  C  CG  . ARG A 1 49  ? 57.265 18.337 48.771 1.00   14.25 ? 66   ARG A CG  1 
ATOM   387  C  CD  . ARG A 1 49  ? 58.231 18.096 47.633 1.00   17.80 ? 66   ARG A CD  1 
ATOM   388  N  NE  . ARG A 1 49  ? 57.965 16.804 46.997 1.00   19.79 ? 66   ARG A NE  1 
ATOM   389  C  CZ  . ARG A 1 49  ? 58.767 16.223 46.109 1.00   21.74 ? 66   ARG A CZ  1 
ATOM   390  N  NH1 . ARG A 1 49  ? 59.896 16.812 45.741 1.00   22.85 ? 66   ARG A NH1 1 
ATOM   391  N  NH2 . ARG A 1 49  ? 58.440 15.044 45.592 1.00   21.86 ? 66   ARG A NH2 1 
ATOM   392  N  N   . LEU A 1 50  ? 57.650 20.435 53.027 1.00   13.58 ? 67   LEU A N   1 
ATOM   393  C  CA  . LEU A 1 50  ? 58.069 21.425 54.009 1.00   14.22 ? 67   LEU A CA  1 
ATOM   394  C  C   . LEU A 1 50  ? 59.582 21.432 54.203 1.00   14.65 ? 67   LEU A C   1 
ATOM   395  O  O   . LEU A 1 50  ? 60.266 20.471 53.844 1.00   15.99 ? 67   LEU A O   1 
ATOM   396  C  CB  . LEU A 1 50  ? 57.381 21.141 55.350 1.00   14.99 ? 67   LEU A CB  1 
ATOM   397  C  CG  . LEU A 1 50  ? 55.853 21.015 55.308 1.00   17.21 ? 67   LEU A CG  1 
ATOM   398  C  CD1 . LEU A 1 50  ? 55.459 19.576 54.997 1.00   20.72 ? 67   LEU A CD1 1 
ATOM   399  C  CD2 . LEU A 1 50  ? 55.268 21.437 56.645 1.00   20.86 ? 67   LEU A CD2 1 
ATOM   400  N  N   . GLY A 1 51  ? 60.094 22.521 54.773 1.00   14.38 ? 69   GLY A N   1 
ATOM   401  C  CA  . GLY A 1 51  ? 61.523 22.641 55.022 1.00   14.50 ? 69   GLY A CA  1 
ATOM   402  C  C   . GLY A 1 51  ? 62.378 22.718 53.772 1.00   14.83 ? 69   GLY A C   1 
ATOM   403  O  O   . GLY A 1 51  ? 63.558 22.370 53.792 1.00   16.76 ? 69   GLY A O   1 
ATOM   404  N  N   . GLU A 1 52  ? 61.789 23.199 52.685 1.00   13.65 ? 70   GLU A N   1 
ATOM   405  C  CA  . GLU A 1 52  ? 62.486 23.310 51.409 1.00   13.98 ? 70   GLU A CA  1 
ATOM   406  C  C   . GLU A 1 52  ? 63.157 24.646 51.141 1.00   15.65 ? 70   GLU A C   1 
ATOM   407  O  O   . GLU A 1 52  ? 62.730 25.690 51.639 1.00   15.31 ? 70   GLU A O   1 
ATOM   408  C  CB  . GLU A 1 52  ? 61.501 23.059 50.261 1.00   14.17 ? 70   GLU A CB  1 
ATOM   409  C  CG  . GLU A 1 52  ? 61.075 21.620 50.099 1.00   16.71 ? 70   GLU A CG  1 
ATOM   410  C  CD  . GLU A 1 52  ? 62.031 20.846 49.223 1.00   16.93 ? 70   GLU A CD  1 
ATOM   411  O  OE1 . GLU A 1 52  ? 63.223 21.220 49.174 1.00   16.73 ? 70   GLU A OE1 1 
ATOM   412  O  OE2 . GLU A 1 52  ? 61.590 19.865 48.593 1.00   18.68 ? 70   GLU A OE2 1 
ATOM   413  N  N   . HIS A 1 53  ? 64.225 24.590 50.352 1.00   16.26 ? 71   HIS A N   1 
ATOM   414  C  CA  . HIS A 1 53  ? 64.912 25.787 49.887 1.00   15.38 ? 71   HIS A CA  1 
ATOM   415  C  C   . HIS A 1 53  ? 65.137 25.538 48.399 1.00   16.07 ? 71   HIS A C   1 
ATOM   416  O  O   . HIS A 1 53  ? 64.576 26.233 47.558 1.00   14.81 ? 71   HIS A O   1 
ATOM   417  C  CB  . HIS A 1 53  ? 66.252 26.035 50.570 1.00   16.35 ? 71   HIS A CB  1 
ATOM   418  C  CG  . HIS A 1 53  ? 66.881 27.325 50.143 1.00   18.83 ? 71   HIS A CG  1 
ATOM   419  N  ND1 . HIS A 1 53  ? 68.102 27.388 49.507 1.00   21.80 ? 71   HIS A ND1 1 
ATOM   420  C  CD2 . HIS A 1 53  ? 66.399 28.591 50.157 1.00   17.01 ? 71   HIS A CD2 1 
ATOM   421  C  CE1 . HIS A 1 53  ? 68.341 28.635 49.141 1.00   18.99 ? 71   HIS A CE1 1 
ATOM   422  N  NE2 . HIS A 1 53  ? 67.323 29.384 49.522 1.00   21.16 ? 71   HIS A NE2 1 
ATOM   423  N  N   . ASN A 1 54  ? 65.958 24.538 48.079 1.00   16.18 ? 72   ASN A N   1 
ATOM   424  C  CA  . ASN A 1 54  ? 66.206 24.168 46.687 1.00   16.41 ? 72   ASN A CA  1 
ATOM   425  C  C   . ASN A 1 54  ? 65.263 22.989 46.450 1.00   16.72 ? 72   ASN A C   1 
ATOM   426  O  O   . ASN A 1 54  ? 65.479 21.902 46.989 1.00   16.93 ? 72   ASN A O   1 
ATOM   427  C  CB  . ASN A 1 54  ? 67.661 23.728 46.493 1.00   17.18 ? 72   ASN A CB  1 
ATOM   428  C  CG  . ASN A 1 54  ? 67.994 23.446 45.039 1.00   17.73 ? 72   ASN A CG  1 
ATOM   429  O  OD1 . ASN A 1 54  ? 67.233 22.784 44.335 1.00   18.77 ? 72   ASN A OD1 1 
ATOM   430  N  ND2 . ASN A 1 54  ? 69.143 23.939 44.587 1.00   19.70 ? 72   ASN A ND2 1 
ATOM   431  N  N   . ILE A 1 55  ? 64.212 23.202 45.663 1.00   17.73 ? 73   ILE A N   1 
ATOM   432  C  CA  . ILE A 1 55  ? 63.231 22.148 45.417 1.00   19.43 ? 73   ILE A CA  1 
ATOM   433  C  C   . ILE A 1 55  ? 63.676 20.999 44.521 1.00   19.85 ? 73   ILE A C   1 
ATOM   434  O  O   . ILE A 1 55  ? 62.944 20.023 44.365 1.00   21.06 ? 73   ILE A O   1 
ATOM   435  C  CB  . ILE A 1 55  ? 61.913 22.723 44.842 1.00   19.02 ? 73   ILE A CB  1 
ATOM   436  C  CG1 . ILE A 1 55  ? 62.208 23.652 43.664 1.00   19.17 ? 73   ILE A CG1 1 
ATOM   437  C  CG2 . ILE A 1 55  ? 61.135 23.435 45.943 1.00   20.87 ? 73   ILE A CG2 1 
ATOM   438  C  CD1 . ILE A 1 55  ? 60.958 24.146 42.956 1.00   21.03 ? 73   ILE A CD1 1 
ATOM   439  N  N   . LYS A 1 56  ? 64.869 21.103 43.943 1.00   21.13 ? 74   LYS A N   1 
ATOM   440  C  CA  . LYS A 1 56  ? 65.375 20.046 43.069 1.00   22.03 ? 74   LYS A CA  1 
ATOM   441  C  C   . LYS A 1 56  ? 66.420 19.162 43.742 1.00   22.86 ? 74   LYS A C   1 
ATOM   442  O  O   . LYS A 1 56  ? 66.719 18.070 43.257 1.00   25.09 ? 74   LYS A O   1 
ATOM   443  C  CB  . LYS A 1 56  ? 65.978 20.652 41.795 1.00   22.79 ? 74   LYS A CB  1 
ATOM   444  C  CG  . LYS A 1 56  ? 64.960 21.255 40.836 1.00   24.68 ? 74   LYS A CG  1 
ATOM   445  C  CD  . LYS A 1 56  ? 63.989 20.207 40.316 0.0000 24.19 ? 74   LYS A CD  1 
ATOM   446  C  CE  . LYS A 1 56  ? 63.019 20.807 39.311 0.0000 24.42 ? 74   LYS A CE  1 
ATOM   447  N  NZ  . LYS A 1 56  ? 62.230 21.925 39.898 0.0000 24.40 ? 74   LYS A NZ  1 
ATOM   448  N  N   . VAL A 1 57  ? 66.967 19.623 44.860 1.00   21.77 ? 75   VAL A N   1 
ATOM   449  C  CA  . VAL A 1 57  ? 68.001 18.870 45.562 1.00   23.69 ? 75   VAL A CA  1 
ATOM   450  C  C   . VAL A 1 57  ? 67.654 18.540 47.007 1.00   23.69 ? 75   VAL A C   1 
ATOM   451  O  O   . VAL A 1 57  ? 67.113 19.378 47.728 1.00   21.56 ? 75   VAL A O   1 
ATOM   452  C  CB  . VAL A 1 57  ? 69.333 19.656 45.561 1.00   24.20 ? 75   VAL A CB  1 
ATOM   453  C  CG1 . VAL A 1 57  ? 70.398 18.894 46.334 1.00   25.87 ? 75   VAL A CG1 1 
ATOM   454  C  CG2 . VAL A 1 57  ? 69.781 19.911 44.131 1.00   26.91 ? 75   VAL A CG2 1 
ATOM   455  N  N   . LEU A 1 58  ? 67.965 17.315 47.430 1.00   22.97 ? 76   LEU A N   1 
ATOM   456  C  CA  . LEU A 1 58  ? 67.717 16.914 48.810 1.00   24.52 ? 76   LEU A CA  1 
ATOM   457  C  C   . LEU A 1 58  ? 68.769 17.601 49.669 1.00   24.60 ? 76   LEU A C   1 
ATOM   458  O  O   . LEU A 1 58  ? 69.969 17.427 49.454 1.00   24.75 ? 76   LEU A O   1 
ATOM   459  C  CB  . LEU A 1 58  ? 67.829 15.397 48.971 1.00   26.59 ? 76   LEU A CB  1 
ATOM   460  C  CG  . LEU A 1 58  ? 66.628 14.572 48.511 1.00   28.75 ? 76   LEU A CG  1 
ATOM   461  C  CD1 . LEU A 1 58  ? 66.925 13.091 48.703 1.00   30.34 ? 76   LEU A CD1 1 
ATOM   462  C  CD2 . LEU A 1 58  ? 65.395 14.975 49.311 1.00   30.04 ? 76   LEU A CD2 1 
ATOM   463  N  N   . GLU A 1 59  ? 68.311 18.380 50.641 1.00   23.37 ? 77   GLU A N   1 
ATOM   464  C  CA  . GLU A 1 59  ? 69.203 19.120 51.518 1.00   24.82 ? 77   GLU A CA  1 
ATOM   465  C  C   . GLU A 1 59  ? 69.282 18.529 52.921 1.00   25.24 ? 77   GLU A C   1 
ATOM   466  O  O   . GLU A 1 59  ? 70.201 18.839 53.679 1.00   26.19 ? 77   GLU A O   1 
ATOM   467  C  CB  . GLU A 1 59  ? 68.748 20.581 51.563 1.00   25.55 ? 77   GLU A CB  1 
ATOM   468  C  CG  . GLU A 1 59  ? 68.766 21.228 50.182 1.00   25.44 ? 77   GLU A CG  1 
ATOM   469  C  CD  . GLU A 1 59  ? 67.746 22.338 50.026 1.00   26.01 ? 77   GLU A CD  1 
ATOM   470  O  OE1 . GLU A 1 59  ? 66.528 22.053 50.121 1.00   22.97 ? 77   GLU A OE1 1 
ATOM   471  O  OE2 . GLU A 1 59  ? 68.166 23.492 49.803 1.00   25.66 ? 77   GLU A OE2 1 
ATOM   472  N  N   . GLY A 1 60  ? 68.316 17.682 53.264 1.00   26.10 ? 78   GLY A N   1 
ATOM   473  C  CA  . GLY A 1 60  ? 68.324 17.050 54.571 1.00   26.97 ? 78   GLY A CA  1 
ATOM   474  C  C   . GLY A 1 60  ? 67.352 17.594 55.600 1.00   27.39 ? 78   GLY A C   1 
ATOM   475  O  O   . GLY A 1 60  ? 67.227 17.029 56.687 1.00   28.86 ? 78   GLY A O   1 
ATOM   476  N  N   . ASN A 1 61  ? 66.658 18.679 55.276 1.00   25.68 ? 79   ASN A N   1 
ATOM   477  C  CA  . ASN A 1 61  ? 65.710 19.262 56.216 1.00   25.43 ? 79   ASN A CA  1 
ATOM   478  C  C   . ASN A 1 61  ? 64.269 19.149 55.739 1.00   23.34 ? 79   ASN A C   1 
ATOM   479  O  O   . ASN A 1 61  ? 63.348 19.605 56.415 1.00   22.14 ? 79   ASN A O   1 
ATOM   480  C  CB  . ASN A 1 61  ? 66.049 20.733 56.457 1.00   28.14 ? 79   ASN A CB  1 
ATOM   481  C  CG  . ASN A 1 61  ? 67.450 20.922 56.991 1.00   31.08 ? 79   ASN A CG  1 
ATOM   482  O  OD1 . ASN A 1 61  ? 67.810 20.366 58.031 1.00   33.42 ? 79   ASN A OD1 1 
ATOM   483  N  ND2 . ASN A 1 61  ? 68.251 21.712 56.286 1.00   33.47 ? 79   ASN A ND2 1 
ATOM   484  N  N   . GLU A 1 62  ? 64.074 18.528 54.582 1.00   21.73 ? 80   GLU A N   1 
ATOM   485  C  CA  . GLU A 1 62  ? 62.737 18.384 54.026 1.00   20.96 ? 80   GLU A CA  1 
ATOM   486  C  C   . GLU A 1 62  ? 61.849 17.388 54.747 1.00   21.43 ? 80   GLU A C   1 
ATOM   487  O  O   . GLU A 1 62  ? 62.321 16.442 55.383 1.00   22.09 ? 80   GLU A O   1 
ATOM   488  C  CB  . GLU A 1 62  ? 62.805 17.974 52.552 1.00   21.47 ? 80   GLU A CB  1 
ATOM   489  C  CG  . GLU A 1 62  ? 63.584 18.926 51.675 1.00   21.11 ? 80   GLU A CG  1 
ATOM   490  C  CD  . GLU A 1 62  ? 65.025 18.498 51.472 1.00   21.01 ? 80   GLU A CD  1 
ATOM   491  O  OE1 . GLU A 1 62  ? 65.573 17.766 52.327 1.00   22.79 ? 80   GLU A OE1 1 
ATOM   492  O  OE2 . GLU A 1 62  ? 65.613 18.911 50.454 1.00   19.63 ? 80   GLU A OE2 1 
ATOM   493  N  N   . GLN A 1 63  ? 60.550 17.624 54.633 1.00   19.10 ? 81   GLN A N   1 
ATOM   494  C  CA  . GLN A 1 63  ? 59.534 16.749 55.189 1.00   18.68 ? 81   GLN A CA  1 
ATOM   495  C  C   . GLN A 1 63  ? 58.477 16.655 54.095 1.00   19.58 ? 81   GLN A C   1 
ATOM   496  O  O   . GLN A 1 63  ? 57.865 17.662 53.732 1.00   18.67 ? 81   GLN A O   1 
ATOM   497  C  CB  . GLN A 1 63  ? 58.925 17.338 56.462 1.00   18.58 ? 81   GLN A CB  1 
ATOM   498  C  CG  . GLN A 1 63  ? 59.837 17.294 57.678 1.00   17.92 ? 81   GLN A CG  1 
ATOM   499  C  CD  . GLN A 1 63  ? 59.140 17.774 58.938 1.00   18.58 ? 81   GLN A CD  1 
ATOM   500  O  OE1 . GLN A 1 63  ? 58.052 17.305 59.273 1.00   18.94 ? 81   GLN A OE1 1 
ATOM   501  N  NE2 . GLN A 1 63  ? 59.766 18.709 59.645 1.00   19.36 ? 81   GLN A NE2 1 
ATOM   502  N  N   . PHE A 1 64  ? 58.296 15.461 53.538 1.00   18.17 ? 82   PHE A N   1 
ATOM   503  C  CA  . PHE A 1 64  ? 57.298 15.260 52.495 1.00   20.53 ? 82   PHE A CA  1 
ATOM   504  C  C   . PHE A 1 64  ? 56.108 14.567 53.135 1.00   21.09 ? 82   PHE A C   1 
ATOM   505  O  O   . PHE A 1 64  ? 56.238 13.465 53.670 1.00   22.07 ? 82   PHE A O   1 
ATOM   506  C  CB  . PHE A 1 64  ? 57.848 14.391 51.355 1.00   20.89 ? 82   PHE A CB  1 
ATOM   507  C  CG  . PHE A 1 64  ? 59.026 14.990 50.629 1.00   22.90 ? 82   PHE A CG  1 
ATOM   508  C  CD1 . PHE A 1 64  ? 59.331 16.345 50.742 1.00   23.25 ? 82   PHE A CD1 1 
ATOM   509  C  CD2 . PHE A 1 64  ? 59.821 14.195 49.808 1.00   24.77 ? 82   PHE A CD2 1 
ATOM   510  C  CE1 . PHE A 1 64  ? 60.409 16.896 50.047 1.00   24.01 ? 82   PHE A CE1 1 
ATOM   511  C  CE2 . PHE A 1 64  ? 60.899 14.737 49.110 1.00   24.70 ? 82   PHE A CE2 1 
ATOM   512  C  CZ  . PHE A 1 64  ? 61.192 16.090 49.230 1.00   24.37 ? 82   PHE A CZ  1 
ATOM   513  N  N   . ILE A 1 65  ? 54.950 15.214 53.078 1.00   19.60 ? 83   ILE A N   1 
ATOM   514  C  CA  . ILE A 1 65  ? 53.738 14.668 53.676 1.00   20.08 ? 83   ILE A CA  1 
ATOM   515  C  C   . ILE A 1 65  ? 52.550 14.820 52.731 1.00   20.44 ? 83   ILE A C   1 
ATOM   516  O  O   . ILE A 1 65  ? 52.269 15.912 52.239 1.00   20.38 ? 83   ILE A O   1 
ATOM   517  C  CB  . ILE A 1 65  ? 53.422 15.390 55.007 1.00   18.37 ? 83   ILE A CB  1 
ATOM   518  C  CG1 . ILE A 1 65  ? 54.645 15.333 55.930 1.00   19.38 ? 83   ILE A CG1 1 
ATOM   519  C  CG2 . ILE A 1 65  ? 52.212 14.750 55.677 1.00   21.33 ? 83   ILE A CG2 1 
ATOM   520  C  CD1 . ILE A 1 65  ? 54.516 16.159 57.191 1.00   19.26 ? 83   ILE A CD1 1 
ATOM   521  N  N   . ASN A 1 66  ? 51.847 13.721 52.473 1.00   21.20 ? 84   ASN A N   1 
ATOM   522  C  CA  . ASN A 1 66  ? 50.693 13.775 51.584 1.00   22.38 ? 84   ASN A CA  1 
ATOM   523  C  C   . ASN A 1 66  ? 49.496 14.410 52.272 1.00   21.70 ? 84   ASN A C   1 
ATOM   524  O  O   . ASN A 1 66  ? 49.332 14.296 53.485 1.00   22.12 ? 84   ASN A O   1 
ATOM   525  C  CB  . ASN A 1 66  ? 50.300 12.372 51.114 1.00   24.86 ? 84   ASN A CB  1 
ATOM   526  C  CG  . ASN A 1 66  ? 51.357 11.733 50.249 1.00   28.51 ? 84   ASN A CG  1 
ATOM   527  O  OD1 . ASN A 1 66  ? 51.882 12.359 49.326 1.00   28.90 ? 84   ASN A OD1 1 
ATOM   528  N  ND2 . ASN A 1 66  ? 51.667 10.473 50.531 1.00   31.32 ? 84   ASN A ND2 1 
ATOM   529  N  N   . ALA A 1 67  ? 48.660 15.082 51.489 1.00   22.31 ? 85   ALA A N   1 
ATOM   530  C  CA  . ALA A 1 67  ? 47.463 15.709 52.031 1.00   23.11 ? 85   ALA A CA  1 
ATOM   531  C  C   . ALA A 1 67  ? 46.399 14.627 52.162 1.00   24.33 ? 85   ALA A C   1 
ATOM   532  O  O   . ALA A 1 67  ? 46.269 13.775 51.281 1.00   25.41 ? 85   ALA A O   1 
ATOM   533  C  CB  . ALA A 1 67  ? 46.976 16.811 51.097 1.00   23.22 ? 85   ALA A CB  1 
ATOM   534  N  N   . VAL A 1 68  ? 45.649 14.650 53.260 1.00   24.52 ? 86   VAL A N   1 
ATOM   535  C  CA  . VAL A 1 68  ? 44.595 13.667 53.470 1.00   25.67 ? 86   VAL A CA  1 
ATOM   536  C  C   . VAL A 1 68  ? 43.242 14.264 53.093 1.00   26.53 ? 86   VAL A C   1 
ATOM   537  O  O   . VAL A 1 68  ? 42.345 13.555 52.634 1.00   25.81 ? 86   VAL A O   1 
ATOM   538  C  CB  . VAL A 1 68  ? 44.555 13.179 54.942 1.00   25.99 ? 86   VAL A CB  1 
ATOM   539  C  CG1 . VAL A 1 68  ? 44.182 14.321 55.871 1.00   25.39 ? 86   VAL A CG1 1 
ATOM   540  C  CG2 . VAL A 1 68  ? 43.564 12.032 55.078 1.00   27.14 ? 86   VAL A CG2 1 
ATOM   541  N  N   . LYS A 1 69  ? 43.100 15.575 53.278 1.00   26.07 ? 87   LYS A N   1 
ATOM   542  C  CA  . LYS A 1 69  ? 41.856 16.254 52.939 1.00   26.73 ? 87   LYS A CA  1 
ATOM   543  C  C   . LYS A 1 69  ? 42.122 17.662 52.409 1.00   26.59 ? 87   LYS A C   1 
ATOM   544  O  O   . LYS A 1 69  ? 42.933 18.406 52.964 1.00   25.97 ? 87   LYS A O   1 
ATOM   545  C  CB  . LYS A 1 69  ? 40.936 16.323 54.160 1.00   28.58 ? 87   LYS A CB  1 
ATOM   546  C  CG  . LYS A 1 69  ? 39.540 16.841 53.854 1.00   32.21 ? 87   LYS A CG  1 
ATOM   547  C  CD  . LYS A 1 69  ? 38.642 16.774 55.083 1.00   34.97 ? 87   LYS A CD  1 
ATOM   548  C  CE  . LYS A 1 69  ? 37.242 17.289 54.779 1.00   36.50 ? 87   LYS A CE  1 
ATOM   549  N  NZ  . LYS A 1 69  ? 36.579 16.507 53.699 1.00   38.44 ? 87   LYS A NZ  1 
ATOM   550  N  N   . ILE A 1 70  ? 41.434 18.014 51.328 1.00   25.08 ? 88   ILE A N   1 
ATOM   551  C  CA  . ILE A 1 70  ? 41.585 19.323 50.707 1.00   24.83 ? 88   ILE A CA  1 
ATOM   552  C  C   . ILE A 1 70  ? 40.227 20.014 50.691 1.00   24.34 ? 88   ILE A C   1 
ATOM   553  O  O   . ILE A 1 70  ? 39.279 19.522 50.077 1.00   24.56 ? 88   ILE A O   1 
ATOM   554  C  CB  . ILE A 1 70  ? 42.117 19.179 49.272 1.00   25.90 ? 88   ILE A CB  1 
ATOM   555  C  CG1 . ILE A 1 70  ? 43.435 18.399 49.295 1.00   26.72 ? 88   ILE A CG1 1 
ATOM   556  C  CG2 . ILE A 1 70  ? 42.328 20.551 48.650 1.00   26.41 ? 88   ILE A CG2 1 
ATOM   557  C  CD1 . ILE A 1 70  ? 44.011 18.122 47.926 1.00   31.16 ? 88   ILE A CD1 1 
ATOM   558  N  N   . ILE A 1 71  ? 40.138 21.154 51.367 1.00   21.80 ? 89   ILE A N   1 
ATOM   559  C  CA  . ILE A 1 71  ? 38.883 21.887 51.458 1.00   21.81 ? 89   ILE A CA  1 
ATOM   560  C  C   . ILE A 1 71  ? 38.918 23.284 50.849 1.00   22.07 ? 89   ILE A C   1 
ATOM   561  O  O   . ILE A 1 71  ? 39.550 24.194 51.389 1.00   21.55 ? 89   ILE A O   1 
ATOM   562  C  CB  . ILE A 1 71  ? 38.447 22.023 52.930 1.00   21.82 ? 89   ILE A CB  1 
ATOM   563  C  CG1 . ILE A 1 71  ? 38.409 20.641 53.585 1.00   22.76 ? 89   ILE A CG1 1 
ATOM   564  C  CG2 . ILE A 1 71  ? 37.085 22.701 53.015 1.00   20.56 ? 89   ILE A CG2 1 
ATOM   565  C  CD1 . ILE A 1 71  ? 38.283 20.680 55.090 1.00   23.74 ? 89   ILE A CD1 1 
ATOM   566  N  N   . ARG A 1 72  ? 38.228 23.452 49.728 1.00   22.66 ? 90   ARG A N   1 
ATOM   567  C  CA  . ARG A 1 72  ? 38.155 24.751 49.076 1.00   22.65 ? 90   ARG A CA  1 
ATOM   568  C  C   . ARG A 1 72  ? 37.034 25.520 49.755 1.00   23.61 ? 90   ARG A C   1 
ATOM   569  O  O   . ARG A 1 72  ? 36.110 24.920 50.307 1.00   22.54 ? 90   ARG A O   1 
ATOM   570  C  CB  . ARG A 1 72  ? 37.850 24.585 47.587 1.00   25.73 ? 90   ARG A CB  1 
ATOM   571  C  CG  . ARG A 1 72  ? 39.018 24.048 46.779 1.00   29.47 ? 90   ARG A CG  1 
ATOM   572  C  CD  . ARG A 1 72  ? 38.597 23.697 45.367 1.00   32.10 ? 90   ARG A CD  1 
ATOM   573  N  NE  . ARG A 1 72  ? 37.696 22.550 45.355 1.00   36.29 ? 90   ARG A NE  1 
ATOM   574  C  CZ  . ARG A 1 72  ? 37.220 21.984 44.252 1.00   38.37 ? 90   ARG A CZ  1 
