data_6YH9
# 
_entry.id   6YH9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   6YH9         pdb_00006yh9 10.2210/pdb6yh9/pdb 
WWPDB D_1292106470 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2021-04-07 
2 'Structure model' 1 1 2021-06-02 
3 'Structure model' 1 2 2024-01-24 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation                      
2 2 'Structure model' citation_author               
3 3 'Structure model' chem_comp_atom                
4 3 'Structure model' chem_comp_bond                
5 3 'Structure model' database_2                    
6 3 'Structure model' pdbx_initial_refinement_model 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                   
2  2 'Structure model' '_citation.journal_abbrev'            
3  2 'Structure model' '_citation.journal_id_CSD'            
4  2 'Structure model' '_citation.journal_id_ISSN'           
5  2 'Structure model' '_citation.journal_volume'            
6  2 'Structure model' '_citation.page_first'                
7  2 'Structure model' '_citation.page_last'                 
8  2 'Structure model' '_citation.pdbx_database_id_DOI'      
9  2 'Structure model' '_citation.pdbx_database_id_PubMed'   
10 2 'Structure model' '_citation.title'                     
11 2 'Structure model' '_citation.year'                      
12 3 'Structure model' '_database_2.pdbx_DOI'                
13 3 'Structure model' '_database_2.pdbx_database_accession' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6YH9 
_pdbx_database_status.recvd_initial_deposition_date   2020-03-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 0000-0001-5080-9367 
'Manakova, E.' 2 0000-0002-6027-2265 
'Grazulis, S.' 3 0000-0002-7928-5218 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemistryopen 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2191-1363 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                567 
_citation.page_last                 580 
_citation.title                     'Switching the Inhibitor-Enzyme Recognition Profile via Chimeric Carbonic Anhydrase XII.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/open.202100042 
_citation.pdbx_database_id_PubMed   33945229 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnoviene, J.'   1  0000-0001-5503-4775 
primary 'Smirnov, A.'       2  ?                   
primary 'Zaksauskas, A.'    3  ?                   
primary 'Zubriene, A.'      4  0000-0001-5996-1883 
primary 'Petrauskas, V.'    5  0000-0001-7983-4128 
primary 'Mickeviciute, A.'  6  ?                   
primary 'Michailoviene, V.' 7  ?                   
primary 'Capkauskaite, E.'  8  ?                   
primary 'Manakova, E.'      9  0000-0002-6027-2265 
primary 'Grazulis, S.'      10 0000-0002-7928-5218 
primary 'Baranauskiene, L.' 11 0000-0002-9924-9177 
primary 'Chen, W.Y.'        12 ?                   
primary 'Ladbury, J.E.'     13 0000-0002-6328-7200 
primary 'Matulis, D.'       14 0000-0002-6178-6276 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                                                          
29220.879 1   4.2.1.1 'A65S, N67K, I91T, F130A, V134S, L203N' ? ? 
2 non-polymer syn 'ZINC ION'                                                                                                      
65.409    1   ?       ?                                       ? ? 
3 non-polymer syn '2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 
530.537   1   ?       ?                                       ? ? 
4 water       nat water                                                                                                           
18.015    202 ?       ?                                       ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                                      ZN  
3 '2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' WWX 
4 water                                                                                                           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  SER n 
1 66  PHE n 
1 67  LYS n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  THR n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 ALA n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 SER n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 ASN n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'          133.103 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'        121.158 
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'         117.146 
WWX non-polymer         . 
'2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 
'C22 H21 F3 N2 O6 S2' 530.537 
ZN  non-polymer         . 'ZINC ION' ? 'Zn 2'                65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 ALA 130 131 131 ALA ALA A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 SER 134 135 135 SER SER A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 ASN 203 204 204 ASN ASN A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 WWX 1   302 1   WWX WWX A . 
D 4 HOH 1   401 98  HOH HOH A . 
D 4 HOH 2   402 179 HOH HOH A . 
D 4 HOH 3   403 195 HOH HOH A . 
D 4 HOH 4   404 22  HOH HOH A . 
D 4 HOH 5   405 155 HOH HOH A . 
D 4 HOH 6   406 132 HOH HOH A . 
D 4 HOH 7   407 174 HOH HOH A . 
D 4 HOH 8   408 156 HOH HOH A . 
D 4 HOH 9   409 202 HOH HOH A . 
D 4 HOH 10  410 110 HOH HOH A . 
D 4 HOH 11  411 83  HOH HOH A . 
D 4 HOH 12  412 56  HOH HOH A . 
D 4 HOH 13  413 166 HOH HOH A . 
D 4 HOH 14  414 66  HOH HOH A . 
D 4 HOH 15  415 99  HOH HOH A . 
D 4 HOH 16  416 35  HOH HOH A . 
D 4 HOH 17  417 74  HOH HOH A . 
D 4 HOH 18  418 121 HOH HOH A . 
D 4 HOH 19  419 18  HOH HOH A . 
D 4 HOH 20  420 194 HOH HOH A . 
D 4 HOH 21  421 101 HOH HOH A . 
D 4 HOH 22  422 170 HOH HOH A . 
D 4 HOH 23  423 159 HOH HOH A . 
D 4 HOH 24  424 175 HOH HOH A . 
D 4 HOH 25  425 157 HOH HOH A . 
D 4 HOH 26  426 78  HOH HOH A . 
D 4 HOH 27  427 13  HOH HOH A . 
D 4 HOH 28  428 87  HOH HOH A . 
D 4 HOH 29  429 180 HOH HOH A . 
D 4 HOH 30  430 14  HOH HOH A . 
D 4 HOH 31  431 76  HOH HOH A . 
D 4 HOH 32  432 59  HOH HOH A . 
D 4 HOH 33  433 143 HOH HOH A . 
D 4 HOH 34  434 92  HOH HOH A . 
D 4 HOH 35  435 90  HOH HOH A . 
D 4 HOH 36  436 69  HOH HOH A . 
D 4 HOH 37  437 120 HOH HOH A . 
D 4 HOH 38  438 34  HOH HOH A . 
D 4 HOH 39  439 149 HOH HOH A . 
D 4 HOH 40  440 36  HOH HOH A . 
D 4 HOH 41  441 201 HOH HOH A . 
D 4 HOH 42  442 43  HOH HOH A . 
D 4 HOH 43  443 191 HOH HOH A . 
D 4 HOH 44  444 145 HOH HOH A . 
D 4 HOH 45  445 173 HOH HOH A . 
D 4 HOH 46  446 81  HOH HOH A . 
D 4 HOH 47  447 62  HOH HOH A . 
D 4 HOH 48  448 71  HOH HOH A . 
D 4 HOH 49  449 111 HOH HOH A . 
D 4 HOH 50  450 39  HOH HOH A . 
D 4 HOH 51  451 150 HOH HOH A . 
D 4 HOH 52  452 5   HOH HOH A . 
D 4 HOH 53  453 25  HOH HOH A . 
D 4 HOH 54  454 165 HOH HOH A . 
D 4 HOH 55  455 130 HOH HOH A . 
D 4 HOH 56  456 79  HOH HOH A . 
D 4 HOH 57  457 72  HOH HOH A . 
D 4 HOH 58  458 29  HOH HOH A . 
D 4 HOH 59  459 126 HOH HOH A . 
D 4 HOH 60  460 26  HOH HOH A . 
D 4 HOH 61  461 53  HOH HOH A . 
D 4 HOH 62  462 64  HOH HOH A . 
D 4 HOH 63  463 51  HOH HOH A . 
D 4 HOH 64  464 96  HOH HOH A . 
D 4 HOH 65  465 52  HOH HOH A . 
D 4 HOH 66  466 40  HOH HOH A . 
D 4 HOH 67  467 163 HOH HOH A . 
D 4 HOH 68  468 6   HOH HOH A . 
D 4 HOH 69  469 46  HOH HOH A . 
D 4 HOH 70  470 73  HOH HOH A . 
D 4 HOH 71  471 109 HOH HOH A . 
D 4 HOH 72  472 17  HOH HOH A . 
D 4 HOH 73  473 154 HOH HOH A . 
D 4 HOH 74  474 10  HOH HOH A . 
D 4 HOH 75  475 7   HOH HOH A . 
D 4 HOH 76  476 148 HOH HOH A . 
D 4 HOH 77  477 128 HOH HOH A . 
D 4 HOH 78  478 89  HOH HOH A . 
D 4 HOH 79  479 30  HOH HOH A . 
D 4 HOH 80  480 186 HOH HOH A . 
D 4 HOH 81  481 8   HOH HOH A . 
D 4 HOH 82  482 181 HOH HOH A . 
D 4 HOH 83  483 3   HOH HOH A . 
D 4 HOH 84  484 147 HOH HOH A . 
D 4 HOH 85  485 94  HOH HOH A . 
D 4 HOH 86  486 27  HOH HOH A . 
D 4 HOH 87  487 9   HOH HOH A . 
D 4 HOH 88  488 61  HOH HOH A . 
D 4 HOH 89  489 84  HOH HOH A . 
D 4 HOH 90  490 47  HOH HOH A . 
D 4 HOH 91  491 192 HOH HOH A . 
D 4 HOH 92  492 188 HOH HOH A . 
D 4 HOH 93  493 168 HOH HOH A . 
D 4 HOH 94  494 119 HOH HOH A . 
D 4 HOH 95  495 21  HOH HOH A . 
D 4 HOH 96  496 38  HOH HOH A . 
D 4 HOH 97  497 197 HOH HOH A . 
D 4 HOH 98  498 42  HOH HOH A . 
D 4 HOH 99  499 32  HOH HOH A . 
D 4 HOH 100 500 125 HOH HOH A . 
D 4 HOH 101 501 33  HOH HOH A . 
D 4 HOH 102 502 146 HOH HOH A . 
D 4 HOH 103 503 1   HOH HOH A . 
D 4 HOH 104 504 93  HOH HOH A . 
D 4 HOH 105 505 24  HOH HOH A . 
D 4 HOH 106 506 187 HOH HOH A . 
D 4 HOH 107 507 97  HOH HOH A . 
D 4 HOH 108 508 45  HOH HOH A . 
D 4 HOH 109 509 77  HOH HOH A . 
D 4 HOH 110 510 141 HOH HOH A . 
D 4 HOH 111 511 57  HOH HOH A . 
D 4 HOH 112 512 169 HOH HOH A . 
D 4 HOH 113 513 4   HOH HOH A . 
D 4 HOH 114 514 19  HOH HOH A . 
D 4 HOH 115 515 67  HOH HOH A . 
D 4 HOH 116 516 16  HOH HOH A . 
D 4 HOH 117 517 193 HOH HOH A . 
D 4 HOH 118 518 185 HOH HOH A . 
D 4 HOH 119 519 28  HOH HOH A . 
D 4 HOH 120 520 11  HOH HOH A . 
D 4 HOH 121 521 104 HOH HOH A . 
D 4 HOH 122 522 158 HOH HOH A . 
D 4 HOH 123 523 133 HOH HOH A . 
D 4 HOH 124 524 189 HOH HOH A . 
D 4 HOH 125 525 171 HOH HOH A . 
D 4 HOH 126 526 48  HOH HOH A . 
D 4 HOH 127 527 123 HOH HOH A . 
D 4 HOH 128 528 65  HOH HOH A . 
D 4 HOH 129 529 151 HOH HOH A . 
D 4 HOH 130 530 196 HOH HOH A . 
D 4 HOH 131 531 136 HOH HOH A . 
D 4 HOH 132 532 124 HOH HOH A . 
D 4 HOH 133 533 54  HOH HOH A . 
D 4 HOH 134 534 2   HOH HOH A . 
D 4 HOH 135 535 100 HOH HOH A . 
D 4 HOH 136 536 70  HOH HOH A . 
D 4 HOH 137 537 91  HOH HOH A . 
D 4 HOH 138 538 108 HOH HOH A . 
D 4 HOH 139 539 102 HOH HOH A . 
D 4 HOH 140 540 58  HOH HOH A . 
D 4 HOH 141 541 95  HOH HOH A . 
D 4 HOH 142 542 161 HOH HOH A . 
D 4 HOH 143 543 63  HOH HOH A . 
D 4 HOH 144 544 152 HOH HOH A . 
D 4 HOH 145 545 50  HOH HOH A . 
D 4 HOH 146 546 68  HOH HOH A . 
D 4 HOH 147 547 31  HOH HOH A . 
D 4 HOH 148 548 15  HOH HOH A . 
D 4 HOH 149 549 118 HOH HOH A . 
D 4 HOH 150 550 75  HOH HOH A . 
D 4 HOH 151 551 20  HOH HOH A . 
D 4 HOH 152 552 107 HOH HOH A . 
D 4 HOH 153 553 55  HOH HOH A . 
D 4 HOH 154 554 86  HOH HOH A . 
D 4 HOH 155 555 82  HOH HOH A . 
D 4 HOH 156 556 134 HOH HOH A . 
D 4 HOH 157 557 85  HOH HOH A . 
D 4 HOH 158 558 41  HOH HOH A . 
D 4 HOH 159 559 106 HOH HOH A . 
D 4 HOH 160 560 162 HOH HOH A . 
D 4 HOH 161 561 137 HOH HOH A . 
D 4 HOH 162 562 112 HOH HOH A . 
D 4 HOH 163 563 113 HOH HOH A . 
D 4 HOH 164 564 177 HOH HOH A . 
D 4 HOH 165 565 23  HOH HOH A . 
D 4 HOH 166 566 60  HOH HOH A . 
D 4 HOH 167 567 44  HOH HOH A . 
D 4 HOH 168 568 199 HOH HOH A . 
D 4 HOH 169 569 37  HOH HOH A . 
D 4 HOH 170 570 103 HOH HOH A . 
D 4 HOH 171 571 49  HOH HOH A . 
D 4 HOH 172 572 164 HOH HOH A . 
D 4 HOH 173 573 142 HOH HOH A . 
D 4 HOH 174 574 183 HOH HOH A . 
D 4 HOH 175 575 12  HOH HOH A . 
D 4 HOH 176 576 88  HOH HOH A . 
D 4 HOH 177 577 80  HOH HOH A . 
D 4 HOH 178 578 140 HOH HOH A . 
D 4 HOH 179 579 127 HOH HOH A . 
D 4 HOH 180 580 176 HOH HOH A . 
D 4 HOH 181 581 131 HOH HOH A . 
D 4 HOH 182 582 135 HOH HOH A . 
D 4 HOH 183 583 200 HOH HOH A . 
D 4 HOH 184 584 122 HOH HOH A . 
D 4 HOH 185 585 105 HOH HOH A . 
D 4 HOH 186 586 160 HOH HOH A . 
D 4 HOH 187 587 190 HOH HOH A . 
D 4 HOH 188 588 114 HOH HOH A . 
D 4 HOH 189 589 184 HOH HOH A . 
D 4 HOH 190 590 178 HOH HOH A . 
D 4 HOH 191 591 144 HOH HOH A . 
D 4 HOH 192 592 138 HOH HOH A . 
D 4 HOH 193 593 139 HOH HOH A . 
D 4 HOH 194 594 182 HOH HOH A . 
D 4 HOH 195 595 172 HOH HOH A . 
D 4 HOH 196 596 117 HOH HOH A . 
D 4 HOH 197 597 116 HOH HOH A . 
D 4 HOH 198 598 115 HOH HOH A . 
D 4 HOH 199 599 167 HOH HOH A . 
D 4 HOH 200 600 129 HOH HOH A . 
D 4 HOH 201 601 153 HOH HOH A . 
D 4 HOH 202 602 198 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
3  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
4  1 Y 1 A LYS 45  ? CE  ? A LYS 45  CE  
5  1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
6  1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
7  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
8  1 Y 1 A LYS 127 ? NZ  ? A LYS 126 NZ  
9  1 Y 1 A LYS 228 ? CE  ? A LYS 227 CE  
10 1 Y 1 A LYS 228 ? NZ  ? A LYS 227 NZ  
11 1 Y 1 A GLN 255 ? CD  ? A GLN 254 CD  
12 1 Y 1 A GLN 255 ? OE1 ? A GLN 254 OE1 
13 1 Y 1 A GLN 255 ? NE2 ? A GLN 254 NE2 
14 1 Y 1 A LYS 257 ? CD  ? A LYS 256 CD  
15 1 Y 1 A LYS 257 ? CE  ? A LYS 256 CE  
16 1 Y 1 A LYS 257 ? NZ  ? A LYS 256 NZ  
17 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
18 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.2.19   2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   103.340 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6YH9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.734 
_cell.length_a_esd                 ? 
_cell.length_b                     40.869 
_cell.length_b_esd                 ? 
_cell.length_c                     70.920 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         6YH9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   6YH9 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.01 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         38.93 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-11-30 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826607 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826607 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6YH9 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.55 
_reflns.d_resolution_low                 69.01 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       33601 
_reflns.number_obs                       33601 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             98.800 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.700 
_reflns.pdbx_Rmerge_I_obs                0.060 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.060 
_reflns.pdbx_netI_over_av_sigmaI         8.300 
_reflns.pdbx_netI_over_sigmaI            18.300 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.068 
_reflns.pdbx_Rpim_I_all                  0.026 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         226751 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
1.550 1.630  ? 2.100  33143 ? ? ? 4869 98.800 ? ? ? ? 0.376 ? ? ? ? ? ? ? ? 6.800 0.376 ? ? 4.500  0.441 0.167 ? 1  1 ? ? ? 
1.630 1.730  ? 2.900  29547 ? ? ? 4587 98.500 ? ? ? ? 0.265 ? ? ? ? ? ? ? ? 6.400 0.265 ? ? 6.100  0.313 0.121 ? 2  1 ? ? ? 
1.730 1.850  ? 4.200  30415 ? ? ? 4353 99.000 ? ? ? ? 0.180 ? ? ? ? ? ? ? ? 7.000 0.180 ? ? 9.300  0.209 0.078 ? 3  1 ? ? ? 
1.850 2.000  ? 6.300  27483 ? ? ? 4043 98.600 ? ? ? ? 0.118 ? ? ? ? ? ? ? ? 6.800 0.118 ? ? 13.800 0.138 0.052 ? 4  1 ? ? ? 
2.000 2.190  ? 8.600  24448 ? ? ? 3708 98.800 ? ? ? ? 0.083 ? ? ? ? ? ? ? ? 6.600 0.083 ? ? 19.500 0.096 0.037 ? 5  1 ? ? ? 
2.190 2.450  ? 10.100 23711 ? ? ? 3407 99.200 ? ? ? ? 0.069 ? ? ? ? ? ? ? ? 7.000 0.069 ? ? 24.300 0.079 0.030 ? 6  1 ? ? ? 
2.450 2.830  ? 11.500 19748 ? ? ? 2977 98.400 ? ? ? ? 0.058 ? ? ? ? ? ? ? ? 6.600 0.058 ? ? 28.700 0.066 0.025 ? 7  1 ? ? ? 
2.830 3.470  ? 13.300 17834 ? ? ? 2546 99.500 ? ? ? ? 0.048 ? ? ? ? ? ? ? ? 7.000 0.048 ? ? 37.700 0.054 0.020 ? 8  1 ? ? ? 
3.470 4.900  ? 17.000 13127 ? ? ? 1987 99.000 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 6.600 0.038 ? ? 42.700 0.042 0.016 ? 9  1 ? ? ? 
4.900 69.007 ? 16.700 7295  ? ? ? 1124 98.800 ? ? ? ? 0.035 ? ? ? ? ? ? ? ? 6.500 0.035 ? ? 43.400 0.040 0.016 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -1.2900 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.4200 
_refine.aniso_B[2][2]                            -1.2900 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            2.1400 
_refine.B_iso_max                                73.290 
_refine.B_iso_mean                               21.0230 
_refine.B_iso_min                                10.760 
_refine.correlation_coeff_Fo_to_Fc               0.9690 
_refine.correlation_coeff_Fo_to_Fc_free          0.9540 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 6YH9 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.5500 
_refine.ls_d_res_low                             40.6200 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     30202 
_refine.ls_number_reflns_R_free                  3386 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.6600 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1698 
_refine.ls_R_factor_R_free                       0.2041 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1660 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      0.2076 
_refine.ls_wR_factor_R_work                      0.1677 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4Q09 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0880 
_refine.pdbx_overall_ESU_R_Free                  0.0900 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.0878 
_refine.overall_SU_R_free                        0.0902 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   0.8683 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.5500 
_refine_hist.d_res_low                        40.6200 
_refine_hist.number_atoms_solvent             202 
_refine_hist.number_atoms_total               2263 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       257 
_refine_hist.pdbx_B_iso_mean_ligand           27.57 
_refine_hist.pdbx_B_iso_mean_solvent          30.89 
_refine_hist.pdbx_number_atoms_protein        2025 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.012  2128 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.817  1.660  2897 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.916  5.000  257  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 35.735 23.689 103  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.726 15.000 338  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 19.210 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.128  0.200  261  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  1657 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.5500 
_refine_ls_shell.d_res_low                        1.5900 
_refine_ls_shell.number_reflns_all                2457 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             245 
_refine_ls_shell.number_reflns_R_work             2212 
_refine_ls_shell.percent_reflns_obs               98.8700 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.2490 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.2330 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     6YH9 
_struct.title                        
;Crystal structure of chimeric carbonic anhydrase XII with 2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6YH9 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              6YH9 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 6YH9 SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6YH9 LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6YH9 THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 6YH9 ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 4 
1 6YH9 SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 5 
1 6YH9 ASN A 203 ? UNP P00918 LEU 203 'engineered mutation' 204 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  11220 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? SER A 134 ? ASP A 130 SER A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? ASP A 161 ? LEU A 157 ASP A 162 1 ? 6 
HELX_P HELX_P7 AA7 VAL A 162 ? LYS A 167 ? VAL A 163 LYS A 168 5 ? 6 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.011 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C WWX . N4 ? ? A ZN  301 A WWX 302 1_555 ? ? ? ? ? ? ? 1.911 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 99.0  ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 112.1 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.3  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? C WWX .   ? A WWX 302 ? 1_555 129.0 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? C WWX .   ? A WWX 302 ? 1_555 105.0 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? C WWX .   ? A WWX 302 ? 1_555 107.5 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 0.91  
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 10.73 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
AA2 7 8  O THR A 91  ? O THR A 91  N PHE A 70  ? N PHE A 70  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A WWX 302 ? 16 'binding site for residue WWX A 302' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  WWX C .   ? WWX A 302 . ? 1_555 ? 
5  AC2 16 ASN A 62  ? ASN A 62  . ? 1_555 ? 
6  AC2 16 THR A 91  ? THR A 91  . ? 1_555 ? 
7  AC2 16 GLN A 92  ? GLN A 92  . ? 1_555 ? 
8  AC2 16 HIS A 94  ? HIS A 94  . ? 1_555 ? 
9  AC2 16 HIS A 96  ? HIS A 96  . ? 1_555 ? 
10 AC2 16 GLU A 106 ? GLU A 106 . ? 1_555 ? 
11 AC2 16 HIS A 119 ? HIS A 119 . ? 1_555 ? 
12 AC2 16 ALA A 130 ? ALA A 131 . ? 1_555 ? 
13 AC2 16 SER A 134 ? SER A 135 . ? 1_555 ? 
14 AC2 16 LEU A 140 ? LEU A 141 . ? 1_555 ? 
15 AC2 16 LEU A 197 ? LEU A 198 . ? 1_555 ? 
16 AC2 16 THR A 198 ? THR A 199 . ? 1_555 ? 
17 AC2 16 THR A 199 ? THR A 200 . ? 1_555 ? 
18 AC2 16 PRO A 201 ? PRO A 202 . ? 1_555 ? 
19 AC2 16 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
20 AC2 16 HOH D .   ? HOH A 429 . ? 1_555 ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    110 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.12 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -144.88 54.66   
2 1 LYS A 111 ? ? 73.89   -2.85   
3 1 PHE A 176 ? ? -151.55 79.37   
4 1 ASN A 244 ? ? -96.02  53.13   
5 1 LYS A 252 ? ? 58.67   -135.92 
6 1 ASN A 253 ? ? -92.79  59.72   
# 
_pdbx_entry_details.entry_id                 6YH9 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
PHE N    N  N N 250 
PHE CA   C  N S 251 
PHE C    C  N N 252 
PHE O    O  N N 253 
PHE CB   C  N N 254 
PHE CG   C  Y N 255 
PHE CD1  C  Y N 256 
PHE CD2  C  Y N 257 
PHE CE1  C  Y N 258 
PHE CE2  C  Y N 259 
PHE CZ   C  Y N 260 
PHE OXT  O  N N 261 
PHE H    H  N N 262 
PHE H2   H  N N 263 
PHE HA   H  N N 264 
PHE HB2  H  N N 265 
PHE HB3  H  N N 266 
PHE HD1  H  N N 267 
PHE HD2  H  N N 268 
PHE HE1  H  N N 269 
PHE HE2  H  N N 270 
PHE HZ   H  N N 271 
PHE HXT  H  N N 272 
PRO N    N  N N 273 
PRO CA   C  N S 274 
PRO C    C  N N 275 
PRO O    O  N N 276 
PRO CB   C  N N 277 
PRO CG   C  N N 278 
PRO CD   C  N N 279 
PRO OXT  O  N N 280 
PRO H    H  N N 281 
PRO HA   H  N N 282 
PRO HB2  H  N N 283 
PRO HB3  H  N N 284 
PRO HG2  H  N N 285 
PRO HG3  H  N N 286 
PRO HD2  H  N N 287 
PRO HD3  H  N N 288 
PRO HXT  H  N N 289 
SER N    N  N N 290 
SER CA   C  N S 291 
SER C    C  N N 292 
SER O    O  N N 293 
SER CB   C  N N 294 
SER OG   O  N N 295 
SER OXT  O  N N 296 
SER H    H  N N 297 
SER H2   H  N N 298 
SER HA   H  N N 299 
SER HB2  H  N N 300 
SER HB3  H  N N 301 
SER HG   H  N N 302 
SER HXT  H  N N 303 
THR N    N  N N 304 
THR CA   C  N S 305 
THR C    C  N N 306 
THR O    O  N N 307 
THR CB   C  N R 308 
THR OG1  O  N N 309 
THR CG2  C  N N 310 
THR OXT  O  N N 311 
THR H    H  N N 312 
THR H2   H  N N 313 
THR HA   H  N N 314 
THR HB   H  N N 315 
THR HG1  H  N N 316 
THR HG21 H  N N 317 
THR HG22 H  N N 318 
THR HG23 H  N N 319 
THR HXT  H  N N 320 
TRP N    N  N N 321 
TRP CA   C  N S 322 
TRP C    C  N N 323 
TRP O    O  N N 324 
TRP CB   C  N N 325 
TRP CG   C  Y N 326 
TRP CD1  C  Y N 327 
TRP CD2  C  Y N 328 
TRP NE1  N  Y N 329 
TRP CE2  C  Y N 330 
TRP CE3  C  Y N 331 
TRP CZ2  C  Y N 332 
TRP CZ3  C  Y N 333 
TRP CH2  C  Y N 334 
TRP OXT  O  N N 335 
TRP H    H  N N 336 
TRP H2   H  N N 337 
TRP HA   H  N N 338 
TRP HB2  H  N N 339 
TRP HB3  H  N N 340 
TRP HD1  H  N N 341 
TRP HE1  H  N N 342 
TRP HE3  H  N N 343 
TRP HZ2  H  N N 344 
TRP HZ3  H  N N 345 
TRP HH2  H  N N 346 
TRP HXT  H  N N 347 
TYR N    N  N N 348 
TYR CA   C  N S 349 
TYR C    C  N N 350 
TYR O    O  N N 351 
TYR CB   C  N N 352 
TYR CG   C  Y N 353 
TYR CD1  C  Y N 354 
TYR CD2  C  Y N 355 
TYR CE1  C  Y N 356 
TYR CE2  C  Y N 357 
TYR CZ   C  Y N 358 
TYR OH   O  N N 359 
TYR OXT  O  N N 360 
TYR H    H  N N 361 
TYR H2   H  N N 362 
TYR HA   H  N N 363 
TYR HB2  H  N N 364 
TYR HB3  H  N N 365 
TYR HD1  H  N N 366 
TYR HD2  H  N N 367 
TYR HE1  H  N N 368 
TYR HE2  H  N N 369 
TYR HH   H  N N 370 
TYR HXT  H  N N 371 
VAL N    N  N N 372 
VAL CA   C  N S 373 
VAL C    C  N N 374 
VAL O    O  N N 375 
VAL CB   C  N N 376 
VAL CG1  C  N N 377 
VAL CG2  C  N N 378 
VAL OXT  O  N N 379 
VAL H    H  N N 380 
VAL H2   H  N N 381 
VAL HA   H  N N 382 
VAL HB   H  N N 383 
VAL HG11 H  N N 384 
VAL HG12 H  N N 385 
VAL HG13 H  N N 386 
VAL HG21 H  N N 387 
VAL HG22 H  N N 388 
VAL HG23 H  N N 389 
VAL HXT  H  N N 390 
WWX O16  O  N N 391 
WWX S14  S  N N 392 
WWX O15  O  N N 393 
WWX C18  C  N N 394 
WWX O20  O  N N 395 
WWX C17  C  N N 396 
WWX C8   C  Y N 397 
WWX C7   C  Y N 398 
WWX F12  F  N N 399 
WWX C6   C  Y N 400 
WWX F11  F  N N 401 
WWX C9   C  Y N 402 
WWX C10  C  Y N 403 
WWX F13  F  N N 404 
WWX C5   C  Y N 405 
WWX S1   S  N N 406 
WWX O3   O  N N 407 
WWX N4   N  N N 408 
WWX O2   O  N N 409 
WWX N19  N  N N 410 
WWX C21  C  N R 411 
WWX C30  C  Y N 412 
WWX C35  C  Y N 413 
WWX C34  C  Y N 414 
WWX C33  C  Y N 415 
WWX C32  C  Y N 416 
WWX C31  C  Y N 417 
WWX C22  C  N S 418 
WWX O29  O  N N 419 
WWX C23  C  Y N 420 
WWX C28  C  Y N 421 
WWX C27  C  Y N 422 
WWX C26  C  Y N 423 
WWX C25  C  Y N 424 
WWX C24  C  Y N 425 
WWX H1   H  N N 426 
WWX H2   H  N N 427 
WWX H3   H  N N 428 
WWX H4   H  N N 429 
WWX H5   H  N N 430 
WWX H6   H  N N 431 
WWX H7   H  N N 432 
WWX H8   H  N N 433 
WWX H9   H  N N 434 
WWX H10  H  N N 435 
WWX H11  H  N N 436 
WWX H12  H  N N 437 
WWX H13  H  N N 438 
WWX H14  H  N N 439 
WWX H15  H  N N 440 
WWX H16  H  N N 441 
WWX H17  H  N N 442 
WWX H18  H  N N 443 
WWX H19  H  N N 444 
WWX H20  H  N N 445 
WWX H21  H  N N 446 
ZN  ZN   ZN N N 447 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
WWX O20 C18  sing N N 376 
WWX C18 C17  sing N N 377 
WWX C17 S14  sing N N 378 
WWX C25 C26  doub Y N 379 
WWX C25 C24  sing Y N 380 
WWX C26 C27  sing Y N 381 
WWX C24 C23  doub Y N 382 
WWX C27 C28  doub Y N 383 
WWX C23 C28  sing Y N 384 
WWX C23 C22  sing N N 385 
WWX O29 C22  sing N N 386 
WWX C22 C21  sing N N 387 
WWX O15 S14  doub N N 388 
WWX S14 O16  doub N N 389 
WWX S14 C8   sing N N 390 
WWX F12 C7   sing N N 391 
WWX C8  C7   doub Y N 392 
WWX C8  C9   sing Y N 393 
WWX C7  C6   sing Y N 394 
WWX C21 N19  sing N N 395 
WWX C21 C30  sing N N 396 
WWX N19 C9   sing N N 397 
WWX F11 C6   sing N N 398 
WWX C9  C10  doub Y N 399 
WWX C6  C5   doub Y N 400 
WWX C10 C5   sing Y N 401 
WWX C10 F13  sing N N 402 
WWX C5  S1   sing N N 403 
WWX C30 C31  doub Y N 404 
WWX C30 C35  sing Y N 405 
WWX C31 C32  sing Y N 406 
WWX C35 C34  doub Y N 407 
WWX O3  S1   doub N N 408 
WWX N4  S1   sing N N 409 
WWX S1  O2   doub N N 410 
WWX C32 C33  doub Y N 411 
WWX C34 C33  sing Y N 412 
WWX C18 H1   sing N N 413 
WWX C18 H2   sing N N 414 
WWX O20 H3   sing N N 415 
WWX C17 H4   sing N N 416 
WWX C17 H5   sing N N 417 
WWX N4  H6   sing N N 418 
WWX N4  H7   sing N N 419 
WWX N19 H8   sing N N 420 
WWX C21 H9   sing N N 421 
WWX C35 H10  sing N N 422 
WWX C34 H11  sing N N 423 
WWX C33 H12  sing N N 424 
WWX C32 H13  sing N N 425 
WWX C31 H14  sing N N 426 
WWX C22 H15  sing N N 427 
WWX O29 H16  sing N N 428 
WWX C28 H17  sing N N 429 
WWX C27 H18  sing N N 430 
WWX C26 H19  sing N N 431 
WWX C25 H20  sing N N 432 
WWX C24 H21  sing N N 433 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WWX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WWX 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4Q09 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6YH9 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.023961 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005681 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024468 
