data_5DOH
# 
_entry.id   5DOH 
# 
_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   5DOH         pdb_00005doh 10.2210/pdb5doh/pdb 
WWPDB D_1000213538 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2016-09-28 
2 'Structure model' 1 1 2017-01-18 
3 'Structure model' 1 2 2017-02-01 
4 'Structure model' 1 3 2018-03-07 
5 'Structure model' 2 0 2019-08-21 
6 'Structure model' 2 1 2024-01-10 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1  2 'Structure model' 'Database references'    
2  3 'Structure model' 'Database references'    
3  4 'Structure model' 'Data collection'        
4  5 'Structure model' Advisory                 
5  5 'Structure model' 'Atomic model'           
6  5 'Structure model' 'Data collection'        
7  5 'Structure model' 'Derived calculations'   
8  6 'Structure model' 'Data collection'        
9  6 'Structure model' 'Database references'    
10 6 'Structure model' 'Derived calculations'   
11 6 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  4 'Structure model' diffrn_source                 
2  5 'Structure model' atom_site                     
3  5 'Structure model' atom_site_anisotrop           
4  5 'Structure model' pdbx_nonpoly_scheme           
5  5 'Structure model' pdbx_struct_assembly          
6  5 'Structure model' pdbx_struct_assembly_gen      
7  5 'Structure model' pdbx_struct_assembly_prop     
8  5 'Structure model' pdbx_validate_close_contact   
9  5 'Structure model' struct_site_gen               
10 6 'Structure model' chem_comp_atom                
11 6 'Structure model' chem_comp_bond                
12 6 'Structure model' database_2                    
13 6 'Structure model' pdbx_initial_refinement_model 
14 6 'Structure model' struct_conn                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_diffrn_source.pdbx_synchrotron_site'       
2  5 'Structure model' '_atom_site.B_iso_or_equiv'                  
3  5 'Structure model' '_atom_site.Cartn_x'                         
4  5 'Structure model' '_atom_site.Cartn_y'                         
5  5 'Structure model' '_atom_site.Cartn_z'                         
6  5 'Structure model' '_atom_site_anisotrop.U[1][1]'               
7  5 'Structure model' '_atom_site_anisotrop.U[1][2]'               
8  5 'Structure model' '_atom_site_anisotrop.U[1][3]'               
9  5 'Structure model' '_atom_site_anisotrop.U[2][2]'               
10 5 'Structure model' '_atom_site_anisotrop.U[2][3]'               
11 5 'Structure model' '_atom_site_anisotrop.U[3][3]'               
12 5 'Structure model' '_pdbx_nonpoly_scheme.auth_seq_num'          
13 5 'Structure model' '_pdbx_validate_close_contact.auth_seq_id_2' 
14 5 'Structure model' '_struct_site_gen.auth_seq_id'               
15 6 'Structure model' '_database_2.pdbx_DOI'                       
16 6 'Structure model' '_database_2.pdbx_database_accession'        
17 6 'Structure model' '_struct_conn.pdbx_dist_value'               
18 6 'Structure model' '_struct_conn.ptnr1_auth_asym_id'            
19 6 'Structure model' '_struct_conn.ptnr1_auth_comp_id'            
20 6 'Structure model' '_struct_conn.ptnr1_auth_seq_id'             
21 6 'Structure model' '_struct_conn.ptnr1_label_asym_id'           
22 6 'Structure model' '_struct_conn.ptnr1_label_atom_id'           
23 6 'Structure model' '_struct_conn.ptnr1_label_comp_id'           
24 6 'Structure model' '_struct_conn.ptnr1_label_seq_id'            
25 6 'Structure model' '_struct_conn.ptnr2_auth_asym_id'            
26 6 'Structure model' '_struct_conn.ptnr2_auth_comp_id'            
27 6 'Structure model' '_struct_conn.ptnr2_auth_seq_id'             
28 6 'Structure model' '_struct_conn.ptnr2_label_asym_id'           
29 6 'Structure model' '_struct_conn.ptnr2_label_atom_id'           
30 6 'Structure model' '_struct_conn.ptnr2_label_comp_id'           
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5DOH 
_pdbx_database_status.recvd_initial_deposition_date   2015-09-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          5DOG 
_pdbx_database_related.content_type   unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            ChemMedChem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1860-7187 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            12 
_citation.language                  ? 
_citation.page_first                161 
_citation.page_last                 176 
_citation.title                     
'Intrinsic Thermodynamics and Structures of 2,4- and 3,4-Substituted Fluorinated Benzenesulfonamides Binding to Carbonic Anhydrases.' 
_citation.year                      2017 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cmdc.201600509 
_citation.pdbx_database_id_PubMed   28001003 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zubriene, A.'      1  ? 
primary 'Smirnov, A.'       2  ? 
primary 'Dudutiene, V.'     3  ? 
primary 'Timm, D.D.'        4  ? 
primary 'Matuliene, J.'     5  ? 
primary 'Michailoviene, V.' 6  ? 
primary 'Zaksauskas, A.'    7  ? 
primary 'Manakova, E.'      8  ? 
primary 'Grazulis, S.'      9  ? 
primary 'Matulis, D.'       10 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                                                   
29289.062 2   4.2.1.1 ? 'human carbonic anhydrase II'                                                                         ? 
2 non-polymer syn 'ZINC ION'                                                                                               65.409 
2   ?       ? '2-[(1S)-2,3-Dihydro-1H-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hy-droxyethyl)thio]benzenesulfonamide' ? 
3 non-polymer syn BICINE                                                                                                   163.172 
2   ?       ? Zn                                                                                                    ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                     78.133 
2   ?       ? BICINE                                                                                                ? 
5 non-polymer syn '2-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 418.454 
2   ?       ? 'DIMETHYL SULFOXIDE'                                                                                  ? 
6 water       nat water                                                                                                    18.015 
538 ?       ? ?                                                                                                     ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                               ZN  
3 BICINE                                                                                                   BCN 
4 'DIMETHYL SULFOXIDE'                                                                                     DMS 
5 '2-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 5DU 
6 water                                                                                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
5DU non-polymer         . '2-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 
? 'C17 H17 F3 N2 O3 S2' 418.454 
ALA 'L-peptide linking' y ALANINE                                                                                                  
? 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE                                                                                                 
? 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                               
? 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                                          
? 'C4 H7 N O4'          133.103 
BCN non-polymer         . BICINE                                                                                                   
? 'C6 H13 N O4'         163.172 
CYS 'L-peptide linking' y CYSTEINE                                                                                                 
? 'C3 H7 N O2 S'        121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                                                     
? 'C2 H6 O S'           78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                                                                
? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                          
? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                                                                                  
? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                                
? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                                                                    
? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                               
? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                                  
? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                                                                   
? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                                                               
? 'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                                            
? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                                                                                  
? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                                                                   
? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                                                                                
? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                               
? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                                 
? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                                                                                                   
? 'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                                                                               
? 'Zn 2'                65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   HIS 3   3   3   HIS HIS B . n 
B 1 4   HIS 4   4   4   HIS HIS B . n 
B 1 5   TRP 5   5   5   TRP TRP B . n 
B 1 6   GLY 6   6   6   GLY GLY B . n 
B 1 7   TYR 7   7   7   TYR TYR B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  HIS 10  10  10  HIS HIS B . n 
B 1 11  ASN 11  11  11  ASN ASN B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  HIS 15  15  15  HIS HIS B . n 
B 1 16  TRP 16  16  16  TRP TRP B . n 
B 1 17  HIS 17  17  17  HIS HIS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  GLY 25  25  25  GLY GLY B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ARG 27  27  27  ARG ARG B . n 
B 1 28  GLN 28  28  28  GLN GLN B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  ASP 32  32  32  ASP ASP B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  THR 35  35  35  THR THR B . n 
B 1 36  HIS 36  36  36  HIS HIS B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  LYS 45  45  45  LYS LYS B . n 
B 1 46  PRO 46  46  46  PRO PRO B . n 
B 1 47  LEU 47  47  47  LEU LEU B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  GLN 53  53  53  GLN GLN B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  ASN 62  62  62  ASN ASN B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  PRO 83  83  83  PRO PRO B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  TYR 88  88  88  TYR TYR B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  GLN 92  92  92  GLN GLN B . n 
B 1 93  PHE 93  93  93  PHE PHE B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  HIS 96  96  96  HIS HIS B . n 
B 1 97  TRP 97  97  97  TRP TRP B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 LEU 100 100 100 LEU LEU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 GLN 103 103 103 GLN GLN B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 HIS 107 107 107 HIS HIS B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 HIS 122 122 122 HIS HIS B . n 
B 1 123 TRP 123 123 123 TRP TRP B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 THR 125 125 125 THR THR B . n 
B 1 126 LYS 126 127 127 LYS LYS B . n 
B 1 127 TYR 127 128 128 TYR TYR B . n 
B 1 128 GLY 128 129 129 GLY GLY B . n 
B 1 129 ASP 129 130 130 ASP ASP B . n 
B 1 130 PHE 130 131 131 PHE PHE B . n 
B 1 131 GLY 131 132 132 GLY GLY B . n 
B 1 132 LYS 132 133 133 LYS LYS B . n 
B 1 133 ALA 133 134 134 ALA ALA B . n 
B 1 134 VAL 134 135 135 VAL VAL B . n 
B 1 135 GLN 135 136 136 GLN GLN B . n 
B 1 136 GLN 136 137 137 GLN GLN B . n 
B 1 137 PRO 137 138 138 PRO PRO B . n 
B 1 138 ASP 138 139 139 ASP ASP B . n 
B 1 139 GLY 139 140 140 GLY GLY B . n 
B 1 140 LEU 140 141 141 LEU LEU B . n 
B 1 141 ALA 141 142 142 ALA ALA B . n 
B 1 142 VAL 142 143 143 VAL VAL B . n 
B 1 143 LEU 143 144 144 LEU LEU B . n 
B 1 144 GLY 144 145 145 GLY GLY B . n 
B 1 145 ILE 145 146 146 ILE ILE B . n 
B 1 146 PHE 146 147 147 PHE PHE B . n 
B 1 147 LEU 147 148 148 LEU LEU B . n 
B 1 148 LYS 148 149 149 LYS LYS B . n 
B 1 149 VAL 149 150 150 VAL VAL B . n 
B 1 150 GLY 150 151 151 GLY GLY B . n 
B 1 151 SER 151 152 152 SER SER B . n 
B 1 152 ALA 152 153 153 ALA ALA B . n 
B 1 153 LYS 153 154 154 LYS LYS B . n 
B 1 154 PRO 154 155 155 PRO PRO B . n 
B 1 155 GLY 155 156 156 GLY GLY B . n 
B 1 156 LEU 156 157 157 LEU LEU B . n 
B 1 157 GLN 157 158 158 GLN GLN B . n 
B 1 158 LYS 158 159 159 LYS LYS B . n 
B 1 159 VAL 159 160 160 VAL VAL B . n 
B 1 160 VAL 160 161 161 VAL VAL B . n 
B 1 161 ASP 161 162 162 ASP ASP B . n 
B 1 162 VAL 162 163 163 VAL VAL B . n 
B 1 163 LEU 163 164 164 LEU LEU B . n 
B 1 164 ASP 164 165 165 ASP ASP B . n 
B 1 165 SER 165 166 166 SER SER B . n 
B 1 166 ILE 166 167 167 ILE ILE B . n 
B 1 167 LYS 167 168 168 LYS LYS B . n 
B 1 168 THR 168 169 169 THR THR B . n 
B 1 169 LYS 169 170 170 LYS LYS B . n 
B 1 170 GLY 170 171 171 GLY GLY B . n 
B 1 171 LYS 171 172 172 LYS LYS B . n 
B 1 172 SER 172 173 173 SER SER B . n 
B 1 173 ALA 173 174 174 ALA ALA B . n 
B 1 174 ASP 174 175 175 ASP ASP B . n 
B 1 175 PHE 175 176 176 PHE PHE B . n 
B 1 176 THR 176 177 177 THR THR B . n 
B 1 177 ASN 177 178 178 ASN ASN B . n 
B 1 178 PHE 178 179 179 PHE PHE B . n 
B 1 179 ASP 179 180 180 ASP ASP B . n 
B 1 180 PRO 180 181 181 PRO PRO B . n 
B 1 181 ARG 181 182 182 ARG ARG B . n 
B 1 182 GLY 182 183 183 GLY GLY B . n 
B 1 183 LEU 183 184 184 LEU LEU B . n 
B 1 184 LEU 184 185 185 LEU LEU B . n 
B 1 185 PRO 185 186 186 PRO PRO B . n 
B 1 186 GLU 186 187 187 GLU GLU B . n 
B 1 187 SER 187 188 188 SER SER B . n 
B 1 188 LEU 188 189 189 LEU LEU B . n 
B 1 189 ASP 189 190 190 ASP ASP B . n 
B 1 190 TYR 190 191 191 TYR TYR B . n 
B 1 191 TRP 191 192 192 TRP TRP B . n 
B 1 192 THR 192 193 193 THR THR B . n 
B 1 193 TYR 193 194 194 TYR TYR B . n 
B 1 194 PRO 194 195 195 PRO PRO B . n 
B 1 195 GLY 195 196 196 GLY GLY B . n 
B 1 196 SER 196 197 197 SER SER B . n 
B 1 197 LEU 197 198 198 LEU LEU B . n 
B 1 198 THR 198 199 199 THR THR B . n 
B 1 199 THR 199 200 200 THR THR B . n 
B 1 200 PRO 200 201 201 PRO PRO B . n 
B 1 201 PRO 201 202 202 PRO PRO B . n 
B 1 202 LEU 202 203 203 LEU LEU B . n 
B 1 203 LEU 203 204 204 LEU LEU B . n 
B 1 204 GLU 204 205 205 GLU GLU B . n 
B 1 205 CYS 205 206 206 CYS CYS B . n 
B 1 206 VAL 206 207 207 VAL VAL B . n 
B 1 207 THR 207 208 208 THR THR B . n 
B 1 208 TRP 208 209 209 TRP TRP B . n 
B 1 209 ILE 209 210 210 ILE ILE B . n 
B 1 210 VAL 210 211 211 VAL VAL B . n 
B 1 211 LEU 211 212 212 LEU LEU B . n 
B 1 212 LYS 212 213 213 LYS LYS B . n 
B 1 213 GLU 213 214 214 GLU GLU B . n 
B 1 214 PRO 214 215 215 PRO PRO B . n 
B 1 215 ILE 215 216 216 ILE ILE B . n 
B 1 216 SER 216 217 217 SER SER B . n 
B 1 217 VAL 217 218 218 VAL VAL B . n 
B 1 218 SER 218 219 219 SER SER B . n 
B 1 219 SER 219 220 220 SER SER B . n 
B 1 220 GLU 220 221 221 GLU GLU B . n 
B 1 221 GLN 221 222 222 GLN GLN B . n 
B 1 222 VAL 222 223 223 VAL VAL B . n 
B 1 223 LEU 223 224 224 LEU LEU B . n 
B 1 224 LYS 224 225 225 LYS LYS B . n 
B 1 225 PHE 225 226 226 PHE PHE B . n 
B 1 226 ARG 226 227 227 ARG ARG B . n 
B 1 227 LYS 227 228 228 LYS LYS B . n 
B 1 228 LEU 228 229 229 LEU LEU B . n 
B 1 229 ASN 229 230 230 ASN ASN B . n 
B 1 230 PHE 230 231 231 PHE PHE B . n 
B 1 231 ASN 231 232 232 ASN ASN B . n 
B 1 232 GLY 232 233 233 GLY GLY B . n 
B 1 233 GLU 233 234 234 GLU GLU B . n 
B 1 234 GLY 234 235 235 GLY GLY B . n 
B 1 235 GLU 235 236 236 GLU GLU B . n 
B 1 236 PRO 236 237 237 PRO PRO B . n 
B 1 237 GLU 237 238 238 GLU GLU B . n 
B 1 238 GLU 238 239 239 GLU GLU B . n 
B 1 239 LEU 239 240 240 LEU LEU B . n 
B 1 240 MET 240 241 241 MET MET B . n 
B 1 241 VAL 241 242 242 VAL VAL B . n 
B 1 242 ASP 242 243 243 ASP ASP B . n 
B 1 243 ASN 243 244 244 ASN ASN B . n 
B 1 244 TRP 244 245 245 TRP TRP B . n 
B 1 245 ARG 245 246 246 ARG ARG B . n 
B 1 246 PRO 246 247 247 PRO PRO B . n 
B 1 247 ALA 247 248 248 ALA ALA B . n 
B 1 248 GLN 248 249 249 GLN GLN B . n 
B 1 249 PRO 249 250 250 PRO PRO B . n 
B 1 250 LEU 250 251 251 LEU LEU B . n 
B 1 251 LYS 251 252 252 LYS LYS B . n 
B 1 252 ASN 252 253 253 ASN ASN B . n 
B 1 253 ARG 253 254 254 ARG ARG B . n 
B 1 254 GLN 254 255 255 GLN GLN B . n 
B 1 255 ILE 255 256 256 ILE ILE B . n 
B 1 256 LYS 256 257 257 LYS LYS B . n 
B 1 257 ALA 257 258 258 ALA ALA B . n 
B 1 258 SER 258 259 259 SER SER B . n 
B 1 259 PHE 259 260 260 PHE PHE B . n 
B 1 260 LYS 260 261 261 LYS LYS B . 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 
C 2 ZN  1   301 1   ZN  ZN  A . 
D 3 BCN 1   302 1   BCN BCN A . 
E 4 DMS 1   303 4   DMS DMS A . 
F 5 5DU 1   304 1   5DU V12 A . 
G 2 ZN  1   301 2   ZN  ZN  B . 
H 3 BCN 1   302 2   BCN BCN B . 
I 4 DMS 1   303 3   DMS DMS B . 
J 5 5DU 1   304 2   5DU V12 B . 
K 6 HOH 1   401 468 HOH HOH A . 
K 6 HOH 2   402 525 HOH HOH A . 
K 6 HOH 3   403 380 HOH HOH A . 
K 6 HOH 4   404 336 HOH HOH A . 
K 6 HOH 5   405 482 HOH HOH A . 
K 6 HOH 6   406 395 HOH HOH A . 
K 6 HOH 7   407 419 HOH HOH A . 
K 6 HOH 8   408 475 HOH HOH A . 
K 6 HOH 9   409 473 HOH HOH A . 
K 6 HOH 10  410 437 HOH HOH A . 
K 6 HOH 11  411 93  HOH HOH A . 
K 6 HOH 12  412 472 HOH HOH A . 
K 6 HOH 13  413 97  HOH HOH A . 
K 6 HOH 14  414 10  HOH HOH A . 
K 6 HOH 15  415 279 HOH HOH A . 
K 6 HOH 16  416 410 HOH HOH A . 
K 6 HOH 17  417 310 HOH HOH A . 
K 6 HOH 18  418 487 HOH HOH A . 
K 6 HOH 19  419 436 HOH HOH A . 
K 6 HOH 20  420 321 HOH HOH A . 
K 6 HOH 21  421 282 HOH HOH A . 
K 6 HOH 22  422 464 HOH HOH A . 
K 6 HOH 23  423 51  HOH HOH A . 
K 6 HOH 24  424 382 HOH HOH A . 
K 6 HOH 25  425 404 HOH HOH A . 
K 6 HOH 26  426 485 HOH HOH A . 
K 6 HOH 27  427 215 HOH HOH A . 
K 6 HOH 28  428 526 HOH HOH A . 
K 6 HOH 29  429 344 HOH HOH A . 
K 6 HOH 30  430 133 HOH HOH A . 
K 6 HOH 31  431 82  HOH HOH A . 
K 6 HOH 32  432 476 HOH HOH A . 
K 6 HOH 33  433 122 HOH HOH A . 
K 6 HOH 34  434 13  HOH HOH A . 
K 6 HOH 35  435 335 HOH HOH A . 
K 6 HOH 36  436 235 HOH HOH A . 
K 6 HOH 37  437 194 HOH HOH A . 
K 6 HOH 38  438 352 HOH HOH A . 
K 6 HOH 39  439 90  HOH HOH A . 
K 6 HOH 40  440 331 HOH HOH A . 
K 6 HOH 41  441 477 HOH HOH A . 
K 6 HOH 42  442 98  HOH HOH A . 
K 6 HOH 43  443 350 HOH HOH A . 
K 6 HOH 44  444 372 HOH HOH A . 
K 6 HOH 45  445 117 HOH HOH A . 
K 6 HOH 46  446 132 HOH HOH A . 
K 6 HOH 47  447 330 HOH HOH A . 
K 6 HOH 48  448 193 HOH HOH A . 
K 6 HOH 49  449 129 HOH HOH A . 
K 6 HOH 50  450 19  HOH HOH A . 
K 6 HOH 51  451 260 HOH HOH A . 
K 6 HOH 52  452 360 HOH HOH A . 
K 6 HOH 53  453 26  HOH HOH A . 
K 6 HOH 54  454 252 HOH HOH A . 
K 6 HOH 55  455 214 HOH HOH A . 
K 6 HOH 56  456 221 HOH HOH A . 
K 6 HOH 57  457 277 HOH HOH A . 
K 6 HOH 58  458 27  HOH HOH A . 
K 6 HOH 59  459 49  HOH HOH A . 
K 6 HOH 60  460 530 HOH HOH A . 
K 6 HOH 61  461 212 HOH HOH A . 
K 6 HOH 62  462 219 HOH HOH A . 
K 6 HOH 63  463 77  HOH HOH A . 
K 6 HOH 64  464 466 HOH HOH A . 
K 6 HOH 65  465 478 HOH HOH A . 
K 6 HOH 66  466 31  HOH HOH A . 
K 6 HOH 67  467 111 HOH HOH A . 
K 6 HOH 68  468 467 HOH HOH A . 
K 6 HOH 69  469 154 HOH HOH A . 
K 6 HOH 70  470 328 HOH HOH A . 
K 6 HOH 71  471 28  HOH HOH A . 
K 6 HOH 72  472 417 HOH HOH A . 
K 6 HOH 73  473 474 HOH HOH A . 
K 6 HOH 74  474 283 HOH HOH A . 
K 6 HOH 75  475 230 HOH HOH A . 
K 6 HOH 76  476 434 HOH HOH A . 
K 6 HOH 77  477 305 HOH HOH A . 
K 6 HOH 78  478 181 HOH HOH A . 
K 6 HOH 79  479 151 HOH HOH A . 
K 6 HOH 80  480 248 HOH HOH A . 
K 6 HOH 81  481 339 HOH HOH A . 
K 6 HOH 82  482 271 HOH HOH A . 
K 6 HOH 83  483 4   HOH HOH A . 
K 6 HOH 84  484 156 HOH HOH A . 
K 6 HOH 85  485 74  HOH HOH A . 
K 6 HOH 86  486 107 HOH HOH A . 
K 6 HOH 87  487 432 HOH HOH A . 
K 6 HOH 88  488 80  HOH HOH A . 
K 6 HOH 89  489 95  HOH HOH A . 
K 6 HOH 90  490 222 HOH HOH A . 
K 6 HOH 91  491 43  HOH HOH A . 
K 6 HOH 92  492 489 HOH HOH A . 
K 6 HOH 93  493 486 HOH HOH A . 
K 6 HOH 94  494 348 HOH HOH A . 
K 6 HOH 95  495 250 HOH HOH A . 
K 6 HOH 96  496 102 HOH HOH A . 
K 6 HOH 97  497 3   HOH HOH A . 
K 6 HOH 98  498 309 HOH HOH A . 
K 6 HOH 99  499 41  HOH HOH A . 
K 6 HOH 100 500 125 HOH HOH A . 
K 6 HOH 101 501 300 HOH HOH A . 
K 6 HOH 102 502 48  HOH HOH A . 
K 6 HOH 103 503 110 HOH HOH A . 
K 6 HOH 104 504 210 HOH HOH A . 
K 6 HOH 105 505 141 HOH HOH A . 
K 6 HOH 106 506 39  HOH HOH A . 
K 6 HOH 107 507 440 HOH HOH A . 
K 6 HOH 108 508 18  HOH HOH A . 
K 6 HOH 109 509 448 HOH HOH A . 
K 6 HOH 110 510 428 HOH HOH A . 
K 6 HOH 111 511 341 HOH HOH A . 
K 6 HOH 112 512 46  HOH HOH A . 
K 6 HOH 113 513 143 HOH HOH A . 
K 6 HOH 114 514 537 HOH HOH A . 
K 6 HOH 115 515 130 HOH HOH A . 
K 6 HOH 116 516 135 HOH HOH A . 
K 6 HOH 117 517 450 HOH HOH A . 
K 6 HOH 118 518 165 HOH HOH A . 
K 6 HOH 119 519 66  HOH HOH A . 
K 6 HOH 120 520 327 HOH HOH A . 
K 6 HOH 121 521 6   HOH HOH A . 
K 6 HOH 122 522 79  HOH HOH A . 
K 6 HOH 123 523 204 HOH HOH A . 
K 6 HOH 124 524 112 HOH HOH A . 
K 6 HOH 125 525 25  HOH HOH A . 
K 6 HOH 126 526 314 HOH HOH A . 
K 6 HOH 127 527 257 HOH HOH A . 
K 6 HOH 128 528 290 HOH HOH A . 
K 6 HOH 129 529 180 HOH HOH A . 
K 6 HOH 130 530 488 HOH HOH A . 
K 6 HOH 131 531 50  HOH HOH A . 
K 6 HOH 132 532 403 HOH HOH A . 
K 6 HOH 133 533 2   HOH HOH A . 
K 6 HOH 134 534 94  HOH HOH A . 
K 6 HOH 135 535 17  HOH HOH A . 
K 6 HOH 136 536 401 HOH HOH A . 
K 6 HOH 137 537 254 HOH HOH A . 
K 6 HOH 138 538 325 HOH HOH A . 
K 6 HOH 139 539 37  HOH HOH A . 
K 6 HOH 140 540 142 HOH HOH A . 
K 6 HOH 141 541 171 HOH HOH A . 
K 6 HOH 142 542 55  HOH HOH A . 
K 6 HOH 143 543 148 HOH HOH A . 
K 6 HOH 144 544 134 HOH HOH A . 
K 6 HOH 145 545 342 HOH HOH A . 
K 6 HOH 146 546 211 HOH HOH A . 
K 6 HOH 147 547 256 HOH HOH A . 
K 6 HOH 148 548 150 HOH HOH A . 
K 6 HOH 149 549 100 HOH HOH A . 
K 6 HOH 150 550 149 HOH HOH A . 
K 6 HOH 151 551 47  HOH HOH A . 
K 6 HOH 152 552 99  HOH HOH A . 
K 6 HOH 153 553 166 HOH HOH A . 
K 6 HOH 154 554 333 HOH HOH A . 
K 6 HOH 155 555 229 HOH HOH A . 
K 6 HOH 156 556 262 HOH HOH A . 
K 6 HOH 157 557 446 HOH HOH A . 
K 6 HOH 158 558 113 HOH HOH A . 
K 6 HOH 159 559 208 HOH HOH A . 
K 6 HOH 160 560 531 HOH HOH A . 
K 6 HOH 161 561 203 HOH HOH A . 
K 6 HOH 162 562 377 HOH HOH A . 
K 6 HOH 163 563 299 HOH HOH A . 
K 6 HOH 164 564 388 HOH HOH A . 
K 6 HOH 165 565 237 HOH HOH A . 
K 6 HOH 166 566 527 HOH HOH A . 
K 6 HOH 167 567 308 HOH HOH A . 
K 6 HOH 168 568 198 HOH HOH A . 
K 6 HOH 169 569 147 HOH HOH A . 
K 6 HOH 170 570 483 HOH HOH A . 
K 6 HOH 171 571 60  HOH HOH A . 
K 6 HOH 172 572 226 HOH HOH A . 
K 6 HOH 173 573 238 HOH HOH A . 
K 6 HOH 174 574 444 HOH HOH A . 
K 6 HOH 175 575 373 HOH HOH A . 
K 6 HOH 176 576 188 HOH HOH A . 
K 6 HOH 177 577 463 HOH HOH A . 
K 6 HOH 178 578 22  HOH HOH A . 
K 6 HOH 179 579 57  HOH HOH A . 
K 6 HOH 180 580 387 HOH HOH A . 
K 6 HOH 181 581 244 HOH HOH A . 
K 6 HOH 182 582 157 HOH HOH A . 
K 6 HOH 183 583 146 HOH HOH A . 
K 6 HOH 184 584 265 HOH HOH A . 
K 6 HOH 185 585 255 HOH HOH A . 
K 6 HOH 186 586 306 HOH HOH A . 
K 6 HOH 187 587 88  HOH HOH A . 
K 6 HOH 188 588 280 HOH HOH A . 
K 6 HOH 189 589 206 HOH HOH A . 
K 6 HOH 190 590 453 HOH HOH A . 
K 6 HOH 191 591 30  HOH HOH A . 
K 6 HOH 192 592 443 HOH HOH A . 
K 6 HOH 193 593 447 HOH HOH A . 
K 6 HOH 194 594 76  HOH HOH A . 
K 6 HOH 195 595 469 HOH HOH A . 
K 6 HOH 196 596 378 HOH HOH A . 
K 6 HOH 197 597 223 HOH HOH A . 
K 6 HOH 198 598 126 HOH HOH A . 
K 6 HOH 199 599 20  HOH HOH A . 
K 6 HOH 200 600 108 HOH HOH A . 
K 6 HOH 201 601 465 HOH HOH A . 
K 6 HOH 202 602 227 HOH HOH A . 
K 6 HOH 203 603 301 HOH HOH A . 
K 6 HOH 204 604 185 HOH HOH A . 
K 6 HOH 205 605 458 HOH HOH A . 
K 6 HOH 206 606 267 HOH HOH A . 
K 6 HOH 207 607 426 HOH HOH A . 
K 6 HOH 208 608 392 HOH HOH A . 
K 6 HOH 209 609 414 HOH HOH A . 
K 6 HOH 210 610 245 HOH HOH A . 
K 6 HOH 211 611 479 HOH HOH A . 
K 6 HOH 212 612 522 HOH HOH A . 
K 6 HOH 213 613 389 HOH HOH A . 
K 6 HOH 214 614 462 HOH HOH A . 
K 6 HOH 215 615 386 HOH HOH A . 
K 6 HOH 216 616 406 HOH HOH A . 
K 6 HOH 217 617 33  HOH HOH A . 
K 6 HOH 218 618 312 HOH HOH A . 
K 6 HOH 219 619 202 HOH HOH A . 
K 6 HOH 220 620 449 HOH HOH A . 
K 6 HOH 221 621 86  HOH HOH A . 
K 6 HOH 222 622 298 HOH HOH A . 
K 6 HOH 223 623 364 HOH HOH A . 
K 6 HOH 224 624 481 HOH HOH A . 
K 6 HOH 225 625 461 HOH HOH A . 
K 6 HOH 226 626 68  HOH HOH A . 
K 6 HOH 227 627 195 HOH HOH A . 
K 6 HOH 228 628 91  HOH HOH A . 
K 6 HOH 229 629 121 HOH HOH A . 
K 6 HOH 230 630 334 HOH HOH A . 
K 6 HOH 231 631 287 HOH HOH A . 
K 6 HOH 232 632 383 HOH HOH A . 
K 6 HOH 233 633 346 HOH HOH A . 
K 6 HOH 234 634 337 HOH HOH A . 
K 6 HOH 235 635 106 HOH HOH A . 
K 6 HOH 236 636 302 HOH HOH A . 
K 6 HOH 237 637 173 HOH HOH A . 
K 6 HOH 238 638 408 HOH HOH A . 
K 6 HOH 239 639 293 HOH HOH A . 
K 6 HOH 240 640 144 HOH HOH A . 
K 6 HOH 241 641 263 HOH HOH A . 
K 6 HOH 242 642 405 HOH HOH A . 
K 6 HOH 243 643 529 HOH HOH A . 
K 6 HOH 244 644 253 HOH HOH A . 
K 6 HOH 245 645 371 HOH HOH A . 
K 6 HOH 246 646 320 HOH HOH A . 
K 6 HOH 247 647 381 HOH HOH A . 
K 6 HOH 248 648 370 HOH HOH A . 
K 6 HOH 249 649 273 HOH HOH A . 
K 6 HOH 250 650 528 HOH HOH A . 
K 6 HOH 251 651 317 HOH HOH A . 
K 6 HOH 252 652 457 HOH HOH A . 
K 6 HOH 253 653 484 HOH HOH A . 
K 6 HOH 254 654 286 HOH HOH A . 
K 6 HOH 255 655 445 HOH HOH A . 
K 6 HOH 256 656 361 HOH HOH A . 
K 6 HOH 257 657 295 HOH HOH A . 
K 6 HOH 258 658 471 HOH HOH A . 
K 6 HOH 259 659 63  HOH HOH A . 
K 6 HOH 260 660 369 HOH HOH A . 
K 6 HOH 261 661 338 HOH HOH A . 
K 6 HOH 262 662 396 HOH HOH A . 
K 6 HOH 263 663 470 HOH HOH A . 
K 6 HOH 264 664 362 HOH HOH A . 
K 6 HOH 265 665 218 HOH HOH A . 
K 6 HOH 266 666 355 HOH HOH A . 
K 6 HOH 267 667 224 HOH HOH A . 
K 6 HOH 268 668 359 HOH HOH A . 
K 6 HOH 269 669 431 HOH HOH A . 
K 6 HOH 270 670 521 HOH HOH A . 
K 6 HOH 271 671 441 HOH HOH A . 
K 6 HOH 272 672 480 HOH HOH A . 
K 6 HOH 273 673 367 HOH HOH A . 
L 6 HOH 1   401 423 HOH HOH B . 
L 6 HOH 2   402 400 HOH HOH B . 
L 6 HOH 3   403 379 HOH HOH B . 
L 6 HOH 4   404 307 HOH HOH B . 
L 6 HOH 5   405 246 HOH HOH B . 
L 6 HOH 6   406 513 HOH HOH B . 
L 6 HOH 7   407 433 HOH HOH B . 
L 6 HOH 8   408 511 HOH HOH B . 
L 6 HOH 9   409 514 HOH HOH B . 
L 6 HOH 10  410 343 HOH HOH B . 
L 6 HOH 11  411 416 HOH HOH B . 
L 6 HOH 12  412 304 HOH HOH B . 
L 6 HOH 13  413 497 HOH HOH B . 
L 6 HOH 14  414 349 HOH HOH B . 
L 6 HOH 15  415 162 HOH HOH B . 
L 6 HOH 16  416 101 HOH HOH B . 
L 6 HOH 17  417 324 HOH HOH B . 
L 6 HOH 18  418 515 HOH HOH B . 
L 6 HOH 19  419 269 HOH HOH B . 
L 6 HOH 20  420 535 HOH HOH B . 
L 6 HOH 21  421 128 HOH HOH B . 
L 6 HOH 22  422 172 HOH HOH B . 
L 6 HOH 23  423 519 HOH HOH B . 
L 6 HOH 24  424 247 HOH HOH B . 
L 6 HOH 25  425 139 HOH HOH B . 
L 6 HOH 26  426 5   HOH HOH B . 
L 6 HOH 27  427 242 HOH HOH B . 
L 6 HOH 28  428 347 HOH HOH B . 
L 6 HOH 29  429 278 HOH HOH B . 
L 6 HOH 30  430 323 HOH HOH B . 
L 6 HOH 31  431 85  HOH HOH B . 
L 6 HOH 32  432 14  HOH HOH B . 
L 6 HOH 33  433 52  HOH HOH B . 
L 6 HOH 34  434 105 HOH HOH B . 
L 6 HOH 35  435 501 HOH HOH B . 
L 6 HOH 36  436 249 HOH HOH B . 
L 6 HOH 37  437 318 HOH HOH B . 
L 6 HOH 38  438 200 HOH HOH B . 
L 6 HOH 39  439 225 HOH HOH B . 
L 6 HOH 40  440 393 HOH HOH B . 
L 6 HOH 41  441 409 HOH HOH B . 
L 6 HOH 42  442 243 HOH HOH B . 
L 6 HOH 43  443 311 HOH HOH B . 
L 6 HOH 44  444 213 HOH HOH B . 
L 6 HOH 45  445 241 HOH HOH B . 
L 6 HOH 46  446 12  HOH HOH B . 
L 6 HOH 47  447 496 HOH HOH B . 
L 6 HOH 48  448 158 HOH HOH B . 
L 6 HOH 49  449 518 HOH HOH B . 
L 6 HOH 50  450 268 HOH HOH B . 
L 6 HOH 51  451 258 HOH HOH B . 
L 6 HOH 52  452 456 HOH HOH B . 
L 6 HOH 53  453 319 HOH HOH B . 
L 6 HOH 54  454 67  HOH HOH B . 
L 6 HOH 55  455 115 HOH HOH B . 
L 6 HOH 56  456 11  HOH HOH B . 
L 6 HOH 57  457 493 HOH HOH B . 
L 6 HOH 58  458 62  HOH HOH B . 
L 6 HOH 59  459 187 HOH HOH B . 
L 6 HOH 60  460 209 HOH HOH B . 
L 6 HOH 61  461 24  HOH HOH B . 
L 6 HOH 62  462 58  HOH HOH B . 
L 6 HOH 63  463 65  HOH HOH B . 
L 6 HOH 64  464 494 HOH HOH B . 
L 6 HOH 65  465 216 HOH HOH B . 
L 6 HOH 66  466 92  HOH HOH B . 
L 6 HOH 67  467 44  HOH HOH B . 
L 6 HOH 68  468 460 HOH HOH B . 
L 6 HOH 69  469 42  HOH HOH B . 
L 6 HOH 70  470 239 HOH HOH B . 
L 6 HOH 71  471 288 HOH HOH B . 
L 6 HOH 72  472 345 HOH HOH B . 
L 6 HOH 73  473 35  HOH HOH B . 
L 6 HOH 74  474 351 HOH HOH B . 
L 6 HOH 75  475 168 HOH HOH B . 
L 6 HOH 76  476 197 HOH HOH B . 
L 6 HOH 77  477 275 HOH HOH B . 
L 6 HOH 78  478 170 HOH HOH B . 
L 6 HOH 79  479 59  HOH HOH B . 
L 6 HOH 80  480 429 HOH HOH B . 
L 6 HOH 81  481 81  HOH HOH B . 
L 6 HOH 82  482 418 HOH HOH B . 
L 6 HOH 83  483 160 HOH HOH B . 
L 6 HOH 84  484 354 HOH HOH B . 
L 6 HOH 85  485 145 HOH HOH B . 
L 6 HOH 86  486 8   HOH HOH B . 
L 6 HOH 87  487 119 HOH HOH B . 
L 6 HOH 88  488 191 HOH HOH B . 
L 6 HOH 89  489 7   HOH HOH B . 
L 6 HOH 90  490 500 HOH HOH B . 
L 6 HOH 91  491 73  HOH HOH B . 
L 6 HOH 92  492 138 HOH HOH B . 
L 6 HOH 93  493 137 HOH HOH B . 
L 6 HOH 94  494 16  HOH HOH B . 
L 6 HOH 95  495 54  HOH HOH B . 
L 6 HOH 96  496 120 HOH HOH B . 
L 6 HOH 97  497 413 HOH HOH B . 
L 6 HOH 98  498 284 HOH HOH B . 
L 6 HOH 99  499 71  HOH HOH B . 
L 6 HOH 100 500 104 HOH HOH B . 
L 6 HOH 101 501 72  HOH HOH B . 
L 6 HOH 102 502 45  HOH HOH B . 
L 6 HOH 103 503 161 HOH HOH B . 
L 6 HOH 104 504 217 HOH HOH B . 
L 6 HOH 105 505 427 HOH HOH B . 
L 6 HOH 106 506 1   HOH HOH B . 
L 6 HOH 107 507 9   HOH HOH B . 
L 6 HOH 108 508 192 HOH HOH B . 
L 6 HOH 109 509 177 HOH HOH B . 
L 6 HOH 110 510 56  HOH HOH B . 
L 6 HOH 111 511 231 HOH HOH B . 
L 6 HOH 112 512 87  HOH HOH B . 
L 6 HOH 113 513 152 HOH HOH B . 
L 6 HOH 114 514 297 HOH HOH B . 
L 6 HOH 115 515 163 HOH HOH B . 
L 6 HOH 116 516 502 HOH HOH B . 
L 6 HOH 117 517 114 HOH HOH B . 
L 6 HOH 118 518 15  HOH HOH B . 
L 6 HOH 119 519 89  HOH HOH B . 
L 6 HOH 120 520 23  HOH HOH B . 
L 6 HOH 121 521 289 HOH HOH B . 
L 6 HOH 122 522 40  HOH HOH B . 
L 6 HOH 123 523 292 HOH HOH B . 
L 6 HOH 124 524 176 HOH HOH B . 
L 6 HOH 125 525 411 HOH HOH B . 
L 6 HOH 126 526 220 HOH HOH B . 
L 6 HOH 127 527 61  HOH HOH B . 
L 6 HOH 128 528 136 HOH HOH B . 
L 6 HOH 129 529 533 HOH HOH B . 
L 6 HOH 130 530 175 HOH HOH B . 
L 6 HOH 131 531 164 HOH HOH B . 
L 6 HOH 132 532 196 HOH HOH B . 
L 6 HOH 133 533 509 HOH HOH B . 
L 6 HOH 134 534 398 HOH HOH B . 
L 6 HOH 135 535 261 HOH HOH B . 
L 6 HOH 136 536 179 HOH HOH B . 
L 6 HOH 137 537 499 HOH HOH B . 
L 6 HOH 138 538 207 HOH HOH B . 
L 6 HOH 139 539 155 HOH HOH B . 
L 6 HOH 140 540 538 HOH HOH B . 
L 6 HOH 141 541 516 HOH HOH B . 
L 6 HOH 142 542 425 HOH HOH B . 
L 6 HOH 143 543 276 HOH HOH B . 
L 6 HOH 144 544 21  HOH HOH B . 
L 6 HOH 145 545 103 HOH HOH B . 
L 6 HOH 146 546 332 HOH HOH B . 
L 6 HOH 147 547 38  HOH HOH B . 
L 6 HOH 148 548 376 HOH HOH B . 
L 6 HOH 149 549 183 HOH HOH B . 
L 6 HOH 150 550 285 HOH HOH B . 
L 6 HOH 151 551 186 HOH HOH B . 
L 6 HOH 152 552 384 HOH HOH B . 
L 6 HOH 153 553 123 HOH HOH B . 
L 6 HOH 154 554 190 HOH HOH B . 
L 6 HOH 155 555 53  HOH HOH B . 
L 6 HOH 156 556 512 HOH HOH B . 
L 6 HOH 157 557 184 HOH HOH B . 
L 6 HOH 158 558 159 HOH HOH B . 
L 6 HOH 159 559 233 HOH HOH B . 
L 6 HOH 160 560 29  HOH HOH B . 
L 6 HOH 161 561 374 HOH HOH B . 
L 6 HOH 162 562 116 HOH HOH B . 
L 6 HOH 163 563 140 HOH HOH B . 
L 6 HOH 164 564 506 HOH HOH B . 
L 6 HOH 165 565 153 HOH HOH B . 
L 6 HOH 166 566 313 HOH HOH B . 
L 6 HOH 167 567 272 HOH HOH B . 
L 6 HOH 168 568 201 HOH HOH B . 
L 6 HOH 169 569 438 HOH HOH B . 
L 6 HOH 170 570 240 HOH HOH B . 
L 6 HOH 171 571 34  HOH HOH B . 
L 6 HOH 172 572 83  HOH HOH B . 
L 6 HOH 173 573 340 HOH HOH B . 
L 6 HOH 174 574 32  HOH HOH B . 
L 6 HOH 175 575 375 HOH HOH B . 
L 6 HOH 176 576 182 HOH HOH B . 
L 6 HOH 177 577 303 HOH HOH B . 
L 6 HOH 178 578 174 HOH HOH B . 
L 6 HOH 179 579 96  HOH HOH B . 
L 6 HOH 180 580 259 HOH HOH B . 
L 6 HOH 181 581 118 HOH HOH B . 
L 6 HOH 182 582 64  HOH HOH B . 
L 6 HOH 183 583 421 HOH HOH B . 
L 6 HOH 184 584 270 HOH HOH B . 
L 6 HOH 185 585 520 HOH HOH B . 
L 6 HOH 186 586 189 HOH HOH B . 
L 6 HOH 187 587 532 HOH HOH B . 
L 6 HOH 188 588 536 HOH HOH B . 
L 6 HOH 189 589 505 HOH HOH B . 
L 6 HOH 190 590 69  HOH HOH B . 
L 6 HOH 191 591 399 HOH HOH B . 
L 6 HOH 192 592 329 HOH HOH B . 
L 6 HOH 193 593 534 HOH HOH B . 
L 6 HOH 194 594 452 HOH HOH B . 
L 6 HOH 195 595 75  HOH HOH B . 
L 6 HOH 196 596 251 HOH HOH B . 
L 6 HOH 197 597 503 HOH HOH B . 
L 6 HOH 198 598 498 HOH HOH B . 
L 6 HOH 199 599 326 HOH HOH B . 
L 6 HOH 200 600 228 HOH HOH B . 
L 6 HOH 201 601 412 HOH HOH B . 
L 6 HOH 202 602 442 HOH HOH B . 
L 6 HOH 203 603 322 HOH HOH B . 
L 6 HOH 204 604 36  HOH HOH B . 
L 6 HOH 205 605 274 HOH HOH B . 
L 6 HOH 206 606 490 HOH HOH B . 
L 6 HOH 207 607 124 HOH HOH B . 
L 6 HOH 208 608 407 HOH HOH B . 
L 6 HOH 209 609 523 HOH HOH B . 
L 6 HOH 210 610 394 HOH HOH B . 
L 6 HOH 211 611 264 HOH HOH B . 
L 6 HOH 212 612 84  HOH HOH B . 
L 6 HOH 213 613 491 HOH HOH B . 
L 6 HOH 214 614 439 HOH HOH B . 
L 6 HOH 215 615 454 HOH HOH B . 
L 6 HOH 216 616 385 HOH HOH B . 
L 6 HOH 217 617 281 HOH HOH B . 
L 6 HOH 218 618 131 HOH HOH B . 
L 6 HOH 219 619 169 HOH HOH B . 
L 6 HOH 220 620 517 HOH HOH B . 
L 6 HOH 221 621 199 HOH HOH B . 
L 6 HOH 222 622 167 HOH HOH B . 
L 6 HOH 223 623 451 HOH HOH B . 
L 6 HOH 224 624 296 HOH HOH B . 
L 6 HOH 225 625 508 HOH HOH B . 
L 6 HOH 226 626 315 HOH HOH B . 
L 6 HOH 227 627 294 HOH HOH B . 
L 6 HOH 228 628 390 HOH HOH B . 
L 6 HOH 229 629 109 HOH HOH B . 
L 6 HOH 230 630 415 HOH HOH B . 
L 6 HOH 231 631 363 HOH HOH B . 
L 6 HOH 232 632 127 HOH HOH B . 
L 6 HOH 233 633 507 HOH HOH B . 
L 6 HOH 234 634 391 HOH HOH B . 
L 6 HOH 235 635 78  HOH HOH B . 
L 6 HOH 236 636 402 HOH HOH B . 
L 6 HOH 237 637 430 HOH HOH B . 
L 6 HOH 238 638 178 HOH HOH B . 
L 6 HOH 239 639 353 HOH HOH B . 
L 6 HOH 240 640 459 HOH HOH B . 
L 6 HOH 241 641 205 HOH HOH B . 
L 6 HOH 242 642 358 HOH HOH B . 
L 6 HOH 243 643 316 HOH HOH B . 
L 6 HOH 244 644 365 HOH HOH B . 
L 6 HOH 245 645 357 HOH HOH B . 
L 6 HOH 246 646 266 HOH HOH B . 
L 6 HOH 247 647 510 HOH HOH B . 
L 6 HOH 248 648 234 HOH HOH B . 
L 6 HOH 249 649 422 HOH HOH B . 
L 6 HOH 250 650 424 HOH HOH B . 
L 6 HOH 251 651 70  HOH HOH B . 
L 6 HOH 252 652 366 HOH HOH B . 
L 6 HOH 253 653 455 HOH HOH B . 
L 6 HOH 254 654 495 HOH HOH B . 
L 6 HOH 255 655 232 HOH HOH B . 
L 6 HOH 256 656 504 HOH HOH B . 
L 6 HOH 257 657 236 HOH HOH B . 
L 6 HOH 258 658 356 HOH HOH B . 
L 6 HOH 259 659 420 HOH HOH B . 
L 6 HOH 260 660 524 HOH HOH B . 
L 6 HOH 261 661 291 HOH HOH B . 
L 6 HOH 262 662 435 HOH HOH B . 
L 6 HOH 263 663 397 HOH HOH B . 
L 6 HOH 264 664 368 HOH HOH B . 
L 6 HOH 265 665 492 HOH HOH B . 
# 
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 159 ? NZ  ? A LYS 158 NZ  
7  1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
8  1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
9  1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
10 1 Y 1 B LYS 9   ? CD  ? B LYS 9   CD  
11 1 Y 1 B LYS 9   ? CE  ? B LYS 9   CE  
12 1 Y 1 B LYS 9   ? NZ  ? B LYS 9   NZ  
13 1 Y 1 B GLN 255 ? CD  ? B GLN 254 CD  
14 1 Y 1 B GLN 255 ? OE1 ? B GLN 254 OE1 
15 1 Y 1 B GLN 255 ? NE2 ? B GLN 254 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.006    2 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.190 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5DOH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.162 
_cell.length_a_esd                 ? 
_cell.length_b                     41.157 
_cell.length_b_esd                 ? 
_cell.length_c                     71.854 
_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                         5DOH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   5DOH 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.01 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         38.5 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer: 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-12-01 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            8.491 
_reflns.entry_id                         5DOH 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.050 
_reflns.d_resolution_low                 69.661 
_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                       195453 
_reflns.number_obs                       195453 
_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             89.400 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.800 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.031 
_reflns.pdbx_netI_over_av_sigmaI         8.754 
_reflns.pdbx_netI_over_sigmaI            17.100 
_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                  0.044 
_reflns.pdbx_Rpim_I_all                  0.023 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         735878 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.05 1.11  ? 2.9  103595 ? ? 27750 ? 86.70 ? ? ? 0.379 0.271 ? ? ? ? ? ? ? ? 3.70 0.271 ? ? 3.70  0.38 0.19 ? 1  1 ? ? 
1.11 1.17  ? 4.8  99829  ? ? 26492 ? 87.50 ? ? ? 0.227 0.158 ? ? ? ? ? ? ? ? 3.80 0.158 ? ? 6.20  0.23 0.12 ? 2  ? ? ? 
1.17 1.25  ? 6.6  95998  ? ? 25291 ? 89.20 ? ? ? 0.167 0.115 ? ? ? ? ? ? ? ? 3.80 0.115 ? ? 8.30  0.17 0.09 ? 3  ? ? ? 
1.25 1.36  ? 9.0  86473  ? ? 23100 ? 87.50 ? ? ? 0.124 0.084 ? ? ? ? ? ? ? ? 3.70 0.084 ? ? 11.00 0.12 0.06 ? 4  ? ? ? 
1.36 1.48  ? 12.6 85035  ? ? 22178 ? 91.30 ? ? ? 0.088 0.059 ? ? ? ? ? ? ? ? 3.80 0.059 ? ? 15.40 0.09 0.05 ? 5  ? ? ? 
1.48 1.66  ? 17.6 72675  ? ? 19483 ? 88.50 ? ? ? 0.063 0.040 ? ? ? ? ? ? ? ? 3.70 0.040 ? ? 21.40 0.06 0.03 ? 6  ? ? ? 
1.66 1.92  ? 21.9 69794  ? ? 18164 ? 93.50 ? ? ? 0.046 0.030 ? ? ? ? ? ? ? ? 3.80 0.030 ? ? 29.40 0.05 0.02 ? 7  ? ? ? 
1.92 2.35  ? 24.9 53832  ? ? 14609 ? 89.20 ? ? ? 0.038 0.025 ? ? ? ? ? ? ? ? 3.70 0.025 ? ? 36.80 0.04 0.02 ? 8  ? ? ? 
2.35 3.32  ? 23.8 45216  ? ? 11967 ? 94.70 ? ? ? 0.034 0.024 ? ? ? ? ? ? ? ? 3.80 0.024 ? ? 42.00 0.03 0.02 ? 9  ? ? ? 
3.32 69.66 ? 23.0 23431  ? ? 6419  ? 92.90 ? ? ? 0.033 0.024 ? ? ? ? ? ? ? ? 3.70 0.024 ? ? 44.60 0.03 0.02 ? 10 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.030 
_refine.aniso_B[1][2]                            0.040 
_refine.aniso_B[1][3]                            0.010 
_refine.aniso_B[2][2]                            -0.140 
_refine.aniso_B[2][3]                            0.020 
_refine.aniso_B[3][3]                            0.180 
_refine.B_iso_max                                138.81 
_refine.B_iso_mean                               16.924 
_refine.B_iso_min                                6.11 
_refine.correlation_coeff_Fo_to_Fc               0.977 
_refine.correlation_coeff_Fo_to_Fc_free          0.971 
_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                                 5DOH 
_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                            1.050 
_refine.ls_d_res_low                             69.660 
_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                     195451 
_refine.ls_number_reflns_R_free                  19404 
_refine.ls_number_reflns_R_work                  176047 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    89.370 
_refine.ls_percent_reflns_R_free                 9.900 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.147 
_refine.ls_R_factor_R_free                       0.172 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.144 
_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                      0.179 
_refine.ls_wR_factor_R_work                      0.148 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      3HLJ 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.032 
_refine.pdbx_overall_ESU_R_Free                  0.033 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.032 
_refine.overall_SU_R_free                        0.032 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   0.917 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4118 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         86 
_refine_hist.number_atoms_solvent             538 
_refine_hist.number_atoms_total               4742 
_refine_hist.d_res_high                       1.050 
_refine_hist.d_res_low                        69.660 
# 
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' ? 0.022  0.020  4564 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.307  1.966  6232 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.702  5.000  563  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 34.356 24.660 206  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.367 15.000 733  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 21.717 15.000 14   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.148  0.200  637  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.021  3588 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 9.286  3.000  4564 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 34.178 5.000  540  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 16.441 5.000  4412 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.050 
_refine_ls_shell.d_res_low                        1.077 
_refine_ls_shell.number_reflns_all                14146 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             1417 
_refine_ls_shell.number_reflns_R_work             12729 
_refine_ls_shell.percent_reflns_obs               87.530 
_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                  0.242 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.212 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     5DOH 
_struct.title                        
;Crystal structure of human carbonic anhydrase isozyme II with 2-[(1S)-2,3-Dihydro-1H-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hydroxyethyl)thio]benzenesulfonamide
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5DOH 
_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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 6 ? 
L N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5DOH A 1 ? 260 ? P00918 1 ? 260 ? 1 261 
2 1 5DOH B 1 ? 260 ? P00918 1 ? 260 ? 1 261 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 software_defined_assembly PISA monomeric 1 
2 software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,K 
2 1 B,G,H,I,J,L 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2  AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3  AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4  AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5  AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6  AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7  AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8  AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9  AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
HELX_P HELX_P10 AB1 GLY B 12  ? ASP B 19  ? GLY B 12  ASP B 19  5 ? 8 
HELX_P HELX_P11 AB2 PHE B 20  ? GLY B 25  ? PHE B 20  GLY B 25  5 ? 6 
HELX_P HELX_P12 AB3 LYS B 126 ? GLY B 128 ? LYS B 127 GLY B 129 5 ? 3 
HELX_P HELX_P13 AB4 ASP B 129 ? VAL B 134 ? ASP B 130 VAL B 135 1 ? 6 
HELX_P HELX_P14 AB5 LYS B 153 ? GLY B 155 ? LYS B 154 GLY B 156 5 ? 3 
HELX_P HELX_P15 AB6 LEU B 156 ? LEU B 163 ? LEU B 157 LEU B 164 1 ? 8 
HELX_P HELX_P16 AB7 ASP B 164 ? LYS B 167 ? ASP B 165 LYS B 168 5 ? 4 
HELX_P HELX_P17 AB8 ASP B 179 ? LEU B 184 ? ASP B 180 LEU B 185 5 ? 6 
HELX_P HELX_P18 AB9 SER B 219 ? ARG B 226 ? SER B 220 ARG B 227 1 ? 8 
# 
_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 C ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.986 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc4 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 F 5DU . S1 ? ? A ZN  301 A 5DU 304 1_555 ? ? ? ? ? ? ? 2.738 ? ? 
metalc5 metalc ? ? B HIS 94  NE2 ? ? ? 1_555 G ZN  . ZN ? ? B HIS 94  B ZN  301 1_555 ? ? ? ? ? ? ? 1.971 ? ? 
metalc6 metalc ? ? B HIS 96  NE2 ? ? ? 1_555 G ZN  . ZN ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc7 metalc ? ? B HIS 119 ND1 ? ? ? 1_555 G ZN  . ZN ? ? B HIS 119 B ZN  301 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc8 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 J 5DU . N4 ? ? B ZN  301 B 5DU 304 1_555 ? ? ? ? ? ? ? 1.953 ? ? 
metalc9 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 J 5DU . O2 ? ? B ZN  301 B 5DU 304 1_555 ? ? ? ? ? ? ? 2.692 ? ? 
# 
_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 ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 104.3 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C 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 ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.8  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 S1  ? F 5DU .   ? A 5DU 304 ? 1_555 93.8  ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 S1  ? F 5DU .   ? A 5DU 304 ? 1_555 128.7 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 S1  ? F 5DU .   ? A 5DU 304 ? 1_555 117.2 ? 
7  NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 104.5 ? 
8  NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 111.7 ? 
9  NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 99.5  ? 
10 NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 N4  ? J 5DU .   ? B 5DU 304 ? 1_555 108.5 ? 
11 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 N4  ? J 5DU .   ? B 5DU 304 ? 1_555 105.2 ? 
12 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 N4  ? J 5DU .   ? B 5DU 304 ? 1_555 124.9 ? 
13 NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 O2  ? J 5DU .   ? B 5DU 304 ? 1_555 94.0  ? 
14 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 O2  ? J 5DU .   ? B 5DU 304 ? 1_555 157.9 ? 
15 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 O2  ? J 5DU .   ? B 5DU 304 ? 1_555 84.4  ? 
16 N4  ? J 5DU .   ? B 5DU 304 ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 O2  ? J 5DU .   ? B 5DU 304 ? 1_555 56.5  ? 
# 
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 -2.51 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 12.19 
3 SER 29  B . ? SER 29  B PRO 30  B ? PRO 30  B 1 -3.46 
4 PRO 200 B . ? PRO 201 B PRO 201 B ? PRO 202 B 1 15.85 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 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      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
AA4 1  ASP B 32  ? ILE B 33  ? ASP B 32  ILE B 33  
AA4 2  THR B 108 ? VAL B 109 ? THR B 108 VAL B 109 
AA5 1  LYS B 39  ? TYR B 40  ? LYS B 39  TYR B 40  
AA5 2  LYS B 256 ? ALA B 257 ? LYS B 257 ALA B 258 
AA5 3  TYR B 190 ? GLY B 195 ? TYR B 191 GLY B 196 
AA5 4  VAL B 206 ? LEU B 211 ? VAL B 207 LEU B 212 
AA5 5  LEU B 140 ? GLY B 150 ? LEU B 141 GLY B 151 
AA5 6  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
AA5 7  TYR B 88  ? TRP B 97  ? TYR B 88  TRP B 97  
AA5 8  PHE B 66  ? PHE B 70  ? PHE B 66  PHE B 70  
AA5 9  SER B 56  ? ASN B 61  ? SER B 56  ASN B 61  
AA5 10 SER B 172 ? ASP B 174 ? SER B 173 ASP B 175 
AA6 1  LEU B 47  ? SER B 50  ? LEU B 47  SER B 50  
AA6 2  VAL B 78  ? GLY B 81  ? VAL B 78  GLY B 81  
AA6 3  TYR B 88  ? TRP B 97  ? TYR B 88  TRP B 97  
AA6 4  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
AA6 5  LEU B 140 ? GLY B 150 ? LEU B 141 GLY B 151 
AA6 6  ILE B 215 ? SER B 218 ? ILE B 216 SER B 219 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
AA4 1 2  N ILE B 33  ? N ILE B 33  O THR B 108 ? O THR B 108 
AA5 1 2  N LYS B 39  ? N LYS B 39  O ALA B 257 ? O ALA B 258 
AA5 2 3  O LYS B 256 ? O LYS B 257 N THR B 192 ? N THR B 193 
AA5 3 4  N GLY B 195 ? N GLY B 196 O VAL B 206 ? O VAL B 207 
AA5 4 5  O ILE B 209 ? O ILE B 210 N GLY B 144 ? N GLY B 145 
AA5 5 6  O ILE B 145 ? O ILE B 146 N LEU B 118 ? N LEU B 118 
AA5 6 7  O HIS B 119 ? O HIS B 119 N HIS B 94  ? N HIS B 94  
AA5 7 8  O PHE B 93  ? O PHE B 93  N VAL B 68  ? N VAL B 68  
AA5 8 9  O GLU B 69  ? O GLU B 69  N LEU B 57  ? N LEU B 57  
AA5 9 10 N ILE B 59  ? N ILE B 59  O ALA B 173 ? O ALA B 174 
AA6 1 2  N SER B 50  ? N SER B 50  O VAL B 78  ? O VAL B 78  
AA6 2 3  N LEU B 79  ? N LEU B 79  O TYR B 88  ? O TYR B 88  
AA6 3 4  N HIS B 94  ? N HIS B 94  O HIS B 119 ? O HIS B 119 
AA6 4 5  N LEU B 118 ? N LEU B 118 O ILE B 145 ? O ILE B 146 
AA6 5 6  N GLY B 150 ? N GLY B 151 O VAL B 217 ? O VAL B 218 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A BCN 302 ? 9  'binding site for residue BCN A 302' 
AC3 Software A DMS 303 ? 4  'binding site for residue DMS A 303' 
AC4 Software A 5DU 304 ? 15 'binding site for residue 5DU A 304' 
AC5 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC6 Software B BCN 302 ? 8  'binding site for residue BCN B 302' 
AC7 Software B DMS 303 ? 5  'binding site for residue DMS B 303' 
AC8 Software B 5DU 304 ? 15 'binding site for residue 5DU B 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  5DU F .   ? 5DU A 304 . ? 1_555 ? 
5  AC2 9  LYS A 148 ? LYS A 149 . ? 1_555 ? 
6  AC2 9  LYS A 212 ? LYS A 213 . ? 1_555 ? 
7  AC2 9  GLU A 213 ? GLU A 214 . ? 1_555 ? 
8  AC2 9  PRO A 214 ? PRO A 215 . ? 1_555 ? 
9  AC2 9  HOH K .   ? HOH A 452 . ? 1_555 ? 
10 AC2 9  HOH K .   ? HOH A 456 . ? 1_555 ? 
11 AC2 9  HOH K .   ? HOH A 487 . ? 1_555 ? 
12 AC2 9  HOH K .   ? HOH A 516 . ? 1_555 ? 
13 AC2 9  HOH K .   ? HOH A 562 . ? 1_555 ? 
14 AC3 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
15 AC3 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
16 AC3 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
17 AC3 4  HOH K .   ? HOH A 468 . ? 1_555 ? 
18 AC4 15 TYR A 7   ? TYR A 7   . ? 1_555 ? 
19 AC4 15 HIS A 64  ? HIS A 64  . ? 1_555 ? 
20 AC4 15 ALA A 65  ? ALA A 65  . ? 1_555 ? 
21 AC4 15 GLN A 92  ? GLN A 92  . ? 1_555 ? 
22 AC4 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
23 AC4 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
24 AC4 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
25 AC4 15 VAL A 121 ? VAL A 121 . ? 1_555 ? 
26 AC4 15 PHE A 130 ? PHE A 131 . ? 1_555 ? 
27 AC4 15 LEU A 140 ? LEU A 141 . ? 1_555 ? 
28 AC4 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
29 AC4 15 THR A 198 ? THR A 199 . ? 1_555 ? 
30 AC4 15 THR A 199 ? THR A 200 . ? 1_555 ? 
31 AC4 15 ZN  C .   ? ZN  A 301 . ? 1_555 ? 
32 AC4 15 HOH K .   ? HOH A 584 . ? 1_555 ? 
33 AC5 4  HIS B 94  ? HIS B 94  . ? 1_555 ? 
34 AC5 4  HIS B 96  ? HIS B 96  . ? 1_555 ? 
35 AC5 4  HIS B 119 ? HIS B 119 . ? 1_555 ? 
36 AC5 4  5DU J .   ? 5DU B 304 . ? 1_555 ? 
37 AC6 8  LYS B 148 ? LYS B 149 . ? 1_555 ? 
38 AC6 8  LYS B 212 ? LYS B 213 . ? 1_555 ? 
39 AC6 8  PRO B 214 ? PRO B 215 . ? 1_555 ? 
40 AC6 8  HOH L .   ? HOH B 418 . ? 1_555 ? 
41 AC6 8  HOH L .   ? HOH B 449 . ? 1_555 ? 
42 AC6 8  HOH L .   ? HOH B 485 . ? 1_555 ? 
43 AC6 8  HOH L .   ? HOH B 492 . ? 1_555 ? 
44 AC6 8  HOH L .   ? HOH B 548 . ? 1_555 ? 
45 AC7 5  TYR B 7   ? TYR B 7   . ? 1_555 ? 
46 AC7 5  ASP B 242 ? ASP B 243 . ? 1_555 ? 
47 AC7 5  TRP B 244 ? TRP B 245 . ? 1_555 ? 
48 AC7 5  PRO B 246 ? PRO B 247 . ? 1_555 ? 
49 AC7 5  HOH L .   ? HOH B 457 . ? 1_555 ? 
50 AC8 15 TYR B 7   ? TYR B 7   . ? 1_555 ? 
51 AC8 15 HIS B 64  ? HIS B 64  . ? 1_555 ? 
52 AC8 15 ALA B 65  ? ALA B 65  . ? 1_555 ? 
53 AC8 15 GLN B 92  ? GLN B 92  . ? 1_555 ? 
54 AC8 15 HIS B 94  ? HIS B 94  . ? 1_555 ? 
55 AC8 15 HIS B 96  ? HIS B 96  . ? 1_555 ? 
56 AC8 15 HIS B 119 ? HIS B 119 . ? 1_555 ? 
57 AC8 15 VAL B 121 ? VAL B 121 . ? 1_555 ? 
58 AC8 15 PHE B 130 ? PHE B 131 . ? 1_555 ? 
59 AC8 15 LEU B 140 ? LEU B 141 . ? 1_555 ? 
60 AC8 15 LEU B 197 ? LEU B 198 . ? 1_555 ? 
61 AC8 15 THR B 198 ? THR B 199 . ? 1_555 ? 
62 AC8 15 THR B 199 ? THR B 200 . ? 1_555 ? 
63 AC8 15 ZN  G .   ? ZN  B 301 . ? 1_555 ? 
64 AC8 15 HOH L .   ? HOH B 437 . ? 1_555 ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ZN  A ZN  301 ? ? N4 A 5DU 304 ? ? 1.43 
2 1 OD2 B ASP 75  ? A O  B HOH 401 ? ? 1.89 
3 1 O   B HOH 412 ? ? O  B HOH 477 ? ? 1.99 
4 1 ND1 A HIS 10  ? B O  A HOH 401 ? ? 2.04 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A HIS 36 ? ? CD2 A HIS 36 ? ? 1.413 1.354 0.059 0.009 N 
2 1 CG B HIS 36 ? ? CD2 B HIS 36 ? ? 1.414 1.354 0.060 0.009 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             O 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_1              186 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             C 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              186 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             N 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             GLU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              187 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                109.73 
_pdbx_validate_rmsd_angle.angle_target_value         122.70 
_pdbx_validate_rmsd_angle.angle_deviation            -12.97 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
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 HIS A 10  ? A -145.91 16.89   
2  1 ASN A 11  ? ? -144.72 15.99   
3  1 ARG A 27  ? ? -143.48 52.40   
4  1 ASP A 75  ? ? -68.33  85.25   
5  1 LYS A 76  ? ? -119.13 -71.99  
6  1 GLU A 106 ? ? -90.89  -60.12  
7  1 LYS A 111 ? ? 75.69   -3.43   
8  1 PHE A 176 ? ? -151.39 69.13   
9  1 ASN A 244 ? ? -94.10  43.46   
10 1 LYS A 252 ? A 54.73   -138.79 
11 1 LYS A 252 ? B 55.71   -137.95 
12 1 ASN B 11  ? ? -158.93 9.97    
13 1 ARG B 27  ? ? -143.42 54.82   
14 1 ASP B 75  ? B -66.55  81.66   
15 1 LYS B 76  ? ? -97.74  -62.41  
16 1 LYS B 111 ? ? 74.72   -4.00   
17 1 PHE B 176 ? ? -153.29 69.27   
18 1 ASN B 244 ? ? -93.36  42.70   
19 1 LYS B 252 ? A 57.03   -139.16 
20 1 LYS B 252 ? B 56.41   -138.04 
# 
_phasing.method   MR 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       665 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.99 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 B MET 1 ? B MET 1 
4 1 Y 1 B SER 2 ? B SER 2 
# 
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 
5DU F13  F  N N 1   
5DU C9   C  Y N 2   
5DU C8   C  Y N 3   
5DU S24  S  N N 4   
5DU C25  C  N N 5   
5DU C26  C  N N 6   
5DU O27  O  N N 7   
5DU C7   C  Y N 8   
5DU F12  F  N N 9   
5DU C6   C  Y N 10  
5DU F11  F  N N 11  
5DU C10  C  Y N 12  
5DU C5   C  Y N 13  
5DU S1   S  N N 14  
5DU O3   O  N N 15  
5DU N4   N  N N 16  
5DU O2   O  N N 17  
5DU N14  N  N N 18  
5DU C15  C  N S 19  
5DU C19  C  Y N 20  
5DU C20  C  Y N 21  
5DU C21  C  Y N 22  
5DU C22  C  Y N 23  
5DU C23  C  Y N 24  
5DU C18  C  Y N 25  
5DU C17  C  N N 26  
5DU C16  C  N N 27  
5DU H1   H  N N 28  
5DU H2   H  N N 29  
5DU H3   H  N N 30  
5DU H4   H  N N 31  
5DU H5   H  N N 32  
5DU H6   H  N N 33  
5DU H7   H  N N 34  
5DU H8   H  N N 35  
5DU H9   H  N N 36  
5DU H10  H  N N 37  
5DU H11  H  N N 38  
5DU H12  H  N N 39  
5DU H13  H  N N 40  
5DU H14  H  N N 41  
5DU H15  H  N N 42  
5DU H16  H  N N 43  
5DU H17  H  N N 44  
ALA N    N  N N 45  
ALA CA   C  N S 46  
ALA C    C  N N 47  
ALA O    O  N N 48  
ALA CB   C  N N 49  
ALA OXT  O  N N 50  
ALA H    H  N N 51  
ALA H2   H  N N 52  
ALA HA   H  N N 53  
ALA HB1  H  N N 54  
ALA HB2  H  N N 55  
ALA HB3  H  N N 56  
ALA HXT  H  N N 57  
ARG N    N  N N 58  
ARG CA   C  N S 59  
ARG C    C  N N 60  
ARG O    O  N N 61  
ARG CB   C  N N 62  
ARG CG   C  N N 63  
ARG CD   C  N N 64  
ARG NE   N  N N 65  
ARG CZ   C  N N 66  
ARG NH1  N  N N 67  
ARG NH2  N  N N 68  
ARG OXT  O  N N 69  
ARG H    H  N N 70  
ARG H2   H  N N 71  
ARG HA   H  N N 72  
ARG HB2  H  N N 73  
ARG HB3  H  N N 74  
ARG HG2  H  N N 75  
ARG HG3  H  N N 76  
ARG HD2  H  N N 77  
ARG HD3  H  N N 78  
ARG HE   H  N N 79  
ARG HH11 H  N N 80  
ARG HH12 H  N N 81  
ARG HH21 H  N N 82  
ARG HH22 H  N N 83  
ARG HXT  H  N N 84  
ASN N    N  N N 85  
ASN CA   C  N S 86  
ASN C    C  N N 87  
ASN O    O  N N 88  
ASN CB   C  N N 89  
ASN CG   C  N N 90  
ASN OD1  O  N N 91  
ASN ND2  N  N N 92  
ASN OXT  O  N N 93  
ASN H    H  N N 94  
ASN H2   H  N N 95  
ASN HA   H  N N 96  
ASN HB2  H  N N 97  
ASN HB3  H  N N 98  
ASN HD21 H  N N 99  
ASN HD22 H  N N 100 
ASN HXT  H  N N 101 
ASP N    N  N N 102 
ASP CA   C  N S 103 
ASP C    C  N N 104 
ASP O    O  N N 105 
ASP CB   C  N N 106 
ASP CG   C  N N 107 
ASP OD1  O  N N 108 
ASP OD2  O  N N 109 
ASP OXT  O  N N 110 
ASP H    H  N N 111 
ASP H2   H  N N 112 
ASP HA   H  N N 113 
ASP HB2  H  N N 114 
ASP HB3  H  N N 115 
ASP HD2  H  N N 116 
ASP HXT  H  N N 117 
BCN N1   N  N N 118 
BCN C1   C  N N 119 
BCN C2   C  N N 120 
BCN O21  O  N N 121 
BCN O22  O  N N 122 
BCN C3   C  N N 123 
BCN C4   C  N N 124 
BCN O4   O  N N 125 
BCN C5   C  N N 126 
BCN C6   C  N N 127 
BCN O6   O  N N 128 
BCN H11  H  N N 129 
BCN H12  H  N N 130 
BCN HO2  H  N N 131 
BCN H31  H  N N 132 
BCN H32  H  N N 133 
BCN H41  H  N N 134 
BCN H42  H  N N 135 
BCN HO4  H  N N 136 
BCN H51  H  N N 137 
BCN H52  H  N N 138 
BCN H61  H  N N 139 
BCN H62  H  N N 140 
BCN HO6  H  N N 141 
CYS N    N  N N 142 
CYS CA   C  N R 143 
CYS C    C  N N 144 
CYS O    O  N N 145 
CYS CB   C  N N 146 
CYS SG   S  N N 147 
CYS OXT  O  N N 148 
CYS H    H  N N 149 
CYS H2   H  N N 150 
CYS HA   H  N N 151 
CYS HB2  H  N N 152 
CYS HB3  H  N N 153 
CYS HG   H  N N 154 
CYS HXT  H  N N 155 
DMS S    S  N N 156 
DMS O    O  N N 157 
DMS C1   C  N N 158 
DMS C2   C  N N 159 
DMS H11  H  N N 160 
DMS H12  H  N N 161 
DMS H13  H  N N 162 
DMS H21  H  N N 163 
DMS H22  H  N N 164 
DMS H23  H  N N 165 
GLN N    N  N N 166 
GLN CA   C  N S 167 
GLN C    C  N N 168 
GLN O    O  N N 169 
GLN CB   C  N N 170 
GLN CG   C  N N 171 
GLN CD   C  N N 172 
GLN OE1  O  N N 173 
GLN NE2  N  N N 174 
GLN OXT  O  N N 175 
GLN H    H  N N 176 
GLN H2   H  N N 177 
GLN HA   H  N N 178 
GLN HB2  H  N N 179 
GLN HB3  H  N N 180 
GLN HG2  H  N N 181 
GLN HG3  H  N N 182 
GLN HE21 H  N N 183 
GLN HE22 H  N N 184 
GLN HXT  H  N N 185 
GLU N    N  N N 186 
GLU CA   C  N S 187 
GLU C    C  N N 188 
GLU O    O  N N 189 
GLU CB   C  N N 190 
GLU CG   C  N N 191 
GLU CD   C  N N 192 
GLU OE1  O  N N 193 
GLU OE2  O  N N 194 
GLU OXT  O  N N 195 
GLU H    H  N N 196 
GLU H2   H  N N 197 
GLU HA   H  N N 198 
GLU HB2  H  N N 199 
GLU HB3  H  N N 200 
GLU HG2  H  N N 201 
GLU HG3  H  N N 202 
GLU HE2  H  N N 203 
GLU HXT  H  N N 204 
GLY N    N  N N 205 
GLY CA   C  N N 206 
GLY C    C  N N 207 
GLY O    O  N N 208 
GLY OXT  O  N N 209 
GLY H    H  N N 210 
GLY H2   H  N N 211 
GLY HA2  H  N N 212 
GLY HA3  H  N N 213 
GLY HXT  H  N N 214 
HIS N    N  N N 215 
HIS CA   C  N S 216 
HIS C    C  N N 217 
HIS O    O  N N 218 
HIS CB   C  N N 219 
HIS CG   C  Y N 220 
HIS ND1  N  Y N 221 
HIS CD2  C  Y N 222 
HIS CE1  C  Y N 223 
HIS NE2  N  Y N 224 
HIS OXT  O  N N 225 
HIS H    H  N N 226 
HIS H2   H  N N 227 
HIS HA   H  N N 228 
HIS HB2  H  N N 229 
HIS HB3  H  N N 230 
HIS HD1  H  N N 231 
HIS HD2  H  N N 232 
HIS HE1  H  N N 233 
HIS HE2  H  N N 234 
HIS HXT  H  N N 235 
HOH O    O  N N 236 
HOH H1   H  N N 237 
HOH H2   H  N N 238 
ILE N    N  N N 239 
ILE CA   C  N S 240 
ILE C    C  N N 241 
ILE O    O  N N 242 
ILE CB   C  N S 243 
ILE CG1  C  N N 244 
ILE CG2  C  N N 245 
ILE CD1  C  N N 246 
ILE OXT  O  N N 247 
ILE H    H  N N 248 
ILE H2   H  N N 249 
ILE HA   H  N N 250 
ILE HB   H  N N 251 
ILE HG12 H  N N 252 
ILE HG13 H  N N 253 
ILE HG21 H  N N 254 
ILE HG22 H  N N 255 
ILE HG23 H  N N 256 
ILE HD11 H  N N 257 
ILE HD12 H  N N 258 
ILE HD13 H  N N 259 
ILE HXT  H  N N 260 
LEU N    N  N N 261 
LEU CA   C  N S 262 
LEU C    C  N N 263 
LEU O    O  N N 264 
LEU CB   C  N N 265 
LEU CG   C  N N 266 
LEU CD1  C  N N 267 
LEU CD2  C  N N 268 
LEU OXT  O  N N 269 
LEU H    H  N N 270 
LEU H2   H  N N 271 
LEU HA   H  N N 272 
LEU HB2  H  N N 273 
LEU HB3  H  N N 274 
LEU HG   H  N N 275 
LEU HD11 H  N N 276 
LEU HD12 H  N N 277 
LEU HD13 H  N N 278 
LEU HD21 H  N N 279 
LEU HD22 H  N N 280 
LEU HD23 H  N N 281 
LEU HXT  H  N N 282 
LYS N    N  N N 283 
LYS CA   C  N S 284 
LYS C    C  N N 285 
LYS O    O  N N 286 
LYS CB   C  N N 287 
LYS CG   C  N N 288 
LYS CD   C  N N 289 
LYS CE   C  N N 290 
LYS NZ   N  N N 291 
LYS OXT  O  N N 292 
LYS H    H  N N 293 
LYS H2   H  N N 294 
LYS HA   H  N N 295 
LYS HB2  H  N N 296 
LYS HB3  H  N N 297 
LYS HG2  H  N N 298 
LYS HG3  H  N N 299 
LYS HD2  H  N N 300 
LYS HD3  H  N N 301 
LYS HE2  H  N N 302 
LYS HE3  H  N N 303 
LYS HZ1  H  N N 304 
LYS HZ2  H  N N 305 
LYS HZ3  H  N N 306 
LYS HXT  H  N N 307 
MET N    N  N N 308 
MET CA   C  N S 309 
MET C    C  N N 310 
MET O    O  N N 311 
MET CB   C  N N 312 
MET CG   C  N N 313 
MET SD   S  N N 314 
MET CE   C  N N 315 
MET OXT  O  N N 316 
MET H    H  N N 317 
MET H2   H  N N 318 
MET HA   H  N N 319 
MET HB2  H  N N 320 
MET HB3  H  N N 321 
MET HG2  H  N N 322 
MET HG3  H  N N 323 
MET HE1  H  N N 324 
MET HE2  H  N N 325 
MET HE3  H  N N 326 
MET HXT  H  N N 327 
PHE N    N  N N 328 
PHE CA   C  N S 329 
PHE C    C  N N 330 
PHE O    O  N N 331 
PHE CB   C  N N 332 
PHE CG   C  Y N 333 
PHE CD1  C  Y N 334 
PHE CD2  C  Y N 335 
PHE CE1  C  Y N 336 
PHE CE2  C  Y N 337 
PHE CZ   C  Y N 338 
PHE OXT  O  N N 339 
PHE H    H  N N 340 
PHE H2   H  N N 341 
PHE HA   H  N N 342 
PHE HB2  H  N N 343 
PHE HB3  H  N N 344 
PHE HD1  H  N N 345 
PHE HD2  H  N N 346 
PHE HE1  H  N N 347 
PHE HE2  H  N N 348 
PHE HZ   H  N N 349 
PHE HXT  H  N N 350 
PRO N    N  N N 351 
PRO CA   C  N S 352 
PRO C    C  N N 353 
PRO O    O  N N 354 
PRO CB   C  N N 355 
PRO CG   C  N N 356 
PRO CD   C  N N 357 
PRO OXT  O  N N 358 
PRO H    H  N N 359 
PRO HA   H  N N 360 
PRO HB2  H  N N 361 
PRO HB3  H  N N 362 
PRO HG2  H  N N 363 
PRO HG3  H  N N 364 
PRO HD2  H  N N 365 
PRO HD3  H  N N 366 
PRO HXT  H  N N 367 
SER N    N  N N 368 
SER CA   C  N S 369 
SER C    C  N N 370 
SER O    O  N N 371 
SER CB   C  N N 372 
SER OG   O  N N 373 
SER OXT  O  N N 374 
SER H    H  N N 375 
SER H2   H  N N 376 
SER HA   H  N N 377 
SER HB2  H  N N 378 
SER HB3  H  N N 379 
SER HG   H  N N 380 
SER HXT  H  N N 381 
THR N    N  N N 382 
THR CA   C  N S 383 
THR C    C  N N 384 
THR O    O  N N 385 
THR CB   C  N R 386 
THR OG1  O  N N 387 
THR CG2  C  N N 388 
THR OXT  O  N N 389 
THR H    H  N N 390 
THR H2   H  N N 391 
THR HA   H  N N 392 
THR HB   H  N N 393 
THR HG1  H  N N 394 
THR HG21 H  N N 395 
THR HG22 H  N N 396 
THR HG23 H  N N 397 
THR HXT  H  N N 398 
TRP N    N  N N 399 
TRP CA   C  N S 400 
TRP C    C  N N 401 
TRP O    O  N N 402 
TRP CB   C  N N 403 
TRP CG   C  Y N 404 
TRP CD1  C  Y N 405 
TRP CD2  C  Y N 406 
TRP NE1  N  Y N 407 
TRP CE2  C  Y N 408 
TRP CE3  C  Y N 409 
TRP CZ2  C  Y N 410 
TRP CZ3  C  Y N 411 
TRP CH2  C  Y N 412 
TRP OXT  O  N N 413 
TRP H    H  N N 414 
TRP H2   H  N N 415 
TRP HA   H  N N 416 
TRP HB2  H  N N 417 
TRP HB3  H  N N 418 
TRP HD1  H  N N 419 
TRP HE1  H  N N 420 
TRP HE3  H  N N 421 
TRP HZ2  H  N N 422 
TRP HZ3  H  N N 423 
TRP HH2  H  N N 424 
TRP HXT  H  N N 425 
TYR N    N  N N 426 
TYR CA   C  N S 427 
TYR C    C  N N 428 
TYR O    O  N N 429 
TYR CB   C  N N 430 
TYR CG   C  Y N 431 
TYR CD1  C  Y N 432 
TYR CD2  C  Y N 433 
TYR CE1  C  Y N 434 
TYR CE2  C  Y N 435 
TYR CZ   C  Y N 436 
TYR OH   O  N N 437 
TYR OXT  O  N N 438 
TYR H    H  N N 439 
TYR H2   H  N N 440 
TYR HA   H  N N 441 
TYR HB2  H  N N 442 
TYR HB3  H  N N 443 
TYR HD1  H  N N 444 
TYR HD2  H  N N 445 
TYR HE1  H  N N 446 
TYR HE2  H  N N 447 
TYR HH   H  N N 448 
TYR HXT  H  N N 449 
VAL N    N  N N 450 
VAL CA   C  N S 451 
VAL C    C  N N 452 
VAL O    O  N N 453 
VAL CB   C  N N 454 
VAL CG1  C  N N 455 
VAL CG2  C  N N 456 
VAL OXT  O  N N 457 
VAL H    H  N N 458 
VAL H2   H  N N 459 
VAL HA   H  N N 460 
VAL HB   H  N N 461 
VAL HG11 H  N N 462 
VAL HG12 H  N N 463 
VAL HG13 H  N N 464 
VAL HG21 H  N N 465 
VAL HG22 H  N N 466 
VAL HG23 H  N N 467 
VAL HXT  H  N N 468 
ZN  ZN   ZN N N 469 
# 
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 
5DU O27 C26  sing N N 1   
5DU C26 C25  sing N N 2   
5DU C23 C18  doub Y N 3   
5DU C23 C22  sing Y N 4   
5DU C17 C18  sing N N 5   
5DU C17 C16  sing N N 6   
5DU C18 C19  sing Y N 7   
5DU C22 C21  doub Y N 8   
5DU C21 C20  sing Y N 9   
5DU C19 C20  doub Y N 10  
5DU C19 C15  sing N N 11  
5DU F13 C9   sing N N 12  
5DU C15 C16  sing N N 13  
5DU C15 N14  sing N N 14  
5DU C25 S24  sing N N 15  
5DU S24 C8   sing N N 16  
5DU N14 C10  sing N N 17  
5DU C9  C8   doub Y N 18  
5DU C9  C10  sing Y N 19  
5DU C8  C7   sing Y N 20  
5DU C10 C5   doub Y N 21  
5DU C7  C6   doub Y N 22  
5DU C7  F12  sing N N 23  
5DU C5  C6   sing Y N 24  
5DU C5  S1   sing N N 25  
5DU C6  F11  sing N N 26  
5DU N4  S1   sing N N 27  
5DU S1  O2   doub N N 28  
5DU S1  O3   doub N N 29  
5DU C25 H1   sing N N 30  
5DU C25 H2   sing N N 31  
5DU C26 H3   sing N N 32  
5DU C26 H4   sing N N 33  
5DU O27 H5   sing N N 34  
5DU N4  H6   sing N N 35  
5DU N4  H7   sing N N 36  
5DU N14 H8   sing N N 37  
5DU C15 H9   sing N N 38  
5DU C20 H10  sing N N 39  
5DU C21 H11  sing N N 40  
5DU C22 H12  sing N N 41  
5DU C23 H13  sing N N 42  
5DU C17 H14  sing N N 43  
5DU C17 H15  sing N N 44  
5DU C16 H16  sing N N 45  
5DU C16 H17  sing N N 46  
ALA N   CA   sing N N 47  
ALA N   H    sing N N 48  
ALA N   H2   sing N N 49  
ALA CA  C    sing N N 50  
ALA CA  CB   sing N N 51  
ALA CA  HA   sing N N 52  
ALA C   O    doub N N 53  
ALA C   OXT  sing N N 54  
ALA CB  HB1  sing N N 55  
ALA CB  HB2  sing N N 56  
ALA CB  HB3  sing N N 57  
ALA OXT HXT  sing N N 58  
ARG N   CA   sing N N 59  
ARG N   H    sing N N 60  
ARG N   H2   sing N N 61  
ARG CA  C    sing N N 62  
ARG CA  CB   sing N N 63  
ARG CA  HA   sing N N 64  
ARG C   O    doub N N 65  
ARG C   OXT  sing N N 66  
ARG CB  CG   sing N N 67  
ARG CB  HB2  sing N N 68  
ARG CB  HB3  sing N N 69  
ARG CG  CD   sing N N 70  
ARG CG  HG2  sing N N 71  
ARG CG  HG3  sing N N 72  
ARG CD  NE   sing N N 73  
ARG CD  HD2  sing N N 74  
ARG CD  HD3  sing N N 75  
ARG NE  CZ   sing N N 76  
ARG NE  HE   sing N N 77  
ARG CZ  NH1  sing N N 78  
ARG CZ  NH2  doub N N 79  
ARG NH1 HH11 sing N N 80  
ARG NH1 HH12 sing N N 81  
ARG NH2 HH21 sing N N 82  
ARG NH2 HH22 sing N N 83  
ARG OXT HXT  sing N N 84  
ASN N   CA   sing N N 85  
ASN N   H    sing N N 86  
ASN N   H2   sing N N 87  
ASN CA  C    sing N N 88  
ASN CA  CB   sing N N 89  
ASN CA  HA   sing N N 90  
ASN C   O    doub N N 91  
ASN C   OXT  sing N N 92  
ASN CB  CG   sing N N 93  
ASN CB  HB2  sing N N 94  
ASN CB  HB3  sing N N 95  
ASN CG  OD1  doub N N 96  
ASN CG  ND2  sing N N 97  
ASN ND2 HD21 sing N N 98  
ASN ND2 HD22 sing N N 99  
ASN OXT HXT  sing N N 100 
ASP N   CA   sing N N 101 
ASP N   H    sing N N 102 
ASP N   H2   sing N N 103 
ASP CA  C    sing N N 104 
ASP CA  CB   sing N N 105 
ASP CA  HA   sing N N 106 
ASP C   O    doub N N 107 
ASP C   OXT  sing N N 108 
ASP CB  CG   sing N N 109 
ASP CB  HB2  sing N N 110 
ASP CB  HB3  sing N N 111 
ASP CG  OD1  doub N N 112 
ASP CG  OD2  sing N N 113 
ASP OD2 HD2  sing N N 114 
ASP OXT HXT  sing N N 115 
BCN N1  C1   sing N N 116 
BCN N1  C3   sing N N 117 
BCN N1  C5   sing N N 118 
BCN C1  C2   sing N N 119 
BCN C1  H11  sing N N 120 
BCN C1  H12  sing N N 121 
BCN C2  O21  doub N N 122 
BCN C2  O22  sing N N 123 
BCN O22 HO2  sing N N 124 
BCN C3  C4   sing N N 125 
BCN C3  H31  sing N N 126 
BCN C3  H32  sing N N 127 
BCN C4  O4   sing N N 128 
BCN C4  H41  sing N N 129 
BCN C4  H42  sing N N 130 
BCN O4  HO4  sing N N 131 
BCN C5  C6   sing N N 132 
BCN C5  H51  sing N N 133 
BCN C5  H52  sing N N 134 
BCN C6  O6   sing N N 135 
BCN C6  H61  sing N N 136 
BCN C6  H62  sing N N 137 
BCN O6  HO6  sing N N 138 
CYS N   CA   sing N N 139 
CYS N   H    sing N N 140 
CYS N   H2   sing N N 141 
CYS CA  C    sing N N 142 
CYS CA  CB   sing N N 143 
CYS CA  HA   sing N N 144 
CYS C   O    doub N N 145 
CYS C   OXT  sing N N 146 
CYS CB  SG   sing N N 147 
CYS CB  HB2  sing N N 148 
CYS CB  HB3  sing N N 149 
CYS SG  HG   sing N N 150 
CYS OXT HXT  sing N N 151 
DMS S   O    doub N N 152 
DMS S   C1   sing N N 153 
DMS S   C2   sing N N 154 
DMS C1  H11  sing N N 155 
DMS C1  H12  sing N N 156 
DMS C1  H13  sing N N 157 
DMS C2  H21  sing N N 158 
DMS C2  H22  sing N N 159 
DMS C2  H23  sing N N 160 
GLN N   CA   sing N N 161 
GLN N   H    sing N N 162 
GLN N   H2   sing N N 163 
GLN CA  C    sing N N 164 
GLN CA  CB   sing N N 165 
GLN CA  HA   sing N N 166 
GLN C   O    doub N N 167 
GLN C   OXT  sing N N 168 
GLN CB  CG   sing N N 169 
GLN CB  HB2  sing N N 170 
GLN CB  HB3  sing N N 171 
GLN CG  CD   sing N N 172 
GLN CG  HG2  sing N N 173 
GLN CG  HG3  sing N N 174 
GLN CD  OE1  doub N N 175 
GLN CD  NE2  sing N N 176 
GLN NE2 HE21 sing N N 177 
GLN NE2 HE22 sing N N 178 
GLN OXT HXT  sing N N 179 
GLU N   CA   sing N N 180 
GLU N   H    sing N N 181 
GLU N   H2   sing N N 182 
GLU CA  C    sing N N 183 
GLU CA  CB   sing N N 184 
GLU CA  HA   sing N N 185 
GLU C   O    doub N N 186 
GLU C   OXT  sing N N 187 
GLU CB  CG   sing N N 188 
GLU CB  HB2  sing N N 189 
GLU CB  HB3  sing N N 190 
GLU CG  CD   sing N N 191 
GLU CG  HG2  sing N N 192 
GLU CG  HG3  sing N N 193 
GLU CD  OE1  doub N N 194 
GLU CD  OE2  sing N N 195 
GLU OE2 HE2  sing N N 196 
GLU OXT HXT  sing N N 197 
GLY N   CA   sing N N 198 
GLY N   H    sing N N 199 
GLY N   H2   sing N N 200 
GLY CA  C    sing N N 201 
GLY CA  HA2  sing N N 202 
GLY CA  HA3  sing N N 203 
GLY C   O    doub N N 204 
GLY C   OXT  sing N N 205 
GLY OXT HXT  sing N N 206 
HIS N   CA   sing N N 207 
HIS N   H    sing N N 208 
HIS N   H2   sing N N 209 
HIS CA  C    sing N N 210 
HIS CA  CB   sing N N 211 
HIS CA  HA   sing N N 212 
HIS C   O    doub N N 213 
HIS C   OXT  sing N N 214 
HIS CB  CG   sing N N 215 
HIS CB  HB2  sing N N 216 
HIS CB  HB3  sing N N 217 
HIS CG  ND1  sing Y N 218 
HIS CG  CD2  doub Y N 219 
HIS ND1 CE1  doub Y N 220 
HIS ND1 HD1  sing N N 221 
HIS CD2 NE2  sing Y N 222 
HIS CD2 HD2  sing N N 223 
HIS CE1 NE2  sing Y N 224 
HIS CE1 HE1  sing N N 225 
HIS NE2 HE2  sing N N 226 
HIS OXT HXT  sing N N 227 
HOH O   H1   sing N N 228 
HOH O   H2   sing N N 229 
ILE N   CA   sing N N 230 
ILE N   H    sing N N 231 
ILE N   H2   sing N N 232 
ILE CA  C    sing N N 233 
ILE CA  CB   sing N N 234 
ILE CA  HA   sing N N 235 
ILE C   O    doub N N 236 
ILE C   OXT  sing N N 237 
ILE CB  CG1  sing N N 238 
ILE CB  CG2  sing N N 239 
ILE CB  HB   sing N N 240 
ILE CG1 CD1  sing N N 241 
ILE CG1 HG12 sing N N 242 
ILE CG1 HG13 sing N N 243 
ILE CG2 HG21 sing N N 244 
ILE CG2 HG22 sing N N 245 
ILE CG2 HG23 sing N N 246 
ILE CD1 HD11 sing N N 247 
ILE CD1 HD12 sing N N 248 
ILE CD1 HD13 sing N N 249 
ILE OXT HXT  sing N N 250 
LEU N   CA   sing N N 251 
LEU N   H    sing N N 252 
LEU N   H2   sing N N 253 
LEU CA  C    sing N N 254 
LEU CA  CB   sing N N 255 
LEU CA  HA   sing N N 256 
LEU C   O    doub N N 257 
LEU C   OXT  sing N N 258 
LEU CB  CG   sing N N 259 
LEU CB  HB2  sing N N 260 
LEU CB  HB3  sing N N 261 
LEU CG  CD1  sing N N 262 
LEU CG  CD2  sing N N 263 
LEU CG  HG   sing N N 264 
LEU CD1 HD11 sing N N 265 
LEU CD1 HD12 sing N N 266 
LEU CD1 HD13 sing N N 267 
LEU CD2 HD21 sing N N 268 
LEU CD2 HD22 sing N N 269 
LEU CD2 HD23 sing N N 270 
LEU OXT HXT  sing N N 271 
LYS N   CA   sing N N 272 
LYS N   H    sing N N 273 
LYS N   H2   sing N N 274 
LYS CA  C    sing N N 275 
LYS CA  CB   sing N N 276 
LYS CA  HA   sing N N 277 
LYS C   O    doub N N 278 
LYS C   OXT  sing N N 279 
LYS CB  CG   sing N N 280 
LYS CB  HB2  sing N N 281 
LYS CB  HB3  sing N N 282 
LYS CG  CD   sing N N 283 
LYS CG  HG2  sing N N 284 
LYS CG  HG3  sing N N 285 
LYS CD  CE   sing N N 286 
LYS CD  HD2  sing N N 287 
LYS CD  HD3  sing N N 288 
LYS CE  NZ   sing N N 289 
LYS CE  HE2  sing N N 290 
LYS CE  HE3  sing N N 291 
LYS NZ  HZ1  sing N N 292 
LYS NZ  HZ2  sing N N 293 
LYS NZ  HZ3  sing N N 294 
LYS OXT HXT  sing N N 295 
MET N   CA   sing N N 296 
MET N   H    sing N N 297 
MET N   H2   sing N N 298 
MET CA  C    sing N N 299 
MET CA  CB   sing N N 300 
MET CA  HA   sing N N 301 
MET C   O    doub N N 302 
MET C   OXT  sing N N 303 
MET CB  CG   sing N N 304 
MET CB  HB2  sing N N 305 
MET CB  HB3  sing N N 306 
MET CG  SD   sing N N 307 
MET CG  HG2  sing N N 308 
MET CG  HG3  sing N N 309 
MET SD  CE   sing N N 310 
MET CE  HE1  sing N N 311 
MET CE  HE2  sing N N 312 
MET CE  HE3  sing N N 313 
MET OXT HXT  sing N N 314 
PHE N   CA   sing N N 315 
PHE N   H    sing N N 316 
PHE N   H2   sing N N 317 
PHE CA  C    sing N N 318 
PHE CA  CB   sing N N 319 
PHE CA  HA   sing N N 320 
PHE C   O    doub N N 321 
PHE C   OXT  sing N N 322 
PHE CB  CG   sing N N 323 
PHE CB  HB2  sing N N 324 
PHE CB  HB3  sing N N 325 
PHE CG  CD1  doub Y N 326 
PHE CG  CD2  sing Y N 327 
PHE CD1 CE1  sing Y N 328 
PHE CD1 HD1  sing N N 329 
PHE CD2 CE2  doub Y N 330 
PHE CD2 HD2  sing N N 331 
PHE CE1 CZ   doub Y N 332 
PHE CE1 HE1  sing N N 333 
PHE CE2 CZ   sing Y N 334 
PHE CE2 HE2  sing N N 335 
PHE CZ  HZ   sing N N 336 
PHE OXT HXT  sing N N 337 
PRO N   CA   sing N N 338 
PRO N   CD   sing N N 339 
PRO N   H    sing N N 340 
PRO CA  C    sing N N 341 
PRO CA  CB   sing N N 342 
PRO CA  HA   sing N N 343 
PRO C   O    doub N N 344 
PRO C   OXT  sing N N 345 
PRO CB  CG   sing N N 346 
PRO CB  HB2  sing N N 347 
PRO CB  HB3  sing N N 348 
PRO CG  CD   sing N N 349 
PRO CG  HG2  sing N N 350 
PRO CG  HG3  sing N N 351 
PRO CD  HD2  sing N N 352 
PRO CD  HD3  sing N N 353 
PRO OXT HXT  sing N N 354 
SER N   CA   sing N N 355 
SER N   H    sing N N 356 
SER N   H2   sing N N 357 
SER CA  C    sing N N 358 
SER CA  CB   sing N N 359 
SER CA  HA   sing N N 360 
SER C   O    doub N N 361 
SER C   OXT  sing N N 362 
SER CB  OG   sing N N 363 
SER CB  HB2  sing N N 364 
SER CB  HB3  sing N N 365 
SER OG  HG   sing N N 366 
SER OXT HXT  sing N N 367 
THR N   CA   sing N N 368 
THR N   H    sing N N 369 
THR N   H2   sing N N 370 
THR CA  C    sing N N 371 
THR CA  CB   sing N N 372 
THR CA  HA   sing N N 373 
THR C   O    doub N N 374 
THR C   OXT  sing N N 375 
THR CB  OG1  sing N N 376 
THR CB  CG2  sing N N 377 
THR CB  HB   sing N N 378 
THR OG1 HG1  sing N N 379 
THR CG2 HG21 sing N N 380 
THR CG2 HG22 sing N N 381 
THR CG2 HG23 sing N N 382 
THR OXT HXT  sing N N 383 
TRP N   CA   sing N N 384 
TRP N   H    sing N N 385 
TRP N   H2   sing N N 386 
TRP CA  C    sing N N 387 
TRP CA  CB   sing N N 388 
TRP CA  HA   sing N N 389 
TRP C   O    doub N N 390 
TRP C   OXT  sing N N 391 
TRP CB  CG   sing N N 392 
TRP CB  HB2  sing N N 393 
TRP CB  HB3  sing N N 394 
TRP CG  CD1  doub Y N 395 
TRP CG  CD2  sing Y N 396 
TRP CD1 NE1  sing Y N 397 
TRP CD1 HD1  sing N N 398 
TRP CD2 CE2  doub Y N 399 
TRP CD2 CE3  sing Y N 400 
TRP NE1 CE2  sing Y N 401 
TRP NE1 HE1  sing N N 402 
TRP CE2 CZ2  sing Y N 403 
TRP CE3 CZ3  doub Y N 404 
TRP CE3 HE3  sing N N 405 
TRP CZ2 CH2  doub Y N 406 
TRP CZ2 HZ2  sing N N 407 
TRP CZ3 CH2  sing Y N 408 
TRP CZ3 HZ3  sing N N 409 
TRP CH2 HH2  sing N N 410 
TRP OXT HXT  sing N N 411 
TYR N   CA   sing N N 412 
TYR N   H    sing N N 413 
TYR N   H2   sing N N 414 
TYR CA  C    sing N N 415 
TYR CA  CB   sing N N 416 
TYR CA  HA   sing N N 417 
TYR C   O    doub N N 418 
TYR C   OXT  sing N N 419 
TYR CB  CG   sing N N 420 
TYR CB  HB2  sing N N 421 
TYR CB  HB3  sing N N 422 
TYR CG  CD1  doub Y N 423 
TYR CG  CD2  sing Y N 424 
TYR CD1 CE1  sing Y N 425 
TYR CD1 HD1  sing N N 426 
TYR CD2 CE2  doub Y N 427 
TYR CD2 HD2  sing N N 428 
TYR CE1 CZ   doub Y N 429 
TYR CE1 HE1  sing N N 430 
TYR CE2 CZ   sing Y N 431 
TYR CE2 HE2  sing N N 432 
TYR CZ  OH   sing N N 433 
TYR OH  HH   sing N N 434 
TYR OXT HXT  sing N N 435 
VAL N   CA   sing N N 436 
VAL N   H    sing N N 437 
VAL N   H2   sing N N 438 
VAL CA  C    sing N N 439 
VAL CA  CB   sing N N 440 
VAL CA  HA   sing N N 441 
VAL C   O    doub N N 442 
VAL C   OXT  sing N N 443 
VAL CB  CG1  sing N N 444 
VAL CB  CG2  sing N N 445 
VAL CB  HB   sing N N 446 
VAL CG1 HG11 sing N N 447 
VAL CG1 HG12 sing N N 448 
VAL CG1 HG13 sing N N 449 
VAL CG2 HG21 sing N N 450 
VAL CG2 HG22 sing N N 451 
VAL CG2 HG23 sing N N 452 
VAL OXT HXT  sing N N 453 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3HLJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    5DOH 
_atom_sites.fract_transf_matrix[1][1]   0.023718 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005999 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024297 
_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]   0.014355 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 3   ? -23.923 1.712   9.333   1.00 21.13  ? 3   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 3   ? -23.598 0.724   8.250   1.00 27.45  ? 3   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 3   ? -22.545 1.183   7.260   1.00 25.85  ? 3   HIS A C   1 
ATOM   4    O  O   . HIS A 1 3   ? -22.806 1.349   6.017   1.00 34.04  ? 3   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 3   ? -24.819 0.301   7.465   1.00 27.00  ? 3   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 3   ? -24.579 -0.961  6.674   1.00 27.17  ? 3   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 3   ? -24.147 -0.970  5.352   1.00 29.16  ? 3   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 3   ? -24.689 -2.307  7.065   1.00 30.96  ? 3   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 3   ? -24.016 -2.246  4.957   1.00 24.80  ? 3   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 3   ? -24.364 -3.066  5.995   1.00 41.02  ? 3   HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 4   ? -21.335 1.375   7.805   1.00 25.24  ? 4   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 4   ? -20.214 1.903   7.035   1.00 31.52  ? 4   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 4   ? -19.481 0.812   6.339   1.00 20.43  ? 4   HIS A C   1 
ATOM   14   O  O   . HIS A 1 4   ? -19.651 -0.397  6.613   1.00 21.09  ? 4   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 4   ? -19.293 2.750   7.909   1.00 37.52  ? 4   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 4   ? -19.073 4.125   7.338   1.00 53.06  ? 4   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 4   ? -20.058 4.803   6.716   1.00 70.47  ? 4   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 4   ? -17.950 4.941   7.293   1.00 68.65  ? 4   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 4   ? -19.595 5.981   6.283   1.00 73.52  ? 4   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 4   ? -18.306 6.077   6.645   1.00 81.97  ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? -18.689 1.202   5.368   1.00 19.96  ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? -17.944 0.244   4.594   1.00 15.48  ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? -16.896 -0.525  5.366   1.00 15.84  ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? -16.404 -0.052  6.398   1.00 17.10  ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? -17.300 0.941   3.373   1.00 16.17  ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? -16.122 1.826   3.736   1.00 13.79  ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? -16.132 3.192   4.029   1.00 16.98  ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? -14.750 1.405   3.775   1.00 13.10  ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? -14.883 3.621   4.260   1.00 16.19  ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? -13.995 2.578   4.148   1.00 15.07  ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? -14.083 0.196   3.550   1.00 13.53  ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? -12.605 2.539   4.295   1.00 15.17  ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? -12.675 0.178   3.716   1.00 15.16  ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? -11.957 1.357   4.044   1.00 16.05  ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? -16.599 -1.722  4.900   1.00 14.64  ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? -15.528 -2.513  5.538   1.00 15.91  ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? -15.201 -3.668  4.634   1.00 13.88  ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? -15.234 -3.512  3.382   1.00 14.65  ? 6   GLY A O   1 
ATOM   39   N  N   A TYR A 1 7   ? -14.668 -4.692  5.375   0.50 10.76  ? 7   TYR A N   1 
ATOM   40   N  N   B TYR A 1 7   ? -15.184 -4.915  5.027   0.50 14.76  ? 7   TYR A N   1 
ATOM   41   C  CA  A TYR A 1 7   ? -14.247 -5.997  4.813   0.50 9.90   ? 7   TYR A CA  1 
ATOM   42   C  CA  B TYR A 1 7   ? -14.778 -5.946  4.017   0.50 11.57  ? 7   TYR A CA  1 
ATOM   43   C  C   A TYR A 1 7   ? -15.016 -7.175  5.483   0.50 12.09  ? 7   TYR A C   1 
ATOM   44   C  C   B TYR A 1 7   ? -15.622 -7.224  4.056   0.50 13.17  ? 7   TYR A C   1 
ATOM   45   O  O   A TYR A 1 7   ? -14.568 -8.341  5.444   0.50 17.95  ? 7   TYR A O   1 
ATOM   46   O  O   B TYR A 1 7   ? -15.297 -8.263  3.400   0.50 18.10  ? 7   TYR A O   1 
ATOM   47   C  CB  A TYR A 1 7   ? -12.766 -6.224  4.994   0.50 8.79   ? 7   TYR A CB  1 
ATOM   48   C  CB  B TYR A 1 7   ? -13.320 -6.350  4.232   0.50 11.80  ? 7   TYR A CB  1 
ATOM   49   C  CG  A TYR A 1 7   ? -11.986 -5.114  4.343   0.50 7.74   ? 7   TYR A CG  1 
ATOM   50   C  CG  B TYR A 1 7   ? -12.320 -5.285  3.806   0.50 10.74  ? 7   TYR A CG  1 
ATOM   51   C  CD1 A TYR A 1 7   ? -11.668 -5.159  2.960   0.50 9.03   ? 7   TYR A CD1 1 
ATOM   52   C  CD1 B TYR A 1 7   ? -11.839 -5.244  2.477   0.50 10.66  ? 7   TYR A CD1 1 
ATOM   53   C  CD2 A TYR A 1 7   ? -11.510 -4.032  5.094   0.50 8.28   ? 7   TYR A CD2 1 
ATOM   54   C  CD2 B TYR A 1 7   ? -11.887 -4.298  4.667   0.50 11.93  ? 7   TYR A CD2 1 
ATOM   55   C  CE1 A TYR A 1 7   ? -10.905 -4.145  2.394   0.50 8.35   ? 7   TYR A CE1 1 
ATOM   56   C  CE1 B TYR A 1 7   ? -10.900 -4.251  2.067   0.50 9.81   ? 7   TYR A CE1 1 
ATOM   57   C  CE2 A TYR A 1 7   ? -10.755 -3.003  4.484   0.50 9.27   ? 7   TYR A CE2 1 
ATOM   58   C  CE2 B TYR A 1 7   ? -10.987 -3.296  4.277   0.50 11.62  ? 7   TYR A CE2 1 
ATOM   59   C  CZ  A TYR A 1 7   ? -10.467 -3.095  3.138   0.50 9.08   ? 7   TYR A CZ  1 
ATOM   60   C  CZ  B TYR A 1 7   ? -10.484 -3.286  2.995   0.50 9.87   ? 7   TYR A CZ  1 
ATOM   61   O  OH  A TYR A 1 7   ? -9.748  -2.140  2.461   0.50 10.67  ? 7   TYR A OH  1 
ATOM   62   O  OH  B TYR A 1 7   ? -9.593  -2.237  2.728   0.50 10.22  ? 7   TYR A OH  1 
ATOM   63   N  N   A GLY A 1 8   ? -16.193 -6.941  6.038   0.50 11.09  ? 8   GLY A N   1 
ATOM   64   N  N   B GLY A 1 8   ? -16.711 -7.082  4.821   0.50 15.00  ? 8   GLY A N   1 
ATOM   65   C  CA  A GLY A 1 8   ? -16.987 -7.984  6.720   0.50 13.57  ? 8   GLY A CA  1 
ATOM   66   C  CA  B GLY A 1 8   ? -17.721 -8.149  4.964   0.50 13.00  ? 8   GLY A CA  1 
ATOM   67   C  C   A GLY A 1 8   ? -17.881 -8.707  5.744   0.50 12.50  ? 8   GLY A C   1 
ATOM   68   C  C   B GLY A 1 8   ? -18.740 -8.411  3.842   0.50 13.98  ? 8   GLY A C   1 
ATOM   69   O  O   A GLY A 1 8   ? -17.763 -8.617  4.533   0.50 10.98  ? 8   GLY A O   1 
ATOM   70   O  O   B GLY A 1 8   ? -18.822 -7.770  2.784   0.50 19.66  ? 8   GLY A O   1 
ATOM   71   N  N   A LYS A 1 9   ? -18.865 -9.416  6.291   0.50 11.60  ? 9   LYS A N   1 
ATOM   72   N  N   B LYS A 1 9   ? -19.589 -9.417  4.067   0.50 15.39  ? 9   LYS A N   1 
ATOM   73   C  CA  A LYS A 1 9   ? -19.765 -10.232 5.470   0.50 12.73  ? 9   LYS A CA  1 
ATOM   74   C  CA  B LYS A 1 9   ? -20.549 -9.796  3.075   0.50 15.98  ? 9   LYS A CA  1 
ATOM   75   C  C   A LYS A 1 9   ? -20.864 -9.501  4.718   0.50 11.61  ? 9   LYS A C   1 
ATOM   76   C  C   B LYS A 1 9   ? -21.494 -8.635  2.818   0.50 13.47  ? 9   LYS A C   1 
ATOM   77   O  O   A LYS A 1 9   ? -21.495 -10.130 3.868   0.50 13.22  ? 9   LYS A O   1 
ATOM   78   O  O   B LYS A 1 9   ? -21.895 -8.456  1.672   0.50 17.55  ? 9   LYS A O   1 
ATOM   79   C  CB  A LYS A 1 9   ? -20.322 -11.410 6.291   0.50 14.03  ? 9   LYS A CB  1 
ATOM   80   C  CB  B LYS A 1 9   ? -21.308 -11.052 3.530   0.50 18.84  ? 9   LYS A CB  1 
ATOM   81   C  CG  A LYS A 1 9   ? -19.281 -12.466 6.659   0.50 17.99  ? 9   LYS A CG  1 
ATOM   82   N  N   A HIS A 1 10  ? -21.062 -8.204  5.004   0.50 12.19  ? 10  HIS A N   1 
ATOM   83   N  N   B HIS A 1 10  ? -21.849 -7.888  3.858   0.50 12.03  ? 10  HIS A N   1 
ATOM   84   C  CA  A HIS A 1 10  ? -22.159 -7.419  4.412   0.50 11.63  ? 10  HIS A CA  1 
ATOM   85   C  CA  B HIS A 1 10  ? -22.790 -6.838  3.791   0.50 12.72  ? 10  HIS A CA  1 
ATOM   86   C  C   A HIS A 1 10  ? -21.957 -5.928  4.097   0.50 11.45  ? 10  HIS A C   1 
ATOM   87   C  C   B HIS A 1 10  ? -22.057 -5.526  3.840   0.50 17.18  ? 10  HIS A C   1 
ATOM   88   O  O   A HIS A 1 10  ? -22.974 -5.222  3.887   0.50 11.39  ? 10  HIS A O   1 
ATOM   89   O  O   B HIS A 1 10  ? -22.707 -4.482  3.649   0.50 15.69  ? 10  HIS A O   1 
ATOM   90   C  CB  A HIS A 1 10  ? -23.424 -7.563  5.265   0.50 12.67  ? 10  HIS A CB  1 
ATOM   91   C  CB  B HIS A 1 10  ? -23.864 -6.945  4.889   0.50 11.31  ? 10  HIS A CB  1 
ATOM   92   C  CG  A HIS A 1 10  ? -23.721 -8.982  5.711   0.50 12.16  ? 10  HIS A CG  1 
ATOM   93   C  CG  B HIS A 1 10  ? -24.469 -8.300  5.038   0.50 12.03  ? 10  HIS A CG  1 
ATOM   94   N  ND1 A HIS A 1 10  ? -24.707 -9.718  5.169   0.50 12.16  ? 10  HIS A ND1 1 
ATOM   95   N  ND1 B HIS A 1 10  ? -25.496 -8.707  4.267   0.50 14.76  ? 10  HIS A ND1 1 
ATOM   96   C  CD2 A HIS A 1 10  ? -23.132 -9.775  6.697   0.50 14.83  ? 10  HIS A CD2 1 
ATOM   97   C  CD2 B HIS A 1 10  ? -24.133 -9.373  5.843   0.50 15.25  ? 10  HIS A CD2 1 
ATOM   98   C  CE1 A HIS A 1 10  ? -24.746 -10.927 5.765   0.50 14.08  ? 10  HIS A CE1 1 
ATOM   99   C  CE1 B HIS A 1 10  ? -25.841 -9.940  4.608   0.50 14.80  ? 10  HIS A CE1 1 
ATOM   100  N  NE2 A HIS A 1 10  ? -23.781 -10.959 6.699   0.50 15.15  ? 10  HIS A NE2 1 
ATOM   101  N  NE2 B HIS A 1 10  ? -24.991 -10.372 5.544   0.50 15.35  ? 10  HIS A NE2 1 
ATOM   102  N  N   . ASN A 1 11  ? -20.723 -5.470  4.046   1.00 19.47  ? 11  ASN A N   1 
ATOM   103  C  CA  . ASN A 1 11  ? -20.261 -4.136  3.778   1.00 17.58  ? 11  ASN A CA  1 
ATOM   104  C  C   . ASN A 1 11  ? -18.946 -4.104  2.986   1.00 16.47  ? 11  ASN A C   1 