ATOM   575  N  NH1 . ARG A 1 72  ? 37.558 22.460 43.060 1.00   38.82 ? 90   ARG A NH1 1 
ATOM   576  N  NH2 . ARG A 1 72  ? 36.412 20.937 44.341 1.00   39.63 ? 90   ARG A NH2 1 
ATOM   577  N  N   . HIS A 1 73  ? 37.115 26.845 49.739 1.00   21.96 ? 91   HIS A N   1 
ATOM   578  C  CA  . HIS A 1 73  ? 36.074 27.638 50.361 1.00   22.07 ? 91   HIS A CA  1 
ATOM   579  C  C   . HIS A 1 73  ? 34.770 27.345 49.620 1.00   23.58 ? 91   HIS A C   1 
ATOM   580  O  O   . HIS A 1 73  ? 34.756 27.223 48.397 1.00   22.39 ? 91   HIS A O   1 
ATOM   581  C  CB  . HIS A 1 73  ? 36.414 29.126 50.283 1.00   22.05 ? 91   HIS A CB  1 
ATOM   582  C  CG  . HIS A 1 73  ? 35.519 29.987 51.115 1.00   21.67 ? 91   HIS A CG  1 
ATOM   583  N  ND1 . HIS A 1 73  ? 34.255 30.360 50.710 1.00   21.88 ? 91   HIS A ND1 1 
ATOM   584  C  CD2 . HIS A 1 73  ? 35.686 30.509 52.354 1.00   21.86 ? 91   HIS A CD2 1 
ATOM   585  C  CE1 . HIS A 1 73  ? 33.683 31.074 51.662 1.00   21.69 ? 91   HIS A CE1 1 
ATOM   586  N  NE2 . HIS A 1 73  ? 34.530 31.179 52.671 1.00   21.16 ? 91   HIS A NE2 1 
ATOM   587  N  N   . PRO A 1 74  ? 33.660 27.210 50.361 1.00   24.84 ? 92   PRO A N   1 
ATOM   588  C  CA  . PRO A 1 74  ? 32.341 26.924 49.785 1.00   26.23 ? 92   PRO A CA  1 
ATOM   589  C  C   . PRO A 1 74  ? 31.898 27.890 48.689 1.00   26.66 ? 92   PRO A C   1 
ATOM   590  O  O   . PRO A 1 74  ? 31.224 27.491 47.738 1.00   28.21 ? 92   PRO A O   1 
ATOM   591  C  CB  . PRO A 1 74  ? 31.418 26.985 51.000 1.00   26.02 ? 92   PRO A CB  1 
ATOM   592  C  CG  . PRO A 1 74  ? 32.299 26.532 52.113 1.00   27.19 ? 92   PRO A CG  1 
ATOM   593  C  CD  . PRO A 1 74  ? 33.583 27.274 51.830 1.00   24.90 ? 92   PRO A CD  1 
ATOM   594  N  N   . LYS A 1 75  ? 32.279 29.158 48.820 1.00   26.88 ? 93   LYS A N   1 
ATOM   595  C  CA  . LYS A 1 75  ? 31.883 30.168 47.848 1.00   26.72 ? 93   LYS A CA  1 
ATOM   596  C  C   . LYS A 1 75  ? 32.943 30.505 46.806 1.00   26.50 ? 93   LYS A C   1 
ATOM   597  O  O   . LYS A 1 75  ? 32.888 31.559 46.172 1.00   25.38 ? 93   LYS A O   1 
ATOM   598  C  CB  . LYS A 1 75  ? 31.448 31.438 48.580 1.00   28.24 ? 93   LYS A CB  1 
ATOM   599  C  CG  . LYS A 1 75  ? 30.273 31.217 49.518 1.00   30.73 ? 93   LYS A CG  1 
ATOM   600  C  CD  . LYS A 1 75  ? 29.844 32.503 50.202 1.00   33.93 ? 93   LYS A CD  1 
ATOM   601  C  CE  . LYS A 1 75  ? 28.677 32.250 51.149 1.00   36.24 ? 93   LYS A CE  1 
ATOM   602  N  NZ  . LYS A 1 75  ? 28.223 33.494 51.831 1.00   38.26 ? 93   LYS A NZ  1 
ATOM   603  N  N   . TYR A 1 76  ? 33.908 29.611 46.626 1.00   25.64 ? 94   TYR A N   1 
ATOM   604  C  CA  . TYR A 1 76  ? 34.953 29.833 45.637 1.00   26.87 ? 94   TYR A CA  1 
ATOM   605  C  C   . TYR A 1 76  ? 34.334 29.885 44.240 1.00   27.89 ? 94   TYR A C   1 
ATOM   606  O  O   . TYR A 1 76  ? 33.546 29.014 43.875 1.00   28.80 ? 94   TYR A O   1 
ATOM   607  C  CB  . TYR A 1 76  ? 35.990 28.708 45.703 1.00   25.51 ? 94   TYR A CB  1 
ATOM   608  C  CG  . TYR A 1 76  ? 36.947 28.683 44.532 1.00   25.25 ? 94   TYR A CG  1 
ATOM   609  C  CD1 . TYR A 1 76  ? 37.712 29.803 44.206 1.00   24.09 ? 94   TYR A CD1 1 
ATOM   610  C  CD2 . TYR A 1 76  ? 37.084 27.540 43.746 1.00   25.35 ? 94   TYR A CD2 1 
ATOM   611  C  CE1 . TYR A 1 76  ? 38.590 29.783 43.122 1.00   24.09 ? 94   TYR A CE1 1 
ATOM   612  C  CE2 . TYR A 1 76  ? 37.959 27.510 42.663 1.00   25.34 ? 94   TYR A CE2 1 
ATOM   613  C  CZ  . TYR A 1 76  ? 38.708 28.634 42.358 1.00   24.89 ? 94   TYR A CZ  1 
ATOM   614  O  OH  . TYR A 1 76  ? 39.578 28.604 41.292 1.00   26.66 ? 94   TYR A OH  1 
ATOM   615  N  N   . ASN A 1 77  ? 34.687 30.913 43.471 1.00   28.69 ? 95   ASN A N   1 
ATOM   616  C  CA  . ASN A 1 77  ? 34.179 31.071 42.108 1.00   30.24 ? 95   ASN A CA  1 
ATOM   617  C  C   . ASN A 1 77  ? 35.337 30.933 41.124 1.00   30.85 ? 95   ASN A C   1 
ATOM   618  O  O   . ASN A 1 77  ? 36.167 31.832 40.995 1.00   30.79 ? 95   ASN A O   1 
ATOM   619  C  CB  . ASN A 1 77  ? 33.513 32.440 41.944 1.00   31.63 ? 95   ASN A CB  1 
ATOM   620  C  CG  . ASN A 1 77  ? 32.950 32.662 40.544 1.00   33.17 ? 95   ASN A CG  1 
ATOM   621  O  OD1 . ASN A 1 77  ? 32.323 33.685 40.276 1.00   35.79 ? 95   ASN A OD1 1 
ATOM   622  N  ND2 . ASN A 1 77  ? 33.176 31.710 39.649 1.00   33.49 ? 95   ASN A ND2 1 
ATOM   623  N  N   . ARG A 1 78  ? 35.381 29.799 40.432 1.00   31.88 ? 96   ARG A N   1 
ATOM   624  C  CA  . ARG A 1 78  ? 36.437 29.511 39.466 1.00   32.73 ? 96   ARG A CA  1 
ATOM   625  C  C   . ARG A 1 78  ? 36.590 30.560 38.365 1.00   33.74 ? 96   ARG A C   1 
ATOM   626  O  O   . ARG A 1 78  ? 37.692 30.782 37.864 1.00   34.41 ? 96   ARG A O   1 
ATOM   627  C  CB  . ARG A 1 78  ? 36.192 28.141 38.828 1.00   33.26 ? 96   ARG A CB  1 
ATOM   628  C  CG  . ARG A 1 78  ? 37.210 27.751 37.768 0.0000 33.76 ? 96   ARG A CG  1 
ATOM   629  C  CD  . ARG A 1 78  ? 36.866 26.409 37.143 0.0000 34.27 ? 96   ARG A CD  1 
ATOM   630  N  NE  . ARG A 1 78  ? 35.536 26.409 36.538 0.0000 34.71 ? 96   ARG A NE  1 
ATOM   631  C  CZ  . ARG A 1 78  ? 35.169 27.196 35.531 0.0000 34.95 ? 96   ARG A CZ  1 
ATOM   632  N  NH1 . ARG A 1 78  ? 36.033 28.053 35.005 0.0000 35.10 ? 96   ARG A NH1 1 
ATOM   633  N  NH2 . ARG A 1 78  ? 33.936 27.125 35.049 0.0000 35.10 ? 96   ARG A NH2 1 
ATOM   634  N  N   . ASP A 1 79  ? 35.493 31.209 37.994 1.00   33.95 ? 97   ASP A N   1 
ATOM   635  C  CA  . ASP A 1 79  ? 35.537 32.206 36.930 1.00   34.99 ? 97   ASP A CA  1 
ATOM   636  C  C   . ASP A 1 79  ? 36.072 33.572 37.347 1.00   33.65 ? 97   ASP A C   1 
ATOM   637  O  O   . ASP A 1 79  ? 36.819 34.205 36.598 1.00   34.22 ? 97   ASP A O   1 
ATOM   638  C  CB  . ASP A 1 79  ? 34.144 32.376 36.317 1.00   37.48 ? 97   ASP A CB  1 
ATOM   639  C  CG  . ASP A 1 79  ? 33.566 31.067 35.812 1.00   39.55 ? 97   ASP A CG  1 
ATOM   640  O  OD1 . ASP A 1 79  ? 34.267 30.358 35.059 1.00   40.53 ? 97   ASP A OD1 1 
ATOM   641  O  OD2 . ASP A 1 79  ? 32.410 30.751 36.165 1.00   41.03 ? 97   ASP A OD2 1 
ATOM   642  N  N   . THR A 1 80  ? 35.692 34.025 38.537 1.00   31.11 ? 98   THR A N   1 
ATOM   643  C  CA  . THR A 1 80  ? 36.121 35.332 39.028 1.00   29.34 ? 98   THR A CA  1 
ATOM   644  C  C   . THR A 1 80  ? 37.234 35.257 40.069 1.00   27.81 ? 98   THR A C   1 
ATOM   645  O  O   . THR A 1 80  ? 37.848 36.271 40.402 1.00   27.21 ? 98   THR A O   1 
ATOM   646  C  CB  . THR A 1 80  ? 34.946 36.085 39.662 1.00   29.39 ? 98   THR A CB  1 
ATOM   647  O  OG1 . THR A 1 80  ? 34.498 35.368 40.819 1.00   29.49 ? 98   THR A OG1 1 
ATOM   648  C  CG2 . THR A 1 80  ? 33.795 36.204 38.672 1.00   31.39 ? 98   THR A CG2 1 
ATOM   649  N  N   . LEU A 1 81  ? 37.481 34.055 40.579 1.00   26.34 ? 99   LEU A N   1 
ATOM   650  C  CA  . LEU A 1 81  ? 38.498 33.828 41.602 1.00   24.45 ? 99   LEU A CA  1 
ATOM   651  C  C   . LEU A 1 81  ? 38.107 34.470 42.930 1.00   23.97 ? 99   LEU A C   1 
ATOM   652  O  O   . LEU A 1 81  ? 38.956 34.747 43.781 1.00   21.38 ? 99   LEU A O   1 
ATOM   653  C  CB  . LEU A 1 81  ? 39.865 34.347 41.139 1.00   25.51 ? 99   LEU A CB  1 
ATOM   654  C  CG  . LEU A 1 81  ? 40.509 33.534 40.011 1.00   26.21 ? 99   LEU A CG  1 
ATOM   655  C  CD1 . LEU A 1 81  ? 41.868 34.116 39.666 1.00   27.98 ? 99   LEU A CD1 1 
ATOM   656  C  CD2 . LEU A 1 81  ? 40.649 32.079 40.442 1.00   27.24 ? 99   LEU A CD2 1 
ATOM   657  N  N   . ASP A 1 82  ? 36.811 34.710 43.101 1.00   22.37 ? 100  ASP A N   1 
ATOM   658  C  CA  . ASP A 1 82  ? 36.305 35.280 44.344 1.00   21.56 ? 100  ASP A CA  1 
ATOM   659  C  C   . ASP A 1 82  ? 36.480 34.179 45.396 1.00   19.55 ? 100  ASP A C   1 
ATOM   660  O  O   . ASP A 1 82  ? 36.301 33.000 45.090 1.00   18.94 ? 100  ASP A O   1 
ATOM   661  C  CB  . ASP A 1 82  ? 34.819 35.627 44.195 1.00   23.04 ? 100  ASP A CB  1 
ATOM   662  C  CG  . ASP A 1 82  ? 34.294 36.479 45.337 1.00   25.55 ? 100  ASP A CG  1 
ATOM   663  O  OD1 . ASP A 1 82  ? 33.057 36.623 45.451 1.00   27.18 ? 100  ASP A OD1 1 
ATOM   664  O  OD2 . ASP A 1 82  ? 35.111 37.016 46.113 1.00   24.46 ? 100  ASP A OD2 1 
ATOM   665  N  N   . ASN A 1 83  ? 36.841 34.562 46.619 1.00   18.34 ? 101  ASN A N   1 
ATOM   666  C  CA  . ASN A 1 83  ? 37.041 33.607 47.711 1.00   17.48 ? 101  ASN A CA  1 
ATOM   667  C  C   . ASN A 1 83  ? 38.063 32.533 47.354 1.00   16.09 ? 101  ASN A C   1 
ATOM   668  O  O   . ASN A 1 83  ? 37.850 31.346 47.603 1.00   15.94 ? 101  ASN A O   1 
ATOM   669  C  CB  . ASN A 1 83  ? 35.714 32.939 48.083 1.00   18.80 ? 101  ASN A CB  1 
ATOM   670  C  CG  . ASN A 1 83  ? 34.649 33.941 48.468 1.00   21.12 ? 101  ASN A CG  1 
ATOM   671  O  OD1 . ASN A 1 83  ? 34.811 34.698 49.422 1.00   20.47 ? 101  ASN A OD1 1 
ATOM   672  N  ND2 . ASN A 1 83  ? 33.551 33.953 47.720 1.00   21.76 ? 101  ASN A ND2 1 
ATOM   673  N  N   . ASP A 1 84  ? 39.184 32.960 46.783 1.00   15.66 ? 102  ASP A N   1 
ATOM   674  C  CA  . ASP A 1 84  ? 40.238 32.042 46.377 1.00   14.13 ? 102  ASP A CA  1 
ATOM   675  C  C   . ASP A 1 84  ? 41.120 31.626 47.557 1.00   14.62 ? 102  ASP A C   1 
ATOM   676  O  O   . ASP A 1 84  ? 42.233 32.125 47.727 1.00   14.19 ? 102  ASP A O   1 
ATOM   677  C  CB  . ASP A 1 84  ? 41.081 32.698 45.273 1.00   14.16 ? 102  ASP A CB  1 
ATOM   678  C  CG  . ASP A 1 84  ? 42.076 31.743 44.636 1.00   13.05 ? 102  ASP A CG  1 
ATOM   679  O  OD1 . ASP A 1 84  ? 41.911 30.516 44.777 1.00   14.24 ? 102  ASP A OD1 1 
ATOM   680  O  OD2 . ASP A 1 84  ? 43.022 32.227 43.975 1.00   14.92 ? 102  ASP A OD2 1 
ATOM   681  N  N   . ILE A 1 85  ? 40.608 30.711 48.375 1.00   14.35 ? 103  ILE A N   1 
ATOM   682  C  CA  . ILE A 1 85  ? 41.350 30.217 49.528 1.00   14.22 ? 103  ILE A CA  1 
ATOM   683  C  C   . ILE A 1 85  ? 40.992 28.752 49.739 1.00   15.29 ? 103  ILE A C   1 
ATOM   684  O  O   . ILE A 1 85  ? 39.878 28.315 49.427 1.00   15.10 ? 103  ILE A O   1 
ATOM   685  C  CB  . ILE A 1 85  ? 41.046 31.053 50.798 1.00   14.51 ? 103  ILE A CB  1 
ATOM   686  C  CG1 . ILE A 1 85  ? 41.974 30.625 51.939 1.00   15.21 ? 103  ILE A CG1 1 
ATOM   687  C  CG2 . ILE A 1 85  ? 39.583 30.899 51.197 1.00   15.59 ? 103  ILE A CG2 1 
ATOM   688  C  CD1 . ILE A 1 85  ? 41.958 31.577 53.118 1.00   18.70 ? 103  ILE A CD1 1 
ATOM   689  N  N   . MET A 1 86  ? 41.942 27.995 50.269 1.00   14.35 ? 104  MET A N   1 
ATOM   690  C  CA  . MET A 1 86  ? 41.750 26.570 50.465 1.00   16.14 ? 104  MET A CA  1 
ATOM   691  C  C   . MET A 1 86  ? 42.572 26.063 51.644 1.00   16.30 ? 104  MET A C   1 
ATOM   692  O  O   . MET A 1 86  ? 43.654 26.581 51.926 1.00   15.60 ? 104  MET A O   1 
ATOM   693  C  CB  . MET A 1 86  ? 42.159 25.873 49.164 1.00   17.77 ? 104  MET A CB  1 
ATOM   694  C  CG  . MET A 1 86  ? 42.458 24.397 49.232 1.00   20.99 ? 104  MET A CG  1 
ATOM   695  S  SD  . MET A 1 86  ? 42.942 23.834 47.579 1.00   19.30 ? 104  MET A SD  1 
ATOM   696  C  CE  . MET A 1 86  ? 44.734 23.870 47.677 1.00   19.74 ? 104  MET A CE  1 
ATOM   697  N  N   . LEU A 1 87  ? 42.040 25.061 52.339 1.00   15.23 ? 105  LEU A N   1 
ATOM   698  C  CA  . LEU A 1 87  ? 42.723 24.463 53.476 1.00   14.83 ? 105  LEU A CA  1 
ATOM   699  C  C   . LEU A 1 87  ? 43.141 23.047 53.119 1.00   15.62 ? 105  LEU A C   1 
ATOM   700  O  O   . LEU A 1 87  ? 42.391 22.310 52.473 1.00   16.38 ? 105  LEU A O   1 
ATOM   701  C  CB  . LEU A 1 87  ? 41.812 24.422 54.707 1.00   15.57 ? 105  LEU A CB  1 
ATOM   702  C  CG  . LEU A 1 87  ? 41.521 25.750 55.409 1.00   18.40 ? 105  LEU A CG  1 
ATOM   703  C  CD1 . LEU A 1 87  ? 40.520 25.530 56.543 1.00   19.67 ? 105  LEU A CD1 1 
ATOM   704  C  CD2 . LEU A 1 87  ? 42.822 26.329 55.947 1.00   19.47 ? 105  LEU A CD2 1 
ATOM   705  N  N   . ILE A 1 88  ? 44.341 22.674 53.544 1.00   14.11 ? 106  ILE A N   1 
ATOM   706  C  CA  . ILE A 1 88  ? 44.874 21.347 53.279 1.00   15.83 ? 106  ILE A CA  1 
ATOM   707  C  C   . ILE A 1 88  ? 45.265 20.679 54.589 1.00   16.55 ? 106  ILE A C   1 
ATOM   708  O  O   . ILE A 1 88  ? 46.065 21.220 55.354 1.00   15.51 ? 106  ILE A O   1 
ATOM   709  C  CB  . ILE A 1 88  ? 46.130 21.422 52.385 1.00   17.03 ? 106  ILE A CB  1 
ATOM   710  C  CG1 . ILE A 1 88  ? 45.781 22.084 51.048 1.00   17.93 ? 106  ILE A CG1 1 
ATOM   711  C  CG2 . ILE A 1 88  ? 46.709 20.026 52.181 1.00   17.51 ? 106  ILE A CG2 1 
ATOM   712  C  CD1 . ILE A 1 88  ? 46.988 22.366 50.171 1.00   20.99 ? 106  ILE A CD1 1 
ATOM   713  N  N   . LYS A 1 89  ? 44.689 19.511 54.862 1.00   16.79 ? 107  LYS A N   1 
ATOM   714  C  CA  . LYS A 1 89  ? 45.033 18.787 56.076 1.00   16.81 ? 107  LYS A CA  1 
ATOM   715  C  C   . LYS A 1 89  ? 46.058 17.720 55.722 1.00   18.12 ? 107  LYS A C   1 
ATOM   716  O  O   . LYS A 1 89  ? 45.849 16.927 54.804 1.00   18.81 ? 107  LYS A O   1 
ATOM   717  C  CB  . LYS A 1 89  ? 43.803 18.117 56.704 1.00   17.52 ? 107  LYS A CB  1 
ATOM   718  C  CG  . LYS A 1 89  ? 44.143 17.414 58.011 1.00   19.67 ? 107  LYS A CG  1 
ATOM   719  C  CD  . LYS A 1 89  ? 42.942 16.762 58.674 1.00   21.03 ? 107  LYS A CD  1 
ATOM   720  C  CE  . LYS A 1 89  ? 43.355 16.161 60.016 1.00   22.47 ? 107  LYS A CE  1 
ATOM   721  N  NZ  . LYS A 1 89  ? 42.229 15.506 60.746 1.00   22.63 ? 107  LYS A NZ  1 
ATOM   722  N  N   . LEU A 1 90  ? 47.168 17.711 56.449 1.00   18.03 ? 108  LEU A N   1 
ATOM   723  C  CA  . LEU A 1 90  ? 48.228 16.742 56.210 1.00   19.59 ? 108  LEU A CA  1 
ATOM   724  C  C   . LEU A 1 90  ? 47.846 15.411 56.853 1.00   20.96 ? 108  LEU A C   1 
ATOM   725  O  O   . LEU A 1 90  ? 47.201 15.386 57.902 1.00   19.95 ? 108  LEU A O   1 
ATOM   726  C  CB  . LEU A 1 90  ? 49.545 17.250 56.802 1.00   18.73 ? 108  LEU A CB  1 
ATOM   727  C  CG  . LEU A 1 90  ? 49.971 18.661 56.376 1.00   20.37 ? 108  LEU A CG  1 
ATOM   728  C  CD1 . LEU A 1 90  ? 51.258 19.045 57.089 1.00   19.55 ? 108  LEU A CD1 1 
ATOM   729  C  CD2 . LEU A 1 90  ? 50.158 18.712 54.868 1.00   21.04 ? 108  LEU A CD2 1 
ATOM   730  N  N   . SER A 1 91  ? 48.237 14.314 56.214 1.00   22.53 ? 109  SER A N   1 
ATOM   731  C  CA  . SER A 1 91  ? 47.933 12.982 56.728 1.00   24.57 ? 109  SER A CA  1 
ATOM   732  C  C   . SER A 1 91  ? 48.545 12.787 58.109 1.00   25.19 ? 109  SER A C   1 
ATOM   733  O  O   . SER A 1 91  ? 48.037 12.015 58.922 1.00   26.52 ? 109  SER A O   1 
ATOM   734  C  CB  . SER A 1 91  ? 48.456 11.914 55.766 1.00   25.31 ? 109  SER A CB  1 
ATOM   735  O  OG  . SER A 1 91  ? 49.838 12.085 55.517 1.00   28.15 ? 109  SER A OG  1 
ATOM   736  N  N   . SER A 1 92  ? 49.645 13.484 58.366 1.00   24.92 ? 110  SER A N   1 
ATOM   737  C  CA  . SER A 1 92  ? 50.317 13.405 59.655 1.00   26.20 ? 110  SER A CA  1 
ATOM   738  C  C   . SER A 1 92  ? 50.850 14.787 60.014 1.00   25.89 ? 110  SER A C   1 
ATOM   739  O  O   . SER A 1 92  ? 51.150 15.590 59.131 1.00   25.56 ? 110  SER A O   1 
ATOM   740  C  CB  . SER A 1 92  ? 51.464 12.392 59.601 1.00   27.24 ? 110  SER A CB  1 
ATOM   741  O  OG  . SER A 1 92  ? 52.428 12.755 58.630 1.00   31.95 ? 110  SER A OG  1 
ATOM   742  N  N   . PRO A 1 93  ? 50.960 15.090 61.315 1.00   25.15 ? 111  PRO A N   1 
ATOM   743  C  CA  . PRO A 1 93  ? 51.464 16.401 61.726 1.00   24.33 ? 111  PRO A CA  1 
ATOM   744  C  C   . PRO A 1 93  ? 52.935 16.581 61.386 1.00   24.39 ? 111  PRO A C   1 
ATOM   745  O  O   . PRO A 1 93  ? 53.733 15.650 61.504 1.00   24.39 ? 111  PRO A O   1 
ATOM   746  C  CB  . PRO A 1 93  ? 51.205 16.413 63.228 1.00   24.74 ? 111  PRO A CB  1 
ATOM   747  C  CG  . PRO A 1 93  ? 51.378 14.974 63.598 1.00   26.08 ? 111  PRO A CG  1 
ATOM   748  C  CD  . PRO A 1 93  ? 50.637 14.259 62.490 1.00   24.56 ? 111  PRO A CD  1 
ATOM   749  N  N   . ALA A 1 94  ? 53.287 17.782 60.946 1.00   21.76 ? 112  ALA A N   1 
ATOM   750  C  CA  . ALA A 1 94  ? 54.665 18.077 60.605 1.00   21.07 ? 112  ALA A CA  1 
ATOM   751  C  C   . ALA A 1 94  ? 55.466 18.177 61.892 1.00   20.80 ? 112  ALA A C   1 
ATOM   752  O  O   . ALA A 1 94  ? 54.920 18.498 62.948 1.00   20.45 ? 112  ALA A O   1 
ATOM   753  C  CB  . ALA A 1 94  ? 54.745 19.394 59.840 1.00   22.10 ? 112  ALA A CB  1 
ATOM   754  N  N   . VAL A 1 95  ? 56.759 17.890 61.805 1.00   20.10 ? 113  VAL A N   1 
ATOM   755  C  CA  . VAL A 1 95  ? 57.629 17.994 62.967 1.00   21.55 ? 113  VAL A CA  1 
ATOM   756  C  C   . VAL A 1 95  ? 58.098 19.440 62.991 1.00   21.04 ? 113  VAL A C   1 
ATOM   757  O  O   . VAL A 1 95  ? 58.761 19.897 62.062 1.00   22.15 ? 113  VAL A O   1 
ATOM   758  C  CB  . VAL A 1 95  ? 58.854 17.065 62.847 1.00   21.62 ? 113  VAL A CB  1 
ATOM   759  C  CG1 . VAL A 1 95  ? 59.771 17.259 64.046 1.00   22.72 ? 113  VAL A CG1 1 
ATOM   760  C  CG2 . VAL A 1 95  ? 58.399 15.620 62.762 1.00   24.92 ? 113  VAL A CG2 1 
ATOM   761  N  N   . ILE A 1 96  ? 57.739 20.158 64.049 1.00   21.64 ? 114  ILE A N   1 
ATOM   762  C  CA  . ILE A 1 96  ? 58.103 21.561 64.181 1.00   22.05 ? 114  ILE A CA  1 