_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]   0.014491 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 11.671  -0.557  7.189   1.00 37.48 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.711  0.061   8.130   1.00 30.12 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 10.021  -1.022  8.956   1.00 30.60 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 10.316  -2.211  8.796   1.00 27.69 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 9.629   0.830   7.372   1.00 26.76 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 9.332   2.108   8.053   1.00 18.37 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 10.106  2.570   9.051   1.00 30.69 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 8.368   3.025   7.819   1.00 36.02 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 9.646   3.746   9.457   1.00 35.22 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 8.567   4.049   8.709   1.00 35.49 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 9.077   -0.579  9.794   1.00 29.34 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 8.418   -1.500  10.703  1.00 23.21 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 7.403   -2.369  9.979   1.00 22.12 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.866   -2.002  8.934   1.00 25.12 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.785   -0.780  11.889  1.00 22.87 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 6.580   0.039   11.543  1.00 20.87 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 6.554   1.353   11.181  1.00 21.94 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 5.207   -0.408  11.567  1.00 18.56 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 5.259   1.768   10.968  1.00 20.82 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 4.411   0.718   11.241  1.00 19.58 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 4.588   -1.621  11.928  1.00 18.18 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 3.011   0.653   11.184  1.00 20.16 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 3.207   -1.684  11.818  1.00 18.93 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 2.435   -0.555  11.486  1.00 17.89 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 7.159   -3.534  10.561  1.00 20.62 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 6.115   -4.408  10.040  1.00 19.58 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.730   -5.465  11.054  1.00 19.80 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.778   -5.221  12.272  1.00 18.49 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 5.463   -6.671  10.547  1.00 17.34 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 5.036   -7.790  11.371  1.00 19.59 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.920   -9.017  11.187  1.00 20.94 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.602   -10.076 11.718  1.00 26.92 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.579   -8.126  11.042  1.00 18.21 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.651   -7.046  11.531  1.00 16.42 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 2.251   -7.006  12.869  1.00 16.89 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 2.207   -6.038  10.681  1.00 17.86 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 1.390   -5.989  13.297  1.00 16.31 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 1.343   -5.036  11.092  1.00 16.10 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.953   -5.001  12.428  1.00 17.12 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 0.120   -3.986  12.859  1.00 17.59 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 7.044   -8.869  10.467  1.00 22.69 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.907   -10.028 10.258  1.00 25.87 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.956   -10.219 11.357  1.00 24.03 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 9.001   -9.474  12.332  1.00 23.80 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.815   -11.240 11.177  1.00 24.88 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.768  -11.660 12.193  1.00 23.73 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.752  -10.535 12.488  1.00 21.16 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 12.218  -10.402 13.607  1.00 22.81 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.551  -12.882 11.680  1.00 26.56 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.677  -13.342 12.593  1.00 29.78 ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? 12.099  -9.755  11.465  1.00 21.71 ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? 13.166  -8.798  11.668  1.00 21.47 ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? 12.651  -7.385  11.914  1.00 21.53 ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? 13.445  -6.506  12.268  1.00 19.69 ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? 14.161  -8.839  10.499  1.00 21.27 ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? 14.808  -10.180 10.381  1.00 22.85 ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? 15.798  -10.593 11.260  1.00 25.19 ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? 14.564  -11.203 9.545   1.00 23.58 ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? 16.161  -11.822 10.935  1.00 24.48 ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? 15.419  -12.218 9.877   1.00 22.00 ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? 11.340  -7.139  11.735  1.00 20.14 ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? 10.874  -5.758  11.880  1.00 18.77 ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? 9.523   -5.701  12.613  1.00 17.40 ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? 8.861   -4.653  12.633  1.00 18.38 ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? 10.730  -5.080  10.522  1.00 19.05 ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? 9.633   -5.715  9.691   1.00 22.35 ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? 9.086   -6.759  10.055  1.00 23.50 ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? 9.304   -5.106  8.559   1.00 25.95 ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? 9.171   -6.832  13.228  1.00 17.57 ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? 7.863   -7.051  13.857  1.00 16.29 ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? 7.810   -6.488  15.268  1.00 16.61 ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? 8.731   -5.790  15.694  1.00 15.30 ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? 6.703   -6.751  16.006  1.00 16.26 ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? 6.479   -6.177  17.325  1.00 16.05 ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? 7.612   -6.223  18.345  1.00 15.34 ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? 7.740   -5.269  19.095  1.00 17.23 ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? 5.300   -7.012  17.820  1.00 17.25 ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? 4.454   -7.232  16.568  1.00 16.37 ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? 5.500   -7.437  15.501  1.00 16.29 ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? 8.427   -7.290  18.319  1.00 17.27 ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? 9.505   -7.333  19.303  1.00 17.50 ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? 10.599  -6.316  19.003  1.00 17.82 ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? 11.485  -6.146  19.853  1.00 17.52 ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? 10.133  -8.729  19.367  1.00 22.39 ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? 9.115   -9.783  19.794  1.00 29.25 ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? 8.344   -9.478  21.069  1.00 37.40 ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? 8.998   -9.146  22.079  1.00 41.44 ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? 7.076   -9.573  21.049  1.00 44.09 ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? 10.592  -5.722  17.805  1.00 17.22 ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? 11.604  -4.779  17.341  1.00 15.80 ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? 11.157  -3.336  17.473  1.00 16.95 ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? 11.980  -2.429  17.406  1.00 16.29 ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? 11.900  -4.995  15.834  1.00 15.41 ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? 12.638  -6.260  15.577  1.00 17.29 ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? 14.034  -6.306  15.580  1.00 17.93 ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? 12.197  -7.513  15.296  1.00 18.12 ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? 14.423  -7.552  15.324  1.00 20.15 ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? 13.324  -8.322  15.134  1.00 18.82 ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? 9.847   -3.119  17.647  1.00 17.38 ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? 9.313   -1.772  17.591  1.00 14.93 ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? 9.874   -0.805  18.635  1.00 14.78 ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? 9.914   0.410   18.393  1.00 15.11 ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? 7.799   -1.825  17.681  1.00 15.51 ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? 7.159   -2.511  16.521  1.00 15.37 ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? 7.698   -2.871  15.319  1.00 15.41 ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? 5.752   -2.788  16.430  1.00 14.91 ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? 6.740   -3.464  14.533  1.00 14.94 ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? 5.536   -3.396  15.176  1.00 15.46 ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? 4.686   -2.664  17.332  1.00 14.77 ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? 4.270   -3.830  14.768  1.00 16.26 ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? 3.437   -3.115  16.957  1.00 16.05 ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? 3.242   -3.648  15.669  1.00 15.41 ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? 10.278  -1.309  19.788  1.00 14.58 ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? 10.737  -0.434  20.840  1.00 15.97 ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? 11.973  0.360   20.421  1.00 15.16 ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? 12.253  1.396   21.007  1.00 16.00 ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? 10.986  -1.169  22.155  1.00 15.57 ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? 12.191  -2.039  22.066  1.00 17.13 ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? 13.400  -1.685  22.673  1.00 17.13 ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? 12.400  -3.208  21.435  1.00 17.36 ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? 14.280  -2.618  22.413  1.00 16.86 ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? 13.719  -3.556  21.682  1.00 17.95 ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? 12.711  -0.131  19.422  1.00 16.49 ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? 13.938  0.596   19.080  1.00 16.80 ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? 13.580  1.935   18.449  1.00 19.43 ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? 14.195  2.959   18.759  1.00 24.19 ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? 14.873  -0.263  18.213  1.00 17.82 ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? 15.315  -1.568  18.883  1.00 15.95 ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? 16.077  -2.482  17.950  1.00 16.92 ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? 15.162  -3.472  17.248  1.00 17.43 ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? 15.882  -4.250  16.210  1.00 16.27 ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 19  ? 12.588  1.950   17.543  1.00 18.11 ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 19  ? 12.215  3.245   17.015  1.00 18.60 ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 19  ? 11.181  3.968   17.859  1.00 18.29 ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 19  ? 11.158  5.185   17.801  1.00 19.89 ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 19  ? 11.615  3.152   15.616  1.00 22.25 ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 19  ? 12.672  2.844   14.584  1.00 28.96 ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 19  ? 13.561  3.714   14.377  1.00 30.11 ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 19  ? 12.639  1.691   14.073  1.00 37.40 ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 20  ? 10.397  3.239   18.688  1.00 17.46 ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 20  ? 9.328   3.835   19.483  1.00 17.07 ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 20  ? 9.413   3.280   20.897  1.00 17.01 ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 20  ? 8.782   2.275   21.245  1.00 17.21 ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 20  ? 7.970   3.525   18.845  1.00 17.48 ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 20  ? 7.928   3.887   17.374  1.00 19.61 ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 20  ? 7.624   5.192   17.000  1.00 20.56 ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 20  ? 8.264   2.968   16.403  1.00 21.81 ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 20  ? 7.584   5.522   15.645  1.00 22.15 ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 20  ? 8.244   3.310   15.054  1.00 23.59 ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 20  ? 7.916   4.602   14.694  1.00 20.97 ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 21  ? 10.312  3.856   21.711  1.00 16.73 ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 21  ? 10.561  3.381   23.069  1.00 18.63 ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 21  ? 9.362   3.280   24.026  1.00 18.65 ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 21  ? 9.431   2.509   24.994  1.00 17.43 ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 21  ? 11.565  4.366   23.661  1.00 21.34 ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 21  ? 12.131  5.083   22.478  1.00 19.65 ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 21  ? 11.184  4.956   21.303  1.00 17.91 ? 21  PRO A CD  1 
ATOM   158  N  N   . ILE A 1 22  ? 8.267   3.994   23.691  1.00 16.93 ? 22  ILE A N   1 
ATOM   159  C  CA  . ILE A 1 22  ? 7.027   3.897   24.432  1.00 17.38 ? 22  ILE A CA  1 
ATOM   160  C  C   . ILE A 1 22  ? 6.458   2.484   24.300  1.00 18.25 ? 22  ILE A C   1 
ATOM   161  O  O   . ILE A 1 22  ? 5.547   2.142   25.054  1.00 18.36 ? 22  ILE A O   1 
ATOM   162  C  CB  . ILE A 1 22  ? 6.016   4.959   23.976  1.00 17.83 ? 22  ILE A CB  1 
ATOM   163  C  CG1 . ILE A 1 22  ? 4.947   5.200   25.036  1.00 16.87 ? 22  ILE A CG1 1 
ATOM   164  C  CG2 . ILE A 1 22  ? 5.343   4.561   22.654  1.00 17.50 ? 22  ILE A CG2 1 
ATOM   165  C  CD1 . ILE A 1 22  ? 3.927   6.229   24.623  1.00 19.90 ? 22  ILE A CD1 1 
ATOM   166  N  N   . ALA A 1 23  ? 6.993   1.670   23.372  1.00 15.31 ? 23  ALA A N   1 
ATOM   167  C  CA  . ALA A 1 23  ? 6.526   0.290   23.235  1.00 17.02 ? 23  ALA A CA  1 
ATOM   168  C  C   . ALA A 1 23  ? 6.619   -0.471  24.543  1.00 18.00 ? 23  ALA A C   1 
ATOM   169  O  O   . ALA A 1 23  ? 5.942   -1.484  24.673  1.00 19.01 ? 23  ALA A O   1 
ATOM   170  C  CB  . ALA A 1 23  ? 7.304   -0.491  22.182  1.00 17.80 ? 23  ALA A CB  1 
ATOM   171  N  N   . LYS A 1 24  ? 7.535   -0.052  25.430  1.00 19.00 ? 24  LYS A N   1 
ATOM   172  C  CA  . LYS A 1 24  ? 7.692   -0.714  26.711  1.00 20.52 ? 24  LYS A CA  1 
ATOM   173  C  C   . LYS A 1 24  ? 7.133   0.175   27.817  1.00 20.53 ? 24  LYS A C   1 
ATOM   174  O  O   . LYS A 1 24  ? 7.577   0.115   28.973  1.00 19.91 ? 24  LYS A O   1 
ATOM   175  C  CB  . LYS A 1 24  ? 9.176   -0.986  26.982  1.00 22.41 ? 24  LYS A CB  1 
ATOM   176  C  CG  . LYS A 1 24  ? 9.800   -1.961  26.002  1.00 23.57 ? 24  LYS A CG  1 
ATOM   177  C  CD  . LYS A 1 24  ? 11.296  -2.032  26.237  1.00 29.27 ? 24  LYS A CD  1 
ATOM   178  C  CE  . LYS A 1 24  ? 11.929  -3.220  25.547  1.00 29.14 ? 24  LYS A CE  1 
ATOM   179  N  NZ  . LYS A 1 24  ? 11.621  -4.502  26.238  1.00 30.12 ? 24  LYS A NZ  1 
ATOM   180  N  N   . GLY A 1 25  ? 6.133   1.004   27.468  1.00 19.17 ? 25  GLY A N   1 
ATOM   181  C  CA  . GLY A 1 25  ? 5.577   1.947   28.431  1.00 20.69 ? 25  GLY A CA  1 
ATOM   182  C  C   . GLY A 1 25  ? 4.575   1.339   29.418  1.00 17.36 ? 25  GLY A C   1 
ATOM   183  O  O   . GLY A 1 25  ? 4.382   0.127   29.469  1.00 19.17 ? 25  GLY A O   1 
ATOM   184  N  N   . GLU A 1 26  ? 3.906   2.241   30.156  1.00 19.39 ? 26  GLU A N   1 
ATOM   185  C  CA  . GLU A 1 26  ? 3.071   1.819   31.263  1.00 20.40 ? 26  GLU A CA  1 
ATOM   186  C  C   . GLU A 1 26  ? 1.629   1.548   30.837  1.00 18.57 ? 26  GLU A C   1 
ATOM   187  O  O   . GLU A 1 26  ? 0.856   0.996   31.632  1.00 20.03 ? 26  GLU A O   1 
ATOM   188  C  CB  . GLU A 1 26  ? 3.143   2.824   32.420  1.00 26.52 ? 26  GLU A CB  1 
ATOM   189  C  CG  . GLU A 1 26  ? 4.539   2.948   33.033  1.00 31.61 ? 26  GLU A CG  1 
ATOM   190  C  CD  . GLU A 1 26  ? 5.125   1.680   33.645  1.00 36.04 ? 26  GLU A CD  1 
ATOM   191  O  OE1 . GLU A 1 26  ? 4.459   1.086   34.517  1.00 44.65 ? 26  GLU A OE1 1 
ATOM   192  O  OE2 . GLU A 1 26  ? 6.263   1.289   33.268  1.00 42.11 ? 26  GLU A OE2 1 
ATOM   193  N  N   . ARG A 1 27  ? 1.274   1.857   29.576  1.00 15.82 ? 27  ARG A N   1 
ATOM   194  C  CA  . ARG A 1 27  ? -0.133  1.703   29.178  1.00 16.72 ? 27  ARG A CA  1 
ATOM   195  C  C   . ARG A 1 27  ? -0.227  1.243   27.714  1.00 14.97 ? 27  ARG A C   1 
ATOM   196  O  O   . ARG A 1 27  ? -0.966  1.823   26.886  1.00 16.71 ? 27  ARG A O   1 
ATOM   197  C  CB  . ARG A 1 27  ? -1.032  2.908   29.554  1.00 18.18 ? 27  ARG A CB  1 
ATOM   198  C  CG  . ARG A 1 27  ? -0.751  4.232   28.843  1.00 21.76 ? 27  ARG A CG  1 
ATOM   199  C  CD  . ARG A 1 27  ? -1.697  5.421   29.093  1.00 24.11 ? 27  ARG A CD  1 
ATOM   200  N  NE  . ARG A 1 27  ? -2.882  5.361   28.228  1.00 25.01 ? 27  ARG A NE  1 
ATOM   201  C  CZ  . ARG A 1 27  ? -3.799  6.300   28.032  1.00 23.12 ? 27  ARG A CZ  1 
ATOM   202  N  NH1 . ARG A 1 27  ? -3.714  7.516   28.586  1.00 21.12 ? 27  ARG A NH1 1 
ATOM   203  N  NH2 . ARG A 1 27  ? -4.777  6.032   27.199  1.00 23.02 ? 27  ARG A NH2 1 
ATOM   204  N  N   . GLN A 1 28  ? 0.454   0.131   27.412  1.00 14.60 ? 28  GLN A N   1 
ATOM   205  C  CA  . GLN A 1 28  ? 0.541   -0.352  26.024  1.00 14.11 ? 28  GLN A CA  1 
ATOM   206  C  C   . GLN A 1 28  ? -0.606  -1.331  25.749  1.00 14.23 ? 28  GLN A C   1 
ATOM   207  O  O   . GLN A 1 28  ? -1.148  -1.915  26.663  1.00 16.18 ? 28  GLN A O   1 
ATOM   208  C  CB  . GLN A 1 28  ? 1.903   -1.007  25.806  1.00 16.54 ? 28  GLN A CB  1 
ATOM   209  C  CG  . GLN A 1 28  ? 2.996   0.047   25.668  1.00 15.16 ? 28  GLN A CG  1 
ATOM   210  C  CD  . GLN A 1 28  ? 2.842   0.827   24.384  1.00 14.52 ? 28  GLN A CD  1 
ATOM   211  O  OE1 . GLN A 1 28  ? 3.073   0.302   23.292  1.00 14.59 ? 28  GLN A OE1 1 
ATOM   212  N  NE2 . GLN A 1 28  ? 2.481   2.107   24.499  1.00 13.90 ? 28  GLN A NE2 1 
ATOM   213  N  N   . SER A 1 29  ? -1.026  -1.395  24.473  1.00 12.83 ? 29  SER A N   1 
ATOM   214  C  CA  . SER A 1 29  ? -2.106  -2.245  24.026  1.00 13.89 ? 29  SER A CA  1 
ATOM   215  C  C   . SER A 1 29  ? -1.603  -3.139  22.904  1.00 14.32 ? 29  SER A C   1 
ATOM   216  O  O   . SER A 1 29  ? -0.636  -2.803  22.228  1.00 13.46 ? 29  SER A O   1 
ATOM   217  C  CB  . SER A 1 29  ? -3.213  -1.371  23.458  1.00 12.83 ? 29  SER A CB  1 
ATOM   218  O  OG  . SER A 1 29  ? -3.838  -0.740  24.568  1.00 14.00 ? 29  SER A OG  1 
ATOM   219  N  N   . PRO A 1 30  ? -2.207  -4.309  22.623  1.00 13.61 ? 30  PRO A N   1 
ATOM   220  C  CA  . PRO A 1 30  ? -3.394  -4.846  23.320  1.00 14.57 ? 30  PRO A CA  1 
ATOM   221  C  C   . PRO A 1 30  ? -2.989  -5.539  24.619  1.00 15.33 ? 30  PRO A C   1 
ATOM   222  O  O   . PRO A 1 30  ? -1.807  -5.513  24.991  1.00 13.33 ? 30  PRO A O   1 
ATOM   223  C  CB  . PRO A 1 30  ? -3.892  -5.897  22.308  1.00 14.74 ? 30  PRO A CB  1 
ATOM   224  C  CG  . PRO A 1 30  ? -2.567  -6.430  21.707  1.00 13.57 ? 30  PRO A CG  1 
ATOM   225  C  CD  . PRO A 1 30  ? -1.720  -5.190  21.544  1.00 13.69 ? 30  PRO A CD  1 
ATOM   226  N  N   . VAL A 1 31  ? -3.989  -6.113  25.326  1.00 14.69 ? 31  VAL A N   1 
ATOM   227  C  CA  . VAL A 1 31  ? -3.754  -6.797  26.586  1.00 15.32 ? 31  VAL A CA  1 
ATOM   228  C  C   . VAL A 1 31  ? -4.635  -8.040  26.561  1.00 14.75 ? 31  VAL A C   1 
ATOM   229  O  O   . VAL A 1 31  ? -5.622  -8.122  25.796  1.00 14.43 ? 31  VAL A O   1 
ATOM   230  C  CB  . VAL A 1 31  ? -4.074  -5.962  27.848  1.00 15.64 ? 31  VAL A CB  1 
ATOM   231  C  CG1 . VAL A 1 31  ? -3.148  -4.757  28.036  1.00 14.09 ? 31  VAL A CG1 1 
ATOM   232  C  CG2 . VAL A 1 31  ? -5.558  -5.560  27.897  1.00 17.24 ? 31  VAL A CG2 1 
ATOM   233  N  N   . ASP A 1 32  ? -4.271  -8.997  27.404  1.00 14.93 ? 32  ASP A N   1 
ATOM   234  C  CA  . ASP A 1 32  ? -5.188  -10.100 27.680  1.00 16.11 ? 32  ASP A CA  1 
ATOM   235  C  C   . ASP A 1 32  ? -6.292  -9.623  28.634  1.00 16.53 ? 32  ASP A C   1 
ATOM   236  O  O   . ASP A 1 32  ? -6.014  -9.029  29.671  1.00 16.84 ? 32  ASP A O   1 
ATOM   237  C  CB  . ASP A 1 32  ? -4.443  -11.272 28.317  1.00 16.91 ? 32  ASP A CB  1 
ATOM   238  C  CG  . ASP A 1 32  ? -5.391  -12.459 28.585  1.00 19.34 ? 32  ASP A CG  1 
ATOM   239  O  OD1 . ASP A 1 32  ? -6.108  -12.884 27.654  1.00 18.73 ? 32  ASP A OD1 1 
ATOM   240  O  OD2 . ASP A 1 32  ? -5.450  -12.910 29.744  1.00 21.79 ? 32  ASP A OD2 1 
ATOM   241  N  N   . ILE A 1 33  ? -7.554  -9.866  28.270  1.00 16.28 ? 33  ILE A N   1 
ATOM   242  C  CA  . ILE A 1 33  ? -8.672  -9.503  29.118  1.00 15.45 ? 33  ILE A CA  1 
ATOM   243  C  C   . ILE A 1 33  ? -8.987  -10.728 29.957  1.00 18.83 ? 33  ILE A C   1 
ATOM   244  O  O   . ILE A 1 33  ? -9.501  -11.704 29.431  1.00 18.91 ? 33  ILE A O   1 
ATOM   245  C  CB  . ILE A 1 33  ? -9.878  -9.033  28.275  1.00 16.07 ? 33  ILE A CB  1 
ATOM   246  C  CG1 . ILE A 1 33  ? -9.495  -7.819  27.444  1.00 14.22 ? 33  ILE A CG1 1 
ATOM   247  C  CG2 . ILE A 1 33  ? -11.067 -8.740  29.193  1.00 17.81 ? 33  ILE A CG2 1 
ATOM   248  C  CD1 . ILE A 1 33  ? -10.476 -7.584  26.280  1.00 15.24 ? 33  ILE A CD1 1 
ATOM   249  N  N   . ASP A 1 34  ? -8.678  -10.626 31.268  1.00 18.27 ? 34  ASP A N   1 
ATOM   250  C  CA  . ASP A 1 34  ? -8.996  -11.678 32.234  1.00 21.46 ? 34  ASP A CA  1 
ATOM   251  C  C   . ASP A 1 34  ? -10.405 -11.399 32.748  1.00 19.53 ? 34  ASP A C   1 
ATOM   252  O  O   . ASP A 1 34  ? -10.625 -10.441 33.503  1.00 20.68 ? 34  ASP A O   1 
ATOM   253  C  CB  . ASP A 1 34  ? -7.933  -11.740 33.345  1.00 22.89 ? 34  ASP A CB  1 
ATOM   254  C  CG  . ASP A 1 34  ? -8.218  -12.711 34.501  1.00 30.11 ? 34  ASP A CG  1 
ATOM   255  O  OD1 . ASP A 1 34  ? -9.337  -13.206 34.615  1.00 29.71 ? 34  ASP A OD1 1 
ATOM   256  O  OD2 . ASP A 1 34  ? -7.304  -12.930 35.311  1.00 38.16 ? 34  ASP A OD2 1 
ATOM   257  N  N   . THR A 1 35  ? -11.364 -12.165 32.231  1.00 20.92 ? 35  THR A N   1 
ATOM   258  C  CA  . THR A 1 35  ? -12.782 -11.906 32.418  1.00 23.54 ? 35  THR A CA  1 
ATOM   259  C  C   . THR A 1 35  ? -13.129 -12.014 33.898  1.00 25.02 ? 35  THR A C   1 
ATOM   260  O  O   . THR A 1 35  ? -14.021 -11.316 34.372  1.00 25.53 ? 35  THR A O   1 
ATOM   261  C  CB  . THR A 1 35  ? -13.648 -12.790 31.515  1.00 28.11 ? 35  THR A CB  1 
ATOM   262  O  OG1 . THR A 1 35  ? -13.525 -14.161 31.912  1.00 26.03 ? 35  THR A OG1 1 
ATOM   263  C  CG2 . THR A 1 35  ? -13.331 -12.624 30.045  1.00 23.38 ? 35  THR A CG2 1 
ATOM   264  N  N   . HIS A 1 36  ? -12.386 -12.859 34.623  1.00 25.68 ? 36  HIS A N   1 
ATOM   265  C  CA  . HIS A 1 36  ? -12.678 -13.113 36.025  1.00 28.68 ? 36  HIS A CA  1 
ATOM   266  C  C   . HIS A 1 36  ? -12.182 -11.983 36.921  1.00 31.28 ? 36  HIS A C   1 
ATOM   267  O  O   . HIS A 1 36  ? -12.773 -11.763 37.974  1.00 38.14 ? 36  HIS A O   1 
ATOM   268  C  CB  . HIS A 1 36  ? -12.216 -14.527 36.439  1.00 26.08 ? 36  HIS A CB  1 
ATOM   269  C  CG  . HIS A 1 36  ? -13.019 -15.563 35.736  1.00 28.53 ? 36  HIS A CG  1 
ATOM   270  N  ND1 . HIS A 1 36  ? -14.325 -15.790 36.062  1.00 30.30 ? 36  HIS A ND1 1 
ATOM   271  C  CD2 . HIS A 1 36  ? -12.727 -16.371 34.697  1.00 29.70 ? 36  HIS A CD2 1 
ATOM   272  C  CE1 . HIS A 1 36  ? -14.834 -16.698 35.247  1.00 31.83 ? 36  HIS A CE1 1 
ATOM   273  N  NE2 . HIS A 1 36  ? -13.867 -17.080 34.409  1.00 35.62 ? 36  HIS A NE2 1 
ATOM   274  N  N   . THR A 1 37  ? -11.139 -11.253 36.511  1.00 29.00 ? 37  THR A N   1 
ATOM   275  C  CA  . THR A 1 37  ? -10.636 -10.176 37.346  1.00 29.82 ? 37  THR A CA  1 
ATOM   276  C  C   . THR A 1 37  ? -11.007 -8.794  36.792  1.00 24.40 ? 37  THR A C   1 
ATOM   277  O  O   . THR A 1 37  ? -10.584 -7.797  37.355  1.00 29.52 ? 37  THR A O   1 
ATOM   278  C  CB  . THR A 1 37  ? -9.116  -10.246 37.562  1.00 33.54 ? 37  THR A CB  1 
ATOM   279  O  OG1 . THR A 1 37  ? -8.499  -10.326 36.283  1.00 32.29 ? 37  THR A OG1 1 
ATOM   280  C  CG2 . THR A 1 37  ? -8.669  -11.441 38.372  1.00 36.09 ? 37  THR A CG2 1 
ATOM   281  N  N   . ALA A 1 38  ? -11.744 -8.712  35.666  1.00 23.95 ? 38  ALA A N   1 
ATOM   282  C  CA  . ALA A 1 38  ? -12.277 -7.405  35.289  1.00 20.94 ? 38  ALA A CA  1 
ATOM   283  C  C   . ALA A 1 38  ? -13.311 -6.975  36.332  1.00 24.43 ? 38  ALA A C   1 
ATOM   284  O  O   . ALA A 1 38  ? -13.992 -7.815  36.924  1.00 26.74 ? 38  ALA A O   1 
ATOM   285  C  CB  . ALA A 1 38  ? -12.842 -7.431  33.895  1.00 20.68 ? 38  ALA A CB  1 
ATOM   286  N  N   . LYS A 1 39  ? -13.356 -5.673  36.628  1.00 21.61 ? 39  LYS A N   1 
ATOM   287  C  CA  . LYS A 1 39  ? -14.273 -5.184  37.653  1.00 25.10 ? 39  LYS A CA  1 
ATOM   288  C  C   . LYS A 1 39  ? -15.521 -4.593  37.005  1.00 24.55 ? 39  LYS A C   1 
ATOM   289  O  O   . LYS A 1 39  ? -15.460 -3.619  36.244  1.00 21.21 ? 39  LYS A O   1 
ATOM   290  C  CB  . LYS A 1 39  ? -13.644 -4.170  38.603  1.00 29.21 ? 39  LYS A CB  1 
ATOM   291  C  CG  . LYS A 1 39  ? -14.638 -3.730  39.669  1.00 36.98 ? 39  LYS A CG  1 
ATOM   292  C  CD  . LYS A 1 39  ? -14.080 -3.382  41.018  1.00 39.38 ? 39  LYS A CD  1 
ATOM   293  C  CE  . LYS A 1 39  ? -15.158 -2.919  41.975  1.00 39.44 ? 39  LYS A CE  1 
ATOM   294  N  NZ  . LYS A 1 39  ? -15.686 -4.033  42.801  1.00 37.04 ? 39  LYS A NZ  1 
ATOM   295  N  N   . TYR A 1 40  ? -16.666 -5.166  37.372  1.00 24.53 ? 40  TYR A N   1 
ATOM   296  C  CA  . TYR A 1 40  ? -17.922 -4.602  36.930  1.00 26.04 ? 40  TYR A CA  1 
ATOM   297  C  C   . TYR A 1 40  ? -18.051 -3.229  37.568  1.00 28.09 ? 40  TYR A C   1 
ATOM   298  O  O   . TYR A 1 40  ? -17.911 -3.079  38.788  1.00 26.46 ? 40  TYR A O   1 
ATOM   299  C  CB  . TYR A 1 40  ? -19.087 -5.494  37.366  1.00 28.82 ? 40  TYR A CB  1 
ATOM   300  C  CG  . TYR A 1 40  ? -20.418 -4.816  37.218  1.00 31.41 ? 40  TYR A CG  1 
ATOM   301  C  CD1 . TYR A 1 40  ? -20.947 -4.538  35.965  1.00 30.90 ? 40  TYR A CD1 1 
ATOM   302  C  CD2 . TYR A 1 40  ? -21.134 -4.409  38.338  1.00 36.46 ? 40  TYR A CD2 1 
ATOM   303  C  CE1 . TYR A 1 40  ? -22.163 -3.883  35.831  1.00 35.20 ? 40  TYR A CE1 1 
ATOM   304  C  CE2 . TYR A 1 40  ? -22.365 -3.780  38.213  1.00 39.54 ? 40  TYR A CE2 1 
ATOM   305  C  CZ  . TYR A 1 40  ? -22.886 -3.517  36.957  1.00 40.90 ? 40  TYR A CZ  1 
ATOM   306  O  OH  . TYR A 1 40  ? -24.088 -2.871  36.844  1.00 42.62 ? 40  TYR A OH  1 
ATOM   307  N  N   . ASP A 1 41  ? -18.305 -2.223  36.739  1.00 23.92 ? 41  ASP A N   1 
ATOM   308  C  CA  . ASP A 1 41  ? -18.505 -0.882  37.243  1.00 31.07 ? 41  ASP A CA  1 
ATOM   309  C  C   . ASP A 1 41  ? -19.941 -0.455  36.949  1.00 35.03 ? 41  ASP A C   1 
ATOM   310  O  O   . ASP A 1 41  ? -20.256 -0.038  35.832  1.00 29.95 ? 41  ASP A O   1 
ATOM   311  C  CB  . ASP A 1 41  ? -17.479 0.092   36.677  1.00 34.70 ? 41  ASP A CB  1 
ATOM   312  C  CG  . ASP A 1 41  ? -17.678 1.461   37.280  1.00 39.10 ? 41  ASP A CG  1 
ATOM   313  O  OD1 . ASP A 1 41  ? -18.730 1.647   37.928  1.00 38.97 ? 41  ASP A OD1 1 
ATOM   314  O  OD2 . ASP A 1 41  ? -16.791 2.311   37.086  1.00 42.87 ? 41  ASP A OD2 1 
ATOM   315  N  N   . PRO A 1 42  ? -20.862 -0.565  37.935  1.00 38.94 ? 42  PRO A N   1 
ATOM   316  C  CA  . PRO A 1 42  ? -22.278 -0.264  37.690  1.00 39.36 ? 42  PRO A CA  1 
ATOM   317  C  C   . PRO A 1 42  ? -22.492 1.207   37.329  1.00 36.56 ? 42  PRO A C   1 
ATOM   318  O  O   . PRO A 1 42  ? -23.545 1.552   36.794  1.00 38.20 ? 42  PRO A O   1 
ATOM   319  C  CB  . PRO A 1 42  ? -22.993 -0.647  39.003  1.00 41.19 ? 42  PRO A CB  1 
ATOM   320  C  CG  . PRO A 1 42  ? -21.891 -0.601  40.055  1.00 44.85 ? 42  PRO A CG  1 
ATOM   321  C  CD  . PRO A 1 42  ? -20.595 -0.948  39.336  1.00 41.60 ? 42  PRO A CD  1 
ATOM   322  N  N   . SER A 1 43  ? -21.484 2.055   37.609  1.00 32.60 ? 43  SER A N   1 
ATOM   323  C  CA  . SER A 1 43  ? -21.528 3.476   37.266  1.00 38.19 ? 43  SER A CA  1 
ATOM   324  C  C   . SER A 1 43  ? -21.168 3.770   35.799  1.00 38.81 ? 43  SER A C   1 
ATOM   325  O  O   . SER A 1 43  ? -21.250 4.924   35.357  1.00 38.01 ? 43  SER A O   1 
ATOM   326  C  CB  . SER A 1 43  ? -20.646 4.262   38.185  1.00 40.32 ? 43  SER A CB  1 
ATOM   327  O  OG  . SER A 1 43  ? -19.337 4.410   37.647  1.00 41.40 ? 43  SER A OG  1 
ATOM   328  N  N   . LEU A 1 44  ? -20.747 2.756   35.029  1.00 32.38 ? 44  LEU A N   1 
ATOM   329  C  CA  . LEU A 1 44  ? -20.405 3.027   33.634  1.00 32.07 ? 44  LEU A CA  1 
ATOM   330  C  C   . LEU A 1 44  ? -21.698 3.161   32.847  1.00 34.64 ? 44  LEU A C   1 
ATOM   331  O  O   . LEU A 1 44  ? -22.638 2.403   33.074  1.00 35.35 ? 44  LEU A O   1 