ATOM   105  O  O   . ASN A 1 11  ? -18.280 -3.103  2.952   1.00 16.91  ? 11  ASN A O   1 
ATOM   106  C  CB  . ASN A 1 11  ? -20.041 -3.359  5.093   1.00 17.89  ? 11  ASN A CB  1 
ATOM   107  C  CG  . ASN A 1 11  ? -18.972 -3.937  6.007   1.00 18.14  ? 11  ASN A CG  1 
ATOM   108  O  OD1 . ASN A 1 11  ? -18.406 -4.992  5.712   1.00 20.73  ? 11  ASN A OD1 1 
ATOM   109  N  ND2 . ASN A 1 11  ? -18.699 -3.272  7.104   1.00 19.88  ? 11  ASN A ND2 1 
ATOM   110  N  N   . GLY A 1 12  ? -18.574 -5.225  2.373   1.00 16.62  ? 12  GLY A N   1 
ATOM   111  C  CA  . GLY A 1 12  ? -17.299 -5.342  1.699   1.00 15.89  ? 12  GLY A CA  1 
ATOM   112  C  C   . GLY A 1 12  ? -17.269 -4.807  0.330   1.00 14.18  ? 12  GLY A C   1 
ATOM   113  O  O   . GLY A 1 12  ? -18.192 -4.112  -0.085  1.00 13.61  ? 12  GLY A O   1 
ATOM   114  N  N   . PRO A 1 13  ? -16.181 -5.077  -0.397  1.00 13.22  ? 13  PRO A N   1 
ATOM   115  C  CA  . PRO A 1 13  ? -15.897 -4.459  -1.700  1.00 13.57  ? 13  PRO A CA  1 
ATOM   116  C  C   . PRO A 1 13  ? -17.042 -4.520  -2.658  1.00 12.95  ? 13  PRO A C   1 
ATOM   117  O  O   . PRO A 1 13  ? -17.224 -3.535  -3.462  1.00 12.99  ? 13  PRO A O   1 
ATOM   118  C  CB  . PRO A 1 13  ? -14.713 -5.278  -2.169  1.00 13.55  ? 13  PRO A CB  1 
ATOM   119  C  CG  . PRO A 1 13  ? -13.944 -5.531  -0.940  1.00 13.56  ? 13  PRO A CG  1 
ATOM   120  C  CD  . PRO A 1 13  ? -15.006 -5.808  0.112   1.00 13.86  ? 13  PRO A CD  1 
ATOM   121  N  N   . GLU A 1 14  ? -17.839 -5.566  -2.673  1.00 13.89  ? 14  GLU A N   1 
ATOM   122  C  CA  . GLU A 1 14  ? -18.936 -5.656  -3.588  1.00 16.47  ? 14  GLU A CA  1 
ATOM   123  C  C   . GLU A 1 14  ? -20.066 -4.654  -3.314  1.00 14.96  ? 14  GLU A C   1 
ATOM   124  O  O   . GLU A 1 14  ? -20.910 -4.436  -4.184  1.00 16.49  ? 14  GLU A O   1 
ATOM   125  C  CB  . GLU A 1 14  ? -19.432 -7.092  -3.688  1.00 20.70  ? 14  GLU A CB  1 
ATOM   126  C  CG  . GLU A 1 14  ? -20.010 -7.693  -2.390  1.00 21.19  ? 14  GLU A CG  1 
ATOM   127  C  CD  . GLU A 1 14  ? -19.202 -8.173  -1.169  1.00 23.00  ? 14  GLU A CD  1 
ATOM   128  O  OE1 . GLU A 1 14  ? -18.036 -7.748  -1.025  1.00 20.49  ? 14  GLU A OE1 1 
ATOM   129  O  OE2 . GLU A 1 14  ? -19.742 -8.974  -0.377  1.00 26.83  ? 14  GLU A OE2 1 
ATOM   130  N  N   . HIS A 1 15  ? -20.095 -4.051  -2.142  1.00 13.56  ? 15  HIS A N   1 
ATOM   131  C  CA  . HIS A 1 15  ? -21.108 -3.051  -1.762  1.00 13.70  ? 15  HIS A CA  1 
ATOM   132  C  C   . HIS A 1 15  ? -20.683 -1.616  -1.933  1.00 13.66  ? 15  HIS A C   1 
ATOM   133  O  O   . HIS A 1 15  ? -21.491 -0.707  -1.887  1.00 14.58  ? 15  HIS A O   1 
ATOM   134  C  CB  . HIS A 1 15  ? -21.497 -3.250  -0.300  1.00 15.06  ? 15  HIS A CB  1 
ATOM   135  C  CG  . HIS A 1 15  ? -22.184 -4.540  -0.068  1.00 15.88  ? 15  HIS A CG  1 
ATOM   136  N  ND1 . HIS A 1 15  ? -23.561 -4.690  -0.222  1.00 18.23  ? 15  HIS A ND1 1 
ATOM   137  C  CD2 . HIS A 1 15  ? -21.688 -5.764  0.277   1.00 19.83  ? 15  HIS A CD2 1 
ATOM   138  C  CE1 . HIS A 1 15  ? -23.877 -5.944  0.028   1.00 25.19  ? 15  HIS A CE1 1 
ATOM   139  N  NE2 . HIS A 1 15  ? -22.769 -6.624  0.324   1.00 22.14  ? 15  HIS A NE2 1 
ATOM   140  N  N   . TRP A 1 16  ? -19.375 -1.393  -2.086  1.00 12.49  ? 16  TRP A N   1 
ATOM   141  C  CA  . TRP A 1 16  ? -18.850 -0.036  -1.982  1.00 11.77  ? 16  TRP A CA  1 
ATOM   142  C  C   . TRP A 1 16  ? -19.387 0.920   -3.007  1.00 11.69  ? 16  TRP A C   1 
ATOM   143  O  O   . TRP A 1 16  ? -19.509 2.119   -2.742  1.00 12.69  ? 16  TRP A O   1 
ATOM   144  C  CB  . TRP A 1 16  ? -17.311 -0.067  -2.088  1.00 11.65  ? 16  TRP A CB  1 
ATOM   145  C  CG  . TRP A 1 16  ? -16.616 -0.774  -0.938  1.00 10.42  ? 16  TRP A CG  1 
ATOM   146  C  CD1 . TRP A 1 16  ? -17.144 -1.214  0.255   1.00 11.49  ? 16  TRP A CD1 1 
ATOM   147  C  CD2 . TRP A 1 16  ? -15.217 -1.077  -0.894  1.00 10.77  ? 16  TRP A CD2 1 
ATOM   148  N  NE1 . TRP A 1 16  ? -16.149 -1.800  1.011   1.00 11.48  ? 16  TRP A NE1 1 
ATOM   149  C  CE2 . TRP A 1 16  ? -14.961 -1.724  0.394   1.00 10.71  ? 16  TRP A CE2 1 
ATOM   150  C  CE3 . TRP A 1 16  ? -14.154 -0.881  -1.796  1.00 10.50  ? 16  TRP A CE3 1 
ATOM   151  C  CZ2 . TRP A 1 16  ? -13.696 -2.137  0.763   1.00 10.01  ? 16  TRP A CZ2 1 
ATOM   152  C  CZ3 . TRP A 1 16  ? -12.906 -1.305  -1.405  1.00 10.44  ? 16  TRP A CZ3 1 
ATOM   153  C  CH2 . TRP A 1 16  ? -12.676 -1.907  -0.167  1.00 10.69  ? 16  TRP A CH2 1 
ATOM   154  N  N   . HIS A 1 17  ? -19.753 0.386   -4.141  1.00 12.30  ? 17  HIS A N   1 
ATOM   155  C  CA  . HIS A 1 17  ? -20.265 1.237   -5.205  1.00 13.05  ? 17  HIS A CA  1 
ATOM   156  C  C   . HIS A 1 17  ? -21.539 2.028   -4.861  1.00 14.41  ? 17  HIS A C   1 
ATOM   157  O  O   . HIS A 1 17  ? -21.826 3.090   -5.473  1.00 15.83  ? 17  HIS A O   1 
ATOM   158  C  CB  . HIS A 1 17  ? -20.549 0.488   -6.542  1.00 14.13  ? 17  HIS A CB  1 
ATOM   159  C  CG  . HIS A 1 17  ? -21.761 -0.400  -6.472  1.00 15.78  ? 17  HIS A CG  1 
ATOM   160  N  ND1 . HIS A 1 17  ? -22.961 -0.020  -6.970  1.00 18.31  ? 17  HIS A ND1 1 
ATOM   161  C  CD2 . HIS A 1 17  ? -21.936 -1.592  -5.829  1.00 18.34  ? 17  HIS A CD2 1 
ATOM   162  C  CE1 . HIS A 1 17  ? -23.848 -0.943  -6.678  1.00 17.72  ? 17  HIS A CE1 1 
ATOM   163  N  NE2 . HIS A 1 17  ? -23.251 -1.924  -6.019  1.00 17.52  ? 17  HIS A NE2 1 
ATOM   164  N  N   . LYS A 1 18  ? -22.323 1.523   -3.912  1.00 14.57  ? 18  LYS A N   1 
ATOM   165  C  CA  . LYS A 1 18  ? -23.557 2.229   -3.523  1.00 16.19  ? 18  LYS A CA  1 
ATOM   166  C  C   . LYS A 1 18  ? -23.226 3.589   -2.876  1.00 16.81  ? 18  LYS A C   1 
ATOM   167  O  O   . LYS A 1 18  ? -23.915 4.593   -3.110  1.00 23.33  ? 18  LYS A O   1 
ATOM   168  C  CB  . LYS A 1 18  ? -24.377 1.375   -2.599  1.00 17.07  ? 18  LYS A CB  1 
ATOM   169  C  CG  . LYS A 1 18  ? -24.977 0.166   -3.293  1.00 18.07  ? 18  LYS A CG  1 
ATOM   170  C  CD  . LYS A 1 18  ? -25.682 -0.794  -2.344  1.00 18.69  ? 18  LYS A CD  1 
ATOM   171  C  CE  . LYS A 1 18  ? -24.703 -1.809  -1.756  1.00 18.77  ? 18  LYS A CE  1 
ATOM   172  N  NZ  . LYS A 1 18  ? -25.350 -2.645  -0.698  1.00 18.78  ? 18  LYS A NZ  1 
ATOM   173  N  N   . ASP A 1 19  ? -22.213 3.636   -2.037  1.00 15.87  ? 19  ASP A N   1 
ATOM   174  C  CA  . ASP A 1 19  ? -21.821 4.938   -1.445  1.00 18.23  ? 19  ASP A CA  1 
ATOM   175  C  C   . ASP A 1 19  ? -20.767 5.684   -2.294  1.00 16.45  ? 19  ASP A C   1 
ATOM   176  O  O   . ASP A 1 19  ? -20.651 6.892   -2.212  1.00 17.80  ? 19  ASP A O   1 
ATOM   177  C  CB  . ASP A 1 19  ? -21.275 4.755   -0.020  1.00 20.18  ? 19  ASP A CB  1 
ATOM   178  C  CG  . ASP A 1 19  ? -22.338 4.768   1.044   1.00 28.79  ? 19  ASP A CG  1 
ATOM   179  O  OD1 . ASP A 1 19  ? -23.383 5.373   0.836   1.00 28.94  ? 19  ASP A OD1 1 
ATOM   180  O  OD2 . ASP A 1 19  ? -22.135 4.126   2.097   1.00 44.21  ? 19  ASP A OD2 1 
ATOM   181  N  N   . PHE A 1 20  ? -20.012 4.952   -3.096  1.00 14.23  ? 20  PHE A N   1 
ATOM   182  C  CA  . PHE A 1 20  ? -18.911 5.489   -3.834  1.00 13.88  ? 20  PHE A CA  1 
ATOM   183  C  C   . PHE A 1 20  ? -18.993 4.975   -5.283  1.00 13.25  ? 20  PHE A C   1 
ATOM   184  O  O   . PHE A 1 20  ? -18.356 4.005   -5.634  1.00 13.21  ? 20  PHE A O   1 
ATOM   185  C  CB  . PHE A 1 20  ? -17.574 5.066   -3.214  1.00 14.27  ? 20  PHE A CB  1 
ATOM   186  C  CG  . PHE A 1 20  ? -17.451 5.454   -1.780  1.00 15.03  ? 20  PHE A CG  1 
ATOM   187  C  CD1 . PHE A 1 20  ? -17.092 6.744   -1.426  1.00 16.33  ? 20  PHE A CD1 1 
ATOM   188  C  CD2 . PHE A 1 20  ? -17.839 4.527   -0.772  1.00 17.79  ? 20  PHE A CD2 1 
ATOM   189  C  CE1 . PHE A 1 20  ? -17.121 7.119   -0.075  1.00 19.23  ? 20  PHE A CE1 1 
ATOM   190  C  CE2 . PHE A 1 20  ? -17.884 4.908   0.569   1.00 20.48  ? 20  PHE A CE2 1 
ATOM   191  C  CZ  . PHE A 1 20  ? -17.466 6.180   0.900   1.00 19.61  ? 20  PHE A CZ  1 
ATOM   192  N  N   . PRO A 1 21  ? -19.875 5.588   -6.092  1.00 13.98  ? 21  PRO A N   1 
ATOM   193  C  CA  . PRO A 1 21  ? -20.105 5.055   -7.428  1.00 15.00  ? 21  PRO A CA  1 
ATOM   194  C  C   . PRO A 1 21  ? -18.877 4.974   -8.357  1.00 14.30  ? 21  PRO A C   1 
ATOM   195  O  O   . PRO A 1 21  ? -18.889 4.195   -9.299  1.00 14.72  ? 21  PRO A O   1 
ATOM   196  C  CB  . PRO A 1 21  ? -21.214 5.993   -8.019  1.00 20.52  ? 21  PRO A CB  1 
ATOM   197  C  CG  . PRO A 1 21  ? -21.773 6.672   -6.867  1.00 25.97  ? 21  PRO A CG  1 
ATOM   198  C  CD  . PRO A 1 21  ? -20.798 6.683   -5.749  1.00 18.25  ? 21  PRO A CD  1 
ATOM   199  N  N   A ILE A 1 22  ? -17.839 5.819   -8.258  0.50 12.67  ? 22  ILE A N   1 
ATOM   200  N  N   B ILE A 1 22  ? -17.824 5.692   -7.940  0.50 11.31  ? 22  ILE A N   1 
ATOM   201  C  CA  A ILE A 1 22  ? -16.572 5.597   -9.036  0.50 11.26  ? 22  ILE A CA  1 
ATOM   202  C  CA  B ILE A 1 22  ? -16.552 5.678   -8.641  0.50 11.26  ? 22  ILE A CA  1 
ATOM   203  C  C   A ILE A 1 22  ? -15.993 4.180   -8.812  0.50 11.19  ? 22  ILE A C   1 
ATOM   204  C  C   B ILE A 1 22  ? -15.923 4.298   -8.573  0.50 10.92  ? 22  ILE A C   1 
ATOM   205  O  O   A ILE A 1 22  ? -15.115 3.787   -9.633  0.50 9.72   ? 22  ILE A O   1 
ATOM   206  O  O   B ILE A 1 22  ? -15.001 4.011   -9.280  0.50 10.41  ? 22  ILE A O   1 
ATOM   207  C  CB  A ILE A 1 22  ? -15.531 6.694   -8.642  0.50 11.99  ? 22  ILE A CB  1 
ATOM   208  C  CB  B ILE A 1 22  ? -15.605 6.779   -8.107  0.50 9.66   ? 22  ILE A CB  1 
ATOM   209  C  CG1 A ILE A 1 22  ? -14.399 6.929   -9.656  0.50 13.78  ? 22  ILE A CG1 1 
ATOM   210  C  CG1 B ILE A 1 22  ? -14.550 7.091   -9.172  0.50 10.41  ? 22  ILE A CG1 1 
ATOM   211  C  CG2 A ILE A 1 22  ? -14.920 6.383   -7.292  0.50 11.07  ? 22  ILE A CG2 1 
ATOM   212  C  CG2 B ILE A 1 22  ? -14.998 6.404   -6.767  0.50 9.77   ? 22  ILE A CG2 1 
ATOM   213  C  CD1 A ILE A 1 22  ? -14.859 7.633   -10.885 0.50 19.58  ? 22  ILE A CD1 1 
ATOM   214  C  CD1 B ILE A 1 22  ? -13.590 8.197   -8.906  0.50 12.76  ? 22  ILE A CD1 1 
ATOM   215  N  N   . ALA A 1 23  ? -16.488 3.413   -7.769  1.00 11.02  ? 23  ALA A N   1 
ATOM   216  C  CA  . ALA A 1 23  ? -16.016 2.022   -7.626  1.00 10.94  ? 23  ALA A CA  1 
ATOM   217  C  C   . ALA A 1 23  ? -16.117 1.301   -8.955  1.00 11.67  ? 23  ALA A C   1 
ATOM   218  O  O   . ALA A 1 23  ? -15.407 0.289   -9.150  1.00 11.68  ? 23  ALA A O   1 
ATOM   219  C  CB  . ALA A 1 23  ? -16.874 1.278   -6.622  1.00 11.28  ? 23  ALA A CB  1 
ATOM   220  N  N   . LYS A 1 24  ? -17.046 1.718   -9.839  1.00 12.29  ? 24  LYS A N   1 
ATOM   221  C  CA  . LYS A 1 24  ? -17.214 1.118   -11.145 1.00 12.46  ? 24  LYS A CA  1 
ATOM   222  C  C   . LYS A 1 24  ? -16.580 2.012   -12.248 1.00 13.57  ? 24  LYS A C   1 
ATOM   223  O  O   . LYS A 1 24  ? -16.993 1.897   -13.389 1.00 15.48  ? 24  LYS A O   1 
ATOM   224  C  CB  . LYS A 1 24  ? -18.695 0.832   -11.458 1.00 14.72  ? 24  LYS A CB  1 
ATOM   225  C  CG  . LYS A 1 24  ? -19.348 -0.146  -10.472 1.00 15.60  ? 24  LYS A CG  1 
ATOM   226  C  CD  . LYS A 1 24  ? -20.811 -0.374  -10.810 1.00 20.61  ? 24  LYS A CD  1 
ATOM   227  C  CE  . LYS A 1 24  ? -21.494 -1.427  -9.940  1.00 22.93  ? 24  LYS A CE  1 
ATOM   228  N  NZ  . LYS A 1 24  ? -21.076 -2.758  -10.381 1.00 31.51  ? 24  LYS A NZ  1 
ATOM   229  N  N   . GLY A 1 25  ? -15.603 2.817   -11.899 1.00 12.61  ? 25  GLY A N   1 
ATOM   230  C  CA  . GLY A 1 25  ? -15.012 3.780   -12.820 1.00 14.68  ? 25  GLY A CA  1 
ATOM   231  C  C   . GLY A 1 25  ? -14.017 3.166   -13.774 1.00 12.92  ? 25  GLY A C   1 
ATOM   232  O  O   . GLY A 1 25  ? -13.834 1.932   -13.874 1.00 13.64  ? 25  GLY A O   1 
ATOM   233  N  N   . GLU A 1 26  ? -13.378 4.048   -14.510 1.00 13.59  ? 26  GLU A N   1 
ATOM   234  C  CA  . GLU A 1 26  ? -12.506 3.670   -15.599 1.00 14.26  ? 26  GLU A CA  1 
ATOM   235  C  C   . GLU A 1 26  ? -11.068 3.412   -15.204 1.00 12.20  ? 26  GLU A C   1 
ATOM   236  O  O   . GLU A 1 26  ? -10.315 2.945   -16.040 1.00 14.17  ? 26  GLU A O   1 
ATOM   237  C  CB  . GLU A 1 26  ? -12.540 4.773   -16.682 1.00 17.87  ? 26  GLU A CB  1 
ATOM   238  C  CG  . GLU A 1 26  ? -13.960 4.989   -17.230 1.00 19.62  ? 26  GLU A CG  1 
ATOM   239  C  CD  . GLU A 1 26  ? -14.550 3.710   -17.866 1.00 29.80  ? 26  GLU A CD  1 
ATOM   240  O  OE1 . GLU A 1 26  ? -13.848 3.082   -18.700 1.00 29.03  ? 26  GLU A OE1 1 
ATOM   241  O  OE2 . GLU A 1 26  ? -15.686 3.323   -17.483 1.00 39.24  ? 26  GLU A OE2 1 
ATOM   242  N  N   . ARG A 1 27  ? -10.639 3.718   -13.980 1.00 10.30  ? 27  ARG A N   1 
ATOM   243  C  CA  . ARG A 1 27  ? -9.265  3.529   -13.600 1.00 8.81   ? 27  ARG A CA  1 
ATOM   244  C  C   . ARG A 1 27  ? -9.179  3.078   -12.171 1.00 8.39   ? 27  ARG A C   1 
ATOM   245  O  O   . ARG A 1 27  ? -8.451  3.662   -11.339 1.00 8.53   ? 27  ARG A O   1 
ATOM   246  C  CB  . ARG A 1 27  ? -8.359  4.743   -13.929 1.00 12.50  ? 27  ARG A CB  1 
ATOM   247  C  CG  . ARG A 1 27  ? -8.705  6.076   -13.354 1.00 13.66  ? 27  ARG A CG  1 
ATOM   248  C  CD  . ARG A 1 27  ? -7.698  7.208   -13.511 1.00 15.25  ? 27  ARG A CD  1 
ATOM   249  N  NE  . ARG A 1 27  ? -6.551  7.100   -12.617 1.00 14.15  ? 27  ARG A NE  1 
ATOM   250  C  CZ  . ARG A 1 27  ? -5.627  8.046   -12.490 1.00 12.06  ? 27  ARG A CZ  1 
ATOM   251  N  NH1 . ARG A 1 27  ? -5.724  9.162   -13.201 1.00 16.20  ? 27  ARG A NH1 1 
ATOM   252  N  NH2 . ARG A 1 27  ? -4.608  7.880   -11.657 1.00 13.70  ? 27  ARG A NH2 1 
ATOM   253  N  N   . GLN A 1 28  ? -9.926  2.024   -11.877 1.00 8.17   ? 28  GLN A N   1 
ATOM   254  C  CA  . GLN A 1 28  ? -9.955  1.470   -10.490 1.00 8.05   ? 28  GLN A CA  1 
ATOM   255  C  C   . GLN A 1 28  ? -8.798  0.500   -10.249 1.00 7.63   ? 28  GLN A C   1 
ATOM   256  O  O   . GLN A 1 28  ? -8.299  -0.190  -11.144 1.00 8.11   ? 28  GLN A O   1 
ATOM   257  C  CB  . GLN A 1 28  ? -11.296 0.808   -10.247 1.00 8.59   ? 28  GLN A CB  1 
ATOM   258  C  CG  . GLN A 1 28  ? -12.441 1.848   -10.134 1.00 9.12   ? 28  GLN A CG  1 
ATOM   259  C  CD  . GLN A 1 28  ? -12.298 2.660   -8.851  1.00 9.04   ? 28  GLN A CD  1 
ATOM   260  O  OE1 . GLN A 1 28  ? -12.476 2.091   -7.763  1.00 8.66   ? 28  GLN A OE1 1 
ATOM   261  N  NE2 . GLN A 1 28  ? -11.970 3.940   -8.953  1.00 8.72   ? 28  GLN A NE2 1 
ATOM   262  N  N   . SER A 1 29  ? -8.402  0.416   -8.965  1.00 7.17   ? 29  SER A N   1 
ATOM   263  C  CA  . SER A 1 29  ? -7.372  -0.467  -8.487  1.00 6.66   ? 29  SER A CA  1 
ATOM   264  C  C   . SER A 1 29  ? -7.887  -1.344  -7.377  1.00 6.31   ? 29  SER A C   1 
ATOM   265  O  O   . SER A 1 29  ? -8.845  -0.979  -6.685  1.00 7.29   ? 29  SER A O   1 
ATOM   266  C  CB  . SER A 1 29  ? -6.220  0.413   -7.960  1.00 6.53   ? 29  SER A CB  1 
ATOM   267  O  OG  . SER A 1 29  ? -5.595  1.134   -9.008  1.00 7.06   ? 29  SER A OG  1 
ATOM   268  N  N   . PRO A 1 30  ? -7.238  -2.481  -7.111  1.00 6.23   ? 30  PRO A N   1 
ATOM   269  C  CA  . PRO A 1 30  ? -6.071  -3.022  -7.828  1.00 6.18   ? 30  PRO A CA  1 
ATOM   270  C  C   . PRO A 1 30  ? -6.469  -3.677  -9.133  1.00 6.48   ? 30  PRO A C   1 
ATOM   271  O  O   . PRO A 1 30  ? -7.659  -3.718  -9.476  1.00 7.33   ? 30  PRO A O   1 
ATOM   272  C  CB  . PRO A 1 30  ? -5.536  -4.039  -6.831  1.00 6.57   ? 30  PRO A CB  1 
ATOM   273  C  CG  . PRO A 1 30  ? -6.808  -4.611  -6.238  1.00 7.34   ? 30  PRO A CG  1 
ATOM   274  C  CD  . PRO A 1 30  ? -7.720  -3.409  -6.066  1.00 7.02   ? 30  PRO A CD  1 
ATOM   275  N  N   . VAL A 1 31  ? -5.471  -4.232  -9.834  1.00 7.22   ? 31  VAL A N   1 
ATOM   276  C  CA  . VAL A 1 31  ? -5.670  -4.975  -11.057 1.00 7.39   ? 31  VAL A CA  1 
ATOM   277  C  C   . VAL A 1 31  ? -4.780  -6.193  -11.005 1.00 7.42   ? 31  VAL A C   1 
ATOM   278  O  O   . VAL A 1 31  ? -3.799  -6.262  -10.242 1.00 7.97   ? 31  VAL A O   1 
ATOM   279  C  CB  . VAL A 1 31  ? -5.331  -4.129  -12.312 1.00 8.49   ? 31  VAL A CB  1 
ATOM   280  C  CG1 . VAL A 1 31  ? -6.276  -2.950  -12.422 1.00 8.88   ? 31  VAL A CG1 1 
ATOM   281  C  CG2 . VAL A 1 31  ? -3.874  -3.726  -12.383 1.00 8.82   ? 31  VAL A CG2 1 
ATOM   282  N  N   . ASP A 1 32  ? -5.124  -7.200  -11.857 1.00 7.65   ? 32  ASP A N   1 
ATOM   283  C  CA  . ASP A 1 32  ? -4.216  -8.281  -12.143 1.00 8.01   ? 32  ASP A CA  1 
ATOM   284  C  C   . ASP A 1 32  ? -3.165  -7.771  -13.125 1.00 7.93   ? 32  ASP A C   1 
ATOM   285  O  O   . ASP A 1 32  ? -3.461  -7.107  -14.150 1.00 10.00  ? 32  ASP A O   1 
ATOM   286  C  CB  . ASP A 1 32  ? -4.957  -9.457  -12.772 1.00 8.92   ? 32  ASP A CB  1 
ATOM   287  C  CG  . ASP A 1 32  ? -4.020  -10.627 -13.031 1.00 9.51   ? 32  ASP A CG  1 
ATOM   288  O  OD1 . ASP A 1 32  ? -3.308  -11.081 -12.111 1.00 9.19   ? 32  ASP A OD1 1 
ATOM   289  O  OD2 . ASP A 1 32  ? -3.949  -11.047 -14.214 1.00 12.32  ? 32  ASP A OD2 1 
ATOM   290  N  N   . ILE A 1 33  ? -1.898  -8.058  -12.821 1.00 7.62   ? 33  ILE A N   1 
ATOM   291  C  CA  . ILE A 1 33  ? -0.744  -7.703  -13.685 1.00 8.54   ? 33  ILE A CA  1 
ATOM   292  C  C   . ILE A 1 33  ? -0.494  -8.939  -14.528 1.00 9.27   ? 33  ILE A C   1 
ATOM   293  O  O   . ILE A 1 33  ? 0.051   -9.924  -14.046 1.00 9.89   ? 33  ILE A O   1 
ATOM   294  C  CB  . ILE A 1 33  ? 0.433   -7.260  -12.839 1.00 8.85   ? 33  ILE A CB  1 
ATOM   295  C  CG1 . ILE A 1 33  ? 0.051   -6.053  -11.981 1.00 9.61   ? 33  ILE A CG1 1 
ATOM   296  C  CG2 . ILE A 1 33  ? 1.629   -7.004  -13.798 1.00 11.15  ? 33  ILE A CG2 1 
ATOM   297  C  CD1 . ILE A 1 33  ? 1.103   -5.754  -10.888 1.00 10.85  ? 33  ILE A CD1 1 
ATOM   298  N  N   A ASP A 1 34  ? -0.904  -8.894  -15.790 0.50 10.88  ? 34  ASP A N   1 
ATOM   299  N  N   B ASP A 1 34  ? -0.810  -8.848  -15.802 0.50 10.53  ? 34  ASP A N   1 
ATOM   300  C  CA  A ASP A 1 34  ? -0.610  -9.946  -16.780 0.50 11.54  ? 34  ASP A CA  1 
ATOM   301  C  CA  B ASP A 1 34  ? -0.528  -9.926  -16.722 0.50 11.66  ? 34  ASP A CA  1 
ATOM   302  C  C   A ASP A 1 34  ? 0.828   -9.663  -17.263 0.50 12.90  ? 34  ASP A C   1 
ATOM   303  C  C   B ASP A 1 34  ? 0.881   -9.641  -17.263 0.50 12.89  ? 34  ASP A C   1 
ATOM   304  O  O   A ASP A 1 34  ? 1.033   -8.698  -18.009 0.50 14.76  ? 34  ASP A O   1 
ATOM   305  O  O   B ASP A 1 34  ? 1.138   -8.685  -18.003 0.50 15.94  ? 34  ASP A O   1 
ATOM   306  C  CB  A ASP A 1 34  ? -1.616  -9.846  -17.943 0.50 12.70  ? 34  ASP A CB  1 
ATOM   307  C  CB  B ASP A 1 34  ? -1.638  -10.037 -17.766 0.50 14.92  ? 34  ASP A CB  1 
ATOM   308  C  CG  A ASP A 1 34  ? -1.361  -10.864 -19.052 0.50 13.66  ? 34  ASP A CG  1 
ATOM   309  C  CG  B ASP A 1 34  ? -1.483  -11.258 -18.631 0.50 18.37  ? 34  ASP A CG  1 
ATOM   310  O  OD1 A ASP A 1 34  ? -0.171  -11.268 -19.223 0.50 13.85  ? 34  ASP A OD1 1 
ATOM   311  O  OD1 B ASP A 1 34  ? -1.864  -12.346 -18.223 0.50 20.07  ? 34  ASP A OD1 1 
ATOM   312  O  OD2 A ASP A 1 34  ? -2.370  -11.208 -19.735 0.50 17.81  ? 34  ASP A OD2 1 
ATOM   313  O  OD2 B ASP A 1 34  ? -0.965  -11.133 -19.747 0.50 20.64  ? 34  ASP A OD2 1 
ATOM   314  N  N   . THR A 1 35  ? 1.834   -10.429 -16.796 1.00 13.83  ? 35  THR A N   1 
ATOM   315  C  CA  . THR A 1 35  ? 3.228   -10.129 -17.011 1.00 13.81  ? 35  THR A CA  1 
ATOM   316  C  C   . THR A 1 35  ? 3.638   -10.276 -18.437 1.00 13.71  ? 35  THR A C   1 
ATOM   317  O  O   . THR A 1 35  ? 4.544   -9.564  -18.895 1.00 17.20  ? 35  THR A O   1 
ATOM   318  C  CB  . THR A 1 35  ? 4.111   -11.011 -16.183 1.00 15.49  ? 35  THR A CB  1 
ATOM   319  O  OG1 . THR A 1 35  ? 3.974   -12.340 -16.670 1.00 16.24  ? 35  THR A OG1 1 
ATOM   320  C  CG2 . THR A 1 35  ? 3.853   -10.895 -14.716 1.00 18.07  ? 35  THR A CG2 1 
ATOM   321  N  N   . HIS A 1 36  ? 2.961   -11.132 -19.186 1.00 15.21  ? 36  HIS A N   1 
ATOM   322  C  CA  . HIS A 1 36  ? 3.233   -11.295 -20.599 1.00 16.28  ? 36  HIS A CA  1 
ATOM   323  C  C   . HIS A 1 36  ? 2.753   -10.148 -21.445 1.00 17.51  ? 36  HIS A C   1 
ATOM   324  O  O   . HIS A 1 36  ? 3.426   -9.827  -22.458 1.00 19.45  ? 36  HIS A O   1 
ATOM   325  C  CB  . HIS A 1 36  ? 2.741   -12.718 -20.998 1.00 18.96  ? 36  HIS A CB  1 
ATOM   326  C  CG  . HIS A 1 36  ? 3.652   -13.813 -20.450 1.00 18.59  ? 36  HIS A CG  1 
ATOM   327  N  ND1 . HIS A 1 36  ? 4.986   -13.922 -20.847 1.00 20.69  ? 36  HIS A ND1 1 
ATOM   328  C  CD2 . HIS A 1 36  ? 3.454   -14.770 -19.429 1.00 21.24  ? 36  HIS A CD2 1 
ATOM   329  C  CE1 . HIS A 1 36  ? 5.573   -14.950 -20.158 1.00 23.77  ? 36  HIS A CE1 1 
ATOM   330  N  NE2 . HIS A 1 36  ? 4.636   -15.464 -19.291 1.00 27.91  ? 36  HIS A NE2 1 
ATOM   331  N  N   . THR A 1 37  ? 1.651   -9.496  -21.008 1.00 17.56  ? 37  THR A N   1 
ATOM   332  C  CA  . THR A 1 37  ? 1.050   -8.393  -21.739 1.00 16.30  ? 37  THR A CA  1 
ATOM   333  C  C   . THR A 1 37  ? 1.618   -6.989  -21.356 1.00 16.73  ? 37  THR A C   1 
ATOM   334  O  O   . THR A 1 37  ? 1.423   -5.993  -22.084 1.00 21.75  ? 37  THR A O   1 
ATOM   335  C  CB  . THR A 1 37  ? -0.468  -8.398  -21.498 1.00 25.83  ? 37  THR A CB  1 
ATOM   336  O  OG1 . THR A 1 37  ? -0.901  -9.566  -22.127 1.00 29.03  ? 37  THR A OG1 1 
ATOM   337  C  CG2 . THR A 1 37  ? -1.184  -7.257  -22.198 1.00 22.84  ? 37  THR A CG2 1 
ATOM   338  N  N   . ALA A 1 38  ? 2.247   -6.917  -20.182 1.00 14.91  ? 38  ALA A N   1 
ATOM   339  C  CA  . ALA A 1 38  ? 2.840   -5.646  -19.778 1.00 14.55  ? 38  ALA A CA  1 
ATOM   340  C  C   . ALA A 1 38  ? 3.927   -5.309  -20.733 1.00 16.70  ? 38  ALA A C   1 
ATOM   341  O  O   . ALA A 1 38  ? 4.600   -6.158  -21.203 1.00 22.12  ? 38  ALA A O   1 
ATOM   342  C  CB  . ALA A 1 38  ? 3.348   -5.767  -18.357 1.00 14.66  ? 38  ALA A CB  1 
ATOM   343  N  N   . LYS A 1 39  ? 4.009   -4.068  -21.136 1.00 16.67  ? 39  LYS A N   1 
ATOM   344  C  CA  . LYS A 1 39  ? 4.984   -3.680  -22.160 1.00 20.80  ? 39  LYS A CA  1 
ATOM   345  C  C   . LYS A 1 39  ? 6.219   -3.077  -21.513 1.00 15.04  ? 39  LYS A C   1 
ATOM   346  O  O   . LYS A 1 39  ? 6.126   -2.107  -20.768 1.00 13.80  ? 39  LYS A O   1 
ATOM   347  C  CB  . LYS A 1 39  ? 4.398   -2.694  -23.095 1.00 30.76  ? 39  LYS A CB  1 
ATOM   348  C  CG  . LYS A 1 39  ? 5.287   -2.528  -24.337 1.00 47.19  ? 39  LYS A CG  1 
ATOM   349  C  CD  . LYS A 1 39  ? 4.791   -1.566  -25.399 1.00 46.51  ? 39  LYS A CD  1 
ATOM   350  C  CE  . LYS A 1 39  ? 5.926   -1.196  -26.344 1.00 52.58  ? 39  LYS A CE  1 
ATOM   351  N  NZ  . LYS A 1 39  ? 6.134   -2.271  -27.352 1.00 79.44  ? 39  LYS A NZ  1 
ATOM   352  N  N   . TYR A 1 40  ? 7.391   -3.601  -21.879 1.00 18.25  ? 40  TYR A N   1 
ATOM   353  C  CA  . TYR A 1 40  ? 8.649   -2.986  -21.482 1.00 14.81  ? 40  TYR A CA  1 
ATOM   354  C  C   . TYR A 1 40  ? 8.706   -1.595  -22.070 1.00 13.75  ? 40  TYR A C   1 
ATOM   355  O  O   . TYR A 1 40  ? 8.547   -1.404  -23.330 1.00 16.77  ? 40  TYR A O   1 
ATOM   356  C  CB  . TYR A 1 40  ? 9.864   -3.819  -21.908 1.00 20.81  ? 40  TYR A CB  1 
ATOM   357  C  CG  . TYR A 1 40  ? 11.175  -3.058  -21.760 1.00 20.75  ? 40  TYR A CG  1 
ATOM   358  C  CD1 . TYR A 1 40  ? 11.604  -2.630  -20.517 1.00 21.24  ? 40  TYR A CD1 1 
ATOM   359  C  CD2 . TYR A 1 40  ? 12.022  -2.808  -22.837 1.00 25.58  ? 40  TYR A CD2 1 
ATOM   360  C  CE1 . TYR A 1 40  ? 12.804  -1.959  -20.340 1.00 22.46  ? 40  TYR A CE1 1 
ATOM   361  C  CE2 . TYR A 1 40  ? 13.228  -2.099  -22.655 1.00 26.56  ? 40  TYR A CE2 1 
ATOM   362  C  CZ  . TYR A 1 40  ? 13.618  -1.702  -21.409 1.00 27.27  ? 40  TYR A CZ  1 
ATOM   363  O  OH  . TYR A 1 40  ? 14.795  -1.016  -21.227 1.00 33.03  ? 40  TYR A OH  1 
ATOM   364  N  N   . ASP A 1 41  ? 8.963   -0.615  -21.251 1.00 13.40  ? 41  ASP A N   1 
ATOM   365  C  CA  . ASP A 1 41  ? 9.058   0.777   -21.730 1.00 14.15  ? 41  ASP A CA  1 
ATOM   366  C  C   . ASP A 1 41  ? 10.468  1.269   -21.453 1.00 15.45  ? 41  ASP A C   1 
ATOM   367  O  O   . ASP A 1 41  ? 10.787  1.625   -20.325 1.00 16.31  ? 41  ASP A O   1 
ATOM   368  C  CB  . ASP A 1 41  ? 8.005   1.651   -21.051 1.00 17.39  ? 41  ASP A CB  1 
ATOM   369  C  CG  . ASP A 1 41  ? 8.011   3.074   -21.561 1.00 20.95  ? 41  ASP A CG  1 
ATOM   370  O  OD1 . ASP A 1 41  ? 8.907   3.398   -22.362 1.00 20.88  ? 41  ASP A OD1 1 
ATOM   371  O  OD2 . ASP A 1 41  ? 7.098   3.888   -21.251 1.00 26.27  ? 41  ASP A OD2 1 
ATOM   372  N  N   . PRO A 1 42  ? 11.288  1.351   -22.507 1.00 19.48  ? 42  PRO A N   1 
ATOM   373  C  CA  . PRO A 1 42  ? 12.673  1.794   -22.296 1.00 23.57  ? 42  PRO A CA  1 
ATOM   374  C  C   . PRO A 1 42  ? 12.766  3.287   -21.890 1.00 23.62  ? 42  PRO A C   1 
ATOM   375  O  O   . PRO A 1 42  ? 13.810  3.762   -21.409 1.00 32.28  ? 42  PRO A O   1 
ATOM   376  C  CB  . PRO A 1 42  ? 13.347  1.486   -23.645 1.00 30.77  ? 42  PRO A CB  1 
ATOM   377  C  CG  . PRO A 1 42  ? 12.223  1.606   -24.613 1.00 26.75  ? 42  PRO A CG  1 
ATOM   378  C  CD  . PRO A 1 42  ? 11.052  0.971   -23.930 1.00 22.88  ? 42  PRO A CD  1 
ATOM   379  N  N   . SER A 1 43  ? 11.677  4.025   -22.033 1.00 21.16  ? 43  SER A N   1 
ATOM   380  C  CA  . SER A 1 43  ? 11.612  5.448   -21.601 1.00 25.00  ? 43  SER A CA  1 
ATOM   381  C  C   . SER A 1 43  ? 11.418  5.572   -20.053 1.00 21.56  ? 43  SER A C   1 
ATOM   382  O  O   . SER A 1 43  ? 11.659  6.656   -19.475 1.00 27.96  ? 43  SER A O   1 
ATOM   383  C  CB  . SER A 1 43  ? 10.513  6.209   -22.384 1.00 24.64  ? 43  SER A CB  1 
ATOM   384  O  OG  . SER A 1 43  ? 9.198   5.996   -21.895 1.00 28.51  ? 43  SER A OG  1 
ATOM   385  N  N   . LEU A 1 44  ? 11.036  4.502   -19.367 1.00 23.79  ? 44  LEU A N   1 
ATOM   386  C  CA  . LEU A 1 44  ? 10.827  4.540   -17.892 1.00 19.35  ? 44  LEU A CA  1 
ATOM   387  C  C   . LEU A 1 44  ? 12.171  4.687   -17.233 1.00 18.24  ? 44  LEU A C   1 
ATOM   388  O  O   . LEU A 1 44  ? 13.162  4.172   -17.722 1.00 25.32  ? 44  LEU A O   1 
ATOM   389  C  CB  . LEU A 1 44  ? 10.102  3.317   -17.402 1.00 17.37  ? 44  LEU A CB  1 
ATOM   390  C  CG  . LEU A 1 44  ? 8.637   3.312   -17.661 1.00 15.25  ? 44  LEU A CG  1 
ATOM   391  C  CD1 . LEU A 1 44  ? 8.235   1.926   -17.242 1.00 18.53  ? 44  LEU A CD1 1 
ATOM   392  C  CD2 . LEU A 1 44  ? 7.900   4.408   -16.921 1.00 18.12  ? 44  LEU A CD2 1 
ATOM   393  N  N   . LYS A 1 45  ? 12.228  5.469   -16.152 1.00 18.71  ? 45  LYS A N   1 
ATOM   394  C  CA  . LYS A 1 45  ? 13.481  5.693   -15.435 1.00 20.10  ? 45  LYS A CA  1 
ATOM   395  C  C   . LYS A 1 45  ? 13.554  4.844   -14.215 1.00 17.64  ? 45  LYS A C   1 
ATOM   396  O  O   . LYS A 1 45  ? 12.544  4.349   -13.774 1.00 17.77  ? 45  LYS A O   1 
ATOM   397  C  CB  . LYS A 1 45  ? 13.622  7.107   -15.020 1.00 20.42  ? 45  LYS A CB  1 
ATOM   398  C  CG  . LYS A 1 45  ? 13.422  8.130   -16.117 1.00 25.57  ? 45  LYS A CG  1 
ATOM   399  C  CD  . LYS A 1 45  ? 13.917  9.507   -15.674 1.00 35.00  ? 45  LYS A CD  1 
ATOM   400  N  N   . PRO A 1 46  ? 14.797  4.591   -13.724 1.00 17.26  ? 46  PRO A N   1 
ATOM   401  C  CA  . PRO A 1 46  ? 14.903  3.925   -12.406 1.00 17.82  ? 46  PRO A CA  1 
ATOM   402  C  C   . PRO A 1 46  ? 14.087  4.701   -11.416 1.00 13.01  ? 46  PRO A C   1 
ATOM   403  O  O   . PRO A 1 46  ? 14.070  5.916   -11.496 1.00 15.34  ? 46  PRO A O   1 
ATOM   404  C  CB  . PRO A 1 46  ? 16.413  3.990   -12.100 1.00 19.29  ? 46  PRO A CB  1 
ATOM   405  C  CG  . PRO A 1 46  ? 17.104  4.133   -13.431 1.00 23.78  ? 46  PRO A CG  1 
ATOM   406  C  CD  . PRO A 1 46  ? 16.119  4.963   -14.244 1.00 22.17  ? 46  PRO A CD  1 
ATOM   407  N  N   . LEU A 1 47  ? 13.508  3.943   -10.499 1.00 16.79  ? 47  LEU A N   1 
ATOM   408  C  CA  . LEU A 1 47  ? 12.782  4.577   -9.422  1.00 14.22  ? 47  LEU A CA  1 
ATOM   409  C  C   . LEU A 1 47  ? 13.839  5.242   -8.516  1.00 17.89  ? 47  LEU A C   1 
ATOM   410  O  O   . LEU A 1 47  ? 14.849  4.621   -8.305  1.00 23.96  ? 47  LEU A O   1 
ATOM   411  C  CB  . LEU A 1 47  ? 11.992  3.565   -8.606  1.00 20.67  ? 47  LEU A CB  1 
ATOM   412  C  CG  . LEU A 1 47  ? 10.865  3.887   -7.738  1.00 19.32  ? 47  LEU A CG  1 
ATOM   413  C  CD1 . LEU A 1 47  ? 9.896   4.820   -8.531  1.00 23.68  ? 47  LEU A CD1 1 
ATOM   414  C  CD2 . LEU A 1 47  ? 10.239  2.584   -7.215  1.00 20.32  ? 47  LEU A CD2 1 
ATOM   415  N  N   . SER A 1 48  ? 13.561  6.419   -7.964  1.00 14.43  ? 48  SER A N   1 
ATOM   416  C  CA  . SER A 1 48  ? 14.416  7.025   -6.954  1.00 14.64  ? 48  SER A CA  1 
ATOM   417  C  C   . SER A 1 48  ? 13.636  7.061   -5.662  1.00 13.38  ? 48  SER A C   1 
ATOM   418  O  O   . SER A 1 48  ? 12.642  7.772   -5.544  1.00 14.35  ? 48  SER A O   1 
ATOM   419  C  CB  . SER A 1 48  ? 14.780  8.435   -7.393  1.00 17.05  ? 48  SER A CB  1 
ATOM   420  O  OG  . SER A 1 48  ? 15.455  9.124   -6.371  1.00 20.14  ? 48  SER A OG  1 
ATOM   421  N  N   . VAL A 1 49  ? 14.092  6.299   -4.727  1.00 15.73  ? 49  VAL A N   1 
ATOM   422  C  CA  . VAL A 1 49  ? 13.490  6.183   -3.440  1.00 16.20  ? 49  VAL A CA  1 
ATOM   423  C  C   . VAL A 1 49  ? 14.458  6.778   -2.414  1.00 17.98  ? 49  VAL A C   1 
ATOM   424  O  O   . VAL A 1 49  ? 15.552  6.256   -2.205  1.00 23.21  ? 49  VAL A O   1 
ATOM   425  C  CB  . VAL A 1 49  ? 13.204  4.706   -3.093  1.00 19.28  ? 49  VAL A CB  1 
ATOM   426  C  CG1 . VAL A 1 49  ? 12.435  4.675   -1.779  1.00 22.09  ? 49  VAL A CG1 1 
ATOM   427  C  CG2 . VAL A 1 49  ? 12.430  4.024   -4.205  1.00 22.24  ? 49  VAL A CG2 1 
ATOM   428  N  N   . SER A 1 50  ? 14.145  7.904   -1.792  1.00 17.28  ? 50  SER A N   1 
ATOM   429  C  CA  . SER A 1 50  ? 15.131  8.600   -0.962  1.00 20.44  ? 50  SER A CA  1 
ATOM   430  C  C   . SER A 1 50  ? 14.499  8.702   0.367   1.00 17.32  ? 50  SER A C   1 
ATOM   431  O  O   . SER A 1 50  ? 13.790  9.649   0.661   1.00 18.62  ? 50  SER A O   1 
ATOM   432  C  CB  . SER A 1 50  ? 15.575  9.982   -1.518  1.00 23.06  ? 50  SER A CB  1 
ATOM   433  O  OG  . SER A 1 50  ? 16.151  9.824   -2.817  1.00 27.17  ? 50  SER A OG  1 
ATOM   434  N  N   . TYR A 1 51  ? 14.756  7.696   1.193   1.00 18.07  ? 51  TYR A N   1 
ATOM   435  C  CA  . TYR A 1 51  ? 14.152  7.596   2.496   1.00 15.42  ? 51  TYR A CA  1 
ATOM   436  C  C   . TYR A 1 51  ? 15.111  7.862   3.664   1.00 18.03  ? 51  TYR A C   1 
ATOM   437  O  O   . TYR A 1 51  ? 14.719  7.750   4.782   1.00 18.84  ? 51  TYR A O   1 
ATOM   438  C  CB  . TYR A 1 51  ? 13.484  6.231   2.711   1.00 15.03  ? 51  TYR A CB  1 
ATOM   439  C  CG  . TYR A 1 51  ? 12.198  5.962   1.932   1.00 13.14  ? 51  TYR A CG  1 
ATOM   440  C  CD1 . TYR A 1 51  ? 11.459  6.978   1.289   1.00 14.68  ? 51  TYR A CD1 1 
ATOM   441  C  CD2 . TYR A 1 51  ? 11.750  4.671   1.828   1.00 12.45  ? 51  TYR A CD2 1 
ATOM   442  C  CE1 . TYR A 1 51  ? 10.258  6.638   0.620   1.00 12.32  ? 51  TYR A CE1 1 
ATOM   443  C  CE2 . TYR A 1 51  ? 10.563  4.353   1.156   1.00 12.72  ? 51  TYR A CE2 1 
ATOM   444  C  CZ  . TYR A 1 51  ? 9.822   5.344   0.566   1.00 11.82  ? 51  TYR A CZ  1 
ATOM   445  O  OH  . TYR A 1 51  ? 8.663   4.990   -0.107  1.00 12.25  ? 51  TYR A OH  1 
ATOM   446  N  N   A ASP A 1 52  ? 16.295  8.350   3.265   0.50 22.72  ? 52  ASP A N   1 
ATOM   447  N  N   B ASP A 1 52  ? 16.393  8.153   3.456   0.50 21.82  ? 52  ASP A N   1 
ATOM   448  C  CA  A ASP A 1 52  ? 17.411  8.697   4.129   0.50 20.75  ? 52  ASP A CA  1 
ATOM   449  C  CA  B ASP A 1 52  ? 17.337  8.453   4.589   0.50 21.47  ? 52  ASP A CA  1 
ATOM   450  C  C   A ASP A 1 52  ? 17.059  9.568   5.324   0.50 18.09  ? 52  ASP A C   1 
ATOM   451  C  C   B ASP A 1 52  ? 16.782  9.425   5.615   0.50 24.10  ? 52  ASP A C   1 
ATOM   452  O  O   A ASP A 1 52  ? 17.664  9.381   6.392   0.50 23.14  ? 52  ASP A O   1 
ATOM   453  O  O   B ASP A 1 52  ? 16.988  9.248   6.829   0.50 24.60  ? 52  ASP A O   1 
ATOM   454  C  CB  A ASP A 1 52  ? 18.607  9.268   3.328   0.50 20.31  ? 52  ASP A CB  1 
ATOM   455  C  CB  B ASP A 1 52  ? 18.693  8.959   4.038   0.50 23.51  ? 52  ASP A CB  1 
ATOM   456  C  CG  A ASP A 1 52  ? 18.174  10.219  2.215   0.50 24.71  ? 52  ASP A CG  1 
ATOM   457  C  CG  B ASP A 1 52  ? 19.830  8.953   5.070   0.50 23.83  ? 52  ASP A CG  1 
ATOM   458  O  OD1 A ASP A 1 52  ? 17.832  9.791   1.077   0.50 22.81  ? 52  ASP A OD1 1 
ATOM   459  O  OD1 B ASP A 1 52  ? 20.153  7.890   5.640   0.50 31.31  ? 52  ASP A OD1 1 
ATOM   460  O  OD2 A ASP A 1 52  ? 18.181  11.437  2.472   0.50 40.98  ? 52  ASP A OD2 1 
ATOM   461  O  OD2 B ASP A 1 52  ? 20.441  10.032  5.290   0.50 36.00  ? 52  ASP A OD2 1 
ATOM   462  N  N   . GLN A 1 53  ? 16.048  10.433  5.169   1.00 22.78  ? 53  GLN A N   1 
ATOM   463  C  CA  . GLN A 1 53  ? 15.667  11.430  6.177   1.00 26.26  ? 53  GLN A CA  1 
ATOM   464  C  C   . GLN A 1 53  ? 14.247  11.212  6.706   1.00 21.39  ? 53  GLN A C   1 
ATOM   465  O  O   . GLN A 1 53  ? 13.671  12.089  7.353   1.00 19.95  ? 53  GLN A O   1 
ATOM   466  C  CB  . GLN A 1 53  ? 15.976  12.874  5.708   1.00 33.64  ? 53  GLN A CB  1 
ATOM   467  C  CG  . GLN A 1 53  ? 17.479  13.143  5.426   1.00 42.08  ? 53  GLN A CG  1 
ATOM   468  C  CD  . GLN A 1 53  ? 18.350  12.997  6.676   1.00 64.01  ? 53  GLN A CD  1 
ATOM   469  O  OE1 . GLN A 1 53  ? 17.881  13.251  7.805   1.00 68.73  ? 53  GLN A OE1 1 
ATOM   470  N  NE2 . GLN A 1 53  ? 19.623  12.515  6.484   1.00 97.76  ? 53  GLN A NE2 1 
ATOM   471  N  N   . ALA A 1 54  ? 13.708  10.024  6.429   1.00 19.19  ? 54  ALA A N   1 
ATOM   472  C  CA  . ALA A 1 54  ? 12.313  9.790   6.845   1.00 16.38  ? 54  ALA A CA  1 
ATOM   473  C  C   . ALA A 1 54  ? 12.150  9.884   8.355   1.00 18.66  ? 54  ALA A C   1 
ATOM   474  O  O   . ALA A 1 54  ? 13.010  9.413   9.108   1.00 24.06  ? 54  ALA A O   1 
ATOM   475  C  CB  . ALA A 1 54  ? 11.784  8.424   6.372   1.00 19.03  ? 54  ALA A CB  1 
ATOM   476  N  N   . THR A 1 55  ? 11.053  10.511  8.797   1.00 14.54  ? 55  THR A N   1 
ATOM   477  C  CA  . THR A 1 55  ? 10.723  10.733  10.211  1.00 17.35  ? 55  THR A CA  1 
ATOM   478  C  C   . THR A 1 55  ? 9.392   10.141  10.521  1.00 13.83  ? 55  THR A C   1 
ATOM   479  O  O   . THR A 1 55  ? 8.385   10.760  10.224  1.00 14.53  ? 55  THR A O   1 
ATOM   480  C  CB  . THR A 1 55  ? 10.644  12.246  10.615  1.00 22.87  ? 55  THR A CB  1 
ATOM   481  O  OG1 . THR A 1 55  ? 11.888  12.906  10.433  1.00 28.27  ? 55  THR A OG1 1 
ATOM   482  C  CG2 . THR A 1 55  ? 10.266  12.302  12.107  1.00 27.41  ? 55  THR A CG2 1 
ATOM   483  N  N   . SER A 1 56  ? 9.407   8.927   11.013  1.00 15.12  ? 56  SER A N   1 
ATOM   484  C  CA  . SER A 1 56  ? 8.170   8.381   11.395  1.00 13.93  ? 56  SER A CA  1 
ATOM   485  C  C   . SER A 1 56  ? 7.830   8.990   12.704  1.00 13.01  ? 56  SER A C   1 
ATOM   486  O  O   . SER A 1 56  ? 8.539   9.474   13.502  1.00 17.99  ? 56  SER A O   1 
ATOM   487  C  CB  . SER A 1 56  ? 8.154   6.811   11.583  1.00 17.61  ? 56  SER A CB  1 
ATOM   488  O  OG  . SER A 1 56  ? 9.000   6.465   12.687  1.00 17.09  ? 56  SER A OG  1 
ATOM   489  N  N   . LEU A 1 57  ? 6.537   9.023   12.878  1.00 11.75  ? 57  LEU A N   1 
ATOM   490  C  CA  . LEU A 1 57  ? 5.977   9.624   14.087  1.00 14.04  ? 57  LEU A CA  1 
ATOM   491  C  C   . LEU A 1 57  ? 5.075   8.702   14.936  1.00 14.67  ? 57  LEU A C   1 
ATOM   492  O  O   . LEU A 1 57  ? 5.071   8.758   16.196  1.00 16.94  ? 57  LEU A O   1 
ATOM   493  C  CB  . LEU A 1 57  ? 5.051   10.760  13.641  1.00 18.48  ? 57  LEU A CB  1 
ATOM   494  C  CG  . LEU A 1 57  ? 5.685   12.052  13.091  1.00 24.96  ? 57  LEU A CG  1 
ATOM   495  C  CD1 . LEU A 1 57  ? 4.682   13.080  12.533  1.00 29.91  ? 57  LEU A CD1 1 
ATOM   496  C  CD2 . LEU A 1 57  ? 6.773   12.665  13.994  1.00 31.19  ? 57  LEU A CD2 1 
ATOM   497  N  N   . ARG A 1 58  ? 4.215   7.930   14.296  1.00 13.99  ? 58  ARG A N   1 
ATOM   498  C  CA  . ARG A 1 58  ? 3.126   7.307   15.050  1.00 14.94  ? 58  ARG A CA  1 
ATOM   499  C  C   . ARG A 1 58  ? 2.550   6.133   14.238  1.00 12.66  ? 58  ARG A C   1 
ATOM   500  O  O   . ARG A 1 58  ? 2.617   6.115   13.025  1.00 15.10  ? 58  ARG A O   1 
ATOM   501  C  CB  . ARG A 1 58  ? 1.975   8.329   15.185  1.00 15.74  ? 58  ARG A CB  1 
ATOM   502  C  CG  . ARG A 1 58  ? 0.917   7.938   16.103  1.00 16.38  ? 58  ARG A CG  1 
ATOM   503  C  CD  . ARG A 1 58  ? -0.064  9.016   16.387  1.00 17.90  ? 58  ARG A CD  1 
ATOM   504  N  NE  . ARG A 1 58  ? -0.978  9.029   15.243  1.00 15.31  ? 58  ARG A NE  1 
ATOM   505  C  CZ  . ARG A 1 58  ? -2.295  9.192   15.288  1.00 15.54  ? 58  ARG A CZ  1 
ATOM   506  N  NH1 . ARG A 1 58  ? -2.945  9.401   16.425  1.00 17.20  ? 58  ARG A NH1 1 
ATOM   507  N  NH2 . ARG A 1 58  ? -2.976  9.147   14.147  1.00 14.08  ? 58  ARG A NH2 1 
ATOM   508  N  N   . ILE A 1 59  ? 1.954   5.158   14.920  1.00 13.02  ? 59  ILE A N   1 
ATOM   509  C  CA  . ILE A 1 59  ? 1.368   4.059   14.258  1.00 11.99  ? 59  ILE A CA  1 
ATOM   510  C  C   . ILE A 1 59  ? -0.052  4.036   14.779  1.00 11.26  ? 59  ILE A C   1 
ATOM   511  O  O   . ILE A 1 59  ? -0.380  4.204   16.031  1.00 15.63  ? 59  ILE A O   1 
ATOM   512  C  CB  . ILE A 1 59  ? 2.014   2.728   14.522  1.00 12.95  ? 59  ILE A CB  1 
ATOM   513  C  CG1 . ILE A 1 59  ? 1.393   1.606   13.645  1.00 13.56  ? 59  ILE A CG1 1 
ATOM   514  C  CG2 . ILE A 1 59  ? 1.957   2.313   16.029  1.00 14.37  ? 59  ILE A CG2 1 
ATOM   515  C  CD1 . ILE A 1 59  ? 2.193   0.353   13.733  1.00 14.05  ? 59  ILE A CD1 1 
ATOM   516  N  N   . LEU A 1 60  ? -1.036  3.860   13.915  1.00 11.52  ? 60  LEU A N   1 
ATOM   517  C  CA  . LEU A 1 60  ? -2.391  3.938   14.124  1.00 10.52  ? 60  LEU A CA  1 
ATOM   518  C  C   . LEU A 1 60  ? -3.271  2.761   13.626  1.00 10.61  ? 60  LEU A C   1 
ATOM   519  O  O   . LEU A 1 60  ? -3.183  2.418   12.482  1.00 12.11  ? 60  LEU A O   1 
ATOM   520  C  CB  . LEU A 1 60  ? -2.990  5.258   13.453  1.00 11.86  ? 60  LEU A CB  1 
ATOM   521  C  CG  . LEU A 1 60  ? -4.529  5.360   13.541  1.00 13.32  ? 60  LEU A CG  1 
ATOM   522  C  CD1 . LEU A 1 60  ? -5.118  5.681   14.915  1.00 13.92  ? 60  LEU A CD1 1 
ATOM   523  C  CD2 . LEU A 1 60  ? -5.048  6.458   12.554  1.00 13.53  ? 60  LEU A CD2 1 
ATOM   524  N  N   . ASN A 1 61  ? -4.132  2.177   14.432  1.00 11.42  ? 61  ASN A N   1 
ATOM   525  C  CA  . ASN A 1 61  ? -5.122  1.233   14.035  1.00 12.15  ? 61  ASN A CA  1 
ATOM   526  C  C   . ASN A 1 61  ? -6.383  2.019   13.596  1.00 12.49  ? 61  ASN A C   1 
ATOM   527  O  O   . ASN A 1 61  ? -6.977  2.599   14.427  1.00 13.63  ? 61  ASN A O   1 
ATOM   528  C  CB  . ASN A 1 61  ? -5.404  0.187   15.083  1.00 12.04  ? 61  ASN A CB  1 
ATOM   529  C  CG  . ASN A 1 61  ? -6.504  -0.771  14.671  1.00 11.11  ? 61  ASN A CG  1 
ATOM   530  O  OD1 . ASN A 1 61  ? -7.379  -0.535  13.797  1.00 13.48  ? 61  ASN A OD1 1 
ATOM   531  N  ND2 . ASN A 1 61  ? -6.485  -2.014  15.274  1.00 13.56  ? 61  ASN A ND2 1 
ATOM   532  N  N   . ASN A 1 62  ? -6.694  2.072   12.286  1.00 14.45  ? 62  ASN A N   1 
ATOM   533  C  CA  . ASN A 1 62  ? -7.735  2.941   11.847  1.00 15.83  ? 62  ASN A CA  1 
ATOM   534  C  C   . ASN A 1 62  ? -9.035  2.169   11.634  1.00 15.23  ? 62  ASN A C   1 
ATOM   535  O  O   . ASN A 1 62  ? -10.023 2.661   11.022  1.00 20.08  ? 62  ASN A O   1 
ATOM   536  C  CB  . ASN A 1 62  ? -7.429  3.741   10.589  1.00 19.03  ? 62  ASN A CB  1 
ATOM   537  C  CG  . ASN A 1 62  ? -7.102  2.818   9.420   1.00 21.94  ? 62  ASN A CG  1 
ATOM   538  O  OD1 . ASN A 1 62  ? -7.634  1.668   9.280   1.00 15.59  ? 62  ASN A OD1 1 
ATOM   539  N  ND2 . ASN A 1 62  ? -6.198  3.276   8.584   1.00 33.75  ? 62  ASN A ND2 1 
ATOM   540  N  N   . GLY A 1 63  ? -9.037  0.917   12.083  1.00 13.42  ? 63  GLY A N   1 
ATOM   541  C  CA  . GLY A 1 63  ? -10.202 0.056   11.948  1.00 12.73  ? 63  GLY A CA  1 
ATOM   542  C  C   . GLY A 1 63  ? -10.271 -0.786  10.682  1.00 14.93  ? 63  GLY A C   1 
ATOM   543  O  O   . GLY A 1 63  ? -11.112 -1.678  10.573  1.00 16.37  ? 63  GLY A O   1 
ATOM   544  N  N   . HIS A 1 64  ? -9.391  -0.507  9.724   1.00 13.17  ? 64  HIS A N   1 
ATOM   545  C  CA  . HIS A 1 64  ? -9.368  -1.258  8.389   1.00 16.38  ? 64  HIS A CA  1 
ATOM   546  C  C   . HIS A 1 64  ? -7.979  -1.887  8.294   1.00 16.51  ? 64  HIS A C   1 
ATOM   547  O  O   . HIS A 1 64  ? -7.868  -3.049  7.815   1.00 18.19  ? 64  HIS A O   1 
ATOM   548  C  CB  . HIS A 1 64  ? -9.680  -0.285  7.234   1.00 17.34  ? 64  HIS A CB  1 
ATOM   549  C  CG  . HIS A 1 64  ? -10.983 0.420   7.376   1.00 17.83  ? 64  HIS A CG  1 
ATOM   550  N  ND1 . HIS A 1 64  ? -12.199 -0.235  7.213   1.00 21.17  ? 64  HIS A ND1 1 
ATOM   551  C  CD2 . HIS A 1 64  ? -11.279 1.763   7.525   1.00 19.17  ? 64  HIS A CD2 1 
ATOM   552  C  CE1 . HIS A 1 64  ? -13.198 0.634   7.346   1.00 20.69  ? 64  HIS A CE1 1 
ATOM   553  N  NE2 . HIS A 1 64  ? -12.654 1.863   7.579   1.00 21.07  ? 64  HIS A NE2 1 
ATOM   554  N  N   . ALA A 1 65  ? -6.920  -1.179  8.711   1.00 13.84  ? 65  ALA A N   1 
ATOM   555  C  CA  . ALA A 1 65  ? -5.528  -1.606  8.676   1.00 12.86  ? 65  ALA A CA  1 
ATOM   556  C  C   . ALA A 1 65  ? -4.769  -0.824  9.784   1.00 11.16  ? 65  ALA A C   1 
ATOM   557  O  O   . ALA A 1 65  ? -5.468  -0.120  10.581  1.00 13.60  ? 65  ALA A O   1 
ATOM   558  C  CB  . ALA A 1 65  ? -4.918  -1.458  7.250   1.00 14.78  ? 65  ALA A CB  1 
ATOM   559  N  N   . PHE A 1 66  ? -3.483  -0.825  9.743   1.00 11.24  ? 66  PHE A N   1 
ATOM   560  C  CA  . PHE A 1 66  ? -2.757  0.124   10.566  1.00 12.15  ? 66  PHE A CA  1 
ATOM   561  C  C   . PHE A 1 66  ? -1.900  0.993   9.676   1.00 11.19  ? 66  PHE A C   1 
ATOM   562  O  O   . PHE A 1 66  ? -1.291  0.517   8.705   1.00 11.71  ? 66  PHE A O   1 
ATOM   563  C  CB  . PHE A 1 66  ? -1.924  -0.574  11.658  1.00 12.84  ? 66  PHE A CB  1 
ATOM   564  C  CG  . PHE A 1 66  ? -0.844  -1.512  11.151  1.00 11.71  ? 66  PHE A CG  1 
ATOM   565  C  CD1 . PHE A 1 66  ? 0.426   -1.042  10.803  1.00 13.01  ? 66  PHE A CD1 1 
ATOM   566  C  CD2 . PHE A 1 66  ? -1.132  -2.883  10.992  1.00 11.45  ? 66  PHE A CD2 1 
ATOM   567  C  CE1 . PHE A 1 66  ? 1.367   -1.890  10.273  1.00 12.59  ? 66  PHE A CE1 1 
ATOM   568  C  CE2 . PHE A 1 66  ? -0.158  -3.743  10.470  1.00 11.04  ? 66  PHE A CE2 1 
ATOM   569  C  CZ  . PHE A 1 66  ? 1.116   -3.267  10.153  1.00 12.32  ? 66  PHE A CZ  1 
ATOM   570  N  N   . ASN A 1 67  ? -1.782  2.280   10.019  1.00 11.46  ? 67  ASN A N   1 
ATOM   571  C  CA  . ASN A 1 67  ? -0.967  3.228   9.282   1.00 11.31  ? 67  ASN A CA  1 
ATOM   572  C  C   . ASN A 1 67  ? 0.326   3.570   10.079  1.00 10.05  ? 67  ASN A C   1 
ATOM   573  O  O   . ASN A 1 67  ? 0.215   3.972   11.271  1.00 12.04  ? 67  ASN A O   1 
ATOM   574  C  CB  . ASN A 1 67  ? -1.675  4.519   9.031   1.00 12.84  ? 67  ASN A CB  1 
ATOM   575  C  CG  . ASN A 1 67  ? -2.879  4.366   8.154   1.00 14.34  ? 67  ASN A CG  1 
ATOM   576  O  OD1 . ASN A 1 67  ? -3.066  3.335   7.430   1.00 14.99  ? 67  ASN A OD1 1 
ATOM   577  N  ND2 . ASN A 1 67  ? -3.755  5.355   8.223   1.00 19.31  ? 67  ASN A ND2 1 
ATOM   578  N  N   . VAL A 1 68  ? 1.487   3.492   9.481   1.00 11.33  ? 68  VAL A N   1 
ATOM   579  C  CA  . VAL A 1 68  ? 2.697   4.063   10.059  1.00 11.42  ? 68  VAL A CA  1 
ATOM   580  C  C   . VAL A 1 68  ? 2.828   5.452   9.395   1.00 12.68  ? 68  VAL A C   1 
ATOM   581  O  O   . VAL A 1 68  ? 2.935   5.563   8.155   1.00 11.81  ? 68  VAL A O   1 
ATOM   582  C  CB  . VAL A 1 68  ? 3.931   3.179   9.826   1.00 12.54  ? 68  VAL A CB  1 
ATOM   583  C  CG1 . VAL A 1 68  ? 5.186   3.921   10.294  1.00 14.62  ? 68  VAL A CG1 1 
ATOM   584  C  CG2 . VAL A 1 68  ? 3.763   1.902   10.599  1.00 14.36  ? 68  VAL A CG2 1 
ATOM   585  N  N   . GLU A 1 69  ? 2.772   6.487   10.191  1.00 12.77  ? 69  GLU A N   1 
ATOM   586  C  CA  . GLU A 1 69  ? 2.713   7.881   9.753   1.00 11.62  ? 69  GLU A CA  1 
ATOM   587  C  C   . GLU A 1 69  ? 4.050   8.573   9.756   1.00 11.94  ? 69  GLU A C   1 
ATOM   588  O  O   . GLU A 1 69  ? 4.891   8.305   10.689  1.00 13.45  ? 69  GLU A O   1 
ATOM   589  C  CB  . GLU A 1 69  ? 1.758   8.647   10.651  1.00 13.23  ? 69  GLU A CB  1 
ATOM   590  C  CG  . GLU A 1 69  ? 0.384   8.082   10.634  1.00 14.21  ? 69  GLU A CG  1 
ATOM   591  C  CD  . GLU A 1 69  ? -0.462  8.535   11.810  1.00 14.83  ? 69  GLU A CD  1 
ATOM   592  O  OE1 . GLU A 1 69  ? 0.068   9.252   12.688  1.00 15.57  ? 69  GLU A OE1 1 
ATOM   593  O  OE2 . GLU A 1 69  ? -1.656  8.170   11.851  1.00 14.95  ? 69  GLU A OE2 1 
ATOM   594  N  N   . PHE A 1 70  ? 4.242   9.472   8.821   1.00 13.02  ? 70  PHE A N   1 
ATOM   595  C  CA  . PHE A 1 70  ? 5.492   10.187  8.724   1.00 12.29  ? 70  PHE A CA  1 
ATOM   596  C  C   . PHE A 1 70  ? 5.238   11.665  8.809   1.00 13.23  ? 70  PHE A C   1 
ATOM   597  O  O   . PHE A 1 70  ? 4.163   12.152  8.408   1.00 14.61  ? 70  PHE A O   1 
ATOM   598  C  CB  . PHE A 1 70  ? 6.213   9.832   7.438   1.00 12.77  ? 70  PHE A CB  1 
ATOM   599  C  CG  . PHE A 1 70  ? 6.777   8.442   7.470   1.00 12.34  ? 70  PHE A CG  1 
ATOM   600  C  CD1 . PHE A 1 70  ? 5.941   7.330   7.254   1.00 13.56  ? 70  PHE A CD1 1 
ATOM   601  C  CD2 . PHE A 1 70  ? 8.120   8.225   7.766   1.00 11.82  ? 70  PHE A CD2 1 
ATOM   602  C  CE1 . PHE A 1 70  ? 6.496   6.056   7.392   1.00 13.87  ? 70  PHE A CE1 1 
ATOM   603  C  CE2 . PHE A 1 70  ? 8.638   6.941   7.923   1.00 13.08  ? 70  PHE A CE2 1 
ATOM   604  C  CZ  . PHE A 1 70  ? 7.816   5.844   7.717   1.00 13.68  ? 70  PHE A CZ  1 
ATOM   605  N  N   A ASP A 1 71  ? 6.079   12.443  9.421   0.50 13.73  ? 71  ASP A N   1 
ATOM   606  N  N   B ASP A 1 71  ? 6.359   12.355  9.064   0.50 12.11  ? 71  ASP A N   1 
ATOM   607  C  CA  A ASP A 1 71  ? 5.925   13.869  9.404   0.50 13.83  ? 71  ASP A CA  1 
ATOM   608  C  CA  B ASP A 1 71  ? 6.411   13.790  9.036   0.50 15.20  ? 71  ASP A CA  1 
ATOM   609  C  C   A ASP A 1 71  ? 6.363   14.217  7.962   0.50 14.52  ? 71  ASP A C   1 
ATOM   610  C  C   B ASP A 1 71  ? 6.514   14.162  7.597   0.50 14.95  ? 71  ASP A C   1 
ATOM   611  O  O   A ASP A 1 71  ? 7.537   14.075  7.693   0.50 16.05  ? 71  ASP A O   1 
ATOM   612  O  O   B ASP A 1 71  ? 7.518   13.946  6.915   0.50 16.63  ? 71  ASP A O   1 
ATOM   613  C  CB  A ASP A 1 71  ? 7.003   14.448  10.249  0.50 18.22  ? 71  ASP A CB  1 
ATOM   614  C  CB  B ASP A 1 71  ? 7.569   14.339  9.835   0.50 19.15  ? 71  ASP A CB  1 
ATOM   615  C  CG  A ASP A 1 71  ? 7.317   15.886  9.879   0.50 24.08  ? 71  ASP A CG  1 
ATOM   616  C  CG  B ASP A 1 71  ? 7.432   15.841  10.102  0.50 23.87  ? 71  ASP A CG  1 
ATOM   617  O  OD1 A ASP A 1 71  ? 6.361   16.594  9.507   0.50 19.70  ? 71  ASP A OD1 1 
ATOM   618  O  OD1 B ASP A 1 71  ? 7.642   16.303  11.222  0.50 24.55  ? 71  ASP A OD1 1 
ATOM   619  O  OD2 A ASP A 1 71  ? 8.482   16.338  9.937   0.50 19.79  ? 71  ASP A OD2 1 
ATOM   620  O  OD2 B ASP A 1 71  ? 7.072   16.525  9.124   0.50 19.54  ? 71  ASP A OD2 1 
ATOM   621  N  N   . ASP A 1 72  ? 5.430   14.730  7.137   1.00 14.27  ? 72  ASP A N   1 
ATOM   622  C  CA  . ASP A 1 72  ? 5.535   15.145  5.717   1.00 14.78  ? 72  ASP A CA  1 
ATOM   623  C  C   . ASP A 1 72  ? 5.490   16.663  5.610   1.00 16.39  ? 72  ASP A C   1 
ATOM   624  O  O   . ASP A 1 72  ? 5.076   17.191  4.604   1.00 18.76  ? 72  ASP A O   1 
ATOM   625  C  CB  . ASP A 1 72  ? 4.434   14.508  4.873   1.00 16.07  ? 72  ASP A CB  1 
ATOM   626  C  CG  . ASP A 1 72  ? 3.057   14.979  5.257   1.00 14.66  ? 72  ASP A CG  1 
ATOM   627  O  OD1 . ASP A 1 72  ? 2.879   15.696  6.312   1.00 18.37  ? 72  ASP A OD1 1 
ATOM   628  O  OD2 . ASP A 1 72  ? 2.137   14.705  4.481   1.00 16.24  ? 72  ASP A OD2 1 
ATOM   629  N  N   . SER A 1 73  ? 5.944   17.369  6.620   1.00 17.36  ? 73  SER A N   1 
ATOM   630  C  CA  . SER A 1 73  ? 5.945   18.870  6.617   1.00 19.38  ? 73  SER A CA  1 
ATOM   631  C  C   . SER A 1 73  ? 7.268   19.455  6.019   1.00 19.39  ? 73  SER A C   1 
ATOM   632  O  O   . SER A 1 73  ? 7.335   20.651  5.829   1.00 18.84  ? 73  SER A O   1 
ATOM   633  C  CB  . SER A 1 73  ? 5.663   19.349  8.023   1.00 23.91  ? 73  SER A CB  1 
ATOM   634  O  OG  . SER A 1 73  ? 6.841   19.200  8.752   1.00 22.17  ? 73  SER A OG  1 
ATOM   635  N  N   . GLN A 1 74  ? 8.253   18.613  5.691   1.00 21.04  ? 74  GLN A N   1 
ATOM   636  C  CA  . GLN A 1 74  ? 9.471   19.032  5.018   1.00 23.51  ? 74  GLN A CA  1 
ATOM   637  C  C   . GLN A 1 74  ? 9.774   18.070  3.953   1.00 20.28  ? 74  GLN A C   1 
ATOM   638  O  O   . GLN A 1 74  ? 9.257   16.961  3.953   1.00 16.34  ? 74  GLN A O   1 
ATOM   639  C  CB  . GLN A 1 74  ? 10.691  19.057  5.941   1.00 28.61  ? 74  GLN A CB  1 
ATOM   640  C  CG  . GLN A 1 74  ? 10.553  20.105  6.995   1.00 32.32  ? 74  GLN A CG  1 
ATOM   641  C  CD  . GLN A 1 74  ? 11.769  20.109  7.851   1.00 31.25  ? 74  GLN A CD  1 
ATOM   642  O  OE1 . GLN A 1 74  ? 12.877  20.400  7.388   1.00 52.06  ? 74  GLN A OE1 1 
ATOM   643  N  NE2 . GLN A 1 74  ? 11.584  19.737  9.112   1.00 38.66  ? 74  GLN A NE2 1 
ATOM   644  N  N   . ASP A 1 75  ? 10.659  18.525  3.062   1.00 23.15  ? 75  ASP A N   1 
ATOM   645  C  CA  . ASP A 1 75  ? 11.162  17.779  1.989   1.00 23.15  ? 75  ASP A CA  1 
ATOM   646  C  C   . ASP A 1 75  ? 12.093  16.605  2.569   1.00 21.03  ? 75  ASP A C   1 
ATOM   647  O  O   . ASP A 1 75  ? 13.328  16.797  2.650   1.00 25.96  ? 75  ASP A O   1 
ATOM   648  C  CB  . ASP A 1 75  ? 11.930  18.829  1.118   1.00 23.12  ? 75  ASP A CB  1 
ATOM   649  C  CG  . ASP A 1 75  ? 12.617  18.228  -0.083  1.00 36.92  ? 75  ASP A CG  1 
ATOM   650  O  OD1 . ASP A 1 75  ? 12.270  17.087  -0.411  1.00 26.55  ? 75  ASP A OD1 1 
ATOM   651  O  OD2 . ASP A 1 75  ? 13.503  18.886  -0.698  1.00 44.90  ? 75  ASP A OD2 1 
ATOM   652  N  N   . LYS A 1 76  ? 11.555  15.458  2.953   1.00 19.38  ? 76  LYS A N   1 
ATOM   653  C  CA  . LYS A 1 76  ? 12.429  14.446  3.549   1.00 23.27  ? 76  LYS A CA  1 
ATOM   654  C  C   . LYS A 1 76  ? 12.492  13.120  2.783   1.00 38.34  ? 76  LYS A C   1 
ATOM   655  O  O   . LYS A 1 76  ? 13.501  12.799  2.159   1.00 41.95  ? 76  LYS A O   1 
ATOM   656  C  CB  . LYS A 1 76  ? 12.034  14.193  5.004   1.00 25.89  ? 76  LYS A CB  1 
ATOM   657  C  CG  . LYS A 1 76  ? 12.277  15.366  5.937   1.00 33.03  ? 76  LYS A CG  1 
ATOM   658  C  CD  . LYS A 1 76  ? 11.510  15.203  7.240   1.00 42.79  ? 76  LYS A CD  1 
ATOM   659  C  CE  . LYS A 1 76  ? 12.198  15.935  8.381   1.00 38.59  ? 76  LYS A CE  1 
ATOM   660  N  NZ  . LYS A 1 76  ? 11.363  15.950  9.614   1.00 88.27  ? 76  LYS A NZ  1 
ATOM   661  N  N   . ALA A 1 77  ? 11.394  12.374  2.868   1.00 35.43  ? 77  ALA A N   1 
ATOM   662  C  CA  . ALA A 1 77  ? 11.248  11.015  2.348   1.00 18.51  ? 77  ALA A CA  1 
ATOM   663  C  C   . ALA A 1 77  ? 10.533  11.122  1.015   1.00 15.06  ? 77  ALA A C   1 
ATOM   664  O  O   . ALA A 1 77  ? 9.336   11.258  0.999   1.00 24.14  ? 77  ALA A O   1 
ATOM   665  C  CB  . ALA A 1 77  ? 10.442  10.226  3.375   1.00 19.15  ? 77  ALA A CB  1 
ATOM   666  N  N   . VAL A 1 78  ? 11.230  11.081  -0.086  1.00 14.02  ? 78  VAL A N   1 
ATOM   667  C  CA  . VAL A 1 78  ? 10.560  11.289  -1.352  1.00 15.17  ? 78  VAL A CA  1 
ATOM   668  C  C   . VAL A 1 78  ? 10.815  10.210  -2.381  1.00 13.73  ? 78  VAL A C   1 
ATOM   669  O  O   . VAL A 1 78  ? 11.849  9.526   -2.455  1.00 15.39  ? 78  VAL A O   1 
ATOM   670  C  CB  . VAL A 1 78  ? 11.007  12.657  -1.950  1.00 19.79  ? 78  VAL A CB  1 
ATOM   671  C  CG1 . VAL A 1 78  ? 10.732  13.795  -0.985  1.00 23.50  ? 78  VAL A CG1 1 
ATOM   672  C  CG2 . VAL A 1 78  ? 12.486  12.606  -2.303  1.00 22.16  ? 78  VAL A CG2 1 
ATOM   673  N  N   . LEU A 1 79  ? 9.782   10.088  -3.224  1.00 11.80  ? 79  LEU A N   1 
ATOM   674  C  CA  . LEU A 1 79  ? 9.770   9.204   -4.380  1.00 12.10  ? 79  LEU A CA  1 
ATOM   675  C  C   . LEU A 1 79  ? 9.764   10.057  -5.604  1.00 12.40  ? 79  LEU A C   1 
ATOM   676  O  O   . LEU A 1 79  ? 8.931   10.996  -5.715  1.00 12.98  ? 79  LEU A O   1 
ATOM   677  C  CB  . LEU A 1 79  ? 8.511   8.311   -4.286  1.00 12.55  ? 79  LEU A CB  1 
ATOM   678  C  CG  . LEU A 1 79  ? 8.413   7.255   -5.330  1.00 12.86  ? 79  LEU A CG  1 
ATOM   679  C  CD1 . LEU A 1 79  ? 9.467   6.190   -5.123  1.00 19.08  ? 79  LEU A CD1 1 
ATOM   680  C  CD2 . LEU A 1 79  ? 7.048   6.585   -5.276  1.00 12.64  ? 79  LEU A CD2 1 
ATOM   681  N  N   . LYS A 1 80  ? 10.631  9.723   -6.540  1.00 12.34  ? 80  LYS A N   1 
ATOM   682  C  CA  . LYS A 1 80  ? 10.671  10.421  -7.811  1.00 13.19  ? 80  LYS A CA  1 
ATOM   683  C  C   . LYS A 1 80  ? 11.221  9.492   -8.871  1.00 13.67  ? 80  LYS A C   1 
ATOM   684  O  O   . LYS A 1 80  ? 11.525  8.352   -8.619  1.00 13.91  ? 80  LYS A O   1 
ATOM   685  C  CB  . LYS A 1 80  ? 11.409  11.747  -7.763  1.00 17.27  ? 80  LYS A CB  1 
ATOM   686  C  CG  . LYS A 1 80  ? 12.841  11.535  -7.535  1.00 18.62  ? 80  LYS A CG  1 
ATOM   687  C  CD  . LYS A 1 80  ? 13.540  12.895  -7.227  1.00 25.09  ? 80  LYS A CD  1 
ATOM   688  C  CE  . LYS A 1 80  ? 14.985  12.882  -7.718  1.00 35.40  ? 80  LYS A CE  1 
ATOM   689  N  NZ  . LYS A 1 80  ? 15.975  11.963  -7.078  1.00 53.92  ? 80  LYS A NZ  1 
ATOM   690  N  N   . GLY A 1 81  ? 11.350  9.983   -10.091 1.00 14.66  ? 81  GLY A N   1 
ATOM   691  C  CA  . GLY A 1 81  ? 11.824  9.110   -11.167 1.00 14.59  ? 81  GLY A CA  1 
ATOM   692  C  C   . GLY A 1 81  ? 10.802  8.092   -11.495 1.00 14.21  ? 81  GLY A C   1 
ATOM   693  O  O   . GLY A 1 81  ? 9.586   8.312   -11.301 1.00 14.27  ? 81  GLY A O   1 
ATOM   694  N  N   . GLY A 1 82  ? 11.289  6.979   -12.014 1.00 18.46  ? 82  GLY A N   1 
ATOM   695  C  CA  . GLY A 1 82  ? 10.380  5.964   -12.441 1.00 22.73  ? 82  GLY A CA  1 
ATOM   696  C  C   . GLY A 1 82  ? 9.534   6.564   -13.548 1.00 17.09  ? 82  GLY A C   1 
ATOM   697  O  O   . GLY A 1 82  ? 10.015  7.245   -14.435 1.00 24.08  ? 82  GLY A O   1 
ATOM   698  N  N   . PRO A 1 83  ? 8.168   6.428   -13.421 1.00 15.82  ? 83  PRO A N   1 
ATOM   699  C  CA  . PRO A 1 83  ? 7.234   6.980   -14.362 1.00 15.98  ? 83  PRO A CA  1 
ATOM   700  C  C   . PRO A 1 83  ? 6.803   8.396   -13.954 1.00 14.76  ? 83  PRO A C   1 
ATOM   701  O  O   . PRO A 1 83  ? 5.991   8.976   -14.647 1.00 18.24  ? 83  PRO A O   1 
ATOM   702  C  CB  . PRO A 1 83  ? 5.982   6.085   -14.210 1.00 16.37  ? 83  PRO A CB  1 
ATOM   703  C  CG  . PRO A 1 83  ? 5.958   5.749   -12.777 1.00 14.63  ? 83  PRO A CG  1 
ATOM   704  C  CD  . PRO A 1 83  ? 7.434   5.620   -12.411 1.00 13.89  ? 83  PRO A CD  1 
ATOM   705  N  N   . LEU A 1 84  ? 7.288   8.935   -12.850 1.00 12.59  ? 84  LEU A N   1 
ATOM   706  C  CA  . LEU A 1 84  ? 6.765   10.156  -12.269 1.00 12.85  ? 84  LEU A CA  1 
ATOM   707  C  C   . LEU A 1 84  ? 7.381   11.396  -12.859 1.00 14.82  ? 84  LEU A C   1 
ATOM   708  O  O   . LEU A 1 84  ? 8.567   11.448  -13.120 1.00 16.49  ? 84  LEU A O   1 
ATOM   709  C  CB  . LEU A 1 84  ? 7.004   10.138  -10.760 1.00 11.30  ? 84  LEU A CB  1 
ATOM   710  C  CG  . LEU A 1 84  ? 6.427   8.916   -10.025 1.00 11.16  ? 84  LEU A CG  1 
ATOM   711  C  CD1 . LEU A 1 84  ? 6.920   8.877   -8.579  1.00 12.41  ? 84  LEU A CD1 1 
ATOM   712  C  CD2 . LEU A 1 84  ? 4.892   8.887   -10.126 1.00 11.70  ? 84  LEU A CD2 1 
ATOM   713  N  N   . ASP A 1 85  ? 6.580   12.457  -12.898 1.00 16.32  ? 85  ASP A N   1 
ATOM   714  C  CA  . ASP A 1 85  ? 7.071   13.823  -13.188 1.00 18.10  ? 85  ASP A CA  1 
ATOM   715  C  C   . ASP A 1 85  ? 7.095   14.485  -11.787 1.00 19.05  ? 85  ASP A C   1 
ATOM   716  O  O   . ASP A 1 85  ? 6.115   14.444  -11.021 1.00 24.06  ? 85  ASP A O   1 
ATOM   717  C  CB  . ASP A 1 85  ? 6.120   14.564  -14.148 1.00 21.57  ? 85  ASP A CB  1 
ATOM   718  C  CG  . ASP A 1 85  ? 6.155   14.044  -15.585 1.00 29.84  ? 85  ASP A CG  1 
ATOM   719  O  OD1 . ASP A 1 85  ? 7.182   13.437  -16.004 1.00 29.93  ? 85  ASP A OD1 1 
ATOM   720  O  OD2 . ASP A 1 85  ? 5.120   14.322  -16.286 1.00 38.71  ? 85  ASP A OD2 1 
ATOM   721  N  N   . GLY A 1 86  ? 8.148   15.153  -11.414 1.00 23.30  ? 86  GLY A N   1 
ATOM   722  C  CA  . GLY A 1 86  ? 8.150   15.738  -10.108 1.00 21.09  ? 86  GLY A CA  1 
ATOM   723  C  C   . GLY A 1 86  ? 8.364   14.814  -8.902  1.00 20.19  ? 86  GLY A C   1 
ATOM   724  O  O   . GLY A 1 86  ? 8.782   13.651  -8.986  1.00 26.75  ? 86  GLY A O   1 
ATOM   725  N  N   A THR A 1 87  ? 8.176   15.428  -7.741  0.50 14.86  ? 87  THR A N   1 
ATOM   726  N  N   B THR A 1 87  ? 7.961   15.314  -7.761  0.50 14.28  ? 87  THR A N   1 
ATOM   727  C  CA  A THR A 1 87  ? 8.523   14.870  -6.426  0.50 16.00  ? 87  THR A CA  1 
ATOM   728  C  CA  B THR A 1 87  ? 8.402   14.709  -6.546  0.50 12.79  ? 87  THR A CA  1 
ATOM   729  C  C   A THR A 1 87  ? 7.255   14.471  -5.708  0.50 12.43  ? 87  THR A C   1 
ATOM   730  C  C   B THR A 1 87  ? 7.277   14.500  -5.559  0.50 13.09  ? 87  THR A C   1 
ATOM   731  O  O   A THR A 1 87  ? 6.247   15.273  -5.734  0.50 10.30  ? 87  THR A O   1 
ATOM   732  O  O   B THR A 1 87  ? 6.429   15.400  -5.228  0.50 12.93  ? 87  THR A O   1 
ATOM   733  C  CB  A THR A 1 87  ? 9.186   15.946  -5.520  0.50 17.63  ? 87  THR A CB  1 
ATOM   734  C  CB  B THR A 1 87  ? 9.454   15.569  -5.859  0.50 12.57  ? 87  THR A CB  1 
ATOM   735  O  OG1 A THR A 1 87  ? 10.356  16.438  -6.151  0.50 21.55  ? 87  THR A OG1 1 
ATOM   736  O  OG1 B THR A 1 87  ? 8.886   16.845  -5.631  0.50 12.66  ? 87  THR A OG1 1 
ATOM   737  C  CG2 A THR A 1 87  ? 9.631   15.379  -4.179  0.50 18.84  ? 87  THR A CG2 1 
ATOM   738  C  CG2 B THR A 1 87  ? 10.741  15.749  -6.695  0.50 12.56  ? 87  THR A CG2 1 
ATOM   739  N  N   . TYR A 1 88  ? 7.294   13.310  -5.024  1.00 11.51  ? 88  TYR A N   1 
ATOM   740  C  CA  . TYR A 1 88  ? 6.167   12.853  -4.185  1.00 10.53  ? 88  TYR A CA  1 
ATOM   741  C  C   . TYR A 1 88  ? 6.698   12.542  -2.797  1.00 10.44  ? 88  TYR A C   1 
ATOM   742  O  O   . TYR A 1 88  ? 7.691   11.851  -2.617  1.00 14.23  ? 88  TYR A O   1 
ATOM   743  C  CB  . TYR A 1 88  ? 5.528   11.633  -4.769  1.00 10.01  ? 88  TYR A CB  1 
ATOM   744  C  CG  . TYR A 1 88  ? 4.769   11.835  -6.074  1.00 9.44   ? 88  TYR A CG  1 
ATOM   745  C  CD1 . TYR A 1 88  ? 5.426   12.160  -7.260  1.00 10.02  ? 88  TYR A CD1 1 
ATOM   746  C  CD2 . TYR A 1 88  ? 3.393   11.658  -6.122  1.00 8.42   ? 88  TYR A CD2 1 
ATOM   747  C  CE1 . TYR A 1 88  ? 4.727   12.318  -8.448  1.00 9.91   ? 88  TYR A CE1 1 
ATOM   748  C  CE2 . TYR A 1 88  ? 2.687   11.820  -7.300  1.00 8.51   ? 88  TYR A CE2 1 
ATOM   749  C  CZ  . TYR A 1 88  ? 3.354   12.150  -8.460  1.00 8.48   ? 88  TYR A CZ  1 
ATOM   750  O  OH  . TYR A 1 88  ? 2.633   12.309  -9.621  1.00 9.51   ? 88  TYR A OH  1 
ATOM   751  N  N   . ARG A 1 89  ? 6.036   13.055  -1.814  1.00 9.68   ? 89  ARG A N   1 
ATOM   752  C  CA  . ARG A 1 89  ? 6.492   12.935  -0.409  1.00 10.81  ? 89  ARG A CA  1 
ATOM   753  C  C   . ARG A 1 89  ? 5.712   11.869  0.324   1.00 9.11   ? 89  ARG A C   1 
ATOM   754  O  O   . ARG A 1 89  ? 4.480   11.775  0.285   1.00 8.78   ? 89  ARG A O   1 
ATOM   755  C  CB  . ARG A 1 89  ? 6.246   14.304  0.247   1.00 13.54  ? 89  ARG A CB  1 
ATOM   756  C  CG  . ARG A 1 89  ? 7.002   14.403  1.528   1.00 13.81  ? 89  ARG A CG  1 
ATOM   757  C  CD  . ARG A 1 89  ? 6.862   15.781  2.107   1.00 14.82  ? 89  ARG A CD  1 
ATOM   758  N  NE  . ARG A 1 89  ? 7.471   16.801  1.269   1.00 15.44  ? 89  ARG A NE  1 
ATOM   759  C  CZ  . ARG A 1 89  ? 7.342   18.112  1.453   1.00 13.50  ? 89  ARG A CZ  1 
ATOM   760  N  NH1 . ARG A 1 89  ? 6.614   18.590  2.457   1.00 17.39  ? 89  ARG A NH1 1 
ATOM   761  N  NH2 . ARG A 1 89  ? 7.945   18.946  0.618   1.00 17.08  ? 89  ARG A NH2 1 
ATOM   762  N  N   . LEU A 1 90  ? 6.483   11.022  1.046   1.00 9.22   ? 90  LEU A N   1 
ATOM   763  C  CA  . LEU A 1 90  ? 5.921   9.936   1.838   1.00 9.67   ? 90  LEU A CA  1 
ATOM   764  C  C   . LEU A 1 90  ? 5.062   10.514  2.984   1.00 10.08  ? 90  LEU A C   1 
ATOM   765  O  O   . LEU A 1 90  ? 5.547   11.338  3.809   1.00 11.98  ? 90  LEU A O   1 
ATOM   766  C  CB  . LEU A 1 90  ? 7.023   9.098   2.423   1.00 10.45  ? 90  LEU A CB  1 
ATOM   767  C  CG  . LEU A 1 90  ? 6.600   7.899   3.317   1.00 12.02  ? 90  LEU A CG  1 
ATOM   768  C  CD1 . LEU A 1 90  ? 5.855   6.850   2.490   1.00 12.80  ? 90  LEU A CD1 1 
ATOM   769  C  CD2 . LEU A 1 90  ? 7.867   7.292   3.948   1.00 14.28  ? 90  LEU A CD2 1 
ATOM   770  N  N   . ILE A 1 91  ? 3.830   10.064  3.105   1.00 9.31   ? 91  ILE A N   1 
ATOM   771  C  CA  . ILE A 1 91  ? 2.910   10.403  4.193   1.00 10.01  ? 91  ILE A CA  1 
ATOM   772  C  C   . ILE A 1 91  ? 2.691   9.234   5.131   1.00 9.11   ? 91  ILE A C   1 
ATOM   773  O  O   . ILE A 1 91  ? 2.614   9.441   6.360   1.00 9.81   ? 91  ILE A O   1 
ATOM   774  C  CB  . ILE A 1 91  ? 1.624   11.065  3.713   1.00 10.87  ? 91  ILE A CB  1 
ATOM   775  C  CG1 . ILE A 1 91  ? 0.731   11.456  4.890   1.00 12.76  ? 91  ILE A CG1 1 
ATOM   776  C  CG2 . ILE A 1 91  ? 0.905   10.209  2.661   1.00 11.12  ? 91  ILE A CG2 1 
ATOM   777  C  CD1 . ILE A 1 91  ? -0.437  12.366  4.449   1.00 15.11  ? 91  ILE A CD1 1 
ATOM   778  N  N   . GLN A 1 92  ? 2.507   7.996   4.639   1.00 8.97   ? 92  GLN A N   1 
ATOM   779  C  CA  . GLN A 1 92  ? 2.272   6.866   5.485   1.00 9.32   ? 92  GLN A CA  1 
ATOM   780  C  C   . GLN A 1 92  ? 2.455   5.596   4.707   1.00 8.88   ? 92  GLN A C   1 
ATOM   781  O  O   . GLN A 1 92  ? 2.531   5.624   3.475   1.00 9.52   ? 92  GLN A O   1 
ATOM   782  C  CB  . GLN A 1 92  ? 0.877   6.878   5.992   1.00 10.99  ? 92  GLN A CB  1 
ATOM   783  C  CG  . GLN A 1 92  ? -0.254  6.922   4.894   1.00 12.27  ? 92  GLN A CG  1 
ATOM   784  C  CD  . GLN A 1 92  ? -0.982  5.609   4.835   1.00 11.39  ? 92  GLN A CD  1 
ATOM   785  O  OE1 . GLN A 1 92  ? -0.478  4.569   4.523   1.00 11.51  ? 92  GLN A OE1 1 
ATOM   786  N  NE2 . GLN A 1 92  ? -2.154  5.571   5.362   1.00 22.23  ? 92  GLN A NE2 1 
ATOM   787  N  N   . PHE A 1 93  ? 2.616   4.501   5.447   1.00 8.57   ? 93  PHE A N   1 
ATOM   788  C  CA  . PHE A 1 93  ? 2.496   3.188   4.814   1.00 8.67   ? 93  PHE A CA  1 
ATOM   789  C  C   . PHE A 1 93  ? 1.524   2.368   5.621   1.00 8.30   ? 93  PHE A C   1 
ATOM   790  O  O   . PHE A 1 93  ? 1.287   2.582   6.826   1.00 9.91   ? 93  PHE A O   1 
ATOM   791  C  CB  . PHE A 1 93  ? 3.814   2.453   4.573   1.00 8.91   ? 93  PHE A CB  1 
ATOM   792  C  CG  . PHE A 1 93  ? 4.569   1.993   5.794   1.00 9.25   ? 93  PHE A CG  1 
ATOM   793  C  CD1 . PHE A 1 93  ? 4.219   0.832   6.460   1.00 10.07  ? 93  PHE A CD1 1 
ATOM   794  C  CD2 . PHE A 1 93  ? 5.711   2.683   6.214   1.00 10.21  ? 93  PHE A CD2 1 
ATOM   795  C  CE1 . PHE A 1 93  ? 4.912   0.407   7.596   1.00 11.65  ? 93  PHE A CE1 1 
ATOM   796  C  CE2 . PHE A 1 93  ? 6.421   2.225   7.341   1.00 11.99  ? 93  PHE A CE2 1 
ATOM   797  C  CZ  . PHE A 1 93  ? 6.038   1.095   8.011   1.00 11.40  ? 93  PHE A CZ  1 
ATOM   798  N  N   . HIS A 1 94  ? 0.981   1.324   4.952   1.00 8.09   ? 94  HIS A N   1 
ATOM   799  C  CA  . HIS A 1 94  ? 0.099   0.337   5.559   1.00 8.34   ? 94  HIS A CA  1 
ATOM   800  C  C   . HIS A 1 94  ? 0.194   -0.938  4.734   1.00 8.10   ? 94  HIS A C   1 
ATOM   801  O  O   . HIS A 1 94  ? 0.818   -0.959  3.676   1.00 7.95   ? 94  HIS A O   1 
ATOM   802  C  CB  . HIS A 1 94  ? -1.343  0.849   5.620   1.00 8.75   ? 94  HIS A CB  1 
ATOM   803  C  CG  . HIS A 1 94  ? -1.896  1.121   4.223   1.00 7.86   ? 94  HIS A CG  1 
ATOM   804  N  ND1 . HIS A 1 94  ? -1.719  2.305   3.586   1.00 8.16   ? 94  HIS A ND1 1 
ATOM   805  C  CD2 . HIS A 1 94  ? -2.484  0.247   3.348   1.00 7.57   ? 94  HIS A CD2 1 
ATOM   806  C  CE1 . HIS A 1 94  ? -2.210  2.180   2.348   1.00 7.90   ? 94  HIS A CE1 1 
ATOM   807  N  NE2 . HIS A 1 94  ? -2.696  0.926   2.155   1.00 7.56   ? 94  HIS A NE2 1 
ATOM   808  N  N   . PHE A 1 95  ? -0.476  -1.975  5.220   1.00 7.87   ? 95  PHE A N   1 
ATOM   809  C  CA  . PHE A 1 95  ? -0.536  -3.265  4.533   1.00 8.03   ? 95  PHE A CA  1 
ATOM   810  C  C   . PHE A 1 95  ? -1.994  -3.688  4.367   1.00 7.84   ? 95  PHE A C   1 
ATOM   811  O  O   . PHE A 1 95  ? -2.896  -3.220  5.031   1.00 8.93   ? 95  PHE A O   1 
ATOM   812  C  CB  . PHE A 1 95  ? 0.195   -4.356  5.373   1.00 8.35   ? 95  PHE A CB  1 
ATOM   813  C  CG  . PHE A 1 95  ? 1.623   -4.089  5.690   1.00 7.97   ? 95  PHE A CG  1 
ATOM   814  C  CD1 . PHE A 1 95  ? 1.953   -3.231  6.735   1.00 9.26   ? 95  PHE A CD1 1 
ATOM   815  C  CD2 . PHE A 1 95  ? 2.661   -4.708  5.011   1.00 8.60   ? 95  PHE A CD2 1 
ATOM   816  C  CE1 . PHE A 1 95  ? 3.258   -3.022  7.103   1.00 9.94   ? 95  PHE A CE1 1 
ATOM   817  C  CE2 . PHE A 1 95  ? 3.973   -4.508  5.347   1.00 9.65   ? 95  PHE A CE2 1 
ATOM   818  C  CZ  . PHE A 1 95  ? 4.291   -3.647  6.417   1.00 9.43   ? 95  PHE A CZ  1 
ATOM   819  N  N   . HIS A 1 96  ? -2.145  -4.656  3.425   1.00 7.58   ? 96  HIS A N   1 
ATOM   820  C  CA  . HIS A 1 96  ? -3.328  -5.468  3.263   1.00 7.99   ? 96  HIS A CA  1 
ATOM   821  C  C   . HIS A 1 96  ? -2.878  -6.910  3.381   1.00 7.49   ? 96  HIS A C   1 
ATOM   822  O  O   . HIS A 1 96  ? -1.814  -7.274  2.888   1.00 8.22   ? 96  HIS A O   1 
ATOM   823  C  CB  . HIS A 1 96  ? -4.016  -5.257  1.891   1.00 7.99   ? 96  HIS A CB  1 
ATOM   824  C  CG  . HIS A 1 96  ? -4.303  -3.818  1.608   1.00 7.49   ? 96  HIS A CG  1 
ATOM   825  N  ND1 . HIS A 1 96  ? -5.524  -3.249  1.752   1.00 8.39   ? 96  HIS A ND1 1 
ATOM   826  C  CD2 . HIS A 1 96  ? -3.462  -2.789  1.206   1.00 7.27   ? 96  HIS A CD2 1 
ATOM   827  C  CE1 . HIS A 1 96  ? -5.474  -1.941  1.455   1.00 7.79   ? 96  HIS A CE1 1 
ATOM   828  N  NE2 . HIS A 1 96  ? -4.244  -1.645  1.107   1.00 7.37   ? 96  HIS A NE2 1 
ATOM   829  N  N   . TRP A 1 97  ? -3.673  -7.759  4.049   1.00 7.37   ? 97  TRP A N   1 
ATOM   830  C  CA  . TRP A 1 97  ? -3.293  -9.150  4.241   1.00 8.16   ? 97  TRP A CA  1 
ATOM   831  C  C   . TRP A 1 97  ? -4.472  -10.062 4.392   1.00 7.81   ? 97  TRP A C   1 
ATOM   832  O  O   . TRP A 1 97  ? -5.629  -9.620  4.488   1.00 8.68   ? 97  TRP A O   1 
ATOM   833  C  CB  . TRP A 1 97  ? -2.354  -9.248  5.483   1.00 9.15   ? 97  TRP A CB  1 
ATOM   834  C  CG  . TRP A 1 97  ? -3.012  -8.857  6.782   1.00 8.94   ? 97  TRP A CG  1 
ATOM   835  C  CD1 . TRP A 1 97  ? -3.686  -9.698  7.651   1.00 9.21   ? 97  TRP A CD1 1 
ATOM   836  C  CD2 . TRP A 1 97  ? -3.034  -7.559  7.367   1.00 8.83   ? 97  TRP A CD2 1 
ATOM   837  N  NE1 . TRP A 1 97  ? -4.090  -8.983  8.742   1.00 10.91  ? 97  TRP A NE1 1 
ATOM   838  C  CE2 . TRP A 1 97  ? -3.770  -7.658  8.589   1.00 9.80   ? 97  TRP A CE2 1 
ATOM   839  C  CE3 . TRP A 1 97  ? -2.575  -6.300  6.946   1.00 8.77   ? 97  TRP A CE3 1 
ATOM   840  C  CZ2 . TRP A 1 97  ? -3.933  -6.572  9.450   1.00 10.09  ? 97  TRP A CZ2 1 
ATOM   841  C  CZ3 . TRP A 1 97  ? -2.795  -5.218  7.782   1.00 9.80   ? 97  TRP A CZ3 1 
ATOM   842  C  CH2 . TRP A 1 97  ? -3.448  -5.363  9.015   1.00 10.63  ? 97  TRP A CH2 1 
ATOM   843  N  N   . GLY A 1 98  ? -4.188  -11.350 4.389   1.00 8.77   ? 98  GLY A N   1 
ATOM   844  C  CA  . GLY A 1 98  ? -5.234  -12.349 4.359   1.00 8.91   ? 98  GLY A CA  1 
ATOM   845  C  C   . GLY A 1 98  ? -5.399  -13.057 5.656   1.00 9.08   ? 98  GLY A C   1 
ATOM   846  O  O   . GLY A 1 98  ? -4.668  -12.909 6.626   1.00 10.43  ? 98  GLY A O   1 
ATOM   847  N  N   . SER A 1 99  ? -6.429  -13.931 5.660   1.00 10.19  ? 99  SER A N   1 
ATOM   848  C  CA  . SER A 1 99  ? -6.667  -14.874 6.756   1.00 11.10  ? 99  SER A CA  1 
ATOM   849  C  C   . SER A 1 99  ? -5.797  -16.108 6.653   1.00 11.45  ? 99  SER A C   1 
ATOM   850  O  O   . SER A 1 99  ? -5.675  -16.855 7.630   1.00 14.14  ? 99  SER A O   1 
ATOM   851  C  CB  . SER A 1 99  ? -8.109  -15.214 6.826   1.00 12.16  ? 99  SER A CB  1 
ATOM   852  O  OG  . SER A 1 99  ? -8.580  -15.743 5.577   1.00 12.99  ? 99  SER A OG  1 
ATOM   853  N  N   . LEU A 1 100 ? -5.191  -16.338 5.494   1.00 11.08  ? 100 LEU A N   1 
ATOM   854  C  CA  . LEU A 1 100 ? -4.401  -17.514 5.117   1.00 12.30  ? 100 LEU A CA  1 
ATOM   855  C  C   . LEU A 1 100 ? -3.294  -17.024 4.275   1.00 11.03  ? 100 LEU A C   1 
ATOM   856  O  O   . LEU A 1 100 ? -3.452  -15.995 3.595   1.00 11.36  ? 100 LEU A O   1 
ATOM   857  C  CB  . LEU A 1 100 ? -5.239  -18.455 4.222   1.00 18.45  ? 100 LEU A CB  1 
ATOM   858  C  CG  . LEU A 1 100 ? -6.577  -18.839 4.805   1.00 18.19  ? 100 LEU A CG  1 
ATOM   859  C  CD1 . LEU A 1 100 ? -7.540  -19.371 3.760   1.00 24.55  ? 100 LEU A CD1 1 
ATOM   860  C  CD2 . LEU A 1 100 ? -6.227  -19.902 5.839   1.00 25.38  ? 100 LEU A CD2 1 
ATOM   861  N  N   . ASP A 1 101 ? -2.200  -17.768 4.217   1.00 11.80  ? 101 ASP A N   1 
ATOM   862  C  CA  . ASP A 1 101 ? -1.021  -17.299 3.462   1.00 11.36  ? 101 ASP A CA  1 
ATOM   863  C  C   . ASP A 1 101 ? -1.295  -17.200 1.970   1.00 10.92  ? 101 ASP A C   1 
ATOM   864  O  O   . ASP A 1 101 ? -0.629  -16.479 1.283   1.00 12.68  ? 101 ASP A O   1 
ATOM   865  C  CB  . ASP A 1 101 ? 0.189   -18.193 3.689   1.00 11.51  ? 101 ASP A CB  1 
ATOM   866  C  CG  . ASP A 1 101 ? 0.687   -18.261 5.113   1.00 12.90  ? 101 ASP A CG  1 
ATOM   867  O  OD1 . ASP A 1 101 ? 0.367   -17.403 5.948   1.00 13.59  ? 101 ASP A OD1 1 
ATOM   868  O  OD2 . ASP A 1 101 ? 1.519   -19.147 5.338   1.00 16.47  ? 101 ASP A OD2 1 
ATOM   869  N  N   . GLY A 1 102 ? -2.280  -17.979 1.514   1.00 11.65  ? 102 GLY A N   1 
ATOM   870  C  CA  . GLY A 1 102 ? -2.595  -17.990 0.079   1.00 12.85  ? 102 GLY A CA  1 
ATOM   871  C  C   . GLY A 1 102 ? -3.428  -16.806 -0.463  1.00 10.57  ? 102 GLY A C   1 
ATOM   872  O  O   . GLY A 1 102 ? -3.744  -16.800 -1.660  1.00 12.13  ? 102 GLY A O   1 
ATOM   873  N  N   . GLN A 1 103 ? -3.721  -15.801 0.339   1.00 9.83   ? 103 GLN A N   1 
ATOM   874  C  CA  . GLN A 1 103 ? -4.399  -14.608 -0.155  1.00 9.30   ? 103 GLN A CA  1 
ATOM   875  C  C   . GLN A 1 103 ? -4.024  -13.460 0.740   1.00 8.52   ? 103 GLN A C   1 
ATOM   876  O  O   . GLN A 1 103 ? -3.469  -13.653 1.833   1.00 9.64   ? 103 GLN A O   1 
ATOM   877  C  CB  . GLN A 1 103 ? -5.907  -14.826 -0.155  1.00 10.19  ? 103 GLN A CB  1 
ATOM   878  C  CG  . GLN A 1 103 ? -6.479  -15.044 1.259   1.00 11.44  ? 103 GLN A CG  1 
ATOM   879  C  CD  . GLN A 1 103 ? -7.885  -15.636 1.192   1.00 13.32  ? 103 GLN A CD  1 
ATOM   880  O  OE1 . GLN A 1 103 ? -8.115  -16.528 0.385   1.00 23.50  ? 103 GLN A OE1 1 
ATOM   881  N  NE2 . GLN A 1 103 ? -8.789  -15.173 1.986   1.00 12.71  ? 103 GLN A NE2 1 
ATOM   882  N  N   . GLY A 1 104 ? -4.324  -12.260 0.266   1.00 7.92   ? 104 GLY A N   1 
ATOM   883  C  CA  . GLY A 1 104 ? -4.048  -11.063 1.047   1.00 8.39   ? 104 GLY A CA  1 
ATOM   884  C  C   . GLY A 1 104 ? -3.609  -9.864  0.201   1.00 7.62   ? 104 GLY A C   1 
ATOM   885  O  O   . GLY A 1 104 ? -3.874  -8.737  0.571   1.00 8.21   ? 104 GLY A O   1 
ATOM   886  N  N   . SER A 1 105 ? -2.904  -10.124 -0.905  1.00 7.21   ? 105 SER A N   1 
ATOM   887  C  CA  . SER A 1 105 ? -2.525  -9.015  -1.780  1.00 7.36   ? 105 SER A CA  1 
ATOM   888  C  C   . SER A 1 105 ? -3.716  -8.460  -2.535  1.00 6.75   ? 105 SER A C   1 
ATOM   889  O  O   . SER A 1 105 ? -4.746  -9.136  -2.723  1.00 7.58   ? 105 SER A O   1 
ATOM   890  C  CB  . SER A 1 105 ? -1.376  -9.376  -2.710  1.00 7.53   ? 105 SER A CB  1 
ATOM   891  O  OG  . SER A 1 105 ? -1.752  -10.338 -3.678  1.00 7.66   ? 105 SER A OG  1 
ATOM   892  N  N   . GLU A 1 106 ? -3.585  -7.208  -2.912  1.00 6.76   ? 106 GLU A N   1 
ATOM   893  C  CA  . GLU A 1 106 ? -4.610  -6.513  -3.718  1.00 7.12   ? 106 GLU A CA  1 
ATOM   894  C  C   . GLU A 1 106 ? -4.274  -6.700  -5.226  1.00 6.60   ? 106 GLU A C   1 
ATOM   895  O  O   . GLU A 1 106 ? -5.069  -7.276  -5.977  1.00 7.47   ? 106 GLU A O   1 
ATOM   896  C  CB  . GLU A 1 106 ? -4.665  -5.048  -3.304  1.00 6.74   ? 106 GLU A CB  1 
ATOM   897  C  CG  . GLU A 1 106 ? -5.129  -4.902  -1.889  1.00 9.30   ? 106 GLU A CG  1 
ATOM   898  C  CD  . GLU A 1 106 ? -5.833  -3.619  -1.597  1.00 7.67   ? 106 GLU A CD  1 
ATOM   899  O  OE1 . GLU A 1 106 ? -5.187  -2.554  -1.852  1.00 7.77   ? 106 GLU A OE1 1 
ATOM   900  O  OE2 . GLU A 1 106 ? -6.991  -3.664  -1.125  1.00 8.77   ? 106 GLU A OE2 1 
ATOM   901  N  N   . HIS A 1 107 ? -3.103  -6.230  -5.632  1.00 6.30   ? 107 HIS A N   1 
ATOM   902  C  CA  . HIS A 1 107 ? -2.628  -6.636  -6.943  1.00 6.28   ? 107 HIS A CA  1 
ATOM   903  C  C   . HIS A 1 107 ? -2.333  -8.127  -6.949  1.00 6.31   ? 107 HIS A C   1 
ATOM   904  O  O   . HIS A 1 107 ? -1.979  -8.726  -5.933  1.00 7.04   ? 107 HIS A O   1 
ATOM   905  C  CB  . HIS A 1 107 ? -1.375  -5.843  -7.324  1.00 6.72   ? 107 HIS A CB  1 
ATOM   906  C  CG  . HIS A 1 107 ? -1.696  -4.379  -7.489  1.00 6.15   ? 107 HIS A CG  1 
ATOM   907  N  ND1 . HIS A 1 107 ? -1.639  -3.490  -6.426  1.00 6.59   ? 107 HIS A ND1 1 
ATOM   908  C  CD2 . HIS A 1 107 ? -2.164  -3.648  -8.555  1.00 6.33   ? 107 HIS A CD2 1 
ATOM   909  C  CE1 . HIS A 1 107 ? -2.074  -2.276  -6.882  1.00 7.13   ? 107 HIS A CE1 1 
ATOM   910  N  NE2 . HIS A 1 107 ? -2.398  -2.370  -8.175  1.00 6.72   ? 107 HIS A NE2 1 
ATOM   911  N  N   . THR A 1 108 ? -2.453  -8.697  -8.135  1.00 7.16   ? 108 THR A N   1 
ATOM   912  C  CA  . THR A 1 108 ? -2.097  -10.070 -8.394  1.00 7.57   ? 108 THR A CA  1 
ATOM   913  C  C   . THR A 1 108 ? -1.138  -10.073 -9.619  1.00 7.30   ? 108 THR A C   1 
ATOM   914  O  O   . THR A 1 108 ? -1.105  -9.111  -10.386 1.00 7.78   ? 108 THR A O   1 
ATOM   915  C  CB  . THR A 1 108 ? -3.302  -10.984 -8.615  1.00 8.22   ? 108 THR A CB  1 
ATOM   916  O  OG1 . THR A 1 108 ? -4.138  -10.492 -9.647  1.00 8.24   ? 108 THR A OG1 1 
ATOM   917  C  CG2 . THR A 1 108 ? -4.142  -11.047 -7.305  1.00 8.61   ? 108 THR A CG2 1 
ATOM   918  N  N   . VAL A 1 109 ? -0.369  -11.166 -9.753  1.00 8.05   ? 109 VAL A N   1 
ATOM   919  C  CA  . VAL A 1 109 ? 0.630   -11.248 -10.836 1.00 8.38   ? 109 VAL A CA  1 
ATOM   920  C  C   . VAL A 1 109 ? 0.304   -12.559 -11.579 1.00 8.79   ? 109 VAL A C   1 
ATOM   921  O  O   . VAL A 1 109 ? 0.480   -13.638 -11.009 1.00 9.10   ? 109 VAL A O   1 
ATOM   922  C  CB  . VAL A 1 109 ? 2.055   -11.258 -10.261 1.00 9.36   ? 109 VAL A CB  1 
ATOM   923  C  CG1 . VAL A 1 109 ? 3.055   -11.382 -11.417 1.00 11.04  ? 109 VAL A CG1 1 
ATOM   924  C  CG2 . VAL A 1 109 ? 2.314   -9.985  -9.470  1.00 9.96   ? 109 VAL A CG2 1 
ATOM   925  N  N   . ASP A 1 110 ? -0.220  -12.423 -12.800 1.00 9.15   ? 110 ASP A N   1 
ATOM   926  C  CA  . ASP A 1 110 ? -0.699  -13.634 -13.534 1.00 11.15  ? 110 ASP A CA  1 
ATOM   927  C  C   . ASP A 1 110 ? -1.627  -14.465 -12.622 1.00 10.00  ? 110 ASP A C   1 
ATOM   928  O  O   . ASP A 1 110 ? -1.543  -15.682 -12.566 1.00 11.02  ? 110 ASP A O   1 
ATOM   929  C  CB  . ASP A 1 110 ? 0.507   -14.478 -14.019 1.00 12.45  ? 110 ASP A CB  1 
ATOM   930  C  CG  . ASP A 1 110 ? 1.359   -13.709 -15.029 1.00 13.08  ? 110 ASP A CG  1 
ATOM   931  O  OD1 . ASP A 1 110 ? 0.788   -12.844 -15.727 1.00 14.24  ? 110 ASP A OD1 1 
ATOM   932  O  OD2 . ASP A 1 110 ? 2.559   -14.017 -15.119 1.00 16.23  ? 110 ASP A OD2 1 
ATOM   933  N  N   . LYS A 1 111 ? -2.497  -13.721 -11.920 1.00 8.81   ? 111 LYS A N   1 
ATOM   934  C  CA  . LYS A 1 111 ? -3.539  -14.257 -11.021 1.00 9.58   ? 111 LYS A CA  1 
ATOM   935  C  C   . LYS A 1 111 ? -2.946  -14.755 -9.678  1.00 9.66   ? 111 LYS A C   1 
ATOM   936  O  O   . LYS A 1 111 ? -3.733  -15.145 -8.826  1.00 11.21  ? 111 LYS A O   1 
ATOM   937  C  CB  . LYS A 1 111 ? -4.465  -15.309 -11.656 1.00 12.23  ? 111 LYS A CB  1 
ATOM   938  C  CG  . LYS A 1 111 ? -5.179  -14.778 -12.904 1.00 16.29  ? 111 LYS A CG  1 
ATOM   939  C  CD  . LYS A 1 111 ? -6.102  -13.564 -12.609 1.00 17.83  ? 111 LYS A CD  1 
ATOM   940  C  CE  . LYS A 1 111 ? -6.879  -12.999 -13.782 1.00 22.18  ? 111 LYS A CE  1 
ATOM   941  N  NZ  . LYS A 1 111 ? -8.091  -13.765 -13.958 1.00 21.36  ? 111 LYS A NZ  1 
ATOM   942  N  N   . LYS A 1 112 ? -1.646  -14.726 -9.496  1.00 9.29   ? 112 LYS A N   1 
ATOM   943  C  CA  . LYS A 1 112 ? -1.072  -15.131 -8.198  1.00 9.25   ? 112 LYS A CA  1 
ATOM   944  C  C   . LYS A 1 112 ? -1.408  -14.099 -7.151  1.00 8.25   ? 112 LYS A C   1 
ATOM   945  O  O   . LYS A 1 112 ? -1.147  -12.906 -7.358  1.00 8.65   ? 112 LYS A O   1 
ATOM   946  C  CB  . LYS A 1 112 ? 0.459   -15.212 -8.292  1.00 11.01  ? 112 LYS A CB  1 
ATOM   947  C  CG  . LYS A 1 112 ? 1.184   -15.598 -7.009  1.00 11.32  ? 112 LYS A CG  1 
ATOM   948  C  CD  . LYS A 1 112 ? 2.678   -15.541 -7.106  1.00 14.23  ? 112 LYS A CD  1 
ATOM   949  C  CE  . LYS A 1 112 ? 3.317   -15.738 -5.783  1.00 15.67  ? 112 LYS A CE  1 
ATOM   950  N  NZ  . LYS A 1 112 ? 3.109   -17.068 -5.277  1.00 15.82  ? 112 LYS A NZ  1 
ATOM   951  N  N   A LYS A 1 113 ? -1.932  -14.575 -6.025  0.50 8.63   ? 113 LYS A N   1 
ATOM   952  N  N   B LYS A 1 113 ? -1.937  -14.563 -6.017  0.50 8.77   ? 113 LYS A N   1 
ATOM   953  C  CA  A LYS A 1 113 ? -2.104  -13.787 -4.815  0.50 8.64   ? 113 LYS A CA  1 
ATOM   954  C  CA  B LYS A 1 113 ? -2.151  -13.760 -4.802  0.50 8.51   ? 113 LYS A CA  1 
ATOM   955  C  C   A LYS A 1 113 ? -0.896  -14.010 -3.907  0.50 8.55   ? 113 LYS A C   1 
ATOM   956  C  C   B LYS A 1 113 ? -1.059  -13.997 -3.771  0.50 8.57   ? 113 LYS A C   1 
ATOM   957  O  O   A LYS A 1 113 ? -0.430  -15.147 -3.714  0.50 9.00   ? 113 LYS A O   1 
ATOM   958  O  O   B LYS A 1 113 ? -0.830  -15.145 -3.385  0.50 9.12   ? 113 LYS A O   1 
ATOM   959  C  CB  A LYS A 1 113 ? -3.384  -14.188 -4.093  0.50 8.79   ? 113 LYS A CB  1 
ATOM   960  C  CB  B LYS A 1 113 ? -3.473  -14.122 -4.170  0.50 9.70   ? 113 LYS A CB  1 
ATOM   961  C  CG  A LYS A 1 113 ? -4.711  -13.872 -4.821  0.50 9.44   ? 113 LYS A CG  1 
ATOM   962  C  CG  B LYS A 1 113 ? -4.673  -13.879 -5.086  0.50 11.09  ? 113 LYS A CG  1 
ATOM   963  C  CD  A LYS A 1 113 ? -5.896  -14.590 -4.150  0.50 10.47  ? 113 LYS A CD  1 
ATOM   964  C  CD  B LYS A 1 113 ? -5.945  -14.320 -4.395  0.50 11.42  ? 113 LYS A CD  1 
ATOM   965  C  CE  A LYS A 1 113 ? -7.221  -14.047 -4.680  0.50 11.31  ? 113 LYS A CE  1 
ATOM   966  C  CE  B LYS A 1 113 ? -7.127  -13.706 -5.135  0.50 14.38  ? 113 LYS A CE  1 
ATOM   967  N  NZ  A LYS A 1 113 ? -7.554  -14.546 -6.048  0.50 12.81  ? 113 LYS A NZ  1 
ATOM   968  N  NZ  B LYS A 1 113 ? -8.379  -14.439 -4.813  0.50 16.93  ? 113 LYS A NZ  1 
ATOM   969  N  N   . TYR A 1 114 ? -0.425  -12.914 -3.341  1.00 8.00   ? 114 TYR A N   1 
ATOM   970  C  CA  . TYR A 1 114 ? 0.593   -12.947 -2.304  1.00 8.22   ? 114 TYR A CA  1 
ATOM   971  C  C   . TYR A 1 114 ? -0.102  -12.909 -0.921  1.00 7.34   ? 114 TYR A C   1 
ATOM   972  O  O   . TYR A 1 114 ? -1.288  -12.617 -0.798  1.00 8.06   ? 114 TYR A O   1 
ATOM   973  C  CB  . TYR A 1 114 ? 1.630   -11.863 -2.449  1.00 8.12   ? 114 TYR A CB  1 
ATOM   974  C  CG  . TYR A 1 114 ? 2.597   -12.078 -3.586  1.00 8.52   ? 114 TYR A CG  1 
ATOM   975  C  CD1 . TYR A 1 114 ? 2.308   -11.641 -4.871  1.00 9.55   ? 114 TYR A CD1 1 
ATOM   976  C  CD2 . TYR A 1 114 ? 3.811   -12.698 -3.366  1.00 9.74   ? 114 TYR A CD2 1 
ATOM   977  C  CE1 . TYR A 1 114 ? 3.199   -11.830 -5.908  1.00 10.96  ? 114 TYR A CE1 1 
ATOM   978  C  CE2 . TYR A 1 114 ? 4.712   -12.892 -4.394  1.00 11.84  ? 114 TYR A CE2 1 
ATOM   979  C  CZ  . TYR A 1 114 ? 4.399   -12.451 -5.666  1.00 11.69  ? 114 TYR A CZ  1 
ATOM   980  O  OH  . TYR A 1 114 ? 5.266   -12.619 -6.724  1.00 18.12  ? 114 TYR A OH  1 
ATOM   981  N  N   . ALA A 1 115 ? 0.685   -13.235 0.117   1.00 8.43   ? 115 ALA A N   1 
ATOM   982  C  CA  . ALA A 1 115 ? 0.141   -13.247 1.486   1.00 8.39   ? 115 ALA A CA  1 
ATOM   983  C  C   . ALA A 1 115 ? -0.242  -11.840 1.975   1.00 8.10   ? 115 ALA A C   1 
ATOM   984  O  O   . ALA A 1 115 ? -1.103  -11.700 2.864   1.00 8.96   ? 115 ALA A O   1 
ATOM   985  C  CB  . ALA A 1 115 ? 1.184   -13.844 2.433   1.00 9.64   ? 115 ALA A CB  1 
ATOM   986  N  N   . ALA A 1 116 ? 0.426   -10.811 1.445   1.00 7.84   ? 116 ALA A N   1 
ATOM   987  C  CA  . ALA A 1 116 ? 0.109   -9.447  1.901   1.00 8.11   ? 116 ALA A CA  1 
ATOM   988  C  C   . ALA A 1 116 ? 0.722   -8.511  0.867   1.00 7.06   ? 116 ALA A C   1 
ATOM   989  O  O   . ALA A 1 116 ? 1.456   -8.912  -0.039  1.00 7.78   ? 116 ALA A O   1 
ATOM   990  C  CB  . ALA A 1 116 ? 0.686   -9.186  3.304   1.00 9.31   ? 116 ALA A CB  1 
ATOM   991  N  N   . GLU A 1 117 ? 0.387   -7.218  1.033   1.00 7.26   ? 117 GLU A N   1 
ATOM   992  C  CA  . GLU A 1 117 ? 0.921   -6.188  0.163   1.00 6.65   ? 117 GLU A CA  1 
ATOM   993  C  C   . GLU A 1 117 ? 1.112   -4.913  0.981   1.00 7.03   ? 117 GLU A C   1 
ATOM   994  O  O   . GLU A 1 117 ? 0.172   -4.488  1.705   1.00 8.15   ? 117 GLU A O   1 
ATOM   995  C  CB  . GLU A 1 117 ? -0.073  -5.954  -1.027  1.00 7.44   ? 117 GLU A CB  1 
ATOM   996  C  CG  . GLU A 1 117 ? 0.463   -5.026  -2.121  1.00 7.92   ? 117 GLU A CG  1 
ATOM   997  C  CD  . GLU A 1 117 ? -0.477  -4.932  -3.316  1.00 6.70   ? 117 GLU A CD  1 
ATOM   998  O  OE1 . GLU A 1 117 ? -1.137  -5.952  -3.592  1.00 7.78   ? 117 GLU A OE1 1 
ATOM   999  O  OE2 . GLU A 1 117 ? -0.513  -3.853  -3.965  1.00 7.82   ? 117 GLU A OE2 1 
ATOM   1000 N  N   . LEU A 1 118 ? 2.305   -4.337  0.872   1.00 7.35   ? 118 LEU A N   1 
ATOM   1001 C  CA  . LEU A 1 118 ? 2.665   -3.103  1.539   1.00 7.02   ? 118 LEU A CA  1 
ATOM   1002 C  C   . LEU A 1 118 ? 2.431   -1.945  0.533   1.00 6.84   ? 118 LEU A C   1 
ATOM   1003 O  O   . LEU A 1 118 ? 2.855   -2.037  -0.630  1.00 7.14   ? 118 LEU A O   1 
ATOM   1004 C  CB  . LEU A 1 118 ? 4.158   -3.177  1.853   1.00 8.29   ? 118 LEU A CB  1 
ATOM   1005 C  CG  . LEU A 1 118 ? 4.904   -1.897  2.254   1.00 8.54   ? 118 LEU A CG  1 
ATOM   1006 C  CD1 . LEU A 1 118 ? 4.312   -1.244  3.463   1.00 9.63   ? 118 LEU A CD1 1 
ATOM   1007 C  CD2 . LEU A 1 118 ? 6.382   -2.262  2.472   1.00 10.21  ? 118 LEU A CD2 1 
ATOM   1008 N  N   . HIS A 1 119 ? 1.808   -0.888  1.034   1.00 6.74   ? 119 HIS A N   1 
ATOM   1009 C  CA  . HIS A 1 119 ? 1.556   0.322   0.241   1.00 6.77   ? 119 HIS A CA  1 
ATOM   1010 C  C   . HIS A 1 119 ? 2.251   1.495   0.930   1.00 6.91   ? 119 HIS A C   1 
ATOM   1011 O  O   . HIS A 1 119 ? 1.872   1.859   2.072   1.00 7.89   ? 119 HIS A O   1 
ATOM   1012 C  CB  . HIS A 1 119 ? 0.070   0.604   0.144   1.00 7.14   ? 119 HIS A CB  1 
ATOM   1013 C  CG  . HIS A 1 119 ? -0.630  -0.351  -0.742  1.00 6.45   ? 119 HIS A CG  1 
ATOM   1014 N  ND1 . HIS A 1 119 ? -1.995  -0.554  -0.734  1.00 6.53   ? 119 HIS A ND1 1 
ATOM   1015 C  CD2 . HIS A 1 119 ? -0.074  -1.193  -1.689  1.00 7.03   ? 119 HIS A CD2 1 
ATOM   1016 C  CE1 . HIS A 1 119 ? -2.254  -1.492  -1.630  1.00 6.81   ? 119 HIS A CE1 1 
ATOM   1017 N  NE2 . HIS A 1 119 ? -1.142  -1.884  -2.227  1.00 7.02   ? 119 HIS A NE2 1 
ATOM   1018 N  N   . LEU A 1 120 ? 3.242   2.085   0.268   1.00 6.72   ? 120 LEU A N   1 
ATOM   1019 C  CA  . LEU A 1 120 ? 3.888   3.338   0.720   1.00 7.56   ? 120 LEU A CA  1 
ATOM   1020 C  C   . LEU A 1 120 ? 3.266   4.457   -0.063  1.00 6.60   ? 120 LEU A C   1 
ATOM   1021 O  O   . LEU A 1 120 ? 3.393   4.492   -1.291  1.00 7.00   ? 120 LEU A O   1 
ATOM   1022 C  CB  . LEU A 1 120 ? 5.394   3.234   0.521   1.00 8.55   ? 120 LEU A CB  1 
ATOM   1023 C  CG  . LEU A 1 120 ? 6.091   2.141   1.396   1.00 9.50   ? 120 LEU A CG  1 
ATOM   1024 C  CD1 . LEU A 1 120 ? 6.955   1.272   0.509   1.00 13.80  ? 120 LEU A CD1 1 
ATOM   1025 C  CD2 . LEU A 1 120 ? 6.929   2.828   2.476   1.00 11.80  ? 120 LEU A CD2 1 
ATOM   1026 N  N   . VAL A 1 121 ? 2.558   5.322   0.627   1.00 7.35   ? 121 VAL A N   1 
ATOM   1027 C  CA  . VAL A 1 121 ? 1.733   6.348   -0.001  1.00 8.03   ? 121 VAL A CA  1 
ATOM   1028 C  C   . VAL A 1 121 ? 2.472   7.699   -0.021  1.00 7.85   ? 121 VAL A C   1 
ATOM   1029 O  O   . VAL A 1 121 ? 2.910   8.156   1.055   1.00 8.36   ? 121 VAL A O   1 
ATOM   1030 C  CB  . VAL A 1 121 ? 0.373   6.498   0.762   1.00 8.89   ? 121 VAL A CB  1 
ATOM   1031 C  CG1 . VAL A 1 121 ? -0.478  7.590   0.120   1.00 10.03  ? 121 VAL A CG1 1 
ATOM   1032 C  CG2 . VAL A 1 121 ? -0.360  5.137   0.860   1.00 9.03   ? 121 VAL A CG2 1 
ATOM   1033 N  N   . HIS A 1 122 ? 2.534   8.315   -1.196  1.00 7.60   ? 122 HIS A N   1 
ATOM   1034 C  CA  . HIS A 1 122 ? 3.220   9.575   -1.394  1.00 7.86   ? 122 HIS A CA  1 
ATOM   1035 C  C   . HIS A 1 122 ? 2.330   10.571  -2.143  1.00 7.48   ? 122 HIS A C   1 
ATOM   1036 O  O   . HIS A 1 122 ? 1.598   10.150  -3.027  1.00 8.24   ? 122 HIS A O   1 
ATOM   1037 C  CB  . HIS A 1 122 ? 4.515   9.391   -2.215  1.00 8.01   ? 122 HIS A CB  1 
ATOM   1038 C  CG  . HIS A 1 122 ? 5.373   8.242   -1.802  1.00 7.92   ? 122 HIS A CG  1 
ATOM   1039 N  ND1 . HIS A 1 122 ? 5.048   6.946   -2.079  1.00 7.90   ? 122 HIS A ND1 1 
ATOM   1040 C  CD2 . HIS A 1 122 ? 6.594   8.188   -1.166  1.00 9.00   ? 122 HIS A CD2 1 
ATOM   1041 C  CE1 . HIS A 1 122 ? 6.007   6.146   -1.629  1.00 8.34   ? 122 HIS A CE1 1 
ATOM   1042 N  NE2 . HIS A 1 122 ? 7.002   6.868   -1.084  1.00 9.05   ? 122 HIS A NE2 1 
ATOM   1043 N  N   . TRP A 1 123 ? 2.420   11.847  -1.801  1.00 7.46   ? 123 TRP A N   1 
ATOM   1044 C  CA  . TRP A 1 123 ? 1.636   12.856  -2.497  1.00 7.96   ? 123 TRP A CA  1 
ATOM   1045 C  C   . TRP A 1 123 ? 2.515   13.822  -3.235  1.00 7.89   ? 123 TRP A C   1 
ATOM   1046 O  O   . TRP A 1 123 ? 3.650   14.168  -2.842  1.00 8.65   ? 123 TRP A O   1 
ATOM   1047 C  CB  . TRP A 1 123 ? 0.674   13.599  -1.516  1.00 9.11   ? 123 TRP A CB  1 
ATOM   1048 C  CG  . TRP A 1 123 ? 1.330   14.228  -0.339  1.00 9.71   ? 123 TRP A CG  1 
ATOM   1049 C  CD1 . TRP A 1 123 ? 1.567   13.626  0.872   1.00 10.89  ? 123 TRP A CD1 1 
ATOM   1050 C  CD2 . TRP A 1 123 ? 1.843   15.563  -0.227  1.00 10.27  ? 123 TRP A CD2 1 
ATOM   1051 N  NE1 . TRP A 1 123 ? 2.170   14.483  1.743   1.00 11.50  ? 123 TRP A NE1 1 
ATOM   1052 C  CE2 . TRP A 1 123 ? 2.361   15.697  1.118   1.00 11.79  ? 123 TRP A CE2 1 
ATOM   1053 C  CE3 . TRP A 1 123 ? 1.927   16.667  -1.069  1.00 11.96  ? 123 TRP A CE3 1 
ATOM   1054 C  CZ2 . TRP A 1 123 ? 2.975   16.863  1.582   1.00 13.94  ? 123 TRP A CZ2 1 
ATOM   1055 C  CZ3 . TRP A 1 123 ? 2.494   17.826  -0.567  1.00 15.72  ? 123 TRP A CZ3 1 
ATOM   1056 C  CH2 . TRP A 1 123 ? 3.015   17.917  0.722   1.00 14.53  ? 123 TRP A CH2 1 
ATOM   1057 N  N   . ASN A 1 124 ? 1.972   14.298  -4.375  1.00 8.20   ? 124 ASN A N   1 
ATOM   1058 C  CA  . ASN A 1 124 ? 2.708   15.167  -5.268  1.00 8.74   ? 124 ASN A CA  1 
ATOM   1059 C  C   . ASN A 1 124 ? 2.862   16.548  -4.689  1.00 9.34   ? 124 ASN A C   1 
ATOM   1060 O  O   . ASN A 1 124 ? 1.840   17.227  -4.424  1.00 8.89   ? 124 ASN A O   1 
ATOM   1061 C  CB  . ASN A 1 124 ? 1.904   15.228  -6.585  1.00 9.18   ? 124 ASN A CB  1 
ATOM   1062 C  CG  . ASN A 1 124 ? 2.686   15.818  -7.722  1.00 9.32   ? 124 ASN A CG  1 
ATOM   1063 O  OD1 . ASN A 1 124 ? 3.523   16.689  -7.523  1.00 10.55  ? 124 ASN A OD1 1 
ATOM   1064 N  ND2 . ASN A 1 124 ? 2.390   15.365  -8.935  1.00 11.03  ? 124 ASN A ND2 1 
ATOM   1065 N  N   . THR A 1 125 ? 4.121   16.958  -4.503  1.00 9.98   ? 125 THR A N   1 
ATOM   1066 C  CA  . THR A 1 125 ? 4.341   18.230  -3.802  1.00 10.99  ? 125 THR A CA  1 
ATOM   1067 C  C   . THR A 1 125 ? 3.846   19.429  -4.555  1.00 12.32  ? 125 THR A C   1 
ATOM   1068 O  O   . THR A 1 125 ? 3.668   20.480  -3.953  1.00 13.09  ? 125 THR A O   1 