ATOM   763  C  C   . ILE A 1 96  ? 59.514 21.731 64.720 1.00   22.96 ? 114  ILE A C   1 
ATOM   764  O  O   . ILE A 1 96  ? 59.862 21.186 65.765 1.00   23.15 ? 114  ILE A O   1 
ATOM   765  C  CB  . ILE A 1 96  ? 57.119 22.303 65.120 1.00   22.48 ? 114  ILE A CB  1 
ATOM   766  C  CG1 . ILE A 1 96  ? 55.690 22.185 64.580 1.00   24.91 ? 114  ILE A CG1 1 
ATOM   767  C  CG2 . ILE A 1 96  ? 57.524 23.763 65.259 1.00   24.17 ? 114  ILE A CG2 1 
ATOM   768  C  CD1 . ILE A 1 96  ? 55.503 22.745 63.181 1.00   24.21 ? 114  ILE A CD1 1 
ATOM   769  N  N   . ASN A 1 97  ? 60.326 22.488 63.993 1.00   21.98 ? 115  ASN A N   1 
ATOM   770  C  CA  . ASN A 1 97  ? 61.697 22.747 64.404 1.00   22.37 ? 115  ASN A CA  1 
ATOM   771  C  C   . ASN A 1 97  ? 62.144 24.113 63.905 1.00   23.10 ? 115  ASN A C   1 
ATOM   772  O  O   . ASN A 1 97  ? 61.317 24.959 63.569 1.00   22.34 ? 115  ASN A O   1 
ATOM   773  C  CB  . ASN A 1 97  ? 62.640 21.650 63.886 1.00   23.28 ? 115  ASN A CB  1 
ATOM   774  C  CG  . ASN A 1 97  ? 62.496 21.403 62.397 1.00   24.82 ? 115  ASN A CG  1 
ATOM   775  O  OD1 . ASN A 1 97  ? 62.551 22.329 61.594 1.00   24.45 ? 115  ASN A OD1 1 
ATOM   776  N  ND2 . ASN A 1 97  ? 62.321 20.142 62.022 1.00   25.86 ? 115  ASN A ND2 1 
ATOM   777  N  N   . ALA A 1 98  ? 63.453 24.326 63.857 1.00   23.71 ? 116  ALA A N   1 
ATOM   778  C  CA  . ALA A 1 98  ? 63.993 25.605 63.418 1.00   25.15 ? 116  ALA A CA  1 
ATOM   779  C  C   . ALA A 1 98  ? 63.748 25.910 61.944 1.00   24.70 ? 116  ALA A C   1 
ATOM   780  O  O   . ALA A 1 98  ? 63.668 27.075 61.559 1.00   26.53 ? 116  ALA A O   1 
ATOM   781  C  CB  . ALA A 1 98  ? 65.485 25.661 63.713 1.00   25.54 ? 116  ALA A CB  1 
ATOM   782  N  N   . ARG A 1 99  ? 63.620 24.873 61.123 1.00   23.79 ? 117  ARG A N   1 
ATOM   783  C  CA  . ARG A 1 99  ? 63.421 25.065 59.691 1.00   22.66 ? 117  ARG A CA  1 
ATOM   784  C  C   . ARG A 1 99  ? 61.992 24.828 59.217 1.00   21.06 ? 117  ARG A C   1 
ATOM   785  O  O   . ARG A 1 99  ? 61.676 25.047 58.046 1.00   19.77 ? 117  ARG A O   1 
ATOM   786  C  CB  . ARG A 1 99  ? 64.383 24.163 58.922 1.00   25.62 ? 117  ARG A CB  1 
ATOM   787  C  CG  . ARG A 1 99  ? 65.837 24.398 59.302 1.00   29.48 ? 117  ARG A CG  1 
ATOM   788  C  CD  . ARG A 1 99  ? 66.754 23.394 58.645 1.00   34.12 ? 117  ARG A CD  1 
ATOM   789  N  NE  . ARG A 1 99  ? 68.118 23.487 59.160 1.00   38.51 ? 117  ARG A NE  1 
ATOM   790  C  CZ  . ARG A 1 99  ? 68.959 24.481 58.893 1.00   40.86 ? 117  ARG A CZ  1 
ATOM   791  N  NH1 . ARG A 1 99  ? 68.584 25.482 58.106 1.00   42.55 ? 117  ARG A NH1 1 
ATOM   792  N  NH2 . ARG A 1 99  ? 70.177 24.477 59.421 1.00   42.18 ? 117  ARG A NH2 1 
ATOM   793  N  N   . VAL A 1 100 ? 61.134 24.380 60.127 1.00   18.35 ? 118  VAL A N   1 
ATOM   794  C  CA  . VAL A 1 100 ? 59.736 24.125 59.804 1.00   17.17 ? 118  VAL A CA  1 
ATOM   795  C  C   . VAL A 1 100 ? 58.872 24.583 60.972 1.00   17.79 ? 118  VAL A C   1 
ATOM   796  O  O   . VAL A 1 100 ? 58.897 23.983 62.046 1.00   17.60 ? 118  VAL A O   1 
ATOM   797  C  CB  . VAL A 1 100 ? 59.484 22.620 59.545 1.00   18.51 ? 118  VAL A CB  1 
ATOM   798  C  CG1 . VAL A 1 100 ? 57.998 22.360 59.348 1.00   18.33 ? 118  VAL A CG1 1 
ATOM   799  C  CG2 . VAL A 1 100 ? 60.270 22.166 58.321 1.00   18.56 ? 118  VAL A CG2 1 
ATOM   800  N  N   . SER A 1 101 ? 58.120 25.660 60.765 1.00   15.28 ? 119  SER A N   1 
ATOM   801  C  CA  . SER A 1 101 ? 57.246 26.180 61.805 1.00   14.58 ? 119  SER A CA  1 
ATOM   802  C  C   . SER A 1 101 ? 56.050 26.896 61.192 1.00   14.67 ? 119  SER A C   1 
ATOM   803  O  O   . SER A 1 101 ? 55.966 27.051 59.972 1.00   14.06 ? 119  SER A O   1 
ATOM   804  C  CB  . SER A 1 101 ? 58.012 27.114 62.747 1.00   17.05 ? 119  SER A CB  1 
ATOM   805  O  OG  . SER A 1 101 ? 58.633 28.160 62.035 1.00   21.18 ? 119  SER A OG  1 
ATOM   806  N  N   . THR A 1 102 ? 55.137 27.340 62.045 1.00   14.42 ? 120  THR A N   1 
ATOM   807  C  CA  . THR A 1 102 ? 53.906 27.973 61.590 1.00   14.56 ? 120  THR A CA  1 
ATOM   808  C  C   . THR A 1 102 ? 53.881 29.495 61.581 1.00   13.61 ? 120  THR A C   1 
ATOM   809  O  O   . THR A 1 102 ? 54.692 30.154 62.231 1.00   14.35 ? 120  THR A O   1 
ATOM   810  C  CB  . THR A 1 102 ? 52.731 27.502 62.447 1.00   15.86 ? 120  THR A CB  1 
ATOM   811  O  OG1 . THR A 1 102 ? 52.967 27.880 63.808 1.00   15.96 ? 120  THR A OG1 1 
ATOM   812  C  CG2 . THR A 1 102 ? 52.584 25.987 62.365 1.00   17.43 ? 120  THR A CG2 1 
ATOM   813  N  N   . ILE A 1 103 ? 52.920 30.041 60.842 1.00   12.61 ? 121  ILE A N   1 
ATOM   814  C  CA  . ILE A 1 103 ? 52.742 31.486 60.744 1.00   12.34 ? 121  ILE A CA  1 
ATOM   815  C  C   . ILE A 1 103 ? 51.374 31.822 61.358 1.00   12.35 ? 121  ILE A C   1 
ATOM   816  O  O   . ILE A 1 103 ? 50.423 31.044 61.243 1.00   12.00 ? 121  ILE A O   1 
ATOM   817  C  CB  . ILE A 1 103 ? 52.845 31.950 59.268 1.00   12.22 ? 121  ILE A CB  1 
ATOM   818  C  CG1 . ILE A 1 103 ? 52.848 33.478 59.189 1.00   14.92 ? 121  ILE A CG1 1 
ATOM   819  C  CG2 . ILE A 1 103 ? 51.716 31.364 58.451 1.00   13.76 ? 121  ILE A CG2 1 
ATOM   820  C  CD1 . ILE A 1 103 ? 54.061 34.117 59.821 1.00   16.29 ? 121  ILE A CD1 1 
ATOM   821  N  N   A SER A 1 104 ? 51.282 32.974 62.013 0.33   11.37 ? 122  SER A N   1 
ATOM   822  N  N   B SER A 1 104 ? 51.289 32.982 62.001 0.33   12.06 ? 122  SER A N   1 
ATOM   823  N  N   C SER A 1 104 ? 51.287 32.983 61.999 0.33   12.17 ? 122  SER A N   1 
ATOM   824  C  CA  A SER A 1 104 ? 50.040 33.384 62.660 0.33   10.91 ? 122  SER A CA  1 
ATOM   825  C  CA  B SER A 1 104 ? 50.063 33.425 62.660 0.33   12.24 ? 122  SER A CA  1 
ATOM   826  C  CA  C SER A 1 104 ? 50.058 33.423 62.656 0.33   12.47 ? 122  SER A CA  1 
ATOM   827  C  C   A SER A 1 104 ? 48.992 33.951 61.707 0.33   11.99 ? 122  SER A C   1 
ATOM   828  C  C   B SER A 1 104 ? 49.000 33.998 61.721 0.33   12.77 ? 122  SER A C   1 
ATOM   829  C  C   C SER A 1 104 ? 48.995 33.982 61.711 0.33   12.89 ? 122  SER A C   1 
ATOM   830  O  O   A SER A 1 104 ? 49.303 34.367 60.591 0.33   11.80 ? 122  SER A O   1 
ATOM   831  O  O   B SER A 1 104 ? 49.308 34.460 60.623 0.33   12.43 ? 122  SER A O   1 
ATOM   832  O  O   C SER A 1 104 ? 49.299 34.418 60.602 0.33   12.60 ? 122  SER A O   1 
ATOM   833  C  CB  A SER A 1 104 ? 50.335 34.419 63.746 0.33   11.18 ? 122  SER A CB  1 
ATOM   834  C  CB  B SER A 1 104 ? 50.411 34.467 63.726 0.33   13.35 ? 122  SER A CB  1 
ATOM   835  C  CB  C SER A 1 104 ? 50.393 34.484 63.708 0.33   13.72 ? 122  SER A CB  1 
ATOM   836  O  OG  A SER A 1 104 ? 50.864 35.603 63.180 0.33   8.80  ? 122  SER A OG  1 
ATOM   837  O  OG  B SER A 1 104 ? 49.252 34.919 64.397 0.33   14.87 ? 122  SER A OG  1 
ATOM   838  O  OG  C SER A 1 104 ? 51.412 34.031 64.580 0.33   16.00 ? 122  SER A OG  1 
ATOM   839  N  N   . LEU A 1 105 ? 47.745 33.967 62.168 1.00   12.98 ? 123  LEU A N   1 
ATOM   840  C  CA  . LEU A 1 105 ? 46.631 34.493 61.382 1.00   13.25 ? 123  LEU A CA  1 
ATOM   841  C  C   . LEU A 1 105 ? 46.530 35.986 61.699 1.00   13.20 ? 123  LEU A C   1 
ATOM   842  O  O   . LEU A 1 105 ? 46.934 36.428 62.777 1.00   14.69 ? 123  LEU A O   1 
ATOM   843  C  CB  . LEU A 1 105 ? 45.321 33.789 61.754 1.00   15.76 ? 123  LEU A CB  1 
ATOM   844  C  CG  . LEU A 1 105 ? 45.217 32.316 61.349 1.00   17.74 ? 123  LEU A CG  1 
ATOM   845  C  CD1 . LEU A 1 105 ? 43.872 31.755 61.785 1.00   19.41 ? 123  LEU A CD1 1 
ATOM   846  C  CD2 . LEU A 1 105 ? 45.385 32.193 59.842 1.00   18.89 ? 123  LEU A CD2 1 
ATOM   847  N  N   . PRO A 1 106 ? 45.979 36.785 60.773 1.00   14.18 ? 124  PRO A N   1 
ATOM   848  C  CA  . PRO A 1 106 ? 45.861 38.229 61.006 1.00   15.11 ? 124  PRO A CA  1 
ATOM   849  C  C   . PRO A 1 106 ? 44.808 38.629 62.031 1.00   15.73 ? 124  PRO A C   1 
ATOM   850  O  O   . PRO A 1 106 ? 43.769 37.981 62.156 1.00   15.77 ? 124  PRO A O   1 
ATOM   851  C  CB  . PRO A 1 106 ? 45.546 38.768 59.618 1.00   16.10 ? 124  PRO A CB  1 
ATOM   852  C  CG  . PRO A 1 106 ? 44.664 37.695 59.065 1.00   15.95 ? 124  PRO A CG  1 
ATOM   853  C  CD  . PRO A 1 106 ? 45.386 36.413 59.477 1.00   14.49 ? 124  PRO A CD  1 
ATOM   854  N  N   . THR A 1 107 ? 45.088 39.708 62.754 1.00   15.71 ? 125  THR A N   1 
ATOM   855  C  CA  . THR A 1 107 ? 44.172 40.216 63.772 1.00   18.34 ? 125  THR A CA  1 
ATOM   856  C  C   . THR A 1 107 ? 43.410 41.435 63.261 1.00   19.43 ? 125  THR A C   1 
ATOM   857  O  O   . THR A 1 107 ? 42.514 41.950 63.931 1.00   20.58 ? 125  THR A O   1 
ATOM   858  C  CB  . THR A 1 107 ? 44.934 40.599 65.054 1.00   19.84 ? 125  THR A CB  1 
ATOM   859  O  OG1 . THR A 1 107 ? 45.998 41.502 64.730 1.00   21.21 ? 125  THR A OG1 1 
ATOM   860  C  CG2 . THR A 1 107 ? 45.519 39.359 65.711 1.00   21.63 ? 125  THR A CG2 1 
ATOM   861  N  N   . ALA A 1 108 ? 43.779 41.888 62.067 1.00   18.22 ? 127  ALA A N   1 
ATOM   862  C  CA  . ALA A 1 108 ? 43.145 43.036 61.426 1.00   18.42 ? 127  ALA A CA  1 
ATOM   863  C  C   . ALA A 1 108 ? 43.500 42.982 59.946 1.00   19.42 ? 127  ALA A C   1 
ATOM   864  O  O   . ALA A 1 108 ? 44.512 42.392 59.570 1.00   18.37 ? 127  ALA A O   1 
ATOM   865  C  CB  . ALA A 1 108 ? 43.659 44.331 62.034 1.00   19.13 ? 127  ALA A CB  1 
ATOM   866  N  N   A PRO A 1 109 ? 42.666 43.590 59.086 0.50   19.35 ? 128  PRO A N   1 
ATOM   867  N  N   B PRO A 1 109 ? 42.672 43.601 59.087 0.50   19.83 ? 128  PRO A N   1 
ATOM   868  C  CA  A PRO A 1 109 ? 42.923 43.593 57.643 0.50   19.89 ? 128  PRO A CA  1 
ATOM   869  C  CA  B PRO A 1 109 ? 42.912 43.617 57.639 0.50   20.40 ? 128  PRO A CA  1 
ATOM   870  C  C   A PRO A 1 109 ? 44.218 44.324 57.302 0.50   20.62 ? 128  PRO A C   1 
ATOM   871  C  C   B PRO A 1 109 ? 44.212 44.340 57.296 0.50   20.90 ? 128  PRO A C   1 
ATOM   872  O  O   A PRO A 1 109 ? 44.723 45.115 58.098 0.50   20.27 ? 128  PRO A O   1 
ATOM   873  O  O   B PRO A 1 109 ? 44.716 45.137 58.086 0.50   20.50 ? 128  PRO A O   1 
ATOM   874  C  CB  A PRO A 1 109 ? 41.687 44.286 57.077 0.50   20.26 ? 128  PRO A CB  1 
ATOM   875  C  CB  B PRO A 1 109 ? 41.694 44.361 57.092 0.50   21.09 ? 128  PRO A CB  1 
ATOM   876  C  CG  A PRO A 1 109 ? 41.317 45.240 58.170 0.50   18.61 ? 128  PRO A CG  1 
ATOM   877  C  CG  B PRO A 1 109 ? 40.634 44.103 58.115 0.50   20.52 ? 128  PRO A CG  1 
ATOM   878  C  CD  A PRO A 1 109 ? 41.469 44.389 59.405 0.50   20.12 ? 128  PRO A CD  1 
ATOM   879  C  CD  B PRO A 1 109 ? 41.388 44.247 59.409 0.50   20.86 ? 128  PRO A CD  1 
ATOM   880  N  N   . PRO A 1 110 ? 44.774 44.069 56.108 1.00   21.88 ? 129  PRO A N   1 
ATOM   881  C  CA  . PRO A 1 110 ? 46.018 44.730 55.712 1.00   22.48 ? 129  PRO A CA  1 
ATOM   882  C  C   . PRO A 1 110 ? 45.793 46.231 55.538 1.00   22.34 ? 129  PRO A C   1 
ATOM   883  O  O   . PRO A 1 110 ? 44.758 46.659 55.032 1.00   22.89 ? 129  PRO A O   1 
ATOM   884  C  CB  . PRO A 1 110 ? 46.380 44.025 54.407 1.00   22.71 ? 129  PRO A CB  1 
ATOM   885  C  CG  . PRO A 1 110 ? 45.047 43.666 53.837 1.00   23.95 ? 129  PRO A CG  1 
ATOM   886  C  CD  . PRO A 1 110 ? 44.282 43.176 55.044 1.00   22.36 ? 129  PRO A CD  1 
ATOM   887  N  N   . ALA A 1 111 ? 46.761 47.023 55.976 1.00   22.53 ? 130  ALA A N   1 
ATOM   888  C  CA  . ALA A 1 111 ? 46.664 48.470 55.873 1.00   22.31 ? 130  ALA A CA  1 
ATOM   889  C  C   . ALA A 1 111 ? 47.555 48.973 54.747 1.00   21.18 ? 130  ALA A C   1 
ATOM   890  O  O   . ALA A 1 111 ? 48.713 48.573 54.636 1.00   20.04 ? 130  ALA A O   1 
ATOM   891  C  CB  . ALA A 1 111 ? 47.071 49.108 57.187 1.00   24.07 ? 130  ALA A CB  1 
ATOM   892  N  N   . ALA A 1 112 ? 47.008 49.848 53.910 1.00   21.81 ? 132  ALA A N   1 
ATOM   893  C  CA  . ALA A 1 112 ? 47.764 50.403 52.797 1.00   21.25 ? 132  ALA A CA  1 
ATOM   894  C  C   . ALA A 1 112 ? 49.076 50.984 53.301 1.00   21.36 ? 132  ALA A C   1 
ATOM   895  O  O   . ALA A 1 112 ? 49.112 51.646 54.340 1.00   22.08 ? 132  ALA A O   1 
ATOM   896  C  CB  . ALA A 1 112 ? 46.946 51.483 52.097 1.00   23.58 ? 132  ALA A CB  1 
ATOM   897  N  N   . GLY A 1 113 ? 50.158 50.721 52.575 1.00   19.52 ? 133  GLY A N   1 
ATOM   898  C  CA  . GLY A 1 113 ? 51.452 51.247 52.969 1.00   20.31 ? 133  GLY A CA  1 
ATOM   899  C  C   . GLY A 1 113 ? 52.311 50.296 53.776 1.00   20.78 ? 133  GLY A C   1 
ATOM   900  O  O   . GLY A 1 113 ? 53.512 50.518 53.929 1.00   23.12 ? 133  GLY A O   1 
ATOM   901  N  N   . THR A 1 114 ? 51.702 49.238 54.299 1.00   20.00 ? 134  THR A N   1 
ATOM   902  C  CA  . THR A 1 114 ? 52.432 48.256 55.091 1.00   20.77 ? 134  THR A CA  1 
ATOM   903  C  C   . THR A 1 114 ? 53.362 47.442 54.198 1.00   19.23 ? 134  THR A C   1 
ATOM   904  O  O   . THR A 1 114 ? 52.971 47.016 53.115 1.00   17.54 ? 134  THR A O   1 
ATOM   905  C  CB  . THR A 1 114 ? 51.471 47.286 55.798 1.00   20.66 ? 134  THR A CB  1 
ATOM   906  O  OG1 . THR A 1 114 ? 50.539 48.030 56.594 1.00   24.77 ? 134  THR A OG1 1 
ATOM   907  C  CG2 . THR A 1 114 ? 52.247 46.332 56.697 1.00   23.83 ? 134  THR A CG2 1 
ATOM   908  N  N   . GLU A 1 115 ? 54.592 47.229 54.652 1.00   19.03 ? 135  GLU A N   1 
ATOM   909  C  CA  . GLU A 1 115 ? 55.548 46.452 53.874 1.00   18.73 ? 135  GLU A CA  1 
ATOM   910  C  C   . GLU A 1 115 ? 55.349 44.979 54.202 1.00   17.32 ? 135  GLU A C   1 
ATOM   911  O  O   . GLU A 1 115 ? 55.267 44.602 55.371 1.00   18.11 ? 135  GLU A O   1 
ATOM   912  C  CB  . GLU A 1 115 ? 56.982 46.877 54.206 1.00   21.45 ? 135  GLU A CB  1 
ATOM   913  C  CG  . GLU A 1 115 ? 58.045 46.167 53.383 0.0000 20.58 ? 135  GLU A CG  1 
ATOM   914  C  CD  . GLU A 1 115 ? 59.445 46.669 53.679 0.0000 20.86 ? 135  GLU A CD  1 
ATOM   915  O  OE1 . GLU A 1 115 ? 59.883 46.561 54.844 0.0000 20.79 ? 135  GLU A OE1 1 
ATOM   916  O  OE2 . GLU A 1 115 ? 60.107 47.171 52.747 0.0000 20.79 ? 135  GLU A OE2 1 
ATOM   917  N  N   . CYS A 1 116 ? 55.255 44.150 53.168 1.00   14.92 ? 136  CYS A N   1 
ATOM   918  C  CA  . CYS A 1 116 ? 55.060 42.717 53.364 1.00   12.98 ? 136  CYS A CA  1 
ATOM   919  C  C   . CYS A 1 116 ? 56.108 41.911 52.615 1.00   13.29 ? 136  CYS A C   1 
ATOM   920  O  O   . CYS A 1 116 ? 56.818 42.437 51.757 1.00   14.27 ? 136  CYS A O   1 
ATOM   921  C  CB  . CYS A 1 116 ? 53.687 42.292 52.859 1.00   11.92 ? 136  CYS A CB  1 
ATOM   922  S  SG  . CYS A 1 116 ? 52.286 43.262 53.491 1.00   15.33 ? 136  CYS A SG  1 
ATOM   923  N  N   . LEU A 1 117 ? 56.183 40.625 52.944 1.00   11.90 ? 137  LEU A N   1 
ATOM   924  C  CA  . LEU A 1 117 ? 57.127 39.714 52.311 1.00   9.96  ? 137  LEU A CA  1 
ATOM   925  C  C   . LEU A 1 117 ? 56.353 38.643 51.547 1.00   10.20 ? 137  LEU A C   1 
ATOM   926  O  O   . LEU A 1 117 ? 55.530 37.931 52.121 1.00   9.73  ? 137  LEU A O   1 
ATOM   927  C  CB  . LEU A 1 117 ? 58.022 39.059 53.369 1.00   11.44 ? 137  LEU A CB  1 
ATOM   928  C  CG  . LEU A 1 117 ? 59.070 38.054 52.879 1.00   13.92 ? 137  LEU A CG  1 
ATOM   929  C  CD1 . LEU A 1 117 ? 60.068 38.746 51.961 1.00   15.85 ? 137  LEU A CD1 1 
ATOM   930  C  CD2 . LEU A 1 117 ? 59.790 37.446 54.076 1.00   17.33 ? 137  LEU A CD2 1 
ATOM   931  N  N   . ILE A 1 118 ? 56.614 38.556 50.248 1.00   8.72  ? 138  ILE A N   1 
ATOM   932  C  CA  . ILE A 1 118 ? 55.967 37.584 49.372 1.00   10.00 ? 138  ILE A CA  1 
ATOM   933  C  C   . ILE A 1 118 ? 57.064 36.614 48.954 1.00   9.46  ? 138  ILE A C   1 
ATOM   934  O  O   . ILE A 1 118 ? 58.192 37.025 48.687 1.00   10.27 ? 138  ILE A O   1 
ATOM   935  C  CB  . ILE A 1 118 ? 55.383 38.277 48.124 1.00   10.14 ? 138  ILE A CB  1 
ATOM   936  C  CG1 . ILE A 1 118 ? 54.423 39.389 48.557 1.00   13.34 ? 138  ILE A CG1 1 
ATOM   937  C  CG2 . ILE A 1 118 ? 54.644 37.262 47.259 1.00   11.49 ? 138  ILE A CG2 1 
ATOM   938  C  CD1 . ILE A 1 118 ? 53.928 40.254 47.409 1.00   15.89 ? 138  ILE A CD1 1 
ATOM   939  N  N   . SER A 1 119 ? 56.746 35.329 48.885 1.00   9.36  ? 139  SER A N   1 
ATOM   940  C  CA  . SER A 1 119 ? 57.771 34.358 48.534 1.00   7.63  ? 139  SER A CA  1 
ATOM   941  C  C   . SER A 1 119 ? 57.251 33.194 47.707 1.00   8.11  ? 139  SER A C   1 
ATOM   942  O  O   . SER A 1 119 ? 56.067 32.880 47.739 1.00   9.03  ? 139  SER A O   1 
ATOM   943  C  CB  . SER A 1 119 ? 58.416 33.824 49.817 1.00   8.20  ? 139  SER A CB  1 
ATOM   944  O  OG  . SER A 1 119 ? 57.421 33.442 50.762 1.00   9.38  ? 139  SER A OG  1 
ATOM   945  N  N   . GLY A 1 120 ? 58.151 32.556 46.965 1.00   8.81  ? 140  GLY A N   1 
ATOM   946  C  CA  . GLY A 1 120 ? 57.747 31.414 46.162 1.00   8.95  ? 140  GLY A CA  1 
ATOM   947  C  C   . GLY A 1 120 ? 58.789 30.947 45.168 1.00   8.86  ? 140  GLY A C   1 
ATOM   948  O  O   . GLY A 1 120 ? 59.844 31.564 45.012 1.00   9.68  ? 140  GLY A O   1 
ATOM   949  N  N   . TRP A 1 121 ? 58.474 29.839 44.501 1.00   10.26 ? 141  TRP A N   1 
ATOM   950  C  CA  . TRP A 1 121 ? 59.328 29.238 43.482 1.00   11.04 ? 141  TRP A CA  1 
ATOM   951  C  C   . TRP A 1 121 ? 58.681 29.458 42.113 1.00   12.20 ? 141  TRP A C   1 