ATOM   332  C  CB  . LEU A 1 44  ? -19.611 1.858   33.055  1.00 29.88 ? 44  LEU A CB  1 
ATOM   333  C  CG  . LEU A 1 44  ? -18.102 1.871   33.281  1.00 26.61 ? 44  LEU A CG  1 
ATOM   334  C  CD1 . LEU A 1 44  ? -17.573 0.495   32.959  1.00 25.04 ? 44  LEU A CD1 1 
ATOM   335  C  CD2 . LEU A 1 44  ? -17.394 2.910   32.423  1.00 26.37 ? 44  LEU A CD2 1 
ATOM   336  N  N   . LYS A 1 45  ? -21.699 4.078   31.879  1.00 33.13 ? 45  LYS A N   1 
ATOM   337  C  CA  . LYS A 1 45  ? -22.907 4.283   31.091  1.00 34.24 ? 45  LYS A CA  1 
ATOM   338  C  C   . LYS A 1 45  ? -22.953 3.286   29.938  1.00 31.14 ? 45  LYS A C   1 
ATOM   339  O  O   . LYS A 1 45  ? -21.934 2.704   29.537  1.00 30.69 ? 45  LYS A O   1 
ATOM   340  C  CB  . LYS A 1 45  ? -22.971 5.725   30.602  1.00 32.67 ? 45  LYS A CB  1 
ATOM   341  C  CG  . LYS A 1 45  ? -23.006 6.751   31.722  1.00 38.25 ? 45  LYS A CG  1 
ATOM   342  C  CD  . LYS A 1 45  ? -22.807 8.173   31.227  1.00 43.88 ? 45  LYS A CD  1 
ATOM   343  N  N   . PRO A 1 46  ? -24.152 3.013   29.372  1.00 25.89 ? 46  PRO A N   1 
ATOM   344  C  CA  . PRO A 1 46  ? -24.219 2.285   28.108  1.00 27.65 ? 46  PRO A CA  1 
ATOM   345  C  C   . PRO A 1 46  ? -23.456 3.116   27.075  1.00 23.72 ? 46  PRO A C   1 
ATOM   346  O  O   . PRO A 1 46  ? -23.399 4.343   27.152  1.00 22.59 ? 46  PRO A O   1 
ATOM   347  C  CB  . PRO A 1 46  ? -25.721 2.212   27.778  1.00 28.18 ? 46  PRO A CB  1 
ATOM   348  C  CG  . PRO A 1 46  ? -26.388 2.425   29.134  1.00 31.76 ? 46  PRO A CG  1 
ATOM   349  C  CD  . PRO A 1 46  ? -25.477 3.378   29.902  1.00 29.34 ? 46  PRO A CD  1 
ATOM   350  N  N   . LEU A 1 47  ? -22.878 2.409   26.110  1.00 27.96 ? 47  LEU A N   1 
ATOM   351  C  CA  . LEU A 1 47  ? -22.123 3.072   25.068  1.00 21.23 ? 47  LEU A CA  1 
ATOM   352  C  C   . LEU A 1 47  ? -23.142 3.650   24.085  1.00 23.40 ? 47  LEU A C   1 
ATOM   353  O  O   . LEU A 1 47  ? -24.116 2.976   23.761  1.00 23.63 ? 47  LEU A O   1 
ATOM   354  C  CB  . LEU A 1 47  ? -21.285 1.973   24.411  1.00 24.09 ? 47  LEU A CB  1 
ATOM   355  C  CG  . LEU A 1 47  ? -20.214 2.391   23.424  1.00 28.41 ? 47  LEU A CG  1 
ATOM   356  C  CD1 . LEU A 1 47  ? -19.181 3.300   24.098  1.00 28.11 ? 47  LEU A CD1 1 
ATOM   357  C  CD2 . LEU A 1 47  ? -19.576 1.152   22.807  1.00 27.05 ? 47  LEU A CD2 1 
ATOM   358  N  N   . SER A 1 48  ? -22.933 4.895   23.647  1.00 19.55 ? 48  SER A N   1 
ATOM   359  C  CA  . SER A 1 48  ? -23.741 5.474   22.595  1.00 21.42 ? 48  SER A CA  1 
ATOM   360  C  C   . SER A 1 48  ? -22.988 5.398   21.263  1.00 21.00 ? 48  SER A C   1 
ATOM   361  O  O   . SER A 1 48  ? -21.996 6.101   21.083  1.00 19.66 ? 48  SER A O   1 
ATOM   362  C  CB  . SER A 1 48  ? -24.040 6.904   22.964  1.00 24.71 ? 48  SER A CB  1 
ATOM   363  O  OG  . SER A 1 48  ? -24.840 7.500   21.961  1.00 26.64 ? 48  SER A OG  1 
ATOM   364  N  N   . VAL A 1 49  ? -23.515 4.624   20.326  1.00 22.78 ? 49  VAL A N   1 
ATOM   365  C  CA  . VAL A 1 49  ? -22.906 4.503   19.010  1.00 22.62 ? 49  VAL A CA  1 
ATOM   366  C  C   . VAL A 1 49  ? -23.875 5.115   18.010  1.00 25.92 ? 49  VAL A C   1 
ATOM   367  O  O   . VAL A 1 49  ? -24.894 4.503   17.719  1.00 29.96 ? 49  VAL A O   1 
ATOM   368  C  CB  . VAL A 1 49  ? -22.636 3.018   18.689  1.00 23.90 ? 49  VAL A CB  1 
ATOM   369  C  CG1 . VAL A 1 49  ? -22.091 2.846   17.279  1.00 26.35 ? 49  VAL A CG1 1 
ATOM   370  C  CG2 . VAL A 1 49  ? -21.734 2.369   19.733  1.00 24.19 ? 49  VAL A CG2 1 
ATOM   371  N  N   . SER A 1 50  ? -23.593 6.347   17.547  1.00 20.70 ? 50  SER A N   1 
ATOM   372  C  CA  . SER A 1 50  ? -24.486 7.054   16.645  1.00 23.76 ? 50  SER A CA  1 
ATOM   373  C  C   . SER A 1 50  ? -23.862 7.107   15.257  1.00 20.97 ? 50  SER A C   1 
ATOM   374  O  O   . SER A 1 50  ? -23.243 8.108   14.923  1.00 19.32 ? 50  SER A O   1 
ATOM   375  C  CB  . SER A 1 50  ? -24.789 8.472   17.092  1.00 27.86 ? 50  SER A CB  1 
ATOM   376  O  OG  . SER A 1 50  ? -25.431 8.468   18.344  1.00 33.62 ? 50  SER A OG  1 
ATOM   377  N  N   . TYR A 1 51  ? -24.141 6.081   14.451  1.00 20.44 ? 51  TYR A N   1 
ATOM   378  C  CA  . TYR A 1 51  ? -23.509 5.907   13.144  1.00 19.18 ? 51  TYR A CA  1 
ATOM   379  C  C   . TYR A 1 51  ? -24.424 6.215   11.958  1.00 18.65 ? 51  TYR A C   1 
ATOM   380  O  O   . TYR A 1 51  ? -24.017 6.073   10.793  1.00 18.12 ? 51  TYR A O   1 
ATOM   381  C  CB  . TYR A 1 51  ? -22.954 4.486   13.043  1.00 19.70 ? 51  TYR A CB  1 
ATOM   382  C  CG  . TYR A 1 51  ? -21.657 4.243   13.781  1.00 18.71 ? 51  TYR A CG  1 
ATOM   383  C  CD1 . TYR A 1 51  ? -20.984 5.252   14.461  1.00 17.68 ? 51  TYR A CD1 1 
ATOM   384  C  CD2 . TYR A 1 51  ? -21.074 2.983   13.728  1.00 17.56 ? 51  TYR A CD2 1 
ATOM   385  C  CE1 . TYR A 1 51  ? -19.768 4.961   15.083  1.00 15.21 ? 51  TYR A CE1 1 
ATOM   386  C  CE2 . TYR A 1 51  ? -19.905 2.666   14.390  1.00 17.10 ? 51  TYR A CE2 1 
ATOM   387  C  CZ  . TYR A 1 51  ? -19.233 3.679   15.047  1.00 16.36 ? 51  TYR A CZ  1 
ATOM   388  O  OH  . TYR A 1 51  ? -18.041 3.332   15.653  1.00 17.39 ? 51  TYR A OH  1 
ATOM   389  N  N   . ASP A 1 52  ? -25.653 6.685   12.226  1.00 20.74 ? 52  ASP A N   1 
ATOM   390  C  CA  . ASP A 1 52  ? -26.653 6.897   11.176  1.00 23.73 ? 52  ASP A CA  1 
ATOM   391  C  C   . ASP A 1 52  ? -26.219 7.790   9.996   1.00 24.45 ? 52  ASP A C   1 
ATOM   392  O  O   . ASP A 1 52  ? -26.663 7.579   8.846   1.00 28.33 ? 52  ASP A O   1 
ATOM   393  C  CB  . ASP A 1 52  ? -27.950 7.440   11.776  1.00 27.65 ? 52  ASP A CB  1 
ATOM   394  C  CG  . ASP A 1 52  ? -27.739 8.490   12.852  1.00 35.13 ? 52  ASP A CG  1 
ATOM   395  O  OD1 . ASP A 1 52  ? -26.978 8.220   13.855  1.00 38.68 ? 52  ASP A OD1 1 
ATOM   396  O  OD2 . ASP A 1 52  ? -28.356 9.582   12.709  1.00 47.30 ? 52  ASP A OD2 1 
ATOM   397  N  N   . GLN A 1 53  ? -25.420 8.816   10.258  1.00 20.24 ? 53  GLN A N   1 
ATOM   398  C  CA  . GLN A 1 53  ? -25.044 9.766   9.212   1.00 20.87 ? 53  GLN A CA  1 
ATOM   399  C  C   . GLN A 1 53  ? -23.612 9.509   8.724   1.00 19.03 ? 53  GLN A C   1 
ATOM   400  O  O   . GLN A 1 53  ? -22.992 10.377  8.100   1.00 17.44 ? 53  GLN A O   1 
ATOM   401  C  CB  . GLN A 1 53  ? -25.230 11.218  9.663   1.00 21.08 ? 53  GLN A CB  1 
ATOM   402  C  CG  . GLN A 1 53  ? -26.680 11.579  9.964   1.00 23.63 ? 53  GLN A CG  1 
ATOM   403  C  CD  . GLN A 1 53  ? -27.551 11.398  8.745   1.00 28.56 ? 53  GLN A CD  1 
ATOM   404  O  OE1 . GLN A 1 53  ? -28.582 10.714  8.782   1.00 33.17 ? 53  GLN A OE1 1 
ATOM   405  N  NE2 . GLN A 1 53  ? -27.125 11.971  7.633   1.00 27.62 ? 53  GLN A NE2 1 
ATOM   406  N  N   . ALA A 1 54  ? -23.098 8.302   8.964   1.00 17.73 ? 54  ALA A N   1 
ATOM   407  C  CA  . ALA A 1 54  ? -21.733 7.993   8.570   1.00 16.43 ? 54  ALA A CA  1 
ATOM   408  C  C   . ALA A 1 54  ? -21.581 8.172   7.065   1.00 17.56 ? 54  ALA A C   1 
ATOM   409  O  O   . ALA A 1 54  ? -22.484 7.831   6.300   1.00 18.84 ? 54  ALA A O   1 
ATOM   410  C  CB  . ALA A 1 54  ? -21.352 6.578   8.987   1.00 18.20 ? 54  ALA A CB  1 
ATOM   411  N  N   . THR A 1 55  ? -20.443 8.775   6.693   1.00 16.20 ? 55  THR A N   1 
ATOM   412  C  CA  . THR A 1 55  ? -20.084 8.921   5.286   1.00 15.06 ? 55  THR A CA  1 
ATOM   413  C  C   . THR A 1 55  ? -18.699 8.313   5.071   1.00 14.82 ? 55  THR A C   1 
ATOM   414  O  O   . THR A 1 55  ? -17.663 8.948   5.305   1.00 14.02 ? 55  THR A O   1 
ATOM   415  C  CB  . THR A 1 55  ? -19.978 10.401  4.878   1.00 17.65 ? 55  THR A CB  1 
ATOM   416  O  OG1 . THR A 1 55  ? -21.287 10.922  5.051   1.00 19.93 ? 55  THR A OG1 1 
ATOM   417  C  CG2 . THR A 1 55  ? -19.608 10.561  3.417   1.00 19.10 ? 55  THR A CG2 1 
ATOM   418  N  N   . SER A 1 56  ? -18.682 7.051   4.621   1.00 13.64 ? 56  SER A N   1 
ATOM   419  C  CA  . SER A 1 56  ? -17.420 6.490   4.164   1.00 14.30 ? 56  SER A CA  1 
ATOM   420  C  C   . SER A 1 56  ? -16.949 7.154   2.871   1.00 15.77 ? 56  SER A C   1 
ATOM   421  O  O   . SER A 1 56  ? -17.750 7.644   2.049   1.00 14.19 ? 56  SER A O   1 
ATOM   422  C  CB  . SER A 1 56  ? -17.492 4.980   4.004   1.00 13.00 ? 56  SER A CB  1 
ATOM   423  O  OG  . SER A 1 56  ? -18.397 4.657   2.918   1.00 13.93 ? 56  SER A OG  1 
ATOM   424  N  N   . LEU A 1 57  ? -15.621 7.226   2.749   1.00 15.48 ? 57  LEU A N   1 
ATOM   425  C  CA  . LEU A 1 57  ? -15.097 7.816   1.522   1.00 16.29 ? 57  LEU A CA  1 
ATOM   426  C  C   . LEU A 1 57  ? -14.230 6.903   0.670   1.00 16.21 ? 57  LEU A C   1 
ATOM   427  O  O   . LEU A 1 57  ? -14.377 6.908   -0.564  1.00 17.21 ? 57  LEU A O   1 
ATOM   428  C  CB  . LEU A 1 57  ? -14.310 9.070   1.857   1.00 16.14 ? 57  LEU A CB  1 
ATOM   429  C  CG  . LEU A 1 57  ? -15.137 10.187  2.489   1.00 16.98 ? 57  LEU A CG  1 
ATOM   430  C  CD1 . LEU A 1 57  ? -14.222 11.233  3.092   1.00 18.40 ? 57  LEU A CD1 1 
ATOM   431  C  CD2 . LEU A 1 57  ? -16.085 10.785  1.439   1.00 19.34 ? 57  LEU A CD2 1 
ATOM   432  N  N   . ARG A 1 58  ? -13.224 6.282   1.279   1.00 14.47 ? 58  ARG A N   1 
ATOM   433  C  CA  . ARG A 1 58  ? -12.220 5.567   0.513   1.00 16.00 ? 58  ARG A CA  1 
ATOM   434  C  C   . ARG A 1 58  ? -11.787 4.343   1.297   1.00 15.01 ? 58  ARG A C   1 
ATOM   435  O  O   . ARG A 1 58  ? -11.904 4.310   2.518   1.00 14.46 ? 58  ARG A O   1 
ATOM   436  C  CB  . ARG A 1 58  ? -10.986 6.459   0.250   1.00 18.25 ? 58  ARG A CB  1 
ATOM   437  C  CG  . ARG A 1 58  ? -11.278 7.683   -0.610  1.00 23.87 ? 58  ARG A CG  1 
ATOM   438  C  CD  . ARG A 1 58  ? -9.999  8.413   -0.985  1.00 26.05 ? 58  ARG A CD  1 
ATOM   439  N  NE  . ARG A 1 58  ? -9.214  7.557   -1.872  1.00 28.32 ? 58  ARG A NE  1 
ATOM   440  C  CZ  . ARG A 1 58  ? -9.526  7.346   -3.154  1.00 27.78 ? 58  ARG A CZ  1 
ATOM   441  N  NH1 . ARG A 1 58  ? -8.771  6.550   -3.891  1.00 30.93 ? 58  ARG A NH1 1 
ATOM   442  N  NH2 . ARG A 1 58  ? -10.596 7.914   -3.694  1.00 28.02 ? 58  ARG A NH2 1 
ATOM   443  N  N   . ILE A 1 59  ? -11.186 3.385   0.594   1.00 15.04 ? 59  ILE A N   1 
ATOM   444  C  CA  . ILE A 1 59  ? -10.519 2.257   1.201   1.00 15.05 ? 59  ILE A CA  1 
ATOM   445  C  C   . ILE A 1 59  ? -9.102  2.166   0.635   1.00 14.99 ? 59  ILE A C   1 
ATOM   446  O  O   . ILE A 1 59  ? -8.880  2.303   -0.571  1.00 15.76 ? 59  ILE A O   1 
ATOM   447  C  CB  . ILE A 1 59  ? -11.341 0.962   0.950   1.00 15.19 ? 59  ILE A CB  1 
ATOM   448  C  CG1 . ILE A 1 59  ? -10.901 -0.229  1.818   1.00 16.21 ? 59  ILE A CG1 1 
ATOM   449  C  CG2 . ILE A 1 59  ? -11.499 0.612   -0.531  1.00 15.86 ? 59  ILE A CG2 1 
ATOM   450  C  CD1 . ILE A 1 59  ? -11.826 -1.427  1.657   1.00 17.37 ? 59  ILE A CD1 1 
ATOM   451  N  N   . LEU A 1 60  ? -8.149  1.852   1.506   1.00 15.26 ? 60  LEU A N   1 
ATOM   452  C  CA  . LEU A 1 60  ? -6.779  1.771   1.022   1.00 17.75 ? 60  LEU A CA  1 
ATOM   453  C  C   . LEU A 1 60  ? -5.994  0.695   1.747   1.00 16.06 ? 60  LEU A C   1 
ATOM   454  O  O   . LEU A 1 60  ? -6.230  0.401   2.931   1.00 17.01 ? 60  LEU A O   1 
ATOM   455  C  CB  . LEU A 1 60  ? -6.090  3.125   1.142   1.00 21.41 ? 60  LEU A CB  1 
ATOM   456  C  CG  . LEU A 1 60  ? -5.679  3.577   2.527   1.00 28.01 ? 60  LEU A CG  1 
ATOM   457  C  CD1 . LEU A 1 60  ? -4.209  3.967   2.505   1.00 32.03 ? 60  LEU A CD1 1 
ATOM   458  C  CD2 . LEU A 1 60  ? -6.519  4.788   2.901   1.00 37.95 ? 60  LEU A CD2 1 
ATOM   459  N  N   . ASN A 1 61  ? -5.055  0.114   0.985   1.00 15.69 ? 61  ASN A N   1 
ATOM   460  C  CA  . ASN A 1 61  ? -4.067  -0.820  1.519   1.00 14.80 ? 61  ASN A CA  1 
ATOM   461  C  C   . ASN A 1 61  ? -2.811  -0.008  1.823   1.00 16.87 ? 61  ASN A C   1 
ATOM   462  O  O   . ASN A 1 61  ? -2.222  0.557   0.912   1.00 16.50 ? 61  ASN A O   1 
ATOM   463  C  CB  . ASN A 1 61  ? -3.792  -1.922  0.488   1.00 14.71 ? 61  ASN A CB  1 
ATOM   464  C  CG  . ASN A 1 61  ? -2.687  -2.869  0.881   1.00 14.83 ? 61  ASN A CG  1 
ATOM   465  O  OD1 . ASN A 1 61  ? -1.822  -2.562  1.712   1.00 15.92 ? 61  ASN A OD1 1 
ATOM   466  N  ND2 . ASN A 1 61  ? -2.738  -4.064  0.340   1.00 14.63 ? 61  ASN A ND2 1 
ATOM   467  N  N   . ASN A 1 62  ? -2.409  0.055   3.099   1.00 16.43 ? 62  ASN A N   1 
ATOM   468  C  CA  . ASN A 1 62  ? -1.278  0.912   3.446   1.00 17.98 ? 62  ASN A CA  1 
ATOM   469  C  C   . ASN A 1 62  ? -0.026  0.082   3.707   1.00 18.58 ? 62  ASN A C   1 
ATOM   470  O  O   . ASN A 1 62  ? 0.981   0.627   4.195   1.00 19.13 ? 62  ASN A O   1 
ATOM   471  C  CB  . ASN A 1 62  ? -1.577  1.790   4.660   1.00 19.28 ? 62  ASN A CB  1 
ATOM   472  C  CG  . ASN A 1 62  ? -2.011  1.023   5.895   1.00 19.93 ? 62  ASN A CG  1 
ATOM   473  O  OD1 . ASN A 1 62  ? -1.763  -0.165  6.041   1.00 18.78 ? 62  ASN A OD1 1 
ATOM   474  N  ND2 . ASN A 1 62  ? -2.749  1.683   6.766   1.00 26.01 ? 62  ASN A ND2 1 
ATOM   475  N  N   . GLY A 1 63  ? -0.097  -1.218  3.394   1.00 19.34 ? 63  GLY A N   1 
ATOM   476  C  CA  . GLY A 1 63  ? 1.046   -2.101  3.553   1.00 18.71 ? 63  GLY A CA  1 
ATOM   477  C  C   . GLY A 1 63  ? 1.143   -2.684  4.965   1.00 17.23 ? 63  GLY A C   1 
ATOM   478  O  O   . GLY A 1 63  ? 1.995   -3.545  5.228   1.00 19.94 ? 63  GLY A O   1 
ATOM   479  N  N   . HIS A 1 64  ? 0.237   -2.258  5.867   1.00 18.40 ? 64  HIS A N   1 
ATOM   480  C  CA  . HIS A 1 64  ? 0.141   -2.816  7.208   1.00 19.35 ? 64  HIS A CA  1 
ATOM   481  C  C   . HIS A 1 64  ? -1.201  -3.499  7.430   1.00 18.59 ? 64  HIS A C   1 
ATOM   482  O  O   . HIS A 1 64  ? -1.239  -4.615  7.933   1.00 20.29 ? 64  HIS A O   1 
ATOM   483  C  CB  . HIS A 1 64  ? 0.389   -1.732  8.257   1.00 21.87 ? 64  HIS A CB  1 
ATOM   484  C  CG  . HIS A 1 64  ? 1.695   -1.022  8.073   1.00 22.27 ? 64  HIS A CG  1 
ATOM   485  N  ND1 . HIS A 1 64  ? 2.911   -1.650  8.254   1.00 22.68 ? 64  HIS A ND1 1 
ATOM   486  C  CD2 . HIS A 1 64  ? 1.965   0.263   7.798   1.00 24.55 ? 64  HIS A CD2 1 
ATOM   487  C  CE1 . HIS A 1 64  ? 3.878   -0.786  8.064   1.00 23.81 ? 64  HIS A CE1 1 
ATOM   488  N  NE2 . HIS A 1 64  ? 3.328   0.400   7.795   1.00 23.06 ? 64  HIS A NE2 1 
ATOM   489  N  N   . SER A 1 65  ? -2.293  -2.822  7.028   1.00 17.65 ? 65  SER A N   1 
ATOM   490  C  CA  . SER A 1 65  ? -3.664  -3.318  7.094   1.00 15.76 ? 65  SER A CA  1 
ATOM   491  C  C   . SER A 1 65  ? -4.378  -2.762  5.870   1.00 15.39 ? 65  SER A C   1 
ATOM   492  O  O   . SER A 1 65  ? -3.737  -2.178  4.999   1.00 16.17 ? 65  SER A O   1 
ATOM   493  C  CB  . SER A 1 65  ? -4.293  -2.881  8.419   1.00 17.96 ? 65  SER A CB  1 
ATOM   494  O  OG  . SER A 1 65  ? -5.619  -3.395  8.575   1.00 21.52 ? 65  SER A OG  1 
ATOM   495  N  N   . PHE A 1 66  ? -5.709  -2.886  5.812   1.00 15.80 ? 66  PHE A N   1 
ATOM   496  C  CA  . PHE A 1 66  ? -6.487  -1.998  4.966   1.00 16.77 ? 66  PHE A CA  1 
ATOM   497  C  C   . PHE A 1 66  ? -7.388  -1.152  5.851   1.00 14.63 ? 66  PHE A C   1 
ATOM   498  O  O   . PHE A 1 66  ? -7.776  -1.605  6.937   1.00 14.85 ? 66  PHE A O   1 
ATOM   499  C  CB  . PHE A 1 66  ? -7.287  -2.766  3.908   1.00 15.97 ? 66  PHE A CB  1 
ATOM   500  C  CG  . PHE A 1 66  ? -8.430  -3.597  4.406   1.00 17.04 ? 66  PHE A CG  1 
ATOM   501  C  CD1 . PHE A 1 66  ? -8.228  -4.916  4.808   1.00 17.25 ? 66  PHE A CD1 1 
ATOM   502  C  CD2 . PHE A 1 66  ? -9.715  -3.066  4.506   1.00 17.25 ? 66  PHE A CD2 1 
ATOM   503  C  CE1 . PHE A 1 66  ? -9.278  -5.673  5.307   1.00 17.72 ? 66  PHE A CE1 1 
ATOM   504  C  CE2 . PHE A 1 66  ? -10.766 -3.844  4.987   1.00 16.53 ? 66  PHE A CE2 1 
ATOM   505  C  CZ  . PHE A 1 66  ? -10.556 -5.147  5.381   1.00 17.82 ? 66  PHE A CZ  1 
ATOM   506  N  N   . LYS A 1 67  ? -7.718  0.057   5.374   1.00 14.84 ? 67  LYS A N   1 
ATOM   507  C  CA  . LYS A 1 67  ? -8.522  0.948   6.191   1.00 16.02 ? 67  LYS A CA  1 
ATOM   508  C  C   . LYS A 1 67  ? -9.607  1.589   5.342   1.00 15.50 ? 67  LYS A C   1 
ATOM   509  O  O   . LYS A 1 67  ? -9.371  1.929   4.185   1.00 16.56 ? 67  LYS A O   1 
ATOM   510  C  CB  . LYS A 1 67  ? -7.704  2.037   6.899   1.00 19.82 ? 67  LYS A CB  1 
ATOM   511  C  CG  . LYS A 1 67  ? -6.873  2.955   6.014   1.00 21.28 ? 67  LYS A CG  1 
ATOM   512  C  CD  . LYS A 1 67  ? -6.360  4.190   6.776   1.00 24.51 ? 67  LYS A CD  1 
ATOM   513  C  CE  . LYS A 1 67  ? -5.438  5.058   5.954   1.00 28.62 ? 67  LYS A CE  1 
ATOM   514  N  NZ  . LYS A 1 67  ? -4.924  6.203   6.748   1.00 31.43 ? 67  LYS A NZ  1 
ATOM   515  N  N   . VAL A 1 68  ? -10.778 1.786   5.965   1.00 13.23 ? 68  VAL A N   1 
ATOM   516  C  CA  . VAL A 1 68  ? -11.852 2.532   5.312   1.00 14.04 ? 68  VAL A CA  1 
ATOM   517  C  C   . VAL A 1 68  ? -11.924 3.858   6.042   1.00 14.98 ? 68  VAL A C   1 
ATOM   518  O  O   . VAL A 1 68  ? -12.051 3.847   7.272   1.00 14.70 ? 68  VAL A O   1 
ATOM   519  C  CB  . VAL A 1 68  ? -13.191 1.794   5.465   1.00 13.86 ? 68  VAL A CB  1 
ATOM   520  C  CG1 . VAL A 1 68  ? -14.346 2.660   4.942   1.00 15.20 ? 68  VAL A CG1 1 
ATOM   521  C  CG2 . VAL A 1 68  ? -13.175 0.486   4.703   1.00 13.85 ? 68  VAL A CG2 1 
ATOM   522  N  N   . GLU A 1 69  ? -11.769 4.963   5.314   1.00 16.06 ? 69  GLU A N   1 
ATOM   523  C  CA  . GLU A 1 69  ? -11.737 6.300   5.886   1.00 15.88 ? 69  GLU A CA  1 
ATOM   524  C  C   . GLU A 1 69  ? -13.084 6.974   5.683   1.00 15.38 ? 69  GLU A C   1 
ATOM   525  O  O   . GLU A 1 69  ? -13.714 6.807   4.622   1.00 14.57 ? 69  GLU A O   1 
ATOM   526  C  CB  . GLU A 1 69  ? -10.637 7.138   5.245   1.00 20.61 ? 69  GLU A CB  1 
ATOM   527  C  CG  . GLU A 1 69  ? -9.279  6.534   5.587   1.00 27.91 ? 69  GLU A CG  1 
ATOM   528  C  CD  . GLU A 1 69  ? -8.044  7.388   5.366   1.00 33.63 ? 69  GLU A CD  1 
ATOM   529  O  OE1 . GLU A 1 69  ? -7.606  7.450   4.217   1.00 45.85 ? 69  GLU A OE1 1 
ATOM   530  O  OE2 . GLU A 1 69  ? -7.502  7.940   6.341   1.00 33.38 ? 69  GLU A OE2 1 
ATOM   531  N  N   . PHE A 1 70  ? -13.472 7.699   6.735   1.00 14.61 ? 70  PHE A N   1 
ATOM   532  C  CA  . PHE A 1 70  ? -14.733 8.428   6.801   1.00 14.06 ? 70  PHE A CA  1 
ATOM   533  C  C   . PHE A 1 70  ? -14.515 9.934   6.721   1.00 15.00 ? 70  PHE A C   1 
ATOM   534  O  O   . PHE A 1 70  ? -13.468 10.424  7.078   1.00 15.88 ? 70  PHE A O   1 
ATOM   535  C  CB  . PHE A 1 70  ? -15.497 8.101   8.098   1.00 14.83 ? 70  PHE A CB  1 
ATOM   536  C  CG  . PHE A 1 70  ? -16.052 6.708   8.062   1.00 15.43 ? 70  PHE A CG  1 
ATOM   537  C  CD1 . PHE A 1 70  ? -15.224 5.618   8.279   1.00 16.42 ? 70  PHE A CD1 1 
ATOM   538  C  CD2 . PHE A 1 70  ? -17.381 6.469   7.753   1.00 15.12 ? 70  PHE A CD2 1 
ATOM   539  C  CE1 . PHE A 1 70  ? -15.684 4.312   8.190   1.00 18.10 ? 70  PHE A CE1 1 
ATOM   540  C  CE2 . PHE A 1 70  ? -17.836 5.169   7.636   1.00 14.72 ? 70  PHE A CE2 1 
ATOM   541  C  CZ  . PHE A 1 70  ? -17.001 4.084   7.849   1.00 15.38 ? 70  PHE A CZ  1 
ATOM   542  N  N   . ASP A 1 71  ? -15.565 10.626  6.263   1.00 13.92 ? 71  ASP A N   1 
ATOM   543  C  CA  . ASP A 1 71  ? -15.638 12.079  6.426   1.00 15.02 ? 71  ASP A CA  1 
ATOM   544  C  C   . ASP A 1 71  ? -15.812 12.405  7.903   1.00 16.20 ? 71  ASP A C   1 
ATOM   545  O  O   . ASP A 1 71  ? -16.890 12.208  8.445   1.00 19.68 ? 71  ASP A O   1 
ATOM   546  C  CB  . ASP A 1 71  ? -16.790 12.611  5.573   1.00 16.99 ? 71  ASP A CB  1 
ATOM   547  C  CG  . ASP A 1 71  ? -16.895 14.125  5.647   1.00 22.81 ? 71  ASP A CG  1 
ATOM   548  O  OD1 . ASP A 1 71  ? -16.085 14.740  6.361   1.00 19.63 ? 71  ASP A OD1 1 
ATOM   549  O  OD2 . ASP A 1 71  ? -17.857 14.663  5.071   1.00 25.91 ? 71  ASP A OD2 1 
ATOM   550  N  N   . ASP A 1 72  ? -14.753 12.906  8.557   1.00 16.71 ? 72  ASP A N   1 
ATOM   551  C  CA  . ASP A 1 72  ? -14.887 13.275  9.956   1.00 16.76 ? 72  ASP A CA  1 
ATOM   552  C  C   . ASP A 1 72  ? -14.809 14.798  10.130  1.00 16.41 ? 72  ASP A C   1 
ATOM   553  O  O   . ASP A 1 72  ? -14.350 15.258  11.159  1.00 17.21 ? 72  ASP A O   1 
ATOM   554  C  CB  . ASP A 1 72  ? -13.755 12.649  10.778  1.00 16.72 ? 72  ASP A CB  1 
ATOM   555  C  CG  . ASP A 1 72  ? -12.350 12.961  10.298  1.00 19.81 ? 72  ASP A CG  1 
ATOM   556  O  OD1 . ASP A 1 72  ? -12.198 13.713  9.310   1.00 20.25 ? 72  ASP A OD1 1 
ATOM   557  O  OD2 . ASP A 1 72  ? -11.372 12.497  10.963  1.00 20.54 ? 72  ASP A OD2 1 
ATOM   558  N  N   . SER A 1 73  ? -15.186 15.544  9.095   1.00 15.85 ? 73  SER A N   1 
ATOM   559  C  CA  . SER A 1 73  ? -15.166 17.015  9.099   1.00 17.24 ? 73  SER A CA  1 
ATOM   560  C  C   . SER A 1 73  ? -16.427 17.586  9.745   1.00 18.31 ? 73  SER A C   1 
ATOM   561  O  O   . SER A 1 73  ? -16.568 18.811  9.882   1.00 19.70 ? 73  SER A O   1 
ATOM   562  C  CB  . SER A 1 73  ? -14.931 17.567  7.721   1.00 17.07 ? 73  SER A CB  1 
ATOM   563  O  OG  . SER A 1 73  ? -16.096 17.393  6.916   1.00 18.82 ? 73  SER A OG  1 
ATOM   564  N  N   . GLN A 1 74  ? -17.362 16.723  10.147  1.00 19.43 ? 74  GLN A N   1 
ATOM   565  C  CA  . GLN A 1 74  ? -18.508 17.183  10.925  1.00 22.22 ? 74  GLN A CA  1 
ATOM   566  C  C   . GLN A 1 74  ? -19.012 16.040  11.794  1.00 22.28 ? 74  GLN A C   1 
ATOM   567  O  O   . GLN A 1 74  ? -18.540 14.924  11.600  1.00 20.81 ? 74  GLN A O   1 
ATOM   568  C  CB  . GLN A 1 74  ? -19.563 17.906  10.070  1.00 28.41 ? 74  GLN A CB  1 
ATOM   569  C  CG  . GLN A 1 74  ? -19.972 17.225  8.783   1.00 35.24 ? 74  GLN A CG  1 
ATOM   570  C  CD  . GLN A 1 74  ? -21.147 17.959  8.167   1.00 34.04 ? 74  GLN A CD  1 
ATOM   571  O  OE1 . GLN A 1 74  ? -21.878 18.675  8.851   1.00 39.12 ? 74  GLN A OE1 1 
ATOM   572  N  NE2 . GLN A 1 74  ? -21.354 17.774  6.878   1.00 33.21 ? 74  GLN A NE2 1 
ATOM   573  N  N   . ASP A 1 75  ? -19.917 16.307  12.760  1.00 25.12 ? 75  ASP A N   1 
ATOM   574  C  CA  . ASP A 1 75  ? -20.370 15.230  13.632  1.00 28.33 ? 75  ASP A CA  1 
ATOM   575  C  C   . ASP A 1 75  ? -21.365 14.383  12.843  1.00 28.52 ? 75  ASP A C   1 
ATOM   576  O  O   . ASP A 1 75  ? -22.486 14.835  12.593  1.00 34.05 ? 75  ASP A O   1 
ATOM   577  C  CB  . ASP A 1 75  ? -21.033 15.717  14.933  1.00 31.07 ? 75  ASP A CB  1 
ATOM   578  C  CG  . ASP A 1 75  ? -20.065 16.283  15.974  1.00 39.62 ? 75  ASP A CG  1 
ATOM   579  O  OD1 . ASP A 1 75  ? -18.840 16.059  15.818  1.00 38.90 ? 75  ASP A OD1 1 
ATOM   580  O  OD2 . ASP A 1 75  ? -20.544 16.936  16.951  1.00 35.48 ? 75  ASP A OD2 1 
ATOM   581  N  N   . LYS A 1 76  ? -20.920 13.221  12.372  1.00 23.70 ? 76  LYS A N   1 
ATOM   582  C  CA  . LYS A 1 76  ? -21.727 12.387  11.504  1.00 24.16 ? 76  LYS A CA  1 
ATOM   583  C  C   . LYS A 1 76  ? -21.861 10.992  12.100  1.00 29.93 ? 76  LYS A C   1 
ATOM   584  O  O   . LYS A 1 76  ? -22.920 10.380  12.032  1.00 35.64 ? 76  LYS A O   1 
ATOM   585  C  CB  . LYS A 1 76  ? -21.097 12.258  10.118  1.00 24.75 ? 76  LYS A CB  1 
ATOM   586  C  CG  . LYS A 1 76  ? -21.395 13.429  9.202   1.00 26.02 ? 76  LYS A CG  1 
ATOM   587  C  CD  . LYS A 1 76  ? -20.748 13.288  7.864   1.00 25.32 ? 76  LYS A CD  1 
ATOM   588  C  CE  . LYS A 1 76  ? -21.629 13.949  6.823   1.00 26.25 ? 76  LYS A CE  1 
ATOM   589  N  NZ  . LYS A 1 76  ? -21.101 13.731  5.467   1.00 32.13 ? 76  LYS A NZ  1 
ATOM   590  N  N   . ALA A 1 77  ? -20.761 10.468  12.609  1.00 24.64 ? 77  ALA A N   1 
ATOM   591  C  CA  . ALA A 1 77  ? -20.757 9.104   13.118  1.00 20.80 ? 77  ALA A CA  1 
ATOM   592  C  C   . ALA A 1 77  ? -19.935 9.198   14.383  1.00 20.05 ? 77  ALA A C   1 
ATOM   593  O  O   . ALA A 1 77  ? -18.736 9.416   14.276  1.00 20.45 ? 77  ALA A O   1 
ATOM   594  C  CB  . ALA A 1 77  ? -20.050 8.213   12.123  1.00 23.15 ? 77  ALA A CB  1 
ATOM   595  N  N   . VAL A 1 78  ? -20.597 9.184   15.531  1.00 18.65 ? 78  VAL A N   1 
ATOM   596  C  CA  . VAL A 1 78  ? -19.866 9.496   16.755  1.00 20.52 ? 78  VAL A CA  1 
ATOM   597  C  C   . VAL A 1 78  ? -20.111 8.423   17.816  1.00 20.50 ? 78  VAL A C   1 
ATOM   598  O  O   . VAL A 1 78  ? -21.101 7.687   17.825  1.00 21.09 ? 78  VAL A O   1 
ATOM   599  C  CB  . VAL A 1 78  ? -20.105 10.926  17.282  1.00 21.58 ? 78  VAL A CB  1 
ATOM   600  C  CG1 . VAL A 1 78  ? -19.893 12.023  16.240  1.00 23.16 ? 78  VAL A CG1 1 
ATOM   601  C  CG2 . VAL A 1 78  ? -21.438 11.080  17.985  1.00 22.62 ? 78  VAL A CG2 1 
ATOM   602  N  N   . LEU A 1 79  ? -19.161 8.381   18.754  1.00 18.39 ? 79  LEU A N   1 
ATOM   603  C  CA  . LEU A 1 79  ? -19.221 7.527   19.902  1.00 20.83 ? 79  LEU A CA  1 
ATOM   604  C  C   . LEU A 1 79  ? -19.223 8.448   21.113  1.00 21.25 ? 79  LEU A C   1 
ATOM   605  O  O   . LEU A 1 79  ? -18.471 9.422   21.165  1.00 20.31 ? 79  LEU A O   1 
ATOM   606  C  CB  . LEU A 1 79  ? -17.956 6.662   19.837  1.00 21.78 ? 79  LEU A CB  1 
ATOM   607  C  CG  . LEU A 1 79  ? -17.799 5.512   20.822  1.00 21.99 ? 79  LEU A CG  1 
ATOM   608  C  CD1 . LEU A 1 79  ? -18.869 4.444   20.618  1.00 22.44 ? 79  LEU A CD1 1 
ATOM   609  C  CD2 . LEU A 1 79  ? -16.425 4.899   20.643  1.00 20.72 ? 79  LEU A CD2 1 
ATOM   610  N  N   . LYS A 1 80  ? -20.143 8.194   22.031  1.00 18.99 ? 80  LYS A N   1 
ATOM   611  C  CA  . LYS A 1 80  ? -20.143 8.898   23.304  1.00 23.51 ? 80  LYS A CA  1 
ATOM   612  C  C   . LYS A 1 80  ? -20.626 7.978   24.416  1.00 23.14 ? 80  LYS A C   1 
ATOM   613  O  O   . LYS A 1 80  ? -20.951 6.817   24.190  1.00 20.77 ? 80  LYS A O   1 
ATOM   614  C  CB  . LYS A 1 80  ? -20.910 10.221  23.269  1.00 26.46 ? 80  LYS A CB  1 
ATOM   615  C  CG  . LYS A 1 80  ? -22.283 10.213  22.612  1.00 29.53 ? 80  LYS A CG  1 
ATOM   616  C  CD  . LYS A 1 80  ? -22.863 11.626  22.471  1.00 31.90 ? 80  LYS A CD  1 
ATOM   617  N  N   . GLY A 1 81  ? -20.609 8.522   25.638  1.00 23.90 ? 81  GLY A N   1 
ATOM   618  C  CA  . GLY A 1 81  ? -21.069 7.737   26.762  1.00 23.35 ? 81  GLY A CA  1 
ATOM   619  C  C   . GLY A 1 81  ? -20.066 6.631   27.101  1.00 25.28 ? 81  GLY A C   1 
ATOM   620  O  O   . GLY A 1 81  ? -18.849 6.800   26.945  1.00 23.23 ? 81  GLY A O   1 
ATOM   621  N  N   . GLY A 1 82  ? -20.609 5.488   27.556  1.00 25.50 ? 82  GLY A N   1 
ATOM   622  C  CA  . GLY A 1 82  ? -19.773 4.461   28.158  1.00 26.92 ? 82  GLY A CA  1 
ATOM   623  C  C   . GLY A 1 82  ? -18.798 5.108   29.125  1.00 24.82 ? 82  GLY A C   1 
ATOM   624  O  O   . GLY A 1 82  ? -19.219 5.916   29.951  1.00 31.42 ? 82  GLY A O   1 
ATOM   625  N  N   . PRO A 1 83  ? -17.467 4.866   29.003  1.00 24.21 ? 83  PRO A N   1 
ATOM   626  C  CA  . PRO A 1 83  ? -16.482 5.487   29.886  1.00 23.86 ? 83  PRO A CA  1 
ATOM   627  C  C   . PRO A 1 83  ? -15.984 6.842   29.385  1.00 23.97 ? 83  PRO A C   1 
ATOM   628  O  O   . PRO A 1 83  ? -15.082 7.410   29.990  1.00 27.04 ? 83  PRO A O   1 
ATOM   629  C  CB  . PRO A 1 83  ? -15.318 4.497   29.778  1.00 24.40 ? 83  PRO A CB  1 
ATOM   630  C  CG  . PRO A 1 83  ? -15.349 4.121   28.311  1.00 21.11 ? 83  PRO A CG  1 
ATOM   631  C  CD  . PRO A 1 83  ? -16.828 4.022   27.973  1.00 22.61 ? 83  PRO A CD  1 
ATOM   632  N  N   . LEU A 1 84  ? -16.566 7.357   28.284  1.00 21.95 ? 84  LEU A N   1 
ATOM   633  C  CA  . LEU A 1 84  ? -16.050 8.541   27.623  1.00 20.85 ? 84  LEU A CA  1 
ATOM   634  C  C   . LEU A 1 84  ? -16.718 9.788   28.193  1.00 23.80 ? 84  LEU A C   1 
ATOM   635  O  O   . LEU A 1 84  ? -17.881 9.740   28.576  1.00 25.42 ? 84  LEU A O   1 
ATOM   636  C  CB  . LEU A 1 84  ? -16.372 8.459   26.134  1.00 20.22 ? 84  LEU A CB  1 
ATOM   637  C  CG  . LEU A 1 84  ? -15.813 7.189   25.482  1.00 18.67 ? 84  LEU A CG  1 
ATOM   638  C  CD1 . LEU A 1 84  ? -16.230 7.144   24.019  1.00 20.94 ? 84  LEU A CD1 1 
ATOM   639  C  CD2 . LEU A 1 84  ? -14.279 7.140   25.587  1.00 19.11 ? 84  LEU A CD2 1 
ATOM   640  N  N   . ASP A 1 85  ? -15.917 10.859  28.211  1.00 29.37 ? 85  ASP A N   1 
ATOM   641  C  CA  . ASP A 1 85  ? -16.337 12.230  28.464  1.00 32.19 ? 85  ASP A CA  1 
ATOM   642  C  C   . ASP A 1 85  ? -16.285 12.937  27.121  1.00 36.91 ? 85  ASP A C   1 
ATOM   643  O  O   . ASP A 1 85  ? -15.278 12.854  26.411  1.00 40.06 ? 85  ASP A O   1 
ATOM   644  C  CB  . ASP A 1 85  ? -15.373 12.899  29.459  1.00 36.57 ? 85  ASP A CB  1 
ATOM   645  C  CG  . ASP A 1 85  ? -15.525 12.460  30.914  1.00 46.80 ? 85  ASP A CG  1 
ATOM   646  O  OD1 . ASP A 1 85  ? -16.648 12.014  31.295  1.00 51.37 ? 85  ASP A OD1 1 
ATOM   647  O  OD2 . ASP A 1 85  ? -14.519 12.568  31.679  1.00 47.25 ? 85  ASP A OD2 1 
ATOM   648  N  N   . GLY A 1 86  ? -17.378 13.596  26.746  1.00 36.68 ? 86  GLY A N   1 
ATOM   649  C  CA  . GLY A 1 86  ? -17.465 14.222  25.435  1.00 32.26 ? 86  GLY A CA  1 
ATOM   650  C  C   . GLY A 1 86  ? -17.777 13.262  24.276  1.00 33.41 ? 86  GLY A C   1 
ATOM   651  O  O   . GLY A 1 86  ? -18.306 12.160  24.451  1.00 31.91 ? 86  GLY A O   1 
ATOM   652  N  N   . THR A 1 87  ? -17.423 13.713  23.069  1.00 29.21 ? 87  THR A N   1 
ATOM   653  C  CA  . THR A 1 87  ? -17.856 13.134  21.813  1.00 23.75 ? 87  THR A CA  1 
ATOM   654  C  C   . THR A 1 87  ? -16.620 12.790  20.987  1.00 21.63 ? 87  THR A C   1 