ATOM   1069 C  CB  . THR A 1 125 ? 5.839   18.375  -3.419  1.00 14.16  ? 125 THR A CB  1 
ATOM   1070 O  OG1 . THR A 1 125 ? 6.639   18.351  -4.598  1.00 19.08  ? 125 THR A OG1 1 
ATOM   1071 C  CG2 . THR A 1 125 ? 6.221   17.299  -2.424  1.00 17.08  ? 125 THR A CG2 1 
ATOM   1072 N  N   . LYS A 1 126 ? 3.528   19.268  -5.881  1.00 11.53  ? 127 LYS A N   1 
ATOM   1073 C  CA  . LYS A 1 126 ? 2.998   20.404  -6.623  1.00 13.67  ? 127 LYS A CA  1 
ATOM   1074 C  C   . LYS A 1 126 ? 1.582   20.805  -6.134  1.00 11.79  ? 127 LYS A C   1 
ATOM   1075 O  O   . LYS A 1 126 ? 1.131   21.882  -6.481  1.00 13.57  ? 127 LYS A O   1 
ATOM   1076 C  CB  . LYS A 1 126 ? 3.036   20.146  -8.092  1.00 15.00  ? 127 LYS A CB  1 
ATOM   1077 C  CG  . LYS A 1 126 ? 1.924   19.307  -8.632  1.00 14.09  ? 127 LYS A CG  1 
ATOM   1078 C  CD  . LYS A 1 126 ? 2.362   18.938  -10.043 1.00 18.51  ? 127 LYS A CD  1 
ATOM   1079 C  CE  . LYS A 1 126 ? 1.293   18.423  -10.892 1.00 24.67  ? 127 LYS A CE  1 
ATOM   1080 N  NZ  . LYS A 1 126 ? 1.892   17.905  -12.132 1.00 51.82  ? 127 LYS A NZ  1 
ATOM   1081 N  N   . TYR A 1 127 ? 0.917   19.945  -5.355  1.00 10.44  ? 128 TYR A N   1 
ATOM   1082 C  CA  . TYR A 1 127 ? -0.400  20.246  -4.825  1.00 11.60  ? 128 TYR A CA  1 
ATOM   1083 C  C   . TYR A 1 127 ? -0.382  20.637  -3.379  1.00 10.70  ? 128 TYR A C   1 
ATOM   1084 O  O   . TYR A 1 127 ? -1.493  20.868  -2.805  1.00 11.55  ? 128 TYR A O   1 
ATOM   1085 C  CB  . TYR A 1 127 ? -1.395  19.092  -5.093  1.00 11.39  ? 128 TYR A CB  1 
ATOM   1086 C  CG  . TYR A 1 127 ? -1.508  18.762  -6.538  1.00 10.30  ? 128 TYR A CG  1 
ATOM   1087 C  CD1 . TYR A 1 127 ? -1.872  19.754  -7.463  1.00 12.45  ? 128 TYR A CD1 1 
ATOM   1088 C  CD2 . TYR A 1 127 ? -1.203  17.520  -7.031  1.00 10.43  ? 128 TYR A CD2 1 
ATOM   1089 C  CE1 . TYR A 1 127 ? -1.943  19.466  -8.785  1.00 12.05  ? 128 TYR A CE1 1 
ATOM   1090 C  CE2 . TYR A 1 127 ? -1.288  17.198  -8.366  1.00 10.10  ? 128 TYR A CE2 1 
ATOM   1091 C  CZ  . TYR A 1 127 ? -1.659  18.210  -9.259  1.00 11.35  ? 128 TYR A CZ  1 
ATOM   1092 O  OH  . TYR A 1 127 ? -1.761  17.974  -10.593 1.00 13.19  ? 128 TYR A OH  1 
ATOM   1093 N  N   . GLY A 1 128 ? 0.776   20.729  -2.724  1.00 10.57  ? 129 GLY A N   1 
ATOM   1094 C  CA  . GLY A 1 128 ? 0.859   21.408  -1.429  1.00 12.36  ? 129 GLY A CA  1 
ATOM   1095 C  C   . GLY A 1 128 ? 0.541   20.552  -0.208  1.00 12.43  ? 129 GLY A C   1 
ATOM   1096 O  O   . GLY A 1 128 ? 1.183   20.706  0.833   1.00 14.68  ? 129 GLY A O   1 
ATOM   1097 N  N   . ASP A 1 129 ? -0.481  19.708  -0.278  1.00 12.55  ? 130 ASP A N   1 
ATOM   1098 C  CA  . ASP A 1 129 ? -0.683  18.762  0.771   1.00 14.31  ? 130 ASP A CA  1 
ATOM   1099 C  C   . ASP A 1 129 ? -1.514  17.583  0.248   1.00 13.77  ? 130 ASP A C   1 
ATOM   1100 O  O   . ASP A 1 129 ? -1.981  17.573  -0.915  1.00 14.34  ? 130 ASP A O   1 
ATOM   1101 C  CB  . ASP A 1 129 ? -1.278  19.342  2.026   1.00 16.34  ? 130 ASP A CB  1 
ATOM   1102 C  CG  . ASP A 1 129 ? -2.603  19.816  1.835   1.00 13.63  ? 130 ASP A CG  1 
ATOM   1103 O  OD1 . ASP A 1 129 ? -3.229  19.608  0.772   1.00 21.29  ? 130 ASP A OD1 1 
ATOM   1104 O  OD2 . ASP A 1 129 ? -3.153  20.457  2.784   1.00 18.57  ? 130 ASP A OD2 1 
ATOM   1105 N  N   . PHE A 1 130 ? -1.671  16.562  1.072   1.00 13.39  ? 131 PHE A N   1 
ATOM   1106 C  CA  . PHE A 1 130 ? -2.358  15.323  0.654   1.00 11.50  ? 131 PHE A CA  1 
ATOM   1107 C  C   . PHE A 1 130 ? -3.829  15.545  0.282   1.00 12.30  ? 131 PHE A C   1 
ATOM   1108 O  O   . PHE A 1 130 ? -4.312  14.958  -0.703  1.00 11.71  ? 131 PHE A O   1 
ATOM   1109 C  CB  . PHE A 1 130 ? -2.280  14.312  1.813   1.00 13.97  ? 131 PHE A CB  1 
ATOM   1110 C  CG  . PHE A 1 130 ? -2.959  13.024  1.550   1.00 11.66  ? 131 PHE A CG  1 
ATOM   1111 C  CD1 . PHE A 1 130 ? -2.345  11.996  0.933   1.00 12.58  ? 131 PHE A CD1 1 
ATOM   1112 C  CD2 . PHE A 1 130 ? -4.273  12.841  1.901   1.00 14.23  ? 131 PHE A CD2 1 
ATOM   1113 C  CE1 . PHE A 1 130 ? -2.994  10.811  0.699   1.00 13.53  ? 131 PHE A CE1 1 
ATOM   1114 C  CE2 . PHE A 1 130 ? -4.923  11.652  1.715   1.00 16.16  ? 131 PHE A CE2 1 
ATOM   1115 C  CZ  . PHE A 1 130 ? -4.263  10.630  1.101   1.00 16.53  ? 131 PHE A CZ  1 
ATOM   1116 N  N   . GLY A 1 131 ? -4.555  16.335  1.087   1.00 15.03  ? 132 GLY A N   1 
ATOM   1117 C  CA  . GLY A 1 131 ? -5.966  16.502  0.812   1.00 16.82  ? 132 GLY A CA  1 
ATOM   1118 C  C   . GLY A 1 131 ? -6.242  17.126  -0.555  1.00 16.55  ? 132 GLY A C   1 
ATOM   1119 O  O   . GLY A 1 131 ? -7.270  16.823  -1.186  1.00 17.73  ? 132 GLY A O   1 
ATOM   1120 N  N   . LYS A 1 132 ? -5.432  18.080  -0.973  1.00 14.67  ? 133 LYS A N   1 
ATOM   1121 C  CA  . LYS A 1 132 ? -5.616  18.629  -2.333  1.00 12.95  ? 133 LYS A CA  1 
ATOM   1122 C  C   . LYS A 1 132 ? -5.100  17.639  -3.385  1.00 12.21  ? 133 LYS A C   1 
ATOM   1123 O  O   . LYS A 1 132 ? -5.660  17.553  -4.459  1.00 12.11  ? 133 LYS A O   1 
ATOM   1124 C  CB  . LYS A 1 132 ? -4.879  19.943  -2.420  1.00 13.98  ? 133 LYS A CB  1 
ATOM   1125 C  CG  . LYS A 1 132 ? -5.601  21.072  -1.696  1.00 19.10  ? 133 LYS A CG  1 
ATOM   1126 C  CD  . LYS A 1 132 ? -6.760  21.563  -2.567  1.00 30.94  ? 133 LYS A CD  1 
ATOM   1127 C  CE  . LYS A 1 132 ? -7.446  22.756  -1.980  1.00 31.46  ? 133 LYS A CE  1 
ATOM   1128 N  NZ  . LYS A 1 132 ? -8.692  22.983  -2.785  1.00 49.93  ? 133 LYS A NZ  1 
ATOM   1129 N  N   . ALA A 1 133 ? -3.998  16.940  -3.077  1.00 11.15  ? 134 ALA A N   1 
ATOM   1130 C  CA  . ALA A 1 133 ? -3.444  15.993  -4.046  1.00 10.06  ? 134 ALA A CA  1 
ATOM   1131 C  C   . ALA A 1 133 ? -4.454  14.921  -4.442  1.00 10.06  ? 134 ALA A C   1 
ATOM   1132 O  O   . ALA A 1 133 ? -4.481  14.529  -5.596  1.00 10.03  ? 134 ALA A O   1 
ATOM   1133 C  CB  . ALA A 1 133 ? -2.167  15.369  -3.466  1.00 10.12  ? 134 ALA A CB  1 
ATOM   1134 N  N   . VAL A 1 134 ? -5.263  14.402  -3.504  1.00 10.56  ? 135 VAL A N   1 
ATOM   1135 C  CA  . VAL A 1 134 ? -6.153  13.273  -3.868  1.00 11.73  ? 135 VAL A CA  1 
ATOM   1136 C  C   . VAL A 1 134 ? -7.285  13.713  -4.794  1.00 11.36  ? 135 VAL A C   1 
ATOM   1137 O  O   . VAL A 1 134 ? -7.966  12.832  -5.359  1.00 12.49  ? 135 VAL A O   1 
ATOM   1138 C  CB  . VAL A 1 134 ? -6.787  12.576  -2.680  1.00 11.98  ? 135 VAL A CB  1 
ATOM   1139 C  CG1 . VAL A 1 134 ? -5.746  11.881  -1.842  1.00 15.58  ? 135 VAL A CG1 1 
ATOM   1140 C  CG2 . VAL A 1 134 ? -7.662  13.464  -1.823  1.00 13.38  ? 135 VAL A CG2 1 
ATOM   1141 N  N   . GLN A 1 135 ? -7.434  15.030  -4.987  1.00 11.19  ? 136 GLN A N   1 
ATOM   1142 C  CA  . GLN A 1 135 ? -8.416  15.549  -5.959  1.00 13.74  ? 136 GLN A CA  1 
ATOM   1143 C  C   . GLN A 1 135 ? -7.880  15.638  -7.373  1.00 12.16  ? 136 GLN A C   1 
ATOM   1144 O  O   . GLN A 1 135 ? -8.555  16.193  -8.272  1.00 14.91  ? 136 GLN A O   1 
ATOM   1145 C  CB  . GLN A 1 135 ? -8.929  16.903  -5.403  1.00 14.34  ? 136 GLN A CB  1 
ATOM   1146 C  CG  . GLN A 1 135 ? -9.658  16.770  -4.109  1.00 18.74  ? 136 GLN A CG  1 
ATOM   1147 C  CD  . GLN A 1 135 ? -10.047 18.114  -3.584  1.00 24.53  ? 136 GLN A CD  1 
ATOM   1148 O  OE1 . GLN A 1 135 ? -9.545  18.600  -2.549  1.00 29.58  ? 136 GLN A OE1 1 
ATOM   1149 N  NE2 . GLN A 1 135 ? -10.928 18.770  -4.321  1.00 26.24  ? 136 GLN A NE2 1 
ATOM   1150 N  N   . GLN A 1 136 ? -6.636  15.192  -7.569  1.00 10.35  ? 137 GLN A N   1 
ATOM   1151 C  CA  . GLN A 1 136 ? -5.963  15.365  -8.867  1.00 10.81  ? 137 GLN A CA  1 
ATOM   1152 C  C   . GLN A 1 136 ? -5.595  14.032  -9.460  1.00 9.89   ? 137 GLN A C   1 
ATOM   1153 O  O   . GLN A 1 136 ? -5.231  13.104  -8.750  1.00 9.67   ? 137 GLN A O   1 
ATOM   1154 C  CB  . GLN A 1 136 ? -4.673  16.186  -8.716  1.00 11.23  ? 137 GLN A CB  1 
ATOM   1155 C  CG  . GLN A 1 136 ? -4.746  17.379  -7.814  1.00 16.02  ? 137 GLN A CG  1 
ATOM   1156 C  CD  . GLN A 1 136 ? -5.713  18.304  -8.265  1.00 16.52  ? 137 GLN A CD  1 
ATOM   1157 O  OE1 . GLN A 1 136 ? -5.990  18.473  -9.508  1.00 16.67  ? 137 GLN A OE1 1 
ATOM   1158 N  NE2 . GLN A 1 136 ? -6.304  18.953  -7.249  1.00 20.55  ? 137 GLN A NE2 1 
ATOM   1159 N  N   . PRO A 1 137 ? -5.570  13.927  -10.805 1.00 10.44  ? 138 PRO A N   1 
ATOM   1160 C  CA  . PRO A 1 137 ? -5.343  12.593  -11.442 1.00 11.02  ? 138 PRO A CA  1 
ATOM   1161 C  C   . PRO A 1 137 ? -3.925  12.097  -11.241 1.00 10.37  ? 138 PRO A C   1 
ATOM   1162 O  O   . PRO A 1 137 ? -3.688  10.910  -11.356 1.00 14.20  ? 138 PRO A O   1 
ATOM   1163 C  CB  . PRO A 1 137 ? -5.673  12.808  -12.920 1.00 15.52  ? 138 PRO A CB  1 
ATOM   1164 C  CG  . PRO A 1 137 ? -5.769  14.269  -13.053 1.00 21.46  ? 138 PRO A CG  1 
ATOM   1165 C  CD  . PRO A 1 137 ? -6.094  14.909  -11.774 1.00 15.15  ? 138 PRO A CD  1 
ATOM   1166 N  N   . ASP A 1 138 ? -2.989  13.023  -10.965 1.00 9.75   ? 139 ASP A N   1 
ATOM   1167 C  CA  . ASP A 1 138 ? -1.562  12.708  -10.690 1.00 9.79   ? 139 ASP A CA  1 
ATOM   1168 C  C   . ASP A 1 138 ? -1.217  13.131  -9.270  1.00 9.04   ? 139 ASP A C   1 
ATOM   1169 O  O   . ASP A 1 138 ? -0.090  13.535  -8.999  1.00 9.29   ? 139 ASP A O   1 
ATOM   1170 C  CB  . ASP A 1 138 ? -0.629  13.330  -11.707 1.00 11.25  ? 139 ASP A CB  1 
ATOM   1171 C  CG  . ASP A 1 138 ? -0.715  14.816  -11.746 1.00 12.19  ? 139 ASP A CG  1 
ATOM   1172 O  OD1 . ASP A 1 138 ? -1.654  15.429  -11.156 1.00 12.23  ? 139 ASP A OD1 1 
ATOM   1173 O  OD2 . ASP A 1 138 ? 0.142   15.413  -12.435 1.00 15.11  ? 139 ASP A OD2 1 
ATOM   1174 N  N   . GLY A 1 139 ? -2.191  13.010  -8.348  1.00 7.92   ? 140 GLY A N   1 
ATOM   1175 C  CA  . GLY A 1 139 ? -1.927  13.476  -7.009  1.00 8.28   ? 140 GLY A CA  1 
ATOM   1176 C  C   . GLY A 1 139 ? -1.091  12.566  -6.126  1.00 7.43   ? 140 GLY A C   1 
ATOM   1177 O  O   . GLY A 1 139 ? -0.388  13.077  -5.249  1.00 8.11   ? 140 GLY A O   1 
ATOM   1178 N  N   . LEU A 1 140 ? -1.208  11.254  -6.300  1.00 7.12   ? 141 LEU A N   1 
ATOM   1179 C  CA  . LEU A 1 140 ? -0.535  10.303  -5.418  1.00 7.26   ? 141 LEU A CA  1 
ATOM   1180 C  C   . LEU A 1 140 ? 0.330   9.382   -6.243  1.00 6.52   ? 141 LEU A C   1 
ATOM   1181 O  O   . LEU A 1 140 ? 0.048   9.060   -7.411  1.00 7.29   ? 141 LEU A O   1 
ATOM   1182 C  CB  . LEU A 1 140 ? -1.509  9.421   -4.629  1.00 7.83   ? 141 LEU A CB  1 
ATOM   1183 C  CG  . LEU A 1 140 ? -2.393  10.121  -3.610  1.00 9.54   ? 141 LEU A CG  1 
ATOM   1184 C  CD1 . LEU A 1 140 ? -3.153  9.073   -2.812  1.00 9.64   ? 141 LEU A CD1 1 
ATOM   1185 C  CD2 . LEU A 1 140 ? -1.763  11.135  -2.710  1.00 10.64  ? 141 LEU A CD2 1 
ATOM   1186 N  N   . ALA A 1 141 ? 1.370   8.856   -5.593  1.00 7.01   ? 142 ALA A N   1 
ATOM   1187 C  CA  . ALA A 1 141 ? 2.164   7.738   -6.116  1.00 7.32   ? 142 ALA A CA  1 
ATOM   1188 C  C   . ALA A 1 141 ? 2.236   6.741   -4.992  1.00 6.58   ? 142 ALA A C   1 
ATOM   1189 O  O   . ALA A 1 141 ? 2.649   7.080   -3.866  1.00 7.68   ? 142 ALA A O   1 
ATOM   1190 C  CB  . ALA A 1 141 ? 3.570   8.170   -6.551  1.00 8.38   ? 142 ALA A CB  1 
ATOM   1191 N  N   . VAL A 1 142 ? 1.756   5.507   -5.262  1.00 6.68   ? 143 VAL A N   1 
ATOM   1192 C  CA  . VAL A 1 142 ? 1.759   4.453   -4.269  1.00 6.67   ? 143 VAL A CA  1 
ATOM   1193 C  C   . VAL A 1 142 ? 2.709   3.402   -4.728  1.00 6.44   ? 143 VAL A C   1 
ATOM   1194 O  O   . VAL A 1 142 ? 2.583   2.874   -5.836  1.00 7.03   ? 143 VAL A O   1 
ATOM   1195 C  CB  . VAL A 1 142 ? 0.361   3.907   -3.920  1.00 7.27   ? 143 VAL A CB  1 
ATOM   1196 C  CG1 . VAL A 1 142 ? 0.493   2.877   -2.776  1.00 8.47   ? 143 VAL A CG1 1 
ATOM   1197 C  CG2 . VAL A 1 142 ? -0.553  5.034   -3.473  1.00 8.59   ? 143 VAL A CG2 1 
ATOM   1198 N  N   . LEU A 1 143 ? 3.729   3.126   -3.884  1.00 7.11   ? 144 LEU A N   1 
ATOM   1199 C  CA  . LEU A 1 143 ? 4.677   2.065   -4.137  1.00 7.10   ? 144 LEU A CA  1 
ATOM   1200 C  C   . LEU A 1 143 ? 4.146   0.827   -3.444  1.00 7.00   ? 144 LEU A C   1 
ATOM   1201 O  O   . LEU A 1 143 ? 3.984   0.793   -2.200  1.00 7.99   ? 144 LEU A O   1 
ATOM   1202 C  CB  . LEU A 1 143 ? 6.026   2.515   -3.531  1.00 8.60   ? 144 LEU A CB  1 
ATOM   1203 C  CG  . LEU A 1 143 ? 7.202   1.538   -3.710  1.00 9.77   ? 144 LEU A CG  1 
ATOM   1204 C  CD1 . LEU A 1 143 ? 7.424   1.201   -5.171  1.00 11.77  ? 144 LEU A CD1 1 
ATOM   1205 C  CD2 . LEU A 1 143 ? 8.473   2.115   -3.057  1.00 11.73  ? 144 LEU A CD2 1 
ATOM   1206 N  N   . GLY A 1 144 ? 3.869   -0.200  -4.239  1.00 6.66   ? 145 GLY A N   1 
ATOM   1207 C  CA  . GLY A 1 144 ? 3.331   -1.466  -3.737  1.00 7.12   ? 145 GLY A CA  1 
ATOM   1208 C  C   . GLY A 1 144 ? 4.394   -2.533  -3.774  1.00 6.96   ? 145 GLY A C   1 
ATOM   1209 O  O   . GLY A 1 144 ? 5.123   -2.687  -4.743  1.00 7.33   ? 145 GLY A O   1 
ATOM   1210 N  N   . ILE A 1 145 ? 4.466   -3.276  -2.648  1.00 6.68   ? 146 ILE A N   1 
ATOM   1211 C  CA  . ILE A 1 145 ? 5.468   -4.333  -2.471  1.00 7.00   ? 146 ILE A CA  1 
ATOM   1212 C  C   . ILE A 1 145 ? 4.762   -5.573  -1.971  1.00 6.95   ? 146 ILE A C   1 
ATOM   1213 O  O   . ILE A 1 145 ? 4.075   -5.513  -0.936  1.00 7.64   ? 146 ILE A O   1 
ATOM   1214 C  CB  . ILE A 1 145 ? 6.587   -3.844  -1.498  1.00 8.05   ? 146 ILE A CB  1 
ATOM   1215 C  CG1 . ILE A 1 145 ? 7.170   -2.543  -2.011  1.00 9.96   ? 146 ILE A CG1 1 
ATOM   1216 C  CG2 . ILE A 1 145 ? 7.613   -4.965  -1.285  1.00 10.45  ? 146 ILE A CG2 1 
ATOM   1217 C  CD1 . ILE A 1 145 ? 8.270   -1.957  -1.110  1.00 9.57   ? 146 ILE A CD1 1 
ATOM   1218 N  N   . PHE A 1 146 ? 4.945   -6.673  -2.640  1.00 6.89   ? 147 PHE A N   1 
ATOM   1219 C  CA  . PHE A 1 146 ? 4.332   -7.932  -2.224  1.00 7.31   ? 147 PHE A CA  1 
ATOM   1220 C  C   . PHE A 1 146 ? 5.090   -8.547  -1.058  1.00 7.53   ? 147 PHE A C   1 
ATOM   1221 O  O   . PHE A 1 146 ? 6.326   -8.426  -1.010  1.00 8.35   ? 147 PHE A O   1 
ATOM   1222 C  CB  . PHE A 1 146 ? 4.340   -8.912  -3.416  1.00 7.59   ? 147 PHE A CB  1 
ATOM   1223 C  CG  . PHE A 1 146 ? 3.462   -8.453  -4.554  1.00 6.62   ? 147 PHE A CG  1 
ATOM   1224 C  CD1 . PHE A 1 146 ? 2.103   -8.251  -4.371  1.00 7.13   ? 147 PHE A CD1 1 
ATOM   1225 C  CD2 . PHE A 1 146 ? 4.001   -8.200  -5.807  1.00 7.80   ? 147 PHE A CD2 1 
ATOM   1226 C  CE1 . PHE A 1 146 ? 1.262   -7.873  -5.460  1.00 7.72   ? 147 PHE A CE1 1 
ATOM   1227 C  CE2 . PHE A 1 146 ? 3.194   -7.836  -6.875  1.00 8.19   ? 147 PHE A CE2 1 
ATOM   1228 C  CZ  . PHE A 1 146 ? 1.847   -7.662  -6.694  1.00 7.47   ? 147 PHE A CZ  1 
ATOM   1229 N  N   . LEU A 1 147 ? 4.367   -9.266  -0.222  1.00 7.66   ? 148 LEU A N   1 
ATOM   1230 C  CA  . LEU A 1 147 ? 4.953   -10.068 0.875   1.00 8.15   ? 148 LEU A CA  1 
ATOM   1231 C  C   . LEU A 1 147 ? 4.601   -11.535 0.642   1.00 7.70   ? 148 LEU A C   1 
ATOM   1232 O  O   . LEU A 1 147 ? 3.424   -11.871 0.430   1.00 8.20   ? 148 LEU A O   1 
ATOM   1233 C  CB  . LEU A 1 147 ? 4.375   -9.657  2.233   1.00 8.64   ? 148 LEU A CB  1 
ATOM   1234 C  CG  . LEU A 1 147 ? 4.925   -8.422  2.907   1.00 9.94   ? 148 LEU A CG  1 
ATOM   1235 C  CD1 . LEU A 1 147 ? 4.688   -7.148  2.087   1.00 10.43  ? 148 LEU A CD1 1 
ATOM   1236 C  CD2 . LEU A 1 147 ? 4.316   -8.229  4.286   1.00 10.07  ? 148 LEU A CD2 1 
ATOM   1237 N  N   . LYS A 1 148 ? 5.617   -12.376 0.712   1.00 8.29   ? 149 LYS A N   1 
ATOM   1238 C  CA  . LYS A 1 148 ? 5.473   -13.804 0.745   1.00 9.37   ? 149 LYS A CA  1 
ATOM   1239 C  C   . LYS A 1 148 ? 5.969   -14.319 2.090   1.00 9.30   ? 149 LYS A C   1 
ATOM   1240 O  O   . LYS A 1 148 ? 6.788   -13.668 2.753   1.00 11.00  ? 149 LYS A O   1 
ATOM   1241 C  CB  . LYS A 1 148 ? 6.233   -14.474 -0.377  1.00 10.32  ? 149 LYS A CB  1 
ATOM   1242 C  CG  . LYS A 1 148 ? 7.725   -14.383 -0.350  1.00 12.91  ? 149 LYS A CG  1 
ATOM   1243 C  CD  . LYS A 1 148 ? 8.358   -15.069 -1.523  1.00 17.97  ? 149 LYS A CD  1 
ATOM   1244 C  CE  . LYS A 1 148 ? 9.818   -15.321 -1.319  1.00 27.03  ? 149 LYS A CE  1 
ATOM   1245 N  NZ  . LYS A 1 148 ? 10.325  -16.145 -2.450  1.00 41.67  ? 149 LYS A NZ  1 
ATOM   1246 N  N   . VAL A 1 149 ? 5.466   -15.474 2.499   1.00 10.69  ? 150 VAL A N   1 
ATOM   1247 C  CA  . VAL A 1 149 ? 5.858   -16.065 3.779   1.00 10.64  ? 150 VAL A CA  1 
ATOM   1248 C  C   . VAL A 1 149 ? 7.089   -16.983 3.593   1.00 10.65  ? 150 VAL A C   1 
ATOM   1249 O  O   . VAL A 1 149 ? 7.023   -17.952 2.813   1.00 11.89  ? 150 VAL A O   1 
ATOM   1250 C  CB  . VAL A 1 149 ? 4.655   -16.812 4.379   1.00 10.74  ? 150 VAL A CB  1 
ATOM   1251 C  CG1 . VAL A 1 149 ? 5.036   -17.588 5.621   1.00 12.15  ? 150 VAL A CG1 1 
ATOM   1252 C  CG2 . VAL A 1 149 ? 3.569   -15.829 4.721   1.00 11.88  ? 150 VAL A CG2 1 
ATOM   1253 N  N   . GLY A 1 150 ? 8.133   -16.711 4.350   1.00 10.85  ? 151 GLY A N   1 
ATOM   1254 C  CA  . GLY A 1 150 ? 9.344   -17.530 4.303   1.00 12.88  ? 151 GLY A CA  1 
ATOM   1255 C  C   . GLY A 1 150 ? 10.229  -17.072 5.419   1.00 12.09  ? 151 GLY A C   1 
ATOM   1256 O  O   . GLY A 1 150 ? 9.851   -17.157 6.589   1.00 13.10  ? 151 GLY A O   1 
ATOM   1257 N  N   . SER A 1 151 ? 11.405  -16.576 5.032   1.00 13.54  ? 152 SER A N   1 
ATOM   1258 C  CA  . SER A 1 151 ? 12.345  -15.985 6.048   1.00 13.53  ? 152 SER A CA  1 
ATOM   1259 C  C   . SER A 1 151 ? 11.738  -14.727 6.633   1.00 11.99  ? 152 SER A C   1 
ATOM   1260 O  O   . SER A 1 151 ? 10.958  -14.019 5.986   1.00 12.25  ? 152 SER A O   1 
ATOM   1261 C  CB  . SER A 1 151 ? 13.735  -15.829 5.445   1.00 24.09  ? 152 SER A CB  1 
ATOM   1262 O  OG  . SER A 1 151 ? 13.762  -14.770 4.534   1.00 31.38  ? 152 SER A OG  1 
ATOM   1263 N  N   . ALA A 1 152 ? 12.022  -14.418 7.911   1.00 13.68  ? 153 ALA A N   1 
ATOM   1264 C  CA  . ALA A 1 152 ? 11.604  -13.185 8.524   1.00 11.79  ? 153 ALA A CA  1 
ATOM   1265 C  C   . ALA A 1 152 ? 12.279  -11.972 7.827   1.00 12.60  ? 153 ALA A C   1 
ATOM   1266 O  O   . ALA A 1 152 ? 13.403  -12.040 7.325   1.00 14.30  ? 153 ALA A O   1 
ATOM   1267 C  CB  . ALA A 1 152 ? 12.006  -13.173 10.030  1.00 15.92  ? 153 ALA A CB  1 
ATOM   1268 N  N   . LYS A 1 153 ? 11.549  -10.819 7.907   1.00 13.53  ? 154 LYS A N   1 
ATOM   1269 C  CA  . LYS A 1 153 ? 12.052  -9.568  7.410   1.00 13.59  ? 154 LYS A CA  1 
ATOM   1270 C  C   . LYS A 1 153 ? 12.489  -8.804  8.733   1.00 13.04  ? 154 LYS A C   1 
ATOM   1271 O  O   . LYS A 1 153 ? 11.649  -8.343  9.500   1.00 12.95  ? 154 LYS A O   1 
ATOM   1272 C  CB  . LYS A 1 153 ? 11.011  -8.748  6.676   1.00 13.75  ? 154 LYS A CB  1 
ATOM   1273 C  CG  . LYS A 1 153 ? 11.516  -7.568  5.914   1.00 18.25  ? 154 LYS A CG  1 
ATOM   1274 C  CD  . LYS A 1 153 ? 12.371  -7.934  4.746   1.00 18.37  ? 154 LYS A CD  1 
ATOM   1275 C  CE  . LYS A 1 153 ? 12.385  -6.747  3.812   1.00 19.07  ? 154 LYS A CE  1 
ATOM   1276 N  NZ  . LYS A 1 153 ? 13.367  -7.019  2.743   1.00 18.33  ? 154 LYS A NZ  1 
ATOM   1277 N  N   . PRO A 1 154 ? 13.785  -8.691  8.983   1.00 14.32  ? 155 PRO A N   1 
ATOM   1278 C  CA  . PRO A 1 154 ? 14.205  -8.076  10.289  1.00 15.25  ? 155 PRO A CA  1 
ATOM   1279 C  C   . PRO A 1 154 ? 13.705  -6.657  10.441  1.00 14.96  ? 155 PRO A C   1 
ATOM   1280 O  O   . PRO A 1 154 ? 13.310  -6.309  11.547  1.00 17.40  ? 155 PRO A O   1 
ATOM   1281 C  CB  . PRO A 1 154 ? 15.727  -8.144  10.248  1.00 16.30  ? 155 PRO A CB  1 
ATOM   1282 C  CG  . PRO A 1 154 ? 15.996  -9.317  9.278   1.00 19.24  ? 155 PRO A CG  1 
ATOM   1283 C  CD  . PRO A 1 154 ? 14.940  -9.188  8.203   1.00 16.53  ? 155 PRO A CD  1 
ATOM   1284 N  N   . GLY A 1 155 ? 13.629  -5.919  9.336   1.00 14.38  ? 156 GLY A N   1 
ATOM   1285 C  CA  . GLY A 1 155 ? 13.280  -4.537  9.401   1.00 17.81  ? 156 GLY A CA  1 
ATOM   1286 C  C   . GLY A 1 155 ? 11.792  -4.342  9.631   1.00 15.75  ? 156 GLY A C   1 
ATOM   1287 O  O   . GLY A 1 155 ? 11.310  -3.218  9.803   1.00 18.79  ? 156 GLY A O   1 
ATOM   1288 N  N   . LEU A 1 156 ? 11.045  -5.420  9.542   1.00 13.16  ? 157 LEU A N   1 
ATOM   1289 C  CA  . LEU A 1 156 ? 9.625   -5.393  9.876   1.00 13.02  ? 157 LEU A CA  1 
ATOM   1290 C  C   . LEU A 1 156 ? 9.314   -5.580  11.350  1.00 13.48  ? 157 LEU A C   1 
ATOM   1291 O  O   . LEU A 1 156 ? 8.214   -5.277  11.823  1.00 13.37  ? 157 LEU A O   1 
ATOM   1292 C  CB  . LEU A 1 156 ? 8.817   -6.400  9.036   1.00 12.56  ? 157 LEU A CB  1 
ATOM   1293 C  CG  . LEU A 1 156 ? 7.298   -6.518  9.205   1.00 12.91  ? 157 LEU A CG  1 
ATOM   1294 C  CD1 . LEU A 1 156 ? 6.522   -5.258  8.836   1.00 14.98  ? 157 LEU A CD1 1 
ATOM   1295 C  CD2 . LEU A 1 156 ? 6.715   -7.679  8.393   1.00 13.52  ? 157 LEU A CD2 1 
ATOM   1296 N  N   . GLN A 1 157 ? 10.261  -6.154  12.111  1.00 14.25  ? 158 GLN A N   1 
ATOM   1297 C  CA  . GLN A 1 157 ? 9.895   -6.628  13.447  1.00 15.68  ? 158 GLN A CA  1 
ATOM   1298 C  C   . GLN A 1 157 ? 9.480   -5.478  14.383  1.00 14.45  ? 158 GLN A C   1 
ATOM   1299 O  O   . GLN A 1 157 ? 8.641   -5.694  15.202  1.00 14.87  ? 158 GLN A O   1 
ATOM   1300 C  CB  . GLN A 1 157 ? 11.065  -7.427  14.053  1.00 16.81  ? 158 GLN A CB  1 
ATOM   1301 C  CG  . GLN A 1 157 ? 10.616  -8.174  15.330  1.00 17.66  ? 158 GLN A CG  1 
ATOM   1302 C  CD  . GLN A 1 157 ? 9.481   -9.174  15.088  1.00 16.00  ? 158 GLN A CD  1 
ATOM   1303 O  OE1 . GLN A 1 157 ? 9.364   -9.792  13.988  1.00 16.88  ? 158 GLN A OE1 1 
ATOM   1304 N  NE2 . GLN A 1 157 ? 8.677   -9.446  16.140  1.00 18.58  ? 158 GLN A NE2 1 
ATOM   1305 N  N   . LYS A 1 158 ? 10.047  -4.268  14.261  1.00 15.54  ? 159 LYS A N   1 
ATOM   1306 C  CA  . LYS A 1 158 ? 9.652   -3.221  15.145  1.00 14.74  ? 159 LYS A CA  1 
ATOM   1307 C  C   . LYS A 1 158 ? 8.165   -2.865  14.938  1.00 14.29  ? 159 LYS A C   1 
ATOM   1308 O  O   . LYS A 1 158 ? 7.503   -2.500  15.898  1.00 15.41  ? 159 LYS A O   1 
ATOM   1309 C  CB  . LYS A 1 158 ? 10.524  -2.006  14.891  1.00 18.14  ? 159 LYS A CB  1 
ATOM   1310 C  CG  . LYS A 1 158 ? 11.931  -2.100  15.526  1.00 21.61  ? 159 LYS A CG  1 
ATOM   1311 C  CD  . LYS A 1 158 ? 12.293  -0.696  15.959  1.00 34.55  ? 159 LYS A CD  1 
ATOM   1312 C  CE  . LYS A 1 158 ? 11.392  0.398   15.330  1.00 36.98  ? 159 LYS A CE  1 
ATOM   1313 N  N   . VAL A 1 159 ? 7.674   -3.006  13.709  1.00 14.31  ? 160 VAL A N   1 
ATOM   1314 C  CA  . VAL A 1 159 ? 6.229   -2.842  13.460  1.00 13.46  ? 160 VAL A CA  1 
ATOM   1315 C  C   . VAL A 1 159 ? 5.428   -3.941  14.141  1.00 14.10  ? 160 VAL A C   1 
ATOM   1316 O  O   . VAL A 1 159 ? 4.472   -3.700  14.884  1.00 14.56  ? 160 VAL A O   1 
ATOM   1317 C  CB  . VAL A 1 159 ? 5.920   -2.792  11.970  1.00 13.59  ? 160 VAL A CB  1 
ATOM   1318 C  CG1 . VAL A 1 159 ? 4.393   -2.869  11.693  1.00 16.05  ? 160 VAL A CG1 1 
ATOM   1319 C  CG2 . VAL A 1 159 ? 6.567   -1.572  11.349  1.00 16.31  ? 160 VAL A CG2 1 
ATOM   1320 N  N   . VAL A 1 160 ? 5.836   -5.177  13.896  1.00 13.35  ? 161 VAL A N   1 
ATOM   1321 C  CA  . VAL A 1 160 ? 5.108   -6.292  14.464  1.00 14.44  ? 161 VAL A CA  1 
ATOM   1322 C  C   . VAL A 1 160 ? 5.065   -6.197  15.968  1.00 15.52  ? 161 VAL A C   1 
ATOM   1323 O  O   . VAL A 1 160 ? 4.044   -6.477  16.562  1.00 15.95  ? 161 VAL A O   1 
ATOM   1324 C  CB  . VAL A 1 160 ? 5.852   -7.672  14.080  1.00 17.78  ? 161 VAL A CB  1 
ATOM   1325 C  CG1 . VAL A 1 160 ? 5.349   -8.866  14.905  1.00 17.88  ? 161 VAL A CG1 1 
ATOM   1326 C  CG2 . VAL A 1 160 ? 5.692   -7.871  12.576  1.00 17.29  ? 161 VAL A CG2 1 
ATOM   1327 N  N   . ASP A 1 161 ? 6.148   -5.767  16.623  1.00 16.22  ? 162 ASP A N   1 
ATOM   1328 C  CA  . ASP A 1 161 ? 6.166   -5.788  18.067  1.00 18.71  ? 162 ASP A CA  1 
ATOM   1329 C  C   . ASP A 1 161 ? 5.297   -4.724  18.726  1.00 19.12  ? 162 ASP A C   1 
ATOM   1330 O  O   . ASP A 1 161 ? 4.923   -4.870  19.913  1.00 24.74  ? 162 ASP A O   1 
ATOM   1331 C  CB  . ASP A 1 161 ? 7.622   -5.715  18.494  1.00 21.23  ? 162 ASP A CB  1 
ATOM   1332 C  CG  . ASP A 1 161 ? 8.294   -7.096  18.452  1.00 21.21  ? 162 ASP A CG  1 
ATOM   1333 O  OD1 . ASP A 1 161 ? 7.537   -8.118  18.556  1.00 23.32  ? 162 ASP A OD1 1 
ATOM   1334 O  OD2 . ASP A 1 161 ? 9.541   -7.115  18.247  1.00 28.29  ? 162 ASP A OD2 1 
ATOM   1335 N  N   . VAL A 1 162 ? 4.919   -3.663  17.987  1.00 17.00  ? 163 VAL A N   1 
ATOM   1336 C  CA  . VAL A 1 162 ? 4.125   -2.596  18.549  1.00 18.06  ? 163 VAL A CA  1 
ATOM   1337 C  C   . VAL A 1 162 ? 2.623   -2.917  18.404  1.00 16.19  ? 163 VAL A C   1 
ATOM   1338 O  O   . VAL A 1 162 ? 1.778   -2.236  18.948  1.00 17.47  ? 163 VAL A O   1 
ATOM   1339 C  CB  . VAL A 1 162 ? 4.533   -1.208  17.956  1.00 19.60  ? 163 VAL A CB  1 
ATOM   1340 C  CG1 . VAL A 1 162 ? 3.995   -0.977  16.564  1.00 18.89  ? 163 VAL A CG1 1 
ATOM   1341 C  CG2 . VAL A 1 162 ? 4.177   -0.027  18.869  1.00 18.36  ? 163 VAL A CG2 1 
ATOM   1342 N  N   . LEU A 1 163 ? 2.322   -3.939  17.565  1.00 16.15  ? 164 LEU A N   1 
ATOM   1343 C  CA  . LEU A 1 163 ? 0.926   -4.162  17.263  1.00 14.59  ? 164 LEU A CA  1 
ATOM   1344 C  C   . LEU A 1 163 ? 0.089   -4.523  18.417  1.00 16.32  ? 164 LEU A C   1 
ATOM   1345 O  O   . LEU A 1 163 ? -1.106  -4.206  18.466  1.00 16.12  ? 164 LEU A O   1 
ATOM   1346 C  CB  . LEU A 1 163 ? 0.727   -5.219  16.184  1.00 15.33  ? 164 LEU A CB  1 
ATOM   1347 C  CG  . LEU A 1 163 ? 1.347   -4.855  14.813  1.00 15.38  ? 164 LEU A CG  1 
ATOM   1348 C  CD1 . LEU A 1 163 ? 1.130   -5.985  13.767  1.00 15.33  ? 164 LEU A CD1 1 
ATOM   1349 C  CD2 . LEU A 1 163 ? 0.858   -3.554  14.218  1.00 15.10  ? 164 LEU A CD2 1 
ATOM   1350 N  N   . ASP A 1 164 ? 0.647   -5.175  19.440  1.00 19.55  ? 165 ASP A N   1 
ATOM   1351 C  CA  . ASP A 1 164 ? -0.133  -5.500  20.633  1.00 22.60  ? 165 ASP A CA  1 
ATOM   1352 C  C   . ASP A 1 164 ? -0.636  -4.209  21.309  1.00 20.04  ? 165 ASP A C   1 
ATOM   1353 O  O   . ASP A 1 164 ? -1.635  -4.317  22.083  1.00 24.23  ? 165 ASP A O   1 
ATOM   1354 C  CB  . ASP A 1 164 ? 0.701   -6.325  21.636  1.00 48.98  ? 165 ASP A CB  1 
ATOM   1355 C  CG  . ASP A 1 164 ? 1.581   -5.445  22.468  1.00 46.62  ? 165 ASP A CG  1 
ATOM   1356 O  OD1 . ASP A 1 164 ? 2.415   -4.723  21.886  1.00 55.23  ? 165 ASP A OD1 1 
ATOM   1357 O  OD2 . ASP A 1 164 ? 1.422   -5.439  23.713  1.00 74.59  ? 165 ASP A OD2 1 
ATOM   1358 N  N   . SER A 1 165 ? 0.040   -3.072  21.100  1.00 19.33  ? 166 SER A N   1 
ATOM   1359 C  CA  . SER A 1 165 ? -0.366  -1.818  21.754  1.00 17.66  ? 166 SER A CA  1 
ATOM   1360 C  C   . SER A 1 165 ? -1.453  -1.065  20.998  1.00 16.59  ? 166 SER A C   1 
ATOM   1361 O  O   . SER A 1 165 ? -1.996  -0.061  21.474  1.00 19.76  ? 166 SER A O   1 
ATOM   1362 C  CB  . SER A 1 165 ? 0.803   -0.919  22.063  1.00 22.32  ? 166 SER A CB  1 
ATOM   1363 O  OG  . SER A 1 165 ? 1.235   -0.405  20.868  1.00 24.15  ? 166 SER A OG  1 
ATOM   1364 N  N   . ILE A 1 166 ? -1.747  -1.544  19.784  1.00 15.35  ? 167 ILE A N   1 
ATOM   1365 C  CA  . ILE A 1 166 ? -2.736  -0.901  18.963  1.00 14.07  ? 167 ILE A CA  1 
ATOM   1366 C  C   . ILE A 1 166 ? -3.735  -1.942  18.436  1.00 14.11  ? 167 ILE A C   1 
ATOM   1367 O  O   . ILE A 1 166 ? -4.168  -1.951  17.283  1.00 12.98  ? 167 ILE A O   1 
ATOM   1368 C  CB  . ILE A 1 166 ? -2.166  -0.040  17.783  1.00 14.32  ? 167 ILE A CB  1 
ATOM   1369 C  CG1 . ILE A 1 166 ? -1.299  -0.906  16.883  1.00 14.25  ? 167 ILE A CG1 1 
ATOM   1370 C  CG2 . ILE A 1 166 ? -1.401  1.165   18.310  1.00 17.77  ? 167 ILE A CG2 1 
ATOM   1371 C  CD1 . ILE A 1 166 ? -1.380  -0.368  15.453  1.00 16.27  ? 167 ILE A CD1 1 
ATOM   1372 N  N   . LYS A 1 167 ? -4.093  -2.849  19.339  1.00 13.86  ? 168 LYS A N   1 
ATOM   1373 C  CA  . LYS A 1 167 ? -4.886  -3.996  18.901  1.00 13.32  ? 168 LYS A CA  1 
ATOM   1374 C  C   . LYS A 1 167 ? -6.191  -3.603  18.256  1.00 12.29  ? 168 LYS A C   1 
ATOM   1375 O  O   . LYS A 1 167 ? -6.684  -4.271  17.299  1.00 13.75  ? 168 LYS A O   1 
ATOM   1376 C  CB  . LYS A 1 167 ? -5.175  -4.930  20.096  1.00 14.91  ? 168 LYS A CB  1 
ATOM   1377 C  CG  . LYS A 1 167 ? -5.995  -6.168  19.719  1.00 16.70  ? 168 LYS A CG  1 
ATOM   1378 C  CD  . LYS A 1 167 ? -6.240  -7.090  20.939  1.00 22.44  ? 168 LYS A CD  1 
ATOM   1379 C  CE  . LYS A 1 167 ? -6.830  -8.430  20.602  1.00 25.06  ? 168 LYS A CE  1 
ATOM   1380 N  NZ  . LYS A 1 167 ? -6.877  -9.248  21.849  1.00 33.31  ? 168 LYS A NZ  1 
ATOM   1381 N  N   . THR A 1 168 ? -6.841  -2.587  18.781  1.00 12.84  ? 169 THR A N   1 
ATOM   1382 C  CA  . THR A 1 168 ? -8.211  -2.306  18.428  1.00 12.60  ? 169 THR A CA  1 
ATOM   1383 C  C   . THR A 1 168 ? -8.314  -0.835  17.754  1.00 11.31  ? 169 THR A C   1 
ATOM   1384 O  O   . THR A 1 168 ? -7.450  -0.021  17.878  1.00 14.05  ? 169 THR A O   1 
ATOM   1385 C  CB  . THR A 1 168 ? -9.176  -2.351  19.649  1.00 14.33  ? 169 THR A CB  1 
ATOM   1386 O  OG1 . THR A 1 168 ? -8.623  -1.577  20.689  1.00 16.48  ? 169 THR A OG1 1 
ATOM   1387 C  CG2 . THR A 1 168 ? -9.341  -3.778  20.138  1.00 15.50  ? 169 THR A CG2 1 
ATOM   1388 N  N   . LYS A 1 169 ? -9.412  -0.761  17.052  1.00 14.61  ? 170 LYS A N   1 
ATOM   1389 C  CA  . LYS A 1 169 ? -9.659  0.449   16.231  1.00 13.34  ? 170 LYS A CA  1 
ATOM   1390 C  C   . LYS A 1 169 ? -9.628  1.737   17.012  1.00 15.59  ? 170 LYS A C   1 
ATOM   1391 O  O   . LYS A 1 169 ? -10.206 1.806   18.137  1.00 16.90  ? 170 LYS A O   1 
ATOM   1392 C  CB  . LYS A 1 169 ? -11.047 0.295   15.700  1.00 12.61  ? 170 LYS A CB  1 
ATOM   1393 C  CG  . LYS A 1 169 ? -11.563 1.502   14.893  1.00 16.07  ? 170 LYS A CG  1 
ATOM   1394 C  CD  . LYS A 1 169 ? -12.852 1.225   14.253  1.00 17.53  ? 170 LYS A CD  1 
ATOM   1395 C  CE  . LYS A 1 169 ? -13.977 0.828   15.201  1.00 24.20  ? 170 LYS A CE  1 
ATOM   1396 N  NZ  . LYS A 1 169 ? -15.298 0.673   14.521  1.00 32.61  ? 170 LYS A NZ  1 
ATOM   1397 N  N   . GLY A 1 170 ? -8.865  2.698   16.506  1.00 15.34  ? 171 GLY A N   1 
ATOM   1398 C  CA  . GLY A 1 170 ? -8.713  3.966   17.213  1.00 16.08  ? 171 GLY A CA  1 
ATOM   1399 C  C   . GLY A 1 170 ? -7.469  4.062   18.081  1.00 15.97  ? 171 GLY A C   1 
ATOM   1400 O  O   . GLY A 1 170 ? -7.216  5.160   18.533  1.00 21.37  ? 171 GLY A O   1 
ATOM   1401 N  N   . LYS A 1 171 ? -6.843  2.954   18.457  1.00 14.38  ? 172 LYS A N   1 
ATOM   1402 C  CA  . LYS A 1 171 ? -5.598  3.008   19.146  1.00 14.90  ? 172 LYS A CA  1 
ATOM   1403 C  C   . LYS A 1 171 ? -4.384  3.501   18.378  1.00 13.73  ? 172 LYS A C   1 
ATOM   1404 O  O   . LYS A 1 171 ? -4.222  3.072   17.228  1.00 13.70  ? 172 LYS A O   1 
ATOM   1405 C  CB  . LYS A 1 171 ? -5.361  1.680   19.854  1.00 16.22  ? 172 LYS A CB  1 
ATOM   1406 C  CG  . LYS A 1 171 ? -6.385  1.249   20.832  1.00 18.99  ? 172 LYS A CG  1 
ATOM   1407 C  CD  . LYS A 1 171 ? -5.889  0.160   21.800  1.00 27.01  ? 172 LYS A CD  1 
ATOM   1408 C  CE  . LYS A 1 171 ? -5.530  0.602   23.173  1.00 41.28  ? 172 LYS A CE  1 
ATOM   1409 N  NZ  . LYS A 1 171 ? -4.596  -0.428  23.766  1.00 34.72  ? 172 LYS A NZ  1 
ATOM   1410 N  N   . SER A 1 172 ? -3.530  4.314   18.922  1.00 14.45  ? 173 SER A N   1 
ATOM   1411 C  CA  . SER A 1 172 ? -2.295  4.765   18.353  1.00 15.37  ? 173 SER A CA  1 
ATOM   1412 C  C   . SER A 1 172 ? -1.137  4.600   19.325  1.00 14.05  ? 173 SER A C   1 
ATOM   1413 O  O   . SER A 1 172 ? -1.363  4.500   20.530  1.00 20.27  ? 173 SER A O   1 
ATOM   1414 C  CB  . SER A 1 172 ? -2.473  6.182   17.856  1.00 17.98  ? 173 SER A CB  1 
ATOM   1415 O  OG  . SER A 1 172 ? -2.922  7.024   18.933  1.00 25.10  ? 173 SER A OG  1 
ATOM   1416 N  N   . ALA A 1 173 ? 0.083   4.634   18.853  1.00 16.93  ? 174 ALA A N   1 
ATOM   1417 C  CA  . ALA A 1 173 ? 1.248   4.617   19.665  1.00 18.50  ? 174 ALA A CA  1 
ATOM   1418 C  C   . ALA A 1 173 ? 2.377   5.386   19.010  1.00 13.06  ? 174 ALA A C   1 
ATOM   1419 O  O   . ALA A 1 173 ? 2.431   5.440   17.788  1.00 15.73  ? 174 ALA A O   1 
ATOM   1420 C  CB  . ALA A 1 173 ? 1.559   3.148   19.950  1.00 22.95  ? 174 ALA A CB  1 
ATOM   1421 N  N   . ASP A 1 174 ? 3.184   6.063   19.829  1.00 19.12  ? 175 ASP A N   1 
ATOM   1422 C  CA  . ASP A 1 174 ? 4.401   6.711   19.298  1.00 19.30  ? 175 ASP A CA  1 
ATOM   1423 C  C   . ASP A 1 174 ? 5.219   5.677   18.555  1.00 15.81  ? 175 ASP A C   1 
ATOM   1424 O  O   . ASP A 1 174 ? 5.335   4.521   19.007  1.00 20.39  ? 175 ASP A O   1 
ATOM   1425 C  CB  . ASP A 1 174 ? 5.225   7.266   20.478  1.00 23.71  ? 175 ASP A CB  1 
ATOM   1426 C  CG  . ASP A 1 174 ? 4.481   8.334   21.229  1.00 30.75  ? 175 ASP A CG  1 
ATOM   1427 O  OD1 . ASP A 1 174 ? 3.880   9.168   20.515  1.00 40.44  ? 175 ASP A OD1 1 
ATOM   1428 O  OD2 . ASP A 1 174 ? 4.450   8.325   22.473  1.00 33.70  ? 175 ASP A OD2 1 
ATOM   1429 N  N   . PHE A 1 175 ? 5.754   6.161   17.427  1.00 15.98  ? 176 PHE A N   1 
ATOM   1430 C  CA  . PHE A 1 175 ? 6.489   5.283   16.553  1.00 15.67  ? 176 PHE A CA  1 
ATOM   1431 C  C   . PHE A 1 175 ? 7.508   6.038   15.816  1.00 14.98  ? 176 PHE A C   1 
ATOM   1432 O  O   . PHE A 1 175 ? 7.291   6.260   14.642  1.00 18.67  ? 176 PHE A O   1 
ATOM   1433 C  CB  . PHE A 1 175 ? 5.491   4.411   15.734  1.00 17.73  ? 176 PHE A CB  1 
ATOM   1434 C  CG  . PHE A 1 175 ? 6.123   3.175   15.175  1.00 16.19  ? 176 PHE A CG  1 
ATOM   1435 C  CD1 . PHE A 1 175 ? 6.389   2.103   15.982  1.00 20.74  ? 176 PHE A CD1 1 
ATOM   1436 C  CD2 . PHE A 1 175 ? 6.414   3.078   13.830  1.00 17.57  ? 176 PHE A CD2 1 
ATOM   1437 C  CE1 . PHE A 1 175 ? 6.963   0.967   15.495  1.00 21.23  ? 176 PHE A CE1 1 
ATOM   1438 C  CE2 . PHE A 1 175 ? 6.921   1.883   13.300  1.00 17.18  ? 176 PHE A CE2 1 
ATOM   1439 C  CZ  . PHE A 1 175 ? 7.228   0.843   14.158  1.00 17.87  ? 176 PHE A CZ  1 
ATOM   1440 N  N   . THR A 1 176 ? 8.511   6.497   16.499  1.00 17.28  ? 177 THR A N   1 
ATOM   1441 C  CA  . THR A 1 176 ? 9.575   7.273   15.951  1.00 14.45  ? 177 THR A CA  1 
ATOM   1442 C  C   . THR A 1 176 ? 10.710  6.450   15.514  1.00 14.18  ? 177 THR A C   1 
ATOM   1443 O  O   . THR A 1 176 ? 10.860  5.274   15.999  1.00 16.87  ? 177 THR A O   1 
ATOM   1444 C  CB  . THR A 1 176 ? 9.997   8.301   17.003  1.00 18.21  ? 177 THR A CB  1 
ATOM   1445 O  OG1 . THR A 1 176 ? 10.285  7.656   18.286  1.00 24.25  ? 177 THR A OG1 1 
ATOM   1446 C  CG2 . THR A 1 176 ? 8.905   9.395   17.176  1.00 26.13  ? 177 THR A CG2 1 
ATOM   1447 N  N   . ASN A 1 177 ? 11.545  7.009   14.641  1.00 15.77  ? 178 ASN A N   1 
ATOM   1448 C  CA  . ASN A 1 177 ? 12.778  6.407   14.206  1.00 15.83  ? 178 ASN A CA  1 
ATOM   1449 C  C   . ASN A 1 177 ? 12.644  5.097   13.454  1.00 16.47  ? 178 ASN A C   1 
ATOM   1450 O  O   . ASN A 1 177 ? 13.551  4.316   13.470  1.00 23.65  ? 178 ASN A O   1 
ATOM   1451 C  CB  . ASN A 1 177 ? 13.697  6.312   15.423  1.00 17.67  ? 178 ASN A CB  1 
ATOM   1452 C  CG  . ASN A 1 177 ? 13.928  7.697   16.030  1.00 18.42  ? 178 ASN A CG  1 
ATOM   1453 O  OD1 . ASN A 1 177 ? 14.579  8.544   15.429  1.00 20.63  ? 178 ASN A OD1 1 
ATOM   1454 N  ND2 . ASN A 1 177 ? 13.282  7.971   17.166  1.00 18.52  ? 178 ASN A ND2 1 
ATOM   1455 N  N   . PHE A 1 178 ? 11.491  4.857   12.851  1.00 14.60  ? 179 PHE A N   1 
ATOM   1456 C  CA  . PHE A 1 178 ? 11.321  3.656   12.073  1.00 15.39  ? 179 PHE A CA  1 
ATOM   1457 C  C   . PHE A 1 178 ? 11.803  3.948   10.685  1.00 14.83  ? 179 PHE A C   1 
ATOM   1458 O  O   . PHE A 1 178 ? 11.395  4.939   10.042  1.00 15.13  ? 179 PHE A O   1 
ATOM   1459 C  CB  . PHE A 1 178 ? 9.905   3.189   12.022  1.00 14.64  ? 179 PHE A CB  1 
ATOM   1460 C  CG  . PHE A 1 178 ? 9.754   1.962   11.153  1.00 15.30  ? 179 PHE A CG  1 
ATOM   1461 C  CD1 . PHE A 1 178 ? 10.115  0.719   11.698  1.00 16.08  ? 179 PHE A CD1 1 
ATOM   1462 C  CD2 . PHE A 1 178 ? 9.398   2.034   9.791   1.00 12.38  ? 179 PHE A CD2 1 
ATOM   1463 C  CE1 . PHE A 1 178 ? 10.075  -0.406  10.929  1.00 16.69  ? 179 PHE A CE1 1 
ATOM   1464 C  CE2 . PHE A 1 178 ? 9.380   0.850   9.002   1.00 12.84  ? 179 PHE A CE2 1 
ATOM   1465 C  CZ  . PHE A 1 178 ? 9.714   -0.344  9.568   1.00 14.74  ? 179 PHE A CZ  1 
ATOM   1466 N  N   . ASP A 1 179 ? 12.640  3.100   10.156  1.00 15.11  ? 180 ASP A N   1 
ATOM   1467 C  CA  . ASP A 1 179 ? 13.315  3.330   8.864   1.00 15.16  ? 180 ASP A CA  1 
ATOM   1468 C  C   . ASP A 1 179 ? 12.654  2.446   7.802   1.00 13.14  ? 180 ASP A C   1 
ATOM   1469 O  O   . ASP A 1 179 ? 12.842  1.232   7.761   1.00 13.32  ? 180 ASP A O   1 
ATOM   1470 C  CB  . ASP A 1 179 ? 14.791  2.942   8.964   1.00 18.28  ? 180 ASP A CB  1 
ATOM   1471 C  CG  . ASP A 1 179 ? 15.575  3.397   7.777   1.00 18.26  ? 180 ASP A CG  1 
ATOM   1472 O  OD1 . ASP A 1 179 ? 15.025  3.560   6.658   1.00 16.54  ? 180 ASP A OD1 1 
ATOM   1473 O  OD2 . ASP A 1 179 ? 16.766  3.626   7.961   1.00 28.49  ? 180 ASP A OD2 1 
ATOM   1474 N  N   . PRO A 1 180 ? 11.845  3.043   6.893   1.00 11.84  ? 181 PRO A N   1 
ATOM   1475 C  CA  . PRO A 1 180 ? 11.109  2.203   5.877   1.00 10.85  ? 181 PRO A CA  1 
ATOM   1476 C  C   . PRO A 1 180 ? 12.085  1.569   4.862   1.00 10.84  ? 181 PRO A C   1 
ATOM   1477 O  O   . PRO A 1 180 ? 11.619  0.697   4.112   1.00 11.89  ? 181 PRO A O   1 
ATOM   1478 C  CB  . PRO A 1 180 ? 10.138  3.205   5.287   1.00 12.88  ? 181 PRO A CB  1 
ATOM   1479 C  CG  . PRO A 1 180 ? 10.780  4.522   5.430   1.00 13.92  ? 181 PRO A CG  1 
ATOM   1480 C  CD  . PRO A 1 180 ? 11.529  4.457   6.811   1.00 13.33  ? 181 PRO A CD  1 
ATOM   1481 N  N   . ARG A 1 181 ? 13.357  1.981   4.803   1.00 11.96  ? 182 ARG A N   1 
ATOM   1482 C  CA  . ARG A 1 181 ? 14.292  1.297   3.893   1.00 12.08  ? 182 ARG A CA  1 
ATOM   1483 C  C   . ARG A 1 181 ? 14.371  -0.178  4.231   1.00 13.33  ? 182 ARG A C   1 
ATOM   1484 O  O   . ARG A 1 181 ? 14.737  -0.963  3.337   1.00 14.59  ? 182 ARG A O   1 
ATOM   1485 C  CB  . ARG A 1 181 ? 15.669  1.972   3.908   1.00 13.60  ? 182 ARG A CB  1 
ATOM   1486 C  CG  . ARG A 1 181 ? 15.618  3.409   3.406   1.00 13.91  ? 182 ARG A CG  1 
ATOM   1487 C  CD  . ARG A 1 181 ? 16.998  4.045   3.483   1.00 17.41  ? 182 ARG A CD  1 
ATOM   1488 N  NE  . ARG A 1 181 ? 17.294  4.295   4.880   1.00 18.37  ? 182 ARG A NE  1 
ATOM   1489 C  CZ  . ARG A 1 181 ? 18.368  4.971   5.228   1.00 21.46  ? 182 ARG A CZ  1 
ATOM   1490 N  NH1 . ARG A 1 181 ? 19.202  5.453   4.293   1.00 26.37  ? 182 ARG A NH1 1 
ATOM   1491 N  NH2 . ARG A 1 181 ? 18.587  5.189   6.512   1.00 23.64  ? 182 ARG A NH2 1 
ATOM   1492 N  N   . GLY A 1 182 ? 14.151  -0.548  5.496   1.00 13.93  ? 183 GLY A N   1 
ATOM   1493 C  CA  . GLY A 1 182 ? 14.229  -1.943  5.852   1.00 15.20  ? 183 GLY A CA  1 
ATOM   1494 C  C   . GLY A 1 182 ? 13.091  -2.787  5.349   1.00 14.35  ? 183 GLY A C   1 
ATOM   1495 O  O   . GLY A 1 182 ? 13.097  -3.997  5.604   1.00 16.71  ? 183 GLY A O   1 
ATOM   1496 N  N   . LEU A 1 183 ? 12.118  -2.220  4.612   1.00 13.41  ? 184 LEU A N   1 
ATOM   1497 C  CA  . LEU A 1 183 ? 11.045  -2.967  4.003   1.00 12.69  ? 184 LEU A CA  1 
ATOM   1498 C  C   . LEU A 1 183 ? 11.175  -3.152  2.530   1.00 12.24  ? 184 LEU A C   1 
ATOM   1499 O  O   . LEU A 1 183 ? 10.210  -3.712  1.919   1.00 14.12  ? 184 LEU A O   1 
ATOM   1500 C  CB  . LEU A 1 183 ? 9.737   -2.268  4.340   1.00 12.90  ? 184 LEU A CB  1 
ATOM   1501 C  CG  . LEU A 1 183 ? 9.437   -2.169  5.845   1.00 14.02  ? 184 LEU A CG  1 
ATOM   1502 C  CD1 . LEU A 1 183 ? 8.189   -1.343  6.011   1.00 16.49  ? 184 LEU A CD1 1 
ATOM   1503 C  CD2 . LEU A 1 183 ? 9.279   -3.469  6.610   1.00 16.33  ? 184 LEU A CD2 1 
ATOM   1504 N  N   . LEU A 1 184 ? 12.261  -2.672  1.949   1.00 13.87  ? 185 LEU A N   1 
ATOM   1505 C  CA  . LEU A 1 184 ? 12.385  -2.719  0.503   1.00 12.67  ? 185 LEU A CA  1 
ATOM   1506 C  C   . LEU A 1 184 ? 13.035  -4.018  0.071   1.00 15.77  ? 185 LEU A C   1 
ATOM   1507 O  O   . LEU A 1 184 ? 13.898  -4.557  0.814   1.00 89.94  ? 185 LEU A O   1 
ATOM   1508 C  CB  . LEU A 1 184 ? 13.162  -1.494  -0.001  1.00 12.03  ? 185 LEU A CB  1 
ATOM   1509 C  CG  . LEU A 1 184 ? 12.580  -0.128  0.397   1.00 10.75  ? 185 LEU A CG  1 
ATOM   1510 C  CD1 . LEU A 1 184 ? 13.502  1.001   -0.043  1.00 13.99  ? 185 LEU A CD1 1 
ATOM   1511 C  CD2 . LEU A 1 184 ? 11.183  0.045   -0.137  1.00 12.62  ? 185 LEU A CD2 1 
ATOM   1512 N  N   . PRO A 1 185 ? 12.751  -4.547  -1.107  1.00 12.62  ? 186 PRO A N   1 
ATOM   1513 C  CA  . PRO A 1 185 ? 13.425  -5.753  -1.606  1.00 13.20  ? 186 PRO A CA  1 
ATOM   1514 C  C   . PRO A 1 185 ? 14.690  -5.189  -2.264  1.00 12.84  ? 186 PRO A C   1 
ATOM   1515 O  O   . PRO A 1 185 ? 14.984  -3.939  -2.409  1.00 16.42  ? 186 PRO A O   1 
ATOM   1516 C  CB  . PRO A 1 185 ? 12.516  -6.291  -2.663  1.00 11.78  ? 186 PRO A CB  1 
ATOM   1517 C  CG  . PRO A 1 185 ? 11.818  -5.051  -3.160  1.00 10.19  ? 186 PRO A CG  1 
ATOM   1518 C  CD  . PRO A 1 185 ? 11.590  -4.194  -1.941  1.00 10.23  ? 186 PRO A CD  1 
ATOM   1519 N  N   A GLU A 1 186 ? 15.465  -6.165  -2.683  0.50 13.58  ? 187 GLU A N   1 
ATOM   1520 N  N   B GLU A 1 186 ? 15.676  -5.983  -2.877  0.50 11.98  ? 187 GLU A N   1 
ATOM   1521 C  CA  A GLU A 1 186 ? 16.732  -5.888  -3.271  0.50 13.19  ? 187 GLU A CA  1 
ATOM   1522 C  CA  B GLU A 1 186 ? 16.949  -5.520  -3.590  0.50 12.45  ? 187 GLU A CA  1 
ATOM   1523 C  C   A GLU A 1 186 ? 16.559  -5.021  -4.500  0.50 12.43  ? 187 GLU A C   1 
ATOM   1524 C  C   B GLU A 1 186 ? 16.693  -4.797  -4.876  0.50 11.48  ? 187 GLU A C   1 
ATOM   1525 O  O   A GLU A 1 186 ? 17.161  -3.950  -4.555  0.50 12.19  ? 187 GLU A O   1 
ATOM   1526 O  O   B GLU A 1 186 ? 17.287  -3.731  -5.257  0.50 13.31  ? 187 GLU A O   1 
ATOM   1527 C  CB  A GLU A 1 186 ? 17.454  -7.180  -3.588  0.50 11.78  ? 187 GLU A CB  1 
ATOM   1528 C  CB  B GLU A 1 186 ? 17.815  -6.694  -4.088  0.50 12.77  ? 187 GLU A CB  1 
ATOM   1529 C  CG  A GLU A 1 186 ? 18.799  -6.974  -4.239  0.50 13.99  ? 187 GLU A CG  1 
ATOM   1530 C  CG  B GLU A 1 186 ? 18.371  -7.500  -2.940  0.50 14.72  ? 187 GLU A CG  1 
ATOM   1531 C  CD  A GLU A 1 186 ? 19.437  -8.293  -4.581  0.50 15.37  ? 187 GLU A CD  1 
ATOM   1532 C  CD  B GLU A 1 186 ? 19.165  -8.720  -3.427  0.50 18.82  ? 187 GLU A CD  1 
ATOM   1533 O  OE1 A GLU A 1 186 ? 19.224  -9.256  -3.816  0.50 18.21  ? 187 GLU A OE1 1 
ATOM   1534 O  OE1 B GLU A 1 186 ? 19.275  -9.024  -4.653  0.50 19.06  ? 187 GLU A OE1 1 
ATOM   1535 O  OE2 A GLU A 1 186 ? 20.133  -8.370  -5.611  0.50 21.07  ? 187 GLU A OE2 1 
ATOM   1536 O  OE2 B GLU A 1 186 ? 19.736  -9.426  -2.597  0.50 20.86  ? 187 GLU A OE2 1 
ATOM   1537 N  N   . SER A 1 187 ? 15.755  -5.447  -5.556  1.00 13.04  ? 188 SER A N   1 
ATOM   1538 C  CA  . SER A 1 187 ? 15.524  -4.810  -6.819  1.00 14.40  ? 188 SER A CA  1 
ATOM   1539 C  C   . SER A 1 187 ? 14.399  -3.791  -6.826  1.00 12.46  ? 188 SER A C   1 
ATOM   1540 O  O   . SER A 1 187 ? 13.368  -4.042  -6.208  1.00 13.65  ? 188 SER A O   1 
ATOM   1541 C  CB  . SER A 1 187 ? 15.153  -5.870  -7.879  1.00 15.19  ? 188 SER A CB  1 
ATOM   1542 O  OG  . SER A 1 187 ? 14.860  -5.303  -9.131  1.00 15.64  ? 188 SER A OG  1 
ATOM   1543 N  N   . LEU A 1 188 ? 14.570  -2.701  -7.533  1.00 12.76  ? 189 LEU A N   1 
ATOM   1544 C  CA  . LEU A 1 188 ? 13.509  -1.725  -7.771  1.00 12.56  ? 189 LEU A CA  1 
ATOM   1545 C  C   . LEU A 1 188 ? 12.868  -1.867  -9.131  1.00 11.50  ? 189 LEU A C   1 
ATOM   1546 O  O   . LEU A 1 188 ? 12.185  -0.931  -9.576  1.00 13.66  ? 189 LEU A O   1 
ATOM   1547 C  CB  . LEU A 1 188 ? 14.005  -0.295  -7.468  1.00 14.97  ? 189 LEU A CB  1 
ATOM   1548 C  CG  . LEU A 1 188 ? 14.456  0.012   -6.054  1.00 16.82  ? 189 LEU A CG  1 
ATOM   1549 C  CD1 . LEU A 1 188 ? 14.971  1.440   -6.002  1.00 17.79  ? 189 LEU A CD1 1 
ATOM   1550 C  CD2 . LEU A 1 188 ? 13.313  -0.221  -5.067  1.00 18.63  ? 189 LEU A CD2 1 
ATOM   1551 N  N   . ASP A 1 189 ? 13.020  -3.023  -9.776  1.00 11.46  ? 190 ASP A N   1 
ATOM   1552 C  CA  . ASP A 1 189 ? 12.255  -3.258  -11.011 1.00 11.99  ? 190 ASP A CA  1 
ATOM   1553 C  C   . ASP A 1 189 ? 10.743  -3.212  -10.718 1.00 9.70   ? 190 ASP A C   1 
ATOM   1554 O  O   . ASP A 1 189 ? 10.302  -3.726  -9.686  1.00 10.04  ? 190 ASP A O   1 
ATOM   1555 C  CB  . ASP A 1 189 ? 12.555  -4.626  -11.636 1.00 15.17  ? 190 ASP A CB  1 
ATOM   1556 C  CG  . ASP A 1 189 ? 13.938  -4.730  -12.309 1.00 18.25  ? 190 ASP A CG  1 
ATOM   1557 O  OD1 . ASP A 1 189 ? 14.584  -3.680  -12.525 1.00 24.11  ? 190 ASP A OD1 1 
ATOM   1558 O  OD2 . ASP A 1 189 ? 14.355  -5.877  -12.583 1.00 25.58  ? 190 ASP A OD2 1 
ATOM   1559 N  N   . TYR A 1 190 ? 9.965   -2.631  -11.633 1.00 9.40   ? 191 TYR A N   1 
ATOM   1560 C  CA  . TYR A 1 190 ? 8.557   -2.376  -11.333 1.00 8.95   ? 191 TYR A CA  1 
ATOM   1561 C  C   . TYR A 1 190 ? 7.673   -2.431  -12.543 1.00 8.29   ? 191 TYR A C   1 
ATOM   1562 O  O   . TYR A 1 190 ? 8.107   -2.312  -13.705 1.00 9.30   ? 191 TYR A O   1 
ATOM   1563 C  CB  . TYR A 1 190 ? 8.378   -0.980  -10.638 1.00 9.65   ? 191 TYR A CB  1 
ATOM   1564 C  CG  . TYR A 1 190 ? 8.800   0.178   -11.512 1.00 9.36   ? 191 TYR A CG  1 
ATOM   1565 C  CD1 . TYR A 1 190 ? 7.859   0.777   -12.362 1.00 9.80   ? 191 TYR A CD1 1 
ATOM   1566 C  CD2 . TYR A 1 190 ? 10.087  0.708   -11.456 1.00 9.97   ? 191 TYR A CD2 1 
ATOM   1567 C  CE1 . TYR A 1 190 ? 8.261   1.851   -13.180 1.00 10.50  ? 191 TYR A CE1 1 
ATOM   1568 C  CE2 . TYR A 1 190 ? 10.478  1.754   -12.263 1.00 11.30  ? 191 TYR A CE2 1 
ATOM   1569 C  CZ  . TYR A 1 190 ? 9.591   2.324   -13.135 1.00 10.69  ? 191 TYR A CZ  1 
ATOM   1570 O  OH  . TYR A 1 190 ? 9.919   3.347   -13.987 1.00 12.40  ? 191 TYR A OH  1 
ATOM   1571 N  N   . TRP A 1 191 ? 6.388   -2.570  -12.229 1.00 7.76   ? 192 TRP A N   1 
ATOM   1572 C  CA  . TRP A 1 191 ? 5.287   -2.318  -13.198 1.00 7.56   ? 192 TRP A CA  1 
ATOM   1573 C  C   . TRP A 1 191 ? 4.578   -1.014  -12.751 1.00 7.36   ? 192 TRP A C   1 
ATOM   1574 O  O   . TRP A 1 191 ? 4.531   -0.671  -11.580 1.00 8.31   ? 192 TRP A O   1 
ATOM   1575 C  CB  . TRP A 1 191 ? 4.257   -3.421  -13.183 1.00 8.37   ? 192 TRP A CB  1 
ATOM   1576 C  CG  . TRP A 1 191 ? 4.788   -4.754  -13.577 1.00 8.70   ? 192 TRP A CG  1 
ATOM   1577 C  CD1 . TRP A 1 191 ? 5.000   -5.202  -14.856 1.00 9.66   ? 192 TRP A CD1 1 
ATOM   1578 C  CD2 . TRP A 1 191 ? 5.062   -5.879  -12.715 1.00 8.62   ? 192 TRP A CD2 1 
ATOM   1579 N  NE1 . TRP A 1 191 ? 5.419   -6.501  -14.841 1.00 10.82  ? 192 TRP A NE1 1 
ATOM   1580 C  CE2 . TRP A 1 191 ? 5.443   -6.959  -13.555 1.00 9.97   ? 192 TRP A CE2 1 
ATOM   1581 C  CE3 . TRP A 1 191 ? 4.940   -6.099  -11.319 1.00 8.94   ? 192 TRP A CE3 1 
ATOM   1582 C  CZ2 . TRP A 1 191 ? 5.737   -8.213  -13.030 1.00 10.53  ? 192 TRP A CZ2 1 
ATOM   1583 C  CZ3 . TRP A 1 191 ? 5.242   -7.354  -10.836 1.00 9.97   ? 192 TRP A CZ3 1 
ATOM   1584 C  CH2 . TRP A 1 191 ? 5.581   -8.401  -11.668 1.00 11.15  ? 192 TRP A CH2 1 
ATOM   1585 N  N   . THR A 1 192 ? 3.990   -0.316  -13.712 1.00 7.30   ? 193 THR A N   1 
ATOM   1586 C  CA  . THR A 1 192 ? 3.281   0.906   -13.391 1.00 7.69   ? 193 THR A CA  1 
ATOM   1587 C  C   . THR A 1 192 ? 2.045   1.072   -14.281 1.00 6.96   ? 193 THR A C   1 
ATOM   1588 O  O   . THR A 1 192 ? 2.022   0.675   -15.440 1.00 8.14   ? 193 THR A O   1 
ATOM   1589 C  CB  . THR A 1 192 ? 4.206   2.126   -13.515 1.00 7.62   ? 193 THR A CB  1 
ATOM   1590 O  OG1 . THR A 1 192 ? 3.523   3.330   -13.114 1.00 8.28   ? 193 THR A OG1 1 
ATOM   1591 C  CG2 . THR A 1 192 ? 4.739   2.345   -14.923 1.00 9.49   ? 193 THR A CG2 1 
ATOM   1592 N  N   . TYR A 1 193 ? 1.015   1.672   -13.704 1.00 7.41   ? 194 TYR A N   1 
ATOM   1593 C  CA  . TYR A 1 193 ? -0.219  1.951   -14.400 1.00 7.37   ? 194 TYR A CA  1 
ATOM   1594 C  C   . TYR A 1 193 ? -0.990  3.018   -13.607 1.00 6.92   ? 194 TYR A C   1 
ATOM   1595 O  O   . TYR A 1 193 ? -0.785  3.215   -12.419 1.00 7.33   ? 194 TYR A O   1 
ATOM   1596 C  CB  . TYR A 1 193 ? -1.070  0.668   -14.597 1.00 7.75   ? 194 TYR A CB  1 
ATOM   1597 C  CG  . TYR A 1 193 ? -1.760  0.202   -13.339 1.00 7.11   ? 194 TYR A CG  1 
ATOM   1598 C  CD1 . TYR A 1 193 ? -1.100  -0.513  -12.363 1.00 7.09   ? 194 TYR A CD1 1 
ATOM   1599 C  CD2 . TYR A 1 193 ? -3.075  0.528   -13.125 1.00 7.36   ? 194 TYR A CD2 1 
ATOM   1600 C  CE1 . TYR A 1 193 ? -1.719  -0.851  -11.163 1.00 6.85   ? 194 TYR A CE1 1 
ATOM   1601 C  CE2 . TYR A 1 193 ? -3.743  0.211   -11.935 1.00 7.79   ? 194 TYR A CE2 1 
ATOM   1602 C  CZ  . TYR A 1 193 ? -3.046  -0.482  -10.937 1.00 6.47   ? 194 TYR A CZ  1 
ATOM   1603 O  OH  . TYR A 1 193 ? -3.704  -0.764  -9.796  1.00 7.28   ? 194 TYR A OH  1 
ATOM   1604 N  N   . PRO A 1 194 ? -1.945  3.710   -14.285 1.00 7.46   ? 195 PRO A N   1 
ATOM   1605 C  CA  . PRO A 1 194 ? -2.798  4.728   -13.617 1.00 7.50   ? 195 PRO A CA  1 
ATOM   1606 C  C   . PRO A 1 194 ? -3.995  4.044   -12.960 1.00 7.07   ? 195 PRO A C   1 
ATOM   1607 O  O   . PRO A 1 194 ? -4.715  3.283   -13.600 1.00 8.00   ? 195 PRO A O   1 
ATOM   1608 C  CB  . PRO A 1 194 ? -3.277  5.621   -14.758 1.00 9.10   ? 195 PRO A CB  1 
ATOM   1609 C  CG  . PRO A 1 194 ? -3.292  4.673   -15.949 1.00 9.87   ? 195 PRO A CG  1 
ATOM   1610 C  CD  . PRO A 1 194 ? -2.158  3.713   -15.776 1.00 9.41   ? 195 PRO A CD  1 
ATOM   1611 N  N   . GLY A 1 195 ? -4.209  4.372   -11.668 1.00 7.02   ? 196 GLY A N   1 
ATOM   1612 C  CA  . GLY A 1 195 ? -5.359  3.766   -10.951 1.00 7.09   ? 196 GLY A CA  1 
ATOM   1613 C  C   . GLY A 1 195 ? -5.876  4.631   -9.871  1.00 6.67   ? 196 GLY A C   1 
ATOM   1614 O  O   . GLY A 1 195 ? -5.968  5.879   -10.008 1.00 7.21   ? 196 GLY A O   1 
ATOM   1615 N  N   . SER A 1 196 ? -6.293  3.964   -8.803  1.00 6.54   ? 197 SER A N   1 
ATOM   1616 C  CA  . SER A 1 196 ? -7.107  4.606   -7.773  1.00 7.19   ? 197 SER A CA  1 
ATOM   1617 C  C   . SER A 1 196 ? -6.642  4.190   -6.395  1.00 6.19   ? 197 SER A C   1 
ATOM   1618 O  O   . SER A 1 196 ? -5.895  3.231   -6.205  1.00 6.57   ? 197 SER A O   1 
ATOM   1619 C  CB  . SER A 1 196 ? -8.582  4.225   -7.918  1.00 7.71   ? 197 SER A CB  1 
ATOM   1620 O  OG  . SER A 1 196 ? -8.833  2.869   -7.513  1.00 7.47   ? 197 SER A OG  1 
ATOM   1621 N  N   . LEU A 1 197 ? -7.164  4.882   -5.357  1.00 6.82   ? 198 LEU A N   1 
ATOM   1622 C  CA  . LEU A 1 197 ? -7.191  4.318   -4.009  1.00 7.40   ? 198 LEU A CA  1 
ATOM   1623 C  C   . LEU A 1 197 ? -7.918  3.008   -4.080  1.00 7.14   ? 198 LEU A C   1 
ATOM   1624 O  O   . LEU A 1 197 ? -8.934  2.836   -4.800  1.00 7.58   ? 198 LEU A O   1 
ATOM   1625 C  CB  . LEU A 1 197 ? -7.917  5.255   -3.046  1.00 8.24   ? 198 LEU A CB  1 
ATOM   1626 C  CG  . LEU A 1 197 ? -7.484  6.677   -2.951  1.00 10.10  ? 198 LEU A CG  1 
ATOM   1627 C  CD1 . LEU A 1 197 ? -8.358  7.487   -1.990  1.00 14.58  ? 198 LEU A CD1 1 
ATOM   1628 C  CD2 . LEU A 1 197 ? -6.080  6.748   -2.516  1.00 12.67  ? 198 LEU A CD2 1 
ATOM   1629 N  N   . THR A 1 198 ? -7.498  2.049   -3.224  1.00 7.45   ? 199 THR A N   1 
ATOM   1630 C  CA  . THR A 1 198 ? -8.171  0.750   -3.172  1.00 8.00   ? 199 THR A CA  1 
ATOM   1631 C  C   . THR A 1 198 ? -9.188  0.657   -2.052  1.00 8.20   ? 199 THR A C   1 
ATOM   1632 O  O   . THR A 1 198 ? -9.783  -0.426  -1.849  1.00 9.04   ? 199 THR A O   1 
ATOM   1633 C  CB  . THR A 1 198 ? -7.180  -0.407  -3.054  1.00 7.30   ? 199 THR A CB  1 
ATOM   1634 O  OG1 . THR A 1 198 ? -6.543  -0.294  -1.797  1.00 7.18   ? 199 THR A OG1 1 
ATOM   1635 C  CG2 . THR A 1 198 ? -6.183  -0.411  -4.195  1.00 8.50   ? 199 THR A CG2 1 
ATOM   1636 N  N   . THR A 1 199 ? -9.385  1.762   -1.295  1.00 9.28   ? 200 THR A N   1 
ATOM   1637 C  CA  . THR A 1 199 ? -10.384 1.873   -0.292  1.00 10.49  ? 200 THR A CA  1 
ATOM   1638 C  C   . THR A 1 199 ? -11.223 3.104   -0.591  1.00 10.10  ? 200 THR A C   1 
ATOM   1639 O  O   . THR A 1 199 ? -10.748 4.034   -1.196  1.00 9.58   ? 200 THR A O   1 
ATOM   1640 C  CB  . THR A 1 199 ? -9.769  2.054   1.116   1.00 12.17  ? 200 THR A CB  1 
ATOM   1641 O  OG1 . THR A 1 199 ? -8.818  3.166   1.082   1.00 16.06  ? 200 THR A OG1 1 
ATOM   1642 C  CG2 . THR A 1 199 ? -9.013  0.788   1.535   1.00 15.12  ? 200 THR A CG2 1 
ATOM   1643 N  N   . PRO A 1 200 ? -12.491 3.094   -0.129  1.00 10.34  ? 201 PRO A N   1 
ATOM   1644 C  CA  . PRO A 1 200 ? -13.267 4.331   -0.200  1.00 11.65  ? 201 PRO A CA  1 
ATOM   1645 C  C   . PRO A 1 200 ? -12.438 5.484   0.348   1.00 11.91  ? 201 PRO A C   1 
ATOM   1646 O  O   . PRO A 1 200 ? -11.790 5.341   1.398   1.00 12.40  ? 201 PRO A O   1 
ATOM   1647 C  CB  . PRO A 1 200 ? -14.501 3.983   0.688   1.00 13.13  ? 201 PRO A CB  1 
ATOM   1648 C  CG  . PRO A 1 200 ? -14.688 2.532   0.435   1.00 12.98  ? 201 PRO A CG  1 
ATOM   1649 C  CD  . PRO A 1 200 ? -13.310 1.997   0.502   1.00 11.80  ? 201 PRO A CD  1 
ATOM   1650 N  N   . PRO A 1 201 ? -12.459 6.626   -0.307  1.00 10.98  ? 202 PRO A N   1 
ATOM   1651 C  CA  . PRO A 1 201 ? -13.393 7.020   -1.395  1.00 11.42  ? 202 PRO A CA  1 
ATOM   1652 C  C   . PRO A 1 201 ? -13.003 6.608   -2.827  1.00 10.30  ? 202 PRO A C   1 
ATOM   1653 O  O   . PRO A 1 201 ? -13.669 7.056   -3.771  1.00 11.16  ? 202 PRO A O   1 
ATOM   1654 C  CB  . PRO A 1 201 ? -13.407 8.577   -1.282  1.00 14.65  ? 202 PRO A CB  1 
ATOM   1655 C  CG  . PRO A 1 201 ? -11.991 8.925   -0.835  1.00 15.27  ? 202 PRO A CG  1 
ATOM   1656 C  CD  . PRO A 1 201 ? -11.705 7.812   0.204   1.00 13.11  ? 202 PRO A CD  1 
ATOM   1657 N  N   . LEU A 1 202 ? -11.983 5.758   -2.995  1.00 9.29   ? 203 LEU A N   1 
ATOM   1658 C  CA  . LEU A 1 202 ? -11.721 5.112   -4.316  1.00 9.08   ? 203 LEU A CA  1 
ATOM   1659 C  C   . LEU A 1 202 ? -11.352 6.120   -5.387  1.00 8.45   ? 203 LEU A C   1 
ATOM   1660 O  O   . LEU A 1 202 ? -11.492 5.878   -6.578  1.00 8.79   ? 203 LEU A O   1 
ATOM   1661 C  CB  . LEU A 1 202 ? -12.884 4.213   -4.770  1.00 8.74   ? 203 LEU A CB  1 
ATOM   1662 C  CG  . LEU A 1 202 ? -13.205 3.090   -3.774  1.00 9.46   ? 203 LEU A CG  1 
ATOM   1663 C  CD1 . LEU A 1 202 ? -14.545 2.401   -4.222  1.00 11.15  ? 203 LEU A CD1 1 
ATOM   1664 C  CD2 . LEU A 1 202 ? -12.109 2.044   -3.747  1.00 10.17  ? 203 LEU A CD2 1 
ATOM   1665 N  N   . LEU A 1 203 ? -10.761 7.248   -4.963  1.00 8.99   ? 204 LEU A N   1 
ATOM   1666 C  CA  . LEU A 1 203 ? -10.472 8.350   -5.871  1.00 9.37   ? 204 LEU A CA  1 
ATOM   1667 C  C   . LEU A 1 203 ? -9.423  7.914   -6.884  1.00 8.71   ? 204 LEU A C   1 
ATOM   1668 O  O   . LEU A 1 203 ? -8.441  7.215   -6.599  1.00 8.38   ? 204 LEU A O   1 
ATOM   1669 C  CB  . LEU A 1 203 ? -9.979  9.573   -5.104  1.00 10.55  ? 204 LEU A CB  1 
ATOM   1670 C  CG  . LEU A 1 203 ? -11.034 10.162  -4.173  1.00 12.83  ? 204 LEU A CG  1 
ATOM   1671 C  CD1 . LEU A 1 203 ? -10.420 11.214  -3.268  1.00 16.20  ? 204 LEU A CD1 1 
ATOM   1672 C  CD2 . LEU A 1 203 ? -12.237 10.748  -4.952  1.00 18.03  ? 204 LEU A CD2 1 
ATOM   1673 N  N   . GLU A 1 204 ? -9.596  8.393   -8.113  1.00 8.89   ? 205 GLU A N   1 
ATOM   1674 C  CA  . GLU A 1 204 ? -8.770  8.032   -9.266  1.00 9.20   ? 205 GLU A CA  1 
ATOM   1675 C  C   . GLU A 1 204 ? -7.609  8.993   -9.416  1.00 8.21   ? 205 GLU A C   1 
ATOM   1676 O  O   . GLU A 1 204 ? -7.496  9.771   -10.362 1.00 10.84  ? 205 GLU A O   1 
ATOM   1677 C  CB  . GLU A 1 204 ? -9.622  7.876   -10.535 1.00 10.10  ? 205 GLU A CB  1 
ATOM   1678 C  CG  . GLU A 1 204 ? -10.533 6.664   -10.390 1.00 10.48  ? 205 GLU A CG  1 
ATOM   1679 C  CD  . GLU A 1 204 ? -11.454 6.403   -11.559 1.00 11.28  ? 205 GLU A CD  1 
ATOM   1680 O  OE1 . GLU A 1 204 ? -11.759 7.337   -12.341 1.00 13.48  ? 205 GLU A OE1 1 
ATOM   1681 O  OE2 . GLU A 1 204 ? -11.864 5.207   -11.744 1.00 10.65  ? 205 GLU A OE2 1 
ATOM   1682 N  N   . CYS A 1 205 ? -6.696  8.903   -8.442  1.00 7.83   ? 206 CYS A N   1 
ATOM   1683 C  CA  . CYS A 1 205 ? -5.639  9.888   -8.210  1.00 8.27   ? 206 CYS A CA  1 
ATOM   1684 C  C   . CYS A 1 205 ? -4.269  9.267   -8.127  1.00 7.53   ? 206 CYS A C   1 
ATOM   1685 O  O   . CYS A 1 205 ? -3.340  9.968   -7.749  1.00 9.29   ? 206 CYS A O   1 
ATOM   1686 C  CB  . CYS A 1 205 ? -5.931  10.726  -6.994  1.00 9.23   ? 206 CYS A CB  1 
ATOM   1687 S  SG  . CYS A 1 205 ? -5.984  9.755   -5.458  1.00 9.62   ? 206 CYS A SG  1 
ATOM   1688 N  N   . VAL A 1 206 ? -4.120  7.975   -8.397  1.00 7.09   ? 207 VAL A N   1 
ATOM   1689 C  CA  . VAL A 1 206 ? -2.897  7.261   -8.050  1.00 7.33   ? 207 VAL A CA  1 
ATOM   1690 C  C   . VAL A 1 206 ? -2.121  6.814   -9.284  1.00 6.96   ? 207 VAL A C   1 
ATOM   1691 O  O   . VAL A 1 206 ? -2.676  6.152   -10.174 1.00 8.45   ? 207 VAL A O   1 
ATOM   1692 C  CB  . VAL A 1 206 ? -3.185  6.001   -7.209  1.00 7.27   ? 207 VAL A CB  1 
ATOM   1693 C  CG1 . VAL A 1 206 ? -1.885  5.268   -6.892  1.00 7.69   ? 207 VAL A CG1 1 
ATOM   1694 C  CG2 . VAL A 1 206 ? -3.915  6.376   -5.907  1.00 8.50   ? 207 VAL A CG2 1 
ATOM   1695 N  N   . THR A 1 207 ? -0.821  7.127   -9.334  1.00 6.71   ? 208 THR A N   1 
ATOM   1696 C  CA  . THR A 1 207 ? 0.114   6.371   -10.196 1.00 6.97   ? 208 THR A CA  1 
ATOM   1697 C  C   . THR A 1 207 ? 0.650   5.229   -9.342  1.00 6.64   ? 208 THR A C   1 
ATOM   1698 O  O   . THR A 1 207 ? 1.326   5.425   -8.341  1.00 6.94   ? 208 THR A O   1 
ATOM   1699 C  CB  . THR A 1 207 ? 1.287   7.263   -10.670 1.00 7.92   ? 208 THR A CB  1 
ATOM   1700 O  OG1 . THR A 1 207 ? 0.803   8.385   -11.400 1.00 8.59   ? 208 THR A OG1 1 
ATOM   1701 C  CG2 . THR A 1 207 ? 2.220   6.472   -11.538 1.00 9.09   ? 208 THR A CG2 1 
ATOM   1702 N  N   . TRP A 1 208 ? 0.296   4.007   -9.782  1.00 6.22   ? 209 TRP A N   1 
ATOM   1703 C  CA  . TRP A 1 208 ? 0.765   2.816   -9.082  1.00 6.48   ? 209 TRP A CA  1 
ATOM   1704 C  C   . TRP A 1 208 ? 2.115   2.410   -9.602  1.00 6.21   ? 209 TRP A C   1 
ATOM   1705 O  O   . TRP A 1 208 ? 2.332   2.352   -10.822 1.00 6.90   ? 209 TRP A O   1 
ATOM   1706 C  CB  . TRP A 1 208 ? -0.278  1.654   -9.282  1.00 6.46   ? 209 TRP A CB  1 
ATOM   1707 C  CG  . TRP A 1 208 ? -1.406  1.774   -8.326  1.00 6.17   ? 209 TRP A CG  1 
ATOM   1708 C  CD1 . TRP A 1 208 ? -2.643  2.340   -8.514  1.00 6.90   ? 209 TRP A CD1 1 
ATOM   1709 C  CD2 . TRP A 1 208 ? -1.348  1.361   -6.965  1.00 6.22   ? 209 TRP A CD2 1 
ATOM   1710 N  NE1 . TRP A 1 208 ? -3.357  2.322   -7.360  1.00 7.69   ? 209 TRP A NE1 1 
ATOM   1711 C  CE2 . TRP A 1 208 ? -2.594  1.722   -6.378  1.00 7.09   ? 209 TRP A CE2 1 
ATOM   1712 C  CE3 . TRP A 1 208 ? -0.372  0.733   -6.157  1.00 6.67   ? 209 TRP A CE3 1 
ATOM   1713 C  CZ2 . TRP A 1 208 ? -2.884  1.476   -5.022  1.00 8.20   ? 209 TRP A CZ2 1 
ATOM   1714 C  CZ3 . TRP A 1 208 ? -0.673  0.455   -4.838  1.00 7.64   ? 209 TRP A CZ3 1 
ATOM   1715 C  CH2 . TRP A 1 208 ? -1.857  0.836   -4.296  1.00 8.37   ? 209 TRP A CH2 1 
ATOM   1716 N  N   . ILE A 1 209 ? 2.997   2.042   -8.672  1.00 6.11   ? 210 ILE A N   1 
ATOM   1717 C  CA  . ILE A 1 209 ? 4.319   1.518   -8.976  1.00 6.66   ? 210 ILE A CA  1 
ATOM   1718 C  C   . ILE A 1 209 ? 4.430   0.255   -8.119  1.00 6.38   ? 210 ILE A C   1 
ATOM   1719 O  O   . ILE A 1 209 ? 4.520   0.349   -6.887  1.00 7.56   ? 210 ILE A O   1 
ATOM   1720 C  CB  . ILE A 1 209 ? 5.412   2.546   -8.627  1.00 7.58   ? 210 ILE A CB  1 
ATOM   1721 C  CG1 . ILE A 1 209 ? 5.187   3.822   -9.455  1.00 9.49   ? 210 ILE A CG1 1 
ATOM   1722 C  CG2 . ILE A 1 209 ? 6.778   1.940   -8.841  1.00 9.55   ? 210 ILE A CG2 1 
ATOM   1723 C  CD1 . ILE A 1 209 ? 6.029   5.015   -8.985  1.00 11.92  ? 210 ILE A CD1 1 
ATOM   1724 N  N   . VAL A 1 210 ? 4.369   -0.894  -8.757  1.00 6.71   ? 211 VAL A N   1 
ATOM   1725 C  CA  . VAL A 1 210 ? 4.349   -2.182  -8.053  1.00 6.31   ? 211 VAL A CA  1 
ATOM   1726 C  C   . VAL A 1 210 ? 5.642   -2.884  -8.335  1.00 6.56   ? 211 VAL A C   1 
ATOM   1727 O  O   . VAL A 1 210 ? 6.000   -3.184  -9.481  1.00 7.54   ? 211 VAL A O   1 
ATOM   1728 C  CB  . VAL A 1 210 ? 3.143   -3.026  -8.514  1.00 7.34   ? 211 VAL A CB  1 
ATOM   1729 C  CG1 . VAL A 1 210 ? 3.163   -4.404  -7.798  1.00 8.37   ? 211 VAL A CG1 1 
ATOM   1730 C  CG2 . VAL A 1 210 ? 1.838   -2.297  -8.245  1.00 8.22   ? 211 VAL A CG2 1 
ATOM   1731 N  N   . LEU A 1 211 ? 6.425   -3.166  -7.279  1.00 7.21   ? 212 LEU A N   1 
ATOM   1732 C  CA  . LEU A 1 211 ? 7.704   -3.831  -7.440  1.00 7.75   ? 212 LEU A CA  1 
ATOM   1733 C  C   . LEU A 1 211 ? 7.515   -5.284  -7.795  1.00 7.41   ? 212 LEU A C   1 
ATOM   1734 O  O   . LEU A 1 211 ? 6.663   -6.000  -7.276  1.00 8.05   ? 212 LEU A O   1 
ATOM   1735 C  CB  . LEU A 1 211 ? 8.557   -3.706  -6.175  1.00 8.73   ? 212 LEU A CB  1 
ATOM   1736 C  CG  . LEU A 1 211 ? 8.899   -2.296  -5.739  1.00 9.15   ? 212 LEU A CG  1 
ATOM   1737 C  CD1 . LEU A 1 211 ? 9.943   -2.373  -4.585  1.00 11.52  ? 212 LEU A CD1 1 
ATOM   1738 C  CD2 . LEU A 1 211 ? 9.411   -1.472  -6.893  1.00 10.20  ? 212 LEU A CD2 1 
ATOM   1739 N  N   . LYS A 1 212 ? 8.368   -5.770  -8.711  1.00 8.19   ? 213 LYS A N   1 
ATOM   1740 C  CA  . LYS A 1 212 ? 8.337   -7.166  -9.091  1.00 9.07   ? 213 LYS A CA  1 
ATOM   1741 C  C   . LYS A 1 212 ? 8.825   -8.095  -8.019  1.00 8.14   ? 213 LYS A C   1 
ATOM   1742 O  O   . LYS A 1 212 ? 8.299   -9.209  -7.866  1.00 10.37  ? 213 LYS A O   1 
ATOM   1743 C  CB  . LYS A 1 212 ? 9.143   -7.389  -10.368 1.00 11.24  ? 213 LYS A CB  1 
ATOM   1744 C  CG  . LYS A 1 212 ? 9.236   -8.831  -10.824 1.00 14.44  ? 213 LYS A CG  1 
ATOM   1745 C  CD  . LYS A 1 212 ? 10.022  -9.025  -12.104 1.00 22.16  ? 213 LYS A CD  1 
ATOM   1746 C  CE  . LYS A 1 212 ? 10.119  -10.434 -12.588 1.00 28.66  ? 213 LYS A CE  1 
ATOM   1747 N  NZ  . LYS A 1 212 ? 11.296  -10.598 -13.494 1.00 42.01  ? 213 LYS A NZ  1 
ATOM   1748 N  N   . GLU A 1 213 ? 9.849   -7.727  -7.266  1.00 8.42   ? 214 GLU A N   1 
ATOM   1749 C  CA  . GLU A 1 213 ? 10.425  -8.616  -6.251  1.00 9.60   ? 214 GLU A CA  1 
ATOM   1750 C  C   . GLU A 1 213 ? 9.683   -8.516  -4.964  1.00 8.40   ? 214 GLU A C   1 
ATOM   1751 O  O   . GLU A 1 213 ? 9.609   -7.416  -4.401  1.00 8.93   ? 214 GLU A O   1 
ATOM   1752 C  CB  . GLU A 1 213 ? 11.906  -8.283  -6.037  1.00 10.29  ? 214 GLU A CB  1 
ATOM   1753 C  CG  . GLU A 1 213 ? 12.568  -9.211  -5.053  1.00 12.51  ? 214 GLU A CG  1 
ATOM   1754 C  CD  . GLU A 1 213 ? 14.067  -9.081  -4.915  1.00 15.48  ? 214 GLU A CD  1 
ATOM   1755 O  OE1 . GLU A 1 213 ? 14.651  -8.124  -5.460  1.00 16.25  ? 214 GLU A OE1 1 
ATOM   1756 O  OE2 . GLU A 1 213 ? 14.656  -9.960  -4.250  1.00 22.19  ? 214 GLU A OE2 1 
ATOM   1757 N  N   A PRO A 1 214 ? 9.125   -9.615  -4.441  0.50 8.75   ? 215 PRO A N   1 
ATOM   1758 N  N   B PRO A 1 214 ? 9.095   -9.614  -4.494  0.50 9.27   ? 215 PRO A N   1 
ATOM   1759 C  CA  A PRO A 1 214 ? 8.429   -9.577  -3.151  0.50 8.63   ? 215 PRO A CA  1 
ATOM   1760 C  CA  B PRO A 1 214 ? 8.494   -9.548  -3.171  0.50 9.39   ? 215 PRO A CA  1 
ATOM   1761 C  C   A PRO A 1 214 ? 9.451   -9.592  -2.014  0.50 9.42   ? 215 PRO A C   1 
ATOM   1762 C  C   B PRO A 1 214 ? 9.573   -9.437  -2.068  0.50 8.60   ? 215 PRO A C   1 
ATOM   1763 O  O   A PRO A 1 214 ? 10.524  -10.116 -2.165  0.50 9.92   ? 215 PRO A O   1 
ATOM   1764 O  O   B PRO A 1 214 ? 10.793  -9.709  -2.321  0.50 9.71   ? 215 PRO A O   1 
ATOM   1765 C  CB  A PRO A 1 214 ? 7.671   -10.888 -3.149  0.50 8.95   ? 215 PRO A CB  1 
ATOM   1766 C  CB  B PRO A 1 214 ? 7.733   -10.879 -3.079  0.50 10.51  ? 215 PRO A CB  1 
ATOM   1767 C  CG  A PRO A 1 214 ? 8.579   -11.832 -3.902  0.50 8.81   ? 215 PRO A CG  1 
ATOM   1768 C  CG  B PRO A 1 214 ? 7.574   -11.359 -4.502  0.50 13.39  ? 215 PRO A CG  1 
ATOM   1769 C  CD  A PRO A 1 214 ? 9.261   -10.998 -4.972  0.50 9.33   ? 215 PRO A CD  1 
ATOM   1770 C  CD  B PRO A 1 214 ? 8.836   -10.907 -5.184  0.50 10.22  ? 215 PRO A CD  1 
ATOM   1771 N  N   . ILE A 1 215 ? 9.105   -9.066  -0.874  1.00 9.29   ? 216 ILE A N   1 
ATOM   1772 C  CA  . ILE A 1 215 ? 9.887   -9.313  0.340   1.00 9.84   ? 216 ILE A CA  1 
ATOM   1773 C  C   . ILE A 1 215 ? 9.376   -10.564 1.002   1.00 8.81   ? 216 ILE A C   1 
ATOM   1774 O  O   . ILE A 1 215 ? 8.187   -10.905 0.886   1.00 10.27  ? 216 ILE A O   1 
ATOM   1775 C  CB  . ILE A 1 215 ? 9.876   -8.110  1.267   1.00 11.03  ? 216 ILE A CB  1 
ATOM   1776 C  CG1 . ILE A 1 215 ? 8.484   -7.730  1.783   1.00 11.84  ? 216 ILE A CG1 1 
ATOM   1777 C  CG2 . ILE A 1 215 ? 10.605  -6.900  0.628   1.00 13.14  ? 216 ILE A CG2 1 
ATOM   1778 C  CD1 . ILE A 1 215 ? 8.537   -6.748  2.973   1.00 14.16  ? 216 ILE A CD1 1 
ATOM   1779 N  N   A SER A 1 216 ? 10.223  -11.236 1.764   0.50 9.85   ? 217 SER A N   1 
ATOM   1780 N  N   B SER A 1 216 ? 10.262  -11.216 1.746   0.50 10.74  ? 217 SER A N   1 
ATOM   1781 C  CA  A SER A 1 216 ? 9.773   -12.338 2.589   0.50 10.40  ? 217 SER A CA  1 
ATOM   1782 C  CA  B SER A 1 216 ? 9.934   -12.365 2.578   0.50 10.30  ? 217 SER A CA  1 
ATOM   1783 C  C   A SER A 1 216 ? 9.614   -11.878 4.009   0.50 10.41  ? 217 SER A C   1 
ATOM   1784 C  C   B SER A 1 216 ? 9.682   -11.923 3.996   0.50 10.29  ? 217 SER A C   1 
ATOM   1785 O  O   A SER A 1 216 ? 10.455  -11.159 4.589   0.50 11.81  ? 217 SER A O   1 
ATOM   1786 O  O   B SER A 1 216 ? 10.540  -11.185 4.532   0.50 11.47  ? 217 SER A O   1 
ATOM   1787 C  CB  A SER A 1 216 ? 10.777  -13.497 2.573   0.50 12.06  ? 217 SER A CB  1 
ATOM   1788 C  CB  B SER A 1 216 ? 11.067  -13.385 2.523   0.50 14.70  ? 217 SER A CB  1 
ATOM   1789 O  OG  A SER A 1 216 ? 11.006  -14.073 1.315   0.50 11.42  ? 217 SER A OG  1 
ATOM   1790 O  OG  B SER A 1 216 ? 10.570  -14.509 3.198   0.50 17.53  ? 217 SER A OG  1 
ATOM   1791 N  N   . VAL A 1 217 ? 8.562   -12.355 4.612   1.00 10.09  ? 218 VAL A N   1 
ATOM   1792 C  CA  . VAL A 1 217 ? 8.305   -12.176 6.041   1.00 10.55  ? 218 VAL A CA  1 
ATOM   1793 C  C   . VAL A 1 217 ? 8.033   -13.528 6.622   1.00 10.42  ? 218 VAL A C   1 
ATOM   1794 O  O   . VAL A 1 217 ? 7.674   -14.479 5.925   1.00 10.94  ? 218 VAL A O   1 
ATOM   1795 C  CB  . VAL A 1 217 ? 7.084   -11.237 6.273   1.00 11.30  ? 218 VAL A CB  1 
ATOM   1796 C  CG1 . VAL A 1 217 ? 7.330   -9.913  5.587   1.00 11.53  ? 218 VAL A CG1 1 
ATOM   1797 C  CG2 . VAL A 1 217 ? 5.812   -11.858 5.762   1.00 12.17  ? 218 VAL A CG2 1 
ATOM   1798 N  N   . SER A 1 218 ? 8.169   -13.707 7.941   1.00 11.00  ? 219 SER A N   1 
ATOM   1799 C  CA  . SER A 1 218 ? 7.967   -15.019 8.491   1.00 10.45  ? 219 SER A CA  1 
ATOM   1800 C  C   . SER A 1 218 ? 6.507   -15.277 8.760   1.00 10.69  ? 219 SER A C   1 
ATOM   1801 O  O   . SER A 1 218 ? 5.678   -14.349 8.926   1.00 11.17  ? 219 SER A O   1 
ATOM   1802 C  CB  . SER A 1 218 ? 8.798   -15.203 9.785   1.00 12.09  ? 219 SER A CB  1 
ATOM   1803 O  OG  . SER A 1 218 ? 8.286   -14.341 10.778  1.00 12.90  ? 219 SER A OG  1 
ATOM   1804 N  N   A SER A 1 219 ? 6.116   -16.546 8.929   0.50 10.74  ? 220 SER A N   1 
ATOM   1805 N  N   B SER A 1 219 ? 6.236   -16.556 8.882   0.50 10.90  ? 220 SER A N   1 
ATOM   1806 C  CA  A SER A 1 219 ? 4.746   -16.882 9.353   0.50 10.94  ? 220 SER A CA  1 
ATOM   1807 C  CA  B SER A 1 219 ? 4.928   -16.940 9.228   0.50 11.81  ? 220 SER A CA  1 
ATOM   1808 C  C   A SER A 1 219 ? 4.399   -16.240 10.668  0.50 12.60  ? 220 SER A C   1 
ATOM   1809 C  C   B SER A 1 219 ? 4.494   -16.254 10.536  0.50 11.87  ? 220 SER A C   1 
ATOM   1810 O  O   A SER A 1 219 ? 3.263   -15.813 10.920  0.50 13.33  ? 220 SER A O   1 
ATOM   1811 O  O   B SER A 1 219 ? 3.383   -15.761 10.624  0.50 12.96  ? 220 SER A O   1 
ATOM   1812 C  CB  A SER A 1 219 ? 4.620   -18.399 9.515   0.50 13.65  ? 220 SER A CB  1 
ATOM   1813 C  CB  B SER A 1 219 ? 4.851   -18.457 9.267   0.50 14.10  ? 220 SER A CB  1 
ATOM   1814 O  OG  A SER A 1 219 ? 5.672   -19.000 10.313  0.50 15.27  ? 220 SER A OG  1 
ATOM   1815 O  OG  B SER A 1 219 ? 3.520   -18.828 9.567   0.50 14.14  ? 220 SER A OG  1 
ATOM   1816 N  N   . GLU A 1 220 ? 5.406   -16.153 11.544  1.00 11.92  ? 221 GLU A N   1 
ATOM   1817 C  CA  . GLU A 1 220 ? 5.147   -15.542 12.818  1.00 14.21  ? 221 GLU A CA  1 
ATOM   1818 C  C   . GLU A 1 220 ? 4.836   -14.064 12.698  1.00 12.95  ? 221 GLU A C   1 
ATOM   1819 O  O   . GLU A 1 220 ? 3.985   -13.522 13.431  1.00 14.14  ? 221 GLU A O   1 
ATOM   1820 C  CB  . GLU A 1 220 ? 6.297   -15.740 13.796  1.00 17.45  ? 221 GLU A CB  1 
ATOM   1821 C  CG  . GLU A 1 220 ? 6.453   -17.252 14.231  1.00 23.35  ? 221 GLU A CG  1 
ATOM   1822 C  CD  . GLU A 1 220 ? 7.429   -18.010 13.321  1.00 28.87  ? 221 GLU A CD  1 
ATOM   1823 O  OE1 . GLU A 1 220 ? 7.877   -17.520 12.254  1.00 23.17  ? 221 GLU A OE1 1 
ATOM   1824 O  OE2 . GLU A 1 220 ? 7.781   -19.145 13.712  1.00 73.90  ? 221 GLU A OE2 1 
ATOM   1825 N  N   . GLN A 1 221 ? 5.517   -13.370 11.799  1.00 12.26  ? 222 GLN A N   1 
ATOM   1826 C  CA  . GLN A 1 221 ? 5.233   -11.937 11.595  1.00 11.94  ? 222 GLN A CA  1 
ATOM   1827 C  C   . GLN A 1 221 ? 3.794   -11.699 11.045  1.00 11.56  ? 222 GLN A C   1 
ATOM   1828 O  O   . GLN A 1 221 ? 3.067   -10.891 11.577  1.00 12.39  ? 222 GLN A O   1 
ATOM   1829 C  CB  . GLN A 1 221 ? 6.300   -11.380 10.659  1.00 11.68  ? 222 GLN A CB  1 
ATOM   1830 C  CG  . GLN A 1 221 ? 7.648   -11.253 11.357  1.00 11.58  ? 222 GLN A CG  1 
ATOM   1831 C  CD  . GLN A 1 221 ? 8.739   -10.689 10.485  1.00 11.28  ? 222 GLN A CD  1 
ATOM   1832 O  OE1 . GLN A 1 221 ? 8.885   -11.076 9.293   1.00 11.58  ? 222 GLN A OE1 1 
ATOM   1833 N  NE2 . GLN A 1 221 ? 9.589   -9.819  11.041  1.00 12.63  ? 222 GLN A NE2 1 
ATOM   1834 N  N   . VAL A 1 222 ? 3.427   -12.488 10.023  1.00 11.31  ? 223 VAL A N   1 
ATOM   1835 C  CA  . VAL A 1 222 ? 2.087   -12.288 9.486   1.00 11.73  ? 223 VAL A CA  1 
ATOM   1836 C  C   . VAL A 1 222 ? 1.003   -12.749 10.455  1.00 11.99  ? 223 VAL A C   1 
ATOM   1837 O  O   . VAL A 1 222 ? -0.077  -12.158 10.497  1.00 12.90  ? 223 VAL A O   1 
ATOM   1838 C  CB  . VAL A 1 222 ? 1.944   -12.829 8.026   1.00 14.62  ? 223 VAL A CB  1 
ATOM   1839 C  CG1 . VAL A 1 222 ? 2.018   -14.325 8.003   1.00 15.73  ? 223 VAL A CG1 1 
ATOM   1840 C  CG2 . VAL A 1 222 ? 0.690   -12.280 7.363   1.00 16.67  ? 223 VAL A CG2 1 
ATOM   1841 N  N   . LEU A 1 223 ? 1.289   -13.772 11.248  1.00 12.53  ? 224 LEU A N   1 
ATOM   1842 C  CA  . LEU A 1 223 ? 0.362   -14.176 12.255  1.00 15.22  ? 224 LEU A CA  1 
ATOM   1843 C  C   . LEU A 1 223 ? 0.050   -13.044 13.227  1.00 13.76  ? 224 LEU A C   1 
ATOM   1844 O  O   . LEU A 1 223 ? -1.130  -12.921 13.664  1.00 14.46  ? 224 LEU A O   1 
ATOM   1845 C  CB  . LEU A 1 223 ? 0.864   -15.437 12.932  1.00 15.98  ? 224 LEU A CB  1 
ATOM   1846 C  CG  . LEU A 1 223 ? 0.600   -16.716 12.097  1.00 18.48  ? 224 LEU A CG  1 
ATOM   1847 C  CD1 . LEU A 1 223 ? 1.514   -17.804 12.655  1.00 21.44  ? 224 LEU A CD1 1 
ATOM   1848 C  CD2 . LEU A 1 223 ? -0.839  -17.193 12.115  1.00 22.17  ? 224 LEU A CD2 1 
ATOM   1849 N  N   . LYS A 1 224 ? 1.041   -12.200 13.518  1.00 13.44  ? 225 LYS A N   1 
ATOM   1850 C  CA  . LYS A 1 224 ? 0.800   -11.106 14.410  1.00 13.84  ? 225 LYS A CA  1 
ATOM   1851 C  C   . LYS A 1 224 ? -0.092  -10.044 13.750  1.00 13.14  ? 225 LYS A C   1 
ATOM   1852 O  O   . LYS A 1 224 ? -0.894  -9.423  14.442  1.00 13.89  ? 225 LYS A O   1 
ATOM   1853 C  CB  . LYS A 1 224 ? 2.112   -10.588 15.005  1.00 16.78  ? 225 LYS A CB  1 
ATOM   1854 C  CG  . LYS A 1 224 ? 2.577   -11.615 16.060  1.00 19.84  ? 225 LYS A CG  1 
ATOM   1855 C  CD  . LYS A 1 224 ? 3.916   -11.336 16.705  1.00 22.17  ? 225 LYS A CD  1 
ATOM   1856 C  CE  . LYS A 1 224 ? 4.169   -12.276 17.856  1.00 36.80  ? 225 LYS A CE  1 
ATOM   1857 N  NZ  . LYS A 1 224 ? 5.574   -12.143 18.342  1.00 31.11  ? 225 LYS A NZ  1 
ATOM   1858 N  N   . PHE A 1 225 ? -0.028  -9.833  12.430  1.00 12.12  ? 226 PHE A N   1 
ATOM   1859 C  CA  . PHE A 1 225 ? -0.904  -8.914  11.760  1.00 11.91  ? 226 PHE A CA  1 
ATOM   1860 C  C   . PHE A 1 225 ? -2.348  -9.427  11.988  1.00 11.98  ? 226 PHE A C   1 
ATOM   1861 O  O   . PHE A 1 225 ? -3.286  -8.651  12.204  1.00 11.82  ? 226 PHE A O   1 
ATOM   1862 C  CB  . PHE A 1 225 ? -0.746  -8.898  10.242  1.00 12.04  ? 226 PHE A CB  1 
ATOM   1863 C  CG  . PHE A 1 225 ? 0.452   -8.142  9.706   1.00 11.36  ? 226 PHE A CG  1 
ATOM   1864 C  CD1 . PHE A 1 225 ? 1.509   -7.734  10.507  1.00 16.30  ? 226 PHE A CD1 1 
ATOM   1865 C  CD2 . PHE A 1 225 ? 0.515   -7.872  8.344   1.00 15.10  ? 226 PHE A CD2 1 
ATOM   1866 C  CE1 . PHE A 1 225 ? 2.590   -7.058  9.953   1.00 17.20  ? 226 PHE A CE1 1 
ATOM   1867 C  CE2 . PHE A 1 225 ? 1.586   -7.201  7.789   1.00 16.80  ? 226 PHE A CE2 1 
ATOM   1868 C  CZ  . PHE A 1 225 ? 2.628   -6.791  8.595   1.00 14.71  ? 226 PHE A CZ  1 
ATOM   1869 N  N   . ARG A 1 226 ? -2.516  -10.751 11.915  1.00 11.48  ? 227 ARG A N   1 
ATOM   1870 C  CA  . ARG A 1 226 ? -3.827  -11.353 11.953  1.00 12.68  ? 227 ARG A CA  1 
ATOM   1871 C  C   . ARG A 1 226 ? -4.409  -11.362 13.381  1.00 12.51  ? 227 ARG A C   1 
ATOM   1872 O  O   . ARG A 1 226 ? -5.548  -11.768 13.515  1.00 13.35  ? 227 ARG A O   1 
ATOM   1873 C  CB  . ARG A 1 226 ? -3.802  -12.794 11.404  1.00 13.07  ? 227 ARG A CB  1 
ATOM   1874 C  CG  . ARG A 1 226 ? -3.333  -12.894 9.953   1.00 12.43  ? 227 ARG A CG  1 
ATOM   1875 C  CD  . ARG A 1 226 ? -3.469  -14.336 9.522   1.00 14.38  ? 227 ARG A CD  1 
ATOM   1876 N  NE  . ARG A 1 226 ? -2.882  -14.493 8.166   1.00 12.67  ? 227 ARG A NE  1 
ATOM   1877 C  CZ  . ARG A 1 226 ? -1.953  -15.370 7.791   1.00 13.56  ? 227 ARG A CZ  1 
ATOM   1878 N  NH1 . ARG A 1 226 ? -1.486  -16.271 8.656   1.00 17.77  ? 227 ARG A NH1 1 
ATOM   1879 N  NH2 . ARG A 1 226 ? -1.421  -15.298 6.619   1.00 14.10  ? 227 ARG A NH2 1 
ATOM   1880 N  N   . LYS A 1 227 ? -3.694  -10.913 14.411  1.00 12.41  ? 228 LYS A N   1 
ATOM   1881 C  CA  . LYS A 1 227 ? -4.247  -10.769 15.770  1.00 14.05  ? 228 LYS A CA  1 
ATOM   1882 C  C   . LYS A 1 227 ? -4.853  -9.406  16.010  1.00 13.36  ? 228 LYS A C   1 
ATOM   1883 O  O   . LYS A 1 227 ? -5.508  -9.204  17.038  1.00 15.61  ? 228 LYS A O   1 
ATOM   1884 C  CB  . LYS A 1 227 ? -3.115  -10.993 16.769  1.00 15.51  ? 228 LYS A CB  1 
ATOM   1885 C  CG  . LYS A 1 227 ? -2.659  -12.423 16.813  1.00 17.89  ? 228 LYS A CG  1 
ATOM   1886 C  CD  . LYS A 1 227 ? -1.576  -12.632 17.869  1.00 25.81  ? 228 LYS A CD  1 
ATOM   1887 C  CE  . LYS A 1 227 ? -2.173  -12.716 19.260  1.00 36.78  ? 228 LYS A CE  1 
ATOM   1888 N  NZ  . LYS A 1 227 ? -1.208  -13.041 20.364  1.00 52.98  ? 228 LYS A NZ  1 
ATOM   1889 N  N   . LEU A 1 228 ? -4.604  -8.457  15.087  1.00 12.53  ? 229 LEU A N   1 
ATOM   1890 C  CA  . LEU A 1 228 ? -5.206  -7.186  15.190  1.00 12.50  ? 229 LEU A CA  1 
ATOM   1891 C  C   . LEU A 1 228 ? -6.685  -7.304  15.085  1.00 12.04  ? 229 LEU A C   1 
ATOM   1892 O  O   . LEU A 1 228 ? -7.262  -8.365  14.633  1.00 12.14  ? 229 LEU A O   1 
ATOM   1893 C  CB  . LEU A 1 228 ? -4.649  -6.225  14.112  1.00 12.29  ? 229 LEU A CB  1 
ATOM   1894 C  CG  . LEU A 1 228 ? -3.250  -5.730  14.310  1.00 12.41  ? 229 LEU A CG  1 
ATOM   1895 C  CD1 . LEU A 1 228 ? -2.761  -5.101  13.028  1.00 13.51  ? 229 LEU A CD1 1 
ATOM   1896 C  CD2 . LEU A 1 228 ? -3.192  -4.740  15.479  1.00 15.80  ? 229 LEU A CD2 1 
ATOM   1897 N  N   . ASN A 1 229 ? -7.381  -6.257  15.478  1.00 12.66  ? 230 ASN A N   1 
ATOM   1898 C  CA  . ASN A 1 229 ? -8.817  -6.292  15.440  1.00 12.13  ? 230 ASN A CA  1 
ATOM   1899 C  C   . ASN A 1 229 ? -9.400  -5.075  14.668  1.00 12.31  ? 230 ASN A C   1 
ATOM   1900 O  O   . ASN A 1 229 ? -8.962  -3.972  14.722  1.00 13.58  ? 230 ASN A O   1 
ATOM   1901 C  CB  . ASN A 1 229 ? -9.385  -6.083  16.882  1.00 13.95  ? 230 ASN A CB  1 
ATOM   1902 C  CG  . ASN A 1 229 ? -9.404  -7.293  17.809  1.00 15.26  ? 230 ASN A CG  1 
ATOM   1903 O  OD1 . ASN A 1 229 ? -9.965  -7.196  18.899  1.00 19.88  ? 230 ASN A OD1 1 
ATOM   1904 N  ND2 . ASN A 1 229 ? -8.789  -8.387  17.429  1.00 15.68  ? 230 ASN A ND2 1 
ATOM   1905 N  N   . PHE A 1 230 ? -10.448 -5.420  13.918  1.00 11.89  ? 231 PHE A N   1 
ATOM   1906 C  CA  . PHE A 1 230 ? -11.246 -4.334  13.221  1.00 12.17  ? 231 PHE A CA  1 
ATOM   1907 C  C   . PHE A 1 230 ? -12.170 -3.609  14.186  1.00 14.59  ? 231 PHE A C   1 
ATOM   1908 O  O   . PHE A 1 230 ? -12.509 -2.464  13.953  1.00 16.29  ? 231 PHE A O   1 
ATOM   1909 C  CB  . PHE A 1 230 ? -12.243 -4.939  12.261  1.00 13.34  ? 231 PHE A CB  1 
ATOM   1910 C  CG  . PHE A 1 230 ? -11.689 -5.530  10.915  1.00 12.16  ? 231 PHE A CG  1 
ATOM   1911 C  CD1 . PHE A 1 230 ? -10.900 -4.776  10.033  1.00 13.49  ? 231 PHE A CD1 1 
ATOM   1912 C  CD2 . PHE A 1 230 ? -12.068 -6.748  10.514  1.00 13.05  ? 231 PHE A CD2 1 
ATOM   1913 C  CE1 . PHE A 1 230 ? -10.453 -5.323  8.847   1.00 14.33  ? 231 PHE A CE1 1 
ATOM   1914 C  CE2 . PHE A 1 230 ? -11.626 -7.330  9.297   1.00 14.18  ? 231 PHE A CE2 1 
ATOM   1915 C  CZ  . PHE A 1 230 ? -10.882 -6.578  8.461   1.00 12.80  ? 231 PHE A CZ  1 
ATOM   1916 N  N   . ASN A 1 231 ? -12.633 -4.282  15.229  1.00 14.36  ? 232 ASN A N   1 
ATOM   1917 C  CA  . ASN A 1 231 ? -13.469 -3.682  16.290  1.00 15.01  ? 232 ASN A CA  1 
ATOM   1918 C  C   . ASN A 1 231 ? -12.639 -2.803  17.193  1.00 12.04  ? 232 ASN A C   1 
ATOM   1919 O  O   . ASN A 1 231 ? -11.428 -2.809  17.322  1.00 14.62  ? 232 ASN A O   1 
ATOM   1920 C  CB  . ASN A 1 231 ? -14.068 -4.793  17.116  1.00 16.09  ? 232 ASN A CB  1 
ATOM   1921 C  CG  . ASN A 1 231 ? -12.992 -5.689  17.663  1.00 15.15  ? 232 ASN A CG  1 
ATOM   1922 O  OD1 . ASN A 1 231 ? -12.513 -6.546  16.942  1.00 17.33  ? 232 ASN A OD1 1 
ATOM   1923 N  ND2 . ASN A 1 231 ? -12.664 -5.522  18.945  1.00 16.77  ? 232 ASN A ND2 1 
ATOM   1924 N  N   . GLY A 1 232 ? -13.418 -1.916  17.910  1.00 15.55  ? 233 GLY A N   1 
ATOM   1925 C  CA  . GLY A 1 232 ? -12.874 -1.112  19.006  1.00 15.78  ? 233 GLY A CA  1 
ATOM   1926 C  C   . GLY A 1 232 ? -12.827 -1.882  20.311  1.00 14.30  ? 233 GLY A C   1 
ATOM   1927 O  O   . GLY A 1 232 ? -13.426 -2.956  20.405  1.00 18.01  ? 233 GLY A O   1 
ATOM   1928 N  N   . GLU A 1 233 ? -12.085 -1.313  21.252  1.00 14.46  ? 234 GLU A N   1 
ATOM   1929 C  CA  . GLU A 1 233 ? -12.036 -1.847  22.600  1.00 15.14  ? 234 GLU A CA  1 
ATOM   1930 C  C   . GLU A 1 233 ? -13.438 -1.979  23.176  1.00 16.66  ? 234 GLU A C   1 
ATOM   1931 O  O   . GLU A 1 233 ? -14.279 -1.111  23.006  1.00 18.60  ? 234 GLU A O   1 
ATOM   1932 C  CB  . GLU A 1 233 ? -11.137 -1.001  23.441  1.00 16.37  ? 234 GLU A CB  1 
ATOM   1933 C  CG  . GLU A 1 233 ? -10.836 -1.571  24.821  1.00 17.76  ? 234 GLU A CG  1 
ATOM   1934 C  CD  . GLU A 1 233 ? -10.058 -0.568  25.658  1.00 27.59  ? 234 GLU A CD  1 
ATOM   1935 O  OE1 . GLU A 1 233 ? -9.810  0.586   25.137  1.00 25.93  ? 234 GLU A OE1 1 
ATOM   1936 O  OE2 . GLU A 1 233 ? -9.709  -0.927  26.841  1.00 25.84  ? 234 GLU A OE2 1 
ATOM   1937 N  N   . GLY A 1 234 ? -13.694 -3.119  23.803  1.00 20.19  ? 235 GLY A N   1 
ATOM   1938 C  CA  . GLY A 1 234 ? -14.992 -3.323  24.465  1.00 21.13  ? 235 GLY A CA  1 
ATOM   1939 C  C   . GLY A 1 234 ? -16.110 -3.772  23.511  1.00 21.91  ? 235 GLY A C   1 
ATOM   1940 O  O   . GLY A 1 234 ? -17.323 -3.794  23.849  1.00 27.45  ? 235 GLY A O   1 
ATOM   1941 N  N   . GLU A 1 235 ? -15.707 -4.148  22.303  1.00 17.80  ? 236 GLU A N   1 
ATOM   1942 C  CA  . GLU A 1 235 ? -16.659 -4.682  21.338  1.00 17.33  ? 236 GLU A CA  1 
ATOM   1943 C  C   . GLU A 1 235 ? -16.203 -6.107  21.015  1.00 18.23  ? 236 GLU A C   1 
ATOM   1944 O  O   . GLU A 1 235 ? -15.014 -6.515  21.199  1.00 20.44  ? 236 GLU A O   1 
ATOM   1945 C  CB  . GLU A 1 235 ? -16.580 -3.900  20.033  1.00 18.02  ? 236 GLU A CB  1 
ATOM   1946 C  CG  . GLU A 1 235 ? -16.985 -2.459  20.238  1.00 21.81  ? 236 GLU A CG  1 
ATOM   1947 C  CD  . GLU A 1 235 ? -16.875 -1.604  18.982  1.00 29.90  ? 236 GLU A CD  1 
ATOM   1948 O  OE1 . GLU A 1 235 ? -16.221 -2.019  17.993  1.00 20.85  ? 236 GLU A OE1 1 
ATOM   1949 O  OE2 . GLU A 1 235 ? -17.493 -0.526  18.961  1.00 32.53  ? 236 GLU A OE2 1 
ATOM   1950 N  N   . PRO A 1 236 ? -17.097 -6.897  20.495  1.00 16.86  ? 237 PRO A N   1 
ATOM   1951 C  CA  . PRO A 1 236 ? -16.747 -8.326  20.268  1.00 18.55  ? 237 PRO A CA  1 
ATOM   1952 C  C   . PRO A 1 236 ? -15.636 -8.404  19.219  1.00 15.92  ? 237 PRO A C   1 
ATOM   1953 O  O   . PRO A 1 236 ? -15.601 -7.579  18.244  1.00 17.68  ? 237 PRO A O   1 
ATOM   1954 C  CB  . PRO A 1 236 ? -18.018 -8.929  19.721  1.00 18.32  ? 237 PRO A CB  1 
ATOM   1955 C  CG  . PRO A 1 236 ? -19.109 -8.134  20.442  1.00 23.95  ? 237 PRO A CG  1 
ATOM   1956 C  CD  . PRO A 1 236 ? -18.554 -6.717  20.270  1.00 22.57  ? 237 PRO A CD  1 
ATOM   1957 N  N   . GLU A 1 237 ? -14.811 -9.445  19.309  1.00 18.10  ? 238 GLU A N   1 
ATOM   1958 C  CA  . GLU A 1 237 ? -13.627 -9.510  18.479  1.00 19.04  ? 238 GLU A CA  1 
ATOM   1959 C  C   . GLU A 1 237 ? -13.907 -9.798  17.014  1.00 16.04  ? 238 GLU A C   1 
ATOM   1960 O  O   . GLU A 1 237 ? -14.588 -10.745 16.740  1.00 15.59  ? 238 GLU A O   1 
ATOM   1961 C  CB  . GLU A 1 237 ? -12.656 -10.556 18.969  1.00 19.12  ? 238 GLU A CB  1 
ATOM   1962 C  CG  . GLU A 1 237 ? -11.348 -10.520 18.214  1.00 22.57  ? 238 GLU A CG  1 
ATOM   1963 C  CD  . GLU A 1 237 ? -10.216 -11.237 18.936  1.00 19.93  ? 238 GLU A CD  1 
ATOM   1964 O  OE1 . GLU A 1 237 ? -10.473 -12.442 19.277  1.00 28.85  ? 238 GLU A OE1 1 
ATOM   1965 O  OE2 . GLU A 1 237 ? -9.077  -10.640 19.115  1.00 19.76  ? 238 GLU A OE2 1 
ATOM   1966 N  N   . GLU A 1 238 ? -13.362 -9.019  16.114  1.00 13.61  ? 239 GLU A N   1 
ATOM   1967 C  CA  . GLU A 1 238 ? -13.434 -9.182  14.706  1.00 13.68  ? 239 GLU A CA  1 
ATOM   1968 C  C   . GLU A 1 238 ? -11.989 -9.103  14.227  1.00 11.34  ? 239 GLU A C   1 
ATOM   1969 O  O   . GLU A 1 238 ? -11.427 -8.067  14.143  1.00 15.44  ? 239 GLU A O   1 
ATOM   1970 C  CB  . GLU A 1 238 ? -14.208 -8.107  14.021  1.00 18.09  ? 239 GLU A CB  1 
ATOM   1971 C  CG  . GLU A 1 238 ? -15.668 -7.834  14.371  1.00 20.66  ? 239 GLU A CG  1 
ATOM   1972 C  CD  . GLU A 1 238 ? -16.159 -6.482  13.830  1.00 30.95  ? 239 GLU A CD  1 
ATOM   1973 O  OE1 . GLU A 1 238 ? -16.125 -6.262  12.597  1.00 32.22  ? 239 GLU A OE1 1 
ATOM   1974 O  OE2 . GLU A 1 238 ? -16.585 -5.627  14.638  1.00 36.77  ? 239 GLU A OE2 1 
ATOM   1975 N  N   . LEU A 1 239 ? -11.400 -10.338 13.904  1.00 13.21  ? 240 LEU A N   1 
ATOM   1976 C  CA  . LEU A 1 239 ? -9.997  -10.319 13.565  1.00 11.48  ? 240 LEU A CA  1 
ATOM   1977 C  C   . LEU A 1 239 ? -9.766  -9.472  12.307  1.00 11.61  ? 240 LEU A C   1 
ATOM   1978 O  O   . LEU A 1 239 ? -10.556 -9.642  11.343  1.00 12.99  ? 240 LEU A O   1 
ATOM   1979 C  CB  . LEU A 1 239 ? -9.457  -11.737 13.374  1.00 12.93  ? 240 LEU A CB  1 
ATOM   1980 C  CG  . LEU A 1 239 ? -9.404  -12.587 14.620  1.00 13.30  ? 240 LEU A CG  1 
ATOM   1981 C  CD1 . LEU A 1 239 ? -8.858  -13.929 14.131  1.00 20.35  ? 240 LEU A CD1 1 
ATOM   1982 C  CD2 . LEU A 1 239 ? -8.583  -11.946 15.694  1.00 14.93  ? 240 LEU A CD2 1 
ATOM   1983 N  N   . MET A 1 240 ? -8.750  -8.632  12.302  1.00 12.30  ? 241 MET A N   1 
ATOM   1984 C  CA  . MET A 1 240 ? -8.380  -7.838  11.138  1.00 12.13  ? 241 MET A CA  1 
ATOM   1985 C  C   . MET A 1 240 ? -7.587  -8.745  10.184  1.00 10.19  ? 241 MET A C   1 
ATOM   1986 O  O   . MET A 1 240 ? -6.435  -8.921  10.272  1.00 11.48  ? 241 MET A O   1 
ATOM   1987 C  CB  . MET A 1 240 ? -7.551  -6.665  11.603  1.00 12.37  ? 241 MET A CB  1 
ATOM   1988 C  CG  . MET A 1 240 ? -7.227  -5.706  10.458  1.00 13.35  ? 241 MET A CG  1 
ATOM   1989 S  SD  . MET A 1 240 ? -6.237  -4.295  10.990  1.00 13.50  ? 241 MET A SD  1 
ATOM   1990 C  CE  . MET A 1 240 ? -7.522  -3.249  11.723  1.00 14.08  ? 241 MET A CE  1 
ATOM   1991 N  N   . VAL A 1 241 ? -8.392  -9.354  9.267   1.00 10.89  ? 242 VAL A N   1 
ATOM   1992 C  CA  . VAL A 1 241 ? -7.917  -10.246 8.179   1.00 9.80   ? 242 VAL A CA  1 
ATOM   1993 C  C   . VAL A 1 241 ? -8.716  -9.986  6.919   1.00 9.64   ? 242 VAL A C   1 
ATOM   1994 O  O   . VAL A 1 241 ? -9.854  -9.564  6.999   1.00 10.53  ? 242 VAL A O   1 
ATOM   1995 C  CB  . VAL A 1 241 ? -8.002  -11.765 8.558   1.00 10.41  ? 242 VAL A CB  1 
ATOM   1996 C  CG1 . VAL A 1 241 ? -7.064  -12.084 9.739   1.00 13.24  ? 242 VAL A CG1 1 
ATOM   1997 C  CG2 . VAL A 1 241 ? -9.386  -12.166 8.853   1.00 12.28  ? 242 VAL A CG2 1 
ATOM   1998 N  N   . ASP A 1 242 ? -8.090  -10.292 5.769   1.00 9.64   ? 243 ASP A N   1 
ATOM   1999 C  CA  . ASP A 1 242 ? -8.808  -10.166 4.499   1.00 8.79   ? 243 ASP A CA  1 
ATOM   2000 C  C   . ASP A 1 242 ? -9.268  -8.742  4.233   1.00 9.34   ? 243 ASP A C   1 
ATOM   2001 O  O   . ASP A 1 242 ? -10.394 -8.504  3.803   1.00 10.49  ? 243 ASP A O   1 
ATOM   2002 C  CB  . ASP A 1 242 ? -9.906  -11.220 4.282   1.00 9.98   ? 243 ASP A CB  1 
ATOM   2003 C  CG  . ASP A 1 242 ? -9.312  -12.624 4.176   1.00 10.07  ? 243 ASP A CG  1 
ATOM   2004 O  OD1 . ASP A 1 242 ? -8.256  -12.780 3.524   1.00 9.56   ? 243 ASP A OD1 1 
ATOM   2005 O  OD2 . ASP A 1 242 ? -9.888  -13.558 4.790   1.00 12.26  ? 243 ASP A OD2 1 
ATOM   2006 N  N   . ASN A 1 243 ? -8.392  -7.790  4.500   1.00 8.81   ? 244 ASN A N   1 
ATOM   2007 C  CA  . ASN A 1 243 ? -8.655  -6.352  4.293   1.00 8.98   ? 244 ASN A CA  1 
ATOM   2008 C  C   . ASN A 1 243 ? -8.138  -5.905  2.907   1.00 7.93   ? 244 ASN A C   1 
ATOM   2009 O  O   . ASN A 1 243 ? -7.519  -4.866  2.800   1.00 9.25   ? 244 ASN A O   1 
ATOM   2010 C  CB  . ASN A 1 243 ? -8.093  -5.511  5.446   1.00 9.36   ? 244 ASN A CB  1 
ATOM   2011 C  CG  . ASN A 1 243 ? -6.647  -5.720  5.657   1.00 9.16   ? 244 ASN A CG  1 
ATOM   2012 O  OD1 . ASN A 1 243 ? -5.998  -6.518  5.010   1.00 9.92   ? 244 ASN A OD1 1 
ATOM   2013 N  ND2 . ASN A 1 243 ? -6.064  -4.933  6.586   1.00 14.10  ? 244 ASN A ND2 1 
ATOM   2014 N  N   . TRP A 1 244 ? -8.400  -6.728  1.883   1.00 7.76   ? 245 TRP A N   1 
ATOM   2015 C  CA  . TRP A 1 244 ? -7.989  -6.465  0.518   1.00 7.61   ? 245 TRP A CA  1 
ATOM   2016 C  C   . TRP A 1 244 ? -9.187  -6.372  -0.404  1.00 7.79   ? 245 TRP A C   1 
ATOM   2017 O  O   . TRP A 1 244 ? -10.164 -7.100  -0.283  1.00 9.49   ? 245 TRP A O   1 
ATOM   2018 C  CB  . TRP A 1 244 ? -7.010  -7.561  0.010   1.00 7.51   ? 245 TRP A CB  1 
ATOM   2019 C  CG  . TRP A 1 244 ? -7.469  -8.959  0.199   1.00 7.19   ? 245 TRP A CG  1 
ATOM   2020 C  CD1 . TRP A 1 244 ? -7.350  -9.723  1.338   1.00 7.97   ? 245 TRP A CD1 1 
ATOM   2021 C  CD2 . TRP A 1 244 ? -8.073  -9.831  -0.734  1.00 7.95   ? 245 TRP A CD2 1 
ATOM   2022 N  NE1 . TRP A 1 244 ? -7.851  -10.982 1.181   1.00 8.48   ? 245 TRP A NE1 1 
ATOM   2023 C  CE2 . TRP A 1 244 ? -8.320  -11.065 -0.102  1.00 8.84   ? 245 TRP A CE2 1 
ATOM   2024 C  CE3 . TRP A 1 244 ? -8.381  -9.683  -2.111  1.00 9.20   ? 245 TRP A CE3 1 
ATOM   2025 C  CZ2 . TRP A 1 244 ? -8.891  -12.156 -0.791  1.00 10.18  ? 245 TRP A CZ2 1 
ATOM   2026 C  CZ3 . TRP A 1 244 ? -8.927  -10.780 -2.787  1.00 10.95  ? 245 TRP A CZ3 1 
ATOM   2027 C  CH2 . TRP A 1 244 ? -9.186  -11.995 -2.117  1.00 10.43  ? 245 TRP A CH2 1 
ATOM   2028 N  N   . ARG A 1 245 ? -9.054  -5.473  -1.370  1.00 7.58   ? 246 ARG A N   1 
ATOM   2029 C  CA  . ARG A 1 245 ? -10.023 -5.362  -2.482  1.00 7.30   ? 246 ARG A CA  1 
ATOM   2030 C  C   . ARG A 1 245 ? -9.529  -6.296  -3.619  1.00 7.21   ? 246 ARG A C   1 
ATOM   2031 O  O   . ARG A 1 245 ? -8.337  -6.275  -3.944  1.00 8.10   ? 246 ARG A O   1 