ATOM   952  O  O   . TRP A 1 121 ? 58.872 28.667 41.190 1.00   12.79 ? 141  TRP A O   1 
ATOM   953  C  CB  . TRP A 1 121 ? 59.472 27.735 43.735 1.00   10.25 ? 141  TRP A CB  1 
ATOM   954  C  CG  . TRP A 1 121 ? 60.298 27.383 44.933 1.00   9.98  ? 141  TRP A CG  1 
ATOM   955  C  CD1 . TRP A 1 121 ? 61.661 27.299 44.992 1.00   10.90 ? 141  TRP A CD1 1 
ATOM   956  C  CD2 . TRP A 1 121 ? 59.817 27.056 46.243 1.00   10.71 ? 141  TRP A CD2 1 
ATOM   957  N  NE1 . TRP A 1 121 ? 62.059 26.934 46.259 1.00   12.62 ? 141  TRP A NE1 1 
ATOM   958  C  CE2 . TRP A 1 121 ? 60.948 26.780 47.047 1.00   10.27 ? 141  TRP A CE2 1 
ATOM   959  C  CE3 . TRP A 1 121 ? 58.540 26.968 46.817 1.00   10.37 ? 141  TRP A CE3 1 
ATOM   960  C  CZ2 . TRP A 1 121 ? 60.842 26.422 48.396 1.00   11.60 ? 141  TRP A CZ2 1 
ATOM   961  C  CZ3 . TRP A 1 121 ? 58.433 26.608 48.164 1.00   12.49 ? 141  TRP A CZ3 1 
ATOM   962  C  CH2 . TRP A 1 121 ? 59.579 26.341 48.936 1.00   11.27 ? 141  TRP A CH2 1 
ATOM   963  N  N   . GLY A 1 122 ? 57.915 30.539 41.998 1.00   10.92 ? 142  GLY A N   1 
ATOM   964  C  CA  . GLY A 1 122 ? 57.238 30.854 40.753 1.00   11.32 ? 142  GLY A CA  1 
ATOM   965  C  C   . GLY A 1 122 ? 58.124 31.470 39.684 1.00   10.91 ? 142  GLY A C   1 
ATOM   966  O  O   . GLY A 1 122 ? 59.313 31.703 39.904 1.00   10.83 ? 142  GLY A O   1 
ATOM   967  N  N   . ASN A 1 123 ? 57.525 31.737 38.523 1.00   10.62 ? 143  ASN A N   1 
ATOM   968  C  CA  . ASN A 1 123 ? 58.220 32.315 37.372 1.00   11.33 ? 143  ASN A CA  1 
ATOM   969  C  C   . ASN A 1 123 ? 58.943 33.605 37.764 1.00   11.07 ? 143  ASN A C   1 
ATOM   970  O  O   . ASN A 1 123 ? 58.409 34.418 38.520 1.00   11.02 ? 143  ASN A O   1 
ATOM   971  C  CB  . ASN A 1 123 ? 57.196 32.591 36.261 1.00   10.10 ? 143  ASN A CB  1 
ATOM   972  C  CG  . ASN A 1 123 ? 57.837 32.830 34.899 1.00   12.80 ? 143  ASN A CG  1 
ATOM   973  O  OD1 . ASN A 1 123 ? 59.059 32.898 34.771 1.00   11.73 ? 143  ASN A OD1 1 
ATOM   974  N  ND2 . ASN A 1 123 ? 57.001 32.967 33.873 1.00   13.85 ? 143  ASN A ND2 1 
ATOM   975  N  N   . THR A 1 124 ? 60.156 33.794 37.249 1.00   10.94 ? 144  THR A N   1 
ATOM   976  C  CA  . THR A 1 124 ? 60.935 34.990 37.569 1.00   11.44 ? 144  THR A CA  1 
ATOM   977  C  C   . THR A 1 124 ? 61.005 35.999 36.426 1.00   11.89 ? 144  THR A C   1 
ATOM   978  O  O   . THR A 1 124 ? 61.720 36.996 36.527 1.00   12.79 ? 144  THR A O   1 
ATOM   979  C  CB  . THR A 1 124 ? 62.379 34.625 37.962 1.00   13.83 ? 144  THR A CB  1 
ATOM   980  O  OG1 . THR A 1 124 ? 63.026 33.986 36.853 1.00   14.58 ? 144  THR A OG1 1 
ATOM   981  C  CG2 . THR A 1 124 ? 62.387 33.680 39.163 1.00   13.96 ? 144  THR A CG2 1 
ATOM   982  N  N   . LEU A 1 125 ? 60.261 35.748 35.350 1.00   12.77 ? 145  LEU A N   1 
ATOM   983  C  CA  . LEU A 1 125 ? 60.262 36.639 34.184 1.00   13.89 ? 145  LEU A CA  1 
ATOM   984  C  C   . LEU A 1 125 ? 58.872 37.171 33.840 1.00   14.27 ? 145  LEU A C   1 
ATOM   985  O  O   . LEU A 1 125 ? 57.871 36.494 34.075 1.00   15.18 ? 145  LEU A O   1 
ATOM   986  C  CB  . LEU A 1 125 ? 60.811 35.897 32.959 1.00   14.56 ? 145  LEU A CB  1 
ATOM   987  C  CG  . LEU A 1 125 ? 62.182 35.225 33.081 1.00   14.76 ? 145  LEU A CG  1 
ATOM   988  C  CD1 . LEU A 1 125 ? 62.468 34.434 31.809 1.00   16.97 ? 145  LEU A CD1 1 
ATOM   989  C  CD2 . LEU A 1 125 ? 63.257 36.264 33.320 1.00   17.73 ? 145  LEU A CD2 1 
ATOM   990  N  N   . SER A 1 126 ? 58.828 38.376 33.264 1.00   14.20 ? 146  SER A N   1 
ATOM   991  C  CA  . SER A 1 126 ? 57.575 39.011 32.850 1.00   15.84 ? 146  SER A CA  1 
ATOM   992  C  C   . SER A 1 126 ? 57.108 38.438 31.513 1.00   15.47 ? 146  SER A C   1 
ATOM   993  O  O   . SER A 1 126 ? 55.926 38.510 31.175 1.00   15.85 ? 146  SER A O   1 
ATOM   994  C  CB  . SER A 1 126 ? 57.757 40.524 32.711 1.00   17.78 ? 146  SER A CB  1 
ATOM   995  O  OG  . SER A 1 126 ? 58.014 41.126 33.964 1.00   22.79 ? 146  SER A OG  1 
ATOM   996  N  N   . PHE A 1 127 ? 58.055 37.895 30.750 1.00   13.76 ? 147  PHE A N   1 
ATOM   997  C  CA  . PHE A 1 127 ? 57.770 37.269 29.459 1.00   13.29 ? 147  PHE A CA  1 
ATOM   998  C  C   . PHE A 1 127 ? 58.630 36.017 29.387 1.00   12.83 ? 147  PHE A C   1 
ATOM   999  O  O   . PHE A 1 127 ? 59.790 36.028 29.808 1.00   12.90 ? 147  PHE A O   1 
ATOM   1000 C  CB  . PHE A 1 127 ? 58.101 38.214 28.296 1.00   14.03 ? 147  PHE A CB  1 
ATOM   1001 C  CG  . PHE A 1 127 ? 57.233 39.435 28.253 1.00   14.15 ? 147  PHE A CG  1 
ATOM   1002 C  CD1 . PHE A 1 127 ? 57.614 40.599 28.912 1.00   16.67 ? 147  PHE A CD1 1 
ATOM   1003 C  CD2 . PHE A 1 127 ? 55.999 39.400 27.611 1.00   16.91 ? 147  PHE A CD2 1 
ATOM   1004 C  CE1 . PHE A 1 127 ? 56.774 41.712 28.937 1.00   18.85 ? 147  PHE A CE1 1 
ATOM   1005 C  CE2 . PHE A 1 127 ? 55.153 40.511 27.632 1.00   17.67 ? 147  PHE A CE2 1 
ATOM   1006 C  CZ  . PHE A 1 127 ? 55.543 41.664 28.296 1.00   16.20 ? 147  PHE A CZ  1 
ATOM   1007 N  N   . GLY A 1 128 ? 58.069 34.939 28.855 1.00   12.22 ? 148  GLY A N   1 
ATOM   1008 C  CA  . GLY A 1 128 ? 58.814 33.695 28.799 1.00   14.64 ? 148  GLY A CA  1 
ATOM   1009 C  C   . GLY A 1 128 ? 58.711 33.055 30.171 1.00   15.63 ? 148  GLY A C   1 
ATOM   1010 O  O   . GLY A 1 128 ? 57.893 33.474 30.990 1.00   15.41 ? 148  GLY A O   1 
ATOM   1011 N  N   . ALA A 1 129 ? 59.536 32.056 30.448 1.00   15.62 ? 149  ALA A N   1 
ATOM   1012 C  CA  . ALA A 1 129 ? 59.463 31.400 31.742 1.00   17.34 ? 149  ALA A CA  1 
ATOM   1013 C  C   . ALA A 1 129 ? 60.805 30.899 32.245 1.00   17.83 ? 149  ALA A C   1 
ATOM   1014 O  O   . ALA A 1 129 ? 61.582 30.295 31.506 1.00   18.48 ? 149  ALA A O   1 
ATOM   1015 C  CB  . ALA A 1 129 ? 58.469 30.247 31.684 1.00   18.43 ? 149  ALA A CB  1 
ATOM   1016 N  N   . ASP A 1 130 ? 61.069 31.172 33.515 1.00   17.10 ? 150  ASP A N   1 
ATOM   1017 C  CA  . ASP A 1 130 ? 62.290 30.732 34.164 1.00   18.17 ? 150  ASP A CA  1 
ATOM   1018 C  C   . ASP A 1 130 ? 61.894 30.428 35.600 1.00   18.11 ? 150  ASP A C   1 
ATOM   1019 O  O   . ASP A 1 130 ? 61.665 31.341 36.395 1.00   17.68 ? 150  ASP A O   1 
ATOM   1020 C  CB  . ASP A 1 130 ? 63.352 31.830 34.147 1.00   22.58 ? 150  ASP A CB  1 
ATOM   1021 C  CG  . ASP A 1 130 ? 64.744 31.300 34.451 1.00   27.13 ? 150  ASP A CG  1 
ATOM   1022 O  OD1 . ASP A 1 130 ? 64.870 30.399 35.306 1.00   29.12 ? 150  ASP A OD1 1 
ATOM   1023 O  OD2 . ASP A 1 130 ? 65.718 31.791 33.842 1.00   30.92 ? 150  ASP A OD2 1 
ATOM   1024 N  N   . TYR A 1 131 ? 61.783 29.143 35.912 1.00   16.53 ? 151  TYR A N   1 
ATOM   1025 C  CA  . TYR A 1 131 ? 61.414 28.700 37.248 1.00   16.31 ? 151  TYR A CA  1 
ATOM   1026 C  C   . TYR A 1 131 ? 62.690 28.380 38.011 1.00   16.75 ? 151  TYR A C   1 
ATOM   1027 O  O   . TYR A 1 131 ? 63.489 27.548 37.584 1.00   19.56 ? 151  TYR A O   1 
ATOM   1028 C  CB  . TYR A 1 131 ? 60.500 27.484 37.141 1.00   16.58 ? 151  TYR A CB  1 
ATOM   1029 C  CG  . TYR A 1 131 ? 59.152 27.852 36.573 1.00   18.07 ? 151  TYR A CG  1 
ATOM   1030 C  CD1 . TYR A 1 131 ? 58.192 28.480 37.368 1.00   17.48 ? 151  TYR A CD1 1 
ATOM   1031 C  CD2 . TYR A 1 131 ? 58.856 27.641 35.225 1.00   18.94 ? 151  TYR A CD2 1 
ATOM   1032 C  CE1 . TYR A 1 131 ? 56.976 28.891 36.841 1.00   19.61 ? 151  TYR A CE1 1 
ATOM   1033 C  CE2 . TYR A 1 131 ? 57.636 28.054 34.685 1.00   19.33 ? 151  TYR A CE2 1 
ATOM   1034 C  CZ  . TYR A 1 131 ? 56.704 28.678 35.500 1.00   20.09 ? 151  TYR A CZ  1 
ATOM   1035 O  OH  . TYR A 1 131 ? 55.503 29.100 34.978 1.00   23.32 ? 151  TYR A OH  1 
ATOM   1036 N  N   . PRO A 1 132 ? 62.897 29.046 39.155 1.00   16.03 ? 152  PRO A N   1 
ATOM   1037 C  CA  . PRO A 1 132 ? 64.071 28.880 40.013 1.00   15.83 ? 152  PRO A CA  1 
ATOM   1038 C  C   . PRO A 1 132 ? 64.094 27.625 40.874 1.00   16.93 ? 152  PRO A C   1 
ATOM   1039 O  O   . PRO A 1 132 ? 63.051 27.089 41.235 1.00   18.55 ? 152  PRO A O   1 
ATOM   1040 C  CB  . PRO A 1 132 ? 64.034 30.141 40.864 1.00   15.65 ? 152  PRO A CB  1 
ATOM   1041 C  CG  . PRO A 1 132 ? 62.567 30.277 41.125 1.00   16.12 ? 152  PRO A CG  1 
ATOM   1042 C  CD  . PRO A 1 132 ? 61.956 30.018 39.749 1.00   14.90 ? 152  PRO A CD  1 
ATOM   1043 N  N   . ASP A 1 133 ? 65.297 27.160 41.197 1.00   17.00 ? 153  ASP A N   1 
ATOM   1044 C  CA  . ASP A 1 133 ? 65.431 25.989 42.052 1.00   17.69 ? 153  ASP A CA  1 
ATOM   1045 C  C   . ASP A 1 133 ? 65.326 26.454 43.500 1.00   15.90 ? 153  ASP A C   1 
ATOM   1046 O  O   . ASP A 1 133 ? 64.804 25.740 44.353 1.00   15.02 ? 153  ASP A O   1 
ATOM   1047 C  CB  . ASP A 1 133 ? 66.787 25.304 41.849 1.00   21.04 ? 153  ASP A CB  1 
ATOM   1048 C  CG  . ASP A 1 133 ? 66.945 24.719 40.464 1.00   25.54 ? 153  ASP A CG  1 
ATOM   1049 O  OD1 . ASP A 1 133 ? 65.964 24.143 39.948 1.00   27.16 ? 153  ASP A OD1 1 
ATOM   1050 O  OD2 . ASP A 1 133 ? 68.055 24.824 39.900 1.00   29.37 ? 153  ASP A OD2 1 
ATOM   1051 N  N   . GLU A 1 134 ? 65.823 27.662 43.759 1.00   15.01 ? 154  GLU A N   1 
ATOM   1052 C  CA  . GLU A 1 134 ? 65.816 28.234 45.101 1.00   15.44 ? 154  GLU A CA  1 
ATOM   1053 C  C   . GLU A 1 134 ? 64.661 29.197 45.354 1.00   12.62 ? 154  GLU A C   1 
ATOM   1054 O  O   . GLU A 1 134 ? 64.216 29.906 44.454 1.00   13.34 ? 154  GLU A O   1 
ATOM   1055 C  CB  . GLU A 1 134 ? 67.138 28.955 45.368 1.00   18.82 ? 154  GLU A CB  1 
ATOM   1056 C  CG  . GLU A 1 134 ? 68.329 28.033 45.543 1.00   24.67 ? 154  GLU A CG  1 
ATOM   1057 C  CD  . GLU A 1 134 ? 69.624 28.805 45.683 1.00   29.42 ? 154  GLU A CD  1 
ATOM   1058 O  OE1 . GLU A 1 134 ? 70.080 29.385 44.676 1.00   32.36 ? 154  GLU A OE1 1 
ATOM   1059 O  OE2 . GLU A 1 134 ? 70.176 28.843 46.802 1.00   33.11 ? 154  GLU A OE2 1 
ATOM   1060 N  N   . LEU A 1 135 ? 64.200 29.216 46.601 1.00   11.62 ? 155  LEU A N   1 
ATOM   1061 C  CA  . LEU A 1 135 ? 63.095 30.065 47.026 1.00   10.51 ? 155  LEU A CA  1 
ATOM   1062 C  C   . LEU A 1 135 ? 63.423 31.546 46.854 1.00   10.71 ? 155  LEU A C   1 
ATOM   1063 O  O   . LEU A 1 135 ? 64.481 32.009 47.285 1.00   11.57 ? 155  LEU A O   1 
ATOM   1064 C  CB  . LEU A 1 135 ? 62.768 29.775 48.493 1.00   10.20 ? 155  LEU A CB  1 
ATOM   1065 C  CG  . LEU A 1 135 ? 61.591 30.542 49.091 1.00   10.16 ? 155  LEU A CG  1 
ATOM   1066 C  CD1 . LEU A 1 135 ? 60.308 30.158 48.360 1.00   9.26  ? 155  LEU A CD1 1 
ATOM   1067 C  CD2 . LEU A 1 135 ? 61.474 30.224 50.575 1.00   12.15 ? 155  LEU A CD2 1 
ATOM   1068 N  N   . LYS A 1 136 ? 62.504 32.281 46.232 1.00   9.51  ? 156  LYS A N   1 
ATOM   1069 C  CA  . LYS A 1 136 ? 62.687 33.710 45.994 1.00   10.31 ? 156  LYS A CA  1 
ATOM   1070 C  C   . LYS A 1 136 ? 61.834 34.545 46.939 1.00   10.04 ? 156  LYS A C   1 
ATOM   1071 O  O   . LYS A 1 136 ? 60.738 34.138 47.340 1.00   7.81  ? 156  LYS A O   1 
ATOM   1072 C  CB  . LYS A 1 136 ? 62.341 34.055 44.544 1.00   11.03 ? 156  LYS A CB  1 
ATOM   1073 C  CG  . LYS A 1 136 ? 63.254 33.393 43.508 1.00   14.35 ? 156  LYS A CG  1 
ATOM   1074 C  CD  . LYS A 1 136 ? 64.680 33.926 43.596 1.00   16.95 ? 156  LYS A CD  1 
ATOM   1075 C  CE  . LYS A 1 136 ? 65.545 33.347 42.483 1.00   21.23 ? 156  LYS A CE  1 
ATOM   1076 N  NZ  . LYS A 1 136 ? 66.927 33.902 42.500 1.00   23.50 ? 156  LYS A NZ  1 
ATOM   1077 N  N   . CYS A 1 137 ? 62.354 35.726 47.265 1.00   9.37  ? 157  CYS A N   1 
ATOM   1078 C  CA  . CYS A 1 137 ? 61.729 36.668 48.190 1.00   9.86  ? 157  CYS A CA  1 
ATOM   1079 C  C   . CYS A 1 137 ? 61.487 38.040 47.561 1.00   10.27 ? 157  CYS A C   1 
ATOM   1080 O  O   . CYS A 1 137 ? 62.227 38.467 46.675 1.00   11.28 ? 157  CYS A O   1 
ATOM   1081 C  CB  . CYS A 1 137 ? 62.633 36.827 49.426 1.00   11.82 ? 157  CYS A CB  1 
ATOM   1082 S  SG  . CYS A 1 137 ? 62.293 35.601 50.726 1.00   11.74 ? 157  CYS A SG  1 
ATOM   1083 N  N   . LEU A 1 138 ? 60.451 38.726 48.030 1.00   9.02  ? 158  LEU A N   1 
ATOM   1084 C  CA  . LEU A 1 138 ? 60.131 40.061 47.532 1.00   9.88  ? 158  LEU A CA  1 
ATOM   1085 C  C   . LEU A 1 138 ? 59.455 40.886 48.615 1.00   11.04 ? 158  LEU A C   1 
ATOM   1086 O  O   . LEU A 1 138 ? 58.476 40.448 49.217 1.00   9.75  ? 158  LEU A O   1 
ATOM   1087 C  CB  . LEU A 1 138 ? 59.198 39.987 46.315 1.00   10.86 ? 158  LEU A CB  1 
ATOM   1088 C  CG  . LEU A 1 138 ? 58.679 41.334 45.791 1.00   11.79 ? 158  LEU A CG  1 
ATOM   1089 C  CD1 . LEU A 1 138 ? 59.834 42.150 45.235 1.00   15.28 ? 158  LEU A CD1 1 
ATOM   1090 C  CD2 . LEU A 1 138 ? 57.630 41.104 44.713 1.00   15.04 ? 158  LEU A CD2 1 
ATOM   1091 N  N   . ASP A 1 139 ? 59.991 42.076 48.870 1.00   10.89 ? 159  ASP A N   1 
ATOM   1092 C  CA  . ASP A 1 139 ? 59.409 42.977 49.855 1.00   13.91 ? 159  ASP A CA  1 
ATOM   1093 C  C   . ASP A 1 139 ? 58.583 43.970 49.053 1.00   12.98 ? 159  ASP A C   1 
ATOM   1094 O  O   . ASP A 1 139 ? 59.097 44.613 48.136 1.00   14.22 ? 159  ASP A O   1 
ATOM   1095 C  CB  . ASP A 1 139 ? 60.511 43.694 50.632 1.00   16.31 ? 159  ASP A CB  1 
ATOM   1096 C  CG  . ASP A 1 139 ? 61.345 42.739 51.456 1.00   19.79 ? 159  ASP A CG  1 
ATOM   1097 O  OD1 . ASP A 1 139 ? 60.821 42.199 52.453 1.00   23.97 ? 159  ASP A OD1 1 
ATOM   1098 O  OD2 . ASP A 1 139 ? 62.519 42.517 51.100 1.00   23.15 ? 159  ASP A OD2 1 
ATOM   1099 N  N   . ALA A 1 140 ? 57.298 44.075 49.378 1.00   13.31 ? 160  ALA A N   1 
ATOM   1100 C  CA  . ALA A 1 140 ? 56.402 44.970 48.652 1.00   13.24 ? 160  ALA A CA  1 
ATOM   1101 C  C   . ALA A 1 140 ? 55.326 45.528 49.566 1.00   14.33 ? 160  ALA A C   1 
ATOM   1102 O  O   . ALA A 1 140 ? 54.922 44.882 50.535 1.00   14.78 ? 160  ALA A O   1 
ATOM   1103 C  CB  . ALA A 1 140 ? 55.757 44.230 47.484 1.00   14.27 ? 160  ALA A CB  1 
ATOM   1104 N  N   . PRO A 1 141 ? 54.840 46.739 49.263 1.00   14.62 ? 161  PRO A N   1 
ATOM   1105 C  CA  . PRO A 1 141 ? 53.805 47.384 50.071 1.00   15.03 ? 161  PRO A CA  1 
ATOM   1106 C  C   . PRO A 1 141 ? 52.372 47.114 49.628 1.00   12.73 ? 161  PRO A C   1 
ATOM   1107 O  O   . PRO A 1 141 ? 52.097 46.889 48.448 1.00   13.39 ? 161  PRO A O   1 
ATOM   1108 C  CB  . PRO A 1 141 ? 54.159 48.855 49.938 1.00   16.09 ? 161  PRO A CB  1 
ATOM   1109 C  CG  . PRO A 1 141 ? 54.538 48.937 48.493 1.00   16.56 ? 161  PRO A CG  1 
ATOM   1110 C  CD  . PRO A 1 141 ? 55.404 47.692 48.286 1.00   15.54 ? 161  PRO A CD  1 
ATOM   1111 N  N   . VAL A 1 142 ? 51.463 47.139 50.596 1.00   13.47 ? 162  VAL A N   1 
ATOM   1112 C  CA  . VAL A 1 142 ? 50.045 46.951 50.335 1.00   13.82 ? 162  VAL A CA  1 
ATOM   1113 C  C   . VAL A 1 142 ? 49.556 48.235 49.660 1.00   14.65 ? 162  VAL A C   1 
ATOM   1114 O  O   . VAL A 1 142 ? 49.888 49.336 50.103 1.00   16.13 ? 162  VAL A O   1 
ATOM   1115 C  CB  . VAL A 1 142 ? 49.264 46.762 51.659 1.00   13.83 ? 162  VAL A CB  1 
ATOM   1116 C  CG1 . VAL A 1 142 ? 47.769 46.690 51.382 1.00   14.60 ? 162  VAL A CG1 1 
ATOM   1117 C  CG2 . VAL A 1 142 ? 49.741 45.504 52.365 1.00   13.72 ? 162  VAL A CG2 1 
ATOM   1118 N  N   . LEU A 1 143 ? 48.782 48.098 48.589 1.00   14.66 ? 163  LEU A N   1 
ATOM   1119 C  CA  . LEU A 1 143 ? 48.263 49.264 47.886 1.00   17.53 ? 163  LEU A CA  1 
ATOM   1120 C  C   . LEU A 1 143 ? 46.867 49.592 48.407 1.00   18.44 ? 163  LEU A C   1 
ATOM   1121 O  O   . LEU A 1 143 ? 46.243 48.774 49.081 1.00   19.07 ? 163  LEU A O   1 
ATOM   1122 C  CB  . LEU A 1 143 ? 48.207 48.989 46.383 1.00   18.11 ? 163  LEU A CB  1 
ATOM   1123 C  CG  . LEU A 1 143 ? 49.548 48.648 45.723 1.00   18.94 ? 163  LEU A CG  1 
ATOM   1124 C  CD1 . LEU A 1 143 ? 49.323 48.324 44.256 1.00   20.45 ? 163  LEU A CD1 1 
ATOM   1125 C  CD2 . LEU A 1 143 ? 50.517 49.808 45.881 1.00   22.05 ? 163  LEU A CD2 1 
ATOM   1126 N  N   . THR A 1 144 ? 46.378 50.792 48.111 1.00   21.34 ? 164  THR A N   1 
ATOM   1127 C  CA  . THR A 1 144 ? 45.041 51.170 48.557 1.00   21.88 ? 164  THR A CA  1 
ATOM   1128 C  C   . THR A 1 144 ? 44.021 50.444 47.682 1.00   22.00 ? 164  THR A C   1 
ATOM   1129 O  O   . THR A 1 144 ? 44.324 50.073 46.547 1.00   22.13 ? 164  THR A O   1 
ATOM   1130 C  CB  . THR A 1 144 ? 44.806 52.690 48.430 1.00   23.03 ? 164  THR A CB  1 
ATOM   1131 O  OG1 . THR A 1 144 ? 44.767 53.054 47.044 1.00   23.57 ? 164  THR A OG1 1 
ATOM   1132 C  CG2 . THR A 1 144 ? 45.919 53.459 49.123 1.00   23.76 ? 164  THR A CG2 1 
ATOM   1133 N  N   . GLN A 1 145 ? 42.818 50.227 48.208 1.00   21.47 ? 165  GLN A N   1 
ATOM   1134 C  CA  . GLN A 1 145 ? 41.778 49.556 47.434 1.00   21.73 ? 165  GLN A CA  1 
ATOM   1135 C  C   . GLN A 1 145 ? 41.452 50.397 46.207 1.00   22.25 ? 165  GLN A C   1 
ATOM   1136 O  O   . GLN A 1 145 ? 41.054 49.873 45.168 1.00   20.76 ? 165  GLN A O   1 
ATOM   1137 C  CB  . GLN A 1 145 ? 40.511 49.359 48.276 1.00   24.67 ? 165  GLN A CB  1 
ATOM   1138 C  CG  . GLN A 1 145 ? 40.661 48.345 49.397 0.0000 23.69 ? 165  GLN A CG  1 
ATOM   1139 C  CD  . GLN A 1 145 ? 40.943 46.947 48.880 0.0000 24.00 ? 165  GLN A CD  1 