ATOM   655  O  O   . THR A 1 87  ? -15.681 13.578  20.919  1.00 21.21 ? 87  THR A O   1 
ATOM   656  C  CB  . THR A 1 87  ? -18.621 14.198  21.029  1.00 27.98 ? 87  THR A CB  1 
ATOM   657  O  OG1 . THR A 1 87  ? -19.764 14.470  21.846  1.00 33.84 ? 87  THR A OG1 1 
ATOM   658  C  CG2 . THR A 1 87  ? -19.030 13.758  19.637  1.00 28.10 ? 87  THR A CG2 1 
ATOM   659  N  N   . TYR A 1 88  ? -16.599 11.568  20.452  1.00 19.62 ? 88  TYR A N   1 
ATOM   660  C  CA  . TYR A 1 88  ? -15.505 11.121  19.609  1.00 17.42 ? 88  TYR A CA  1 
ATOM   661  C  C   . TYR A 1 88  ? -16.037 10.829  18.210  1.00 19.13 ? 88  TYR A C   1 
ATOM   662  O  O   . TYR A 1 88  ? -17.031 10.110  18.060  1.00 19.72 ? 88  TYR A O   1 
ATOM   663  C  CB  . TYR A 1 88  ? -14.853 9.888   20.236  1.00 15.52 ? 88  TYR A CB  1 
ATOM   664  C  CG  . TYR A 1 88  ? -14.113 10.084  21.542  1.00 15.64 ? 88  TYR A CG  1 
ATOM   665  C  CD1 . TYR A 1 88  ? -14.791 10.423  22.716  1.00 17.36 ? 88  TYR A CD1 1 
ATOM   666  C  CD2 . TYR A 1 88  ? -12.743 9.876   21.613  1.00 16.54 ? 88  TYR A CD2 1 
ATOM   667  C  CE1 . TYR A 1 88  ? -14.089 10.627  23.900  1.00 17.29 ? 88  TYR A CE1 1 
ATOM   668  C  CE2 . TYR A 1 88  ? -12.034 10.042  22.796  1.00 15.76 ? 88  TYR A CE2 1 
ATOM   669  C  CZ  . TYR A 1 88  ? -12.712 10.459  23.931  1.00 17.00 ? 88  TYR A CZ  1 
ATOM   670  O  OH  . TYR A 1 88  ? -12.011 10.574  25.106  1.00 17.99 ? 88  TYR A OH  1 
ATOM   671  N  N   . ARG A 1 89  ? -15.333 11.345  17.191  1.00 16.52 ? 89  ARG A N   1 
ATOM   672  C  CA  . ARG A 1 89  ? -15.796 11.230  15.812  1.00 16.94 ? 89  ARG A CA  1 
ATOM   673  C  C   . ARG A 1 89  ? -15.099 10.033  15.157  1.00 14.36 ? 89  ARG A C   1 
ATOM   674  O  O   . ARG A 1 89  ? -13.877 9.913   15.269  1.00 13.84 ? 89  ARG A O   1 
ATOM   675  C  CB  . ARG A 1 89  ? -15.394 12.462  14.984  1.00 18.25 ? 89  ARG A CB  1 
ATOM   676  C  CG  . ARG A 1 89  ? -16.308 13.666  15.114  1.00 25.03 ? 89  ARG A CG  1 
ATOM   677  C  CD  . ARG A 1 89  ? -15.988 14.670  14.024  1.00 21.20 ? 89  ARG A CD  1 
ATOM   678  N  NE  . ARG A 1 89  ? -16.586 15.966  14.332  1.00 24.73 ? 89  ARG A NE  1 
ATOM   679  C  CZ  . ARG A 1 89  ? -16.201 17.136  13.835  1.00 28.05 ? 89  ARG A CZ  1 
ATOM   680  N  NH1 . ARG A 1 89  ? -15.214 17.190  12.966  1.00 26.31 ? 89  ARG A NH1 1 
ATOM   681  N  NH2 . ARG A 1 89  ? -16.800 18.260  14.213  1.00 30.11 ? 89  ARG A NH2 1 
ATOM   682  N  N   . LEU A 1 90  ? -15.874 9.172   14.448  1.00 15.24 ? 90  LEU A N   1 
ATOM   683  C  CA  . LEU A 1 90  ? -15.262 8.054   13.733  1.00 13.05 ? 90  LEU A CA  1 
ATOM   684  C  C   . LEU A 1 90  ? -14.453 8.613   12.558  1.00 14.79 ? 90  LEU A C   1 
ATOM   685  O  O   . LEU A 1 90  ? -14.966 9.347   11.711  1.00 16.93 ? 90  LEU A O   1 
ATOM   686  C  CB  . LEU A 1 90  ? -16.384 7.197   13.128  1.00 13.26 ? 90  LEU A CB  1 
ATOM   687  C  CG  . LEU A 1 90  ? -15.947 6.038   12.224  1.00 13.15 ? 90  LEU A CG  1 
ATOM   688  C  CD1 . LEU A 1 90  ? -15.101 5.040   12.970  1.00 15.29 ? 90  LEU A CD1 1 
ATOM   689  C  CD2 . LEU A 1 90  ? -17.167 5.340   11.594  1.00 13.88 ? 90  LEU A CD2 1 
ATOM   690  N  N   . THR A 1 91  ? -13.202 8.181   12.446  1.00 14.54 ? 91  THR A N   1 
ATOM   691  C  CA  . THR A 1 91  ? -12.364 8.612   11.328  1.00 14.91 ? 91  THR A CA  1 
ATOM   692  C  C   . THR A 1 91  ? -12.043 7.446   10.384  1.00 14.64 ? 91  THR A C   1 
ATOM   693  O  O   . THR A 1 91  ? -11.921 7.644   9.157   1.00 14.79 ? 91  THR A O   1 
ATOM   694  C  CB  . THR A 1 91  ? -11.138 9.348   11.890  1.00 16.71 ? 91  THR A CB  1 
ATOM   695  O  OG1 . THR A 1 91  ? -10.409 9.866   10.787  1.00 20.18 ? 91  THR A OG1 1 
ATOM   696  C  CG2 . THR A 1 91  ? -10.242 8.503   12.753  1.00 16.03 ? 91  THR A CG2 1 
ATOM   697  N  N   . GLN A 1 92  ? -11.895 6.218   10.915  1.00 13.83 ? 92  GLN A N   1 
ATOM   698  C  CA  . GLN A 1 92  ? -11.523 5.097   10.070  1.00 13.72 ? 92  GLN A CA  1 
ATOM   699  C  C   . GLN A 1 92  ? -11.814 3.799   10.813  1.00 12.73 ? 92  GLN A C   1 
ATOM   700  O  O   . GLN A 1 92  ? -11.918 3.777   12.054  1.00 12.51 ? 92  GLN A O   1 
ATOM   701  C  CB  . GLN A 1 92  ? -10.059 5.150   9.611   1.00 14.26 ? 92  GLN A CB  1 
ATOM   702  C  CG  . GLN A 1 92  ? -9.102  5.094   10.804  1.00 14.07 ? 92  GLN A CG  1 
ATOM   703  C  CD  . GLN A 1 92  ? -8.343  3.786   10.798  1.00 17.89 ? 92  GLN A CD  1 
ATOM   704  O  OE1 . GLN A 1 92  ? -8.914  2.732   10.983  1.00 19.21 ? 92  GLN A OE1 1 
ATOM   705  N  NE2 . GLN A 1 92  ? -7.043  3.836   10.576  1.00 25.85 ? 92  GLN A NE2 1 
ATOM   706  N  N   . PHE A 1 93  ? -11.942 2.722   10.036  1.00 13.31 ? 93  PHE A N   1 
ATOM   707  C  CA  . PHE A 1 93  ? -11.803 1.413   10.635  1.00 11.86 ? 93  PHE A CA  1 
ATOM   708  C  C   . PHE A 1 93  ? -10.796 0.591   9.845   1.00 13.52 ? 93  PHE A C   1 
ATOM   709  O  O   . PHE A 1 93  ? -10.531 0.836   8.654   1.00 12.25 ? 93  PHE A O   1 
ATOM   710  C  CB  . PHE A 1 93  ? -13.139 0.700   10.837  1.00 11.75 ? 93  PHE A CB  1 
ATOM   711  C  CG  . PHE A 1 93  ? -13.856 0.301   9.582   1.00 11.64 ? 93  PHE A CG  1 
ATOM   712  C  CD1 . PHE A 1 93  ? -13.465 -0.837  8.869   1.00 13.41 ? 93  PHE A CD1 1 
ATOM   713  C  CD2 . PHE A 1 93  ? -15.036 0.924   9.242   1.00 11.19 ? 93  PHE A CD2 1 
ATOM   714  C  CE1 . PHE A 1 93  ? -14.156 -1.259  7.739   1.00 13.83 ? 93  PHE A CE1 1 
ATOM   715  C  CE2 . PHE A 1 93  ? -15.719 0.500   8.107   1.00 12.23 ? 93  PHE A CE2 1 
ATOM   716  C  CZ  . PHE A 1 93  ? -15.295 -0.580  7.365   1.00 13.96 ? 93  PHE A CZ  1 
ATOM   717  N  N   . HIS A 1 94  ? -10.264 -0.421  10.527  1.00 12.45 ? 94  HIS A N   1 
ATOM   718  C  CA  . HIS A 1 94  ? -9.318  -1.337  9.917   1.00 11.71 ? 94  HIS A CA  1 
ATOM   719  C  C   . HIS A 1 94  ? -9.429  -2.656  10.659  1.00 12.71 ? 94  HIS A C   1 
ATOM   720  O  O   . HIS A 1 94  ? -10.122 -2.758  11.685  1.00 12.28 ? 94  HIS A O   1 
ATOM   721  C  CB  . HIS A 1 94  ? -7.891  -0.736  9.901   1.00 10.76 ? 94  HIS A CB  1 
ATOM   722  C  CG  . HIS A 1 94  ? -7.425  -0.615  11.318  1.00 10.78 ? 94  HIS A CG  1 
ATOM   723  N  ND1 . HIS A 1 94  ? -7.577  0.573   12.036  1.00 12.93 ? 94  HIS A ND1 1 
ATOM   724  C  CD2 . HIS A 1 94  ? -6.765  -1.515  12.046  1.00 16.01 ? 94  HIS A CD2 1 
ATOM   725  C  CE1 . HIS A 1 94  ? -7.068  0.324   13.273  1.00 11.39 ? 94  HIS A CE1 1 
ATOM   726  N  NE2 . HIS A 1 94  ? -6.665  -1.029  13.306  1.00 11.45 ? 94  HIS A NE2 1 
ATOM   727  N  N   . PHE A 1 95  ? -8.671  -3.660  10.201  1.00 11.75 ? 95  PHE A N   1 
ATOM   728  C  CA  . PHE A 1 95  ? -8.705  -4.964  10.847  1.00 13.31 ? 95  PHE A CA  1 
ATOM   729  C  C   . PHE A 1 95  ? -7.286  -5.480  11.105  1.00 11.53 ? 95  PHE A C   1 
ATOM   730  O  O   . PHE A 1 95  ? -6.309  -4.995  10.507  1.00 12.62 ? 95  PHE A O   1 
ATOM   731  C  CB  . PHE A 1 95  ? -9.428  -6.032  10.022  1.00 13.29 ? 95  PHE A CB  1 
ATOM   732  C  CG  . PHE A 1 95  ? -10.874 -5.745  9.693   1.00 14.65 ? 95  PHE A CG  1 
ATOM   733  C  CD1 . PHE A 1 95  ? -11.222 -4.898  8.645   1.00 13.90 ? 95  PHE A CD1 1 
ATOM   734  C  CD2 . PHE A 1 95  ? -11.876 -6.418  10.381  1.00 15.11 ? 95  PHE A CD2 1 
ATOM   735  C  CE1 . PHE A 1 95  ? -12.578 -4.698  8.344   1.00 14.14 ? 95  PHE A CE1 1 
ATOM   736  C  CE2 . PHE A 1 95  ? -13.222 -6.213  10.074  1.00 15.60 ? 95  PHE A CE2 1 
ATOM   737  C  CZ  . PHE A 1 95  ? -13.568 -5.355  9.052   1.00 14.60 ? 95  PHE A CZ  1 
ATOM   738  N  N   . HIS A 1 96  ? -7.211  -6.472  12.007  1.00 12.69 ? 96  HIS A N   1 
ATOM   739  C  CA  . HIS A 1 96  ? -6.026  -7.275  12.201  1.00 11.07 ? 96  HIS A CA  1 
ATOM   740  C  C   . HIS A 1 96  ? -6.460  -8.723  12.055  1.00 11.10 ? 96  HIS A C   1 
ATOM   741  O  O   . HIS A 1 96  ? -7.534  -9.089  12.541  1.00 12.51 ? 96  HIS A O   1 
ATOM   742  C  CB  . HIS A 1 96  ? -5.438  -7.044  13.623  1.00 10.85 ? 96  HIS A CB  1 
ATOM   743  C  CG  . HIS A 1 96  ? -5.125  -5.613  13.904  1.00 11.11 ? 96  HIS A CG  1 
ATOM   744  N  ND1 . HIS A 1 96  ? -3.899  -5.026  13.609  1.00 12.35 ? 96  HIS A ND1 1 
ATOM   745  C  CD2 . HIS A 1 96  ? -5.930  -4.633  14.357  1.00 12.66 ? 96  HIS A CD2 1 
ATOM   746  C  CE1 . HIS A 1 96  ? -3.969  -3.715  13.914  1.00 12.16 ? 96  HIS A CE1 1 
ATOM   747  N  NE2 . HIS A 1 96  ? -5.177  -3.458  14.420  1.00 12.09 ? 96  HIS A NE2 1 
ATOM   748  N  N   . TRP A 1 97  ? -5.638  -9.572  11.415  1.00 11.32 ? 97  TRP A N   1 
ATOM   749  C  CA  . TRP A 1 97  ? -6.091  -10.945 11.237  1.00 12.21 ? 97  TRP A CA  1 
ATOM   750  C  C   . TRP A 1 97  ? -4.891  -11.874 11.153  1.00 13.29 ? 97  TRP A C   1 
ATOM   751  O  O   . TRP A 1 97  ? -3.720  -11.452 11.083  1.00 15.70 ? 97  TRP A O   1 
ATOM   752  C  CB  . TRP A 1 97  ? -7.006  -11.093 9.993   1.00 13.35 ? 97  TRP A CB  1 
ATOM   753  C  CG  . TRP A 1 97  ? -6.356  -10.719 8.709   1.00 12.82 ? 97  TRP A CG  1 
ATOM   754  C  CD1 . TRP A 1 97  ? -5.643  -11.559 7.878   1.00 14.47 ? 97  TRP A CD1 1 
ATOM   755  C  CD2 . TRP A 1 97  ? -6.245  -9.394  8.157   1.00 12.88 ? 97  TRP A CD2 1 
ATOM   756  N  NE1 . TRP A 1 97  ? -5.168  -10.851 6.824   1.00 14.32 ? 97  TRP A NE1 1 
ATOM   757  C  CE2 . TRP A 1 97  ? -5.550  -9.522  6.936   1.00 13.33 ? 97  TRP A CE2 1 
ATOM   758  C  CE3 . TRP A 1 97  ? -6.777  -8.133  8.496   1.00 12.82 ? 97  TRP A CE3 1 
ATOM   759  C  CZ2 . TRP A 1 97  ? -5.289  -8.444  6.109   1.00 14.51 ? 97  TRP A CZ2 1 
ATOM   760  C  CZ3 . TRP A 1 97  ? -6.509  -7.035  7.688   1.00 14.35 ? 97  TRP A CZ3 1 
ATOM   761  C  CH2 . TRP A 1 97  ? -5.797  -7.199  6.477   1.00 14.26 ? 97  TRP A CH2 1 
ATOM   762  N  N   . GLY A 1 98  ? -5.224  -13.155 11.139  1.00 13.55 ? 98  GLY A N   1 
ATOM   763  C  CA  . GLY A 1 98  ? -4.252  -14.226 11.222  1.00 15.74 ? 98  GLY A CA  1 
ATOM   764  C  C   . GLY A 1 98  ? -4.011  -14.962 9.910   1.00 15.62 ? 98  GLY A C   1 
ATOM   765  O  O   . GLY A 1 98  ? -4.715  -14.785 8.916   1.00 17.02 ? 98  GLY A O   1 
ATOM   766  N  N   . SER A 1 99  ? -3.005  -15.838 9.959   1.00 17.50 ? 99  SER A N   1 
ATOM   767  C  CA  . SER A 1 99  ? -2.697  -16.714 8.844   1.00 18.86 ? 99  SER A CA  1 
ATOM   768  C  C   . SER A 1 99  ? -3.591  -17.945 8.925   1.00 20.25 ? 99  SER A C   1 
ATOM   769  O  O   . SER A 1 99  ? -3.684  -18.693 7.946   1.00 23.09 ? 99  SER A O   1 
ATOM   770  C  CB  . SER A 1 99  ? -1.245  -17.141 8.883   1.00 17.25 ? 99  SER A CB  1 
ATOM   771  O  OG  . SER A 1 99  ? -0.846  -17.556 10.192  1.00 18.71 ? 99  SER A OG  1 
ATOM   772  N  N   . LEU A 1 100 ? -4.150  -18.198 10.105  1.00 19.69 ? 100 LEU A N   1 
ATOM   773  C  CA  . LEU A 1 100 ? -5.096  -19.289 10.279  1.00 23.27 ? 100 LEU A CA  1 
ATOM   774  C  C   . LEU A 1 100 ? -6.119  -18.861 11.335  1.00 24.76 ? 100 LEU A C   1 
ATOM   775  O  O   . LEU A 1 100 ? -5.919  -17.834 11.979  1.00 21.24 ? 100 LEU A O   1 
ATOM   776  C  CB  . LEU A 1 100 ? -4.346  -20.570 10.667  1.00 28.90 ? 100 LEU A CB  1 
ATOM   777  C  CG  . LEU A 1 100 ? -3.378  -20.414 11.841  1.00 33.44 ? 100 LEU A CG  1 
ATOM   778  C  CD1 . LEU A 1 100 ? -3.416  -21.625 12.759  1.00 44.22 ? 100 LEU A CD1 1 
ATOM   779  C  CD2 . LEU A 1 100 ? -1.957  -20.180 11.356  1.00 38.95 ? 100 LEU A CD2 1 
ATOM   780  N  N   . ASP A 1 101 ? -7.216  -19.626 11.489  1.00 22.70 ? 101 ASP A N   1 
ATOM   781  C  CA  . ASP A 1 101 ? -8.376  -19.077 12.184  1.00 21.24 ? 101 ASP A CA  1 
ATOM   782  C  C   . ASP A 1 101 ? -8.117  -18.999 13.686  1.00 22.46 ? 101 ASP A C   1 
ATOM   783  O  O   . ASP A 1 101 ? -8.814  -18.252 14.388  1.00 23.32 ? 101 ASP A O   1 
ATOM   784  C  CB  . ASP A 1 101 ? -9.655  -19.888 11.933  1.00 21.15 ? 101 ASP A CB  1 
ATOM   785  C  CG  . ASP A 1 101 ? -10.160 -19.938 10.495  1.00 23.92 ? 101 ASP A CG  1 
ATOM   786  O  OD1 . ASP A 1 101 ? -9.720  -19.146 9.642   1.00 23.15 ? 101 ASP A OD1 1 
ATOM   787  O  OD2 . ASP A 1 101 ? -11.080 -20.741 10.255  1.00 28.57 ? 101 ASP A OD2 1 
ATOM   788  N  N   . GLY A 1 102 ? -7.102  -19.724 14.185  1.00 18.98 ? 102 GLY A N   1 
ATOM   789  C  CA  . GLY A 1 102 ? -6.859  -19.743 15.624  1.00 20.91 ? 102 GLY A CA  1 
ATOM   790  C  C   . GLY A 1 102 ? -6.005  -18.593 16.154  1.00 18.74 ? 102 GLY A C   1 
ATOM   791  O  O   . GLY A 1 102 ? -5.687  -18.558 17.353  1.00 22.63 ? 102 GLY A O   1 
ATOM   792  N  N   . GLN A 1 103 ? -5.688  -17.612 15.304  1.00 19.26 ? 103 GLN A N   1 
ATOM   793  C  CA  . GLN A 1 103 ? -5.017  -16.395 15.770  1.00 17.91 ? 103 GLN A CA  1 
ATOM   794  C  C   . GLN A 1 103 ? -5.375  -15.241 14.832  1.00 16.34 ? 103 GLN A C   1 
ATOM   795  O  O   . GLN A 1 103 ? -5.920  -15.460 13.748  1.00 16.89 ? 103 GLN A O   1 
ATOM   796  C  CB  . GLN A 1 103 ? -3.509  -16.664 15.795  1.00 17.93 ? 103 GLN A CB  1 
ATOM   797  C  CG  . GLN A 1 103 ? -2.952  -16.849 14.372  1.00 16.57 ? 103 GLN A CG  1 
ATOM   798  C  CD  . GLN A 1 103 ? -1.542  -17.411 14.376  1.00 21.53 ? 103 GLN A CD  1 
ATOM   799  O  OE1 . GLN A 1 103 ? -0.658  -16.975 13.638  1.00 21.35 ? 103 GLN A OE1 1 
ATOM   800  N  NE2 . GLN A 1 103 ? -1.326  -18.429 15.189  1.00 23.41 ? 103 GLN A NE2 1 
ATOM   801  N  N   . GLY A 1 104 ? -5.038  -14.006 15.220  1.00 15.27 ? 104 GLY A N   1 
ATOM   802  C  CA  . GLY A 1 104 ? -5.347  -12.844 14.404  1.00 14.18 ? 104 GLY A CA  1 
ATOM   803  C  C   . GLY A 1 104 ? -5.839  -11.657 15.226  1.00 13.69 ? 104 GLY A C   1 
ATOM   804  O  O   . GLY A 1 104 ? -5.606  -10.471 14.888  1.00 13.51 ? 104 GLY A O   1 
ATOM   805  N  N   . SER A 1 105 ? -6.492  -11.948 16.355  1.00 13.01 ? 105 SER A N   1 
ATOM   806  C  CA  . SER A 1 105 ? -6.881  -10.819 17.190  1.00 14.65 ? 105 SER A CA  1 
ATOM   807  C  C   . SER A 1 105 ? -5.696  -10.288 18.003  1.00 13.98 ? 105 SER A C   1 
ATOM   808  O  O   . SER A 1 105 ? -4.700  -10.950 18.262  1.00 14.37 ? 105 SER A O   1 
ATOM   809  C  CB  . SER A 1 105 ? -8.059  -11.148 18.111  1.00 14.26 ? 105 SER A CB  1 
ATOM   810  O  OG  . SER A 1 105 ? -7.662  -12.019 19.167  1.00 16.86 ? 105 SER A OG  1 
ATOM   811  N  N   . GLU A 1 106 ? -5.831  -9.034  18.395  1.00 13.17 ? 106 GLU A N   1 
ATOM   812  C  CA  . GLU A 1 106 ? -4.792  -8.407  19.228  1.00 12.80 ? 106 GLU A CA  1 
ATOM   813  C  C   . GLU A 1 106 ? -5.162  -8.557  20.697  1.00 14.15 ? 106 GLU A C   1 
ATOM   814  O  O   . GLU A 1 106 ? -4.372  -9.071  21.501  1.00 14.19 ? 106 GLU A O   1 
ATOM   815  C  CB  . GLU A 1 106 ? -4.744  -6.923  18.877  1.00 13.61 ? 106 GLU A CB  1 
ATOM   816  C  CG  . GLU A 1 106 ? -4.338  -6.692  17.418  1.00 14.31 ? 106 GLU A CG  1 
ATOM   817  C  CD  . GLU A 1 106 ? -3.639  -5.388  17.072  1.00 14.96 ? 106 GLU A CD  1 
ATOM   818  O  OE1 . GLU A 1 106 ? -4.199  -4.335  17.368  1.00 14.86 ? 106 GLU A OE1 1 
ATOM   819  O  OE2 . GLU A 1 106 ? -2.520  -5.438  16.542  1.00 16.42 ? 106 GLU A OE2 1 
ATOM   820  N  N   . HIS A 1 107 ? -6.356  -8.092  21.080  1.00 14.22 ? 107 HIS A N   1 
ATOM   821  C  CA  . HIS A 1 107 ? -6.777  -8.396  22.443  1.00 12.69 ? 107 HIS A CA  1 
ATOM   822  C  C   . HIS A 1 107 ? -7.065  -9.887  22.487  1.00 14.67 ? 107 HIS A C   1 
ATOM   823  O  O   . HIS A 1 107 ? -7.411  -10.462 21.454  1.00 13.43 ? 107 HIS A O   1 
ATOM   824  C  CB  . HIS A 1 107 ? -8.047  -7.642  22.823  1.00 12.34 ? 107 HIS A CB  1 
ATOM   825  C  CG  . HIS A 1 107 ? -7.742  -6.189  22.990  1.00 13.41 ? 107 HIS A CG  1 
ATOM   826  N  ND1 . HIS A 1 107 ? -7.793  -5.288  21.956  1.00 15.51 ? 107 HIS A ND1 1 
ATOM   827  C  CD2 . HIS A 1 107 ? -7.271  -5.530  24.067  1.00 13.76 ? 107 HIS A CD2 1 
ATOM   828  C  CE1 . HIS A 1 107 ? -7.395  -4.094  22.398  1.00 14.57 ? 107 HIS A CE1 1 
ATOM   829  N  NE2 . HIS A 1 107 ? -7.069  -4.206  23.719  1.00 13.54 ? 107 HIS A NE2 1 
ATOM   830  N  N   . THR A 1 108 ? -6.934  -10.455 23.676  1.00 14.95 ? 108 THR A N   1 
ATOM   831  C  CA  . THR A 1 108 ? -7.339  -11.845 23.886  1.00 14.61 ? 108 THR A CA  1 
ATOM   832  C  C   . THR A 1 108 ? -8.311  -11.881 25.071  1.00 14.15 ? 108 THR A C   1 
ATOM   833  O  O   . THR A 1 108 ? -8.365  -10.968 25.884  1.00 15.88 ? 108 THR A O   1 
ATOM   834  C  CB  . THR A 1 108 ? -6.132  -12.780 24.053  1.00 16.95 ? 108 THR A CB  1 
ATOM   835  O  OG1 . THR A 1 108 ? -5.294  -12.388 25.144  1.00 18.03 ? 108 THR A OG1 1 
ATOM   836  C  CG2 . THR A 1 108 ? -5.288  -12.871 22.801  1.00 15.66 ? 108 THR A CG2 1 
ATOM   837  N  N   . VAL A 1 109 ? -9.059  -12.986 25.193  1.00 15.26 ? 109 VAL A N   1 
ATOM   838  C  CA  . VAL A 1 109 ? -10.025 -13.028 26.280  1.00 16.60 ? 109 VAL A CA  1 
ATOM   839  C  C   . VAL A 1 109 ? -9.730  -14.311 27.054  1.00 16.58 ? 109 VAL A C   1 
ATOM   840  O  O   . VAL A 1 109 ? -9.912  -15.397 26.537  1.00 18.75 ? 109 VAL A O   1 
ATOM   841  C  CB  . VAL A 1 109 ? -11.456 -13.027 25.696  1.00 17.15 ? 109 VAL A CB  1 
ATOM   842  C  CG1 . VAL A 1 109 ? -12.478 -13.087 26.823  1.00 18.29 ? 109 VAL A CG1 1 
ATOM   843  C  CG2 . VAL A 1 109 ? -11.729 -11.788 24.841  1.00 16.83 ? 109 VAL A CG2 1 
ATOM   844  N  N   . ASP A 1 110 ? -9.269  -14.201 28.294  1.00 17.45 ? 110 ASP A N   1 
ATOM   845  C  CA  . ASP A 1 110 ? -8.880  -15.437 28.973  1.00 20.39 ? 110 ASP A CA  1 
ATOM   846  C  C   . ASP A 1 110 ? -7.918  -16.247 28.108  1.00 18.47 ? 110 ASP A C   1 
ATOM   847  O  O   . ASP A 1 110 ? -8.001  -17.488 28.088  1.00 20.83 ? 110 ASP A O   1 
ATOM   848  C  CB  . ASP A 1 110 ? -10.104 -16.256 29.414  1.00 20.54 ? 110 ASP A CB  1 
ATOM   849  C  CG  . ASP A 1 110 ? -10.973 -15.508 30.428  1.00 20.21 ? 110 ASP A CG  1 
ATOM   850  O  OD1 . ASP A 1 110 ? -10.418 -14.725 31.170  1.00 22.89 ? 110 ASP A OD1 1 
ATOM   851  O  OD2 . ASP A 1 110 ? -12.216 -15.723 30.438  1.00 26.67 ? 110 ASP A OD2 1 
ATOM   852  N  N   . LYS A 1 111 ? -6.981  -15.549 27.441  1.00 17.71 ? 111 LYS A N   1 
ATOM   853  C  CA  . LYS A 1 111 ? -5.931  -16.098 26.580  1.00 18.90 ? 111 LYS A CA  1 
ATOM   854  C  C   . LYS A 1 111 ? -6.435  -16.599 25.227  1.00 17.30 ? 111 LYS A C   1 
ATOM   855  O  O   . LYS A 1 111 ? -5.617  -16.965 24.382  1.00 19.48 ? 111 LYS A O   1 
ATOM   856  C  CB  . LYS A 1 111 ? -5.141  -17.242 27.200  1.00 20.21 ? 111 LYS A CB  1 
ATOM   857  C  CG  . LYS A 1 111 ? -4.437  -16.892 28.491  1.00 26.54 ? 111 LYS A CG  1 
ATOM   858  C  CD  . LYS A 1 111 ? -3.472  -15.796 28.256  1.00 28.42 ? 111 LYS A CD  1 
ATOM   859  C  CE  . LYS A 1 111 ? -2.800  -15.404 29.552  1.00 37.32 ? 111 LYS A CE  1 
ATOM   860  N  NZ  . LYS A 1 111 ? -1.426  -14.942 29.283  1.00 38.48 ? 111 LYS A NZ  1 
ATOM   861  N  N   . LYS A 1 112 ? -7.755  -16.542 24.997  1.00 17.21 ? 112 LYS A N   1 
ATOM   862  C  CA  . LYS A 1 112 ? -8.329  -16.947 23.718  1.00 17.92 ? 112 LYS A CA  1 
ATOM   863  C  C   . LYS A 1 112 ? -8.054  -15.899 22.629  1.00 18.78 ? 112 LYS A C   1 
ATOM   864  O  O   . LYS A 1 112 ? -8.337  -14.707 22.817  1.00 17.64 ? 112 LYS A O   1 
ATOM   865  C  CB  . LYS A 1 112 ? -9.828  -17.214 23.839  1.00 19.40 ? 112 LYS A CB  1 
ATOM   866  C  CG  . LYS A 1 112 ? -10.515 -17.377 22.495  1.00 21.07 ? 112 LYS A CG  1 
ATOM   867  C  CD  . LYS A 1 112 ? -12.010 -17.692 22.552  1.00 26.40 ? 112 LYS A CD  1 
ATOM   868  C  CE  . LYS A 1 112 ? -12.475 -18.103 21.160  1.00 26.64 ? 112 LYS A CE  1 
ATOM   869  N  NZ  . LYS A 1 112 ? -13.938 -18.328 21.093  1.00 37.29 ? 112 LYS A NZ  1 
ATOM   870  N  N   . LYS A 1 113 ? -7.553  -16.359 21.475  1.00 17.64 ? 113 LYS A N   1 
ATOM   871  C  CA  . LYS A 1 113 ? -7.304  -15.511 20.316  1.00 16.38 ? 113 LYS A CA  1 
ATOM   872  C  C   . LYS A 1 113 ? -8.461  -15.740 19.362  1.00 16.67 ? 113 LYS A C   1 
ATOM   873  O  O   . LYS A 1 113 ? -8.843  -16.898 19.133  1.00 18.98 ? 113 LYS A O   1 
ATOM   874  C  CB  . LYS A 1 113 ? -6.002  -15.830 19.582  1.00 16.30 ? 113 LYS A CB  1 
ATOM   875  C  CG  . LYS A 1 113 ? -4.752  -15.585 20.438  1.00 18.20 ? 113 LYS A CG  1 
ATOM   876  C  CD  . LYS A 1 113 ? -3.549  -16.250 19.783  1.00 19.58 ? 113 LYS A CD  1 
ATOM   877  C  CE  . LYS A 1 113 ? -2.215  -15.670 20.182  1.00 24.15 ? 113 LYS A CE  1 
ATOM   878  N  NZ  . LYS A 1 113 ? -1.674  -16.375 21.356  1.00 29.19 ? 113 LYS A NZ  1 
ATOM   879  N  N   . TYR A 1 114 ? -8.994  -14.644 18.821  1.00 14.78 ? 114 TYR A N   1 
ATOM   880  C  CA  . TYR A 1 114 ? -9.971  -14.709 17.742  1.00 14.18 ? 114 TYR A CA  1 
ATOM   881  C  C   . TYR A 1 114 ? -9.287  -14.704 16.386  1.00 13.60 ? 114 TYR A C   1 
ATOM   882  O  O   . TYR A 1 114 ? -8.118  -14.408 16.295  1.00 14.26 ? 114 TYR A O   1 
ATOM   883  C  CB  . TYR A 1 114 ? -11.015 -13.609 17.913  1.00 14.61 ? 114 TYR A CB  1 
ATOM   884  C  CG  . TYR A 1 114 ? -11.962 -13.888 19.049  1.00 15.83 ? 114 TYR A CG  1 
ATOM   885  C  CD1 . TYR A 1 114 ? -11.649 -13.521 20.345  1.00 18.66 ? 114 TYR A CD1 1 
ATOM   886  C  CD2 . TYR A 1 114 ? -13.170 -14.536 18.819  1.00 18.76 ? 114 TYR A CD2 1 
ATOM   887  C  CE1 . TYR A 1 114 ? -12.503 -13.793 21.403  1.00 22.23 ? 114 TYR A CE1 1 
ATOM   888  C  CE2 . TYR A 1 114 ? -14.055 -14.783 19.864  1.00 19.99 ? 114 TYR A CE2 1 
ATOM   889  C  CZ  . TYR A 1 114 ? -13.708 -14.418 21.155  1.00 20.39 ? 114 TYR A CZ  1 
ATOM   890  O  OH  . TYR A 1 114 ? -14.548 -14.651 22.212  1.00 28.52 ? 114 TYR A OH  1 
ATOM   891  N  N   . ALA A 1 115 ? -10.034 -14.947 15.301  1.00 13.64 ? 115 ALA A N   1 
ATOM   892  C  CA  . ALA A 1 115 ? -9.471  -14.999 13.965  1.00 14.96 ? 115 ALA A CA  1 
ATOM   893  C  C   . ALA A 1 115 ? -9.100  -13.606 13.478  1.00 13.46 ? 115 ALA A C   1 
ATOM   894  O  O   . ALA A 1 115 ? -8.290  -13.449 12.554  1.00 16.07 ? 115 ALA A O   1 
ATOM   895  C  CB  . ALA A 1 115 ? -10.493 -15.601 13.022  1.00 16.00 ? 115 ALA A CB  1 
ATOM   896  N  N   . ALA A 1 116 ? -9.813  -12.615 14.028  1.00 13.51 ? 116 ALA A N   1 
ATOM   897  C  CA  . ALA A 1 116 ? -9.522  -11.255 13.617  1.00 12.43 ? 116 ALA A CA  1 
ATOM   898  C  C   . ALA A 1 116 ? -10.085 -10.263 14.629  1.00 11.98 ? 116 ALA A C   1 
ATOM   899  O  O   . ALA A 1 116 ? -10.817 -10.623 15.541  1.00 12.04 ? 116 ALA A O   1 
ATOM   900  C  CB  . ALA A 1 116 ? -10.117 -10.987 12.237  1.00 11.67 ? 116 ALA A CB  1 
ATOM   901  N  N   . GLU A 1 117 ? -9.712  -8.978  14.465  1.00 12.49 ? 117 GLU A N   1 
ATOM   902  C  CA  . GLU A 1 117 ? -10.294 -7.946  15.312  1.00 12.44 ? 117 GLU A CA  1 
ATOM   903  C  C   . GLU A 1 117 ? -10.482 -6.711  14.447  1.00 12.95 ? 117 GLU A C   1 
ATOM   904  O  O   . GLU A 1 117 ? -9.595  -6.369  13.666  1.00 13.22 ? 117 GLU A O   1 
ATOM   905  C  CB  . GLU A 1 117 ? -9.326  -7.714  16.496  1.00 13.82 ? 117 GLU A CB  1 
ATOM   906  C  CG  . GLU A 1 117 ? -9.859  -6.772  17.603  1.00 14.33 ? 117 GLU A CG  1 
ATOM   907  C  CD  . GLU A 1 117 ? -8.941  -6.723  18.827  1.00 15.35 ? 117 GLU A CD  1 
ATOM   908  O  OE1 . GLU A 1 117 ? -8.269  -7.737  19.130  1.00 14.94 ? 117 GLU A OE1 1 
ATOM   909  O  OE2 . GLU A 1 117 ? -8.916  -5.662  19.450  1.00 17.14 ? 117 GLU A OE2 1 
ATOM   910  N  N   . LEU A 1 118 ? -11.662 -6.101  14.560  1.00 12.42 ? 118 LEU A N   1 
ATOM   911  C  CA  . LEU A 1 118 ? -12.048 -4.858  13.897  1.00 12.29 ? 118 LEU A CA  1 
ATOM   912  C  C   . LEU A 1 118 ? -11.846 -3.718  14.894  1.00 12.96 ? 118 LEU A C   1 
ATOM   913  O  O   . LEU A 1 118 ? -12.231 -3.830  16.052  1.00 12.55 ? 118 LEU A O   1 
ATOM   914  C  CB  . LEU A 1 118 ? -13.529 -5.002  13.509  1.00 12.37 ? 118 LEU A CB  1 
ATOM   915  C  CG  . LEU A 1 118 ? -14.272 -3.685  13.253  1.00 11.71 ? 118 LEU A CG  1 
ATOM   916  C  CD1 . LEU A 1 118 ? -13.693 -3.048  11.971  1.00 13.62 ? 118 LEU A CD1 1 
ATOM   917  C  CD2 . LEU A 1 118 ? -15.738 -4.038  12.930  1.00 13.09 ? 118 LEU A CD2 1 
ATOM   918  N  N   . HIS A 1 119 ? -11.157 -2.664  14.441  1.00 13.42 ? 119 HIS A N   1 
ATOM   919  C  CA  . HIS A 1 119 ? -10.932 -1.447  15.196  1.00 12.72 ? 119 HIS A CA  1 
ATOM   920  C  C   . HIS A 1 119 ? -11.610 -0.266  14.510  1.00 12.01 ? 119 HIS A C   1 
ATOM   921  O  O   . HIS A 1 119 ? -11.240 0.068   13.381  1.00 12.43 ? 119 HIS A O   1 
ATOM   922  C  CB  . HIS A 1 119 ? -9.438  -1.175  15.337  1.00 13.52 ? 119 HIS A CB  1 
ATOM   923  C  CG  . HIS A 1 119 ? -8.798  -2.173  16.249  1.00 13.25 ? 119 HIS A CG  1 
ATOM   924  N  ND1 . HIS A 1 119 ? -7.423  -2.424  16.254  1.00 13.39 ? 119 HIS A ND1 1 
ATOM   925  C  CD2 . HIS A 1 119 ? -9.342  -3.019  17.159  1.00 12.91 ? 119 HIS A CD2 1 
ATOM   926  C  CE1 . HIS A 1 119 ? -7.179  -3.345  17.168  1.00 13.02 ? 119 HIS A CE1 1 
ATOM   927  N  NE2 . HIS A 1 119 ? -8.304  -3.696  17.751  1.00 13.48 ? 119 HIS A NE2 1 
ATOM   928  N  N   . LEU A 1 120 ? -12.588 0.319   15.203  1.00 12.76 ? 120 LEU A N   1 
ATOM   929  C  CA  . LEU A 1 120 ? -13.192 1.573   14.756  1.00 13.82 ? 120 LEU A CA  1 
ATOM   930  C  C   . LEU A 1 120 ? -12.578 2.697   15.572  1.00 13.15 ? 120 LEU A C   1 
ATOM   931  O  O   . LEU A 1 120 ? -12.754 2.758   16.783  1.00 12.47 ? 120 LEU A O   1 
ATOM   932  C  CB  . LEU A 1 120 ? -14.707 1.520   14.949  1.00 13.74 ? 120 LEU A CB  1 
ATOM   933  C  CG  . LEU A 1 120 ? -15.387 0.444   14.113  1.00 15.25 ? 120 LEU A CG  1 
ATOM   934  C  CD1 . LEU A 1 120 ? -16.206 -0.461  15.005  1.00 17.05 ? 120 LEU A CD1 1 
ATOM   935  C  CD2 . LEU A 1 120 ? -16.276 1.127   13.051  1.00 16.54 ? 120 LEU A CD2 1 
ATOM   936  N  N   . VAL A 1 121 ? -11.828 3.548   14.891  1.00 12.23 ? 121 VAL A N   1 
ATOM   937  C  CA  . VAL A 1 121 ? -10.965 4.546   15.543  1.00 11.82 ? 121 VAL A CA  1 
ATOM   938  C  C   . VAL A 1 121 ? -11.679 5.896   15.545  1.00 13.31 ? 121 VAL A C   1 
ATOM   939  O  O   . VAL A 1 121 ? -12.104 6.359   14.484  1.00 12.84 ? 121 VAL A O   1 
ATOM   940  C  CB  . VAL A 1 121 ? -9.621  4.678   14.794  1.00 11.93 ? 121 VAL A CB  1 
ATOM   941  C  CG1 . VAL A 1 121 ? -8.691  5.631   15.528  1.00 15.55 ? 121 VAL A CG1 1 
ATOM   942  C  CG2 . VAL A 1 121 ? -8.967  3.331   14.648  1.00 13.58 ? 121 VAL A CG2 1 
ATOM   943  N  N   . HIS A 1 122 ? -11.795 6.511   16.729  1.00 11.20 ? 122 HIS A N   1 
ATOM   944  C  CA  . HIS A 1 122 ? -12.501 7.784   16.891  1.00 11.92 ? 122 HIS A CA  1 
ATOM   945  C  C   . HIS A 1 122 ? -11.615 8.783   17.621  1.00 14.17 ? 122 HIS A C   1 
ATOM   946  O  O   . HIS A 1 122 ? -10.819 8.389   18.477  1.00 13.37 ? 122 HIS A O   1 
ATOM   947  C  CB  . HIS A 1 122 ? -13.763 7.592   17.749  1.00 12.99 ? 122 HIS A CB  1 
ATOM   948  C  CG  . HIS A 1 122 ? -14.675 6.491   17.356  1.00 12.58 ? 122 HIS A CG  1 
ATOM   949  N  ND1 . HIS A 1 122 ? -14.352 5.135   17.555  1.00 13.62 ? 122 HIS A ND1 1 
ATOM   950  C  CD2 . HIS A 1 122 ? -15.912 6.510   16.775  1.00 13.48 ? 122 HIS A CD2 1 
ATOM   951  C  CE1 . HIS A 1 122 ? -15.354 4.398   17.120  1.00 13.46 ? 122 HIS A CE1 1 
ATOM   952  N  NE2 . HIS A 1 122 ? -16.317 5.197   16.643  1.00 12.79 ? 122 HIS A NE2 1 
ATOM   953  N  N   . TRP A 1 123 ? -11.773 10.088  17.335  1.00 13.35 ? 123 TRP A N   1 
ATOM   954  C  CA  . TRP A 1 123 ? -10.983 11.092  18.036  1.00 14.65 ? 123 TRP A CA  1 
ATOM   955  C  C   . TRP A 1 123 ? -11.901 12.055  18.783  1.00 16.57 ? 123 TRP A C   1 
ATOM   956  O  O   . TRP A 1 123 ? -13.001 12.381  18.324  1.00 15.62 ? 123 TRP A O   1 
ATOM   957  C  CB  . TRP A 1 123 ? -10.021 11.862  17.108  1.00 14.57 ? 123 TRP A CB  1 
ATOM   958  C  CG  . TRP A 1 123 ? -10.664 12.409  15.867  1.00 14.42 ? 123 TRP A CG  1 
ATOM   959  C  CD1 . TRP A 1 123 ? -10.793 11.787  14.655  1.00 16.92 ? 123 TRP A CD1 1 
ATOM   960  C  CD2 . TRP A 1 123 ? -11.130 13.759  15.690  1.00 15.49 ? 123 TRP A CD2 1 
ATOM   961  N  NE1 . TRP A 1 123 ? -11.392 12.625  13.766  1.00 17.90 ? 123 TRP A NE1 1 
ATOM   962  C  CE2 . TRP A 1 123 ? -11.614 13.844  14.360  1.00 15.72 ? 123 TRP A CE2 1 
ATOM   963  C  CE3 . TRP A 1 123 ? -11.251 14.878  16.521  1.00 16.93 ? 123 TRP A CE3 1 
ATOM   964  C  CZ2 . TRP A 1 123 ? -12.154 15.020  13.855  1.00 19.49 ? 123 TRP A CZ2 1 
ATOM   965  C  CZ3 . TRP A 1 123 ? -11.807 16.034  16.030  1.00 17.19 ? 123 TRP A CZ3 1 
ATOM   966  C  CH2 . TRP A 1 123 ? -12.258 16.099  14.704  1.00 17.52 ? 123 TRP A CH2 1 
ATOM   967  N  N   . ASN A 1 124 ? -11.406 12.460  19.949  1.00 14.51 ? 124 ASN A N   1 
ATOM   968  C  CA  . ASN A 1 124 ? -12.093 13.415  20.806  1.00 15.79 ? 124 ASN A CA  1 
ATOM   969  C  C   . ASN A 1 124 ? -12.249 14.778  20.139  1.00 16.98 ? 124 ASN A C   1 
ATOM   970  O  O   . ASN A 1 124 ? -11.251 15.428  19.853  1.00 16.05 ? 124 ASN A O   1 
ATOM   971  C  CB  . ASN A 1 124 ? -11.280 13.481  22.107  1.00 16.40 ? 124 ASN A CB  1 
ATOM   972  C  CG  . ASN A 1 124 ? -12.034 14.117  23.250  1.00 19.91 ? 124 ASN A CG  1 
ATOM   973  O  OD1 . ASN A 1 124 ? -12.887 14.974  23.028  1.00 20.35 ? 124 ASN A OD1 1 
ATOM   974  N  ND2 . ASN A 1 124 ? -11.649 13.763  24.472  1.00 20.85 ? 124 ASN A ND2 1 
ATOM   975  N  N   . THR A 1 125 ? -13.504 15.211  19.897  1.00 18.06 ? 125 THR A N   1 
ATOM   976  C  CA  . THR A 1 125 ? -13.732 16.468  19.190  1.00 19.26 ? 125 THR A CA  1 
ATOM   977  C  C   . THR A 1 125 ? -13.150 17.663  19.955  1.00 20.30 ? 125 THR A C   1 