ATOM   2032 C  CB  . ARG A 1 245 ? -10.076 -3.909  -2.974  1.00 7.83   ? 246 ARG A CB  1 
ATOM   2033 C  CG  . ARG A 1 245 ? -11.172 -3.685  -3.986  1.00 8.42   ? 246 ARG A CG  1 
ATOM   2034 C  CD  . ARG A 1 245 ? -11.123 -2.303  -4.610  1.00 8.41   ? 246 ARG A CD  1 
ATOM   2035 N  NE  . ARG A 1 245 ? -12.345 -2.012  -5.349  1.00 8.87   ? 246 ARG A NE  1 
ATOM   2036 C  CZ  . ARG A 1 245 ? -12.554 -1.013  -6.169  1.00 8.56   ? 246 ARG A CZ  1 
ATOM   2037 N  NH1 . ARG A 1 245 ? -11.576 -0.224  -6.553  1.00 9.47   ? 246 ARG A NH1 1 
ATOM   2038 N  NH2 . ARG A 1 245 ? -13.809 -0.768  -6.613  1.00 10.48  ? 246 ARG A NH2 1 
ATOM   2039 N  N   A PRO A 1 246 ? -10.476 -7.062  -4.225  0.50 8.45   ? 247 PRO A N   1 
ATOM   2040 N  N   B PRO A 1 246 ? -10.424 -7.074  -4.229  0.50 8.72   ? 247 PRO A N   1 
ATOM   2041 C  CA  A PRO A 1 246 ? -10.078 -7.905  -5.345  0.50 8.37   ? 247 PRO A CA  1 
ATOM   2042 C  CA  B PRO A 1 246 ? -9.982  -7.902  -5.339  0.50 8.63   ? 247 PRO A CA  1 
ATOM   2043 C  C   A PRO A 1 246 ? -9.729  -7.092  -6.576  0.50 7.95   ? 247 PRO A C   1 
ATOM   2044 C  C   B PRO A 1 246 ? -9.646  -7.081  -6.565  0.50 8.11   ? 247 PRO A C   1 
ATOM   2045 O  O   A PRO A 1 246 ? -10.092 -5.913  -6.725  0.50 8.08   ? 247 PRO A O   1 
ATOM   2046 O  O   B PRO A 1 246 ? -9.991  -5.909  -6.721  0.50 8.44   ? 247 PRO A O   1 
ATOM   2047 C  CB  A PRO A 1 246 ? -11.332 -8.768  -5.600  0.50 10.84  ? 247 PRO A CB  1 
ATOM   2048 C  CB  B PRO A 1 246 ? -11.205 -8.797  -5.609  0.50 12.00  ? 247 PRO A CB  1 
ATOM   2049 C  CG  A PRO A 1 246 ? -12.103 -8.717  -4.353  0.50 11.90  ? 247 PRO A CG  1 
ATOM   2050 C  CG  B PRO A 1 246 ? -12.355 -8.003  -5.175  0.50 14.66  ? 247 PRO A CG  1 
ATOM   2051 C  CD  A PRO A 1 246 ? -11.868 -7.333  -3.801  0.50 10.49  ? 247 PRO A CD  1 
ATOM   2052 C  CD  B PRO A 1 246 ? -11.877 -7.242  -3.957  0.50 11.64  ? 247 PRO A CD  1 
ATOM   2053 N  N   . ALA A 1 247 ? -9.052  -7.747  -7.539  1.00 8.42   ? 248 ALA A N   1 
ATOM   2054 C  CA  . ALA A 1 247 ? -8.716  -7.119  -8.808  1.00 8.47   ? 248 ALA A CA  1 
ATOM   2055 C  C   . ALA A 1 247 ? -9.928  -6.614  -9.561  1.00 8.32   ? 248 ALA A C   1 
ATOM   2056 O  O   . ALA A 1 247 ? -10.978 -7.285  -9.579  1.00 10.34  ? 248 ALA A O   1 
ATOM   2057 C  CB  . ALA A 1 247 ? -7.931  -8.109  -9.659  1.00 10.66  ? 248 ALA A CB  1 
ATOM   2058 N  N   . GLN A 1 248 ? -9.786  -5.421  -10.129 1.00 8.49   ? 249 GLN A N   1 
ATOM   2059 C  CA  . GLN A 1 248 ? -10.835 -4.703  -10.864 1.00 9.27   ? 249 GLN A CA  1 
ATOM   2060 C  C   . GLN A 1 248 ? -10.525 -4.730  -12.353 1.00 9.28   ? 249 GLN A C   1 
ATOM   2061 O  O   . GLN A 1 248 ? -9.387  -4.945  -12.768 1.00 9.87   ? 249 GLN A O   1 
ATOM   2062 C  CB  . GLN A 1 248 ? -10.878 -3.278  -10.347 1.00 9.73   ? 249 GLN A CB  1 
ATOM   2063 C  CG  . GLN A 1 248 ? -11.218 -3.185  -8.831  1.00 9.62   ? 249 GLN A CG  1 
ATOM   2064 C  CD  . GLN A 1 248 ? -12.535 -3.859  -8.505  1.00 11.05  ? 249 GLN A CD  1 
ATOM   2065 O  OE1 . GLN A 1 248 ? -13.559 -3.542  -9.107  1.00 13.65  ? 249 GLN A OE1 1 
ATOM   2066 N  NE2 . GLN A 1 248 ? -12.545 -4.805  -7.536  1.00 12.16  ? 249 GLN A NE2 1 
ATOM   2067 N  N   . PRO A 1 249 ? -11.534 -4.416  -13.191 1.00 11.15  ? 250 PRO A N   1 
ATOM   2068 C  CA  . PRO A 1 249 ? -11.345 -4.442  -14.660 1.00 13.24  ? 250 PRO A CA  1 
ATOM   2069 C  C   . PRO A 1 249 ? -10.275 -3.454  -15.074 1.00 10.99  ? 250 PRO A C   1 
ATOM   2070 O  O   . PRO A 1 249 ? -10.285 -2.282  -14.705 1.00 11.22  ? 250 PRO A O   1 
ATOM   2071 C  CB  . PRO A 1 249 ? -12.751 -4.060  -15.170 1.00 15.53  ? 250 PRO A CB  1 
ATOM   2072 C  CG  . PRO A 1 249 ? -13.706 -4.541  -14.136 1.00 16.75  ? 250 PRO A CG  1 
ATOM   2073 C  CD  . PRO A 1 249 ? -12.949 -4.204  -12.824 1.00 14.27  ? 250 PRO A CD  1 
ATOM   2074 N  N   . LEU A 1 250 ? -9.408  -3.938  -15.957 1.00 11.60  ? 251 LEU A N   1 
ATOM   2075 C  CA  . LEU A 1 250 ? -8.326  -3.081  -16.478 1.00 10.59  ? 251 LEU A CA  1 
ATOM   2076 C  C   . LEU A 1 250 ? -8.840  -1.998  -17.385 1.00 10.30  ? 251 LEU A C   1 
ATOM   2077 O  O   . LEU A 1 250 ? -8.274  -0.906  -17.463 1.00 10.82  ? 251 LEU A O   1 
ATOM   2078 C  CB  . LEU A 1 250 ? -7.314  -3.932  -17.240 1.00 12.15  ? 251 LEU A CB  1 
ATOM   2079 C  CG  . LEU A 1 250 ? -5.985  -3.233  -17.620 1.00 13.30  ? 251 LEU A CG  1 
ATOM   2080 C  CD1 . LEU A 1 250 ? -5.203  -2.642  -16.408 1.00 12.92  ? 251 LEU A CD1 1 
ATOM   2081 C  CD2 . LEU A 1 250 ? -5.069  -4.195  -18.385 1.00 16.67  ? 251 LEU A CD2 1 
ATOM   2082 N  N   A LYS A 1 251 ? -9.926  -2.267  -18.099 0.50 12.42  ? 252 LYS A N   1 
ATOM   2083 N  N   B LYS A 1 251 ? -9.914  -2.283  -18.113 0.50 12.52  ? 252 LYS A N   1 
ATOM   2084 C  CA  A LYS A 1 251 ? -10.551 -1.238  -18.978 0.50 13.36  ? 252 LYS A CA  1 
ATOM   2085 C  CA  B LYS A 1 251 ? -10.553 -1.258  -18.985 0.50 13.77  ? 252 LYS A CA  1 
ATOM   2086 C  C   A LYS A 1 251 ? -9.525  -0.697  -19.936 0.50 13.48  ? 252 LYS A C   1 
ATOM   2087 C  C   B LYS A 1 251 ? -9.528  -0.697  -19.949 0.50 13.69  ? 252 LYS A C   1 
ATOM   2088 O  O   A LYS A 1 251 ? -8.734  -1.498  -20.471 0.50 15.64  ? 252 LYS A O   1 
ATOM   2089 O  O   B LYS A 1 251 ? -8.734  -1.480  -20.496 0.50 15.60  ? 252 LYS A O   1 
ATOM   2090 C  CB  A LYS A 1 251 ? -11.333 -0.198  -18.187 0.50 15.41  ? 252 LYS A CB  1 
ATOM   2091 C  CB  B LYS A 1 251 ? -11.345 -0.229  -18.173 0.50 15.44  ? 252 LYS A CB  1 
ATOM   2092 C  CG  A LYS A 1 251 ? -12.447 -0.885  -17.443 0.50 18.41  ? 252 LYS A CG  1 
ATOM   2093 C  CG  B LYS A 1 251 ? -12.510 -0.886  -17.459 0.50 18.79  ? 252 LYS A CG  1 
ATOM   2094 C  CD  A LYS A 1 251 ? -13.353 0.078   -16.721 0.50 21.23  ? 252 LYS A CD  1 
ATOM   2095 C  CD  B LYS A 1 251 ? -13.402 0.116   -16.751 0.50 21.78  ? 252 LYS A CD  1 
ATOM   2096 C  CE  A LYS A 1 251 ? -14.592 -0.642  -16.330 0.50 23.93  ? 252 LYS A CE  1 
ATOM   2097 C  CE  B LYS A 1 251 ? -14.783 -0.431  -16.576 0.50 26.46  ? 252 LYS A CE  1 
ATOM   2098 N  NZ  A LYS A 1 251 ? -15.431 0.184   -15.433 0.50 20.78  ? 252 LYS A NZ  1 
ATOM   2099 N  NZ  B LYS A 1 251 ? -15.289 -1.006  -17.854 0.50 30.59  ? 252 LYS A NZ  1 
ATOM   2100 N  N   . ASN A 1 252 ? -9.500  0.597   -20.190 1.00 13.91  ? 253 ASN A N   1 
ATOM   2101 C  CA  . ASN A 1 252 ? -8.623  1.084   -21.217 1.00 19.46  ? 253 ASN A CA  1 
ATOM   2102 C  C   . ASN A 1 252 ? -7.316  1.510   -20.632 1.00 19.53  ? 253 ASN A C   1 
ATOM   2103 O  O   . ASN A 1 252 ? -7.024  2.699   -20.606 1.00 21.86  ? 253 ASN A O   1 
ATOM   2104 C  CB  . ASN A 1 252 ? -9.383  2.228   -21.975 1.00 24.10  ? 253 ASN A CB  1 
ATOM   2105 C  CG  . ASN A 1 252 ? -8.652  2.695   -23.197 1.00 26.40  ? 253 ASN A CG  1 
ATOM   2106 O  OD1 . ASN A 1 252 ? -8.183  1.895   -24.020 1.00 48.91  ? 253 ASN A OD1 1 
ATOM   2107 N  ND2 . ASN A 1 252 ? -8.504  4.017   -23.320 1.00 28.01  ? 253 ASN A ND2 1 
ATOM   2108 N  N   . ARG A 1 253 ? -6.513  0.490   -20.046 1.00 14.11  ? 254 ARG A N   1 
ATOM   2109 C  CA  . ARG A 1 253 ? -5.256  0.811   -19.512 1.00 11.10  ? 254 ARG A CA  1 
ATOM   2110 C  C   . ARG A 1 253 ? -4.196  -0.114  -19.982 1.00 12.18  ? 254 ARG A C   1 
ATOM   2111 O  O   . ARG A 1 253 ? -4.475  -1.295  -20.230 1.00 18.48  ? 254 ARG A O   1 
ATOM   2112 C  CB  . ARG A 1 253 ? -5.325  0.875   -17.985 1.00 10.51  ? 254 ARG A CB  1 
ATOM   2113 C  CG  . ARG A 1 253 ? -6.166  2.019   -17.519 1.00 10.13  ? 254 ARG A CG  1 
ATOM   2114 C  CD  . ARG A 1 253 ? -6.324  2.001   -15.976 1.00 9.46   ? 254 ARG A CD  1 
ATOM   2115 N  NE  . ARG A 1 253 ? -7.150  0.878   -15.547 1.00 9.16   ? 254 ARG A NE  1 
ATOM   2116 C  CZ  . ARG A 1 253 ? -7.389  0.564   -14.273 1.00 8.04   ? 254 ARG A CZ  1 
ATOM   2117 N  NH1 . ARG A 1 253 ? -6.795  1.267   -13.277 1.00 8.00   ? 254 ARG A NH1 1 
ATOM   2118 N  NH2 . ARG A 1 253 ? -8.220  -0.396  -13.950 1.00 8.40   ? 254 ARG A NH2 1 
ATOM   2119 N  N   . GLN A 1 254 ? -2.964  0.426   -20.012 1.00 11.66  ? 255 GLN A N   1 
ATOM   2120 C  CA  . GLN A 1 254 ? -1.755  -0.339  -20.276 1.00 13.91  ? 255 GLN A CA  1 
ATOM   2121 C  C   . GLN A 1 254 ? -0.890  -0.372  -19.040 1.00 11.81  ? 255 GLN A C   1 
ATOM   2122 O  O   . GLN A 1 254 ? -0.667  0.677   -18.366 1.00 14.77  ? 255 GLN A O   1 
ATOM   2123 C  CB  . GLN A 1 254 ? -0.973  0.401   -21.338 1.00 18.39  ? 255 GLN A CB  1 
ATOM   2124 C  CG  . GLN A 1 254 ? 0.323   -0.186  -21.711 1.00 29.50  ? 255 GLN A CG  1 
ATOM   2125 C  CD  . GLN A 1 254 ? 0.041   -1.116  -22.821 1.00 54.84  ? 255 GLN A CD  1 
ATOM   2126 O  OE1 . GLN A 1 254 ? -1.116  -1.298  -23.183 1.00 50.32  ? 255 GLN A OE1 1 
ATOM   2127 N  NE2 . GLN A 1 254 ? 1.062   -1.678  -23.385 1.00 128.48 ? 255 GLN A NE2 1 
ATOM   2128 N  N   . ILE A 1 255 ? -0.424  -1.566  -18.669 1.00 10.19  ? 256 ILE A N   1 
ATOM   2129 C  CA  . ILE A 1 255 ? 0.592   -1.703  -17.602 1.00 9.57   ? 256 ILE A CA  1 
ATOM   2130 C  C   . ILE A 1 255 ? 1.968   -1.741  -18.296 1.00 9.69   ? 256 ILE A C   1 
ATOM   2131 O  O   . ILE A 1 255 ? 2.157   -2.454  -19.264 1.00 11.55  ? 256 ILE A O   1 
ATOM   2132 C  CB  . ILE A 1 255 ? 0.334   -2.940  -16.801 1.00 9.98   ? 256 ILE A CB  1 
ATOM   2133 C  CG1 . ILE A 1 255 ? -1.115  -2.932  -16.244 1.00 10.31  ? 256 ILE A CG1 1 
ATOM   2134 C  CG2 . ILE A 1 255 ? 1.399   -3.062  -15.714 1.00 11.41  ? 256 ILE A CG2 1 
ATOM   2135 C  CD1 . ILE A 1 255 ? -1.418  -4.125  -15.401 1.00 11.83  ? 256 ILE A CD1 1 
ATOM   2136 N  N   . LYS A 1 256 ? 2.873   -0.902  -17.812 1.00 9.51   ? 257 LYS A N   1 
ATOM   2137 C  CA  . LYS A 1 256 ? 4.213   -0.797  -18.346 1.00 10.04  ? 257 LYS A CA  1 
ATOM   2138 C  C   . LYS A 1 256 ? 5.201   -1.424  -17.385 1.00 9.60   ? 257 LYS A C   1 
ATOM   2139 O  O   . LYS A 1 256 ? 5.020   -1.337  -16.177 1.00 11.31  ? 257 LYS A O   1 
ATOM   2140 C  CB  . LYS A 1 256 ? 4.553   0.674   -18.616 1.00 11.30  ? 257 LYS A CB  1 
ATOM   2141 C  CG  . LYS A 1 256 ? 3.596   1.250   -19.633 1.00 16.77  ? 257 LYS A CG  1 
ATOM   2142 C  CD  . LYS A 1 256 ? 3.934   2.570   -20.199 1.00 23.99  ? 257 LYS A CD  1 
ATOM   2143 C  CE  . LYS A 1 256 ? 2.699   3.091   -20.907 1.00 34.55  ? 257 LYS A CE  1 
ATOM   2144 N  NZ  . LYS A 1 256 ? 2.713   4.589   -21.081 1.00 38.20  ? 257 LYS A NZ  1 
ATOM   2145 N  N   . ALA A 1 257 ? 6.239   -2.057  -17.902 1.00 10.08  ? 258 ALA A N   1 
ATOM   2146 C  CA  . ALA A 1 257 ? 7.300   -2.641  -17.147 1.00 10.36  ? 258 ALA A CA  1 
ATOM   2147 C  C   . ALA A 1 257 ? 8.611   -1.853  -17.329 1.00 10.52  ? 258 ALA A C   1 
ATOM   2148 O  O   . ALA A 1 257 ? 8.917   -1.386  -18.444 1.00 11.60  ? 258 ALA A O   1 
ATOM   2149 C  CB  . ALA A 1 257 ? 7.509   -4.097  -17.560 1.00 12.32  ? 258 ALA A CB  1 
ATOM   2150 N  N   . SER A 1 258 ? 9.332   -1.689  -16.215 1.00 9.98   ? 259 SER A N   1 
ATOM   2151 C  CA  . SER A 1 258 ? 10.603  -0.993  -16.238 1.00 12.48  ? 259 SER A CA  1 
ATOM   2152 C  C   . SER A 1 258 ? 11.729  -1.926  -16.666 1.00 12.89  ? 259 SER A C   1 
ATOM   2153 O  O   . SER A 1 258 ? 12.853  -1.434  -16.772 1.00 16.88  ? 259 SER A O   1 
ATOM   2154 C  CB  . SER A 1 258 ? 10.930  -0.436  -14.865 1.00 12.36  ? 259 SER A CB  1 
ATOM   2155 O  OG  . SER A 1 258 ? 11.337  -1.454  -13.968 1.00 11.62  ? 259 SER A OG  1 
ATOM   2156 N  N   . PHE A 1 259 ? 11.472  -3.188  -16.885 1.00 14.22  ? 260 PHE A N   1 
ATOM   2157 C  CA  . PHE A 1 259 ? 12.505  -4.204  -17.055 1.00 16.10  ? 260 PHE A CA  1 
ATOM   2158 C  C   . PHE A 1 259 ? 12.107  -5.113  -18.172 1.00 19.48  ? 260 PHE A C   1 
ATOM   2159 O  O   . PHE A 1 259 ? 10.910  -5.271  -18.496 1.00 20.18  ? 260 PHE A O   1 
ATOM   2160 C  CB  . PHE A 1 259 ? 12.673  -4.958  -15.774 1.00 16.45  ? 260 PHE A CB  1 
ATOM   2161 C  CG  . PHE A 1 259 ? 11.407  -5.700  -15.364 1.00 14.04  ? 260 PHE A CG  1 
ATOM   2162 C  CD1 . PHE A 1 259 ? 10.409  -5.050  -14.640 1.00 13.21  ? 260 PHE A CD1 1 
ATOM   2163 C  CD2 . PHE A 1 259 ? 11.170  -6.981  -15.773 1.00 19.22  ? 260 PHE A CD2 1 
ATOM   2164 C  CE1 . PHE A 1 259 ? 9.196   -5.685  -14.310 1.00 14.20  ? 260 PHE A CE1 1 
ATOM   2165 C  CE2 . PHE A 1 259 ? 9.988   -7.616  -15.443 1.00 19.17  ? 260 PHE A CE2 1 
ATOM   2166 C  CZ  . PHE A 1 259 ? 9.011   -6.988  -14.711 1.00 17.19  ? 260 PHE A CZ  1 
ATOM   2167 N  N   . LYS A 1 260 ? 13.203  -5.656  -18.731 1.00 33.10  ? 261 LYS A N   1 
ATOM   2168 C  CA  . LYS A 1 260 ? 13.432  -6.856  -19.578 1.00 54.73  ? 261 LYS A CA  1 
ATOM   2169 C  C   . LYS A 1 260 ? 13.268  -6.701  -21.077 1.00 101.12 ? 261 LYS A C   1 
ATOM   2170 O  O   . LYS A 1 260 ? 14.184  -6.232  -21.754 1.00 99.79  ? 261 LYS A O   1 
ATOM   2171 C  CB  . LYS A 1 260 ? 12.819  -8.167  -19.034 1.00 41.09  ? 261 LYS A CB  1 
ATOM   2172 C  CG  . LYS A 1 260 ? 13.604  -8.722  -17.832 1.00 37.90  ? 261 LYS A CG  1 
ATOM   2173 O  OXT . LYS A 1 260 ? 12.243  -7.063  -21.622 1.00 138.81 ? 261 LYS A OXT 1 
ATOM   2174 N  N   . HIS B 1 3   ? 3.676   22.263  22.339  1.00 24.44  ? 3   HIS B N   1 
ATOM   2175 C  CA  . HIS B 1 3   ? 3.354   21.279  23.459  1.00 25.08  ? 3   HIS B CA  1 
ATOM   2176 C  C   . HIS B 1 3   ? 2.277   21.757  24.420  1.00 30.63  ? 3   HIS B C   1 
ATOM   2177 O  O   . HIS B 1 3   ? 2.514   21.915  25.667  1.00 38.10  ? 3   HIS B O   1 
ATOM   2178 C  CB  . HIS B 1 3   ? 4.577   20.845  24.253  1.00 29.55  ? 3   HIS B CB  1 
ATOM   2179 C  CG  . HIS B 1 3   ? 4.344   19.567  25.056  1.00 31.45  ? 3   HIS B CG  1 
ATOM   2180 N  ND1 . HIS B 1 3   ? 4.517   18.307  24.529  1.00 40.29  ? 3   HIS B ND1 1 
ATOM   2181 C  CD2 . HIS B 1 3   ? 3.954   19.387  26.391  1.00 29.29  ? 3   HIS B CD2 1 
ATOM   2182 C  CE1 . HIS B 1 3   ? 4.205   17.400  25.470  1.00 30.70  ? 3   HIS B CE1 1 
ATOM   2183 N  NE2 . HIS B 1 3   ? 3.866   18.050  26.608  1.00 41.14  ? 3   HIS B NE2 1 
ATOM   2184 N  N   . HIS B 1 4   ? 1.083   22.018  23.861  1.00 26.05  ? 4   HIS B N   1 
ATOM   2185 C  CA  . HIS B 1 4   ? 0.069   22.497  24.721  1.00 42.10  ? 4   HIS B CA  1 
ATOM   2186 C  C   . HIS B 1 4   ? -0.737  21.417  25.316  1.00 20.44  ? 4   HIS B C   1 
ATOM   2187 O  O   . HIS B 1 4   ? -0.629  20.200  24.962  1.00 20.85  ? 4   HIS B O   1 
ATOM   2188 C  CB  . HIS B 1 4   ? -0.743  23.654  24.158  1.00 80.72  ? 4   HIS B CB  1 
ATOM   2189 C  CG  . HIS B 1 4   ? -0.494  24.953  24.885  1.00 96.90  ? 4   HIS B CG  1 
ATOM   2190 N  ND1 . HIS B 1 4   ? -0.717  25.090  26.205  1.00 121.33 ? 4   HIS B ND1 1 
ATOM   2191 C  CD2 . HIS B 1 4   ? 0.015   26.172  24.444  1.00 98.28  ? 4   HIS B CD2 1 
ATOM   2192 C  CE1 . HIS B 1 4   ? -0.390  26.337  26.588  1.00 110.71 ? 4   HIS B CE1 1 
ATOM   2193 N  NE2 . HIS B 1 4   ? 0.058   26.999  25.510  1.00 120.27 ? 4   HIS B NE2 1 
ATOM   2194 N  N   . TRP B 1 5   ? -1.566  21.802  26.240  1.00 21.73  ? 5   TRP B N   1 
ATOM   2195 C  CA  . TRP B 1 5   ? -2.302  20.848  27.025  1.00 15.97  ? 5   TRP B CA  1 
ATOM   2196 C  C   . TRP B 1 5   ? -3.323  20.051  26.231  1.00 16.58  ? 5   TRP B C   1 
ATOM   2197 O  O   . TRP B 1 5   ? -3.845  20.558  25.219  1.00 17.63  ? 5   TRP B O   1 
ATOM   2198 C  CB  . TRP B 1 5   ? -2.889  21.552  28.261  1.00 15.48  ? 5   TRP B CB  1 
ATOM   2199 C  CG  . TRP B 1 5   ? -4.074  22.430  27.908  1.00 14.43  ? 5   TRP B CG  1 
ATOM   2200 C  CD1 . TRP B 1 5   ? -4.073  23.789  27.600  1.00 15.89  ? 5   TRP B CD1 1 
ATOM   2201 C  CD2 . TRP B 1 5   ? -5.462  22.004  27.828  1.00 13.70  ? 5   TRP B CD2 1 
ATOM   2202 N  NE1 . TRP B 1 5   ? -5.337  24.217  27.353  1.00 15.82  ? 5   TRP B NE1 1 
ATOM   2203 C  CE2 . TRP B 1 5   ? -6.217  23.185  27.476  1.00 15.84  ? 5   TRP B CE2 1 
ATOM   2204 C  CE3 . TRP B 1 5   ? -6.146  20.795  28.053  1.00 14.09  ? 5   TRP B CE3 1 
ATOM   2205 C  CZ2 . TRP B 1 5   ? -7.583  23.158  27.305  1.00 16.90  ? 5   TRP B CZ2 1 
ATOM   2206 C  CZ3 . TRP B 1 5   ? -7.560  20.785  27.897  1.00 14.37  ? 5   TRP B CZ3 1 
ATOM   2207 C  CH2 . TRP B 1 5   ? -8.254  21.973  27.537  1.00 16.34  ? 5   TRP B CH2 1 
ATOM   2208 N  N   . GLY B 1 6   ? -3.649  18.847  26.709  1.00 14.68  ? 6   GLY B N   1 
ATOM   2209 C  CA  . GLY B 1 6   ? -4.740  18.092  26.076  1.00 15.18  ? 6   GLY B CA  1 
ATOM   2210 C  C   . GLY B 1 6   ? -5.008  16.907  26.997  1.00 15.06  ? 6   GLY B C   1 
ATOM   2211 O  O   . GLY B 1 6   ? -4.992  17.053  28.217  1.00 14.58  ? 6   GLY B O   1 
ATOM   2212 N  N   A TYR B 1 7   ? -5.121  15.656  26.573  0.50 15.24  ? 7   TYR B N   1 
ATOM   2213 N  N   B TYR B 1 7   ? -5.467  15.852  26.300  0.50 11.29  ? 7   TYR B N   1 
ATOM   2214 C  CA  A TYR B 1 7   ? -5.453  14.633  27.613  0.50 12.91  ? 7   TYR B CA  1 
ATOM   2215 C  CA  B TYR B 1 7   ? -5.972  14.571  26.823  0.50 10.32  ? 7   TYR B CA  1 
ATOM   2216 C  C   A TYR B 1 7   ? -4.592  13.386  27.591  0.50 14.02  ? 7   TYR B C   1 
ATOM   2217 C  C   B TYR B 1 7   ? -5.232  13.368  26.196  0.50 12.31  ? 7   TYR B C   1 
ATOM   2218 O  O   A TYR B 1 7   ? -4.919  12.311  28.244  0.50 17.47  ? 7   TYR B O   1 
ATOM   2219 O  O   B TYR B 1 7   ? -5.694  12.218  26.288  0.50 17.25  ? 7   TYR B O   1 
ATOM   2220 C  CB  A TYR B 1 7   ? -6.929  14.248  27.378  0.50 13.43  ? 7   TYR B CB  1 
ATOM   2221 C  CB  B TYR B 1 7   ? -7.460  14.353  26.630  0.50 9.69   ? 7   TYR B CB  1 
ATOM   2222 C  CG  A TYR B 1 7   ? -7.879  15.328  27.822  0.50 10.17  ? 7   TYR B CG  1 
ATOM   2223 C  CG  B TYR B 1 7   ? -8.243  15.473  27.293  0.50 7.90   ? 7   TYR B CG  1 
ATOM   2224 C  CD1 A TYR B 1 7   ? -8.372  15.339  29.130  0.50 10.85  ? 7   TYR B CD1 1 
ATOM   2225 C  CD1 B TYR B 1 7   ? -8.574  15.408  28.639  0.50 8.66   ? 7   TYR B CD1 1 
ATOM   2226 C  CD2 A TYR B 1 7   ? -8.316  16.310  26.949  0.50 12.01  ? 7   TYR B CD2 1 
ATOM   2227 C  CD2 B TYR B 1 7   ? -8.722  16.546  26.557  0.50 8.68   ? 7   TYR B CD2 1 
ATOM   2228 C  CE1 A TYR B 1 7   ? -9.273  16.333  29.533  0.50 10.10  ? 7   TYR B CE1 1 
ATOM   2229 C  CE1 B TYR B 1 7   ? -9.315  16.406  29.243  0.50 8.00   ? 7   TYR B CE1 1 
ATOM   2230 C  CE2 A TYR B 1 7   ? -9.201  17.290  27.340  0.50 11.48  ? 7   TYR B CE2 1 
ATOM   2231 C  CE2 B TYR B 1 7   ? -9.461  17.550  27.148  0.50 9.70   ? 7   TYR B CE2 1 
ATOM   2232 C  CZ  A TYR B 1 7   ? -9.676  17.313  28.624  0.50 9.98   ? 7   TYR B CZ  1 
ATOM   2233 C  CZ  B TYR B 1 7   ? -9.758  17.475  28.493  0.50 9.07   ? 7   TYR B CZ  1 
ATOM   2234 O  OH  A TYR B 1 7   ? -10.563 18.331  28.937  0.50 9.92   ? 7   TYR B OH  1 
ATOM   2235 O  OH  B TYR B 1 7   ? -10.496 18.473  29.091  0.50 10.74  ? 7   TYR B OH  1 
ATOM   2236 N  N   A GLY B 1 8   ? -3.513  13.541  26.829  0.50 13.96  ? 8   GLY B N   1 
ATOM   2237 N  N   B GLY B 1 8   ? -4.076  13.616  25.579  0.50 11.43  ? 8   GLY B N   1 
ATOM   2238 C  CA  A GLY B 1 8   ? -2.502  12.473  26.707  0.50 13.21  ? 8   GLY B CA  1 
ATOM   2239 C  CA  B GLY B 1 8   ? -3.258  12.598  24.927  0.50 13.93  ? 8   GLY B CA  1 
ATOM   2240 C  C   A GLY B 1 8   ? -1.463  12.200  27.820  0.50 14.29  ? 8   GLY B C   1 
ATOM   2241 C  C   B GLY B 1 8   ? -2.346  11.902  25.884  0.50 13.69  ? 8   GLY B C   1 
ATOM   2242 O  O   A GLY B 1 8   ? -1.357  12.816  28.910  0.50 17.83  ? 8   GLY B O   1 
ATOM   2243 O  O   B GLY B 1 8   ? -2.443  11.963  27.080  0.50 11.76  ? 8   GLY B O   1 
ATOM   2244 N  N   A LYS B 1 9   ? -0.679  11.163  27.556  0.50 16.36  ? 9   LYS B N   1 
ATOM   2245 N  N   B LYS B 1 9   ? -1.390  11.164  25.336  0.50 11.22  ? 9   LYS B N   1 
ATOM   2246 C  CA  A LYS B 1 9   ? 0.336   10.753  28.483  0.50 16.64  ? 9   LYS B CA  1 
ATOM   2247 C  CA  B LYS B 1 9   ? -0.483  10.355  26.149  0.50 13.11  ? 9   LYS B CA  1 
ATOM   2248 C  C   A LYS B 1 9   ? 1.311   11.879  28.826  0.50 13.70  ? 9   LYS B C   1 
ATOM   2249 C  C   B LYS B 1 9   ? 0.653   11.141  26.867  0.50 12.74  ? 9   LYS B C   1 
ATOM   2250 O  O   A LYS B 1 9   ? 1.705   12.024  29.978  0.50 17.42  ? 9   LYS B O   1 
ATOM   2251 O  O   B LYS B 1 9   ? 1.295   10.526  27.751  0.50 12.78  ? 9   LYS B O   1 
ATOM   2252 C  CB  A LYS B 1 9   ? 1.087   9.581   27.881  0.50 19.19  ? 9   LYS B CB  1 
ATOM   2253 C  CB  B LYS B 1 9   ? 0.066   9.179   25.317  0.50 15.15  ? 9   LYS B CB  1 
ATOM   2254 C  CG  A LYS B 1 9   ? 2.267   9.256   28.715  0.50 22.81  ? 9   LYS B CG  1 
ATOM   2255 C  CG  B LYS B 1 9   ? -0.931  8.045   25.053  0.50 19.72  ? 9   LYS B CG  1 
ATOM   2256 N  N   A HIS B 1 10  ? 1.684   12.645  27.793  0.50 12.01  ? 10  HIS B N   1 
ATOM   2257 N  N   B HIS B 1 10  ? 0.910   12.413  26.463  0.50 11.83  ? 10  HIS B N   1 
ATOM   2258 C  CA  A HIS B 1 10  ? 2.600   13.744  27.887  0.50 12.39  ? 10  HIS B CA  1 
ATOM   2259 C  CA  B HIS B 1 10  ? 2.028   13.286  26.944  0.50 10.90  ? 10  HIS B CA  1 
ATOM   2260 C  C   A HIS B 1 10  ? 1.890   15.067  27.876  0.50 12.98  ? 10  HIS B C   1 
ATOM   2261 C  C   B HIS B 1 10  ? 1.810   14.735  27.438  0.50 12.22  ? 10  HIS B C   1 
ATOM   2262 O  O   A HIS B 1 10  ? 2.560   16.103  28.070  0.50 14.39  ? 10  HIS B O   1 
ATOM   2263 O  O   B HIS B 1 10  ? 2.796   15.479  27.610  0.50 13.84  ? 10  HIS B O   1 
ATOM   2264 C  CB  A HIS B 1 10  ? 3.665   13.678  26.773  0.50 12.97  ? 10  HIS B CB  1 
ATOM   2265 C  CB  B HIS B 1 10  ? 3.079   13.373  25.839  0.50 13.00  ? 10  HIS B CB  1 
ATOM   2266 C  CG  A HIS B 1 10  ? 4.250   12.313  26.583  0.50 12.53  ? 10  HIS B CG  1 
ATOM   2267 C  CG  B HIS B 1 10  ? 3.641   12.050  25.454  0.50 11.80  ? 10  HIS B CG  1 
ATOM   2268 N  ND1 A HIS B 1 10  ? 5.291   11.885  27.330  0.50 13.16  ? 10  HIS B ND1 1 
ATOM   2269 N  ND1 B HIS B 1 10  ? 4.581   11.451  26.191  0.50 13.28  ? 10  HIS B ND1 1 
ATOM   2270 C  CD2 A HIS B 1 10  ? 3.881   11.257  25.770  0.50 16.52  ? 10  HIS B CD2 1 
ATOM   2271 C  CD2 B HIS B 1 10  ? 3.300   11.174  24.417  0.50 13.58  ? 10  HIS B CD2 1 
ATOM   2272 C  CE1 A HIS B 1 10  ? 5.553   10.614  27.007  0.50 16.34  ? 10  HIS B CE1 1 
ATOM   2273 C  CE1 B HIS B 1 10  ? 4.875   10.270  25.628  0.50 13.50  ? 10  HIS B CE1 1 
ATOM   2274 N  NE2 A HIS B 1 10  ? 4.687   10.236  26.058  0.50 15.53  ? 10  HIS B NE2 1 
ATOM   2275 N  NE2 B HIS B 1 10  ? 4.081   10.098  24.534  0.50 15.35  ? 10  HIS B NE2 1 
ATOM   2276 N  N   . ASN B 1 11  ? 0.563   15.130  27.686  1.00 20.14  ? 11  ASN B N   1 
ATOM   2277 C  CA  . ASN B 1 11  ? 0.037   16.472  27.873  1.00 18.01  ? 11  ASN B CA  1 
ATOM   2278 C  C   . ASN B 1 11  ? -1.298  16.490  28.627  1.00 17.17  ? 11  ASN B C   1 
ATOM   2279 O  O   . ASN B 1 11  ? -1.965  17.497  28.674  1.00 17.38  ? 11  ASN B O   1 
ATOM   2280 C  CB  . ASN B 1 11  ? -0.160  17.203  26.523  1.00 16.55  ? 11  ASN B CB  1 
ATOM   2281 C  CG  . ASN B 1 11  ? -1.257  16.631  25.617  1.00 18.15  ? 11  ASN B CG  1 
ATOM   2282 O  OD1 . ASN B 1 11  ? -1.888  15.627  25.915  1.00 21.32  ? 11  ASN B OD1 1 
ATOM   2283 N  ND2 . ASN B 1 11  ? -1.511  17.301  24.521  1.00 18.99  ? 11  ASN B ND2 1 
ATOM   2284 N  N   . GLY B 1 12  ? -1.684  15.351  29.175  1.00 15.35  ? 12  GLY B N   1 
ATOM   2285 C  CA  . GLY B 1 12  ? -2.950  15.251  29.877  1.00 14.77  ? 12  GLY B CA  1 
ATOM   2286 C  C   . GLY B 1 12  ? -2.964  15.786  31.274  1.00 14.23  ? 12  GLY B C   1 
ATOM   2287 O  O   . GLY B 1 12  ? -2.023  16.436  31.707  1.00 13.44  ? 12  GLY B O   1 
ATOM   2288 N  N   . PRO B 1 13  ? -4.035  15.512  32.008  1.00 12.74  ? 13  PRO B N   1 
ATOM   2289 C  CA  . PRO B 1 13  ? -4.284  16.130  33.292  1.00 13.18  ? 13  PRO B CA  1 
ATOM   2290 C  C   . PRO B 1 13  ? -3.153  16.077  34.287  1.00 13.26  ? 13  PRO B C   1 
ATOM   2291 O  O   . PRO B 1 13  ? -3.012  17.036  35.060  1.00 13.56  ? 13  PRO B O   1 
ATOM   2292 C  CB  . PRO B 1 13  ? -5.496  15.328  33.795  1.00 13.19  ? 13  PRO B CB  1 
ATOM   2293 C  CG  . PRO B 1 13  ? -6.271  15.035  32.552  1.00 14.50  ? 13  PRO B CG  1 
ATOM   2294 C  CD  . PRO B 1 13  ? -5.223  14.794  31.489  1.00 13.83  ? 13  PRO B CD  1 
ATOM   2295 N  N   . GLU B 1 14  ? -2.351  15.017  34.319  1.00 13.83  ? 14  GLU B N   1 
ATOM   2296 C  CA  . GLU B 1 14  ? -1.277  14.928  35.274  1.00 17.18  ? 14  GLU B CA  1 
ATOM   2297 C  C   . GLU B 1 14  ? -0.118  15.914  34.987  1.00 16.18  ? 14  GLU B C   1 
ATOM   2298 O  O   . GLU B 1 14  ? 0.774   16.130  35.858  1.00 17.53  ? 14  GLU B O   1 
ATOM   2299 C  CB  . GLU B 1 14  ? -0.823  13.461  35.304  1.00 21.93  ? 14  GLU B CB  1 
ATOM   2300 C  CG  . GLU B 1 14  ? -0.231  12.974  33.945  1.00 20.17  ? 14  GLU B CG  1 
ATOM   2301 C  CD  . GLU B 1 14  ? -1.073  12.401  32.776  1.00 20.62  ? 14  GLU B CD  1 
ATOM   2302 O  OE1 . GLU B 1 14  ? -2.257  12.780  32.652  1.00 19.75  ? 14  GLU B OE1 1 
ATOM   2303 O  OE2 . GLU B 1 14  ? -0.529  11.587  32.002  1.00 27.21  ? 14  GLU B OE2 1 
ATOM   2304 N  N   . HIS B 1 15  ? -0.122  16.512  33.785  1.00 13.41  ? 15  HIS B N   1 
ATOM   2305 C  CA  . HIS B 1 15  ? 0.864   17.526  33.395  1.00 13.59  ? 15  HIS B CA  1 
ATOM   2306 C  C   . HIS B 1 15  ? 0.439   18.968  33.551  1.00 13.57  ? 15  HIS B C   1 
ATOM   2307 O  O   . HIS B 1 15  ? 1.285   19.874  33.484  1.00 14.65  ? 15  HIS B O   1 
ATOM   2308 C  CB  . HIS B 1 15  ? 1.234   17.288  31.919  1.00 15.82  ? 15  HIS B CB  1 
ATOM   2309 C  CG  . HIS B 1 15  ? 1.947   16.016  31.678  1.00 16.75  ? 15  HIS B CG  1 
ATOM   2310 N  ND1 . HIS B 1 15  ? 3.304   15.870  31.842  1.00 20.48  ? 15  HIS B ND1 1 
ATOM   2311 C  CD2 . HIS B 1 15  ? 1.451   14.796  31.315  1.00 18.34  ? 15  HIS B CD2 1 
ATOM   2312 C  CE1 . HIS B 1 15  ? 3.621   14.599  31.588  1.00 23.41  ? 15  HIS B CE1 1 
ATOM   2313 N  NE2 . HIS B 1 15  ? 2.510   13.939  31.242  1.00 21.21  ? 15  HIS B NE2 1 
ATOM   2314 N  N   . TRP B 1 16  ? -0.847  19.209  33.689  1.00 12.28  ? 16  TRP B N   1 
ATOM   2315 C  CA  . TRP B 1 16  ? -1.385  20.547  33.622  1.00 11.60  ? 16  TRP B CA  1 
ATOM   2316 C  C   . TRP B 1 16  ? -0.806  21.516  34.625  1.00 11.70  ? 16  TRP B C   1 
ATOM   2317 O  O   . TRP B 1 16  ? -0.694  22.702  34.377  1.00 12.81  ? 16  TRP B O   1 
ATOM   2318 C  CB  . TRP B 1 16  ? -2.896  20.477  33.717  1.00 11.79  ? 16  TRP B CB  1 
ATOM   2319 C  CG  . TRP B 1 16  ? -3.596  19.806  32.575  1.00 10.63  ? 16  TRP B CG  1 
ATOM   2320 C  CD1 . TRP B 1 16  ? -3.075  19.349  31.363  1.00 11.33  ? 16  TRP B CD1 1 
ATOM   2321 C  CD2 . TRP B 1 16  ? -5.012  19.507  32.523  1.00 10.46  ? 16  TRP B CD2 1 
ATOM   2322 N  NE1 . TRP B 1 16  ? -4.070  18.798  30.588  1.00 11.45  ? 16  TRP B NE1 1 
ATOM   2323 C  CE2 . TRP B 1 16  ? -5.258  18.863  31.235  1.00 10.42  ? 16  TRP B CE2 1 
ATOM   2324 C  CE3 . TRP B 1 16  ? -6.066  19.704  33.392  1.00 10.54  ? 16  TRP B CE3 1 
ATOM   2325 C  CZ2 . TRP B 1 16  ? -6.521  18.444  30.862  1.00 9.92   ? 16  TRP B CZ2 1 
ATOM   2326 C  CZ3 . TRP B 1 16  ? -7.330  19.280  33.008  1.00 10.85  ? 16  TRP B CZ3 1 
ATOM   2327 C  CH2 . TRP B 1 16  ? -7.553  18.666  31.776  1.00 11.04  ? 16  TRP B CH2 1 
ATOM   2328 N  N   . HIS B 1 17  ? -0.454  20.973  35.771  1.00 12.23  ? 17  HIS B N   1 
ATOM   2329 C  CA  . HIS B 1 17  ? 0.063   21.821  36.865  1.00 13.03  ? 17  HIS B CA  1 
ATOM   2330 C  C   . HIS B 1 17  ? 1.296   22.610  36.473  1.00 14.06  ? 17  HIS B C   1 
ATOM   2331 O  O   . HIS B 1 17  ? 1.613   23.655  37.088  1.00 15.40  ? 17  HIS B O   1 
ATOM   2332 C  CB  . HIS B 1 17  ? 0.337   21.048  38.148  1.00 14.04  ? 17  HIS B CB  1 
ATOM   2333 C  CG  . HIS B 1 17  ? 1.556   20.175  38.075  1.00 15.06  ? 17  HIS B CG  1 
ATOM   2334 N  ND1 . HIS B 1 17  ? 2.754   20.580  38.595  1.00 18.89  ? 17  HIS B ND1 1 
ATOM   2335 C  CD2 . HIS B 1 17  ? 1.744   19.000  37.470  1.00 18.28  ? 17  HIS B CD2 1 
ATOM   2336 C  CE1 . HIS B 1 17  ? 3.646   19.687  38.314  1.00 18.66  ? 17  HIS B CE1 1 
ATOM   2337 N  NE2 . HIS B 1 17  ? 3.052   18.684  37.661  1.00 17.41  ? 17  HIS B NE2 1 
ATOM   2338 N  N   . LYS B 1 18  ? 2.071   22.119  35.505  1.00 13.85  ? 18  LYS B N   1 
ATOM   2339 C  CA  . LYS B 1 18  ? 3.312   22.824  35.136  1.00 16.82  ? 18  LYS B CA  1 
ATOM   2340 C  C   . LYS B 1 18  ? 3.033   24.163  34.473  1.00 18.54  ? 18  LYS B C   1 
ATOM   2341 O  O   . LYS B 1 18  ? 3.706   25.139  34.731  1.00 24.09  ? 18  LYS B O   1 
ATOM   2342 C  CB  . LYS B 1 18  ? 4.145   21.957  34.238  1.00 17.06  ? 18  LYS B CB  1 
ATOM   2343 C  CG  . LYS B 1 18  ? 4.744   20.737  34.951  1.00 18.60  ? 18  LYS B CG  1 
ATOM   2344 C  CD  . LYS B 1 18  ? 5.447   19.804  33.981  1.00 18.53  ? 18  LYS B CD  1 
ATOM   2345 C  CE  . LYS B 1 18  ? 4.471   18.806  33.371  1.00 18.32  ? 18  LYS B CE  1 
ATOM   2346 N  NZ  . LYS B 1 18  ? 5.129   17.972  32.343  1.00 18.55  ? 18  LYS B NZ  1 
ATOM   2347 N  N   . ASP B 1 19  ? 1.986   24.226  33.651  1.00 15.71  ? 19  ASP B N   1 
ATOM   2348 C  CA  . ASP B 1 19  ? 1.585   25.523  33.078  1.00 18.12  ? 19  ASP B CA  1 
ATOM   2349 C  C   . ASP B 1 19  ? 0.578   26.262  33.943  1.00 16.29  ? 19  ASP B C   1 
ATOM   2350 O  O   . ASP B 1 19  ? 0.426   27.457  33.793  1.00 17.37  ? 19  ASP B O   1 
ATOM   2351 C  CB  . ASP B 1 19  ? 1.029   25.302  31.666  1.00 20.44  ? 19  ASP B CB  1 
ATOM   2352 C  CG  . ASP B 1 19  ? 2.091   25.265  30.607  1.00 27.17  ? 19  ASP B CG  1 
ATOM   2353 O  OD1 . ASP B 1 19  ? 3.143   25.914  30.811  1.00 28.35  ? 19  ASP B OD1 1 
ATOM   2354 O  OD2 . ASP B 1 19  ? 1.849   24.551  29.608  1.00 49.02  ? 19  ASP B OD2 1 
ATOM   2355 N  N   . PHE B 1 20  ? -0.225  25.520  34.705  1.00 13.52  ? 20  PHE B N   1 
ATOM   2356 C  CA  . PHE B 1 20  ? -1.290  26.073  35.450  1.00 13.82  ? 20  PHE B CA  1 
ATOM   2357 C  C   . PHE B 1 20  ? -1.174  25.554  36.893  1.00 13.70  ? 20  PHE B C   1 
ATOM   2358 O  O   . PHE B 1 20  ? -1.867  24.601  37.253  1.00 13.20  ? 20  PHE B O   1 
ATOM   2359 C  CB  . PHE B 1 20  ? -2.640  25.639  34.843  1.00 13.88  ? 20  PHE B CB  1 
ATOM   2360 C  CG  . PHE B 1 20  ? -2.759  26.040  33.421  1.00 15.25  ? 20  PHE B CG  1 
ATOM   2361 C  CD1 . PHE B 1 20  ? -3.125  27.331  33.107  1.00 17.08  ? 20  PHE B CD1 1 
ATOM   2362 C  CD2 . PHE B 1 20  ? -2.360  25.135  32.391  1.00 17.84  ? 20  PHE B CD2 1 
ATOM   2363 C  CE1 . PHE B 1 20  ? -3.125  27.751  31.759  1.00 19.62  ? 20  PHE B CE1 1 
ATOM   2364 C  CE2 . PHE B 1 20  ? -2.378  25.509  31.063  1.00 19.68  ? 20  PHE B CE2 1 
ATOM   2365 C  CZ  . PHE B 1 20  ? -2.758  26.826  30.764  1.00 19.32  ? 20  PHE B CZ  1 
ATOM   2366 N  N   . PRO B 1 21  ? -0.367  26.195  37.728  1.00 14.27  ? 21  PRO B N   1 
ATOM   2367 C  CA  . PRO B 1 21  ? -0.119  25.637  39.054  1.00 15.91  ? 21  PRO B CA  1 
ATOM   2368 C  C   . PRO B 1 21  ? -1.350  25.562  39.959  1.00 13.80  ? 21  PRO B C   1 
ATOM   2369 O  O   . PRO B 1 21  ? -1.336  24.780  40.907  1.00 14.09  ? 21  PRO B O   1 
ATOM   2370 C  CB  . PRO B 1 21  ? 0.976   26.592  39.648  1.00 17.85  ? 21  PRO B CB  1 
ATOM   2371 C  CG  . PRO B 1 21  ? 1.345   27.459  38.561  1.00 30.26  ? 21  PRO B CG  1 
ATOM   2372 C  CD  . PRO B 1 21  ? 0.634   27.188  37.311  1.00 17.80  ? 21  PRO B CD  1 
ATOM   2373 N  N   A ILE B 1 22  ? -2.381  26.271  39.518  0.50 11.99  ? 22  ILE B N   1 
ATOM   2374 N  N   B ILE B 1 22  ? -2.381  26.396  39.824  0.50 12.63  ? 22  ILE B N   1 
ATOM   2375 C  CA  A ILE B 1 22  ? -3.651  26.253  40.192  0.50 10.79  ? 22  ILE B CA  1 
ATOM   2376 C  CA  B ILE B 1 22  ? -3.626  26.183  40.601  0.50 12.64  ? 22  ILE B CA  1 
ATOM   2377 C  C   A ILE B 1 22  ? -4.287  24.870  40.172  0.50 10.25  ? 22  ILE B C   1 
ATOM   2378 C  C   B ILE B 1 22  ? -4.213  24.746  40.406  0.50 11.18  ? 22  ILE B C   1 
ATOM   2379 O  O   A ILE B 1 22  ? -5.209  24.596  40.917  0.50 10.57  ? 22  ILE B O   1 
ATOM   2380 O  O   B ILE B 1 22  ? -5.113  24.349  41.231  0.50 10.97  ? 22  ILE B O   1 
ATOM   2381 C  CB  A ILE B 1 22  ? -4.614  27.366  39.679  0.50 10.02  ? 22  ILE B CB  1 
ATOM   2382 C  CB  B ILE B 1 22  ? -4.674  27.265  40.169  0.50 10.31  ? 22  ILE B CB  1 
ATOM   2383 C  CG1 A ILE B 1 22  ? -5.662  27.707  40.751  0.50 12.27  ? 22  ILE B CG1 1 
ATOM   2384 C  CG1 B ILE B 1 22  ? -5.783  27.556  41.154  0.50 11.44  ? 22  ILE B CG1 1 
ATOM   2385 C  CG2 A ILE B 1 22  ? -5.174  26.991  38.338  0.50 10.29  ? 22  ILE B CG2 1 
ATOM   2386 C  CG2 B ILE B 1 22  ? -5.247  26.890  38.830  0.50 10.81  ? 22  ILE B CG2 1 
ATOM   2387 C  CD1 A ILE B 1 22  ? -5.125  27.948  42.154  0.50 17.48  ? 22  ILE B CD1 1 
ATOM   2388 C  CD1 B ILE B 1 22  ? -6.648  28.704  40.631  0.50 11.84  ? 22  ILE B CD1 1 
ATOM   2389 N  N   . ALA B 1 23  ? -3.772  23.976  39.353  1.00 11.29  ? 23  ALA B N   1 
ATOM   2390 C  CA  . ALA B 1 23  ? -4.195  22.590  39.252  1.00 11.31  ? 23  ALA B CA  1 
ATOM   2391 C  C   . ALA B 1 23  ? -4.104  21.874  40.584  1.00 11.49  ? 23  ALA B C   1 
ATOM   2392 O  O   . ALA B 1 23  ? -4.813  20.880  40.774  1.00 11.60  ? 23  ALA B O   1 
ATOM   2393 C  CB  . ALA B 1 23  ? -3.325  21.839  38.237  1.00 11.59  ? 23  ALA B CB  1 
ATOM   2394 N  N   . LYS B 1 24  ? -3.166  22.295  41.441  1.00 12.36  ? 24  LYS B N   1 
ATOM   2395 C  CA  . LYS B 1 24  ? -3.004  21.714  42.781  1.00 12.96  ? 24  LYS B CA  1 
ATOM   2396 C  C   . LYS B 1 24  ? -3.632  22.596  43.874  1.00 14.21  ? 24  LYS B C   1 
ATOM   2397 O  O   . LYS B 1 24  ? -3.230  22.485  45.031  1.00 16.56  ? 24  LYS B O   1 
ATOM   2398 C  CB  . LYS B 1 24  ? -1.537  21.384  43.110  1.00 14.73  ? 24  LYS B CB  1 
ATOM   2399 C  CG  . LYS B 1 24  ? -0.919  20.412  42.109  1.00 15.99  ? 24  LYS B CG  1 
ATOM   2400 C  CD  . LYS B 1 24  ? 0.591   20.264  42.403  1.00 20.13  ? 24  LYS B CD  1 
ATOM   2401 C  CE  . LYS B 1 24  ? 1.290   19.227  41.531  1.00 21.53  ? 24  LYS B CE  1 
ATOM   2402 N  NZ  . LYS B 1 24  ? 0.983   17.805  41.853  1.00 29.82  ? 24  LYS B NZ  1 
ATOM   2403 N  N   . GLY B 1 25  ? -4.627  23.372  43.520  1.00 12.93  ? 25  GLY B N   1 
ATOM   2404 C  CA  . GLY B 1 25  ? -5.207  24.358  44.440  1.00 14.78  ? 25  GLY B CA  1 
ATOM   2405 C  C   . GLY B 1 25  ? -6.230  23.735  45.400  1.00 12.91  ? 25  GLY B C   1 
ATOM   2406 O  O   . GLY B 1 25  ? -6.398  22.497  45.494  1.00 13.84  ? 25  GLY B O   1 
ATOM   2407 N  N   . GLU B 1 26  ? -6.855  24.618  46.143  1.00 13.58  ? 26  GLU B N   1 
ATOM   2408 C  CA  . GLU B 1 26  ? -7.712  24.270  47.213  1.00 13.72  ? 26  GLU B CA  1 
ATOM   2409 C  C   . GLU B 1 26  ? -9.139  23.998  46.814  1.00 12.11  ? 26  GLU B C   1 
ATOM   2410 O  O   . GLU B 1 26  ? -9.902  23.508  47.656  1.00 14.01  ? 26  GLU B O   1 
ATOM   2411 C  CB  . GLU B 1 26  ? -7.688  25.357  48.304  1.00 18.71  ? 26  GLU B CB  1 
ATOM   2412 C  CG  . GLU B 1 26  ? -6.304  25.586  48.878  1.00 21.18  ? 26  GLU B CG  1 
ATOM   2413 C  CD  . GLU B 1 26  ? -5.661  24.305  49.463  1.00 27.30  ? 26  GLU B CD  1 
ATOM   2414 O  OE1 . GLU B 1 26  ? -6.327  23.616  50.278  1.00 31.70  ? 26  GLU B OE1 1 
ATOM   2415 O  OE2 . GLU B 1 26  ? -4.516  23.961  49.049  1.00 37.34  ? 26  GLU B OE2 1 
ATOM   2416 N  N   . ARG B 1 27  ? -9.573  24.316  45.601  1.00 10.22  ? 27  ARG B N   1 
ATOM   2417 C  CA  . ARG B 1 27  ? -10.966 24.114  45.224  1.00 8.71   ? 27  ARG B CA  1 
ATOM   2418 C  C   . ARG B 1 27  ? -11.038 23.670  43.754  1.00 8.13   ? 27  ARG B C   1 
ATOM   2419 O  O   . ARG B 1 27  ? -11.738 24.281  42.931  1.00 8.75   ? 27  ARG B O   1 
ATOM   2420 C  CB  . ARG B 1 27  ? -11.857 25.306  45.535  1.00 12.03  ? 27  ARG B CB  1 
ATOM   2421 C  CG  . ARG B 1 27  ? -11.496 26.621  44.985  1.00 14.51  ? 27  ARG B CG  1 
ATOM   2422 C  CD  . ARG B 1 27  ? -12.505 27.779  45.124  1.00 16.95  ? 27  ARG B CD  1 
ATOM   2423 N  NE  . ARG B 1 27  ? -13.659 27.686  44.233  1.00 14.01  ? 27  ARG B NE  1 
ATOM   2424 C  CZ  . ARG B 1 27  ? -14.596 28.621  44.125  1.00 11.69  ? 27  ARG B CZ  1 
ATOM   2425 N  NH1 . ARG B 1 27  ? -14.513 29.722  44.852  1.00 16.09  ? 27  ARG B NH1 1 
ATOM   2426 N  NH2 . ARG B 1 27  ? -15.613 28.460  43.292  1.00 13.19  ? 27  ARG B NH2 1 
ATOM   2427 N  N   . GLN B 1 28  ? -10.309 22.604  43.483  1.00 8.30   ? 28  GLN B N   1 
ATOM   2428 C  CA  . GLN B 1 28  ? -10.276 22.051  42.117  1.00 7.66   ? 28  GLN B CA  1 
ATOM   2429 C  C   . GLN B 1 28  ? -11.433 21.085  41.864  1.00 7.44   ? 28  GLN B C   1 
ATOM   2430 O  O   . GLN B 1 28  ? -11.916 20.403  42.754  1.00 8.33   ? 28  GLN B O   1 
ATOM   2431 C  CB  . GLN B 1 28  ? -8.911  21.401  41.856  1.00 8.49   ? 28  GLN B CB  1 
ATOM   2432 C  CG  . GLN B 1 28  ? -7.776  22.457  41.746  1.00 8.63   ? 28  GLN B CG  1 
ATOM   2433 C  CD  . GLN B 1 28  ? -7.926  23.246  40.477  1.00 8.31   ? 28  GLN B CD  1 
ATOM   2434 O  OE1 . GLN B 1 28  ? -7.736  22.670  39.386  1.00 8.53   ? 28  GLN B OE1 1 
ATOM   2435 N  NE2 . GLN B 1 28  ? -8.232  24.518  40.593  1.00 8.85   ? 28  GLN B NE2 1 
ATOM   2436 N  N   . SER B 1 29  ? -11.806 20.990  40.583  1.00 7.14   ? 29  SER B N   1 
ATOM   2437 C  CA  . SER B 1 29  ? -12.853 20.124  40.110  1.00 6.77   ? 29  SER B CA  1 
ATOM   2438 C  C   . SER B 1 29  ? -12.334 19.250  38.983  1.00 6.69   ? 29  SER B C   1 
ATOM   2439 O  O   . SER B 1 29  ? -11.361 19.595  38.305  1.00 7.31   ? 29  SER B O   1 
ATOM   2440 C  CB  . SER B 1 29  ? -13.998 20.995  39.565  1.00 6.70   ? 29  SER B CB  1 
ATOM   2441 O  OG  . SER B 1 29  ? -14.619 21.714  40.624  1.00 7.10   ? 29  SER B OG  1 
ATOM   2442 N  N   . PRO B 1 30  ? -12.979 18.117  38.714  1.00 6.23   ? 30  PRO B N   1 
ATOM   2443 C  CA  . PRO B 1 30  ? -14.134 17.554  39.445  1.00 6.75   ? 30  PRO B CA  1 
ATOM   2444 C  C   . PRO B 1 30  ? -13.743 16.890  40.736  1.00 6.36   ? 30  PRO B C   1 
ATOM   2445 O  O   . PRO B 1 30  ? -12.555 16.867  41.093  1.00 7.36   ? 30  PRO B O   1 
ATOM   2446 C  CB  . PRO B 1 30  ? -14.680 16.532  38.423  1.00 6.53   ? 30  PRO B CB  1 
ATOM   2447 C  CG  . PRO B 1 30  ? -13.409 15.972  37.853  1.00 7.32   ? 30  PRO B CG  1 
ATOM   2448 C  CD  . PRO B 1 30  ? -12.489 17.172  37.685  1.00 7.52   ? 30  PRO B CD  1 
ATOM   2449 N  N   . VAL B 1 31  ? -14.724 16.359  41.432  1.00 7.08   ? 31  VAL B N   1 
ATOM   2450 C  CA  . VAL B 1 31  ? -14.568 15.608  42.668  1.00 7.19   ? 31  VAL B CA  1 
ATOM   2451 C  C   . VAL B 1 31  ? -15.420 14.382  42.620  1.00 7.24   ? 31  VAL B C   1 
ATOM   2452 O  O   . VAL B 1 31  ? -16.409 14.317  41.870  1.00 7.79   ? 31  VAL B O   1 
ATOM   2453 C  CB  . VAL B 1 31  ? -14.884 16.462  43.915  1.00 8.05   ? 31  VAL B CB  1 
ATOM   2454 C  CG1 . VAL B 1 31  ? -13.925 17.639  44.032  1.00 9.35   ? 31  VAL B CG1 1 
ATOM   2455 C  CG2 . VAL B 1 31  ? -16.321 16.856  43.988  1.00 8.42   ? 31  VAL B CG2 1 
ATOM   2456 N  N   . ASP B 1 32  ? -15.088 13.387  43.470  1.00 7.62   ? 32  ASP B N   1 
ATOM   2457 C  CA  . ASP B 1 32  ? -16.005 12.293  43.763  1.00 7.70   ? 32  ASP B CA  1 
ATOM   2458 C  C   . ASP B 1 32  ? -17.055 12.824  44.748  1.00 7.84   ? 32  ASP B C   1 
ATOM   2459 O  O   . ASP B 1 32  ? -16.747 13.485  45.750  1.00 10.14  ? 32  ASP B O   1 
ATOM   2460 C  CB  . ASP B 1 32  ? -15.285 11.119  44.385  1.00 9.35   ? 32  ASP B CB  1 
ATOM   2461 C  CG  . ASP B 1 32  ? -16.216 9.951   44.664  1.00 9.34   ? 32  ASP B CG  1 
ATOM   2462 O  OD1 . ASP B 1 32  ? -16.903 9.511   43.729  1.00 9.51   ? 32  ASP B OD1 1 
ATOM   2463 O  OD2 . ASP B 1 32  ? -16.283 9.525   45.861  1.00 12.32  ? 32  ASP B OD2 1 
ATOM   2464 N  N   . ILE B 1 33  ? -18.315 12.535  44.446  1.00 7.74   ? 33  ILE B N   1 
ATOM   2465 C  CA  . ILE B 1 33  ? -19.469 12.889  45.310  1.00 8.26   ? 33  ILE B CA  1 
ATOM   2466 C  C   . ILE B 1 33  ? -19.718 11.636  46.145  1.00 9.01   ? 33  ILE B C   1 
ATOM   2467 O  O   . ILE B 1 33  ? -20.270 10.659  45.665  1.00 10.03  ? 33  ILE B O   1 
ATOM   2468 C  CB  . ILE B 1 33  ? -20.640 13.321  44.462  1.00 8.90   ? 33  ILE B CB  1 
ATOM   2469 C  CG1 . ILE B 1 33  ? -20.288 14.540  43.646  1.00 9.42   ? 33  ILE B CG1 1 
ATOM   2470 C  CG2 . ILE B 1 33  ? -21.836 13.588  45.443  1.00 11.02  ? 33  ILE B CG2 1 
ATOM   2471 C  CD1 . ILE B 1 33  ? -21.317 14.815  42.514  1.00 10.74  ? 33  ILE B CD1 1 
ATOM   2472 N  N   . ASP B 1 34  ? -19.366 11.726  47.406  1.00 10.90  ? 34  ASP B N   1 
ATOM   2473 C  CA  . ASP B 1 34  ? -19.642 10.636  48.382  1.00 11.69  ? 34  ASP B CA  1 
ATOM   2474 C  C   . ASP B 1 34  ? -21.059 10.934  48.884  1.00 12.57  ? 34  ASP B C   1 
ATOM   2475 O  O   . ASP B 1 34  ? -21.319 11.874  49.645  1.00 14.50  ? 34  ASP B O   1 
ATOM   2476 C  CB  . ASP B 1 34  ? -18.618 10.647  49.474  1.00 13.87  ? 34  ASP B CB  1 
ATOM   2477 C  CG  . ASP B 1 34  ? -18.859 9.624   50.558  1.00 20.31  ? 34  ASP B CG  1 
ATOM   2478 O  OD1 . ASP B 1 34  ? -20.023 9.272   50.833  1.00 21.32  ? 34  ASP B OD1 1 
ATOM   2479 O  OD2 . ASP B 1 34  ? -17.851 9.203   51.167  1.00 31.46  ? 34  ASP B OD2 1 
ATOM   2480 N  N   . THR B 1 35  ? -22.024 10.156  48.425  1.00 13.68  ? 35  THR B N   1 
ATOM   2481 C  CA  . THR B 1 35  ? -23.414 10.454  48.635  1.00 13.99  ? 35  THR B CA  1 
ATOM   2482 C  C   . THR B 1 35  ? -23.837 10.314  50.042  1.00 14.12  ? 35  THR B C   1 
ATOM   2483 O  O   . THR B 1 35  ? -24.772 11.009  50.495  1.00 16.99  ? 35  THR B O   1 
ATOM   2484 C  CB  . THR B 1 35  ? -24.333 9.555   47.807  1.00 15.25  ? 35  THR B CB  1 
ATOM   2485 O  OG1 . THR B 1 35  ? -24.199 8.227   48.310  1.00 16.13  ? 35  THR B OG1 1 
ATOM   2486 C  CG2 . THR B 1 35  ? -24.065 9.668   46.311  1.00 18.22  ? 35  THR B CG2 1 
ATOM   2487 N  N   . HIS B 1 36  ? -23.174 9.461   50.812  1.00 15.47  ? 36  HIS B N   1 
ATOM   2488 C  CA  . HIS B 1 36  ? -23.419 9.270   52.231  1.00 17.09  ? 36  HIS B CA  1 
ATOM   2489 C  C   . HIS B 1 36  ? -22.953 10.421  53.079  1.00 17.80  ? 36  HIS B C   1 
ATOM   2490 O  O   . HIS B 1 36  ? -23.643 10.761  54.086  1.00 20.73  ? 36  HIS B O   1 
ATOM   2491 C  CB  . HIS B 1 36  ? -22.936 7.852   52.639  1.00 18.28  ? 36  HIS B CB  1 
ATOM   2492 C  CG  . HIS B 1 36  ? -23.861 6.766   52.099  1.00 17.91  ? 36  HIS B CG  1 
ATOM   2493 N  ND1 . HIS B 1 36  ? -25.201 6.700   52.492  1.00 23.33  ? 36  HIS B ND1 1 
ATOM   2494 C  CD2 . HIS B 1 36  ? -23.684 5.812   51.071  1.00 19.99  ? 36  HIS B CD2 1 
ATOM   2495 C  CE1 . HIS B 1 36  ? -25.822 5.663   51.821  1.00 22.01  ? 36  HIS B CE1 1 
ATOM   2496 N  NE2 . HIS B 1 36  ? -24.905 5.112   50.956  1.00 25.45  ? 36  HIS B NE2 1 
ATOM   2497 N  N   . THR B 1 37  ? -21.872 11.091  52.611  1.00 19.13  ? 37  THR B N   1 
ATOM   2498 C  CA  . THR B 1 37  ? -21.250 12.210  53.362  1.00 19.22  ? 37  THR B CA  1 
ATOM   2499 C  C   . THR B 1 37  ? -21.810 13.606  52.966  1.00 17.05  ? 37  THR B C   1 
ATOM   2500 O  O   . THR B 1 37  ? -21.670 14.545  53.718  1.00 21.17  ? 37  THR B O   1 
ATOM   2501 C  CB  . THR B 1 37  ? -19.714 12.218  53.102  1.00 28.05  ? 37  THR B CB  1 
ATOM   2502 O  OG1 . THR B 1 37  ? -19.157 11.030  53.689  1.00 48.55  ? 37  THR B OG1 1 
ATOM   2503 C  CG2 . THR B 1 37  ? -18.998 13.402  53.783  1.00 23.76  ? 37  THR B CG2 1 
ATOM   2504 N  N   . ALA B 1 38  ? -22.413 13.700  51.802  1.00 15.02  ? 38  ALA B N   1 
ATOM   2505 C  CA  . ALA B 1 38  ? -23.051 14.961  51.384  1.00 13.99  ? 38  ALA B CA  1 
ATOM   2506 C  C   . ALA B 1 38  ? -24.129 15.300  52.348  1.00 17.30  ? 38  ALA B C   1 
ATOM   2507 O  O   . ALA B 1 38  ? -24.806 14.440  52.828  1.00 22.32  ? 38  ALA B O   1 
ATOM   2508 C  CB  . ALA B 1 38  ? -23.619 14.795  49.997  1.00 14.89  ? 38  ALA B CB  1 
ATOM   2509 N  N   . LYS B 1 39  ? -24.282 16.546  52.691  1.00 15.44  ? 39  LYS B N   1 
ATOM   2510 C  CA  . LYS B 1 39  ? -25.271 16.805  53.698  1.00 21.06  ? 39  LYS B CA  1 
ATOM   2511 C  C   . LYS B 1 39  ? -26.449 17.497  53.125  1.00 15.44  ? 39  LYS B C   1 
ATOM   2512 O  O   . LYS B 1 39  ? -26.343 18.467  52.382  1.00 14.62  ? 39  LYS B O   1 
ATOM   2513 C  CB  . LYS B 1 39  ? -24.725 17.601  54.852  1.00 30.45  ? 39  LYS B CB  1 
ATOM   2514 C  CG  . LYS B 1 39  ? -25.720 17.646  55.987  1.00 31.17  ? 39  LYS B CG  1 
ATOM   2515 C  CD  . LYS B 1 39  ? -25.137 18.567  56.993  1.00 25.19  ? 39  LYS B CD  1 
ATOM   2516 C  CE  . LYS B 1 39  ? -26.167 19.264  57.809  1.00 29.88  ? 39  LYS B CE  1 
ATOM   2517 N  NZ  . LYS B 1 39  ? -26.408 18.367  58.947  1.00 30.26  ? 39  LYS B NZ  1 
ATOM   2518 N  N   . TYR B 1 40  ? -27.629 16.992  53.466  1.00 17.64  ? 40  TYR B N   1 
ATOM   2519 C  CA  . TYR B 1 40  ? -28.840 17.595  53.091  1.00 15.28  ? 40  TYR B CA  1 
ATOM   2520 C  C   . TYR B 1 40  ? -28.927 18.974  53.673  1.00 13.48  ? 40  TYR B C   1 
ATOM   2521 O  O   . TYR B 1 40  ? -28.761 19.133  54.915  1.00 16.71  ? 40  TYR B O   1 
ATOM   2522 C  CB  . TYR B 1 40  ? -30.050 16.772  53.497  1.00 21.25  ? 40  TYR B CB  1 
ATOM   2523 C  CG  . TYR B 1 40  ? -31.337 17.507  53.345  1.00 19.65  ? 40  TYR B CG  1 
ATOM   2524 C  CD1 . TYR B 1 40  ? -31.793 17.923  52.088  1.00 18.76  ? 40  TYR B CD1 1 
ATOM   2525 C  CD2 . TYR B 1 40  ? -32.139 17.758  54.447  1.00 28.32  ? 40  TYR B CD2 1 
ATOM   2526 C  CE1 . TYR B 1 40  ? -33.010 18.579  51.952  1.00 20.92  ? 40  TYR B CE1 1 
ATOM   2527 C  CE2 . TYR B 1 40  ? -33.360 18.445  54.322  1.00 29.29  ? 40  TYR B CE2 1 
ATOM   2528 C  CZ  . TYR B 1 40  ? -33.777 18.864  53.086  1.00 26.18  ? 40  TYR B CZ  1 
ATOM   2529 O  OH  . TYR B 1 40  ? -34.971 19.522  52.917  1.00 31.96  ? 40  TYR B OH  1 
ATOM   2530 N  N   . ASP B 1 41  ? -29.187 19.968  52.867  1.00 13.59  ? 41  ASP B N   1 
ATOM   2531 C  CA  . ASP B 1 41  ? -29.287 21.366  53.340  1.00 13.83  ? 41  ASP B CA  1 
ATOM   2532 C  C   . ASP B 1 41  ? -30.672 21.855  53.089  1.00 16.31  ? 41  ASP B C   1 
ATOM   2533 O  O   . ASP B 1 41  ? -31.002 22.205  51.939  1.00 15.75  ? 41  ASP B O   1 
ATOM   2534 C  CB  . ASP B 1 41  ? -28.229 22.220  52.647  1.00 17.34  ? 41  ASP B CB  1 
ATOM   2535 C  CG  . ASP B 1 41  ? -28.211 23.626  53.119  1.00 19.97  ? 41  ASP B CG  1 
ATOM   2536 O  OD1 . ASP B 1 41  ? -29.088 23.999  53.937  1.00 21.17  ? 41  ASP B OD1 1 
ATOM   2537 O  OD2 . ASP B 1 41  ? -27.251 24.390  52.794  1.00 25.20  ? 41  ASP B OD2 1 
ATOM   2538 N  N   . PRO B 1 42  ? -31.496 21.937  54.136  1.00 18.58  ? 42  PRO B N   1 
ATOM   2539 C  CA  . PRO B 1 42  ? -32.883 22.384  53.914  1.00 22.80  ? 42  PRO B CA  1 
ATOM   2540 C  C   . PRO B 1 42  ? -32.958 23.850  53.495  1.00 24.08  ? 42  PRO B C   1 
ATOM   2541 O  O   . PRO B 1 42  ? -34.013 24.308  53.055  1.00 32.89  ? 42  PRO B O   1 
ATOM   2542 C  CB  . PRO B 1 42  ? -33.561 22.142  55.273  1.00 29.11  ? 42  PRO B CB  1 
ATOM   2543 C  CG  . PRO B 1 42  ? -32.410 22.190  56.240  1.00 28.06  ? 42  PRO B CG  1 
ATOM   2544 C  CD  . PRO B 1 42  ? -31.275 21.523  55.558  1.00 21.95  ? 42  PRO B CD  1 
ATOM   2545 N  N   . SER B 1 43  ? -31.878 24.607  53.646  1.00 22.11  ? 43  SER B N   1 
ATOM   2546 C  CA  . SER B 1 43  ? -31.821 26.036  53.173  1.00 25.48  ? 43  SER B CA  1 
ATOM   2547 C  C   . SER B 1 43  ? -31.606 26.185  51.656  1.00 22.10  ? 43  SER B C   1 
ATOM   2548 O  O   . SER B 1 43  ? -31.823 27.297  51.078  1.00 27.54  ? 43  SER B O   1 
ATOM   2549 C  CB  . SER B 1 43  ? -30.729 26.835  53.894  1.00 23.71  ? 43  SER B CB  1 
ATOM   2550 O  OG  . SER B 1 43  ? -29.410 26.521  53.544  1.00 24.77  ? 43  SER B OG  1 
ATOM   2551 N  N   . LEU B 1 44  ? -31.283 25.085  50.983  1.00 22.78  ? 44  LEU B N   1 
ATOM   2552 C  CA  . LEU B 1 44  ? -31.071 25.148  49.501  1.00 18.51  ? 44  LEU B CA  1 
ATOM   2553 C  C   . LEU B 1 44  ? -32.421 25.274  48.849  1.00 17.73  ? 44  LEU B C   1 
ATOM   2554 O  O   . LEU B 1 44  ? -33.407 24.766  49.302  1.00 25.55  ? 44  LEU B O   1 
ATOM   2555 C  CB  . LEU B 1 44  ? -30.325 23.947  49.006  1.00 16.51  ? 44  LEU B CB  1 
ATOM   2556 C  CG  . LEU B 1 44  ? -28.843 23.915  49.238  1.00 15.64  ? 44  LEU B CG  1 
ATOM   2557 C  CD1 . LEU B 1 44  ? -28.435 22.519  48.837  1.00 16.55  ? 44  LEU B CD1 1 
ATOM   2558 C  CD2 . LEU B 1 44  ? -28.081 24.999  48.517  1.00 15.80  ? 44  LEU B CD2 1 
ATOM   2559 N  N   . LYS B 1 45  ? -32.486 26.064  47.780  1.00 18.85  ? 45  LYS B N   1 
ATOM   2560 C  CA  . LYS B 1 45  ? -33.776 26.274  47.066  1.00 18.18  ? 45  LYS B CA  1 
ATOM   2561 C  C   . LYS B 1 45  ? -33.815 25.418  45.832  1.00 16.97  ? 45  LYS B C   1 
ATOM   2562 O  O   . LYS B 1 45  ? -32.786 24.945  45.383  1.00 17.49  ? 45  LYS B O   1 
ATOM   2563 C  CB  . LYS B 1 45  ? -33.900 27.679  46.659  1.00 17.94  ? 45  LYS B CB  1 
ATOM   2564 C  CG  . LYS B 1 45  ? -33.654 28.638  47.763  1.00 23.59  ? 45  LYS B CG  1 
ATOM   2565 C  CD  . LYS B 1 45  ? -33.708 30.043  47.225  1.00 27.73  ? 45  LYS B CD  1 
ATOM   2566 C  CE  . LYS B 1 45  ? -32.874 30.976  48.097  1.00 39.40  ? 45  LYS B CE  1 
ATOM   2567 N  NZ  . LYS B 1 45  ? -33.549 31.269  49.386  1.00 48.38  ? 45  LYS B NZ  1 
ATOM   2568 N  N   . PRO B 1 46  ? -35.038 25.147  45.314  1.00 16.57  ? 46  PRO B N   1 
ATOM   2569 C  CA  . PRO B 1 46  ? -35.114 24.506  43.987  1.00 17.30  ? 46  PRO B CA  1 
ATOM   2570 C  C   . PRO B 1 46  ? -34.294 25.298  42.995  1.00 13.66  ? 46  PRO B C   1 
ATOM   2571 O  O   . PRO B 1 46  ? -34.242 26.514  43.065  1.00 15.66  ? 46  PRO B O   1 
ATOM   2572 C  CB  . PRO B 1 46  ? -36.633 24.578  43.692  1.00 19.84  ? 46  PRO B CB  1 
ATOM   2573 C  CG  . PRO B 1 46  ? -37.335 24.709  45.007  1.00 24.35  ? 46  PRO B CG  1 
ATOM   2574 C  CD  . PRO B 1 46  ? -36.378 25.471  45.873  1.00 20.69  ? 46  PRO B CD  1 
ATOM   2575 N  N   . LEU B 1 47  ? -33.729 24.545  42.081  1.00 16.79  ? 47  LEU B N   1 
ATOM   2576 C  CA  . LEU B 1 47  ? -32.993 25.156  41.010  1.00 14.39  ? 47  LEU B CA  1 
ATOM   2577 C  C   . LEU B 1 47  ? -34.050 25.787  40.095  1.00 17.33  ? 47  LEU B C   1 
ATOM   2578 O  O   . LEU B 1 47  ? -35.039 25.149  39.843  1.00 22.26  ? 47  LEU B O   1 
ATOM   2579 C  CB  . LEU B 1 47  ? -32.259 24.094  40.234  1.00 18.69  ? 47  LEU B CB  1 
ATOM   2580 C  CG  . LEU B 1 47  ? -31.099 24.462  39.407  1.00 20.57  ? 47  LEU B CG  1 
ATOM   2581 C  CD1 . LEU B 1 47  ? -30.090 25.318  40.236  1.00 23.77  ? 47  LEU B CD1 1 
ATOM   2582 C  CD2 . LEU B 1 47  ? -30.479 23.202  38.805  1.00 21.01  ? 47  LEU B CD2 1 
ATOM   2583 N  N   . SER B 1 48  ? -33.800 26.980  39.572  1.00 13.73  ? 48  SER B N   1 
ATOM   2584 C  CA  . SER B 1 48  ? -34.637 27.609  38.577  1.00 14.84  ? 48  SER B CA  1 
ATOM   2585 C  C   . SER B 1 48  ? -33.851 27.655  37.271  1.00 13.81  ? 48  SER B C   1 
ATOM   2586 O  O   . SER B 1 48  ? -32.827 28.342  37.138  1.00 14.51  ? 48  SER B O   1 
ATOM   2587 C  CB  . SER B 1 48  ? -35.002 29.028  39.026  1.00 16.82  ? 48  SER B CB  1 
ATOM   2588 O  OG  . SER B 1 48  ? -35.598 29.757  38.000  1.00 20.03  ? 48  SER B OG  1 
ATOM   2589 N  N   . VAL B 1 49  ? -34.272 26.852  36.338  1.00 15.66  ? 49  VAL B N   1 
ATOM   2590 C  CA  . VAL B 1 49  ? -33.687 26.773  35.019  1.00 16.00  ? 49  VAL B CA  1 
ATOM   2591 C  C   . VAL B 1 49  ? -34.683 27.351  34.035  1.00 17.11  ? 49  VAL B C   1 
ATOM   2592 O  O   . VAL B 1 49  ? -35.728 26.765  33.845  1.00 24.45  ? 49  VAL B O   1 
ATOM   2593 C  CB  . VAL B 1 49  ? -33.418 25.306  34.650  1.00 19.00  ? 49  VAL B CB  1 
ATOM   2594 C  CG1 . VAL B 1 49  ? -32.653 25.268  33.344  1.00 24.55  ? 49  VAL B CG1 1 
ATOM   2595 C  CG2 . VAL B 1 49  ? -32.635 24.573  35.725  1.00 21.74  ? 49  VAL B CG2 1 
ATOM   2596 N  N   . SER B 1 50  ? -34.401 28.491  33.439  1.00 16.32  ? 50  SER B N   1 
ATOM   2597 C  CA  . SER B 1 50  ? -35.344 29.170  32.590  1.00 19.72  ? 50  SER B CA  1 
ATOM   2598 C  C   . SER B 1 50  ? -34.690 29.264  31.260  1.00 17.14  ? 50  SER B C   1 
ATOM   2599 O  O   . SER B 1 50  ? -34.047 30.256  30.922  1.00 18.24  ? 50  SER B O   1 
ATOM   2600 C  CB  . SER B 1 50  ? -35.723 30.538  33.169  1.00 21.55  ? 50  SER B CB  1 
ATOM   2601 O  OG  . SER B 1 50  ? -36.287 30.447  34.474  1.00 27.94  ? 50  SER B OG  1 
ATOM   2602 N  N   . TYR B 1 51  ? -34.973 28.266  30.436  1.00 17.86  ? 51  TYR B N   1 
ATOM   2603 C  CA  . TYR B 1 51  ? -34.361 28.168  29.137  1.00 15.73  ? 51  TYR B CA  1 
ATOM   2604 C  C   . TYR B 1 51  ? -35.314 28.436  27.962  1.00 18.15  ? 51  TYR B C   1 
ATOM   2605 O  O   . TYR B 1 51  ? -34.935 28.277  26.817  1.00 20.57  ? 51  TYR B O   1 
ATOM   2606 C  CB  . TYR B 1 51  ? -33.668 26.807  28.907  1.00 15.46  ? 51  TYR B CB  1 
ATOM   2607 C  CG  . TYR B 1 51  ? -32.396 26.521  29.655  1.00 13.73  ? 51  TYR B CG  1 
ATOM   2608 C  CD1 . TYR B 1 51  ? -31.656 27.539  30.294  1.00 15.26  ? 51  TYR B CD1 1 
ATOM   2609 C  CD2 . TYR B 1 51  ? -31.946 25.221  29.764  1.00 12.50  ? 51  TYR B CD2 1 
ATOM   2610 C  CE1 . TYR B 1 51  ? -30.482 27.205  31.008  1.00 11.88  ? 51  TYR B CE1 1 
ATOM   2611 C  CE2 . TYR B 1 51  ? -30.755 24.902  30.430  1.00 12.52  ? 51  TYR B CE2 1 
ATOM   2612 C  CZ  . TYR B 1 51  ? -30.034 25.895  31.058  1.00 11.61  ? 51  TYR B CZ  1 
ATOM   2613 O  OH  . TYR B 1 51  ? -28.876 25.567  31.703  1.00 11.86  ? 51  TYR B OH  1 
ATOM   2614 N  N   . ASP B 1 52  ? -36.536 28.878  28.221  1.00 20.14  ? 52  ASP B N   1 
ATOM   2615 C  CA  . ASP B 1 52  ? -37.585 29.109  27.194  1.00 22.20  ? 52  ASP B CA  1 
ATOM   2616 C  C   . ASP B 1 52  ? -37.182 30.064  26.081  1.00 23.01  ? 52  ASP B C   1 
ATOM   2617 O  O   . ASP B 1 52  ? -37.568 29.860  24.922  1.00 26.11  ? 52  ASP B O   1 
ATOM   2618 C  CB  . ASP B 1 52  ? -38.883 29.544  27.899  1.00 28.92  ? 52  ASP B CB  1 
ATOM   2619 C  CG  . ASP B 1 52  ? -38.636 30.611  29.013  1.00 41.54  ? 52  ASP B CG  1 
ATOM   2620 O  OD1 . ASP B 1 52  ? -38.127 30.249  30.117  1.00 51.76  ? 52  ASP B OD1 1 
ATOM   2621 O  OD2 . ASP B 1 52  ? -38.946 31.791  28.770  1.00 61.94  ? 52  ASP B OD2 1 
ATOM   2622 N  N   . GLN B 1 53  ? -36.286 31.001  26.380  1.00 23.06  ? 53  GLN B N   1 
ATOM   2623 C  CA  . GLN B 1 53  ? -35.902 31.962  25.327  1.00 24.15  ? 53  GLN B CA  1 
ATOM   2624 C  C   . GLN B 1 53  ? -34.472 31.761  24.863  1.00 18.60  ? 53  GLN B C   1 
ATOM   2625 O  O   . GLN B 1 53  ? -33.879 32.636  24.242  1.00 19.94  ? 53  GLN B O   1 
ATOM   2626 C  CB  . GLN B 1 53  ? -36.169 33.411  25.769  1.00 29.10  ? 53  GLN B CB  1 
ATOM   2627 C  CG  . GLN B 1 53  ? -37.655 33.711  25.860  1.00 37.16  ? 53  GLN B CG  1 
ATOM   2628 C  CD  . GLN B 1 53  ? -38.269 33.823  24.479  1.00 60.52  ? 53  GLN B CD  1 
ATOM   2629 O  OE1 . GLN B 1 53  ? -37.667 34.406  23.570  1.00 60.48  ? 53  GLN B OE1 1 
ATOM   2630 N  NE2 . GLN B 1 53  ? -39.448 33.258  24.305  1.00 80.26  ? 53  GLN B NE2 1 
ATOM   2631 N  N   . ALA B 1 54  ? -33.930 30.604  25.143  1.00 18.81  ? 54  ALA B N   1 
ATOM   2632 C  CA  . ALA B 1 54  ? -32.548 30.389  24.787  1.00 16.64  ? 54  ALA B CA  1 
ATOM   2633 C  C   . ALA B 1 54  ? -32.404 30.500  23.267  1.00 17.28  ? 54  ALA B C   1 
ATOM   2634 O  O   . ALA B 1 54  ? -33.256 30.024  22.507  1.00 24.06  ? 54  ALA B O   1 
ATOM   2635 C  CB  . ALA B 1 54  ? -32.016 29.013  25.284  1.00 18.62  ? 54  ALA B CB  1 
ATOM   2636 N  N   . THR B 1 55  ? -31.305 31.118  22.821  1.00 14.34  ? 55  THR B N   1 
ATOM   2637 C  CA  . THR B 1 55  ? -30.936 31.303  21.380  1.00 16.46  ? 55  THR B CA  1 
ATOM   2638 C  C   . THR B 1 55  ? -29.578 30.721  21.097  1.00 13.41  ? 55  THR B C   1 
ATOM   2639 O  O   . THR B 1 55  ? -28.554 31.351  21.375  1.00 14.50  ? 55  THR B O   1 
ATOM   2640 C  CB  . THR B 1 55  ? -30.803 32.814  20.972  1.00 23.44  ? 55  THR B CB  1 
ATOM   2641 O  OG1 . THR B 1 55  ? -32.036 33.498  21.144  1.00 30.01  ? 55  THR B OG1 1 
ATOM   2642 C  CG2 . THR B 1 55  ? -30.375 32.889  19.484  1.00 26.42  ? 55  THR B CG2 1 
ATOM   2643 N  N   . SER B 1 56  ? -29.612 29.504  20.623  1.00 14.94  ? 56  SER B N   1 
ATOM   2644 C  CA  . SER B 1 56  ? -28.419 28.934  20.231  1.00 13.50  ? 56  SER B CA  1 
ATOM   2645 C  C   . SER B 1 56  ? -28.013 29.567  18.928  1.00 13.72  ? 56  SER B C   1 
ATOM   2646 O  O   . SER B 1 56  ? -28.738 30.050  18.122  1.00 17.66  ? 56  SER B O   1 
ATOM   2647 C  CB  . SER B 1 56  ? -28.413 27.399  20.051  1.00 15.44  ? 56  SER B CB  1 
ATOM   2648 O  OG  . SER B 1 56  ? -29.180 27.027  18.905  1.00 17.21  ? 56  SER B OG  1 
ATOM   2649 N  N   . LEU B 1 57  ? -26.704 29.580  18.733  1.00 11.86  ? 57  LEU B N   1 
ATOM   2650 C  CA  . LEU B 1 57  ? -26.138 30.217  17.538  1.00 14.06  ? 57  LEU B CA  1 
ATOM   2651 C  C   . LEU B 1 57  ? -25.290 29.282  16.672  1.00 13.81  ? 57  LEU B C   1 
ATOM   2652 O  O   . LEU B 1 57  ? -25.280 29.345  15.435  1.00 16.57  ? 57  LEU B O   1 
ATOM   2653 C  CB  . LEU B 1 57  ? -25.220 31.390  17.960  1.00 19.84  ? 57  LEU B CB  1 
ATOM   2654 C  CG  . LEU B 1 57  ? -25.898 32.630  18.566  1.00 24.88  ? 57  LEU B CG  1 
ATOM   2655 C  CD1 . LEU B 1 57  ? -24.892 33.681  19.101  1.00 29.01  ? 57  LEU B CD1 1 
ATOM   2656 C  CD2 . LEU B 1 57  ? -26.956 33.238  17.611  1.00 39.96  ? 57  LEU B CD2 1 
ATOM   2657 N  N   . ARG B 1 58  ? -24.395 28.518  17.291  1.00 15.67  ? 58  ARG B N   1 
ATOM   2658 C  CA  . ARG B 1 58  ? -23.343 27.855  16.535  1.00 14.47  ? 58  ARG B CA  1 
ATOM   2659 C  C   . ARG B 1 58  ? -22.755 26.702  17.361  1.00 12.69  ? 58  ARG B C   1 
ATOM   2660 O  O   . ARG B 1 58  ? -22.823 26.691  18.582  1.00 14.08  ? 58  ARG B O   1 
ATOM   2661 C  CB  . ARG B 1 58  ? -22.237 28.890  16.362  1.00 14.43  ? 58  ARG B CB  1 
ATOM   2662 C  CG  . ARG B 1 58  ? -21.155 28.479  15.464  1.00 16.64  ? 58  ARG B CG  1 
ATOM   2663 C  CD  . ARG B 1 58  ? -20.108 29.549  15.226  1.00 16.93  ? 58  ARG B CD  1 
ATOM   2664 N  NE  . ARG B 1 58  ? -19.220 29.567  16.377  1.00 14.82  ? 58  ARG B NE  1 
ATOM   2665 C  CZ  . ARG B 1 58  ? -17.912 29.759  16.336  1.00 14.30  ? 58  ARG B CZ  1 
ATOM   2666 N  NH1 . ARG B 1 58  ? -17.274 29.975  15.193  1.00 17.59  ? 58  ARG B NH1 1 
ATOM   2667 N  NH2 . ARG B 1 58  ? -17.233 29.724  17.472  1.00 14.42  ? 58  ARG B NH2 1 
ATOM   2668 N  N   . ILE B 1 59  ? -22.178 25.714  16.695  1.00 12.76  ? 59  ILE B N   1 
ATOM   2669 C  CA  . ILE B 1 59  ? -21.559 24.630  17.335  1.00 12.12  ? 59  ILE B CA  1 
ATOM   2670 C  C   . ILE B 1 59  ? -20.117 24.634  16.839  1.00 11.74  ? 59  ILE B C   1 
ATOM   2671 O  O   . ILE B 1 59  ? -19.785 24.768  15.588  1.00 15.45  ? 59  ILE B O   1 
ATOM   2672 C  CB  . ILE B 1 59  ? -22.218 23.323  17.072  1.00 13.55  ? 59  ILE B CB  1 
ATOM   2673 C  CG1 . ILE B 1 59  ? -21.650 22.164  17.966  1.00 12.73  ? 59  ILE B CG1 1 
ATOM   2674 C  CG2 . ILE B 1 59  ? -22.199 22.896  15.593  1.00 13.70  ? 59  ILE B CG2 1 
ATOM   2675 C  CD1 . ILE B 1 59  ? -22.473 20.929  17.887  1.00 14.24  ? 59  ILE B CD1 1 
ATOM   2676 N  N   . LEU B 1 60  ? -19.149 24.432  17.713  1.00 11.78  ? 60  LEU B N   1 
ATOM   2677 C  CA  . LEU B 1 60  ? -17.766 24.511  17.474  1.00 10.95  ? 60  LEU B CA  1 
ATOM   2678 C  C   . LEU B 1 60  ? -16.905 23.355  17.974  1.00 11.95  ? 60  LEU B C   1 
ATOM   2679 O  O   . LEU B 1 60  ? -17.018 23.000  19.136  1.00 11.84  ? 60  LEU B O   1 
ATOM   2680 C  CB  . LEU B 1 60  ? -17.196 25.825  18.149  1.00 11.95  ? 60  LEU B CB  1 
ATOM   2681 C  CG  . LEU B 1 60  ? -15.667 25.961  18.080  1.00 12.86  ? 60  LEU B CG  1 
ATOM   2682 C  CD1 . LEU B 1 60  ? -15.154 26.255  16.670  1.00 13.09  ? 60  LEU B CD1 1 
ATOM   2683 C  CD2 . LEU B 1 60  ? -15.119 27.057  19.057  1.00 13.62  ? 60  LEU B CD2 1 
ATOM   2684 N  N   . ASN B 1 61  ? -16.056 22.749  17.157  1.00 11.45  ? 61  ASN B N   1 
ATOM   2685 C  CA  . ASN B 1 61  ? -15.070 21.792  17.600  1.00 12.65  ? 61  ASN B CA  1 
ATOM   2686 C  C   . ASN B 1 61  ? -13.835 22.598  18.020  1.00 11.74  ? 61  ASN B C   1 
ATOM   2687 O  O   . ASN B 1 61  ? -13.204 23.159  17.179  1.00 14.31  ? 61  ASN B O   1 
ATOM   2688 C  CB  . ASN B 1 61  ? -14.770 20.767  16.508  1.00 11.78  ? 61  ASN B CB  1 
ATOM   2689 C  CG  . ASN B 1 61  ? -13.688 19.780  16.933  1.00 11.44  ? 61  ASN B CG  1 
ATOM   2690 O  OD1 . ASN B 1 61  ? -12.833 20.009  17.813  1.00 13.59  ? 61  ASN B OD1 1 
ATOM   2691 N  ND2 . ASN B 1 61  ? -13.720 18.558  16.337  1.00 13.37  ? 61  ASN B ND2 1 
ATOM   2692 N  N   . ASN B 1 62  ? -13.566 22.655  19.311  1.00 13.27  ? 62  ASN B N   1 
ATOM   2693 C  CA  . ASN B 1 62  ? -12.501 23.526  19.771  1.00 15.29  ? 62  ASN B CA  1 
ATOM   2694 C  C   . ASN B 1 62  ? -11.171 22.771  19.966  1.00 15.17  ? 62  ASN B C   1 
ATOM   2695 O  O   . ASN B 1 62  ? -10.191 23.278  20.561  1.00 21.76  ? 62  ASN B O   1 
ATOM   2696 C  CB  . ASN B 1 62  ? -12.786 24.299  21.014  1.00 18.66  ? 62  ASN B CB  1 
ATOM   2697 C  CG  . ASN B 1 62  ? -13.125 23.364  22.157  1.00 19.60  ? 62  ASN B CG  1 
ATOM   2698 O  OD1 . ASN B 1 62  ? -12.588 22.239  22.337  1.00 15.29  ? 62  ASN B OD1 1 
ATOM   2699 N  ND2 . ASN B 1 62  ? -14.078 23.806  22.962  1.00 32.46  ? 62  ASN B ND2 1 
ATOM   2700 N  N   . GLY B 1 63  ? -11.172 21.483  19.571  1.00 13.39  ? 63  GLY B N   1 
ATOM   2701 C  CA  . GLY B 1 63  ? -10.016 20.692  19.664  1.00 13.34  ? 63  GLY B CA  1 
ATOM   2702 C  C   . GLY B 1 63  ? -9.929  19.837  20.962  1.00 15.11  ? 63  GLY B C   1 
ATOM   2703 O  O   . GLY B 1 63  ? -9.070  18.986  21.083  1.00 16.90  ? 63  GLY B O   1 
ATOM   2704 N  N   . HIS B 1 64  ? -10.833 20.058  21.884  1.00 13.28  ? 64  HIS B N   1 
ATOM   2705 C  CA  . HIS B 1 64  ? -10.871 19.362  23.237  1.00 16.80  ? 64  HIS B CA  1 
ATOM   2706 C  C   . HIS B 1 64  ? -12.241 18.674  23.330  1.00 14.82  ? 64  HIS B C   1 
ATOM   2707 O  O   . HIS B 1 64  ? -12.330 17.524  23.802  1.00 17.18  ? 64  HIS B O   1 
ATOM   2708 C  CB  . HIS B 1 64  ? -10.612 20.392  24.369  1.00 17.45  ? 64  HIS B CB  1 
ATOM   2709 C  CG  . HIS B 1 64  ? -9.335  21.079  24.247  1.00 18.72  ? 64  HIS B CG  1 
ATOM   2710 N  ND1 . HIS B 1 64  ? -8.129  20.418  24.386  1.00 22.44  ? 64  HIS B ND1 1 
ATOM   2711 C  CD2 . HIS B 1 64  ? -9.046  22.415  24.081  1.00 20.76  ? 64  HIS B CD2 1 
ATOM   2712 C  CE1 . HIS B 1 64  ? -7.136  21.303  24.289  1.00 21.05  ? 64  HIS B CE1 1 
ATOM   2713 N  NE2 . HIS B 1 64  ? -7.681  22.525  24.078  1.00 22.61  ? 64  HIS B NE2 1 
ATOM   2714 N  N   . ALA B 1 65  ? -13.285 19.384  22.921  1.00 13.99  ? 65  ALA B N   1 
ATOM   2715 C  CA  . ALA B 1 65  ? -14.663 18.950  22.946  1.00 12.95  ? 65  ALA B CA  1 
ATOM   2716 C  C   . ALA B 1 65  ? -15.432 19.755  21.866  1.00 11.20  ? 65  ALA B C   1 
ATOM   2717 O  O   . ALA B 1 65  ? -14.778 20.451  21.025  1.00 13.26  ? 65  ALA B O   1 
ATOM   2718 C  CB  . ALA B 1 65  ? -15.279 19.126  24.343  1.00 14.35  ? 65  ALA B CB  1 
ATOM   2719 N  N   . PHE B 1 66  ? -16.738 19.753  21.864  1.00 12.32  ? 66  PHE B N   1 
ATOM   2720 C  CA  . PHE B 1 66  ? -17.522 20.696  21.048  1.00 10.77  ? 66  PHE B CA  1 
ATOM   2721 C  C   . PHE B 1 66  ? -18.349 21.566  21.924  1.00 10.64  ? 66  PHE B C   1 
ATOM   2722 O  O   . PHE B 1 66  ? -18.911 21.081  22.923  1.00 11.54  ? 66  PHE B O   1 
ATOM   2723 C  CB  . PHE B 1 66  ? -18.328 19.988  19.971  1.00 12.78  ? 66  PHE B CB  1 
ATOM   2724 C  CG  . PHE B 1 66  ? -19.386 19.054  20.462  1.00 11.18  ? 66  PHE B CG  1 
ATOM   2725 C  CD1 . PHE B 1 66  ? -20.648 19.531  20.824  1.00 12.16  ? 66  PHE B CD1 1 
ATOM   2726 C  CD2 . PHE B 1 66  ? -19.099 17.697  20.622  1.00 12.50  ? 66  PHE B CD2 1 
ATOM   2727 C  CE1 . PHE B 1 66  ? -21.571 18.668  21.345  1.00 13.37  ? 66  PHE B CE1 1 
ATOM   2728 C  CE2 . PHE B 1 66  ? -20.079 16.826  21.136  1.00 11.77  ? 66  PHE B CE2 1 
ATOM   2729 C  CZ  . PHE B 1 66  ? -21.327 17.294  21.484  1.00 12.74  ? 66  PHE B CZ  1 
ATOM   2730 N  N   . ASN B 1 67  ? -18.428 22.851  21.589  1.00 11.39  ? 67  ASN B N   1 
ATOM   2731 C  CA  . ASN B 1 67  ? -19.261 23.781  22.333  1.00 10.84  ? 67  ASN B CA  1 
ATOM   2732 C  C   . ASN B 1 67  ? -20.536 24.157  21.533  1.00 10.12  ? 67  ASN B C   1 
ATOM   2733 O  O   . ASN B 1 67  ? -20.394 24.553  20.333  1.00 12.16  ? 67  ASN B O   1 
ATOM   2734 C  CB  . ASN B 1 67  ? -18.516 25.077  22.582  1.00 11.90  ? 67  ASN B CB  1 
ATOM   2735 C  CG  . ASN B 1 67  ? -17.307 24.934  23.439  1.00 16.77  ? 67  ASN B CG  1 
ATOM   2736 O  OD1 . ASN B 1 67  ? -17.134 23.929  24.202  1.00 15.18  ? 67  ASN B OD1 1 
ATOM   2737 N  ND2 . ASN B 1 67  ? -16.436 25.940  23.350  1.00 19.53  ? 67  ASN B ND2 1 
ATOM   2738 N  N   . VAL B 1 68  ? -21.687 24.062  22.133  1.00 11.11  ? 68  VAL B N   1 
ATOM   2739 C  CA  . VAL B 1 68  ? -22.893 24.639  21.561  1.00 12.18  ? 68  VAL B CA  1 
ATOM   2740 C  C   . VAL B 1 68  ? -23.053 26.016  22.203  1.00 11.44  ? 68  VAL B C   1 
ATOM   2741 O  O   . VAL B 1 68  ? -23.182 26.112  23.451  1.00 11.50  ? 68  VAL B O   1 
ATOM   2742 C  CB  . VAL B 1 68  ? -24.128 23.764  21.792  1.00 12.36  ? 68  VAL B CB  1 
ATOM   2743 C  CG1 . VAL B 1 68  ? -25.387 24.508  21.300  1.00 13.95  ? 68  VAL B CG1 1 
ATOM   2744 C  CG2 . VAL B 1 68  ? -23.974 22.476  21.016  1.00 14.36  ? 68  VAL B CG2 1 
ATOM   2745 N  N   . GLU B 1 69  ? -22.994 27.056  21.414  1.00 11.27  ? 69  GLU B N   1 
ATOM   2746 C  CA  . GLU B 1 69  ? -22.916 28.456  21.861  1.00 11.79  ? 69  GLU B CA  1 
ATOM   2747 C  C   . GLU B 1 69  ? -24.287 29.127  21.857  1.00 11.19  ? 69  GLU B C   1 
ATOM   2748 O  O   . GLU B 1 69  ? -25.088 28.879  20.899  1.00 13.27  ? 69  GLU B O   1 
ATOM   2749 C  CB  . GLU B 1 69  ? -22.013 29.213  20.930  1.00 12.06  ? 69  GLU B CB  1 
ATOM   2750 C  CG  . GLU B 1 69  ? -20.638 28.675  21.001  1.00 13.28  ? 69  GLU B CG  1 
ATOM   2751 C  CD  . GLU B 1 69  ? -19.800 29.121  19.830  1.00 13.22  ? 69  GLU B CD  1 
ATOM   2752 O  OE1 . GLU B 1 69  ? -20.270 29.839  18.895  1.00 14.42  ? 69  GLU B OE1 1 
ATOM   2753 O  OE2 . GLU B 1 69  ? -18.583 28.771  19.764  1.00 14.48  ? 69  GLU B OE2 1 
ATOM   2754 N  N   . PHE B 1 70  ? -24.490 30.027  22.794  1.00 12.49  ? 70  PHE B N   1 
ATOM   2755 C  CA  . PHE B 1 70  ? -25.739 30.764  22.883  1.00 12.53  ? 70  PHE B CA  1 
ATOM   2756 C  C   . PHE B 1 70  ? -25.484 32.247  22.803  1.00 12.18  ? 70  PHE B C   1 
ATOM   2757 O  O   . PHE B 1 70  ? -24.426 32.740  23.222  1.00 14.44  ? 70  PHE B O   1 
ATOM   2758 C  CB  . PHE B 1 70  ? -26.434 30.415  24.178  1.00 12.44  ? 70  PHE B CB  1 
ATOM   2759 C  CG  . PHE B 1 70  ? -27.001 29.015  24.156  1.00 12.19  ? 70  PHE B CG  1 
ATOM   2760 C  CD1 . PHE B 1 70  ? -26.152 27.898  24.348  1.00 12.60  ? 70  PHE B CD1 1 
ATOM   2761 C  CD2 . PHE B 1 70  ? -28.311 28.797  23.862  1.00 12.01  ? 70  PHE B CD2 1 
ATOM   2762 C  CE1 . PHE B 1 70  ? -26.656 26.625  24.202  1.00 14.62  ? 70  PHE B CE1 1 
ATOM   2763 C  CE2 . PHE B 1 70  ? -28.823 27.498  23.699  1.00 13.21  ? 70  PHE B CE2 1 
ATOM   2764 C  CZ  . PHE B 1 70  ? -27.970 26.403  23.902  1.00 13.62  ? 70  PHE B CZ  1 
ATOM   2765 N  N   . ASP B 1 71  ? -26.472 32.987  22.379  1.00 14.95  ? 71  ASP B N   1 
ATOM   2766 C  CA  . ASP B 1 71  ? -26.372 34.427  22.424  1.00 16.05  ? 71  ASP B CA  1 
ATOM   2767 C  C   . ASP B 1 71  ? -26.663 34.790  23.867  1.00 14.98  ? 71  ASP B C   1 
ATOM   2768 O  O   . ASP B 1 71  ? -27.750 34.581  24.382  1.00 20.99  ? 71  ASP B O   1 
ATOM   2769 C  CB  . ASP B 1 71  ? -27.454 34.976  21.512  1.00 24.94  ? 71  ASP B CB  1 
ATOM   2770 C  CG  . ASP B 1 71  ? -27.697 36.503  21.697  1.00 27.40  ? 71  ASP B CG  1 
ATOM   2771 O  OD1 . ASP B 1 71  ? -26.841 37.120  22.283  1.00 23.51  ? 71  ASP B OD1 1 
ATOM   2772 O  OD2 . ASP B 1 71  ? -28.726 37.071  21.283  1.00 72.57  ? 71  ASP B OD2 1 
ATOM   2773 N  N   . ASP B 1 72  ? -25.628 35.314  24.529  1.00 14.16  ? 72  ASP B N   1 
ATOM   2774 C  CA  . ASP B 1 72  ? -25.725 35.742  25.925  1.00 14.83  ? 72  ASP B CA  1 
ATOM   2775 C  C   . ASP B 1 72  ? -25.693 37.239  26.019  1.00 15.65  ? 72  ASP B C   1 
ATOM   2776 O  O   . ASP B 1 72  ? -25.269 37.764  27.049  1.00 18.13  ? 72  ASP B O   1 
ATOM   2777 C  CB  . ASP B 1 72  ? -24.601 35.112  26.777  1.00 14.52  ? 72  ASP B CB  1 
ATOM   2778 C  CG  . ASP B 1 72  ? -23.256 35.559  26.355  1.00 14.12  ? 72  ASP B CG  1 
ATOM   2779 O  OD1 . ASP B 1 72  ? -23.113 36.248  25.289  1.00 18.52  ? 72  ASP B OD1 1 
ATOM   2780 O  OD2 . ASP B 1 72  ? -22.312 35.280  27.101  1.00 17.00  ? 72  ASP B OD2 1 
ATOM   2781 N  N   . SER B 1 73  ? -26.172 37.950  25.020  1.00 16.74  ? 73  SER B N   1 
ATOM   2782 C  CA  . SER B 1 73  ? -26.087 39.438  25.078  1.00 20.54  ? 73  SER B CA  1 
ATOM   2783 C  C   . SER B 1 73  ? -27.424 40.028  25.647  1.00 21.04  ? 73  SER B C   1 
ATOM   2784 O  O   . SER B 1 73  ? -27.537 41.235  25.829  1.00 19.03  ? 73  SER B O   1 
ATOM   2785 C  CB  . SER B 1 73  ? -25.794 39.942  23.690  1.00 26.71  ? 73  SER B CB  1 
ATOM   2786 O  OG  . SER B 1 73  ? -26.939 39.765  22.902  1.00 22.55  ? 73  SER B OG  1 
ATOM   2787 N  N   . GLN B 1 74  ? -28.398 39.178  25.969  1.00 22.68  ? 74  GLN B N   1 
ATOM   2788 C  CA  . GLN B 1 74  ? -29.586 39.613  26.639  1.00 25.87  ? 74  GLN B CA  1 
ATOM   2789 C  C   . GLN B 1 74  ? -29.956 38.620  27.644  1.00 22.15  ? 74  GLN B C   1 
ATOM   2790 O  O   . GLN B 1 74  ? -29.465 37.533  27.612  1.00 17.47  ? 74  GLN B O   1 
ATOM   2791 C  CB  . GLN B 1 74  ? -30.753 39.622  25.717  1.00 28.75  ? 74  GLN B CB  1 
ATOM   2792 C  CG  . GLN B 1 74  ? -30.627 40.576  24.655  1.00 30.78  ? 74  GLN B CG  1 
ATOM   2793 C  CD  . GLN B 1 74  ? -31.956 40.754  24.125  1.00 33.31  ? 74  GLN B CD  1 
ATOM   2794 O  OE1 . GLN B 1 74  ? -32.858 41.230  24.817  1.00 53.14  ? 74  GLN B OE1 1 
ATOM   2795 N  NE2 . GLN B 1 74  ? -32.148 40.300  22.924  1.00 29.57  ? 74  GLN B NE2 1 
ATOM   2796 N  N   A ASP B 1 75  ? -30.782 38.934  28.653  0.50 30.27  ? 75  ASP B N   1 
ATOM   2797 N  N   B ASP B 1 75  ? -30.882 39.110  28.451  0.50 16.85  ? 75  ASP B N   1 
ATOM   2798 C  CA  A ASP B 1 75  ? -31.059 37.944  29.731  0.50 24.84  ? 75  ASP B CA  1 
ATOM   2799 C  CA  B ASP B 1 75  ? -31.442 38.403  29.479  0.50 18.24  ? 75  ASP B CA  1 
ATOM   2800 C  C   A ASP B 1 75  ? -32.157 37.017  29.370  0.50 24.80  ? 75  ASP B C   1 
ATOM   2801 C  C   B ASP B 1 75  ? -32.298 37.210  28.967  0.50 21.59  ? 75  ASP B C   1 
ATOM   2802 O  O   A ASP B 1 75  ? -33.332 37.204  29.706  0.50 43.19  ? 75  ASP B O   1 
ATOM   2803 O  O   B ASP B 1 75  ? -33.502 37.428  28.858  0.50 25.16  ? 75  ASP B O   1 
ATOM   2804 C  CB  A ASP B 1 75  ? -31.386 38.686  31.027  0.50 26.81  ? 75  ASP B CB  1 
ATOM   2805 C  CB  B ASP B 1 75  ? -32.241 39.413  30.356  0.50 20.65  ? 75  ASP B CB  1 
ATOM   2806 C  CG  A ASP B 1 75  ? -30.555 38.284  32.229  0.50 20.41  ? 75  ASP B CG  1 
ATOM   2807 C  CG  B ASP B 1 75  ? -32.859 38.746  31.581  0.50 25.56  ? 75  ASP B CG  1 
ATOM   2808 O  OD1 A ASP B 1 75  ? -29.796 37.301  32.183  0.50 16.07  ? 75  ASP B OD1 1 
ATOM   2809 O  OD1 B ASP B 1 75  ? -33.729 39.351  32.234  0.50 32.37  ? 75  ASP B OD1 1 
ATOM   2810 O  OD2 A ASP B 1 75  ? -30.700 38.987  33.258  0.50 28.14  ? 75  ASP B OD2 1 
ATOM   2811 O  OD2 B ASP B 1 75  ? -32.467 37.594  31.881  0.50 23.42  ? 75  ASP B OD2 1 
ATOM   2812 N  N   . LYS B 1 76  ? -31.730 36.043  28.616  1.00 22.03  ? 76  LYS B N   1 
ATOM   2813 C  CA  . LYS B 1 76  ? -32.624 35.058  27.994  1.00 25.93  ? 76  LYS B CA  1 
ATOM   2814 C  C   . LYS B 1 76  ? -32.783 33.716  28.718  1.00 34.83  ? 76  LYS B C   1 
ATOM   2815 O  O   . LYS B 1 76  ? -33.868 33.323  29.148  1.00 36.79  ? 76  LYS B O   1 
ATOM   2816 C  CB  . LYS B 1 76  ? -32.195 34.801  26.551  1.00 24.76  ? 76  LYS B CB  1 
ATOM   2817 C  CG  . LYS B 1 76  ? -32.350 36.007  25.645  1.00 45.13  ? 76  LYS B CG  1 
ATOM   2818 C  CD  . LYS B 1 76  ? -31.908 35.694  24.229  1.00 54.21  ? 76  LYS B CD  1 
ATOM   2819 C  CE  . LYS B 1 76  ? -32.205 36.841  23.287  1.00 64.88  ? 76  LYS B CE  1 
ATOM   2820 N  NZ  . LYS B 1 76  ? -31.896 36.496  21.868  1.00 47.05  ? 76  LYS B NZ  1 
ATOM   2821 N  N   . ALA B 1 77  ? -31.660 33.030  28.810  1.00 46.11  ? 77  ALA B N   1 
ATOM   2822 C  CA  . ALA B 1 77  ? -31.489 31.627  29.295  1.00 20.35  ? 77  ALA B CA  1 
ATOM   2823 C  C   . ALA B 1 77  ? -30.748 31.714  30.626  1.00 16.18  ? 77  ALA B C   1 
ATOM   2824 O  O   . ALA B 1 77  ? -29.541 31.871  30.650  1.00 23.32  ? 77  ALA B O   1 
ATOM   2825 C  CB  . ALA B 1 77  ? -30.666 30.858  28.292  1.00 19.42  ? 77  ALA B CB  1 
ATOM   2826 N  N   . VAL B 1 78  ? -31.460 31.622  31.714  1.00 14.48  ? 78  VAL B N   1 
ATOM   2827 C  CA  . VAL B 1 78  ? -30.812 31.901  32.959  1.00 15.59  ? 78  VAL B CA  1 
ATOM   2828 C  C   . VAL B 1 78  ? -31.044 30.807  33.991  1.00 13.14  ? 78  VAL B C   1 
ATOM   2829 O  O   . VAL B 1 78  ? -32.059 30.109  34.038  1.00 15.74  ? 78  VAL B O   1 
ATOM   2830 C  CB  . VAL B 1 78  ? -31.217 33.263  33.525  1.00 20.28  ? 78  VAL B CB  1 
ATOM   2831 C  CG1 . VAL B 1 78  ? -30.989 34.423  32.579  1.00 22.69  ? 78  VAL B CG1 1 
ATOM   2832 C  CG2 . VAL B 1 78  ? -32.623 33.194  33.890  1.00 23.61  ? 78  VAL B CG2 1 
ATOM   2833 N  N   . LEU B 1 79  ? -29.995 30.670  34.804  1.00 11.51  ? 79  LEU B N   1 
ATOM   2834 C  CA  . LEU B 1 79  ? -30.020 29.798  35.980  1.00 11.62  ? 79  LEU B CA  1 
ATOM   2835 C  C   . LEU B 1 79  ? -29.989 30.623  37.224  1.00 11.59  ? 79  LEU B C   1 
ATOM   2836 O  O   . LEU B 1 79  ? -29.142 31.561  37.324  1.00 13.20  ? 79  LEU B O   1 
ATOM   2837 C  CB  . LEU B 1 79  ? -28.741 28.900  35.886  1.00 13.28  ? 79  LEU B CB  1 
ATOM   2838 C  CG  . LEU B 1 79  ? -28.594 27.833  36.959  1.00 13.10  ? 79  LEU B CG  1 
ATOM   2839 C  CD1 . LEU B 1 79  ? -29.654 26.773  36.786  1.00 19.26  ? 79  LEU B CD1 1 
ATOM   2840 C  CD2 . LEU B 1 79  ? -27.247 27.155  36.837  1.00 12.98  ? 79  LEU B CD2 1 
ATOM   2841 N  N   . LYS B 1 80  ? -30.866 30.323  38.160  1.00 13.17  ? 80  LYS B N   1 
ATOM   2842 C  CA  . LYS B 1 80  ? -30.902 31.023  39.448  1.00 13.73  ? 80  LYS B CA  1 
ATOM   2843 C  C   . LYS B 1 80  ? -31.475 30.093  40.495  1.00 13.80  ? 80  LYS B C   1 
ATOM   2844 O  O   . LYS B 1 80  ? -31.754 28.940  40.207  1.00 13.50  ? 80  LYS B O   1 
ATOM   2845 C  CB  . LYS B 1 80  ? -31.639 32.320  39.372  1.00 17.28  ? 80  LYS B CB  1 
ATOM   2846 C  CG  . LYS B 1 80  ? -33.075 32.099  39.092  1.00 18.86  ? 80  LYS B CG  1 
ATOM   2847 C  CD  . LYS B 1 80  ? -33.777 33.440  39.074  1.00 23.31  ? 80  LYS B CD  1 
ATOM   2848 C  CE  . LYS B 1 80  ? -35.326 33.305  39.171  1.00 33.17  ? 80  LYS B CE  1 
ATOM   2849 N  NZ  . LYS B 1 80  ? -36.060 32.649  38.043  1.00 62.80  ? 80  LYS B NZ  1 
ATOM   2850 N  N   . GLY B 1 81  ? -31.558 30.570  41.741  1.00 14.46  ? 81  GLY B N   1 
ATOM   2851 C  CA  . GLY B 1 81  ? -32.022 29.749  42.822  1.00 15.65  ? 81  GLY B CA  1 
ATOM   2852 C  C   . GLY B 1 81  ? -31.030 28.699  43.117  1.00 14.89  ? 81  GLY B C   1 
ATOM   2853 O  O   . GLY B 1 81  ? -29.838 28.888  42.920  1.00 14.06  ? 81  GLY B O   1 
ATOM   2854 N  N   . GLY B 1 82  ? -31.504 27.581  43.626  1.00 19.53  ? 82  GLY B N   1 
ATOM   2855 C  CA  . GLY B 1 82  ? -30.588 26.540  43.970  1.00 19.89  ? 82  GLY B CA  1 
ATOM   2856 C  C   . GLY B 1 82  ? -29.750 27.153  45.102  1.00 15.92  ? 82  GLY B C   1 
ATOM   2857 O  O   . GLY B 1 82  ? -30.242 27.814  46.002  1.00 22.29  ? 82  GLY B O   1 
ATOM   2858 N  N   . PRO B 1 83  ? -28.376 26.993  45.017  1.00 15.66  ? 83  PRO B N   1 
ATOM   2859 C  CA  . PRO B 1 83  ? -27.451 27.559  45.948  1.00 15.93  ? 83  PRO B CA  1 
ATOM   2860 C  C   . PRO B 1 83  ? -27.011 28.985  45.569  1.00 14.54  ? 83  PRO B C   1 
ATOM   2861 O  O   . PRO B 1 83  ? -26.231 29.570  46.267  1.00 17.37  ? 83  PRO B O   1 
ATOM   2862 C  CB  . PRO B 1 83  ? -26.169 26.669  45.813  1.00 15.72  ? 83  PRO B CB  1 
ATOM   2863 C  CG  . PRO B 1 83  ? -26.184 26.336  44.373  1.00 14.76  ? 83  PRO B CG  1 
ATOM   2864 C  CD  . PRO B 1 83  ? -27.665 26.169  44.021  1.00 15.01  ? 83  PRO B CD  1 
ATOM   2865 N  N   . LEU B 1 84  ? -27.487 29.523  44.475  1.00 12.90  ? 84  LEU B N   1 
ATOM   2866 C  CA  . LEU B 1 84  ? -26.957 30.723  43.865  1.00 12.99  ? 84  LEU B CA  1 
ATOM   2867 C  C   . LEU B 1 84  ? -27.599 31.956  44.461  1.00 15.06  ? 84  LEU B C   1 
ATOM   2868 O  O   . LEU B 1 84  ? -28.806 32.011  44.742  1.00 16.65  ? 84  LEU B O   1 
ATOM   2869 C  CB  . LEU B 1 84  ? -27.244 30.704  42.372  1.00 11.80  ? 84  LEU B CB  1 
ATOM   2870 C  CG  . LEU B 1 84  ? -26.640 29.487  41.634  1.00 10.35  ? 84  LEU B CG  1 
ATOM   2871 C  CD1 . LEU B 1 84  ? -27.136 29.440  40.188  1.00 11.41  ? 84  LEU B CD1 1 
ATOM   2872 C  CD2 . LEU B 1 84  ? -25.087 29.459  41.746  1.00 11.68  ? 84  LEU B CD2 1 
ATOM   2873 N  N   . ASP B 1 85  ? -26.834 33.043  44.511  1.00 16.43  ? 85  ASP B N   1 
ATOM   2874 C  CA  . ASP B 1 85  ? -27.302 34.400  44.766  1.00 18.58  ? 85  ASP B CA  1 
ATOM   2875 C  C   . ASP B 1 85  ? -27.296 35.071  43.389  1.00 18.17  ? 85  ASP B C   1 
ATOM   2876 O  O   . ASP B 1 85  ? -26.305 35.051  42.620  1.00 24.00  ? 85  ASP B O   1 
ATOM   2877 C  CB  . ASP B 1 85  ? -26.348 35.060  45.745  1.00 21.05  ? 85  ASP B CB  1 
ATOM   2878 C  CG  . ASP B 1 85  ? -26.516 34.559  47.143  1.00 29.06  ? 85  ASP B CG  1 
ATOM   2879 O  OD1 . ASP B 1 85  ? -27.602 33.998  47.525  1.00 35.42  ? 85  ASP B OD1 1 
ATOM   2880 O  OD2 . ASP B 1 85  ? -25.527 34.732  47.904  1.00 45.35  ? 85  ASP B OD2 1 
ATOM   2881 N  N   . GLY B 1 86  ? -28.356 35.741  43.031  1.00 23.29  ? 86  GLY B N   1 
ATOM   2882 C  CA  . GLY B 1 86  ? -28.345 36.347  41.740  1.00 22.64  ? 86  GLY B CA  1 
ATOM   2883 C  C   . GLY B 1 86  ? -28.600 35.411  40.541  1.00 20.92  ? 86  GLY B C   1 
ATOM   2884 O  O   . GLY B 1 86  ? -29.061 34.259  40.663  1.00 25.80  ? 86  GLY B O   1 
ATOM   2885 N  N   A THR B 1 87  ? -28.404 35.986  39.355  0.50 15.20  ? 87  THR B N   1 
ATOM   2886 N  N   B THR B 1 87  ? -28.204 35.894  39.376  0.50 14.67  ? 87  THR B N   1 
ATOM   2887 C  CA  A THR B 1 87  ? -28.739 35.418  38.031  0.50 14.51  ? 87  THR B CA  1 
ATOM   2888 C  CA  B THR B 1 87  ? -28.643 35.297  38.131  0.50 14.29  ? 87  THR B CA  1 
ATOM   2889 C  C   A THR B 1 87  ? -27.459 35.046  37.327  0.50 12.31  ? 87  THR B C   1 
ATOM   2890 C  C   B THR B 1 87  ? -27.489 35.104  37.138  0.50 13.14  ? 87  THR B C   1 
ATOM   2891 O  O   A THR B 1 87  ? -26.472 35.854  37.365  0.50 9.92   ? 87  THR B O   1 
ATOM   2892 O  O   B THR B 1 87  ? -26.638 36.005  36.829  0.50 12.74  ? 87  THR B O   1 
ATOM   2893 C  CB  A THR B 1 87  ? -29.441 36.485  37.131  0.50 18.23  ? 87  THR B CB  1 
ATOM   2894 C  CB  B THR B 1 87  ? -29.735 36.152  37.482  0.50 12.90  ? 87  THR B CB  1 
ATOM   2895 O  OG1 A THR B 1 87  ? -30.579 37.007  37.786  0.50 21.15  ? 87  THR B OG1 1 
ATOM   2896 O  OG1 B THR B 1 87  ? -29.150 37.417  37.267  0.50 13.19  ? 87  THR B OG1 1 
ATOM   2897 C  CG2 A THR B 1 87  ? -29.951 35.867  35.840  0.50 19.32  ? 87  THR B CG2 1 
ATOM   2898 C  CG2 B THR B 1 87  ? -30.992 36.292  38.319  0.50 14.14  ? 87  THR B CG2 1 
ATOM   2899 N  N   . TYR B 1 88  ? -27.511 33.924  36.621  1.00 11.18  ? 88  TYR B N   1 
ATOM   2900 C  CA  . TYR B 1 88  ? -26.400 33.436  35.777  1.00 10.22  ? 88  TYR B CA  1 
ATOM   2901 C  C   . TYR B 1 88  ? -26.903 33.128  34.405  1.00 10.12  ? 88  TYR B C   1 
ATOM   2902 O  O   . TYR B 1 88  ? -27.896 32.444  34.224  1.00 14.30  ? 88  TYR B O   1 
ATOM   2903 C  CB  . TYR B 1 88  ? -25.727 32.220  36.379  1.00 10.78  ? 88  TYR B CB  1 
ATOM   2904 C  CG  . TYR B 1 88  ? -25.016 32.421  37.688  1.00 9.35   ? 88  TYR B CG  1 
ATOM   2905 C  CD1 . TYR B 1 88  ? -25.665 32.746  38.883  1.00 10.46  ? 88  TYR B CD1 1 
ATOM   2906 C  CD2 . TYR B 1 88  ? -23.635 32.298  37.722  1.00 8.95   ? 88  TYR B CD2 1 
ATOM   2907 C  CE1 . TYR B 1 88  ? -24.944 32.950  40.073  1.00 10.33  ? 88  TYR B CE1 1 
ATOM   2908 C  CE2 . TYR B 1 88  ? -22.887 32.425  38.913  1.00 8.51   ? 88  TYR B CE2 1 
ATOM   2909 C  CZ  . TYR B 1 88  ? -23.560 32.719  40.077  1.00 8.83   ? 88  TYR B CZ  1 
ATOM   2910 O  OH  . TYR B 1 88  ? -22.846 32.814  41.249  1.00 9.72   ? 88  TYR B OH  1 
ATOM   2911 N  N   . ARG B 1 89  ? -26.251 33.640  33.415  1.00 9.63   ? 89  ARG B N   1 
ATOM   2912 C  CA  . ARG B 1 89  ? -26.678 33.527  32.001  1.00 10.20  ? 89  ARG B CA  1 
ATOM   2913 C  C   . ARG B 1 89  ? -25.930 32.437  31.267  1.00 8.65   ? 89  ARG B C   1 
ATOM   2914 O  O   . ARG B 1 89  ? -24.704 32.336  31.325  1.00 8.68   ? 89  ARG B O   1 
ATOM   2915 C  CB  . ARG B 1 89  ? -26.381 34.863  31.326  1.00 13.78  ? 89  ARG B CB  1 
ATOM   2916 C  CG  . ARG B 1 89  ? -27.207 34.979  30.099  1.00 13.65  ? 89  ARG B CG  1 
ATOM   2917 C  CD  . ARG B 1 89  ? -27.080 36.354  29.520  1.00 15.12  ? 89  ARG B CD  1 
ATOM   2918 N  NE  . ARG B 1 89  ? -27.676 37.380  30.366  1.00 15.96  ? 89  ARG B NE  1 
ATOM   2919 C  CZ  . ARG B 1 89  ? -27.542 38.689  30.175  1.00 14.07  ? 89  ARG B CZ  1 
ATOM   2920 N  NH1 . ARG B 1 89  ? -26.822 39.156  29.160  1.00 17.65  ? 89  ARG B NH1 1 
ATOM   2921 N  NH2 . ARG B 1 89  ? -28.131 39.535  31.009  1.00 16.44  ? 89  ARG B NH2 1 
ATOM   2922 N  N   . LEU B 1 90  ? -26.713 31.613  30.556  1.00 9.28   ? 90  LEU B N   1 
ATOM   2923 C  CA  . LEU B 1 90  ? -26.149 30.506  29.769  1.00 9.05   ? 90  LEU B CA  1 
ATOM   2924 C  C   . LEU B 1 90  ? -25.276 31.074  28.632  1.00 10.35  ? 90  LEU B C   1 
ATOM   2925 O  O   . LEU B 1 90  ? -25.764 31.912  27.803  1.00 12.16  ? 90  LEU B O   1 
ATOM   2926 C  CB  . LEU B 1 90  ? -27.218 29.664  29.172  1.00 9.91   ? 90  LEU B CB  1 
ATOM   2927 C  CG  . LEU B 1 90  ? -26.806 28.494  28.280  1.00 11.56  ? 90  LEU B CG  1 
ATOM   2928 C  CD1 . LEU B 1 90  ? -26.065 27.427  29.103  1.00 11.90  ? 90  LEU B CD1 1 
ATOM   2929 C  CD2 . LEU B 1 90  ? -28.045 27.852  27.646  1.00 13.92  ? 90  LEU B CD2 1 
ATOM   2930 N  N   . ILE B 1 91  ? -24.037 30.624  28.529  1.00 9.37   ? 91  ILE B N   1 
ATOM   2931 C  CA  . ILE B 1 91  ? -23.150 30.982  27.413  1.00 10.19  ? 91  ILE B CA  1 
ATOM   2932 C  C   . ILE B 1 91  ? -22.908 29.808  26.476  1.00 8.96   ? 91  ILE B C   1 
ATOM   2933 O  O   . ILE B 1 91  ? -22.823 30.023  25.256  1.00 10.28  ? 91  ILE B O   1 
ATOM   2934 C  CB  . ILE B 1 91  ? -21.836 31.618  27.915  1.00 9.86   ? 91  ILE B CB  1 
ATOM   2935 C  CG1 . ILE B 1 91  ? -20.894 32.015  26.727  1.00 12.95  ? 91  ILE B CG1 1 
ATOM   2936 C  CG2 . ILE B 1 91  ? -21.087 30.756  28.938  1.00 11.16  ? 91  ILE B CG2 1 
ATOM   2937 C  CD1 . ILE B 1 91  ? -19.713 32.881  27.173  1.00 15.15  ? 91  ILE B CD1 1 
ATOM   2938 N  N   . GLN B 1 92  ? -22.752 28.578  26.974  1.00 9.03   ? 92  GLN B N   1 
ATOM   2939 C  CA  . GLN B 1 92  ? -22.500 27.434  26.122  1.00 9.28   ? 92  GLN B CA  1 
ATOM   2940 C  C   . GLN B 1 92  ? -22.689 26.182  26.907  1.00 8.78   ? 92  GLN B C   1 
ATOM   2941 O  O   . GLN B 1 92  ? -22.754 26.196  28.134  1.00 9.31   ? 92  GLN B O   1 
ATOM   2942 C  CB  . GLN B 1 92  ? -21.063 27.448  25.612  1.00 11.18  ? 92  GLN B CB  1 
ATOM   2943 C  CG  . GLN B 1 92  ? -19.983 27.475  26.693  1.00 11.79  ? 92  GLN B CG  1 
ATOM   2944 C  CD  . GLN B 1 92  ? -19.217 26.150  26.809  1.00 11.71  ? 92  GLN B CD  1 
ATOM   2945 O  OE1 . GLN B 1 92  ? -19.716 25.129  27.080  1.00 11.68  ? 92  GLN B OE1 1 
ATOM   2946 N  NE2 . GLN B 1 92  ? -18.046 26.129  26.308  1.00 21.50  ? 92  GLN B NE2 1 
ATOM   2947 N  N   . PHE B 1 93  ? -22.867 25.082  26.178  1.00 8.61   ? 93  PHE B N   1 
ATOM   2948 C  CA  . PHE B 1 93  ? -22.704 23.768  26.791  1.00 8.97   ? 93  PHE B CA  1 
ATOM   2949 C  C   . PHE B 1 93  ? -21.747 22.929  25.985  1.00 8.48   ? 93  PHE B C   1 
ATOM   2950 O  O   . PHE B 1 93  ? -21.503 23.154  24.776  1.00 10.21  ? 93  PHE B O   1 
ATOM   2951 C  CB  . PHE B 1 93  ? -24.053 23.047  27.041  1.00 9.21   ? 93  PHE B CB  1 
ATOM   2952 C  CG  . PHE B 1 93  ? -24.786 22.574  25.824  1.00 9.34   ? 93  PHE B CG  1 
ATOM   2953 C  CD1 . PHE B 1 93  ? -24.421 21.424  25.148  1.00 10.14  ? 93  PHE B CD1 1 
ATOM   2954 C  CD2 . PHE B 1 93  ? -25.927 23.256  25.373  1.00 10.47  ? 93  PHE B CD2 1 
ATOM   2955 C  CE1 . PHE B 1 93  ? -25.145 20.987  24.049  1.00 10.99  ? 93  PHE B CE1 1 
ATOM   2956 C  CE2 . PHE B 1 93  ? -26.651 22.788  24.291  1.00 12.13  ? 93  PHE B CE2 1 
ATOM   2957 C  CZ  . PHE B 1 93  ? -26.267 21.671  23.614  1.00 12.04  ? 93  PHE B CZ  1 
ATOM   2958 N  N   . HIS B 1 94  ? -21.207 21.894  26.657  1.00 8.44   ? 94  HIS B N   1 
ATOM   2959 C  CA  . HIS B 1 94  ? -20.312 20.923  26.049  1.00 8.47   ? 94  HIS B CA  1 
ATOM   2960 C  C   . HIS B 1 94  ? -20.409 19.640  26.895  1.00 7.60   ? 94  HIS B C   1 
ATOM   2961 O  O   . HIS B 1 94  ? -21.050 19.622  27.937  1.00 8.14   ? 94  HIS B O   1 
ATOM   2962 C  CB  . HIS B 1 94  ? -18.874 21.432  25.991  1.00 8.85   ? 94  HIS B CB  1 
ATOM   2963 C  CG  . HIS B 1 94  ? -18.324 21.704  27.388  1.00 7.90   ? 94  HIS B CG  1 
ATOM   2964 N  ND1 . HIS B 1 94  ? -18.491 22.869  28.013  1.00 8.32   ? 94  HIS B ND1 1 
ATOM   2965 C  CD2 . HIS B 1 94  ? -17.700 20.819  28.279  1.00 7.80   ? 94  HIS B CD2 1 
ATOM   2966 C  CE1 . HIS B 1 94  ? -18.024 22.751  29.284  1.00 8.00   ? 94  HIS B CE1 1 
ATOM   2967 N  NE2 . HIS B 1 94  ? -17.519 21.504  29.477  1.00 7.92   ? 94  HIS B NE2 1 
ATOM   2968 N  N   . PHE B 1 95  ? -19.744 18.606  26.407  1.00 7.70   ? 95  PHE B N   1 
ATOM   2969 C  CA  . PHE B 1 95  ? -19.692 17.309  27.090  1.00 8.06   ? 95  PHE B CA  1 
ATOM   2970 C  C   . PHE B 1 95  ? -18.249 16.879  27.266  1.00 7.46   ? 95  PHE B C   1 
ATOM   2971 O  O   . PHE B 1 95  ? -17.326 17.335  26.606  1.00 8.46   ? 95  PHE B O   1 
ATOM   2972 C  CB  . PHE B 1 95  ? -20.401 16.227  26.231  1.00 8.28   ? 95  PHE B CB  1 
ATOM   2973 C  CG  . PHE B 1 95  ? -21.821 16.501  25.906  1.00 7.87   ? 95  PHE B CG  1 
ATOM   2974 C  CD1 . PHE B 1 95  ? -22.159 17.361  24.870  1.00 9.95   ? 95  PHE B CD1 1 
ATOM   2975 C  CD2 . PHE B 1 95  ? -22.874 15.885  26.615  1.00 8.98   ? 95  PHE B CD2 1 
ATOM   2976 C  CE1 . PHE B 1 95  ? -23.489 17.573  24.506  1.00 10.30  ? 95  PHE B CE1 1 
ATOM   2977 C  CE2 . PHE B 1 95  ? -24.190 16.075  26.263  1.00 9.78   ? 95  PHE B CE2 1 
ATOM   2978 C  CZ  . PHE B 1 95  ? -24.501 16.952  25.211  1.00 10.15  ? 95  PHE B CZ  1 
ATOM   2979 N  N   . HIS B 1 96  ? -18.067 15.925  28.184  1.00 7.62   ? 96  HIS B N   1 
ATOM   2980 C  CA  . HIS B 1 96  ? -16.905 15.116  28.356  1.00 7.34   ? 96  HIS B CA  1 
ATOM   2981 C  C   . HIS B 1 96  ? -17.310 13.660  28.233  1.00 7.67   ? 96  HIS B C   1 
ATOM   2982 O  O   . HIS B 1 96  ? -18.407 13.308  28.721  1.00 7.86   ? 96  HIS B O   1 
ATOM   2983 C  CB  . HIS B 1 96  ? -16.207 15.322  29.723  1.00 8.34   ? 96  HIS B CB  1 
ATOM   2984 C  CG  . HIS B 1 96  ? -15.910 16.763  29.994  1.00 7.56   ? 96  HIS B CG  1 
ATOM   2985 N  ND1 . HIS B 1 96  ? -14.682 17.324  29.856  1.00 8.28   ? 96  HIS B ND1 1 
ATOM   2986 C  CD2 . HIS B 1 96  ? -16.740 17.805  30.416  1.00 7.41   ? 96  HIS B CD2 1 
ATOM   2987 C  CE1 . HIS B 1 96  ? -14.745 18.633  30.180  1.00 8.07   ? 96  HIS B CE1 1 
ATOM   2988 N  NE2 . HIS B 1 96  ? -15.977 18.944  30.511  1.00 7.14   ? 96  HIS B NE2 1 
ATOM   2989 N  N   . TRP B 1 97  ? -16.532 12.818  27.566  1.00 7.47   ? 97  TRP B N   1 
ATOM   2990 C  CA  . TRP B 1 97  ? -16.928 11.433  27.378  1.00 8.14   ? 97  TRP B CA  1 
ATOM   2991 C  C   . TRP B 1 97  ? -15.737 10.515  27.215  1.00 7.49   ? 97  TRP B C   1 
ATOM   2992 O  O   . TRP B 1 97  ? -14.578 10.955  27.142  1.00 8.56   ? 97  TRP B O   1 
ATOM   2993 C  CB  . TRP B 1 97  ? -17.884 11.319  26.128  1.00 8.89   ? 97  TRP B CB  1 
ATOM   2994 C  CG  . TRP B 1 97  ? -17.234 11.707  24.826  1.00 8.91   ? 97  TRP B CG  1 