ATOM   1140 O  OE1 . GLN A 1 145 ? 40.152 46.379 48.127 0.0000 23.93 ? 165  GLN A OE1 1 
ATOM   1141 N  NE2 . GLN A 1 145 ? 42.077 46.385 49.283 0.0000 23.93 ? 165  GLN A NE2 1 
ATOM   1142 N  N   . ALA A 1 146 ? 41.630 51.708 46.335 1.00   23.52 ? 166  ALA A N   1 
ATOM   1143 C  CA  . ALA A 1 146 ? 41.364 52.625 45.235 1.00   23.92 ? 166  ALA A CA  1 
ATOM   1144 C  C   . ALA A 1 146 ? 42.261 52.276 44.050 1.00   23.67 ? 166  ALA A C   1 
ATOM   1145 O  O   . ALA A 1 146 ? 41.782 52.083 42.934 1.00   24.32 ? 166  ALA A O   1 
ATOM   1146 C  CB  . ALA A 1 146 ? 41.614 54.060 45.680 1.00   24.82 ? 166  ALA A CB  1 
ATOM   1147 N  N   . GLU A 1 147 ? 43.563 52.188 44.308 1.00   24.10 ? 167  GLU A N   1 
ATOM   1148 C  CA  . GLU A 1 147 ? 44.535 51.857 43.270 1.00   22.69 ? 167  GLU A CA  1 
ATOM   1149 C  C   . GLU A 1 147 ? 44.283 50.464 42.698 1.00   21.18 ? 167  GLU A C   1 
ATOM   1150 O  O   . GLU A 1 147 ? 44.413 50.242 41.496 1.00   19.34 ? 167  GLU A O   1 
ATOM   1151 C  CB  . GLU A 1 147 ? 45.950 51.922 43.840 1.00   23.39 ? 167  GLU A CB  1 
ATOM   1152 C  CG  . GLU A 1 147 ? 46.358 53.298 44.329 1.00   28.20 ? 167  GLU A CG  1 
ATOM   1153 C  CD  . GLU A 1 147 ? 47.724 53.301 44.986 1.00   30.39 ? 167  GLU A CD  1 
ATOM   1154 O  OE1 . GLU A 1 147 ? 47.895 52.619 46.021 1.00   32.37 ? 167  GLU A OE1 1 
ATOM   1155 O  OE2 . GLU A 1 147 ? 48.630 53.986 44.466 1.00   33.43 ? 167  GLU A OE2 1 
ATOM   1156 N  N   . CYS A 1 148 ? 43.919 49.531 43.570 1.00   19.85 ? 168  CYS A N   1 
ATOM   1157 C  CA  . CYS A 1 148 ? 43.656 48.153 43.172 1.00   19.89 ? 168  CYS A CA  1 
ATOM   1158 C  C   . CYS A 1 148 ? 42.503 48.089 42.179 1.00   21.29 ? 168  CYS A C   1 
ATOM   1159 O  O   . CYS A 1 148 ? 42.614 47.469 41.122 1.00   20.28 ? 168  CYS A O   1 
ATOM   1160 C  CB  . CYS A 1 148 ? 43.322 47.327 44.413 1.00   19.77 ? 168  CYS A CB  1 
ATOM   1161 S  SG  . CYS A 1 148 ? 43.448 45.511 44.297 1.00   17.56 ? 168  CYS A SG  1 
ATOM   1162 N  N   . LYS A 1 149 ? 41.393 48.732 42.526 1.00   22.18 ? 169  LYS A N   1 
ATOM   1163 C  CA  . LYS A 1 149 ? 40.220 48.740 41.661 1.00   23.42 ? 169  LYS A CA  1 
ATOM   1164 C  C   . LYS A 1 149 ? 40.494 49.472 40.349 1.00   23.16 ? 169  LYS A C   1 
ATOM   1165 O  O   . LYS A 1 149 ? 39.978 49.090 39.300 1.00   24.74 ? 169  LYS A O   1 
ATOM   1166 C  CB  . LYS A 1 149 ? 39.037 49.392 42.385 1.00   24.05 ? 169  LYS A CB  1 
ATOM   1167 C  CG  . LYS A 1 149 ? 38.537 48.599 43.583 1.00   23.78 ? 169  LYS A CG  1 
ATOM   1168 C  CD  . LYS A 1 149 ? 37.331 49.267 44.230 1.00   24.89 ? 169  LYS A CD  1 
ATOM   1169 C  CE  . LYS A 1 149 ? 36.823 48.462 45.415 0.0000 24.56 ? 169  LYS A CE  1 
ATOM   1170 N  NZ  . LYS A 1 149 ? 35.638 49.099 46.054 0.0000 24.69 ? 169  LYS A NZ  1 
ATOM   1171 N  N   . ALA A 1 150 ? 41.310 50.519 40.411 1.00   23.65 ? 170  ALA A N   1 
ATOM   1172 C  CA  . ALA A 1 150 ? 41.641 51.293 39.219 1.00   24.19 ? 170  ALA A CA  1 
ATOM   1173 C  C   . ALA A 1 150 ? 42.450 50.453 38.235 1.00   24.45 ? 170  ALA A C   1 
ATOM   1174 O  O   . ALA A 1 150 ? 42.337 50.623 37.020 1.00   25.96 ? 170  ALA A O   1 
ATOM   1175 C  CB  . ALA A 1 150 ? 42.425 52.538 39.607 1.00   23.65 ? 170  ALA A CB  1 
ATOM   1176 N  N   . SER A 1 151 ? 43.265 49.546 38.766 1.00   23.51 ? 171  SER A N   1 
ATOM   1177 C  CA  . SER A 1 151 ? 44.098 48.681 37.936 1.00   22.70 ? 171  SER A CA  1 
ATOM   1178 C  C   . SER A 1 151 ? 43.297 47.548 37.303 1.00   21.42 ? 171  SER A C   1 
ATOM   1179 O  O   . SER A 1 151 ? 43.605 47.096 36.200 1.00   23.33 ? 171  SER A O   1 
ATOM   1180 C  CB  . SER A 1 151 ? 45.237 48.083 38.772 1.00   21.90 ? 171  SER A CB  1 
ATOM   1181 O  OG  . SER A 1 151 ? 46.064 49.093 39.318 1.00   24.61 ? 171  SER A OG  1 
ATOM   1182 N  N   . TYR A 1 152 ? 42.269 47.088 38.007 1.00   21.30 ? 172  TYR A N   1 
ATOM   1183 C  CA  . TYR A 1 152 ? 41.435 45.996 37.520 1.00   21.95 ? 172  TYR A CA  1 
ATOM   1184 C  C   . TYR A 1 152 ? 39.956 46.348 37.649 1.00   23.88 ? 172  TYR A C   1 
ATOM   1185 O  O   . TYR A 1 152 ? 39.230 45.762 38.452 1.00   23.39 ? 172  TYR A O   1 
ATOM   1186 C  CB  . TYR A 1 152 ? 41.738 44.726 38.316 1.00   20.70 ? 172  TYR A CB  1 
ATOM   1187 C  CG  . TYR A 1 152 ? 43.174 44.257 38.199 1.00   20.34 ? 172  TYR A CG  1 
ATOM   1188 C  CD1 . TYR A 1 152 ? 43.632 43.634 37.039 1.00   20.10 ? 172  TYR A CD1 1 
ATOM   1189 C  CD2 . TYR A 1 152 ? 44.069 44.425 39.253 1.00   20.30 ? 172  TYR A CD2 1 
ATOM   1190 C  CE1 . TYR A 1 152 ? 44.949 43.183 36.934 1.00   20.63 ? 172  TYR A CE1 1 
ATOM   1191 C  CE2 . TYR A 1 152 ? 45.388 43.982 39.159 1.00   19.40 ? 172  TYR A CE2 1 
ATOM   1192 C  CZ  . TYR A 1 152 ? 45.820 43.360 37.999 1.00   19.77 ? 172  TYR A CZ  1 
ATOM   1193 O  OH  . TYR A 1 152 ? 47.115 42.902 37.913 1.00   18.05 ? 172  TYR A OH  1 
ATOM   1194 N  N   . PRO A 1 153 ? 39.489 47.318 36.850 1.00   25.48 ? 173  PRO A N   1 
ATOM   1195 C  CA  . PRO A 1 153 ? 38.089 47.749 36.881 1.00   25.31 ? 173  PRO A CA  1 
ATOM   1196 C  C   . PRO A 1 153 ? 37.077 46.605 36.837 1.00   24.96 ? 173  PRO A C   1 
ATOM   1197 O  O   . PRO A 1 153 ? 37.120 45.758 35.947 1.00   26.99 ? 173  PRO A O   1 
ATOM   1198 C  CB  . PRO A 1 153 ? 37.990 48.663 35.664 1.00   26.17 ? 173  PRO A CB  1 
ATOM   1199 C  CG  . PRO A 1 153 ? 39.351 49.284 35.618 1.00   25.67 ? 173  PRO A CG  1 
ATOM   1200 C  CD  . PRO A 1 153 ? 40.255 48.096 35.859 1.00   25.70 ? 173  PRO A CD  1 
ATOM   1201 N  N   . GLY A 1 154 ? 36.176 46.586 37.816 1.00   25.56 ? 174  GLY A N   1 
ATOM   1202 C  CA  . GLY A 1 154 ? 35.144 45.566 37.880 1.00   26.54 ? 174  GLY A CA  1 
ATOM   1203 C  C   . GLY A 1 154 ? 35.583 44.128 38.097 1.00   27.07 ? 174  GLY A C   1 
ATOM   1204 O  O   . GLY A 1 154 ? 34.823 43.202 37.815 1.00   27.89 ? 174  GLY A O   1 
ATOM   1205 N  N   . LYS A 1 155 ? 36.794 43.926 38.604 1.00   26.33 ? 175  LYS A N   1 
ATOM   1206 C  CA  . LYS A 1 155 ? 37.287 42.572 38.839 1.00   25.91 ? 175  LYS A CA  1 
ATOM   1207 C  C   . LYS A 1 155 ? 37.690 42.327 40.291 1.00   25.15 ? 175  LYS A C   1 
ATOM   1208 O  O   . LYS A 1 155 ? 37.928 41.187 40.686 1.00   26.06 ? 175  LYS A O   1 
ATOM   1209 C  CB  . LYS A 1 155 ? 38.485 42.279 37.926 1.00   25.62 ? 175  LYS A CB  1 
ATOM   1210 C  CG  . LYS A 1 155 ? 38.157 42.266 36.439 1.00   26.93 ? 175  LYS A CG  1 
ATOM   1211 C  CD  . LYS A 1 155 ? 39.394 41.970 35.606 0.0000 26.58 ? 175  LYS A CD  1 
ATOM   1212 C  CE  . LYS A 1 155 ? 39.067 41.936 34.122 0.0000 26.71 ? 175  LYS A CE  1 
ATOM   1213 N  NZ  . LYS A 1 155 ? 38.065 40.882 33.800 0.0000 26.65 ? 175  LYS A NZ  1 
ATOM   1214 N  N   . ILE A 1 156 ? 37.758 43.393 41.082 1.00   23.74 ? 176  ILE A N   1 
ATOM   1215 C  CA  . ILE A 1 156 ? 38.152 43.275 42.483 1.00   24.30 ? 176  ILE A CA  1 
ATOM   1216 C  C   . ILE A 1 156 ? 36.949 43.127 43.412 1.00   25.55 ? 176  ILE A C   1 
ATOM   1217 O  O   . ILE A 1 156 ? 36.072 43.990 43.450 1.00   27.25 ? 176  ILE A O   1 
ATOM   1218 C  CB  . ILE A 1 156 ? 38.979 44.506 42.931 1.00   23.51 ? 176  ILE A CB  1 
ATOM   1219 C  CG1 . ILE A 1 156 ? 40.190 44.683 42.009 1.00   23.70 ? 176  ILE A CG1 1 
ATOM   1220 C  CG2 . ILE A 1 156 ? 39.435 44.338 44.377 1.00   22.95 ? 176  ILE A CG2 1 
ATOM   1221 C  CD1 . ILE A 1 156 ? 41.138 43.494 41.987 1.00   23.68 ? 176  ILE A CD1 1 
ATOM   1222 N  N   . THR A 1 157 ? 36.915 42.028 44.158 1.00   24.93 ? 177  THR A N   1 
ATOM   1223 C  CA  . THR A 1 157 ? 35.825 41.775 45.095 1.00   25.17 ? 177  THR A CA  1 
ATOM   1224 C  C   . THR A 1 157 ? 36.281 42.095 46.515 1.00   25.01 ? 177  THR A C   1 
ATOM   1225 O  O   . THR A 1 157 ? 37.416 42.526 46.734 1.00   23.61 ? 177  THR A O   1 
ATOM   1226 C  CB  . THR A 1 157 ? 35.372 40.307 45.051 1.00   25.14 ? 177  THR A CB  1 
ATOM   1227 O  OG1 . THR A 1 157 ? 36.418 39.470 45.560 1.00   25.26 ? 177  THR A OG1 1 
ATOM   1228 C  CG2 . THR A 1 157 ? 35.051 39.892 43.627 1.00   24.20 ? 177  THR A CG2 1 
ATOM   1229 N  N   . ASN A 1 158 ? 35.394 41.874 47.480 1.00   23.73 ? 178  ASN A N   1 
ATOM   1230 C  CA  . ASN A 1 158 ? 35.698 42.149 48.878 1.00   23.86 ? 178  ASN A CA  1 
ATOM   1231 C  C   . ASN A 1 158 ? 36.752 41.206 49.462 1.00   21.98 ? 178  ASN A C   1 
ATOM   1232 O  O   . ASN A 1 158 ? 37.337 41.496 50.504 1.00   23.06 ? 178  ASN A O   1 
ATOM   1233 C  CB  . ASN A 1 158 ? 34.416 42.065 49.716 1.00   25.11 ? 178  ASN A CB  1 
ATOM   1234 C  CG  . ASN A 1 158 ? 33.347 43.031 49.245 0.0000 24.74 ? 178  ASN A CG  1 
ATOM   1235 O  OD1 . ASN A 1 158 ? 33.552 44.245 49.232 0.0000 24.90 ? 178  ASN A OD1 1 
ATOM   1236 N  ND2 . ASN A 1 158 ? 32.196 42.495 48.854 0.0000 24.90 ? 178  ASN A ND2 1 
ATOM   1237 N  N   . SER A 1 159 ? 36.999 40.086 48.790 1.00   21.68 ? 179  SER A N   1 
ATOM   1238 C  CA  . SER A 1 159 ? 37.980 39.119 49.283 1.00   19.58 ? 179  SER A CA  1 
ATOM   1239 C  C   . SER A 1 159 ? 39.379 39.359 48.725 1.00   18.64 ? 179  SER A C   1 
ATOM   1240 O  O   . SER A 1 159 ? 40.298 38.600 49.013 1.00   17.04 ? 179  SER A O   1 
ATOM   1241 C  CB  . SER A 1 159 ? 37.551 37.692 48.925 1.00   21.45 ? 179  SER A CB  1 
ATOM   1242 O  OG  . SER A 1 159 ? 37.761 37.410 47.549 1.00   22.60 ? 179  SER A OG  1 
ATOM   1243 N  N   . MET A 1 160 ? 39.542 40.426 47.948 1.00   16.82 ? 180  MET A N   1 
ATOM   1244 C  CA  . MET A 1 160 ? 40.832 40.714 47.321 1.00   16.79 ? 180  MET A CA  1 
ATOM   1245 C  C   . MET A 1 160 ? 41.498 42.028 47.713 1.00   16.31 ? 180  MET A C   1 
ATOM   1246 O  O   . MET A 1 160 ? 40.834 42.994 48.088 1.00   18.32 ? 180  MET A O   1 
ATOM   1247 C  CB  . MET A 1 160 ? 40.661 40.723 45.799 1.00   16.68 ? 180  MET A CB  1 
ATOM   1248 C  CG  . MET A 1 160 ? 40.058 39.467 45.200 1.00   17.42 ? 180  MET A CG  1 
ATOM   1249 S  SD  . MET A 1 160 ? 39.590 39.735 43.468 1.00   19.39 ? 180  MET A SD  1 
ATOM   1250 C  CE  . MET A 1 160 ? 38.510 38.352 43.197 1.00   20.31 ? 180  MET A CE  1 
ATOM   1251 N  N   . PHE A 1 161 ? 42.825 42.051 47.633 1.00   15.25 ? 181  PHE A N   1 
ATOM   1252 C  CA  . PHE A 1 161 ? 43.576 43.272 47.880 1.00   12.97 ? 181  PHE A CA  1 
ATOM   1253 C  C   . PHE A 1 161 ? 44.844 43.220 47.041 1.00   13.63 ? 181  PHE A C   1 
ATOM   1254 O  O   . PHE A 1 161 ? 45.284 42.143 46.626 1.00   13.34 ? 181  PHE A O   1 
ATOM   1255 C  CB  . PHE A 1 161 ? 43.871 43.500 49.377 1.00   13.11 ? 181  PHE A CB  1 
ATOM   1256 C  CG  . PHE A 1 161 ? 44.933 42.613 49.964 1.00   13.74 ? 181  PHE A CG  1 
ATOM   1257 C  CD1 . PHE A 1 161 ? 44.674 41.273 50.238 1.00   13.17 ? 181  PHE A CD1 1 
ATOM   1258 C  CD2 . PHE A 1 161 ? 46.172 43.143 50.322 1.00   13.52 ? 181  PHE A CD2 1 
ATOM   1259 C  CE1 . PHE A 1 161 ? 45.632 40.473 50.868 1.00   12.85 ? 181  PHE A CE1 1 
ATOM   1260 C  CE2 . PHE A 1 161 ? 47.139 42.355 50.951 1.00   14.77 ? 181  PHE A CE2 1 
ATOM   1261 C  CZ  . PHE A 1 161 ? 46.865 41.013 51.226 1.00   12.79 ? 181  PHE A CZ  1 
ATOM   1262 N  N   . CYS A 1 162 ? 45.403 44.386 46.746 1.00   13.31 ? 182  CYS A N   1 
ATOM   1263 C  CA  . CYS A 1 162 ? 46.601 44.446 45.922 1.00   14.34 ? 182  CYS A CA  1 
ATOM   1264 C  C   . CYS A 1 162 ? 47.871 44.760 46.692 1.00   13.40 ? 182  CYS A C   1 
ATOM   1265 O  O   . CYS A 1 162 ? 47.865 45.528 47.656 1.00   13.56 ? 182  CYS A O   1 
ATOM   1266 C  CB  . CYS A 1 162 ? 46.443 45.504 44.834 1.00   16.26 ? 182  CYS A CB  1 
ATOM   1267 S  SG  . CYS A 1 162 ? 45.275 45.194 43.472 1.00   17.64 ? 182  CYS A SG  1 
ATOM   1268 N  N   . VAL A 1 163 ? 48.971 44.169 46.239 1.00   13.02 ? 183  VAL A N   1 
ATOM   1269 C  CA  . VAL A 1 163 ? 50.277 44.393 46.843 1.00   11.82 ? 183  VAL A CA  1 
ATOM   1270 C  C   . VAL A 1 163 ? 51.259 44.486 45.683 1.00   13.16 ? 183  VAL A C   1 
ATOM   1271 O  O   . VAL A 1 163 ? 51.159 43.717 44.727 1.00   13.14 ? 183  VAL A O   1 
ATOM   1272 C  CB  . VAL A 1 163 ? 50.697 43.214 47.749 1.00   12.91 ? 183  VAL A CB  1 
ATOM   1273 C  CG1 . VAL A 1 163 ? 52.071 43.479 48.348 1.00   14.41 ? 183  VAL A CG1 1 
ATOM   1274 C  CG2 . VAL A 1 163 ? 49.668 43.009 48.849 1.00   14.11 ? 183  VAL A CG2 1 
ATOM   1275 N  N   . GLY A 1 164 ? 52.188 45.434 45.752 1.00   13.64 ? 184  GLY A N   1 
ATOM   1276 C  CA  . GLY A 1 164 ? 53.160 45.561 44.681 1.00   15.06 ? 184  GLY A CA  1 
ATOM   1277 C  C   . GLY A 1 164 ? 53.543 46.978 44.306 1.00   16.69 ? 184  GLY A C   1 
ATOM   1278 O  O   . GLY A 1 164 ? 53.508 47.890 45.134 1.00   16.03 ? 184  GLY A O   1 
ATOM   1279 N  N   . PHE A 1 165 A 53.912 47.154 43.041 1.00   17.61 ? 184  PHE A N   1 
ATOM   1280 C  CA  . PHE A 1 165 A 54.335 48.450 42.528 1.00   18.43 ? 184  PHE A CA  1 
ATOM   1281 C  C   . PHE A 1 165 A 53.643 48.750 41.206 1.00   19.43 ? 184  PHE A C   1 
ATOM   1282 O  O   . PHE A 1 165 A 53.692 47.949 40.274 1.00   20.13 ? 184  PHE A O   1 
ATOM   1283 C  CB  . PHE A 1 165 A 55.854 48.464 42.324 1.00   18.14 ? 184  PHE A CB  1 
ATOM   1284 C  CG  . PHE A 1 165 A 56.633 48.011 43.528 1.00   17.93 ? 184  PHE A CG  1 
ATOM   1285 C  CD1 . PHE A 1 165 A 56.777 46.654 43.814 1.00   19.28 ? 184  PHE A CD1 1 
ATOM   1286 C  CD2 . PHE A 1 165 A 57.204 48.939 44.390 1.00   18.87 ? 184  PHE A CD2 1 
ATOM   1287 C  CE1 . PHE A 1 165 A 57.479 46.230 44.943 1.00   17.04 ? 184  PHE A CE1 1 
ATOM   1288 C  CE2 . PHE A 1 165 A 57.908 48.527 45.521 1.00   20.47 ? 184  PHE A CE2 1 
ATOM   1289 C  CZ  . PHE A 1 165 A 58.046 47.169 45.798 1.00   18.12 ? 184  PHE A CZ  1 
ATOM   1290 N  N   . LEU A 1 166 ? 53.001 49.908 41.125 1.00   20.37 ? 185  LEU A N   1 
ATOM   1291 C  CA  . LEU A 1 166 ? 52.298 50.295 39.909 1.00   21.69 ? 185  LEU A CA  1 
ATOM   1292 C  C   . LEU A 1 166 ? 53.250 50.487 38.727 1.00   21.01 ? 185  LEU A C   1 
ATOM   1293 O  O   . LEU A 1 166 ? 52.844 50.369 37.572 1.00   20.72 ? 185  LEU A O   1 
ATOM   1294 C  CB  . LEU A 1 166 ? 51.495 51.575 40.156 1.00   23.06 ? 185  LEU A CB  1 
ATOM   1295 C  CG  . LEU A 1 166 ? 50.378 51.457 41.201 1.00   24.82 ? 185  LEU A CG  1 
ATOM   1296 C  CD1 . LEU A 1 166 ? 49.719 52.813 41.411 1.00   27.44 ? 185  LEU A CD1 1 
ATOM   1297 C  CD2 . LEU A 1 166 ? 49.355 50.427 40.744 1.00   25.22 ? 185  LEU A CD2 1 
ATOM   1298 N  N   . GLU A 1 167 ? 54.514 50.783 39.017 1.00   21.59 ? 186  GLU A N   1 
ATOM   1299 C  CA  . GLU A 1 167 ? 55.506 50.977 37.965 1.00   23.96 ? 186  GLU A CA  1 
ATOM   1300 C  C   . GLU A 1 167 ? 55.951 49.642 37.370 1.00   24.64 ? 186  GLU A C   1 
ATOM   1301 O  O   . GLU A 1 167 ? 56.614 49.609 36.332 1.00   25.62 ? 186  GLU A O   1 
ATOM   1302 C  CB  . GLU A 1 167 ? 56.730 51.729 38.503 1.00   27.07 ? 186  GLU A CB  1 
ATOM   1303 C  CG  . GLU A 1 167 ? 57.394 51.081 39.712 1.00   32.45 ? 186  GLU A CG  1 
ATOM   1304 C  CD  . GLU A 1 167 ? 56.867 51.619 41.035 1.00   36.07 ? 186  GLU A CD  1 
ATOM   1305 O  OE1 . GLU A 1 167 ? 55.633 51.627 41.237 1.00   36.81 ? 186  GLU A OE1 1 
ATOM   1306 O  OE2 . GLU A 1 167 ? 57.694 52.029 41.877 1.00   37.76 ? 186  GLU A OE2 1 
ATOM   1307 N  N   . GLY A 1 168 ? 55.585 48.547 38.034 1.00   22.82 ? 187  GLY A N   1 
ATOM   1308 C  CA  . GLY A 1 168 ? 55.949 47.223 37.554 1.00   23.05 ? 187  GLY A CA  1 
ATOM   1309 C  C   . GLY A 1 168 ? 57.375 46.831 37.900 1.00   21.04 ? 187  GLY A C   1 
ATOM   1310 O  O   . GLY A 1 168 ? 58.048 47.528 38.659 1.00   23.64 ? 187  GLY A O   1 
ATOM   1311 N  N   . GLY A 1 169 ? 57.836 45.712 37.350 1.00   19.69 ? 188  GLY A N   1 
ATOM   1312 C  CA  . GLY A 1 169 ? 59.195 45.264 37.610 1.00   18.27 ? 188  GLY A CA  1 
ATOM   1313 C  C   . GLY A 1 169 ? 59.374 44.288 38.766 1.00   17.41 ? 188  GLY A C   1 
ATOM   1314 O  O   . GLY A 1 169 ? 60.303 43.477 38.756 1.00   16.82 ? 188  GLY A O   1 
ATOM   1315 N  N   . LYS A 1 170 A 58.502 44.370 39.766 1.00   15.98 ? 188  LYS A N   1 
ATOM   1316 C  CA  . LYS A 1 170 A 58.565 43.487 40.936 1.00   15.22 ? 188  LYS A CA  1 
ATOM   1317 C  C   . LYS A 1 170 A 57.157 42.972 41.187 1.00   14.33 ? 188  LYS A C   1 
ATOM   1318 O  O   . LYS A 1 170 A 56.236 43.769 41.358 1.00   14.64 ? 188  LYS A O   1 
ATOM   1319 C  CB  . LYS A 1 170 A 59.043 44.258 42.166 1.00   16.98 ? 188  LYS A CB  1 
ATOM   1320 C  CG  . LYS A 1 170 A 60.463 44.774 42.088 1.00   20.62 ? 188  LYS A CG  1 
ATOM   1321 C  CD  . LYS A 1 170 A 60.774 45.583 43.336 1.00   24.01 ? 188  LYS A CD  1 
ATOM   1322 C  CE  . LYS A 1 170 A 62.162 46.185 43.303 1.00   28.36 ? 188  LYS A CE  1 
ATOM   1323 N  NZ  . LYS A 1 170 A 62.368 47.067 44.488 1.00   28.10 ? 188  LYS A NZ  1 
ATOM   1324 N  N   . ASP A 1 171 ? 56.994 41.652 41.244 1.00   10.75 ? 189  ASP A N   1 
ATOM   1325 C  CA  . ASP A 1 171 ? 55.663 41.073 41.419 1.00   10.96 ? 189  ASP A CA  1 
ATOM   1326 C  C   . ASP A 1 171 ? 55.782 39.564 41.658 1.00   11.40 ? 189  ASP A C   1 
ATOM   1327 O  O   . ASP A 1 171 ? 56.866 38.993 41.522 1.00   12.16 ? 189  ASP A O   1 
ATOM   1328 C  CB  . ASP A 1 171 ? 54.884 41.345 40.119 1.00   11.67 ? 189  ASP A CB  1 