ATOM   978  O  O   . THR A 1 125 ? -12.894 18.692  19.285  1.00 21.26 ? 125 THR A O   1 
ATOM   979  C  CB  . THR A 1 125 ? -15.204 16.633  18.799  1.00 22.34 ? 125 THR A CB  1 
ATOM   980  O  OG1 . THR A 1 125 ? -15.990 16.692  19.997  1.00 23.63 ? 125 THR A OG1 1 
ATOM   981  C  CG2 . THR A 1 125 ? -15.640 15.472  17.942  1.00 21.75 ? 125 THR A CG2 1 
ATOM   982  N  N   . LYS A 1 126 ? -12.828 17.536  21.372  1.00 20.60 ? 127 LYS A N   1 
ATOM   983  C  CA  . LYS A 1 126 ? -12.197 18.769  21.929  1.00 28.62 ? 127 LYS A CA  1 
ATOM   984  C  C   . LYS A 1 126 ? -10.826 19.080  21.315  1.00 27.06 ? 127 LYS A C   1 
ATOM   985  O  O   . LYS A 1 126 ? -10.362 20.216  21.426  1.00 25.75 ? 127 LYS A O   1 
ATOM   986  C  CB  . LYS A 1 126 ? -12.210 18.691  23.459  1.00 33.02 ? 127 LYS A CB  1 
ATOM   987  C  CG  . LYS A 1 126 ? -11.208 17.768  24.121  1.00 33.98 ? 127 LYS A CG  1 
ATOM   988  C  CD  . LYS A 1 126 ? -11.549 17.602  25.599  1.00 35.47 ? 127 LYS A CD  1 
ATOM   989  C  CE  . LYS A 1 126 ? -10.607 16.696  26.364  1.00 37.82 ? 127 LYS A CE  1 
ATOM   990  N  N   . TYR A 1 127 ? -10.180 18.112  20.639  1.00 21.27 ? 128 TYR A N   1 
ATOM   991  C  CA  . TYR A 1 127 ? -8.843  18.299  20.078  1.00 20.14 ? 128 TYR A CA  1 
ATOM   992  C  C   . TYR A 1 127 ? -8.849  18.684  18.596  1.00 18.33 ? 128 TYR A C   1 
ATOM   993  O  O   . TYR A 1 127 ? -7.789  18.929  18.005  1.00 20.38 ? 128 TYR A O   1 
ATOM   994  C  CB  . TYR A 1 127 ? -7.921  17.099  20.380  1.00 20.47 ? 128 TYR A CB  1 
ATOM   995  C  CG  . TYR A 1 127 ? -7.802  16.833  21.854  1.00 22.31 ? 128 TYR A CG  1 
ATOM   996  C  CD1 . TYR A 1 127 ? -7.399  17.863  22.699  1.00 26.11 ? 128 TYR A CD1 1 
ATOM   997  C  CD2 . TYR A 1 127 ? -8.138  15.614  22.419  1.00 21.67 ? 128 TYR A CD2 1 
ATOM   998  C  CE1 . TYR A 1 127 ? -7.324  17.682  24.066  1.00 25.76 ? 128 TYR A CE1 1 
ATOM   999  C  CE2 . TYR A 1 127 ? -8.037  15.404  23.793  1.00 22.91 ? 128 TYR A CE2 1 
ATOM   1000 C  CZ  . TYR A 1 127 ? -7.630  16.452  24.611  1.00 26.65 ? 128 TYR A CZ  1 
ATOM   1001 O  OH  . TYR A 1 127 ? -7.534  16.286  25.964  1.00 25.69 ? 128 TYR A OH  1 
ATOM   1002 N  N   . GLY A 1 128 ? -10.025 18.704  17.945  1.00 18.23 ? 129 GLY A N   1 
ATOM   1003 C  CA  . GLY A 1 128 ? -10.105 19.312  16.617  1.00 20.24 ? 129 GLY A CA  1 
ATOM   1004 C  C   . GLY A 1 128 ? -9.658  18.448  15.440  1.00 22.63 ? 129 GLY A C   1 
ATOM   1005 O  O   . GLY A 1 128 ? -10.167 18.609  14.333  1.00 23.55 ? 129 GLY A O   1 
ATOM   1006 N  N   . ASP A 1 129 ? -8.681  17.553  15.642  1.00 22.40 ? 130 ASP A N   1 
ATOM   1007 C  CA  . ASP A 1 129 ? -8.302  16.632  14.589  1.00 24.77 ? 130 ASP A CA  1 
ATOM   1008 C  C   . ASP A 1 129 ? -7.627  15.408  15.214  1.00 24.48 ? 130 ASP A C   1 
ATOM   1009 O  O   . ASP A 1 129 ? -7.174  15.466  16.364  1.00 22.35 ? 130 ASP A O   1 
ATOM   1010 C  CB  . ASP A 1 129 ? -7.444  17.323  13.521  1.00 30.97 ? 130 ASP A CB  1 
ATOM   1011 C  CG  . ASP A 1 129 ? -5.983  17.428  13.895  1.00 40.29 ? 130 ASP A CG  1 
ATOM   1012 O  OD1 . ASP A 1 129 ? -5.630  18.412  14.561  1.00 48.18 ? 130 ASP A OD1 1 
ATOM   1013 O  OD2 . ASP A 1 129 ? -5.192  16.527  13.491  1.00 43.43 ? 130 ASP A OD2 1 
ATOM   1014 N  N   . ALA A 1 130 ? -7.554  14.320  14.439  1.00 24.12 ? 131 ALA A N   1 
ATOM   1015 C  CA  . ALA A 1 130 ? -6.982  13.052  14.892  1.00 25.51 ? 131 ALA A CA  1 
ATOM   1016 C  C   . ALA A 1 130 ? -5.505  13.192  15.270  1.00 24.01 ? 131 ALA A C   1 
ATOM   1017 O  O   . ALA A 1 130 ? -5.064  12.602  16.255  1.00 21.36 ? 131 ALA A O   1 
ATOM   1018 C  CB  . ALA A 1 130 ? -7.189  11.966  13.871  1.00 23.79 ? 131 ALA A CB  1 
ATOM   1019 N  N   . GLY A 1 131 ? -4.729  13.985  14.500  1.00 24.27 ? 132 GLY A N   1 
ATOM   1020 C  CA  . GLY A 1 131 ? -3.320  14.173  14.833  1.00 22.63 ? 132 GLY A CA  1 
ATOM   1021 C  C   . GLY A 1 131 ? -3.120  14.801  16.209  1.00 23.14 ? 132 GLY A C   1 
ATOM   1022 O  O   . GLY A 1 131 ? -2.296  14.353  17.011  1.00 23.48 ? 132 GLY A O   1 
ATOM   1023 N  N   . LYS A 1 132 ? -3.825  15.907  16.469  1.00 21.75 ? 133 LYS A N   1 
ATOM   1024 C  CA  . LYS A 1 132 ? -3.677  16.542  17.754  1.00 24.01 ? 133 LYS A CA  1 
ATOM   1025 C  C   . LYS A 1 132 ? -4.205  15.598  18.824  1.00 21.43 ? 133 LYS A C   1 
ATOM   1026 O  O   . LYS A 1 132 ? -3.604  15.510  19.890  1.00 20.72 ? 133 LYS A O   1 
ATOM   1027 C  CB  . LYS A 1 132 ? -4.354  17.919  17.766  1.00 27.00 ? 133 LYS A CB  1 
ATOM   1028 C  CG  . LYS A 1 132 ? -3.768  18.964  16.811  1.00 31.64 ? 133 LYS A CG  1 
ATOM   1029 C  CD  . LYS A 1 132 ? -2.371  19.507  17.159  1.00 38.51 ? 133 LYS A CD  1 
ATOM   1030 C  CE  . LYS A 1 132 ? -2.342  20.581  18.229  1.00 43.03 ? 133 LYS A CE  1 
ATOM   1031 N  NZ  . LYS A 1 132 ? -2.350  20.002  19.594  1.00 40.60 ? 133 LYS A NZ  1 
ATOM   1032 N  N   . ALA A 1 133 ? -5.325  14.904  18.545  1.00 20.10 ? 134 ALA A N   1 
ATOM   1033 C  CA  . ALA A 1 133 ? -5.902  13.993  19.541  1.00 17.94 ? 134 ALA A CA  1 
ATOM   1034 C  C   . ALA A 1 133 ? -4.887  12.915  19.919  1.00 17.86 ? 134 ALA A C   1 
ATOM   1035 O  O   . ALA A 1 133 ? -4.844  12.484  21.071  1.00 18.77 ? 134 ALA A O   1 
ATOM   1036 C  CB  . ALA A 1 133 ? -7.177  13.354  18.990  1.00 16.06 ? 134 ALA A CB  1 
ATOM   1037 N  N   . SER A 1 134 ? -4.056  12.488  18.961  1.00 17.78 ? 135 SER A N   1 
ATOM   1038 C  CA  . SER A 1 134 ? -3.122  11.390  19.215  1.00 20.03 ? 135 SER A CA  1 
ATOM   1039 C  C   . SER A 1 134 ? -2.052  11.788  20.230  1.00 19.83 ? 135 SER A C   1 
ATOM   1040 O  O   . SER A 1 134 ? -1.363  10.943  20.785  1.00 21.22 ? 135 SER A O   1 
ATOM   1041 C  CB  . SER A 1 134 ? -2.502  10.862  17.932  1.00 21.18 ? 135 SER A CB  1 
ATOM   1042 O  OG  . SER A 1 134 ? -1.490  11.747  17.487  1.00 24.61 ? 135 SER A OG  1 
ATOM   1043 N  N   . GLN A 1 135 ? -1.931  13.091  20.521  1.00 21.15 ? 136 GLN A N   1 
ATOM   1044 C  CA  . GLN A 1 135 ? -0.899  13.544  21.444  1.00 23.34 ? 136 GLN A CA  1 
ATOM   1045 C  C   . GLN A 1 135 ? -1.463  13.691  22.852  1.00 23.89 ? 136 GLN A C   1 
ATOM   1046 O  O   . GLN A 1 135 ? -0.767  14.167  23.758  1.00 28.60 ? 136 GLN A O   1 
ATOM   1047 C  CB  . GLN A 1 135 ? -0.340  14.895  20.978  1.00 27.36 ? 136 GLN A CB  1 
ATOM   1048 C  CG  . GLN A 1 135 ? 0.173   14.891  19.540  1.00 31.84 ? 136 GLN A CG  1 
ATOM   1049 C  CD  . GLN A 1 135 ? 1.221   13.826  19.315  1.00 42.54 ? 136 GLN A CD  1 
ATOM   1050 O  OE1 . GLN A 1 135 ? 2.185   13.685  20.074  1.00 51.36 ? 136 GLN A OE1 1 
ATOM   1051 N  NE2 . GLN A 1 135 ? 1.040   13.060  18.254  1.00 41.80 ? 136 GLN A NE2 1 
ATOM   1052 N  N   . GLN A 1 136 ? -2.712  13.274  23.063  1.00 21.86 ? 137 GLN A N   1 
ATOM   1053 C  CA  . GLN A 1 136 ? -3.381  13.555  24.326  1.00 21.18 ? 137 GLN A CA  1 
ATOM   1054 C  C   . GLN A 1 136 ? -3.764  12.235  24.987  1.00 21.35 ? 137 GLN A C   1 
ATOM   1055 O  O   . GLN A 1 136 ? -4.087  11.263  24.298  1.00 20.63 ? 137 GLN A O   1 
ATOM   1056 C  CB  . GLN A 1 136 ? -4.634  14.423  24.117  1.00 24.97 ? 137 GLN A CB  1 
ATOM   1057 C  CG  . GLN A 1 136 ? -4.406  15.651  23.238  1.00 28.73 ? 137 GLN A CG  1 
ATOM   1058 C  CD  . GLN A 1 136 ? -3.448  16.620  23.890  1.00 34.29 ? 137 GLN A CD  1 
ATOM   1059 O  OE1 . GLN A 1 136 ? -3.308  16.646  25.111  1.00 30.62 ? 137 GLN A OE1 1 
ATOM   1060 N  NE2 . GLN A 1 136 ? -2.767  17.399  23.065  1.00 34.86 ? 137 GLN A NE2 1 
ATOM   1061 N  N   . PRO A 1 137 ? -3.749  12.134  26.339  1.00 23.34 ? 138 PRO A N   1 
ATOM   1062 C  CA  . PRO A 1 137 ? -4.015  10.870  27.014  1.00 20.65 ? 138 PRO A CA  1 
ATOM   1063 C  C   . PRO A 1 137 ? -5.448  10.377  26.866  1.00 20.36 ? 138 PRO A C   1 
ATOM   1064 O  O   . PRO A 1 137 ? -5.676  9.166   26.943  1.00 20.71 ? 138 PRO A O   1 
ATOM   1065 C  CB  . PRO A 1 137 ? -3.703  11.084  28.508  1.00 25.22 ? 138 PRO A CB  1 
ATOM   1066 C  CG  . PRO A 1 137 ? -3.518  12.589  28.636  1.00 24.47 ? 138 PRO A CG  1 
ATOM   1067 C  CD  . PRO A 1 137 ? -3.339  13.208  27.259  1.00 24.38 ? 138 PRO A CD  1 
ATOM   1068 N  N   . ASP A 1 138 ? -6.368  11.314  26.571  1.00 17.89 ? 139 ASP A N   1 
ATOM   1069 C  CA  . ASP A 1 138 ? -7.749  11.010  26.289  1.00 19.28 ? 139 ASP A CA  1 
ATOM   1070 C  C   . ASP A 1 138 ? -8.114  11.382  24.854  1.00 17.37 ? 139 ASP A C   1 
ATOM   1071 O  O   . ASP A 1 138 ? -9.257  11.763  24.622  1.00 18.80 ? 139 ASP A O   1 
ATOM   1072 C  CB  . ASP A 1 138 ? -8.713  11.720  27.256  1.00 22.10 ? 139 ASP A CB  1 
ATOM   1073 C  CG  . ASP A 1 138 ? -8.569  13.230  27.258  1.00 27.26 ? 139 ASP A CG  1 
ATOM   1074 O  OD1 . ASP A 1 138 ? -7.629  13.756  26.583  1.00 26.61 ? 139 ASP A OD1 1 
ATOM   1075 O  OD2 . ASP A 1 138 ? -9.418  13.892  27.913  1.00 30.55 ? 139 ASP A OD2 1 
ATOM   1076 N  N   . GLY A 1 139 ? -7.162  11.258  23.924  1.00 15.94 ? 140 GLY A N   1 
ATOM   1077 C  CA  . GLY A 1 139 ? -7.329  11.690  22.537  1.00 13.36 ? 140 GLY A CA  1 
ATOM   1078 C  C   . GLY A 1 139 ? -8.238  10.793  21.701  1.00 14.64 ? 140 GLY A C   1 
ATOM   1079 O  O   . GLY A 1 139 ? -9.012  11.326  20.894  1.00 15.14 ? 140 GLY A O   1 
ATOM   1080 N  N   . LEU A 1 140 ? -8.097  9.448   21.835  1.00 13.31 ? 141 LEU A N   1 
ATOM   1081 C  CA  . LEU A 1 140 ? -8.753  8.534   20.911  1.00 14.74 ? 141 LEU A CA  1 
ATOM   1082 C  C   . LEU A 1 140 ? -9.598  7.543   21.704  1.00 13.92 ? 141 LEU A C   1 
ATOM   1083 O  O   . LEU A 1 140 ? -9.294  7.245   22.859  1.00 13.53 ? 141 LEU A O   1 
ATOM   1084 C  CB  . LEU A 1 140 ? -7.710  7.760   20.091  1.00 15.42 ? 141 LEU A CB  1 
ATOM   1085 C  CG  . LEU A 1 140 ? -6.725  8.599   19.255  1.00 16.31 ? 141 LEU A CG  1 
ATOM   1086 C  CD1 . LEU A 1 140 ? -5.870  7.657   18.398  1.00 15.61 ? 141 LEU A CD1 1 
ATOM   1087 C  CD2 . LEU A 1 140 ? -7.467  9.532   18.314  1.00 16.99 ? 141 LEU A CD2 1 
ATOM   1088 N  N   . ALA A 1 141 ? -10.665 7.064   21.061  1.00 12.50 ? 142 ALA A N   1 
ATOM   1089 C  CA  . ALA A 1 141 ? -11.398 5.920   21.589  1.00 14.44 ? 142 ALA A CA  1 
ATOM   1090 C  C   . ALA A 1 141 ? -11.476 4.918   20.447  1.00 13.64 ? 142 ALA A C   1 
ATOM   1091 O  O   . ALA A 1 141 ? -11.880 5.249   19.316  1.00 14.43 ? 142 ALA A O   1 
ATOM   1092 C  CB  . ALA A 1 141 ? -12.781 6.335   22.059  1.00 13.62 ? 142 ALA A CB  1 
ATOM   1093 N  N   . VAL A 1 142 ? -11.002 3.698   20.720  1.00 13.80 ? 143 VAL A N   1 
ATOM   1094 C  CA  . VAL A 1 142 ? -11.065 2.670   19.709  1.00 14.41 ? 143 VAL A CA  1 
ATOM   1095 C  C   . VAL A 1 142 ? -12.066 1.614   20.181  1.00 12.37 ? 143 VAL A C   1 
ATOM   1096 O  O   . VAL A 1 142 ? -11.959 1.121   21.298  1.00 14.78 ? 143 VAL A O   1 
ATOM   1097 C  CB  . VAL A 1 142 ? -9.699  2.023   19.398  1.00 13.35 ? 143 VAL A CB  1 
ATOM   1098 C  CG1 . VAL A 1 142 ? -9.894  0.987   18.285  1.00 14.65 ? 143 VAL A CG1 1 
ATOM   1099 C  CG2 . VAL A 1 142 ? -8.711  3.083   18.910  1.00 15.77 ? 143 VAL A CG2 1 
ATOM   1100 N  N   . LEU A 1 143 ? -13.079 1.344   19.349  1.00 12.06 ? 144 LEU A N   1 
ATOM   1101 C  CA  . LEU A 1 143 ? -14.074 0.322   19.611  1.00 12.85 ? 144 LEU A CA  1 
ATOM   1102 C  C   . LEU A 1 143 ? -13.537 -0.945  18.940  1.00 14.03 ? 144 LEU A C   1 
ATOM   1103 O  O   . LEU A 1 143 ? -13.351 -0.964  17.712  1.00 14.26 ? 144 LEU A O   1 
ATOM   1104 C  CB  . LEU A 1 143 ? -15.406 0.738   18.962  1.00 13.92 ? 144 LEU A CB  1 
ATOM   1105 C  CG  . LEU A 1 143 ? -16.578 -0.217  19.140  1.00 15.48 ? 144 LEU A CG  1 
ATOM   1106 C  CD1 . LEU A 1 143 ? -16.877 -0.440  20.614  1.00 16.19 ? 144 LEU A CD1 1 
ATOM   1107 C  CD2 . LEU A 1 143 ? -17.792 0.390   18.474  1.00 16.63 ? 144 LEU A CD2 1 
ATOM   1108 N  N   . GLY A 1 144 ? -13.245 -1.965  19.745  1.00 13.93 ? 145 GLY A N   1 
ATOM   1109 C  CA  . GLY A 1 144 ? -12.685 -3.203  19.200  1.00 12.31 ? 145 GLY A CA  1 
ATOM   1110 C  C   . GLY A 1 144 ? -13.739 -4.311  19.220  1.00 12.72 ? 145 GLY A C   1 
ATOM   1111 O  O   . GLY A 1 144 ? -14.449 -4.482  20.215  1.00 12.47 ? 145 GLY A O   1 
ATOM   1112 N  N   . ILE A 1 145 ? -13.831 -5.055  18.127  1.00 11.37 ? 146 ILE A N   1 
ATOM   1113 C  CA  . ILE A 1 145 ? -14.840 -6.099  17.974  1.00 11.58 ? 146 ILE A CA  1 
ATOM   1114 C  C   . ILE A 1 145 ? -14.117 -7.337  17.467  1.00 12.60 ? 146 ILE A C   1 
ATOM   1115 O  O   . ILE A 1 145 ? -13.414 -7.279  16.458  1.00 12.96 ? 146 ILE A O   1 
ATOM   1116 C  CB  . ILE A 1 145 ? -15.914 -5.623  16.966  1.00 12.19 ? 146 ILE A CB  1 
ATOM   1117 C  CG1 . ILE A 1 145 ? -16.614 -4.344  17.452  1.00 13.10 ? 146 ILE A CG1 1 
ATOM   1118 C  CG2 . ILE A 1 145 ? -16.902 -6.767  16.782  1.00 14.43 ? 146 ILE A CG2 1 
ATOM   1119 C  CD1 . ILE A 1 145 ? -17.602 -3.775  16.454  1.00 14.13 ? 146 ILE A CD1 1 
ATOM   1120 N  N   . PHE A 1 146 ? -14.326 -8.478  18.134  1.00 12.41 ? 147 PHE A N   1 
ATOM   1121 C  CA  . PHE A 1 146 ? -13.677 -9.728  17.735  1.00 12.43 ? 147 PHE A CA  1 
ATOM   1122 C  C   . PHE A 1 146 ? -14.435 -10.368 16.575  1.00 12.87 ? 147 PHE A C   1 
ATOM   1123 O  O   . PHE A 1 146 ? -15.655 -10.256 16.522  1.00 15.16 ? 147 PHE A O   1 
ATOM   1124 C  CB  . PHE A 1 146 ? -13.699 -10.681 18.923  1.00 12.86 ? 147 PHE A CB  1 
ATOM   1125 C  CG  . PHE A 1 146 ? -12.863 -10.195 20.069  1.00 12.64 ? 147 PHE A CG  1 
ATOM   1126 C  CD1 . PHE A 1 146 ? -11.491 -10.028 19.923  1.00 13.06 ? 147 PHE A CD1 1 
ATOM   1127 C  CD2 . PHE A 1 146 ? -13.452 -9.908  21.283  1.00 12.83 ? 147 PHE A CD2 1 
ATOM   1128 C  CE1 . PHE A 1 146 ? -10.708 -9.659  21.013  1.00 12.04 ? 147 PHE A CE1 1 
ATOM   1129 C  CE2 . PHE A 1 146 ? -12.661 -9.573  22.381  1.00 14.48 ? 147 PHE A CE2 1 
ATOM   1130 C  CZ  . PHE A 1 146 ? -11.297 -9.430  22.239  1.00 13.44 ? 147 PHE A CZ  1 
ATOM   1131 N  N   . LEU A 1 147 ? -13.716 -11.016 15.653  1.00 13.07 ? 148 LEU A N   1 
ATOM   1132 C  CA  . LEU A 1 147 ? -14.350 -11.826 14.618  1.00 12.87 ? 148 LEU A CA  1 
ATOM   1133 C  C   . LEU A 1 147 ? -14.021 -13.303 14.877  1.00 13.41 ? 148 LEU A C   1 
ATOM   1134 O  O   . LEU A 1 147 ? -12.848 -13.654 15.033  1.00 14.60 ? 148 LEU A O   1 
ATOM   1135 C  CB  . LEU A 1 147 ? -13.757 -11.400 13.275  1.00 12.91 ? 148 LEU A CB  1 
ATOM   1136 C  CG  . LEU A 1 147 ? -14.349 -10.133 12.602  1.00 13.87 ? 148 LEU A CG  1 
ATOM   1137 C  CD1 . LEU A 1 147 ? -14.109 -8.877  13.438  1.00 15.55 ? 148 LEU A CD1 1 
ATOM   1138 C  CD2 . LEU A 1 147 ? -13.705 -9.910  11.232  1.00 14.22 ? 148 LEU A CD2 1 
ATOM   1139 N  N   . LYS A 1 148 ? -15.071 -14.140 14.929  1.00 14.86 ? 149 LYS A N   1 
ATOM   1140 C  CA  . LYS A 1 148 ? -14.889 -15.582 14.906  1.00 14.62 ? 149 LYS A CA  1 
ATOM   1141 C  C   . LYS A 1 148 ? -15.361 -16.107 13.564  1.00 16.06 ? 149 LYS A C   1 
ATOM   1142 O  O   . LYS A 1 148 ? -16.206 -15.489 12.935  1.00 15.37 ? 149 LYS A O   1 
ATOM   1143 C  CB  . LYS A 1 148 ? -15.635 -16.285 16.042  1.00 18.97 ? 149 LYS A CB  1 
ATOM   1144 C  CG  . LYS A 1 148 ? -17.152 -16.256 15.977  1.00 22.47 ? 149 LYS A CG  1 
ATOM   1145 C  CD  . LYS A 1 148 ? -17.748 -16.903 17.234  1.00 26.67 ? 149 LYS A CD  1 
ATOM   1146 C  CE  . LYS A 1 148 ? -19.237 -17.144 17.099  1.00 34.89 ? 149 LYS A CE  1 
ATOM   1147 N  NZ  . LYS A 1 148 ? -19.776 -17.859 18.284  1.00 44.14 ? 149 LYS A NZ  1 
ATOM   1148 N  N   . VAL A 1 149 ? -14.849 -17.278 13.177  1.00 15.89 ? 150 VAL A N   1 
ATOM   1149 C  CA  . VAL A 1 149 ? -15.221 -17.814 11.873  1.00 16.38 ? 150 VAL A CA  1 
ATOM   1150 C  C   . VAL A 1 149 ? -16.394 -18.779 12.028  1.00 17.72 ? 150 VAL A C   1 
ATOM   1151 O  O   . VAL A 1 149 ? -16.332 -19.744 12.805  1.00 17.68 ? 150 VAL A O   1 
ATOM   1152 C  CB  . VAL A 1 149 ? -14.014 -18.505 11.196  1.00 17.08 ? 150 VAL A CB  1 
ATOM   1153 C  CG1 . VAL A 1 149 ? -14.421 -19.317 9.957   1.00 18.63 ? 150 VAL A CG1 1 
ATOM   1154 C  CG2 . VAL A 1 149 ? -12.970 -17.456 10.821  1.00 20.56 ? 150 VAL A CG2 1 
ATOM   1155 N  N   . GLY A 1 150 ? -17.428 -18.561 11.200  1.00 16.85 ? 151 GLY A N   1 
ATOM   1156 C  CA  . GLY A 1 150 ? -18.650 -19.330 11.300  1.00 16.73 ? 151 GLY A CA  1 
ATOM   1157 C  C   . GLY A 1 150 ? -19.603 -18.899 10.203  1.00 15.96 ? 151 GLY A C   1 
ATOM   1158 O  O   . GLY A 1 150 ? -19.231 -18.961 9.046   1.00 15.27 ? 151 GLY A O   1 
ATOM   1159 N  N   . SER A 1 151 ? -20.772 -18.381 10.607  1.00 17.04 ? 152 SER A N   1 
ATOM   1160 C  CA  . SER A 1 151 ? -21.722 -17.762 9.677   1.00 18.36 ? 152 SER A CA  1 
ATOM   1161 C  C   . SER A 1 151 ? -21.115 -16.500 9.068   1.00 17.26 ? 152 SER A C   1 
ATOM   1162 O  O   . SER A 1 151 ? -20.296 -15.868 9.691   1.00 16.34 ? 152 SER A O   1 
ATOM   1163 C  CB  . SER A 1 151 ? -22.977 -17.351 10.456  1.00 19.84 ? 152 SER A CB  1 
ATOM   1164 O  OG  . SER A 1 151 ? -23.642 -18.508 10.893  1.00 29.35 ? 152 SER A OG  1 
ATOM   1165 N  N   . ALA A 1 152 ? -21.521 -16.133 7.845   1.00 15.54 ? 153 ALA A N   1 
ATOM   1166 C  CA  . ALA A 1 152 ? -21.047 -14.907 7.232   1.00 16.87 ? 153 ALA A CA  1 
ATOM   1167 C  C   . ALA A 1 152 ? -21.709 -13.724 7.933   1.00 16.28 ? 153 ALA A C   1 
ATOM   1168 O  O   . ALA A 1 152 ? -22.818 -13.836 8.469   1.00 18.85 ? 153 ALA A O   1 
ATOM   1169 C  CB  . ALA A 1 152 ? -21.394 -14.900 5.751   1.00 18.64 ? 153 ALA A CB  1 
ATOM   1170 N  N   . LYS A 1 153 ? -21.025 -12.580 7.858   1.00 14.35 ? 154 LYS A N   1 
ATOM   1171 C  CA  . LYS A 1 153 ? -21.592 -11.318 8.287   1.00 15.60 ? 154 LYS A CA  1 
ATOM   1172 C  C   . LYS A 1 153 ? -21.979 -10.561 7.021   1.00 14.94 ? 154 LYS A C   1 
ATOM   1173 O  O   . LYS A 1 153 ? -21.124 -10.142 6.240   1.00 16.18 ? 154 LYS A O   1 
ATOM   1174 C  CB  . LYS A 1 153 ? -20.512 -10.582 9.109   1.00 15.74 ? 154 LYS A CB  1 
ATOM   1175 C  CG  . LYS A 1 153 ? -20.993 -9.300  9.796   1.00 16.08 ? 154 LYS A CG  1 
ATOM   1176 C  CD  . LYS A 1 153 ? -21.972 -9.682  10.917  1.00 17.57 ? 154 LYS A CD  1 
ATOM   1177 C  CE  . LYS A 1 153 ? -22.295 -8.537  11.861  1.00 22.09 ? 154 LYS A CE  1 
ATOM   1178 N  NZ  . LYS A 1 153 ? -23.338 -8.951  12.830  1.00 25.19 ? 154 LYS A NZ  1 
ATOM   1179 N  N   . PRO A 1 154 ? -23.283 -10.436 6.719   1.00 15.25 ? 155 PRO A N   1 
ATOM   1180 C  CA  . PRO A 1 154 ? -23.687 -9.846  5.443   1.00 14.81 ? 155 PRO A CA  1 
ATOM   1181 C  C   . PRO A 1 154 ? -23.186 -8.414  5.300   1.00 14.67 ? 155 PRO A C   1 
ATOM   1182 O  O   . PRO A 1 154 ? -22.812 -8.026  4.208   1.00 15.01 ? 155 PRO A O   1 
ATOM   1183 C  CB  . PRO A 1 154 ? -25.217 -9.908  5.560   1.00 15.59 ? 155 PRO A CB  1 
ATOM   1184 C  CG  . PRO A 1 154 ? -25.425 -11.149 6.341   1.00 16.23 ? 155 PRO A CG  1 
ATOM   1185 C  CD  . PRO A 1 154 ? -24.409 -11.027 7.471   1.00 16.59 ? 155 PRO A CD  1 
ATOM   1186 N  N   . GLY A 1 155 ? -23.113 -7.666  6.403   1.00 13.32 ? 156 GLY A N   1 
ATOM   1187 C  CA  . GLY A 1 155 ? -22.702 -6.268  6.321   1.00 13.51 ? 156 GLY A CA  1 
ATOM   1188 C  C   . GLY A 1 155 ? -21.194 -6.080  6.098   1.00 15.94 ? 156 GLY A C   1 
ATOM   1189 O  O   . GLY A 1 155 ? -20.766 -4.945  5.860   1.00 16.81 ? 156 GLY A O   1 
ATOM   1190 N  N   . LEU A 1 156 ? -20.401 -7.170  6.129   1.00 14.91 ? 157 LEU A N   1 
ATOM   1191 C  CA  . LEU A 1 156 ? -18.984 -7.091  5.799   1.00 15.24 ? 157 LEU A CA  1 
ATOM   1192 C  C   . LEU A 1 156 ? -18.739 -7.352  4.322   1.00 14.80 ? 157 LEU A C   1 
ATOM   1193 O  O   . LEU A 1 156 ? -17.683 -7.044  3.784   1.00 15.26 ? 157 LEU A O   1 
ATOM   1194 C  CB  . LEU A 1 156 ? -18.248 -8.114  6.684   1.00 15.74 ? 157 LEU A CB  1 
ATOM   1195 C  CG  . LEU A 1 156 ? -16.743 -8.275  6.466   1.00 16.30 ? 157 LEU A CG  1 
ATOM   1196 C  CD1 . LEU A 1 156 ? -16.023 -7.004  6.909   1.00 16.86 ? 157 LEU A CD1 1 
ATOM   1197 C  CD2 . LEU A 1 156 ? -16.231 -9.493  7.211   1.00 17.04 ? 157 LEU A CD2 1 
ATOM   1198 N  N   . GLN A 1 157 ? -19.754 -7.901  3.644   1.00 17.36 ? 158 GLN A N   1 
ATOM   1199 C  CA  . GLN A 1 157 ? -19.527 -8.340  2.277   1.00 15.96 ? 158 GLN A CA  1 
ATOM   1200 C  C   . GLN A 1 157 ? -19.068 -7.205  1.365   1.00 14.79 ? 158 GLN A C   1 
ATOM   1201 O  O   . GLN A 1 157 ? -18.229 -7.459  0.500   1.00 14.26 ? 158 GLN A O   1 
ATOM   1202 C  CB  . GLN A 1 157 ? -20.742 -9.108  1.751   1.00 15.45 ? 158 GLN A CB  1 
ATOM   1203 C  CG  . GLN A 1 157 ? -20.377 -9.895  0.496   1.00 16.77 ? 158 GLN A CG  1 
ATOM   1204 C  CD  . GLN A 1 157 ? -19.324 -10.963 0.719   1.00 16.53 ? 158 GLN A CD  1 
ATOM   1205 O  OE1 . GLN A 1 157 ? -19.162 -11.504 1.818   1.00 17.35 ? 158 GLN A OE1 1 
ATOM   1206 N  NE2 . GLN A 1 157 ? -18.582 -11.310 -0.315  1.00 17.28 ? 158 GLN A NE2 1 
ATOM   1207 N  N   . LYS A 1 158 ? -19.601 -5.975  1.517   1.00 15.87 ? 159 LYS A N   1 
ATOM   1208 C  CA  . LYS A 1 158 ? -19.224 -4.898  0.634   1.00 16.08 ? 159 LYS A CA  1 
ATOM   1209 C  C   . LYS A 1 158 ? -17.717 -4.637  0.723   1.00 16.18 ? 159 LYS A C   1 
ATOM   1210 O  O   . LYS A 1 158 ? -17.096 -4.307  -0.267  1.00 17.48 ? 159 LYS A O   1 
ATOM   1211 C  CB  . LYS A 1 158 ? -20.107 -3.670  0.882   1.00 18.64 ? 159 LYS A CB  1 
ATOM   1212 C  CG  . LYS A 1 158 ? -19.763 -2.457  0.042   1.00 25.25 ? 159 LYS A CG  1 
ATOM   1213 C  CD  . LYS A 1 158 ? -20.700 -1.285  0.321   1.00 29.60 ? 159 LYS A CD  1 
ATOM   1214 C  CE  . LYS A 1 158 ? -20.259 0.026   -0.325  1.00 32.03 ? 159 LYS A CE  1 
ATOM   1215 N  NZ  . LYS A 1 158 ? -20.798 0.200   -1.705  1.00 29.18 ? 159 LYS A NZ  1 
ATOM   1216 N  N   . VAL A 1 159 ? -17.158 -4.790  1.924   1.00 13.57 ? 160 VAL A N   1 
ATOM   1217 C  CA  . VAL A 1 159 ? -15.724 -4.632  2.137   1.00 13.56 ? 160 VAL A CA  1 
ATOM   1218 C  C   . VAL A 1 159 ? -14.942 -5.744  1.409   1.00 14.93 ? 160 VAL A C   1 
ATOM   1219 O  O   . VAL A 1 159 ? -14.003 -5.488  0.659   1.00 16.01 ? 160 VAL A O   1 
ATOM   1220 C  CB  . VAL A 1 159 ? -15.441 -4.614  3.654   1.00 13.20 ? 160 VAL A CB  1 
ATOM   1221 C  CG1 . VAL A 1 159 ? -13.928 -4.695  3.886   1.00 15.44 ? 160 VAL A CG1 1 
ATOM   1222 C  CG2 . VAL A 1 159 ? -15.941 -3.300  4.258   1.00 15.63 ? 160 VAL A CG2 1 
ATOM   1223 N  N   . VAL A 1 160 ? -15.300 -7.002  1.686   1.00 15.05 ? 161 VAL A N   1 
ATOM   1224 C  CA  . VAL A 1 160 ? -14.535 -8.136  1.186   1.00 16.41 ? 161 VAL A CA  1 
ATOM   1225 C  C   . VAL A 1 160 ? -14.533 -8.122  -0.344  1.00 16.34 ? 161 VAL A C   1 
ATOM   1226 O  O   . VAL A 1 160 ? -13.518 -8.413  -0.979  1.00 17.23 ? 161 VAL A O   1 
ATOM   1227 C  CB  . VAL A 1 160 ? -15.161 -9.391  1.819   1.00 21.76 ? 161 VAL A CB  1 
ATOM   1228 C  CG1 . VAL A 1 160 ? -15.307 -10.588 0.904   1.00 27.89 ? 161 VAL A CG1 1 
ATOM   1229 C  CG2 . VAL A 1 160 ? -14.475 -9.644  3.150   1.00 24.19 ? 161 VAL A CG2 1 
ATOM   1230 N  N   . ASP A 1 161 ? -15.633 -7.691  -0.933  1.00 15.59 ? 162 ASP A N   1 
ATOM   1231 C  CA  . ASP A 1 161 ? -15.735 -7.783  -2.372  1.00 16.85 ? 162 ASP A CA  1 
ATOM   1232 C  C   . ASP A 1 161 ? -14.889 -6.763  -3.138  1.00 18.61 ? 162 ASP A C   1 
ATOM   1233 O  O   . ASP A 1 161 ? -14.716 -6.943  -4.338  1.00 18.95 ? 162 ASP A O   1 
ATOM   1234 C  CB  . ASP A 1 161 ? -17.178 -7.602  -2.824  1.00 17.18 ? 162 ASP A CB  1 
ATOM   1235 C  CG  . ASP A 1 161 ? -17.960 -8.895  -2.712  1.00 20.46 ? 162 ASP A CG  1 
ATOM   1236 O  OD1 . ASP A 1 161 ? -17.326 -9.973  -2.736  1.00 20.69 ? 162 ASP A OD1 1 
ATOM   1237 O  OD2 . ASP A 1 161 ? -19.209 -8.792  -2.661  1.00 22.53 ? 162 ASP A OD2 1 
ATOM   1238 N  N   . VAL A 1 162 ? -14.416 -5.688  -2.499  1.00 16.86 ? 163 VAL A N   1 
ATOM   1239 C  CA  . VAL A 1 162 ? -13.553 -4.691  -3.150  1.00 17.63 ? 163 VAL A CA  1 
ATOM   1240 C  C   . VAL A 1 162 ? -12.059 -4.930  -2.896  1.00 16.75 ? 163 VAL A C   1 
ATOM   1241 O  O   . VAL A 1 162 ? -11.217 -4.264  -3.495  1.00 15.76 ? 163 VAL A O   1 
ATOM   1242 C  CB  . VAL A 1 162 ? -13.955 -3.260  -2.715  1.00 18.85 ? 163 VAL A CB  1 
ATOM   1243 C  CG1 . VAL A 1 162 ? -13.522 -2.901  -1.305  1.00 16.94 ? 163 VAL A CG1 1 
ATOM   1244 C  CG2 . VAL A 1 162 ? -13.524 -2.195  -3.676  1.00 28.46 ? 163 VAL A CG2 1 
ATOM   1245 N  N   . LEU A 1 163 ? -11.701 -5.914  -2.058  1.00 16.78 ? 164 LEU A N   1 
ATOM   1246 C  CA  . LEU A 1 163 ? -10.317 -6.060  -1.643  1.00 16.02 ? 164 LEU A CA  1 
ATOM   1247 C  C   . LEU A 1 163 ? -9.444  -6.470  -2.834  1.00 17.52 ? 164 LEU A C   1 
ATOM   1248 O  O   . LEU A 1 163 ? -8.273  -6.126  -2.830  1.00 17.55 ? 164 LEU A O   1 
ATOM   1249 C  CB  . LEU A 1 163 ? -10.202 -7.061  -0.494  1.00 15.90 ? 164 LEU A CB  1 
ATOM   1250 C  CG  . LEU A 1 163 ? -10.772 -6.647  0.871   1.00 16.53 ? 164 LEU A CG  1 
ATOM   1251 C  CD1 . LEU A 1 163 ? -10.550 -7.774  1.893   1.00 16.80 ? 164 LEU A CD1 1 
ATOM   1252 C  CD2 . LEU A 1 163 ? -10.153 -5.343  1.378   1.00 14.82 ? 164 LEU A CD2 1 
ATOM   1253 N  N   . ASP A 1 164 ? -10.003 -7.163  -3.845  1.00 18.64 ? 165 ASP A N   1 
ATOM   1254 C  CA  . ASP A 1 164 ? -9.151  -7.521  -4.977  1.00 21.93 ? 165 ASP A CA  1 
ATOM   1255 C  C   . ASP A 1 164 ? -8.641  -6.259  -5.694  1.00 20.60 ? 165 ASP A C   1 
ATOM   1256 O  O   . ASP A 1 164 ? -7.667  -6.350  -6.443  1.00 20.78 ? 165 ASP A O   1 
ATOM   1257 C  CB  . ASP A 1 164 ? -9.912  -8.413  -5.956  1.00 27.00 ? 165 ASP A CB  1 
ATOM   1258 C  CG  . ASP A 1 164 ? -10.958 -7.619  -6.720  1.00 29.91 ? 165 ASP A CG  1 
ATOM   1259 O  OD1 . ASP A 1 164 ? -11.948 -7.095  -6.067  1.00 34.79 ? 165 ASP A OD1 1 
ATOM   1260 O  OD2 . ASP A 1 164 ? -10.767 -7.459  -7.951  1.00 36.67 ? 165 ASP A OD2 1 
ATOM   1261 N  N   . SER A 1 165 ? -9.312  -5.111  -5.503  1.00 18.47 ? 166 SER A N   1 
ATOM   1262 C  CA  . SER A 1 165 ? -8.943  -3.875  -6.170  1.00 19.92 ? 166 SER A CA  1 
ATOM   1263 C  C   . SER A 1 165 ? -7.834  -3.121  -5.425  1.00 17.53 ? 166 SER A C   1 
ATOM   1264 O  O   . SER A 1 165 ? -7.329  -2.103  -5.931  1.00 19.18 ? 166 SER A O   1 
ATOM   1265 C  CB  . SER A 1 165 ? -10.159 -3.003  -6.422  1.00 21.21 ? 166 SER A CB  1 
ATOM   1266 O  OG  . SER A 1 165 ? -10.546 -2.354  -5.215  1.00 24.84 ? 166 SER A OG  1 
ATOM   1267 N  N   . ILE A 1 166 ? -7.522  -3.554  -4.191  1.00 16.88 ? 167 ILE A N   1 
ATOM   1268 C  CA  . ILE A 1 166 ? -6.493  -2.901  -3.389  1.00 16.99 ? 167 ILE A CA  1 
ATOM   1269 C  C   . ILE A 1 166 ? -5.495  -3.936  -2.891  1.00 15.32 ? 167 ILE A C   1 
ATOM   1270 O  O   . ILE A 1 166 ? -5.089  -3.965  -1.713  1.00 15.72 ? 167 ILE A O   1 
ATOM   1271 C  CB  . ILE A 1 166 ? -7.085  -2.055  -2.235  1.00 15.94 ? 167 ILE A CB  1 
ATOM   1272 C  CG1 . ILE A 1 166 ? -7.922  -2.920  -1.294  1.00 16.43 ? 167 ILE A CG1 1 
ATOM   1273 C  CG2 . ILE A 1 166 ? -7.880  -0.865  -2.775  1.00 16.20 ? 167 ILE A CG2 1 
ATOM   1274 C  CD1 . ILE A 1 166 ? -8.053  -2.285  0.087   1.00 15.84 ? 167 ILE A CD1 1 
ATOM   1275 N  N   . LYS A 1 167 ? -5.059  -4.843  -3.801  1.00 16.10 ? 168 LYS A N   1 
ATOM   1276 C  CA  . LYS A 1 167 ? -4.281  -5.990  -3.379  1.00 17.29 ? 168 LYS A CA  1 
ATOM   1277 C  C   . LYS A 1 167 ? -2.949  -5.565  -2.740  1.00 16.14 ? 168 LYS A C   1 
ATOM   1278 O  O   . LYS A 1 167 ? -2.525  -6.198  -1.769  1.00 17.39 ? 168 LYS A O   1 
ATOM   1279 C  CB  . LYS A 1 167 ? -3.991  -6.924  -4.557  1.00 20.90 ? 168 LYS A CB  1 
ATOM   1280 C  CG  . LYS A 1 167 ? -3.270  -8.205  -4.142  1.00 22.05 ? 168 LYS A CG  1 
ATOM   1281 C  CD  . LYS A 1 167 ? -3.055  -9.146  -5.323  1.00 28.39 ? 168 LYS A CD  1 
ATOM   1282 C  CE  . LYS A 1 167 ? -1.668  -9.743  -5.389  1.00 35.29 ? 168 LYS A CE  1 
ATOM   1283 N  NZ  . LYS A 1 167 ? -1.308  -10.072 -6.790  1.00 40.33 ? 168 LYS A NZ  1 
ATOM   1284 N  N   . THR A 1 168 ? -2.300  -4.522  -3.300  1.00 16.06 ? 169 THR A N   1 
ATOM   1285 C  CA  . THR A 1 168 ? -0.919  -4.239  -2.883  1.00 18.00 ? 169 THR A CA  1 
ATOM   1286 C  C   . THR A 1 168 ? -0.810  -2.865  -2.231  1.00 17.72 ? 169 THR A C   1 
ATOM   1287 O  O   . THR A 1 168 ? -1.683  -2.006  -2.336  1.00 16.89 ? 169 THR A O   1 
ATOM   1288 C  CB  . THR A 1 168 ? 0.036   -4.410  -4.077  1.00 20.87 ? 169 THR A CB  1 
ATOM   1289 O  OG1 . THR A 1 168 ? -0.598  -3.668  -5.110  1.00 20.75 ? 169 THR A OG1 1 
ATOM   1290 C  CG2 . THR A 1 168 ? 0.188   -5.864  -4.471  1.00 20.06 ? 169 THR A CG2 1 
ATOM   1291 N  N   . LYS A 1 169 ? 0.254   -2.706  -1.447  1.00 18.78 ? 170 LYS A N   1 
ATOM   1292 C  CA  . LYS A 1 169 ? 0.481   -1.498  -0.691  1.00 19.50 ? 170 LYS A CA  1 
ATOM   1293 C  C   . LYS A 1 169 ? 0.402   -0.282  -1.600  1.00 21.49 ? 170 LYS A C   1 
ATOM   1294 O  O   . LYS A 1 169 ? 0.979   -0.244  -2.696  1.00 21.59 ? 170 LYS A O   1 
ATOM   1295 C  CB  . LYS A 1 169 ? 1.885   -1.572  -0.091  1.00 20.46 ? 170 LYS A CB  1 
ATOM   1296 C  CG  . LYS A 1 169 ? 2.305   -0.312  0.638   1.00 22.16 ? 170 LYS A CG  1 
ATOM   1297 C  CD  . LYS A 1 169 ? 3.696   -0.429  1.216   1.00 25.72 ? 170 LYS A CD  1 
ATOM   1298 C  CE  . LYS A 1 169 ? 4.144   0.905   1.777   1.00 28.74 ? 170 LYS A CE  1 
ATOM   1299 N  NZ  . LYS A 1 169 ? 4.020   0.906   3.256   1.00 35.91 ? 170 LYS A NZ  1 
ATOM   1300 N  N   . GLY A 1 170 ? -0.361  0.696   -1.142  1.00 19.52 ? 171 GLY A N   1 