ATOM   2995 C  CD1 . TRP B 1 97  ? -16.558 10.889  23.966  1.00 9.38   ? 97  TRP B CD1 1 
ATOM   2996 C  CD2 . TRP B 1 97  ? -17.163 13.009  24.246  1.00 8.99   ? 97  TRP B CD2 1 
ATOM   2997 N  NE1 . TRP B 1 97  ? -16.124 11.603  22.886  1.00 10.05  ? 97  TRP B NE1 1 
ATOM   2998 C  CE2 . TRP B 1 97  ? -16.470 12.911  23.029  1.00 9.60   ? 97  TRP B CE2 1 
ATOM   2999 C  CE3 . TRP B 1 97  ? -17.641 14.274  24.654  1.00 8.60   ? 97  TRP B CE3 1 
ATOM   3000 C  CZ2 . TRP B 1 97  ? -16.296 14.012  22.174  1.00 10.19  ? 97  TRP B CZ2 1 
ATOM   3001 C  CZ3 . TRP B 1 97  ? -17.435 15.366  23.839  1.00 9.58   ? 97  TRP B CZ3 1 
ATOM   3002 C  CH2 . TRP B 1 97  ? -16.760 15.220  22.613  1.00 10.89  ? 97  TRP B CH2 1 
ATOM   3003 N  N   . GLY B 1 98  ? -16.041 9.224   27.231  1.00 8.67   ? 98  GLY B N   1 
ATOM   3004 C  CA  . GLY B 1 98  ? -15.013 8.217   27.274  1.00 8.63   ? 98  GLY B CA  1 
ATOM   3005 C  C   . GLY B 1 98  ? -14.810 7.525   25.967  1.00 9.15   ? 98  GLY B C   1 
ATOM   3006 O  O   . GLY B 1 98  ? -15.543 7.664   24.977  1.00 9.90   ? 98  GLY B O   1 
ATOM   3007 N  N   . SER B 1 99  ? -13.790 6.641   25.971  1.00 9.66   ? 99  SER B N   1 
ATOM   3008 C  CA  . SER B 1 99  ? -13.549 5.704   24.859  1.00 10.90  ? 99  SER B CA  1 
ATOM   3009 C  C   . SER B 1 99  ? -14.435 4.477   24.975  1.00 11.88  ? 99  SER B C   1 
ATOM   3010 O  O   . SER B 1 99  ? -14.581 3.742   23.988  1.00 13.71  ? 99  SER B O   1 
ATOM   3011 C  CB  . SER B 1 99  ? -12.103 5.346   24.773  1.00 12.25  ? 99  SER B CB  1 
ATOM   3012 O  OG  . SER B 1 99  ? -11.663 4.840   26.026  1.00 12.09  ? 99  SER B OG  1 
ATOM   3013 N  N   . LEU B 1 100 ? -15.034 4.241   26.140  1.00 11.49  ? 100 LEU B N   1 
ATOM   3014 C  CA  . LEU B 1 100 ? -15.800 3.059   26.517  1.00 12.33  ? 100 LEU B CA  1 
ATOM   3015 C  C   . LEU B 1 100 ? -16.946 3.568   27.332  1.00 11.39  ? 100 LEU B C   1 
ATOM   3016 O  O   . LEU B 1 100 ? -16.798 4.588   28.019  1.00 11.26  ? 100 LEU B O   1 
ATOM   3017 C  CB  . LEU B 1 100 ? -14.990 2.139   27.478  1.00 16.91  ? 100 LEU B CB  1 
ATOM   3018 C  CG  . LEU B 1 100 ? -13.656 1.729   26.898  1.00 20.58  ? 100 LEU B CG  1 
ATOM   3019 C  CD1 . LEU B 1 100 ? -12.714 1.135   27.928  1.00 24.99  ? 100 LEU B CD1 1 
ATOM   3020 C  CD2 . LEU B 1 100 ? -14.000 0.728   25.806  1.00 23.58  ? 100 LEU B CD2 1 
ATOM   3021 N  N   . ASP B 1 101 ? -18.028 2.815   27.413  1.00 11.93  ? 101 ASP B N   1 
ATOM   3022 C  CA  . ASP B 1 101 ? -19.196 3.279   28.143  1.00 10.84  ? 101 ASP B CA  1 
ATOM   3023 C  C   . ASP B 1 101 ? -18.909 3.359   29.640  1.00 10.65  ? 101 ASP B C   1 
ATOM   3024 O  O   . ASP B 1 101 ? -19.576 4.098   30.342  1.00 12.57  ? 101 ASP B O   1 
ATOM   3025 C  CB  . ASP B 1 101 ? -20.428 2.393   27.963  1.00 12.46  ? 101 ASP B CB  1 
ATOM   3026 C  CG  . ASP B 1 101 ? -20.923 2.310   26.537  1.00 13.68  ? 101 ASP B CG  1 
ATOM   3027 O  OD1 . ASP B 1 101 ? -20.576 3.164   25.676  1.00 14.02  ? 101 ASP B OD1 1 
ATOM   3028 O  OD2 . ASP B 1 101 ? -21.713 1.385   26.272  1.00 17.28  ? 101 ASP B OD2 1 
ATOM   3029 N  N   . GLY B 1 102 ? -17.920 2.585   30.106  1.00 11.78  ? 102 GLY B N   1 
ATOM   3030 C  CA  . GLY B 1 102 ? -17.603 2.582   31.517  1.00 13.29  ? 102 GLY B CA  1 
ATOM   3031 C  C   . GLY B 1 102 ? -16.781 3.771   32.077  1.00 11.17  ? 102 GLY B C   1 
ATOM   3032 O  O   . GLY B 1 102 ? -16.467 3.773   33.287  1.00 12.03  ? 102 GLY B O   1 
ATOM   3033 N  N   . GLN B 1 103 ? -16.528 4.791   31.290  1.00 10.12  ? 103 GLN B N   1 
ATOM   3034 C  CA  . GLN B 1 103 ? -15.816 5.956   31.760  1.00 8.95   ? 103 GLN B CA  1 
ATOM   3035 C  C   . GLN B 1 103 ? -16.193 7.119   30.871  1.00 8.18   ? 103 GLN B C   1 
ATOM   3036 O  O   . GLN B 1 103 ? -16.734 6.932   29.781  1.00 8.95   ? 103 GLN B O   1 
ATOM   3037 C  CB  . GLN B 1 103 ? -14.312 5.751   31.774  1.00 10.19  ? 103 GLN B CB  1 
ATOM   3038 C  CG  . GLN B 1 103 ? -13.726 5.515   30.352  1.00 11.32  ? 103 GLN B CG  1 
ATOM   3039 C  CD  . GLN B 1 103 ? -12.331 4.943   30.435  1.00 13.59  ? 103 GLN B CD  1 
ATOM   3040 O  OE1 . GLN B 1 103 ? -12.100 4.010   31.202  1.00 23.64  ? 103 GLN B OE1 1 
ATOM   3041 N  NE2 . GLN B 1 103 ? -11.427 5.450   29.666  1.00 13.38  ? 103 GLN B NE2 1 
ATOM   3042 N  N   . GLY B 1 104 ? -15.903 8.326   31.342  1.00 7.87   ? 104 GLY B N   1 
ATOM   3043 C  CA  . GLY B 1 104 ? -16.187 9.530   30.551  1.00 7.57   ? 104 GLY B CA  1 
ATOM   3044 C  C   . GLY B 1 104 ? -16.611 10.716  31.412  1.00 7.53   ? 104 GLY B C   1 
ATOM   3045 O  O   . GLY B 1 104 ? -16.327 11.838  31.052  1.00 8.22   ? 104 GLY B O   1 
ATOM   3046 N  N   . SER B 1 105 ? -17.295 10.460  32.531  1.00 7.54   ? 105 SER B N   1 
ATOM   3047 C  CA  . SER B 1 105 ? -17.690 11.567  33.377  1.00 7.21   ? 105 SER B CA  1 
ATOM   3048 C  C   . SER B 1 105 ? -16.496 12.115  34.148  1.00 6.82   ? 105 SER B C   1 
ATOM   3049 O  O   . SER B 1 105 ? -15.478 11.443  34.341  1.00 7.77   ? 105 SER B O   1 
ATOM   3050 C  CB  . SER B 1 105 ? -18.835 11.216  34.322  1.00 7.31   ? 105 SER B CB  1 
ATOM   3051 O  OG  . SER B 1 105 ? -18.474 10.242  35.300  1.00 7.52   ? 105 SER B OG  1 
ATOM   3052 N  N   . GLU B 1 106 ? -16.643 13.374  34.544  1.00 6.62   ? 106 GLU B N   1 
ATOM   3053 C  CA  . GLU B 1 106 ? -15.612 14.067  35.344  1.00 7.16   ? 106 GLU B CA  1 
ATOM   3054 C  C   . GLU B 1 106 ? -15.939 13.885  36.836  1.00 6.75   ? 106 GLU B C   1 
ATOM   3055 O  O   . GLU B 1 106 ? -15.141 13.309  37.595  1.00 7.13   ? 106 GLU B O   1 
ATOM   3056 C  CB  . GLU B 1 106 ? -15.568 15.546  34.919  1.00 7.04   ? 106 GLU B CB  1 
ATOM   3057 C  CG  . GLU B 1 106 ? -15.067 15.679  33.483  1.00 9.21   ? 106 GLU B CG  1 
ATOM   3058 C  CD  . GLU B 1 106 ? -14.403 16.968  33.217  1.00 7.65   ? 106 GLU B CD  1 
ATOM   3059 O  OE1 . GLU B 1 106 ? -15.038 18.018  33.465  1.00 7.35   ? 106 GLU B OE1 1 
ATOM   3060 O  OE2 . GLU B 1 106 ? -13.252 16.935  32.742  1.00 8.83   ? 106 GLU B OE2 1 
ATOM   3061 N  N   . HIS B 1 107 ? -17.123 14.345  37.247  1.00 6.71   ? 107 HIS B N   1 
ATOM   3062 C  CA  . HIS B 1 107 ? -17.586 13.943  38.556  1.00 6.41   ? 107 HIS B CA  1 
ATOM   3063 C  C   . HIS B 1 107 ? -17.870 12.459  38.552  1.00 6.15   ? 107 HIS B C   1 
ATOM   3064 O  O   . HIS B 1 107 ? -18.221 11.855  37.542  1.00 7.02   ? 107 HIS B O   1 
ATOM   3065 C  CB  . HIS B 1 107 ? -18.843 14.747  38.944  1.00 6.62   ? 107 HIS B CB  1 
ATOM   3066 C  CG  . HIS B 1 107 ? -18.531 16.198  39.080  1.00 6.28   ? 107 HIS B CG  1 
ATOM   3067 N  ND1 . HIS B 1 107 ? -18.572 17.096  38.043  1.00 6.68   ? 107 HIS B ND1 1 
ATOM   3068 C  CD2 . HIS B 1 107 ? -18.054 16.926  40.176  1.00 6.81   ? 107 HIS B CD2 1 
ATOM   3069 C  CE1 . HIS B 1 107 ? -18.125 18.294  38.495  1.00 7.47   ? 107 HIS B CE1 1 
ATOM   3070 N  NE2 . HIS B 1 107 ? -17.823 18.215  39.793  1.00 6.69   ? 107 HIS B NE2 1 
ATOM   3071 N  N   . THR B 1 108 ? -17.753 11.869  39.767  1.00 7.32   ? 108 THR B N   1 
ATOM   3072 C  CA  . THR B 1 108 ? -18.123 10.515  40.030  1.00 7.34   ? 108 THR B CA  1 
ATOM   3073 C  C   . THR B 1 108 ? -19.063 10.492  41.227  1.00 7.60   ? 108 THR B C   1 
ATOM   3074 O  O   . THR B 1 108 ? -19.128 11.470  42.007  1.00 7.95   ? 108 THR B O   1 
ATOM   3075 C  CB  . THR B 1 108 ? -16.906 9.599   40.240  1.00 8.19   ? 108 THR B CB  1 
ATOM   3076 O  OG1 . THR B 1 108 ? -16.061 10.089  41.263  1.00 8.42   ? 108 THR B OG1 1 
ATOM   3077 C  CG2 . THR B 1 108 ? -16.101 9.546   38.938  1.00 9.06   ? 108 THR B CG2 1 
ATOM   3078 N  N   . VAL B 1 109 ? -19.857 9.408   41.357  1.00 8.01   ? 109 VAL B N   1 
ATOM   3079 C  CA  . VAL B 1 109 ? -20.875 9.322   42.439  1.00 8.54   ? 109 VAL B CA  1 
ATOM   3080 C  C   . VAL B 1 109 ? -20.527 8.028   43.188  1.00 8.97   ? 109 VAL B C   1 
ATOM   3081 O  O   . VAL B 1 109 ? -20.676 6.936   42.632  1.00 9.38   ? 109 VAL B O   1 
ATOM   3082 C  CB  . VAL B 1 109 ? -22.283 9.311   41.884  1.00 9.12   ? 109 VAL B CB  1 
ATOM   3083 C  CG1 . VAL B 1 109 ? -23.312 9.187   43.004  1.00 10.82  ? 109 VAL B CG1 1 
ATOM   3084 C  CG2 . VAL B 1 109 ? -22.537 10.604  41.063  1.00 10.67  ? 109 VAL B CG2 1 
ATOM   3085 N  N   . ASP B 1 110 ? -20.019 8.147   44.408  1.00 9.40   ? 110 ASP B N   1 
ATOM   3086 C  CA  . ASP B 1 110 ? -19.516 6.944   45.133  1.00 11.62  ? 110 ASP B CA  1 
ATOM   3087 C  C   . ASP B 1 110 ? -18.609 6.112   44.227  1.00 10.62  ? 110 ASP B C   1 
ATOM   3088 O  O   . ASP B 1 110 ? -18.674 4.897   44.174  1.00 10.72  ? 110 ASP B O   1 
ATOM   3089 C  CB  . ASP B 1 110 ? -20.730 6.103   45.635  1.00 12.13  ? 110 ASP B CB  1 
ATOM   3090 C  CG  . ASP B 1 110 ? -21.582 6.861   46.628  1.00 13.10  ? 110 ASP B CG  1 
ATOM   3091 O  OD1 . ASP B 1 110 ? -21.020 7.740   47.316  1.00 14.29  ? 110 ASP B OD1 1 
ATOM   3092 O  OD2 . ASP B 1 110 ? -22.751 6.540   46.725  1.00 15.91  ? 110 ASP B OD2 1 
ATOM   3093 N  N   . LYS B 1 111 ? -17.721 6.851   43.540  1.00 9.22   ? 111 LYS B N   1 
ATOM   3094 C  CA  . LYS B 1 111 ? -16.696 6.315   42.650  1.00 9.78   ? 111 LYS B CA  1 
ATOM   3095 C  C   . LYS B 1 111 ? -17.244 5.815   41.301  1.00 10.06  ? 111 LYS B C   1 
ATOM   3096 O  O   . LYS B 1 111 ? -16.450 5.446   40.409  1.00 11.20  ? 111 LYS B O   1 
ATOM   3097 C  CB  . LYS B 1 111 ? -15.759 5.268   43.264  1.00 11.79  ? 111 LYS B CB  1 
ATOM   3098 C  CG  . LYS B 1 111 ? -14.993 5.803   44.493  1.00 15.08  ? 111 LYS B CG  1 
ATOM   3099 C  CD  . LYS B 1 111 ? -14.122 7.033   44.215  1.00 18.28  ? 111 LYS B CD  1 
ATOM   3100 C  CE  . LYS B 1 111 ? -13.382 7.605   45.429  1.00 24.17  ? 111 LYS B CE  1 
ATOM   3101 N  NZ  . LYS B 1 111 ? -12.132 6.862   45.618  1.00 23.35  ? 111 LYS B NZ  1 
ATOM   3102 N  N   . LYS B 1 112 ? -18.550 5.836   41.106  1.00 9.22   ? 112 LYS B N   1 
ATOM   3103 C  CA  . LYS B 1 112 ? -19.154 5.445   39.816  1.00 9.33   ? 112 LYS B CA  1 
ATOM   3104 C  C   . LYS B 1 112 ? -18.811 6.491   38.768  1.00 8.56   ? 112 LYS B C   1 
ATOM   3105 O  O   . LYS B 1 112 ? -19.079 7.680   38.964  1.00 8.71   ? 112 LYS B O   1 
ATOM   3106 C  CB  . LYS B 1 112 ? -20.699 5.375   39.929  1.00 10.81  ? 112 LYS B CB  1 
ATOM   3107 C  CG  . LYS B 1 112 ? -21.384 4.998   38.589  1.00 12.13  ? 112 LYS B CG  1 
ATOM   3108 C  CD  . LYS B 1 112 ? -22.894 5.058   38.689  1.00 14.96  ? 112 LYS B CD  1 
ATOM   3109 C  CE  . LYS B 1 112 ? -23.589 4.842   37.402  1.00 16.24  ? 112 LYS B CE  1 
ATOM   3110 N  NZ  . LYS B 1 112 ? -23.350 3.523   36.893  1.00 16.00  ? 112 LYS B NZ  1 
ATOM   3111 N  N   A LYS B 1 113 ? -18.394 5.985   37.621  0.50 9.10   ? 113 LYS B N   1 
ATOM   3112 N  N   B LYS B 1 113 ? -18.208 6.041   37.651  0.50 8.85   ? 113 LYS B N   1 
ATOM   3113 C  CA  A LYS B 1 113 ? -18.162 6.799   36.453  0.50 8.91   ? 113 LYS B CA  1 
ATOM   3114 C  CA  B LYS B 1 113 ? -18.007 6.849   36.408  0.50 8.61   ? 113 LYS B CA  1 
ATOM   3115 C  C   A LYS B 1 113 ? -19.326 6.563   35.539  0.50 8.39   ? 113 LYS B C   1 
ATOM   3116 C  C   B LYS B 1 113 ? -19.132 6.577   35.376  0.50 8.86   ? 113 LYS B C   1 
ATOM   3117 O  O   A LYS B 1 113 ? -19.764 5.441   35.344  0.50 9.64   ? 113 LYS B O   1 
ATOM   3118 O  O   B LYS B 1 113 ? -19.403 5.429   35.001  0.50 9.01   ? 113 LYS B O   1 
ATOM   3119 C  CB  A LYS B 1 113 ? -16.905 6.353   35.728  0.50 8.58   ? 113 LYS B CB  1 
ATOM   3120 C  CB  B LYS B 1 113 ? -16.682 6.520   35.719  0.50 10.61  ? 113 LYS B CB  1 
ATOM   3121 C  CG  A LYS B 1 113 ? -15.585 6.581   36.516  0.50 9.72   ? 113 LYS B CG  1 
ATOM   3122 C  CG  B LYS B 1 113 ? -15.449 6.886   36.542  0.50 10.44  ? 113 LYS B CG  1 
ATOM   3123 C  CD  A LYS B 1 113 ? -14.390 6.006   35.772  0.50 10.79  ? 113 LYS B CD  1 
ATOM   3124 C  CD  B LYS B 1 113 ? -14.194 6.297   35.972  0.50 11.15  ? 113 LYS B CD  1 
ATOM   3125 C  CE  A LYS B 1 113 ? -13.034 6.559   36.317  0.50 11.95  ? 113 LYS B CE  1 
ATOM   3126 C  CE  B LYS B 1 113 ? -13.008 6.898   36.722  0.50 15.25  ? 113 LYS B CE  1 
ATOM   3127 N  NZ  A LYS B 1 113 ? -12.629 6.013   37.616  0.50 13.14  ? 113 LYS B NZ  1 
ATOM   3128 N  NZ  B LYS B 1 113 ? -11.809 6.101   36.437  0.50 15.72  ? 113 LYS B NZ  1 
ATOM   3129 N  N   . TYR B 1 114 ? -19.807 7.653   34.953  1.00 8.30   ? 114 TYR B N   1 
ATOM   3130 C  CA  . TYR B 1 114 ? -20.802 7.622   33.932  1.00 7.90   ? 114 TYR B CA  1 
ATOM   3131 C  C   . TYR B 1 114 ? -20.110 7.665   32.543  1.00 7.69   ? 114 TYR B C   1 
ATOM   3132 O  O   . TYR B 1 114 ? -18.921 7.962   32.410  1.00 8.41   ? 114 TYR B O   1 
ATOM   3133 C  CB  . TYR B 1 114 ? -21.845 8.718   34.060  1.00 7.76   ? 114 TYR B CB  1 
ATOM   3134 C  CG  . TYR B 1 114 ? -22.818 8.512   35.209  1.00 8.44   ? 114 TYR B CG  1 
ATOM   3135 C  CD1 . TYR B 1 114 ? -22.518 8.938   36.498  1.00 9.80   ? 114 TYR B CD1 1 
ATOM   3136 C  CD2 . TYR B 1 114 ? -24.037 7.896   34.996  1.00 9.95   ? 114 TYR B CD2 1 
ATOM   3137 C  CE1 . TYR B 1 114 ? -23.408 8.753   37.540  1.00 12.01  ? 114 TYR B CE1 1 
ATOM   3138 C  CE2 . TYR B 1 114 ? -24.936 7.706   36.030  1.00 12.32  ? 114 TYR B CE2 1 
ATOM   3139 C  CZ  . TYR B 1 114 ? -24.612 8.139   37.302  1.00 13.03  ? 114 TYR B CZ  1 
ATOM   3140 O  OH  . TYR B 1 114 ? -25.482 7.971   38.359  1.00 17.91  ? 114 TYR B OH  1 
ATOM   3141 N  N   . ALA B 1 115 ? -20.904 7.357   31.497  1.00 8.75   ? 115 ALA B N   1 
ATOM   3142 C  CA  . ALA B 1 115 ? -20.329 7.333   30.124  1.00 8.15   ? 115 ALA B CA  1 
ATOM   3143 C  C   . ALA B 1 115 ? -19.979 8.740   29.641  1.00 8.31   ? 115 ALA B C   1 
ATOM   3144 O  O   . ALA B 1 115 ? -19.132 8.873   28.750  1.00 8.71   ? 115 ALA B O   1 
ATOM   3145 C  CB  . ALA B 1 115 ? -21.383 6.714   29.203  1.00 10.05  ? 115 ALA B CB  1 
ATOM   3146 N  N   . ALA B 1 116 ? -20.635 9.764   30.177  1.00 8.10   ? 116 ALA B N   1 
ATOM   3147 C  CA  . ALA B 1 116 ? -20.338 11.145  29.735  1.00 8.14   ? 116 ALA B CA  1 
ATOM   3148 C  C   . ALA B 1 116 ? -20.961 12.070  30.746  1.00 7.14   ? 116 ALA B C   1 
ATOM   3149 O  O   . ALA B 1 116 ? -21.682 11.663  31.663  1.00 7.73   ? 116 ALA B O   1 
ATOM   3150 C  CB  . ALA B 1 116 ? -20.866 11.382  28.308  1.00 8.80   ? 116 ALA B CB  1 
ATOM   3151 N  N   . GLU B 1 117 ? -20.619 13.360  30.581  1.00 6.98   ? 117 GLU B N   1 
ATOM   3152 C  CA  . GLU B 1 117 ? -21.119 14.384  31.447  1.00 6.75   ? 117 GLU B CA  1 
ATOM   3153 C  C   . GLU B 1 117 ? -21.322 15.666  30.632  1.00 7.13   ? 117 GLU B C   1 
ATOM   3154 O  O   . GLU B 1 117 ? -20.396 16.099  29.920  1.00 8.37   ? 117 GLU B O   1 
ATOM   3155 C  CB  . GLU B 1 117 ? -20.165 14.621  32.639  1.00 7.15   ? 117 GLU B CB  1 
ATOM   3156 C  CG  . GLU B 1 117 ? -20.673 15.543  33.714  1.00 7.55   ? 117 GLU B CG  1 
ATOM   3157 C  CD  . GLU B 1 117 ? -19.743 15.641  34.937  1.00 6.82   ? 117 GLU B CD  1 
ATOM   3158 O  OE1 . GLU B 1 117 ? -19.069 14.619  35.216  1.00 7.63   ? 117 GLU B OE1 1 
ATOM   3159 O  OE2 . GLU B 1 117 ? -19.695 16.715  35.566  1.00 7.83   ? 117 GLU B OE2 1 
ATOM   3160 N  N   . LEU B 1 118 ? -22.519 16.232  30.756  1.00 7.16   ? 118 LEU B N   1 
ATOM   3161 C  CA  . LEU B 1 118 ? -22.889 17.483  30.081  1.00 7.17   ? 118 LEU B CA  1 
ATOM   3162 C  C   . LEU B 1 118 ? -22.648 18.629  31.069  1.00 7.06   ? 118 LEU B C   1 
ATOM   3163 O  O   . LEU B 1 118 ? -23.070 18.539  32.252  1.00 7.11   ? 118 LEU B O   1 
ATOM   3164 C  CB  . LEU B 1 118 ? -24.377 17.393  29.751  1.00 7.93   ? 118 LEU B CB  1 
ATOM   3165 C  CG  . LEU B 1 118 ? -25.132 18.670  29.375  1.00 8.48   ? 118 LEU B CG  1 
ATOM   3166 C  CD1 . LEU B 1 118 ? -24.524 19.337  28.138  1.00 9.32   ? 118 LEU B CD1 1 
ATOM   3167 C  CD2 . LEU B 1 118 ? -26.607 18.325  29.127  1.00 10.36  ? 118 LEU B CD2 1 
ATOM   3168 N  N   . HIS B 1 119 ? -22.038 19.682  30.582  1.00 7.00   ? 119 HIS B N   1 
ATOM   3169 C  CA  . HIS B 1 119 ? -21.775 20.903  31.374  1.00 7.06   ? 119 HIS B CA  1 
ATOM   3170 C  C   . HIS B 1 119 ? -22.478 22.081  30.667  1.00 6.77   ? 119 HIS B C   1 
ATOM   3171 O  O   . HIS B 1 119 ? -22.077 22.438  29.541  1.00 7.85   ? 119 HIS B O   1 
ATOM   3172 C  CB  . HIS B 1 119 ? -20.302 21.186  31.457  1.00 6.50   ? 119 HIS B CB  1 
ATOM   3173 C  CG  . HIS B 1 119 ? -19.585 20.224  32.366  1.00 6.56   ? 119 HIS B CG  1 
ATOM   3174 N  ND1 . HIS B 1 119 ? -18.225 20.019  32.344  1.00 6.55   ? 119 HIS B ND1 1 
ATOM   3175 C  CD2 . HIS B 1 119 ? -20.126 19.376  33.294  1.00 7.01   ? 119 HIS B CD2 1 
ATOM   3176 C  CE1 . HIS B 1 119 ? -17.957 19.079  33.256  1.00 7.33   ? 119 HIS B CE1 1 
ATOM   3177 N  NE2 . HIS B 1 119 ? -19.085 18.697  33.849  1.00 7.11   ? 119 HIS B NE2 1 
ATOM   3178 N  N   . LEU B 1 120 ? -23.456 22.669  31.342  1.00 7.20   ? 120 LEU B N   1 
ATOM   3179 C  CA  . LEU B 1 120 ? -24.130 23.913  30.889  1.00 7.62   ? 120 LEU B CA  1 
ATOM   3180 C  C   . LEU B 1 120 ? -23.482 25.030  31.686  1.00 7.01   ? 120 LEU B C   1 
ATOM   3181 O  O   . LEU B 1 120 ? -23.601 25.068  32.911  1.00 7.16   ? 120 LEU B O   1 
ATOM   3182 C  CB  . LEU B 1 120 ? -25.627 23.806  31.096  1.00 7.99   ? 120 LEU B CB  1 
ATOM   3183 C  CG  . LEU B 1 120 ? -26.304 22.702  30.210  1.00 9.27   ? 120 LEU B CG  1 
ATOM   3184 C  CD1 . LEU B 1 120 ? -27.183 21.842  31.073  1.00 14.04  ? 120 LEU B CD1 1 
ATOM   3185 C  CD2 . LEU B 1 120 ? -27.167 23.397  29.122  1.00 11.81  ? 120 LEU B CD2 1 
ATOM   3186 N  N   . VAL B 1 121 ? -22.772 25.900  30.983  1.00 7.47   ? 121 VAL B N   1 
ATOM   3187 C  CA  . VAL B 1 121 ? -21.936 26.936  31.619  1.00 8.04   ? 121 VAL B CA  1 
ATOM   3188 C  C   . VAL B 1 121 ? -22.677 28.266  31.629  1.00 7.93   ? 121 VAL B C   1 
ATOM   3189 O  O   . VAL B 1 121 ? -23.129 28.737  30.569  1.00 8.49   ? 121 VAL B O   1 
ATOM   3190 C  CB  . VAL B 1 121 ? -20.602 27.065  30.854  1.00 8.67   ? 121 VAL B CB  1 
ATOM   3191 C  CG1 . VAL B 1 121 ? -19.739 28.142  31.495  1.00 9.38   ? 121 VAL B CG1 1 
ATOM   3192 C  CG2 . VAL B 1 121 ? -19.869 25.728  30.754  1.00 9.42   ? 121 VAL B CG2 1 
ATOM   3193 N  N   . HIS B 1 122 ? -22.737 28.894  32.815  1.00 7.63   ? 122 HIS B N   1 
ATOM   3194 C  CA  . HIS B 1 122 ? -23.429 30.147  33.013  1.00 7.68   ? 122 HIS B CA  1 
ATOM   3195 C  C   . HIS B 1 122 ? -22.541 31.142  33.752  1.00 7.52   ? 122 HIS B C   1 
ATOM   3196 O  O   . HIS B 1 122 ? -21.801 30.726  34.633  1.00 8.59   ? 122 HIS B O   1 
ATOM   3197 C  CB  . HIS B 1 122 ? -24.708 29.965  33.819  1.00 8.22   ? 122 HIS B CB  1 
ATOM   3198 C  CG  . HIS B 1 122 ? -25.593 28.829  33.411  1.00 8.00   ? 122 HIS B CG  1 
ATOM   3199 N  ND1 . HIS B 1 122 ? -25.260 27.523  33.671  1.00 7.77   ? 122 HIS B ND1 1 
ATOM   3200 C  CD2 . HIS B 1 122 ? -26.830 28.764  32.767  1.00 8.49   ? 122 HIS B CD2 1 
ATOM   3201 C  CE1 . HIS B 1 122 ? -26.249 26.728  33.259  1.00 8.52   ? 122 HIS B CE1 1 
ATOM   3202 N  NE2 . HIS B 1 122 ? -27.217 27.445  32.687  1.00 9.19   ? 122 HIS B NE2 1 
ATOM   3203 N  N   . TRP B 1 123 ? -22.628 32.417  33.398  1.00 7.81   ? 123 TRP B N   1 
ATOM   3204 C  CA  . TRP B 1 123 ? -21.844 33.432  34.113  1.00 7.77   ? 123 TRP B CA  1 
ATOM   3205 C  C   . TRP B 1 123 ? -22.733 34.397  34.859  1.00 7.87   ? 123 TRP B C   1 
ATOM   3206 O  O   . TRP B 1 123 ? -23.850 34.748  34.451  1.00 8.65   ? 123 TRP B O   1 
ATOM   3207 C  CB  . TRP B 1 123 ? -20.900 34.202  33.135  1.00 9.84   ? 123 TRP B CB  1 
ATOM   3208 C  CG  . TRP B 1 123 ? -21.552 34.797  31.955  1.00 9.74   ? 123 TRP B CG  1 
ATOM   3209 C  CD1 . TRP B 1 123 ? -21.746 34.203  30.735  1.00 10.97  ? 123 TRP B CD1 1 
ATOM   3210 C  CD2 . TRP B 1 123 ? -22.069 36.147  31.831  1.00 10.31  ? 123 TRP B CD2 1 
ATOM   3211 N  NE1 . TRP B 1 123 ? -22.380 35.061  29.871  1.00 12.00  ? 123 TRP B NE1 1 
ATOM   3212 C  CE2 . TRP B 1 123 ? -22.576 36.266  30.482  1.00 11.98  ? 123 TRP B CE2 1 
ATOM   3213 C  CE3 . TRP B 1 123 ? -22.135 37.253  32.660  1.00 11.47  ? 123 TRP B CE3 1 
ATOM   3214 C  CZ2 . TRP B 1 123 ? -23.127 37.427  30.010  1.00 14.53  ? 123 TRP B CZ2 1 
ATOM   3215 C  CZ3 . TRP B 1 123 ? -22.718 38.410  32.199  1.00 13.80  ? 123 TRP B CZ3 1 
ATOM   3216 C  CH2 . TRP B 1 123 ? -23.187 38.498  30.898  1.00 14.18  ? 123 TRP B CH2 1 
ATOM   3217 N  N   . ASN B 1 124 ? -22.181 34.863  35.988  1.00 8.04   ? 124 ASN B N   1 
ATOM   3218 C  CA  . ASN B 1 124 ? -22.929 35.738  36.890  1.00 8.76   ? 124 ASN B CA  1 
ATOM   3219 C  C   . ASN B 1 124 ? -23.091 37.105  36.318  1.00 9.29   ? 124 ASN B C   1 
ATOM   3220 O  O   . ASN B 1 124 ? -22.071 37.804  36.042  1.00 9.16   ? 124 ASN B O   1 
ATOM   3221 C  CB  . ASN B 1 124 ? -22.135 35.795  38.205  1.00 9.41   ? 124 ASN B CB  1 
ATOM   3222 C  CG  . ASN B 1 124 ? -22.896 36.400  39.330  1.00 9.82   ? 124 ASN B CG  1 
ATOM   3223 O  OD1 . ASN B 1 124 ? -23.748 37.260  39.127  1.00 11.09  ? 124 ASN B OD1 1 
ATOM   3224 N  ND2 . ASN B 1 124 ? -22.603 35.942  40.553  1.00 11.48  ? 124 ASN B ND2 1 
ATOM   3225 N  N   . THR B 1 125 ? -24.337 37.525  36.124  1.00 9.91   ? 125 THR B N   1 
ATOM   3226 C  CA  . THR B 1 125 ? -24.623 38.843  35.570  1.00 11.84  ? 125 THR B CA  1 
ATOM   3227 C  C   . THR B 1 125 ? -24.115 40.064  36.276  1.00 12.83  ? 125 THR B C   1 
ATOM   3228 O  O   . THR B 1 125 ? -24.077 41.150  35.698  1.00 12.56  ? 125 THR B O   1 
ATOM   3229 C  CB  . THR B 1 125 ? -26.119 39.005  35.243  1.00 13.80  ? 125 THR B CB  1 
ATOM   3230 O  OG1 . THR B 1 125 ? -26.893 38.835  36.436  1.00 18.43  ? 125 THR B OG1 1 
ATOM   3231 C  CG2 . THR B 1 125 ? -26.554 37.976  34.210  1.00 16.65  ? 125 THR B CG2 1 
ATOM   3232 N  N   A LYS B 1 126 ? -23.711 39.904  37.518  0.50 12.28  ? 127 LYS B N   1 
ATOM   3233 N  N   B LYS B 1 126 ? -23.705 39.843  37.576  0.50 10.15  ? 127 LYS B N   1 
ATOM   3234 C  CA  A LYS B 1 126 ? -23.201 41.061  38.192  0.50 14.82  ? 127 LYS B CA  1 
ATOM   3235 C  CA  B LYS B 1 126 ? -23.140 40.960  38.299  0.50 11.40  ? 127 LYS B CA  1 
ATOM   3236 C  C   A LYS B 1 126 ? -21.769 41.362  37.784  0.50 11.24  ? 127 LYS B C   1 
ATOM   3237 C  C   B LYS B 1 126 ? -21.825 41.412  37.670  0.50 12.29  ? 127 LYS B C   1 
ATOM   3238 O  O   A LYS B 1 126 ? -21.255 42.385  38.226  0.50 11.01  ? 127 LYS B O   1 
ATOM   3239 O  O   B LYS B 1 126 ? -21.443 42.583  37.848  0.50 14.21  ? 127 LYS B O   1 
ATOM   3240 C  CB  A LYS B 1 126 ? -23.338 40.934  39.701  0.50 12.76  ? 127 LYS B CB  1 
ATOM   3241 C  CB  B LYS B 1 126 ? -23.021 40.679  39.808  0.50 11.70  ? 127 LYS B CB  1 
ATOM   3242 C  CG  A LYS B 1 126 ? -22.281 40.065  40.332  0.50 13.27  ? 127 LYS B CG  1 
ATOM   3243 C  CG  B LYS B 1 126 ? -21.928 39.709  40.237  0.50 12.84  ? 127 LYS B CG  1 
ATOM   3244 C  CD  A LYS B 1 126 ? -22.758 39.606  41.688  0.50 14.89  ? 127 LYS B CD  1 
ATOM   3245 C  CD  B LYS B 1 126 ? -22.095 39.318  41.705  0.50 14.59  ? 127 LYS B CD  1 
ATOM   3246 C  CE  A LYS B 1 126 ? -21.663 38.815  42.372  0.50 14.74  ? 127 LYS B CE  1 
ATOM   3247 C  CE  B LYS B 1 126 ? -21.873 40.505  42.644  0.50 17.69  ? 127 LYS B CE  1 
ATOM   3248 N  NZ  A LYS B 1 126 ? -22.116 38.372  43.716  0.50 17.24  ? 127 LYS B NZ  1 
ATOM   3249 N  NZ  B LYS B 1 126 ? -22.150 40.142  44.061  0.50 17.19  ? 127 LYS B NZ  1 
ATOM   3250 N  N   . TYR B 1 127 ? -21.140 40.523  36.961  1.00 10.67  ? 128 TYR B N   1 
ATOM   3251 C  CA  . TYR B 1 127 ? -19.802 40.801  36.411  1.00 11.50  ? 128 TYR B CA  1 
ATOM   3252 C  C   . TYR B 1 127 ? -19.811 41.214  34.974  1.00 10.55  ? 128 TYR B C   1 
ATOM   3253 O  O   . TYR B 1 127 ? -18.711 41.455  34.413  1.00 11.44  ? 128 TYR B O   1 
ATOM   3254 C  CB  . TYR B 1 127 ? -18.813 39.675  36.689  1.00 12.19  ? 128 TYR B CB  1 
ATOM   3255 C  CG  . TYR B 1 127 ? -18.702 39.343  38.155  1.00 10.58  ? 128 TYR B CG  1 
ATOM   3256 C  CD1 . TYR B 1 127 ? -18.346 40.319  39.073  1.00 12.33  ? 128 TYR B CD1 1 
ATOM   3257 C  CD2 . TYR B 1 127 ? -18.988 38.104  38.631  1.00 10.06  ? 128 TYR B CD2 1 
ATOM   3258 C  CE1 . TYR B 1 127 ? -18.261 40.028  40.425  1.00 12.05  ? 128 TYR B CE1 1 
ATOM   3259 C  CE2 . TYR B 1 127 ? -18.917 37.788  39.953  1.00 10.41  ? 128 TYR B CE2 1 
ATOM   3260 C  CZ  . TYR B 1 127 ? -18.540 38.771  40.877  1.00 11.08  ? 128 TYR B CZ  1 
ATOM   3261 O  OH  . TYR B 1 127 ? -18.477 38.545  42.204  1.00 13.54  ? 128 TYR B OH  1 
ATOM   3262 N  N   . GLY B 1 128 ? -20.986 41.299  34.362  1.00 10.71  ? 129 GLY B N   1 
ATOM   3263 C  CA  . GLY B 1 128 ? -21.097 41.980  33.044  1.00 12.81  ? 129 GLY B CA  1 
ATOM   3264 C  C   . GLY B 1 128 ? -20.742 41.126  31.827  1.00 12.01  ? 129 GLY B C   1 
ATOM   3265 O  O   . GLY B 1 128 ? -21.367 41.270  30.778  1.00 14.23  ? 129 GLY B O   1 
ATOM   3266 N  N   . ASP B 1 129 ? -19.730 40.273  31.899  1.00 12.47  ? 130 ASP B N   1 
ATOM   3267 C  CA  . ASP B 1 129 ? -19.502 39.353  30.824  1.00 14.63  ? 130 ASP B CA  1 
ATOM   3268 C  C   . ASP B 1 129 ? -18.686 38.144  31.357  1.00 14.40  ? 130 ASP B C   1 
ATOM   3269 O  O   . ASP B 1 129 ? -18.200 38.144  32.516  1.00 14.92  ? 130 ASP B O   1 
ATOM   3270 C  CB  . ASP B 1 129 ? -18.931 39.936  29.591  1.00 16.19  ? 130 ASP B CB  1 
ATOM   3271 C  CG  . ASP B 1 129 ? -17.549 40.406  29.761  1.00 12.98  ? 130 ASP B CG  1 
ATOM   3272 O  OD1 . ASP B 1 129 ? -16.958 40.187  30.817  1.00 20.07  ? 130 ASP B OD1 1 
ATOM   3273 O  OD2 . ASP B 1 129 ? -17.064 41.024  28.808  1.00 18.66  ? 130 ASP B OD2 1 
ATOM   3274 N  N   . PHE B 1 130 ? -18.516 37.128  30.532  1.00 13.38  ? 131 PHE B N   1 
ATOM   3275 C  CA  . PHE B 1 130 ? -17.863 35.901  30.969  1.00 12.09  ? 131 PHE B CA  1 
ATOM   3276 C  C   . PHE B 1 130 ? -16.387 36.116  31.341  1.00 12.47  ? 131 PHE B C   1 
ATOM   3277 O  O   . PHE B 1 130 ? -15.901 35.541  32.318  1.00 11.52  ? 131 PHE B O   1 
ATOM   3278 C  CB  . PHE B 1 130 ? -17.974 34.874  29.816  1.00 12.98  ? 131 PHE B CB  1 
ATOM   3279 C  CG  . PHE B 1 130 ? -17.241 33.611  30.045  1.00 12.53  ? 131 PHE B CG  1 
ATOM   3280 C  CD1 . PHE B 1 130 ? -17.877 32.580  30.676  1.00 12.44  ? 131 PHE B CD1 1 
ATOM   3281 C  CD2 . PHE B 1 130 ? -15.911 33.422  29.666  1.00 14.39  ? 131 PHE B CD2 1 
ATOM   3282 C  CE1 . PHE B 1 130 ? -17.248 31.370  30.941  1.00 13.88  ? 131 PHE B CE1 1 
ATOM   3283 C  CE2 . PHE B 1 130 ? -15.279 32.238  29.902  1.00 16.04  ? 131 PHE B CE2 1 
ATOM   3284 C  CZ  . PHE B 1 130 ? -15.946 31.207  30.569  1.00 16.69  ? 131 PHE B CZ  1 
ATOM   3285 N  N   . GLY B 1 131 ? -15.663 36.912  30.549  1.00 14.76  ? 132 GLY B N   1 
ATOM   3286 C  CA  . GLY B 1 131 ? -14.243 37.070  30.823  1.00 15.37  ? 132 GLY B CA  1 
ATOM   3287 C  C   . GLY B 1 131 ? -13.950 37.718  32.183  1.00 15.82  ? 132 GLY B C   1 
ATOM   3288 O  O   . GLY B 1 131 ? -12.929 37.407  32.837  1.00 16.87  ? 132 GLY B O   1 
ATOM   3289 N  N   . LYS B 1 132 ? -14.769 38.653  32.619  1.00 13.74  ? 133 LYS B N   1 
ATOM   3290 C  CA  . LYS B 1 132 ? -14.581 39.216  33.948  1.00 13.10  ? 133 LYS B CA  1 
ATOM   3291 C  C   . LYS B 1 132 ? -15.116 38.214  34.997  1.00 12.60  ? 133 LYS B C   1 
ATOM   3292 O  O   . LYS B 1 132 ? -14.558 38.118  36.077  1.00 12.36  ? 133 LYS B O   1 
ATOM   3293 C  CB  . LYS B 1 132 ? -15.348 40.517  34.018  1.00 13.38  ? 133 LYS B CB  1 
ATOM   3294 C  CG  . LYS B 1 132 ? -14.675 41.644  33.252  1.00 19.21  ? 133 LYS B CG  1 
ATOM   3295 C  CD  . LYS B 1 132 ? -13.482 42.112  34.052  1.00 44.56  ? 133 LYS B CD  1 
ATOM   3296 C  CE  . LYS B 1 132 ? -13.012 43.506  33.778  1.00 31.85  ? 133 LYS B CE  1 
ATOM   3297 N  NZ  . LYS B 1 132 ? -11.905 43.872  34.750  1.00 39.28  ? 133 LYS B NZ  1 
ATOM   3298 N  N   . ALA B 1 133 ? -16.207 37.523  34.678  1.00 11.31  ? 134 ALA B N   1 
ATOM   3299 C  CA  . ALA B 1 133 ? -16.757 36.560  35.664  1.00 10.17  ? 134 ALA B CA  1 
ATOM   3300 C  C   . ALA B 1 133 ? -15.755 35.497  36.067  1.00 10.09  ? 134 ALA B C   1 
ATOM   3301 O  O   . ALA B 1 133 ? -15.749 35.119  37.229  1.00 10.06  ? 134 ALA B O   1 
ATOM   3302 C  CB  . ALA B 1 133 ? -18.010 35.936  35.078  1.00 10.00  ? 134 ALA B CB  1 
ATOM   3303 N  N   . VAL B 1 134 ? -14.948 34.984  35.135  1.00 10.78  ? 135 VAL B N   1 
ATOM   3304 C  CA  . VAL B 1 134 ? -14.050 33.873  35.489  1.00 11.59  ? 135 VAL B CA  1 
ATOM   3305 C  C   . VAL B 1 134 ? -12.945 34.313  36.421  1.00 11.57  ? 135 VAL B C   1 
ATOM   3306 O  O   . VAL B 1 134 ? -12.243 33.418  36.976  1.00 12.44  ? 135 VAL B O   1 
ATOM   3307 C  CB  . VAL B 1 134 ? -13.438 33.164  34.304  1.00 12.75  ? 135 VAL B CB  1 
ATOM   3308 C  CG1 . VAL B 1 134 ? -14.514 32.498  33.473  1.00 15.45  ? 135 VAL B CG1 1 
ATOM   3309 C  CG2 . VAL B 1 134 ? -12.538 34.062  33.441  1.00 13.93  ? 135 VAL B CG2 1 
ATOM   3310 N  N   . GLN B 1 135 ? -12.802 35.628  36.612  1.00 11.76  ? 136 GLN B N   1 
ATOM   3311 C  CA  . GLN B 1 135 ? -11.818 36.122  37.567  1.00 13.39  ? 136 GLN B CA  1 
ATOM   3312 C  C   . GLN B 1 135 ? -12.360 36.251  38.962  1.00 11.84  ? 136 GLN B C   1 
ATOM   3313 O  O   . GLN B 1 135 ? -11.698 36.818  39.873  1.00 14.50  ? 136 GLN B O   1 
ATOM   3314 C  CB  . GLN B 1 135 ? -11.251 37.460  37.048  1.00 14.61  ? 136 GLN B CB  1 
ATOM   3315 C  CG  . GLN B 1 135 ? -10.618 37.367  35.688  1.00 18.23  ? 136 GLN B CG  1 
ATOM   3316 C  CD  . GLN B 1 135 ? -10.182 38.713  35.182  1.00 21.51  ? 136 GLN B CD  1 
ATOM   3317 O  OE1 . GLN B 1 135 ? -10.692 39.182  34.155  1.00 29.55  ? 136 GLN B OE1 1 
ATOM   3318 N  NE2 . GLN B 1 135 ? -9.306  39.395  35.931  1.00 25.09  ? 136 GLN B NE2 1 
ATOM   3319 N  N   . GLN B 1 136 ? -13.572 35.774  39.179  1.00 10.81  ? 137 GLN B N   1 
ATOM   3320 C  CA  . GLN B 1 136 ? -14.252 35.934  40.482  1.00 10.65  ? 137 GLN B CA  1 
ATOM   3321 C  C   . GLN B 1 136 ? -14.599 34.600  41.073  1.00 10.26  ? 137 GLN B C   1 
ATOM   3322 O  O   . GLN B 1 136 ? -14.986 33.689  40.367  1.00 9.79   ? 137 GLN B O   1 
ATOM   3323 C  CB  . GLN B 1 136 ? -15.553 36.761  40.340  1.00 11.56  ? 137 GLN B CB  1 
ATOM   3324 C  CG  . GLN B 1 136 ? -15.466 37.953  39.443  1.00 14.83  ? 137 GLN B CG  1 
ATOM   3325 C  CD  . GLN B 1 136 ? -14.484 38.892  39.871  1.00 16.31  ? 137 GLN B CD  1 
ATOM   3326 O  OE1 . GLN B 1 136 ? -14.200 39.063  41.111  1.00 16.53  ? 137 GLN B OE1 1 
ATOM   3327 N  NE2 . GLN B 1 136 ? -13.915 39.569  38.822  1.00 19.83  ? 137 GLN B NE2 1 
ATOM   3328 N  N   . PRO B 1 137 ? -14.638 34.499  42.439  1.00 10.38  ? 138 PRO B N   1 
ATOM   3329 C  CA  . PRO B 1 137 ? -14.873 33.164  43.052  1.00 10.47  ? 138 PRO B CA  1 
ATOM   3330 C  C   . PRO B 1 137 ? -16.305 32.675  42.880  1.00 10.50  ? 138 PRO B C   1 
ATOM   3331 O  O   . PRO B 1 137 ? -16.541 31.491  42.988  1.00 13.98  ? 138 PRO B O   1 
ATOM   3332 C  CB  . PRO B 1 137 ? -14.582 33.333  44.494  1.00 13.24  ? 138 PRO B CB  1 
ATOM   3333 C  CG  . PRO B 1 137 ? -14.419 34.750  44.673  1.00 22.57  ? 138 PRO B CG  1 
ATOM   3334 C  CD  . PRO B 1 137 ? -14.133 35.479  43.409  1.00 14.18  ? 138 PRO B CD  1 
ATOM   3335 N  N   . ASP B 1 138 ? -17.222 33.603  42.601  1.00 10.19  ? 139 ASP B N   1 
ATOM   3336 C  CA  . ASP B 1 138 ? -18.630 33.280  42.301  1.00 9.80   ? 139 ASP B CA  1 
ATOM   3337 C  C   . ASP B 1 138 ? -18.985 33.693  40.892  1.00 8.60   ? 139 ASP B C   1 
ATOM   3338 O  O   . ASP B 1 138 ? -20.127 34.115  40.613  1.00 9.62   ? 139 ASP B O   1 
ATOM   3339 C  CB  . ASP B 1 138 ? -19.596 33.901  43.319  1.00 12.09  ? 139 ASP B CB  1 
ATOM   3340 C  CG  . ASP B 1 138 ? -19.510 35.382  43.359  1.00 12.51  ? 139 ASP B CG  1 
ATOM   3341 O  OD1 . ASP B 1 138 ? -18.575 35.999  42.772  1.00 12.19  ? 139 ASP B OD1 1 
ATOM   3342 O  OD2 . ASP B 1 138 ? -20.363 35.987  44.072  1.00 15.13  ? 139 ASP B OD2 1 
ATOM   3343 N  N   . GLY B 1 139 ? -18.017 33.587  39.963  1.00 8.25   ? 140 GLY B N   1 
ATOM   3344 C  CA  . GLY B 1 139 ? -18.307 34.052  38.629  1.00 8.60   ? 140 GLY B CA  1 
ATOM   3345 C  C   . GLY B 1 139 ? -19.127 33.149  37.742  1.00 7.66   ? 140 GLY B C   1 
ATOM   3346 O  O   . GLY B 1 139 ? -19.836 33.650  36.855  1.00 8.02   ? 140 GLY B O   1 
ATOM   3347 N  N   . LEU B 1 140 ? -19.007 31.834  37.911  1.00 7.14   ? 141 LEU B N   1 
ATOM   3348 C  CA  . LEU B 1 140 ? -19.679 30.876  37.038  1.00 7.49   ? 141 LEU B CA  1 
ATOM   3349 C  C   . LEU B 1 140 ? -20.534 29.942  37.856  1.00 6.67   ? 141 LEU B C   1 
ATOM   3350 O  O   . LEU B 1 140 ? -20.259 29.640  39.028  1.00 7.19   ? 141 LEU B O   1 
ATOM   3351 C  CB  . LEU B 1 140 ? -18.728 30.007  36.242  1.00 8.02   ? 141 LEU B CB  1 
ATOM   3352 C  CG  . LEU B 1 140 ? -17.829 30.680  35.214  1.00 9.17   ? 141 LEU B CG  1 
ATOM   3353 C  CD1 . LEU B 1 140 ? -17.043 29.630  34.451  1.00 9.39   ? 141 LEU B CD1 1 
ATOM   3354 C  CD2 . LEU B 1 140 ? -18.434 31.716  34.343  1.00 11.00  ? 141 LEU B CD2 1 
ATOM   3355 N  N   . ALA B 1 141 ? -21.589 29.433  37.208  1.00 6.93   ? 142 ALA B N   1 
ATOM   3356 C  CA  . ALA B 1 141 ? -22.407 28.311  37.745  1.00 7.46   ? 142 ALA B CA  1 
ATOM   3357 C  C   . ALA B 1 141 ? -22.441 27.308  36.615  1.00 7.12   ? 142 ALA B C   1 
ATOM   3358 O  O   . ALA B 1 141 ? -22.859 27.658  35.478  1.00 8.06   ? 142 ALA B O   1 
ATOM   3359 C  CB  . ALA B 1 141 ? -23.798 28.768  38.155  1.00 8.40   ? 142 ALA B CB  1 
ATOM   3360 N  N   . VAL B 1 142 ? -21.953 26.098  36.867  1.00 6.72   ? 143 VAL B N   1 
ATOM   3361 C  CA  . VAL B 1 142 ? -21.967 25.044  35.868  1.00 7.00   ? 143 VAL B CA  1 
ATOM   3362 C  C   . VAL B 1 142 ? -22.907 23.989  36.368  1.00 6.71   ? 143 VAL B C   1 
ATOM   3363 O  O   . VAL B 1 142 ? -22.798 23.451  37.449  1.00 7.05   ? 143 VAL B O   1 
ATOM   3364 C  CB  . VAL B 1 142 ? -20.597 24.495  35.531  1.00 7.41   ? 143 VAL B CB  1 
ATOM   3365 C  CG1 . VAL B 1 142 ? -20.736 23.441  34.402  1.00 8.27   ? 143 VAL B CG1 1 
ATOM   3366 C  CG2 . VAL B 1 142 ? -19.643 25.599  35.081  1.00 8.56   ? 143 VAL B CG2 1 
ATOM   3367 N  N   . LEU B 1 143 ? -23.932 23.701  35.503  1.00 6.83   ? 144 LEU B N   1 
ATOM   3368 C  CA  . LEU B 1 143 ? -24.895 22.639  35.743  1.00 7.14   ? 144 LEU B CA  1 
ATOM   3369 C  C   . LEU B 1 143 ? -24.357 21.406  35.047  1.00 6.82   ? 144 LEU B C   1 
ATOM   3370 O  O   . LEU B 1 143 ? -24.209 21.359  33.822  1.00 7.73   ? 144 LEU B O   1 
ATOM   3371 C  CB  . LEU B 1 143 ? -26.248 23.085  35.158  1.00 8.55   ? 144 LEU B CB  1 
ATOM   3372 C  CG  . LEU B 1 143 ? -27.401 22.119  35.328  1.00 9.58   ? 144 LEU B CG  1 
ATOM   3373 C  CD1 . LEU B 1 143 ? -27.627 21.784  36.782  1.00 11.68  ? 144 LEU B CD1 1 
ATOM   3374 C  CD2 . LEU B 1 143 ? -28.670 22.692  34.653  1.00 11.60  ? 144 LEU B CD2 1 
ATOM   3375 N  N   . GLY B 1 144 ? -24.079 20.375  35.851  1.00 6.54   ? 145 GLY B N   1 
ATOM   3376 C  CA  . GLY B 1 144 ? -23.553 19.133  35.339  1.00 6.95   ? 145 GLY B CA  1 
ATOM   3377 C  C   . GLY B 1 144 ? -24.613 18.034  35.379  1.00 6.69   ? 145 GLY B C   1 
ATOM   3378 O  O   . GLY B 1 144 ? -25.326 17.894  36.366  1.00 7.61   ? 145 GLY B O   1 
ATOM   3379 N  N   . ILE B 1 145 ? -24.670 17.299  34.284  1.00 6.73   ? 146 ILE B N   1 
ATOM   3380 C  CA  . ILE B 1 145 ? -25.694 16.251  34.090  1.00 6.89   ? 146 ILE B CA  1 
ATOM   3381 C  C   . ILE B 1 145 ? -24.981 15.010  33.581  1.00 6.86   ? 146 ILE B C   1 
ATOM   3382 O  O   . ILE B 1 145 ? -24.294 15.055  32.561  1.00 7.71   ? 146 ILE B O   1 
ATOM   3383 C  CB  . ILE B 1 145 ? -26.800 16.733  33.121  1.00 8.17   ? 146 ILE B CB  1 
ATOM   3384 C  CG1 . ILE B 1 145 ? -27.390 18.022  33.640  1.00 10.04  ? 146 ILE B CG1 1 
ATOM   3385 C  CG2 . ILE B 1 145 ? -27.825 15.624  32.888  1.00 9.71   ? 146 ILE B CG2 1 
ATOM   3386 C  CD1 . ILE B 1 145 ? -28.489 18.634  32.758  1.00 10.00  ? 146 ILE B CD1 1 
ATOM   3387 N  N   . PHE B 1 146 ? -25.165 13.905  34.278  1.00 6.75   ? 147 PHE B N   1 
ATOM   3388 C  CA  . PHE B 1 146 ? -24.535 12.648  33.854  1.00 7.03   ? 147 PHE B CA  1 
ATOM   3389 C  C   . PHE B 1 146 ? -25.309 12.035  32.677  1.00 7.21   ? 147 PHE B C   1 
ATOM   3390 O  O   . PHE B 1 146 ? -26.550 12.145  32.629  1.00 8.38   ? 147 PHE B O   1 
ATOM   3391 C  CB  . PHE B 1 146 ? -24.543 11.660  35.022  1.00 7.50   ? 147 PHE B CB  1 
ATOM   3392 C  CG  . PHE B 1 146 ? -23.672 12.129  36.182  1.00 6.74   ? 147 PHE B CG  1 
ATOM   3393 C  CD1 . PHE B 1 146 ? -22.314 12.320  35.990  1.00 7.38   ? 147 PHE B CD1 1 
ATOM   3394 C  CD2 . PHE B 1 146 ? -24.205 12.385  37.422  1.00 7.95   ? 147 PHE B CD2 1 
ATOM   3395 C  CE1 . PHE B 1 146 ? -21.501 12.712  37.064  1.00 7.95   ? 147 PHE B CE1 1 
ATOM   3396 C  CE2 . PHE B 1 146 ? -23.409 12.761  38.472  1.00 7.84   ? 147 PHE B CE2 1 
ATOM   3397 C  CZ  . PHE B 1 146 ? -22.079 12.918  38.311  1.00 7.41   ? 147 PHE B CZ  1 
ATOM   3398 N  N   . LEU B 1 147 ? -24.586 11.303  31.846  1.00 7.69   ? 148 LEU B N   1 
ATOM   3399 C  CA  . LEU B 1 147 ? -25.159 10.506  30.744  1.00 8.14   ? 148 LEU B CA  1 
ATOM   3400 C  C   . LEU B 1 147 ? -24.832 9.044   30.980  1.00 8.08   ? 148 LEU B C   1 
ATOM   3401 O  O   . LEU B 1 147 ? -23.662 8.697   31.188  1.00 8.59   ? 148 LEU B O   1 
ATOM   3402 C  CB  . LEU B 1 147 ? -24.580 10.909  29.404  1.00 8.96   ? 148 LEU B CB  1 
ATOM   3403 C  CG  . LEU B 1 147 ? -25.136 12.160  28.715  1.00 9.20   ? 148 LEU B CG  1 
ATOM   3404 C  CD1 . LEU B 1 147 ? -24.913 13.417  29.560  1.00 10.39  ? 148 LEU B CD1 1 
ATOM   3405 C  CD2 . LEU B 1 147 ? -24.531 12.363  27.347  1.00 10.23  ? 148 LEU B CD2 1 
ATOM   3406 N  N   . LYS B 1 148 ? -25.862 8.211   30.905  1.00 8.84   ? 149 LYS B N   1 
ATOM   3407 C  CA  . LYS B 1 148 ? -25.705 6.768   30.874  1.00 9.70   ? 149 LYS B CA  1 
ATOM   3408 C  C   . LYS B 1 148 ? -26.182 6.258   29.523  1.00 9.78   ? 149 LYS B C   1 
ATOM   3409 O  O   . LYS B 1 148 ? -27.016 6.914   28.888  1.00 11.13  ? 149 LYS B O   1 
ATOM   3410 C  CB  . LYS B 1 148 ? -26.437 6.088   32.015  1.00 10.41  ? 149 LYS B CB  1 
ATOM   3411 C  CG  . LYS B 1 148 ? -27.937 6.188   31.961  1.00 11.79  ? 149 LYS B CG  1 
ATOM   3412 C  CD  . LYS B 1 148 ? -28.562 5.519   33.159  1.00 17.83  ? 149 LYS B CD  1 
ATOM   3413 C  CE  . LYS B 1 148 ? -30.069 5.484   33.125  1.00 24.55  ? 149 LYS B CE  1 
ATOM   3414 N  NZ  . LYS B 1 148 ? -30.588 4.613   34.220  1.00 45.94  ? 149 LYS B NZ  1 
ATOM   3415 N  N   . VAL B 1 149 ? -25.708 5.094   29.132  1.00 10.79  ? 150 VAL B N   1 
ATOM   3416 C  CA  . VAL B 1 149 ? -26.092 4.504   27.828  1.00 10.85  ? 150 VAL B CA  1 
ATOM   3417 C  C   . VAL B 1 149 ? -27.299 3.599   28.013  1.00 10.64  ? 150 VAL B C   1 
ATOM   3418 O  O   . VAL B 1 149 ? -27.239 2.637   28.786  1.00 12.11  ? 150 VAL B O   1 
ATOM   3419 C  CB  . VAL B 1 149 ? -24.871 3.768   27.232  1.00 11.16  ? 150 VAL B CB  1 
ATOM   3420 C  CG1 . VAL B 1 149 ? -25.278 2.996   25.975  1.00 11.92  ? 150 VAL B CG1 1 
ATOM   3421 C  CG2 . VAL B 1 149 ? -23.779 4.753   26.918  1.00 12.75  ? 150 VAL B CG2 1 
ATOM   3422 N  N   . GLY B 1 150 ? -28.364 3.885   27.282  1.00 11.17  ? 151 GLY B N   1 
ATOM   3423 C  CA  . GLY B 1 150 ? -29.562 3.054   27.338  1.00 12.23  ? 151 GLY B CA  1 
ATOM   3424 C  C   . GLY B 1 150 ? -30.451 3.506   26.209  1.00 11.68  ? 151 GLY B C   1 
ATOM   3425 O  O   . GLY B 1 150 ? -30.073 3.406   25.029  1.00 13.46  ? 151 GLY B O   1 
ATOM   3426 N  N   . SER B 1 151 ? -31.634 4.009   26.558  1.00 13.29  ? 152 SER B N   1 
ATOM   3427 C  CA  . SER B 1 151 ? -32.512 4.592   25.564  1.00 13.89  ? 152 SER B CA  1 
ATOM   3428 C  C   . SER B 1 151 ? -31.930 5.848   24.985  1.00 11.79  ? 152 SER B C   1 
ATOM   3429 O  O   . SER B 1 151 ? -31.174 6.561   25.622  1.00 12.71  ? 152 SER B O   1 
ATOM   3430 C  CB  . SER B 1 151 ? -33.874 4.806   26.109  1.00 19.64  ? 152 SER B CB  1 
ATOM   3431 O  OG  . SER B 1 151 ? -33.887 5.795   27.075  1.00 28.65  ? 152 SER B OG  1 
ATOM   3432 N  N   . ALA B 1 152 ? -32.235 6.145   23.716  1.00 13.87  ? 153 ALA B N   1 
ATOM   3433 C  CA  . ALA B 1 152 ? -31.856 7.399   23.099  1.00 11.71  ? 153 ALA B CA  1 
ATOM   3434 C  C   . ALA B 1 152 ? -32.486 8.593   23.769  1.00 12.98  ? 153 ALA B C   1 
ATOM   3435 O  O   . ALA B 1 152 ? -33.592 8.540   24.309  1.00 14.57  ? 153 ALA B O   1 
ATOM   3436 C  CB  . ALA B 1 152 ? -32.251 7.421   21.621  1.00 16.46  ? 153 ALA B CB  1 
ATOM   3437 N  N   . LYS B 1 153 ? -31.767 9.750   23.679  1.00 13.77  ? 154 LYS B N   1 
ATOM   3438 C  CA  . LYS B 1 153 ? -32.283 11.006  24.196  1.00 13.83  ? 154 LYS B CA  1 
ATOM   3439 C  C   . LYS B 1 153 ? -32.722 11.760  22.916  1.00 12.92  ? 154 LYS B C   1 
ATOM   3440 O  O   . LYS B 1 153 ? -31.866 12.220  22.142  1.00 12.92  ? 154 LYS B O   1 
ATOM   3441 C  CB  . LYS B 1 153 ? -31.253 11.833  24.960  1.00 15.72  ? 154 LYS B CB  1 
ATOM   3442 C  CG  . LYS B 1 153 ? -31.791 13.033  25.645  1.00 17.65  ? 154 LYS B CG  1 
ATOM   3443 C  CD  . LYS B 1 153 ? -32.595 12.642  26.863  1.00 18.95  ? 154 LYS B CD  1 
ATOM   3444 C  CE  . LYS B 1 153 ? -32.590 13.849  27.827  1.00 17.98  ? 154 LYS B CE  1 
ATOM   3445 N  NZ  . LYS B 1 153 ? -33.598 13.513  28.840  1.00 19.91  ? 154 LYS B NZ  1 
ATOM   3446 N  N   . PRO B 1 154 ? -34.032 11.886  22.658  1.00 14.42  ? 155 PRO B N   1 
ATOM   3447 C  CA  . PRO B 1 154 ? -34.408 12.488  21.334  1.00 15.55  ? 155 PRO B CA  1 
ATOM   3448 C  C   . PRO B 1 154 ? -33.913 13.916  21.175  1.00 15.49  ? 155 PRO B C   1 
ATOM   3449 O  O   . PRO B 1 154 ? -33.496 14.270  20.045  1.00 17.08  ? 155 PRO B O   1 
ATOM   3450 C  CB  . PRO B 1 154 ? -35.946 12.386  21.349  1.00 16.78  ? 155 PRO B CB  1 
ATOM   3451 C  CG  . PRO B 1 154 ? -36.214 11.247  22.351  1.00 19.34  ? 155 PRO B CG  1 
ATOM   3452 C  CD  . PRO B 1 154 ? -35.207 11.359  23.409  1.00 16.00  ? 155 PRO B CD  1 
ATOM   3453 N  N   . GLY B 1 155 ? -33.825 14.659  22.283  1.00 15.22  ? 156 GLY B N   1 
ATOM   3454 C  CA  . GLY B 1 155 ? -33.452 16.019  22.219  1.00 16.73  ? 156 GLY B CA  1 
ATOM   3455 C  C   . GLY B 1 155 ? -32.002 16.245  22.017  1.00 14.88  ? 156 GLY B C   1 
ATOM   3456 O  O   . GLY B 1 155 ? -31.567 17.366  21.876  1.00 17.84  ? 156 GLY B O   1 
ATOM   3457 N  N   . LEU B 1 156 ? -31.231 15.165  22.056  1.00 14.01  ? 157 LEU B N   1 
ATOM   3458 C  CA  . LEU B 1 156 ? -29.805 15.189  21.762  1.00 12.80  ? 157 LEU B CA  1 
ATOM   3459 C  C   . LEU B 1 156 ? -29.503 14.994  20.271  1.00 13.78  ? 157 LEU B C   1 
ATOM   3460 O  O   . LEU B 1 156 ? -28.409 15.297  19.772  1.00 13.64  ? 157 LEU B O   1 
ATOM   3461 C  CB  . LEU B 1 156 ? -29.055 14.148  22.592  1.00 13.42  ? 157 LEU B CB  1 
ATOM   3462 C  CG  . LEU B 1 156 ? -27.528 14.036  22.406  1.00 13.28  ? 157 LEU B CG  1 
ATOM   3463 C  CD1 . LEU B 1 156 ? -26.763 15.344  22.761  1.00 15.83  ? 157 LEU B CD1 1 
ATOM   3464 C  CD2 . LEU B 1 156 ? -26.962 12.882  23.228  1.00 13.50  ? 157 LEU B CD2 1 
ATOM   3465 N  N   . GLN B 1 157 ? -30.463 14.414  19.519  1.00 15.12  ? 158 GLN B N   1 
ATOM   3466 C  CA  . GLN B 1 157 ? -30.128 13.956  18.137  1.00 15.56  ? 158 GLN B CA  1 
ATOM   3467 C  C   . GLN B 1 157 ? -29.774 15.092  17.227  1.00 13.71  ? 158 GLN B C   1 
ATOM   3468 O  O   . GLN B 1 157 ? -28.856 14.882  16.423  1.00 14.35  ? 158 GLN B O   1 
ATOM   3469 C  CB  . GLN B 1 157 ? -31.243 13.111  17.583  1.00 17.38  ? 158 GLN B CB  1 
ATOM   3470 C  CG  . GLN B 1 157 ? -30.848 12.404  16.276  1.00 17.65  ? 158 GLN B CG  1 
ATOM   3471 C  CD  . GLN B 1 157 ? -29.756 11.382  16.514  1.00 16.29  ? 158 GLN B CD  1 
ATOM   3472 O  OE1 . GLN B 1 157 ? -29.618 10.802  17.648  1.00 17.65  ? 158 GLN B OE1 1 
ATOM   3473 N  NE2 . GLN B 1 157 ? -28.945 11.144  15.491  1.00 19.26  ? 158 GLN B NE2 1 
ATOM   3474 N  N   . LYS B 1 158 ? -30.370 16.282  17.316  1.00 15.02  ? 159 LYS B N   1 
ATOM   3475 C  CA  . LYS B 1 158 ? -29.872 17.351  16.475  1.00 15.85  ? 159 LYS B CA  1 
ATOM   3476 C  C   . LYS B 1 158 ? -28.381 17.682  16.675  1.00 15.10  ? 159 LYS B C   1 
ATOM   3477 O  O   . LYS B 1 158 ? -27.679 18.015  15.709  1.00 16.63  ? 159 LYS B O   1 
ATOM   3478 C  CB  . LYS B 1 158 ? -30.727 18.593  16.723  1.00 18.07  ? 159 LYS B CB  1 
ATOM   3479 C  CG  . LYS B 1 158 ? -32.125 18.430  16.028  1.00 22.29  ? 159 LYS B CG  1 
ATOM   3480 C  CD  . LYS B 1 158 ? -32.984 19.681  16.207  1.00 40.44  ? 159 LYS B CD  1 
ATOM   3481 C  CE  . LYS B 1 158 ? -32.155 20.957  16.303  1.00 63.12  ? 159 LYS B CE  1 
ATOM   3482 N  NZ  . LYS B 1 158 ? -32.916 22.127  16.834  1.00 95.42  ? 159 LYS B NZ  1 
ATOM   3483 N  N   . VAL B 1 159 ? -27.909 17.582  17.920  1.00 14.56  ? 160 VAL B N   1 
ATOM   3484 C  CA  . VAL B 1 159 ? -26.465 17.748  18.159  1.00 12.81  ? 160 VAL B CA  1 
ATOM   3485 C  C   . VAL B 1 159 ? -25.658 16.631  17.487  1.00 13.65  ? 160 VAL B C   1 
ATOM   3486 O  O   . VAL B 1 159 ? -24.731 16.882  16.737  1.00 14.56  ? 160 VAL B O   1 
ATOM   3487 C  CB  . VAL B 1 159 ? -26.146 17.786  19.681  1.00 12.80  ? 160 VAL B CB  1 
ATOM   3488 C  CG1 . VAL B 1 159 ? -24.642 17.734  19.918  1.00 14.69  ? 160 VAL B CG1 1 
ATOM   3489 C  CG2 . VAL B 1 159 ? -26.837 18.975  20.300  1.00 14.14  ? 160 VAL B CG2 1 
ATOM   3490 N  N   . VAL B 1 160 ? -26.059 15.374  17.709  1.00 13.85  ? 161 VAL B N   1 
ATOM   3491 C  CA  . VAL B 1 160 ? -25.365 14.295  17.151  1.00 14.98  ? 161 VAL B CA  1 
ATOM   3492 C  C   . VAL B 1 160 ? -25.311 14.391  15.657  1.00 15.31  ? 161 VAL B C   1 
ATOM   3493 O  O   . VAL B 1 160 ? -24.287 14.100  15.068  1.00 15.74  ? 161 VAL B O   1 
ATOM   3494 C  CB  . VAL B 1 160 ? -26.135 12.903  17.514  1.00 16.68  ? 161 VAL B CB  1 
ATOM   3495 C  CG1 . VAL B 1 160 ? -25.596 11.722  16.719  1.00 18.98  ? 161 VAL B CG1 1 
ATOM   3496 C  CG2 . VAL B 1 160 ? -25.951 12.727  19.014  1.00 16.88  ? 161 VAL B CG2 1 
ATOM   3497 N  N   . ASP B 1 161 ? -26.390 14.817  15.005  1.00 15.90  ? 162 ASP B N   1 
ATOM   3498 C  CA  . ASP B 1 161 ? -26.408 14.788  13.564  1.00 19.37  ? 162 ASP B CA  1 
ATOM   3499 C  C   . ASP B 1 161 ? -25.544 15.869  12.910  1.00 19.58  ? 162 ASP B C   1 
ATOM   3500 O  O   . ASP B 1 161 ? -25.190 15.742  11.731  1.00 25.87  ? 162 ASP B O   1 
ATOM   3501 C  CB  . ASP B 1 161 ? -27.843 14.858  13.122  1.00 22.61  ? 162 ASP B CB  1 
ATOM   3502 C  CG  . ASP B 1 161 ? -28.524 13.477  13.155  1.00 19.87  ? 162 ASP B CG  1 
ATOM   3503 O  OD1 . ASP B 1 161 ? -27.787 12.419  13.108  1.00 24.83  ? 162 ASP B OD1 1 
ATOM   3504 O  OD2 . ASP B 1 161 ? -29.751 13.511  13.325  1.00 25.30  ? 162 ASP B OD2 1 
ATOM   3505 N  N   . VAL B 1 162 ? -25.181 16.927  13.633  1.00 17.30  ? 163 VAL B N   1 
ATOM   3506 C  CA  . VAL B 1 162 ? -24.426 18.007  13.069  1.00 17.22  ? 163 VAL B CA  1 
ATOM   3507 C  C   . VAL B 1 162 ? -22.912 17.655  13.226  1.00 15.94  ? 163 VAL B C   1 
ATOM   3508 O  O   . VAL B 1 162 ? -22.049 18.342  12.697  1.00 17.03  ? 163 VAL B O   1 
ATOM   3509 C  CB  . VAL B 1 162 ? -24.828 19.376  13.679  1.00 17.17  ? 163 VAL B CB  1 
ATOM   3510 C  CG1 . VAL B 1 162 ? -24.276 19.598  15.072  1.00 18.54  ? 163 VAL B CG1 1 
ATOM   3511 C  CG2 . VAL B 1 162 ? -24.389 20.552  12.820  1.00 17.44  ? 163 VAL B CG2 1 
ATOM   3512 N  N   . LEU B 1 163 ? -22.595 16.647  14.082  1.00 14.74  ? 164 LEU B N   1 
ATOM   3513 C  CA  . LEU B 1 163 ? -21.201 16.401  14.365  1.00 13.78  ? 164 LEU B CA  1 
ATOM   3514 C  C   . LEU B 1 163 ? -20.355 16.070  13.174  1.00 16.44  ? 164 LEU B C   1 
ATOM   3515 O  O   . LEU B 1 163 ? -19.148 16.357  13.125  1.00 15.54  ? 164 LEU B O   1 
ATOM   3516 C  CB  . LEU B 1 163 ? -20.897 15.373  15.464  1.00 14.30  ? 164 LEU B CB  1 
ATOM   3517 C  CG  . LEU B 1 163 ? -21.574 15.720  16.818  1.00 14.88  ? 164 LEU B CG  1 
ATOM   3518 C  CD1 . LEU B 1 163 ? -21.344 14.591  17.826  1.00 15.07  ? 164 LEU B CD1 1 
ATOM   3519 C  CD2 . LEU B 1 163 ? -21.021 17.005  17.377  1.00 15.09  ? 164 LEU B CD2 1 
ATOM   3520 N  N   . ASP B 1 164 ? -20.915 15.389  12.171  1.00 18.40  ? 165 ASP B N   1 
ATOM   3521 C  CA  . ASP B 1 164 ? -20.087 15.077  10.970  1.00 22.92  ? 165 ASP B CA  1 
ATOM   3522 C  C   . ASP B 1 164 ? -19.609 16.364  10.274  1.00 20.95  ? 165 ASP B C   1 
ATOM   3523 O  O   . ASP B 1 164 ? -18.609 16.259  9.539   1.00 24.61  ? 165 ASP B O   1 
ATOM   3524 C  CB  . ASP B 1 164 ? -20.841 14.211  9.975   1.00 43.08  ? 165 ASP B CB  1 
ATOM   3525 C  CG  . ASP B 1 164 ? -21.804 15.008  9.179   1.00 45.43  ? 165 ASP B CG  1 
ATOM   3526 O  OD1 . ASP B 1 164 ? -22.712 15.605  9.784   1.00 46.53  ? 165 ASP B OD1 1 
ATOM   3527 O  OD2 . ASP B 1 164 ? -21.654 15.061  7.943   1.00 109.01 ? 165 ASP B OD2 1 
ATOM   3528 N  N   . SER B 1 165 ? -20.270 17.511  10.522  1.00 19.01  ? 166 SER B N   1 
ATOM   3529 C  CA  . SER B 1 165 ? -19.847 18.756  9.867   1.00 18.53  ? 166 SER B CA  1 
ATOM   3530 C  C   . SER B 1 165 ? -18.757 19.509  10.625  1.00 16.85  ? 166 SER B C   1 
ATOM   3531 O  O   . SER B 1 165 ? -18.191 20.494  10.127  1.00 19.42  ? 166 SER B O   1 
ATOM   3532 C  CB  . SER B 1 165 ? -21.028 19.622  9.540   1.00 21.70  ? 166 SER B CB  1 
ATOM   3533 O  OG  . SER B 1 165 ? -21.502 20.177  10.720  1.00 22.49  ? 166 SER B OG  1 
ATOM   3534 N  N   . ILE B 1 166 ? -18.480 19.042  11.864  1.00 15.04  ? 167 ILE B N   1 
ATOM   3535 C  CA  . ILE B 1 166 ? -17.467 19.694  12.672  1.00 13.24  ? 167 ILE B CA  1 
ATOM   3536 C  C   . ILE B 1 166 ? -16.458 18.637  13.171  1.00 13.84  ? 167 ILE B C   1 
ATOM   3537 O  O   . ILE B 1 166 ? -16.023 18.621  14.321  1.00 13.72  ? 167 ILE B O   1 
ATOM   3538 C  CB  . ILE B 1 166 ? -17.992 20.542  13.858  1.00 14.48  ? 167 ILE B CB  1 
ATOM   3539 C  CG1 . ILE B 1 166 ? -18.850 19.676  14.783  1.00 14.75  ? 167 ILE B CG1 1 
ATOM   3540 C  CG2 . ILE B 1 166 ? -18.783 21.728  13.323  1.00 17.25  ? 167 ILE B CG2 1 
ATOM   3541 C  CD1 . ILE B 1 166 ? -18.842 20.207  16.195  1.00 15.57  ? 167 ILE B CD1 1 
ATOM   3542 N  N   . LYS B 1 167 ? -16.093 17.731  12.263  1.00 13.58  ? 168 LYS B N   1 
ATOM   3543 C  CA  . LYS B 1 167 ? -15.306 16.600  12.708  1.00 13.99  ? 168 LYS B CA  1 
ATOM   3544 C  C   . LYS B 1 167 ? -13.998 16.981  13.384  1.00 13.30  ? 168 LYS B C   1 
ATOM   3545 O  O   . LYS B 1 167 ? -13.505 16.306  14.339  1.00 13.24  ? 168 LYS B O   1 
ATOM   3546 C  CB  . LYS B 1 167 ? -14.970 15.642  11.498  1.00 15.37  ? 168 LYS B CB  1 
ATOM   3547 C  CG  . LYS B 1 167 ? -14.238 14.377  11.949  1.00 16.24  ? 168 LYS B CG  1 
ATOM   3548 C  CD  . LYS B 1 167 ? -14.012 13.547  10.698  1.00 22.11  ? 168 LYS B CD  1 
ATOM   3549 C  CE  . LYS B 1 167 ? -13.274 12.253  10.897  1.00 33.46  ? 168 LYS B CE  1 
ATOM   3550 N  NZ  . LYS B 1 167 ? -13.270 11.477  9.623   1.00 44.36  ? 168 LYS B NZ  1 
ATOM   3551 N  N   . THR B 1 168 ? -13.368 17.997  12.842  1.00 12.69  ? 169 THR B N   1 
ATOM   3552 C  CA  . THR B 1 168 ? -11.997 18.269  13.189  1.00 12.74  ? 169 THR B CA  1 
ATOM   3553 C  C   . THR B 1 168 ? -11.875 19.743  13.847  1.00 12.28  ? 169 THR B C   1 
ATOM   3554 O  O   . THR B 1 168 ? -12.793 20.563  13.735  1.00 13.67  ? 169 THR B O   1 
ATOM   3555 C  CB  . THR B 1 168 ? -11.056 18.221  11.954  1.00 15.30  ? 169 THR B CB  1 
ATOM   3556 O  OG1 . THR B 1 168 ? -11.657 18.992  10.909  1.00 16.04  ? 169 THR B OG1 1 
ATOM   3557 C  CG2 . THR B 1 168 ? -10.856 16.783  11.492  1.00 15.25  ? 169 THR B CG2 1 
ATOM   3558 N  N   . LYS B 1 169 ? -10.790 19.827  14.597  1.00 14.24  ? 170 LYS B N   1 
ATOM   3559 C  CA  . LYS B 1 169 ? -10.507 21.034  15.414  1.00 13.12  ? 170 LYS B CA  1 
ATOM   3560 C  C   . LYS B 1 169 ? -10.567 22.326  14.622  1.00 15.43  ? 170 LYS B C   1 
ATOM   3561 O  O   . LYS B 1 169 ? -9.991  22.402  13.482  1.00 16.97  ? 170 LYS B O   1 
ATOM   3562 C  CB  . LYS B 1 169 ? -9.115  20.859  15.933  1.00 13.16  ? 170 LYS B CB  1 
ATOM   3563 C  CG  . LYS B 1 169 ? -8.589  22.064  16.709  1.00 15.40  ? 170 LYS B CG  1 
ATOM   3564 C  CD  . LYS B 1 169 ? -7.272  21.798  17.366  1.00 18.74  ? 170 LYS B CD  1 
ATOM   3565 C  CE  . LYS B 1 169 ? -6.184  21.316  16.414  1.00 26.56  ? 170 LYS B CE  1 
ATOM   3566 N  NZ  . LYS B 1 169 ? -4.868  21.359  17.116  1.00 32.89  ? 170 LYS B NZ  1 
ATOM   3567 N  N   . GLY B 1 170 ? -11.343 23.271  15.130  1.00 15.14  ? 171 GLY B N   1 
ATOM   3568 C  CA  . GLY B 1 170 ? -11.514 24.520  14.401  1.00 16.70  ? 171 GLY B CA  1 
ATOM   3569 C  C   . GLY B 1 170 ? -12.722 24.623  13.543  1.00 15.29  ? 171 GLY B C   1 
ATOM   3570 O  O   . GLY B 1 170 ? -13.000 25.750  13.117  1.00 20.38  ? 171 GLY B O   1 
ATOM   3571 N  N   . LYS B 1 171 ? -13.408 23.522  13.275  1.00 15.58  ? 172 LYS B N   1 
ATOM   3572 C  CA  . LYS B 1 171 ? -14.568 23.580  12.405  1.00 15.49  ? 172 LYS B CA  1 
ATOM   3573 C  C   . LYS B 1 171 ? -15.783 24.053  13.251  1.00 13.76  ? 172 LYS B C   1 
ATOM   3574 O  O   . LYS B 1 171 ? -15.902 23.648  14.393  1.00 14.12  ? 172 LYS B O   1 
ATOM   3575 C  CB  . LYS B 1 171 ? -14.865 22.285  11.740  1.00 16.09  ? 172 LYS B CB  1 
ATOM   3576 C  CG  . LYS B 1 171 ? -13.831 21.819  10.757  1.00 17.78  ? 172 LYS B CG  1 
ATOM   3577 C  CD  . LYS B 1 171 ? -14.370 20.676  9.916   1.00 23.25  ? 172 LYS B CD  1 
ATOM   3578 C  CE  . LYS B 1 171 ? -14.008 20.855  8.445   1.00 31.89  ? 172 LYS B CE  1 
ATOM   3579 N  NZ  . LYS B 1 171 ? -14.897 20.057  7.561   1.00 46.77  ? 172 LYS B NZ  1 
ATOM   3580 N  N   . SER B 1 172 ? -16.655 24.878  12.699  1.00 14.99  ? 173 SER B N   1 
ATOM   3581 C  CA  . SER B 1 172 ? -17.894 25.321  13.275  1.00 16.02  ? 173 SER B CA  1 
ATOM   3582 C  C   . SER B 1 172 ? -18.998 25.150  12.291  1.00 15.65  ? 173 SER B C   1 
ATOM   3583 O  O   . SER B 1 172 ? -18.742 25.104  11.088  1.00 18.62  ? 173 SER B O   1 
ATOM   3584 C  CB  . SER B 1 172 ? -17.766 26.736  13.744  1.00 17.52  ? 173 SER B CB  1 
ATOM   3585 O  OG  . SER B 1 172 ? -17.342 27.603  12.687  1.00 23.66  ? 173 SER B OG  1 
ATOM   3586 N  N   . ALA B 1 173 ? -20.244 25.152  12.749  1.00 16.81  ? 174 ALA B N   1 
ATOM   3587 C  CA  . ALA B 1 173 ? -21.436 25.110  11.950  1.00 17.40  ? 174 ALA B CA  1 
ATOM   3588 C  C   . ALA B 1 173 ? -22.588 25.927  12.588  1.00 15.09  ? 174 ALA B C   1 
ATOM   3589 O  O   . ALA B 1 173 ? -22.649 26.005  13.819  1.00 15.11  ? 174 ALA B O   1 
ATOM   3590 C  CB  . ALA B 1 173 ? -21.861 23.687  11.695  1.00 20.60  ? 174 ALA B CB  1 
ATOM   3591 N  N   . ASP B 1 174 ? -23.423 26.585  11.771  1.00 16.30  ? 175 ASP B N   1 
ATOM   3592 C  CA  . ASP B 1 174 ? -24.587 27.304  12.342  1.00 18.06  ? 175 ASP B CA  1 
ATOM   3593 C  C   . ASP B 1 174 ? -25.396 26.264  13.075  1.00 16.92  ? 175 ASP B C   1 
ATOM   3594 O  O   . ASP B 1 174 ? -25.553 25.098  12.632  1.00 20.24  ? 175 ASP B O   1 
ATOM   3595 C  CB  . ASP B 1 174 ? -25.426 27.890  11.200  1.00 23.97  ? 175 ASP B CB  1 
ATOM   3596 C  CG  . ASP B 1 174 ? -24.688 28.925  10.416  1.00 35.42  ? 175 ASP B CG  1 
ATOM   3597 O  OD1 . ASP B 1 174 ? -23.832 29.633  10.995  1.00 74.40  ? 175 ASP B OD1 1 
ATOM   3598 O  OD2 . ASP B 1 174 ? -24.992 29.027  9.215   1.00 38.22  ? 175 ASP B OD2 1 
ATOM   3599 N  N   . PHE B 1 175 ? -25.953 26.732  14.173  1.00 15.22  ? 176 PHE B N   1 
ATOM   3600 C  CA  . PHE B 1 175 ? -26.692 25.835  15.060  1.00 16.14  ? 176 PHE B CA  1 
ATOM   3601 C  C   . PHE B 1 175 ? -27.705 26.602  15.798  1.00 15.24  ? 176 PHE B C   1 
ATOM   3602 O  O   . PHE B 1 175 ? -27.501 26.842  16.958  1.00 18.48  ? 176 PHE B O   1 
ATOM   3603 C  CB  . PHE B 1 175 ? -25.726 24.996  15.906  1.00 16.58  ? 176 PHE B CB  1 
ATOM   3604 C  CG  . PHE B 1 175 ? -26.329 23.743  16.444  1.00 16.00  ? 176 PHE B CG  1 
ATOM   3605 C  CD1 . PHE B 1 175 ? -26.630 22.710  15.633  1.00 19.86  ? 176 PHE B CD1 1 
ATOM   3606 C  CD2 . PHE B 1 175 ? -26.551 23.623  17.786  1.00 18.32  ? 176 PHE B CD2 1 
ATOM   3607 C  CE1 . PHE B 1 175 ? -27.177 21.557  16.098  1.00 21.68  ? 176 PHE B CE1 1 
ATOM   3608 C  CE2 . PHE B 1 175 ? -27.056 22.426  18.293  1.00 18.10  ? 176 PHE B CE2 1 
ATOM   3609 C  CZ  . PHE B 1 175 ? -27.405 21.396  17.440  1.00 19.20  ? 176 PHE B CZ  1 
ATOM   3610 N  N   . THR B 1 176 ? -28.691 27.053  15.118  1.00 16.69  ? 177 THR B N   1 
ATOM   3611 C  CA  . THR B 1 176 ? -29.771 27.832  15.675  1.00 13.85  ? 177 THR B CA  1 
ATOM   3612 C  C   . THR B 1 176 ? -30.923 27.012  16.104  1.00 13.76  ? 177 THR B C   1 
ATOM   3613 O  O   . THR B 1 176 ? -31.080 25.839  15.600  1.00 16.05  ? 177 THR B O   1 
ATOM   3614 C  CB  . THR B 1 176 ? -30.152 28.917  14.646  1.00 21.95  ? 177 THR B CB  1 
ATOM   3615 O  OG1 . THR B 1 176 ? -30.521 28.260  13.398  1.00 102.13 ? 177 THR B OG1 1 
ATOM   3616 C  CG2 . THR B 1 176 ? -29.019 29.921  14.406  1.00 32.31  ? 177 THR B CG2 1 
ATOM   3617 N  N   . ASN B 1 177 ? -31.748 27.573  16.972  1.00 15.87  ? 178 ASN B N   1 
ATOM   3618 C  CA  . ASN B 1 177 ? -32.985 26.998  17.397  1.00 16.35  ? 178 ASN B CA  1 
ATOM   3619 C  C   . ASN B 1 177 ? -32.838 25.683  18.162  1.00 16.79  ? 178 ASN B C   1 
ATOM   3620 O  O   . ASN B 1 177 ? -33.766 24.934  18.173  1.00 22.34  ? 178 ASN B O   1 
ATOM   3621 C  CB  . ASN B 1 177 ? -33.927 26.892  16.199  1.00 18.81  ? 178 ASN B CB  1 
ATOM   3622 C  CG  . ASN B 1 177 ? -34.182 28.271  15.609  1.00 17.79  ? 178 ASN B CG  1 
ATOM   3623 O  OD1 . ASN B 1 177 ? -34.833 29.097  16.213  1.00 20.34  ? 178 ASN B OD1 1 
ATOM   3624 N  ND2 . ASN B 1 177 ? -33.556 28.544  14.473  1.00 17.74  ? 178 ASN B ND2 1 
ATOM   3625 N  N   . PHE B 1 178 ? -31.664 25.446  18.756  1.00 15.81  ? 179 PHE B N   1 
ATOM   3626 C  CA  . PHE B 1 178 ? -31.540 24.246  19.585  1.00 15.60  ? 179 PHE B CA  1 
ATOM   3627 C  C   . PHE B 1 178 ? -32.009 24.529  20.947  1.00 14.63  ? 179 PHE B C   1 
ATOM   3628 O  O   . PHE B 1 178 ? -31.601 25.524  21.562  1.00 15.15  ? 179 PHE B O   1 
ATOM   3629 C  CB  . PHE B 1 178 ? -30.130 23.770  19.619  1.00 15.35  ? 179 PHE B CB  1 
ATOM   3630 C  CG  . PHE B 1 178 ? -29.984 22.529  20.465  1.00 13.88  ? 179 PHE B CG  1 
ATOM   3631 C  CD1 . PHE B 1 178 ? -30.357 21.277  19.930  1.00 15.01  ? 179 PHE B CD1 1 
ATOM   3632 C  CD2 . PHE B 1 178 ? -29.588 22.609  21.813  1.00 12.84  ? 179 PHE B CD2 1 
ATOM   3633 C  CE1 . PHE B 1 178 ? -30.378 20.169  20.728  1.00 16.18  ? 179 PHE B CE1 1 
ATOM   3634 C  CE2 . PHE B 1 178 ? -29.598 21.432  22.605  1.00 12.79  ? 179 PHE B CE2 1 
ATOM   3635 C  CZ  . PHE B 1 178 ? -29.972 20.216  22.060  1.00 14.32  ? 179 PHE B CZ  1 
ATOM   3636 N  N   . ASP B 1 179 ? -32.885 23.691  21.466  1.00 14.95  ? 180 ASP B N   1 
ATOM   3637 C  CA  . ASP B 1 179 ? -33.527 23.885  22.754  1.00 14.59  ? 180 ASP B CA  1 
ATOM   3638 C  C   . ASP B 1 179 ? -32.866 23.007  23.816  1.00 12.52  ? 180 ASP B C   1 
ATOM   3639 O  O   . ASP B 1 179 ? -33.096 21.810  23.854  1.00 13.54  ? 180 ASP B O   1 
ATOM   3640 C  CB  . ASP B 1 179 ? -35.010 23.528  22.649  1.00 17.70  ? 180 ASP B CB  1 
ATOM   3641 C  CG  . ASP B 1 179 ? -35.784 23.950  23.872  1.00 18.76  ? 180 ASP B CG  1 
ATOM   3642 O  OD1 . ASP B 1 179 ? -35.234 24.136  24.965  1.00 16.25  ? 180 ASP B OD1 1 
ATOM   3643 O  OD2 . ASP B 1 179 ? -36.968 24.142  23.727  1.00 26.52  ? 180 ASP B OD2 1 
ATOM   3644 N  N   . PRO B 1 180 ? -32.073 23.607  24.738  1.00 11.48  ? 181 PRO B N   1 
ATOM   3645 C  CA  . PRO B 1 180 ? -31.337 22.754  25.725  1.00 11.33  ? 181 PRO B CA  1 
ATOM   3646 C  C   . PRO B 1 180 ? -32.292 22.141  26.758  1.00 11.24  ? 181 PRO B C   1 
ATOM   3647 O  O   . PRO B 1 180 ? -31.850 21.278  27.499  1.00 11.88  ? 181 PRO B O   1 
ATOM   3648 C  CB  . PRO B 1 180 ? -30.322 23.789  26.292  1.00 13.06  ? 181 PRO B CB  1 
ATOM   3649 C  CG  . PRO B 1 180 ? -31.017 25.112  26.179  1.00 13.41  ? 181 PRO B CG  1 
ATOM   3650 C  CD  . PRO B 1 180 ? -31.693 25.022  24.793  1.00 12.84  ? 181 PRO B CD  1 
ATOM   3651 N  N   . ARG B 1 181 ? -33.566 22.539  26.781  1.00 11.77  ? 182 ARG B N   1 
ATOM   3652 C  CA  . ARG B 1 181 ? -34.508 21.880  27.757  1.00 12.32  ? 182 ARG B CA  1 
ATOM   3653 C  C   . ARG B 1 181 ? -34.593 20.395  27.407  1.00 13.10  ? 182 ARG B C   1 
ATOM   3654 O  O   . ARG B 1 181 ? -34.884 19.579  28.278  1.00 14.57  ? 182 ARG B O   1 
ATOM   3655 C  CB  . ARG B 1 181 ? -35.913 22.500  27.716  1.00 13.44  ? 182 ARG B CB  1 
ATOM   3656 C  CG  . ARG B 1 181 ? -35.839 23.964  28.187  1.00 14.65  ? 182 ARG B CG  1 
ATOM   3657 C  CD  . ARG B 1 181 ? -37.173 24.646  28.125  1.00 16.61  ? 182 ARG B CD  1 
ATOM   3658 N  NE  . ARG B 1 181 ? -37.543 24.879  26.736  1.00 18.54  ? 182 ARG B NE  1 
ATOM   3659 C  CZ  . ARG B 1 181 ? -38.608 25.577  26.373  1.00 24.01  ? 182 ARG B CZ  1 
ATOM   3660 N  NH1 . ARG B 1 181 ? -39.393 26.095  27.305  1.00 26.74  ? 182 ARG B NH1 1 
ATOM   3661 N  NH2 . ARG B 1 181 ? -38.892 25.754  25.089  1.00 24.85  ? 182 ARG B NH2 1 
ATOM   3662 N  N   . GLY B 1 182 ? -34.369 20.031  26.140  1.00 13.91  ? 183 GLY B N   1 
ATOM   3663 C  CA  . GLY B 1 182 ? -34.390 18.638  25.719  1.00 15.60  ? 183 GLY B CA  1 
ATOM   3664 C  C   . GLY B 1 182 ? -33.266 17.774  26.240  1.00 14.91  ? 183 GLY B C   1 
ATOM   3665 O  O   . GLY B 1 182 ? -33.288 16.573  25.973  1.00 17.73  ? 183 GLY B O   1 
ATOM   3666 N  N   . LEU B 1 183 ? -32.323 18.347  26.998  1.00 12.73  ? 184 LEU B N   1 
ATOM   3667 C  CA  . LEU B 1 183 ? -31.220 17.627  27.583  1.00 12.12  ? 184 LEU B CA  1 
ATOM   3668 C  C   . LEU B 1 183 ? -31.394 17.438  29.076  1.00 12.32  ? 184 LEU B C   1 
ATOM   3669 O  O   . LEU B 1 183 ? -30.450 16.888  29.708  1.00 14.03  ? 184 LEU B O   1 
ATOM   3670 C  CB  . LEU B 1 183 ? -29.909 18.338  27.265  1.00 12.16  ? 184 LEU B CB  1 
ATOM   3671 C  CG  . LEU B 1 183 ? -29.640 18.443  25.777  1.00 13.37  ? 184 LEU B CG  1 
ATOM   3672 C  CD1 . LEU B 1 183 ? -28.371 19.248  25.617  1.00 15.63  ? 184 LEU B CD1 1 
ATOM   3673 C  CD2 . LEU B 1 183 ? -29.561 17.122  25.010  1.00 16.39  ? 184 LEU B CD2 1 
ATOM   3674 N  N   . LEU B 1 184 ? -32.501 17.895  29.664  1.00 13.58  ? 185 LEU B N   1 
ATOM   3675 C  CA  . LEU B 1 184 ? -32.614 17.869  31.108  1.00 12.24  ? 185 LEU B CA  1 
ATOM   3676 C  C   . LEU B 1 184 ? -33.381 16.616  31.633  1.00 16.05  ? 185 LEU B C   1 
ATOM   3677 O  O   . LEU B 1 184 ? -34.463 16.277  31.135  1.00 18.40  ? 185 LEU B O   1 
ATOM   3678 C  CB  . LEU B 1 184 ? -33.407 19.083  31.638  1.00 12.06  ? 185 LEU B CB  1 
ATOM   3679 C  CG  . LEU B 1 184 ? -32.806 20.425  31.212  1.00 10.90  ? 185 LEU B CG  1 
ATOM   3680 C  CD1 . LEU B 1 184 ? -33.729 21.532  31.669  1.00 13.35  ? 185 LEU B CD1 1 
ATOM   3681 C  CD2 . LEU B 1 184 ? -31.430 20.621  31.771  1.00 13.21  ? 185 LEU B CD2 1 
ATOM   3682 N  N   . PRO B 1 185 ? -32.823 15.960  32.644  1.00 12.16  ? 186 PRO B N   1 
ATOM   3683 C  CA  . PRO B 1 185 ? -33.519 14.840  33.273  1.00 13.04  ? 186 PRO B CA  1 
ATOM   3684 C  C   . PRO B 1 185 ? -34.771 15.360  33.958  1.00 13.50  ? 186 PRO B C   1 
ATOM   3685 O  O   . PRO B 1 185 ? -34.943 16.571  34.093  1.00 16.40  ? 186 PRO B O   1 
ATOM   3686 C  CB  . PRO B 1 185 ? -32.516 14.361  34.316  1.00 11.72  ? 186 PRO B CB  1 
ATOM   3687 C  CG  . PRO B 1 185 ? -31.811 15.607  34.728  1.00 10.57  ? 186 PRO B CG  1 
ATOM   3688 C  CD  . PRO B 1 185 ? -31.792 16.527  33.532  1.00 9.98   ? 186 PRO B CD  1 
ATOM   3689 N  N   . GLU B 1 186 ? -35.632 14.451  34.389  1.00 10.42  ? 187 GLU B N   1 
ATOM   3690 C  CA  . GLU B 1 186 ? -36.893 14.820  35.012  1.00 11.82  ? 187 GLU B CA  1 
ATOM   3691 C  C   . GLU B 1 186 ? -36.726 15.689  36.240  1.00 11.59  ? 187 GLU B C   1 
ATOM   3692 O  O   . GLU B 1 186 ? -37.275 16.786  36.332  1.00 12.80  ? 187 GLU B O   1 
ATOM   3693 C  CB  . GLU B 1 186 ? -37.654 13.550  35.406  1.00 12.35  ? 187 GLU B CB  1 
ATOM   3694 C  CG  . GLU B 1 186 ? -38.723 13.088  34.428  1.00 16.64  ? 187 GLU B CG  1 
ATOM   3695 C  CD  . GLU B 1 186 ? -39.456 11.856  34.929  1.00 16.82  ? 187 GLU B CD  1 
ATOM   3696 O  OE1 . GLU B 1 186 ? -39.502 11.656  36.161  1.00 19.39  ? 187 GLU B OE1 1 
ATOM   3697 O  OE2 . GLU B 1 186 ? -39.981 11.086  34.096  1.00 24.53  ? 187 GLU B OE2 1 
ATOM   3698 N  N   . SER B 1 187 ? -35.972 15.158  37.189  1.00 13.04  ? 188 SER B N   1 
ATOM   3699 C  CA  . SER B 1 187 ? -35.737 15.773  38.438  1.00 14.19  ? 188 SER B CA  1 
ATOM   3700 C  C   . SER B 1 187 ? -34.626 16.791  38.432  1.00 12.59  ? 188 SER B C   1 
ATOM   3701 O  O   . SER B 1 187 ? -33.578 16.529  37.806  1.00 13.98  ? 188 SER B O   1 
ATOM   3702 C  CB  . SER B 1 187 ? -35.353 14.686  39.424  1.00 15.53  ? 188 SER B CB  1 
ATOM   3703 O  OG  . SER B 1 187 ? -35.055 15.236  40.724  1.00 15.38  ? 188 SER B OG  1 
ATOM   3704 N  N   . LEU B 1 188 ? -34.809 17.877  39.165  1.00 11.99  ? 189 LEU B N   1 
ATOM   3705 C  CA  . LEU B 1 188 ? -33.722 18.834  39.376  1.00 12.63  ? 189 LEU B CA  1 
ATOM   3706 C  C   . LEU B 1 188 ? -33.084 18.694  40.735  1.00 12.02  ? 189 LEU B C   1 
ATOM   3707 O  O   . LEU B 1 188 ? -32.392 19.644  41.187  1.00 13.38  ? 189 LEU B O   1 
ATOM   3708 C  CB  . LEU B 1 188 ? -34.165 20.256  39.061  1.00 15.21  ? 189 LEU B CB  1 
ATOM   3709 C  CG  . LEU B 1 188 ? -34.646 20.577  37.653  1.00 16.82  ? 189 LEU B CG  1 
ATOM   3710 C  CD1 . LEU B 1 188 ? -35.102 22.011  37.596  1.00 19.13  ? 189 LEU B CD1 1 
ATOM   3711 C  CD2 . LEU B 1 188 ? -33.543 20.310  36.624  1.00 19.70  ? 189 LEU B CD2 1 
ATOM   3712 N  N   . ASP B 1 189 ? -33.223 17.571  41.415  1.00 11.19  ? 190 ASP B N   1 
ATOM   3713 C  CA  . ASP B 1 189 ? -32.449 17.328  42.675  1.00 11.80  ? 190 ASP B CA  1 
ATOM   3714 C  C   . ASP B 1 189 ? -30.966 17.356  42.352  1.00 9.77   ? 190 ASP B C   1 
ATOM   3715 O  O   . ASP B 1 189 ? -30.509 16.849  41.306  1.00 9.63   ? 190 ASP B O   1 
ATOM   3716 C  CB  . ASP B 1 189 ? -32.816 15.954  43.246  1.00 14.15  ? 190 ASP B CB  1 
ATOM   3717 C  CG  . ASP B 1 189 ? -34.193 15.880  43.897  1.00 18.03  ? 190 ASP B CG  1 
ATOM   3718 O  OD1 . ASP B 1 189 ? -34.861 16.919  44.108  1.00 28.29  ? 190 ASP B OD1 1 
ATOM   3719 O  OD2 . ASP B 1 189 ? -34.555 14.714  44.200  1.00 27.50  ? 190 ASP B OD2 1 
ATOM   3720 N  N   . TYR B 1 190 ? -30.185 17.967  43.254  1.00 9.36   ? 191 TYR B N   1 
ATOM   3721 C  CA  . TYR B 1 190 ? -28.779 18.221  42.934  1.00 8.86   ? 191 TYR B CA  1 
ATOM   3722 C  C   . TYR B 1 190 ? -27.885 18.138  44.165  1.00 8.06   ? 191 TYR B C   1 
ATOM   3723 O  O   . TYR B 1 190 ? -28.329 18.282  45.327  1.00 9.20   ? 191 TYR B O   1 
ATOM   3724 C  CB  . TYR B 1 190 ? -28.629 19.612  42.270  1.00 9.40   ? 191 TYR B CB  1 
ATOM   3725 C  CG  . TYR B 1 190 ? -29.033 20.762  43.118  1.00 9.13   ? 191 TYR B CG  1 
ATOM   3726 C  CD1 . TYR B 1 190 ? -28.093 21.355  43.985  1.00 9.90   ? 191 TYR B CD1 1 
ATOM   3727 C  CD2 . TYR B 1 190 ? -30.312 21.287  43.069  1.00 10.37  ? 191 TYR B CD2 1 
ATOM   3728 C  CE1 . TYR B 1 190 ? -28.473 22.428  44.812  1.00 10.46  ? 191 TYR B CE1 1 
ATOM   3729 C  CE2 . TYR B 1 190 ? -30.695 22.341  43.896  1.00 11.33  ? 191 TYR B CE2 1 
ATOM   3730 C  CZ  . TYR B 1 190 ? -29.783 22.913  44.762  1.00 10.79  ? 191 TYR B CZ  1 
ATOM   3731 O  OH  . TYR B 1 190 ? -30.136 23.920  45.611  1.00 12.36  ? 191 TYR B OH  1 
ATOM   3732 N  N   . TRP B 1 191 ? -26.604 18.008  43.861  1.00 7.71   ? 192 TRP B N   1 
ATOM   3733 C  CA  . TRP B 1 191 ? -25.501 18.269  44.815  1.00 7.96   ? 192 TRP B CA  1 
ATOM   3734 C  C   . TRP B 1 191 ? -24.803 19.559  44.371  1.00 7.25   ? 192 TRP B C   1 
ATOM   3735 O  O   . TRP B 1 191 ? -24.756 19.911  43.195  1.00 8.60   ? 192 TRP B O   1 
ATOM   3736 C  CB  . TRP B 1 191 ? -24.464 17.156  44.789  1.00 8.46   ? 192 TRP B CB  1 
ATOM   3737 C  CG  . TRP B 1 191 ? -24.972 15.813  45.186  1.00 8.35   ? 192 TRP B CG  1 
ATOM   3738 C  CD1 . TRP B 1 191 ? -25.239 15.363  46.488  1.00 9.95   ? 192 TRP B CD1 1 
ATOM   3739 C  CD2 . TRP B 1 191 ? -25.232 14.690  44.332  1.00 8.60   ? 192 TRP B CD2 1 
ATOM   3740 N  NE1 . TRP B 1 191 ? -25.626 14.087  46.474  1.00 10.84  ? 192 TRP B NE1 1 
ATOM   3741 C  CE2 . TRP B 1 191 ? -25.670 13.628  45.183  1.00 10.32  ? 192 TRP B CE2 1 
ATOM   3742 C  CE3 . TRP B 1 191 ? -25.141 14.484  42.935  1.00 9.31   ? 192 TRP B CE3 1 
ATOM   3743 C  CZ2 . TRP B 1 191 ? -25.976 12.370  44.666  1.00 10.98  ? 192 TRP B CZ2 1 
ATOM   3744 C  CZ3 . TRP B 1 191 ? -25.417 13.211  42.465  1.00 10.19  ? 192 TRP B CZ3 1 
ATOM   3745 C  CH2 . TRP B 1 191 ? -25.829 12.172  43.319  1.00 11.19  ? 192 TRP B CH2 1 
ATOM   3746 N  N   . THR B 1 192 ? -24.210 20.277  45.325  1.00 7.35   ? 193 THR B N   1 
ATOM   3747 C  CA  . THR B 1 192 ? -23.487 21.494  44.991  1.00 7.27   ? 193 THR B CA  1 
ATOM   3748 C  C   . THR B 1 192 ? -22.260 21.646  45.870  1.00 7.25   ? 193 THR B C   1 
ATOM   3749 O  O   . THR B 1 192 ? -22.237 21.265  47.055  1.00 8.25   ? 193 THR B O   1 
ATOM   3750 C  CB  . THR B 1 192 ? -24.437 22.719  45.120  1.00 7.98   ? 193 THR B CB  1 
ATOM   3751 O  OG1 . THR B 1 192 ? -23.749 23.906  44.739  1.00 8.02   ? 193 THR B OG1 1 
ATOM   3752 C  CG2 . THR B 1 192 ? -24.967 22.926  46.542  1.00 9.15   ? 193 THR B CG2 1 
ATOM   3753 N  N   . TYR B 1 193 ? -21.226 22.258  45.317  1.00 7.25   ? 194 TYR B N   1 
ATOM   3754 C  CA  . TYR B 1 193 ? -19.989 22.513  46.028  1.00 7.47   ? 194 TYR B CA  1 
ATOM   3755 C  C   . TYR B 1 193 ? -19.222 23.598  45.229  1.00 6.87   ? 194 TYR B C   1 
ATOM   3756 O  O   . TYR B 1 193 ? -19.428 23.788  44.036  1.00 7.46   ? 194 TYR B O   1 
ATOM   3757 C  CB  . TYR B 1 193 ? -19.147 21.257  46.216  1.00 7.79   ? 194 TYR B CB  1 
ATOM   3758 C  CG  . TYR B 1 193 ? -18.447 20.782  44.964  1.00 7.32   ? 194 TYR B CG  1 
ATOM   3759 C  CD1 . TYR B 1 193 ? -19.127 20.068  43.978  1.00 7.07   ? 194 TYR B CD1 1 
ATOM   3760 C  CD2 . TYR B 1 193 ? -17.138 21.120  44.733  1.00 7.55   ? 194 TYR B CD2 1 
ATOM   3761 C  CE1 . TYR B 1 193 ? -18.494 19.712  42.777  1.00 7.20   ? 194 TYR B CE1 1 
ATOM   3762 C  CE2 . TYR B 1 193 ? -16.488 20.794  43.550  1.00 7.57   ? 194 TYR B CE2 1 
ATOM   3763 C  CZ  . TYR B 1 193 ? -17.177 20.093  42.578  1.00 6.76   ? 194 TYR B CZ  1 
ATOM   3764 O  OH  . TYR B 1 193 ? -16.503 19.823  41.395  1.00 7.19   ? 194 TYR B OH  1 
ATOM   3765 N  N   . PRO B 1 194 ? -18.265 24.284  45.906  1.00 7.49   ? 195 PRO B N   1 
ATOM   3766 C  CA  . PRO B 1 194 ? -17.423 25.311  45.225  1.00 7.75   ? 195 PRO B CA  1 
ATOM   3767 C  C   . PRO B 1 194 ? -16.204 24.622  44.561  1.00 7.09   ? 195 PRO B C   1 
ATOM   3768 O  O   . PRO B 1 194 ? -15.484 23.872  45.214  1.00 7.88   ? 195 PRO B O   1 
ATOM   3769 C  CB  . PRO B 1 194 ? -16.952 26.214  46.365  1.00 9.01   ? 195 PRO B CB  1 
ATOM   3770 C  CG  . PRO B 1 194 ? -16.907 25.284  47.566  1.00 9.96   ? 195 PRO B CG  1 
ATOM   3771 C  CD  . PRO B 1 194 ? -18.049 24.300  47.380  1.00 9.46   ? 195 PRO B CD  1 
ATOM   3772 N  N   . GLY B 1 195 ? -15.988 24.950  43.279  1.00 6.93   ? 196 GLY B N   1 
ATOM   3773 C  CA  . GLY B 1 195 ? -14.875 24.343  42.570  1.00 7.36   ? 196 GLY B CA  1 
ATOM   3774 C  C   . GLY B 1 195 ? -14.345 25.212  41.465  1.00 6.64   ? 196 GLY B C   1 
ATOM   3775 O  O   . GLY B 1 195 ? -14.236 26.464  41.608  1.00 7.38   ? 196 GLY B O   1 
ATOM   3776 N  N   . SER B 1 196 ? -13.927 24.554  40.411  1.00 6.60   ? 197 SER B N   1 
ATOM   3777 C  CA  . SER B 1 196 ? -13.110 25.184  39.384  1.00 6.90   ? 197 SER B CA  1 
ATOM   3778 C  C   . SER B 1 196 ? -13.588 24.781  37.998  1.00 6.21   ? 197 SER B C   1 
ATOM   3779 O  O   . SER B 1 196 ? -14.318 23.818  37.812  1.00 6.85   ? 197 SER B O   1 
ATOM   3780 C  CB  . SER B 1 196 ? -11.619 24.808  39.534  1.00 7.56   ? 197 SER B CB  1 
ATOM   3781 O  OG  . SER B 1 196 ? -11.376 23.446  39.135  1.00 7.35   ? 197 SER B OG  1 
ATOM   3782 N  N   . LEU B 1 197 ? -13.040 25.460  36.963  1.00 6.84   ? 198 LEU B N   1 
ATOM   3783 C  CA  . LEU B 1 197 ? -13.020 24.904  35.628  1.00 6.94   ? 198 LEU B CA  1 
ATOM   3784 C  C   . LEU B 1 197 ? -12.299 23.592  35.674  1.00 7.29   ? 198 LEU B C   1 
ATOM   3785 O  O   . LEU B 1 197 ? -11.308 23.427  36.404  1.00 7.56   ? 198 LEU B O   1 
ATOM   3786 C  CB  . LEU B 1 197 ? -12.311 25.845  34.666  1.00 8.19   ? 198 LEU B CB  1 
ATOM   3787 C  CG  . LEU B 1 197 ? -12.732 27.267  34.584  1.00 10.49  ? 198 LEU B CG  1 
ATOM   3788 C  CD1 . LEU B 1 197 ? -11.884 28.040  33.593  1.00 14.56  ? 198 LEU B CD1 1 
ATOM   3789 C  CD2 . LEU B 1 197 ? -14.102 27.339  34.143  1.00 12.90  ? 198 LEU B CD2 1 
ATOM   3790 N  N   . THR B 1 198 ? -12.723 22.631  34.839  1.00 7.56   ? 199 THR B N   1 
ATOM   3791 C  CA  . THR B 1 198 ? -12.045 21.331  34.767  1.00 7.88   ? 199 THR B CA  1 
ATOM   3792 C  C   . THR B 1 198 ? -11.011 21.236  33.655  1.00 8.10   ? 199 THR B C   1 
ATOM   3793 O  O   . THR B 1 198 ? -10.419 20.166  33.468  1.00 9.19   ? 199 THR B O   1 
ATOM   3794 C  CB  . THR B 1 198 ? -13.036 20.173  34.688  1.00 7.04   ? 199 THR B CB  1 
ATOM   3795 O  OG1 . THR B 1 198 ? -13.659 20.292  33.417  1.00 7.57   ? 199 THR B OG1 1 
ATOM   3796 C  CG2 . THR B 1 198 ? -14.038 20.152  35.818  1.00 8.12   ? 199 THR B CG2 1 
ATOM   3797 N  N   . THR B 1 199 ? -10.807 22.336  32.896  1.00 9.84   ? 200 THR B N   1 
ATOM   3798 C  CA  . THR B 1 199 ? -9.824  22.436  31.879  1.00 10.16  ? 200 THR B CA  1 
ATOM   3799 C  C   . THR B 1 199 ? -8.991  23.683  32.196  1.00 9.99   ? 200 THR B C   1 
ATOM   3800 O  O   . THR B 1 199 ? -9.449  24.615  32.815  1.00 9.96   ? 200 THR B O   1 
ATOM   3801 C  CB  . THR B 1 199 ? -10.446 22.616  30.502  1.00 12.16  ? 200 THR B CB  1 
ATOM   3802 O  OG1 . THR B 1 199 ? -11.370 23.730  30.525  1.00 16.53  ? 200 THR B OG1 1 
ATOM   3803 C  CG2 . THR B 1 199 ? -11.156 21.357  30.082  1.00 15.88  ? 200 THR B CG2 1 
ATOM   3804 N  N   . PRO B 1 200 ? -7.707  23.682  31.756  1.00 10.90  ? 201 PRO B N   1 
ATOM   3805 C  CA  . PRO B 1 200 ? -6.948  24.914  31.808  1.00 10.99  ? 201 PRO B CA  1 
ATOM   3806 C  C   . PRO B 1 200 ? -7.761  26.082  31.250  1.00 11.96  ? 201 PRO B C   1 
ATOM   3807 O  O   . PRO B 1 200 ? -8.408  25.938  30.221  1.00 12.72  ? 201 PRO B O   1 
ATOM   3808 C  CB  . PRO B 1 200 ? -5.717  24.566  30.910  1.00 13.36  ? 201 PRO B CB  1 
ATOM   3809 C  CG  . PRO B 1 200 ? -5.525  23.122  31.178  1.00 12.78  ? 201 PRO B CG  1 
ATOM   3810 C  CD  . PRO B 1 200 ? -6.911  22.572  31.127  1.00 12.81  ? 201 PRO B CD  1 
ATOM   3811 N  N   . PRO B 1 201 ? -7.770  27.221  31.938  1.00 11.28  ? 202 PRO B N   1 
ATOM   3812 C  CA  . PRO B 1 201 ? -6.820  27.626  33.036  1.00 11.89  ? 202 PRO B CA  1 
ATOM   3813 C  C   . PRO B 1 201 ? -7.206  27.175  34.454  1.00 10.30  ? 202 PRO B C   1 
ATOM   3814 O  O   . PRO B 1 201 ? -6.542  27.638  35.397  1.00 10.78  ? 202 PRO B O   1 
ATOM   3815 C  CB  . PRO B 1 201 ? -6.830  29.180  32.893  1.00 14.94  ? 202 PRO B CB  1 
ATOM   3816 C  CG  . PRO B 1 201 ? -8.217  29.478  32.414  1.00 15.35  ? 202 PRO B CG  1 
ATOM   3817 C  CD  . PRO B 1 201 ? -8.503  28.390  31.404  1.00 13.22  ? 202 PRO B CD  1 
ATOM   3818 N  N   . LEU B 1 202 ? -8.216  26.343  34.601  1.00 9.49   ? 203 LEU B N   1 
ATOM   3819 C  CA  . LEU B 1 202 ? -8.484  25.692  35.922  1.00 9.17   ? 203 LEU B CA  1 
ATOM   3820 C  C   . LEU B 1 202 ? -8.861  26.695  36.974  1.00 8.61   ? 203 LEU B C   1 
ATOM   3821 O  O   . LEU B 1 202 ? -8.697  26.453  38.188  1.00 8.99   ? 203 LEU B O   1 
ATOM   3822 C  CB  . LEU B 1 202 ? -7.320  24.793  36.368  1.00 9.20   ? 203 LEU B CB  1 
ATOM   3823 C  CG  . LEU B 1 202 ? -6.997  23.654  35.398  1.00 9.16   ? 203 LEU B CG  1 
ATOM   3824 C  CD1 . LEU B 1 202 ? -5.694  22.989  35.849  1.00 11.25  ? 203 LEU B CD1 1 
ATOM   3825 C  CD2 . LEU B 1 202 ? -8.090  22.623  35.355  1.00 9.94   ? 203 LEU B CD2 1 
ATOM   3826 N  N   . LEU B 1 203 ? -9.470  27.838  36.572  1.00 8.84   ? 204 LEU B N   1 
ATOM   3827 C  CA  . LEU B 1 203 ? -9.746  28.928  37.508  1.00 9.36   ? 204 LEU B CA  1 
ATOM   3828 C  C   . LEU B 1 203 ? -10.806 28.503  38.515  1.00 8.24   ? 204 LEU B C   1 
ATOM   3829 O  O   . LEU B 1 203 ? -11.753 27.788  38.213  1.00 8.41   ? 204 LEU B O   1 
ATOM   3830 C  CB  . LEU B 1 203 ? -10.234 30.142  36.707  1.00 10.14  ? 204 LEU B CB  1 
ATOM   3831 C  CG  . LEU B 1 203 ? -9.191  30.753  35.777  1.00 12.83  ? 204 LEU B CG  1 
ATOM   3832 C  CD1 . LEU B 1 203 ? -9.810  31.808  34.896  1.00 15.03  ? 204 LEU B CD1 1 
ATOM   3833 C  CD2 . LEU B 1 203 ? -8.048  31.366  36.625  1.00 17.66  ? 204 LEU B CD2 1 
ATOM   3834 N  N   . GLU B 1 204 ? -10.639 28.986  39.747  1.00 8.83   ? 205 GLU B N   1 
ATOM   3835 C  CA  . GLU B 1 204 ? -11.427 28.620  40.873  1.00 9.10   ? 205 GLU B CA  1 
ATOM   3836 C  C   . GLU B 1 204 ? -12.612 29.581  41.029  1.00 8.57   ? 205 GLU B C   1 
ATOM   3837 O  O   . GLU B 1 204 ? -12.728 30.355  41.980  1.00 11.43  ? 205 GLU B O   1 
ATOM   3838 C  CB  . GLU B 1 204 ? -10.600 28.449  42.178  1.00 9.86   ? 205 GLU B CB  1 
ATOM   3839 C  CG  . GLU B 1 204 ? -9.703  27.246  42.018  1.00 9.99   ? 205 GLU B CG  1 
ATOM   3840 C  CD  . GLU B 1 204 ? -8.751  26.982  43.180  1.00 11.42  ? 205 GLU B CD  1 
ATOM   3841 O  OE1 . GLU B 1 204 ? -8.440  27.925  43.948  1.00 13.99  ? 205 GLU B OE1 1 
ATOM   3842 O  OE2 . GLU B 1 204 ? -8.349  25.803  43.358  1.00 10.81  ? 205 GLU B OE2 1 
ATOM   3843 N  N   . CYS B 1 205 ? -13.521 29.488  40.055  1.00 8.08   ? 206 CYS B N   1 
ATOM   3844 C  CA  . CYS B 1 205 ? -14.571 30.469  39.833  1.00 8.32   ? 206 CYS B CA  1 
ATOM   3845 C  C   . CYS B 1 205 ? -15.944 29.845  39.734  1.00 7.54   ? 206 CYS B C   1 
ATOM   3846 O  O   . CYS B 1 205 ? -16.874 30.548  39.367  1.00 9.33   ? 206 CYS B O   1 
ATOM   3847 C  CB  . CYS B 1 205 ? -14.284 31.319  38.591  1.00 9.40   ? 206 CYS B CB  1 
ATOM   3848 S  SG  . CYS B 1 205 ? -14.235 30.336  37.068  1.00 9.62   ? 206 CYS B SG  1 
ATOM   3849 N  N   . VAL B 1 206 ? -16.089 28.553  40.014  1.00 7.24   ? 207 VAL B N   1 
ATOM   3850 C  CA  . VAL B 1 206 ? -17.318 27.846  39.661  1.00 7.11   ? 207 VAL B CA  1 
ATOM   3851 C  C   . VAL B 1 206 ? -18.103 27.401  40.902  1.00 7.01   ? 207 VAL B C   1 
ATOM   3852 O  O   . VAL B 1 206 ? -17.514 26.729  41.789  1.00 8.41   ? 207 VAL B O   1 
ATOM   3853 C  CB  . VAL B 1 206 ? -17.032 26.581  38.816  1.00 7.42   ? 207 VAL B CB  1 
ATOM   3854 C  CG1 . VAL B 1 206 ? -18.331 25.870  38.495  1.00 7.69   ? 207 VAL B CG1 1 
ATOM   3855 C  CG2 . VAL B 1 206 ? -16.284 26.938  37.535  1.00 8.31   ? 207 VAL B CG2 1 
ATOM   3856 N  N   . THR B 1 207 ? -19.398 27.714  40.949  1.00 6.55   ? 208 THR B N   1 
ATOM   3857 C  CA  . THR B 1 207 ? -20.328 26.961  41.811  1.00 7.20   ? 208 THR B CA  1 
ATOM   3858 C  C   . THR B 1 207 ? -20.870 25.815  40.978  1.00 6.61   ? 208 THR B C   1 
ATOM   3859 O  O   . THR B 1 207 ? -21.547 26.006  39.956  1.00 7.47   ? 208 THR B O   1 
ATOM   3860 C  CB  . THR B 1 207 ? -21.507 27.840  42.261  1.00 7.88   ? 208 THR B CB  1 
ATOM   3861 O  OG1 . THR B 1 207 ? -20.998 28.979  42.995  1.00 8.65   ? 208 THR B OG1 1 
ATOM   3862 C  CG2 . THR B 1 207 ? -22.428 27.064  43.142  1.00 8.85   ? 208 THR B CG2 1 
ATOM   3863 N  N   . TRP B 1 208 ? -20.505 24.595  41.392  1.00 6.47   ? 209 TRP B N   1 
ATOM   3864 C  CA  . TRP B 1 208 ? -20.987 23.401  40.689  1.00 6.54   ? 209 TRP B CA  1 
ATOM   3865 C  C   . TRP B 1 208 ? -22.324 22.993  41.226  1.00 6.37   ? 209 TRP B C   1 
ATOM   3866 O  O   . TRP B 1 208 ? -22.548 22.936  42.429  1.00 7.01   ? 209 TRP B O   1 
ATOM   3867 C  CB  . TRP B 1 208 ? -19.953 22.241  40.899  1.00 7.11   ? 209 TRP B CB  1 
ATOM   3868 C  CG  . TRP B 1 208 ? -18.820 22.350  39.938  1.00 6.42   ? 209 TRP B CG  1 
ATOM   3869 C  CD1 . TRP B 1 208 ? -17.594 22.913  40.130  1.00 7.33   ? 209 TRP B CD1 1 
ATOM   3870 C  CD2 . TRP B 1 208 ? -18.869 21.940  38.574  1.00 6.47   ? 209 TRP B CD2 1 
ATOM   3871 N  NE1 . TRP B 1 208 ? -16.874 22.890  38.964  1.00 7.65   ? 209 TRP B NE1 1 
ATOM   3872 C  CE2 . TRP B 1 208 ? -17.614 22.295  37.979  1.00 7.22   ? 209 TRP B CE2 1 
ATOM   3873 C  CE3 . TRP B 1 208 ? -19.842 21.321  37.780  1.00 6.66   ? 209 TRP B CE3 1 
ATOM   3874 C  CZ2 . TRP B 1 208 ? -17.334 22.044  36.627  1.00 7.92   ? 209 TRP B CZ2 1 
ATOM   3875 C  CZ3 . TRP B 1 208 ? -19.535 21.037  36.469  1.00 7.77   ? 209 TRP B CZ3 1 
ATOM   3876 C  CH2 . TRP B 1 208 ? -18.344 21.411  35.893  1.00 8.35   ? 209 TRP B CH2 1 
ATOM   3877 N  N   . ILE B 1 209 ? -23.208 22.624  40.275  1.00 6.43   ? 210 ILE B N   1 
ATOM   3878 C  CA  . ILE B 1 209 ? -24.547 22.093  40.590  1.00 6.64   ? 210 ILE B CA  1 
ATOM   3879 C  C   . ILE B 1 209 ? -24.640 20.838  39.727  1.00 6.34   ? 210 ILE B C   1 
ATOM   3880 O  O   . ILE B 1 209 ? -24.726 20.926  38.508  1.00 7.65   ? 210 ILE B O   1 
ATOM   3881 C  CB  . ILE B 1 209 ? -25.629 23.116  40.247  1.00 7.84   ? 210 ILE B CB  1 
ATOM   3882 C  CG1 . ILE B 1 209 ? -25.433 24.387  41.103  1.00 9.39   ? 210 ILE B CG1 1 
ATOM   3883 C  CG2 . ILE B 1 209 ? -26.999 22.518  40.457  1.00 9.35   ? 210 ILE B CG2 1 
ATOM   3884 C  CD1 . ILE B 1 209 ? -26.221 25.584  40.584  1.00 11.58  ? 210 ILE B CD1 1 
ATOM   3885 N  N   . VAL B 1 210 ? -24.574 19.678  40.384  1.00 6.48   ? 211 VAL B N   1 
ATOM   3886 C  CA  . VAL B 1 210 ? -24.573 18.390  39.672  1.00 6.69   ? 211 VAL B CA  1 
ATOM   3887 C  C   . VAL B 1 210 ? -25.864 17.681  39.947  1.00 6.52   ? 211 VAL B C   1 
ATOM   3888 O  O   . VAL B 1 210 ? -26.208 17.394  41.099  1.00 7.54   ? 211 VAL B O   1 
ATOM   3889 C  CB  . VAL B 1 210 ? -23.344 17.536  40.124  1.00 7.27   ? 211 VAL B CB  1 
ATOM   3890 C  CG1 . VAL B 1 210 ? -23.378 16.185  39.429  1.00 8.53   ? 211 VAL B CG1 1 
ATOM   3891 C  CG2 . VAL B 1 210 ? -22.057 18.285  39.844  1.00 8.24   ? 211 VAL B CG2 1 
ATOM   3892 N  N   . LEU B 1 211 ? -26.642 17.420  38.892  1.00 7.23   ? 212 LEU B N   1 
ATOM   3893 C  CA  . LEU B 1 211 ? -27.930 16.749  39.064  1.00 8.03   ? 212 LEU B CA  1 
ATOM   3894 C  C   . LEU B 1 211 ? -27.741 15.294  39.413  1.00 7.64   ? 212 LEU B C   1 
ATOM   3895 O  O   . LEU B 1 211 ? -26.896 14.575  38.905  1.00 8.05   ? 212 LEU B O   1 
ATOM   3896 C  CB  . LEU B 1 211 ? -28.763 16.873  37.798  1.00 8.66   ? 212 LEU B CB  1 
ATOM   3897 C  CG  . LEU B 1 211 ? -29.129 18.276  37.369  1.00 9.14   ? 212 LEU B CG  1 
ATOM   3898 C  CD1 . LEU B 1 211 ? -30.177 18.217  36.211  1.00 11.73  ? 212 LEU B CD1 1 
ATOM   3899 C  CD2 . LEU B 1 211 ? -29.631 19.141  38.502  1.00 9.91   ? 212 LEU B CD2 1 
ATOM   3900 N  N   . LYS B 1 212 ? -28.606 14.805  40.322  1.00 8.57   ? 213 LYS B N   1 
ATOM   3901 C  CA  . LYS B 1 212 ? -28.539 13.393  40.705  1.00 9.60   ? 213 LYS B CA  1 
ATOM   3902 C  C   . LYS B 1 212 ? -29.032 12.477  39.635  1.00 8.39   ? 213 LYS B C   1 
ATOM   3903 O  O   . LYS B 1 212 ? -28.518 11.365  39.496  1.00 10.57  ? 213 LYS B O   1 
ATOM   3904 C  CB  . LYS B 1 212 ? -29.350 13.197  42.010  1.00 11.03  ? 213 LYS B CB  1 
ATOM   3905 C  CG  . LYS B 1 212 ? -29.476 11.745  42.438  1.00 16.13  ? 213 LYS B CG  1 
ATOM   3906 C  CD  . LYS B 1 212 ? -30.218 11.524  43.720  1.00 21.87  ? 213 LYS B CD  1 
ATOM   3907 C  CE  . LYS B 1 212 ? -30.395 10.074  44.059  1.00 30.80  ? 213 LYS B CE  1 
ATOM   3908 N  NZ  . LYS B 1 212 ? -31.527 9.872   45.022  1.00 43.24  ? 213 LYS B NZ  1 
ATOM   3909 N  N   . GLU B 1 213 ? -30.054 12.851  38.869  1.00 8.41   ? 214 GLU B N   1 
ATOM   3910 C  CA  . GLU B 1 213 ? -30.665 11.961  37.895  1.00 9.50   ? 214 GLU B CA  1 
ATOM   3911 C  C   . GLU B 1 213 ? -29.917 12.066  36.596  1.00 8.74   ? 214 GLU B C   1 
ATOM   3912 O  O   . GLU B 1 213 ? -29.833 13.175  36.019  1.00 9.07   ? 214 GLU B O   1 
ATOM   3913 C  CB  . GLU B 1 213 ? -32.114 12.303  37.666  1.00 9.99   ? 214 GLU B CB  1 
ATOM   3914 C  CG  . GLU B 1 213 ? -32.769 11.373  36.683  1.00 13.55  ? 214 GLU B CG  1 
ATOM   3915 C  CD  . GLU B 1 213 ? -34.236 11.528  36.545  1.00 16.38  ? 214 GLU B CD  1 
ATOM   3916 O  OE1 . GLU B 1 213 ? -34.867 12.447  37.127  1.00 15.83  ? 214 GLU B OE1 1 
ATOM   3917 O  OE2 . GLU B 1 213 ? -34.765 10.596  35.864  1.00 27.01  ? 214 GLU B OE2 1 
ATOM   3918 N  N   A PRO B 1 214 ? -29.371 10.959  36.070  0.50 8.82   ? 215 PRO B N   1 
ATOM   3919 N  N   B PRO B 1 214 ? -29.283 10.979  36.083  0.50 9.65   ? 215 PRO B N   1 
ATOM   3920 C  CA  A PRO B 1 214 ? -28.727 11.023  34.759  0.50 8.42   ? 215 PRO B CA  1 
ATOM   3921 C  CA  B PRO B 1 214 ? -28.636 11.025  34.758  0.50 8.81   ? 215 PRO B CA  1 
ATOM   3922 C  C   A PRO B 1 214 ? -29.752 11.050  33.649  0.50 9.48   ? 215 PRO B C   1 
ATOM   3923 C  C   B PRO B 1 214 ? -29.681 11.038  33.653  0.50 9.95   ? 215 PRO B C   1 
ATOM   3924 O  O   A PRO B 1 214 ? -30.917 10.657  33.861  0.50 10.96  ? 215 PRO B O   1 
ATOM   3925 O  O   B PRO B 1 214 ? -30.822 10.648  33.874  0.50 11.47  ? 215 PRO B O   1 
ATOM   3926 C  CB  A PRO B 1 214 ? -27.958 9.689   34.692  0.50 9.49   ? 215 PRO B CB  1 
ATOM   3927 C  CB  B PRO B 1 214 ? -27.850 9.694   34.704  0.50 10.38  ? 215 PRO B CB  1 
ATOM   3928 C  CG  A PRO B 1 214 ? -28.793 8.747   35.524  0.50 9.30   ? 215 PRO B CG  1 
ATOM   3929 C  CG  B PRO B 1 214 ? -27.715 9.276   36.149  0.50 14.79  ? 215 PRO B CG  1 
ATOM   3930 C  CD  A PRO B 1 214 ? -29.336 9.595   36.649  0.50 8.70   ? 215 PRO B CD  1 
ATOM   3931 C  CD  B PRO B 1 214 ? -28.982 9.727   36.806  0.50 13.16  ? 215 PRO B CD  1 
ATOM   3932 N  N   . ILE B 1 215 ? -29.313 11.504  32.483  1.00 9.14   ? 216 ILE B N   1 
ATOM   3933 C  CA  . ILE B 1 215 ? -30.116 11.250  31.280  1.00 9.58   ? 216 ILE B CA  1 
ATOM   3934 C  C   . ILE B 1 215 ? -29.561 10.013  30.616  1.00 9.24   ? 216 ILE B C   1 
ATOM   3935 O  O   . ILE B 1 215 ? -28.381 9.661   30.735  1.00 10.58  ? 216 ILE B O   1 
ATOM   3936 C  CB  . ILE B 1 215 ? -30.127 12.482  30.368  1.00 10.65  ? 216 ILE B CB  1 
ATOM   3937 C  CG1 . ILE B 1 215 ? -28.729 12.852  29.838  1.00 11.37  ? 216 ILE B CG1 1 
ATOM   3938 C  CG2 . ILE B 1 215 ? -30.826 13.657  31.036  1.00 12.13  ? 216 ILE B CG2 1 
ATOM   3939 C  CD1 . ILE B 1 215 ? -28.736 13.832  28.641  1.00 12.62  ? 216 ILE B CD1 1 
ATOM   3940 N  N   . SER B 1 216 ? -30.456 9.342   29.856  1.00 10.74  ? 217 SER B N   1 
ATOM   3941 C  CA  . SER B 1 216 ? -30.045 8.201   29.033  1.00 10.19  ? 217 SER B CA  1 
ATOM   3942 C  C   . SER B 1 216 ? -29.851 8.661   27.624  1.00 10.27  ? 217 SER B C   1 
ATOM   3943 O  O   . SER B 1 216 ? -30.717 9.390   27.077  1.00 11.73  ? 217 SER B O   1 
ATOM   3944 C  CB  . SER B 1 216 ? -31.189 7.159   29.074  1.00 14.85  ? 217 SER B CB  1 
ATOM   3945 O  OG  . SER B 1 216 ? -31.245 6.484   30.277  1.00 17.88  ? 217 SER B OG  1 
ATOM   3946 N  N   . VAL B 1 217 ? -28.765 8.207   27.008  1.00 10.28  ? 218 VAL B N   1 
ATOM   3947 C  CA  . VAL B 1 217 ? -28.496 8.383   25.564  1.00 10.81  ? 218 VAL B CA  1 
ATOM   3948 C  C   . VAL B 1 217 ? -28.248 7.059   24.992  1.00 10.30  ? 218 VAL B C   1 
ATOM   3949 O  O   . VAL B 1 217 ? -27.897 6.091   25.692  1.00 10.54  ? 218 VAL B O   1 
ATOM   3950 C  CB  . VAL B 1 217 ? -27.299 9.339   25.359  1.00 11.18  ? 218 VAL B CB  1 
ATOM   3951 C  CG1 . VAL B 1 217 ? -27.572 10.656  26.045  1.00 12.19  ? 218 VAL B CG1 1 
ATOM   3952 C  CG2 . VAL B 1 217 ? -26.029 8.714   25.860  1.00 12.25  ? 218 VAL B CG2 1 
ATOM   3953 N  N   . SER B 1 218 ? -28.425 6.872   23.687  1.00 10.70  ? 219 SER B N   1 
ATOM   3954 C  CA  . SER B 1 218 ? -28.184 5.565   23.112  1.00 10.76  ? 219 SER B CA  1 
ATOM   3955 C  C   . SER B 1 218 ? -26.740 5.307   22.842  1.00 10.99  ? 219 SER B C   1 
ATOM   3956 O  O   . SER B 1 218 ? -25.914 6.235   22.695  1.00 11.02  ? 219 SER B O   1 
ATOM   3957 C  CB  . SER B 1 218 ? -28.990 5.364   21.828  1.00 12.47  ? 219 SER B CB  1 
ATOM   3958 O  OG  . SER B 1 218 ? -28.513 6.245   20.871  1.00 13.35  ? 219 SER B OG  1 