ATOM   1329 C  CG  . ASP A 1 171 ? 53.394 41.079 40.225 1.00   12.79 ? 189  ASP A CG  1 
ATOM   1330 O  OD1 . ASP A 1 171 ? 52.873 40.844 41.337 1.00   13.73 ? 189  ASP A OD1 1 
ATOM   1331 O  OD2 . ASP A 1 171 ? 52.735 41.123 39.159 1.00   11.50 ? 189  ASP A OD2 1 
ATOM   1332 N  N   . SER A 1 172 ? 54.682 38.925 42.046 1.00   9.24  ? 190  SER A N   1 
ATOM   1333 C  CA  . SER A 1 172 ? 54.692 37.470 42.197 1.00   10.40 ? 190  SER A CA  1 
ATOM   1334 C  C   . SER A 1 172 ? 54.276 36.983 40.805 1.00   10.38 ? 190  SER A C   1 
ATOM   1335 O  O   . SER A 1 172 ? 53.972 37.804 39.938 1.00   10.67 ? 190  SER A O   1 
ATOM   1336 C  CB  . SER A 1 172 ? 53.692 37.009 43.270 1.00   10.55 ? 190  SER A CB  1 
ATOM   1337 O  OG  . SER A 1 172 ? 52.391 37.516 43.032 1.00   12.47 ? 190  SER A OG  1 
ATOM   1338 N  N   . CYS A 1 173 ? 54.244 35.676 40.573 1.00   10.20 ? 191  CYS A N   1 
ATOM   1339 C  CA  . CYS A 1 173 ? 53.887 35.191 39.242 1.00   11.95 ? 191  CYS A CA  1 
ATOM   1340 C  C   . CYS A 1 173 ? 53.398 33.741 39.269 1.00   12.75 ? 191  CYS A C   1 
ATOM   1341 O  O   . CYS A 1 173 ? 53.180 33.170 40.338 1.00   11.62 ? 191  CYS A O   1 
ATOM   1342 C  CB  . CYS A 1 173 ? 55.119 35.339 38.336 1.00   10.98 ? 191  CYS A CB  1 
ATOM   1343 S  SG  . CYS A 1 173 ? 54.863 35.294 36.527 1.00   12.73 ? 191  CYS A SG  1 
ATOM   1344 N  N   A GLN A 1 174 ? 53.226 33.157 38.087 0.66   12.97 ? 192  GLN A N   1 
ATOM   1345 N  N   B GLN A 1 174 ? 53.221 33.157 38.088 0.33   13.02 ? 192  GLN A N   1 
ATOM   1346 C  CA  A GLN A 1 174 ? 52.779 31.771 37.960 0.66   14.92 ? 192  GLN A CA  1 
ATOM   1347 C  CA  B GLN A 1 174 ? 52.755 31.779 37.972 0.33   14.33 ? 192  GLN A CA  1 
ATOM   1348 C  C   A GLN A 1 174 ? 53.555 30.847 38.897 0.66   13.04 ? 192  GLN A C   1 
ATOM   1349 C  C   B GLN A 1 174 ? 53.548 30.840 38.880 0.33   13.19 ? 192  GLN A C   1 
ATOM   1350 O  O   A GLN A 1 174 ? 54.782 30.923 38.989 0.66   12.87 ? 192  GLN A O   1 
ATOM   1351 O  O   B GLN A 1 174 ? 54.777 30.901 38.936 0.33   13.25 ? 192  GLN A O   1 
ATOM   1352 C  CB  A GLN A 1 174 ? 52.966 31.282 36.517 0.66   17.61 ? 192  GLN A CB  1 
ATOM   1353 C  CB  B GLN A 1 174 ? 52.853 31.309 36.516 0.33   16.10 ? 192  GLN A CB  1 
ATOM   1354 C  CG  A GLN A 1 174 ? 51.728 31.344 35.630 0.66   24.69 ? 192  GLN A CG  1 
ATOM   1355 C  CG  B GLN A 1 174 ? 51.964 32.086 35.546 0.33   20.20 ? 192  GLN A CG  1 
ATOM   1356 C  CD  A GLN A 1 174 ? 51.214 32.752 35.411 0.66   27.39 ? 192  GLN A CD  1 
ATOM   1357 C  CD  B GLN A 1 174 ? 50.479 31.872 35.795 0.33   21.78 ? 192  GLN A CD  1 
ATOM   1358 O  OE1 A GLN A 1 174 ? 51.962 33.647 35.016 0.66   30.05 ? 192  GLN A OE1 1 
ATOM   1359 O  OE1 B GLN A 1 174 ? 49.638 32.536 35.191 0.33   25.09 ? 192  GLN A OE1 1 
ATOM   1360 N  NE2 A GLN A 1 174 ? 49.925 32.950 35.652 0.66   31.86 ? 192  GLN A NE2 1 
ATOM   1361 N  NE2 B GLN A 1 174 ? 50.151 30.939 36.680 0.33   22.79 ? 192  GLN A NE2 1 
ATOM   1362 N  N   . ARG A 1 175 ? 52.821 29.980 39.587 1.00   12.55 ? 193  ARG A N   1 
ATOM   1363 C  CA  . ARG A 1 175 ? 53.390 29.011 40.522 1.00   12.57 ? 193  ARG A CA  1 
ATOM   1364 C  C   . ARG A 1 175 ? 53.829 29.576 41.871 1.00   11.98 ? 193  ARG A C   1 
ATOM   1365 O  O   . ARG A 1 175 ? 54.360 28.855 42.704 1.00   11.18 ? 193  ARG A O   1 
ATOM   1366 C  CB  . ARG A 1 175 ? 54.507 28.201 39.860 1.00   14.10 ? 193  ARG A CB  1 
ATOM   1367 C  CG  . ARG A 1 175 ? 53.985 27.439 38.651 1.00   16.29 ? 193  ARG A CG  1 
ATOM   1368 C  CD  . ARG A 1 175 ? 54.994 26.474 38.073 1.00   19.18 ? 193  ARG A CD  1 
ATOM   1369 N  NE  . ARG A 1 175 ? 54.570 26.031 36.748 1.00   22.36 ? 193  ARG A NE  1 
ATOM   1370 C  CZ  . ARG A 1 175 ? 55.301 25.266 35.946 1.00   24.78 ? 193  ARG A CZ  1 
ATOM   1371 N  NH1 . ARG A 1 175 ? 56.499 24.848 36.332 1.00   24.97 ? 193  ARG A NH1 1 
ATOM   1372 N  NH2 . ARG A 1 175 ? 54.841 24.937 34.748 1.00   28.40 ? 193  ARG A NH2 1 
ATOM   1373 N  N   . ASP A 1 176 ? 53.619 30.875 42.070 1.00   12.79 ? 194  ASP A N   1 
ATOM   1374 C  CA  . ASP A 1 176 ? 53.871 31.487 43.372 1.00   10.46 ? 194  ASP A CA  1 
ATOM   1375 C  C   . ASP A 1 176 ? 52.487 31.361 44.011 1.00   9.92  ? 194  ASP A C   1 
ATOM   1376 O  O   . ASP A 1 176 ? 52.323 31.485 45.222 1.00   10.76 ? 194  ASP A O   1 
ATOM   1377 C  CB  . ASP A 1 176 ? 54.208 32.976 43.265 1.00   9.48  ? 194  ASP A CB  1 
ATOM   1378 C  CG  . ASP A 1 176 ? 55.657 33.229 42.914 1.00   10.66 ? 194  ASP A CG  1 
ATOM   1379 O  OD1 . ASP A 1 176 ? 56.533 32.484 43.406 1.00   11.59 ? 194  ASP A OD1 1 
ATOM   1380 O  OD2 . ASP A 1 176 ? 55.917 34.193 42.164 1.00   11.26 ? 194  ASP A OD2 1 
ATOM   1381 N  N   . SER A 1 177 ? 51.496 31.136 43.149 1.00   10.64 ? 195  SER A N   1 
ATOM   1382 C  CA  . SER A 1 177 ? 50.094 30.983 43.531 1.00   10.70 ? 195  SER A CA  1 
ATOM   1383 C  C   . SER A 1 177 ? 49.915 30.135 44.784 1.00   9.25  ? 195  SER A C   1 
ATOM   1384 O  O   . SER A 1 177 ? 50.550 29.086 44.927 1.00   11.26 ? 195  SER A O   1 
ATOM   1385 C  CB  . SER A 1 177 ? 49.308 30.331 42.385 1.00   13.83 ? 195  SER A CB  1 
ATOM   1386 O  OG  . SER A 1 177 ? 49.398 31.091 41.193 1.00   17.34 ? 195  SER A OG  1 
ATOM   1387 N  N   . GLY A 1 178 ? 49.045 30.599 45.677 1.00   8.88  ? 196  GLY A N   1 
ATOM   1388 C  CA  . GLY A 1 178 ? 48.768 29.884 46.910 1.00   9.18  ? 196  GLY A CA  1 
ATOM   1389 C  C   . GLY A 1 178 ? 49.746 30.217 48.018 1.00   9.90  ? 196  GLY A C   1 
ATOM   1390 O  O   . GLY A 1 178 ? 49.510 29.888 49.183 1.00   10.55 ? 196  GLY A O   1 
ATOM   1391 N  N   . GLY A 1 179 ? 50.837 30.881 47.640 1.00   10.20 ? 197  GLY A N   1 
ATOM   1392 C  CA  . GLY A 1 179 ? 51.878 31.258 48.579 1.00   9.99  ? 197  GLY A CA  1 
ATOM   1393 C  C   . GLY A 1 179 ? 51.505 32.363 49.545 1.00   10.68 ? 197  GLY A C   1 
ATOM   1394 O  O   . GLY A 1 179 ? 50.462 33.003 49.413 1.00   9.92  ? 197  GLY A O   1 
ATOM   1395 N  N   . PRO A 1 180 ? 52.374 32.633 50.523 1.00   9.62  ? 198  PRO A N   1 
ATOM   1396 C  CA  . PRO A 1 180 ? 52.127 33.663 51.529 1.00   9.85  ? 198  PRO A CA  1 
ATOM   1397 C  C   . PRO A 1 180 ? 52.538 35.100 51.255 1.00   11.23 ? 198  PRO A C   1 
ATOM   1398 O  O   . PRO A 1 180 ? 53.474 35.380 50.505 1.00   9.81  ? 198  PRO A O   1 
ATOM   1399 C  CB  . PRO A 1 180 ? 52.877 33.123 52.735 1.00   10.48 ? 198  PRO A CB  1 
ATOM   1400 C  CG  . PRO A 1 180 ? 54.117 32.573 52.092 1.00   11.92 ? 198  PRO A CG  1 
ATOM   1401 C  CD  . PRO A 1 180 ? 53.583 31.855 50.857 1.00   9.27  ? 198  PRO A CD  1 
ATOM   1402 N  N   . VAL A 1 181 ? 51.801 35.996 51.900 1.00   9.69  ? 199  VAL A N   1 
ATOM   1403 C  CA  . VAL A 1 181 ? 52.077 37.422 51.902 1.00   9.13  ? 199  VAL A CA  1 
ATOM   1404 C  C   . VAL A 1 181 ? 52.049 37.661 53.404 1.00   9.14  ? 199  VAL A C   1 
ATOM   1405 O  O   . VAL A 1 181 ? 50.989 37.617 54.027 1.00   10.53 ? 199  VAL A O   1 
ATOM   1406 C  CB  . VAL A 1 181 ? 50.975 38.251 51.239 1.00   10.71 ? 199  VAL A CB  1 
ATOM   1407 C  CG1 . VAL A 1 181 ? 51.278 39.736 51.426 1.00   11.86 ? 199  VAL A CG1 1 
ATOM   1408 C  CG2 . VAL A 1 181 ? 50.902 37.914 49.763 1.00   12.67 ? 199  VAL A CG2 1 
ATOM   1409 N  N   . VAL A 1 182 ? 53.221 37.873 53.991 1.00   8.35  ? 200  VAL A N   1 
ATOM   1410 C  CA  . VAL A 1 182 ? 53.315 38.070 55.430 1.00   8.34  ? 200  VAL A CA  1 
ATOM   1411 C  C   . VAL A 1 182 ? 53.659 39.511 55.743 1.00   10.13 ? 200  VAL A C   1 
ATOM   1412 O  O   . VAL A 1 182 ? 54.611 40.056 55.195 1.00   10.90 ? 200  VAL A O   1 
ATOM   1413 C  CB  . VAL A 1 182 ? 54.399 37.144 56.033 1.00   10.26 ? 200  VAL A CB  1 
ATOM   1414 C  CG1 . VAL A 1 182 ? 54.623 37.471 57.508 1.00   10.63 ? 200  VAL A CG1 1 
ATOM   1415 C  CG2 . VAL A 1 182 ? 53.975 35.687 55.873 1.00   12.14 ? 200  VAL A CG2 1 
ATOM   1416 N  N   . CYS A 1 183 ? 52.874 40.127 56.619 1.00   11.88 ? 201  CYS A N   1 
ATOM   1417 C  CA  . CYS A 1 183 ? 53.121 41.511 56.999 1.00   14.73 ? 201  CYS A CA  1 
ATOM   1418 C  C   . CYS A 1 183 ? 53.093 41.564 58.520 1.00   17.87 ? 201  CYS A C   1 
ATOM   1419 O  O   . CYS A 1 183 ? 52.143 41.092 59.142 1.00   15.52 ? 201  CYS A O   1 
ATOM   1420 C  CB  . CYS A 1 183 ? 52.035 42.435 56.439 1.00   14.67 ? 201  CYS A CB  1 
ATOM   1421 S  SG  . CYS A 1 183 ? 51.359 42.010 54.797 1.00   15.18 ? 201  CYS A SG  1 
ATOM   1422 N  N   . ASN A 1 184 ? 54.142 42.121 59.115 1.00   19.63 ? 202  ASN A N   1 
ATOM   1423 C  CA  . ASN A 1 184 ? 54.218 42.232 60.569 1.00   21.99 ? 202  ASN A CA  1 
ATOM   1424 C  C   . ASN A 1 184 ? 54.026 40.885 61.263 1.00   20.50 ? 202  ASN A C   1 
ATOM   1425 O  O   . ASN A 1 184 ? 53.325 40.790 62.272 1.00   21.43 ? 202  ASN A O   1 
ATOM   1426 C  CB  . ASN A 1 184 ? 53.165 43.226 61.071 1.00   25.78 ? 202  ASN A CB  1 
ATOM   1427 C  CG  . ASN A 1 184 ? 53.378 44.626 60.525 1.00   30.64 ? 202  ASN A CG  1 
ATOM   1428 O  OD1 . ASN A 1 184 ? 52.512 45.491 60.653 1.00   34.79 ? 202  ASN A OD1 1 
ATOM   1429 N  ND2 . ASN A 1 184 ? 54.537 44.858 59.919 1.00   32.97 ? 202  ASN A ND2 1 
ATOM   1430 N  N   . GLY A 1 185 ? 54.638 39.844 60.711 1.00   18.71 ? 203  GLY A N   1 
ATOM   1431 C  CA  . GLY A 1 185 ? 54.542 38.526 61.314 1.00   17.95 ? 203  GLY A CA  1 
ATOM   1432 C  C   . GLY A 1 185 ? 53.220 37.790 61.208 1.00   16.64 ? 203  GLY A C   1 
ATOM   1433 O  O   . GLY A 1 185 ? 53.051 36.748 61.839 1.00   18.56 ? 203  GLY A O   1 
ATOM   1434 N  N   . GLN A 1 186 ? 52.281 38.310 60.425 1.00   13.98 ? 204  GLN A N   1 
ATOM   1435 C  CA  . GLN A 1 186 ? 50.993 37.638 60.269 1.00   12.40 ? 204  GLN A CA  1 
ATOM   1436 C  C   . GLN A 1 186 ? 50.713 37.339 58.800 1.00   12.58 ? 204  GLN A C   1 
ATOM   1437 O  O   . GLN A 1 186 ? 51.145 38.079 57.917 1.00   11.95 ? 204  GLN A O   1 
ATOM   1438 C  CB  . GLN A 1 186 ? 49.855 38.499 60.823 1.00   14.17 ? 204  GLN A CB  1 
ATOM   1439 C  CG  . GLN A 1 186 ? 50.021 38.913 62.275 1.00   15.99 ? 204  GLN A CG  1 
ATOM   1440 C  CD  . GLN A 1 186 ? 48.868 39.772 62.751 1.00   19.62 ? 204  GLN A CD  1 
ATOM   1441 O  OE1 . GLN A 1 186 ? 48.330 40.572 61.992 1.00   19.93 ? 204  GLN A OE1 1 
ATOM   1442 N  NE2 . GLN A 1 186 ? 48.489 39.617 64.017 1.00   24.14 ? 204  GLN A NE2 1 
ATOM   1443 N  N   . LEU A 1 187 ? 49.986 36.256 58.546 1.00   10.27 ? 209  LEU A N   1 
ATOM   1444 C  CA  . LEU A 1 187 ? 49.637 35.871 57.177 1.00   11.40 ? 209  LEU A CA  1 
ATOM   1445 C  C   . LEU A 1 187 ? 48.465 36.731 56.714 1.00   12.41 ? 209  LEU A C   1 
ATOM   1446 O  O   . LEU A 1 187 ? 47.316 36.460 57.060 1.00   14.02 ? 209  LEU A O   1 
ATOM   1447 C  CB  . LEU A 1 187 ? 49.236 34.390 57.124 1.00   10.71 ? 209  LEU A CB  1 
ATOM   1448 C  CG  . LEU A 1 187 ? 48.823 33.849 55.754 1.00   11.57 ? 209  LEU A CG  1 
ATOM   1449 C  CD1 . LEU A 1 187 ? 50.025 33.848 54.812 1.00   12.21 ? 209  LEU A CD1 1 
ATOM   1450 C  CD2 . LEU A 1 187 ? 48.283 32.438 55.919 1.00   15.37 ? 209  LEU A CD2 1 
ATOM   1451 N  N   . GLN A 1 188 ? 48.754 37.770 55.934 1.00   10.38 ? 210  GLN A N   1 
ATOM   1452 C  CA  . GLN A 1 188 ? 47.707 38.669 55.457 1.00   11.36 ? 210  GLN A CA  1 
ATOM   1453 C  C   . GLN A 1 188 ? 47.097 38.267 54.122 1.00   11.83 ? 210  GLN A C   1 
ATOM   1454 O  O   . GLN A 1 188 ? 45.927 38.550 53.852 1.00   10.23 ? 210  GLN A O   1 
ATOM   1455 C  CB  . GLN A 1 188 ? 48.255 40.092 55.349 1.00   10.93 ? 210  GLN A CB  1 
ATOM   1456 C  CG  . GLN A 1 188 ? 48.497 40.775 56.686 1.00   14.72 ? 210  GLN A CG  1 
ATOM   1457 C  CD  . GLN A 1 188 ? 47.208 41.148 57.394 1.00   15.71 ? 210  GLN A CD  1 
ATOM   1458 O  OE1 . GLN A 1 188 ? 46.115 40.960 56.860 1.00   17.64 ? 210  GLN A OE1 1 
ATOM   1459 N  NE2 . GLN A 1 188 ? 47.331 41.687 58.600 1.00   17.15 ? 210  GLN A NE2 1 
ATOM   1460 N  N   . GLY A 1 189 ? 47.879 37.613 53.274 1.00   11.27 ? 211  GLY A N   1 
ATOM   1461 C  CA  . GLY A 1 189 ? 47.330 37.231 51.992 1.00   10.58 ? 211  GLY A CA  1 
ATOM   1462 C  C   . GLY A 1 189 ? 47.844 35.945 51.395 1.00   10.32 ? 211  GLY A C   1 
ATOM   1463 O  O   . GLY A 1 189 ? 48.814 35.352 51.867 1.00   9.65  ? 211  GLY A O   1 
ATOM   1464 N  N   . VAL A 1 190 ? 47.158 35.524 50.341 1.00   10.25 ? 212  VAL A N   1 
ATOM   1465 C  CA  . VAL A 1 190 ? 47.489 34.327 49.584 1.00   9.92  ? 212  VAL A CA  1 
ATOM   1466 C  C   . VAL A 1 190 ? 47.648 34.763 48.123 1.00   10.07 ? 212  VAL A C   1 
ATOM   1467 O  O   . VAL A 1 190 ? 46.787 35.458 47.583 1.00   9.19  ? 212  VAL A O   1 
ATOM   1468 C  CB  . VAL A 1 190 ? 46.350 33.285 49.684 1.00   11.43 ? 212  VAL A CB  1 
ATOM   1469 C  CG1 . VAL A 1 190 ? 46.643 32.088 48.782 1.00   13.04 ? 212  VAL A CG1 1 
ATOM   1470 C  CG2 . VAL A 1 190 ? 46.193 32.832 51.136 1.00   12.86 ? 212  VAL A CG2 1 
ATOM   1471 N  N   . VAL A 1 191 ? 48.751 34.371 47.490 1.00   10.01 ? 213  VAL A N   1 
ATOM   1472 C  CA  . VAL A 1 191 ? 48.981 34.731 46.089 1.00   9.32  ? 213  VAL A CA  1 
ATOM   1473 C  C   . VAL A 1 191 ? 47.825 34.182 45.251 1.00   10.64 ? 213  VAL A C   1 
ATOM   1474 O  O   . VAL A 1 191 ? 47.588 32.973 45.226 1.00   10.90 ? 213  VAL A O   1 
ATOM   1475 C  CB  . VAL A 1 191 ? 50.312 34.143 45.567 1.00   8.34  ? 213  VAL A CB  1 
ATOM   1476 C  CG1 . VAL A 1 191 ? 50.524 34.567 44.116 1.00   8.40  ? 213  VAL A CG1 1 
ATOM   1477 C  CG2 . VAL A 1 191 ? 51.472 34.621 46.430 1.00   9.42  ? 213  VAL A CG2 1 
ATOM   1478 N  N   . SER A 1 192 ? 47.113 35.067 44.558 1.00   10.65 ? 214  SER A N   1 
ATOM   1479 C  CA  . SER A 1 192 ? 45.960 34.640 43.772 1.00   11.95 ? 214  SER A CA  1 
ATOM   1480 C  C   . SER A 1 192 ? 46.083 34.846 42.262 1.00   12.98 ? 214  SER A C   1 
ATOM   1481 O  O   . SER A 1 192 ? 46.171 33.877 41.505 1.00   14.09 ? 214  SER A O   1 
ATOM   1482 C  CB  . SER A 1 192 ? 44.702 35.344 44.292 1.00   12.25 ? 214  SER A CB  1 
ATOM   1483 O  OG  . SER A 1 192 ? 43.529 34.853 43.660 1.00   12.96 ? 214  SER A OG  1 
ATOM   1484 N  N   . TRP A 1 193 ? 46.093 36.098 41.818 1.00   13.23 ? 215  TRP A N   1 
ATOM   1485 C  CA  . TRP A 1 193 ? 46.182 36.355 40.386 1.00   14.22 ? 215  TRP A CA  1 
ATOM   1486 C  C   . TRP A 1 193 ? 46.703 37.734 40.010 1.00   14.32 ? 215  TRP A C   1 
ATOM   1487 O  O   . TRP A 1 193 ? 47.104 38.523 40.863 1.00   14.64 ? 215  TRP A O   1 
ATOM   1488 C  CB  . TRP A 1 193 ? 44.810 36.155 39.732 1.00   15.00 ? 215  TRP A CB  1 
ATOM   1489 C  CG  . TRP A 1 193 ? 43.748 37.109 40.219 1.00   17.13 ? 215  TRP A CG  1 
ATOM   1490 C  CD1 . TRP A 1 193 ? 43.006 36.996 41.359 1.00   17.44 ? 215  TRP A CD1 1 
ATOM   1491 C  CD2 . TRP A 1 193 ? 43.314 38.318 39.577 1.00   17.52 ? 215  TRP A CD2 1 
ATOM   1492 N  NE1 . TRP A 1 193 ? 42.136 38.057 41.466 1.00   17.99 ? 215  TRP A NE1 1 
ATOM   1493 C  CE2 . TRP A 1 193 ? 42.305 38.883 40.387 1.00   18.58 ? 215  TRP A CE2 1 
ATOM   1494 C  CE3 . TRP A 1 193 ? 43.683 38.978 38.393 1.00   19.43 ? 215  TRP A CE3 1 
ATOM   1495 C  CZ2 . TRP A 1 193 ? 41.655 40.079 40.054 1.00   20.47 ? 215  TRP A CZ2 1 
ATOM   1496 C  CZ3 . TRP A 1 193 ? 43.037 40.169 38.061 1.00   21.03 ? 215  TRP A CZ3 1 
ATOM   1497 C  CH2 . TRP A 1 193 ? 42.033 40.706 38.892 1.00   20.88 ? 215  TRP A CH2 1 
ATOM   1498 N  N   . GLY A 1 194 ? 46.683 37.999 38.705 1.00   13.55 ? 216  GLY A N   1 
ATOM   1499 C  CA  . GLY A 1 194 ? 47.124 39.271 38.164 1.00   15.11 ? 216  GLY A CA  1 
ATOM   1500 C  C   . GLY A 1 194 ? 47.183 39.146 36.654 1.00   15.68 ? 216  GLY A C   1 
ATOM   1501 O  O   . GLY A 1 194 ? 47.101 38.036 36.134 1.00   17.79 ? 216  GLY A O   1 
ATOM   1502 N  N   . HIS A 1 195 ? 47.289 40.268 35.949 1.00   16.35 ? 217  HIS A N   1 
ATOM   1503 C  CA  . HIS A 1 195 ? 47.393 40.236 34.492 1.00   17.97 ? 217  HIS A CA  1 
ATOM   1504 C  C   . HIS A 1 195 ? 48.880 40.329 34.174 1.00   16.08 ? 217  HIS A C   1 
ATOM   1505 O  O   . HIS A 1 195 ? 49.513 41.352 34.436 1.00   17.37 ? 217  HIS A O   1 
ATOM   1506 C  CB  . HIS A 1 195 ? 46.644 41.411 33.858 1.00   20.48 ? 217  HIS A CB  1 
ATOM   1507 C  CG  . HIS A 1 195 ? 45.153 41.291 33.935 1.00   25.53 ? 217  HIS A CG  1 
ATOM   1508 N  ND1 . HIS A 1 195 ? 44.512 40.089 34.148 1.00   27.73 ? 217  HIS A ND1 1 
ATOM   1509 C  CD2 . HIS A 1 195 ? 44.175 42.216 33.780 1.00   27.16 ? 217  HIS A CD2 1 
ATOM   1510 C  CE1 . HIS A 1 195 ? 43.205 40.278 34.121 1.00   27.93 ? 217  HIS A CE1 1 
ATOM   1511 N  NE2 . HIS A 1 195 ? 42.974 41.560 33.898 1.00   28.56 ? 217  HIS A NE2 1 
ATOM   1512 N  N   . GLY A 1 196 ? 49.432 39.257 33.615 1.00   16.98 ? 219  GLY A N   1 
ATOM   1513 C  CA  . GLY A 1 196 ? 50.850 39.229 33.317 1.00   16.06 ? 219  GLY A CA  1 
ATOM   1514 C  C   . GLY A 1 196 ? 51.589 39.144 34.640 1.00   15.11 ? 219  GLY A C   1 
ATOM   1515 O  O   . GLY A 1 196 ? 51.007 38.741 35.650 1.00   16.30 ? 219  GLY A O   1 
ATOM   1516 N  N   . CYS A 1 197 ? 52.864 39.516 34.636 1.00   14.05 ? 220  CYS A N   1 