ATOM   1301 C  CA  . GLY A 1 170 ? -0.509  1.975   -1.802  1.00 18.52 ? 171 GLY A CA  1 
ATOM   1302 C  C   . GLY A 1 170 ? -1.723  2.062   -2.721  1.00 20.54 ? 171 GLY A C   1 
ATOM   1303 O  O   . GLY A 1 170 ? -2.022  3.149   -3.184  1.00 24.40 ? 171 GLY A O   1 
ATOM   1304 N  N   . LYS A 1 171 ? -2.421  0.938   -2.954  1.00 16.53 ? 172 LYS A N   1 
ATOM   1305 C  CA  . LYS A 1 171 ? -3.634  0.981   -3.771  1.00 17.29 ? 172 LYS A CA  1 
ATOM   1306 C  C   . LYS A 1 171 ? -4.836  1.429   -2.938  1.00 17.00 ? 172 LYS A C   1 
ATOM   1307 O  O   . LYS A 1 171 ? -4.966  1.072   -1.764  1.00 17.49 ? 172 LYS A O   1 
ATOM   1308 C  CB  . LYS A 1 171 ? -3.901  -0.384  -4.405  1.00 17.53 ? 172 LYS A CB  1 
ATOM   1309 C  CG  . LYS A 1 171 ? -2.865  -0.783  -5.469  1.00 22.03 ? 172 LYS A CG  1 
ATOM   1310 C  CD  . LYS A 1 171 ? -3.308  -1.977  -6.279  1.00 24.82 ? 172 LYS A CD  1 
ATOM   1311 C  CE  . LYS A 1 171 ? -4.359  -1.616  -7.315  1.00 29.07 ? 172 LYS A CE  1 
ATOM   1312 N  NZ  . LYS A 1 171 ? -4.551  -2.692  -8.322  1.00 33.31 ? 172 LYS A NZ  1 
ATOM   1313 N  N   . SER A 1 172 ? -5.730  2.183   -3.570  1.00 18.97 ? 173 SER A N   1 
ATOM   1314 C  CA  . SER A 1 172 ? -6.909  2.667   -2.883  1.00 17.12 ? 173 SER A CA  1 
ATOM   1315 C  C   . SER A 1 172 ? -8.037  2.755   -3.908  1.00 17.96 ? 173 SER A C   1 
ATOM   1316 O  O   . SER A 1 172 ? -7.824  2.684   -5.116  1.00 19.28 ? 173 SER A O   1 
ATOM   1317 C  CB  . SER A 1 172 ? -6.680  4.007   -2.195  1.00 19.74 ? 173 SER A CB  1 
ATOM   1318 O  OG  . SER A 1 172 ? -6.425  5.028   -3.153  1.00 22.16 ? 173 SER A OG  1 
ATOM   1319 N  N   . ALA A 1 173 ? -9.261  2.843   -3.399  1.00 17.89 ? 174 ALA A N   1 
ATOM   1320 C  CA  . ALA A 1 173 ? -10.433 2.990   -4.261  1.00 17.62 ? 174 ALA A CA  1 
ATOM   1321 C  C   . ALA A 1 173 ? -11.455 3.872   -3.548  1.00 19.82 ? 174 ALA A C   1 
ATOM   1322 O  O   . ALA A 1 173 ? -11.528 3.882   -2.312  1.00 18.03 ? 174 ALA A O   1 
ATOM   1323 C  CB  . ALA A 1 173 ? -11.014 1.618   -4.464  1.00 19.12 ? 174 ALA A CB  1 
ATOM   1324 N  N   . ASP A 1 174 ? -12.311 4.539   -4.314  1.00 19.46 ? 175 ASP A N   1 
ATOM   1325 C  CA  . ASP A 1 174 ? -13.447 5.174   -3.654  1.00 20.79 ? 175 ASP A CA  1 
ATOM   1326 C  C   . ASP A 1 174 ? -14.299 4.092   -2.985  1.00 18.66 ? 175 ASP A C   1 
ATOM   1327 O  O   . ASP A 1 174 ? -14.418 2.936   -3.419  1.00 18.69 ? 175 ASP A O   1 
ATOM   1328 C  CB  . ASP A 1 174 ? -14.290 6.019   -4.624  1.00 25.94 ? 175 ASP A CB  1 
ATOM   1329 C  CG  . ASP A 1 174 ? -13.511 7.104   -5.359  1.00 33.05 ? 175 ASP A CG  1 
ATOM   1330 O  OD1 . ASP A 1 174 ? -12.813 7.890   -4.693  1.00 43.17 ? 175 ASP A OD1 1 
ATOM   1331 O  OD2 . ASP A 1 174 ? -13.611 7.158   -6.615  1.00 43.88 ? 175 ASP A OD2 1 
ATOM   1332 N  N   . PHE A 1 175 ? -14.891 4.481   -1.849  1.00 16.49 ? 176 PHE A N   1 
ATOM   1333 C  CA  . PHE A 1 175 ? -15.673 3.488   -1.117  1.00 15.99 ? 176 PHE A CA  1 
ATOM   1334 C  C   . PHE A 1 175 ? -16.771 4.210   -0.346  1.00 17.34 ? 176 PHE A C   1 
ATOM   1335 O  O   . PHE A 1 175 ? -16.657 4.427   0.858   1.00 16.31 ? 176 PHE A O   1 
ATOM   1336 C  CB  . PHE A 1 175 ? -14.745 2.682   -0.200  1.00 16.02 ? 176 PHE A CB  1 
ATOM   1337 C  CG  . PHE A 1 175 ? -15.373 1.423   0.359   1.00 14.92 ? 176 PHE A CG  1 
ATOM   1338 C  CD1 . PHE A 1 175 ? -15.706 0.365   -0.476  1.00 18.01 ? 176 PHE A CD1 1 
ATOM   1339 C  CD2 . PHE A 1 175 ? -15.642 1.286   1.722   1.00 15.04 ? 176 PHE A CD2 1 
ATOM   1340 C  CE1 . PHE A 1 175 ? -16.236 -0.830  0.025   1.00 15.41 ? 176 PHE A CE1 1 
ATOM   1341 C  CE2 . PHE A 1 175 ? -16.204 0.110   2.218   1.00 15.60 ? 176 PHE A CE2 1 
ATOM   1342 C  CZ  . PHE A 1 175 ? -16.470 -0.953  1.384   1.00 17.33 ? 176 PHE A CZ  1 
ATOM   1343 N  N   . THR A 1 176 ? -17.848 4.573   -1.044  1.00 16.51 ? 177 THR A N   1 
ATOM   1344 C  CA  . THR A 1 176 ? -18.916 5.335   -0.431  1.00 15.72 ? 177 THR A CA  1 
ATOM   1345 C  C   . THR A 1 176 ? -20.111 4.472   -0.033  1.00 14.18 ? 177 THR A C   1 
ATOM   1346 O  O   . THR A 1 176 ? -20.247 3.319   -0.453  1.00 17.84 ? 177 THR A O   1 
ATOM   1347 C  CB  . THR A 1 176 ? -19.387 6.442   -1.360  1.00 18.68 ? 177 THR A CB  1 
ATOM   1348 O  OG1 . THR A 1 176 ? -19.932 5.881   -2.554  1.00 20.34 ? 177 THR A OG1 1 
ATOM   1349 C  CG2 . THR A 1 176 ? -18.268 7.398   -1.697  1.00 20.58 ? 177 THR A CG2 1 
ATOM   1350 N  N   . ASN A 1 177 ? -20.923 5.048   0.854   1.00 15.39 ? 178 ASN A N   1 
ATOM   1351 C  CA  . ASN A 1 177 ? -22.177 4.486   1.301   1.00 15.66 ? 178 ASN A CA  1 
ATOM   1352 C  C   . ASN A 1 177 ? -21.948 3.147   1.991   1.00 17.86 ? 178 ASN A C   1 
ATOM   1353 O  O   . ASN A 1 177 ? -22.863 2.337   1.975   1.00 20.57 ? 178 ASN A O   1 
ATOM   1354 C  CB  . ASN A 1 177 ? -23.147 4.344   0.115   1.00 16.21 ? 178 ASN A CB  1 
ATOM   1355 C  CG  . ASN A 1 177 ? -23.480 5.727   -0.419  1.00 16.78 ? 178 ASN A CG  1 
ATOM   1356 O  OD1 . ASN A 1 177 ? -24.198 6.470   0.216   1.00 19.84 ? 178 ASN A OD1 1 
ATOM   1357 N  ND2 . ASN A 1 177 ? -22.890 6.092   -1.532  1.00 17.76 ? 178 ASN A ND2 1 
ATOM   1358 N  N   . PHE A 1 178 ? -20.798 2.964   2.669   1.00 16.74 ? 179 PHE A N   1 
ATOM   1359 C  CA  . PHE A 1 178 ? -20.664 1.785   3.500   1.00 16.67 ? 179 PHE A CA  1 
ATOM   1360 C  C   . PHE A 1 178 ? -21.160 2.094   4.913   1.00 15.78 ? 179 PHE A C   1 
ATOM   1361 O  O   . PHE A 1 178 ? -20.706 3.062   5.518   1.00 17.01 ? 179 PHE A O   1 
ATOM   1362 C  CB  . PHE A 1 178 ? -19.195 1.331   3.568   1.00 16.15 ? 179 PHE A CB  1 
ATOM   1363 C  CG  . PHE A 1 178 ? -19.067 0.112   4.440   1.00 14.48 ? 179 PHE A CG  1 
ATOM   1364 C  CD1 . PHE A 1 178 ? -19.458 -1.137  3.968   1.00 16.35 ? 179 PHE A CD1 1 
ATOM   1365 C  CD2 . PHE A 1 178 ? -18.734 0.264   5.787   1.00 15.38 ? 179 PHE A CD2 1 
ATOM   1366 C  CE1 . PHE A 1 178 ? -19.424 -2.233  4.803   1.00 16.69 ? 179 PHE A CE1 1 
ATOM   1367 C  CE2 . PHE A 1 178 ? -18.725 -0.840  6.625   1.00 15.96 ? 179 PHE A CE2 1 
ATOM   1368 C  CZ  . PHE A 1 178 ? -19.054 -2.077  6.138   1.00 15.60 ? 179 PHE A CZ  1 
ATOM   1369 N  N   . ASP A 1 179 ? -22.093 1.279   5.419   1.00 13.59 ? 180 ASP A N   1 
ATOM   1370 C  CA  . ASP A 1 179 ? -22.688 1.465   6.729   1.00 14.39 ? 180 ASP A CA  1 
ATOM   1371 C  C   . ASP A 1 179 ? -21.964 0.656   7.792   1.00 14.88 ? 180 ASP A C   1 
ATOM   1372 O  O   . ASP A 1 179 ? -22.181 -0.565  7.893   1.00 13.42 ? 180 ASP A O   1 
ATOM   1373 C  CB  . ASP A 1 179 ? -24.169 1.088   6.632   1.00 17.12 ? 180 ASP A CB  1 
ATOM   1374 C  CG  . ASP A 1 179 ? -24.925 1.459   7.894   1.00 18.61 ? 180 ASP A CG  1 
ATOM   1375 O  OD1 . ASP A 1 179 ? -24.283 1.805   8.883   1.00 18.49 ? 180 ASP A OD1 1 
ATOM   1376 O  OD2 . ASP A 1 179 ? -26.178 1.448   7.835   1.00 23.64 ? 180 ASP A OD2 1 
ATOM   1377 N  N   . PRO A 1 180 ? -21.169 1.269   8.693   1.00 14.31 ? 181 PRO A N   1 
ATOM   1378 C  CA  . PRO A 1 180 ? -20.463 0.485   9.706   1.00 15.89 ? 181 PRO A CA  1 
ATOM   1379 C  C   . PRO A 1 180 ? -21.376 -0.110  10.775  1.00 15.19 ? 181 PRO A C   1 
ATOM   1380 O  O   . PRO A 1 180 ? -20.958 -1.015  11.506  1.00 15.28 ? 181 PRO A O   1 
ATOM   1381 C  CB  . PRO A 1 180 ? -19.478 1.479   10.291  1.00 14.76 ? 181 PRO A CB  1 
ATOM   1382 C  CG  . PRO A 1 180 ? -20.184 2.813   10.141  1.00 15.91 ? 181 PRO A CG  1 
ATOM   1383 C  CD  . PRO A 1 180 ? -20.835 2.707   8.752   1.00 14.25 ? 181 PRO A CD  1 
ATOM   1384 N  N   . ARG A 1 181 ? -22.654 0.277   10.779  1.00 15.64 ? 182 ARG A N   1 
ATOM   1385 C  CA  . ARG A 1 181 ? -23.580 -0.385  11.706  1.00 16.47 ? 182 ARG A CA  1 
ATOM   1386 C  C   . ARG A 1 181 ? -23.691 -1.867  11.384  1.00 15.35 ? 182 ARG A C   1 
ATOM   1387 O  O   . ARG A 1 181 ? -24.090 -2.672  12.229  1.00 17.64 ? 182 ARG A O   1 
ATOM   1388 C  CB  . ARG A 1 181 ? -24.953 0.298   11.695  1.00 16.96 ? 182 ARG A CB  1 
ATOM   1389 C  CG  . ARG A 1 181 ? -24.918 1.700   12.282  1.00 19.67 ? 182 ARG A CG  1 
ATOM   1390 C  CD  . ARG A 1 181 ? -26.230 2.416   12.158  1.00 18.86 ? 182 ARG A CD  1 
ATOM   1391 N  NE  . ARG A 1 181 ? -26.602 2.600   10.773  1.00 18.55 ? 182 ARG A NE  1 
ATOM   1392 C  CZ  . ARG A 1 181 ? -27.591 3.384   10.347  1.00 20.84 ? 182 ARG A CZ  1 
ATOM   1393 N  NH1 . ARG A 1 181 ? -28.349 4.010   11.237  1.00 22.80 ? 182 ARG A NH1 1 
ATOM   1394 N  NH2 . ARG A 1 181 ? -27.841 3.510   9.049   1.00 21.48 ? 182 ARG A NH2 1 
ATOM   1395 N  N   . GLY A 1 182 ? -23.431 -2.245  10.122  1.00 13.64 ? 183 GLY A N   1 
ATOM   1396 C  CA  . GLY A 1 182 ? -23.590 -3.641  9.701   1.00 14.40 ? 183 GLY A CA  1 
ATOM   1397 C  C   . GLY A 1 182 ? -22.442 -4.546  10.144  1.00 15.34 ? 183 GLY A C   1 
ATOM   1398 O  O   . GLY A 1 182 ? -22.452 -5.755  9.830   1.00 15.65 ? 183 GLY A O   1 
ATOM   1399 N  N   . LEU A 1 183 ? -21.493 -3.982  10.918  1.00 15.45 ? 184 LEU A N   1 
ATOM   1400 C  CA  . LEU A 1 183 ? -20.381 -4.751  11.466  1.00 14.48 ? 184 LEU A CA  1 
ATOM   1401 C  C   . LEU A 1 183 ? -20.521 -4.932  12.979  1.00 15.31 ? 184 LEU A C   1 
ATOM   1402 O  O   . LEU A 1 183 ? -19.627 -5.513  13.590  1.00 15.93 ? 184 LEU A O   1 
ATOM   1403 C  CB  . LEU A 1 183 ? -19.088 -3.961  11.187  1.00 15.53 ? 184 LEU A CB  1 
ATOM   1404 C  CG  . LEU A 1 183 ? -18.776 -3.803  9.704   1.00 15.40 ? 184 LEU A CG  1 
ATOM   1405 C  CD1 . LEU A 1 183 ? -17.521 -2.953  9.542   1.00 16.13 ? 184 LEU A CD1 1 
ATOM   1406 C  CD2 . LEU A 1 183 ? -18.662 -5.151  9.004   1.00 18.06 ? 184 LEU A CD2 1 
ATOM   1407 N  N   . LEU A 1 184 ? -21.607 -4.425  13.582  1.00 13.74 ? 185 LEU A N   1 
ATOM   1408 C  CA  . LEU A 1 184 ? -21.685 -4.478  15.042  1.00 14.70 ? 185 LEU A CA  1 
ATOM   1409 C  C   . LEU A 1 184 ? -22.440 -5.730  15.454  1.00 15.68 ? 185 LEU A C   1 
ATOM   1410 O  O   . LEU A 1 184 ? -23.453 -6.065  14.821  1.00 19.14 ? 185 LEU A O   1 
ATOM   1411 C  CB  . LEU A 1 184 ? -22.468 -3.268  15.546  1.00 14.75 ? 185 LEU A CB  1 
ATOM   1412 C  CG  . LEU A 1 184 ? -21.838 -1.935  15.153  1.00 15.13 ? 185 LEU A CG  1 
ATOM   1413 C  CD1 . LEU A 1 184 ? -22.715 -0.801  15.677  1.00 15.84 ? 185 LEU A CD1 1 
ATOM   1414 C  CD2 . LEU A 1 184 ? -20.439 -1.827  15.759  1.00 17.22 ? 185 LEU A CD2 1 
ATOM   1415 N  N   . PRO A 1 185 ? -22.068 -6.356  16.594  1.00 15.51 ? 186 PRO A N   1 
ATOM   1416 C  CA  . PRO A 1 185 ? -22.854 -7.459  17.160  1.00 14.42 ? 186 PRO A CA  1 
ATOM   1417 C  C   . PRO A 1 185 ? -24.112 -6.928  17.868  1.00 13.34 ? 186 PRO A C   1 
ATOM   1418 O  O   . PRO A 1 185 ? -24.291 -5.719  18.024  1.00 14.65 ? 186 PRO A O   1 
ATOM   1419 C  CB  . PRO A 1 185 ? -21.856 -8.024  18.199  1.00 15.06 ? 186 PRO A CB  1 
ATOM   1420 C  CG  . PRO A 1 185 ? -21.117 -6.815  18.656  1.00 14.61 ? 186 PRO A CG  1 
ATOM   1421 C  CD  . PRO A 1 185 ? -20.867 -6.019  17.379  1.00 14.20 ? 186 PRO A CD  1 
ATOM   1422 N  N   . GLU A 1 186 ? -24.977 -7.828  18.342  1.00 16.75 ? 187 GLU A N   1 
ATOM   1423 C  CA  . GLU A 1 186 ? -26.224 -7.405  18.982  1.00 18.55 ? 187 GLU A CA  1 
ATOM   1424 C  C   . GLU A 1 186 ? -25.962 -6.630  20.269  1.00 18.63 ? 187 GLU A C   1 
ATOM   1425 O  O   . GLU A 1 186 ? -26.613 -5.620  20.539  1.00 20.69 ? 187 GLU A O   1 
ATOM   1426 C  CB  . GLU A 1 186 ? -27.055 -8.612  19.417  1.00 21.35 ? 187 GLU A CB  1 
ATOM   1427 C  CG  . GLU A 1 186 ? -27.682 -9.388  18.274  1.00 26.14 ? 187 GLU A CG  1 
ATOM   1428 C  CD  . GLU A 1 186 ? -28.467 -10.616 18.753  1.00 29.93 ? 187 GLU A CD  1 
ATOM   1429 O  OE1 . GLU A 1 186 ? -28.501 -10.861 19.960  1.00 26.38 ? 187 GLU A OE1 1 
ATOM   1430 O  OE2 . GLU A 1 186 ? -29.085 -11.289 17.909  1.00 36.22 ? 187 GLU A OE2 1 
ATOM   1431 N  N   . SER A 1 187 ? -24.990 -7.092  21.063  1.00 17.47 ? 188 SER A N   1 
ATOM   1432 C  CA  . SER A 1 187 ? -24.808 -6.532  22.393  1.00 18.47 ? 188 SER A CA  1 
ATOM   1433 C  C   . SER A 1 187 ? -23.740 -5.440  22.342  1.00 19.28 ? 188 SER A C   1 
ATOM   1434 O  O   . SER A 1 187 ? -22.741 -5.623  21.638  1.00 17.72 ? 188 SER A O   1 
ATOM   1435 C  CB  . SER A 1 187 ? -24.420 -7.609  23.389  1.00 19.86 ? 188 SER A CB  1 
ATOM   1436 O  OG  . SER A 1 187 ? -24.214 -7.080  24.695  1.00 19.15 ? 188 SER A OG  1 
ATOM   1437 N  N   . LEU A 1 188 ? -23.927 -4.378  23.146  1.00 16.57 ? 189 LEU A N   1 
ATOM   1438 C  CA  . LEU A 1 188 ? -22.858 -3.402  23.323  1.00 16.10 ? 189 LEU A CA  1 
ATOM   1439 C  C   . LEU A 1 188 ? -22.224 -3.570  24.701  1.00 16.22 ? 189 LEU A C   1 
ATOM   1440 O  O   . LEU A 1 188 ? -21.566 -2.634  25.138  1.00 19.01 ? 189 LEU A O   1 
ATOM   1441 C  CB  . LEU A 1 188 ? -23.339 -1.946  23.166  1.00 16.93 ? 189 LEU A CB  1 
ATOM   1442 C  CG  . LEU A 1 188 ? -23.802 -1.580  21.753  1.00 17.57 ? 189 LEU A CG  1 
ATOM   1443 C  CD1 . LEU A 1 188 ? -24.273 -0.135  21.688  1.00 19.38 ? 189 LEU A CD1 1 
ATOM   1444 C  CD2 . LEU A 1 188 ? -22.684 -1.826  20.729  1.00 20.51 ? 189 LEU A CD2 1 
ATOM   1445 N  N   . ASP A 1 189 ? -22.364 -4.737  25.340  1.00 17.56 ? 190 ASP A N   1 
ATOM   1446 C  CA  . ASP A 1 189 ? -21.623 -4.900  26.600  1.00 16.85 ? 190 ASP A CA  1 
ATOM   1447 C  C   . ASP A 1 189 ? -20.125 -4.863  26.289  1.00 16.98 ? 190 ASP A C   1 
ATOM   1448 O  O   . ASP A 1 189 ? -19.696 -5.329  25.228  1.00 16.16 ? 190 ASP A O   1 
ATOM   1449 C  CB  . ASP A 1 189 ? -21.960 -6.230  27.269  1.00 18.36 ? 190 ASP A CB  1 
ATOM   1450 C  CG  . ASP A 1 189 ? -23.355 -6.275  27.911  1.00 19.75 ? 190 ASP A CG  1 
ATOM   1451 O  OD1 . ASP A 1 189 ? -24.010 -5.249  28.012  1.00 26.78 ? 190 ASP A OD1 1 
ATOM   1452 O  OD2 . ASP A 1 189 ? -23.771 -7.345  28.215  1.00 25.69 ? 190 ASP A OD2 1 
ATOM   1453 N  N   . TYR A 1 190 ? -19.320 -4.350  27.231  1.00 15.62 ? 191 TYR A N   1 
ATOM   1454 C  CA  . TYR A 1 190 ? -17.938 -4.048  26.877  1.00 14.82 ? 191 TYR A CA  1 
ATOM   1455 C  C   . TYR A 1 190 ? -17.031 -4.124  28.103  1.00 13.18 ? 191 TYR A C   1 
ATOM   1456 O  O   . TYR A 1 190 ? -17.483 -4.017  29.236  1.00 15.08 ? 191 TYR A O   1 
ATOM   1457 C  CB  . TYR A 1 190 ? -17.822 -2.676  26.178  1.00 14.08 ? 191 TYR A CB  1 
ATOM   1458 C  CG  . TYR A 1 190 ? -18.174 -1.487  27.038  1.00 16.09 ? 191 TYR A CG  1 
ATOM   1459 C  CD1 . TYR A 1 190 ? -17.269 -0.933  27.944  1.00 16.23 ? 191 TYR A CD1 1 
ATOM   1460 C  CD2 . TYR A 1 190 ? -19.444 -0.931  26.978  1.00 15.63 ? 191 TYR A CD2 1 
ATOM   1461 C  CE1 . TYR A 1 190 ? -17.613 0.166   28.735  1.00 16.04 ? 191 TYR A CE1 1 
ATOM   1462 C  CE2 . TYR A 1 190 ? -19.803 0.155   27.760  1.00 15.67 ? 191 TYR A CE2 1 
ATOM   1463 C  CZ  . TYR A 1 190 ? -18.900 0.686   28.679  1.00 17.73 ? 191 TYR A CZ  1 
ATOM   1464 O  OH  . TYR A 1 190 ? -19.324 1.737   29.441  1.00 17.34 ? 191 TYR A OH  1 
ATOM   1465 N  N   . TRP A 1 191 ? -15.750 -4.308  27.810  1.00 14.37 ? 192 TRP A N   1 
ATOM   1466 C  CA  . TRP A 1 191 ? -14.658 -4.043  28.741  1.00 11.99 ? 192 TRP A CA  1 
ATOM   1467 C  C   . TRP A 1 191 ? -13.992 -2.745  28.294  1.00 13.64 ? 192 TRP A C   1 
ATOM   1468 O  O   . TRP A 1 191 ? -13.934 -2.442  27.108  1.00 15.45 ? 192 TRP A O   1 
ATOM   1469 C  CB  . TRP A 1 191 ? -13.639 -5.165  28.665  1.00 13.61 ? 192 TRP A CB  1 
ATOM   1470 C  CG  . TRP A 1 191 ? -14.148 -6.512  29.082  1.00 16.25 ? 192 TRP A CG  1 
ATOM   1471 C  CD1 . TRP A 1 191 ? -14.456 -6.939  30.351  1.00 15.66 ? 192 TRP A CD1 1 
ATOM   1472 C  CD2 . TRP A 1 191 ? -14.396 -7.612  28.201  1.00 16.28 ? 192 TRP A CD2 1 
ATOM   1473 N  NE1 . TRP A 1 191 ? -14.896 -8.237  30.300  1.00 18.01 ? 192 TRP A NE1 1 
ATOM   1474 C  CE2 . TRP A 1 191 ? -14.895 -8.671  28.992  1.00 18.53 ? 192 TRP A CE2 1 
ATOM   1475 C  CE3 . TRP A 1 191 ? -14.289 -7.784  26.808  1.00 15.94 ? 192 TRP A CE3 1 
ATOM   1476 C  CZ2 . TRP A 1 191 ? -15.198 -9.922  28.445  1.00 16.73 ? 192 TRP A CZ2 1 
ATOM   1477 C  CZ3 . TRP A 1 191 ? -14.599 -9.015  26.277  1.00 18.16 ? 192 TRP A CZ3 1 
ATOM   1478 C  CH2 . TRP A 1 191 ? -15.057 -10.070 27.075  1.00 18.16 ? 192 TRP A CH2 1 
ATOM   1479 N  N   . THR A 1 192 ? -13.379 -2.039  29.241  1.00 13.15 ? 193 THR A N   1 
ATOM   1480 C  CA  . THR A 1 192 ? -12.708 -0.782  28.927  1.00 12.81 ? 193 THR A CA  1 
ATOM   1481 C  C   . THR A 1 192 ? -11.444 -0.627  29.768  1.00 14.49 ? 193 THR A C   1 
ATOM   1482 O  O   . THR A 1 192 ? -11.415 -0.985  30.929  1.00 15.48 ? 193 THR A O   1 
ATOM   1483 C  CB  . THR A 1 192 ? -13.640 0.428   29.017  1.00 13.97 ? 193 THR A CB  1 
ATOM   1484 O  OG1 . THR A 1 192 ? -12.931 1.599   28.613  1.00 14.53 ? 193 THR A OG1 1 
ATOM   1485 C  CG2 . THR A 1 192 ? -14.168 0.700   30.424  1.00 15.05 ? 193 THR A CG2 1 
ATOM   1486 N  N   . TYR A 1 193 ? -10.378 -0.151  29.145  1.00 13.27 ? 194 TYR A N   1 
ATOM   1487 C  CA  . TYR A 1 193 ? -9.151  0.137   29.893  1.00 14.39 ? 194 TYR A CA  1 
ATOM   1488 C  C   . TYR A 1 193 ? -8.383  1.216   29.132  1.00 13.61 ? 194 TYR A C   1 
ATOM   1489 O  O   . TYR A 1 193 ? -8.592  1.406   27.908  1.00 13.79 ? 194 TYR A O   1 
ATOM   1490 C  CB  . TYR A 1 193 ? -8.325  -1.132  30.134  1.00 13.91 ? 194 TYR A CB  1 
ATOM   1491 C  CG  . TYR A 1 193 ? -7.648  -1.598  28.876  1.00 14.60 ? 194 TYR A CG  1 
ATOM   1492 C  CD1 . TYR A 1 193 ? -8.362  -2.298  27.883  1.00 13.61 ? 194 TYR A CD1 1 
ATOM   1493 C  CD2 . TYR A 1 193 ? -6.333  -1.242  28.643  1.00 15.40 ? 194 TYR A CD2 1 
ATOM   1494 C  CE1 . TYR A 1 193 ? -7.754  -2.655  26.686  1.00 12.96 ? 194 TYR A CE1 1 
ATOM   1495 C  CE2 . TYR A 1 193 ? -5.718  -1.599  27.443  1.00 14.22 ? 194 TYR A CE2 1 
ATOM   1496 C  CZ  . TYR A 1 193 ? -6.422  -2.313  26.489  1.00 13.96 ? 194 TYR A CZ  1 
ATOM   1497 O  OH  . TYR A 1 193 ? -5.739  -2.582  25.331  1.00 14.09 ? 194 TYR A OH  1 
ATOM   1498 N  N   . PRO A 1 194 ? -7.433  1.921   29.791  1.00 14.02 ? 195 PRO A N   1 
ATOM   1499 C  CA  . PRO A 1 194 ? -6.608  2.926   29.134  1.00 14.42 ? 195 PRO A CA  1 
ATOM   1500 C  C   . PRO A 1 194 ? -5.383  2.275   28.501  1.00 13.64 ? 195 PRO A C   1 
ATOM   1501 O  O   . PRO A 1 194 ? -4.638  1.566   29.172  1.00 14.79 ? 195 PRO A O   1 
ATOM   1502 C  CB  . PRO A 1 194 ? -6.129  3.866   30.257  1.00 16.68 ? 195 PRO A CB  1 
ATOM   1503 C  CG  . PRO A 1 194 ? -6.228  3.030   31.521  1.00 16.87 ? 195 PRO A CG  1 
ATOM   1504 C  CD  . PRO A 1 194 ? -7.269  1.940   31.271  1.00 14.45 ? 195 PRO A CD  1 
ATOM   1505 N  N   . GLY A 1 195 ? -5.179  2.526   27.208  1.00 12.83 ? 196 GLY A N   1 
ATOM   1506 C  CA  . GLY A 1 195 ? -4.051  1.910   26.519  1.00 14.06 ? 196 GLY A CA  1 
ATOM   1507 C  C   . GLY A 1 195 ? -3.489  2.784   25.402  1.00 13.97 ? 196 GLY A C   1 
ATOM   1508 O  O   . GLY A 1 195 ? -3.408  4.008   25.550  1.00 12.30 ? 196 GLY A O   1 
ATOM   1509 N  N   . SER A 1 196 ? -3.099  2.143   24.278  1.00 13.88 ? 197 SER A N   1 
ATOM   1510 C  CA  . SER A 1 196 ? -2.258  2.806   23.274  1.00 13.78 ? 197 SER A CA  1 
ATOM   1511 C  C   . SER A 1 196 ? -2.751  2.407   21.889  1.00 12.83 ? 197 SER A C   1 
ATOM   1512 O  O   . SER A 1 196 ? -3.492  1.431   21.722  1.00 13.25 ? 197 SER A O   1 
ATOM   1513 C  CB  . SER A 1 196 ? -0.821  2.373   23.359  1.00 13.44 ? 197 SER A CB  1 
ATOM   1514 O  OG  . SER A 1 196 ? -0.655  1.001   23.030  1.00 14.20 ? 197 SER A OG  1 
ATOM   1515 N  N   . LEU A 1 197 ? -2.217  3.089   20.898  1.00 13.49 ? 198 LEU A N   1 
ATOM   1516 C  CA  . LEU A 1 197 ? -2.242  2.534   19.560  1.00 14.54 ? 198 LEU A CA  1 
ATOM   1517 C  C   . LEU A 1 197 ? -1.461  1.211   19.558  1.00 14.17 ? 198 LEU A C   1 
ATOM   1518 O  O   . LEU A 1 197 ? -0.512  1.032   20.325  1.00 13.73 ? 198 LEU A O   1 
ATOM   1519 C  CB  . LEU A 1 197 ? -1.544  3.521   18.628  1.00 16.55 ? 198 LEU A CB  1 
ATOM   1520 C  CG  . LEU A 1 197 ? -2.222  4.884   18.518  1.00 17.27 ? 198 LEU A CG  1 
ATOM   1521 C  CD1 . LEU A 1 197 ? -1.359  5.735   17.596  1.00 19.75 ? 198 LEU A CD1 1 
ATOM   1522 C  CD2 . LEU A 1 197 ? -3.645  4.759   17.959  1.00 18.32 ? 198 LEU A CD2 1 
ATOM   1523 N  N   . THR A 1 198 ? -1.903  0.263   18.714  1.00 13.03 ? 199 THR A N   1 
ATOM   1524 C  CA  . THR A 1 198 ? -1.207  -1.025  18.645  1.00 13.36 ? 199 THR A CA  1 
ATOM   1525 C  C   . THR A 1 198 ? -0.247  -1.121  17.456  1.00 13.18 ? 199 THR A C   1 
ATOM   1526 O  O   . THR A 1 198 ? 0.376   -2.160  17.274  1.00 13.04 ? 199 THR A O   1 
ATOM   1527 C  CB  . THR A 1 198 ? -2.171  -2.202  18.606  1.00 11.39 ? 199 THR A CB  1 
ATOM   1528 O  OG1 . THR A 1 198 ? -2.835  -2.172  17.337  1.00 11.67 ? 199 THR A OG1 1 
ATOM   1529 C  CG2 . THR A 1 198 ? -3.193  -2.152  19.712  1.00 11.81 ? 199 THR A CG2 1 
ATOM   1530 N  N   . THR A 1 199 ? -0.114  -0.026  16.711  1.00 15.48 ? 200 THR A N   1 
ATOM   1531 C  CA  . THR A 1 199 ? 0.921   0.117   15.707  1.00 15.25 ? 200 THR A CA  1 
ATOM   1532 C  C   . THR A 1 199 ? 1.755   1.358   16.017  1.00 15.41 ? 200 THR A C   1 
ATOM   1533 O  O   . THR A 1 199 ? 1.261   2.283   16.670  1.00 13.69 ? 200 THR A O   1 
ATOM   1534 C  CB  . THR A 1 199 ? 0.299   0.330   14.313  1.00 17.67 ? 200 THR A CB  1 
ATOM   1535 O  OG1 . THR A 1 199 ? -0.681  1.373   14.397  1.00 20.56 ? 200 THR A OG1 1 
ATOM   1536 C  CG2 . THR A 1 199 ? -0.335  -0.931  13.777  1.00 17.49 ? 200 THR A CG2 1 
ATOM   1537 N  N   . PRO A 1 200 ? 3.034   1.389   15.576  1.00 14.68 ? 201 PRO A N   1 
ATOM   1538 C  CA  . PRO A 1 200 ? 3.854   2.608   15.651  1.00 15.31 ? 201 PRO A CA  1 
ATOM   1539 C  C   . PRO A 1 200 ? 3.013   3.789   15.183  1.00 16.39 ? 201 PRO A C   1 
ATOM   1540 O  O   . PRO A 1 200 ? 2.277   3.718   14.162  1.00 17.64 ? 201 PRO A O   1 
ATOM   1541 C  CB  . PRO A 1 200 ? 5.002   2.249   14.673  1.00 15.09 ? 201 PRO A CB  1 
ATOM   1542 C  CG  . PRO A 1 200 ? 5.198   0.781   14.906  1.00 14.97 ? 201 PRO A CG  1 
ATOM   1543 C  CD  . PRO A 1 200 ? 3.765   0.263   14.959  1.00 15.30 ? 201 PRO A CD  1 
ATOM   1544 N  N   . PRO A 1 201 ? 3.053   4.932   15.893  1.00 16.67 ? 202 PRO A N   1 
ATOM   1545 C  CA  . PRO A 1 201 ? 4.034   5.184   16.964  1.00 15.46 ? 202 PRO A CA  1 
ATOM   1546 C  C   . PRO A 1 201 ? 3.646   4.795   18.393  1.00 14.55 ? 202 PRO A C   1 
ATOM   1547 O  O   . PRO A 1 201 ? 4.316   5.180   19.360  1.00 16.60 ? 202 PRO A O   1 
ATOM   1548 C  CB  . PRO A 1 201 ? 4.162   6.724   16.863  1.00 17.67 ? 202 PRO A CB  1 
ATOM   1549 C  CG  . PRO A 1 201 ? 2.774   7.170   16.513  1.00 22.66 ? 202 PRO A CG  1 
ATOM   1550 C  CD  . PRO A 1 201 ? 2.254   6.117   15.568  1.00 18.90 ? 202 PRO A CD  1 
ATOM   1551 N  N   . LEU A 1 202 ? 2.585   3.979   18.534  1.00 15.89 ? 203 LEU A N   1 
ATOM   1552 C  CA  . LEU A 1 202 ? 2.247   3.376   19.828  1.00 14.40 ? 203 LEU A CA  1 
ATOM   1553 C  C   . LEU A 1 202 ? 1.877   4.403   20.897  1.00 15.12 ? 203 LEU A C   1 
ATOM   1554 O  O   . LEU A 1 202 ? 2.005   4.106   22.087  1.00 15.43 ? 203 LEU A O   1 
ATOM   1555 C  CB  . LEU A 1 202 ? 3.357   2.435   20.318  1.00 14.72 ? 203 LEU A CB  1 
ATOM   1556 C  CG  . LEU A 1 202 ? 3.795   1.356   19.298  1.00 13.83 ? 203 LEU A CG  1 
ATOM   1557 C  CD1 . LEU A 1 202 ? 5.100   0.745   19.790  1.00 14.61 ? 203 LEU A CD1 1 
ATOM   1558 C  CD2 . LEU A 1 202 ? 2.697   0.295   19.191  1.00 14.04 ? 203 LEU A CD2 1 
ATOM   1559 N  N   . ASN A 1 203 ? 1.362   5.572   20.491  1.00 17.02 ? 204 ASN A N   1 
ATOM   1560 C  CA  . ASN A 1 203 ? 0.976   6.626   21.411  1.00 17.13 ? 204 ASN A CA  1 
ATOM   1561 C  C   . ASN A 1 203 ? 0.010   6.105   22.470  1.00 16.98 ? 204 ASN A C   1 
ATOM   1562 O  O   . ASN A 1 203 ? -0.958  5.412   22.158  1.00 15.65 ? 204 ASN A O   1 
ATOM   1563 C  CB  . ASN A 1 203 ? 0.353   7.782   20.625  1.00 19.41 ? 204 ASN A CB  1 
ATOM   1564 C  CG  . ASN A 1 203 ? 1.342   8.448   19.694  1.00 24.95 ? 204 ASN A CG  1 
ATOM   1565 O  OD1 . ASN A 1 203 ? 2.514   8.076   19.637  1.00 29.67 ? 204 ASN A OD1 1 
ATOM   1566 N  ND2 . ASN A 1 203 ? 0.901   9.511   19.034  1.00 28.07 ? 204 ASN A ND2 1 
ATOM   1567 N  N   . GLU A 1 204 ? 0.266   6.501   23.727  1.00 15.63 ? 205 GLU A N   1 
ATOM   1568 C  CA  . GLU A 1 204 ? -0.600  6.158   24.842  1.00 15.53 ? 205 GLU A CA  1 
ATOM   1569 C  C   . GLU A 1 204 ? -1.756  7.147   24.937  1.00 15.96 ? 205 GLU A C   1 
ATOM   1570 O  O   . GLU A 1 204 ? -1.847  7.908   25.879  1.00 19.33 ? 205 GLU A O   1 
ATOM   1571 C  CB  . GLU A 1 204 ? 0.304   6.060   26.067  1.00 15.02 ? 205 GLU A CB  1 
ATOM   1572 C  CG  . GLU A 1 204 ? 1.138   4.794   26.004  1.00 16.55 ? 205 GLU A CG  1 
ATOM   1573 C  CD  . GLU A 1 204 ? 2.039   4.529   27.186  1.00 16.44 ? 205 GLU A CD  1 
ATOM   1574 O  OE1 . GLU A 1 204 ? 2.344   5.482   27.916  1.00 21.64 ? 205 GLU A OE1 1 
ATOM   1575 O  OE2 . GLU A 1 204 ? 2.433   3.357   27.342  1.00 17.51 ? 205 GLU A OE2 1 
ATOM   1576 N  N   . CYS A 1 205 ? -2.716  7.046   24.008  1.00 14.51 ? 206 CYS A N   1 
ATOM   1577 C  CA  . CYS A 1 205 ? -3.719  8.078   23.836  1.00 14.70 ? 206 CYS A CA  1 
ATOM   1578 C  C   . CYS A 1 205 ? -5.116  7.492   23.672  1.00 13.98 ? 206 CYS A C   1 
ATOM   1579 O  O   . CYS A 1 205 ? -6.045  8.199   23.276  1.00 16.06 ? 206 CYS A O   1 
ATOM   1580 C  CB  . CYS A 1 205 ? -3.386  8.915   22.597  1.00 16.21 ? 206 CYS A CB  1 
ATOM   1581 S  SG  . CYS A 1 205 ? -3.353  7.983   21.024  1.00 17.52 ? 206 CYS A SG  1 
ATOM   1582 N  N   . VAL A 1 206 ? -5.243  6.176   23.914  1.00 13.55 ? 207 VAL A N   1 
ATOM   1583 C  CA  . VAL A 1 206 ? -6.465  5.460   23.557  1.00 13.89 ? 207 VAL A CA  1 
ATOM   1584 C  C   . VAL A 1 206 ? -7.259  5.031   24.801  1.00 14.51 ? 207 VAL A C   1 
ATOM   1585 O  O   . VAL A 1 206 ? -6.680  4.437   25.719  1.00 16.36 ? 207 VAL A O   1 
ATOM   1586 C  CB  . VAL A 1 206 ? -6.162  4.207   22.723  1.00 14.12 ? 207 VAL A CB  1 
ATOM   1587 C  CG1 . VAL A 1 206 ? -7.461  3.438   22.394  1.00 14.42 ? 207 VAL A CG1 1 
ATOM   1588 C  CG2 . VAL A 1 206 ? -5.420  4.520   21.425  1.00 15.36 ? 207 VAL A CG2 1 
ATOM   1589 N  N   . THR A 1 207 ? -8.568  5.313   24.792  1.00 12.71 ? 208 THR A N   1 
ATOM   1590 C  CA  . THR A 1 207 ? -9.492  4.629   25.662  1.00 14.25 ? 208 THR A CA  1 
ATOM   1591 C  C   . THR A 1 207 ? -10.007 3.457   24.830  1.00 13.37 ? 208 THR A C   1 
ATOM   1592 O  O   . THR A 1 207 ? -10.707 3.657   23.816  1.00 13.23 ? 208 THR A O   1 
ATOM   1593 C  CB  . THR A 1 207 ? -10.644 5.546   26.139  1.00 14.23 ? 208 THR A CB  1 
ATOM   1594 O  OG1 . THR A 1 207 ? -10.080 6.619   26.915  1.00 15.29 ? 208 THR A OG1 1 
ATOM   1595 C  CG2 . THR A 1 207 ? -11.668 4.796   26.971  1.00 14.70 ? 208 THR A CG2 1 
ATOM   1596 N  N   . TRP A 1 208 ? -9.663  2.237   25.240  1.00 14.23 ? 209 TRP A N   1 
ATOM   1597 C  CA  . TRP A 1 208 ? -10.103 1.004   24.605  1.00 13.64 ? 209 TRP A CA  1 
ATOM   1598 C  C   . TRP A 1 208 ? -11.486 0.600   25.080  1.00 12.96 ? 209 TRP A C   1 
ATOM   1599 O  O   . TRP A 1 208 ? -11.750 0.606   26.264  1.00 14.78 ? 209 TRP A O   1 
ATOM   1600 C  CB  . TRP A 1 208 ? -9.087  -0.133  24.818  1.00 13.95 ? 209 TRP A CB  1 
ATOM   1601 C  CG  . TRP A 1 208 ? -7.979  -0.053  23.816  1.00 13.21 ? 209 TRP A CG  1 
ATOM   1602 C  CD1 . TRP A 1 208 ? -6.730  0.484   24.019  1.00 13.81 ? 209 TRP A CD1 1 
ATOM   1603 C  CD2 . TRP A 1 208 ? -8.033  -0.443  22.431  1.00 14.12 ? 209 TRP A CD2 1 
ATOM   1604 N  NE1 . TRP A 1 208 ? -6.012  0.437   22.854  1.00 14.99 ? 209 TRP A NE1 1 
ATOM   1605 C  CE2 . TRP A 1 208 ? -6.785  -0.102  21.852  1.00 13.38 ? 209 TRP A CE2 1 
ATOM   1606 C  CE3 . TRP A 1 208 ? -9.018  -1.052  21.630  1.00 13.27 ? 209 TRP A CE3 1 
ATOM   1607 C  CZ2 . TRP A 1 208 ? -6.462  -0.386  20.521  1.00 13.16 ? 209 TRP A CZ2 1 
ATOM   1608 C  CZ3 . TRP A 1 208 ? -8.706  -1.352  20.311  1.00 13.30 ? 209 TRP A CZ3 1 
ATOM   1609 C  CH2 . TRP A 1 208 ? -7.463  -1.002  19.782  1.00 13.61 ? 209 TRP A CH2 1 
ATOM   1610 N  N   . ILE A 1 209 ? -12.392 0.371   24.125  1.00 12.43 ? 210 ILE A N   1 
ATOM   1611 C  CA  . ILE A 1 209 ? -13.695 -0.197  24.433  1.00 14.01 ? 210 ILE A CA  1 
ATOM   1612 C  C   . ILE A 1 209 ? -13.816 -1.482  23.612  1.00 13.05 ? 210 ILE A C   1 
ATOM   1613 O  O   . ILE A 1 209 ? -13.905 -1.411  22.377  1.00 14.02 ? 210 ILE A O   1 
ATOM   1614 C  CB  . ILE A 1 209 ? -14.795 0.818   24.046  1.00 13.31 ? 210 ILE A CB  1 
ATOM   1615 C  CG1 . ILE A 1 209 ? -14.540 2.122   24.814  1.00 15.67 ? 210 ILE A CG1 1 
ATOM   1616 C  CG2 . ILE A 1 209 ? -16.177 0.213   24.307  1.00 12.76 ? 210 ILE A CG2 1 
ATOM   1617 C  CD1 . ILE A 1 209 ? -15.395 3.323   24.433  1.00 16.94 ? 210 ILE A CD1 1 
ATOM   1618 N  N   . VAL A 1 210 ? -13.760 -2.656  24.263  1.00 13.76 ? 211 VAL A N   1 
ATOM   1619 C  CA  . VAL A 1 210 ? -13.727 -3.943  23.577  1.00 13.41 ? 211 VAL A CA  1 
ATOM   1620 C  C   . VAL A 1 210 ? -15.033 -4.675  23.836  1.00 12.12 ? 211 VAL A C   1 
ATOM   1621 O  O   . VAL A 1 210 ? -15.429 -4.842  24.989  1.00 14.51 ? 211 VAL A O   1 
ATOM   1622 C  CB  . VAL A 1 210 ? -12.527 -4.795  24.032  1.00 13.34 ? 211 VAL A CB  1 
ATOM   1623 C  CG1 . VAL A 1 210 ? -12.504 -6.137  23.302  1.00 12.98 ? 211 VAL A CG1 1 