ATOM   3959 N  N   A SER B 1 219 ? -26.455 4.015   22.747  0.50 11.24  ? 220 SER B N   1 
ATOM   3960 N  N   B SER B 1 219 ? -26.364 4.044   22.679  0.50 11.04  ? 220 SER B N   1 
ATOM   3961 C  CA  A SER B 1 219 ? -25.140 3.626   22.378  0.50 12.95  ? 220 SER B CA  1 
ATOM   3962 C  CA  B SER B 1 219 ? -24.993 3.713   22.271  0.50 11.81  ? 220 SER B CA  1 
ATOM   3963 C  C   A SER B 1 219 ? -24.765 4.341   21.070  0.50 13.36  ? 220 SER B C   1 
ATOM   3964 C  C   B SER B 1 219 ? -24.652 4.326   20.902  0.50 11.78  ? 220 SER B C   1 
ATOM   3965 O  O   A SER B 1 219 ? -23.646 4.785   20.986  0.50 11.68  ? 220 SER B O   1 
ATOM   3966 O  O   B SER B 1 219 ? -23.511 4.749   20.601  0.50 13.76  ? 220 SER B O   1 
ATOM   3967 C  CB  A SER B 1 219 ? -25.025 2.091   22.292  0.50 15.60  ? 220 SER B CB  1 
ATOM   3968 C  CB  B SER B 1 219 ? -24.936 2.204   22.183  0.50 14.34  ? 220 SER B CB  1 
ATOM   3969 O  OG  A SER B 1 219 ? -25.911 1.570   21.303  0.50 14.43  ? 220 SER B OG  1 
ATOM   3970 O  OG  B SER B 1 219 ? -23.659 1.758   21.964  0.50 13.67  ? 220 SER B OG  1 
ATOM   3971 N  N   . GLU B 1 220 ? -25.670 4.440   20.051  1.00 12.21  ? 221 GLU B N   1 
ATOM   3972 C  CA  . GLU B 1 220 ? -25.387 5.052   18.778  1.00 14.43  ? 221 GLU B CA  1 
ATOM   3973 C  C   . GLU B 1 220 ? -25.096 6.522   18.924  1.00 13.00  ? 221 GLU B C   1 
ATOM   3974 O  O   . GLU B 1 220 ? -24.248 7.058   18.195  1.00 13.96  ? 221 GLU B O   1 
ATOM   3975 C  CB  . GLU B 1 220 ? -26.473 4.841   17.783  1.00 19.34  ? 221 GLU B CB  1 
ATOM   3976 C  CG  . GLU B 1 220 ? -26.625 3.314   17.407  1.00 21.40  ? 221 GLU B CG  1 
ATOM   3977 C  CD  . GLU B 1 220 ? -27.605 2.589   18.320  1.00 29.87  ? 221 GLU B CD  1 
ATOM   3978 O  OE1 . GLU B 1 220 ? -28.108 3.095   19.336  1.00 21.65  ? 221 GLU B OE1 1 
ATOM   3979 O  OE2 . GLU B 1 220 ? -27.887 1.413   18.017  1.00 95.84  ? 221 GLU B OE2 1 
ATOM   3980 N  N   . GLN B 1 221 ? -25.750 7.221   19.822  1.00 11.94  ? 222 GLN B N   1 
ATOM   3981 C  CA  . GLN B 1 221 ? -25.440 8.625   20.021  1.00 11.57  ? 222 GLN B CA  1 
ATOM   3982 C  C   . GLN B 1 221 ? -24.021 8.854   20.566  1.00 11.01  ? 222 GLN B C   1 
ATOM   3983 O  O   . GLN B 1 221 ? -23.304 9.704   20.048  1.00 12.22  ? 222 GLN B O   1 
ATOM   3984 C  CB  . GLN B 1 221 ? -26.511 9.205   20.968  1.00 11.17  ? 222 GLN B CB  1 
ATOM   3985 C  CG  . GLN B 1 221 ? -27.872 9.327   20.287  1.00 11.67  ? 222 GLN B CG  1 
ATOM   3986 C  CD  . GLN B 1 221 ? -28.967 9.883   21.140  1.00 11.30  ? 222 GLN B CD  1 
ATOM   3987 O  OE1 . GLN B 1 221 ? -29.110 9.500   22.321  1.00 11.79  ? 222 GLN B OE1 1 
ATOM   3988 N  NE2 . GLN B 1 221 ? -29.818 10.759  20.561  1.00 12.90  ? 222 GLN B NE2 1 
ATOM   3989 N  N   . VAL B 1 222 ? -23.650 8.095   21.614  1.00 11.76  ? 223 VAL B N   1 
ATOM   3990 C  CA  . VAL B 1 222 ? -22.335 8.298   22.161  1.00 11.54  ? 223 VAL B CA  1 
ATOM   3991 C  C   . VAL B 1 222 ? -21.246 7.816   21.198  1.00 11.97  ? 223 VAL B C   1 
ATOM   3992 O  O   . VAL B 1 222 ? -20.158 8.433   21.115  1.00 13.24  ? 223 VAL B O   1 
ATOM   3993 C  CB  . VAL B 1 222 ? -22.182 7.781   23.591  1.00 13.49  ? 223 VAL B CB  1 
ATOM   3994 C  CG1 . VAL B 1 222 ? -22.218 6.308   23.588  1.00 16.42  ? 223 VAL B CG1 1 
ATOM   3995 C  CG2 . VAL B 1 222 ? -20.956 8.340   24.310  1.00 16.18  ? 223 VAL B CG2 1 
ATOM   3996 N  N   . LEU B 1 223 ? -21.558 6.825   20.370  1.00 12.66  ? 224 LEU B N   1 
ATOM   3997 C  CA  . LEU B 1 223 ? -20.594 6.397   19.357  1.00 15.69  ? 224 LEU B CA  1 
ATOM   3998 C  C   . LEU B 1 223 ? -20.291 7.516   18.410  1.00 12.80  ? 224 LEU B C   1 
ATOM   3999 O  O   . LEU B 1 223 ? -19.134 7.636   17.941  1.00 15.01  ? 224 LEU B O   1 
ATOM   4000 C  CB  . LEU B 1 223 ? -21.045 5.134   18.650  1.00 17.13  ? 224 LEU B CB  1 
ATOM   4001 C  CG  . LEU B 1 223 ? -20.811 3.855   19.497  1.00 18.09  ? 224 LEU B CG  1 
ATOM   4002 C  CD1 . LEU B 1 223 ? -21.688 2.739   18.978  1.00 24.37  ? 224 LEU B CD1 1 
ATOM   4003 C  CD2 . LEU B 1 223 ? -19.376 3.381   19.493  1.00 21.41  ? 224 LEU B CD2 1 
ATOM   4004 N  N   . LYS B 1 224 ? -21.271 8.374   18.106  1.00 13.31  ? 225 LYS B N   1 
ATOM   4005 C  CA  . LYS B 1 224 ? -21.030 9.480   17.200  1.00 14.00  ? 225 LYS B CA  1 
ATOM   4006 C  C   . LYS B 1 224 ? -20.130 10.543  17.851  1.00 13.17  ? 225 LYS B C   1 
ATOM   4007 O  O   . LYS B 1 224 ? -19.308 11.158  17.178  1.00 13.20  ? 225 LYS B O   1 
ATOM   4008 C  CB  . LYS B 1 224 ? -22.324 10.008  16.622  1.00 16.99  ? 225 LYS B CB  1 
ATOM   4009 C  CG  . LYS B 1 224 ? -22.825 8.923   15.584  1.00 20.66  ? 225 LYS B CG  1 
ATOM   4010 C  CD  . LYS B 1 224 ? -24.167 9.187   14.929  1.00 22.03  ? 225 LYS B CD  1 
ATOM   4011 C  CE  . LYS B 1 224 ? -24.652 8.111   13.956  1.00 27.76  ? 225 LYS B CE  1 
ATOM   4012 N  NZ  . LYS B 1 224 ? -25.975 8.494   13.350  1.00 27.72  ? 225 LYS B NZ  1 
ATOM   4013 N  N   . PHE B 1 225 ? -20.228 10.753  19.161  1.00 11.71  ? 226 PHE B N   1 
ATOM   4014 C  CA  . PHE B 1 225 ? -19.339 11.666  19.852  1.00 12.02  ? 226 PHE B CA  1 
ATOM   4015 C  C   . PHE B 1 225 ? -17.906 11.152  19.645  1.00 12.13  ? 226 PHE B C   1 
ATOM   4016 O  O   . PHE B 1 225 ? -16.955 11.933  19.429  1.00 12.09  ? 226 PHE B O   1 
ATOM   4017 C  CB  . PHE B 1 225 ? -19.505 11.687  21.383  1.00 11.99  ? 226 PHE B CB  1 
ATOM   4018 C  CG  . PHE B 1 225 ? -20.693 12.450  21.913  1.00 11.24  ? 226 PHE B CG  1 
ATOM   4019 C  CD1 . PHE B 1 225 ? -21.743 12.873  21.110  1.00 15.76  ? 226 PHE B CD1 1 
ATOM   4020 C  CD2 . PHE B 1 225 ? -20.755 12.709  23.273  1.00 15.65  ? 226 PHE B CD2 1 
ATOM   4021 C  CE1 . PHE B 1 225 ? -22.817 13.557  21.670  1.00 16.21  ? 226 PHE B CE1 1 
ATOM   4022 C  CE2 . PHE B 1 225 ? -21.817 13.385  23.832  1.00 16.10  ? 226 PHE B CE2 1 
ATOM   4023 C  CZ  . PHE B 1 225 ? -22.851 13.812  23.030  1.00 14.51  ? 226 PHE B CZ  1 
ATOM   4024 N  N   . ARG B 1 226 ? -17.727 9.833   19.697  1.00 11.35  ? 227 ARG B N   1 
ATOM   4025 C  CA  . ARG B 1 226 ? -16.407 9.257   19.671  1.00 12.02  ? 227 ARG B CA  1 
ATOM   4026 C  C   . ARG B 1 226 ? -15.833 9.216   18.220  1.00 12.38  ? 227 ARG B C   1 
ATOM   4027 O  O   . ARG B 1 226 ? -14.651 8.810   18.093  1.00 13.54  ? 227 ARG B O   1 
ATOM   4028 C  CB  . ARG B 1 226 ? -16.437 7.809   20.203  1.00 12.75  ? 227 ARG B CB  1 
ATOM   4029 C  CG  . ARG B 1 226 ? -16.885 7.707   21.638  1.00 12.30  ? 227 ARG B CG  1 
ATOM   4030 C  CD  . ARG B 1 226 ? -16.791 6.265   22.125  1.00 14.16  ? 227 ARG B CD  1 
ATOM   4031 N  NE  . ARG B 1 226 ? -17.373 6.115   23.469  1.00 12.61  ? 227 ARG B NE  1 
ATOM   4032 C  CZ  . ARG B 1 226 ? -18.290 5.230   23.833  1.00 12.57  ? 227 ARG B CZ  1 
ATOM   4033 N  NH1 . ARG B 1 226 ? -18.774 4.348   22.955  1.00 16.30  ? 227 ARG B NH1 1 
ATOM   4034 N  NH2 . ARG B 1 226 ? -18.793 5.264   25.026  1.00 14.08  ? 227 ARG B NH2 1 
ATOM   4035 N  N   . LYS B 1 227 ? -16.542 9.669   17.218  1.00 12.08  ? 228 LYS B N   1 
ATOM   4036 C  CA  . LYS B 1 227 ? -16.004 9.812   15.834  1.00 13.72  ? 228 LYS B CA  1 
ATOM   4037 C  C   . LYS B 1 227 ? -15.397 11.167  15.614  1.00 12.44  ? 228 LYS B C   1 
ATOM   4038 O  O   . LYS B 1 227 ? -14.735 11.400  14.592  1.00 15.26  ? 228 LYS B O   1 
ATOM   4039 C  CB  . LYS B 1 227 ? -17.132 9.562   14.841  1.00 15.40  ? 228 LYS B CB  1 
ATOM   4040 C  CG  . LYS B 1 227 ? -17.551 8.147   14.819  1.00 16.87  ? 228 LYS B CG  1 
ATOM   4041 C  CD  . LYS B 1 227 ? -18.611 7.931   13.760  1.00 23.98  ? 228 LYS B CD  1 
ATOM   4042 C  CE  . LYS B 1 227 ? -18.019 7.393   12.462  1.00 38.89  ? 228 LYS B CE  1 
ATOM   4043 N  NZ  . LYS B 1 227 ? -18.924 7.410   11.271  1.00 56.57  ? 228 LYS B NZ  1 
ATOM   4044 N  N   . LEU B 1 228 ? -15.601 12.132  16.541  1.00 11.98  ? 229 LEU B N   1 
ATOM   4045 C  CA  . LEU B 1 228 ? -15.026 13.418  16.431  1.00 12.73  ? 229 LEU B CA  1 
ATOM   4046 C  C   . LEU B 1 228 ? -13.544 13.266  16.561  1.00 12.38  ? 229 LEU B C   1 
ATOM   4047 O  O   . LEU B 1 228 ? -12.957 12.212  16.968  1.00 12.35  ? 229 LEU B O   1 
ATOM   4048 C  CB  . LEU B 1 228 ? -15.588 14.368  17.518  1.00 11.91  ? 229 LEU B CB  1 
ATOM   4049 C  CG  . LEU B 1 228 ? -17.000 14.839  17.306  1.00 12.60  ? 229 LEU B CG  1 
ATOM   4050 C  CD1 . LEU B 1 228 ? -17.471 15.477  18.566  1.00 14.67  ? 229 LEU B CD1 1 
ATOM   4051 C  CD2 . LEU B 1 228 ? -17.010 15.842  16.161  1.00 15.05  ? 229 LEU B CD2 1 
ATOM   4052 N  N   . ASN B 1 229 ? -12.824 14.309  16.177  1.00 12.51  ? 230 ASN B N   1 
ATOM   4053 C  CA  . ASN B 1 229 ? -11.406 14.273  16.175  1.00 11.74  ? 230 ASN B CA  1 
ATOM   4054 C  C   . ASN B 1 229 ? -10.822 15.487  16.970  1.00 11.52  ? 230 ASN B C   1 
ATOM   4055 O  O   . ASN B 1 229 ? -11.249 16.591  16.910  1.00 13.35  ? 230 ASN B O   1 
ATOM   4056 C  CB  . ASN B 1 229 ? -10.747 14.491  14.765  1.00 14.29  ? 230 ASN B CB  1 
ATOM   4057 C  CG  . ASN B 1 229 ? -10.796 13.289  13.797  1.00 14.74  ? 230 ASN B CG  1 
ATOM   4058 O  OD1 . ASN B 1 229 ? -10.306 13.385  12.673  1.00 17.18  ? 230 ASN B OD1 1 
ATOM   4059 N  ND2 . ASN B 1 229 ? -11.380 12.170  14.215  1.00 15.98  ? 230 ASN B ND2 1 
ATOM   4060 N  N   . PHE B 1 230 ? -9.729  15.140  17.683  1.00 12.02  ? 231 PHE B N   1 
ATOM   4061 C  CA  . PHE B 1 230 ? -8.971  16.225  18.393  1.00 12.19  ? 231 PHE B CA  1 
ATOM   4062 C  C   . PHE B 1 230 ? -8.069  16.977  17.420  1.00 15.09  ? 231 PHE B C   1 
ATOM   4063 O  O   . PHE B 1 230 ? -7.705  18.114  17.658  1.00 16.34  ? 231 PHE B O   1 
ATOM   4064 C  CB  . PHE B 1 230 ? -7.980  15.634  19.374  1.00 12.78  ? 231 PHE B CB  1 
ATOM   4065 C  CG  . PHE B 1 230 ? -8.547  15.037  20.691  1.00 12.11  ? 231 PHE B CG  1 
ATOM   4066 C  CD1 . PHE B 1 230 ? -9.355  15.806  21.570  1.00 12.64  ? 231 PHE B CD1 1 
ATOM   4067 C  CD2 . PHE B 1 230 ? -8.152  13.820  21.129  1.00 12.34  ? 231 PHE B CD2 1 
ATOM   4068 C  CE1 . PHE B 1 230 ? -9.730  15.295  22.778  1.00 13.89  ? 231 PHE B CE1 1 
ATOM   4069 C  CE2 . PHE B 1 230 ? -8.596  13.243  22.346  1.00 13.23  ? 231 PHE B CE2 1 
ATOM   4070 C  CZ  . PHE B 1 230 ? -9.337  14.013  23.155  1.00 12.49  ? 231 PHE B CZ  1 
ATOM   4071 N  N   . ASN B 1 231 ? -7.590  16.298  16.382  1.00 14.11  ? 232 ASN B N   1 
ATOM   4072 C  CA  . ASN B 1 231 ? -6.753  16.917  15.334  1.00 15.55  ? 232 ASN B CA  1 
ATOM   4073 C  C   . ASN B 1 231 ? -7.582  17.802  14.440  1.00 12.34  ? 232 ASN B C   1 
ATOM   4074 O  O   . ASN B 1 231 ? -8.809  17.777  14.287  1.00 15.50  ? 232 ASN B O   1 
ATOM   4075 C  CB  . ASN B 1 231 ? -6.151  15.797  14.514  1.00 15.46  ? 232 ASN B CB  1 
ATOM   4076 C  CG  . ASN B 1 231 ? -7.187  14.875  13.937  1.00 15.59  ? 232 ASN B CG  1 
ATOM   4077 O  OD1 . ASN B 1 231 ? -7.747  14.039  14.656  1.00 16.40  ? 232 ASN B OD1 1 
ATOM   4078 N  ND2 . ASN B 1 231 ? -7.492  15.039  12.648  1.00 17.47  ? 232 ASN B ND2 1 
ATOM   4079 N  N   . GLY B 1 232 ? -6.803  18.678  13.747  1.00 15.69  ? 233 GLY B N   1 
ATOM   4080 C  CA  . GLY B 1 232 ? -7.338  19.445  12.608  1.00 15.96  ? 233 GLY B CA  1 
ATOM   4081 C  C   . GLY B 1 232 ? -7.369  18.695  11.306  1.00 14.79  ? 233 GLY B C   1 
ATOM   4082 O  O   . GLY B 1 232 ? -6.752  17.648  11.235  1.00 18.03  ? 233 GLY B O   1 
ATOM   4083 N  N   . GLU B 1 233 ? -8.090  19.276  10.348  1.00 15.02  ? 234 GLU B N   1 
ATOM   4084 C  CA  . GLU B 1 233 ? -8.193  18.690  9.030   1.00 15.01  ? 234 GLU B CA  1 
ATOM   4085 C  C   . GLU B 1 233 ? -6.781  18.619  8.444   1.00 16.20  ? 234 GLU B C   1 
ATOM   4086 O  O   . GLU B 1 233 ? -5.958  19.528  8.561   1.00 19.27  ? 234 GLU B O   1 
ATOM   4087 C  CB  . GLU B 1 233 ? -9.096  19.527  8.188   1.00 16.03  ? 234 GLU B CB  1 
ATOM   4088 C  CG  . GLU B 1 233 ? -9.350  18.994  6.786   1.00 20.20  ? 234 GLU B CG  1 
ATOM   4089 C  CD  . GLU B 1 233 ? -10.142 19.975  5.978   1.00 24.37  ? 234 GLU B CD  1 
ATOM   4090 O  OE1 . GLU B 1 233 ? -10.436 21.079  6.485   1.00 25.25  ? 234 GLU B OE1 1 
ATOM   4091 O  OE2 . GLU B 1 233 ? -10.460 19.652  4.815   1.00 24.51  ? 234 GLU B OE2 1 
ATOM   4092 N  N   . GLY B 1 234 ? -6.503  17.472  7.808   1.00 21.28  ? 235 GLY B N   1 
ATOM   4093 C  CA  . GLY B 1 234 ? -5.246  17.278  7.123   1.00 19.82  ? 235 GLY B CA  1 
ATOM   4094 C  C   . GLY B 1 234 ? -4.130  16.819  8.072   1.00 22.76  ? 235 GLY B C   1 
ATOM   4095 O  O   . GLY B 1 234 ? -2.928  16.734  7.701   1.00 27.32  ? 235 GLY B O   1 
ATOM   4096 N  N   . GLU B 1 235 ? -4.537  16.480  9.318   1.00 17.79  ? 236 GLU B N   1 
ATOM   4097 C  CA  . GLU B 1 235 ? -3.588  15.901  10.280  1.00 16.30  ? 236 GLU B CA  1 
ATOM   4098 C  C   . GLU B 1 235 ? -4.022  14.451  10.598  1.00 18.51  ? 236 GLU B C   1 
ATOM   4099 O  O   . GLU B 1 235 ? -5.188  14.070  10.437  1.00 19.52  ? 236 GLU B O   1 
ATOM   4100 C  CB  . GLU B 1 235 ? -3.608  16.666  11.619  1.00 17.82  ? 236 GLU B CB  1 
ATOM   4101 C  CG  . GLU B 1 235 ? -3.209  18.112  11.411  1.00 18.62  ? 236 GLU B CG  1 
ATOM   4102 C  CD  . GLU B 1 235 ? -3.348  18.971  12.641  1.00 25.77  ? 236 GLU B CD  1 
ATOM   4103 O  OE1 . GLU B 1 235 ? -3.998  18.550  13.645  1.00 20.42  ? 236 GLU B OE1 1 
ATOM   4104 O  OE2 . GLU B 1 235 ? -2.826  20.100  12.598  1.00 30.62  ? 236 GLU B OE2 1 
ATOM   4105 N  N   . PRO B 1 236 ? -3.110  13.639  11.108  1.00 17.40  ? 237 PRO B N   1 
ATOM   4106 C  CA  . PRO B 1 236 ? -3.452  12.225  11.345  1.00 19.07  ? 237 PRO B CA  1 
ATOM   4107 C  C   . PRO B 1 236 ? -4.537  12.152  12.433  1.00 15.82  ? 237 PRO B C   1 
ATOM   4108 O  O   . PRO B 1 236 ? -4.574  13.002  13.380  1.00 17.88  ? 237 PRO B O   1 
ATOM   4109 C  CB  . PRO B 1 236 ? -2.169  11.655  11.873  1.00 19.23  ? 237 PRO B CB  1 
ATOM   4110 C  CG  . PRO B 1 236 ? -1.128  12.425  11.127  1.00 22.24  ? 237 PRO B CG  1 
ATOM   4111 C  CD  . PRO B 1 236 ? -1.653  13.816  11.335  1.00 20.09  ? 237 PRO B CD  1 
ATOM   4112 N  N   . GLU B 1 237 ? -5.361  11.134  12.344  1.00 18.36  ? 238 GLU B N   1 
ATOM   4113 C  CA  . GLU B 1 237 ? -6.559  11.101  13.135  1.00 17.72  ? 238 GLU B CA  1 
ATOM   4114 C  C   . GLU B 1 237 ? -6.271  10.799  14.574  1.00 15.67  ? 238 GLU B C   1 
ATOM   4115 O  O   . GLU B 1 237 ? -5.609  9.819   14.867  1.00 14.69  ? 238 GLU B O   1 
ATOM   4116 C  CB  . GLU B 1 237 ? -7.537  10.043  12.626  1.00 18.04  ? 238 GLU B CB  1 
ATOM   4117 C  CG  . GLU B 1 237 ? -8.863  10.091  13.388  1.00 22.27  ? 238 GLU B CG  1 
ATOM   4118 C  CD  . GLU B 1 237 ? -9.934  9.336   12.673  1.00 20.74  ? 238 GLU B CD  1 
ATOM   4119 O  OE1 . GLU B 1 237 ? -9.680  8.104   12.405  1.00 28.34  ? 238 GLU B OE1 1 
ATOM   4120 O  OE2 . GLU B 1 237 ? -11.080 9.907   12.480  1.00 19.42  ? 238 GLU B OE2 1 
ATOM   4121 N  N   . GLU B 1 238 ? -6.781  11.567  15.497  1.00 14.84  ? 239 GLU B N   1 
ATOM   4122 C  CA  . GLU B 1 238 ? -6.755  11.322  16.913  1.00 14.16  ? 239 GLU B CA  1 
ATOM   4123 C  C   . GLU B 1 238 ? -8.186  11.436  17.412  1.00 12.07  ? 239 GLU B C   1 
ATOM   4124 O  O   . GLU B 1 238 ? -8.738  12.523  17.513  1.00 15.72  ? 239 GLU B O   1 
ATOM   4125 C  CB  . GLU B 1 238 ? -5.947  12.414  17.635  1.00 18.40  ? 239 GLU B CB  1 
ATOM   4126 C  CG  . GLU B 1 238 ? -4.493  12.724  17.222  1.00 22.81  ? 239 GLU B CG  1 
ATOM   4127 C  CD  . GLU B 1 238 ? -3.960  14.091  17.764  1.00 36.28  ? 239 GLU B CD  1 
ATOM   4128 O  OE1 . GLU B 1 238 ? -4.170  14.382  18.982  1.00 32.80  ? 239 GLU B OE1 1 
ATOM   4129 O  OE2 . GLU B 1 238 ? -3.368  14.881  16.992  1.00 63.15  ? 239 GLU B OE2 1 
ATOM   4130 N  N   . LEU B 1 239 ? -8.793  10.231  17.700  1.00 12.53  ? 240 LEU B N   1 
ATOM   4131 C  CA  . LEU B 1 239 ? -10.192 10.261  18.022  1.00 11.90  ? 240 LEU B CA  1 
ATOM   4132 C  C   . LEU B 1 239 ? -10.413 11.111  19.315  1.00 11.83  ? 240 LEU B C   1 
ATOM   4133 O  O   . LEU B 1 239 ? -9.650  10.940  20.271  1.00 12.72  ? 240 LEU B O   1 
ATOM   4134 C  CB  . LEU B 1 239 ? -10.735 8.853   18.236  1.00 12.64  ? 240 LEU B CB  1 
ATOM   4135 C  CG  . LEU B 1 239 ? -10.813 7.970   17.005  1.00 12.95  ? 240 LEU B CG  1 
ATOM   4136 C  CD1 . LEU B 1 239 ? -11.338 6.616   17.461  1.00 18.30  ? 240 LEU B CD1 1 
ATOM   4137 C  CD2 . LEU B 1 239 ? -11.616 8.631   15.914  1.00 14.28  ? 240 LEU B CD2 1 
ATOM   4138 N  N   . MET B 1 240 ? -11.427 11.937  19.314  1.00 12.14  ? 241 MET B N   1 
ATOM   4139 C  CA  . MET B 1 240 ? -11.813 12.751  20.465  1.00 12.00  ? 241 MET B CA  1 
ATOM   4140 C  C   . MET B 1 240 ? -12.627 11.848  21.400  1.00 10.19  ? 241 MET B C   1 
ATOM   4141 O  O   . MET B 1 240 ? -13.796 11.670  21.329  1.00 11.13  ? 241 MET B O   1 
ATOM   4142 C  CB  . MET B 1 240 ? -12.688 13.893  20.010  1.00 11.62  ? 241 MET B CB  1 
ATOM   4143 C  CG  . MET B 1 240 ? -12.933 14.875  21.173  1.00 12.96  ? 241 MET B CG  1 
ATOM   4144 S  SD  . MET B 1 240 ? -13.978 16.280  20.617  1.00 13.18  ? 241 MET B SD  1 
ATOM   4145 C  CE  . MET B 1 240 ? -12.633 17.325  20.006  1.00 15.48  ? 241 MET B CE  1 
ATOM   4146 N  N   . VAL B 1 241 ? -11.821 11.238  22.327  1.00 10.64  ? 242 VAL B N   1 
ATOM   4147 C  CA  . VAL B 1 241 ? -12.311 10.332  23.436  1.00 10.05  ? 242 VAL B CA  1 
ATOM   4148 C  C   . VAL B 1 241 ? -11.467 10.588  24.698  1.00 9.54   ? 242 VAL B C   1 
ATOM   4149 O  O   . VAL B 1 241 ? -10.338 11.006  24.626  1.00 10.40  ? 242 VAL B O   1 
ATOM   4150 C  CB  . VAL B 1 241 ? -12.215 8.819   23.053  1.00 10.61  ? 242 VAL B CB  1 
ATOM   4151 C  CG1 . VAL B 1 241 ? -13.163 8.506   21.866  1.00 13.09  ? 242 VAL B CG1 1 
ATOM   4152 C  CG2 . VAL B 1 241 ? -10.794 8.391   22.781  1.00 11.92  ? 242 VAL B CG2 1 
ATOM   4153 N  N   . ASP B 1 242 ? -12.118 10.289  25.843  1.00 8.89   ? 243 ASP B N   1 
ATOM   4154 C  CA  . ASP B 1 242 ? -11.426 10.430  27.124  1.00 9.18   ? 243 ASP B CA  1 
ATOM   4155 C  C   . ASP B 1 242 ? -10.953 11.848  27.368  1.00 9.36   ? 243 ASP B C   1 
ATOM   4156 O  O   . ASP B 1 242 ? -9.837  12.076  27.813  1.00 10.65  ? 243 ASP B O   1 
ATOM   4157 C  CB  . ASP B 1 242 ? -10.336 9.382   27.323  1.00 9.90   ? 243 ASP B CB  1 
ATOM   4158 C  CG  . ASP B 1 242 ? -10.917 7.962   27.434  1.00 9.65   ? 243 ASP B CG  1 
ATOM   4159 O  OD1 . ASP B 1 242 ? -11.969 7.794   28.099  1.00 9.80   ? 243 ASP B OD1 1 
ATOM   4160 O  OD2 . ASP B 1 242 ? -10.331 7.019   26.853  1.00 12.06  ? 243 ASP B OD2 1 
ATOM   4161 N  N   . ASN B 1 243 ? -11.820 12.800  27.102  1.00 8.66   ? 244 ASN B N   1 
ATOM   4162 C  CA  . ASN B 1 243 ? -11.579 14.209  27.318  1.00 8.87   ? 244 ASN B CA  1 
ATOM   4163 C  C   . ASN B 1 243 ? -12.085 14.684  28.694  1.00 7.71   ? 244 ASN B C   1 
ATOM   4164 O  O   . ASN B 1 243 ? -12.705 15.711  28.807  1.00 9.28   ? 244 ASN B O   1 
ATOM   4165 C  CB  . ASN B 1 243 ? -12.134 15.065  26.163  1.00 9.51   ? 244 ASN B CB  1 
ATOM   4166 C  CG  . ASN B 1 243 ? -13.592 14.867  25.954  1.00 8.98   ? 244 ASN B CG  1 
ATOM   4167 O  OD1 . ASN B 1 243 ? -14.235 14.063  26.612  1.00 10.17  ? 244 ASN B OD1 1 
ATOM   4168 N  ND2 . ASN B 1 243 ? -14.142 15.661  25.031  1.00 13.25  ? 244 ASN B ND2 1 
ATOM   4169 N  N   . TRP B 1 244 ? -11.826 13.865  29.726  1.00 7.74   ? 245 TRP B N   1 
ATOM   4170 C  CA  . TRP B 1 244 ? -12.240 14.120  31.114  1.00 7.57   ? 245 TRP B CA  1 
ATOM   4171 C  C   . TRP B 1 244 ? -11.037 14.210  32.025  1.00 7.71   ? 245 TRP B C   1 
ATOM   4172 O  O   . TRP B 1 244 ? -10.034 13.493  31.879  1.00 9.45   ? 245 TRP B O   1 
ATOM   4173 C  CB  . TRP B 1 244 ? -13.211 12.997  31.602  1.00 7.84   ? 245 TRP B CB  1 
ATOM   4174 C  CG  . TRP B 1 244 ? -12.725 11.625  31.406  1.00 7.57   ? 245 TRP B CG  1 
ATOM   4175 C  CD1 . TRP B 1 244 ? -12.861 10.845  30.278  1.00 8.11   ? 245 TRP B CD1 1 
ATOM   4176 C  CD2 . TRP B 1 244 ? -12.139 10.747  32.361  1.00 8.06   ? 245 TRP B CD2 1 
ATOM   4177 N  NE1 . TRP B 1 244 ? -12.344 9.608   30.437  1.00 8.26   ? 245 TRP B NE1 1 
ATOM   4178 C  CE2 . TRP B 1 244 ? -11.915 9.503   31.733  1.00 8.79   ? 245 TRP B CE2 1 
ATOM   4179 C  CE3 . TRP B 1 244 ? -11.832 10.883  33.744  1.00 9.26   ? 245 TRP B CE3 1 
ATOM   4180 C  CZ2 . TRP B 1 244 ? -11.348 8.421   32.419  1.00 9.92   ? 245 TRP B CZ2 1 
ATOM   4181 C  CZ3 . TRP B 1 244 ? -11.263 9.801   34.401  1.00 10.58  ? 245 TRP B CZ3 1 
ATOM   4182 C  CH2 . TRP B 1 244 ? -11.034 8.580   33.737  1.00 10.43  ? 245 TRP B CH2 1 
ATOM   4183 N  N   . ARG B 1 245 ? -11.163 15.081  33.010  1.00 7.66   ? 246 ARG B N   1 
ATOM   4184 C  CA  . ARG B 1 245 ? -10.192 15.217  34.092  1.00 7.54   ? 246 ARG B CA  1 
ATOM   4185 C  C   . ARG B 1 245 ? -10.691 14.287  35.210  1.00 7.42   ? 246 ARG B C   1 
ATOM   4186 O  O   . ARG B 1 245 ? -11.862 14.306  35.544  1.00 8.12   ? 246 ARG B O   1 
ATOM   4187 C  CB  . ARG B 1 245 ? -10.139 16.673  34.580  1.00 8.23   ? 246 ARG B CB  1 
ATOM   4188 C  CG  . ARG B 1 245 ? -9.030  16.901  35.609  1.00 8.58   ? 246 ARG B CG  1 
ATOM   4189 C  CD  . ARG B 1 245 ? -9.083  18.262  36.223  1.00 8.41   ? 246 ARG B CD  1 
ATOM   4190 N  NE  . ARG B 1 245 ? -7.819  18.608  36.875  1.00 9.17   ? 246 ARG B NE  1 
ATOM   4191 C  CZ  . ARG B 1 245 ? -7.645  19.588  37.761  1.00 8.78   ? 246 ARG B CZ  1 
ATOM   4192 N  NH1 . ARG B 1 245 ? -8.653  20.365  38.143  1.00 9.35   ? 246 ARG B NH1 1 
ATOM   4193 N  NH2 . ARG B 1 245 ? -6.439  19.787  38.271  1.00 10.67  ? 246 ARG B NH2 1 
ATOM   4194 N  N   A PRO B 1 246 ? -9.786  13.487  35.798  0.50 8.12   ? 247 PRO B N   1 
ATOM   4195 N  N   B PRO B 1 246 ? -9.754  13.554  35.855  0.50 8.34   ? 247 PRO B N   1 
ATOM   4196 C  CA  A PRO B 1 246 ? -10.203 12.667  36.932  0.50 8.47   ? 247 PRO B CA  1 
ATOM   4197 C  CA  B PRO B 1 246 ? -10.182 12.696  36.961  0.50 8.65   ? 247 PRO B CA  1 
ATOM   4198 C  C   A PRO B 1 246 ? -10.555 13.500  38.182  0.50 8.16   ? 247 PRO B C   1 
ATOM   4199 C  C   B PRO B 1 246 ? -10.532 13.505  38.199  0.50 8.56   ? 247 PRO B C   1 
ATOM   4200 O  O   A PRO B 1 246 ? -10.201 14.680  38.330  0.50 8.37   ? 247 PRO B O   1 
ATOM   4201 O  O   B PRO B 1 246 ? -10.163 14.680  38.346  0.50 8.75   ? 247 PRO B O   1 
ATOM   4202 C  CB  A PRO B 1 246 ? -8.993  11.794  37.180  0.50 10.67  ? 247 PRO B CB  1 
ATOM   4203 C  CB  B PRO B 1 246 ? -8.983  11.824  37.234  0.50 12.15  ? 247 PRO B CB  1 
ATOM   4204 C  CG  A PRO B 1 246 ? -8.147  11.795  35.919  0.50 9.32   ? 247 PRO B CG  1 
ATOM   4205 C  CG  B PRO B 1 246 ? -7.827  12.536  36.679  0.50 11.86  ? 247 PRO B CG  1 
ATOM   4206 C  CD  A PRO B 1 246 ? -8.401  13.163  35.339  0.50 8.62   ? 247 PRO B CD  1 
ATOM   4207 C  CD  B PRO B 1 246 ? -8.278  13.516  35.648  0.50 10.32  ? 247 PRO B CD  1 
ATOM   4208 N  N   . ALA B 1 247 ? -11.173 12.823  39.151  1.00 8.41   ? 248 ALA B N   1 
ATOM   4209 C  CA  . ALA B 1 247 ? -11.502 13.464  40.446  1.00 8.89   ? 248 ALA B CA  1 
ATOM   4210 C  C   . ALA B 1 247 ? -10.268 13.968  41.161  1.00 8.84   ? 248 ALA B C   1 
ATOM   4211 O  O   . ALA B 1 247 ? -9.232  13.293  41.195  1.00 10.57  ? 248 ALA B O   1 
ATOM   4212 C  CB  . ALA B 1 247 ? -12.295 12.469  41.311  1.00 10.59  ? 248 ALA B CB  1 
ATOM   4213 N  N   . GLN B 1 248 ? -10.440 15.156  41.758  1.00 8.54   ? 249 GLN B N   1 
ATOM   4214 C  CA  . GLN B 1 248 ? -9.361  15.879  42.480  1.00 9.19   ? 249 GLN B CA  1 
ATOM   4215 C  C   . GLN B 1 248 ? -9.700  15.856  43.962  1.00 9.66   ? 249 GLN B C   1 
ATOM   4216 O  O   . GLN B 1 248 ? -10.840 15.645  44.389  1.00 9.96   ? 249 GLN B O   1 
ATOM   4217 C  CB  . GLN B 1 248 ? -9.330  17.296  41.953  1.00 10.24  ? 249 GLN B CB  1 
ATOM   4218 C  CG  . GLN B 1 248 ? -8.997  17.389  40.446  1.00 10.02  ? 249 GLN B CG  1 
ATOM   4219 C  CD  . GLN B 1 248 ? -7.675  16.730  40.111  1.00 10.55  ? 249 GLN B CD  1 
ATOM   4220 O  OE1 . GLN B 1 248 ? -6.664  17.068  40.712  1.00 13.09  ? 249 GLN B OE1 1 
ATOM   4221 N  NE2 . GLN B 1 248 ? -7.657  15.803  39.161  1.00 11.61  ? 249 GLN B NE2 1 
ATOM   4222 N  N   . PRO B 1 249 ? -8.679  16.168  44.798  1.00 11.63  ? 250 PRO B N   1 
ATOM   4223 C  CA  . PRO B 1 249 ? -8.870  16.143  46.255  1.00 13.10  ? 250 PRO B CA  1 
ATOM   4224 C  C   . PRO B 1 249 ? -9.938  17.126  46.686  1.00 10.72  ? 250 PRO B C   1 
ATOM   4225 O  O   . PRO B 1 249 ? -9.936  18.301  46.338  1.00 11.25  ? 250 PRO B O   1 
ATOM   4226 C  CB  . PRO B 1 249 ? -7.458  16.510  46.779  1.00 16.17  ? 250 PRO B CB  1 
ATOM   4227 C  CG  . PRO B 1 249 ? -6.499  16.039  45.767  1.00 18.53  ? 250 PRO B CG  1 
ATOM   4228 C  CD  . PRO B 1 249 ? -7.272  16.369  44.441  1.00 13.96  ? 250 PRO B CD  1 
ATOM   4229 N  N   . LEU B 1 250 ? -10.830 16.661  47.556  1.00 11.23  ? 251 LEU B N   1 
ATOM   4230 C  CA  . LEU B 1 250 ? -11.908 17.498  48.079  1.00 10.18  ? 251 LEU B CA  1 
ATOM   4231 C  C   . LEU B 1 250 ? -11.381 18.592  48.996  1.00 10.59  ? 251 LEU B C   1 
ATOM   4232 O  O   . LEU B 1 250 ? -11.936 19.686  49.083  1.00 10.84  ? 251 LEU B O   1 
ATOM   4233 C  CB  . LEU B 1 250 ? -12.925 16.640  48.852  1.00 12.87  ? 251 LEU B CB  1 
ATOM   4234 C  CG  . LEU B 1 250 ? -14.228 17.376  49.221  1.00 12.94  ? 251 LEU B CG  1 
ATOM   4235 C  CD1 . LEU B 1 250 ? -15.024 17.905  48.006  1.00 13.47  ? 251 LEU B CD1 1 
ATOM   4236 C  CD2 . LEU B 1 250 ? -15.133 16.416  49.994  1.00 16.68  ? 251 LEU B CD2 1 
ATOM   4237 N  N   A LYS B 1 251 ? -10.309 18.310  49.736  0.50 12.44  ? 252 LYS B N   1 
ATOM   4238 N  N   B LYS B 1 251 ? -10.302 18.297  49.721  0.50 12.35  ? 252 LYS B N   1 
ATOM   4239 C  CA  A LYS B 1 251 ? -9.668  19.354  50.605  0.50 12.39  ? 252 LYS B CA  1 
ATOM   4240 C  CA  B LYS B 1 251 ? -9.639  19.327  50.581  0.50 13.07  ? 252 LYS B CA  1 
ATOM   4241 C  C   A LYS B 1 251 ? -10.705 19.901  51.575  0.50 13.60  ? 252 LYS B C   1 
ATOM   4242 C  C   B LYS B 1 251 ? -10.678 19.896  51.565  0.50 13.14  ? 252 LYS B C   1 
ATOM   4243 O  O   A LYS B 1 251 ? -11.507 19.109  52.116  0.50 16.14  ? 252 LYS B O   1 
ATOM   4244 O  O   B LYS B 1 251 ? -11.481 19.092  52.093  0.50 15.42  ? 252 LYS B O   1 
ATOM   4245 C  CB  A LYS B 1 251 ? -8.903  20.412  49.821  0.50 15.57  ? 252 LYS B CB  1 
ATOM   4246 C  CB  B LYS B 1 251 ? -8.839  20.340  49.765  0.50 14.23  ? 252 LYS B CB  1 
ATOM   4247 C  CG  A LYS B 1 251 ? -7.827  19.737  48.986  0.50 18.89  ? 252 LYS B CG  1 
ATOM   4248 C  CG  B LYS B 1 251 ? -7.564  19.710  49.188  0.50 17.44  ? 252 LYS B CG  1 
ATOM   4249 C  CD  A LYS B 1 251 ? -6.598  20.577  48.766  0.50 22.31  ? 252 LYS B CD  1 
ATOM   4250 C  CD  B LYS B 1 251 ? -6.816  20.651  48.299  0.50 15.04  ? 252 LYS B CD  1 
ATOM   4251 C  CE  A LYS B 1 251 ? -5.802  19.909  47.655  0.50 18.92  ? 252 LYS B CE  1 
ATOM   4252 C  CE  B LYS B 1 251 ? -5.357  20.250  48.242  0.50 20.44  ? 252 LYS B CE  1 
ATOM   4253 N  NZ  A LYS B 1 251 ? -4.738  20.765  47.067  0.50 20.88  ? 252 LYS B NZ  1 
ATOM   4254 N  NZ  B LYS B 1 251 ? -4.845  19.879  49.587  0.50 30.78  ? 252 LYS B NZ  1 
ATOM   4255 N  N   . ASN B 1 252 ? -10.717 21.184  51.812  1.00 13.75  ? 253 ASN B N   1 
ATOM   4256 C  CA  . ASN B 1 252 ? -11.580 21.670  52.811  1.00 19.97  ? 253 ASN B CA  1 
ATOM   4257 C  C   . ASN B 1 252 ? -12.890 22.108  52.222  1.00 17.05  ? 253 ASN B C   1 
ATOM   4258 O  O   . ASN B 1 252 ? -13.184 23.303  52.152  1.00 19.13  ? 253 ASN B O   1 
ATOM   4259 C  CB  . ASN B 1 252 ? -10.857 22.847  53.543  1.00 24.71  ? 253 ASN B CB  1 
ATOM   4260 C  CG  . ASN B 1 252 ? -11.614 23.313  54.756  1.00 26.71  ? 253 ASN B CG  1 
ATOM   4261 O  OD1 . ASN B 1 252 ? -12.324 22.527  55.401  1.00 44.11  ? 253 ASN B OD1 1 
ATOM   4262 N  ND2 . ASN B 1 252 ? -11.571 24.620  55.024  1.00 30.76  ? 253 ASN B ND2 1 
ATOM   4263 N  N   . ARG B 1 253 ? -13.694 21.088  51.629  1.00 15.04  ? 254 ARG B N   1 
ATOM   4264 C  CA  . ARG B 1 253 ? -14.948 21.384  51.138  1.00 11.14  ? 254 ARG B CA  1 
ATOM   4265 C  C   . ARG B 1 253 ? -16.035 20.441  51.608  1.00 11.72  ? 254 ARG B C   1 
ATOM   4266 O  O   . ARG B 1 253 ? -15.786 19.260  51.830  1.00 19.86  ? 254 ARG B O   1 
ATOM   4267 C  CB  . ARG B 1 253 ? -14.904 21.472  49.613  1.00 10.01  ? 254 ARG B CB  1 
ATOM   4268 C  CG  . ARG B 1 253 ? -14.024 22.580  49.102  1.00 10.07  ? 254 ARG B CG  1 
ATOM   4269 C  CD  . ARG B 1 253 ? -13.880 22.586  47.598  1.00 9.37   ? 254 ARG B CD  1 
ATOM   4270 N  NE  . ARG B 1 253 ? -13.072 21.451  47.156  1.00 8.98   ? 254 ARG B NE  1 
ATOM   4271 C  CZ  . ARG B 1 253 ? -12.804 21.160  45.882  1.00 7.44   ? 254 ARG B CZ  1 
ATOM   4272 N  NH1 . ARG B 1 253 ? -13.425 21.868  44.898  1.00 7.71   ? 254 ARG B NH1 1 
ATOM   4273 N  NH2 . ARG B 1 253 ? -11.996 20.200  45.570  1.00 8.51   ? 254 ARG B NH2 1 
ATOM   4274 N  N   . GLN B 1 254 ? -17.257 20.992  51.641  1.00 11.95  ? 255 GLN B N   1 
ATOM   4275 C  CA  . GLN B 1 254 ? -18.436 20.220  51.912  1.00 12.93  ? 255 GLN B CA  1 
ATOM   4276 C  C   . GLN B 1 254 ? -19.326 20.205  50.672  1.00 12.38  ? 255 GLN B C   1 
ATOM   4277 O  O   . GLN B 1 254 ? -19.569 21.272  49.995  1.00 16.19  ? 255 GLN B O   1 
ATOM   4278 C  CB  . GLN B 1 254 ? -19.276 20.871  53.004  1.00 17.87  ? 255 GLN B CB  1 
ATOM   4279 C  CG  . GLN B 1 254 ? -20.033 19.890  53.903  1.00 33.41  ? 255 GLN B CG  1 
ATOM   4280 N  N   . ILE B 1 255 ? -19.794 19.016  50.295  1.00 10.30  ? 256 ILE B N   1 
ATOM   4281 C  CA  . ILE B 1 255 ? -20.777 18.886  49.238  1.00 9.85   ? 256 ILE B CA  1 
ATOM   4282 C  C   . ILE B 1 255 ? -22.155 18.840  49.917  1.00 9.98   ? 256 ILE B C   1 
ATOM   4283 O  O   . ILE B 1 255 ? -22.380 18.115  50.884  1.00 11.93  ? 256 ILE B O   1 
ATOM   4284 C  CB  . ILE B 1 255 ? -20.539 17.636  48.396  1.00 9.66   ? 256 ILE B CB  1 
ATOM   4285 C  CG1 . ILE B 1 255 ? -19.101 17.630  47.862  1.00 10.54  ? 256 ILE B CG1 1 
ATOM   4286 C  CG2 . ILE B 1 255 ? -21.651 17.503  47.341  1.00 11.63  ? 256 ILE B CG2 1 
ATOM   4287 C  CD1 . ILE B 1 255 ? -18.763 16.456  47.011  1.00 12.21  ? 256 ILE B CD1 1 
ATOM   4288 N  N   . LYS B 1 256 ? -23.087 19.678  49.415  1.00 9.66   ? 257 LYS B N   1 
ATOM   4289 C  CA  . LYS B 1 256 ? -24.441 19.804  49.968  1.00 9.97   ? 257 LYS B CA  1 
ATOM   4290 C  C   . LYS B 1 256 ? -25.437 19.163  49.013  1.00 9.45   ? 257 LYS B C   1 
ATOM   4291 O  O   . LYS B 1 256 ? -25.227 19.246  47.793  1.00 11.53  ? 257 LYS B O   1 
ATOM   4292 C  CB  . LYS B 1 256 ? -24.806 21.284  50.233  1.00 10.83  ? 257 LYS B CB  1 
ATOM   4293 C  CG  . LYS B 1 256 ? -23.805 21.813  51.257  1.00 16.82  ? 257 LYS B CG  1 
ATOM   4294 C  CD  . LYS B 1 256 ? -23.952 23.223  51.673  1.00 22.52  ? 257 LYS B CD  1 
ATOM   4295 C  CE  . LYS B 1 256 ? -22.766 23.652  52.533  1.00 32.38  ? 257 LYS B CE  1 
ATOM   4296 N  NZ  . LYS B 1 256 ? -22.860 25.059  53.078  1.00 31.02  ? 257 LYS B NZ  1 
ATOM   4297 N  N   . ALA B 1 257 ? -26.467 18.511  49.514  1.00 10.06  ? 258 ALA B N   1 
ATOM   4298 C  CA  . ALA B 1 257 ? -27.526 17.936  48.776  1.00 10.36  ? 258 ALA B CA  1 
ATOM   4299 C  C   . ALA B 1 257 ? -28.800 18.760  48.949  1.00 10.23  ? 258 ALA B C   1 
ATOM   4300 O  O   . ALA B 1 257 ? -29.149 19.199  50.049  1.00 11.75  ? 258 ALA B O   1 
ATOM   4301 C  CB  . ALA B 1 257 ? -27.766 16.470  49.167  1.00 12.47  ? 258 ALA B CB  1 
ATOM   4302 N  N   . SER B 1 258 ? -29.544 18.896  47.839  1.00 9.87   ? 259 SER B N   1 
ATOM   4303 C  CA  . SER B 1 258 ? -30.816 19.593  47.872  1.00 11.88  ? 259 SER B CA  1 
ATOM   4304 C  C   . SER B 1 258 ? -31.939 18.684  48.288  1.00 12.44  ? 259 SER B C   1 
ATOM   4305 O  O   . SER B 1 258 ? -33.090 19.176  48.367  1.00 16.24  ? 259 SER B O   1 
ATOM   4306 C  CB  . SER B 1 258 ? -31.147 20.131  46.505  1.00 12.36  ? 259 SER B CB  1 
ATOM   4307 O  OG  . SER B 1 258 ? -31.529 19.107  45.592  1.00 11.58  ? 259 SER B OG  1 
ATOM   4308 N  N   . PHE B 1 259 ? -31.708 17.404  48.492  1.00 13.21  ? 260 PHE B N   1 
ATOM   4309 C  CA  . PHE B 1 259 ? -32.729 16.367  48.666  1.00 15.68  ? 260 PHE B CA  1 
ATOM   4310 C  C   . PHE B 1 259 ? -32.284 15.465  49.785  1.00 17.47  ? 260 PHE B C   1 
ATOM   4311 O  O   . PHE B 1 259 ? -31.096 15.296  50.066  1.00 19.55  ? 260 PHE B O   1 
ATOM   4312 C  CB  . PHE B 1 259 ? -32.900 15.588  47.373  1.00 15.51  ? 260 PHE B CB  1 
ATOM   4313 C  CG  . PHE B 1 259 ? -31.614 14.889  46.946  1.00 14.33  ? 260 PHE B CG  1 
ATOM   4314 C  CD1 . PHE B 1 259 ? -30.621 15.551  46.239  1.00 12.62  ? 260 PHE B CD1 1 
ATOM   4315 C  CD2 . PHE B 1 259 ? -31.344 13.593  47.395  1.00 17.97  ? 260 PHE B CD2 1 
ATOM   4316 C  CE1 . PHE B 1 259 ? -29.418 14.921  45.900  1.00 14.11  ? 260 PHE B CE1 1 
ATOM   4317 C  CE2 . PHE B 1 259 ? -30.152 12.952  47.053  1.00 18.90  ? 260 PHE B CE2 1 
ATOM   4318 C  CZ  . PHE B 1 259 ? -29.184 13.612  46.325  1.00 18.54  ? 260 PHE B CZ  1 
ATOM   4319 N  N   . LYS B 1 260 ? -33.318 14.874  50.293  1.00 40.63  ? 261 LYS B N   1 
ATOM   4320 C  CA  . LYS B 1 260 ? -33.369 13.746  51.217  1.00 41.67  ? 261 LYS B CA  1 
ATOM   4321 C  C   . LYS B 1 260 ? -32.708 13.885  52.604  1.00 60.81  ? 261 LYS B C   1 
ATOM   4322 O  O   . LYS B 1 260 ? -33.399 14.081  53.606  1.00 65.39  ? 261 LYS B O   1 
ATOM   4323 C  CB  . LYS B 1 260 ? -32.931 12.461  50.510  1.00 48.03  ? 261 LYS B CB  1 
ATOM   4324 C  CG  . LYS B 1 260 ? -33.868 12.025  49.351  1.00 50.24  ? 261 LYS B CG  1 
ATOM   4325 C  CD  . LYS B 1 260 ? -33.934 10.508  49.190  1.00 64.85  ? 261 LYS B CD  1 
ATOM   4326 C  CE  . LYS B 1 260 ? -32.886 9.995   48.198  1.00 51.52  ? 261 LYS B CE  1 
ATOM   4327 N  NZ  . LYS B 1 260 ? -33.144 8.616   47.735  1.00 65.00  ? 261 LYS B NZ  1 
ATOM   4328 O  OXT . LYS B 1 260 ? -31.486 13.803  52.731  1.00 79.14  ? 261 LYS B OXT 1 
HETATM 4329 ZN ZN  . ZN  C 2 .   ? -3.442  0.128   0.497   1.00 7.09   ? 301 ZN  A ZN  1 
HETATM 4330 N  N1  . BCN D 3 .   ? 10.388  -12.708 -7.524  1.00 24.51  ? 302 BCN A N1  1 
HETATM 4331 C  C1  . BCN D 3 .   ? 9.584   -12.334 -8.587  1.00 25.31  ? 302 BCN A C1  1 
HETATM 4332 C  C2  . BCN D 3 .   ? 9.888   -13.274 -9.705  1.00 27.79  ? 302 BCN A C2  1 
HETATM 4333 O  O21 . BCN D 3 .   ? 9.191   -13.161 -10.782 1.00 30.12  ? 302 BCN A O21 1 
HETATM 4334 O  O22 . BCN D 3 .   ? 10.724  -14.129 -9.686  1.00 34.62  ? 302 BCN A O22 1 
HETATM 4335 C  C3  . BCN D 3 .   ? 11.577  -12.140 -7.204  1.00 21.10  ? 302 BCN A C3  1 
HETATM 4336 C  C4  . BCN D 3 .   ? 12.631  -11.175 -7.673  1.00 30.20  ? 302 BCN A C4  1 
HETATM 4337 O  O4  . BCN D 3 .   ? 12.481  -10.574 -8.983  1.00 28.63  ? 302 BCN A O4  1 
HETATM 4338 C  C5  . BCN D 3 .   ? 9.910   -13.725 -6.602  1.00 17.48  ? 302 BCN A C5  1 
HETATM 4339 C  C6  . BCN D 3 .   ? 11.099  -14.074 -5.732  1.00 30.77  ? 302 BCN A C6  1 
HETATM 4340 O  O6  . BCN D 3 .   ? 10.791  -14.475 -4.507  1.00 40.04  ? 302 BCN A O6  1 
HETATM 4341 S  S   . DMS E 4 .   ? -11.493 -9.886  0.850   1.00 20.34  ? 303 DMS A S   1 
HETATM 4342 O  O   . DMS E 4 .   ? -12.041 -11.172 1.364   1.00 27.87  ? 303 DMS A O   1 
HETATM 4343 C  C1  . DMS E 4 .   ? -11.776 -9.749  -0.788  1.00 18.19  ? 303 DMS A C1  1 
HETATM 4344 C  C2  . DMS E 4 .   ? -12.575 -8.642  1.181   1.00 22.82  ? 303 DMS A C2  1 
HETATM 4345 F  F13 . 5DU F 5 .   ? -5.303  5.424   3.969   1.00 42.62  ? 304 5DU A F13 1 
HETATM 4346 C  C9  . 5DU F 5 .   ? -4.938  5.218   2.677   1.00 25.74  ? 304 5DU A C9  1 
HETATM 4347 C  C8  . 5DU F 5 .   ? -4.562  6.360   2.010   1.00 25.18  ? 304 5DU A C8  1 
HETATM 4348 S  S24 . 5DU F 5 .   ? -4.627  7.824   2.899   1.00 36.51  ? 304 5DU A S24 1 
HETATM 4349 C  C25 . 5DU F 5 .   ? -2.984  7.746   3.050   1.00 18.59  ? 304 5DU A C25 1 
HETATM 4350 C  C26 . 5DU F 5 .   ? -2.883  9.012   3.952   1.00 29.69  ? 304 5DU A C26 1 
HETATM 4351 O  O27 . 5DU F 5 .   ? -3.432  8.902   5.263   1.00 44.34  ? 304 5DU A O27 1 
HETATM 4352 C  C7  . 5DU F 5 .   ? -4.161  6.240   0.722   1.00 18.55  ? 304 5DU A C7  1 
HETATM 4353 F  F12 . 5DU F 5 .   ? -3.707  7.360   0.149   1.00 23.02  ? 304 5DU A F12 1 
HETATM 4354 C  C6  . 5DU F 5 .   ? -4.246  5.059   0.074   1.00 16.93  ? 304 5DU A C6  1 
HETATM 4355 F  F11 . 5DU F 5 .   ? -3.842  5.144   -1.217  1.00 20.86  ? 304 5DU A F11 1 
HETATM 4356 C  C10 . 5DU F 5 .   ? -5.097  3.982   2.101   1.00 20.63  ? 304 5DU A C10 1 
HETATM 4357 C  C5  . 5DU F 5 .   ? -4.749  3.945   0.759   1.00 18.22  ? 304 5DU A C5  1 
HETATM 4358 S  S1  . 5DU F 5 .   ? -4.735  2.426   -0.242  1.00 16.18  ? 304 5DU A S1  1 
HETATM 4359 O  O3  . 5DU F 5 .   ? -5.972  2.213   -1.125  1.00 16.44  ? 304 5DU A O3  1 
HETATM 4360 N  N4  . 5DU F 5 .   ? -4.629  0.912   0.664   1.00 11.96  ? 304 5DU A N4  1 
HETATM 4361 O  O2  . 5DU F 5 .   ? -3.561  2.334   -1.232  1.00 11.31  ? 304 5DU A O2  1 
HETATM 4362 N  N14 . 5DU F 5 .   ? -5.622  2.824   2.733   1.00 29.30  ? 304 5DU A N14 1 
HETATM 4363 C  C15 . 5DU F 5 .   ? -5.853  2.800   4.210   1.00 22.26  ? 304 5DU A C15 1 
HETATM 4364 C  C19 . 5DU F 5 .   ? -6.320  1.422   4.391   1.00 19.03  ? 304 5DU A C19 1 
HETATM 4365 C  C20 . 5DU F 5 .   ? -5.597  0.310   4.228   1.00 21.67  ? 304 5DU A C20 1 
HETATM 4366 C  C21 . 5DU F 5 .   ? -6.209  -0.996  4.341   1.00 23.79  ? 304 5DU A C21 1 
HETATM 4367 C  C22 . 5DU F 5 .   ? -7.597  -1.098  4.493   1.00 17.79  ? 304 5DU A C22 1 
HETATM 4368 C  C23 . 5DU F 5 .   ? -8.332  0.116   4.677   1.00 21.55  ? 304 5DU A C23 1 
HETATM 4369 C  C18 . 5DU F 5 .   ? -7.668  1.366   4.590   1.00 20.67  ? 304 5DU A C18 1 
HETATM 4370 C  C17 . 5DU F 5 .   ? -8.298  2.732   4.690   1.00 26.13  ? 304 5DU A C17 1 
HETATM 4371 C  C16 . 5DU F 5 .   ? -7.053  3.643   4.724   1.00 26.02  ? 304 5DU A C16 1 
HETATM 4372 ZN ZN  . ZN  G 2 .   ? -16.771 20.709  31.118  1.00 7.08   ? 301 ZN  B ZN  1 
HETATM 4373 N  N1  . BCN H 3 .   ? -30.486 7.803   39.121  1.00 25.55  ? 302 BCN B N1  1 
HETATM 4374 C  C1  . BCN H 3 .   ? -29.683 8.208   40.184  1.00 25.90  ? 302 BCN B C1  1 
HETATM 4375 C  C2  . BCN H 3 .   ? -29.772 7.112   41.205  1.00 41.13  ? 302 BCN B C2  1 
HETATM 4376 O  O21 . BCN H 3 .   ? -30.244 5.886   40.925  1.00 55.64  ? 302 BCN B O21 1 
HETATM 4377 O  O22 . BCN H 3 .   ? -29.455 7.309   42.286  1.00 33.75  ? 302 BCN B O22 1 
HETATM 4378 C  C3  . BCN H 3 .   ? -30.133 6.833   38.222  1.00 17.52  ? 302 BCN B C3  1 
HETATM 4379 C  C4  . BCN H 3 .   ? -30.475 6.034   37.030  1.00 34.00  ? 302 BCN B C4  1 
HETATM 4380 O  O4  . BCN H 3 .   ? -31.643 6.520   36.399  1.00 49.57  ? 302 BCN B O4  1 
HETATM 4381 C  C5  . BCN H 3 .   ? -31.732 8.449   38.875  1.00 18.59  ? 302 BCN B C5  1 
HETATM 4382 C  C6  . BCN H 3 .   ? -32.452 8.766   40.195  1.00 39.97  ? 302 BCN B C6  1 
HETATM 4383 O  O6  . BCN H 3 .   ? -32.647 10.016  40.689  1.00 27.80  ? 302 BCN B O6  1 
HETATM 4384 S  S   . DMS I 4 .   ? -8.724  10.693  30.760  1.00 20.76  ? 303 DMS B S   1 
HETATM 4385 O  O   . DMS I 4 .   ? -8.252  9.364   30.274  1.00 28.54  ? 303 DMS B O   1 
HETATM 4386 C  C1  . DMS I 4 .   ? -8.392  10.852  32.369  1.00 20.01  ? 303 DMS B C1  1 
HETATM 4387 C  C2  . DMS I 4 .   ? -7.777  11.942  30.258  1.00 20.75  ? 303 DMS B C2  1 
HETATM 4388 F  F13 . 5DU J 5 .   ? -15.872 25.740  27.428  1.00 25.36  ? 304 5DU B F13 1 
HETATM 4389 C  C9  . 5DU J 5 .   ? -15.902 25.647  28.843  1.00 18.66  ? 304 5DU B C9  1 
HETATM 4390 C  C8  . 5DU J 5 .   ? -16.316 26.842  29.441  1.00 18.53  ? 304 5DU B C8  1 
HETATM 4391 S  S24 . 5DU J 5 .   ? -16.756 28.296  28.550  1.00 22.84  ? 304 5DU B S24 1 
HETATM 4392 C  C25 . 5DU J 5 .   ? -15.271 28.674  27.602  1.00 29.93  ? 304 5DU B C25 1 
HETATM 4393 C  C26 . 5DU J 5 .   ? -15.628 29.393  26.305  1.00 29.22  ? 304 5DU B C26 1 
HETATM 4394 O  O27 . 5DU J 5 .   ? -16.892 28.987  25.856  1.00 30.45  ? 304 5DU B O27 1 
HETATM 4395 C  C7  . 5DU J 5 .   ? -16.353 26.807  30.843  1.00 17.36  ? 304 5DU B C7  1 
HETATM 4396 F  F12 . 5DU J 5 .   ? -16.752 27.887  31.816  1.00 20.03  ? 304 5DU B F12 1 
HETATM 4397 C  C6  . 5DU J 5 .   ? -16.175 25.702  31.567  1.00 16.33  ? 304 5DU B C6  1 
HETATM 4398 F  F11 . 5DU J 5 .   ? -16.409 25.705  32.902  1.00 18.70  ? 304 5DU B F11 1 
HETATM 4399 C  C10 . 5DU J 5 .   ? -15.530 24.499  29.505  1.00 19.86  ? 304 5DU B C10 1 
HETATM 4400 C  C5  . 5DU J 5 .   ? -15.637 24.539  30.962  1.00 17.97  ? 304 5DU B C5  1 
HETATM 4401 S  S1  . 5DU J 5 .   ? -15.519 23.272  32.063  1.00 16.58  ? 304 5DU B S1  1 
HETATM 4402 O  O3  . 5DU J 5 .   ? -14.708 23.666  33.146  1.00 21.09  ? 304 5DU B O3  1 
HETATM 4403 N  N4  . 5DU J 5 .   ? -15.246 21.788  31.689  1.00 17.85  ? 304 5DU B N4  1 
HETATM 4404 O  O2  . 5DU J 5 .   ? -17.007 22.977  32.548  1.00 23.53  ? 304 5DU B O2  1 
HETATM 4405 N  N14 . 5DU J 5 .   ? -15.156 23.348  28.702  1.00 24.55  ? 304 5DU B N14 1 
HETATM 4406 C  C15 . 5DU J 5 .   ? -14.436 23.368  27.447  1.00 19.48  ? 304 5DU B C15 1 
HETATM 4407 C  C19 . 5DU J 5 .   ? -13.929 22.000  27.238  1.00 17.79  ? 304 5DU B C19 1 
HETATM 4408 C  C20 . 5DU J 5 .   ? -14.569 20.819  27.398  1.00 18.24  ? 304 5DU B C20 1 
HETATM 4409 C  C21 . 5DU J 5 .   ? -13.912 19.552  27.227  1.00 18.89  ? 304 5DU B C21 1 
HETATM 4410 C  C22 . 5DU J 5 .   ? -12.557 19.562  27.016  1.00 17.01  ? 304 5DU B C22 1 
HETATM 4411 C  C23 . 5DU J 5 .   ? -11.896 20.776  26.879  1.00 19.12  ? 304 5DU B C23 1 
HETATM 4412 C  C18 . 5DU J 5 .   ? -12.602 21.977  27.004  1.00 18.66  ? 304 5DU B C18 1 
HETATM 4413 C  C17 . 5DU J 5 .   ? -12.049 23.325  26.936  1.00 20.93  ? 304 5DU B C17 1 
HETATM 4414 C  C16 . 5DU J 5 .   ? -13.133 24.195  27.549  1.00 25.41  ? 304 5DU B C16 1 
HETATM 4415 O  O   . HOH K 6 .   ? -26.652 -7.065  4.630   1.00 22.91  ? 401 HOH A O   1 
HETATM 4416 O  O   . HOH K 6 .   ? -24.863 -9.511  2.300   1.00 33.83  ? 402 HOH A O   1 
HETATM 4417 O  O   . HOH K 6 .   ? -6.764  19.899  -5.287  1.00 29.03  ? 403 HOH A O   1 
HETATM 4418 O  O   . HOH K 6 .   ? 0.388   -4.000  -22.508 1.00 26.18  ? 404 HOH A O   1 
HETATM 4419 O  O   . HOH K 6 .   ? 4.261   -6.686  21.168  1.00 35.13  ? 405 HOH A O   1 
HETATM 4420 O  O   . HOH K 6 .   ? -9.695  -15.362 -13.114 1.00 52.34  ? 406 HOH A O   1 
HETATM 4421 O  O   . HOH K 6 .   ? -19.102 -11.301 -0.773  1.00 41.99  ? 407 HOH A O   1 
HETATM 4422 O  O   . HOH K 6 .   ? 7.342   -5.477  -23.456 1.00 79.90  ? 408 HOH A O   1 
HETATM 4423 O  O   . HOH K 6 .   ? 5.365   -8.485  -21.579 1.00 32.08  ? 409 HOH A O   1 
HETATM 4424 O  O   . HOH K 6 .   ? 15.426  11.328  2.739   1.00 41.64  ? 410 HOH A O   1 
HETATM 4425 O  O   . HOH K 6 .   ? -14.607 -0.709  -13.240 1.00 24.29  ? 411 HOH A O   1 
HETATM 4426 O  O   . HOH K 6 .   ? 1.037   -13.280 -18.320 1.00 23.61  ? 412 HOH A O   1 
HETATM 4427 O  O   . HOH K 6 .   ? -12.574 -9.590  6.368   1.00 19.90  ? 413 HOH A O   1 
HETATM 4428 O  O   . HOH K 6 .   ? -8.878  -2.256  0.089   1.00 9.68   ? 414 HOH A O   1 
HETATM 4429 O  O   . HOH K 6 .   ? -12.793 -2.510  8.159   1.00 23.47  ? 415 HOH A O   1 
HETATM 4430 O  O   . HOH K 6 .   ? 14.018  -12.394 -3.878  1.00 37.78  ? 416 HOH A O   1 
HETATM 4431 O  O   . HOH K 6 .   ? 10.369  10.146  -14.360 1.00 28.96  ? 417 HOH A O   1 
HETATM 4432 O  O   . HOH K 6 .   ? -14.586 0.709   21.249  1.00 33.03  ? 418 HOH A O   1 
HETATM 4433 O  O   . HOH K 6 .   ? 10.878  -4.968  17.909  1.00 57.73  ? 419 HOH A O   1 
HETATM 4434 O  O   . HOH K 6 .   ? 2.685   15.046  -15.999 1.00 31.59  ? 420 HOH A O   1 
HETATM 4435 O  O   . HOH K 6 .   ? 8.173   -19.521 10.463  1.00 77.18  ? 421 HOH A O   1 
HETATM 4436 O  O   . HOH K 6 .   ? -14.482 -4.793  7.931   1.00 27.08  ? 422 HOH A O   1 
HETATM 4437 O  O   . HOH K 6 .   ? -3.715  -2.830  22.292  1.00 24.91  ? 423 HOH A O   1 
HETATM 4438 O  O   . HOH K 6 .   ? -21.293 -5.257  -6.587  1.00 32.94  ? 424 HOH A O   1 
HETATM 4439 O  O   . HOH K 6 .   ? -0.076  17.677  -13.773 1.00 27.36  ? 425 HOH A O   1 
HETATM 4440 O  O   . HOH K 6 .   ? -15.381 3.050   13.535  1.00 40.03  ? 426 HOH A O   1 
HETATM 4441 O  O   . HOH K 6 .   ? -17.460 -6.208  17.080  1.00 23.89  ? 427 HOH A O   1 
HETATM 4442 O  O   . HOH K 6 .   ? -12.245 9.882   -12.102 1.00 35.67  ? 428 HOH A O   1 
HETATM 4443 O  O   . HOH K 6 .   ? -7.357  -17.575 9.494   1.00 27.18  ? 429 HOH A O   1 
HETATM 4444 O  O   . HOH K 6 .   ? 2.332   14.336  -13.370 1.00 27.07  ? 430 HOH A O   1 
HETATM 4445 O  O   . HOH K 6 .   ? 4.247   -14.756 -13.258 1.00 20.98  ? 431 HOH A O   1 
HETATM 4446 O  O   . HOH K 6 .   ? 1.870   12.535  9.620   1.00 37.58  ? 432 HOH A O   1 
HETATM 4447 O  O   . HOH K 6 .   ? 9.897   -14.874 12.781  1.00 26.21  ? 433 HOH A O   1 
HETATM 4448 O  O   . HOH K 6 .   ? -1.387  -1.989  7.927   1.00 10.06  ? 434 HOH A O   1 
HETATM 4449 O  O   . HOH K 6 .   ? -0.960  7.702   -13.238 1.00 16.21  ? 435 HOH A O   1 
HETATM 4450 O  O   . HOH K 6 .   ? 13.868  -0.999  -13.353 1.00 57.10  ? 436 HOH A O   1 
HETATM 4451 O  O   . HOH K 6 .   ? -16.452 -3.700  12.024  1.00 27.82  ? 437 HOH A O   1 
HETATM 4452 O  O   . HOH K 6 .   ? 15.493  0.692   -19.325 1.00 35.92  ? 438 HOH A O   1 
HETATM 4453 O  O   . HOH K 6 .   ? -18.125 -3.634  26.374  1.00 37.63  ? 439 HOH A O   1 
HETATM 4454 O  O   . HOH K 6 .   ? 17.391  4.163   -7.671  1.00 72.48  ? 440 HOH A O   1 
HETATM 4455 O  O   . HOH K 6 .   ? 3.705   16.409  9.581   1.00 39.72  ? 441 HOH A O   1 
HETATM 4456 O  O   . HOH K 6 .   ? -3.037  7.877   9.592   1.00 16.50  ? 442 HOH A O   1 
HETATM 4457 O  O   . HOH K 6 .   ? 15.558  -13.553 7.734   1.00 37.84  ? 443 HOH A O   1 
HETATM 4458 O  O   . HOH K 6 .   ? 12.069  -16.482 2.216   1.00 19.69  ? 444 HOH A O   1 
HETATM 4459 O  O   . HOH K 6 .   ? -14.433 -1.607  -10.753 1.00 18.94  ? 445 HOH A O   1 
HETATM 4460 O  O   . HOH K 6 .   ? 14.082  10.387  -4.405  1.00 19.64  ? 446 HOH A O   1 
HETATM 4461 O  O   . HOH K 6 .   ? 6.265   -13.681 -17.005 1.00 38.48  ? 447 HOH A O   1 
HETATM 4462 O  O   . HOH K 6 .   ? 8.538   -19.380 1.129   1.00 19.71  ? 448 HOH A O   1 
HETATM 4463 O  O   . HOH K 6 .   ? 0.418   14.977  7.085   1.00 31.91  ? 449 HOH A O   1 
HETATM 4464 O  O   . HOH K 6 .   ? -13.735 6.823   -14.075 1.00 17.53  ? 450 HOH A O   1 
HETATM 4465 O  O   . HOH K 6 .   ? 2.947   -20.429 7.219   1.00 21.67  ? 451 HOH A O   1 
HETATM 4466 O  O   . HOH K 6 .   ? 6.709   -12.126 -10.606 1.00 18.61  ? 452 HOH A O   1 
HETATM 4467 O  O   . HOH K 6 .   ? 0.513   10.509  -9.765  1.00 9.64   ? 453 HOH A O   1 
HETATM 4468 O  O   . HOH K 6 .   ? -16.309 -9.348  0.291   1.00 31.27  ? 454 HOH A O   1 
HETATM 4469 O  O   . HOH K 6 .   ? -3.288  -13.132 -15.801 1.00 26.80  ? 455 HOH A O   1 
HETATM 4470 O  O   . HOH K 6 .   ? 11.839  -12.339 -2.965  1.00 30.57  ? 456 HOH A O   1 
HETATM 4471 O  O   . HOH K 6 .   ? 15.793  -4.189  2.708   1.00 31.14  ? 457 HOH A O   1 
HETATM 4472 O  O   . HOH K 6 .   ? -7.630  -6.920  -13.344 1.00 10.62  ? 458 HOH A O   1 
HETATM 4473 O  O   . HOH K 6 .   ? -2.156  -13.620 4.453   1.00 10.31  ? 459 HOH A O   1 
HETATM 4474 O  O   . HOH K 6 .   ? 12.919  -12.976 -0.260  1.00 30.19  ? 460 HOH A O   1 
HETATM 4475 O  O   . HOH K 6 .   ? -11.941 -13.876 6.534   1.00 20.82  ? 461 HOH A O   1 
HETATM 4476 O  O   . HOH K 6 .   ? 15.849  7.947   -11.233 1.00 24.11  ? 462 HOH A O   1 
HETATM 4477 O  O   . HOH K 6 .   ? 0.303   -16.457 -1.298  1.00 11.38  ? 463 HOH A O   1 
HETATM 4478 O  O   . HOH K 6 .   ? -15.761 -10.862 4.026   1.00 40.63  ? 464 HOH A O   1 
HETATM 4479 O  O   . HOH K 6 .   ? 9.596   16.815  -0.796  1.00 26.77  ? 465 HOH A O   1 
HETATM 4480 O  O   . HOH K 6 .   ? -5.422  -10.183 -16.327 1.00 19.44  ? 466 HOH A O   1 
HETATM 4481 O  O   . HOH K 6 .   ? -6.356  -11.165 18.717  1.00 21.74  ? 467 HOH A O   1 
HETATM 4482 O  O   . HOH K 6 .   ? -13.504 -11.652 3.603   1.00 48.18  ? 468 HOH A O   1 
HETATM 4483 O  O   . HOH K 6 .   ? -10.121 2.869   -18.750 1.00 26.13  ? 469 HOH A O   1 
HETATM 4484 O  O   . HOH K 6 .   ? 5.796   5.321   -19.343 1.00 33.29  ? 470 HOH A O   1 
HETATM 4485 O  O   . HOH K 6 .   ? -10.107 0.708   20.623  1.00 15.71  ? 471 HOH A O   1 
HETATM 4486 O  O   . HOH K 6 .   ? 14.146  1.842   14.431  1.00 29.16  ? 472 HOH A O   1 
HETATM 4487 O  O   . HOH K 6 .   ? 6.914   -12.262 -21.818 1.00 30.62  ? 473 HOH A O   1 
HETATM 4488 O  O   . HOH K 6 .   ? -1.446  2.447   22.394  1.00 28.47  ? 474 HOH A O   1 
HETATM 4489 O  O   . HOH K 6 .   ? 8.506   5.968   19.490  1.00 77.55  ? 475 HOH A O   1 
HETATM 4490 O  O   . HOH K 6 .   ? 17.050  -11.204 -4.681  1.00 42.84  ? 476 HOH A O   1 
HETATM 4491 O  O   . HOH K 6 .   ? 13.308  -9.217  -1.362  1.00 26.93  ? 477 HOH A O   1 
HETATM 4492 O  O   . HOH K 6 .   ? -11.420 -9.973  -9.297  1.00 24.65  ? 478 HOH A O   1 
HETATM 4493 O  O   . HOH K 6 .   ? 0.724   10.370  8.112   1.00 19.20  ? 479 HOH A O   1 
HETATM 4494 O  O   . HOH K 6 .   ? 3.151   -20.571 3.657   1.00 56.58  ? 480 HOH A O   1 
HETATM 4495 O  O   . HOH K 6 .   ? 8.510   -10.565 19.320  1.00 28.26  ? 481 HOH A O   1 
HETATM 4496 O  O   . HOH K 6 .   ? 5.513   10.728  18.052  1.00 26.78  ? 482 HOH A O   1 
HETATM 4497 O  O   . HOH K 6 .   ? 6.916   -6.602  -4.610  1.00 8.65   ? 483 HOH A O   1 
HETATM 4498 O  O   . HOH K 6 .   ? 16.077  5.188   0.269   1.00 24.51  ? 484 HOH A O   1 
HETATM 4499 O  O   . HOH K 6 .   ? -15.524 8.919   -4.566  1.00 16.67  ? 485 HOH A O   1 
HETATM 4500 O  O   . HOH K 6 .   ? 10.246  12.527  -11.023 1.00 17.86  ? 486 HOH A O   1 
HETATM 4501 O  O   . HOH K 6 .   ? 14.810  -9.247  -8.374  1.00 40.29  ? 487 HOH A O   1 
HETATM 4502 O  O   . HOH K 6 .   ? 0.994   -17.675 8.611   1.00 24.04  ? 488 HOH A O   1 
HETATM 4503 O  O   . HOH K 6 .   ? 9.273   11.829  6.882   1.00 14.36  ? 489 HOH A O   1 
HETATM 4504 O  O   . HOH K 6 .   ? -2.815  -14.989 14.337  1.00 19.99  ? 490 HOH A O   1 
HETATM 4505 O  O   . HOH K 6 .   ? -6.620  -9.369  -5.092  1.00 8.88   ? 491 HOH A O   1 
HETATM 4506 O  O   . HOH K 6 .   ? 6.346   6.874   23.845  1.00 52.90  ? 492 HOH A O   1 
HETATM 4507 O  O   . HOH K 6 .   ? -17.034 1.223   16.884  1.00 41.08  ? 493 HOH A O   1 
HETATM 4508 O  O   . HOH K 6 .   ? -11.272 16.623  -8.423  1.00 33.16  ? 494 HOH A O   1 
HETATM 4509 O  O   . HOH K 6 .   ? 15.442  -8.806  -1.875  1.00 22.43  ? 495 HOH A O   1 
HETATM 4510 O  O   . HOH K 6 .   ? 7.933   12.545  4.483   1.00 17.23  ? 496 HOH A O   1 
HETATM 4511 O  O   . HOH K 6 .   ? -5.580  -11.723 -2.250  1.00 9.23   ? 497 HOH A O   1 
HETATM 4512 O  O   . HOH K 6 .   ? 9.899   17.671  -3.197  1.00 25.25  ? 498 HOH A O   1 
HETATM 4513 O  O   . HOH K 6 .   ? 7.847   22.535  7.785   1.00 13.60  ? 499 HOH A O   1 
HETATM 4514 O  O   . HOH K 6 .   ? -5.896  -6.681  -15.386 1.00 18.49  ? 500 HOH A O   1 
HETATM 4515 O  O   . HOH K 6 .   ? -10.370 -17.726 4.867   1.00 31.80  ? 501 HOH A O   1 
HETATM 4516 O  O   . HOH K 6 .   ? 4.960   21.873  -1.943  1.00 17.39  ? 502 HOH A O   1 
HETATM 4517 O  O   . HOH K 6 .   ? 12.723  -4.107  13.115  1.00 20.35  ? 503 HOH A O   1 
HETATM 4518 O  O   . HOH K 6 .   ? 8.456   -1.986  18.447  1.00 27.03  ? 504 HOH A O   1 
HETATM 4519 O  O   . HOH K 6 .   ? -9.622  12.628  -7.571  1.00 17.20  ? 505 HOH A O   1 
HETATM 4520 O  O   . HOH K 6 .   ? 3.722   12.131  -12.164 1.00 17.01  ? 506 HOH A O   1 
HETATM 4521 O  O   . HOH K 6 .   ? 13.116  1.605   -18.819 1.00 29.83  ? 507 HOH A O   1 
HETATM 4522 O  O   . HOH K 6 .   ? 11.503  -5.393  -7.820  1.00 11.89  ? 508 HOH A O   1 
HETATM 4523 O  O   . HOH K 6 .   ? -17.810 0.644   21.458  1.00 32.71  ? 509 HOH A O   1 
HETATM 4524 O  O   . HOH K 6 .   ? -9.104  -4.247  -20.616 1.00 26.05  ? 510 HOH A O   1 
HETATM 4525 O  O   . HOH K 6 .   ? -9.661  15.753  -0.250  1.00 29.25  ? 511 HOH A O   1 
HETATM 4526 O  O   . HOH K 6 .   ? -3.327  22.737  -3.744  1.00 12.72  ? 512 HOH A O   1 
HETATM 4527 O  O   . HOH K 6 .   ? 3.336   -16.708 1.202   1.00 14.09  ? 513 HOH A O   1 
HETATM 4528 O  O   . HOH K 6 .   ? -9.773  2.840   26.768  1.00 30.06  ? 514 HOH A O   1 
HETATM 4529 O  O   . HOH K 6 .   ? -25.465 -0.717  1.309   1.00 22.43  ? 515 HOH A O   1 
HETATM 4530 O  O   . HOH K 6 .   ? 7.347   -14.395 -6.197  1.00 20.37  ? 516 HOH A O   1 
HETATM 4531 O  O   . HOH K 6 .   ? -21.876 1.515   -0.249  1.00 25.77  ? 517 HOH A O   1 
HETATM 4532 O  O   . HOH K 6 .   ? 13.317  -11.424 4.507   1.00 18.79  ? 518 HOH A O   1 
HETATM 4533 O  O   . HOH K 6 .   ? 4.590   -16.731 -2.939  1.00 13.34  ? 519 HOH A O   1 
HETATM 4534 O  O   . HOH K 6 .   ? -13.658 4.462   7.696   1.00 37.07  ? 520 HOH A O   1 
HETATM 4535 O  O   . HOH K 6 .   ? -6.306  -14.093 -8.581  1.00 12.48  ? 521 HOH A O   1 
HETATM 4536 O  O   . HOH K 6 .   ? 3.822   16.005  -11.457 1.00 23.18  ? 522 HOH A O   1 
HETATM 4537 O  O   . HOH K 6 .   ? -2.737  -6.867  -16.835 1.00 15.82  ? 523 HOH A O   1 
HETATM 4538 O  O   . HOH K 6 .   ? 14.762  -5.927  6.745   1.00 18.58  ? 524 HOH A O   1 
HETATM 4539 O  O   . HOH K 6 .   ? 11.815  7.500   11.075  1.00 19.00  ? 525 HOH A O   1 
HETATM 4540 O  O   . HOH K 6 .   ? 9.704   -2.555  -25.600 1.00 86.13  ? 526 HOH A O   1 
HETATM 4541 O  O   . HOH K 6 .   ? -12.584 -11.398 10.551  1.00 18.79  ? 527 HOH A O   1 
HETATM 4542 O  O   . HOH K 6 .   ? 15.748  -4.788  -17.956 1.00 50.28  ? 528 HOH A O   1 
HETATM 4543 O  O   . HOH K 6 .   ? 5.943   -10.510 -8.638  1.00 13.76  ? 529 HOH A O   1 
HETATM 4544 O  O   . HOH K 6 .   ? -16.783 -0.167  23.836  1.00 35.17  ? 530 HOH A O   1 
HETATM 4545 O  O   . HOH K 6 .   ? -18.737 -2.022  -5.271  1.00 14.39  ? 531 HOH A O   1 
HETATM 4546 O  O   . HOH K 6 .   ? 14.034  -16.050 8.979   1.00 57.55  ? 532 HOH A O   1 
HETATM 4547 O  O   . HOH K 6 .   ? -6.752  -11.460 -9.359  1.00 10.27  ? 533 HOH A O   1 
HETATM 4548 O  O   . HOH K 6 .   ? 3.774   21.751  0.593   1.00 17.47  ? 534 HOH A O   1 
HETATM 4549 O  O   . HOH K 6 .   ? 6.218   -8.103  -17.184 1.00 17.70  ? 535 HOH A O   1 
HETATM 4550 O  O   . HOH K 6 .   ? 4.856   7.954   -16.999 1.00 35.37  ? 536 HOH A O   1 
HETATM 4551 O  O   . HOH K 6 .   ? 0.564   23.559  -4.305  1.00 16.17  ? 537 HOH A O   1 
HETATM 4552 O  O   . HOH K 6 .   ? 5.012   11.216  -16.030 1.00 40.78  ? 538 HOH A O   1 
HETATM 4553 O  O   . HOH K 6 .   ? -23.533 2.078   -8.750  1.00 20.95  ? 539 HOH A O   1 
HETATM 4554 O  O   . HOH K 6 .   ? 12.154  5.643   18.895  1.00 57.50  ? 540 HOH A O   1 
HETATM 4555 O  O   . HOH K 6 .   ? 6.124   17.671  -7.969  1.00 16.70  ? 541 HOH A O   1 
HETATM 4556 O  O   . HOH K 6 .   ? -2.065  20.795  5.364   1.00 17.17  ? 542 HOH A O   1 
HETATM 4557 O  O   . HOH K 6 .   ? 5.338   21.098  2.656   1.00 15.18  ? 543 HOH A O   1 
HETATM 4558 O  O   . HOH K 6 .   ? -3.447  -3.520  -21.634 1.00 17.29  ? 544 HOH A O   1 
HETATM 4559 O  O   . HOH K 6 .   ? 2.895   -7.035  19.084  1.00 29.19  ? 545 HOH A O   1 
HETATM 4560 O  O   . HOH K 6 .   ? -5.381  -14.090 15.129  1.00 21.61  ? 546 HOH A O   1 
HETATM 4561 O  O   . HOH K 6 .   ? -7.656  -17.356 -5.698  1.00 29.69  ? 547 HOH A O   1 
HETATM 4562 O  O   . HOH K 6 .   ? 13.210  -1.222  9.137   1.00 21.71  ? 548 HOH A O   1 
HETATM 4563 O  O   . HOH K 6 .   ? 2.928   -15.067 -10.880 1.00 13.67  ? 549 HOH A O   1 
HETATM 4564 O  O   . HOH K 6 .   ? -10.145 -12.456 -15.419 1.00 31.26  ? 550 HOH A O   1 
HETATM 4565 O  O   . HOH K 6 .   ? -15.018 -3.036  -5.182  1.00 13.53  ? 551 HOH A O   1 
HETATM 4566 O  O   . HOH K 6 .   ? 1.875   4.544   -15.090 1.00 19.07  ? 552 HOH A O   1 
HETATM 4567 O  O   . HOH K 6 .   ? -18.353 5.061   -11.958 1.00 30.58  ? 553 HOH A O   1 
HETATM 4568 O  O   . HOH K 6 .   ? -19.112 -9.791  9.106   1.00 33.46  ? 554 HOH A O   1 
HETATM 4569 O  O   . HOH K 6 .   ? -25.913 4.665   -5.146  1.00 31.76  ? 555 HOH A O   1 
HETATM 4570 O  O   . HOH K 6 .   ? -11.628 -4.515  -18.608 1.00 27.61  ? 556 HOH A O   1 
HETATM 4571 O  O   . HOH K 6 .   ? 3.451   0.985   22.055  1.00 30.56  ? 557 HOH A O   1 
HETATM 4572 O  O   . HOH K 6 .   ? -11.371 10.608  -8.555  1.00 18.94  ? 558 HOH A O   1 
HETATM 4573 O  O   . HOH K 6 .   ? -1.571  -18.038 -10.921 1.00 19.67  ? 559 HOH A O   1 
HETATM 4574 O  O   . HOH K 6 .   ? -15.065 -1.734  12.847  1.00 28.87  ? 560 HOH A O   1 
HETATM 4575 O  O   . HOH K 6 .   ? -21.393 3.134   -10.245 1.00 24.40  ? 561 HOH A O   1 
HETATM 4576 O  O   . HOH K 6 .   ? 12.587  -7.753  -9.565  1.00 19.21  ? 562 HOH A O   1 
HETATM 4577 O  O   . HOH K 6 .   ? -2.936  -6.757  22.906  1.00 35.12  ? 563 HOH A O   1 
HETATM 4578 O  O   . HOH K 6 .   ? -19.683 3.738   3.567   1.00 33.43  ? 564 HOH A O   1 
HETATM 4579 O  O   . HOH K 6 .   ? 16.789  -2.198  -9.307  1.00 21.45  ? 565 HOH A O   1 
HETATM 4580 O  O   . HOH K 6 .   ? -9.040  -15.640 -2.200  1.00 27.87  ? 566 HOH A O   1 
HETATM 4581 O  O   . HOH K 6 .   ? 2.495   -16.553 -16.499 1.00 26.32  ? 567 HOH A O   1 
HETATM 4582 O  O   . HOH K 6 .   ? -3.769  -17.930 -8.051  1.00 22.27  ? 568 HOH A O   1 
HETATM 4583 O  O   . HOH K 6 .   ? 13.909  1.084   -10.729 1.00 16.53  ? 569 HOH A O   1 
HETATM 4584 O  O   . HOH K 6 .   ? -0.554  -8.340  17.102  1.00 26.03  ? 570 HOH A O   1 
HETATM 4585 O  O   . HOH K 6 .   ? -9.663  -6.692  -16.804 1.00 23.47  ? 571 HOH A O   1 
HETATM 4586 O  O   . HOH K 6 .   ? -14.936 -11.296 21.531  1.00 19.15  ? 572 HOH A O   1 
HETATM 4587 O  O   . HOH K 6 .   ? 0.518   22.644  -9.209  1.00 16.66  ? 573 HOH A O   1 
HETATM 4588 O  O   . HOH K 6 .   ? -23.142 -1.969  2.271   1.00 28.49  ? 574 HOH A O   1 
HETATM 4589 O  O   . HOH K 6 .   ? -9.882  -12.501 -6.361  1.00 20.71  ? 575 HOH A O   1 
HETATM 4590 O  O   . HOH K 6 .   ? 2.688   9.670   -13.195 1.00 21.73  ? 576 HOH A O   1 
HETATM 4591 O  O   . HOH K 6 .   ? -15.894 2.639   7.376   1.00 29.32  ? 577 HOH A O   1 
HETATM 4592 O  O   . HOH K 6 .   ? -11.379 0.284   -13.699 1.00 14.22  ? 578 HOH A O   1 
HETATM 4593 O  O   . HOH K 6 .   ? 13.763  1.035   11.872  1.00 23.02  ? 579 HOH A O   1 
HETATM 4594 O  O   . HOH K 6 .   ? 16.257  -5.827  -14.791 1.00 75.28  ? 580 HOH A O   1 
HETATM 4595 O  O   . HOH K 6 .   ? -1.570  0.374   -25.527 1.00 39.19  ? 581 HOH A O   1 
HETATM 4596 O  O   . HOH K 6 .   ? 0.057   16.566  3.631   1.00 19.44  ? 582 HOH A O   1 
HETATM 4597 O  O   . HOH K 6 .   ? -1.004  -3.985  -20.213 1.00 17.97  ? 583 HOH A O   1 
HETATM 4598 O  O   . HOH K 6 .   ? -1.750  9.462   7.597   1.00 25.36  ? 584 HOH A O   1 
HETATM 4599 O  O   . HOH K 6 .   ? 11.212  -17.797 9.108   1.00 23.99  ? 585 HOH A O   1 
HETATM 4600 O  O   . HOH K 6 .   ? 2.841   5.371   22.672  1.00 24.27  ? 586 HOH A O   1 
HETATM 4601 O  O   . HOH K 6 .   ? 12.878  -9.857  1.692   1.00 20.27  ? 587 HOH A O   1 
HETATM 4602 O  O   . HOH K 6 .   ? -12.913 -12.774 14.594  1.00 30.35  ? 588 HOH A O   1 
HETATM 4603 O  O   . HOH K 6 .   ? -15.254 -5.431  -6.530  1.00 26.97  ? 589 HOH A O   1 
HETATM 4604 O  O   . HOH K 6 .   ? 1.080   2.950   -17.637 1.00 22.71  ? 590 HOH A O   1 
HETATM 4605 O  O   . HOH K 6 .   ? -8.073  -10.503 -7.077  1.00 10.10  ? 591 HOH A O   1 
HETATM 4606 O  O   . HOH K 6 .   ? -3.352  16.476  -13.354 1.00 35.29  ? 592 HOH A O   1 
HETATM 4607 O  O   . HOH K 6 .   ? -24.890 -5.128  8.065   1.00 74.39  ? 593 HOH A O   1 
HETATM 4608 O  O   . HOH K 6 .   ? -17.787 7.874   -5.920  1.00 15.97  ? 594 HOH A O   1 
HETATM 4609 O  O   . HOH K 6 .   ? -24.082 7.526   -3.614  1.00 34.98  ? 595 HOH A O   1 
HETATM 4610 O  O   . HOH K 6 .   ? -4.329  17.302  3.900   1.00 74.48  ? 596 HOH A O   1 
HETATM 4611 O  O   . HOH K 6 .   ? -3.137  3.364   -19.450 1.00 23.54  ? 597 HOH A O   1 
HETATM 4612 O  O   . HOH K 6 .   ? -9.068  10.789  -12.732 1.00 109.90 ? 598 HOH A O   1 
HETATM 4613 O  O   . HOH K 6 .   ? -23.189 -3.977  -8.599  1.00 25.70  ? 599 HOH A O   1 
HETATM 4614 O  O   . HOH K 6 .   ? -0.526  -6.121  -18.352 1.00 20.62  ? 600 HOH A O   1 
HETATM 4615 O  O   . HOH K 6 .   ? -20.238 -6.920  7.625   1.00 23.09  ? 601 HOH A O   1 
HETATM 4616 O  O   . HOH K 6 .   ? 14.661  -7.675  13.897  1.00 23.96  ? 602 HOH A O   1 
HETATM 4617 O  O   . HOH K 6 .   ? 1.076   19.340  3.544   1.00 22.56  ? 603 HOH A O   1 
HETATM 4618 O  O   . HOH K 6 .   ? 6.682   20.694  -6.537  1.00 76.84  ? 604 HOH A O   1 
HETATM 4619 O  O   . HOH K 6 .   ? 11.541  20.990  -1.742  1.00 105.84 ? 605 HOH A O   1 
HETATM 4620 O  O   . HOH K 6 .   ? 5.081   -18.243 -7.398  1.00 33.61  ? 606 HOH A O   1 
HETATM 4621 O  O   . HOH K 6 .   ? -16.522 -4.053  9.208   1.00 32.30  ? 607 HOH A O   1 
HETATM 4622 O  O   . HOH K 6 .   ? -2.642  -6.952  18.299  1.00 28.16  ? 608 HOH A O   1 
HETATM 4623 O  O   . HOH K 6 .   ? 8.408   -7.159  -18.873 1.00 32.48  ? 609 HOH A O   1 
HETATM 4624 O  O   . HOH K 6 .   ? -10.531 2.403   22.640  1.00 31.86  ? 610 HOH A O   1 
HETATM 4625 O  O   . HOH K 6 .   ? -8.628  13.242  -10.142 1.00 29.97  ? 611 HOH A O   1 
HETATM 4626 O  O   . HOH K 6 .   ? -7.134  6.187   7.626   1.00 78.94  ? 612 HOH A O   1 
HETATM 4627 O  O   . HOH K 6 .   ? -10.056 -0.727  -23.802 1.00 58.58  ? 613 HOH A O   1 
HETATM 4628 O  O   . HOH K 6 .   ? -7.314  -13.144 -17.031 1.00 25.93  ? 614 HOH A O   1 
HETATM 4629 O  O   . HOH K 6 .   ? -20.287 -0.790  1.914   1.00 28.59  ? 615 HOH A O   1 
HETATM 4630 O  O   . HOH K 6 .   ? 13.481  9.957   12.284  1.00 27.28  ? 616 HOH A O   1 
HETATM 4631 O  O   . HOH K 6 .   ? 2.811   -15.405 -1.116  1.00 11.88  ? 617 HOH A O   1 
HETATM 4632 O  O   . HOH K 6 .   ? 15.439  6.313   11.680  1.00 48.08  ? 618 HOH A O   1 
HETATM 4633 O  O   . HOH K 6 .   ? -9.959  -13.834 -11.220 1.00 39.58  ? 619 HOH A O   1 
HETATM 4634 O  O   . HOH K 6 .   ? -19.920 -3.738  21.770  1.00 49.90  ? 620 HOH A O   1 
HETATM 4635 O  O   . HOH K 6 .   ? -18.765 -2.932  -7.972  1.00 26.63  ? 621 HOH A O   1 
HETATM 4636 O  O   . HOH K 6 .   ? 15.207  12.921  -3.862  1.00 30.53  ? 622 HOH A O   1 
HETATM 4637 O  O   . HOH K 6 .   ? -21.995 -4.787  7.910   1.00 27.53  ? 623 HOH A O   1 
HETATM 4638 O  O   . HOH K 6 .   ? 11.794  -19.800 3.683   1.00 28.83  ? 624 HOH A O   1 
HETATM 4639 O  O   . HOH K 6 .   ? -15.536 -9.014  -3.189  1.00 35.94  ? 625 HOH A O   1 
HETATM 4640 O  O   . HOH K 6 .   ? -1.934  23.603  -5.884  1.00 14.03  ? 626 HOH A O   1 
HETATM 4641 O  O   . HOH K 6 .   ? 5.247   -14.428 -9.809  1.00 33.51  ? 627 HOH A O   1 
HETATM 4642 O  O   . HOH K 6 .   ? -8.651  -11.296 -11.367 1.00 23.13  ? 628 HOH A O   1 
HETATM 4643 O  O   . HOH K 6 .   ? 7.696   21.754  -1.763  1.00 21.47  ? 629 HOH A O   1 
HETATM 4644 O  O   . HOH K 6 .   ? -14.724 -9.487  23.403  1.00 38.55  ? 630 HOH A O   1 
HETATM 4645 O  O   . HOH K 6 .   ? -16.431 -3.883  -11.468 1.00 43.34  ? 631 HOH A O   1 
HETATM 4646 O  O   . HOH K 6 .   ? -20.361 7.378   2.704   1.00 40.62  ? 632 HOH A O   1 
HETATM 4647 O  O   . HOH K 6 .   ? 14.992  10.857  -10.800 1.00 91.16  ? 633 HOH A O   1 
HETATM 4648 O  O   . HOH K 6 .   ? 18.032  6.665   -8.989  1.00 107.85 ? 634 HOH A O   1 
HETATM 4649 O  O   . HOH K 6 .   ? -8.185  -15.694 -9.677  1.00 26.91  ? 635 HOH A O   1 
HETATM 4650 O  O   . HOH K 6 .   ? -5.191  22.290  -5.664  1.00 23.46  ? 636 HOH A O   1 
HETATM 4651 O  O   . HOH K 6 .   ? -12.965 -11.749 7.761   1.00 25.06  ? 637 HOH A O   1 
HETATM 4652 O  O   . HOH K 6 .   ? -0.318  3.387   -23.188 1.00 25.38  ? 638 HOH A O   1 
HETATM 4653 O  O   . HOH K 6 .   ? 0.462   6.722   -15.061 1.00 24.82  ? 639 HOH A O   1 
HETATM 4654 O  O   . HOH K 6 .   ? 6.856   -16.137 -4.384  1.00 24.55  ? 640 HOH A O   1 
HETATM 4655 O  O   . HOH K 6 .   ? 19.608  1.250   3.820   1.00 56.34  ? 641 HOH A O   1 
HETATM 4656 O  O   . HOH K 6 .   ? 3.992   5.417   -17.401 1.00 26.27  ? 642 HOH A O   1 
HETATM 4657 O  O   . HOH K 6 .   ? -10.750 -14.020 -8.366  1.00 34.17  ? 643 HOH A O   1 
HETATM 4658 O  O   . HOH K 6 .   ? -8.006  -10.113 -15.778 1.00 28.35  ? 644 HOH A O   1 
HETATM 4659 O  O   . HOH K 6 .   ? 9.761   -0.368  -27.337 1.00 38.00  ? 645 HOH A O   1 
HETATM 4660 O  O   . HOH K 6 .   ? -0.821  4.808   -19.020 1.00 22.78  ? 646 HOH A O   1 
HETATM 4661 O  O   . HOH K 6 .   ? 14.030  -5.289  15.450  1.00 30.41  ? 647 HOH A O   1 
HETATM 4662 O  O   . HOH K 6 .   ? 14.160  15.681  -4.713  1.00 42.43  ? 648 HOH A O   1 
HETATM 4663 O  O   . HOH K 6 .   ? -11.891 14.198  -6.798  1.00 27.77  ? 649 HOH A O   1 
HETATM 4664 O  O   . HOH K 6 .   ? -12.004 -12.367 -4.544  1.00 33.11  ? 650 HOH A O   1 
HETATM 4665 O  O   . HOH K 6 .   ? 7.711   -10.292 -15.652 1.00 30.31  ? 651 HOH A O   1 
HETATM 4666 O  O   . HOH K 6 .   ? -4.094  -19.014 -10.473 1.00 27.63  ? 652 HOH A O   1 
HETATM 4667 O  O   . HOH K 6 .   ? -2.515  -8.437  19.985  1.00 39.05  ? 653 HOH A O   1 
HETATM 4668 O  O   . HOH K 6 .   ? -11.559 -15.721 8.660   1.00 29.67  ? 654 HOH A O   1 
HETATM 4669 O  O   . HOH K 6 .   ? 1.383   2.887   23.626  1.00 37.36  ? 655 HOH A O   1 
HETATM 4670 O  O   . HOH K 6 .   ? -11.650 5.033   20.686  1.00 37.25  ? 656 HOH A O   1 
HETATM 4671 O  O   . HOH K 6 .   ? -5.317  -7.876  -18.034 1.00 38.45  ? 657 HOH A O   1 
HETATM 4672 O  O   . HOH K 6 .   ? -13.249 8.282   -16.386 1.00 34.64  ? 658 HOH A O   1 
HETATM 4673 O  O   . HOH K 6 .   ? -8.949  -9.333  -13.212 1.00 16.23  ? 659 HOH A O   1 
HETATM 4674 O  O   . HOH K 6 .   ? -1.030  6.968   -17.206 1.00 24.98  ? 660 HOH A O   1 
HETATM 4675 O  O   . HOH K 6 .   ? -6.013  -13.787 18.126  1.00 31.87  ? 661 HOH A O   1 
HETATM 4676 O  O   . HOH K 6 .   ? 11.196  -18.823 1.111   1.00 31.20  ? 662 HOH A O   1 
HETATM 4677 O  O   . HOH K 6 .   ? -16.388 7.227   -13.296 1.00 62.09  ? 663 HOH A O   1 
HETATM 4678 O  O   . HOH K 6 .   ? -8.683  -15.650 10.907  1.00 34.39  ? 664 HOH A O   1 
HETATM 4679 O  O   . HOH K 6 .   ? 16.733  0.537   -10.202 1.00 20.27  ? 665 HOH A O   1 
HETATM 4680 O  O   . HOH K 6 .   ? 2.817   -17.706 -10.362 1.00 21.15  ? 666 HOH A O   1 
HETATM 4681 O  O   . HOH K 6 .   ? -21.790 2.352   -12.796 1.00 48.54  ? 667 HOH A O   1 
HETATM 4682 O  O   . HOH K 6 .   ? -17.186 -12.722 22.001  1.00 16.91  ? 668 HOH A O   1 
HETATM 4683 O  O   . HOH K 6 .   ? -24.209 0.283   -12.637 1.00 31.50  ? 669 HOH A O   1 
HETATM 4684 O  O   . HOH K 6 .   ? -7.564  8.075   1.798   1.00 30.19  ? 670 HOH A O   1 
HETATM 4685 O  O   . HOH K 6 .   ? -18.653 -14.230 8.667   1.00 43.08  ? 671 HOH A O   1 
HETATM 4686 O  O   . HOH K 6 .   ? -13.856 11.725  -8.027  1.00 29.25  ? 672 HOH A O   1 
HETATM 4687 O  O   . HOH K 6 .   ? 19.815  6.136   -11.705 1.00 32.98  ? 673 HOH A O   1 
HETATM 4688 O  O   . HOH L 6 .   ? -30.095 38.301  34.912  1.00 26.53  ? 401 HOH B O   1 
HETATM 4689 O  O   . HOH L 6 .   ? -35.426 31.774  28.897  1.00 32.02  ? 402 HOH B O   1 
HETATM 4690 O  O   . HOH L 6 .   ? -13.597 40.604  36.856  1.00 24.83  ? 403 HOH B O   1 
HETATM 4691 O  O   . HOH L 6 .   ? -20.562 16.524  54.075  1.00 27.22  ? 404 HOH B O   1 
HETATM 4692 O  O   . HOH L 6 .   ? -16.396 10.674  52.244  1.00 32.33  ? 405 HOH B O   1 
HETATM 4693 O  O   . HOH L 6 .   ? -24.699 13.883  10.301  1.00 47.98  ? 406 HOH B O   1 
HETATM 4694 O  O   . HOH L 6 .   ? -1.151  9.229   32.026  1.00 43.36  ? 407 HOH B O   1 
HETATM 4695 O  O   . HOH L 6 .   ? -11.218 46.042  33.841  1.00 27.32  ? 408 HOH B O   1 
HETATM 4696 O  O   . HOH L 6 .   ? -19.140 28.977  11.705  1.00 28.12  ? 409 HOH B O   1 
HETATM 4697 O  O   . HOH L 6 .   ? -21.171 7.245   49.957  1.00 24.61  ? 410 HOH B O   1 
HETATM 4698 O  O   . HOH L 6 .   ? -13.404 22.165  57.634  1.00 45.56  ? 411 HOH B O   1 
HETATM 4699 O  O   . HOH L 6 .   ? -27.998 0.297   21.866  1.00 17.86  ? 412 HOH B O   1 
HETATM 4700 O  O   . HOH L 6 .   ? -25.640 12.104  53.334  1.00 32.64  ? 413 HOH B O   1 
HETATM 4701 O  O   . HOH L 6 .   ? -7.303  13.295  9.294   1.00 33.75  ? 414 HOH B O   1 
HETATM 4702 O  O   . HOH L 6 .   ? -2.288  17.033  5.273   1.00 73.25  ? 415 HOH B O   1 
HETATM 4703 O  O   . HOH L 6 .   ? -31.227 30.199  17.685  1.00 19.99  ? 416 HOH B O   1 
HETATM 4704 O  O   . HOH L 6 .   ? -5.779  21.424  10.244  1.00 36.76  ? 417 HOH B O   1 
HETATM 4705 O  O   . HOH L 6 .   ? -32.074 8.255   34.576  1.00 29.42  ? 418 HOH B O   1 
HETATM 4706 O  O   . HOH L 6 .   ? -30.668 30.721  45.932  1.00 28.83  ? 419 HOH B O   1 
HETATM 4707 O  O   . HOH L 6 .   ? -38.653 28.712  32.094  1.00 43.93  ? 420 HOH B O   1 
HETATM 4708 O  O   . HOH L 6 .   ? -7.666  10.976  25.222  1.00 20.61  ? 421 HOH B O   1 
HETATM 4709 O  O   . HOH L 6 .   ? -22.477 34.854  44.980  1.00 25.64  ? 422 HOH B O   1 
HETATM 4710 O  O   . HOH L 6 .   ? -2.687  14.345  14.577  1.00 24.60  ? 423 HOH B O   1 
HETATM 4711 O  O   . HOH L 6 .   ? -20.801 44.134  35.907  1.00 16.84  ? 424 HOH B O   1 
HETATM 4712 O  O   . HOH L 6 .   ? -5.728  19.944  44.846  1.00 24.92  ? 425 HOH B O   1 
HETATM 4713 O  O   . HOH L 6 .   ? -11.313 18.316  31.523  1.00 9.71   ? 426 HOH B O   1 
HETATM 4714 O  O   . HOH L 6 .   ? -3.769  16.854  19.569  1.00 32.80  ? 427 HOH B O   1 
HETATM 4715 O  O   . HOH L 6 .   ? -25.553 31.219  13.681  1.00 82.98  ? 428 HOH B O   1 
HETATM 4716 O  O   . HOH L 6 .   ? -12.927 3.163   22.081  1.00 34.86  ? 429 HOH B O   1 
HETATM 4717 O  O   . HOH L 6 .   ? -35.654 18.850  48.154  1.00 86.20  ? 430 HOH B O   1 
HETATM 4718 O  O   . HOH L 6 .   ? -34.257 30.937  36.027  1.00 18.33  ? 431 HOH B O   1 
HETATM 4719 O  O   . HOH L 6 .   ? -18.841 18.594  23.695  1.00 10.36  ? 432 HOH B O   1 
HETATM 4720 O  O   . HOH L 6 .   ? -16.481 17.756  9.355   1.00 22.95  ? 433 HOH B O   1 
HETATM 4721 O  O   . HOH L 6 .   ? -24.420 5.834   44.847  1.00 20.93  ? 434 HOH B O   1 
HETATM 4722 O  O   . HOH L 6 .   ? -37.355 17.028  43.341  1.00 35.68  ? 435 HOH B O   1 
HETATM 4723 O  O   . HOH L 6 .   ? -19.255 28.262  44.821  1.00 16.20  ? 436 HOH B O   1 
HETATM 4724 O  O   . HOH L 6 .   ? -18.417 30.050  24.001  1.00 24.09  ? 437 HOH B O   1 
HETATM 4725 O  O   . HOH L 6 .   ? 1.022   15.328  38.354  1.00 29.13  ? 438 HOH B O   1 
HETATM 4726 O  O   . HOH L 6 .   ? -7.427  18.044  23.486  1.00 24.16  ? 439 HOH B O   1 
HETATM 4727 O  O   . HOH L 6 .   ? -2.735  21.135  10.177  1.00 33.80  ? 440 HOH B O   1 
HETATM 4728 O  O   . HOH L 6 .   ? -20.044 38.261  45.368  1.00 27.21  ? 441 HOH B O   1 
HETATM 4729 O  O   . HOH L 6 .   ? -26.017 25.890  51.002  1.00 32.63  ? 442 HOH B O   1 
HETATM 4730 O  O   . HOH L 6 .   ? -22.126 33.178  21.990  1.00 32.17  ? 443 HOH B O   1 
HETATM 4731 O  O   . HOH L 6 .   ? -3.544  10.925  31.267  1.00 101.30 ? 444 HOH B O   1 
HETATM 4732 O  O   . HOH L 6 .   ? -23.036 0.081   28.162  1.00 26.98  ? 445 HOH B O   1 
HETATM 4733 O  O   . HOH L 6 .   ? -20.730 31.077  41.391  1.00 9.55   ? 446 HOH B O   1 
HETATM 4734 O  O   . HOH L 6 .   ? -27.097 8.328   53.391  1.00 30.25  ? 447 HOH B O   1 
HETATM 4735 O  O   . HOH L 6 .   ? -28.607 26.450  12.530  1.00 79.68  ? 448 HOH B O   1 
HETATM 4736 O  O   . HOH L 6 .   ? -34.848 11.299  39.888  1.00 34.62  ? 449 HOH B O   1 
HETATM 4737 O  O   . HOH L 6 .   ? -16.996 7.465   47.415  1.00 27.26  ? 450 HOH B O   1 
HETATM 4738 O  O   . HOH L 6 .   ? -23.183 0.154   24.398  1.00 22.50  ? 451 HOH B O   1 
HETATM 4739 O  O   . HOH L 6 .   ? -15.404 8.769   50.155  1.00 32.56  ? 452 HOH B O   1 
HETATM 4740 O  O   . HOH L 6 .   ? -26.496 6.854   48.553  1.00 37.47  ? 453 HOH B O   1 
HETATM 4741 O  O   . HOH L 6 .   ? -24.008 36.566  43.095  1.00 23.09  ? 454 HOH B O   1 
HETATM 4742 O  O   . HOH L 6 .   ? -5.802  18.980  42.399  1.00 19.29  ? 455 HOH B O   1 
HETATM 4743 O  O   . HOH L 6 .   ? -6.446  27.400  45.682  1.00 19.34  ? 456 HOH B O   1 
HETATM 4744 O  O   . HOH L 6 .   ? -6.634  8.590   28.259  1.00 40.69  ? 457 HOH B O   1 
HETATM 4745 O  O   . HOH L 6 .   ? -14.775 10.387  47.926  1.00 17.89  ? 458 HOH B O   1 
HETATM 4746 O  O   . HOH L 6 .   ? -10.154 23.510  50.344  1.00 26.72  ? 459 HOH B O   1 
HETATM 4747 O  O   . HOH L 6 .   ? -28.695 1.231   30.576  1.00 19.14  ? 460 HOH B O   1 
HETATM 4748 O  O   . HOH L 6 .   ? -12.585 13.654  44.931  1.00 10.54  ? 461 HOH B O   1 
HETATM 4749 O  O   . HOH L 6 .   ? -18.073 6.956   27.163  1.00 10.64  ? 462 HOH B O   1 
HETATM 4750 O  O   . HOH L 6 .   ? -30.473 33.092  42.654  1.00 17.79  ? 463 HOH B O   1 
HETATM 4751 O  O   . HOH L 6 .   ? 1.451   21.983  31.797  1.00 29.84  ? 464 HOH B O   1 
HETATM 4752 O  O   . HOH L 6 .   ? -36.370 25.856  31.376  1.00 25.62  ? 465 HOH B O   1 
HETATM 4753 O  O   . HOH L 6 .   ? -32.928 16.417  18.486  1.00 19.78  ? 466 HOH B O   1 
HETATM 4754 O  O   . HOH L 6 .   ? -5.793  15.760  23.604  1.00 25.58  ? 467 HOH B O   1 
HETATM 4755 O  O   . HOH L 6 .   ? -12.208 17.730  8.563   1.00 25.30  ? 468 HOH B O   1 
HETATM 4756 O  O   . HOH L 6 .   ? 3.321   22.626  40.301  1.00 20.93  ? 469 HOH B O   1 
HETATM 4757 O  O   . HOH L 6 .   ? -36.057 28.539  42.912  1.00 23.39  ? 470 HOH B O   1 
HETATM 4758 O  O   . HOH L 6 .   ? -35.691 11.773  33.588  1.00 22.24  ? 471 HOH B O   1 
HETATM 4759 O  O   . HOH L 6 .   ? -23.568 21.591  9.641   1.00 34.18  ? 472 HOH B O   1 
HETATM 4760 O  O   . HOH L 6 .   ? -10.162 21.284  10.994  1.00 15.58  ? 473 HOH B O   1 
HETATM 4761 O  O   . HOH L 6 .   ? -11.792 26.893  10.942  1.00 65.39  ? 474 HOH B O   1 
HETATM 4762 O  O   . HOH L 6 .   ? -10.599 33.204  39.155  1.00 17.25  ? 475 HOH B O   1 
HETATM 4763 O  O   . HOH L 6 .   ? -25.186 24.925  54.517  1.00 27.32  ? 476 HOH B O   1 
HETATM 4764 O  O   . HOH L 6 .   ? -29.407 1.510   21.153  1.00 25.15  ? 477 HOH B O   1 
HETATM 4765 O  O   . HOH L 6 .   ? -14.347 13.902  47.003  1.00 18.03  ? 478 HOH B O   1 
HETATM 4766 O  O   . HOH L 6 .   ? -13.585 11.233  36.707  1.00 9.24   ? 479 HOH B O   1 
HETATM 4767 O  O   . HOH L 6 .   ? 2.922   18.539  29.278  1.00 27.04  ? 480 HOH B O   1 
HETATM 4768 O  O   . HOH L 6 .   ? -28.123 33.122  27.098  1.00 16.63  ? 481 HOH B O   1 
HETATM 4769 O  O   . HOH L 6 .   ? -10.583 36.327  31.911  1.00 26.73  ? 482 HOH B O   1 
HETATM 4770 O  O   . HOH L 6 .   ? -8.694  10.621  40.880  1.00 25.20  ? 483 HOH B O   1 
HETATM 4771 O  O   . HOH L 6 .   ? -18.748 23.034  9.251   1.00 28.39  ? 484 HOH B O   1 
HETATM 4772 O  O   . HOH L 6 .   ? -27.528 6.207   37.866  1.00 20.63  ? 485 HOH B O   1 
HETATM 4773 O  O   . HOH L 6 .   ? -27.148 13.979  36.235  1.00 8.91   ? 486 HOH B O   1 
HETATM 4774 O  O   . HOH L 6 .   ? -21.188 2.839   23.016  1.00 24.24  ? 487 HOH B O   1 
HETATM 4775 O  O   . HOH L 6 .   ? -8.215  6.691   25.129  1.00 20.97  ? 488 HOH B O   1 
HETATM 4776 O  O   . HOH L 6 .   ? -14.633 8.871   33.860  1.00 8.59   ? 489 HOH B O   1 
HETATM 4777 O  O   . HOH L 6 .   ? -34.175 19.549  44.987  1.00 57.22  ? 490 HOH B O   1 
HETATM 4778 O  O   . HOH L 6 .   ? -16.897 43.306  35.355  1.00 13.36  ? 491 HOH B O   1 
HETATM 4779 O  O   . HOH L 6 .   ? -26.937 8.433   42.245  1.00 18.15  ? 492 HOH B O   1 
HETATM 4780 O  O   . HOH L 6 .   ? -13.876 9.414   12.882  1.00 24.46  ? 493 HOH B O   1 
HETATM 4781 O  O   . HOH L 6 .   ? -31.731 15.185  39.476  1.00 11.99  ? 494 HOH B O   1 
HETATM 4782 O  O   . HOH L 6 .   ? -23.942 32.725  43.781  1.00 16.97  ? 495 HOH B O   1 
HETATM 4783 O  O   . HOH L 6 .   ? 5.178   19.894  30.361  1.00 20.23  ? 496 HOH B O   1 
HETATM 4784 O  O   . HOH L 6 .   ? -3.424  20.274  7.753   1.00 35.24  ? 497 HOH B O   1 
HETATM 4785 O  O   . HOH L 6 .   ? -20.473 35.713  24.671  1.00 39.96  ? 498 HOH B O   1 
HETATM 4786 O  O   . HOH L 6 .   ? -4.684  29.518  36.207  1.00 17.26  ? 499 HOH B O   1 
HETATM 4787 O  O   . HOH L 6 .   ? -28.650 18.557  13.177  1.00 26.17  ? 500 HOH B O   1 
HETATM 4788 O  O   . HOH L 6 .   ? -25.167 42.470  33.524  1.00 17.21  ? 501 HOH B O   1 
HETATM 4789 O  O   . HOH L 6 .   ? -28.072 43.112  23.865  1.00 13.73  ? 502 HOH B O   1 
HETATM 4790 O  O   . HOH L 6 .   ? -16.798 17.117  53.268  1.00 17.28  ? 503 HOH B O   1 
HETATM 4791 O  O   . HOH L 6 .   ? -33.475 9.101   27.079  1.00 19.54  ? 504 HOH B O   1 
HETATM 4792 O  O   . HOH L 6 .   ? -25.033 28.515  48.538  1.00 31.72  ? 505 HOH B O   1 
HETATM 4793 O  O   . HOH L 6 .   ? -13.477 9.109   40.987  1.00 10.77  ? 506 HOH B O   1 
HETATM 4794 O  O   . HOH L 6 .   ? -13.881 6.479   40.185  1.00 12.67  ? 507 HOH B O   1 
HETATM 4795 O  O   . HOH L 6 .   ? -12.631 4.374   46.749  1.00 25.52  ? 508 HOH B O   1 
HETATM 4796 O  O   . HOH L 6 .   ? -26.179 10.062  40.248  1.00 13.66  ? 509 HOH B O   1 
HETATM 4797 O  O   . HOH L 6 .   ? -32.291 4.058   29.408  1.00 21.19  ? 510 HOH B O   1 
HETATM 4798 O  O   . HOH L 6 .   ? -29.930 18.171  57.250  1.00 33.85  ? 511 HOH B O   1 
HETATM 4799 O  O   . HOH L 6 .   ? -29.451 32.400  24.705  1.00 14.16  ? 512 HOH B O   1 
HETATM 4800 O  O   . HOH L 6 .   ? -34.977 14.654  24.866  1.00 20.16  ? 513 HOH B O   1 
HETATM 4801 O  O   . HOH L 6 .   ? -33.479 11.311  32.978  1.00 27.11  ? 514 HOH B O   1 
HETATM 4802 O  O   . HOH L 6 .   ? -20.893 30.970  23.479  1.00 19.37  ? 515 HOH B O   1 
HETATM 4803 O  O   . HOH L 6 .   ? -37.255 14.634  42.342  1.00 36.86  ? 516 HOH B O   1 
HETATM 4804 O  O   . HOH L 6 .   ? -33.410 19.376  22.512  1.00 21.49  ? 517 HOH B O   1 
HETATM 4805 O  O   . HOH L 6 .   ? -26.431 12.475  48.781  1.00 17.81  ? 518 HOH B O   1 
HETATM 4806 O  O   . HOH L 6 .   ? -23.950 42.325  31.014  1.00 16.61  ? 519 HOH B O   1 
HETATM 4807 O  O   . HOH L 6 .   ? -32.028 28.086  20.514  1.00 19.08  ? 520 HOH B O   1 
HETATM 4808 O  O   . HOH L 6 .   ? -36.311 14.648  46.381  1.00 72.99  ? 521 HOH B O   1 
HETATM 4809 O  O   . HOH L 6 .   ? -18.080 41.369  26.220  1.00 17.22  ? 522 HOH B O   1 
HETATM 4810 O  O   . HOH L 6 .   ? -20.710 43.213  40.848  1.00 17.54  ? 523 HOH B O   1 
HETATM 4811 O  O   . HOH L 6 .   ? -17.356 5.558   17.326  1.00 19.60  ? 524 HOH B O   1 
HETATM 4812 O  O   . HOH L 6 .   ? -11.096 16.317  52.231  1.00 24.35  ? 525 HOH B O   1 
HETATM 4813 O  O   . HOH L 6 .   ? 5.723   25.222  36.679  1.00 30.64  ? 526 HOH B O   1 
HETATM 4814 O  O   . HOH L 6 .   ? -1.515  18.562  36.877  1.00 15.13  ? 527 HOH B O   1 
HETATM 4815 O  O   . HOH L 6 .   ? -9.989  8.146   46.902  1.00 38.57  ? 528 HOH B O   1 
HETATM 4816 O  O   . HOH L 6 .   ? -4.103  19.569  22.599  1.00 37.17  ? 529 HOH B O   1 
HETATM 4817 O  O   . HOH L 6 .   ? -26.350 38.243  39.564  1.00 16.19  ? 530 HOH B O   1 
HETATM 4818 O  O   . HOH L 6 .   ? -25.583 41.686  28.971  1.00 15.13  ? 531 HOH B O   1 
HETATM 4819 O  O   . HOH L 6 .   ? -17.468 13.719  48.470  1.00 16.36  ? 532 HOH B O   1 
HETATM 4820 O  O   . HOH L 6 .   ? -12.614 3.198   37.354  1.00 31.50  ? 533 HOH B O   1 
HETATM 4821 O  O   . HOH L 6 .   ? -33.309 22.019  50.315  1.00 29.10  ? 534 HOH B O   1 
HETATM 4822 O  O   . HOH L 6 .   ? -23.152 13.566  12.534  1.00 27.25  ? 535 HOH B O   1 
HETATM 4823 O  O   . HOH L 6 .   ? -22.866 30.256  44.692  1.00 21.41  ? 536 HOH B O   1 
HETATM 4824 O  O   . HOH L 6 .   ? -35.789 21.294  50.869  1.00 33.94  ? 537 HOH B O   1 
HETATM 4825 O  O   . HOH L 6 .   ? -7.579  9.174   21.044  1.00 19.83  ? 538 HOH B O   1 
HETATM 4826 O  O   . HOH L 6 .   ? -23.512 3.883   30.445  1.00 14.21  ? 539 HOH B O   1 
HETATM 4827 O  O   . HOH L 6 .   ? -5.221  18.894  18.769  1.00 28.17  ? 540 HOH B O   1 
HETATM 4828 O  O   . HOH L 6 .   ? -33.216 7.634   31.955  1.00 33.68  ? 541 HOH B O   1 
HETATM 4829 O  O   . HOH L 6 .   ? -34.031 4.471   22.299  1.00 53.64  ? 542 HOH B O   1 
HETATM 4830 O  O   . HOH L 6 .   ? -14.834 6.489   16.475  1.00 23.37  ? 543 HOH B O   1 
HETATM 4831 O  O   . HOH L 6 .   ? 2.996   16.567  40.277  1.00 25.22  ? 544 HOH B O   1 
HETATM 4832 O  O   . HOH L 6 .   ? -23.147 5.537   42.509  1.00 14.53  ? 545 HOH B O   1 
HETATM 4833 O  O   . HOH L 6 .   ? -17.373 13.833  8.721   1.00 32.50  ? 546 HOH B O   1 
HETATM 4834 O  O   . HOH L 6 .   ? -5.185  17.527  36.830  1.00 14.43  ? 547 HOH B O   1 
HETATM 4835 O  O   . HOH L 6 .   ? -32.845 12.800  41.244  1.00 19.62  ? 548 HOH B O   1 
HETATM 4836 O  O   . HOH L 6 .   ? -11.263 31.440  44.167  1.00 55.83  ? 549 HOH B O   1 
HETATM 4837 O  O   . HOH L 6 .   ? -8.494  16.147  50.224  1.00 26.56  ? 550 HOH B O   1 
HETATM 4838 O  O   . HOH L 6 .   ? 1.153   23.698  41.793  1.00 24.98  ? 551 HOH B O   1 
HETATM 4839 O  O   . HOH L 6 .   ? -1.192  10.864  22.490  1.00 32.55  ? 552 HOH B O   1 
HETATM 4840 O  O   . HOH L 6 .   ? -8.816  31.163  40.165  1.00 18.60  ? 553 HOH B O   1 
HETATM 4841 O  O   . HOH L 6 .   ? -20.258 37.107  27.946  1.00 19.54  ? 554 HOH B O   1 
HETATM 4842 O  O   . HOH L 6 .   ? -22.118 25.150  46.757  1.00 17.48  ? 555 HOH B O   1 
HETATM 4843 O  O   . HOH L 6 .   ? -15.962 39.830  43.253  1.00 29.12  ? 556 HOH B O   1 
HETATM 4844 O  O   . HOH L 6 .   ? -18.621 2.543   42.514  1.00 20.83  ? 557 HOH B O   1 
HETATM 4845 O  O   . HOH L 6 .   ? -36.031 15.644  49.673  1.00 81.12  ? 558 HOH B O   1 
HETATM 4846 O  O   . HOH L 6 .   ? -22.730 3.905   47.929  1.00 37.06  ? 559 HOH B O   1 
HETATM 4847 O  O   . HOH L 6 .   ? -8.857  20.873  45.300  1.00 14.18  ? 560 HOH B O   1 
HETATM 4848 O  O   . HOH L 6 .   ? 0.073   13.776  24.042  1.00 25.03  ? 561 HOH B O   1 
HETATM 4849 O  O   . HOH L 6 .   ? -34.151 21.656  42.331  1.00 16.64  ? 562 HOH B O   1 
HETATM 4850 O  O   . HOH L 6 .   ? -10.331 8.060   38.001  1.00 20.81  ? 563 HOH B O   1 
HETATM 4851 O  O   . HOH L 6 .   ? -33.079 38.037  34.750  1.00 41.11  ? 564 HOH B O   1 
HETATM 4852 O  O   . HOH L 6 .   ? -19.224 16.592  51.805  1.00 17.85  ? 565 HOH B O   1 
HETATM 4853 O  O   . HOH L 6 .   ? -19.756 12.268  14.522  1.00 22.79  ? 566 HOH B O   1 
HETATM 4854 O  O   . HOH L 6 .   ? -35.430 33.467  35.314  1.00 33.27  ? 567 HOH B O   1 
HETATM 4855 O  O   . HOH L 6 .   ? -16.424 2.634   39.625  1.00 22.55  ? 568 HOH B O   1 
HETATM 4856 O  O   . HOH L 6 .   ? -5.750  27.016  26.620  1.00 47.68  ? 569 HOH B O   1 
HETATM 4857 O  O   . HOH L 6 .   ? -7.284  7.828   16.992  1.00 26.31  ? 570 HOH B O   1 
HETATM 4858 O  O   . HOH L 6 .   ? -34.089 21.624  19.772  1.00 23.93  ? 571 HOH B O   1 
HETATM 4859 O  O   . HOH L 6 .   ? -2.442  28.477  37.581  1.00 16.22  ? 572 HOH B O   1 
HETATM 4860 O  O   . HOH L 6 .   ? -16.899 37.067  44.949  1.00 31.52  ? 573 HOH B O   1 
HETATM 4861 O  O   . HOH L 6 .   ? -12.155 10.085  38.669  1.00 10.13  ? 574 HOH B O   1 
HETATM 4862 O  O   . HOH L 6 .   ? -31.438 2.822   22.481  1.00 23.77  ? 575 HOH B O   1 
HETATM 4863 O  O   . HOH L 6 .   ? -4.930  15.172  38.199  1.00 26.71  ? 576 HOH B O   1 
HETATM 4864 O  O   . HOH L 6 .   ? -22.994 25.879  8.928   1.00 25.45  ? 577 HOH B O   1 
HETATM 4865 O  O   . HOH L 6 .   ? -10.538 1.558   30.638  1.00 38.26  ? 578 HOH B O   1 
HETATM 4866 O  O   . HOH L 6 .   ? -10.735 13.826  48.409  1.00 23.43  ? 579 HOH B O   1 
HETATM 4867 O  O   . HOH L 6 .   ? -5.315  9.275   10.037  1.00 19.12  ? 580 HOH B O   1 
HETATM 4868 O  O   . HOH L 6 .   ? -1.880  25.678  43.678  1.00 30.97  ? 581 HOH B O   1 
HETATM 4869 O  O   . HOH L 6 .   ? -33.108 10.691  29.896  1.00 21.82  ? 582 HOH B O   1 
HETATM 4870 O  O   . HOH L 6 .   ? 4.810   15.493  23.601  1.00 36.03  ? 583 HOH B O   1 
HETATM 4871 O  O   . HOH L 6 .   ? -17.089 23.890  50.977  1.00 23.58  ? 584 HOH B O   1 
HETATM 4872 O  O   . HOH L 6 .   ? -13.859 17.846  53.648  1.00 34.56  ? 585 HOH B O   1 
HETATM 4873 O  O   . HOH L 6 .   ? -34.850 12.922  17.727  1.00 22.94  ? 586 HOH B O   1 
HETATM 4874 O  O   . HOH L 6 .   ? 1.267   18.527  23.340  1.00 34.18  ? 587 HOH B O   1 
HETATM 4875 O  O   . HOH L 6 .   ? -21.265 39.898  28.097  1.00 22.04  ? 588 HOH B O   1 
HETATM 4876 O  O   . HOH L 6 .   ? -23.825 36.796  21.945  1.00 41.94  ? 589 HOH B O   1 
HETATM 4877 O  O   . HOH L 6 .   ? -19.691 14.448  49.997  1.00 21.06  ? 590 HOH B O   1 
HETATM 4878 O  O   . HOH L 6 .   ? -15.514 25.890  10.033  1.00 26.86  ? 591 HOH B O   1 
HETATM 4879 O  O   . HOH L 6 .   ? -25.191 2.375   39.075  1.00 28.88  ? 592 HOH B O   1 
HETATM 4880 O  O   . HOH L 6 .   ? 3.990   24.569  38.831  1.00 30.54  ? 593 HOH B O   1 
HETATM 4881 O  O   . HOH L 6 .   ? -3.644  16.499  22.414  1.00 31.30  ? 594 HOH B O   1 
HETATM 4882 O  O   . HOH L 6 .   ? -31.173 9.618   13.957  1.00 21.33  ? 595 HOH B O   1 
HETATM 4883 O  O   . HOH L 6 .   ? -17.668 13.634  13.371  1.00 28.56  ? 596 HOH B O   1 
HETATM 4884 O  O   . HOH L 6 .   ? -38.079 28.137  35.551  1.00 71.19  ? 597 HOH B O   1 
HETATM 4885 O  O   . HOH L 6 .   ? -28.608 13.425  50.503  1.00 78.96  ? 598 HOH B O   1 
HETATM 4886 O  O   . HOH L 6 .   ? 5.060   12.168  30.455  1.00 26.76  ? 599 HOH B O   1 
HETATM 4887 O  O   . HOH L 6 .   ? -9.713  22.943  8.938   1.00 31.28  ? 600 HOH B O   1 
HETATM 4888 O  O   . HOH L 6 .   ? -12.886 7.489   48.641  1.00 29.04  ? 601 HOH B O   1 
HETATM 4889 O  O   . HOH L 6 .   ? -11.578 33.937  41.773  1.00 28.69  ? 602 HOH B O   1 
HETATM 4890 O  O   . HOH L 6 .   ? -22.502 35.523  47.302  1.00 102.01 ? 603 HOH B O   1 
HETATM 4891 O  O   . HOH L 6 .   ? -23.005 5.176   32.724  1.00 11.91  ? 604 HOH B O   1 
HETATM 4892 O  O   . HOH L 6 .   ? -35.610 26.853  20.141  1.00 40.27  ? 605 HOH B O   1 
HETATM 4893 O  O   . HOH L 6 .   ? 0.562   20.709  20.842  1.00 45.53  ? 606 HOH B O   1 
HETATM 4894 O  O   . HOH L 6 .   ? -1.488  17.689  39.520  1.00 24.72  ? 607 HOH B O   1 
HETATM 4895 O  O   . HOH L 6 .   ? 0.320   19.863  29.581  1.00 36.31  ? 608 HOH B O   1 
HETATM 4896 O  O   . HOH L 6 .   ? -7.460  7.494   9.876   1.00 37.83  ? 609 HOH B O   1 
HETATM 4897 O  O   . HOH L 6 .   ? -10.284 19.598  55.325  1.00 47.01  ? 610 HOH B O   1 
HETATM 4898 O  O   . HOH L 6 .   ? 4.983   6.812   26.585  1.00 35.12  ? 611 HOH B O   1 
HETATM 4899 O  O   . HOH L 6 .   ? -18.316 44.182  37.533  1.00 13.99  ? 612 HOH B O   1 
HETATM 4900 O  O   . HOH L 6 .   ? -4.789  11.536  34.808  1.00 38.20  ? 613 HOH B O   1 
HETATM 4901 O  O   . HOH L 6 .   ? -14.680 16.496  7.750   1.00 39.09  ? 614 HOH B O   1 
HETATM 4902 O  O   . HOH L 6 .   ? -35.092 31.202  42.028  1.00 56.79  ? 615 HOH B O   1 
HETATM 4903 O  O   . HOH L 6 .   ? -19.900 23.908  54.823  1.00 25.79  ? 616 HOH B O   1 
HETATM 4904 O  O   . HOH L 6 .   ? 6.232   16.539  28.914  1.00 33.41  ? 617 HOH B O   1 
HETATM 4905 O  O   . HOH L 6 .   ? -11.512 9.296   42.960  1.00 23.35  ? 618 HOH B O   1 
HETATM 4906 O  O   . HOH L 6 .   ? -27.927 42.349  33.344  1.00 21.44  ? 619 HOH B O   1 
HETATM 4907 O  O   . HOH L 6 .   ? -22.669 28.741  46.974  1.00 33.35  ? 620 HOH B O   1 
HETATM 4908 O  O   . HOH L 6 .   ? 1.840   15.830  23.751  1.00 27.66  ? 621 HOH B O   1 
HETATM 4909 O  O   . HOH L 6 .   ? -7.292  8.933   23.899  1.00 24.90  ? 622 HOH B O   1 
HETATM 4910 O  O   . HOH L 6 .   ? -5.797  11.118  8.182   1.00 36.61  ? 623 HOH B O   1 
HETATM 4911 O  O   . HOH L 6 .   ? -14.986 42.903  37.315  1.00 21.48  ? 624 HOH B O   1 
HETATM 4912 O  O   . HOH L 6 .   ? -9.661  6.373   39.993  1.00 39.45  ? 625 HOH B O   1 
HETATM 4913 O  O   . HOH L 6 .   ? -20.603 27.202  46.742  1.00 23.85  ? 626 HOH B O   1 
HETATM 4914 O  O   . HOH L 6 .   ? 5.155   18.408  40.869  1.00 21.42  ? 627 HOH B O   1 
HETATM 4915 O  O   . HOH L 6 .   ? 0.093   28.284  29.152  1.00 54.08  ? 628 HOH B O   1 
HETATM 4916 O  O   . HOH L 6 .   ? -12.043 4.886   41.333  1.00 26.98  ? 629 HOH B O   1 
HETATM 4917 O  O   . HOH L 6 .   ? -3.619  17.186  43.195  1.00 38.72  ? 630 HOH B O   1 
HETATM 4918 O  O   . HOH L 6 .   ? -27.078 4.486   35.996  1.00 21.71  ? 631 HOH B O   1 
HETATM 4919 O  O   . HOH L 6 .   ? -25.730 5.975   41.851  1.00 28.68  ? 632 HOH B O   1 
HETATM 4920 O  O   . HOH L 6 .   ? -34.219 36.208  36.374  1.00 53.69  ? 633 HOH B O   1 
HETATM 4921 O  O   . HOH L 6 .   ? -29.931 20.315  58.884  1.00 34.78  ? 634 HOH B O   1 