ATOM   1517 C  CA  . CYS A 1 197 ? 53.676 39.511 35.846 1.00   13.46 ? 220  CYS A CA  1 
ATOM   1518 C  C   . CYS A 1 197 ? 54.634 40.686 35.817 1.00   14.65 ? 220  CYS A C   1 
ATOM   1519 O  O   . CYS A 1 197 ? 55.452 40.806 34.905 1.00   14.53 ? 220  CYS A O   1 
ATOM   1520 C  CB  . CYS A 1 197 ? 54.479 38.221 35.959 1.00   14.29 ? 220  CYS A CB  1 
ATOM   1521 S  SG  . CYS A 1 197 ? 53.472 36.730 36.193 1.00   13.73 ? 220  CYS A SG  1 
ATOM   1522 N  N   . ALA A 1 198 ? 54.528 41.548 36.822 1.00   12.01 ? 221  ALA A N   1 
ATOM   1523 C  CA  . ALA A 1 198 ? 55.383 42.719 36.934 1.00   12.79 ? 221  ALA A CA  1 
ATOM   1524 C  C   . ALA A 1 198 ? 55.181 43.711 35.785 1.00   13.89 ? 221  ALA A C   1 
ATOM   1525 O  O   . ALA A 1 198 ? 56.092 44.461 35.436 1.00   15.27 ? 221  ALA A O   1 
ATOM   1526 C  CB  . ALA A 1 198 ? 56.849 42.290 37.020 1.00   13.25 ? 221  ALA A CB  1 
ATOM   1527 N  N   . TRP A 1 199 A 53.987 43.704 35.196 1.00   13.72 ? 221  TRP A N   1 
ATOM   1528 C  CA  . TRP A 1 199 A 53.670 44.630 34.112 1.00   15.62 ? 221  TRP A CA  1 
ATOM   1529 C  C   . TRP A 1 199 A 53.233 45.956 34.731 1.00   17.17 ? 221  TRP A C   1 
ATOM   1530 O  O   . TRP A 1 199 A 52.727 45.990 35.855 1.00   18.10 ? 221  TRP A O   1 
ATOM   1531 C  CB  . TRP A 1 199 A 52.533 44.086 33.240 1.00   15.19 ? 221  TRP A CB  1 
ATOM   1532 C  CG  . TRP A 1 199 A 52.892 42.887 32.400 1.00   16.68 ? 221  TRP A CG  1 
ATOM   1533 C  CD1 . TRP A 1 199 A 54.068 42.188 32.416 1.00   15.73 ? 221  TRP A CD1 1 
ATOM   1534 C  CD2 . TRP A 1 199 A 52.048 42.228 31.446 1.00   15.98 ? 221  TRP A CD2 1 
ATOM   1535 N  NE1 . TRP A 1 199 A 54.006 41.134 31.533 1.00   15.67 ? 221  TRP A NE1 1 
ATOM   1536 C  CE2 . TRP A 1 199 A 52.778 41.136 30.925 1.00   15.80 ? 221  TRP A CE2 1 
ATOM   1537 C  CE3 . TRP A 1 199 A 50.745 42.454 30.983 1.00   17.01 ? 221  TRP A CE3 1 
ATOM   1538 C  CZ2 . TRP A 1 199 A 52.246 40.270 29.962 1.00   17.60 ? 221  TRP A CZ2 1 
ATOM   1539 C  CZ3 . TRP A 1 199 A 50.214 41.592 30.024 1.00   18.50 ? 221  TRP A CZ3 1 
ATOM   1540 C  CH2 . TRP A 1 199 A 50.967 40.513 29.526 1.00   18.52 ? 221  TRP A CH2 1 
ATOM   1541 N  N   . LYS A 1 200 ? 53.423 47.046 33.997 1.00   17.52 ? 222  LYS A N   1 
ATOM   1542 C  CA  . LYS A 1 200 ? 53.043 48.366 34.486 1.00   19.28 ? 222  LYS A CA  1 
ATOM   1543 C  C   . LYS A 1 200 ? 51.541 48.449 34.764 1.00   18.60 ? 222  LYS A C   1 
ATOM   1544 O  O   . LYS A 1 200 ? 50.727 47.942 33.992 1.00   18.89 ? 222  LYS A O   1 
ATOM   1545 C  CB  . LYS A 1 200 ? 53.443 49.434 33.459 1.00   21.42 ? 222  LYS A CB  1 
ATOM   1546 C  CG  . LYS A 1 200 ? 53.189 50.867 33.901 1.00   25.06 ? 222  LYS A CG  1 
ATOM   1547 C  CD  . LYS A 1 200 ? 53.656 51.857 32.842 1.00   26.93 ? 222  LYS A CD  1 
ATOM   1548 C  CE  . LYS A 1 200 ? 53.424 53.293 33.285 0.0000 26.36 ? 222  LYS A CE  1 
ATOM   1549 N  NZ  . LYS A 1 200 ? 53.889 54.269 32.261 0.0000 26.61 ? 222  LYS A NZ  1 
ATOM   1550 N  N   . ASN A 1 201 ? 51.189 49.087 35.877 1.00   18.20 ? 223  ASN A N   1 
ATOM   1551 C  CA  . ASN A 1 201 ? 49.797 49.275 36.281 1.00   18.86 ? 223  ASN A CA  1 
ATOM   1552 C  C   . ASN A 1 201 ? 48.982 47.996 36.476 1.00   18.68 ? 223  ASN A C   1 
ATOM   1553 O  O   . ASN A 1 201 ? 47.757 48.016 36.389 1.00   18.37 ? 223  ASN A O   1 
ATOM   1554 C  CB  . ASN A 1 201 ? 49.079 50.191 35.279 1.00   23.66 ? 223  ASN A CB  1 
ATOM   1555 C  CG  . ASN A 1 201 ? 49.670 51.589 35.239 1.00   26.15 ? 223  ASN A CG  1 
ATOM   1556 O  OD1 . ASN A 1 201 ? 49.781 52.256 36.267 1.00   31.35 ? 223  ASN A OD1 1 
ATOM   1557 N  ND2 . ASN A 1 201 ? 50.045 52.042 34.046 1.00   30.68 ? 223  ASN A ND2 1 
ATOM   1558 N  N   A ARG A 1 202 ? 49.666 46.882 36.725 0.66   17.49 ? 224  ARG A N   1 
ATOM   1559 N  N   B ARG A 1 202 ? 49.663 46.889 36.750 0.33   17.48 ? 224  ARG A N   1 
ATOM   1560 C  CA  A ARG A 1 202 ? 48.997 45.601 36.944 0.66   17.38 ? 224  ARG A CA  1 
ATOM   1561 C  CA  B ARG A 1 202 ? 48.976 45.624 36.967 0.33   16.98 ? 224  ARG A CA  1 
ATOM   1562 C  C   A ARG A 1 202 ? 49.647 44.874 38.123 0.66   17.00 ? 224  ARG A C   1 
ATOM   1563 C  C   B ARG A 1 202 ? 49.631 44.880 38.120 0.33   16.79 ? 224  ARG A C   1 
ATOM   1564 O  O   A ARG A 1 202 ? 50.377 43.897 37.946 0.66   15.87 ? 224  ARG A O   1 
ATOM   1565 O  O   B ARG A 1 202 ? 50.346 43.896 37.924 0.33   16.30 ? 224  ARG A O   1 
ATOM   1566 C  CB  A ARG A 1 202 ? 49.071 44.725 35.684 0.66   18.87 ? 224  ARG A CB  1 
ATOM   1567 C  CB  B ARG A 1 202 ? 49.007 44.781 35.693 0.33   17.19 ? 224  ARG A CB  1 
ATOM   1568 C  CG  A ARG A 1 202 ? 48.362 45.308 34.457 0.66   22.37 ? 224  ARG A CG  1 
ATOM   1569 C  CG  B ARG A 1 202 ? 48.564 45.568 34.476 0.33   18.18 ? 224  ARG A CG  1 
ATOM   1570 C  CD  A ARG A 1 202 ? 46.873 45.501 34.707 0.66   25.74 ? 224  ARG A CD  1 
ATOM   1571 C  CD  B ARG A 1 202 ? 48.249 44.690 33.289 0.33   18.82 ? 224  ARG A CD  1 
ATOM   1572 N  NE  A ARG A 1 202 ? 46.205 46.235 33.631 0.66   30.35 ? 224  ARG A NE  1 
ATOM   1573 N  NE  B ARG A 1 202 ? 47.856 45.508 32.146 0.33   19.51 ? 224  ARG A NE  1 
ATOM   1574 C  CZ  A ARG A 1 202 ? 45.641 45.677 32.563 0.66   31.77 ? 224  ARG A CZ  1 
ATOM   1575 C  CZ  B ARG A 1 202 ? 47.306 45.031 31.037 0.33   20.55 ? 224  ARG A CZ  1 
ATOM   1576 N  NH1 A ARG A 1 202 ? 45.651 44.360 32.404 0.66   32.65 ? 224  ARG A NH1 1 
ATOM   1577 N  NH1 B ARG A 1 202 ? 47.076 43.731 30.914 0.33   20.98 ? 224  ARG A NH1 1 
ATOM   1578 N  NH2 A ARG A 1 202 ? 45.062 46.443 31.646 0.66   33.71 ? 224  ARG A NH2 1 
ATOM   1579 N  NH2 B ARG A 1 202 ? 46.987 45.858 30.051 0.33   20.89 ? 224  ARG A NH2 1 
ATOM   1580 N  N   . PRO A 1 203 ? 49.388 45.352 39.351 1.00   16.41 ? 225  PRO A N   1 
ATOM   1581 C  CA  . PRO A 1 203 ? 49.953 44.741 40.555 1.00   15.69 ? 225  PRO A CA  1 
ATOM   1582 C  C   . PRO A 1 203 ? 49.339 43.376 40.836 1.00   15.27 ? 225  PRO A C   1 
ATOM   1583 O  O   . PRO A 1 203 ? 48.351 42.990 40.215 1.00   15.94 ? 225  PRO A O   1 
ATOM   1584 C  CB  . PRO A 1 203 ? 49.625 45.768 41.637 1.00   16.08 ? 225  PRO A CB  1 
ATOM   1585 C  CG  . PRO A 1 203 ? 48.288 46.275 41.192 1.00   15.84 ? 225  PRO A CG  1 
ATOM   1586 C  CD  . PRO A 1 203 ? 48.501 46.479 39.702 1.00   16.88 ? 225  PRO A CD  1 
ATOM   1587 N  N   . GLY A 1 204 ? 49.937 42.636 41.764 1.00   13.67 ? 226  GLY A N   1 
ATOM   1588 C  CA  . GLY A 1 204 ? 49.399 41.333 42.100 1.00   12.18 ? 226  GLY A CA  1 
ATOM   1589 C  C   . GLY A 1 204 ? 48.142 41.453 42.947 1.00   10.89 ? 226  GLY A C   1 
ATOM   1590 O  O   . GLY A 1 204 ? 48.006 42.386 43.733 1.00   12.63 ? 226  GLY A O   1 
ATOM   1591 N  N   . VAL A 1 205 ? 47.221 40.511 42.778 1.00   11.16 ? 227  VAL A N   1 
ATOM   1592 C  CA  . VAL A 1 205 ? 45.979 40.497 43.544 1.00   11.26 ? 227  VAL A CA  1 
ATOM   1593 C  C   . VAL A 1 205 ? 46.074 39.310 44.496 1.00   11.57 ? 227  VAL A C   1 
ATOM   1594 O  O   . VAL A 1 205 ? 46.466 38.206 44.100 1.00   11.10 ? 227  VAL A O   1 
ATOM   1595 C  CB  . VAL A 1 205 ? 44.755 40.350 42.619 1.00   12.32 ? 227  VAL A CB  1 
ATOM   1596 C  CG1 . VAL A 1 205 ? 43.470 40.404 43.442 1.00   14.32 ? 227  VAL A CG1 1 
ATOM   1597 C  CG2 . VAL A 1 205 ? 44.768 41.463 41.577 1.00   14.24 ? 227  VAL A CG2 1 
ATOM   1598 N  N   . TYR A 1 206 ? 45.725 39.551 45.752 1.00   10.50 ? 228  TYR A N   1 
ATOM   1599 C  CA  . TYR A 1 206 ? 45.824 38.537 46.792 1.00   11.56 ? 228  TYR A CA  1 
ATOM   1600 C  C   . TYR A 1 206 ? 44.533 38.338 47.573 1.00   12.16 ? 228  TYR A C   1 
ATOM   1601 O  O   . TYR A 1 206 ? 43.724 39.255 47.696 1.00   11.95 ? 228  TYR A O   1 
ATOM   1602 C  CB  . TYR A 1 206 ? 46.945 38.929 47.762 1.00   11.09 ? 228  TYR A CB  1 
ATOM   1603 C  CG  . TYR A 1 206 ? 48.286 39.106 47.079 1.00   10.00 ? 228  TYR A CG  1 
ATOM   1604 C  CD1 . TYR A 1 206 ? 48.601 40.288 46.398 1.00   9.21  ? 228  TYR A CD1 1 
ATOM   1605 C  CD2 . TYR A 1 206 ? 49.210 38.065 47.051 1.00   10.65 ? 228  TYR A CD2 1 
ATOM   1606 C  CE1 . TYR A 1 206 ? 49.810 40.420 45.703 1.00   10.79 ? 228  TYR A CE1 1 
ATOM   1607 C  CE2 . TYR A 1 206 ? 50.414 38.186 46.360 1.00   10.36 ? 228  TYR A CE2 1 
ATOM   1608 C  CZ  . TYR A 1 206 ? 50.706 39.362 45.689 1.00   11.91 ? 228  TYR A CZ  1 
ATOM   1609 O  OH  . TYR A 1 206 ? 51.888 39.467 44.992 1.00   10.95 ? 228  TYR A OH  1 
ATOM   1610 N  N   . THR A 1 207 ? 44.345 37.135 48.105 1.00   11.12 ? 229  THR A N   1 
ATOM   1611 C  CA  . THR A 1 207 ? 43.158 36.849 48.899 1.00   11.80 ? 229  THR A CA  1 
ATOM   1612 C  C   . THR A 1 207 ? 43.366 37.409 50.306 1.00   12.10 ? 229  THR A C   1 
ATOM   1613 O  O   . THR A 1 207 ? 44.403 37.181 50.927 1.00   12.82 ? 229  THR A O   1 
ATOM   1614 C  CB  . THR A 1 207 ? 42.907 35.337 48.998 1.00   13.05 ? 229  THR A CB  1 
ATOM   1615 O  OG1 . THR A 1 207 ? 42.781 34.792 47.679 1.00   14.42 ? 229  THR A OG1 1 
ATOM   1616 C  CG2 . THR A 1 207 ? 41.632 35.060 49.782 1.00   14.10 ? 229  THR A CG2 1 
ATOM   1617 N  N   . LYS A 1 208 ? 42.377 38.147 50.798 1.00   13.21 ? 230  LYS A N   1 
ATOM   1618 C  CA  . LYS A 1 208 ? 42.437 38.754 52.125 1.00   13.08 ? 230  LYS A CA  1 
ATOM   1619 C  C   . LYS A 1 208 ? 42.125 37.695 53.188 1.00   13.20 ? 230  LYS A C   1 
ATOM   1620 O  O   . LYS A 1 208 ? 40.963 37.391 53.452 1.00   13.77 ? 230  LYS A O   1 
ATOM   1621 C  CB  . LYS A 1 208 ? 41.420 39.902 52.196 1.00   15.20 ? 230  LYS A CB  1 
ATOM   1622 C  CG  . LYS A 1 208 ? 41.580 40.825 53.393 1.00   19.06 ? 230  LYS A CG  1 
ATOM   1623 C  CD  . LYS A 1 208 ? 40.534 41.939 53.374 1.00   23.64 ? 230  LYS A CD  1 
ATOM   1624 C  CE  . LYS A 1 208 ? 40.642 42.789 52.116 1.00   25.96 ? 230  LYS A CE  1 
ATOM   1625 N  NZ  . LYS A 1 208 ? 39.628 43.883 52.084 1.00   29.61 ? 230  LYS A NZ  1 
ATOM   1626 N  N   . VAL A 1 209 ? 43.167 37.140 53.801 1.00   10.70 ? 231  VAL A N   1 
ATOM   1627 C  CA  . VAL A 1 209 ? 42.994 36.097 54.810 1.00   10.68 ? 231  VAL A CA  1 
ATOM   1628 C  C   . VAL A 1 209 ? 42.115 36.506 55.995 1.00   11.87 ? 231  VAL A C   1 
ATOM   1629 O  O   . VAL A 1 209 ? 41.373 35.680 56.531 1.00   13.11 ? 231  VAL A O   1 
ATOM   1630 C  CB  . VAL A 1 209 ? 44.369 35.608 55.332 1.00   11.29 ? 231  VAL A CB  1 
ATOM   1631 C  CG1 . VAL A 1 209 ? 44.181 34.574 56.440 1.00   11.75 ? 231  VAL A CG1 1 
ATOM   1632 C  CG2 . VAL A 1 209 ? 45.165 35.001 54.186 1.00   12.89 ? 231  VAL A CG2 1 
ATOM   1633 N  N   . TYR A 1 210 ? 42.191 37.770 56.398 1.00   10.75 ? 232  TYR A N   1 
ATOM   1634 C  CA  . TYR A 1 210 ? 41.400 38.257 57.529 1.00   12.61 ? 232  TYR A CA  1 
ATOM   1635 C  C   . TYR A 1 210 ? 39.906 37.940 57.410 1.00   12.78 ? 232  TYR A C   1 
ATOM   1636 O  O   . TYR A 1 210 ? 39.243 37.658 58.408 1.00   12.90 ? 232  TYR A O   1 
ATOM   1637 C  CB  . TYR A 1 210 ? 41.582 39.772 57.682 1.00   13.45 ? 232  TYR A CB  1 
ATOM   1638 C  CG  . TYR A 1 210 ? 40.775 40.371 58.818 1.00   14.40 ? 232  TYR A CG  1 
ATOM   1639 C  CD1 . TYR A 1 210 ? 41.201 40.259 60.142 1.00   16.00 ? 232  TYR A CD1 1 
ATOM   1640 C  CD2 . TYR A 1 210 ? 39.579 41.043 58.566 1.00   16.31 ? 232  TYR A CD2 1 
ATOM   1641 C  CE1 . TYR A 1 210 ? 40.453 40.807 61.190 1.00   17.96 ? 232  TYR A CE1 1 
ATOM   1642 C  CE2 . TYR A 1 210 ? 38.828 41.590 59.601 1.00   18.24 ? 232  TYR A CE2 1 
ATOM   1643 C  CZ  . TYR A 1 210 ? 39.269 41.471 60.908 1.00   19.43 ? 232  TYR A CZ  1 
ATOM   1644 O  OH  . TYR A 1 210 ? 38.519 42.017 61.929 1.00   21.23 ? 232  TYR A OH  1 
ATOM   1645 N  N   . ASN A 1 211 ? 39.377 38.001 56.192 1.00   13.99 ? 233  ASN A N   1 
ATOM   1646 C  CA  . ASN A 1 211 ? 37.961 37.726 55.950 1.00   15.78 ? 233  ASN A CA  1 
ATOM   1647 C  C   . ASN A 1 211 ? 37.563 36.283 56.250 1.00   16.73 ? 233  ASN A C   1 
ATOM   1648 O  O   . ASN A 1 211 ? 36.376 35.981 56.408 1.00   18.66 ? 233  ASN A O   1 
ATOM   1649 C  CB  . ASN A 1 211 ? 37.617 38.016 54.486 1.00   17.94 ? 233  ASN A CB  1 
ATOM   1650 C  CG  . ASN A 1 211 ? 37.662 39.488 54.153 1.00   21.05 ? 233  ASN A CG  1 
ATOM   1651 O  OD1 . ASN A 1 211 ? 38.309 40.277 54.841 1.00   23.35 ? 233  ASN A OD1 1 
ATOM   1652 N  ND2 . ASN A 1 211 ? 36.980 39.866 53.081 1.00   23.88 ? 233  ASN A ND2 1 
ATOM   1653 N  N   . TYR A 1 212 ? 38.551 35.399 56.342 1.00   15.66 ? 234  TYR A N   1 
ATOM   1654 C  CA  . TYR A 1 212 ? 38.290 33.980 56.556 1.00   15.59 ? 234  TYR A CA  1 
ATOM   1655 C  C   . TYR A 1 212 ? 38.759 33.391 57.879 1.00   15.52 ? 234  TYR A C   1 
ATOM   1656 O  O   . TYR A 1 212 ? 38.750 32.171 58.048 1.00   17.96 ? 234  TYR A O   1 
ATOM   1657 C  CB  . TYR A 1 212 ? 38.924 33.195 55.408 1.00   16.43 ? 234  TYR A CB  1 
ATOM   1658 C  CG  . TYR A 1 212 ? 38.475 33.694 54.059 1.00   15.23 ? 234  TYR A CG  1 
ATOM   1659 C  CD1 . TYR A 1 212 ? 37.240 33.324 53.539 1.00   16.08 ? 234  TYR A CD1 1 
ATOM   1660 C  CD2 . TYR A 1 212 ? 39.255 34.593 53.333 1.00   15.28 ? 234  TYR A CD2 1 
ATOM   1661 C  CE1 . TYR A 1 212 ? 36.785 33.837 52.330 1.00   17.16 ? 234  TYR A CE1 1 
ATOM   1662 C  CE2 . TYR A 1 212 ? 38.810 35.113 52.127 1.00   16.20 ? 234  TYR A CE2 1 
ATOM   1663 C  CZ  . TYR A 1 212 ? 37.575 34.731 51.632 1.00   17.16 ? 234  TYR A CZ  1 
ATOM   1664 O  OH  . TYR A 1 212 ? 37.125 35.249 50.443 1.00   18.93 ? 234  TYR A OH  1 
ATOM   1665 N  N   . VAL A 1 213 ? 39.157 34.239 58.819 1.00   16.26 ? 235  VAL A N   1 
ATOM   1666 C  CA  . VAL A 1 213 ? 39.645 33.739 60.098 1.00   17.88 ? 235  VAL A CA  1 
ATOM   1667 C  C   . VAL A 1 213 ? 38.645 32.823 60.796 1.00   18.65 ? 235  VAL A C   1 
ATOM   1668 O  O   . VAL A 1 213 ? 39.015 31.752 61.275 1.00   18.37 ? 235  VAL A O   1 
ATOM   1669 C  CB  . VAL A 1 213 ? 40.037 34.895 61.038 1.00   18.45 ? 235  VAL A CB  1 
ATOM   1670 C  CG1 . VAL A 1 213 ? 40.411 34.351 62.408 1.00   21.11 ? 235  VAL A CG1 1 
ATOM   1671 C  CG2 . VAL A 1 213 ? 41.217 35.656 60.445 1.00   19.95 ? 235  VAL A CG2 1 
ATOM   1672 N  N   . ASP A 1 214 ? 37.383 33.232 60.848 1.00   19.28 ? 236  ASP A N   1 
ATOM   1673 C  CA  . ASP A 1 214 ? 36.369 32.409 61.495 1.00   22.07 ? 236  ASP A CA  1 
ATOM   1674 C  C   . ASP A 1 214 ? 36.147 31.103 60.742 1.00   21.11 ? 236  ASP A C   1 
ATOM   1675 O  O   . ASP A 1 214 ? 36.003 30.047 61.357 1.00   23.16 ? 236  ASP A O   1 
ATOM   1676 C  CB  . ASP A 1 214 ? 35.050 33.173 61.615 1.00   24.49 ? 236  ASP A CB  1 
ATOM   1677 C  CG  . ASP A 1 214 ? 35.160 34.379 62.527 1.00   28.91 ? 236  ASP A CG  1 
ATOM   1678 O  OD1 . ASP A 1 214 ? 35.746 34.245 63.621 1.00   30.58 ? 236  ASP A OD1 1 
ATOM   1679 O  OD2 . ASP A 1 214 ? 34.655 35.459 62.154 1.00   34.21 ? 236  ASP A OD2 1 
ATOM   1680 N  N   . TRP A 1 215 ? 36.119 31.174 59.415 1.00   20.21 ? 237  TRP A N   1 
ATOM   1681 C  CA  . TRP A 1 215 ? 35.923 29.984 58.594 1.00   20.09 ? 237  TRP A CA  1 
ATOM   1682 C  C   . TRP A 1 215 ? 37.069 29.001 58.809 1.00   20.55 ? 237  TRP A C   1 
ATOM   1683 O  O   . TRP A 1 215 ? 36.856 27.791 58.897 1.00   21.30 ? 237  TRP A O   1 
ATOM   1684 C  CB  . TRP A 1 215 ? 35.857 30.354 57.112 1.00   20.05 ? 237  TRP A CB  1 
ATOM   1685 C  CG  . TRP A 1 215 ? 35.744 29.156 56.207 1.00   22.00 ? 237  TRP A CG  1 
ATOM   1686 C  CD1 . TRP A 1 215 ? 34.653 28.350 56.046 1.00   22.28 ? 237  TRP A CD1 1 
ATOM   1687 C  CD2 . TRP A 1 215 ? 36.771 28.613 55.367 1.00   21.98 ? 237  TRP A CD2 1 
ATOM   1688 N  NE1 . TRP A 1 215 ? 34.937 27.338 55.157 1.00   22.69 ? 237  TRP A NE1 1 
ATOM   1689 C  CE2 . TRP A 1 215 ? 36.230 27.476 54.725 1.00   22.35 ? 237  TRP A CE2 1 
ATOM   1690 C  CE3 . TRP A 1 215 ? 38.097 28.977 55.093 1.00   22.46 ? 237  TRP A CE3 1 
ATOM   1691 C  CZ2 . TRP A 1 215 ? 36.969 26.699 53.827 1.00   23.31 ? 237  TRP A CZ2 1 
ATOM   1692 C  CZ3 . TRP A 1 215 ? 38.833 28.203 54.199 1.00   23.47 ? 237  TRP A CZ3 1 
ATOM   1693 C  CH2 . TRP A 1 215 ? 38.265 27.076 53.577 1.00   23.22 ? 237  TRP A CH2 1 
ATOM   1694 N  N   . ILE A 1 216 ? 38.288 29.525 58.879 1.00   18.62 ? 238  ILE A N   1 
ATOM   1695 C  CA  . ILE A 1 216 ? 39.454 28.677 59.085 1.00   19.37 ? 238  ILE A CA  1 
ATOM   1696 C  C   . ILE A 1 216 ? 39.385 27.979 60.437 1.00   19.97 ? 238  ILE A C   1 
ATOM   1697 O  O   . ILE A 1 216 ? 39.580 26.769 60.523 1.00   21.08 ? 238  ILE A O   1 
ATOM   1698 C  CB  . ILE A 1 216 ? 40.763 29.492 58.998 1.00   18.65 ? 238  ILE A CB  1 
ATOM   1699 C  CG1 . ILE A 1 216 ? 40.973 29.973 57.560 1.00   17.65 ? 238  ILE A CG1 1 
ATOM   1700 C  CG2 . ILE A 1 216 ? 41.942 28.641 59.457 1.00   18.12 ? 238  ILE A CG2 1 
ATOM   1701 C  CD1 . ILE A 1 216 ? 42.191 30.871 57.375 1.00   18.12 ? 238  ILE A CD1 1 
ATOM   1702 N  N   . LYS A 1 217 ? 39.103 28.741 61.490 1.00   20.79 ? 239  LYS A N   1 
ATOM   1703 C  CA  . LYS A 1 217 ? 39.012 28.171 62.831 1.00   23.90 ? 239  LYS A CA  1 
ATOM   1704 C  C   . LYS A 1 217 ? 37.940 27.089 62.911 1.00   24.78 ? 239  LYS A C   1 
ATOM   1705 O  O   . LYS A 1 217 ? 38.192 25.991 63.407 1.00   24.89 ? 239  LYS A O   1 