ATOM   1624 C  CG2 . VAL A 1 210 ? -11.217 -4.082  23.719  1.00 14.21 ? 211 VAL A CG2 1 
ATOM   1625 N  N   . LEU A 1 211 ? -15.810 -4.903  22.774  1.00 12.20 ? 212 LEU A N   1 
ATOM   1626 C  CA  . LEU A 1 211 ? -17.094 -5.535  22.986  1.00 13.30 ? 212 LEU A CA  1 
ATOM   1627 C  C   . LEU A 1 211 ? -16.941 -7.011  23.352  1.00 14.84 ? 212 LEU A C   1 
ATOM   1628 O  O   . LEU A 1 211 ? -16.111 -7.720  22.798  1.00 15.08 ? 212 LEU A O   1 
ATOM   1629 C  CB  . LEU A 1 211 ? -17.908 -5.417  21.698  1.00 13.30 ? 212 LEU A CB  1 
ATOM   1630 C  CG  . LEU A 1 211 ? -18.226 -4.004  21.236  1.00 12.58 ? 212 LEU A CG  1 
ATOM   1631 C  CD1 . LEU A 1 211 ? -19.223 -4.121  20.062  1.00 14.20 ? 212 LEU A CD1 1 
ATOM   1632 C  CD2 . LEU A 1 211 ? -18.797 -3.120  22.375  1.00 13.95 ? 212 LEU A CD2 1 
ATOM   1633 N  N   . LYS A 1 212 ? -17.819 -7.457  24.260  1.00 15.19 ? 213 LYS A N   1 
ATOM   1634 C  CA  . LYS A 1 212 ? -17.813 -8.835  24.733  1.00 16.76 ? 213 LYS A CA  1 
ATOM   1635 C  C   . LYS A 1 212 ? -18.247 -9.834  23.665  1.00 15.93 ? 213 LYS A C   1 
ATOM   1636 O  O   . LYS A 1 212 ? -17.707 -10.947 23.619  1.00 16.58 ? 213 LYS A O   1 
ATOM   1637 C  CB  . LYS A 1 212 ? -18.689 -8.896  26.002  1.00 20.84 ? 213 LYS A CB  1 
ATOM   1638 C  CG  . LYS A 1 212 ? -19.288 -10.236 26.435  1.00 28.51 ? 213 LYS A CG  1 
ATOM   1639 C  CD  . LYS A 1 212 ? -20.672 -10.069 27.122  1.00 29.57 ? 213 LYS A CD  1 
ATOM   1640 C  CE  . LYS A 1 212 ? -21.820 -9.808  26.148  1.00 35.32 ? 213 LYS A CE  1 
ATOM   1641 N  NZ  . LYS A 1 212 ? -23.129 -9.673  26.843  1.00 40.72 ? 213 LYS A NZ  1 
ATOM   1642 N  N   . GLU A 1 213 ? -19.209 -9.453  22.818  1.00 15.33 ? 214 GLU A N   1 
ATOM   1643 C  CA  . GLU A 1 213 ? -19.810 -10.359 21.852  1.00 14.56 ? 214 GLU A CA  1 
ATOM   1644 C  C   . GLU A 1 213 ? -19.058 -10.253 20.518  1.00 13.93 ? 214 GLU A C   1 
ATOM   1645 O  O   . GLU A 1 213 ? -18.971 -9.177  19.947  1.00 15.56 ? 214 GLU A O   1 
ATOM   1646 C  CB  . GLU A 1 213 ? -21.268 -9.950  21.608  1.00 15.80 ? 214 GLU A CB  1 
ATOM   1647 C  CG  . GLU A 1 213 ? -22.053 -10.924 20.714  1.00 19.52 ? 214 GLU A CG  1 
ATOM   1648 C  CD  . GLU A 1 213 ? -23.501 -10.458 20.457  1.00 23.88 ? 214 GLU A CD  1 
ATOM   1649 O  OE1 . GLU A 1 213 ? -24.064 -9.792  21.315  1.00 23.79 ? 214 GLU A OE1 1 
ATOM   1650 O  OE2 . GLU A 1 213 ? -24.055 -10.739 19.362  1.00 31.22 ? 214 GLU A OE2 1 
ATOM   1651 N  N   . PRO A 1 214 ? -18.466 -11.348 19.991  1.00 14.64 ? 215 PRO A N   1 
ATOM   1652 C  CA  . PRO A 1 214 ? -17.820 -11.308 18.694  1.00 13.83 ? 215 PRO A CA  1 
ATOM   1653 C  C   . PRO A 1 214 ? -18.882 -11.274 17.612  1.00 15.10 ? 215 PRO A C   1 
ATOM   1654 O  O   . PRO A 1 214 ? -20.040 -11.637 17.851  1.00 18.26 ? 215 PRO A O   1 
ATOM   1655 C  CB  . PRO A 1 214 ? -17.060 -12.646 18.621  1.00 15.79 ? 215 PRO A CB  1 
ATOM   1656 C  CG  . PRO A 1 214 ? -17.818 -13.545 19.530  1.00 21.76 ? 215 PRO A CG  1 
ATOM   1657 C  CD  . PRO A 1 214 ? -18.315 -12.665 20.653  1.00 18.15 ? 215 PRO A CD  1 
ATOM   1658 N  N   . ILE A 1 215 ? -18.437 -10.863 16.426  1.00 13.44 ? 216 ILE A N   1 
ATOM   1659 C  CA  . ILE A 1 215 ? -19.263 -11.091 15.250  1.00 14.59 ? 216 ILE A CA  1 
ATOM   1660 C  C   . ILE A 1 215 ? -18.734 -12.364 14.605  1.00 14.61 ? 216 ILE A C   1 
ATOM   1661 O  O   . ILE A 1 215 ? -17.546 -12.678 14.733  1.00 14.97 ? 216 ILE A O   1 
ATOM   1662 C  CB  . ILE A 1 215 ? -19.289 -9.894  14.281  1.00 15.03 ? 216 ILE A CB  1 
ATOM   1663 C  CG1 . ILE A 1 215 ? -17.905 -9.499  13.760  1.00 15.43 ? 216 ILE A CG1 1 
ATOM   1664 C  CG2 . ILE A 1 215 ? -20.004 -8.657  14.852  1.00 16.28 ? 216 ILE A CG2 1 
ATOM   1665 C  CD1 . ILE A 1 215 ? -17.935 -8.484  12.594  1.00 15.57 ? 216 ILE A CD1 1 
ATOM   1666 N  N   A SER A 1 216 ? -19.621 -13.092 13.931  0.50 15.11 ? 217 SER A N   1 
ATOM   1667 N  N   B SER A 1 216 ? -19.615 -13.001 13.836  0.50 15.15 ? 217 SER A N   1 
ATOM   1668 C  CA  A SER A 1 216 ? -19.189 -14.236 13.138  0.50 15.67 ? 217 SER A CA  1 
ATOM   1669 C  CA  B SER A 1 216 ? -19.320 -14.205 13.077  0.50 16.04 ? 217 SER A CA  1 
ATOM   1670 C  C   A SER A 1 216 ? -19.027 -13.765 11.700  0.50 15.69 ? 217 SER A C   1 
ATOM   1671 C  C   B SER A 1 216 ? -19.073 -13.785 11.635  0.50 15.77 ? 217 SER A C   1 
ATOM   1672 O  O   A SER A 1 216 ? -19.868 -13.013 11.196  0.50 17.11 ? 217 SER A O   1 
ATOM   1673 O  O   B SER A 1 216 ? -19.903 -13.067 11.064  0.50 17.30 ? 217 SER A O   1 
ATOM   1674 C  CB  A SER A 1 216 ? -20.181 -15.374 13.199  0.50 17.01 ? 217 SER A CB  1 
ATOM   1675 C  CB  B SER A 1 216 ? -20.522 -15.124 13.147  0.50 17.02 ? 217 SER A CB  1 
ATOM   1676 O  OG  A SER A 1 216 ? -20.383 -15.853 14.525  0.50 18.03 ? 217 SER A OG  1 
ATOM   1677 O  OG  B SER A 1 216 ? -20.263 -16.370 12.528  0.50 18.41 ? 217 SER A OG  1 
ATOM   1678 N  N   . VAL A 1 217 ? -17.932 -14.198 11.079  1.00 14.03 ? 218 VAL A N   1 
ATOM   1679 C  CA  . VAL A 1 217 ? -17.674 -13.984 9.664   1.00 14.13 ? 218 VAL A CA  1 
ATOM   1680 C  C   . VAL A 1 217 ? -17.425 -15.352 9.042   1.00 14.69 ? 218 VAL A C   1 
ATOM   1681 O  O   . VAL A 1 217 ? -17.122 -16.314 9.740   1.00 14.93 ? 218 VAL A O   1 
ATOM   1682 C  CB  . VAL A 1 217 ? -16.484 -13.058 9.407   1.00 14.24 ? 218 VAL A CB  1 
ATOM   1683 C  CG1 . VAL A 1 217 ? -16.763 -11.682 10.001  1.00 14.10 ? 218 VAL A CG1 1 
ATOM   1684 C  CG2 . VAL A 1 217 ? -15.195 -13.668 10.001  1.00 15.07 ? 218 VAL A CG2 1 
ATOM   1685 N  N   . SER A 1 218 ? -17.622 -15.469 7.728   1.00 14.66 ? 219 SER A N   1 
ATOM   1686 C  CA  . SER A 1 218 ? -17.380 -16.805 7.174   1.00 13.54 ? 219 SER A CA  1 
ATOM   1687 C  C   . SER A 1 218 ? -15.918 -17.023 6.801   1.00 14.63 ? 219 SER A C   1 
ATOM   1688 O  O   . SER A 1 218 ? -15.103 -16.096 6.663   1.00 15.49 ? 219 SER A O   1 
ATOM   1689 C  CB  . SER A 1 218 ? -18.270 -17.002 5.949   1.00 14.76 ? 219 SER A CB  1 
ATOM   1690 O  OG  . SER A 1 218 ? -17.860 -16.188 4.877   1.00 16.28 ? 219 SER A OG  1 
ATOM   1691 N  N   . SER A 1 219 ? -15.576 -18.312 6.595   1.00 14.75 ? 220 SER A N   1 
ATOM   1692 C  CA  . SER A 1 219 ? -14.269 -18.659 6.056   1.00 16.15 ? 220 SER A CA  1 
ATOM   1693 C  C   . SER A 1 219 ? -13.971 -17.906 4.756   1.00 17.71 ? 220 SER A C   1 
ATOM   1694 O  O   . SER A 1 219 ? -12.857 -17.391 4.596   1.00 18.67 ? 220 SER A O   1 
ATOM   1695 C  CB  . SER A 1 219 ? -14.119 -20.176 5.948   1.00 18.05 ? 220 SER A CB  1 
ATOM   1696 O  OG  . SER A 1 219 ? -15.096 -20.662 5.029   1.00 21.41 ? 220 SER A OG  1 
ATOM   1697 N  N   . GLU A 1 220 ? -14.959 -17.798 3.840   1.00 17.20 ? 221 GLU A N   1 
ATOM   1698 C  CA  . GLU A 1 220 ? -14.705 -17.160 2.558   1.00 15.80 ? 221 GLU A CA  1 
ATOM   1699 C  C   . GLU A 1 220 ? -14.399 -15.675 2.736   1.00 16.09 ? 221 GLU A C   1 
ATOM   1700 O  O   . GLU A 1 220 ? -13.590 -15.131 2.001   1.00 16.68 ? 221 GLU A O   1 
ATOM   1701 C  CB  . GLU A 1 220 ? -15.910 -17.300 1.626   1.00 18.09 ? 221 GLU A CB  1 
ATOM   1702 C  CG  . GLU A 1 220 ? -16.146 -18.753 1.262   1.00 21.45 ? 221 GLU A CG  1 
ATOM   1703 C  CD  . GLU A 1 220 ? -17.238 -19.432 2.063   1.00 26.49 ? 221 GLU A CD  1 
ATOM   1704 O  OE1 . GLU A 1 220 ? -17.465 -19.073 3.246   1.00 24.96 ? 221 GLU A OE1 1 
ATOM   1705 O  OE2 . GLU A 1 220 ? -17.903 -20.325 1.465   1.00 33.00 ? 221 GLU A OE2 1 
ATOM   1706 N  N   . GLN A 1 221 ? -15.043 -15.035 3.727   1.00 14.74 ? 222 GLN A N   1 
ATOM   1707 C  CA  . GLN A 1 221 ? -14.779 -13.624 4.027   1.00 13.55 ? 222 GLN A CA  1 
ATOM   1708 C  C   . GLN A 1 221 ? -13.339 -13.432 4.529   1.00 14.93 ? 222 GLN A C   1 
ATOM   1709 O  O   . GLN A 1 221 ? -12.631 -12.555 4.031   1.00 15.31 ? 222 GLN A O   1 
ATOM   1710 C  CB  . GLN A 1 221 ? -15.809 -13.111 5.024   1.00 13.96 ? 222 GLN A CB  1 
ATOM   1711 C  CG  . GLN A 1 221 ? -17.170 -12.959 4.318   1.00 14.08 ? 222 GLN A CG  1 
ATOM   1712 C  CD  . GLN A 1 221 ? -18.252 -12.430 5.223   1.00 14.79 ? 222 GLN A CD  1 
ATOM   1713 O  OE1 . GLN A 1 221 ? -18.369 -12.796 6.403   1.00 13.77 ? 222 GLN A OE1 1 
ATOM   1714 N  NE2 . GLN A 1 221 ? -19.084 -11.585 4.655   1.00 13.52 ? 222 GLN A NE2 1 
ATOM   1715 N  N   . VAL A 1 222 ? -12.923 -14.231 5.521   1.00 16.06 ? 223 VAL A N   1 
ATOM   1716 C  CA  . VAL A 1 222 ? -11.571 -14.043 6.061   1.00 17.20 ? 223 VAL A CA  1 
ATOM   1717 C  C   . VAL A 1 222 ? -10.505 -14.455 5.038   1.00 20.01 ? 223 VAL A C   1 
ATOM   1718 O  O   . VAL A 1 222 ? -9.419  -13.870 5.025   1.00 19.36 ? 223 VAL A O   1 
ATOM   1719 C  CB  . VAL A 1 222 ? -11.351 -14.684 7.443   1.00 22.47 ? 223 VAL A CB  1 
ATOM   1720 C  CG1 . VAL A 1 222 ? -11.381 -16.205 7.390   1.00 24.98 ? 223 VAL A CG1 1 
ATOM   1721 C  CG2 . VAL A 1 222 ? -10.002 -14.241 7.998   1.00 21.95 ? 223 VAL A CG2 1 
ATOM   1722 N  N   . LEU A 1 223 ? -10.819 -15.427 4.169   1.00 18.97 ? 224 LEU A N   1 
ATOM   1723 C  CA  . LEU A 1 223 ? -9.872  -15.837 3.143   1.00 21.01 ? 224 LEU A CA  1 
ATOM   1724 C  C   . LEU A 1 223 ? -9.565  -14.680 2.187   1.00 21.07 ? 224 LEU A C   1 
ATOM   1725 O  O   . LEU A 1 223 ? -8.432  -14.549 1.703   1.00 20.69 ? 224 LEU A O   1 
ATOM   1726 C  CB  . LEU A 1 223 ? -10.405 -17.065 2.405   1.00 25.70 ? 224 LEU A CB  1 
ATOM   1727 C  CG  . LEU A 1 223 ? -9.302  -18.042 2.010   1.00 38.40 ? 224 LEU A CG  1 
ATOM   1728 C  CD1 . LEU A 1 223 ? -9.003  -19.015 3.153   1.00 38.84 ? 224 LEU A CD1 1 
ATOM   1729 C  CD2 . LEU A 1 223 ? -9.646  -18.763 0.709   1.00 42.75 ? 224 LEU A CD2 1 
ATOM   1730 N  N   . LYS A 1 224 ? -10.559 -13.812 1.928   1.00 17.99 ? 225 LYS A N   1 
ATOM   1731 C  CA  . LYS A 1 224 ? -10.299 -12.624 1.135   1.00 18.44 ? 225 LYS A CA  1 
ATOM   1732 C  C   . LYS A 1 224 ? -9.332  -11.649 1.821   1.00 16.24 ? 225 LYS A C   1 
ATOM   1733 O  O   . LYS A 1 224 ? -8.549  -11.032 1.128   1.00 16.26 ? 225 LYS A O   1 
ATOM   1734 C  CB  . LYS A 1 224 ? -11.602 -12.019 0.613   1.00 21.09 ? 225 LYS A CB  1 
ATOM   1735 C  CG  . LYS A 1 224 ? -12.254 -12.909 -0.439  1.00 26.10 ? 225 LYS A CG  1 
ATOM   1736 C  CD  . LYS A 1 224 ? -13.657 -12.543 -0.873  1.00 32.03 ? 225 LYS A CD  1 
ATOM   1737 C  CE  . LYS A 1 224 ? -13.886 -12.828 -2.344  1.00 38.60 ? 225 LYS A CE  1 
ATOM   1738 N  NZ  . LYS A 1 224 ? -15.327 -12.925 -2.674  1.00 48.25 ? 225 LYS A NZ  1 
ATOM   1739 N  N   . PHE A 1 225 ? -9.435  -11.429 3.133   1.00 16.14 ? 226 PHE A N   1 
ATOM   1740 C  CA  . PHE A 1 225 ? -8.430  -10.657 3.831   1.00 14.65 ? 226 PHE A CA  1 
ATOM   1741 C  C   . PHE A 1 225 ? -7.028  -11.206 3.531   1.00 16.09 ? 226 PHE A C   1 
ATOM   1742 O  O   . PHE A 1 225 ? -6.086  -10.441 3.365   1.00 16.56 ? 226 PHE A O   1 
ATOM   1743 C  CB  . PHE A 1 225 ? -8.635  -10.753 5.345   1.00 14.51 ? 226 PHE A CB  1 
ATOM   1744 C  CG  . PHE A 1 225 ? -9.763  -9.955  5.968   1.00 16.96 ? 226 PHE A CG  1 
ATOM   1745 C  CD1 . PHE A 1 225 ? -10.834 -9.469  5.233   1.00 18.60 ? 226 PHE A CD1 1 
ATOM   1746 C  CD2 . PHE A 1 225 ? -9.815  -9.827  7.353   1.00 17.57 ? 226 PHE A CD2 1 
ATOM   1747 C  CE1 . PHE A 1 225 ? -11.838 -8.726  5.834   1.00 18.95 ? 226 PHE A CE1 1 
ATOM   1748 C  CE2 . PHE A 1 225 ? -10.846 -9.131  7.965   1.00 20.26 ? 226 PHE A CE2 1 
ATOM   1749 C  CZ  . PHE A 1 225 ? -11.850 -8.593  7.203   1.00 19.52 ? 226 PHE A CZ  1 
ATOM   1750 N  N   . ARG A 1 226 ? -6.879  -12.531 3.631   1.00 14.72 ? 227 ARG A N   1 
ATOM   1751 C  CA  . ARG A 1 226 ? -5.557  -13.145 3.576   1.00 16.44 ? 227 ARG A CA  1 
ATOM   1752 C  C   . ARG A 1 226 ? -4.966  -13.111 2.162   1.00 17.07 ? 227 ARG A C   1 
ATOM   1753 O  O   . ARG A 1 226 ? -3.845  -13.575 1.983   1.00 19.24 ? 227 ARG A O   1 
ATOM   1754 C  CB  . ARG A 1 226 ? -5.650  -14.612 3.993   1.00 15.70 ? 227 ARG A CB  1 
ATOM   1755 C  CG  . ARG A 1 226 ? -6.042  -14.796 5.453   1.00 15.18 ? 227 ARG A CG  1 
ATOM   1756 C  CD  . ARG A 1 226 ? -5.951  -16.249 5.933   1.00 17.16 ? 227 ARG A CD  1 
ATOM   1757 N  NE  . ARG A 1 226 ? -6.465  -16.382 7.302   1.00 18.07 ? 227 ARG A NE  1 
ATOM   1758 C  CZ  . ARG A 1 226 ? -7.394  -17.247 7.716   1.00 18.73 ? 227 ARG A CZ  1 
ATOM   1759 N  NH1 . ARG A 1 226 ? -7.909  -18.173 6.905   1.00 21.32 ? 227 ARG A NH1 1 
ATOM   1760 N  NH2 . ARG A 1 226 ? -7.795  -17.229 8.971   1.00 20.63 ? 227 ARG A NH2 1 
ATOM   1761 N  N   . LYS A 1 227 ? -5.736  -12.693 1.164   1.00 17.79 ? 228 LYS A N   1 
ATOM   1762 C  CA  . LYS A 1 227 ? -5.200  -12.544 -0.184  1.00 18.11 ? 228 LYS A CA  1 
ATOM   1763 C  C   . LYS A 1 227 ? -4.537  -11.190 -0.407  1.00 18.58 ? 228 LYS A C   1 
ATOM   1764 O  O   . LYS A 1 227 ? -3.916  -10.973 -1.437  1.00 19.09 ? 228 LYS A O   1 
ATOM   1765 C  CB  . LYS A 1 227 ? -6.329  -12.695 -1.204  1.00 20.01 ? 228 LYS A CB  1 
ATOM   1766 C  CG  . LYS A 1 227 ? -6.821  -14.128 -1.370  1.00 20.98 ? 228 LYS A CG  1 
ATOM   1767 C  CD  . LYS A 1 227 ? -7.863  -14.232 -2.488  1.00 28.93 ? 228 LYS A CD  1 
ATOM   1768 N  N   . LEU A 1 228 ? -4.665  -10.235 0.529   1.00 16.08 ? 229 LEU A N   1 
ATOM   1769 C  CA  . LEU A 1 228 ? -3.995  -8.950  0.409   1.00 16.03 ? 229 LEU A CA  1 
ATOM   1770 C  C   . LEU A 1 228 ? -2.494  -9.164  0.592   1.00 16.09 ? 229 LEU A C   1 
ATOM   1771 O  O   . LEU A 1 228 ? -2.063  -10.199 1.093   1.00 18.04 ? 229 LEU A O   1 
ATOM   1772 C  CB  . LEU A 1 228 ? -4.520  -7.994  1.501   1.00 15.00 ? 229 LEU A CB  1 
ATOM   1773 C  CG  . LEU A 1 228 ? -5.996  -7.597  1.328   1.00 16.38 ? 229 LEU A CG  1 
ATOM   1774 C  CD1 . LEU A 1 228 ? -6.504  -6.949  2.600   1.00 16.28 ? 229 LEU A CD1 1 
ATOM   1775 C  CD2 . LEU A 1 228 ? -6.123  -6.608  0.177   1.00 17.26 ? 229 LEU A CD2 1 
ATOM   1776 N  N   . ASN A 1 229 ? -1.735  -8.195  0.104   1.00 17.41 ? 230 ASN A N   1 
ATOM   1777 C  CA  . ASN A 1 229 ? -0.283  -8.239  0.160   1.00 16.97 ? 230 ASN A CA  1 
ATOM   1778 C  C   . ASN A 1 229 ? 0.268   -7.107  1.023   1.00 16.65 ? 230 ASN A C   1 
ATOM   1779 O  O   . ASN A 1 229 ? -0.215  -5.972  1.032   1.00 19.22 ? 230 ASN A O   1 
ATOM   1780 C  CB  . ASN A 1 229 ? 0.304   -8.018  -1.236  1.00 18.52 ? 230 ASN A CB  1 
ATOM   1781 C  CG  . ASN A 1 229 ? 0.247   -9.199  -2.183  1.00 21.51 ? 230 ASN A CG  1 
ATOM   1782 O  OD1 . ASN A 1 229 ? 0.881   -9.141  -3.232  1.00 24.80 ? 230 ASN A OD1 1 
ATOM   1783 N  ND2 . ASN A 1 229 ? -0.465  -10.251 -1.829  1.00 22.37 ? 230 ASN A ND2 1 
ATOM   1784 N  N   . PHE A 1 230 ? 1.355   -7.400  1.738   1.00 19.10 ? 231 PHE A N   1 
ATOM   1785 C  CA  . PHE A 1 230 ? 2.035   -6.343  2.466   1.00 18.39 ? 231 PHE A CA  1 
ATOM   1786 C  C   . PHE A 1 230 ? 2.855   -5.479  1.517   1.00 19.54 ? 231 PHE A C   1 
ATOM   1787 O  O   . PHE A 1 230 ? 3.039   -4.277  1.738   1.00 19.38 ? 231 PHE A O   1 
ATOM   1788 C  CB  . PHE A 1 230 ? 3.019   -6.878  3.510   1.00 17.47 ? 231 PHE A CB  1 
ATOM   1789 C  CG  . PHE A 1 230 ? 2.487   -7.462  4.795   1.00 19.54 ? 231 PHE A CG  1 
ATOM   1790 C  CD1 . PHE A 1 230 ? 1.782   -6.674  5.704   1.00 20.10 ? 231 PHE A CD1 1 
ATOM   1791 C  CD2 . PHE A 1 230 ? 2.800   -8.766  5.155   1.00 18.06 ? 231 PHE A CD2 1 
ATOM   1792 C  CE1 . PHE A 1 230 ? 1.391   -7.191  6.934   1.00 19.99 ? 231 PHE A CE1 1 
ATOM   1793 C  CE2 . PHE A 1 230 ? 2.419   -9.288  6.390   1.00 19.38 ? 231 PHE A CE2 1 
ATOM   1794 C  CZ  . PHE A 1 230 ? 1.680   -8.503  7.267   1.00 18.62 ? 231 PHE A CZ  1 
ATOM   1795 N  N   . ASN A 1 231 ? 3.375   -6.111  0.456   1.00 20.56 ? 232 ASN A N   1 
ATOM   1796 C  CA  . ASN A 1 231 ? 4.323   -5.487  -0.464  1.00 22.23 ? 232 ASN A CA  1 
ATOM   1797 C  C   . ASN A 1 231 ? 3.621   -4.595  -1.490  1.00 22.01 ? 232 ASN A C   1 
ATOM   1798 O  O   . ASN A 1 231 ? 2.437   -4.768  -1.785  1.00 19.45 ? 232 ASN A O   1 
ATOM   1799 C  CB  . ASN A 1 231 ? 5.052   -6.567  -1.272  1.00 21.77 ? 232 ASN A CB  1 
ATOM   1800 C  CG  . ASN A 1 231 ? 4.087   -7.554  -1.906  1.00 20.62 ? 232 ASN A CG  1 
ATOM   1801 O  OD1 . ASN A 1 231 ? 3.552   -8.429  -1.231  1.00 21.58 ? 232 ASN A OD1 1 
ATOM   1802 N  ND2 . ASN A 1 231 ? 3.861   -7.416  -3.207  1.00 21.35 ? 232 ASN A ND2 1 
ATOM   1803 N  N   . GLY A 1 232 ? 4.377   -3.653  -2.082  1.00 19.93 ? 233 GLY A N   1 
ATOM   1804 C  CA  . GLY A 1 232 ? 3.903   -2.898  -3.235  1.00 23.12 ? 233 GLY A CA  1 
ATOM   1805 C  C   . GLY A 1 232 ? 4.019   -3.744  -4.504  1.00 25.41 ? 233 GLY A C   1 
ATOM   1806 O  O   . GLY A 1 232 ? 4.686   -4.779  -4.491  1.00 24.68 ? 233 GLY A O   1 
ATOM   1807 N  N   . GLU A 1 233 ? 3.278   -3.353  -5.547  1.00 26.51 ? 234 GLU A N   1 
ATOM   1808 C  CA  . GLU A 1 233 ? 3.327   -4.155  -6.754  1.00 35.67 ? 234 GLU A CA  1 
ATOM   1809 C  C   . GLU A 1 233 ? 4.740   -4.078  -7.316  1.00 36.93 ? 234 GLU A C   1 
ATOM   1810 O  O   . GLU A 1 233 ? 5.238   -2.970  -7.505  1.00 36.30 ? 234 GLU A O   1 
ATOM   1811 C  CB  . GLU A 1 233 ? 2.372   -3.650  -7.828  1.00 33.71 ? 234 GLU A CB  1 
ATOM   1812 C  CG  . GLU A 1 233 ? 2.141   -4.732  -8.874  1.00 42.66 ? 234 GLU A CG  1 
ATOM   1813 C  CD  . GLU A 1 233 ? 1.317   -4.301  -10.074 1.00 50.36 ? 234 GLU A CD  1 
ATOM   1814 O  OE1 . GLU A 1 233 ? 0.386   -3.487  -9.879  1.00 54.10 ? 234 GLU A OE1 1 
ATOM   1815 O  OE2 . GLU A 1 233 ? 1.620   -4.774  -11.213 1.00 51.47 ? 234 GLU A OE2 1 
ATOM   1816 N  N   . GLY A 1 234 ? 5.348   -5.249  -7.564  1.00 38.98 ? 235 GLY A N   1 
ATOM   1817 C  CA  . GLY A 1 234 ? 6.696   -5.326  -8.105  1.00 40.21 ? 235 GLY A CA  1 
ATOM   1818 C  C   . GLY A 1 234 ? 7.814   -5.473  -7.066  1.00 45.71 ? 235 GLY A C   1 
ATOM   1819 O  O   . GLY A 1 234 ? 8.979   -5.337  -7.443  1.00 44.20 ? 235 GLY A O   1 
ATOM   1820 N  N   . GLU A 1 235 ? 7.477   -5.692  -5.775  1.00 36.18 ? 236 GLU A N   1 
ATOM   1821 C  CA  . GLU A 1 235 ? 8.386   -6.238  -4.762  1.00 34.17 ? 236 GLU A CA  1 
ATOM   1822 C  C   . GLU A 1 235 ? 7.978   -7.693  -4.558  1.00 29.13 ? 236 GLU A C   1 
ATOM   1823 O  O   . GLU A 1 235 ? 6.894   -8.046  -5.013  1.00 27.21 ? 236 GLU A O   1 
ATOM   1824 C  CB  . GLU A 1 235 ? 8.190   -5.613  -3.368  1.00 37.33 ? 236 GLU A CB  1 
ATOM   1825 C  CG  . GLU A 1 235 ? 8.423   -4.109  -3.255  1.00 42.04 ? 236 GLU A CG  1 
ATOM   1826 C  CD  . GLU A 1 235 ? 7.546   -3.325  -2.263  1.00 50.24 ? 236 GLU A CD  1 
ATOM   1827 O  OE1 . GLU A 1 235 ? 7.295   -3.801  -1.111  1.00 39.73 ? 236 GLU A OE1 1 
ATOM   1828 O  OE2 . GLU A 1 235 ? 7.097   -2.218  -2.639  1.00 50.44 ? 236 GLU A OE2 1 
ATOM   1829 N  N   . PRO A 1 236 ? 8.775   -8.580  -3.895  1.00 24.66 ? 237 PRO A N   1 
ATOM   1830 C  CA  . PRO A 1 236 ? 8.362   -9.968  -3.659  1.00 26.72 ? 237 PRO A CA  1 
ATOM   1831 C  C   . PRO A 1 236 ? 7.054   -10.067 -2.875  1.00 25.45 ? 237 PRO A C   1 
ATOM   1832 O  O   . PRO A 1 236 ? 6.829   -9.251  -1.978  1.00 26.67 ? 237 PRO A O   1 
ATOM   1833 C  CB  . PRO A 1 236 ? 9.436   -10.490 -2.687  1.00 27.86 ? 237 PRO A CB  1 
ATOM   1834 C  CG  . PRO A 1 236 ? 10.649  -9.701  -3.084  1.00 26.37 ? 237 PRO A CG  1 
ATOM   1835 C  CD  . PRO A 1 236 ? 10.118  -8.314  -3.351  1.00 26.53 ? 237 PRO A CD  1 
ATOM   1836 N  N   . GLU A 1 237 ? 6.237   -11.077 -3.217  1.00 26.82 ? 238 GLU A N   1 
ATOM   1837 C  CA  . GLU A 1 237 ? 4.911   -11.262 -2.650  1.00 28.54 ? 238 GLU A CA  1 
ATOM   1838 C  C   . GLU A 1 237 ? 5.013   -11.792 -1.222  1.00 26.49 ? 238 GLU A C   1 
ATOM   1839 O  O   . GLU A 1 237 ? 5.535   -12.887 -0.971  1.00 27.66 ? 238 GLU A O   1 
ATOM   1840 C  CB  . GLU A 1 237 ? 4.092   -12.190 -3.547  1.00 28.04 ? 238 GLU A CB  1 
ATOM   1841 C  CG  . GLU A 1 237 ? 2.700   -12.532 -3.056  1.00 30.87 ? 238 GLU A CG  1 
ATOM   1842 C  CD  . GLU A 1 237 ? 2.043   -13.521 -4.017  1.00 38.56 ? 238 GLU A CD  1 
ATOM   1843 O  OE1 . GLU A 1 237 ? 2.564   -13.701 -5.139  1.00 38.02 ? 238 GLU A OE1 1 
ATOM   1844 O  OE2 . GLU A 1 237 ? 1.022   -14.135 -3.655  1.00 44.09 ? 238 GLU A OE2 1 
ATOM   1845 N  N   . GLU A 1 238 ? 4.453   -11.010 -0.283  1.00 24.79 ? 239 GLU A N   1 
ATOM   1846 C  CA  . GLU A 1 238 ? 4.310   -11.418 1.101   1.00 25.74 ? 239 GLU A CA  1 
ATOM   1847 C  C   . GLU A 1 238 ? 2.853   -11.169 1.452   1.00 22.42 ? 239 GLU A C   1 
ATOM   1848 O  O   . GLU A 1 238 ? 2.413   -10.017 1.390   1.00 22.52 ? 239 GLU A O   1 
ATOM   1849 C  CB  . GLU A 1 238 ? 5.153   -10.548 2.043   1.00 30.44 ? 239 GLU A CB  1 
ATOM   1850 C  CG  . GLU A 1 238 ? 6.623   -10.936 2.105   1.00 36.15 ? 239 GLU A CG  1 
ATOM   1851 C  CD  . GLU A 1 238 ? 7.423   -10.041 3.050   1.00 39.49 ? 239 GLU A CD  1 
ATOM   1852 O  OE1 . GLU A 1 238 ? 7.366   -10.273 4.280   1.00 39.57 ? 239 GLU A OE1 1 
ATOM   1853 O  OE2 . GLU A 1 238 ? 8.062   -9.079  2.554   1.00 38.85 ? 239 GLU A OE2 1 
ATOM   1854 N  N   . LEU A 1 239 ? 2.122   -12.251 1.717   1.00 20.92 ? 240 LEU A N   1 
ATOM   1855 C  CA  . LEU A 1 239 ? 0.710   -12.099 2.024   1.00 20.14 ? 240 LEU A CA  1 
ATOM   1856 C  C   . LEU A 1 239 ? 0.590   -11.276 3.293   1.00 19.42 ? 240 LEU A C   1 
ATOM   1857 O  O   . LEU A 1 239 ? 1.345   -11.465 4.250   1.00 19.68 ? 240 LEU A O   1 
ATOM   1858 C  CB  . LEU A 1 239 ? 0.054   -13.461 2.252   1.00 21.79 ? 240 LEU A CB  1 
ATOM   1859 C  CG  . LEU A 1 239 ? -0.102  -14.356 1.030   1.00 22.37 ? 240 LEU A CG  1 
ATOM   1860 C  CD1 . LEU A 1 239 ? -0.854  -15.596 1.458   1.00 27.03 ? 240 LEU A CD1 1 
ATOM   1861 C  CD2 . LEU A 1 239 ? -0.841  -13.628 -0.090  1.00 23.43 ? 240 LEU A CD2 1 
ATOM   1862 N  N   . MET A 1 240 ? -0.432  -10.411 3.299   1.00 18.38 ? 241 MET A N   1 
ATOM   1863 C  CA  . MET A 1 240 ? -0.777  -9.653  4.497   1.00 15.83 ? 241 MET A CA  1 
ATOM   1864 C  C   . MET A 1 240 ? -1.584  -10.552 5.437   1.00 15.76 ? 241 MET A C   1 
ATOM   1865 O  O   . MET A 1 240 ? -2.788  -10.703 5.299   1.00 15.61 ? 241 MET A O   1 
ATOM   1866 C  CB  . MET A 1 240 ? -1.546  -8.389  4.100   1.00 16.25 ? 241 MET A CB  1 
ATOM   1867 C  CG  . MET A 1 240 ? -1.929  -7.503  5.257   1.00 16.11 ? 241 MET A CG  1 
ATOM   1868 S  SD  . MET A 1 240 ? -2.903  -6.080  4.763   1.00 17.63 ? 241 MET A SD  1 
ATOM   1869 C  CE  . MET A 1 240 ? -1.628  -5.032  4.042   1.00 16.41 ? 241 MET A CE  1 
ATOM   1870 N  N   . VAL A 1 241 ? -0.891  -11.178 6.401   1.00 16.90 ? 242 VAL A N   1 
ATOM   1871 C  CA  . VAL A 1 241 ? -1.464  -12.039 7.426   1.00 15.13 ? 242 VAL A CA  1 
ATOM   1872 C  C   . VAL A 1 241 ? -0.621  -11.859 8.660   1.00 13.53 ? 242 VAL A C   1 
ATOM   1873 O  O   . VAL A 1 241 ? 0.525   -11.454 8.523   1.00 16.56 ? 242 VAL A O   1 
ATOM   1874 C  CB  . VAL A 1 241 ? -1.483  -13.535 7.038   1.00 17.78 ? 242 VAL A CB  1 
ATOM   1875 C  CG1 . VAL A 1 241 ? -2.427  -13.802 5.864   1.00 16.36 ? 242 VAL A CG1 1 
ATOM   1876 C  CG2 . VAL A 1 241 ? -0.087  -14.054 6.723   1.00 18.74 ? 242 VAL A CG2 1 
ATOM   1877 N  N   . ASP A 1 242 ? -1.250  -12.126 9.808   1.00 13.31 ? 243 ASP A N   1 
ATOM   1878 C  CA  . ASP A 1 242 ? -0.610  -11.998 11.095  1.00 14.16 ? 243 ASP A CA  1 
ATOM   1879 C  C   . ASP A 1 242 ? -0.123  -10.563 11.302  1.00 15.80 ? 243 ASP A C   1 
ATOM   1880 O  O   . ASP A 1 242 ? 0.978   -10.322 11.847  1.00 16.14 ? 243 ASP A O   1 
ATOM   1881 C  CB  . ASP A 1 242 ? 0.425   -13.105 11.311  1.00 14.56 ? 243 ASP A CB  1 
ATOM   1882 C  CG  . ASP A 1 242 ? -0.137  -14.507 11.444  1.00 15.60 ? 243 ASP A CG  1 
ATOM   1883 O  OD1 . ASP A 1 242 ? -1.195  -14.726 12.111  1.00 15.46 ? 243 ASP A OD1 1 
ATOM   1884 O  OD2 . ASP A 1 242 ? 0.545   -15.431 10.887  1.00 19.00 ? 243 ASP A OD2 1 
ATOM   1885 N  N   . ASN A 1 243 ? -1.008  -9.624  11.001  1.00 14.15 ? 244 ASN A N   1 
ATOM   1886 C  CA  . ASN A 1 243 ? -0.716  -8.211  11.244  1.00 13.70 ? 244 ASN A CA  1 
ATOM   1887 C  C   . ASN A 1 243 ? -1.312  -7.795  12.583  1.00 14.09 ? 244 ASN A C   1 
ATOM   1888 O  O   . ASN A 1 243 ? -2.005  -6.783  12.668  1.00 14.66 ? 244 ASN A O   1 
ATOM   1889 C  CB  . ASN A 1 243 ? -1.210  -7.305  10.109  1.00 14.71 ? 244 ASN A CB  1 
ATOM   1890 C  CG  . ASN A 1 243 ? -2.670  -7.518  9.782   1.00 16.16 ? 244 ASN A CG  1 
ATOM   1891 O  OD1 . ASN A 1 243 ? -3.302  -8.422  10.330  1.00 15.54 ? 244 ASN A OD1 1 
ATOM   1892 N  ND2 . ASN A 1 243 ? -3.224  -6.651  8.938   1.00 14.68 ? 244 ASN A ND2 1 
ATOM   1893 N  N   . TRP A 1 244 ? -0.976  -8.546  13.633  1.00 13.02 ? 245 TRP A N   1 
ATOM   1894 C  CA  . TRP A 1 244 ? -1.464  -8.278  14.971  1.00 12.85 ? 245 TRP A CA  1 
ATOM   1895 C  C   . TRP A 1 244 ? -0.286  -8.155  15.908  1.00 13.12 ? 245 TRP A C   1 
ATOM   1896 O  O   . TRP A 1 244 ? 0.659   -8.925  15.798  1.00 15.83 ? 245 TRP A O   1 
ATOM   1897 C  CB  . TRP A 1 244 ? -2.427  -9.382  15.449  1.00 13.42 ? 245 TRP A CB  1 
ATOM   1898 C  CG  . TRP A 1 244 ? -1.949  -10.803 15.281  1.00 14.85 ? 245 TRP A CG  1 
ATOM   1899 C  CD1 . TRP A 1 244 ? -2.040  -11.562 14.145  1.00 13.98 ? 245 TRP A CD1 1 
ATOM   1900 C  CD2 . TRP A 1 244 ? -1.395  -11.673 16.296  1.00 15.54 ? 245 TRP A CD2 1 
ATOM   1901 N  NE1 . TRP A 1 244 ? -1.576  -12.841 14.371  1.00 13.11 ? 245 TRP A NE1 1 
ATOM   1902 C  CE2 . TRP A 1 244 ? -1.141  -12.917 15.671  1.00 14.66 ? 245 TRP A CE2 1 
ATOM   1903 C  CE3 . TRP A 1 244 ? -1.080  -11.519 17.663  1.00 16.56 ? 245 TRP A CE3 1 
ATOM   1904 C  CZ2 . TRP A 1 244 ? -0.593  -14.003 16.356  1.00 14.80 ? 245 TRP A CZ2 1 
ATOM   1905 C  CZ3 . TRP A 1 244 ? -0.539  -12.589 18.337  1.00 17.83 ? 245 TRP A CZ3 1 
ATOM   1906 C  CH2 . TRP A 1 244 ? -0.287  -13.804 17.684  1.00 17.11 ? 245 TRP A CH2 1 
ATOM   1907 N  N   . ARG A 1 245 ? -0.424  -7.244  16.877  1.00 14.57 ? 246 ARG A N   1 
ATOM   1908 C  CA  . ARG A 1 245 ? 0.557   -7.158  17.974  1.00 13.20 ? 246 ARG A CA  1 
ATOM   1909 C  C   . ARG A 1 245 ? 0.063   -8.042  19.091  1.00 17.80 ? 246 ARG A C   1 
ATOM   1910 O  O   . ARG A 1 245 ? -1.144  -8.094  19.353  1.00 16.74 ? 246 ARG A O   1 
ATOM   1911 C  CB  . ARG A 1 245 ? 0.634   -5.716  18.492  1.00 13.96 ? 246 ARG A CB  1 
ATOM   1912 C  CG  . ARG A 1 245 ? 1.712   -5.505  19.557  1.00 13.62 ? 246 ARG A CG  1 
ATOM   1913 C  CD  . ARG A 1 245 ? 1.621   -4.055  20.053  1.00 12.89 ? 246 ARG A CD  1 
ATOM   1914 N  NE  . ARG A 1 245 ? 2.865   -3.803  20.832  1.00 14.43 ? 246 ARG A NE  1 
ATOM   1915 C  CZ  . ARG A 1 245 ? 3.046   -2.766  21.665  1.00 16.96 ? 246 ARG A CZ  1 
ATOM   1916 N  NH1 . ARG A 1 245 ? 2.046   -1.951  21.953  1.00 14.36 ? 246 ARG A NH1 1 
ATOM   1917 N  NH2 . ARG A 1 245 ? 4.257   -2.554  22.217  1.00 16.89 ? 246 ARG A NH2 1 
ATOM   1918 N  N   . PRO A 1 246 ? 0.955   -8.820  19.738  1.00 17.47 ? 247 PRO A N   1 
ATOM   1919 C  CA  . PRO A 1 246 ? 0.544   -9.656  20.865  1.00 16.92 ? 247 PRO A CA  1 
ATOM   1920 C  C   . PRO A 1 246 ? 0.239   -8.857  22.122  1.00 16.85 ? 247 PRO A C   1 
ATOM   1921 O  O   . PRO A 1 246 ? 0.604   -7.671  22.242  1.00 14.80 ? 247 PRO A O   1 
ATOM   1922 C  CB  . PRO A 1 246 ? 1.762   -10.585 21.091  1.00 18.50 ? 247 PRO A CB  1 
ATOM   1923 C  CG  . PRO A 1 246 ? 2.544   -10.503 19.795  1.00 21.56 ? 247 PRO A CG  1 
ATOM   1924 C  CD  . PRO A 1 246 ? 2.339   -9.088  19.293  1.00 19.89 ? 247 PRO A CD  1 
ATOM   1925 N  N   . ALA A 1 247 ? -0.411  -9.552  23.061  1.00 18.20 ? 248 ALA A N   1 
ATOM   1926 C  CA  . ALA A 1 247 ? -0.769  -8.965  24.338  1.00 16.34 ? 248 ALA A CA  1 
ATOM   1927 C  C   . ALA A 1 247 ? 0.485   -8.421  25.044  1.00 16.50 ? 248 ALA A C   1 
ATOM   1928 O  O   . ALA A 1 247 ? 1.555   -9.060  25.059  1.00 17.47 ? 248 ALA A O   1 
ATOM   1929 C  CB  . ALA A 1 247 ? -1.467  -10.030 25.148  1.00 19.44 ? 248 ALA A CB  1 
ATOM   1930 N  N   . GLN A 1 248 ? 0.314   -7.240  25.627  1.00 17.09 ? 249 GLN A N   1 
ATOM   1931 C  CA  . GLN A 1 248 ? 1.376   -6.549  26.339  1.00 16.35 ? 249 GLN A CA  1 
ATOM   1932 C  C   . GLN A 1 248 ? 1.028   -6.561  27.818  1.00 15.90 ? 249 GLN A C   1 
ATOM   1933 O  O   . GLN A 1 248 ? -0.111  -6.732  28.245  1.00 16.58 ? 249 GLN A O   1 
ATOM   1934 C  CB  . GLN A 1 248 ? 1.457   -5.099  25.847  1.00 16.18 ? 249 GLN A CB  1 
ATOM   1935 C  CG  . GLN A 1 248 ? 1.725   -4.966  24.328  1.00 17.33 ? 249 GLN A CG  1 
ATOM   1936 C  CD  . GLN A 1 248 ? 3.052   -5.602  23.965  1.00 18.86 ? 249 GLN A CD  1 
ATOM   1937 O  OE1 . GLN A 1 248 ? 4.072   -5.349  24.606  1.00 18.96 ? 249 GLN A OE1 1 
ATOM   1938 N  NE2 . GLN A 1 248 ? 3.045   -6.535  23.016  1.00 18.64 ? 249 GLN A NE2 1 
ATOM   1939 N  N   . PRO A 1 249 ? 2.026   -6.346  28.696  1.00 19.28 ? 250 PRO A N   1 
ATOM   1940 C  CA  . PRO A 1 249 ? 1.724   -6.486  30.103  1.00 18.09 ? 250 PRO A CA  1 
ATOM   1941 C  C   . PRO A 1 249 ? 0.795   -5.362  30.585  1.00 16.98 ? 250 PRO A C   1 
ATOM   1942 O  O   . PRO A 1 249 ? 0.902   -4.198  30.189  1.00 18.70 ? 250 PRO A O   1 
ATOM   1943 C  CB  . PRO A 1 249 ? 3.097   -6.590  30.767  1.00 21.95 ? 250 PRO A CB  1 
ATOM   1944 C  CG  . PRO A 1 249 ? 4.085   -6.078  29.722  1.00 20.94 ? 250 PRO A CG  1 
ATOM   1945 C  CD  . PRO A 1 249 ? 3.423   -6.074  28.365  1.00 19.07 ? 250 PRO A CD  1 
ATOM   1946 N  N   . LEU A 1 250 ? -0.139  -5.763  31.444  1.00 17.51 ? 251 LEU A N   1 