HETATM 4922 O  O   . HOH L 6 .   ? -24.813 45.022  34.553  1.00 14.40  ? 635 HOH B O   1 
HETATM 4923 O  O   . HOH L 6 .   ? -11.245 9.158   48.929  1.00 23.90  ? 636 HOH B O   1 
HETATM 4924 O  O   . HOH L 6 .   ? -31.030 17.317  12.375  1.00 82.28  ? 637 HOH B O   1 
HETATM 4925 O  O   . HOH L 6 .   ? -8.380  34.846  38.402  1.00 28.47  ? 638 HOH B O   1 
HETATM 4926 O  O   . HOH L 6 .   ? -12.157 10.624  47.384  1.00 29.58  ? 639 HOH B O   1 
HETATM 4927 O  O   . HOH L 6 .   ? -21.697 23.343  8.029   1.00 32.17  ? 640 HOH B O   1 
HETATM 4928 O  O   . HOH L 6 .   ? -34.263 15.424  16.066  1.00 31.46  ? 641 HOH B O   1 
HETATM 4929 O  O   . HOH L 6 .   ? -8.144  8.106   36.297  1.00 30.97  ? 642 HOH B O   1 
HETATM 4930 O  O   . HOH L 6 .   ? -19.440 25.408  50.621  1.00 23.98  ? 643 HOH B O   1 
HETATM 4931 O  O   . HOH L 6 .   ? -17.444 12.209  11.420  1.00 33.47  ? 644 HOH B O   1 
HETATM 4932 O  O   . HOH L 6 .   ? -20.528 45.292  32.915  1.00 12.31  ? 645 HOH B O   1 
HETATM 4933 O  O   . HOH L 6 .   ? -8.666  4.855   22.957  1.00 28.23  ? 646 HOH B O   1 
HETATM 4934 O  O   . HOH L 6 .   ? -16.101 1.496   42.069  1.00 30.89  ? 647 HOH B O   1 
HETATM 4935 O  O   . HOH L 6 .   ? -28.005 10.338  47.445  1.00 29.21  ? 648 HOH B O   1 
HETATM 4936 O  O   . HOH L 6 .   ? -24.181 25.969  49.010  1.00 29.82  ? 649 HOH B O   1 
HETATM 4937 O  O   . HOH L 6 .   ? -31.551 1.783   30.339  1.00 33.43  ? 650 HOH B O   1 
HETATM 4938 O  O   . HOH L 6 .   ? -11.241 11.263  44.794  1.00 16.54  ? 651 HOH B O   1 
HETATM 4939 O  O   . HOH L 6 .   ? -19.175 27.493  48.893  1.00 26.22  ? 652 HOH B O   1 
HETATM 4940 O  O   . HOH L 6 .   ? -14.235 6.866   13.494  1.00 34.93  ? 653 HOH B O   1 
HETATM 4941 O  O   . HOH L 6 .   ? -3.800  27.767  44.973  1.00 40.53  ? 654 HOH B O   1 
HETATM 4942 O  O   . HOH L 6 .   ? -15.395 12.967  50.073  1.00 61.18  ? 655 HOH B O   1 
HETATM 4943 O  O   . HOH L 6 .   ? -12.695 28.115  21.695  1.00 32.54  ? 656 HOH B O   1 
HETATM 4944 O  O   . HOH L 6 .   ? -36.948 21.099  41.806  1.00 20.05  ? 657 HOH B O   1 
HETATM 4945 O  O   . HOH L 6 .   ? -22.981 2.866   41.966  1.00 22.66  ? 658 HOH B O   1 
HETATM 4946 O  O   . HOH L 6 .   ? 3.985   20.919  44.340  1.00 27.93  ? 659 HOH B O   1 
HETATM 4947 O  O   . HOH L 6 .   ? -12.592 28.622  29.716  1.00 29.81  ? 660 HOH B O   1 
HETATM 4948 O  O   . HOH L 6 .   ? 1.875   22.816  44.288  1.00 43.24  ? 661 HOH B O   1 
HETATM 4949 O  O   . HOH L 6 .   ? -21.539 31.397  48.940  1.00 32.54  ? 662 HOH B O   1 
HETATM 4950 O  O   . HOH L 6 .   ? -6.413  32.317  39.615  1.00 26.46  ? 663 HOH B O   1 
HETATM 4951 O  O   . HOH L 6 .   ? -40.102 26.814  43.309  1.00 42.77  ? 664 HOH B O   1 
HETATM 4952 O  O   . HOH L 6 .   ? -5.910  9.156   37.253  1.00 51.35  ? 665 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS A 3   ? 0.2046 0.3517 0.2465 -0.0241 -0.0250 -0.0228 3   HIS A N   
2    C  CA  . HIS A 3   ? 0.1506 0.3996 0.4925 -0.0467 0.0668  -0.1691 3   HIS A CA  
3    C  C   . HIS A 3   ? 0.2041 0.3980 0.3801 -0.0864 -0.0164 -0.0776 3   HIS A C   
4    O  O   . HIS A 3   ? 0.3582 0.5307 0.4043 0.0452  -0.1908 -0.0135 3   HIS A O   
5    C  CB  . HIS A 3   ? 0.2565 0.3217 0.4476 0.1039  -0.0632 -0.1149 3   HIS A CB  
6    C  CG  . HIS A 3   ? 0.3310 0.3407 0.3605 0.1037  -0.0168 -0.0877 3   HIS A CG  
7    N  ND1 . HIS A 3   ? 0.3389 0.3998 0.3689 0.1052  -0.0377 -0.1677 3   HIS A ND1 
8    C  CD2 . HIS A 3   ? 0.3759 0.3310 0.4691 0.0038  -0.0544 -0.0028 3   HIS A CD2 
9    C  CE1 . HIS A 3   ? 0.2556 0.3152 0.3713 0.0627  -0.0076 -0.0768 3   HIS A CE1 
10   N  NE2 . HIS A 3   ? 0.5975 0.3718 0.5889 -0.0465 0.2378  -0.0013 3   HIS A NE2 
11   N  N   . HIS A 4   ? 0.1863 0.4246 0.3479 -0.0060 0.0414  -0.1730 4   HIS A N   
12   C  CA  . HIS A 4   ? 0.2926 0.3436 0.5613 -0.0428 0.2296  -0.2180 4   HIS A CA  
13   C  C   . HIS A 4   ? 0.1802 0.2847 0.3113 0.0722  0.0590  -0.0421 4   HIS A C   
14   O  O   . HIS A 4   ? 0.2108 0.2865 0.3037 0.0328  0.1031  -0.0148 4   HIS A O   
15   C  CB  . HIS A 4   ? 0.2606 0.6248 0.5403 -0.0575 0.1823  -0.2691 4   HIS A CB  
16   C  CG  . HIS A 4   ? 0.5587 0.7092 0.7481 0.0062  0.3454  -0.2166 4   HIS A CG  
17   N  ND1 . HIS A 4   ? 0.3533 0.8834 1.4407 -0.3776 -0.1659 -0.1801 4   HIS A ND1 
18   C  CD2 . HIS A 4   ? 0.5777 0.8144 1.2160 -0.0163 0.1694  -0.1369 4   HIS A CD2 
19   C  CE1 . HIS A 4   ? 0.8478 0.4410 1.5044 -0.0192 0.1181  -0.4501 4   HIS A CE1 
20   N  NE2 . HIS A 4   ? 0.6484 0.9082 1.5579 0.0302  0.4427  0.0939  4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.2029 0.2540 0.3012 0.0362  0.0877  -0.0646 5   TRP A N   
22   C  CA  . TRP A 5   ? 0.1650 0.1701 0.2531 0.0121  0.0737  -0.0394 5   TRP A CA  
23   C  C   . TRP A 5   ? 0.1740 0.1880 0.2396 0.0153  0.0998  -0.0083 5   TRP A C   
24   O  O   . TRP A 5   ? 0.2192 0.1741 0.2565 0.0216  0.0763  -0.0283 5   TRP A O   
25   C  CB  . TRP A 5   ? 0.1569 0.1694 0.2881 0.0027  0.0715  0.0195  5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1670 0.1824 0.1746 0.0305  0.0430  -0.0155 5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.2023 0.2036 0.2389 0.0183  0.0454  -0.0597 5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.1421 0.1906 0.1648 0.0081  0.0264  0.0133  5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.2067 0.1957 0.2127 0.0005  0.0384  -0.0263 5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.2021 0.1818 0.1884 -0.0078 0.0524  -0.0167 5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.1596 0.1815 0.1728 0.0231  0.0274  0.0366  5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.1914 0.2267 0.1580 -0.0384 -0.0017 0.0041  5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.1731 0.2400 0.1629 -0.0122 0.0286  0.0520  5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.1765 0.2529 0.1802 -0.0082 0.0208  0.0509  5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.2088 0.1425 0.2049 -0.0170 0.0803  -0.0093 6   GLY A N   
36   C  CA  . GLY A 6   ? 0.2098 0.1413 0.2531 0.0469  0.0949  0.0231  6   GLY A CA  
37   C  C   . GLY A 6   ? 0.1357 0.1599 0.2314 -0.0026 0.0892  0.0080  6   GLY A C   
38   O  O   . GLY A 6   ? 0.1503 0.1753 0.2310 -0.0262 0.0838  -0.0276 6   GLY A O   
39   N  N   A TYR A 7   ? 0.0891 0.1173 0.2026 -0.0331 0.0480  -0.0237 7   TYR A N   
40   N  N   B TYR A 7   ? 0.1240 0.1220 0.3147 -0.0502 0.0582  0.0066  7   TYR A N   
41   C  CA  A TYR A 7   ? 0.1000 0.1115 0.1645 0.0007  0.0052  -0.0080 7   TYR A CA  
42   C  CA  B TYR A 7   ? 0.1148 0.1509 0.1738 0.0003  -0.0020 0.0634  7   TYR A CA  
43   C  C   A TYR A 7   ? 0.0800 0.1340 0.2452 -0.0030 -0.0102 0.0143  7   TYR A C   
44   C  C   B TYR A 7   ? 0.0971 0.1733 0.2296 0.0133  0.0164  0.0516  7   TYR A C   
45   O  O   A TYR A 7   ? 0.1057 0.1315 0.4449 -0.0076 0.0230  0.0214  7   TYR A O   
46   O  O   B TYR A 7   ? 0.0993 0.1429 0.4453 0.0267  0.0549  0.0822  7   TYR A O   
47   C  CB  A TYR A 7   ? 0.0886 0.0976 0.1474 0.0148  0.0299  0.0066  7   TYR A CB  
48   C  CB  B TYR A 7   ? 0.1137 0.1840 0.1506 -0.0116 -0.0103 0.0322  7   TYR A CB  
49   C  CG  A TYR A 7   ? 0.0930 0.1083 0.0926 0.0028  0.0068  -0.0054 7   TYR A CG  
50   C  CG  B TYR A 7   ? 0.1317 0.1624 0.1139 -0.0031 -0.0175 0.0493  7   TYR A CG  
51   C  CD1 A TYR A 7   ? 0.1369 0.1057 0.1004 0.0099  0.0046  0.0063  7   TYR A CD1 
52   C  CD1 B TYR A 7   ? 0.1049 0.1643 0.1356 0.0013  0.0366  0.0232  7   TYR A CD1 
53   C  CD2 A TYR A 7   ? 0.0997 0.1166 0.0980 0.0068  0.0188  -0.0173 7   TYR A CD2 
54   C  CD2 B TYR A 7   ? 0.1098 0.1745 0.1689 0.0054  0.0085  0.0088  7   TYR A CD2 
55   C  CE1 A TYR A 7   ? 0.0908 0.1263 0.1001 0.0096  0.0063  -0.0027 7   TYR A CE1 
56   C  CE1 B TYR A 7   ? 0.0768 0.1151 0.1805 0.0182  0.0155  0.0114  7   TYR A CE1 
57   C  CE2 A TYR A 7   ? 0.1162 0.1196 0.1164 0.0020  0.0183  -0.0099 7   TYR A CE2 
58   C  CE2 B TYR A 7   ? 0.1567 0.1555 0.1292 0.0155  0.0218  0.0052  7   TYR A CE2 
59   C  CZ  A TYR A 7   ? 0.1119 0.1002 0.1328 0.0137  0.0366  -0.0086 7   TYR A CZ  
60   C  CZ  B TYR A 7   ? 0.1206 0.1189 0.1353 0.0263  0.0217  0.0299  7   TYR A CZ  
61   O  OH  A TYR A 7   ? 0.1248 0.1261 0.1544 -0.0162 0.0000  0.0160  7   TYR A OH  
62   O  OH  B TYR A 7   ? 0.1530 0.1090 0.1260 0.0223  0.0260  0.0232  7   TYR A OH  
63   N  N   A GLY A 8   ? 0.0878 0.1240 0.2093 -0.0012 0.0098  -0.0157 8   GLY A N   
64   N  N   B GLY A 8   ? 0.1652 0.2060 0.1985 -0.0280 0.0751  0.0511  8   GLY A N   
65   C  CA  A GLY A 8   ? 0.1272 0.1581 0.2302 -0.0243 -0.0386 0.0414  8   GLY A CA  
66   C  CA  B GLY A 8   ? 0.1544 0.1128 0.2267 0.0088  0.0238  -0.0138 8   GLY A CA  
67   C  C   A GLY A 8   ? 0.1279 0.2164 0.1307 -0.0147 -0.0329 0.0632  8   GLY A C   
68   C  C   B GLY A 8   ? 0.0776 0.2009 0.2524 0.0231  -0.0076 0.0478  8   GLY A C   
69   O  O   A GLY A 8   ? 0.1178 0.1464 0.1527 -0.0318 0.0066  0.0322  8   GLY A O   
70   O  O   B GLY A 8   ? 0.2110 0.1886 0.3472 0.0973  0.2038  0.1350  8   GLY A O   
71   N  N   A LYS A 9   ? 0.1403 0.1438 0.1567 -0.0276 -0.0249 0.0203  9   LYS A N   
72   N  N   B LYS A 9   ? 0.1441 0.1585 0.2822 -0.0038 -0.0296 0.0333  9   LYS A N   
73   C  CA  A LYS A 9   ? 0.1600 0.1992 0.1242 -0.0353 -0.0236 0.0344  9   LYS A CA  
74   C  CA  B LYS A 9   ? 0.1348 0.2157 0.2567 0.0138  0.0024  -0.0232 9   LYS A CA  
75   C  C   A LYS A 9   ? 0.1430 0.1476 0.1501 -0.0445 -0.0218 0.0216  9   LYS A C   
76   C  C   B LYS A 9   ? 0.1202 0.1435 0.2480 -0.0152 0.0593  -0.0183 9   LYS A C   
77   O  O   A LYS A 9   ? 0.1565 0.2108 0.1348 -0.0250 -0.0266 0.0068  9   LYS A O   
78   O  O   B LYS A 9   ? 0.1851 0.2319 0.2495 -0.0110 0.0782  0.0184  9   LYS A O   
79   C  CB  A LYS A 9   ? 0.1744 0.1651 0.1933 -0.0533 -0.0450 0.0318  9   LYS A CB  
80   C  CB  B LYS A 9   ? 0.2524 0.1203 0.3431 0.0535  -0.0544 0.0057  9   LYS A CB  
81   C  CG  A LYS A 9   ? 0.2529 0.1759 0.2547 -0.0344 -0.0077 0.1243  9   LYS A CG  
82   N  N   A HIS A 10  ? 0.0979 0.1687 0.1965 -0.0557 0.0207  0.0070  10  HIS A N   
83   N  N   B HIS A 10  ? 0.1334 0.1518 0.1714 -0.0181 0.0318  0.0156  10  HIS A N   
84   C  CA  A HIS A 10  ? 0.0913 0.2131 0.1375 -0.0423 -0.0063 0.0186  10  HIS A CA  
85   C  CA  B HIS A 10  ? 0.0675 0.2461 0.1695 -0.0081 0.0027  0.0406  10  HIS A CA  
86   C  C   A HIS A 10  ? 0.0478 0.2313 0.1556 0.0148  -0.0148 0.0265  10  HIS A C   
87   C  C   B HIS A 10  ? 0.1526 0.2202 0.2800 0.0028  0.1054  0.0236  10  HIS A C   
88   O  O   A HIS A 10  ? 0.0648 0.1692 0.1987 0.0059  -0.0384 0.0511  10  HIS A O   
89   O  O   B HIS A 10  ? 0.1446 0.1685 0.2827 -0.0263 0.0947  0.0242  10  HIS A O   
90   C  CB  A HIS A 10  ? 0.0635 0.2384 0.1794 -0.0122 0.0267  0.0820  10  HIS A CB  
91   C  CB  B HIS A 10  ? 0.1017 0.1419 0.1861 -0.0030 0.0324  0.0086  10  HIS A CB  
92   C  CG  A HIS A 10  ? 0.1042 0.2061 0.1515 -0.0119 0.0137  0.0489  10  HIS A CG  
93   C  CG  B HIS A 10  ? 0.1080 0.1574 0.1913 -0.0111 0.0103  0.0219  10  HIS A CG  
94   N  ND1 A HIS A 10  ? 0.1682 0.1818 0.1119 -0.0190 0.0060  0.0271  10  HIS A ND1 
95   N  ND1 B HIS A 10  ? 0.1342 0.1767 0.2497 -0.0505 0.0129  0.0183  10  HIS A ND1 
96   C  CD2 A HIS A 10  ? 0.1398 0.2495 0.1740 -0.0428 0.0109  0.0948  10  HIS A CD2 
97   C  CD2 B HIS A 10  ? 0.1428 0.2169 0.2197 0.0249  -0.0485 0.0465  10  HIS A CD2 
98   C  CE1 A HIS A 10  ? 0.1430 0.1694 0.2224 -0.0318 0.0263  0.0298  10  HIS A CE1 
99   C  CE1 B HIS A 10  ? 0.1821 0.1726 0.2074 -0.0702 0.0055  0.0118  10  HIS A CE1 
100  N  NE2 A HIS A 10  ? 0.1872 0.1966 0.1916 -0.0087 0.0476  0.0751  10  HIS A NE2 
101  N  NE2 B HIS A 10  ? 0.2002 0.1890 0.1941 -0.0052 0.0575  0.0472  10  HIS A NE2 
102  N  N   . ASN A 11  ? 0.1568 0.2088 0.3740 -0.0430 0.1519  -0.0270 11  ASN A N   
103  C  CA  . ASN A 11  ? 0.1439 0.2031 0.3206 -0.0741 0.0979  -0.0405 11  ASN A CA  
104  C  C   . ASN A 11  ? 0.1738 0.1653 0.2863 -0.0595 0.1168  -0.0280 11  ASN A C   
105  O  O   . ASN A 11  ? 0.1650 0.2017 0.2757 -0.0671 0.1174  -0.0606 11  ASN A O   
106  C  CB  . ASN A 11  ? 0.1633 0.2117 0.3045 -0.0405 0.1237  -0.0504 11  ASN A CB  
107  C  CG  . ASN A 11  ? 0.2312 0.1793 0.2786 -0.0262 0.1233  0.0023  11  ASN A CG  
108  O  OD1 . ASN A 11  ? 0.2527 0.2081 0.3267 -0.0320 0.1196  -0.0476 11  ASN A OD1 
109  N  ND2 . ASN A 11  ? 0.2608 0.2080 0.2865 0.0020  0.1307  -0.0227 11  ASN A ND2 
110  N  N   . GLY A 12  ? 0.1743 0.1877 0.2693 -0.0384 0.1160  -0.0355 12  GLY A N   
111  C  CA  . GLY A 12  ? 0.1439 0.2089 0.2509 -0.0419 0.1005  0.0063  12  GLY A CA  
112  C  C   . GLY A 12  ? 0.1495 0.1495 0.2397 -0.0266 0.0637  -0.0458 12  GLY A C   
113  O  O   . GLY A 12  ? 0.1099 0.1604 0.2468 -0.0326 0.0546  -0.0331 12  GLY A O   
114  N  N   . PRO A 13  ? 0.1299 0.1230 0.2493 -0.0131 0.0800  -0.0032 13  PRO A N   
115  C  CA  . PRO A 13  ? 0.1125 0.1317 0.2711 -0.0218 0.0656  0.0038  13  PRO A CA  
116  C  C   . PRO A 13  ? 0.1541 0.1164 0.2213 -0.0046 0.0693  0.0103  13  PRO A C   
117  O  O   . PRO A 13  ? 0.1036 0.1583 0.2316 0.0043  0.0474  0.0171  13  PRO A O   
118  C  CB  . PRO A 13  ? 0.1711 0.1425 0.2011 0.0094  0.0887  0.0166  13  PRO A CB  
119  C  CG  . PRO A 13  ? 0.1489 0.1571 0.2090 0.0073  0.0588  0.0359  13  PRO A CG  
120  C  CD  . PRO A 13  ? 0.1456 0.1785 0.2022 -0.0182 0.0851  -0.0100 13  PRO A CD  
121  N  N   . GLU A 14  ? 0.1826 0.1193 0.2257 -0.0300 0.0628  -0.0115 14  GLU A N   
122  C  CA  . GLU A 14  ? 0.2177 0.1697 0.2383 -0.0476 0.0738  -0.0394 14  GLU A CA  
123  C  C   . GLU A 14  ? 0.1261 0.2072 0.2350 -0.0759 0.0375  -0.0461 14  GLU A C   
124  O  O   . GLU A 14  ? 0.1748 0.1860 0.2657 -0.0798 0.0715  -0.0680 14  GLU A O   
125  C  CB  . GLU A 14  ? 0.3526 0.1572 0.2766 -0.0386 0.0476  -0.0183 14  GLU A CB  
126  C  CG  . GLU A 14  ? 0.2434 0.2739 0.2876 -0.0384 -0.0289 0.0509  14  GLU A CG  
127  C  CD  . GLU A 14  ? 0.2928 0.2390 0.3418 -0.0637 -0.0684 0.0286  14  GLU A CD  
128  O  OE1 . GLU A 14  ? 0.2469 0.2387 0.2926 -0.0974 -0.0666 0.0869  14  GLU A OE1 
129  O  OE2 . GLU A 14  ? 0.5335 0.1976 0.2883 0.0241  0.0974  0.0264  14  GLU A OE2 
130  N  N   . HIS A 15  ? 0.1421 0.1414 0.2316 -0.0423 0.0498  -0.0239 15  HIS A N   
131  C  CA  . HIS A 15  ? 0.1319 0.1686 0.2198 -0.0441 0.0557  -0.0397 15  HIS A CA  
132  C  C   . HIS A 15  ? 0.0983 0.1612 0.2594 -0.0342 0.0553  -0.0302 15  HIS A C   
133  O  O   . HIS A 15  ? 0.0860 0.1678 0.3001 -0.0275 0.0252  -0.0474 15  HIS A O   
134  C  CB  . HIS A 15  ? 0.1121 0.1844 0.2755 -0.0631 0.0555  -0.0487 15  HIS A CB  
135  C  CG  . HIS A 15  ? 0.1418 0.2161 0.2452 -0.0769 0.0568  -0.0551 15  HIS A CG  
136  N  ND1 . HIS A 15  ? 0.1632 0.2793 0.2500 -0.1142 0.0458  -0.0434 15  HIS A ND1 
137  C  CD2 . HIS A 15  ? 0.2430 0.2001 0.3104 -0.1173 0.1180  -0.0233 15  HIS A CD2 
138  C  CE1 . HIS A 15  ? 0.3098 0.3427 0.3043 -0.2268 -0.0046 0.0068  15  HIS A CE1 
139  N  NE2 . HIS A 15  ? 0.2942 0.2614 0.2856 -0.1673 0.0617  -0.0351 15  HIS A NE2 
140  N  N   . TRP A 16  ? 0.0868 0.1369 0.2506 -0.0247 0.0256  -0.0210 16  TRP A N   
141  C  CA  . TRP A 16  ? 0.0703 0.1209 0.2558 -0.0172 0.0124  0.0048  16  TRP A CA  
142  C  C   . TRP A 16  ? 0.0494 0.1460 0.2486 -0.0164 0.0107  -0.0434 16  TRP A C   
143  O  O   . TRP A 16  ? 0.0781 0.1374 0.2664 -0.0109 -0.0120 -0.0265 16  TRP A O   
144  C  CB  . TRP A 16  ? 0.0716 0.1524 0.2187 -0.0210 0.0304  -0.0005 16  TRP A CB  
145  C  CG  . TRP A 16  ? 0.0965 0.1112 0.1880 0.0055  0.0046  0.0074  16  TRP A CG  
146  C  CD1 . TRP A 16  ? 0.1182 0.1404 0.1777 -0.0071 0.0509  -0.0041 16  TRP A CD1 
147  C  CD2 . TRP A 16  ? 0.0891 0.0948 0.2251 -0.0082 0.0340  -0.0131 16  TRP A CD2 
148  N  NE1 . TRP A 16  ? 0.0980 0.1401 0.1978 -0.0130 0.0399  -0.0054 16  TRP A NE1 
149  C  CE2 . TRP A 16  ? 0.1054 0.1089 0.1923 -0.0083 0.0496  -0.0003 16  TRP A CE2 
150  C  CE3 . TRP A 16  ? 0.0754 0.1184 0.2050 -0.0143 0.0225  -0.0110 16  TRP A CE3 
151  C  CZ2 . TRP A 16  ? 0.1094 0.1102 0.1606 -0.0003 0.0344  -0.0077 16  TRP A CZ2 
152  C  CZ3 . TRP A 16  ? 0.0833 0.1116 0.2016 -0.0035 0.0146  0.0070  16  TRP A CZ3 
153  C  CH2 . TRP A 16  ? 0.1005 0.1169 0.1885 -0.0100 0.0298  0.0094  16  TRP A CH2 
154  N  N   . HIS A 17  ? 0.0771 0.1490 0.2412 -0.0151 0.0076  0.0094  17  HIS A N   
155  C  CA  . HIS A 17  ? 0.0653 0.1793 0.2509 -0.0185 0.0063  -0.0390 17  HIS A CA  
156  C  C   . HIS A 17  ? 0.0675 0.1643 0.3154 -0.0013 -0.0272 -0.0430 17  HIS A C   
157  O  O   . HIS A 17  ? 0.0658 0.2105 0.3251 0.0059  -0.0214 -0.0270 17  HIS A O   
158  C  CB  . HIS A 17  ? 0.0740 0.1891 0.2734 -0.0057 -0.0046 -0.0267 17  HIS A CB  
159  C  CG  . HIS A 17  ? 0.0712 0.2099 0.3183 -0.0206 -0.0264 -0.0732 17  HIS A CG  
160  N  ND1 . HIS A 17  ? 0.1008 0.2700 0.3246 -0.0110 -0.0221 -0.0671 17  HIS A ND1 
161  C  CD2 . HIS A 17  ? 0.1193 0.2255 0.3519 -0.0533 -0.0083 -0.1022 17  HIS A CD2 
162  C  CE1 . HIS A 17  ? 0.0873 0.2766 0.3091 -0.0458 0.0173  -0.0808 17  HIS A CE1 
163  N  NE2 . HIS A 17  ? 0.1297 0.2125 0.3235 -0.0423 -0.0098 -0.0900 17  HIS A NE2 
164  N  N   . LYS A 18  ? 0.0596 0.1748 0.3190 -0.0220 0.0148  -0.0353 18  LYS A N   
165  C  CA  . LYS A 18  ? 0.0621 0.2284 0.3246 0.0017  -0.0010 -0.0636 18  LYS A CA  
166  C  C   . LYS A 18  ? 0.0733 0.2265 0.3386 0.0121  -0.0073 -0.0540 18  LYS A C   
167  O  O   . LYS A 18  ? 0.1202 0.2336 0.5325 0.0505  -0.0746 -0.1492 18  LYS A O   
168  C  CB  . LYS A 18  ? 0.0939 0.2448 0.3097 -0.0188 0.0105  -0.0851 18  LYS A CB  
169  C  CG  . LYS A 18  ? 0.1089 0.2522 0.3251 -0.0553 -0.0040 -0.0557 18  LYS A CG  
170  C  CD  . LYS A 18  ? 0.0883 0.2958 0.3258 -0.0621 0.0203  -0.0995 18  LYS A CD  
171  C  CE  . LYS A 18  ? 0.0988 0.2843 0.3300 -0.0754 0.0113  -0.1111 18  LYS A CE  
172  N  NZ  . LYS A 18  ? 0.0742 0.2991 0.3400 -0.0855 0.0533  -0.1212 18  LYS A NZ  
173  N  N   . ASP A 19  ? 0.0803 0.2280 0.2944 -0.0080 0.0087  -0.0715 19  ASP A N   
174  C  CA  . ASP A 19  ? 0.1368 0.2152 0.3404 0.0028  0.0081  -0.0808 19  ASP A CA  
175  C  C   . ASP A 19  ? 0.0755 0.1678 0.3815 0.0163  0.0179  -0.0753 19  ASP A C   
176  O  O   . ASP A 19  ? 0.1164 0.1782 0.3815 0.0281  0.0248  -0.0680 19  ASP A O   
177  C  CB  . ASP A 19  ? 0.1538 0.3027 0.3100 -0.0403 0.0001  -0.0859 19  ASP A CB  
178  C  CG  . ASP A 19  ? 0.2181 0.4074 0.4679 -0.0049 0.1124  -0.0197 19  ASP A CG  
179  O  OD1 . ASP A 19  ? 0.2833 0.4440 0.3718 0.0463  0.1125  -0.0781 19  ASP A OD1 
180  O  OD2 . ASP A 19  ? 0.4779 0.6525 0.5493 -0.0303 0.0447  0.0773  19  ASP A OD2 
181  N  N   . PHE A 20  ? 0.0604 0.1553 0.3249 0.0041  -0.0174 -0.0399 20  PHE A N   
182  C  CA  . PHE A 20  ? 0.0688 0.1458 0.3127 0.0121  -0.0121 -0.0485 20  PHE A CA  
183  C  C   . PHE A 20  ? 0.0760 0.1500 0.2773 0.0165  0.0142  -0.0006 20  PHE A C   
184  O  O   . PHE A 20  ? 0.0942 0.1376 0.2700 0.0115  -0.0109 -0.0177 20  PHE A O   
185  C  CB  . PHE A 20  ? 0.1018 0.1669 0.2732 0.0099  -0.0109 -0.0439 20  PHE A CB  
186  C  CG  . PHE A 20  ? 0.0771 0.2240 0.2700 0.0456  0.0006  -0.0645 20  PHE A CG  
187  C  CD1 . PHE A 20  ? 0.0930 0.2331 0.2940 0.0241  0.0228  -0.0584 20  PHE A CD1 
188  C  CD2 . PHE A 20  ? 0.0934 0.2757 0.3068 0.0168  0.0333  -0.0410 20  PHE A CD2 
189  C  CE1 . PHE A 20  ? 0.1152 0.2967 0.3186 0.0052  0.0109  -0.0913 20  PHE A CE1 
190  C  CE2 . PHE A 20  ? 0.1615 0.3059 0.3104 0.0269  -0.0019 -0.0621 20  PHE A CE2 
191  C  CZ  . PHE A 20  ? 0.1106 0.3253 0.3091 0.0364  0.0239  -0.0674 20  PHE A CZ  
192  N  N   . PRO A 21  ? 0.0916 0.1703 0.2691 0.0273  -0.0136 -0.0195 21  PRO A N   
193  C  CA  . PRO A 21  ? 0.0724 0.1860 0.3115 0.0318  -0.0390 -0.0239 21  PRO A CA  
194  C  C   . PRO A 21  ? 0.0904 0.1744 0.2786 0.0160  -0.0639 0.0189  21  PRO A C   
195  O  O   . PRO A 21  ? 0.1032 0.1861 0.2700 -0.0020 -0.0577 -0.0046 21  PRO A O   
196  C  CB  . PRO A 21  ? 0.1348 0.3364 0.3084 0.1238  -0.0855 -0.0671 21  PRO A CB  
197  C  CG  . PRO A 21  ? 0.2849 0.3458 0.3558 0.1849  -0.1077 -0.0793 21  PRO A CG  
198  C  CD  . PRO A 21  ? 0.1395 0.2140 0.3398 0.0592  -0.0307 -0.0263 21  PRO A CD  
199  N  N   A ILE A 22  ? 0.0458 0.1924 0.2432 0.0222  -0.0155 -0.0135 22  ILE A N   
200  N  N   B ILE A 22  ? 0.0829 0.1177 0.2291 0.0412  -0.0504 0.0163  22  ILE A N   
201  C  CA  A ILE A 22  ? 0.0359 0.1570 0.2350 0.0273  -0.0157 0.0054  22  ILE A CA  
202  C  CA  B ILE A 22  ? 0.1098 0.1468 0.1712 0.0119  -0.0419 0.0063  22  ILE A CA  
203  C  C   A ILE A 22  ? 0.0789 0.1353 0.2107 -0.0035 -0.0230 0.0137  22  ILE A C   
204  C  C   B ILE A 22  ? 0.1048 0.1278 0.1824 -0.0077 -0.0324 -0.0035 22  ILE A C   
205  O  O   A ILE A 22  ? 0.0737 0.1048 0.1907 0.0146  -0.0184 0.0152  22  ILE A O   
206  O  O   B ILE A 22  ? 0.1123 0.1368 0.1463 -0.0097 -0.0230 -0.0207 22  ILE A O   
207  C  CB  A ILE A 22  ? 0.1164 0.1460 0.1929 0.0160  -0.0215 -0.0007 22  ILE A CB  
208  C  CB  B ILE A 22  ? 0.0851 0.1229 0.1590 0.0156  -0.0289 0.0200  22  ILE A CB  
209  C  CG1 A ILE A 22  ? 0.1648 0.1692 0.1896 -0.0253 0.0059  -0.0153 22  ILE A CG1 
210  C  CG1 B ILE A 22  ? 0.1093 0.1172 0.1692 0.0217  -0.0226 0.0173  22  ILE A CG1 
211  C  CG2 A ILE A 22  ? 0.1085 0.1209 0.1909 -0.0102 -0.0083 0.0105  22  ILE A CG2 
212  C  CG2 B ILE A 22  ? 0.1157 0.1507 0.1046 0.0447  -0.0083 -0.0164 22  ILE A CG2 
213  C  CD1 A ILE A 22  ? 0.1902 0.2576 0.2960 0.0406  -0.0373 0.0631  22  ILE A CD1 
214  C  CD1 B ILE A 22  ? 0.1289 0.1186 0.2372 -0.0031 -0.0516 0.0359  22  ILE A CD1 
215  N  N   . ALA A 23  ? 0.0732 0.1414 0.2038 0.0131  -0.0179 0.0071  23  ALA A N   
216  C  CA  . ALA A 23  ? 0.0874 0.1247 0.2035 0.0083  -0.0012 0.0088  23  ALA A CA  
217  C  C   . ALA A 23  ? 0.0816 0.1352 0.2263 0.0019  -0.0161 0.0331  23  ALA A C   
218  O  O   . ALA A 23  ? 0.0917 0.1441 0.2080 0.0103  -0.0200 0.0057  23  ALA A O   
219  C  CB  . ALA A 23  ? 0.0684 0.1339 0.2259 -0.0035 -0.0211 0.0189  23  ALA A CB  
220  N  N   . LYS A 24  ? 0.1229 0.1365 0.2074 -0.0013 -0.0300 0.0132  24  LYS A N   
221  C  CA  . LYS A 24  ? 0.1024 0.1551 0.2157 0.0097  -0.0184 0.0093  24  LYS A CA  
222  C  C   . LYS A 24  ? 0.1307 0.1749 0.2099 0.0227  -0.0496 0.0199  24  LYS A C   
223  O  O   . LYS A 24  ? 0.1354 0.2284 0.2240 0.0184  -0.0520 0.0144  24  LYS A O   
224  C  CB  . LYS A 24  ? 0.1172 0.1993 0.2426 -0.0200 -0.0315 -0.0183 24  LYS A CB  
225  C  CG  . LYS A 24  ? 0.1266 0.2497 0.2161 -0.0132 -0.0214 -0.0388 24  LYS A CG  
226  C  CD  . LYS A 24  ? 0.1280 0.3506 0.3045 -0.0542 -0.0295 -0.0342 24  LYS A CD  
227  C  CE  . LYS A 24  ? 0.1553 0.3770 0.3386 -0.1086 0.0046  -0.0781 24  LYS A CE  
228  N  NZ  . LYS A 24  ? 0.3858 0.3068 0.5047 -0.0746 0.0310  -0.0289 24  LYS A NZ  
229  N  N   . GLY A 25  ? 0.0926 0.1621 0.2245 0.0105  -0.0421 0.0188  25  GLY A N   
230  C  CA  . GLY A 25  ? 0.1516 0.1815 0.2248 0.0142  -0.0353 0.0489  25  GLY A CA  
231  C  C   . GLY A 25  ? 0.1439 0.1915 0.1553 0.0168  -0.0430 0.0478  25  GLY A C   
232  O  O   . GLY A 25  ? 0.1384 0.2097 0.1702 -0.0019 -0.0436 0.0322  25  GLY A O   
233  N  N   . GLU A 26  ? 0.1430 0.2205 0.1528 0.0003  -0.0586 0.0526  26  GLU A N   
234  C  CA  . GLU A 26  ? 0.1473 0.2511 0.1436 0.0164  -0.0480 0.0350  26  GLU A CA  
235  C  C   . GLU A 26  ? 0.1507 0.1855 0.1272 -0.0071 -0.0373 0.0401  26  GLU A C   
236  O  O   . GLU A 26  ? 0.1850 0.2380 0.1151 0.0082  -0.0529 0.0010  26  GLU A O   
237  C  CB  . GLU A 26  ? 0.1957 0.2935 0.1895 -0.0046 -0.0775 0.1005  26  GLU A CB  
238  C  CG  . GLU A 26  ? 0.1992 0.3467 0.1995 0.0294  -0.0732 0.0786  26  GLU A CG  
239  C  CD  . GLU A 26  ? 0.4481 0.4871 0.1968 -0.0126 -0.1400 0.0148  26  GLU A CD  
240  O  OE1 . GLU A 26  ? 0.3928 0.4275 0.2825 -0.0315 -0.0983 0.0535  26  GLU A OE1 
241  O  OE2 . GLU A 26  ? 0.4361 0.5439 0.5109 -0.0987 -0.1689 -0.0012 26  GLU A OE2 
242  N  N   . ARG A 27  ? 0.1198 0.1395 0.1321 -0.0008 -0.0364 0.0412  27  ARG A N   
243  C  CA  . ARG A 27  ? 0.1011 0.1132 0.1202 -0.0007 -0.0160 0.0242  27  ARG A CA  
244  C  C   . ARG A 27  ? 0.1057 0.1058 0.1072 0.0035  -0.0093 0.0198  27  ARG A C   
245  O  O   . ARG A 27  ? 0.0944 0.1222 0.1072 -0.0046 -0.0185 0.0093  27  ARG A O   
246  C  CB  . ARG A 27  ? 0.1903 0.1350 0.1495 -0.0120 -0.0344 0.0417  27  ARG A CB  
247  C  CG  . ARG A 27  ? 0.1800 0.1860 0.1528 -0.0013 -0.0273 0.0194  27  ARG A CG  
248  C  CD  . ARG A 27  ? 0.2190 0.2433 0.1169 -0.0317 -0.0317 0.0066  27  ARG A CD  
249  N  NE  . ARG A 27  ? 0.2263 0.1665 0.1447 -0.0126 0.0060  0.0209  27  ARG A NE  
250  C  CZ  . ARG A 27  ? 0.1794 0.1723 0.1063 -0.0236 0.0093  -0.0176 27  ARG A CZ  
251  N  NH1 . ARG A 27  ? 0.1704 0.2587 0.1861 -0.0447 -0.0274 0.1422  27  ARG A NH1 
252  N  NH2 . ARG A 27  ? 0.1843 0.1727 0.1635 -0.0023 0.0031  0.0328  27  ARG A NH2 
253  N  N   . GLN A 28  ? 0.1031 0.1050 0.1023 0.0017  -0.0243 0.0278  28  GLN A N   
254  C  CA  . GLN A 28  ? 0.0795 0.1027 0.1233 0.0031  -0.0193 0.0137  28  GLN A CA  
255  C  C   . GLN A 28  ? 0.0913 0.0926 0.1058 -0.0057 -0.0114 0.0104  28  GLN A C   
256  O  O   . GLN A 28  ? 0.1009 0.1119 0.0954 0.0104  -0.0230 0.0027  28  GLN A O   
257  C  CB  . GLN A 28  ? 0.0741 0.1099 0.1421 0.0040  -0.0165 0.0126  28  GLN A CB  
258  C  CG  . GLN A 28  ? 0.0876 0.1196 0.1393 -0.0063 -0.0156 0.0309  28  GLN A CG  
259  C  CD  . GLN A 28  ? 0.0940 0.1036 0.1456 0.0120  -0.0357 0.0197  28  GLN A CD  
260  O  OE1 . GLN A 28  ? 0.0847 0.1013 0.1430 0.0087  -0.0089 0.0196  28  GLN A OE1 
261  N  NE2 . GLN A 28  ? 0.0768 0.1124 0.1421 0.0023  -0.0142 0.0286  28  GLN A NE2 
262  N  N   . SER A 29  ? 0.0727 0.0978 0.1018 -0.0046 -0.0135 0.0147  29  SER A N   
263  C  CA  . SER A 29  ? 0.0640 0.0873 0.1015 0.0020  -0.0082 0.0126  29  SER A CA  
264  C  C   . SER A 29  ? 0.0715 0.0825 0.0856 0.0031  -0.0098 0.0081  29  SER A C   
265  O  O   . SER A 29  ? 0.0780 0.0886 0.1103 0.0074  0.0048  0.0087  29  SER A O   
266  C  CB  . SER A 29  ? 0.0693 0.0803 0.0983 -0.0068 -0.0085 0.0110  29  SER A CB  
267  O  OG  . SER A 29  ? 0.0856 0.0780 0.1045 -0.0043 -0.0024 0.0142  29  SER A OG  
268  N  N   . PRO A 30  ? 0.0623 0.0740 0.1005 0.0031  -0.0062 0.0141  30  PRO A N   
269  C  CA  . PRO A 30  ? 0.0609 0.0769 0.0970 -0.0010 0.0000  0.0015  30  PRO A CA  
270  C  C   . PRO A 30  ? 0.0816 0.0715 0.0927 -0.0076 -0.0003 0.0054  30  PRO A C   
271  O  O   . PRO A 30  ? 0.0882 0.0874 0.1027 -0.0074 -0.0131 0.0007  30  PRO A O   
272  C  CB  . PRO A 30  ? 0.0769 0.0794 0.0932 -0.0035 0.0038  0.0124  30  PRO A CB  
273  C  CG  . PRO A 30  ? 0.0799 0.0938 0.1049 -0.0082 0.0065  0.0088  30  PRO A CG  
274  C  CD  . PRO A 30  ? 0.0847 0.0878 0.0940 -0.0044 0.0035  0.0152  30  PRO A CD  
275  N  N   . VAL A 31  ? 0.0975 0.0835 0.0931 -0.0099 -0.0001 -0.0057 31  VAL A N   
276  C  CA  . VAL A 31  ? 0.1114 0.0859 0.0834 -0.0035 -0.0113 -0.0099 31  VAL A CA  
277  C  C   . VAL A 31  ? 0.0988 0.0826 0.1001 -0.0176 0.0017  0.0013  31  VAL A C   
278  O  O   . VAL A 31  ? 0.0931 0.0970 0.1125 -0.0040 -0.0156 -0.0199 31  VAL A O   
279  C  CB  . VAL A 31  ? 0.1198 0.0891 0.1134 -0.0054 -0.0008 0.0082  31  VAL A CB  
280  C  CG1 . VAL A 31  ? 0.1240 0.0974 0.1157 0.0052  -0.0015 0.0065  31  VAL A CG1 
281  C  CG2 . VAL A 31  ? 0.1062 0.1011 0.1277 -0.0118 0.0151  0.0037  31  VAL A CG2 
282  N  N   . ASP A 32  ? 0.1023 0.0848 0.1032 -0.0096 -0.0093 -0.0092 32  ASP A N   
283  C  CA  . ASP A 32  ? 0.1238 0.0781 0.1026 -0.0124 0.0041  -0.0093 32  ASP A CA  
284  C  C   . ASP A 32  ? 0.1087 0.0956 0.0969 -0.0198 -0.0086 -0.0186 32  ASP A C   
285  O  O   . ASP A 32  ? 0.1172 0.1425 0.1202 -0.0001 -0.0057 0.0192  32  ASP A O   
286  C  CB  . ASP A 32  ? 0.1236 0.0922 0.1231 -0.0212 -0.0054 -0.0220 32  ASP A CB  
287  C  CG  . ASP A 32  ? 0.1506 0.0935 0.1173 -0.0190 -0.0040 -0.0248 32  ASP A CG  
288  O  OD1 . ASP A 32  ? 0.1339 0.0995 0.1157 -0.0048 -0.0133 -0.0111 32  ASP A OD1 
289  O  OD2 . ASP A 32  ? 0.2223 0.1239 0.1216 0.0175  -0.0130 -0.0335 32  ASP A OD2 
290  N  N   . ILE A 33  ? 0.0973 0.0998 0.0923 -0.0103 0.0012  -0.0160 33  ILE A N   
291  C  CA  . ILE A 33  ? 0.1108 0.1008 0.1128 -0.0082 0.0087  -0.0076 33  ILE A CA  
292  C  C   . ILE A 33  ? 0.1281 0.1225 0.1015 -0.0177 0.0277  -0.0217 33  ILE A C   
293  O  O   . ILE A 33  ? 0.1441 0.1119 0.1198 -0.0097 0.0138  -0.0239 33  ILE A O   
294  C  CB  . ILE A 33  ? 0.0947 0.1130 0.1287 -0.0073 -0.0006 -0.0228 33  ILE A CB  
295  C  CG1 . ILE A 33  ? 0.1299 0.1076 0.1277 -0.0183 -0.0130 -0.0359 33  ILE A CG1 
296  C  CG2 . ILE A 33  ? 0.1128 0.1430 0.1678 -0.0226 0.0256  -0.0122 33  ILE A CG2 
297  C  CD1 . ILE A 33  ? 0.1191 0.1469 0.1462 -0.0013 -0.0178 -0.0406 33  ILE A CD1 
298  N  N   A ASP A 34  ? 0.1604 0.1465 0.1063 -0.0324 0.0192  -0.0200 34  ASP A N   
299  N  N   B ASP A 34  ? 0.1561 0.1334 0.1105 -0.0162 0.0083  -0.0386 34  ASP A N   
300  C  CA  A ASP A 34  ? 0.1805 0.1506 0.1075 -0.0522 0.0421  -0.0377 34  ASP A CA  
301  C  CA  B ASP A 34  ? 0.1756 0.1485 0.1187 -0.0348 0.0278  -0.0617 34  ASP A CA  
302  C  C   A ASP A 34  ? 0.2036 0.1535 0.1330 -0.0736 0.0529  -0.0595 34  ASP A C   
303  C  C   B ASP A 34  ? 0.2194 0.1555 0.1146 -0.0564 0.0551  -0.0724 34  ASP A C   
304  O  O   A ASP A 34  ? 0.2378 0.1754 0.1476 -0.0969 0.0357  -0.0355 34  ASP A O   
305  O  O   B ASP A 34  ? 0.2750 0.1864 0.1442 -0.0362 0.0678  -0.0310 34  ASP A O   
306  C  CB  A ASP A 34  ? 0.1715 0.2034 0.1076 -0.0445 0.0593  -0.0359 34  ASP A CB  
307  C  CB  B ASP A 34  ? 0.2520 0.1570 0.1578 -0.0355 -0.0162 -0.0540 34  ASP A CB  
308  C  CG  A ASP A 34  ? 0.1833 0.1914 0.1445 -0.0724 0.0197  -0.0627 34  ASP A CG  
309  C  CG  B ASP A 34  ? 0.3847 0.1775 0.1358 -0.0888 0.0192  -0.0665 34  ASP A CG  
310  O  OD1 A ASP A 34  ? 0.2092 0.1975 0.1193 -0.0593 0.0245  -0.0710 34  ASP A OD1 
311  O  OD1 B ASP A 34  ? 0.3497 0.2049 0.2076 -0.1288 0.0315  -0.0825 34  ASP A OD1 
312  O  OD2 A ASP A 34  ? 0.1755 0.3228 0.1783 -0.0430 0.0114  -0.1413 34  ASP A OD2 
313  O  OD2 B ASP A 34  ? 0.3147 0.2678 0.2017 -0.0606 0.0625  -0.0588 34  ASP A OD2 
314  N  N   . THR A 35  ? 0.1888 0.1872 0.1492 -0.0507 0.0454  -0.0817 35  THR A N   
315  C  CA  . THR A 35  ? 0.1802 0.1985 0.1459 -0.0777 0.0500  -0.0610 35  THR A CA  
316  C  C   . THR A 35  ? 0.2011 0.1729 0.1468 -0.0617 0.0719  -0.0592 35  THR A C   
317  O  O   . THR A 35  ? 0.2727 0.2065 0.1743 -0.0991 0.0710  -0.0631 35  THR A O   
318  C  CB  . THR A 35  ? 0.1596 0.2268 0.2020 -0.0395 0.0395  -0.0905 35  THR A CB  
319  O  OG1 . THR A 35  ? 0.2034 0.2175 0.1961 -0.0538 0.0571  -0.0848 35  THR A OG1 
320  C  CG2 . THR A 35  ? 0.2177 0.2675 0.2012 -0.0766 0.0707  -0.0991 35  THR A CG2 
321  N  N   . HIS A 36  ? 0.2827 0.1636 0.1314 -0.0581 0.0627  -0.0722 36  HIS A N   
322  C  CA  . HIS A 36  ? 0.3127 0.1708 0.1351 -0.0331 0.0723  -0.0575 36  HIS A CA  
323  C  C   . HIS A 36  ? 0.3055 0.2154 0.1442 -0.0549 0.0707  -0.0662 36  HIS A C   
324  O  O   . HIS A 36  ? 0.2533 0.3479 0.1376 -0.0869 0.0251  -0.0487 36  HIS A O   
325  C  CB  . HIS A 36  ? 0.3504 0.2275 0.1425 -0.0434 0.0102  -0.1005 36  HIS A CB  
326  C  CG  . HIS A 36  ? 0.3772 0.1536 0.1756 -0.0383 -0.0181 -0.0703 36  HIS A CG  
327  N  ND1 . HIS A 36  ? 0.3666 0.2412 0.1783 0.0311  -0.0614 -0.0412 36  HIS A ND1 
328  C  CD2 . HIS A 36  ? 0.4242 0.1597 0.2230 -0.0586 -0.0901 -0.0687 36  HIS A CD2 
329  C  CE1 . HIS A 36  ? 0.3970 0.2669 0.2391 0.0449  -0.1535 -0.0685 36  HIS A CE1 
330  N  NE2 . HIS A 36  ? 0.5196 0.2475 0.2930 -0.0465 0.0103  -0.0714 36  HIS A NE2 
331  N  N   . THR A 37  ? 0.3249 0.1703 0.1719 -0.0672 0.0829  -0.0447 37  THR A N   
332  C  CA  . THR A 37  ? 0.2906 0.1868 0.1419 -0.0762 0.0304  -0.0694 37  THR A CA  
333  C  C   . THR A 37  ? 0.2480 0.2108 0.1767 -0.0905 0.0333  -0.0176 37  THR A C   
334  O  O   . THR A 37  ? 0.4104 0.2504 0.1653 -0.1315 -0.0320 -0.0210 37  THR A O   
335  C  CB  . THR A 37  ? 0.2836 0.2379 0.4600 -0.0799 -0.1180 -0.0759 37  THR A CB  
336  O  OG1 . THR A 37  ? 0.3637 0.2933 0.4458 -0.0975 -0.0232 -0.1155 37  THR A OG1 
337  C  CG2 . THR A 37  ? 0.3063 0.3429 0.2185 -0.1040 -0.0372 -0.1052 37  THR A CG2 
338  N  N   . ALA A 38  ? 0.2511 0.1955 0.1198 -0.0754 0.0476  -0.0439 38  ALA A N   
339  C  CA  . ALA A 38  ? 0.2536 0.1705 0.1288 -0.0603 0.0549  -0.0390 38  ALA A CA  
340  C  C   . ALA A 38  ? 0.2612 0.1903 0.1829 -0.0672 0.0930  -0.0829 38  ALA A C   
341  O  O   . ALA A 38  ? 0.3244 0.2053 0.3109 -0.0791 0.1653  -0.0799 38  ALA A O   
342  C  CB  . ALA A 38  ? 0.2005 0.1794 0.1770 -0.0511 0.0240  -0.0115 38  ALA A CB  
343  N  N   . LYS A 39  ? 0.2865 0.2124 0.1345 -0.1203 0.0221  -0.0070 39  LYS A N   
344  C  CA  . LYS A 39  ? 0.3115 0.3564 0.1224 -0.1817 0.0282  -0.0111 39  LYS A CA  
345  C  C   . LYS A 39  ? 0.2185 0.2458 0.1072 -0.0982 0.0255  -0.0026 39  LYS A C   
346  O  O   . LYS A 39  ? 0.1642 0.2433 0.1168 -0.0588 0.0131  -0.0092 39  LYS A O   
347  C  CB  . LYS A 39  ? 0.3181 0.5842 0.2664 -0.3233 -0.1512 0.2316  39  LYS A CB  
348  C  CG  . LYS A 39  ? 0.4575 0.9268 0.4086 -0.2833 -0.1209 0.2034  39  LYS A CG  
349  C  CD  . LYS A 39  ? 0.5658 0.8529 0.3486 -0.0802 -0.0491 0.0637  39  LYS A CD  
350  C  CE  . LYS A 39  ? 0.7728 0.7174 0.5073 0.1339  0.2994  -0.1783 39  LYS A CE  
351  N  NZ  . LYS A 39  ? 0.5730 1.4259 1.0190 0.0214  0.0784  -0.3928 39  LYS A NZ  
352  N  N   . TYR A 40  ? 0.2899 0.2705 0.1328 -0.0903 0.0511  -0.0463 40  TYR A N   
353  C  CA  . TYR A 40  ? 0.2143 0.2002 0.1481 -0.0209 0.0626  -0.0189 40  TYR A CA  
354  C  C   . TYR A 40  ? 0.1557 0.2154 0.1512 0.0021  0.0264  -0.0324 40  TYR A C   
355  O  O   . TYR A 40  ? 0.2141 0.3086 0.1142 -0.0658 0.0265  -0.0207 40  TYR A O   
356  C  CB  . TYR A 40  ? 0.3143 0.2854 0.1908 0.0595  0.1031  -0.0335 40  TYR A CB  
357  C  CG  . TYR A 40  ? 0.2734 0.3289 0.1859 0.0873  0.0944  -0.0054 40  TYR A CG  
358  C  CD1 . TYR A 40  ? 0.2921 0.3170 0.1977 0.0571  0.0344  0.0487  40  TYR A CD1 
359  C  CD2 . TYR A 40  ? 0.3282 0.3948 0.2490 -0.0315 0.1367  -0.0566 40  TYR A CD2 
360  C  CE1 . TYR A 40  ? 0.2770 0.3835 0.1928 0.0665  0.0582  0.0206  40  TYR A CE1 
361  C  CE2 . TYR A 40  ? 0.2763 0.5103 0.2222 -0.0152 0.0811  -0.0240 40  TYR A CE2 
362  C  CZ  . TYR A 40  ? 0.2343 0.5784 0.2232 0.0021  0.0498  0.0176  40  TYR A CZ  
363  O  OH  . TYR A 40  ? 0.2249 0.7102 0.3199 -0.0617 0.0623  0.0637  40  TYR A OH  
364  N  N   . ASP A 41  ? 0.1603 0.1763 0.1724 -0.0362 0.0295  -0.0049 41  ASP A N   
365  C  CA  . ASP A 41  ? 0.1902 0.1870 0.1604 -0.0068 0.0258  0.0006  41  ASP A CA  
366  C  C   . ASP A 41  ? 0.2142 0.2238 0.1492 -0.0392 0.0329  0.0189  41  ASP A C   
367  O  O   . ASP A 41  ? 0.1907 0.2658 0.1631 -0.0351 0.0076  -0.0115 41  ASP A O   
368  C  CB  . ASP A 41  ? 0.2624 0.2149 0.1833 0.0373  -0.0205 0.0124  41  ASP A CB  
369  C  CG  . ASP A 41  ? 0.3285 0.2815 0.1859 0.0507  -0.0280 0.0604  41  ASP A CG  
370  O  OD1 . ASP A 41  ? 0.3064 0.2480 0.2389 -0.0087 -0.0283 0.0922  41  ASP A OD1 
371  O  OD2 . ASP A 41  ? 0.3391 0.3055 0.3537 0.0970  -0.0909 0.0048  41  ASP A OD2 
372  N  N   . PRO A 42  ? 0.1951 0.3684 0.1764 -0.0644 0.0392  0.0416  42  PRO A N   
373  C  CA  . PRO A 42  ? 0.2380 0.4165 0.2411 -0.1303 0.0913  -0.0526 42  PRO A CA  
374  C  C   . PRO A 42  ? 0.2572 0.3626 0.2775 -0.1347 0.0749  -0.0320 42  PRO A C   
375  O  O   . PRO A 42  ? 0.3007 0.6068 0.3186 -0.2188 0.0995  -0.1039 42  PRO A O   
376  C  CB  . PRO A 42  ? 0.2515 0.7098 0.2076 -0.0887 0.0961  -0.0732 42  PRO A CB  
377  C  CG  . PRO A 42  ? 0.2608 0.5097 0.2459 -0.0953 0.0482  0.0646  42  PRO A CG  
378  C  CD  . PRO A 42  ? 0.3194 0.3932 0.1568 -0.0844 0.0971  0.0129  42  PRO A CD  
379  N  N   . SER A 43  ? 0.2811 0.3244 0.1982 -0.1030 0.0344  0.0403  43  SER A N   
380  C  CA  . SER A 43  ? 0.3664 0.2741 0.3093 -0.0688 -0.0003 0.0680  43  SER A CA  
381  C  C   . SER A 43  ? 0.2908 0.2511 0.2770 -0.0837 -0.0230 0.0410  43  SER A C   
382  O  O   . SER A 43  ? 0.4781 0.2917 0.2924 -0.1773 -0.0432 0.0379  43  SER A O   
383  C  CB  . SER A 43  ? 0.3490 0.3463 0.2408 -0.0238 0.0121  0.0709  43  SER A CB  
384  O  OG  . SER A 43  ? 0.3483 0.2707 0.4639 0.0027  -0.0719 0.1076  43  SER A OG  
385  N  N   . LEU A 44  ? 0.3402 0.3504 0.2133 -0.1462 -0.0489 0.0683  44  LEU A N   
386  C  CA  . LEU A 44  ? 0.2444 0.2610 0.2296 -0.0458 -0.0302 -0.0118 44  LEU A CA  
387  C  C   . LEU A 44  ? 0.2203 0.2560 0.2166 -0.0099 0.0091  -0.0277 44  LEU A C   
388  O  O   . LEU A 44  ? 0.2100 0.4589 0.2928 0.0362  -0.0294 -0.0816 44  LEU A O   
389  C  CB  . LEU A 44  ? 0.2058 0.2678 0.1861 0.0230  0.0364  0.0504  44  LEU A CB  
390  C  CG  . LEU A 44  ? 0.1682 0.2599 0.1512 0.0175  -0.0068 -0.0148 44  LEU A CG  
391  C  CD1 . LEU A 44  ? 0.2364 0.2802 0.1872 -0.0019 0.0384  0.0238  44  LEU A CD1 
392  C  CD2 . LEU A 44  ? 0.2394 0.2216 0.2273 0.0276  -0.0335 -0.0452 44  LEU A CD2 
393  N  N   . LYS A 45  ? 0.2054 0.2795 0.2259 -0.0449 -0.0076 -0.0148 45  LYS A N   
394  C  CA  . LYS A 45  ? 0.2157 0.2572 0.2906 -0.0657 -0.0511 0.0307  45  LYS A CA  
395  C  C   . LYS A 45  ? 0.1521 0.2578 0.2601 -0.0758 0.0040  0.0270  45  LYS A C   
396  O  O   . LYS A 45  ? 0.1547 0.2448 0.2754 -0.0377 -0.0040 0.0163  45  LYS A O   
397  C  CB  . LYS A 45  ? 0.2939 0.2500 0.2317 -0.0987 -0.0194 0.0245  45  LYS A CB  
398  C  CG  . LYS A 45  ? 0.2579 0.4113 0.3021 -0.0049 0.0401  0.1039  45  LYS A CG  
399  C  CD  . LYS A 45  ? 0.6093 0.2951 0.4253 0.1411  0.0688  0.0285  45  LYS A CD  
400  N  N   . PRO A 46  ? 0.1368 0.2567 0.2623 -0.0148 0.0386  -0.0215 46  PRO A N   
401  C  CA  . PRO A 46  ? 0.1670 0.3032 0.2069 0.0057  0.0381  -0.0187 46  PRO A CA  
402  C  C   . PRO A 46  ? 0.0789 0.1967 0.2186 -0.0166 0.0222  -0.0107 46  PRO A C   
403  O  O   . PRO A 46  ? 0.1282 0.1887 0.2658 0.0024  -0.0152 -0.0006 46  PRO A O   
404  C  CB  . PRO A 46  ? 0.1557 0.2739 0.3030 0.0107  0.0264  -0.0346 46  PRO A CB  
405  C  CG  . PRO A 46  ? 0.1041 0.4512 0.3481 -0.0222 0.0218  0.0804  46  PRO A CG  
406  C  CD  . PRO A 46  ? 0.1581 0.3420 0.3422 -0.0513 -0.0026 0.0790  46  PRO A CD  
407  N  N   . LEU A 47  ? 0.1370 0.2522 0.2486 -0.0142 0.0421  -0.0200 47  LEU A N   
408  C  CA  . LEU A 47  ? 0.1026 0.2155 0.2222 0.0177  -0.0006 -0.0054 47  LEU A CA  
409  C  C   . LEU A 47  ? 0.1019 0.2092 0.3684 0.0392  -0.0570 -0.0870 47  LEU A C   
410  O  O   . LEU A 47  ? 0.1092 0.2836 0.5173 0.0688  -0.0917 -0.1586 47  LEU A O   
411  C  CB  . LEU A 47  ? 0.2104 0.2930 0.2818 -0.1040 0.0630  -0.0377 47  LEU A CB  
412  C  CG  . LEU A 47  ? 0.1164 0.2766 0.3407 0.0054  0.0013  0.0540  47  LEU A CG  
413  C  CD1 . LEU A 47  ? 0.0710 0.2987 0.5299 0.0370  0.0007  0.0320  47  LEU A CD1 
414  C  CD2 . LEU A 47  ? 0.1272 0.3100 0.3348 -0.0048 0.0337  0.0896  47  LEU A CD2 
415  N  N   . SER A 48  ? 0.0995 0.2131 0.2354 0.0159  -0.0060 -0.0654 48  SER A N   
416  C  CA  . SER A 48  ? 0.1172 0.2065 0.2325 -0.0125 -0.0026 -0.0599 48  SER A CA  
417  C  C   . SER A 48  ? 0.1039 0.1817 0.2225 0.0267  -0.0026 -0.0278 48  SER A C   
418  O  O   . SER A 48  ? 0.1240 0.1959 0.2249 0.0289  0.0024  -0.0181 48  SER A O   
419  C  CB  . SER A 48  ? 0.1595 0.2212 0.2671 -0.0127 -0.0120 -0.0568 48  SER A CB  
420  O  OG  . SER A 48  ? 0.1785 0.2813 0.3052 -0.0535 0.0533  -0.1096 48  SER A OG  
421  N  N   . VAL A 49  ? 0.1779 0.1885 0.2311 0.0491  -0.0092 -0.0320 49  VAL A N   
422  C  CA  . VAL A 49  ? 0.1650 0.2273 0.2232 0.0948  -0.0201 0.0017  49  VAL A CA  
423  C  C   . VAL A 49  ? 0.1913 0.2358 0.2558 0.0833  -0.0285 -0.0085 49  VAL A C   
424  O  O   . VAL A 49  ? 0.2569 0.3585 0.2662 0.1763  -0.0734 -0.0392 49  VAL A O   
425  C  CB  . VAL A 49  ? 0.2680 0.2364 0.2278 0.1217  0.0410  0.0192  49  VAL A CB  
426  C  CG1 . VAL A 49  ? 0.3495 0.2090 0.2809 0.0520  0.0573  0.0147  49  VAL A CG1 
427  C  CG2 . VAL A 49  ? 0.2081 0.2434 0.3935 0.0905  0.0111  -0.0142 49  VAL A CG2 
428  N  N   . SER A 50  ? 0.1747 0.2423 0.2394 0.0839  -0.0425 -0.0255 50  SER A N   
429  C  CA  . SER A 50  ? 0.1456 0.3027 0.3280 0.0439  -0.0555 -0.0138 50  SER A CA  
430  C  C   . SER A 50  ? 0.0962 0.2558 0.3059 0.0425  -0.0608 -0.0294 50  SER A C   
431  O  O   . SER A 50  ? 0.1784 0.2361 0.2926 0.0538  -0.0733 -0.0351 50  SER A O   
432  C  CB  . SER A 50  ? 0.1776 0.3461 0.3521 -0.0083 -0.0087 -0.0494 50  SER A CB  
433  O  OG  . SER A 50  ? 0.2309 0.4429 0.3585 0.0410  -0.0137 0.0178  50  SER A OG  
434  N  N   . TYR A 51  ? 0.1539 0.2583 0.2741 0.0560  -0.0720 -0.0242 51  TYR A N   
435  C  CA  . TYR A 51  ? 0.1182 0.1968 0.2707 0.0165  -0.0706 -0.0370 51  TYR A CA  
436  C  C   . TYR A 51  ? 0.2082 0.2190 0.2578 0.0480  -0.0564 -0.0701 51  TYR A C   
437  O  O   . TYR A 51  ? 0.2163 0.2357 0.2635 -0.0087 -0.0810 -0.0443 51  TYR A O   
438  C  CB  . TYR A 51  ? 0.1511 0.1669 0.2529 0.0283  -0.0527 -0.0157 51  TYR A CB  
439  C  CG  . TYR A 51  ? 0.1448 0.1784 0.1756 0.0472  -0.0502 -0.0286 51  TYR A CG  
440  C  CD1 . TYR A 51  ? 0.1937 0.1381 0.2257 0.0232  -0.0707 -0.0220 51  TYR A CD1 
441  C  CD2 . TYR A 51  ? 0.1723 0.1353 0.1651 0.0280  -0.0390 -0.0028 51  TYR A CD2 
442  C  CE1 . TYR A 51  ? 0.1439 0.1439 0.1802 0.0295  -0.0441 -0.0254 51  TYR A CE1 
443  C  CE2 . TYR A 51  ? 0.1507 0.1439 0.1886 0.0474  -0.0494 -0.0038 51  TYR A CE2 
444  C  CZ  . TYR A 51  ? 0.1314 0.1412 0.1764 0.0144  -0.0303 -0.0005 51  TYR A CZ  
445  O  OH  . TYR A 51  ? 0.1433 0.1343 0.1875 0.0164  -0.0357 -0.0041 51  TYR A OH  
446  N  N   A ASP A 52  ? 0.1262 0.2657 0.4711 0.0832  -0.0776 -0.0179 52  ASP A N   
447  N  N   B ASP A 52  ? 0.2110 0.3210 0.2967 -0.0108 -0.1164 -0.1475 52  ASP A N   
448  C  CA  A ASP A 52  ? 0.2141 0.3091 0.2653 0.0292  0.0003  -0.0193 52  ASP A CA  
449  C  CA  B ASP A 52  ? 0.1553 0.3452 0.3149 0.1140  -0.1423 -0.1305 52  ASP A CA  
450  C  C   A ASP A 52  ? 0.0744 0.3138 0.2991 -0.0038 0.0077  -0.0412 52  ASP A C   
451  C  C   B ASP A 52  ? 0.2026 0.3134 0.3995 0.0670  -0.0788 -0.1395 52  ASP A C   
452  O  O   A ASP A 52  ? 0.1689 0.3140 0.3962 0.0065  -0.1093 -0.0141 52  ASP A O   
453  O  O   B ASP A 52  ? 0.1738 0.3910 0.3697 -0.0026 -0.0051 -0.1932 52  ASP A O   
454  C  CB  A ASP A 52  ? 0.2176 0.2590 0.2948 -0.0313 -0.0361 -0.0531 52  ASP A CB  
455  C  CB  B ASP A 52  ? 0.2053 0.3887 0.2991 0.0392  -0.1128 -0.1704 52  ASP A CB  
456  C  CG  A ASP A 52  ? 0.2736 0.3170 0.3483 0.0636  0.0114  0.0008  52  ASP A CG  
457  C  CG  B ASP A 52  ? 0.1664 0.3996 0.3393 -0.0515 -0.0923 -0.1014 52  ASP A CG  
458  O  OD1 A ASP A 52  ? 0.2509 0.2307 0.3847 0.0024  -0.0149 0.0001  52  ASP A OD1 
459  O  OD1 B ASP A 52  ? 0.3483 0.3571 0.4839 -0.1345 -0.1633 -0.0886 52  ASP A OD1 
460  O  OD2 A ASP A 52  ? 0.5618 0.3865 0.6085 -0.0182 0.0034  -0.1004 52  ASP A OD2 
461  O  OD2 B ASP A 52  ? 0.4149 0.3833 0.5695 -0.1347 0.1650  -0.1572 52  ASP A OD2 
462  N  N   . GLN A 53  ? 0.1792 0.2691 0.4169 0.0181  -0.0992 -0.1263 53  GLN A N   
463  C  CA  . GLN A 53  ? 0.2226 0.3050 0.4699 0.0114  -0.1041 -0.1456 53  GLN A CA  
464  C  C   . GLN A 53  ? 0.2693 0.2198 0.3233 0.0350  -0.0746 -0.0756 53  GLN A C   
465  O  O   . GLN A 53  ? 0.2298 0.2119 0.3161 0.0049  -0.0621 -0.0350 53  GLN A O   
466  C  CB  . GLN A 53  ? 0.3298 0.3734 0.5746 -0.1384 -0.0054 -0.1696 53  GLN A CB  
467  C  CG  . GLN A 53  ? 0.3646 0.4251 0.8087 -0.0894 0.2592  -0.2264 53  GLN A CG  
468  C  CD  . GLN A 53  ? 0.8731 0.5342 1.0247 -0.1685 -0.0700 -0.6647 53  GLN A CD  
469  O  OE1 . GLN A 53  ? 0.6058 0.8306 1.1748 -0.3898 0.1617  -0.3265 53  GLN A OE1 
470  N  NE2 . GLN A 53  ? 1.0010 0.8454 1.8679 -0.0577 -0.0753 -0.6916 53  GLN A NE2 
471  N  N   . ALA A 54  ? 0.2339 0.1903 0.3050 0.0467  -0.0630 -0.0311 54  ALA A N   
472  C  CA  . ALA A 54  ? 0.2362 0.1700 0.2161 0.0315  -0.0340 0.0252  54  ALA A CA  
473  C  C   . ALA A 54  ? 0.2870 0.1810 0.2407 0.0524  -0.0776 0.0263  54  ALA A C   
474  O  O   . ALA A 54  ? 0.3116 0.3034 0.2991 0.0630  -0.1061 0.0793  54  ALA A O   
475  C  CB  . ALA A 54  ? 0.2849 0.1860 0.2520 -0.0083 -0.0417 0.0109  54  ALA A CB  
476  N  N   . THR A 55  ? 0.2276 0.1563 0.1684 -0.0065 -0.0615 -0.0234 55  THR A N   
477  C  CA  . THR A 55  ? 0.2644 0.1668 0.2278 -0.0526 -0.0869 -0.0366 55  THR A CA  
478  C  C   . THR A 55  ? 0.2739 0.1184 0.1330 0.0031  -0.0649 -0.0297 55  THR A C   
479  O  O   . THR A 55  ? 0.2517 0.1304 0.1701 -0.0219 -0.0549 -0.0368 55  THR A O   
480  C  CB  . THR A 55  ? 0.3729 0.2495 0.2465 -0.0597 0.0013  -0.1116 55  THR A CB  
481  O  OG1 . THR A 55  ? 0.3292 0.2675 0.4772 -0.0012 -0.1696 -0.0789 55  THR A OG1 
482  C  CG2 . THR A 55  ? 0.5008 0.3172 0.2234 -0.1912 -0.0052 -0.0998 55  THR A CG2 
483  N  N   . SER A 56  ? 0.2734 0.1375 0.1634 -0.0346 -0.0709 -0.0157 56  SER A N   
484  C  CA  . SER A 56  ? 0.2874 0.1304 0.1112 -0.0015 -0.0553 -0.0116 56  SER A CA  
485  C  C   . SER A 56  ? 0.1806 0.1621 0.1518 0.0081  -0.0292 -0.0419 56  SER A C   
486  O  O   . SER A 56  ? 0.3646 0.1615 0.1571 -0.0522 -0.0860 -0.0359 56  SER A O   
487  C  CB  . SER A 56  ? 0.4167 0.1270 0.1253 -0.0038 -0.1088 -0.0080 56  SER A CB  
488  O  OG  . SER A 56  ? 0.3614 0.1315 0.1563 -0.0003 -0.1093 -0.0223 56  SER A OG  
489  N  N   . LEU A 57  ? 0.2122 0.1207 0.1133 -0.0074 -0.0244 -0.0401 57  LEU A N   
490  C  CA  . LEU A 57  ? 0.2082 0.1151 0.2099 -0.0212 0.0000  -0.0463 57  LEU A CA  
491  C  C   . LEU A 57  ? 0.3073 0.1133 0.1366 -0.0278 -0.0219 -0.0192 57  LEU A C   
492  O  O   . LEU A 57  ? 0.3695 0.1557 0.1182 -0.0483 -0.0445 -0.0320 57  LEU A O   
493  C  CB  . LEU A 57  ? 0.3486 0.1758 0.1775 0.0348  0.0071  -0.0617 57  LEU A CB  
494  C  CG  . LEU A 57  ? 0.6438 0.1184 0.1861 -0.0643 -0.0663 0.0087  57  LEU A CG  
495  C  CD1 . LEU A 57  ? 0.6769 0.2003 0.2588 0.0348  0.0122  0.0130  57  LEU A CD1 
496  C  CD2 . LEU A 57  ? 0.7383 0.1951 0.2513 -0.1450 -0.1042 -0.0388 57  LEU A CD2 
497  N  N   . ARG A 58  ? 0.2205 0.1337 0.1771 -0.0216 -0.0122 -0.0405 58  ARG A N   
498  C  CA  . ARG A 58  ? 0.2626 0.1457 0.1590 0.0046  -0.0318 -0.0610 58  ARG A CA  
499  C  C   . ARG A 58  ? 0.2462 0.1247 0.1101 0.0038  -0.0132 -0.0241 58  ARG A C   
500  O  O   . ARG A 58  ? 0.3398 0.1381 0.0957 -0.0178 -0.0078 -0.0335 58  ARG A O   
501  C  CB  . ARG A 58  ? 0.2133 0.2134 0.1713 -0.0098 0.0250  -0.0310 58  ARG A CB  
502  C  CG  . ARG A 58  ? 0.1689 0.1750 0.2782 0.0183  0.0210  -0.1174 58  ARG A CG  
503  C  CD  . ARG A 58  ? 0.2657 0.2343 0.1800 0.0758  -0.0233 -0.0668 58  ARG A CD  
504  N  NE  . ARG A 58  ? 0.1923 0.1965 0.1931 0.0115  0.0023  -0.0194 58  ARG A NE  
505  C  CZ  . ARG A 58  ? 0.1782 0.2493 0.1630 0.0502  0.0006  -0.0439 58  ARG A CZ  
506  N  NH1 . ARG A 58  ? 0.2436 0.2072 0.2026 0.0555  0.0427  -0.0657 58  ARG A NH1 
507  N  NH2 . ARG A 58  ? 0.1952 0.1509 0.1885 0.0212  0.0142  -0.0317 58  ARG A NH2 
508  N  N   . ILE A 59  ? 0.2445 0.1448 0.1050 0.0000  -0.0057 -0.0305 59  ILE A N   
509  C  CA  . ILE A 59  ? 0.1940 0.1264 0.1351 0.0005  -0.0085 -0.0339 59  ILE A CA  
510  C  C   . ILE A 59  ? 0.1932 0.1009 0.1337 -0.0155 -0.0511 -0.0247 59  ILE A C   
511  O  O   . ILE A 59  ? 0.3116 0.2000 0.0820 -0.0129 -0.0502 -0.0355 59  ILE A O   
512  C  CB  . ILE A 59  ? 0.2836 0.1067 0.1014 0.0000  -0.0414 -0.0265 59  ILE A CB  
513  C  CG1 . ILE A 59  ? 0.2854 0.1288 0.1010 0.0252  -0.0392 -0.0208 59  ILE A CG1 
514  C  CG2 . ILE A 59  ? 0.3226 0.1301 0.0930 0.0034  -0.0640 -0.0093 59  ILE A CG2 
515  C  CD1 . ILE A 59  ? 0.2919 0.1372 0.1045 0.0096  -0.0454 -0.0031 59  ILE A CD1 
516  N  N   . LEU A 60  ? 0.1380 0.1225 0.1770 0.0019  -0.0192 -0.0077 60  LEU A N   
517  C  CA  . LEU A 60  ? 0.1773 0.1118 0.1106 -0.0201 -0.0355 -0.0087 60  LEU A CA  
518  C  C   . LEU A 60  ? 0.1946 0.0983 0.1099 -0.0057 -0.0077 -0.0131 60  LEU A C   
519  O  O   . LEU A 60  ? 0.2342 0.1327 0.0932 0.0255  0.0049  -0.0265 60  LEU A O   
520  C  CB  . LEU A 60  ? 0.1709 0.1049 0.1747 0.0089  -0.0195 -0.0182 60  LEU A CB  
521  C  CG  . LEU A 60  ? 0.2355 0.1182 0.1524 0.0043  0.0137  -0.0304 60  LEU A CG  
522  C  CD1 . LEU A 60  ? 0.2129 0.1418 0.1739 0.0226  0.0093  -0.0368 60  LEU A CD1 
523  C  CD2 . LEU A 60  ? 0.2055 0.1062 0.2021 0.0102  -0.0215 -0.0066 60  LEU A CD2 
524  N  N   . ASN A 61  ? 0.2056 0.0913 0.1368 0.0006  0.0035  -0.0348 61  ASN A N   
525  C  CA  . ASN A 61  ? 0.2075 0.1395 0.1145 0.0292  0.0238  0.0303  61  ASN A CA  
526  C  C   . ASN A 61  ? 0.2197 0.1403 0.1142 0.0362  0.0062  -0.0078 61  ASN A C   
527  O  O   . ASN A 61  ? 0.2389 0.1299 0.1490 0.0256  0.0125  -0.0370 61  ASN A O   
528  C  CB  . ASN A 61  ? 0.2176 0.1184 0.1212 0.0015  0.0171  -0.0127 61  ASN A CB  
529  C  CG  . ASN A 61  ? 0.1544 0.1460 0.1213 0.0307  0.0236  0.0357  61  ASN A CG  
530  O  OD1 . ASN A 61  ? 0.2337 0.1326 0.1457 0.0485  0.0071  -0.0108 61  ASN A OD1 
531  N  ND2 . ASN A 61  ? 0.2583 0.1436 0.1132 0.0386  0.0333  0.0111  61  ASN A ND2 
532  N  N   . ASN A 62  ? 0.3156 0.1168 0.1166 0.0515  -0.0035 -0.0007 62  ASN A N   
533  C  CA  . ASN A 62  ? 0.2842 0.1328 0.1844 0.0078  -0.0571 -0.0073 62  ASN A CA  
534  C  C   . ASN A 62  ? 0.2657 0.1712 0.1415 0.0898  -0.0051 0.0000  62  ASN A C   
535  O  O   . ASN A 62  ? 0.3521 0.2157 0.1952 0.1365  -0.0362 -0.0370 62  ASN A O   
536  C  CB  . ASN A 62  ? 0.3452 0.1770 0.2006 0.0302  -0.0570 -0.0003 62  ASN A CB  
537  C  CG  . ASN A 62  ? 0.4445 0.2407 0.1483 0.0588  -0.0250 0.0612  62  ASN A CG  
538  O  OD1 . ASN A 62  ? 0.2601 0.1823 0.1500 0.0571  -0.0027 0.0013  62  ASN A OD1 
539  N  ND2 . ASN A 62  ? 0.5978 0.4271 0.2572 -0.0772 0.0381  0.0251  62  ASN A ND2 
540  N  N   . GLY A 63  ? 0.2032 0.1624 0.1440 0.0141  0.0043  -0.0266 63  GLY A N   
541  C  CA  . GLY A 63  ? 0.1669 0.1817 0.1350 0.0373  0.0233  -0.0178 63  GLY A CA  
542  C  C   . GLY A 63  ? 0.2301 0.1261 0.2108 -0.0017 0.0194  0.0127  63  GLY A C   
543  O  O   . GLY A 63  ? 0.1931 0.1812 0.2475 0.0163  0.0595  -0.0324 63  GLY A O   
544  N  N   . HIS A 64  ? 0.1916 0.1552 0.1534 0.0307  0.0276  -0.0226 64  HIS A N   
545  C  CA  . HIS A 64  ? 0.1970 0.2230 0.2023 0.0390  0.0480  -0.0781 64  HIS A CA  
546  C  C   . HIS A 64  ? 0.2146 0.2080 0.2046 0.0357  0.0366  -0.0932 64  HIS A C   
547  O  O   . HIS A 64  ? 0.2182 0.2331 0.2396 0.0250  0.0186  -0.1206 64  HIS A O   
548  C  CB  . HIS A 64  ? 0.1720 0.3291 0.1577 0.0253  0.0265  -0.0372 64  HIS A CB  
549  C  CG  . HIS A 64  ? 0.2187 0.3169 0.1416 0.0469  0.0043  0.0087  64  HIS A CG  
550  N  ND1 . HIS A 64  ? 0.2331 0.3583 0.2127 0.0573  0.0245  0.0465  64  HIS A ND1 
551  C  CD2 . HIS A 64  ? 0.2439 0.2887 0.1958 0.0698  0.0149  0.0571  64  HIS A CD2 
552  C  CE1 . HIS A 64  ? 0.2457 0.3336 0.2069 0.0769  0.0452  0.0298  64  HIS A CE1 
553  N  NE2 . HIS A 64  ? 0.2073 0.3449 0.2481 0.0716  0.0297  0.0533  64  HIS A NE2 
554  N  N   . ALA A 65  ? 0.2132 0.1536 0.1588 0.0344  0.0008  -0.0527 65  ALA A N   
555  C  CA  . ALA A 65  ? 0.2090 0.1391 0.1405 0.0452  0.0127  -0.0317 65  ALA A CA  
556  C  C   . ALA A 65  ? 0.2276 0.1224 0.0738 0.0217  0.0104  -0.0188 65  ALA A C   
557  O  O   . ALA A 65  ? 0.2433 0.1532 0.1202 0.0419  0.0205  -0.0370 65  ALA A O   
558  C  CB  . ALA A 65  ? 0.2273 0.2150 0.1191 0.0335  0.0038  -0.0518 65  ALA A CB  
559  N  N   . PHE A 66  ? 0.2049 0.1155 0.1064 0.0249  -0.0055 -0.0111 66  PHE A N   
560  C  CA  . PHE A 66  ? 0.2653 0.1006 0.0953 0.0194  -0.0109 -0.0156 66  PHE A CA  
561  C  C   . PHE A 66  ? 0.2339 0.1118 0.0794 0.0309  -0.0120 -0.0125 66  PHE A C   
562  O  O   . PHE A 66  ? 0.2462 0.1080 0.0904 0.0229  -0.0093 -0.0138 66  PHE A O   
563  C  CB  . PHE A 66  ? 0.2469 0.1460 0.0948 0.0306  -0.0109 -0.0125 66  PHE A CB  
564  C  CG  . PHE A 66  ? 0.2444 0.1190 0.0816 0.0388  -0.0286 -0.0070 66  PHE A CG  
565  C  CD1 . PHE A 66  ? 0.2331 0.1805 0.0807 0.0160  -0.0331 0.0005  66  PHE A CD1 
566  C  CD2 . PHE A 66  ? 0.2041 0.1440 0.0869 0.0062  -0.0113 0.0063  66  PHE A CD2 
567  C  CE1 . PHE A 66  ? 0.2206 0.1401 0.1175 0.0063  -0.0350 -0.0054 66  PHE A CE1 
568  C  CE2 . PHE A 66  ? 0.1931 0.1295 0.0967 0.0251  -0.0299 0.0017  66  PHE A CE2 
569  C  CZ  . PHE A 66  ? 0.2090 0.1562 0.1026 0.0289  -0.0500 0.0161  66  PHE A CZ  
570  N  N   . ASN A 67  ? 0.1902 0.1238 0.1212 0.0109  -0.0197 -0.0403 67  ASN A N   
571  C  CA  . ASN A 67  ? 0.2214 0.1015 0.1064 0.0166  0.0000  0.0000  67  ASN A CA  
572  C  C   . ASN A 67  ? 0.1914 0.0786 0.1118 0.0065  -0.0412 -0.0028 67  ASN A C   
573  O  O   . ASN A 67  ? 0.2240 0.1370 0.0965 0.0226  -0.0232 -0.0364 67  ASN A O   
574  C  CB  . ASN A 67  ? 0.2148 0.1386 0.1343 0.0397  -0.0288 0.0132  67  ASN A CB  
575  C  CG  . ASN A 67  ? 0.2241 0.1297 0.1909 0.0289  -0.0186 0.0017  67  ASN A CG  
576  O  OD1 . ASN A 67  ? 0.2336 0.1694 0.1662 0.0399  -0.0412 -0.0057 67  ASN A OD1 
577  N  ND2 . ASN A 67  ? 0.2678 0.1720 0.2939 0.0636  -0.0855 0.0136  67  ASN A ND2 
578  N  N   . VAL A 68  ? 0.2197 0.1040 0.1067 0.0015  -0.0173 -0.0148 68  VAL A N   
579  C  CA  . VAL A 68  ? 0.2268 0.1222 0.0847 -0.0329 -0.0297 -0.0099 68  VAL A CA  
580  C  C   . VAL A 68  ? 0.2795 0.0992 0.1027 -0.0143 -0.0474 -0.0132 68  VAL A C   
581  O  O   . VAL A 68  ? 0.2626 0.0931 0.0927 -0.0189 -0.0176 -0.0141 68  VAL A O   
582  C  CB  . VAL A 68  ? 0.2402 0.0921 0.1439 0.0040  -0.0399 -0.0037 68  VAL A CB  
583  C  CG1 . VAL A 68  ? 0.2522 0.1724 0.1306 -0.0443 -0.0781 0.0071  68  VAL A CG1 
584  C  CG2 . VAL A 68  ? 0.2576 0.1400 0.1482 0.0081  -0.0229 0.0254  68  VAL A CG2 
585  N  N   . GLU A 69  ? 0.2685 0.0973 0.1191 -0.0049 -0.0230 -0.0153 69  GLU A N   
586  C  CA  . GLU A 69  ? 0.2249 0.1168 0.0996 -0.0038 0.0092  -0.0063 69  GLU A CA  
587  C  C   . GLU A 69  ? 0.2404 0.1200 0.0931 -0.0186 -0.0189 -0.0351 69  GLU A C   
588  O  O   . GLU A 69  ? 0.2567 0.1206 0.1337 -0.0156 -0.0403 -0.0093 69  GLU A O   
589  C  CB  . GLU A 69  ? 0.1873 0.1573 0.1578 -0.0153 0.0299  -0.0208 69  GLU A CB  
590  C  CG  . GLU A 69  ? 0.1686 0.2067 0.1643 0.0089  0.0171  -0.0515 69  GLU A CG  
591  C  CD  . GLU A 69  ? 0.2231 0.1489 0.1914 -0.0082 0.0208  -0.0233 69  GLU A CD  
592  O  OE1 . GLU A 69  ? 0.2286 0.1800 0.1828 0.0035  -0.0013 -0.0313 69  GLU A OE1 
593  O  OE2 . GLU A 69  ? 0.2050 0.1649 0.1979 0.0086  0.0198  -0.0285 69  GLU A OE2 
594  N  N   . PHE A 70  ? 0.2777 0.1186 0.0983 -0.0083 -0.0148 -0.0104 70  PHE A N   
595  C  CA  . PHE A 70  ? 0.2159 0.0921 0.1590 -0.0182 -0.0566 -0.0126 70  PHE A CA  
596  C  C   . PHE A 70  ? 0.2454 0.1132 0.1440 -0.0165 -0.0568 0.0020  70  PHE A C   
597  O  O   . PHE A 70  ? 0.2617 0.1074 0.1860 -0.0132 -0.0649 -0.0328 70  PHE A O   
598  C  CB  . PHE A 70  ? 0.2522 0.1127 0.1200 -0.0103 -0.0509 -0.0115 70  PHE A CB  
599  C  CG  . PHE A 70  ? 0.2418 0.0980 0.1287 -0.0154 -0.0351 -0.0216 70  PHE A CG  
600  C  CD1 . PHE A 70  ? 0.2924 0.1005 0.1221 -0.0285 -0.0333 -0.0381 70  PHE A CD1 
601  C  CD2 . PHE A 70  ? 0.2204 0.1074 0.1211 -0.0326 -0.0414 -0.0019 70  PHE A CD2 
602  C  CE1 . PHE A 70  ? 0.2635 0.1110 0.1526 -0.0326 -0.0085 -0.0482 70  PHE A CE1 
603  C  CE2 . PHE A 70  ? 0.2469 0.1123 0.1378 -0.0207 -0.0425 -0.0217 70  PHE A CE2 
604  C  CZ  . PHE A 70  ? 0.2610 0.1103 0.1484 -0.0038 -0.0182 -0.0054 70  PHE A CZ  
605  N  N   A ASP A 71  ? 0.3345 0.0877 0.0992 -0.0082 -0.0537 -0.0297 71  ASP A N   
606  N  N   B ASP A 71  ? 0.2111 0.1006 0.1482 -0.0094 -0.0353 -0.0524 71  ASP A N   
607  C  CA  A ASP A 71  ? 0.2685 0.0910 0.1658 -0.0105 -0.0712 -0.0471 71  ASP A CA  
608  C  CA  B ASP A 71  ? 0.2317 0.1067 0.2389 0.0052  0.0247  -0.0326 71  ASP A CA  
609  C  C   A ASP A 71  ? 0.2615 0.0458 0.2443 0.0077  -0.0062 -0.0149 71  ASP A C   
610  C  C   B ASP A 71  ? 0.1984 0.1199 0.2498 0.0015  0.0071  -0.0306 71  ASP A C   
611  O  O   A ASP A 71  ? 0.2384 0.1559 0.2154 -0.0151 -0.0068 -0.0267 71  ASP A O   
612  O  O   B ASP A 71  ? 0.2978 0.1655 0.1683 0.0595  -0.0060 -0.0063 71  ASP A O   
613  C  CB  A ASP A 71  ? 0.2233 0.1150 0.3540 0.0113  -0.1089 -0.1142 71  ASP A CB  
614  C  CB  B ASP A 71  ? 0.3063 0.1216 0.2998 -0.0419 -0.0149 -0.0478 71  ASP A CB  
615  C  CG  A ASP A 71  ? 0.3540 0.1763 0.3847 -0.0167 -0.1618 -0.0031 71  ASP A CG  
616  C  CG  B ASP A 71  ? 0.3723 0.1288 0.4056 -0.0283 -0.2204 -0.0798 71  ASP A CG  
617  O  OD1 A ASP A 71  ? 0.2536 0.1005 0.3943 -0.0296 -0.0219 -0.0705 71  ASP A OD1 
618  O  OD1 B ASP A 71  ? 0.3792 0.1977 0.3555 0.0170  -0.0331 -0.0995 71  ASP A OD1 
619  O  OD2 A ASP A 71  ? 0.3152 0.1115 0.3249 0.0326  -0.1054 -0.0335 71  ASP A OD2 
620  O  OD2 B ASP A 71  ? 0.2770 0.1415 0.3235 -0.0746 -0.0416 -0.0388 71  ASP A OD2 
621  N  N   . ASP A 72  ? 0.2472 0.0856 0.2091 0.0034  -0.0184 -0.0135 72  ASP A N   
622  C  CA  . ASP A 72  ? 0.2419 0.0923 0.2272 -0.0031 0.0294  -0.0096 72  ASP A CA  
623  C  C   . ASP A 72  ? 0.2748 0.0894 0.2583 0.0258  0.0509  -0.0120 72  ASP A C   
624  O  O   . ASP A 72  ? 0.3720 0.1067 0.2340 0.0289  0.0406  0.0017  72  ASP A O   
625  C  CB  . ASP A 72  ? 0.2985 0.1148 0.1972 0.0377  0.0068  -0.0189 72  ASP A CB  
626  C  CG  . ASP A 72  ? 0.2527 0.1676 0.1367 0.0007  0.0015  -0.0160 72  ASP A CG  
627  O  OD1 . ASP A 72  ? 0.2380 0.2849 0.1747 0.0305  -0.0555 -0.0784 72  ASP A OD1 
628  O  OD2 . ASP A 72  ? 0.2556 0.2266 0.1345 0.0218  -0.0122 -0.0291 72  ASP A OD2 
629  N  N   . SER A 73  ? 0.2757 0.0839 0.2996 -0.0007 0.0326  -0.0549 73  SER A N   
630  C  CA  . SER A 73  ? 0.3188 0.0998 0.3176 0.0215  0.0644  -0.0121 73  SER A CA  
631  C  C   . SER A 73  ? 0.3134 0.1005 0.3228 0.0143  0.0826  0.0237  73  SER A C   
632  O  O   . SER A 73  ? 0.3149 0.0904 0.3106 -0.0010 0.0263  -0.0110 73  SER A O   
633  C  CB  . SER A 73  ? 0.4291 0.1018 0.3772 0.0221  0.0469  -0.0870 73  SER A CB  
634  O  OG  . SER A 73  ? 0.3842 0.1397 0.3181 -0.0311 0.1058  -0.0635 73  SER A OG  
635  N  N   . GLN A 74  ? 0.2696 0.1114 0.4181 -0.0043 0.0944  0.0044  74  GLN A N   
636  C  CA  . GLN A 74  ? 0.2687 0.1395 0.4851 0.0086  0.1268  -0.0082 74  GLN A CA  
637  C  C   . GLN A 74  ? 0.3007 0.1459 0.3239 0.0313  0.0520  0.0231  74  GLN A C   
638  O  O   . GLN A 74  ? 0.2346 0.1606 0.2255 0.0485  -0.0518 -0.0366 74  GLN A O   
639  C  CB  . GLN A 74  ? 0.2554 0.1634 0.6680 0.0068  0.1057  -0.0509 74  GLN A CB  
640  C  CG  . GLN A 74  ? 0.1700 0.2921 0.7659 -0.0208 0.0474  -0.1343 74  GLN A CG  
641  C  CD  . GLN A 74  ? 0.2426 0.3111 0.6334 0.0166  0.0342  -0.1224 74  GLN A CD  
642  O  OE1 . GLN A 74  ? 0.4686 0.5067 1.0026 -0.0010 0.3088  -0.0719 74  GLN A OE1 
643  N  NE2 . GLN A 74  ? 0.3883 0.3822 0.6980 -0.0199 -0.0768 0.0386  74  GLN A NE2 
644  N  N   . ASP A 75  ? 0.2969 0.3034 0.2791 0.1259  0.0491  0.0764  75  ASP A N   
645  C  CA  . ASP A 75  ? 0.3609 0.1683 0.3504 0.0599  0.0148  0.0419  75  ASP A CA  
646  C  C   . ASP A 75  ? 0.1759 0.3100 0.3129 0.0379  0.0261  0.0465  75  ASP A C   
647  O  O   . ASP A 75  ? 0.2275 0.2937 0.4650 -0.0027 -0.0679 -0.0478 75  ASP A O   
648  C  CB  . ASP A 75  ? 0.3397 0.2845 0.2542 -0.0059 0.0410  -0.0118 75  ASP A CB  
649  C  CG  . ASP A 75  ? 0.6919 0.2667 0.4442 0.0096  0.1058  -0.2159 75  ASP A CG  
650  O  OD1 . ASP A 75  ? 0.2182 0.2872 0.5031 0.0116  -0.0370 -0.1472 75  ASP A OD1 
651  O  OD2 . ASP A 75  ? 0.5073 0.5787 0.6200 -0.0219 0.0674  -0.0166 75  ASP A OD2 
652  N  N   . LYS A 76  ? 0.2393 0.2060 0.2910 0.0621  -0.0689 -0.0929 76  LYS A N   
653  C  CA  . LYS A 76  ? 0.1893 0.1282 0.5666 0.0240  -0.0333 -0.0159 76  LYS A CA  
654  C  C   . LYS A 76  ? 0.3097 0.2488 0.8981 0.0390  -0.2060 -0.2480 76  LYS A C   
655  O  O   . LYS A 76  ? 0.4126 0.5026 0.6784 0.2115  -0.2538 -0.2222 76  LYS A O   
656  C  CB  . LYS A 76  ? 0.4465 0.1537 0.3831 0.0172  -0.1306 0.0041  76  LYS A CB  
657  C  CG  . LYS A 76  ? 0.5465 0.2242 0.4840 0.0283  -0.0763 -0.0993 76  LYS A CG  
658  C  CD  . LYS A 76  ? 0.8952 0.2405 0.4900 -0.1334 0.0282  -0.1395 76  LYS A CD  
659  C  CE  . LYS A 76  ? 0.6402 0.2134 0.6126 0.0251  -0.0537 -0.0683 76  LYS A CE  
660  N  NZ  . LYS A 76  ? 1.5410 0.4553 1.3575 -0.1474 0.8596  -0.2268 76  LYS A NZ  
661  N  N   . ALA A 77  ? 0.3080 0.4444 0.5935 0.0156  -0.3179 -0.2337 77  ALA A N   
662  C  CA  . ALA A 77  ? 0.2012 0.2542 0.2477 0.0419  -0.0944 -0.0146 77  ALA A CA  
663  C  C   . ALA A 77  ? 0.1296 0.1621 0.2804 0.0192  -0.0816 0.0027  77  ALA A C   
664  O  O   . ALA A 77  ? 0.1281 0.4377 0.3512 0.0137  -0.0507 0.1517  77  ALA A O   
665  C  CB  . ALA A 77  ? 0.2448 0.2278 0.2549 0.0234  -0.0829 -0.0401 77  ALA A CB  
666  N  N   . VAL A 78  ? 0.1736 0.1456 0.2133 0.0118  -0.0668 -0.0225 78  VAL A N   
667  C  CA  . VAL A 78  ? 0.2255 0.1377 0.2132 0.0176  -0.0851 -0.0328 78  VAL A CA  
668  C  C   . VAL A 78  ? 0.1590 0.1105 0.2520 0.0135  -0.0513 -0.0292 78  VAL A C   
669  O  O   . VAL A 78  ? 0.1679 0.1427 0.2739 0.0351  -0.0724 -0.0357 78  VAL A O   
670  C  CB  . VAL A 78  ? 0.3032 0.1758 0.2727 -0.0298 -0.0952 0.0287  78  VAL A CB  
671  C  CG1 . VAL A 78  ? 0.3693 0.1296 0.3939 -0.0329 -0.1235 -0.0288 78  VAL A CG1 
672  C  CG2 . VAL A 78  ? 0.3021 0.1941 0.3454 -0.0164 -0.0019 0.0089  78  VAL A CG2 
673  N  N   . LEU A 79  ? 0.1462 0.1236 0.1784 0.0065  -0.0342 -0.0091 79  LEU A N   
674  C  CA  . LEU A 79  ? 0.1215 0.1372 0.2010 0.0059  -0.0055 -0.0208 79  LEU A CA  
675  C  C   . LEU A 79  ? 0.1467 0.1345 0.1897 0.0197  0.0068  -0.0055 79  LEU A C   
676  O  O   . LEU A 79  ? 0.1341 0.1528 0.2063 0.0146  0.0135  0.0076  79  LEU A O   
677  C  CB  . LEU A 79  ? 0.1202 0.1500 0.2064 0.0078  -0.0189 -0.0216 79  LEU A CB  
678  C  CG  . LEU A 79  ? 0.1327 0.1802 0.1756 0.0024  -0.0028 -0.0355 79  LEU A CG  
679  C  CD1 . LEU A 79  ? 0.1669 0.1480 0.4099 0.0093  0.0116  -0.0728 79  LEU A CD1 
680  C  CD2 . LEU A 79  ? 0.1269 0.1683 0.1849 -0.0020 -0.0010 -0.0220 79  LEU A CD2 
681  N  N   . LYS A 80  ? 0.1333 0.1572 0.1783 0.0096  0.0206  -0.0063 80  LYS A N   
682  C  CA  . LYS A 80  ? 0.1370 0.1513 0.2126 0.0082  0.0193  -0.0040 80  LYS A CA  
683  C  C   . LYS A 80  ? 0.1229 0.1764 0.2199 -0.0098 0.0472  -0.0108 80  LYS A C   
684  O  O   . LYS A 80  ? 0.1450 0.1503 0.2329 -0.0006 -0.0028 -0.0175 80  LYS A O   
685  C  CB  . LYS A 80  ? 0.2230 0.1827 0.2502 -0.0443 0.0265  -0.0054 80  LYS A CB  
686  C  CG  . LYS A 80  ? 0.1846 0.2123 0.3106 -0.0513 0.0399  -0.0375 80  LYS A CG  
687  C  CD  . LYS A 80  ? 0.2138 0.2369 0.5024 -0.0644 -0.0335 0.0175  80  LYS A CD  
688  C  CE  . LYS A 80  ? 0.2038 0.4016 0.7394 -0.1171 -0.0328 -0.0074 80  LYS A CE  
689  N  NZ  . LYS A 80  ? 0.5291 0.6690 0.8506 0.0434  -0.1064 0.2198  80  LYS A NZ  
690  N  N   . GLY A 81  ? 0.1639 0.1871 0.2058 -0.0038 0.0315  -0.0148 81  GLY A N   
691  C  CA  . GLY A 81  ? 0.1659 0.1767 0.2115 -0.0141 0.0662  -0.0280 81  GLY A CA  
692  C  C   . GLY A 81  ? 0.1432 0.1573 0.2393 -0.0251 0.0544  -0.0017 81  GLY A C   
693  O  O   . GLY A 81  ? 0.1380 0.1627 0.2414 0.0087  0.0362  0.0172  81  GLY A O   
694  N  N   . GLY A 82  ? 0.1334 0.2111 0.3565 0.0148  0.0467  -0.0421 82  GLY A N   
695  C  CA  . GLY A 82  ? 0.2002 0.2184 0.4451 0.0035  0.0204  -0.0430 82  GLY A CA  
696  C  C   . GLY A 82  ? 0.1862 0.2141 0.2487 -0.0631 0.0636  -0.0791 82  GLY A C   
697  O  O   . GLY A 82  ? 0.2624 0.4014 0.2511 -0.1527 0.1055  -0.0678 82  GLY A O   
698  N  N   . PRO A 83  ? 0.1595 0.1644 0.2770 -0.0305 0.0469  -0.0441 83  PRO A N   
699  C  CA  . PRO A 83  ? 0.2203 0.1779 0.2090 -0.0766 0.0465  -0.0505 83  PRO A CA  
700  C  C   . PRO A 83  ? 0.1411 0.2283 0.1913 -0.0644 -0.0126 0.0148  83  PRO A C   
701  O  O   . PRO A 83  ? 0.2144 0.2714 0.2071 -0.0406 -0.0427 0.0070  83  PRO A O   
702  C  CB  . PRO A 83  ? 0.1962 0.2149 0.2108 -0.0626 -0.0031 -0.0138 83  PRO A CB  
703  C  CG  . PRO A 83  ? 0.1788 0.1657 0.2115 -0.0274 0.0131  -0.0165 83  PRO A CG  
704  C  CD  . PRO A 83  ? 0.1297 0.1415 0.2563 -0.0027 0.0615  -0.0214 83  PRO A CD  
705  N  N   . LEU A 84  ? 0.1503 0.1570 0.1708 -0.0377 0.0280  0.0081  84  LEU A N   
706  C  CA  . LEU A 84  ? 0.1780 0.1350 0.1750 -0.0359 0.0000  0.0205  84  LEU A CA  
707  C  C   . LEU A 84  ? 0.1621 0.1733 0.2275 -0.0636 -0.0129 0.0241  84  LEU A C   
708  O  O   . LEU A 84  ? 0.1865 0.1891 0.2508 -0.0522 0.0333  0.0500  84  LEU A O   
709  C  CB  . LEU A 84  ? 0.1159 0.1243 0.1891 -0.0197 0.0219  0.0093  84  LEU A CB  
710  C  CG  . LEU A 84  ? 0.1121 0.1089 0.2029 -0.0174 0.0277  0.0065  84  LEU A CG  
711  C  CD1 . LEU A 84  ? 0.1563 0.1357 0.1792 -0.0276 -0.0127 0.0130  84  LEU A CD1 
712  C  CD2 . LEU A 84  ? 0.1168 0.1229 0.2045 -0.0127 0.0149  0.0223  84  LEU A CD2 
713  N  N   . ASP A 85  ? 0.2590 0.1456 0.2152 -0.0297 0.0059  0.0423  85  ASP A N   
714  C  CA  . ASP A 85  ? 0.2843 0.1429 0.2606 -0.0060 0.0593  0.0719  85  ASP A CA  
715  C  C   . ASP A 85  ? 0.2418 0.1080 0.3738 -0.0346 0.0408  -0.0065 85  ASP A C   
716  O  O   . ASP A 85  ? 0.3477 0.2770 0.2894 -0.0706 0.0362  0.0703  85  ASP A O   
717  C  CB  . ASP A 85  ? 0.3693 0.1897 0.2605 -0.0472 0.0631  0.0710  85  ASP A CB  
718  C  CG  . ASP A 85  ? 0.4262 0.4009 0.3064 0.0653  0.2387  -0.0186 85  ASP A CG  
719  O  OD1 . ASP A 85  ? 0.3463 0.5170 0.2736 0.1000  0.0641  -0.0161 85  ASP A OD1 
720  O  OD2 . ASP A 85  ? 0.4354 0.4377 0.5975 -0.0220 0.0021  0.1657  85  ASP A OD2 
721  N  N   . GLY A 86  ? 0.2793 0.2786 0.3273 0.0076  0.0034  -0.1281 86  GLY A N   
722  C  CA  . GLY A 86  ? 0.2547 0.2761 0.2705 0.0500  0.0066  -0.0443 86  GLY A CA  
723  C  C   . GLY A 86  ? 0.2651 0.2648 0.2372 0.0631  -0.0366 -0.0520 86  GLY A C   
724  O  O   . GLY A 86  ? 0.3501 0.3377 0.3282 0.1668  -0.0017 -0.0250 86  GLY A O   
725  N  N   A THR A 87  ? 0.2199 0.1207 0.2239 -0.0379 -0.0222 0.0104  87  THR A N   
726  N  N   B THR A 87  ? 0.1323 0.1994 0.2108 -0.0129 0.0174  0.0081  87  THR A N   
727  C  CA  A THR A 87  ? 0.1560 0.2204 0.2316 -0.0260 -0.0179 0.0230  87  THR A CA  
728  C  CA  B THR A 87  ? 0.1333 0.1115 0.2411 -0.0362 0.0270  0.0322  87  THR A CA  
729  C  C   A THR A 87  ? 0.1340 0.1225 0.2158 0.0017  -0.0010 0.0060  87  THR A C   
730  C  C   B THR A 87  ? 0.1230 0.1274 0.2468 -0.0328 0.0157  0.0225  87  THR A C   
731  O  O   A THR A 87  ? 0.1349 0.0978 0.1588 -0.0081 0.0293  -0.0038 87  THR A O   
732  O  O   B THR A 87  ? 0.1715 0.1128 0.2067 -0.0059 -0.0443 0.0122  87  THR A O   
733  C  CB  A THR A 87  ? 0.1872 0.1574 0.3251 -0.0447 -0.0516 0.0544  87  THR A CB  
734  C  CB  B THR A 87  ? 0.1175 0.1254 0.2347 -0.0226 0.0326  0.0260  87  THR A CB  
735  O  OG1 A THR A 87  ? 0.2592 0.2658 0.2935 -0.0877 -0.0247 0.0511  87  THR A OG1 
736  O  OG1 B THR A 87  ? 0.1648 0.1323 0.1841 -0.0082 0.0055  -0.0298 87  THR A OG1 
737  C  CG2 A THR A 87  ? 0.2177 0.2001 0.2978 -0.0674 -0.0395 0.0452  87  THR A CG2 
738  C  CG2 B THR A 87  ? 0.1198 0.1347 0.2229 -0.0573 0.0255  -0.0073 87  THR A CG2 
739  N  N   . TYR A 88  ? 0.1172 0.1077 0.2122 -0.0168 0.0076  0.0098  88  TYR A N   
740  C  CA  . TYR A 88  ? 0.1071 0.1186 0.1744 -0.0102 -0.0035 0.0013  88  TYR A CA  
741  C  C   . TYR A 88  ? 0.0976 0.1191 0.1799 -0.0076 -0.0300 -0.0096 88  TYR A C   
742  O  O   . TYR A 88  ? 0.1384 0.1914 0.2108 0.0460  -0.0527 -0.0230 88  TYR A O   
743  C  CB  . TYR A 88  ? 0.1155 0.0856 0.1791 -0.0041 -0.0187 0.0043  88  TYR A CB  
744  C  CG  . TYR A 88  ? 0.1081 0.0824 0.1679 -0.0057 -0.0073 0.0113  88  TYR A CG  
745  C  CD1 . TYR A 88  ? 0.1196 0.1168 0.1439 -0.0197 0.0088  -0.0017 88  TYR A CD1 
746  C  CD2 . TYR A 88  ? 0.1200 0.0683 0.1316 -0.0118 -0.0006 0.0063  88  TYR A CD2 
747  C  CE1 . TYR A 88  ? 0.0974 0.1290 0.1500 -0.0077 0.0172  0.0114  88  TYR A CE1 
748  C  CE2 . TYR A 88  ? 0.1325 0.0775 0.1133 -0.0001 0.0104  -0.0010 88  TYR A CE2 
749  C  CZ  . TYR A 88  ? 0.1032 0.0895 0.1292 0.0010  0.0017  0.0144  88  TYR A CZ  
750  O  OH  . TYR A 88  ? 0.1218 0.1030 0.1363 -0.0044 0.0035  0.0098  88  TYR A OH  
751  N  N   . ARG A 89  ? 0.1111 0.1005 0.1561 -0.0164 -0.0240 0.0140  89  ARG A N   
752  C  CA  . ARG A 89  ? 0.1568 0.0891 0.1649 -0.0229 -0.0494 -0.0124 89  ARG A CA  
753  C  C   . ARG A 89  ? 0.1535 0.0702 0.1225 0.0172  -0.0253 -0.0307 89  ARG A C   
754  O  O   . ARG A 89  ? 0.1283 0.0777 0.1273 0.0068  -0.0197 -0.0114 89  ARG A O   
755  C  CB  . ARG A 89  ? 0.2069 0.0847 0.2225 0.0041  -0.0913 -0.0267 89  ARG A CB  
756  C  CG  . ARG A 89  ? 0.2375 0.1186 0.1683 0.0119  -0.0463 -0.0219 89  ARG A CG  
757  C  CD  . ARG A 89  ? 0.2475 0.1058 0.2096 -0.0177 -0.0381 -0.0148 89  ARG A CD  
758  N  NE  . ARG A 89  ? 0.2852 0.1083 0.1931 0.0057  -0.0373 -0.0274 89  ARG A NE  
759  C  CZ  . ARG A 89  ? 0.2328 0.1053 0.1747 0.0081  -0.0120 -0.0105 89  ARG A CZ  
760  N  NH1 . ARG A 89  ? 0.2243 0.1546 0.2815 -0.0276 0.0373  -0.0901 89  ARG A NH1 
761  N  NH2 . ARG A 89  ? 0.2874 0.1166 0.2448 -0.0388 -0.0153 -0.0152 89  ARG A NH2 
762  N  N   . LEU A 90  ? 0.1292 0.0900 0.1310 0.0142  -0.0311 -0.0200 90  LEU A N   
763  C  CA  . LEU A 90  ? 0.1597 0.0729 0.1344 0.0100  -0.0296 -0.0109 90  LEU A CA  
764  C  C   . LEU A 90  ? 0.1547 0.0904 0.1377 0.0122  -0.0443 -0.0253 90  LEU A C   
765  O  O   . LEU A 90  ? 0.1881 0.1216 0.1451 0.0038  -0.0384 -0.0480 90  LEU A O   
766  C  CB  . LEU A 90  ? 0.1720 0.0873 0.1376 0.0328  -0.0307 -0.0126 90  LEU A CB  
767  C  CG  . LEU A 90  ? 0.2222 0.1102 0.1243 0.0480  -0.0388 -0.0043 90  LEU A CG  
768  C  CD1 . LEU A 90  ? 0.2500 0.0772 0.1590 0.0109  -0.0181 -0.0057 90  LEU A CD1 
769  C  CD2 . LEU A 90  ? 0.2372 0.1641 0.1410 0.0683  -0.0483 0.0131  90  LEU A CD2 
770  N  N   . ILE A 91  ? 0.1717 0.0775 0.1045 0.0060  -0.0057 -0.0085 91  ILE A N   
771  C  CA  . ILE A 91  ? 0.1970 0.0824 0.1008 0.0119  -0.0133 -0.0141 91  ILE A CA  
772  C  C   . ILE A 91  ? 0.1639 0.0829 0.0992 0.0161  -0.0137 -0.0159 91  ILE A C   
773  O  O   . ILE A 91  ? 0.1984 0.0838 0.0903 0.0146  -0.0175 -0.0141 91  ILE A O   
774  C  CB  . ILE A 91  ? 0.2198 0.0828 0.1105 0.0252  -0.0120 -0.0049 91  ILE A CB  
775  C  CG1 . ILE A 91  ? 0.2089 0.1599 0.1160 0.0617  -0.0116 -0.0188 91  ILE A CG1 
776  C  CG2 . ILE A 91  ? 0.1890 0.0978 0.1356 0.0259  -0.0193 -0.0043 91  ILE A CG2 
777  C  CD1 . ILE A 91  ? 0.2313 0.1876 0.1550 0.0881  0.0017  0.0035  91  ILE A CD1 
778  N  N   . GLN A 92  ? 0.1726 0.0703 0.0979 0.0149  -0.0143 -0.0164 92  GLN A N   
779  C  CA  . GLN A 92  ? 0.1858 0.0737 0.0944 0.0104  -0.0144 -0.0100 92  GLN A CA  
780  C  C   . GLN A 92  ? 0.1673 0.0702 0.0998 0.0074  -0.0238 -0.0082 92  GLN A C   
781  O  O   . GLN A 92  ? 0.2026 0.0775 0.0816 0.0105  -0.0078 -0.0065 92  GLN A O   
782  C  CB  . GLN A 92  ? 0.1991 0.0967 0.1218 0.0038  -0.0132 -0.0199 92  GLN A CB  
783  C  CG  . GLN A 92  ? 0.2113 0.0926 0.1622 0.0049  -0.0178 -0.0109 92  GLN A CG  
784  C  CD  . GLN A 92  ? 0.1831 0.1076 0.1421 0.0142  0.0089  -0.0255 92  GLN A CD  
785  O  OE1 . GLN A 92  ? 0.1917 0.0903 0.1552 0.0024  -0.0236 -0.0242 92  GLN A OE1 
786  N  NE2 . GLN A 92  ? 0.2337 0.1799 0.4309 0.0041  0.0790  -0.0807 92  GLN A NE2 
787  N  N   . PHE A 93  ? 0.1684 0.0666 0.0905 -0.0019 -0.0185 -0.0082 93  PHE A N   
788  C  CA  . PHE A 93  ? 0.1680 0.0615 0.0996 -0.0088 -0.0227 -0.0034 93  PHE A CA  
789  C  C   . PHE A 93  ? 0.1497 0.0718 0.0939 0.0185  -0.0305 -0.0148 93  PHE A C   
790  O  O   . PHE A 93  ? 0.2075 0.0843 0.0846 0.0046  -0.0199 -0.0195 93  PHE A O   
791  C  CB  . PHE A 93  ? 0.1657 0.0874 0.0852 0.0092  -0.0388 -0.0102 93  PHE A CB  
792  C  CG  . PHE A 93  ? 0.1624 0.0703 0.1184 0.0073  -0.0538 -0.0093 93  PHE A CG  
793  C  CD1 . PHE A 93  ? 0.1918 0.0848 0.1057 -0.0003 -0.0395 0.0037  93  PHE A CD1 
794  C  CD2 . PHE A 93  ? 0.1812 0.0864 0.1202 0.0051  -0.0551 -0.0204 93  PHE A CD2 
795  C  CE1 . PHE A 93  ? 0.2236 0.0808 0.1380 -0.0046 -0.0666 0.0097  93  PHE A CE1 
796  C  CE2 . PHE A 93  ? 0.2293 0.1014 0.1245 -0.0104 -0.0750 -0.0049 93  PHE A CE2 
797  C  CZ  . PHE A 93  ? 0.2055 0.0969 0.1307 -0.0142 -0.0718 -0.0024 93  PHE A CZ  
798  N  N   . HIS A 94  ? 0.1555 0.0705 0.0812 0.0093  -0.0231 -0.0083 94  HIS A N   
799  C  CA  . HIS A 94  ? 0.1608 0.0751 0.0807 0.0081  -0.0135 -0.0140 94  HIS A CA  
800  C  C   . HIS A 94  ? 0.1657 0.0688 0.0732 0.0113  -0.0161 0.0003  94  HIS A C   
801  O  O   . HIS A 94  ? 0.1425 0.0819 0.0773 0.0008  -0.0082 -0.0103 94  HIS A O   
802  C  CB  . HIS A 94  ? 0.1537 0.0900 0.0886 0.0221  -0.0074 -0.0094 94  HIS A CB  
803  C  CG  . HIS A 94  ? 0.1324 0.0803 0.0857 0.0208  0.0026  -0.0074 94  HIS A CG  
804  N  ND1 . HIS A 94  ? 0.1448 0.0732 0.0917 0.0166  -0.0122 -0.0020 94  HIS A ND1 
805  C  CD2 . HIS A 94  ? 0.1341 0.0882 0.0653 0.0193  -0.0115 0.0000  94  HIS A CD2 
806  C  CE1 . HIS A 94  ? 0.1252 0.0781 0.0966 0.0183  -0.0096 -0.0103 94  HIS A CE1 
807  N  NE2 . HIS A 94  ? 0.1275 0.0688 0.0908 0.0201  0.0017  -0.0068 94  HIS A NE2 
808  N  N   . PHE A 95  ? 0.1369 0.0736 0.0883 0.0151  -0.0194 -0.0107 95  PHE A N   
809  C  CA  . PHE A 95  ? 0.1395 0.0702 0.0952 0.0068  -0.0210 -0.0097 95  PHE A CA  
810  C  C   . PHE A 95  ? 0.1534 0.0676 0.0767 0.0175  -0.0076 0.0023  95  PHE A C   
811  O  O   . PHE A 95  ? 0.1483 0.0936 0.0973 0.0218  -0.0035 -0.0175 95  PHE A O   
812  C  CB  . PHE A 95  ? 0.1455 0.0746 0.0973 0.0118  -0.0216 -0.0048 95  PHE A CB  
813  C  CG  . PHE A 95  ? 0.1460 0.0689 0.0878 0.0034  -0.0282 0.0017  95  PHE A CG  
814  C  CD1 . PHE A 95  ? 0.1624 0.0901 0.0992 0.0137  -0.0280 0.0019  95  PHE A CD1 
815  C  CD2 . PHE A 95  ? 0.1472 0.0908 0.0885 0.0278  -0.0273 0.0015  95  PHE A CD2 
816  C  CE1 . PHE A 95  ? 0.1615 0.1146 0.1015 0.0115  -0.0324 0.0115  95  PHE A CE1 
817  C  CE2 . PHE A 95  ? 0.1510 0.0986 0.1168 0.0049  -0.0428 0.0270  95  PHE A CE2 
818  C  CZ  . PHE A 95  ? 0.1362 0.1013 0.1206 -0.0006 -0.0344 0.0293  95  PHE A CZ  
819  N  N   . HIS A 96  ? 0.1323 0.0794 0.0762 0.0074  -0.0107 0.0024  96  HIS A N   
820  C  CA  . HIS A 96  ? 0.1474 0.0710 0.0851 0.0037  -0.0038 0.0046  96  HIS A CA  
821  C  C   . HIS A 96  ? 0.1250 0.0734 0.0860 0.0125  -0.0074 -0.0010 96  HIS A C   
822  O  O   . HIS A 96  ? 0.1292 0.0795 0.1032 0.0165  0.0043  0.0005  96  HIS A O   
823  C  CB  . HIS A 96  ? 0.1310 0.0793 0.0930 0.0208  -0.0008 0.0132  96  HIS A CB  
824  C  CG  . HIS A 96  ? 0.1121 0.0957 0.0767 0.0048  -0.0048 0.0044  96  HIS A CG  
825  N  ND1 . HIS A 96  ? 0.1229 0.0872 0.1085 0.0030  0.0066  -0.0034 96  HIS A ND1 
826  C  CD2 . HIS A 96  ? 0.1062 0.0806 0.0895 0.0076  -0.0077 0.0057  96  HIS A CD2 
827  C  CE1 . HIS A 96  ? 0.1083 0.0841 0.1036 0.0051  0.0034  0.0010  96  HIS A CE1 
828  N  NE2 . HIS A 96  ? 0.1039 0.0859 0.0901 0.0068  0.0010  -0.0013 96  HIS A NE2 
829  N  N   . TRP A 97  ? 0.1268 0.0758 0.0772 0.0143  0.0003  0.0023  97  TRP A N   
830  C  CA  . TRP A 97  ? 0.1333 0.0759 0.1010 0.0184  0.0007  0.0021  97  TRP A CA  
831  C  C   . TRP A 97  ? 0.1290 0.0797 0.0881 0.0109  0.0199  0.0091  97  TRP A C   
832  O  O   . TRP A 97  ? 0.1511 0.0820 0.0966 0.0171  0.0226  0.0086  97  TRP A O   
833  C  CB  . TRP A 97  ? 0.1676 0.0930 0.0869 0.0335  -0.0086 -0.0035 97  TRP A CB  
834  C  CG  . TRP A 97  ? 0.1685 0.0803 0.0905 0.0146  -0.0131 0.0057  97  TRP A CG  
835  C  CD1 . TRP A 97  ? 0.1647 0.0948 0.0904 0.0309  0.0103  0.0092  97  TRP A CD1 
836  C  CD2 . TRP A 97  ? 0.1580 0.0821 0.0953 0.0324  0.0024  0.0015  97  TRP A CD2 
837  N  NE1 . TRP A 97  ? 0.2270 0.0886 0.0987 0.0223  0.0148  0.0105  97  TRP A NE1 
838  C  CE2 . TRP A 97  ? 0.2135 0.0881 0.0706 0.0243  0.0060  0.0126  97  TRP A CE2 
839  C  CE3 . TRP A 97  ? 0.1565 0.0813 0.0952 0.0173  -0.0291 -0.0015 97  TRP A CE3 
840  C  CZ2 . TRP A 97  ? 0.1902 0.0957 0.0973 0.0276  0.0008  0.0015  97  TRP A CZ2 
841  C  CZ3 . TRP A 97  ? 0.1897 0.0945 0.0879 0.0199  0.0038  -0.0027 97  TRP A CZ3 
842  C  CH2 . TRP A 97  ? 0.2108 0.0964 0.0965 0.0262  0.0007  -0.0065 97  TRP A CH2 
843  N  N   . GLY A 98  ? 0.1488 0.0802 0.1044 0.0148  0.0043  0.0066  98  GLY A N   
844  C  CA  . GLY A 98  ? 0.1481 0.0931 0.0971 -0.0068 0.0177  -0.0010 98  GLY A CA  
845  C  C   . GLY A 98  ? 0.1474 0.0842 0.1132 0.0115  0.0142  0.0098  98  GLY A C   
846  O  O   . GLY A 98  ? 0.1908 0.0886 0.1166 0.0222  0.0082  0.0208  98  GLY A O   
847  N  N   . SER A 99  ? 0.1762 0.0956 0.1155 0.0043  0.0197  0.0220  99  SER A N   
848  C  CA  . SER A 99  ? 0.1882 0.1087 0.1248 0.0142  0.0171  0.0439  99  SER A CA  
849  C  C   . SER A 99  ? 0.1952 0.0816 0.1580 0.0006  0.0013  0.0406  99  SER A C   
850  O  O   . SER A 99  ? 0.2364 0.1349 0.1659 0.0116  0.0104  0.0548  99  SER A O   
851  C  CB  . SER A 99  ? 0.2058 0.1074 0.1488 0.0092  0.0174  0.0390  99  SER A CB  
852  O  OG  . SER A 99  ? 0.1689 0.1026 0.2217 -0.0098 0.0390  0.0285  99  SER A OG  
853  N  N   . LEU A 100 ? 0.1559 0.1039 0.1609 0.0109  0.0165  0.0381  100 LEU A N   
854  C  CA  . LEU A 100 ? 0.1722 0.0767 0.2185 0.0005  0.0093  0.0318  100 LEU A CA  
855  C  C   . LEU A 100 ? 0.1701 0.0807 0.1684 0.0249  0.0083  0.0092  100 LEU A C   
856  O  O   . LEU A 100 ? 0.1841 0.0808 0.1666 0.0208  0.0060  0.0147  100 LEU A O   
857  C  CB  . LEU A 100 ? 0.2657 0.1679 0.2675 -0.0542 0.0568  -0.0652 100 LEU A CB  
858  C  CG  . LEU A 100 ? 0.2178 0.2064 0.2666 -0.0118 0.0043  -0.0160 100 LEU A CG  
859  C  CD1 . LEU A 100 ? 0.2382 0.3835 0.3109 -0.1335 0.0240  -0.0176 100 LEU A CD1 
860  C  CD2 . LEU A 100 ? 0.4153 0.2319 0.3169 -0.0346 0.1625  0.1075  100 LEU A CD2 
861  N  N   . ASP A 101 ? 0.1609 0.0936 0.1937 0.0142  -0.0066 -0.0030 101 ASP A N   
862  C  CA  . ASP A 101 ? 0.1779 0.0838 0.1701 0.0126  -0.0023 -0.0035 101 ASP A CA  
863  C  C   . ASP A 101 ? 0.1675 0.0652 0.1820 0.0076  0.0161  -0.0076 101 ASP A C   
864  O  O   . ASP A 101 ? 0.2021 0.1067 0.1728 -0.0028 0.0108  -0.0111 101 ASP A O   
865  C  CB  . ASP A 101 ? 0.1650 0.0953 0.1771 0.0160  -0.0133 -0.0186 101 ASP A CB  
866  C  CG  . ASP A 101 ? 0.1960 0.1052 0.1889 0.0187  -0.0164 -0.0160 101 ASP A CG  
867  O  OD1 . ASP A 101 ? 0.1972 0.1439 0.1752 0.0311  0.0027  -0.0013 101 ASP A OD1 
868  O  OD2 . ASP A 101 ? 0.2379 0.1949 0.1926 0.0910  -0.0245 -0.0209 101 ASP A OD2 
869  N  N   . GLY A 102 ? 0.1752 0.0976 0.1696 0.0320  -0.0184 -0.0228 102 GLY A N   
870  C  CA  . GLY A 102 ? 0.1868 0.1011 0.2001 0.0177  0.0092  -0.0252 102 GLY A CA  
871  C  C   . GLY A 102 ? 0.1561 0.1042 0.1411 0.0087  0.0196  -0.0201 102 GLY A C   
872  O  O   . GLY A 102 ? 0.1972 0.1209 0.1428 0.0068  0.0228  -0.0273 102 GLY A O   
873  N  N   . GLN A 103 ? 0.1445 0.0927 0.1362 0.0160  0.0077  -0.0115 103 GLN A N   
874  C  CA  . GLN A 103 ? 0.1544 0.0887 0.1102 0.0001  0.0020  0.0030  103 GLN A CA  
875  C  C   . GLN A 103 ? 0.1351 0.0696 0.1189 0.0098  0.0217  -0.0024 103 GLN A C   
876  O  O   . GLN A 103 ? 0.1670 0.0886 0.1103 0.0094  0.0017  0.0038  103 GLN A O   
877  C  CB  . GLN A 103 ? 0.1667 0.0944 0.1260 -0.0140 0.0236  -0.0082 103 GLN A CB  
878  C  CG  . GLN A 103 ? 0.1492 0.1221 0.1632 -0.0137 0.0361  0.0043  103 GLN A CG  
879  C  CD  . GLN A 103 ? 0.1949 0.1168 0.1943 -0.0428 0.0582  -0.0447 103 GLN A CD  
880  O  OE1 . GLN A 103 ? 0.2518 0.2793 0.3616 -0.1429 0.1474  -0.1838 103 GLN A OE1 
881  N  NE2 . GLN A 103 ? 0.1685 0.1370 0.1772 -0.0291 0.0296  -0.0340 103 GLN A NE2 
882  N  N   . GLY A 104 ? 0.1191 0.0821 0.0995 -0.0028 0.0099  -0.0023 104 GLY A N   
883  C  CA  . GLY A 104 ? 0.1287 0.0791 0.1106 0.0077  0.0093  -0.0057 104 GLY A CA  
884  C  C   . GLY A 104 ? 0.1062 0.0760 0.1072 0.0162  -0.0085 -0.0041 104 GLY A C   
885  O  O   . GLY A 104 ? 0.1216 0.0807 0.1094 0.0087  0.0049  -0.0017 104 GLY A O   
886  N  N   . SER A 105 ? 0.0948 0.0816 0.0973 0.0080  -0.0021 0.0041  105 SER A N   
887  C  CA  . SER A 105 ? 0.1130 0.0755 0.0909 0.0065  -0.0024 -0.0034 105 SER A CA  
888  C  C   . SER A 105 ? 0.0885 0.0733 0.0947 0.0049  0.0060  -0.0027 105 SER A C   
889  O  O   . SER A 105 ? 0.1032 0.0817 0.1027 -0.0017 -0.0085 0.0082  105 SER A O   
890  C  CB  . SER A 105 ? 0.1103 0.0817 0.0938 0.0063  -0.0020 -0.0082 105 SER A CB  
891  O  OG  . SER A 105 ? 0.1171 0.0741 0.1000 0.0096  0.0000  -0.0037 105 SER A OG  
892  N  N   . GLU A 106 ? 0.0982 0.0728 0.0856 0.0076  0.0021  0.0028  106 GLU A N   
893  C  CA  . GLU A 106 ? 0.1124 0.0773 0.0807 0.0219  -0.0068 0.0054  106 GLU A CA  
894  C  C   . GLU A 106 ? 0.0891 0.0635 0.0979 -0.0006 -0.0052 0.0031  106 GLU A C   
895  O  O   . GLU A 106 ? 0.0901 0.0869 0.1067 -0.0003 -0.0070 -0.0023 106 GLU A O   
896  C  CB  . GLU A 106 ? 0.0973 0.0803 0.0782 0.0083  -0.0068 -0.0082 106 GLU A CB  
897  C  CG  . GLU A 106 ? 0.1557 0.0869 0.1105 0.0153  0.0300  -0.0068 106 GLU A CG  
898  C  CD  . GLU A 106 ? 0.1075 0.0828 0.1010 0.0094  -0.0086 0.0027  106 GLU A CD  
899  O  OE1 . GLU A 106 ? 0.0891 0.0857 0.1202 0.0076  0.0103  0.0006  106 GLU A OE1 
900  O  OE2 . GLU A 106 ? 0.1067 0.1039 0.1227 0.0020  0.0076  0.0124  106 GLU A OE2 
901  N  N   . HIS A 107 ? 0.0878 0.0672 0.0841 -0.0043 -0.0015 -0.0116 107 HIS A N   
902  C  CA  . HIS A 107 ? 0.0881 0.0688 0.0816 -0.0012 -0.0102 -0.0038 107 HIS A CA  
903  C  C   . HIS A 107 ? 0.0813 0.0714 0.0870 -0.0026 0.0000  -0.0120 107 HIS A C   
904  O  O   . HIS A 107 ? 0.0995 0.0776 0.0901 0.0051  -0.0038 -0.0066 107 HIS A O   
905  C  CB  . HIS A 107 ? 0.0868 0.0762 0.0923 0.0041  0.0074  -0.0046 107 HIS A CB  
906  C  CG  . HIS A 107 ? 0.0768 0.0719 0.0848 -0.0037 -0.0005 -0.0060 107 HIS A CG  
907  N  ND1 . HIS A 107 ? 0.0913 0.0734 0.0852 -0.0043 -0.0100 -0.0007 107 HIS A ND1 
908  C  CD2 . HIS A 107 ? 0.0702 0.0773 0.0930 -0.0126 -0.0054 0.0089  107 HIS A CD2 
909  C  CE1 . HIS A 107 ? 0.0882 0.0775 0.1052 -0.0212 -0.0046 0.0038  107 HIS A CE1 
910  N  NE2 . HIS A 107 ? 0.0917 0.0790 0.0846 -0.0114 -0.0054 0.0051  107 HIS A NE2 
911  N  N   . THR A 108 ? 0.0900 0.0843 0.0975 0.0000  0.0027  -0.0115 108 THR A N   
912  C  CA  . THR A 108 ? 0.1172 0.0654 0.1050 -0.0052 0.0037  -0.0041 108 THR A CA  
913  C  C   . THR A 108 ? 0.1023 0.0685 0.1062 -0.0080 -0.0081 -0.0185 108 THR A C   
914  O  O   . THR A 108 ? 0.1084 0.0811 0.1062 -0.0077 -0.0013 -0.0104 108 THR A O   
915  C  CB  . THR A 108 ? 0.1105 0.0829 0.1189 -0.0037 -0.0220 -0.0104 108 THR A CB  
916  O  OG1 . THR A 108 ? 0.1108 0.0903 0.1119 -0.0110 -0.0068 -0.0054 108 THR A OG1 
917  C  CG2 . THR A 108 ? 0.1118 0.1139 0.1013 -0.0131 -0.0115 -0.0121 108 THR A CG2 
918  N  N   . VAL A 109 ? 0.1064 0.0833 0.1159 -0.0089 -0.0001 -0.0209 109 VAL A N   
919  C  CA  . VAL A 109 ? 0.1202 0.0873 0.1107 0.0024  0.0093  -0.0267 109 VAL A CA  
920  C  C   . VAL A 109 ? 0.1092 0.0900 0.1345 0.0076  -0.0017 -0.0208 109 VAL A C   
921  O  O   . VAL A 109 ? 0.1292 0.0803 0.1361 0.0015  0.0105  -0.0263 109 VAL A O   
922  C  CB  . VAL A 109 ? 0.1206 0.0934 0.1418 -0.0006 0.0098  -0.0273 109 VAL A CB  
923  C  CG1 . VAL A 109 ? 0.1357 0.1252 0.1587 -0.0074 0.0303  -0.0432 109 VAL A CG1 
924  C  CG2 . VAL A 109 ? 0.1132 0.1139 0.1511 -0.0088 -0.0063 -0.0430 109 VAL A CG2 
925  N  N   . ASP A 110 ? 0.1330 0.0998 0.1148 -0.0118 0.0104  -0.0324 110 ASP A N   
926  C  CA  . ASP A 110 ? 0.1885 0.1004 0.1347 -0.0167 0.0161  -0.0485 110 ASP A CA  
927  C  C   . ASP A 110 ? 0.1817 0.0878 0.1105 -0.0126 0.0013  -0.0318 110 ASP A C   
928  O  O   . ASP A 110 ? 0.1875 0.0960 0.1351 -0.0122 0.0040  -0.0331 110 ASP A O   
929  C  CB  . ASP A 110 ? 0.1938 0.1142 0.1648 -0.0147 0.0361  -0.0604 110 ASP A CB  
930  C  CG  . ASP A 110 ? 0.2108 0.1440 0.1421 -0.0182 0.0293  -0.0608 110 ASP A CG  
931  O  OD1 . ASP A 110 ? 0.2111 0.1577 0.1721 -0.0450 0.0515  -0.0608 110 ASP A OD1 
932  O  OD2 . ASP A 110 ? 0.1967 0.2301 0.1897 -0.0174 0.0423  -0.0557 110 ASP A OD2 
933  N  N   . LYS A 111 ? 0.1268 0.0991 0.1089 -0.0093 -0.0038 -0.0162 111 LYS A N   
934  C  CA  . LYS A 111 ? 0.1483 0.0904 0.1251 -0.0252 0.0006  -0.0210 111 LYS A CA  
935  C  C   . LYS A 111 ? 0.1668 0.0885 0.1119 -0.0119 -0.0054 -0.0172 111 LYS A C   
936  O  O   . LYS A 111 ? 0.1621 0.1215 0.1422 -0.0121 0.0031  -0.0024 111 LYS A O   
937  C  CB  . LYS A 111 ? 0.1705 0.1592 0.1347 -0.0560 -0.0230 -0.0228 111 LYS A CB  
938  C  CG  . LYS A 111 ? 0.2578 0.2005 0.1606 -0.1108 -0.0443 -0.0054 111 LYS A CG  
939  C  CD  . LYS A 111 ? 0.2011 0.2490 0.2273 -0.0377 -0.0705 0.0804  111 LYS A CD  
940  C  CE  . LYS A 111 ? 0.2188 0.3779 0.2459 -0.0798 -0.0758 0.0846  111 LYS A CE  
941  N  NZ  . LYS A 111 ? 0.2134 0.2858 0.3122 0.0006  -0.0377 -0.0489 111 LYS A NZ  
942  N  N   . LYS A 112 ? 0.1506 0.0799 0.1224 0.0070  -0.0100 -0.0168 112 LYS A N   
943  C  CA  . LYS A 112 ? 0.1439 0.0882 0.1193 0.0081  0.0040  -0.0041 112 LYS A CA  
944  C  C   . LYS A 112 ? 0.1191 0.0785 0.1157 0.0073  -0.0142 -0.0107 112 LYS A C   
945  O  O   . LYS A 112 ? 0.1392 0.0740 0.1154 0.0023  -0.0026 -0.0048 112 LYS A O   
946  C  CB  . LYS A 112 ? 0.1509 0.1182 0.1492 0.0359  -0.0046 -0.0087 112 LYS A CB  
947  C  CG  . LYS A 112 ? 0.1412 0.1213 0.1676 0.0177  -0.0168 0.0141  112 LYS A CG  
948  C  CD  . LYS A 112 ? 0.1473 0.1889 0.2041 0.0196  -0.0231 -0.0198 112 LYS A CD  
949  C  CE  . LYS A 112 ? 0.2073 0.1700 0.2180 0.0230  -0.0452 -0.0272 112 LYS A CE  
950  N  NZ  . LYS A 112 ? 0.2030 0.1825 0.2152 0.0335  -0.0430 -0.0434 112 LYS A NZ  
951  N  N   A LYS A 113 ? 0.1350 0.0848 0.1080 -0.0124 -0.0017 -0.0037 113 LYS A N   
952  N  N   B LYS A 113 ? 0.1349 0.0876 0.1106 -0.0152 -0.0015 -0.0015 113 LYS A N   
953  C  CA  A LYS A 113 ? 0.1424 0.0715 0.1141 -0.0035 0.0032  -0.0118 113 LYS A CA  
954  C  CA  B LYS A 113 ? 0.1319 0.0833 0.1081 -0.0121 -0.0126 -0.0103 113 LYS A CA  
955  C  C   A LYS A 113 ? 0.1313 0.0605 0.1331 0.0065  0.0098  -0.0215 113 LYS A C   
956  C  C   B LYS A 113 ? 0.1264 0.0877 0.1114 -0.0081 -0.0091 0.0091  113 LYS A C   
957  O  O   A LYS A 113 ? 0.1387 0.0511 0.1518 0.0076  0.0041  -0.0161 113 LYS A O   
958  O  O   B LYS A 113 ? 0.1383 0.0891 0.1193 -0.0066 -0.0085 0.0121  113 LYS A O   
959  C  CB  A LYS A 113 ? 0.1184 0.1015 0.1137 -0.0049 -0.0071 -0.0038 113 LYS A CB  
960  C  CB  B LYS A 113 ? 0.1281 0.1058 0.1344 -0.0265 -0.0049 0.0021  113 LYS A CB  
961  C  CG  A LYS A 113 ? 0.1159 0.1446 0.0980 -0.0228 0.0035  -0.0215 113 LYS A CG  
962  C  CG  B LYS A 113 ? 0.1075 0.1409 0.1729 -0.0165 -0.0038 0.0162  113 LYS A CG  
963  C  CD  A LYS A 113 ? 0.1045 0.1545 0.1386 0.0005  0.0178  0.0289  113 LYS A CD  
964  C  CD  B LYS A 113 ? 0.1184 0.1076 0.2079 -0.0313 -0.0043 0.0040  113 LYS A CD  
965  C  CE  A LYS A 113 ? 0.1136 0.1473 0.1686 0.0153  0.0375  0.0126  113 LYS A CE  
966  C  CE  B LYS A 113 ? 0.1542 0.1881 0.2038 -0.0313 -0.0294 0.0107  113 LYS A CE  
967  N  NZ  A LYS A 113 ? 0.0723 0.1902 0.2241 0.0020  -0.0260 0.0133  113 LYS A NZ  
968  N  NZ  B LYS A 113 ? 0.1932 0.1938 0.2563 -0.0419 0.0339  -0.0155 113 LYS A NZ  
969  N  N   . TYR A 114 ? 0.1151 0.0803 0.1085 -0.0012 -0.0120 -0.0092 114 TYR A N   
970  C  CA  . TYR A 114 ? 0.1081 0.0768 0.1272 0.0077  -0.0149 -0.0168 114 TYR A CA  
971  C  C   . TYR A 114 ? 0.0992 0.0646 0.1148 0.0057  -0.0124 0.0021  114 TYR A C   
972  O  O   . TYR A 114 ? 0.1090 0.0838 0.1130 -0.0003 0.0010  0.0070  114 TYR A O   
973  C  CB  . TYR A 114 ? 0.1134 0.0725 0.1222 0.0027  0.0015  -0.0102 114 TYR A CB  
974  C  CG  . TYR A 114 ? 0.1222 0.0745 0.1269 -0.0076 -0.0126 -0.0174 114 TYR A CG  