ATOM   1706 C  CB  . LYS A 1 217 ? 38.696 29.260 63.857 1.00   25.30 ? 239  LYS A CB  1 
ATOM   1707 C  CG  . LYS A 1 217 ? 39.805 30.270 64.075 1.00   26.78 ? 239  LYS A CG  1 
ATOM   1708 C  CD  . LYS A 1 217 ? 39.410 31.271 65.149 1.00   30.14 ? 239  LYS A CD  1 
ATOM   1709 C  CE  . LYS A 1 217 ? 40.538 32.245 65.444 1.00   33.47 ? 239  LYS A CE  1 
ATOM   1710 N  NZ  . LYS A 1 217 ? 40.170 33.211 66.517 1.00   34.69 ? 239  LYS A NZ  1 
ATOM   1711 N  N   . ASP A 1 218 ? 36.745 27.403 62.424 1.00   25.89 ? 240  ASP A N   1 
ATOM   1712 C  CA  . ASP A 1 218 ? 35.639 26.452 62.462 1.00   27.57 ? 240  ASP A CA  1 
ATOM   1713 C  C   . ASP A 1 218 ? 35.888 25.210 61.616 1.00   26.71 ? 240  ASP A C   1 
ATOM   1714 O  O   . ASP A 1 218 ? 35.637 24.089 62.060 1.00   27.63 ? 240  ASP A O   1 
ATOM   1715 C  CB  . ASP A 1 218 ? 34.340 27.128 62.015 1.00   30.32 ? 240  ASP A CB  1 
ATOM   1716 C  CG  . ASP A 1 218 ? 33.880 28.202 62.984 1.00   33.41 ? 240  ASP A CG  1 
ATOM   1717 O  OD1 . ASP A 1 218 ? 33.934 27.958 64.207 1.00   36.71 ? 240  ASP A OD1 1 
ATOM   1718 O  OD2 . ASP A 1 218 ? 33.456 29.285 62.528 1.00   36.80 ? 240  ASP A OD2 1 
ATOM   1719 N  N   . THR A 1 219 ? 36.382 25.407 60.400 1.00   25.57 ? 241  THR A N   1 
ATOM   1720 C  CA  . THR A 1 219 ? 36.654 24.293 59.503 1.00   23.54 ? 241  THR A CA  1 
ATOM   1721 C  C   . THR A 1 219 ? 37.706 23.351 60.081 1.00   24.00 ? 241  THR A C   1 
ATOM   1722 O  O   . THR A 1 219 ? 37.560 22.131 60.009 1.00   24.04 ? 241  THR A O   1 
ATOM   1723 C  CB  . THR A 1 219 ? 37.130 24.794 58.127 1.00   23.97 ? 241  THR A CB  1 
ATOM   1724 O  OG1 . THR A 1 219 ? 36.101 25.596 57.534 1.00   24.22 ? 241  THR A OG1 1 
ATOM   1725 C  CG2 . THR A 1 219 ? 37.445 23.622 57.209 1.00   23.53 ? 241  THR A CG2 1 
ATOM   1726 N  N   . ILE A 1 220 ? 38.766 23.912 60.652 1.00   23.14 ? 242  ILE A N   1 
ATOM   1727 C  CA  . ILE A 1 220 ? 39.820 23.087 61.230 1.00   22.78 ? 242  ILE A CA  1 
ATOM   1728 C  C   . ILE A 1 220 ? 39.308 22.311 62.442 1.00   25.37 ? 242  ILE A C   1 
ATOM   1729 O  O   . ILE A 1 220 ? 39.602 21.128 62.598 1.00   25.64 ? 242  ILE A O   1 
ATOM   1730 C  CB  . ILE A 1 220 ? 41.041 23.945 61.637 1.00   21.96 ? 242  ILE A CB  1 
ATOM   1731 C  CG1 . ILE A 1 220 ? 41.773 24.414 60.376 1.00   18.59 ? 242  ILE A CG1 1 
ATOM   1732 C  CG2 . ILE A 1 220 ? 41.976 23.150 62.539 1.00   20.86 ? 242  ILE A CG2 1 
ATOM   1733 C  CD1 . ILE A 1 220 ? 42.958 25.316 60.645 1.00   21.23 ? 242  ILE A CD1 1 
ATOM   1734 N  N   . ALA A 1 221 ? 38.535 22.980 63.290 1.00   26.10 ? 243  ALA A N   1 
ATOM   1735 C  CA  . ALA A 1 221 ? 37.989 22.345 64.484 1.00   29.04 ? 243  ALA A CA  1 
ATOM   1736 C  C   . ALA A 1 221 ? 37.063 21.188 64.128 1.00   29.96 ? 243  ALA A C   1 
ATOM   1737 O  O   . ALA A 1 221 ? 37.013 20.182 64.836 1.00   31.64 ? 243  ALA A O   1 
ATOM   1738 C  CB  . ALA A 1 221 ? 37.237 23.374 65.322 1.00   28.71 ? 243  ALA A CB  1 
ATOM   1739 N  N   . ALA A 1 222 ? 36.340 21.328 63.021 1.00   30.96 ? 244  ALA A N   1 
ATOM   1740 C  CA  . ALA A 1 222 ? 35.400 20.304 62.583 1.00   32.44 ? 244  ALA A CA  1 
ATOM   1741 C  C   . ALA A 1 222 ? 36.025 19.179 61.761 1.00   33.60 ? 244  ALA A C   1 
ATOM   1742 O  O   . ALA A 1 222 ? 35.348 18.206 61.424 1.00   34.62 ? 244  ALA A O   1 
ATOM   1743 C  CB  . ALA A 1 222 ? 34.270 20.952 61.791 1.00   32.88 ? 244  ALA A CB  1 
ATOM   1744 N  N   . ASN A 1 223 ? 37.310 19.301 61.443 1.00   33.31 ? 245  ASN A N   1 
ATOM   1745 C  CA  . ASN A 1 223 ? 37.989 18.280 60.651 1.00   33.10 ? 245  ASN A CA  1 
ATOM   1746 C  C   . ASN A 1 223 ? 39.268 17.761 61.290 1.00   33.36 ? 245  ASN A C   1 
ATOM   1747 O  O   . ASN A 1 223 ? 40.128 17.203 60.609 1.00   33.07 ? 245  ASN A O   1 
ATOM   1748 C  CB  . ASN A 1 223 ? 38.300 18.827 59.257 1.00   33.32 ? 245  ASN A CB  1 
ATOM   1749 C  CG  . ASN A 1 223 ? 37.065 18.938 58.389 1.00   34.54 ? 245  ASN A CG  1 
ATOM   1750 O  OD1 . ASN A 1 223 ? 36.522 17.933 57.934 1.00   35.76 ? 245  ASN A OD1 1 
ATOM   1751 N  ND2 . ASN A 1 223 ? 36.609 20.163 58.161 1.00   34.16 ? 245  ASN A ND2 1 
ATOM   1752 N  N   . SER A 1 224 ? 39.391 17.938 62.599 1.00   34.40 ? 246  SER A N   1 
ATOM   1753 C  CA  . SER A 1 224 ? 40.575 17.479 63.314 1.00   36.41 ? 246  SER A CA  1 
ATOM   1754 C  C   . SER A 1 224 ? 40.186 16.521 64.433 1.00   37.68 ? 246  SER A C   1 
ATOM   1755 O  O   . SER A 1 224 ? 38.970 16.307 64.624 1.00   37.87 ? 246  SER A O   1 
ATOM   1756 C  CB  . SER A 1 224 ? 41.334 18.672 63.899 1.00   36.66 ? 246  SER A CB  1 
ATOM   1757 O  OG  . SER A 1 224 ? 41.736 19.573 62.881 1.00   37.63 ? 246  SER A OG  1 
ATOM   1758 O  OXT . SER A 1 224 ? 41.099 16.000 65.109 1.00   38.04 ? 246  SER A OXT 1 
HETATM 1759 C  C1  . BEN B 2 .   ? 50.342 36.789 39.375 1.00   15.49 ? 250  BEN A C1  1 
HETATM 1760 C  C2  . BEN B 2 .   ? 50.371 35.932 40.466 1.00   15.59 ? 250  BEN A C2  1 
HETATM 1761 C  C3  . BEN B 2 .   ? 49.897 34.586 40.246 1.00   15.67 ? 250  BEN A C3  1 
HETATM 1762 C  C4  . BEN B 2 .   ? 49.398 34.060 38.996 1.00   17.20 ? 250  BEN A C4  1 
HETATM 1763 C  C5  . BEN B 2 .   ? 49.393 35.010 37.891 1.00   18.48 ? 250  BEN A C5  1 
HETATM 1764 C  C6  . BEN B 2 .   ? 49.871 36.366 38.113 1.00   17.05 ? 250  BEN A C6  1 
HETATM 1765 C  C   . BEN B 2 .   ? 50.796 38.137 39.511 1.00   14.92 ? 250  BEN A C   1 
HETATM 1766 N  N1  . BEN B 2 .   ? 50.976 38.678 40.728 1.00   14.17 ? 250  BEN A N1  1 
HETATM 1767 N  N2  . BEN B 2 .   ? 51.068 38.919 38.475 1.00   15.53 ? 250  BEN A N2  1 
HETATM 1768 CA CA  . CA  C 3 .   ? 65.303 20.355 48.733 1.00   17.31 ? 260  CA  A CA  1 
HETATM 1769 O  O   . HOH D 4 .   ? 63.125 37.130 41.526 1.00   16.98 ? 2001 HOH A O   1 
HETATM 1770 O  O   . HOH D 4 .   ? 64.530 44.293 41.544 1.00   37.52 ? 2002 HOH A O   1 
HETATM 1771 O  O   . HOH D 4 .   ? 63.960 38.222 53.549 1.00   38.33 ? 2003 HOH A O   1 
HETATM 1772 O  O   . HOH D 4 .   ? 69.638 37.356 45.461 1.00   26.27 ? 2004 HOH A O   1 
HETATM 1773 O  O   . HOH D 4 .   ? 65.410 36.775 40.107 1.00   38.68 ? 2005 HOH A O   1 
HETATM 1774 O  O   . HOH D 4 .   ? 65.945 36.045 53.395 1.00   32.22 ? 2006 HOH A O   1 
HETATM 1775 O  O   . HOH D 4 .   ? 72.480 34.503 53.268 1.00   36.94 ? 2007 HOH A O   1 
HETATM 1776 O  O   . HOH D 4 .   ? 69.403 31.670 58.633 1.00   35.64 ? 2008 HOH A O   1 
HETATM 1777 O  O   . HOH D 4 .   ? 72.562 36.888 56.608 1.00   30.64 ? 2009 HOH A O   1 
HETATM 1778 O  O   . HOH D 4 .   ? 66.162 34.509 38.966 1.00   42.54 ? 2010 HOH A O   1 
HETATM 1779 O  O   . HOH D 4 .   ? 67.867 23.172 53.988 1.00   40.99 ? 2011 HOH A O   1 
HETATM 1780 O  O   . HOH D 4 .   ? 64.268 28.159 52.173 1.00   19.04 ? 2012 HOH A O   1 
HETATM 1781 O  O   . HOH D 4 .   ? 64.734 29.254 60.349 1.00   43.61 ? 2013 HOH A O   1 
HETATM 1782 O  O   . HOH D 4 .   ? 60.539 34.153 59.121 1.00   48.70 ? 2014 HOH A O   1 
HETATM 1783 O  O   . HOH D 4 .   ? 62.494 29.182 53.894 1.00   17.85 ? 2015 HOH A O   1 
HETATM 1784 O  O   . HOH D 4 .   ? 58.503 24.733 55.520 1.00   20.65 ? 2016 HOH A O   1 
HETATM 1785 O  O   . HOH D 4 .   ? 56.450 35.183 52.982 1.00   11.65 ? 2017 HOH A O   1 
HETATM 1786 O  O   . HOH D 4 .   ? 58.529 36.193 57.442 1.00   22.30 ? 2018 HOH A O   1 
HETATM 1787 O  O   . HOH D 4 .   ? 59.076 24.072 52.035 1.00   14.68 ? 2019 HOH A O   1 
HETATM 1788 O  O   . HOH D 4 .   ? 58.354 20.557 45.001 1.00   17.62 ? 2020 HOH A O   1 
HETATM 1789 O  O   . HOH D 4 .   ? 54.199 14.253 44.633 1.00   48.94 ? 2021 HOH A O   1 
HETATM 1790 O  O   . HOH D 4 .   ? 54.182 22.376 37.690 1.00   33.28 ? 2022 HOH A O   1 
HETATM 1791 O  O   . HOH D 4 .   ? 50.113 26.627 39.090 1.00   33.53 ? 2023 HOH A O   1 
HETATM 1792 O  O   . HOH D 4 .   ? 64.152 16.780 45.841 1.00   31.24 ? 2024 HOH A O   1 
HETATM 1793 O  O   . HOH D 4 .   ? 49.494 30.867 51.834 1.00   15.39 ? 2025 HOH A O   1 
HETATM 1794 O  O   . HOH D 4 .   ? 47.198 21.063 63.530 1.00   22.26 ? 2026 HOH A O   1 
HETATM 1795 O  O   . HOH D 4 .   ? 44.852 18.791 63.557 1.00   35.01 ? 2027 HOH A O   1 
HETATM 1796 O  O   . HOH D 4 .   ? 47.136 25.783 39.822 1.00   36.29 ? 2028 HOH A O   1 
HETATM 1797 O  O   . HOH D 4 .   ? 43.403 17.134 39.901 1.00   41.94 ? 2029 HOH A O   1 
HETATM 1798 O  O   . HOH D 4 .   ? 46.942 13.898 48.461 1.00   36.77 ? 2030 HOH A O   1 
HETATM 1799 O  O   . HOH D 4 .   ? 63.533 40.948 36.633 1.00   40.60 ? 2031 HOH A O   1 
HETATM 1800 O  O   . HOH D 4 .   ? 65.932 21.131 53.264 1.00   33.11 ? 2032 HOH A O   1 
HETATM 1801 O  O   . HOH D 4 .   ? 60.677 19.633 46.038 1.00   17.76 ? 2033 HOH A O   1 
HETATM 1802 O  O   . HOH D 4 .   ? 60.825 26.734 53.323 1.00   19.27 ? 2034 HOH A O   1 
HETATM 1803 O  O   . HOH D 4 .   ? 64.024 18.670 47.703 1.00   19.73 ? 2035 HOH A O   1 
HETATM 1804 O  O   . HOH D 4 .   ? 70.731 25.660 46.363 1.00   37.54 ? 2036 HOH A O   1 
HETATM 1805 O  O   . HOH D 4 .   ? 71.326 15.365 48.010 1.00   26.33 ? 2037 HOH A O   1 
HETATM 1806 O  O   . HOH D 4 .   ? 68.884 15.195 45.648 1.00   27.21 ? 2038 HOH A O   1 
HETATM 1807 O  O   . HOH D 4 .   ? 62.671 19.098 58.982 1.00   25.57 ? 2039 HOH A O   1 
HETATM 1808 O  O   . HOH D 4 .   ? 57.436 14.677 59.144 1.00   36.01 ? 2040 HOH A O   1 
HETATM 1809 O  O   . HOH D 4 .   ? 56.586 51.867 46.358 1.00   39.30 ? 2041 HOH A O   1 
HETATM 1810 O  O   . HOH D 4 .   ? 59.582 13.022 54.272 1.00   35.24 ? 2042 HOH A O   1 
HETATM 1811 O  O   . HOH D 4 .   ? 52.521 11.254 53.847 1.00   31.16 ? 2043 HOH A O   1 
HETATM 1812 O  O   . HOH D 4 .   ? 39.631 16.272 49.851 1.00   40.36 ? 2044 HOH A O   1 
HETATM 1813 O  O   . HOH D 4 .   ? 36.913 21.205 48.416 1.00   37.16 ? 2045 HOH A O   1 
HETATM 1814 O  O   . HOH D 4 .   ? 34.000 25.328 46.539 1.00   44.44 ? 2046 HOH A O   1 
HETATM 1815 O  O   . HOH D 4 .   ? 34.004 32.472 55.224 1.00   38.63 ? 2047 HOH A O   1 
HETATM 1816 O  O   . HOH D 4 .   ? 41.093 36.226 44.144 1.00   21.80 ? 2048 HOH A O   1 
HETATM 1817 O  O   . HOH D 4 .   ? 43.288 15.416 63.249 1.00   41.81 ? 2049 HOH A O   1 
HETATM 1818 O  O   . HOH D 4 .   ? 55.033 13.701 60.032 1.00   38.11 ? 2050 HOH A O   1 
HETATM 1819 O  O   . HOH D 4 .   ? 54.325 17.828 65.384 1.00   45.77 ? 2051 HOH A O   1 
HETATM 1820 O  O   . HOH D 4 .   ? 61.863 19.155 66.724 1.00   39.64 ? 2052 HOH A O   1 
HETATM 1821 O  O   . HOH D 4 .   ? 56.429 18.993 66.630 1.00   34.63 ? 2053 HOH A O   1 
HETATM 1822 O  O   . HOH D 4 .   ? 60.234 26.485 65.787 1.00   42.93 ? 2054 HOH A O   1 
HETATM 1823 O  O   . HOH D 4 .   ? 65.605 22.370 64.731 1.00   50.33 ? 2055 HOH A O   1 
HETATM 1824 O  O   . HOH D 4 .   ? 62.420 26.013 55.698 1.00   20.91 ? 2056 HOH A O   1 
HETATM 1825 O  O   . HOH D 4 .   ? 61.350 28.295 63.293 1.00   42.70 ? 2057 HOH A O   1 
HETATM 1826 O  O   . HOH D 4 .   ? 57.403 30.450 61.179 1.00   35.05 ? 2058 HOH A O   1 
HETATM 1827 O  O   . HOH D 4 .   ? 55.351 26.636 65.092 1.00   36.68 ? 2059 HOH A O   1 
HETATM 1828 O  O   . HOH D 4 .   ? 53.904 32.692 63.904 1.00   26.65 ? 2060 HOH A O   1 
HETATM 1829 O  O   . HOH D 4 .   ? 47.323 36.002 65.515 1.00   23.09 ? 2061 HOH A O   1 
HETATM 1830 O  O   . HOH D 4 .   ? 40.325 44.515 63.481 1.00   37.93 ? 2062 HOH A O   1 
HETATM 1831 O  O   . HOH D 4 .   ? 46.910 44.985 59.687 1.00   34.81 ? 2063 HOH A O   1 
HETATM 1832 O  O   . HOH D 4 .   ? 43.631 47.575 58.984 1.00   41.60 ? 2064 HOH A O   1 
HETATM 1833 O  O   . HOH D 4 .   ? 47.088 52.896 55.874 1.00   43.70 ? 2065 HOH A O   1 
HETATM 1834 O  O   . HOH D 4 .   ? 56.135 43.371 57.503 1.00   33.69 ? 2066 HOH A O   1 
HETATM 1835 O  O   . HOH D 4 .   ? 54.513 30.728 46.954 1.00   11.43 ? 2067 HOH A O   1 
HETATM 1836 O  O   . HOH D 4 .   ? 60.310 32.684 42.311 1.00   10.10 ? 2068 HOH A O   1 
HETATM 1837 O  O   . HOH D 4 .   ? 63.385 38.486 38.199 1.00   20.60 ? 2069 HOH A O   1 
HETATM 1838 O  O   . HOH D 4 .   ? 55.460 35.738 32.883 1.00   29.22 ? 2070 HOH A O   1 
HETATM 1839 O  O   . HOH D 4 .   ? 53.717 36.730 30.402 1.00   36.49 ? 2071 HOH A O   1 
HETATM 1840 O  O   . HOH D 4 .   ? 61.430 39.983 33.381 1.00   29.09 ? 2072 HOH A O   1 
HETATM 1841 O  O   . HOH D 4 .   ? 60.351 42.633 34.314 1.00   35.89 ? 2073 HOH A O   1 
HETATM 1842 O  O   . HOH D 4 .   ? 61.664 37.993 29.254 1.00   15.90 ? 2074 HOH A O   1 
HETATM 1843 O  O   . HOH D 4 .   ? 55.029 34.227 29.951 1.00   34.07 ? 2075 HOH A O   1 
HETATM 1844 O  O   . HOH D 4 .   ? 62.594 27.058 33.903 1.00   34.54 ? 2076 HOH A O   1 
HETATM 1845 O  O   . HOH D 4 .   ? 54.632 28.822 32.549 1.00   34.99 ? 2077 HOH A O   1 
HETATM 1846 O  O   . HOH D 4 .   ? 60.478 26.530 40.454 1.00   20.69 ? 2078 HOH A O   1 
HETATM 1847 O  O   . HOH D 4 .   ? 67.622 28.274 39.683 1.00   38.42 ? 2079 HOH A O   1 
HETATM 1848 O  O   . HOH D 4 .   ? 69.905 23.133 41.640 1.00   37.24 ? 2080 HOH A O   1 
HETATM 1849 O  O   . HOH D 4 .   ? 67.468 29.587 41.887 1.00   33.16 ? 2081 HOH A O   1 
HETATM 1850 O  O   . HOH D 4 .   ? 61.315 45.779 47.094 1.00   25.00 ? 2082 HOH A O   1 
HETATM 1851 O  O   . HOH D 4 .   ? 64.111 44.153 49.776 1.00   28.86 ? 2083 HOH A O   1 
HETATM 1852 O  O   . HOH D 4 .   ? 62.506 43.179 47.499 1.00   16.65 ? 2084 HOH A O   1 
HETATM 1853 O  O   . HOH D 4 .   ? 58.991 43.193 53.956 1.00   36.86 ? 2085 HOH A O   1 
HETATM 1854 O  O   . HOH D 4 .   ? 51.231 51.791 49.277 1.00   37.55 ? 2086 HOH A O   1 
HETATM 1855 O  O   . HOH D 4 .   ? 44.399 46.797 47.801 1.00   17.07 ? 2087 HOH A O   1 
HETATM 1856 O  O   . HOH D 4 .   ? 38.370 52.483 47.667 1.00   40.45 ? 2088 HOH A O   1 
HETATM 1857 O  O   . HOH D 4 .   ? 39.454 53.257 42.047 1.00   31.55 ? 2089 HOH A O   1 
HETATM 1858 O  O   . HOH D 4 .   ? 40.746 52.505 35.767 1.00   42.11 ? 2090 HOH A O   1 
HETATM 1859 O  O   . HOH D 4 .   ? 42.589 50.321 34.240 1.00   39.92 ? 2091 HOH A O   1 
HETATM 1860 O  O   . HOH D 4 .   ? 37.489 38.930 39.333 1.00   37.19 ? 2092 HOH A O   1 
HETATM 1861 O  O   . HOH D 4 .   ? 40.020 35.891 46.614 1.00   20.23 ? 2093 HOH A O   1 
HETATM 1862 O  O   . HOH D 4 .   ? 54.218 50.588 45.482 1.00   25.59 ? 2094 HOH A O   1 
HETATM 1863 O  O   . HOH D 4 .   ? 52.267 46.771 38.483 1.00   34.19 ? 2095 HOH A O   1 
HETATM 1864 O  O   . HOH D 4 .   ? 53.275 51.861 43.195 1.00   34.66 ? 2096 HOH A O   1 
HETATM 1865 O  O   . HOH D 4 .   ? 62.296 43.163 36.988 1.00   35.80 ? 2097 HOH A O   1 
HETATM 1866 O  O   . HOH D 4 .   ? 53.599 44.551 41.508 1.00   17.12 ? 2098 HOH A O   1 
HETATM 1867 O  O   . HOH D 4 .   ? 54.138 33.177 33.788 1.00   27.88 ? 2099 HOH A O   1 
HETATM 1868 O  O   . HOH D 4 .   ? 57.552 24.517 38.780 1.00   34.30 ? 2100 HOH A O   1 
HETATM 1869 O  O   . HOH D 4 .   ? 55.688 28.774 45.250 1.00   11.74 ? 2101 HOH A O   1 
HETATM 1870 O  O   . HOH D 4 .   ? 57.375 24.381 33.096 1.00   43.56 ? 2102 HOH A O   1 
HETATM 1871 O  O   . HOH D 4 .   ? 50.109 29.547 39.145 1.00   29.74 ? 2103 HOH A O   1 
HETATM 1872 O  O   . HOH D 4 .   ? 49.784 42.067 59.871 1.00   29.99 ? 2104 HOH A O   1 
HETATM 1873 O  O   . HOH D 4 .   ? 56.984 40.052 59.236 1.00   31.51 ? 2105 HOH A O   1 
HETATM 1874 O  O   . HOH D 4 .   ? 49.673 37.558 65.905 1.00   30.97 ? 2106 HOH A O   1 
HETATM 1875 O  O   . HOH D 4 .   ? 47.119 42.947 61.926 1.00   34.13 ? 2107 HOH A O   1 
HETATM 1876 O  O   . HOH D 4 .   ? 44.101 39.779 55.458 1.00   14.14 ? 2108 HOH A O   1 
HETATM 1877 O  O   . HOH D 4 .   ? 45.753 32.790 39.056 1.00   28.93 ? 2109 HOH A O   1 
HETATM 1878 O  O   . HOH D 4 .   ? 57.026 45.430 33.184 1.00   39.60 ? 2110 HOH A O   1 
HETATM 1879 O  O   . HOH D 4 .   ? 55.037 46.629 31.584 1.00   24.57 ? 2111 HOH A O   1 
HETATM 1880 O  O   . HOH D 4 .   ? 51.606 42.189 36.107 1.00   15.65 ? 2112 HOH A O   1 
HETATM 1881 O  O   . HOH D 4 .   ? 53.170 44.371 38.640 1.00   26.65 ? 2113 HOH A O   1 
HETATM 1882 O  O   . HOH D 4 .   ? 45.826 48.387 34.486 1.00   39.37 ? 2114 HOH A O   1 
HETATM 1883 O  O   . HOH D 4 .   ? 49.214 37.798 43.168 1.00   14.00 ? 2115 HOH A O   1 
HETATM 1884 O  O   . HOH D 4 .   ? 52.661 41.660 43.835 1.00   13.12 ? 2116 HOH A O   1 
HETATM 1885 O  O   . HOH D 4 .   ? 39.088 45.048 54.491 1.00   36.40 ? 2117 HOH A O   1 
HETATM 1886 O  O   . HOH D 4 .   ? 35.814 42.119 62.235 1.00   23.25 ? 2118 HOH A O   1 
HETATM 1887 O  O   . HOH D 4 .   ? 36.775 38.308 59.564 1.00   35.44 ? 2119 HOH A O   1 
HETATM 1888 O  O   . HOH D 4 .   ? 34.313 37.806 56.824 1.00   43.96 ? 2120 HOH A O   1 
HETATM 1889 O  O   . HOH D 4 .   ? 38.123 42.992 55.830 1.00   37.06 ? 2121 HOH A O   1 
HETATM 1890 O  O   . HOH D 4 .   ? 36.096 35.896 59.871 1.00   30.66 ? 2122 HOH A O   1 
HETATM 1891 O  O   . HOH D 4 .   ? 35.286 33.662 58.192 1.00   29.08 ? 2123 HOH A O   1 
HETATM 1892 O  O   . HOH D 4 .   ? 40.142 25.740 65.418 1.00   31.36 ? 2124 HOH A O   1 
HETATM 1893 O  O   . HOH D 4 .   ? 36.012 27.120 65.828 1.00   42.97 ? 2125 HOH A O   1 
# 