ATOM   1947 C  CA  . LEU A 1 250 ? -1.191  -4.890  31.962  1.00 17.97 ? 251 LEU A CA  1 
ATOM   1948 C  C   . LEU A 1 250 ? -0.612  -3.797  32.868  1.00 19.55 ? 251 LEU A C   1 
ATOM   1949 O  O   . LEU A 1 250 ? -1.132  -2.662  32.922  1.00 17.98 ? 251 LEU A O   1 
ATOM   1950 C  CB  . LEU A 1 250 ? -2.242  -5.744  32.686  1.00 19.08 ? 251 LEU A CB  1 
ATOM   1951 C  CG  . LEU A 1 250 ? -3.483  -4.978  33.135  1.00 21.14 ? 251 LEU A CG  1 
ATOM   1952 C  CD1 . LEU A 1 250 ? -4.285  -4.426  31.934  1.00 20.37 ? 251 LEU A CD1 1 
ATOM   1953 C  CD2 . LEU A 1 250 ? -4.350  -5.911  33.964  1.00 24.48 ? 251 LEU A CD2 1 
ATOM   1954 N  N   . LYS A 1 251 ? 0.446   -4.163  33.619  1.00 21.31 ? 252 LYS A N   1 
ATOM   1955 C  CA  . LYS A 1 251 ? 1.089   -3.217  34.520  1.00 22.59 ? 252 LYS A CA  1 
ATOM   1956 C  C   . LYS A 1 251 ? 0.058   -2.703  35.531  1.00 23.78 ? 252 LYS A C   1 
ATOM   1957 O  O   . LYS A 1 251 ? -0.724  -3.490  36.069  1.00 26.89 ? 252 LYS A O   1 
ATOM   1958 C  CB  . LYS A 1 251 ? 1.879   -2.169  33.739  1.00 23.67 ? 252 LYS A CB  1 
ATOM   1959 C  CG  . LYS A 1 251 ? 3.012   -2.783  32.935  1.00 24.14 ? 252 LYS A CG  1 
ATOM   1960 C  CD  . LYS A 1 251 ? 4.029   -1.820  32.417  1.00 27.93 ? 252 LYS A CD  1 
ATOM   1961 C  CE  . LYS A 1 251 ? 5.238   -2.585  31.918  1.00 30.65 ? 252 LYS A CE  1 
ATOM   1962 N  NZ  . LYS A 1 251 ? 6.035   -1.794  30.948  1.00 30.93 ? 252 LYS A NZ  1 
ATOM   1963 N  N   . ASN A 1 252 ? 0.060   -1.400  35.777  1.00 22.36 ? 253 ASN A N   1 
ATOM   1964 C  CA  . ASN A 1 252 ? -0.777  -0.840  36.831  1.00 31.88 ? 253 ASN A CA  1 
ATOM   1965 C  C   . ASN A 1 252 ? -2.109  -0.407  36.218  1.00 30.53 ? 253 ASN A C   1 
ATOM   1966 O  O   . ASN A 1 252 ? -2.404  0.800   36.212  1.00 33.85 ? 253 ASN A O   1 
ATOM   1967 C  CB  . ASN A 1 252 ? -0.076  0.357   37.499  1.00 34.73 ? 253 ASN A CB  1 
ATOM   1968 C  CG  . ASN A 1 252 ? -0.817  0.877   38.715  1.00 45.13 ? 253 ASN A CG  1 
ATOM   1969 O  OD1 . ASN A 1 252 ? -1.556  0.135   39.368  1.00 48.69 ? 253 ASN A OD1 1 
ATOM   1970 N  ND2 . ASN A 1 252 ? -0.632  2.152   39.026  1.00 47.64 ? 253 ASN A ND2 1 
ATOM   1971 N  N   . ARG A 1 253 ? -2.843  -1.365  35.618  1.00 20.64 ? 254 ARG A N   1 
ATOM   1972 C  CA  . ARG A 1 253 ? -4.164  -1.041  35.093  1.00 21.43 ? 254 ARG A CA  1 
ATOM   1973 C  C   . ARG A 1 253 ? -5.190  -2.058  35.564  1.00 22.91 ? 254 ARG A C   1 
ATOM   1974 O  O   . ARG A 1 253 ? -4.884  -3.242  35.735  1.00 25.01 ? 254 ARG A O   1 
ATOM   1975 C  CB  . ARG A 1 253 ? -4.133  -0.973  33.556  1.00 18.25 ? 254 ARG A CB  1 
ATOM   1976 C  CG  . ARG A 1 253 ? -3.271  0.177   33.052  1.00 18.05 ? 254 ARG A CG  1 
ATOM   1977 C  CD  . ARG A 1 253 ? -3.077  0.147   31.539  1.00 16.50 ? 254 ARG A CD  1 
ATOM   1978 N  NE  . ARG A 1 253 ? -2.243  -0.942  31.062  1.00 17.30 ? 254 ARG A NE  1 
ATOM   1979 C  CZ  . ARG A 1 253 ? -2.011  -1.206  29.775  1.00 15.37 ? 254 ARG A CZ  1 
ATOM   1980 N  NH1 . ARG A 1 253 ? -2.674  -0.546  28.830  1.00 15.78 ? 254 ARG A NH1 1 
ATOM   1981 N  NH2 . ARG A 1 253 ? -1.204  -2.203  29.454  1.00 15.41 ? 254 ARG A NH2 1 
ATOM   1982 N  N   . GLN A 1 254 ? -6.436  -1.591  35.699  1.00 21.14 ? 255 GLN A N   1 
ATOM   1983 C  CA  . GLN A 1 254 ? -7.587  -2.430  35.954  1.00 21.52 ? 255 GLN A CA  1 
ATOM   1984 C  C   . GLN A 1 254 ? -8.464  -2.332  34.709  1.00 22.74 ? 255 GLN A C   1 
ATOM   1985 O  O   . GLN A 1 254 ? -8.664  -1.240  34.178  1.00 26.06 ? 255 GLN A O   1 
ATOM   1986 C  CB  . GLN A 1 254 ? -8.350  -1.819  37.140  1.00 22.97 ? 255 GLN A CB  1 
ATOM   1987 C  CG  . GLN A 1 254 ? -9.182  -2.833  37.920  1.00 30.43 ? 255 GLN A CG  1 
ATOM   1988 N  N   . ILE A 1 255 ? -8.930  -3.474  34.229  1.00 19.02 ? 256 ILE A N   1 
ATOM   1989 C  CA  . ILE A 1 255 ? -9.928  -3.486  33.166  1.00 18.73 ? 256 ILE A CA  1 
ATOM   1990 C  C   . ILE A 1 255 ? -11.289 -3.408  33.851  1.00 19.47 ? 256 ILE A C   1 
ATOM   1991 O  O   . ILE A 1 255 ? -11.556 -4.152  34.803  1.00 18.52 ? 256 ILE A O   1 
ATOM   1992 C  CB  . ILE A 1 255 ? -9.759  -4.760  32.301  1.00 16.61 ? 256 ILE A CB  1 
ATOM   1993 C  CG1 . ILE A 1 255 ? -8.320  -4.839  31.765  1.00 20.15 ? 256 ILE A CG1 1 
ATOM   1994 C  CG2 . ILE A 1 255 ? -10.825 -4.849  31.184  1.00 17.75 ? 256 ILE A CG2 1 
ATOM   1995 C  CD1 . ILE A 1 255 ? -8.062  -6.000  30.828  1.00 21.16 ? 256 ILE A CD1 1 
ATOM   1996 N  N   . LYS A 1 256 ? -12.168 -2.552  33.325  1.00 16.76 ? 257 LYS A N   1 
ATOM   1997 C  CA  . LYS A 1 256 ? -13.500 -2.408  33.875  1.00 16.62 ? 257 LYS A CA  1 
ATOM   1998 C  C   . LYS A 1 256 ? -14.495 -3.103  32.948  1.00 18.90 ? 257 LYS A C   1 
ATOM   1999 O  O   . LYS A 1 256 ? -14.244 -3.145  31.738  1.00 18.44 ? 257 LYS A O   1 
ATOM   2000 C  CB  . LYS A 1 256 ? -13.858 -0.928  34.031  1.00 18.35 ? 257 LYS A CB  1 
ATOM   2001 C  CG  . LYS A 1 256 ? -13.059 -0.220  35.123  1.00 22.33 ? 257 LYS A CG  1 
ATOM   2002 N  N   . ALA A 1 257 ? -15.569 -3.662  33.516  1.00 16.22 ? 258 ALA A N   1 
ATOM   2003 C  CA  . ALA A 1 257 ? -16.621 -4.220  32.672  1.00 16.98 ? 258 ALA A CA  1 
ATOM   2004 C  C   . ALA A 1 257 ? -17.910 -3.400  32.787  1.00 19.88 ? 258 ALA A C   1 
ATOM   2005 O  O   . ALA A 1 257 ? -18.231 -2.913  33.877  1.00 19.57 ? 258 ALA A O   1 
ATOM   2006 C  CB  . ALA A 1 257 ? -16.869 -5.669  32.993  1.00 16.59 ? 258 ALA A CB  1 
ATOM   2007 N  N   . SER A 1 258 ? -18.691 -3.327  31.682  1.00 18.61 ? 259 SER A N   1 
ATOM   2008 C  CA  . SER A 1 258 ? -19.980 -2.653  31.730  1.00 20.25 ? 259 SER A CA  1 
ATOM   2009 C  C   . SER A 1 258 ? -21.082 -3.613  32.205  1.00 21.14 ? 259 SER A C   1 
ATOM   2010 O  O   . SER A 1 258 ? -22.253 -3.222  32.302  1.00 22.88 ? 259 SER A O   1 
ATOM   2011 C  CB  . SER A 1 258 ? -20.324 -2.080  30.395  1.00 20.34 ? 259 SER A CB  1 
ATOM   2012 O  OG  . SER A 1 258 ? -20.782 -3.108  29.527  1.00 19.09 ? 259 SER A OG  1 
ATOM   2013 N  N   . PHE A 1 259 ? -20.729 -4.869  32.474  1.00 21.27 ? 260 PHE A N   1 
ATOM   2014 C  CA  . PHE A 1 259 ? -21.744 -5.898  32.659  1.00 23.25 ? 260 PHE A CA  1 
ATOM   2015 C  C   . PHE A 1 259 ? -21.310 -6.876  33.746  1.00 31.30 ? 260 PHE A C   1 
ATOM   2016 O  O   . PHE A 1 259 ? -20.109 -6.988  34.059  1.00 26.62 ? 260 PHE A O   1 
ATOM   2017 C  CB  . PHE A 1 259 ? -22.001 -6.650  31.350  1.00 21.99 ? 260 PHE A CB  1 
ATOM   2018 C  CG  . PHE A 1 259 ? -20.771 -7.358  30.833  1.00 20.44 ? 260 PHE A CG  1 
ATOM   2019 C  CD1 . PHE A 1 259 ? -19.778 -6.648  30.161  1.00 20.43 ? 260 PHE A CD1 1 
ATOM   2020 C  CD2 . PHE A 1 259 ? -20.543 -8.695  31.134  1.00 22.49 ? 260 PHE A CD2 1 
ATOM   2021 C  CE1 . PHE A 1 259 ? -18.598 -7.278  29.793  1.00 20.43 ? 260 PHE A CE1 1 
ATOM   2022 C  CE2 . PHE A 1 259 ? -19.366 -9.326  30.759  1.00 21.17 ? 260 PHE A CE2 1 
ATOM   2023 C  CZ  . PHE A 1 259 ? -18.403 -8.610  30.064  1.00 21.15 ? 260 PHE A CZ  1 
ATOM   2024 N  N   . LYS A 1 260 ? -22.353 -7.574  34.249  1.00 39.31 ? 261 LYS A N   1 
ATOM   2025 C  CA  . LYS A 1 260 ? -22.405 -8.740  35.128  1.00 53.97 ? 261 LYS A CA  1 
ATOM   2026 C  C   . LYS A 1 260 ? -22.036 -8.386  36.577  1.00 64.60 ? 261 LYS A C   1 
ATOM   2027 O  O   . LYS A 1 260 ? -22.412 -7.319  37.093  1.00 73.29 ? 261 LYS A O   1 
ATOM   2028 C  CB  . LYS A 1 260 ? -21.768 -10.002 34.528  1.00 57.47 ? 261 LYS A CB  1 
ATOM   2029 C  CG  . LYS A 1 260 ? -22.467 -10.589 33.298  1.00 59.54 ? 261 LYS A CG  1 
ATOM   2030 C  CD  . LYS A 1 260 ? -23.975 -10.361 33.196  1.00 62.83 ? 261 LYS A CD  1 
ATOM   2031 O  OXT . LYS A 1 260 ? -21.382 -9.162  37.277  1.00 72.88 ? 261 LYS A OXT 1 
HETATM 2032 ZN ZN  . ZN  B 2 .   ? -5.952  -1.713  15.057  1.00 13.22 ? 301 ZN  A ZN  1 
HETATM 2033 O  O16 . WWX C 3 .   ? -4.133  1.748   9.300   1.00 37.01 ? 302 WWX A O16 1 
HETATM 2034 S  S14 . WWX C 3 .   ? -3.102  2.541   10.121  1.00 34.80 ? 302 WWX A S14 1 
HETATM 2035 O  O15 . WWX C 3 .   ? -3.323  4.046   9.817   1.00 34.19 ? 302 WWX A O15 1 
HETATM 2036 C  C18 . WWX C 3 .   ? -0.536  2.180   10.766  1.00 32.49 ? 302 WWX A C18 1 
HETATM 2037 O  O20 . WWX C 3 .   ? -0.627  3.536   11.103  1.00 42.34 ? 302 WWX A O20 1 
HETATM 2038 C  C17 . WWX C 3 .   ? -1.454  2.018   9.573   1.00 35.77 ? 302 WWX A C17 1 
HETATM 2039 C  C8  . WWX C 3 .   ? -3.527  2.205   11.832  1.00 26.03 ? 302 WWX A C8  1 
HETATM 2040 C  C7  . WWX C 3 .   ? -3.467  0.872   12.214  1.00 26.46 ? 302 WWX A C7  1 
HETATM 2041 F  F12 . WWX C 3 .   ? -3.045  -0.080  11.335  1.00 26.70 ? 302 WWX A F12 1 
HETATM 2042 C  C6  . WWX C 3 .   ? -3.780  0.466   13.497  1.00 22.01 ? 302 WWX A C6  1 
HETATM 2043 F  F11 . WWX C 3 .   ? -3.635  -0.848  13.751  1.00 23.50 ? 302 WWX A F11 1 
HETATM 2044 C  C9  . WWX C 3 .   ? -3.954  3.169   12.745  1.00 25.10 ? 302 WWX A C9  1 
HETATM 2045 C  C10 . WWX C 3 .   ? -4.252  2.738   14.049  1.00 23.04 ? 302 WWX A C10 1 
HETATM 2046 F  F13 . WWX C 3 .   ? -4.677  3.642   14.955  1.00 25.03 ? 302 WWX A F13 1 
HETATM 2047 C  C5  . WWX C 3 .   ? -4.194  1.380   14.459  1.00 21.31 ? 302 WWX A C5  1 
HETATM 2048 S  S1  . WWX C 3 .   ? -4.759  0.842   16.134  1.00 23.87 ? 302 WWX A S1  1 
HETATM 2049 O  O3  . WWX C 3 .   ? -3.973  1.363   17.357  1.00 25.13 ? 302 WWX A O3  1 
HETATM 2050 N  N4  . WWX C 3 .   ? -4.607  -0.958  16.186  1.00 20.58 ? 302 WWX A N4  1 
HETATM 2051 O  O2  . WWX C 3 .   ? -6.215  1.334   16.276  1.00 23.27 ? 302 WWX A O2  1 
HETATM 2052 N  N19 . WWX C 3 .   ? -4.004  4.537   12.348  1.00 25.25 ? 302 WWX A N19 1 
HETATM 2053 C  C21 . WWX C 3 .   ? -3.551  5.685   13.194  1.00 26.31 ? 302 WWX A C21 1 
HETATM 2054 C  C30 . WWX C 3 .   ? -4.691  6.642   13.444  1.00 25.22 ? 302 WWX A C30 1 
HETATM 2055 C  C35 . WWX C 3 .   ? -4.797  7.316   14.678  1.00 26.03 ? 302 WWX A C35 1 
HETATM 2056 C  C34 . WWX C 3 .   ? -5.885  8.185   14.890  1.00 25.93 ? 302 WWX A C34 1 
HETATM 2057 C  C33 . WWX C 3 .   ? -6.820  8.377   13.874  1.00 26.32 ? 302 WWX A C33 1 
HETATM 2058 C  C32 . WWX C 3 .   ? -6.719  7.699   12.640  1.00 28.06 ? 302 WWX A C32 1 
HETATM 2059 C  C31 . WWX C 3 .   ? -5.645  6.841   12.437  1.00 28.73 ? 302 WWX A C31 1 
HETATM 2060 C  C22 . WWX C 3 .   ? -2.382  6.427   12.512  1.00 27.92 ? 302 WWX A C22 1 
HETATM 2061 O  O29 . WWX C 3 .   ? -2.756  6.747   11.216  1.00 28.26 ? 302 WWX A O29 1 
HETATM 2062 C  C23 . WWX C 3 .   ? -1.918  7.619   13.301  1.00 28.55 ? 302 WWX A C23 1 
HETATM 2063 C  C28 . WWX C 3 .   ? -2.438  8.914   13.064  1.00 30.14 ? 302 WWX A C28 1 
HETATM 2064 C  C27 . WWX C 3 .   ? -1.972  9.994   13.890  1.00 32.32 ? 302 WWX A C27 1 
HETATM 2065 C  C26 . WWX C 3 .   ? -1.019  9.794   14.909  1.00 30.85 ? 302 WWX A C26 1 
HETATM 2066 C  C25 . WWX C 3 .   ? -0.500  8.521   15.107  1.00 30.63 ? 302 WWX A C25 1 
HETATM 2067 C  C24 . WWX C 3 .   ? -0.957  7.438   14.328  1.00 30.30 ? 302 WWX A C24 1 
HETATM 2068 O  O   . HOH D 4 .   ? -13.723 -16.230 29.036  1.00 40.89 ? 401 HOH A O   1 
HETATM 2069 O  O   . HOH D 4 .   ? -24.874 -10.435 17.345  1.00 38.13 ? 402 HOH A O   1 
HETATM 2070 O  O   . HOH D 4 .   ? -4.138  20.127  20.939  1.00 38.50 ? 403 HOH A O   1 
HETATM 2071 O  O   . HOH D 4 .   ? -17.208 19.053  5.776   1.00 14.29 ? 404 HOH A O   1 
HETATM 2072 O  O   . HOH D 4 .   ? -24.719 9.809   13.428  1.00 30.33 ? 405 HOH A O   1 
HETATM 2073 O  O   . HOH D 4 .   ? -0.595  -12.416 -3.789  1.00 41.69 ? 406 HOH A O   1 
HETATM 2074 O  O   . HOH D 4 .   ? -13.779 -18.358 18.731  1.00 39.19 ? 407 HOH A O   1 
HETATM 2075 O  O   . HOH D 4 .   ? -25.826 13.653  6.474   1.00 30.03 ? 408 HOH A O   1 
HETATM 2076 O  O   . HOH D 4 .   ? 7.100   -1.661  -5.015  1.00 40.69 ? 409 HOH A O   1 
HETATM 2077 O  O   . HOH D 4 .   ? -30.689 -10.906 16.074  1.00 29.32 ? 410 HOH A O   1 
HETATM 2078 O  O   . HOH D 4 .   ? 15.652  3.440   20.695  1.00 31.23 ? 411 HOH A O   1 
HETATM 2079 O  O   . HOH D 4 .   ? -9.751  -18.200 16.707  1.00 26.87 ? 412 HOH A O   1 
HETATM 2080 O  O   . HOH D 4 .   ? -10.685 -19.447 7.346   1.00 42.46 ? 413 HOH A O   1 
HETATM 2081 O  O   . HOH D 4 .   ? -19.607 -16.713 3.143   1.00 29.62 ? 414 HOH A O   1 
HETATM 2082 O  O   . HOH D 4 .   ? 7.775   2.562   31.704  1.00 43.17 ? 415 HOH A O   1 
HETATM 2083 O  O   . HOH D 4 .   ? -5.953  -20.255 19.215  1.00 25.16 ? 416 HOH A O   1 
HETATM 2084 O  O   . HOH D 4 .   ? 0.723   0.937   34.169  1.00 27.59 ? 417 HOH A O   1 
HETATM 2085 O  O   . HOH D 4 .   ? -4.244  2.361   37.029  1.00 39.64 ? 418 HOH A O   1 
HETATM 2086 O  O   . HOH D 4 .   ? -13.576 -9.020  -5.294  1.00 18.26 ? 419 HOH A O   1 
HETATM 2087 O  O   . HOH D 4 .   ? -1.666  -3.022  11.277  1.00 35.87 ? 420 HOH A O   1 
HETATM 2088 O  O   . HOH D 4 .   ? 11.677  -6.722  22.354  1.00 32.31 ? 421 HOH A O   1 
HETATM 2089 O  O   . HOH D 4 .   ? -10.584 -15.362 33.932  1.00 42.22 ? 422 HOH A O   1 
HETATM 2090 O  O   . HOH D 4 .   ? -18.576 17.444  18.553  1.00 41.90 ? 423 HOH A O   1 
HETATM 2091 O  O   . HOH D 4 .   ? -6.040  16.432  11.045  1.00 39.98 ? 424 HOH A O   1 
HETATM 2092 O  O   . HOH D 4 .   ? -13.638 -5.329  -6.936  1.00 33.96 ? 425 HOH A O   1 
HETATM 2093 O  O   . HOH D 4 .   ? -25.639 3.395   15.492  1.00 34.72 ? 426 HOH A O   1 
HETATM 2094 O  O   . HOH D 4 .   ? 4.252   5.012   29.614  1.00 22.18 ? 427 HOH A O   1 
HETATM 2095 O  O   . HOH D 4 .   ? -20.535 -6.572  -2.361  1.00 31.31 ? 428 HOH A O   1 
HETATM 2096 O  O   . HOH D 4 .   ? -0.356  3.924   13.978  1.00 39.93 ? 429 HOH A O   1 
HETATM 2097 O  O   . HOH D 4 .   ? -0.626  -4.042  15.392  1.00 16.00 ? 430 HOH A O   1 
HETATM 2098 O  O   . HOH D 4 .   ? -6.245  -14.874 31.289  1.00 27.82 ? 431 HOH A O   1 
HETATM 2099 O  O   . HOH D 4 .   ? -26.706 2.779   23.381  1.00 34.90 ? 432 HOH A O   1 
HETATM 2100 O  O   . HOH D 4 .   ? 12.157  -0.377  15.618  1.00 29.81 ? 433 HOH A O   1 
HETATM 2101 O  O   . HOH D 4 .   ? -0.744  -16.072 -3.481  1.00 35.66 ? 434 HOH A O   1 
HETATM 2102 O  O   . HOH D 4 .   ? -15.721 -10.427 -4.779  1.00 31.75 ? 435 HOH A O   1 
HETATM 2103 O  O   . HOH D 4 .   ? -4.135  -11.905 31.804  1.00 33.35 ? 436 HOH A O   1 
HETATM 2104 O  O   . HOH D 4 .   ? -18.847 -20.745 4.757   1.00 25.91 ? 437 HOH A O   1 
HETATM 2105 O  O   . HOH D 4 .   ? -21.179 -18.616 13.582  1.00 30.61 ? 438 HOH A O   1 
HETATM 2106 O  O   . HOH D 4 .   ? -16.015 -14.673 32.664  1.00 41.60 ? 439 HOH A O   1 
HETATM 2107 O  O   . HOH D 4 .   ? -15.360 15.913  23.223  1.00 27.77 ? 440 HOH A O   1 
HETATM 2108 O  O   . HOH D 4 .   ? -12.373 -22.480 11.788  1.00 33.87 ? 441 HOH A O   1 
HETATM 2109 O  O   . HOH D 4 .   ? -13.154 10.717  27.501  1.00 32.69 ? 442 HOH A O   1 
HETATM 2110 O  O   . HOH D 4 .   ? 3.101   8.015   27.625  1.00 37.25 ? 443 HOH A O   1 
HETATM 2111 O  O   . HOH D 4 .   ? -3.691  -8.888  30.968  1.00 27.56 ? 444 HOH A O   1 
HETATM 2112 O  O   . HOH D 4 .   ? -16.494 -16.376 21.608  1.00 33.88 ? 445 HOH A O   1 
HETATM 2113 O  O   . HOH D 4 .   ? 4.872   -2.299  28.462  1.00 35.79 ? 446 HOH A O   1 
HETATM 2114 O  O   . HOH D 4 .   ? -23.349 8.591   20.029  1.00 28.10 ? 447 HOH A O   1 
HETATM 2115 O  O   . HOH D 4 .   ? 11.815  1.668   25.867  1.00 28.97 ? 448 HOH A O   1 
HETATM 2116 O  O   . HOH D 4 .   ? 4.941   -3.557  26.398  1.00 25.36 ? 449 HOH A O   1 
HETATM 2117 O  O   . HOH D 4 .   ? -27.266 -12.253 16.193  1.00 43.83 ? 450 HOH A O   1 
HETATM 2118 O  O   . HOH D 4 .   ? -15.252 -10.043 37.745  1.00 37.12 ? 451 HOH A O   1 
HETATM 2119 O  O   . HOH D 4 .   ? -3.852  -13.468 17.853  1.00 15.54 ? 452 HOH A O   1 
HETATM 2120 O  O   . HOH D 4 .   ? -7.288  -15.474 11.093  1.00 18.00 ? 453 HOH A O   1 
HETATM 2121 O  O   . HOH D 4 .   ? -4.519  -20.627 6.267   1.00 31.39 ? 454 HOH A O   1 
HETATM 2122 O  O   . HOH D 4 .   ? 8.484   -8.233  -0.109  1.00 29.36 ? 455 HOH A O   1 
HETATM 2123 O  O   . HOH D 4 .   ? 3.353   -13.046 5.118   1.00 25.21 ? 456 HOH A O   1 
HETATM 2124 O  O   . HOH D 4 .   ? 5.907   7.181   20.226  1.00 20.46 ? 457 HOH A O   1 
HETATM 2125 O  O   . HOH D 4 .   ? -13.035 -16.112 -0.454  1.00 32.75 ? 458 HOH A O   1 
HETATM 2126 O  O   . HOH D 4 .   ? -18.236 -4.166  -2.713  1.00 28.41 ? 459 HOH A O   1 
HETATM 2127 O  O   . HOH D 4 .   ? -17.336 10.483  11.082  1.00 23.91 ? 460 HOH A O   1 
HETATM 2128 O  O   . HOH D 4 .   ? -19.589 10.995  26.527  1.00 30.06 ? 461 HOH A O   1 
HETATM 2129 O  O   . HOH D 4 .   ? -12.583 19.731  13.867  1.00 38.74 ? 462 HOH A O   1 
HETATM 2130 O  O   . HOH D 4 .   ? -24.468 4.732   8.487   1.00 36.12 ? 463 HOH A O   1 
HETATM 2131 O  O   . HOH D 4 .   ? -3.271  -12.954 -3.166  1.00 27.69 ? 464 HOH A O   1 
HETATM 2132 O  O   . HOH D 4 .   ? -12.425 -9.044  -3.375  1.00 20.48 ? 465 HOH A O   1 
HETATM 2133 O  O   . HOH D 4 .   ? -9.807  8.691   25.179  1.00 19.39 ? 466 HOH A O   1 
HETATM 2134 O  O   . HOH D 4 .   ? -13.237 14.567  26.943  1.00 39.66 ? 467 HOH A O   1 
HETATM 2135 O  O   . HOH D 4 .   ? 1.186   -1.474  -5.115  1.00 23.90 ? 468 HOH A O   1 
HETATM 2136 O  O   . HOH D 4 .   ? -26.011 -2.462  14.148  1.00 19.68 ? 469 HOH A O   1 
HETATM 2137 O  O   . HOH D 4 .   ? 2.077   -11.706 24.669  1.00 27.63 ? 470 HOH A O   1 
HETATM 2138 O  O   . HOH D 4 .   ? 6.561   -3.363  6.592   1.00 40.96 ? 471 HOH A O   1 
HETATM 2139 O  O   . HOH D 4 .   ? -1.833  -8.752  28.878  1.00 18.49 ? 472 HOH A O   1 
HETATM 2140 O  O   . HOH D 4 .   ? -23.300 -2.455  28.680  1.00 31.89 ? 473 HOH A O   1 
HETATM 2141 O  O   . HOH D 4 .   ? -22.611 -2.819  6.399   1.00 19.93 ? 474 HOH A O   1 
HETATM 2142 O  O   . HOH D 4 .   ? -16.346 -8.308  20.130  1.00 15.20 ? 475 HOH A O   1 
HETATM 2143 O  O   . HOH D 4 .   ? -2.944  -4.296  37.465  1.00 44.36 ? 476 HOH A O   1 
HETATM 2144 O  O   . HOH D 4 .   ? -7.929  0.410   -6.861  1.00 29.37 ? 477 HOH A O   1 
HETATM 2145 O  O   . HOH D 4 .   ? -0.945  -5.089  -7.437  1.00 38.72 ? 478 HOH A O   1 
HETATM 2146 O  O   . HOH D 4 .   ? -5.381  -4.847  -6.712  1.00 24.91 ? 479 HOH A O   1 
HETATM 2147 O  O   . HOH D 4 .   ? -22.355 -0.628  34.154  1.00 30.67 ? 480 HOH A O   1 
HETATM 2148 O  O   . HOH D 4 .   ? -17.252 -20.388 7.764   1.00 17.90 ? 481 HOH A O   1 
HETATM 2149 O  O   . HOH D 4 .   ? 1.999   10.882  16.861  1.00 43.90 ? 482 HOH A O   1 
HETATM 2150 O  O   . HOH D 4 .   ? -20.491 7.742   1.718   1.00 18.16 ? 483 HOH A O   1 
HETATM 2151 O  O   . HOH D 4 .   ? 1.483   -6.660  34.213  1.00 30.63 ? 484 HOH A O   1 
HETATM 2152 O  O   . HOH D 4 .   ? 0.229   10.682  23.035  1.00 29.92 ? 485 HOH A O   1 
HETATM 2153 O  O   . HOH D 4 .   ? 9.104   -3.727  20.948  1.00 20.74 ? 486 HOH A O   1 
HETATM 2154 O  O   . HOH D 4 .   ? -2.779  -11.156 20.606  1.00 17.82 ? 487 HOH A O   1 
HETATM 2155 O  O   . HOH D 4 .   ? -25.338 -6.232  12.794  1.00 31.38 ? 488 HOH A O   1 
HETATM 2156 O  O   . HOH D 4 .   ? 3.491   -4.311  7.438   1.00 27.94 ? 489 HOH A O   1 
HETATM 2157 O  O   . HOH D 4 .   ? -25.303 6.328   26.773  1.00 34.12 ? 490 HOH A O   1 
HETATM 2158 O  O   . HOH D 4 .   ? -12.044 7.814   28.472  1.00 35.19 ? 491 HOH A O   1 
HETATM 2159 O  O   . HOH D 4 .   ? -14.319 20.121  17.374  1.00 34.35 ? 492 HOH A O   1 
HETATM 2160 O  O   . HOH D 4 .   ? -4.066  -15.907 0.484   1.00 30.83 ? 493 HOH A O   1 
HETATM 2161 O  O   . HOH D 4 .   ? -18.823 -12.248 -3.317  1.00 22.76 ? 494 HOH A O   1 
HETATM 2162 O  O   . HOH D 4 .   ? -24.244 11.923  6.150   1.00 21.27 ? 495 HOH A O   1 
HETATM 2163 O  O   . HOH D 4 .   ? -24.386 -7.656  8.881   1.00 19.37 ? 496 HOH A O   1 
HETATM 2164 O  O   . HOH D 4 .   ? -11.687 12.673  28.984  1.00 35.77 ? 497 HOH A O   1 
HETATM 2165 O  O   . HOH D 4 .   ? 13.948  0.433   24.405  1.00 24.07 ? 498 HOH A O   1 
HETATM 2166 O  O   . HOH D 4 .   ? -22.285 -5.783  2.631   1.00 21.55 ? 499 HOH A O   1 
HETATM 2167 O  O   . HOH D 4 .   ? -22.732 -11.330 16.975  1.00 35.04 ? 500 HOH A O   1 
HETATM 2168 O  O   . HOH D 4 .   ? -15.383 -12.387 24.194  1.00 23.65 ? 501 HOH A O   1 
HETATM 2169 O  O   . HOH D 4 .   ? -6.664  -8.719  32.371  1.00 25.68 ? 502 HOH A O   1 
HETATM 2170 O  O   . HOH D 4 .   ? -21.238 5.655   4.617   1.00 16.37 ? 503 HOH A O   1 
HETATM 2171 O  O   . HOH D 4 .   ? -10.814 10.126  7.908   1.00 25.41 ? 504 HOH A O   1 
HETATM 2172 O  O   . HOH D 4 .   ? -11.310 3.014   30.401  1.00 30.11 ? 505 HOH A O   1 
HETATM 2173 O  O   . HOH D 4 .   ? -18.904 17.199  5.655   1.00 34.66 ? 506 HOH A O   1 
HETATM 2174 O  O   . HOH D 4 .   ? -7.659  -22.157 10.375  1.00 30.26 ? 507 HOH A O   1 
HETATM 2175 O  O   . HOH D 4 .   ? 2.699   -15.604 9.101   1.00 21.70 ? 508 HOH A O   1 
HETATM 2176 O  O   . HOH D 4 .   ? 11.117  -9.087  8.921   1.00 29.97 ? 509 HOH A O   1 
HETATM 2177 O  O   . HOH D 4 .   ? 8.740   -9.352  16.430  1.00 30.40 ? 510 HOH A O   1 
HETATM 2178 O  O   . HOH D 4 .   ? -14.991 9.031   -2.315  1.00 27.08 ? 511 HOH A O   1 
HETATM 2179 O  O   . HOH D 4 .   ? 5.248   3.427   3.547   1.00 37.56 ? 512 HOH A O   1 
HETATM 2180 O  O   . HOH D 4 .   ? -18.517 9.916   8.687   1.00 16.91 ? 513 HOH A O   1 
HETATM 2181 O  O   . HOH D 4 .   ? -2.635  -13.314 24.967  1.00 18.52 ? 514 HOH A O   1 
HETATM 2182 O  O   . HOH D 4 .   ? -25.304 7.929   6.226   1.00 29.92 ? 515 HOH A O   1 
HETATM 2183 O  O   . HOH D 4 .   ? 5.500   -4.898  20.778  1.00 18.18 ? 516 HOH A O   1 
HETATM 2184 O  O   . HOH D 4 .   ? 2.178   -15.931 -6.836  1.00 41.64 ? 517 HOH A O   1 
HETATM 2185 O  O   . HOH D 4 .   ? -18.819 -4.291  41.178  1.00 35.72 ? 518 HOH A O   1 
HETATM 2186 O  O   . HOH D 4 .   ? -3.009  -15.885 24.158  1.00 20.08 ? 519 HOH A O   1 
HETATM 2187 O  O   . HOH D 4 .   ? -20.845 -7.077  23.318  1.00 16.79 ? 520 HOH A O   1 
HETATM 2188 O  O   . HOH D 4 .   ? -3.664  5.595   -2.865  1.00 29.37 ? 521 HOH A O   1 
HETATM 2189 O  O   . HOH D 4 .   ? -18.275 12.229  12.603  1.00 31.78 ? 522 HOH A O   1 
HETATM 2190 O  O   . HOH D 4 .   ? 5.958   -10.728 18.707  1.00 40.89 ? 523 HOH A O   1 
HETATM 2191 O  O   . HOH D 4 .   ? -12.771 -0.777  -6.022  1.00 31.25 ? 524 HOH A O   1 
HETATM 2192 O  O   . HOH D 4 .   ? -5.317  -19.662 23.528  1.00 40.68 ? 525 HOH A O   1 
HETATM 2193 O  O   . HOH D 4 .   ? 0.311   -8.455  32.285  1.00 30.13 ? 526 HOH A O   1 
HETATM 2194 O  O   . HOH D 4 .   ? -12.682 -18.518 14.574  1.00 29.62 ? 527 HOH A O   1 
HETATM 2195 O  O   . HOH D 4 .   ? -22.735 -13.279 11.424  1.00 26.36 ? 528 HOH A O   1 
HETATM 2196 O  O   . HOH D 4 .   ? -16.301 -14.002 37.116  1.00 36.75 ? 529 HOH A O   1 
HETATM 2197 O  O   . HOH D 4 .   ? 10.228  1.914   11.838  1.00 43.63 ? 530 HOH A O   1 
HETATM 2198 O  O   . HOH D 4 .   ? 4.411   4.458   10.432  1.00 37.63 ? 531 HOH A O   1 
HETATM 2199 O  O   . HOH D 4 .   ? -25.524 -14.775 8.252   1.00 38.81 ? 532 HOH A O   1 
HETATM 2200 O  O   . HOH D 4 .   ? -6.616  -16.655 0.983   1.00 27.80 ? 533 HOH A O   1 
HETATM 2201 O  O   . HOH D 4 .   ? 1.915   -1.675  29.107  1.00 19.22 ? 534 HOH A O   1 
HETATM 2202 O  O   . HOH D 4 .   ? 4.604   -3.401  4.023   1.00 36.69 ? 535 HOH A O   1 
HETATM 2203 O  O   . HOH D 4 .   ? 14.946  0.050   14.624  1.00 24.78 ? 536 HOH A O   1 
HETATM 2204 O  O   . HOH D 4 .   ? -12.420 -16.805 26.298  1.00 29.77 ? 537 HOH A O   1 
HETATM 2205 O  O   . HOH D 4 .   ? 5.148   -6.834  7.678   1.00 28.66 ? 538 HOH A O   1 
HETATM 2206 O  O   . HOH D 4 .   ? -8.340  -5.962  35.579  1.00 23.81 ? 539 HOH A O   1 
HETATM 2207 O  O   . HOH D 4 .   ? -17.985 4.037   -3.884  1.00 28.01 ? 540 HOH A O   1 
HETATM 2208 O  O   . HOH D 4 .   ? -23.295 -0.712  26.443  1.00 26.62 ? 541 HOH A O   1 
HETATM 2209 O  O   . HOH D 4 .   ? -18.302 20.549  15.161  1.00 48.26 ? 542 HOH A O   1 
HETATM 2210 O  O   . HOH D 4 .   ? -8.458  14.722  11.715  1.00 28.41 ? 543 HOH A O   1 
HETATM 2211 O  O   . HOH D 4 .   ? -17.992 -8.944  34.377  1.00 31.81 ? 544 HOH A O   1 
HETATM 2212 O  O   . HOH D 4 .   ? 6.018   -7.116  22.184  1.00 28.01 ? 545 HOH A O   1 
HETATM 2213 O  O   . HOH D 4 .   ? -26.038 -3.949  25.101  1.00 24.51 ? 546 HOH A O   1 
HETATM 2214 O  O   . HOH D 4 .   ? 3.275   -11.442 9.475   1.00 28.31 ? 547 HOH A O   1 
HETATM 2215 O  O   . HOH D 4 .   ? -23.168 -0.849  3.749   1.00 22.19 ? 548 HOH A O   1 
HETATM 2216 O  O   . HOH D 4 .   ? 13.702  -5.649  24.543  1.00 34.01 ? 549 HOH A O   1 
HETATM 2217 O  O   . HOH D 4 .   ? -6.323  -8.720  -7.493  1.00 35.68 ? 550 HOH A O   1 
HETATM 2218 O  O   . HOH D 4 .   ? -15.866 -9.913  32.580  1.00 23.11 ? 551 HOH A O   1 
HETATM 2219 O  O   . HOH D 4 .   ? 10.837  -2.569  13.237  1.00 28.62 ? 552 HOH A O   1 
HETATM 2220 O  O   . HOH D 4 .   ? -16.402 -7.245  39.428  1.00 32.77 ? 553 HOH A O   1 
HETATM 2221 O  O   . HOH D 4 .   ? -8.865  -8.108  33.804  1.00 30.50 ? 554 HOH A O   1 
HETATM 2222 O  O   . HOH D 4 .   ? 2.207   8.709   23.767  1.00 23.91 ? 555 HOH A O   1 
HETATM 2223 O  O   . HOH D 4 .   ? -24.981 -6.326  33.732  1.00 45.55 ? 556 HOH A O   1 
HETATM 2224 O  O   . HOH D 4 .   ? -11.594 16.495  10.102  1.00 35.64 ? 557 HOH A O   1 
HETATM 2225 O  O   . HOH D 4 .   ? -7.508  -19.316 21.412  1.00 28.73 ? 558 HOH A O   1 
HETATM 2226 O  O   . HOH D 4 .   ? 13.519  -3.611  12.900  1.00 28.21 ? 559 HOH A O   1 
HETATM 2227 O  O   . HOH D 4 .   ? -20.340 19.229  13.144  1.00 42.91 ? 560 HOH A O   1 
HETATM 2228 O  O   . HOH D 4 .   ? 12.288  -3.747  7.178   1.00 39.71 ? 561 HOH A O   1 
HETATM 2229 O  O   . HOH D 4 .   ? -0.804  -13.185 26.959  1.00 28.85 ? 562 HOH A O   1 
HETATM 2230 O  O   . HOH D 4 .   ? 0.387   -14.320 21.999  1.00 32.88 ? 563 HOH A O   1 
HETATM 2231 O  O   . HOH D 4 .   ? -23.934 -17.422 6.620   1.00 35.89 ? 564 HOH A O   1 
HETATM 2232 O  O   . HOH D 4 .   ? -1.425  -12.343 22.565  1.00 20.02 ? 565 HOH A O   1 
HETATM 2233 O  O   . HOH D 4 .   ? -4.933  2.870   -6.408  1.00 25.98 ? 566 HOH A O   1 
HETATM 2234 O  O   . HOH D 4 .   ? -8.696  -10.061 -1.752  1.00 28.84 ? 567 HOH A O   1 
HETATM 2235 O  O   . HOH D 4 .   ? -0.295  2.646   -5.671  1.00 33.88 ? 568 HOH A O   1 
HETATM 2236 O  O   . HOH D 4 .   ? -22.386 -11.677 13.919  1.00 23.93 ? 569 HOH A O   1 
HETATM 2237 O  O   . HOH D 4 .   ? -24.396 -9.344  1.928   1.00 24.83 ? 570 HOH A O   1 
HETATM 2238 O  O   . HOH D 4 .   ? 8.157   6.279   21.582  1.00 20.57 ? 571 HOH A O   1 
HETATM 2239 O  O   . HOH D 4 .   ? -2.401  -17.728 5.261   1.00 32.03 ? 572 HOH A O   1 
HETATM 2240 O  O   . HOH D 4 .   ? 15.486  -10.538 14.394  1.00 32.30 ? 573 HOH A O   1 
HETATM 2241 O  O   . HOH D 4 .   ? 7.267   -10.634 14.699  1.00 38.67 ? 574 HOH A O   1 
HETATM 2242 O  O   . HOH D 4 .   ? 1.950   -11.550 14.599  1.00 20.96 ? 575 HOH A O   1 
HETATM 2243 O  O   . HOH D 4 .   ? -20.727 -19.559 6.252   1.00 30.46 ? 576 HOH A O   1 
HETATM 2244 O  O   . HOH D 4 .   ? 14.716  5.986   19.777  1.00 30.93 ? 577 HOH A O   1 
HETATM 2245 O  O   . HOH D 4 .   ? 5.392   -10.358 8.112   1.00 35.68 ? 578 HOH A O   1 
HETATM 2246 O  O   . HOH D 4 .   ? -6.839  -9.066  -2.693  1.00 29.84 ? 579 HOH A O   1 
HETATM 2247 O  O   . HOH D 4 .   ? -0.650  11.385  25.576  1.00 41.85 ? 580 HOH A O   1 
HETATM 2248 O  O   . HOH D 4 .   ? -6.063  -19.666 4.603   1.00 35.84 ? 581 HOH A O   1 
HETATM 2249 O  O   . HOH D 4 .   ? -31.004 5.528   12.574  1.00 40.90 ? 582 HOH A O   1 
HETATM 2250 O  O   . HOH D 4 .   ? -9.824  16.960  11.390  1.00 34.42 ? 583 HOH A O   1 
HETATM 2251 O  O   . HOH D 4 .   ? -12.102 -17.300 16.626  1.00 27.63 ? 584 HOH A O   1 
HETATM 2252 O  O   . HOH D 4 .   ? 4.529   8.831   22.353  1.00 36.31 ? 585 HOH A O   1 
HETATM 2253 O  O   . HOH D 4 .   ? -17.324 19.665  17.337  1.00 36.78 ? 586 HOH A O   1 
HETATM 2254 O  O   . HOH D 4 .   ? -9.273  5.295   30.086  1.00 40.98 ? 587 HOH A O   1 
HETATM 2255 O  O   . HOH D 4 .   ? 1.693   -9.860  28.518  1.00 35.30 ? 588 HOH A O   1 
HETATM 2256 O  O   . HOH D 4 .   ? 9.489   -4.713  23.361  1.00 36.09 ? 589 HOH A O   1 
HETATM 2257 O  O   . HOH D 4 .   ? -3.446  -6.134  -8.174  1.00 34.46 ? 590 HOH A O   1 
HETATM 2258 O  O   . HOH D 4 .   ? 6.911   -5.619  27.030  1.00 38.82 ? 591 HOH A O   1 
HETATM 2259 O  O   . HOH D 4 .   ? 12.367  -6.916  7.310   1.00 49.11 ? 592 HOH A O   1 
HETATM 2260 O  O   . HOH D 4 .   ? -26.682 -6.713  7.216   1.00 34.02 ? 593 HOH A O   1 
HETATM 2261 O  O   . HOH D 4 .   ? -27.315 -2.791  10.156  1.00 46.83 ? 594 HOH A O   1 
HETATM 2262 O  O   . HOH D 4 .   ? -1.387  -17.341 25.111  1.00 35.64 ? 595 HOH A O   1 
HETATM 2263 O  O   . HOH D 4 .   ? -27.101 5.070   25.219  1.00 30.10 ? 596 HOH A O   1 
HETATM 2264 O  O   . HOH D 4 .   ? 15.835  -1.055  25.814  1.00 26.63 ? 597 HOH A O   1 
HETATM 2265 O  O   . HOH D 4 .   ? -0.274  -11.052 28.680  1.00 30.10 ? 598 HOH A O   1 
HETATM 2266 O  O   . HOH D 4 .   ? -2.208  2.849   -7.293  1.00 34.83 ? 599 HOH A O   1 
HETATM 2267 O  O   . HOH D 4 .   ? 3.332   4.877   2.257   1.00 33.00 ? 600 HOH A O   1 
HETATM 2268 O  O   . HOH D 4 .   ? -17.171 -12.124 31.237  1.00 39.59 ? 601 HOH A O   1 
HETATM 2269 O  O   . HOH D 4 .   ? -15.523 17.751  25.802  1.00 43.04 ? 602 HOH A O   1 
# 