975  C  CD1 . TYR A 114 ? 0.1430 0.0856 0.1342 -0.0136 -0.0035 -0.0142 114 TYR A CD1 
976  C  CD2 . TYR A 114 ? 0.1101 0.0895 0.1704 0.0059  0.0015  -0.0333 114 TYR A CD2 
977  C  CE1 . TYR A 114 ? 0.1900 0.1036 0.1225 -0.0131 0.0120  -0.0099 114 TYR A CE1 
978  C  CE2 . TYR A 114 ? 0.1655 0.1155 0.1689 0.0093  0.0087  -0.0216 114 TYR A CE2 
979  C  CZ  . TYR A 114 ? 0.1535 0.1199 0.1709 0.0026  0.0388  -0.0225 114 TYR A CZ  
980  O  OH  . TYR A 114 ? 0.2590 0.1988 0.2303 -0.0154 0.1004  -0.0255 114 TYR A OH  
981  N  N   . ALA A 115 ? 0.1368 0.0698 0.1133 0.0166  -0.0174 -0.0010 115 ALA A N   
982  C  CA  . ALA A 115 ? 0.1256 0.0692 0.1236 0.0097  -0.0092 0.0043  115 ALA A CA  
983  C  C   . ALA A 115 ? 0.1343 0.0732 0.1001 0.0120  -0.0175 -0.0043 115 ALA A C   
984  O  O   . ALA A 115 ? 0.1402 0.0811 0.1191 0.0188  0.0034  0.0074  115 ALA A O   
985  C  CB  . ALA A 115 ? 0.1430 0.0842 0.1387 0.0259  -0.0096 0.0049  115 ALA A CB  
986  N  N   . ALA A 116 ? 0.1283 0.0680 0.1014 0.0060  -0.0108 -0.0057 116 ALA A N   
987  C  CA  . ALA A 116 ? 0.1411 0.0720 0.0948 0.0035  -0.0140 -0.0052 116 ALA A CA  
988  C  C   . ALA A 116 ? 0.1026 0.0737 0.0918 0.0017  -0.0152 -0.0118 116 ALA A C   
989  O  O   . ALA A 116 ? 0.1280 0.0706 0.0970 0.0118  -0.0017 -0.0081 116 ALA A O   
990  C  CB  . ALA A 116 ? 0.1618 0.0841 0.1077 0.0137  -0.0166 -0.0020 116 ALA A CB  
991  N  N   . GLU A 117 ? 0.1143 0.0653 0.0960 0.0031  -0.0102 0.0003  117 GLU A N   
992  C  CA  . GLU A 117 ? 0.1057 0.0631 0.0838 0.0048  -0.0034 -0.0017 117 GLU A CA  
993  C  C   . GLU A 117 ? 0.1216 0.0684 0.0769 0.0142  -0.0089 -0.0038 117 GLU A C   
994  O  O   . GLU A 117 ? 0.1154 0.0910 0.1032 0.0062  0.0010  -0.0201 117 GLU A O   
995  C  CB  . GLU A 117 ? 0.1164 0.0797 0.0864 0.0024  -0.0120 -0.0066 117 GLU A CB  
996  C  CG  . GLU A 117 ? 0.1220 0.0815 0.0974 -0.0086 -0.0248 -0.0060 117 GLU A CG  
997  C  CD  . GLU A 117 ? 0.0925 0.0768 0.0851 -0.0046 0.0057  -0.0172 117 GLU A CD  
998  O  OE1 . GLU A 117 ? 0.1032 0.0895 0.1027 -0.0028 -0.0071 -0.0089 117 GLU A OE1 
999  O  OE2 . GLU A 117 ? 0.1305 0.0727 0.0940 0.0023  -0.0222 -0.0034 117 GLU A OE2 
1000 N  N   . LEU A 118 ? 0.1139 0.0706 0.0947 0.0089  -0.0177 -0.0054 118 LEU A N   
1001 C  CA  . LEU A 118 ? 0.1159 0.0631 0.0878 -0.0003 -0.0274 -0.0031 118 LEU A CA  
1002 C  C   . LEU A 118 ? 0.1106 0.0601 0.0891 0.0020  -0.0182 -0.0038 118 LEU A C   
1003 O  O   . LEU A 118 ? 0.1229 0.0706 0.0776 0.0057  -0.0176 -0.0043 118 LEU A O   
1004 C  CB  . LEU A 118 ? 0.1347 0.0764 0.1036 0.0046  -0.0388 0.0037  118 LEU A CB  
1005 C  CG  . LEU A 118 ? 0.1313 0.0855 0.1077 0.0078  -0.0361 -0.0122 118 LEU A CG  
1006 C  CD1 . LEU A 118 ? 0.1726 0.0852 0.1079 0.0020  -0.0516 -0.0227 118 LEU A CD1 
1007 C  CD2 . LEU A 118 ? 0.1310 0.1121 0.1446 -0.0099 -0.0531 -0.0046 118 LEU A CD2 
1008 N  N   . HIS A 119 ? 0.1083 0.0617 0.0860 0.0043  -0.0193 -0.0049 119 HIS A N   
1009 C  CA  . HIS A 119 ? 0.1172 0.0658 0.0742 0.0098  -0.0136 -0.0097 119 HIS A CA  
1010 C  C   . HIS A 119 ? 0.1132 0.0672 0.0820 0.0168  -0.0179 -0.0110 119 HIS A C   
1011 O  O   . HIS A 119 ? 0.1363 0.0754 0.0878 0.0003  -0.0155 -0.0114 119 HIS A O   
1012 C  CB  . HIS A 119 ? 0.1236 0.0584 0.0890 -0.0026 -0.0148 -0.0044 119 HIS A CB  
1013 C  CG  . HIS A 119 ? 0.0891 0.0812 0.0745 0.0110  0.0043  0.0068  119 HIS A CG  
1014 N  ND1 . HIS A 119 ? 0.1036 0.0775 0.0668 0.0035  0.0000  0.0012  119 HIS A ND1 
1015 C  CD2 . HIS A 119 ? 0.1027 0.0766 0.0878 0.0017  -0.0103 0.0007  119 HIS A CD2 
1016 C  CE1 . HIS A 119 ? 0.1080 0.0746 0.0763 0.0071  0.0028  0.0062  119 HIS A CE1 
1017 N  NE2 . HIS A 119 ? 0.0931 0.0870 0.0865 -0.0021 -0.0113 -0.0071 119 HIS A NE2 
1018 N  N   . LEU A 120 ? 0.1087 0.0601 0.0864 0.0012  -0.0152 -0.0054 120 LEU A N   
1019 C  CA  . LEU A 120 ? 0.1136 0.0702 0.1035 -0.0099 -0.0265 -0.0094 120 LEU A CA  
1020 C  C   . LEU A 120 ? 0.1105 0.0600 0.0802 -0.0031 -0.0149 -0.0073 120 LEU A C   
1021 O  O   . LEU A 120 ? 0.1053 0.0657 0.0948 0.0065  -0.0142 -0.0010 120 LEU A O   
1022 C  CB  . LEU A 120 ? 0.1184 0.0788 0.1275 -0.0019 -0.0441 -0.0012 120 LEU A CB  
1023 C  CG  . LEU A 120 ? 0.1440 0.0873 0.1295 0.0126  -0.0522 -0.0104 120 LEU A CG  
1024 C  CD1 . LEU A 120 ? 0.2500 0.1254 0.1489 0.0907  -0.0259 -0.0023 120 LEU A CD1 
1025 C  CD2 . LEU A 120 ? 0.1782 0.1353 0.1348 -0.0081 -0.0744 0.0048  120 LEU A CD2 
1026 N  N   . VAL A 121 ? 0.1218 0.0688 0.0883 0.0062  -0.0142 -0.0109 121 VAL A N   
1027 C  CA  . VAL A 121 ? 0.1416 0.0590 0.1044 0.0138  -0.0149 -0.0170 121 VAL A CA  
1028 C  C   . VAL A 121 ? 0.1372 0.0654 0.0953 0.0143  -0.0060 0.0017  121 VAL A C   
1029 O  O   . VAL A 121 ? 0.1513 0.0719 0.0943 0.0006  -0.0183 -0.0098 121 VAL A O   
1030 C  CB  . VAL A 121 ? 0.1483 0.0683 0.1211 0.0159  0.0080  0.0052  121 VAL A CB  
1031 C  CG1 . VAL A 121 ? 0.1577 0.1068 0.1164 0.0339  0.0080  0.0055  121 VAL A CG1 
1032 C  CG2 . VAL A 121 ? 0.1333 0.0860 0.1236 -0.0024 0.0082  0.0063  121 VAL A CG2 
1033 N  N   . HIS A 122 ? 0.1344 0.0644 0.0899 0.0137  -0.0186 -0.0027 122 HIS A N   
1034 C  CA  . HIS A 122 ? 0.1342 0.0628 0.1017 0.0040  -0.0100 0.0024  122 HIS A CA  
1035 C  C   . HIS A 122 ? 0.1105 0.0725 0.1011 -0.0019 -0.0186 -0.0126 122 HIS A C   
1036 O  O   . HIS A 122 ? 0.1409 0.0639 0.1080 0.0100  -0.0182 -0.0076 122 HIS A O   
1037 C  CB  . HIS A 122 ? 0.1200 0.0688 0.1155 0.0017  -0.0124 -0.0043 122 HIS A CB  
1038 C  CG  . HIS A 122 ? 0.1120 0.0702 0.1186 0.0031  -0.0179 -0.0054 122 HIS A CG  
1039 N  ND1 . HIS A 122 ? 0.1133 0.0731 0.1136 0.0046  -0.0108 -0.0110 122 HIS A ND1 
1040 C  CD2 . HIS A 122 ? 0.1172 0.0992 0.1254 0.0184  -0.0297 -0.0129 122 HIS A CD2 
1041 C  CE1 . HIS A 122 ? 0.0978 0.0860 0.1328 0.0082  -0.0070 -0.0078 122 HIS A CE1 
1042 N  NE2 . HIS A 122 ? 0.1005 0.0983 0.1450 0.0111  -0.0152 -0.0098 122 HIS A NE2 
1043 N  N   . TRP A 123 ? 0.1148 0.0631 0.1054 0.0019  -0.0143 0.0005  123 TRP A N   
1044 C  CA  . TRP A 123 ? 0.1238 0.0653 0.1132 0.0023  -0.0171 -0.0020 123 TRP A CA  
1045 C  C   . TRP A 123 ? 0.1123 0.0627 0.1243 0.0087  -0.0046 0.0135  123 TRP A C   
1046 O  O   . TRP A 123 ? 0.1123 0.0851 0.1309 -0.0052 -0.0111 0.0089  123 TRP A O   
1047 C  CB  . TRP A 123 ? 0.1325 0.0917 0.1216 0.0201  -0.0168 0.0043  123 TRP A CB  
1048 C  CG  . TRP A 123 ? 0.1557 0.0860 0.1271 0.0295  -0.0008 -0.0041 123 TRP A CG  
1049 C  CD1 . TRP A 123 ? 0.1938 0.0958 0.1242 0.0359  -0.0170 -0.0098 123 TRP A CD1 
1050 C  CD2 . TRP A 123 ? 0.2017 0.0771 0.1114 0.0317  0.0010  -0.0032 123 TRP A CD2 
1051 N  NE1 . TRP A 123 ? 0.2225 0.0807 0.1336 0.0154  -0.0193 -0.0017 123 TRP A NE1 
1052 C  CE2 . TRP A 123 ? 0.2234 0.0812 0.1433 0.0171  -0.0091 -0.0092 123 TRP A CE2 
1053 C  CE3 . TRP A 123 ? 0.2497 0.0626 0.1421 0.0461  0.0098  -0.0098 123 TRP A CE3 
1054 C  CZ2 . TRP A 123 ? 0.2960 0.0833 0.1501 0.0113  0.0052  -0.0098 123 TRP A CZ2 
1055 C  CZ3 . TRP A 123 ? 0.3705 0.0815 0.1449 0.0254  -0.0048 0.0046  123 TRP A CZ3 
1056 C  CH2 . TRP A 123 ? 0.3136 0.0747 0.1636 0.0015  -0.0013 -0.0071 123 TRP A CH2 
1057 N  N   . ASN A 124 ? 0.1194 0.0716 0.1202 -0.0020 -0.0077 0.0110  124 ASN A N   
1058 C  CA  . ASN A 124 ? 0.1262 0.0690 0.1368 -0.0125 -0.0171 0.0232  124 ASN A CA  
1059 C  C   . ASN A 124 ? 0.1377 0.0786 0.1384 -0.0122 -0.0038 0.0264  124 ASN A C   
1060 O  O   . ASN A 124 ? 0.1220 0.0837 0.1321 -0.0094 -0.0037 0.0071  124 ASN A O   
1061 C  CB  . ASN A 124 ? 0.1432 0.0861 0.1193 -0.0076 0.0015  0.0093  124 ASN A CB  
1062 C  CG  . ASN A 124 ? 0.1597 0.0698 0.1245 0.0093  0.0179  0.0071  124 ASN A CG  
1063 O  OD1 . ASN A 124 ? 0.1762 0.0824 0.1421 -0.0197 0.0114  0.0109  124 ASN A OD1 
1064 N  ND2 . ASN A 124 ? 0.1928 0.0938 0.1325 0.0001  0.0027  0.0131  124 ASN A ND2 
1065 N  N   . THR A 125 ? 0.1398 0.0788 0.1606 -0.0185 -0.0155 0.0171  125 THR A N   
1066 C  CA  . THR A 125 ? 0.1451 0.0907 0.1815 -0.0195 -0.0194 -0.0013 125 THR A CA  
1067 C  C   . THR A 125 ? 0.1917 0.0720 0.2040 -0.0252 0.0142  -0.0099 125 THR A C   
1068 O  O   . THR A 125 ? 0.1978 0.0934 0.2060 -0.0193 -0.0193 -0.0142 125 THR A O   
1069 C  CB  . THR A 125 ? 0.1670 0.1327 0.2380 -0.0178 -0.0335 -0.0182 125 THR A CB  
1070 O  OG1 . THR A 125 ? 0.2207 0.1548 0.3492 -0.0887 0.0335  -0.0094 125 THR A OG1 
1071 C  CG2 . THR A 125 ? 0.2118 0.1266 0.3104 -0.0023 -0.1304 -0.0181 125 THR A CG2 
1072 N  N   . LYS A 126 ? 0.1755 0.0859 0.1766 -0.0059 0.0006  0.0179  127 LYS A N   
1073 C  CA  . LYS A 126 ? 0.2405 0.1005 0.1782 0.0109  0.0065  0.0295  127 LYS A CA  
1074 C  C   . LYS A 126 ? 0.2161 0.0636 0.1680 -0.0121 -0.0107 0.0131  127 LYS A C   
1075 O  O   . LYS A 126 ? 0.2415 0.0851 0.1889 0.0109  0.0086  0.0309  127 LYS A O   
1076 C  CB  . LYS A 126 ? 0.2515 0.1265 0.1915 0.0229  -0.0120 0.0379  127 LYS A CB  
1077 C  CG  . LYS A 126 ? 0.1888 0.1695 0.1768 0.0111  0.0142  0.0156  127 LYS A CG  
1078 C  CD  . LYS A 126 ? 0.3269 0.1999 0.1764 0.0653  0.0272  0.0240  127 LYS A CD  
1079 C  CE  . LYS A 126 ? 0.2044 0.3765 0.3564 -0.0559 0.0926  0.0073  127 LYS A CE  
1080 N  NZ  . LYS A 126 ? 0.6905 1.0770 0.2011 -0.1367 0.1326  0.0186  127 LYS A NZ  
1081 N  N   . TYR A 127 ? 0.1861 0.0772 0.1331 -0.0040 -0.0073 -0.0044 128 TYR A N   
1082 C  CA  . TYR A 127 ? 0.2182 0.0747 0.1475 0.0080  -0.0159 0.0062  128 TYR A CA  
1083 C  C   . TYR A 127 ? 0.1717 0.0863 0.1486 0.0253  0.0035  0.0038  128 TYR A C   
1084 O  O   . TYR A 127 ? 0.1870 0.0900 0.1618 0.0020  -0.0082 -0.0015 128 TYR A O   
1085 C  CB  . TYR A 127 ? 0.1782 0.0882 0.1665 0.0109  -0.0127 -0.0103 128 TYR A CB  
1086 C  CG  . TYR A 127 ? 0.1546 0.0817 0.1547 0.0076  -0.0289 0.0070  128 TYR A CG  
1087 C  CD1 . TYR A 127 ? 0.2003 0.1040 0.1685 0.0103  -0.0188 0.0186  128 TYR A CD1 
1088 C  CD2 . TYR A 127 ? 0.1556 0.0936 0.1469 0.0017  -0.0066 0.0088  128 TYR A CD2 
1089 C  CE1 . TYR A 127 ? 0.2123 0.1085 0.1368 -0.0126 -0.0331 0.0196  128 TYR A CE1 
1090 C  CE2 . TYR A 127 ? 0.1318 0.1083 0.1437 -0.0120 -0.0052 0.0282  128 TYR A CE2 
1091 C  CZ  . TYR A 127 ? 0.1791 0.1212 0.1307 -0.0059 0.0030  0.0230  128 TYR A CZ  
1092 O  OH  . TYR A 127 ? 0.2204 0.1321 0.1488 -0.0251 -0.0162 0.0476  128 TYR A OH  
1093 N  N   . GLY A 128 ? 0.1722 0.0820 0.1474 0.0204  -0.0153 -0.0096 129 GLY A N   
1094 C  CA  . GLY A 128 ? 0.2309 0.0759 0.1629 0.0209  -0.0031 -0.0057 129 GLY A CA  
1095 C  C   . GLY A 128 ? 0.2473 0.0768 0.1482 0.0076  -0.0137 -0.0186 129 GLY A C   
1096 O  O   . GLY A 128 ? 0.2962 0.1105 0.1509 0.0093  -0.0414 -0.0359 129 GLY A O   
1097 N  N   . ASP A 129 ? 0.2608 0.0944 0.1216 -0.0118 -0.0184 0.0012  130 ASP A N   
1098 C  CA  . ASP A 129 ? 0.3160 0.1044 0.1233 -0.0059 0.0054  -0.0114 130 ASP A CA  
1099 C  C   . ASP A 129 ? 0.2838 0.1068 0.1324 0.0006  -0.0059 -0.0034 130 ASP A C   
1100 O  O   . ASP A 129 ? 0.3219 0.1094 0.1134 -0.0272 -0.0015 -0.0019 130 ASP A O   
1101 C  CB  . ASP A 129 ? 0.2691 0.1467 0.2046 -0.0041 0.0447  -0.0262 130 ASP A CB  
1102 C  CG  . ASP A 129 ? 0.2930 0.0962 0.1284 -0.0174 0.0386  -0.0173 130 ASP A CG  
1103 O  OD1 . ASP A 129 ? 0.4000 0.1764 0.2326 0.0603  -0.0207 0.0146  130 ASP A OD1 
1104 O  OD2 . ASP A 129 ? 0.3264 0.1582 0.2208 0.0098  0.0870  -0.0414 130 ASP A OD2 
1105 N  N   . PHE A 130 ? 0.2883 0.1005 0.1199 -0.0063 0.0160  -0.0035 131 PHE A N   
1106 C  CA  . PHE A 130 ? 0.2240 0.1071 0.1057 -0.0038 -0.0037 -0.0076 131 PHE A CA  
1107 C  C   . PHE A 130 ? 0.2273 0.0979 0.1420 0.0170  0.0438  0.0020  131 PHE A C   
1108 O  O   . PHE A 130 ? 0.2070 0.1105 0.1274 0.0178  0.0265  -0.0049 131 PHE A O   
1109 C  CB  . PHE A 130 ? 0.2736 0.1055 0.1513 -0.0038 -0.0188 0.0156  131 PHE A CB  
1110 C  CG  . PHE A 130 ? 0.1712 0.1071 0.1648 -0.0054 0.0204  0.0187  131 PHE A CG  
1111 C  CD1 . PHE A 130 ? 0.2361 0.0996 0.1420 0.0177  0.0071  0.0115  131 PHE A CD1 
1112 C  CD2 . PHE A 130 ? 0.2240 0.1261 0.1905 0.0185  0.0419  0.0219  131 PHE A CD2 
1113 C  CE1 . PHE A 130 ? 0.2237 0.1255 0.1647 0.0384  0.0184  0.0177  131 PHE A CE1 
1114 C  CE2 . PHE A 130 ? 0.2400 0.1821 0.1917 -0.0121 -0.0074 0.0000  131 PHE A CE2 
1115 C  CZ  . PHE A 130 ? 0.2500 0.1940 0.1842 -0.0013 -0.0017 0.0187  131 PHE A CZ  
1116 N  N   . GLY A 131 ? 0.2802 0.1351 0.1554 0.0346  0.0599  -0.0230 132 GLY A N   
1117 C  CA  . GLY A 131 ? 0.2653 0.1670 0.2065 0.0516  0.1298  -0.0013 132 GLY A CA  
1118 C  C   . GLY A 131 ? 0.2371 0.1887 0.2029 0.0496  0.0917  -0.0307 132 GLY A C   
1119 O  O   . GLY A 131 ? 0.2630 0.1233 0.2870 0.0339  0.0625  0.0275  132 GLY A O   
1120 N  N   . LYS A 132 ? 0.2450 0.1224 0.1898 0.0502  0.0368  -0.0245 133 LYS A N   
1121 C  CA  . LYS A 132 ? 0.2070 0.1005 0.1844 0.0434  0.0173  -0.0129 133 LYS A CA  
1122 C  C   . LYS A 132 ? 0.1864 0.0931 0.1841 0.0465  0.0153  0.0126  133 LYS A C   
1123 O  O   . LYS A 132 ? 0.1605 0.1234 0.1763 0.0395  0.0068  0.0182  133 LYS A O   
1124 C  CB  . LYS A 132 ? 0.2017 0.1124 0.2169 0.0245  -0.0010 -0.0024 133 LYS A CB  
1125 C  CG  . LYS A 132 ? 0.2284 0.1186 0.3786 0.0164  0.0080  -0.0430 133 LYS A CG  
1126 C  CD  . LYS A 132 ? 0.3477 0.1941 0.6337 0.0641  -0.1616 -0.1939 133 LYS A CD  
1127 C  CE  . LYS A 132 ? 0.3107 0.1838 0.7005 0.1011  -0.1466 -0.0850 133 LYS A CE  
1128 N  NZ  . LYS A 132 ? 0.6001 0.4266 0.8701 0.3783  -0.3804 -0.2373 133 LYS A NZ  
1129 N  N   . ALA A 133 ? 0.1724 0.1010 0.1500 0.0474  0.0209  0.0085  134 ALA A N   
1130 C  CA  . ALA A 133 ? 0.1483 0.1023 0.1314 0.0368  0.0082  -0.0006 134 ALA A CA  
1131 C  C   . ALA A 133 ? 0.1606 0.1177 0.1040 0.0489  0.0205  -0.0043 134 ALA A C   
1132 O  O   . ALA A 133 ? 0.1269 0.1405 0.1134 0.0307  0.0040  0.0024  134 ALA A O   
1133 C  CB  . ALA A 133 ? 0.1530 0.1146 0.1166 0.0412  -0.0040 0.0074  134 ALA A CB  
1134 N  N   . VAL A 134 ? 0.1615 0.1064 0.1332 0.0335  0.0245  0.0068  135 VAL A N   
1135 C  CA  . VAL A 134 ? 0.1832 0.1242 0.1383 0.0324  0.0408  -0.0153 135 VAL A CA  
1136 C  C   . VAL A 134 ? 0.1685 0.1155 0.1474 0.0241  0.0359  0.0035  135 VAL A C   
1137 O  O   . VAL A 134 ? 0.1552 0.1312 0.1881 0.0046  0.0461  0.0028  135 VAL A O   
1138 C  CB  . VAL A 134 ? 0.1565 0.1308 0.1676 0.0187  0.0570  -0.0038 135 VAL A CB  
1139 C  CG1 . VAL A 134 ? 0.2509 0.1500 0.1912 0.0657  0.0131  0.0076  135 VAL A CG1 
1140 C  CG2 . VAL A 134 ? 0.2132 0.1352 0.1597 0.0353  0.0599  0.0177  135 VAL A CG2 
1141 N  N   . GLN A 135 ? 0.1477 0.1089 0.1685 0.0236  0.0266  0.0032  136 GLN A N   
1142 C  CA  . GLN A 135 ? 0.1699 0.1442 0.2078 0.0350  0.0087  0.0266  136 GLN A CA  
1143 C  C   . GLN A 135 ? 0.1376 0.1405 0.1840 0.0198  -0.0204 0.0121  136 GLN A C   
1144 O  O   . GLN A 135 ? 0.1416 0.2119 0.2128 0.0445  -0.0065 0.0524  136 GLN A O   
1145 C  CB  . GLN A 135 ? 0.1799 0.1543 0.2107 0.0586  0.0197  0.0109  136 GLN A CB  
1146 C  CG  . GLN A 135 ? 0.2290 0.2264 0.2567 0.0922  0.0597  -0.0303 136 GLN A CG  
1147 C  CD  . GLN A 135 ? 0.3691 0.2412 0.3215 0.1088  0.0346  -0.0001 136 GLN A CD  
1148 O  OE1 . GLN A 135 ? 0.2561 0.3885 0.4790 0.0951  0.0496  -0.0851 136 GLN A OE1 
1149 N  NE2 . GLN A 135 ? 0.3282 0.2472 0.4212 0.1234  -0.0564 -0.0979 136 GLN A NE2 
1150 N  N   . GLN A 136 ? 0.1238 0.1184 0.1508 0.0159  0.0100  0.0175  137 GLN A N   
1151 C  CA  . GLN A 136 ? 0.1469 0.1400 0.1236 0.0023  -0.0030 0.0175  137 GLN A CA  
1152 C  C   . GLN A 136 ? 0.1234 0.1356 0.1168 -0.0107 -0.0216 0.0194  137 GLN A C   
1153 O  O   . GLN A 136 ? 0.1484 0.1092 0.1096 0.0043  -0.0162 0.0157  137 GLN A O   
1154 C  CB  . GLN A 136 ? 0.1543 0.1044 0.1679 0.0021  -0.0203 0.0198  137 GLN A CB  
1155 C  CG  . GLN A 136 ? 0.2831 0.1362 0.1889 -0.0087 0.0421  0.0057  137 GLN A CG  
1156 C  CD  . GLN A 136 ? 0.2237 0.1636 0.2401 -0.0263 0.0205  -0.0197 137 GLN A CD  
1157 O  OE1 . GLN A 136 ? 0.2048 0.1509 0.2777 0.0178  0.0086  0.0728  137 GLN A OE1 
1158 N  NE2 . GLN A 136 ? 0.2849 0.2396 0.2563 0.0035  0.0285  -0.0317 137 GLN A NE2 
1159 N  N   . PRO A 137 ? 0.1177 0.1630 0.1159 0.0017  -0.0153 0.0199  138 PRO A N   
1160 C  CA  . PRO A 137 ? 0.1557 0.1686 0.0940 -0.0233 -0.0104 -0.0100 138 PRO A CA  
1161 C  C   . PRO A 137 ? 0.1362 0.1598 0.0978 -0.0190 -0.0098 0.0021  138 PRO A C   
1162 O  O   . PRO A 137 ? 0.2163 0.1492 0.1738 -0.0177 -0.0087 -0.0366 138 PRO A O   
1163 C  CB  . PRO A 137 ? 0.2366 0.2567 0.0964 -0.0293 -0.0242 0.0164  138 PRO A CB  
1164 C  CG  . PRO A 137 ? 0.3607 0.3131 0.1415 0.0254  -0.0630 0.0548  138 PRO A CG  
1165 C  CD  . PRO A 137 ? 0.1975 0.2397 0.1386 0.0384  -0.0300 0.0586  138 PRO A CD  
1166 N  N   . ASP A 138 ? 0.1345 0.1331 0.1027 -0.0091 -0.0049 0.0131  139 ASP A N   
1167 C  CA  . ASP A 138 ? 0.1308 0.1333 0.1076 0.0003  -0.0046 0.0070  139 ASP A CA  
1168 C  C   . ASP A 138 ? 0.1238 0.0964 0.1230 0.0098  -0.0187 -0.0096 139 ASP A C   
1169 O  O   . ASP A 138 ? 0.1289 0.1105 0.1132 -0.0052 0.0021  0.0019  139 ASP A O   
1170 C  CB  . ASP A 138 ? 0.1684 0.1502 0.1087 -0.0077 0.0185  -0.0049 139 ASP A CB  
1171 C  CG  . ASP A 138 ? 0.1544 0.1729 0.1356 -0.0275 0.0070  0.0102  139 ASP A CG  
1172 O  OD1 . ASP A 138 ? 0.1870 0.1240 0.1536 -0.0219 -0.0023 0.0408  139 ASP A OD1 
1173 O  OD2 . ASP A 138 ? 0.2167 0.1961 0.1614 -0.0425 0.0210  0.0403  139 ASP A OD2 
1174 N  N   . GLY A 139 ? 0.1203 0.0883 0.0922 0.0057  0.0003  0.0086  140 GLY A N   
1175 C  CA  . GLY A 139 ? 0.1211 0.0882 0.1054 0.0063  -0.0199 -0.0038 140 GLY A CA  
1176 C  C   . GLY A 139 ? 0.1087 0.0684 0.1049 0.0046  -0.0048 0.0017  140 GLY A C   
1177 O  O   . GLY A 139 ? 0.1233 0.0790 0.1058 -0.0065 -0.0126 -0.0007 140 GLY A O   
1178 N  N   . LEU A 140 ? 0.1022 0.0680 0.1005 0.0035  -0.0065 0.0068  141 LEU A N   
1179 C  CA  . LEU A 140 ? 0.1037 0.0775 0.0944 0.0017  0.0000  0.0135  141 LEU A CA  
1180 C  C   . LEU A 140 ? 0.0934 0.0622 0.0918 -0.0126 -0.0082 0.0015  141 LEU A C   
1181 O  O   . LEU A 140 ? 0.1006 0.0714 0.1046 -0.0008 -0.0057 -0.0065 141 LEU A O   
1182 C  CB  . LEU A 140 ? 0.1046 0.0816 0.1110 -0.0037 0.0087  0.0037  141 LEU A CB  
1183 C  CG  . LEU A 140 ? 0.1380 0.0970 0.1273 -0.0219 0.0116  -0.0065 141 LEU A CG  
1184 C  CD1 . LEU A 140 ? 0.1238 0.1033 0.1392 -0.0174 0.0286  -0.0028 141 LEU A CD1 
1185 C  CD2 . LEU A 140 ? 0.1310 0.1101 0.1630 -0.0093 0.0130  -0.0302 141 LEU A CD2 
1186 N  N   . ALA A 141 ? 0.0976 0.0654 0.1031 -0.0013 -0.0031 0.0017  142 ALA A N   
1187 C  CA  . ALA A 141 ? 0.1083 0.0603 0.1094 0.0068  0.0068  -0.0071 142 ALA A CA  
1188 C  C   . ALA A 141 ? 0.0799 0.0731 0.0967 0.0065  -0.0044 -0.0114 142 ALA A C   
1189 O  O   . ALA A 141 ? 0.1137 0.0756 0.1022 0.0023  -0.0205 -0.0152 142 ALA A O   
1190 C  CB  . ALA A 141 ? 0.1040 0.0974 0.1169 0.0052  0.0083  0.0006  142 ALA A CB  
1191 N  N   . VAL A 142 ? 0.0909 0.0645 0.0982 0.0026  -0.0049 -0.0083 143 VAL A N   
1192 C  CA  . VAL A 142 ? 0.1010 0.0696 0.0829 0.0019  -0.0136 -0.0068 143 VAL A CA  
1193 C  C   . VAL A 142 ? 0.0920 0.0694 0.0830 -0.0017 0.0012  0.0028  143 VAL A C   
1194 O  O   . VAL A 142 ? 0.1083 0.0766 0.0821 0.0003  -0.0126 -0.0082 143 VAL A O   
1195 C  CB  . VAL A 142 ? 0.0930 0.0916 0.0917 -0.0063 -0.0104 -0.0081 143 VAL A CB  
1196 C  CG1 . VAL A 142 ? 0.1216 0.1026 0.0975 -0.0066 -0.0052 0.0066  143 VAL A CG1 
1197 C  CG2 . VAL A 142 ? 0.1063 0.1321 0.0877 0.0063  -0.0017 -0.0190 143 VAL A CG2 
1198 N  N   . LEU A 143 ? 0.0986 0.0619 0.1096 0.0020  -0.0208 -0.0028 144 LEU A N   
1199 C  CA  . LEU A 143 ? 0.0895 0.0687 0.1115 0.0130  -0.0238 -0.0071 144 LEU A CA  
1200 C  C   . LEU A 143 ? 0.0905 0.0768 0.0984 0.0175  -0.0215 -0.0107 144 LEU A C   
1201 O  O   . LEU A 143 ? 0.1242 0.0797 0.0997 0.0043  -0.0091 -0.0115 144 LEU A O   
1202 C  CB  . LEU A 143 ? 0.1027 0.1019 0.1220 0.0088  -0.0261 -0.0098 144 LEU A CB  
1203 C  CG  . LEU A 143 ? 0.1071 0.0965 0.1677 -0.0031 -0.0164 -0.0032 144 LEU A CG  
1204 C  CD1 . LEU A 143 ? 0.1154 0.1597 0.1721 0.0281  -0.0172 -0.0631 144 LEU A CD1 
1205 C  CD2 . LEU A 143 ? 0.1057 0.1608 0.1791 0.0080  -0.0311 -0.0054 144 LEU A CD2 
1206 N  N   . GLY A 144 ? 0.0869 0.0681 0.0979 0.0035  -0.0076 -0.0054 145 GLY A N   
1207 C  CA  . GLY A 144 ? 0.0960 0.0744 0.1000 0.0049  -0.0017 0.0055  145 GLY A CA  
1208 C  C   . GLY A 144 ? 0.1022 0.0745 0.0878 0.0041  -0.0129 -0.0126 145 GLY A C   
1209 O  O   . GLY A 144 ? 0.0989 0.0830 0.0962 0.0147  -0.0015 -0.0006 145 GLY A O   
1210 N  N   . ILE A 145 ? 0.0992 0.0649 0.0895 -0.0006 -0.0155 -0.0013 146 ILE A N   
1211 C  CA  . ILE A 145 ? 0.0982 0.0641 0.1033 0.0096  -0.0194 -0.0103 146 ILE A CA  
1212 C  C   . ILE A 145 ? 0.1001 0.0684 0.0954 0.0110  -0.0237 -0.0071 146 ILE A C   
1213 O  O   . ILE A 145 ? 0.1127 0.0715 0.1059 0.0089  -0.0137 -0.0066 146 ILE A O   
1214 C  CB  . ILE A 145 ? 0.0982 0.0793 0.1281 -0.0049 -0.0289 -0.0160 146 ILE A CB  
1215 C  CG1 . ILE A 145 ? 0.1298 0.0995 0.1490 -0.0244 -0.0480 0.0000  146 ILE A CG1 
1216 C  CG2 . ILE A 145 ? 0.1191 0.0954 0.1823 0.0201  -0.0623 -0.0007 146 ILE A CG2 
1217 C  CD1 . ILE A 145 ? 0.1096 0.1018 0.1523 0.0040  -0.0575 -0.0074 146 ILE A CD1 
1218 N  N   . PHE A 146 ? 0.0971 0.0619 0.1026 -0.0032 -0.0177 -0.0057 147 PHE A N   
1219 C  CA  . PHE A 146 ? 0.1141 0.0680 0.0956 -0.0026 -0.0148 -0.0021 147 PHE A CA  
1220 C  C   . PHE A 146 ? 0.1075 0.0718 0.1067 0.0185  -0.0162 0.0046  147 PHE A C   
1221 O  O   . PHE A 146 ? 0.1163 0.0877 0.1132 0.0023  -0.0335 0.0044  147 PHE A O   
1222 C  CB  . PHE A 146 ? 0.1106 0.0728 0.1045 0.0104  -0.0181 -0.0141 147 PHE A CB  
1223 C  CG  . PHE A 146 ? 0.0810 0.0737 0.0969 0.0052  -0.0172 -0.0126 147 PHE A CG  
1224 C  CD1 . PHE A 146 ? 0.0918 0.0769 0.1018 -0.0023 -0.0159 -0.0071 147 PHE A CD1 
1225 C  CD2 . PHE A 146 ? 0.1062 0.0696 0.1204 0.0020  -0.0105 -0.0193 147 PHE A CD2 
1226 C  CE1 . PHE A 146 ? 0.1075 0.0803 0.1055 -0.0008 -0.0197 -0.0020 147 PHE A CE1 
1227 C  CE2 . PHE A 146 ? 0.1068 0.0794 0.1250 0.0035  -0.0070 -0.0166 147 PHE A CE2 
1228 C  CZ  . PHE A 146 ? 0.1023 0.0788 0.1024 0.0043  -0.0148 -0.0081 147 PHE A CZ  
1229 N  N   . LEU A 147 ? 0.1155 0.0698 0.1055 0.0135  -0.0175 0.0008  148 LEU A N   
1230 C  CA  . LEU A 147 ? 0.1368 0.0683 0.1045 0.0204  -0.0186 0.0076  148 LEU A CA  
1231 C  C   . LEU A 147 ? 0.1152 0.0734 0.1039 0.0170  -0.0136 -0.0088 148 LEU A C   
1232 O  O   . LEU A 147 ? 0.1189 0.0741 0.1184 0.0023  -0.0126 -0.0057 148 LEU A O   
1233 C  CB  . LEU A 147 ? 0.1400 0.0795 0.1087 0.0203  -0.0171 -0.0057 148 LEU A CB  
1234 C  CG  . LEU A 147 ? 0.1976 0.0685 0.1114 0.0085  -0.0342 0.0037  148 LEU A CG  
1235 C  CD1 . LEU A 147 ? 0.2061 0.0869 0.1032 0.0241  -0.0370 0.0006  148 LEU A CD1 
1236 C  CD2 . LEU A 147 ? 0.1763 0.1039 0.1024 0.0098  -0.0284 -0.0093 148 LEU A CD2 
1237 N  N   . LYS A 148 ? 0.1238 0.0653 0.1256 0.0124  -0.0208 0.0010  149 LYS A N   
1238 C  CA  . LYS A 148 ? 0.1483 0.0649 0.1430 0.0146  -0.0186 -0.0052 149 LYS A CA  
1239 C  C   . LYS A 148 ? 0.1196 0.0803 0.1532 0.0186  -0.0320 -0.0083 149 LYS A C   
1240 O  O   . LYS A 148 ? 0.1712 0.1146 0.1317 -0.0174 -0.0406 0.0144  149 LYS A O   
1241 C  CB  . LYS A 148 ? 0.1723 0.0940 0.1256 0.0264  -0.0271 -0.0162 149 LYS A CB  
1242 C  CG  . LYS A 148 ? 0.1765 0.1344 0.1796 0.0452  -0.0046 -0.0348 149 LYS A CG  
1243 C  CD  . LYS A 148 ? 0.2361 0.2238 0.2230 0.0454  0.0331  -0.0344 149 LYS A CD  
1244 C  CE  . LYS A 148 ? 0.2687 0.3901 0.3682 0.0656  0.0643  -0.0922 149 LYS A CE  
1245 N  NZ  . LYS A 148 ? 0.5764 0.5327 0.4742 0.2372  0.1508  -0.1685 149 LYS A NZ  
1246 N  N   . VAL A 149 ? 0.1645 0.0794 0.1621 -0.0013 -0.0282 0.0099  150 VAL A N   
1247 C  CA  . VAL A 149 ? 0.1668 0.0834 0.1539 0.0040  -0.0174 0.0261  150 VAL A CA  
1248 C  C   . VAL A 149 ? 0.1669 0.0908 0.1468 0.0121  -0.0122 0.0063  150 VAL A C   
1249 O  O   . VAL A 149 ? 0.1747 0.1081 0.1685 0.0181  -0.0370 -0.0127 150 VAL A O   
1250 C  CB  . VAL A 149 ? 0.1606 0.0882 0.1592 0.0144  -0.0283 0.0102  150 VAL A CB  
1251 C  CG1 . VAL A 149 ? 0.1739 0.1407 0.1468 -0.0037 -0.0135 0.0225  150 VAL A CG1 
1252 C  CG2 . VAL A 149 ? 0.1447 0.1296 0.1768 0.0098  -0.0076 0.0043  150 VAL A CG2 
1253 N  N   . GLY A 150 ? 0.1658 0.0932 0.1533 0.0281  -0.0386 0.0017  151 GLY A N   
1254 C  CA  . GLY A 150 ? 0.1736 0.1333 0.1821 0.0570  -0.0480 -0.0364 151 GLY A CA  
1255 C  C   . GLY A 150 ? 0.2067 0.1052 0.1474 0.0375  -0.0507 -0.0052 151 GLY A C   
1256 O  O   . GLY A 150 ? 0.2039 0.1209 0.1728 0.0469  -0.0498 0.0054  151 GLY A O   
1257 N  N   . SER A 151 ? 0.1908 0.1148 0.2085 0.0362  -0.0480 0.0086  152 SER A N   
1258 C  CA  . SER A 151 ? 0.1847 0.1342 0.1951 0.0280  -0.0555 0.0178  152 SER A CA  
1259 C  C   . SER A 151 ? 0.1888 0.1102 0.1562 0.0116  -0.0350 0.0219  152 SER A C   
1260 O  O   . SER A 151 ? 0.1867 0.1190 0.1598 0.0344  -0.0441 0.0055  152 SER A O   
1261 C  CB  . SER A 151 ? 0.1752 0.4580 0.2820 -0.0658 -0.0663 -0.0465 152 SER A CB  
1262 O  OG  . SER A 151 ? 0.3018 0.5281 0.3623 0.1366  -0.0171 -0.0233 152 SER A OG  
1263 N  N   . ALA A 152 ? 0.2153 0.1257 0.1783 0.0130  -0.0753 0.0005  153 ALA A N   
1264 C  CA  . ALA A 152 ? 0.1996 0.1186 0.1293 0.0087  -0.0311 0.0055  153 ALA A CA  
1265 C  C   . ALA A 152 ? 0.1965 0.1333 0.1486 0.0020  -0.0527 0.0247  153 ALA A C   
1266 O  O   . ALA A 152 ? 0.1943 0.1448 0.2039 0.0006  -0.0414 0.0251  153 ALA A O   
1267 C  CB  . ALA A 152 ? 0.2910 0.1643 0.1494 -0.0186 -0.0741 0.0280  153 ALA A CB  
1268 N  N   . LYS A 153 ? 0.2263 0.1128 0.1747 0.0121  -0.0895 0.0040  154 LYS A N   
1269 C  CA  . LYS A 153 ? 0.2221 0.1093 0.1847 -0.0065 -0.0700 -0.0035 154 LYS A CA  
1270 C  C   . LYS A 153 ? 0.2010 0.1361 0.1582 -0.0219 -0.0432 0.0211  154 LYS A C   
1271 O  O   . LYS A 153 ? 0.2116 0.1350 0.1455 -0.0120 -0.0650 0.0226  154 LYS A O   
1272 C  CB  . LYS A 153 ? 0.2353 0.1136 0.1733 0.0121  -0.0795 -0.0077 154 LYS A CB  
1273 C  CG  . LYS A 153 ? 0.3546 0.1002 0.2383 -0.0054 -0.1185 0.0161  154 LYS A CG  
1274 C  CD  . LYS A 153 ? 0.3298 0.1370 0.2311 -0.0156 -0.1032 0.0228  154 LYS A CD  
1275 C  CE  . LYS A 153 ? 0.3303 0.2022 0.1918 -0.0135 -0.0697 0.0187  154 LYS A CE  
1276 N  NZ  . LYS A 153 ? 0.2114 0.2069 0.2779 -0.0012 -0.0294 0.0916  154 LYS A NZ  
1277 N  N   . PRO A 154 ? 0.2243 0.1403 0.1794 0.0043  -0.0838 -0.0005 155 PRO A N   
1278 C  CA  . PRO A 154 ? 0.2217 0.1733 0.1841 0.0137  -0.0948 0.0017  155 PRO A CA  
1279 C  C   . PRO A 154 ? 0.2287 0.1703 0.1692 0.0041  -0.1133 0.0046  155 PRO A C   
1280 O  O   . PRO A 154 ? 0.3160 0.1714 0.1737 0.0052  -0.1105 -0.0162 155 PRO A O   
1281 C  CB  . PRO A 154 ? 0.2090 0.1932 0.2168 -0.0010 -0.0873 -0.0138 155 PRO A CB  
1282 C  CG  . PRO A 154 ? 0.2361 0.2205 0.2745 0.0196  -0.0531 -0.0024 155 PRO A CG  
1283 C  CD  . PRO A 154 ? 0.2354 0.1779 0.2146 -0.0012 -0.0649 -0.0205 155 PRO A CD  
1284 N  N   . GLY A 155 ? 0.2340 0.1290 0.1831 -0.0271 -0.0776 0.0066  156 GLY A N   
1285 C  CA  . GLY A 155 ? 0.2919 0.1266 0.2579 -0.0066 -0.0728 0.0237  156 GLY A CA  
1286 C  C   . GLY A 155 ? 0.3192 0.1036 0.1755 0.0003  -0.0868 -0.0298 156 GLY A C   
1287 O  O   . GLY A 155 ? 0.2960 0.1236 0.2944 -0.0109 -0.0657 -0.0344 156 GLY A O   
1288 N  N   . LEU A 156 ? 0.2018 0.1376 0.1606 0.0015  -0.0461 -0.0008 157 LEU A N   
1289 C  CA  . LEU A 156 ? 0.2509 0.0942 0.1495 0.0062  -0.0568 0.0087  157 LEU A CA  
1290 C  C   . LEU A 156 ? 0.2666 0.1058 0.1395 0.0074  -0.0768 0.0195  157 LEU A C   
1291 O  O   . LEU A 156 ? 0.2477 0.1257 0.1344 0.0217  -0.0538 -0.0017 157 LEU A O   
1292 C  CB  . LEU A 156 ? 0.1972 0.1293 0.1508 0.0273  -0.0684 -0.0096 157 LEU A CB  
1293 C  CG  . LEU A 156 ? 0.2233 0.1317 0.1352 0.0368  -0.0579 -0.0094 157 LEU A CG  
1294 C  CD1 . LEU A 156 ? 0.2542 0.1536 0.1609 0.0564  -0.0738 0.0026  157 LEU A CD1 
1295 C  CD2 . LEU A 156 ? 0.2161 0.1588 0.1386 0.0031  -0.0353 -0.0035 157 LEU A CD2 
1296 N  N   . GLN A 157 ? 0.2533 0.1303 0.1577 0.0135  -0.0885 0.0005  158 GLN A N   
1297 C  CA  . GLN A 157 ? 0.3213 0.1498 0.1243 0.0666  -0.0936 0.0137  158 GLN A CA  
1298 C  C   . GLN A 157 ? 0.2684 0.1388 0.1419 0.0456  -0.0912 -0.0055 158 GLN A C   
1299 O  O   . GLN A 157 ? 0.2515 0.1541 0.1595 0.0266  -0.0750 0.0181  158 GLN A O   
1300 C  CB  . GLN A 157 ? 0.2989 0.1766 0.1630 0.0680  -0.0706 0.0070  158 GLN A CB  
1301 C  CG  . GLN A 157 ? 0.3513 0.1498 0.1700 0.0149  -0.1013 0.0518  158 GLN A CG  
1302 C  CD  . GLN A 157 ? 0.3276 0.1273 0.1527 0.0441  -0.0615 0.0010  158 GLN A CD  
1303 O  OE1 . GLN A 157 ? 0.3605 0.1333 0.1472 0.0234  -0.0759 0.0038  158 GLN A OE1 
1304 N  NE2 . GLN A 157 ? 0.3720 0.1843 0.1498 0.0907  -0.0511 0.0353  158 GLN A NE2 
1305 N  N   . LYS A 158 ? 0.3190 0.1234 0.1480 0.0351  -0.1159 -0.0131 159 LYS A N   
1306 C  CA  . LYS A 158 ? 0.2736 0.1386 0.1475 0.0078  -0.0825 -0.0108 159 LYS A CA  
1307 C  C   . LYS A 158 ? 0.2632 0.1501 0.1295 0.0122  -0.0631 -0.0068 159 LYS A C   
1308 O  O   . LYS A 158 ? 0.2833 0.1506 0.1513 0.0263  -0.0535 0.0046  159 LYS A O   
1309 C  CB  . LYS A 158 ? 0.3361 0.1340 0.2189 -0.0066 -0.1062 -0.0436 159 LYS A CB  
1310 C  CG  . LYS A 158 ? 0.3641 0.2921 0.1647 -0.0148 -0.0851 -0.0390 159 LYS A CG  
1311 C  CD  . LYS A 158 ? 0.3799 0.3585 0.5741 -0.0074 -0.1889 -0.1733 159 LYS A CD  
1312 C  CE  . LYS A 158 ? 0.6161 0.4702 0.3188 -0.0710 -0.1925 0.0108  159 LYS A CE  
1313 N  N   . VAL A 159 ? 0.2874 0.1248 0.1315 0.0006  -0.0813 0.0085  160 VAL A N   
1314 C  CA  . VAL A 159 ? 0.2712 0.1242 0.1159 0.0131  -0.0472 -0.0113 160 VAL A CA  
1315 C  C   . VAL A 159 ? 0.2486 0.1164 0.1705 -0.0055 -0.0653 0.0186  160 VAL A C   
1316 O  O   . VAL A 159 ? 0.2734 0.1298 0.1500 0.0163  -0.0755 0.0013  160 VAL A O   
1317 C  CB  . VAL A 159 ? 0.2709 0.1221 0.1230 0.0131  -0.0577 0.0103  160 VAL A CB  
1318 C  CG1 . VAL A 159 ? 0.3016 0.1536 0.1545 0.0447  -0.0584 -0.0182 160 VAL A CG1 
1319 C  CG2 . VAL A 159 ? 0.3215 0.1574 0.1407 -0.0203 -0.0785 0.0397  160 VAL A CG2 
1320 N  N   . VAL A 160 ? 0.2795 0.0989 0.1288 0.0126  -0.0610 0.0140  161 VAL A N   
1321 C  CA  . VAL A 160 ? 0.2946 0.1171 0.1368 0.0032  -0.0434 0.0082  161 VAL A CA  
1322 C  C   . VAL A 160 ? 0.3055 0.1184 0.1657 0.0164  -0.0342 0.0262  161 VAL A C   
1323 O  O   . VAL A 160 ? 0.3054 0.1380 0.1626 0.0375  -0.0282 0.0060  161 VAL A O   
1324 C  CB  . VAL A 160 ? 0.3650 0.1319 0.1785 0.0006  0.0266  -0.0074 161 VAL A CB  
1325 C  CG1 . VAL A 160 ? 0.3025 0.1621 0.2146 0.0250  -0.0414 0.0271  161 VAL A CG1 
1326 C  CG2 . VAL A 160 ? 0.3183 0.1409 0.1977 0.0277  -0.0408 -0.0081 161 VAL A CG2 
1327 N  N   . ASP A 161 ? 0.3506 0.1324 0.1331 0.0403  -0.0707 0.0160  162 ASP A N   
1328 C  CA  . ASP A 161 ? 0.3702 0.2047 0.1358 0.0646  -0.0649 0.0230  162 ASP A CA  
1329 C  C   . ASP A 161 ? 0.3605 0.2360 0.1297 0.0675  -0.0806 0.0179  162 ASP A C   
1330 O  O   . ASP A 161 ? 0.5073 0.2849 0.1477 0.1272  -0.0241 0.0154  162 ASP A O   
1331 C  CB  . ASP A 161 ? 0.4115 0.2369 0.1582 0.0692  -0.0551 0.0445  162 ASP A CB  
1332 C  CG  . ASP A 161 ? 0.4634 0.1827 0.1595 0.0154  -0.0384 0.0623  162 ASP A CG  
1333 O  OD1 . ASP A 161 ? 0.4237 0.2734 0.1889 0.0890  -0.0432 0.0395  162 ASP A OD1 
1334 O  OD2 . ASP A 161 ? 0.4560 0.3829 0.2358 0.0370  -0.0987 0.0272  162 ASP A OD2 
1335 N  N   . VAL A 162 ? 0.3652 0.1526 0.1281 0.0639  -0.0775 -0.0184 163 VAL A N   
1336 C  CA  . VAL A 162 ? 0.3368 0.2117 0.1375 0.0631  -0.0489 -0.0153 163 VAL A CA  
1337 C  C   . VAL A 162 ? 0.3522 0.1418 0.1209 0.0640  -0.0230 -0.0223 163 VAL A C   
1338 O  O   . VAL A 162 ? 0.3731 0.1667 0.1238 0.0410  -0.0320 -0.0008 163 VAL A O   
1339 C  CB  . VAL A 162 ? 0.3831 0.1609 0.2006 0.0133  -0.0794 -0.0146 163 VAL A CB  
1340 C  CG1 . VAL A 162 ? 0.4007 0.1448 0.1720 0.0189  -0.0639 -0.0156 163 VAL A CG1 
1341 C  CG2 . VAL A 162 ? 0.3113 0.2045 0.1816 0.0138  -0.0199 -0.0188 163 VAL A CG2 
1342 N  N   . LEU A 163 ? 0.2985 0.1717 0.1432 0.0540  -0.0608 -0.0197 164 LEU A N   
1343 C  CA  . LEU A 163 ? 0.3111 0.1332 0.1098 0.0434  0.0119  -0.0146 164 LEU A CA  
1344 C  C   . LEU A 163 ? 0.3425 0.1362 0.1411 0.0311  0.0024  0.0083  164 LEU A C   
1345 O  O   . LEU A 163 ? 0.3303 0.1694 0.1128 0.0076  0.0157  -0.0142 164 LEU A O   
1346 C  CB  . LEU A 163 ? 0.3355 0.1446 0.1023 0.0288  -0.0219 0.0086  164 LEU A CB  
1347 C  CG  . LEU A 163 ? 0.3253 0.1307 0.1282 0.0221  -0.0342 -0.0130 164 LEU A CG  
1348 C  CD1 . LEU A 163 ? 0.2982 0.1403 0.1439 0.0256  -0.0381 -0.0186 164 LEU A CD1 
1349 C  CD2 . LEU A 163 ? 0.3152 0.1357 0.1227 0.0133  -0.0296 0.0071  164 LEU A CD2 
1350 N  N   . ASP A 164 ? 0.4731 0.1596 0.1098 0.0417  -0.0160 0.0307  165 ASP A N   
1351 C  CA  . ASP A 164 ? 0.5213 0.1770 0.1601 0.0297  -0.0024 0.0379  165 ASP A CA  
1352 C  C   . ASP A 164 ? 0.3652 0.2723 0.1236 -0.0214 0.0212  -0.0289 165 ASP A C   
1353 O  O   . ASP A 164 ? 0.4108 0.2662 0.2433 -0.0110 0.0715  0.0124  165 ASP A O   
1354 C  CB  . ASP A 164 ? 0.9031 0.4411 0.5166 0.0621  -0.2551 0.2379  165 ASP A CB  
1355 C  CG  . ASP A 164 ? 0.7055 0.5116 0.5541 0.2300  -0.2122 0.1851  165 ASP A CG  
1356 O  OD1 . ASP A 164 ? 0.7472 1.1311 0.2203 0.1542  0.0790  -0.0377 165 ASP A OD1 
1357 O  OD2 . ASP A 164 ? 0.8185 1.4232 0.5922 0.3853  0.1959  0.5533  165 ASP A OD2 
1358 N  N   . SER A 165 ? 0.3959 0.2062 0.1322 0.0184  -0.0427 -0.0263 166 SER A N   
1359 C  CA  . SER A 165 ? 0.3169 0.2379 0.1160 0.0287  -0.0055 -0.0003 166 SER A CA  
1360 C  C   . SER A 165 ? 0.3330 0.2022 0.0949 0.0366  0.0041  -0.0164 166 SER A C   
1361 O  O   . SER A 165 ? 0.4196 0.1990 0.1321 0.0487  -0.0423 -0.0590 166 SER A O   
1362 C  CB  . SER A 165 ? 0.4402 0.2120 0.1955 0.0057  0.0071  -0.0225 166 SER A CB  
1363 O  OG  . SER A 165 ? 0.5333 0.2083 0.1757 0.0000  -0.0094 -0.0494 166 SER A OG  
1364 N  N   . ILE A 166 ? 0.3064 0.1667 0.1101 0.0293  -0.0115 -0.0041 167 ILE A N   
1365 C  CA  . ILE A 166 ? 0.2513 0.1341 0.1492 0.0181  0.0071  -0.0359 167 ILE A CA  
1366 C  C   . ILE A 166 ? 0.2547 0.1719 0.1096 0.0230  -0.0114 0.0175  167 ILE A C   
1367 O  O   . ILE A 166 ? 0.2477 0.1440 0.1014 0.0108  0.0003  -0.0068 167 ILE A O   
1368 C  CB  . ILE A 166 ? 0.2879 0.1392 0.1171 0.0238  -0.0063 -0.0166 167 ILE A CB  
1369 C  CG1 . ILE A 166 ? 0.2624 0.1722 0.1067 0.0328  0.0005  0.0092  167 ILE A CG1 
1370 C  CG2 . ILE A 166 ? 0.3343 0.1629 0.1777 -0.0003 -0.0368 -0.0313 167 ILE A CG2 
1371 C  CD1 . ILE A 166 ? 0.3386 0.1645 0.1148 0.0333  0.0141  0.0252  167 ILE A CD1 
1372 N  N   . LYS A 167 ? 0.2597 0.1369 0.1298 0.0046  -0.0183 -0.0170 168 LYS A N   
1373 C  CA  . LYS A 167 ? 0.1993 0.1844 0.1222 0.0049  0.0046  0.0174  168 LYS A CA  
1374 C  C   . LYS A 167 ? 0.1916 0.1630 0.1121 -0.0077 0.0239  -0.0335 168 LYS A C   
1375 O  O   . LYS A 167 ? 0.2623 0.1474 0.1127 0.0342  0.0019  0.0051  168 LYS A O   
1376 C  CB  . LYS A 167 ? 0.2685 0.1532 0.1448 0.0135  -0.0132 0.0170  168 LYS A CB  
1377 C  CG  . LYS A 167 ? 0.2418 0.2076 0.1851 -0.0063 0.0292  0.0350  168 LYS A CG  
1378 C  CD  . LYS A 167 ? 0.3817 0.2029 0.2680 -0.0055 -0.0160 0.1071  168 LYS A CD  
1379 C  CE  . LYS A 167 ? 0.3815 0.2980 0.2725 0.0167  0.0728  0.0277  168 LYS A CE  
1380 N  NZ  . LYS A 167 ? 0.5949 0.3190 0.3517 0.0776  0.0000  0.1354  168 LYS A NZ  
1381 N  N   . THR A 168 ? 0.1948 0.1609 0.1321 0.0052  0.0071  -0.0219 169 THR A N   
1382 C  CA  . THR A 168 ? 0.1992 0.1728 0.1066 -0.0038 0.0375  -0.0326 169 THR A CA  
1383 C  C   . THR A 168 ? 0.1377 0.1861 0.1059 -0.0195 0.0193  -0.0088 169 THR A C   
1384 O  O   . THR A 168 ? 0.2372 0.1450 0.1516 0.0065  0.0284  -0.0266 169 THR A O   
1385 C  CB  . THR A 168 ? 0.2231 0.1831 0.1383 0.0175  0.0282  -0.0108 169 THR A CB  
1386 O  OG1 . THR A 168 ? 0.2881 0.2040 0.1339 0.0157  0.0425  -0.0284 169 THR A OG1 
1387 C  CG2 . THR A 168 ? 0.2418 0.1825 0.1647 -0.0120 0.0526  -0.0148 169 THR A CG2 
1388 N  N   . LYS A 169 ? 0.2204 0.1782 0.1565 0.0553  0.0562  -0.0156 170 LYS A N   
1389 C  CA  . LYS A 169 ? 0.1876 0.1527 0.1665 0.0121  0.0127  -0.0188 170 LYS A CA  
1390 C  C   . LYS A 169 ? 0.2123 0.2155 0.1644 -0.0120 0.0310  -0.0971 170 LYS A C   
1391 O  O   . LYS A 169 ? 0.2944 0.2046 0.1431 0.0434  0.0375  -0.0284 170 LYS A O   
1392 C  CB  . LYS A 169 ? 0.1858 0.1457 0.1476 -0.0066 0.0447  -0.0164 170 LYS A CB  
1393 C  CG  . LYS A 169 ? 0.2408 0.1814 0.1882 0.0122  0.0144  -0.0339 170 LYS A CG  
1394 C  CD  . LYS A 169 ? 0.2240 0.1958 0.2461 0.0040  0.0445  -0.0645 170 LYS A CD  
1395 C  CE  . LYS A 169 ? 0.2107 0.3993 0.3095 0.0023  0.0318  -0.0175 170 LYS A CE  
1396 N  NZ  . LYS A 169 ? 0.2775 0.6452 0.3163 -0.0054 -0.0108 -0.0606 170 LYS A NZ  
1397 N  N   . GLY A 170 ? 0.2646 0.1307 0.1872 0.0372  0.0089  -0.0099 171 GLY A N   
1398 C  CA  . GLY A 170 ? 0.2267 0.1404 0.2436 0.0275  0.0012  -0.0749 171 GLY A CA  
1399 C  C   . GLY A 170 ? 0.2567 0.1490 0.2011 0.0098  0.0111  -0.0750 171 GLY A C   
1400 O  O   . GLY A 170 ? 0.3714 0.1600 0.2802 0.0540  -0.0046 -0.0979 171 GLY A O   
1401 N  N   . LYS A 171 ? 0.2032 0.1385 0.2046 0.0074  0.0406  -0.0690 172 LYS A N   
1402 C  CA  . LYS A 171 ? 0.2017 0.1316 0.2328 0.0122  -0.0017 -0.0615 172 LYS A CA  
1403 C  C   . LYS A 171 ? 0.2186 0.1724 0.1306 -0.0307 0.0172  -0.0081 172 LYS A C   
1404 O  O   . LYS A 171 ? 0.2411 0.1708 0.1085 0.0060  0.0149  -0.0348 172 LYS A O   
1405 C  CB  . LYS A 171 ? 0.3400 0.1808 0.0954 0.0406  0.0307  -0.0263 172 LYS A CB  
1406 C  CG  . LYS A 171 ? 0.3048 0.2269 0.1897 0.0507  0.0388  0.0000  172 LYS A CG  
1407 C  CD  . LYS A 171 ? 0.5436 0.2447 0.2379 -0.0185 -0.0666 0.0026  172 LYS A CD  
1408 C  CE  . LYS A 171 ? 0.9401 0.4178 0.2106 0.0059  -0.1422 0.0441  172 LYS A CE  
1409 N  NZ  . LYS A 171 ? 0.8190 0.2784 0.2216 0.0159  0.1032  -0.0043 172 LYS A NZ  
1410 N  N   . SER A 172 ? 0.2020 0.1697 0.1771 -0.0024 -0.0175 -0.0925 173 SER A N   
1411 C  CA  . SER A 172 ? 0.2029 0.1916 0.1891 -0.0251 0.0038  -0.0313 173 SER A CA  
1412 C  C   . SER A 172 ? 0.2118 0.1696 0.1521 -0.0500 -0.0248 -0.0511 173 SER A C   
1413 O  O   . SER A 172 ? 0.4419 0.2430 0.0851 -0.0575 -0.0230 -0.0373 173 SER A O   
1414 C  CB  . SER A 172 ? 0.3492 0.1802 0.1535 -0.0034 0.0425  -0.0296 173 SER A CB  
1415 O  OG  . SER A 172 ? 0.5504 0.1764 0.2266 -0.0373 0.0989  -0.0904 173 SER A OG  
1416 N  N   . ALA A 173 ? 0.2451 0.2251 0.1728 -0.0820 -0.0259 -0.0086 174 ALA A N   
1417 C  CA  . ALA A 173 ? 0.2339 0.3080 0.1607 -0.0522 -0.0305 -0.0940 174 ALA A CA  
1418 C  C   . ALA A 173 ? 0.1195 0.2192 0.1572 -0.0077 -0.0074 -0.0533 174 ALA A C   
1419 O  O   . ALA A 173 ? 0.3037 0.1967 0.0970 -0.0386 -0.0108 -0.0348 174 ALA A O   
1420 C  CB  . ALA A 173 ? 0.4503 0.2822 0.1395 -0.0742 -0.0476 -0.0335 174 ALA A CB  
1421 N  N   . ASP A 174 ? 0.2897 0.2960 0.1406 -0.0538 -0.0142 -0.0874 175 ASP A N   
1422 C  CA  . ASP A 174 ? 0.3215 0.2400 0.1717 -0.0741 -0.0003 -0.0701 175 ASP A CA  
1423 C  C   . ASP A 174 ? 0.2469 0.2155 0.1380 -0.0344 -0.0555 0.0153  175 ASP A C   
1424 O  O   . ASP A 174 ? 0.3725 0.2405 0.1616 -0.0434 -0.0037 0.0372  175 ASP A O   
1425 C  CB  . ASP A 174 ? 0.2700 0.3434 0.2872 -0.0344 -0.0604 -0.1040 175 ASP A CB  
1426 C  CG  . ASP A 174 ? 0.5414 0.4316 0.1952 0.0625  -0.1238 -0.1295 175 ASP A CG  
1427 O  OD1 . ASP A 174 ? 0.7132 0.5674 0.2556 0.1180  -0.1829 -0.0590 175 ASP A OD1 
1428 O  OD2 . ASP A 174 ? 0.5381 0.5426 0.1995 0.0983  0.0008  -0.0586 175 ASP A OD2 
1429 N  N   . PHE A 175 ? 0.3133 0.1792 0.1145 -0.0189 -0.0155 -0.0055 176 PHE A N   
1430 C  CA  . PHE A 175 ? 0.2196 0.2160 0.1597 -0.0311 -0.0299 -0.0553 176 PHE A CA  
1431 C  C   . PHE A 175 ? 0.2585 0.1230 0.1872 -0.0230 -0.0568 0.0012  176 PHE A C   
1432 O  O   . PHE A 175 ? 0.3567 0.2187 0.1339 -0.0498 -0.0878 0.0113  176 PHE A O   
1433 C  CB  . PHE A 175 ? 0.3790 0.1497 0.1449 -0.0130 -0.0549 -0.0377 176 PHE A CB  
1434 C  CG  . PHE A 175 ? 0.3016 0.1535 0.1598 -0.0373 -0.0542 0.0000  176 PHE A CG  
1435 C  CD1 . PHE A 175 ? 0.4559 0.1103 0.2216 -0.0483 -0.0480 0.0229  176 PHE A CD1 
1436 C  CD2 . PHE A 175 ? 0.3725 0.1447 0.1502 -0.0303 -0.0965 -0.0207 176 PHE A CD2 
1437 C  CE1 . PHE A 175 ? 0.5088 0.1333 0.1642 -0.0386 -0.0595 0.0211  176 PHE A CE1 
1438 C  CE2 . PHE A 175 ? 0.3251 0.1466 0.1808 -0.0232 -0.0979 -0.0186 176 PHE A CE2 
1439 C  CZ  . PHE A 175 ? 0.3556 0.1287 0.1944 -0.0142 -0.0794 0.0104  176 PHE A CZ  
1440 N  N   . THR A 176 ? 0.3380 0.2021 0.1160 -0.0348 -0.0816 -0.0379 177 THR A N   
1441 C  CA  . THR A 176 ? 0.2389 0.1622 0.1481 -0.0520 -0.0324 -0.0331 177 THR A CA  
1442 C  C   . THR A 176 ? 0.2524 0.1368 0.1495 -0.0013 -0.0671 -0.0509 177 THR A C   
1443 O  O   . THR A 176 ? 0.3668 0.1332 0.1407 0.0120  -0.0917 -0.0299 177 THR A O   
1444 C  CB  . THR A 176 ? 0.3398 0.1661 0.1858 -0.0203 -0.0834 -0.0571 177 THR A CB  
1445 O  OG1 . THR A 176 ? 0.5816 0.2011 0.1386 -0.0909 -0.1240 -0.0240 177 THR A OG1 
1446 C  CG2 . THR A 176 ? 0.4110 0.2504 0.3312 0.0173  -0.0397 -0.1914 177 THR A CG2 
1447 N  N   . ASN A 177 ? 0.3300 0.1562 0.1130 -0.0242 -0.0882 -0.0201 178 ASN A N   
1448 C  CA  . ASN A 177 ? 0.2967 0.1499 0.1546 0.0111  -0.0727 -0.0328 178 ASN A CA  
1449 C  C   . ASN A 177 ? 0.3179 0.1508 0.1569 0.0176  -0.1032 -0.0293 178 ASN A C   
1450 O  O   . ASN A 177 ? 0.4072 0.1937 0.2975 0.0509  -0.1655 -0.1263 178 ASN A O   
1451 C  CB  . ASN A 177 ? 0.3163 0.1465 0.2085 -0.0160 -0.1180 -0.0456 178 ASN A CB  
1452 C  CG  . ASN A 177 ? 0.3892 0.1348 0.1756 -0.0340 -0.1137 -0.0054 178 ASN A CG  
1453 O  OD1 . ASN A 177 ? 0.3837 0.1570 0.2430 -0.0450 -0.0623 -0.0553 178 ASN A OD1 
1454 N  ND2 . ASN A 177 ? 0.3792 0.1650 0.1592 -0.0113 -0.1026 -0.0489 178 ASN A ND2 
1455 N  N   . PHE A 178 ? 0.3169 0.1256 0.1121 -0.0160 -0.0766 -0.0171 179 PHE A N   
1456 C  CA  . PHE A 178 ? 0.3170 0.1378 0.1298 -0.0020 -0.0776 -0.0310 179 PHE A CA  
1457 C  C   . PHE A 178 ? 0.3163 0.1018 0.1451 0.0027  -0.0961 -0.0307 179 PHE A C   
1458 O  O   . PHE A 178 ? 0.3147 0.1342 0.1261 0.0154  -0.0683 -0.0264 179 PHE A O   
1459 C  CB  . PHE A 178 ? 0.3005 0.1318 0.1236 0.0149  -0.0408 -0.0218 179 PHE A CB  
1460 C  CG  . PHE A 178 ? 0.3237 0.1125 0.1450 -0.0052 -0.0666 -0.0318 179 PHE A CG  
1461 C  CD1 . PHE A 178 ? 0.3528 0.1239 0.1342 -0.0159 -0.0527 -0.0248 179 PHE A CD1 
1462 C  CD2 . PHE A 178 ? 0.1960 0.1411 0.1330 -0.0060 -0.0428 -0.0326 179 PHE A CD2 
1463 C  CE1 . PHE A 178 ? 0.3452 0.1279 0.1609 0.0000  -0.0665 -0.0250 179 PHE A CE1 
1464 C  CE2 . PHE A 178 ? 0.2240 0.1268 0.1369 0.0003  -0.0375 -0.0322 179 PHE A CE2 
1465 C  CZ  . PHE A 178 ? 0.2879 0.1164 0.1556 -0.0040 -0.0504 -0.0263 179 PHE A CZ  
1466 N  N   . ASP A 179 ? 0.2734 0.1236 0.1770 -0.0186 -0.1107 -0.0322 180 ASP A N   
1467 C  CA  . ASP A 179 ? 0.2369 0.1586 0.1802 -0.0280 -0.1077 -0.0097 180 ASP A CA  
1468 C  C   . ASP A 179 ? 0.2398 0.1341 0.1253 0.0152  -0.0529 -0.0233 180 ASP A C   
1469 O  O   . ASP A 179 ? 0.2312 0.1299 0.1448 0.0164  -0.0670 -0.0185 180 ASP A O   
1470 C  CB  . ASP A 179 ? 0.2524 0.2170 0.2251 -0.0274 -0.1314 -0.0194 180 ASP A CB  
1471 C  CG  . ASP A 179 ? 0.2529 0.1837 0.2569 -0.0412 -0.1181 -0.0320 180 ASP A CG  
1472 O  OD1 . ASP A 179 ? 0.2434 0.1599 0.2249 -0.0241 -0.0913 -0.0480 180 ASP A OD1 
1473 O  OD2 . ASP A 179 ? 0.2344 0.4810 0.3668 -0.0103 -0.1439 -0.0463 180 ASP A OD2 
1474 N  N   . PRO A 180 ? 0.2002 0.1114 0.1381 0.0083  -0.0573 -0.0210 181 PRO A N   
1475 C  CA  . PRO A 180 ? 0.1542 0.1216 0.1363 -0.0071 -0.0505 -0.0223 181 PRO A CA  
1476 C  C   . PRO A 180 ? 0.1555 0.1164 0.1396 -0.0091 -0.0417 -0.0206 181 PRO A C   
1477 O  O   . PRO A 180 ? 0.1788 0.1306 0.1422 0.0041  -0.0452 -0.0307 181 PRO A O   
1478 C  CB  . PRO A 180 ? 0.1665 0.1552 0.1676 0.0136  -0.0657 -0.0274 181 PRO A CB  
1479 C  CG  . PRO A 180 ? 0.2234 0.1493 0.1560 0.0080  -0.0790 -0.0258 181 PRO A CG  
1480 C  CD  . PRO A 180 ? 0.2188 0.1277 0.1597 0.0105  -0.0825 -0.0179 181 PRO A CD  
1481 N  N   . ARG A 181 ? 0.1539 0.1477 0.1527 -0.0088 -0.0454 -0.0261 182 ARG A N   
1482 C  CA  . ARG A 181 ? 0.1475 0.1427 0.1686 0.0250  -0.0361 -0.0248 182 ARG A CA  
1483 C  C   . ARG A 181 ? 0.1649 0.1431 0.1984 0.0006  -0.0988 -0.0120 182 ARG A C   
1484 O  O   . ARG A 181 ? 0.1983 0.1372 0.2187 0.0221  -0.0750 -0.0414 182 ARG A O   
1485 C  CB  . ARG A 181 ? 0.1577 0.1508 0.2083 0.0066  -0.0357 -0.0399 182 ARG A CB  
1486 C  CG  . ARG A 181 ? 0.1761 0.1578 0.1944 0.0116  -0.0278 -0.0185 182 ARG A CG  
1487 C  CD  . ARG A 181 ? 0.1909 0.2256 0.2450 -0.0154 0.0020  -0.0386 182 ARG A CD  
1488 N  NE  . ARG A 181 ? 0.1653 0.2320 0.3005 0.0263  -0.0485 -0.0998 182 ARG A NE  
1489 C  CZ  . ARG A 181 ? 0.1675 0.3043 0.3436 -0.0297 0.0322  -0.1444 182 ARG A CZ  
1490 N  NH1 . ARG A 181 ? 0.2045 0.3786 0.4187 -0.0635 0.0590  -0.1289 182 ARG A NH1 
1491 N  NH2 . ARG A 181 ? 0.2256 0.2975 0.3750 -0.0026 -0.0399 -0.1491 182 ARG A NH2 
1492 N  N   . GLY A 182 ? 0.1916 0.1464 0.1912 -0.0024 -0.1121 -0.0044 183 GLY A N   
1493 C  CA  . GLY A 182 ? 0.2313 0.1298 0.2162 0.0167  -0.0948 -0.0098 183 GLY A CA  
1494 C  C   . GLY A 182 ? 0.2138 0.1305 0.2006 0.0082  -0.0829 -0.0403 183 GLY A C   
1495 O  O   . GLY A 182 ? 0.2657 0.1303 0.2387 0.0024  -0.1102 -0.0118 183 GLY A O   
1496 N  N   . LEU A 183 ? 0.2375 0.1182 0.1536 -0.0041 -0.0931 -0.0068 184 LEU A N   
1497 C  CA  . LEU A 183 ? 0.2171 0.0908 0.1740 -0.0046 -0.0681 -0.0080 184 LEU A CA  
1498 C  C   . LEU A 183 ? 0.2073 0.1107 0.1471 0.0189  -0.0873 -0.0222 184 LEU A C   
1499 O  O   . LEU A 183 ? 0.2177 0.1490 0.1696 -0.0109 -0.0794 -0.0239 184 LEU A O   
1500 C  CB  . LEU A 183 ? 0.2146 0.1396 0.1357 -0.0432 -0.0430 -0.0143 184 LEU A CB  
1501 C  CG  . LEU A 183 ? 0.2522 0.1611 0.1193 -0.0362 -0.0588 0.0041  184 LEU A CG  
1502 C  CD1 . LEU A 183 ? 0.2380 0.2300 0.1582 -0.0666 -0.0595 -0.0524 184 LEU A CD1 
1503 C  CD2 . LEU A 183 ? 0.2888 0.1775 0.1539 -0.0555 -0.0326 0.0208  184 LEU A CD2 
1504 N  N   . LEU A 184 ? 0.2169 0.1268 0.1833 -0.0118 -0.0650 -0.0237 185 LEU A N   
1505 C  CA  . LEU A 184 ? 0.1656 0.1309 0.1846 0.0335  -0.0650 -0.0401 185 LEU A CA  
1506 C  C   . LEU A 184 ? 0.1996 0.1743 0.2251 0.0771  -0.0996 -0.0711 185 LEU A C   
1507 O  O   . LEU A 184 ? 1.4458 1.5139 0.4577 0.9779  -0.4704 -0.4532 185 LEU A O   
1508 C  CB  . LEU A 184 ? 0.1207 0.1623 0.1740 0.0310  -0.0362 -0.0361 185 LEU A CB  
1509 C  CG  . LEU A 184 ? 0.0885 0.1527 0.1670 -0.0007 -0.0200 -0.0230 185 LEU A CG  
1510 C  CD1 . LEU A 184 ? 0.1606 0.1899 0.1807 -0.0392 -0.0251 -0.0073 185 LEU A CD1 
1511 C  CD2 . LEU A 184 ? 0.1040 0.1554 0.2198 0.0113  -0.0288 -0.0388 185 LEU A CD2 
1512 N  N   . PRO A 185 ? 0.1376 0.1359 0.2060 0.0299  -0.0709 -0.0419 186 PRO A N   
1513 C  CA  . PRO A 185 ? 0.1676 0.1362 0.1975 0.0245  -0.0705 -0.0476 186 PRO A CA  
1514 C  C   . PRO A 185 ? 0.1111 0.1337 0.2429 0.0190  -0.0781 -0.0491 186 PRO A C   
1515 O  O   . PRO A 185 ? 0.0868 0.1398 0.3970 0.0133  -0.0777 -0.0821 186 PRO A O   
1516 C  CB  . PRO A 185 ? 0.1449 0.1200 0.1825 -0.0040 -0.0272 -0.0304 186 PRO A CB  
1517 C  CG  . PRO A 185 ? 0.1014 0.1439 0.1414 -0.0121 -0.0265 -0.0089 186 PRO A CG  
1518 C  CD  . PRO A 185 ? 0.1274 0.1324 0.1288 -0.0100 -0.0476 -0.0135 186 PRO A CD  
1519 N  N   A GLU A 186 ? 0.1502 0.1502 0.2153 0.0548  -0.0892 0.0086  187 GLU A N   
1520 N  N   B GLU A 186 ? 0.1738 0.1005 0.1807 0.0006  -0.0403 -0.0408 187 GLU A N   
1521 C  CA  A GLU A 186 ? 0.1220 0.1606 0.2181 0.0232  -0.0895 -0.0212 187 GLU A CA  
1522 C  CA  B GLU A 186 ? 0.1306 0.1292 0.2132 0.0154  0.0060  -0.0284 187 GLU A CA  
1523 C  C   A GLU A 186 ? 0.0661 0.1695 0.2366 -0.0151 -0.0129 -0.0141 187 GLU A C   
1524 C  C   B GLU A 186 ? 0.0832 0.1229 0.2301 0.0000  -0.0003 -0.0315 187 GLU A C   
1525 O  O   A GLU A 186 ? 0.0980 0.1852 0.1799 -0.0379 -0.0242 0.0102  187 GLU A O   
1526 O  O   B GLU A 186 ? 0.1468 0.1781 0.1808 -0.0439 0.0085  -0.0080 187 GLU A O   
1527 C  CB  A GLU A 186 ? 0.0874 0.1696 0.1902 0.0219  -0.0375 0.0104  187 GLU A CB  
1528 C  CB  B GLU A 186 ? 0.0929 0.1758 0.2163 0.0489  0.0260  0.0024  187 GLU A CB  
1529 C  CG  A GLU A 186 ? 0.1225 0.1712 0.2380 0.0300  -0.0141 0.0120  187 GLU A CG  
1530 C  CG  B GLU A 186 ? 0.1694 0.1608 0.2287 0.0507  -0.0760 -0.0564 187 GLU A CG  
1531 C  CD  A GLU A 186 ? 0.1423 0.1845 0.2567 0.0232  -0.0377 -0.0375 187 GLU A CD  
1532 C  CD  B GLU A 186 ? 0.1870 0.1941 0.3337 0.1118  -0.0644 -0.0221 187 GLU A CD  
1533 O  OE1 A GLU A 186 ? 0.1983 0.1898 0.3037 0.0608  -0.0040 0.0037  187 GLU A OE1 
1534 O  OE1 B GLU A 186 ? 0.2743 0.1674 0.2824 0.0856  0.0480  0.0272  187 GLU A OE1 
1535 O  OE2 A GLU A 186 ? 0.2455 0.2407 0.3140 -0.0283 0.0245  -0.1155 187 GLU A OE2 
1536 O  OE2 B GLU A 186 ? 0.2948 0.1974 0.3003 0.0511  -0.0745 0.0129  187 GLU A OE2 
1537 N  N   . SER A 187 ? 0.0882 0.1504 0.2565 0.0173  -0.0329 -0.0337 188 SER A N   
1538 C  CA  . SER A 187 ? 0.0829 0.1515 0.3129 0.0230  -0.0375 -0.0480 188 SER A CA  
1539 C  C   . SER A 187 ? 0.0776 0.1578 0.2380 0.0125  -0.0130 -0.0381 188 SER A C   
1540 O  O   . SER A 187 ? 0.1010 0.1924 0.2249 0.0254  0.0010  0.0038  188 SER A O   
1541 C  CB  . SER A 187 ? 0.1394 0.1958 0.2418 0.0295  -0.0280 -0.0454 188 SER A CB  
1542 O  OG  . SER A 187 ? 0.1133 0.2101 0.2707 0.0264  -0.0093 -0.0505 188 SER A OG  
1543 N  N   . LEU A 188 ? 0.0995 0.1429 0.2423 0.0142  -0.0192 -0.0118 189 LEU A N   
1544 C  CA  . LEU A 188 ? 0.0916 0.1484 0.2371 -0.0024 -0.0063 -0.0140 189 LEU A CA  
1545 C  C   . LEU A 188 ? 0.0930 0.1430 0.2010 0.0060  0.0184  0.0109  189 LEU A C   
1546 O  O   . LEU A 188 ? 0.1238 0.1653 0.2299 0.0078  -0.0017 0.0296  189 LEU A O   
1547 C  CB  . LEU A 188 ? 0.1114 0.1942 0.2632 0.0242  -0.0175 -0.0304 189 LEU A CB  
1548 C  CG  . LEU A 188 ? 0.1106 0.2082 0.3199 -0.0063 -0.0131 -0.0885 189 LEU A CG  
1549 C  CD1 . LEU A 188 ? 0.1536 0.1849 0.3373 0.0019  -0.0247 -0.0706 189 LEU A CD1 
1550 C  CD2 . LEU A 188 ? 0.1130 0.3370 0.2578 0.0249  -0.0408 -0.0776 189 LEU A CD2 
1551 N  N   . ASP A 189 ? 0.0693 0.1673 0.1986 0.0043  0.0046  0.0118  190 ASP A N   
1552 C  CA  . ASP A 189 ? 0.0910 0.1735 0.1911 0.0135  0.0245  0.0055  190 ASP A CA  
1553 C  C   . ASP A 189 ? 0.0954 0.1289 0.1441 0.0178  0.0087  -0.0046 190 ASP A C   
1554 O  O   . ASP A 189 ? 0.0939 0.1354 0.1520 0.0057  0.0049  0.0007  190 ASP A O   
1555 C  CB  . ASP A 189 ? 0.1128 0.2382 0.2251 0.0785  0.0220  -0.0588 190 ASP A CB  
1556 C  CG  . ASP A 189 ? 0.1623 0.3310 0.2002 0.0683  0.0377  0.0094  190 ASP A CG  
1557 O  OD1 . ASP A 189 ? 0.1424 0.5024 0.2712 0.0562  0.0632  0.0551  190 ASP A OD1 
1558 O  OD2 . ASP A 189 ? 0.2230 0.4643 0.2845 0.1718  0.0049  -0.0658 190 ASP A OD2 
1559 N  N   . TYR A 190 ? 0.0834 0.1451 0.1286 0.0100  0.0156  -0.0132 191 TYR A N   
1560 C  CA  . TYR A 190 ? 0.0807 0.1342 0.1251 0.0110  0.0000  -0.0086 191 TYR A CA  
1561 C  C   . TYR A 190 ? 0.0833 0.1096 0.1220 0.0159  0.0135  -0.0086 191 TYR A C   
1562 O  O   . TYR A 190 ? 0.1074 0.1351 0.1110 0.0041  0.0282  -0.0021 191 TYR A O   
1563 C  CB  . TYR A 190 ? 0.1334 0.1202 0.1128 0.0116  0.0027  -0.0057 191 TYR A CB  
1564 C  CG  . TYR A 190 ? 0.1181 0.1208 0.1166 0.0168  0.0038  -0.0142 191 TYR A CG  
1565 C  CD1 . TYR A 190 ? 0.1018 0.1328 0.1375 0.0162  0.0104  -0.0237 191 TYR A CD1 
1566 C  CD2 . TYR A 190 ? 0.1213 0.1333 0.1238 0.0031  0.0239  -0.0083 191 TYR A CD2 
1567 C  CE1 . TYR A 190 ? 0.1379 0.1250 0.1358 0.0074  0.0013  -0.0125 191 TYR A CE1 
1568 C  CE2 . TYR A 190 ? 0.1209 0.1486 0.1597 0.0077  0.0083  0.0000  191 TYR A CE2 
1569 C  CZ  . TYR A 190 ? 0.1288 0.1318 0.1455 -0.0086 0.0116  -0.0017 191 TYR A CZ  
1570 O  OH  . TYR A 190 ? 0.1573 0.1483 0.1652 -0.0291 -0.0006 0.0184  191 TYR A OH  
1571 N  N   . TRP A 191 ? 0.0865 0.0930 0.1151 0.0071  0.0026  -0.0038 192 TRP A N   
1572 C  CA  . TRP A 191 ? 0.0864 0.1005 0.1004 0.0019  0.0199  -0.0077 192 TRP A CA  
1573 C  C   . TRP A 191 ? 0.0982 0.1027 0.0788 -0.0015 0.0148  -0.0003 192 TRP A C   
1574 O  O   . TRP A 191 ? 0.1209 0.1102 0.0847 0.0227  0.0122  -0.0028 192 TRP A O   
1575 C  CB  . TRP A 191 ? 0.0995 0.1053 0.1130 0.0024  0.0104  -0.0052 192 TRP A CB  
1576 C  CG  . TRP A 191 ? 0.1177 0.1054 0.1074 -0.0068 0.0070  -0.0197 192 TRP A CG  
1577 C  CD1 . TRP A 191 ? 0.1465 0.1036 0.1168 -0.0100 0.0230  -0.0136 192 TRP A CD1 
1578 C  CD2 . TRP A 191 ? 0.0825 0.0980 0.1466 -0.0028 0.0000  -0.0063 192 TRP A CD2 
1579 N  NE1 . TRP A 191 ? 0.1645 0.1049 0.1415 -0.0080 0.0125  -0.0315 192 TRP A NE1 
1580 C  CE2 . TRP A 191 ? 0.1307 0.1008 0.1474 -0.0030 0.0028  -0.0132 192 TRP A CE2 
1581 C  CE3 . TRP A 191 ? 0.0904 0.1290 0.1202 -0.0157 0.0017  0.0096  192 TRP A CE3 
1582 C  CZ2 . TRP A 191 ? 0.1292 0.1045 0.1662 -0.0078 -0.0148 -0.0156 192 TRP A CZ2 
1583 C  CZ3 . TRP A 191 ? 0.0926 0.1345 0.1516 -0.0017 0.0063  0.0073  192 TRP A CZ3 
1584 C  CH2 . TRP A 191 ? 0.1118 0.1247 0.1870 -0.0063 -0.0132 0.0020  192 TRP A CH2 
1585 N  N   . THR A 192 ? 0.0834 0.1013 0.0926 0.0028  0.0001  -0.0038 193 THR A N   
1586 C  CA  . THR A 192 ? 0.1019 0.0983 0.0916 -0.0030 0.0063  0.0019  193 THR A CA  
1587 C  C   . THR A 192 ? 0.0846 0.0900 0.0898 -0.0068 0.0137  -0.0032 193 THR A C   
1588 O  O   . THR A 192 ? 0.1020 0.1193 0.0878 -0.0015 0.0065  -0.0080 193 THR A O   
1589 C  CB  . THR A 192 ? 0.0907 0.1040 0.0948 -0.0049 0.0126  -0.0046 193 THR A CB  
1590 O  OG1 . THR A 192 ? 0.1049 0.0988 0.1106 -0.0049 0.0102  0.0000  193 THR A OG1 
1591 C  CG2 . THR A 192 ? 0.1381 0.1220 0.1001 -0.0173 0.0196  0.0114  193 THR A CG2 
1592 N  N   . TYR A 193 ? 0.0873 0.0996 0.0944 -0.0071 -0.0130 0.0082  194 TYR A N   
1593 C  CA  . TYR A 193 ? 0.0982 0.1001 0.0819 -0.0093 -0.0006 -0.0006 194 TYR A CA  
1594 C  C   . TYR A 193 ? 0.0892 0.0868 0.0866 -0.0108 -0.0082 0.0098  194 TYR A C   
1595 O  O   . TYR A 193 ? 0.0925 0.1024 0.0834 -0.0017 -0.0088 -0.0019 194 TYR A O   
1596 C  CB  . TYR A 193 ? 0.1137 0.1094 0.0710 -0.0156 -0.0081 0.0020  194 TYR A CB  
1597 C  CG  . TYR A 193 ? 0.0921 0.0832 0.0948 -0.0060 -0.0070 -0.0065 194 TYR A CG  
1598 C  CD1 . TYR A 193 ? 0.1046 0.0832 0.0815 -0.0131 -0.0066 -0.0088 194 TYR A CD1 
1599 C  CD2 . TYR A 193 ? 0.0936 0.0876 0.0982 -0.0132 -0.0129 0.0070  194 TYR A CD2 
1600 C  CE1 . TYR A 193 ? 0.0837 0.0824 0.0940 0.0006  -0.0116 -0.0012 194 TYR A CE1 
1601 C  CE2 . TYR A 193 ? 0.0967 0.0996 0.0993 -0.0137 -0.0174 0.0137  194 TYR A CE2 
1602 C  CZ  . TYR A 193 ? 0.0755 0.0785 0.0914 -0.0104 -0.0071 0.0008  194 TYR A CZ  
1603 O  OH  . TYR A 193 ? 0.0953 0.0844 0.0966 -0.0098 -0.0003 0.0000  194 TYR A OH  
1604 N  N   . PRO A 194 ? 0.0847 0.1152 0.0834 -0.0153 -0.0046 0.0092  195 PRO A N   
1605 C  CA  . PRO A 194 ? 0.0896 0.0926 0.1024 -0.0088 -0.0038 0.0168  195 PRO A CA  
1606 C  C   . PRO A 194 ? 0.0802 0.0848 0.1036 0.0020  -0.0230 0.0149  195 PRO A C   
1607 O  O   . PRO A 194 ? 0.0974 0.1132 0.0931 -0.0219 -0.0185 0.0041  195 PRO A O   
1608 C  CB  . PRO A 194 ? 0.1202 0.1238 0.1018 0.0071  0.0083  0.0296  195 PRO A CB  
1609 C  CG  . PRO A 194 ? 0.1375 0.1430 0.0944 -0.0057 -0.0034 0.0315  195 PRO A CG  
1610 C  CD  . PRO A 194 ? 0.1283 0.1502 0.0788 0.0171  -0.0008 0.0113  195 PRO A CD  
1611 N  N   . GLY A 195 ? 0.0820 0.0838 0.1010 -0.0044 -0.0046 0.0137  196 GLY A N   
1612 C  CA  . GLY A 195 ? 0.0802 0.0835 0.1055 -0.0082 -0.0023 0.0049  196 GLY A CA  
1613 C  C   . GLY A 195 ? 0.0728 0.0756 0.1048 -0.0028 -0.0138 0.0125  196 GLY A C   
1614 O  O   . GLY A 195 ? 0.0969 0.0772 0.0996 -0.0008 -0.0098 0.0091  196 GLY A O   
1615 N  N   . SER A 196 ? 0.0759 0.0744 0.0980 0.0051  -0.0035 0.0080  197 SER A N   
1616 C  CA  . SER A 196 ? 0.0798 0.0900 0.1032 0.0094  -0.0005 0.0156  197 SER A CA  
1617 C  C   . SER A 196 ? 0.0546 0.0760 0.1044 0.0034  -0.0110 -0.0017 197 SER A C   
1618 O  O   . SER A 196 ? 0.0666 0.0825 0.1004 0.0083  -0.0038 0.0077  197 SER A O   
1619 C  CB  . SER A 196 ? 0.0798 0.0861 0.1268 0.0082  -0.0127 0.0109  197 SER A CB  
1620 O  OG  . SER A 196 ? 0.0732 0.0864 0.1240 -0.0001 -0.0060 0.0154  197 SER A OG  
1621 N  N   . LEU A 197 ? 0.0782 0.0759 0.1049 0.0019  0.0031  0.0074  198 LEU A N   
1622 C  CA  . LEU A 197 ? 0.0923 0.0856 0.1031 0.0093  -0.0019 0.0152  198 LEU A CA  
1623 C  C   . LEU A 197 ? 0.0710 0.0860 0.1142 0.0073  0.0083  0.0111  198 LEU A C   
1624 O  O   . LEU A 197 ? 0.0741 0.1042 0.1094 0.0046  0.0020  0.0195  198 LEU A O   
1625 C  CB  . LEU A 197 ? 0.1018 0.0964 0.1146 0.0062  0.0027  -0.0015 198 LEU A CB  
1626 C  CG  . LEU A 197 ? 0.1436 0.1133 0.1268 -0.0027 0.0243  -0.0098 198 LEU A CG  
1627 C  CD1 . LEU A 197 ? 0.2146 0.1488 0.1905 0.0493  0.0055  -0.0386 198 LEU A CD1 
1628 C  CD2 . LEU A 197 ? 0.1414 0.1499 0.1898 -0.0339 0.0498  -0.0421 198 LEU A CD2 
1629 N  N   . THR A 198 ? 0.0834 0.0935 0.1059 -0.0063 -0.0006 0.0115  199 THR A N   
1630 C  CA  . THR A 198 ? 0.0795 0.0917 0.1326 -0.0024 -0.0034 0.0206  199 THR A CA  
1631 C  C   . THR A 198 ? 0.0663 0.1061 0.1388 0.0038  -0.0030 0.0197  199 THR A C   
1632 O  O   . THR A 198 ? 0.0736 0.1087 0.1612 -0.0032 0.0062  0.0208  199 THR A O   
1633 C  CB  . THR A 198 ? 0.0932 0.0931 0.0909 -0.0065 -0.0080 0.0052  199 THR A CB  
1634 O  OG1 . THR A 198 ? 0.0846 0.0864 0.1015 0.0048  -0.0048 -0.0017 199 THR A OG1 
1635 C  CG2 . THR A 198 ? 0.0983 0.1163 0.1085 -0.0024 0.0087  0.0137  199 THR A CG2 
1636 N  N   . THR A 199 ? 0.0979 0.1154 0.1391 0.0104  0.0168  0.0125  200 THR A N   
1637 C  CA  . THR A 199 ? 0.1401 0.1221 0.1362 0.0118  0.0281  0.0244  200 THR A CA  
1638 C  C   . THR A 199 ? 0.1146 0.1206 0.1483 0.0151  0.0318  0.0107  200 THR A C   
1639 O  O   . THR A 199 ? 0.1085 0.1137 0.1418 0.0162  0.0241  0.0153  200 THR A O   
1640 C  CB  . THR A 199 ? 0.1568 0.1547 0.1507 0.0151  0.0215  0.0181  200 THR A CB  
1641 O  OG1 . THR A 199 ? 0.2576 0.1597 0.1928 0.0110  -0.0527 0.0188  200 THR A OG1 
1642 C  CG2 . THR A 199 ? 0.2179 0.1580 0.1985 0.0390  -0.0046 0.0403  200 THR A CG2 
1643 N  N   . PRO A 200 ? 0.1264 0.1261 0.1401 0.0153  0.0318  0.0083  201 PRO A N   
1644 C  CA  . PRO A 200 ? 0.1348 0.1403 0.1675 0.0245  0.0249  0.0159  201 PRO A CA  
1645 C  C   . PRO A 200 ? 0.1439 0.1370 0.1714 0.0414  0.0372  -0.0006 201 PRO A C   
1646 O  O   . PRO A 200 ? 0.1589 0.1648 0.1473 0.0024  0.0129  -0.0107 201 PRO A O   
1647 C  CB  . PRO A 200 ? 0.1128 0.1885 0.1974 0.0329  0.0304  0.0017  201 PRO A CB  
1648 C  CG  . PRO A 200 ? 0.1229 0.1793 0.1907 0.0208  0.0251  0.0370  201 PRO A CG  
1649 C  CD  . PRO A 200 ? 0.1261 0.1589 0.1633 0.0142  0.0465  0.0199  201 PRO A CD  
1650 N  N   . PRO A 201 ? 0.1234 0.1411 0.1525 0.0293  0.0142  -0.0066 202 PRO A N   
1651 C  CA  . PRO A 201 ? 0.1497 0.1327 0.1515 0.0377  0.0251  0.0020  202 PRO A CA  
1652 C  C   . PRO A 201 ? 0.1115 0.1166 0.1629 0.0140  0.0122  0.0057  202 PRO A C   
1653 O  O   . PRO A 201 ? 0.1159 0.1362 0.1715 0.0282  0.0160  0.0059  202 PRO A O   
1654 C  CB  . PRO A 201 ? 0.1844 0.1377 0.2346 0.0500  0.0480  -0.0326 202 PRO A CB  
1655 C  CG  . PRO A 201 ? 0.2050 0.1530 0.2220 0.0300  0.0348  0.0035  202 PRO A CG  
1656 C  CD  . PRO A 201 ? 0.2005 0.1428 0.1548 -0.0142 0.0219  -0.0102 202 PRO A CD  
1657 N  N   . LEU A 202 ? 0.1085 0.1071 0.1372 0.0135  0.0102  0.0000  203 LEU A N   
1658 C  CA  . LEU A 202 ? 0.1068 0.1075 0.1306 -0.0013 0.0043  0.0140  203 LEU A CA  
1659 C  C   . LEU A 202 ? 0.0878 0.0952 0.1379 0.0159  0.0087  0.0032  203 LEU A C   
1660 O  O   . LEU A 202 ? 0.0958 0.0967 0.1412 0.0043  0.0043  0.0131  203 LEU A O   
1661 C  CB  . LEU A 202 ? 0.0648 0.1067 0.1605 0.0007  0.0034  0.0080  203 LEU A CB  
1662 C  CG  . LEU A 202 ? 0.0763 0.1103 0.1729 -0.0023 0.0181  0.0286  203 LEU A CG  
1663 C  CD1 . LEU A 202 ? 0.0989 0.1152 0.2091 0.0026  0.0006  0.0293  203 LEU A CD1 
1664 C  CD2 . LEU A 202 ? 0.0983 0.1142 0.1738 0.0130  0.0105  0.0207  203 LEU A CD2 
1665 N  N   . LEU A 203 ? 0.0820 0.0958 0.1638 0.0057  0.0031  0.0105  204 LEU A N   
1666 C  CA  . LEU A 203 ? 0.0839 0.0952 0.1768 0.0000  0.0049  0.0132  204 LEU A CA  
1667 C  C   . LEU A 203 ? 0.0922 0.0816 0.1569 0.0071  -0.0071 0.0070  204 LEU A C   
1668 O  O   . LEU A 203 ? 0.0992 0.0888 0.1304 0.0130  -0.0035 0.0129  204 LEU A O   
1669 C  CB  . LEU A 203 ? 0.1296 0.0978 0.1736 0.0077  0.0144  -0.0078 204 LEU A CB  
1670 C  CG  . LEU A 203 ? 0.1553 0.1103 0.2215 0.0049  0.0557  -0.0196 204 LEU A CG  
1671 C  CD1 . LEU A 203 ? 0.2369 0.1243 0.2540 -0.0161 0.0951  -0.0485 204 LEU A CD1 
1672 C  CD2 . LEU A 203 ? 0.1541 0.1606 0.3700 0.0637  0.0438  -0.0175 204 LEU A CD2 
1673 N  N   . GLU A 204 ? 0.0857 0.1087 0.1433 0.0165  -0.0010 0.0201  205 GLU A N   
1674 C  CA  . GLU A 204 ? 0.1262 0.0863 0.1371 0.0026  -0.0324 0.0320  205 GLU A CA  
1675 C  C   . GLU A 204 ? 0.0983 0.0772 0.1362 0.0153  -0.0185 0.0176  205 GLU A C   
1676 O  O   . GLU A 204 ? 0.1347 0.1370 0.1402 -0.0267 -0.0383 0.0483  205 GLU A O   
1677 C  CB  . GLU A 204 ? 0.1136 0.1168 0.1532 -0.0141 -0.0494 0.0329  205 GLU A CB  
1678 C  CG  . GLU A 204 ? 0.1053 0.1202 0.1727 -0.0071 -0.0498 0.0320  205 GLU A CG  
1679 C  CD  . GLU A 204 ? 0.1274 0.1287 0.1723 0.0083  -0.0513 0.0230  205 GLU A CD  
1680 O  OE1 . GLU A 204 ? 0.1474 0.1509 0.2137 -0.0163 -0.0835 0.0494  205 GLU A OE1 
1681 O  OE2 . GLU A 204 ? 0.1093 0.1298 0.1655 0.0038  -0.0428 0.0111  205 GLU A OE2 
1682 N  N   . CYS A 205 ? 0.0784 0.0881 0.1310 0.0041  -0.0179 0.0097  206 CYS A N   
1683 C  CA  . CYS A 205 ? 0.1096 0.0816 0.1229 0.0023  -0.0115 0.0034  206 CYS A CA  
1684 C  C   . CYS A 205 ? 0.0802 0.0854 0.1206 -0.0024 -0.0097 0.0131  206 CYS A C   
1685 O  O   . CYS A 205 ? 0.1067 0.0852 0.1607 -0.0054 -0.0303 -0.0028 206 CYS A O   
1686 C  CB  . CYS A 205 ? 0.1190 0.0957 0.1360 0.0147  -0.0005 -0.0019 206 CYS A CB  
1687 S  SG  . CYS A 205 ? 0.1366 0.1036 0.1252 0.0015  -0.0043 0.0038  206 CYS A SG  
1688 N  N   . VAL A 206 ? 0.0817 0.0736 0.1137 0.0031  -0.0054 0.0037  207 VAL A N   
1689 C  CA  . VAL A 206 ? 0.0785 0.0838 0.1163 0.0068  -0.0031 0.0017  207 VAL A CA  
1690 C  C   . VAL A 206 ? 0.0776 0.0762 0.1106 0.0010  -0.0175 -0.0049 207 VAL A C   
1691 O  O   . VAL A 206 ? 0.0942 0.1042 0.1225 -0.0023 -0.0110 -0.0178 207 VAL A O   
1692 C  CB  . VAL A 206 ? 0.0766 0.0816 0.1181 -0.0030 -0.0068 0.0013  207 VAL A CB  
1693 C  CG1 . VAL A 206 ? 0.0777 0.0860 0.1282 -0.0052 -0.0160 0.0142  207 VAL A CG1 
1694 C  CG2 . VAL A 206 ? 0.0900 0.1151 0.1177 -0.0043 0.0094  0.0127  207 VAL A CG2 
1695 N  N   . THR A 207 ? 0.0766 0.0710 0.1071 0.0013  -0.0114 0.0070  208 THR A N   
1696 C  CA  . THR A 207 ? 0.0913 0.0784 0.0951 0.0030  -0.0031 0.0034  208 THR A CA  
1697 C  C   . THR A 207 ? 0.0876 0.0764 0.0879 0.0000  -0.0082 -0.0087 208 THR A C   
1698 O  O   . THR A 207 ? 0.0925 0.0764 0.0947 -0.0057 -0.0127 -0.0078 208 THR A O   
1699 C  CB  . THR A 207 ? 0.0982 0.0780 0.1248 0.0049  0.0001  0.0087  208 THR A CB  
1700 O  OG1 . THR A 207 ? 0.1146 0.0951 0.1168 -0.0028 0.0000  0.0187  208 THR A OG1 
1701 C  CG2 . THR A 207 ? 0.1059 0.1049 0.1343 0.0076  0.0218  0.0044  208 THR A CG2 
1702 N  N   . TRP A 208 ? 0.0870 0.0680 0.0812 -0.0031 0.0007  -0.0008 209 TRP A N   
1703 C  CA  . TRP A 208 ? 0.0842 0.0731 0.0890 -0.0068 -0.0135 0.0019  209 TRP A CA  
1704 C  C   . TRP A 208 ? 0.0706 0.0764 0.0886 -0.0019 0.0008  0.0027  209 TRP A C   
1705 O  O   . TRP A 208 ? 0.0847 0.0967 0.0804 -0.0013 0.0013  -0.0051 209 TRP A O   
1706 C  CB  . TRP A 208 ? 0.0703 0.0768 0.0983 -0.0052 -0.0024 -0.0054 209 TRP A CB  
1707 C  CG  . TRP A 208 ? 0.0711 0.0719 0.0913 -0.0133 -0.0073 0.0068  209 TRP A CG  
1708 C  CD1 . TRP A 208 ? 0.0768 0.0728 0.1123 -0.0023 -0.0126 -0.0017 209 TRP A CD1 
1709 C  CD2 . TRP A 208 ? 0.0496 0.0745 0.1121 -0.0105 -0.0028 0.0114  209 TRP A CD2 
1710 N  NE1 . TRP A 208 ? 0.0878 0.0938 0.1105 -0.0012 -0.0049 -0.0007 209 TRP A NE1 
1711 C  CE2 . TRP A 208 ? 0.0724 0.0807 0.1159 -0.0071 -0.0041 -0.0013 209 TRP A CE2 
1712 C  CE3 . TRP A 208 ? 0.0824 0.0806 0.0904 -0.0057 -0.0118 -0.0006 209 TRP A CE3 
1713 C  CZ2 . TRP A 208 ? 0.0825 0.0952 0.1340 -0.0230 0.0071  0.0038  209 TRP A CZ2 
1714 C  CZ3 . TRP A 208 ? 0.1110 0.0854 0.0936 -0.0091 0.0037  0.0028  209 TRP A CZ3 
1715 C  CH2 . TRP A 208 ? 0.1187 0.0878 0.1114 -0.0157 0.0074  -0.0003 209 TRP A CH2 
1716 N  N   . ILE A 209 ? 0.0733 0.0725 0.0863 0.0012  -0.0026 -0.0027 210 ILE A N   
1717 C  CA  . ILE A 209 ? 0.0711 0.0759 0.1058 0.0007  -0.0020 -0.0026 210 ILE A CA  
1718 C  C   . ILE A 209 ? 0.0716 0.0745 0.0964 0.0054  -0.0013 -0.0059 210 ILE A C   
1719 O  O   . ILE A 209 ? 0.1134 0.0843 0.0894 0.0007  -0.0052 -0.0031 210 ILE A O   
1720 C  CB  . ILE A 209 ? 0.0720 0.0806 0.1353 -0.0065 0.0051  0.0005  210 ILE A CB  
1721 C  CG1 . ILE A 209 ? 0.0960 0.0942 0.1704 -0.0142 -0.0020 0.0152  210 ILE A CG1 
1722 C  CG2 . ILE A 209 ? 0.0719 0.1371 0.1536 -0.0104 0.0066  -0.0204 210 ILE A CG2 
1723 C  CD1 . ILE A 209 ? 0.1341 0.0997 0.2190 -0.0276 -0.0120 0.0049  210 ILE A CD1 
1724 N  N   . VAL A 210 ? 0.0737 0.0680 0.1130 0.0000  0.0010  -0.0017 211 VAL A N   
1725 C  CA  . VAL A 210 ? 0.0759 0.0782 0.0854 0.0076  0.0013  -0.0037 211 VAL A CA  
1726 C  C   . VAL A 210 ? 0.0844 0.0692 0.0956 -0.0048 -0.0023 -0.0124 211 VAL A C   
1727 O  O   . VAL A 210 ? 0.0966 0.0920 0.0978 0.0130  0.0038  -0.0142 211 VAL A O   
1728 C  CB  . VAL A 210 ? 0.0861 0.0832 0.1094 -0.0015 -0.0103 0.0012  211 VAL A CB  
1729 C  CG1 . VAL A 210 ? 0.1114 0.0798 0.1266 -0.0065 -0.0054 -0.0118 211 VAL A CG1 
1730 C  CG2 . VAL A 210 ? 0.1014 0.0851 0.1255 0.0054  -0.0054 -0.0073 211 VAL A CG2 
1731 N  N   . LEU A 211 ? 0.0789 0.0940 0.1010 0.0132  0.0000  -0.0031 212 LEU A N   
1732 C  CA  . LEU A 211 ? 0.0715 0.1039 0.1191 0.0030  -0.0031 -0.0049 212 LEU A CA  
1733 C  C   . LEU A 211 ? 0.0720 0.1045 0.1048 0.0192  -0.0078 -0.0091 212 LEU A C   
1734 O  O   . LEU A 211 ? 0.0835 0.1096 0.1127 0.0062  0.0017  -0.0082 212 LEU A O   
1735 C  CB  . LEU A 211 ? 0.0832 0.1207 0.1278 0.0137  -0.0052 -0.0156 212 LEU A CB  
1736 C  CG  . LEU A 211 ? 0.0903 0.1110 0.1464 0.0046  -0.0218 -0.0080 212 LEU A CG  
1737 C  CD1 . LEU A 211 ? 0.1002 0.1650 0.1722 0.0108  -0.0524 -0.0395 212 LEU A CD1 
1738 C  CD2 . LEU A 211 ? 0.1052 0.1159 0.1662 -0.0097 -0.0153 -0.0120 212 LEU A CD2 
1739 N  N   . LYS A 212 ? 0.0905 0.1098 0.1107 0.0217  -0.0083 -0.0113 213 LYS A N   
1740 C  CA  . LYS A 212 ? 0.1127 0.1168 0.1150 0.0262  -0.0048 -0.0178 213 LYS A CA  
1741 C  C   . LYS A 212 ? 0.0948 0.0970 0.1171 0.0157  0.0000  -0.0219 213 LYS A C   
1742 O  O   . LYS A 212 ? 0.1191 0.1114 0.1635 0.0082  -0.0373 -0.0231 213 LYS A O   
1743 C  CB  . LYS A 212 ? 0.1524 0.1536 0.1209 0.0617  0.0092  -0.0182 213 LYS A CB  
1744 C  CG  . LYS A 212 ? 0.1941 0.1694 0.1849 0.0333  -0.0165 -0.0434 213 LYS A CG  
1745 C  CD  . LYS A 212 ? 0.3772 0.2820 0.1826 0.1527  0.0177  -0.0428 213 LYS A CD  
1746 C  CE  . LYS A 212 ? 0.4814 0.3165 0.2910 0.0546  0.1277  -0.1341 213 LYS A CE  
1747 N  NZ  . LYS A 212 ? 0.5588 0.5989 0.4384 0.0232  0.2108  -0.2039 213 LYS A NZ  
1748 N  N   . GLU A 213 ? 0.0851 0.1022 0.1325 0.0162  -0.0138 -0.0140 214 GLU A N   
1749 C  CA  . GLU A 213 ? 0.1163 0.1124 0.1358 0.0166  -0.0157 -0.0120 214 GLU A CA  
1750 C  C   . GLU A 213 ? 0.0869 0.0949 0.1371 0.0185  -0.0285 -0.0136 214 GLU A C   
1751 O  O   . GLU A 213 ? 0.1033 0.0993 0.1365 0.0052  -0.0167 -0.0269 214 GLU A O   
1752 C  CB  . GLU A 213 ? 0.0978 0.1381 0.1550 0.0226  -0.0217 -0.0261 214 GLU A CB  
1753 C  CG  . GLU A 213 ? 0.1243 0.1544 0.1965 0.0428  -0.0527 -0.0161 214 GLU A CG  
1754 C  CD  . GLU A 213 ? 0.1499 0.2362 0.2020 0.0496  -0.0582 -0.0165 214 GLU A CD  
1755 O  OE1 . GLU A 213 ? 0.1300 0.1643 0.3231 0.0237  -0.0670 -0.0441 214 GLU A OE1 
1756 O  OE2 . GLU A 213 ? 0.2296 0.2712 0.3420 0.0666  -0.0582 0.0340  214 GLU A OE2 
1757 N  N   A PRO A 214 ? 0.1259 0.0879 0.1186 0.0126  -0.0253 -0.0096 215 PRO A N   
1758 N  N   B PRO A 214 ? 0.1322 0.0872 0.1327 0.0092  -0.0231 -0.0116 215 PRO A N   
1759 C  CA  A PRO A 214 ? 0.1099 0.0984 0.1193 0.0086  -0.0199 -0.0081 215 PRO A CA  
1760 C  CA  B PRO A 214 ? 0.1184 0.1064 0.1317 0.0028  -0.0221 0.0015  215 PRO A CA  
1761 C  C   A PRO A 214 ? 0.1314 0.0917 0.1347 0.0294  -0.0434 0.0000  215 PRO A C   
1762 C  C   B PRO A 214 ? 0.0948 0.0935 0.1380 -0.0010 -0.0277 0.0197  215 PRO A C   
1763 O  O   A PRO A 214 ? 0.1378 0.0997 0.1394 0.0304  -0.0375 0.0012  215 PRO A O   
1764 O  O   B PRO A 214 ? 0.1059 0.1287 0.1341 0.0085  -0.0399 0.0138  215 PRO A O   
1765 C  CB  A PRO A 214 ? 0.1195 0.0821 0.1380 0.0110  -0.0168 -0.0135 215 PRO A CB  
1766 C  CB  B PRO A 214 ? 0.1234 0.0980 0.1775 0.0021  -0.0122 -0.0040 215 PRO A CB  
1767 C  CG  A PRO A 214 ? 0.1207 0.0803 0.1334 0.0175  -0.0193 -0.0104 215 PRO A CG  
1768 C  CG  B PRO A 214 ? 0.1636 0.1493 0.1956 0.0017  0.0278  -0.0194 215 PRO A CG  
1769 C  CD  A PRO A 214 ? 0.1389 0.0872 0.1281 0.0166  -0.0263 -0.0094 215 PRO A CD  
1770 C  CD  B PRO A 214 ? 0.1269 0.0870 0.1745 0.0285  -0.0065 -0.0342 215 PRO A CD  
1771 N  N   . ILE A 215 ? 0.1391 0.1010 0.1127 -0.0013 -0.0303 0.0109  216 ILE A N   
1772 C  CA  . ILE A 215 ? 0.1453 0.0931 0.1351 -0.0005 -0.0529 0.0159  216 ILE A CA  
1773 C  C   . ILE A 215 ? 0.1089 0.0995 0.1262 0.0043  -0.0227 0.0035  216 ILE A C   
1774 O  O   . ILE A 215 ? 0.1261 0.0995 0.1645 0.0102  -0.0285 0.0175  216 ILE A O   
1775 C  CB  . ILE A 215 ? 0.1733 0.0966 0.1490 0.0000  -0.0450 0.0203  216 ILE A CB  
1776 C  CG1 . ILE A 215 ? 0.2159 0.1115 0.1221 0.0147  -0.0449 -0.0129 216 ILE A CG1 
1777 C  CG2 . ILE A 215 ? 0.2189 0.1221 0.1580 -0.0324 -0.0599 0.0274  216 ILE A CG2 
1778 C  CD1 . ILE A 215 ? 0.2653 0.1412 0.1316 0.0020  -0.0342 -0.0274 216 ILE A CD1 
1779 N  N   A SER A 216 ? 0.1268 0.1014 0.1462 -0.0031 -0.0362 0.0146  217 SER A N   
1780 N  N   B SER A 216 ? 0.1451 0.1142 0.1483 0.0111  -0.0372 0.0152  217 SER A N   
1781 C  CA  A SER A 216 ? 0.1535 0.0842 0.1576 0.0364  -0.0189 0.0329  217 SER A CA  
1782 C  CA  B SER A 216 ? 0.1184 0.1206 0.1521 -0.0172 -0.0412 0.0071  217 SER A CA  
1783 C  C   A SER A 216 ? 0.1425 0.1067 0.1460 -0.0060 -0.0452 0.0120  217 SER A C   
1784 C  C   B SER A 216 ? 0.1472 0.0895 0.1541 0.0031  -0.0339 0.0055  217 SER A C   
1785 O  O   A SER A 216 ? 0.1659 0.1251 0.1579 0.0010  -0.0728 0.0027  217 SER A O   
1786 O  O   B SER A 216 ? 0.1471 0.1187 0.1700 -0.0153 -0.0307 0.0131  217 SER A O   
1787 C  CB  A SER A 216 ? 0.2029 0.0736 0.1815 0.0292  0.0271  0.0146  217 SER A CB  
1788 C  CB  B SER A 216 ? 0.2773 0.1130 0.1683 0.0467  0.0027  0.0173  217 SER A CB  
1789 O  OG  A SER A 216 ? 0.1554 0.1189 0.1594 0.0406  -0.0074 0.0062  217 SER A OG  
1790 O  OG  B SER A 216 ? 0.2937 0.1474 0.2247 0.0353  0.0288  0.0251  217 SER A OG  
1791 N  N   . VAL A 217 ? 0.1565 0.0978 0.1289 0.0136  -0.0359 0.0126  218 VAL A N   
1792 C  CA  . VAL A 217 ? 0.1774 0.0923 0.1309 0.0166  -0.0335 0.0013  218 VAL A CA  
1793 C  C   . VAL A 217 ? 0.1563 0.0821 0.1571 0.0137  -0.0262 0.0023  218 VAL A C   
1794 O  O   . VAL A 217 ? 0.1782 0.0975 0.1396 0.0248  -0.0427 0.0068  218 VAL A O   
1795 C  CB  . VAL A 217 ? 0.1626 0.0794 0.1871 0.0209  -0.0428 0.0124  218 VAL A CB  
1796 C  CG1 . VAL A 217 ? 0.1908 0.0910 0.1560 0.0274  -0.0357 0.0118  218 VAL A CG1 
1797 C  CG2 . VAL A 217 ? 0.1592 0.1071 0.1958 0.0252  -0.0342 0.0161  218 VAL A CG2 
1798 N  N   . SER A 218 ? 0.1894 0.0938 0.1347 0.0276  -0.0373 0.0155  219 SER A N   
1799 C  CA  . SER A 218 ? 0.1638 0.0864 0.1468 0.0142  -0.0261 0.0152  219 SER A CA  
1800 C  C   . SER A 218 ? 0.2025 0.0781 0.1254 0.0225  -0.0238 0.0052  219 SER A C   
1801 O  O   . SER A 218 ? 0.1911 0.0932 0.1398 0.0154  -0.0317 0.0020  219 SER A O   
1802 C  CB  . SER A 218 ? 0.2328 0.0914 0.1350 0.0074  -0.0469 0.0219  219 SER A CB  
1803 O  OG  . SER A 218 ? 0.2342 0.1169 0.1387 0.0348  -0.0414 0.0001  219 SER A OG  
1804 N  N   A SER A 219 ? 0.1699 0.0777 0.1601 0.0284  0.0026  0.0060  220 SER A N   
1805 N  N   B SER A 219 ? 0.1905 0.0807 0.1429 0.0103  -0.0326 -0.0057 220 SER A N   
1806 C  CA  A SER A 219 ? 0.1557 0.0724 0.1875 0.0318  0.0068  -0.0280 220 SER A CA  
1807 C  CA  B SER A 219 ? 0.1970 0.1031 0.1485 -0.0032 -0.0283 -0.0096 220 SER A CA  
1808 C  C   A SER A 219 ? 0.1959 0.1013 0.1816 -0.0062 0.0013  -0.0077 220 SER A C   
1809 C  C   B SER A 219 ? 0.1958 0.1027 0.1523 0.0038  -0.0083 0.0142  220 SER A C   
1810 O  O   A SER A 219 ? 0.2260 0.0913 0.1890 0.0199  0.0308  -0.0196 220 SER A O   
1811 O  O   B SER A 219 ? 0.1732 0.1533 0.1657 -0.0041 0.0119  -0.0048 220 SER A O   
1812 C  CB  A SER A 219 ? 0.2425 0.0794 0.1967 -0.0087 -0.0043 -0.0364 220 SER A CB  
1813 C  CB  B SER A 219 ? 0.2151 0.1033 0.2171 0.0309  0.0120  0.0515  220 SER A CB  
1814 O  OG  A SER A 219 ? 0.2800 0.0810 0.2189 0.0094  -0.0057 0.0037  220 SER A OG  
1815 O  OG  B SER A 219 ? 0.2250 0.0989 0.2133 0.0060  -0.0109 -0.0071 220 SER A OG  
1816 N  N   . GLU A 220 ? 0.2161 0.0921 0.1447 0.0188  -0.0142 0.0100  221 GLU A N   
1817 C  CA  . GLU A 220 ? 0.2904 0.1103 0.1393 0.0167  -0.0189 0.0074  221 GLU A CA  
1818 C  C   . GLU A 220 ? 0.2626 0.1049 0.1245 -0.0032 -0.0120 -0.0010 221 GLU A C   
1819 O  O   . GLU A 220 ? 0.2640 0.1283 0.1447 0.0110  0.0226  0.0017  221 GLU A O   
1820 C  CB  . GLU A 220 ? 0.3560 0.1701 0.1370 0.0579  -0.0200 0.0293  221 GLU A CB  
1821 C  CG  . GLU A 220 ? 0.4284 0.2198 0.2387 0.0193  -0.0754 0.1203  221 GLU A CG  
1822 C  CD  . GLU A 220 ? 0.4013 0.3824 0.3133 -0.0650 0.0645  0.0242  221 GLU A CD  
1823 O  OE1 . GLU A 220 ? 0.3274 0.2064 0.3465 0.0944  0.0201  0.0485  221 GLU A OE1 
1824 O  OE2 . GLU A 220 ? 0.5805 1.2335 0.9940 0.5896  0.2579  0.9766  221 GLU A OE2 
1825 N  N   . GLN A 221 ? 0.2275 0.0926 0.1456 0.0171  -0.0260 0.0054  222 GLN A N   
1826 C  CA  . GLN A 221 ? 0.2195 0.0927 0.1414 0.0212  -0.0127 -0.0060 222 GLN A CA  
1827 C  C   . GLN A 221 ? 0.2111 0.1019 0.1261 0.0227  -0.0263 -0.0132 222 GLN A C   
1828 O  O   . GLN A 221 ? 0.2312 0.1079 0.1315 0.0306  0.0049  -0.0109 222 GLN A O   
1829 C  CB  . GLN A 221 ? 0.2062 0.1070 0.1306 0.0137  -0.0449 0.0052  222 GLN A CB  
1830 C  CG  . GLN A 221 ? 0.2056 0.1049 0.1292 0.0136  -0.0494 0.0065  222 GLN A CG  
1831 C  CD  . GLN A 221 ? 0.2002 0.0817 0.1465 0.0188  -0.0395 0.0038  222 GLN A CD  
1832 O  OE1 . GLN A 221 ? 0.1933 0.1068 0.1395 0.0241  -0.0317 -0.0031 222 GLN A OE1 
1833 N  NE2 . GLN A 221 ? 0.2304 0.0976 0.1518 0.0087  -0.0542 -0.0020 222 GLN A NE2 
1834 N  N   . VAL A 222 ? 0.2038 0.0979 0.1277 0.0207  -0.0283 -0.0006 223 VAL A N   
1835 C  CA  . VAL A 222 ? 0.1978 0.1114 0.1360 0.0199  -0.0086 -0.0196 223 VAL A CA  
1836 C  C   . VAL A 222 ? 0.1988 0.1054 0.1513 0.0147  -0.0193 -0.0161 223 VAL A C   
1837 O  O   . VAL A 222 ? 0.2140 0.1238 0.1520 0.0299  -0.0063 -0.0284 223 VAL A O   
1838 C  CB  . VAL A 222 ? 0.2335 0.1603 0.1617 0.0249  -0.0692 -0.0439 223 VAL A CB  
1839 C  CG1 . VAL A 222 ? 0.2216 0.1731 0.2028 0.0340  -0.0458 -0.0485 223 VAL A CG1 
1840 C  CG2 . VAL A 222 ? 0.2563 0.1932 0.1837 0.0493  -0.0615 -0.0373 223 VAL A CG2 
1841 N  N   . LEU A 223 ? 0.2098 0.1139 0.1524 0.0035  -0.0001 -0.0068 224 LEU A N   
1842 C  CA  . LEU A 223 ? 0.2804 0.1213 0.1765 0.0178  0.0463  0.0082  224 LEU A CA  
1843 C  C   . LEU A 223 ? 0.2351 0.1375 0.1500 0.0199  0.0164  0.0126  224 LEU A C   
1844 O  O   . LEU A 223 ? 0.2237 0.1596 0.1662 0.0195  0.0181  0.0207  224 LEU A O   
1845 C  CB  . LEU A 223 ? 0.2727 0.1098 0.2247 0.0353  0.0353  0.0197  224 LEU A CB  
1846 C  CG  . LEU A 223 ? 0.3441 0.1477 0.2100 -0.0062 0.0086  -0.0043 224 LEU A CG  
1847 C  CD1 . LEU A 223 ? 0.3000 0.1643 0.3504 -0.0015 0.0023  -0.0071 224 LEU A CD1 
1848 C  CD2 . LEU A 223 ? 0.3050 0.2138 0.3233 0.0282  0.0443  0.0388  224 LEU A CD2 
1849 N  N   . LYS A 224 ? 0.2666 0.1152 0.1289 0.0264  0.0031  0.0054  225 LYS A N   
1850 C  CA  . LYS A 224 ? 0.2357 0.1412 0.1486 0.0225  0.0162  -0.0013 225 LYS A CA  
1851 C  C   . LYS A 224 ? 0.2526 0.1250 0.1215 0.0170  -0.0063 -0.0154 225 LYS A C   
1852 O  O   . LYS A 224 ? 0.2633 0.1449 0.1191 0.0223  0.0082  -0.0082 225 LYS A O   
1853 C  CB  . LYS A 224 ? 0.2610 0.2031 0.1731 0.0144  -0.0390 -0.0322 225 LYS A CB  
1854 C  CG  . LYS A 224 ? 0.2698 0.2651 0.2190 0.0450  -0.0408 -0.0020 225 LYS A CG  
1855 C  CD  . LYS A 224 ? 0.3865 0.2063 0.2494 0.0230  -0.1071 0.0248  225 LYS A CD  
1856 C  CE  . LYS A 224 ? 0.5945 0.3905 0.4131 0.0822  -0.2109 0.1711  225 LYS A CE  
1857 N  NZ  . LYS A 224 ? 0.5257 0.3332 0.3231 0.1424  0.0710  0.1140  225 LYS A NZ  
1858 N  N   . PHE A 225 ? 0.2295 0.1230 0.1076 0.0060  0.0088  0.0001  226 PHE A N   
1859 C  CA  . PHE A 225 ? 0.2238 0.1068 0.1220 0.0182  0.0266  0.0021  226 PHE A CA  
1860 C  C   . PHE A 225 ? 0.2376 0.1116 0.1058 0.0280  0.0281  -0.0063 226 PHE A C   
1861 O  O   . PHE A 225 ? 0.2327 0.1146 0.1017 0.0296  0.0259  0.0159  226 PHE A O   
1862 C  CB  . PHE A 225 ? 0.2441 0.1054 0.1080 0.0122  0.0252  -0.0137 226 PHE A CB  
1863 C  CG  . PHE A 225 ? 0.2085 0.0864 0.1366 0.0408  0.0230  0.0254  226 PHE A CG  
1864 C  CD1 . PHE A 225 ? 0.2861 0.1714 0.1615 -0.0227 0.0208  -0.0217 226 PHE A CD1 
1865 C  CD2 . PHE A 225 ? 0.2221 0.2021 0.1495 0.0522  0.0120  0.0513  226 PHE A CD2 
1866 C  CE1 . PHE A 225 ? 0.3237 0.1583 0.1714 -0.0260 0.0337  -0.0010 226 PHE A CE1 
1867 C  CE2 . PHE A 225 ? 0.2081 0.2266 0.2034 0.0340  0.0041  0.0894  226 PHE A CE2 
1868 C  CZ  . PHE A 225 ? 0.2177 0.1378 0.2034 0.0395  0.0282  0.0640  226 PHE A CZ  
1869 N  N   . ARG A 226 ? 0.2155 0.1087 0.1116 0.0071  0.0182  0.0030  227 ARG A N   
1870 C  CA  . ARG A 226 ? 0.2296 0.1301 0.1220 0.0494  0.0102  0.0020  227 ARG A CA  
1871 C  C   . ARG A 226 ? 0.2126 0.1182 0.1441 0.0232  0.0425  0.0132  227 ARG A C   
1872 O  O   . ARG A 226 ? 0.2106 0.1486 0.1481 0.0167  0.0331  0.0074  227 ARG A O   
1873 C  CB  . ARG A 226 ? 0.2610 0.1076 0.1280 0.0230  0.0219  0.0000  227 ARG A CB  
1874 C  CG  . ARG A 226 ? 0.2320 0.1189 0.1211 0.0333  0.0021  -0.0060 227 ARG A CG  
1875 C  CD  . ARG A 226 ? 0.2838 0.1245 0.1381 0.0167  -0.0057 -0.0226 227 ARG A CD  
1876 N  NE  . ARG A 226 ? 0.2364 0.1103 0.1343 0.0515  -0.0208 0.0046  227 ARG A NE  
1877 C  CZ  . ARG A 226 ? 0.2700 0.1186 0.1265 0.0696  -0.0200 0.0019  227 ARG A CZ  
1878 N  NH1 . ARG A 226 ? 0.3118 0.1632 0.2002 0.0979  -0.0241 0.0377  227 ARG A NH1 
1879 N  NH2 . ARG A 226 ? 0.2763 0.1224 0.1369 0.0701  -0.0031 -0.0063 227 ARG A NH2 
1880 N  N   . LYS A 227 ? 0.2397 0.1152 0.1164 0.0361  0.0127  0.0192  228 LYS A N   
1881 C  CA  . LYS A 227 ? 0.2825 0.1509 0.1004 0.0718  0.0215  0.0436  228 LYS A CA  
1882 C  C   . LYS A 227 ? 0.2561 0.1523 0.0992 0.0430  0.0081  0.0226  228 LYS A C   
1883 O  O   . LYS A 227 ? 0.3377 0.1572 0.0979 0.0644  0.0419  0.0210  228 LYS A O   
1884 C  CB  . LYS A 227 ? 0.2994 0.1753 0.1146 0.0538  0.0226  0.0229  228 LYS A CB  
1885 C  CG  . LYS A 227 ? 0.3361 0.1905 0.1532 0.0909  0.0137  0.0208  228 LYS A CG  
1886 C  CD  . LYS A 227 ? 0.4384 0.3095 0.2326 0.2008  -0.0392 0.0546  228 LYS A CD  
1887 C  CE  . LYS A 227 ? 0.5253 0.5996 0.2723 0.2079  -0.0141 0.1731  228 LYS A CE  
1888 N  NZ  . LYS A 227 ? 0.5799 0.8549 0.5781 0.0414  -0.2129 0.3115  228 LYS A NZ  
1889 N  N   . LEU A 228 ? 0.2569 0.1259 0.0932 0.0390  0.0267  0.0089  229 LEU A N   
1890 C  CA  . LEU A 228 ? 0.1879 0.1599 0.1269 0.0632  -0.0010 0.0120  229 LEU A CA  
1891 C  C   . LEU A 228 ? 0.2680 0.1080 0.0813 0.0384  0.0148  0.0010  229 LEU A C   
1892 O  O   . LEU A 228 ? 0.1981 0.1410 0.1221 0.0272  0.0276  0.0146  229 LEU A O   
1893 C  CB  . LEU A 228 ? 0.2536 0.1141 0.0992 0.0487  0.0223  0.0171  229 LEU A CB  
1894 C  CG  . LEU A 228 ? 0.2162 0.1394 0.1159 0.0181  -0.0043 -0.0006 229 LEU A CG  
1895 C  CD1 . LEU A 228 ? 0.2382 0.1691 0.1059 0.0324  0.0103  0.0255  229 LEU A CD1 
1896 C  CD2 . LEU A 228 ? 0.2867 0.1622 0.1511 0.0057  0.0322  -0.0298 229 LEU A CD2 
1897 N  N   . ASN A 229 ? 0.2237 0.1317 0.1254 0.0284  0.0206  0.0019  230 ASN A N   
1898 C  CA  . ASN A 229 ? 0.2176 0.1394 0.1040 -0.0159 0.0052  0.0143  230 ASN A CA  
1899 C  C   . ASN A 229 ? 0.1625 0.1644 0.1405 -0.0390 0.0276  -0.0306 230 ASN A C   
1900 O  O   . ASN A 229 ? 0.2196 0.1432 0.1532 0.0164  0.0261  0.0175  230 ASN A O   
1901 C  CB  . ASN A 229 ? 0.2233 0.1676 0.1388 -0.0073 0.0283  -0.0127 230 ASN A CB  
1902 C  CG  . ASN A 229 ? 0.2894 0.1905 0.0997 0.0586  0.0254  0.0262  230 ASN A CG  
1903 O  OD1 . ASN A 229 ? 0.4095 0.2173 0.1282 0.0590  0.0745  0.0317  230 ASN A OD1 
1904 N  ND2 . ASN A 229 ? 0.2736 0.1483 0.1737 0.0373  0.0507  0.0428  230 ASN A ND2 
1905 N  N   . PHE A 230 ? 0.1670 0.1393 0.1454 0.0401  0.0449  -0.0094 231 PHE A N   
1906 C  CA  . PHE A 230 ? 0.1869 0.1402 0.1351 0.0209  0.0179  -0.0108 231 PHE A CA  
1907 C  C   . PHE A 230 ? 0.2561 0.1458 0.1524 0.0533  0.0298  0.0066  231 PHE A C   
1908 O  O   . PHE A 230 ? 0.2840 0.1756 0.1590 0.0934  0.0599  0.0063  231 PHE A O   
1909 C  CB  . PHE A 230 ? 0.1705 0.1476 0.1886 0.0386  0.0483  0.0054  231 PHE A CB  
1910 C  CG  . PHE A 230 ? 0.2222 0.1278 0.1118 0.0255  0.0234  -0.0012 231 PHE A CG  
1911 C  CD1 . PHE A 230 ? 0.2029 0.1530 0.1564 0.0306  0.0399  -0.0008 231 PHE A CD1 
1912 C  CD2 . PHE A 230 ? 0.1757 0.1782 0.1415 -0.0386 0.0100  0.0170  231 PHE A CD2 
1913 C  CE1 . PHE A 230 ? 0.2407 0.1509 0.1526 0.0291  0.0588  0.0031  231 PHE A CE1 
1914 C  CE2 . PHE A 230 ? 0.2491 0.1483 0.1412 0.0021  0.0137  0.0121  231 PHE A CE2 
1915 C  CZ  . PHE A 230 ? 0.1797 0.1762 0.1303 0.0370  0.0148  -0.0082 231 PHE A CZ  
1916 N  N   . ASN A 231 ? 0.2380 0.1809 0.1268 0.0353  0.0546  -0.0054 232 ASN A N   
1917 C  CA  . ASN A 231 ? 0.2073 0.2096 0.1533 0.0183  0.0302  0.0115  232 ASN A CA  
1918 C  C   . ASN A 231 ? 0.1397 0.1755 0.1421 -0.0236 0.0144  -0.0230 232 ASN A C   
1919 O  O   . ASN A 231 ? 0.2002 0.1750 0.1800 0.0000  0.0204  -0.0031 232 ASN A O   
1920 C  CB  . ASN A 231 ? 0.2462 0.1923 0.1728 0.0027  0.0838  -0.0076 232 ASN A CB  
1921 C  CG  . ASN A 231 ? 0.1978 0.1805 0.1974 -0.0337 0.0423  -0.0317 232 ASN A CG  
1922 O  OD1 . ASN A 231 ? 0.2992 0.1652 0.1940 0.0110  0.0923  -0.0001 232 ASN A OD1 
1923 N  ND2 . ASN A 231 ? 0.2741 0.2111 0.1518 -0.0305 0.0502  -0.0240 232 ASN A ND2 
1924 N  N   . GLY A 232 ? 0.2350 0.1664 0.1895 -0.0017 0.0542  -0.0335 233 GLY A N   
1925 C  CA  . GLY A 232 ? 0.2294 0.2099 0.1599 0.0295  0.0160  -0.0329 233 GLY A CA  
1926 C  C   . GLY A 232 ? 0.1767 0.1606 0.2058 -0.0296 -0.0109 -0.0359 233 GLY A C   
1927 O  O   . GLY A 232 ? 0.2479 0.2319 0.2044 -0.0702 0.0776  -0.0970 233 GLY A O   
1928 N  N   . GLU A 233 ? 0.1933 0.1645 0.1915 -0.0366 0.0436  -0.0166 234 GLU A N   
1929 C  CA  . GLU A 233 ? 0.2122 0.1797 0.1835 -0.0412 0.0474  -0.0052 234 GLU A CA  
1930 C  C   . GLU A 233 ? 0.2172 0.2342 0.1814 -0.0439 0.0307  -0.0104 234 GLU A C   
1931 O  O   . GLU A 233 ? 0.2307 0.2544 0.2214 -0.0331 0.0328  -0.0485 234 GLU A O   
1932 C  CB  . GLU A 233 ? 0.2563 0.2125 0.1527 -0.0373 0.0055  -0.0324 234 GLU A CB  
1933 C  CG  . GLU A 233 ? 0.2773 0.2545 0.1430 0.0368  0.0265  -0.0182 234 GLU A CG  
1934 C  CD  . GLU A 233 ? 0.3876 0.4329 0.2275 -0.0913 0.0182  0.0031  234 GLU A CD  
1935 O  OE1 . GLU A 233 ? 0.3251 0.3856 0.2745 0.0485  0.0584  -0.0850 234 GLU A OE1 
1936 O  OE2 . GLU A 233 ? 0.4072 0.3151 0.2594 0.0493  -0.0388 -0.0099 234 GLU A OE2 
1937 N  N   . GLY A 234 ? 0.3337 0.2441 0.1890 -0.0515 0.1111  -0.0074 235 GLY A N   
1938 C  CA  . GLY A 234 ? 0.2858 0.2680 0.2488 -0.0734 0.0668  -0.0772 235 GLY A CA  
1939 C  C   . GLY A 234 ? 0.3061 0.3086 0.2178 -0.0874 0.0846  -0.0931 235 GLY A C   
1940 O  O   . GLY A 234 ? 0.3170 0.4754 0.2504 -0.1413 0.1280  -0.1196 235 GLY A O   
1941 N  N   . GLU A 235 ? 0.2249 0.2120 0.2393 -0.0606 0.0912  -0.0511 236 GLU A N   
1942 C  CA  . GLU A 235 ? 0.2723 0.1555 0.2304 -0.0754 0.0357  -0.0386 236 GLU A CA  
1943 C  C   . GLU A 235 ? 0.2520 0.2163 0.2241 -0.0562 0.0976  -0.0790 236 GLU A C   
1944 O  O   . GLU A 235 ? 0.2405 0.2933 0.2426 -0.0394 0.0631  -0.0384 236 GLU A O   
1945 C  CB  . GLU A 235 ? 0.2802 0.1849 0.2195 -0.0395 0.0491  -0.0298 236 GLU A CB  
1946 C  CG  . GLU A 235 ? 0.3194 0.2047 0.3043 -0.0384 0.1356  -0.0593 236 GLU A CG  
1947 C  CD  . GLU A 235 ? 0.5357 0.2003 0.4000 0.0807  0.2381  -0.0454 236 GLU A CD  
1948 O  OE1 . GLU A 235 ? 0.2305 0.2387 0.3226 0.0307  0.0832  -0.0626 236 GLU A OE1 
1949 O  OE2 . GLU A 235 ? 0.5286 0.2793 0.4280 0.1421  0.2326  -0.0044 236 GLU A OE2 
1950 N  N   . PRO A 236 ? 0.1907 0.2263 0.2236 -0.0524 0.0692  -0.0876 237 PRO A N   
1951 C  CA  . PRO A 236 ? 0.2712 0.1918 0.2416 -0.1070 0.1058  -0.0747 237 PRO A CA  
1952 C  C   . PRO A 236 ? 0.2451 0.1819 0.1779 0.0206  0.0829  -0.0026 237 PRO A C   
1953 O  O   . PRO A 236 ? 0.2533 0.1939 0.2246 0.0083  0.1045  0.0170  237 PRO A O   
1954 C  CB  . PRO A 236 ? 0.2583 0.1861 0.2517 -0.0395 0.0803  -0.0687 237 PRO A CB  
1955 C  CG  . PRO A 236 ? 0.2258 0.2702 0.4138 -0.0725 0.1318  -0.1572 237 PRO A CG  
1956 C  CD  . PRO A 236 ? 0.1740 0.2486 0.4347 -0.0467 0.0720  -0.0899 237 PRO A CD  
1957 N  N   . GLU A 237 ? 0.2996 0.1474 0.2407 0.0104  0.0921  0.0021  238 GLU A N   
1958 C  CA  . GLU A 237 ? 0.3294 0.2220 0.1720 0.0015  0.0755  0.0172  238 GLU A CA  
1959 C  C   . GLU A 237 ? 0.2369 0.1561 0.2163 -0.0076 0.0684  -0.0008 238 GLU A C   
1960 O  O   . GLU A 237 ? 0.2269 0.2038 0.1613 -0.0331 0.0322  0.0065  238 GLU A O   
1961 C  CB  . GLU A 237 ? 0.2908 0.1855 0.2497 0.0241  0.0379  0.0326  238 GLU A CB  
1962 C  CG  . GLU A 237 ? 0.3318 0.2976 0.2280 0.0465  0.0553  0.0654  238 GLU A CG  
1963 C  CD  . GLU A 237 ? 0.3334 0.2074 0.2163 -0.0099 0.0035  0.0776  238 GLU A CD  
1964 O  OE1 . GLU A 237 ? 0.4106 0.2447 0.4408 -0.0461 -0.1360 0.0996  238 GLU A OE1 
1965 O  OE2 . GLU A 237 ? 0.3032 0.2032 0.2441 0.0099  0.0617  0.0599  238 GLU A OE2 
1966 N  N   . GLU A 238 ? 0.1974 0.1563 0.1633 0.0313  0.0399  0.0281  239 GLU A N   
1967 C  CA  . GLU A 238 ? 0.1680 0.1966 0.1551 0.0093  0.0443  0.0291  239 GLU A CA  
1968 C  C   . GLU A 238 ? 0.1453 0.1635 0.1218 -0.0275 0.0276  -0.0100 239 GLU A C   
1969 O  O   . GLU A 238 ? 0.2468 0.1420 0.1979 0.0148  0.0688  0.0015  239 GLU A O   
1970 C  CB  . GLU A 238 ? 0.2422 0.2390 0.2060 0.0790  0.0414  0.0127  239 GLU A CB  
1971 C  CG  . GLU A 238 ? 0.2369 0.2012 0.3468 -0.0108 0.0483  0.0461  239 GLU A CG  
1972 C  CD  . GLU A 238 ? 0.4612 0.3765 0.3379 0.2159  0.0335  0.0632  239 GLU A CD  
1973 O  OE1 . GLU A 238 ? 0.5207 0.3291 0.3743 0.1014  0.1057  0.0582  239 GLU A OE1 
1974 O  OE2 . GLU A 238 ? 0.2366 0.4194 0.7408 0.1120  -0.0692 -0.1683 239 GLU A OE2 
1975 N  N   . LEU A 239 ? 0.1993 0.1849 0.1177 0.0449  0.0284  0.0115  240 LEU A N   
1976 C  CA  . LEU A 239 ? 0.1620 0.1535 0.1208 0.0183  0.0373  0.0087  240 LEU A CA  
1977 C  C   . LEU A 239 ? 0.1791 0.1802 0.0816 0.0403  0.0274  -0.0098 240 LEU A C   
1978 O  O   . LEU A 239 ? 0.2117 0.1562 0.1255 0.0274  0.0551  0.0093  240 LEU A O   
1979 C  CB  . LEU A 239 ? 0.2028 0.1272 0.1611 -0.0048 0.0384  0.0093  240 LEU A CB  
1980 C  CG  . LEU A 239 ? 0.1517 0.1605 0.1932 0.0104  0.0082  0.0476  240 LEU A CG  
1981 C  CD1 . LEU A 239 ? 0.3341 0.1227 0.3161 -0.0032 -0.0364 0.0450  240 LEU A CD1 
1982 C  CD2 . LEU A 239 ? 0.2060 0.1577 0.2035 -0.0030 0.0175  0.0269  240 LEU A CD2 
1983 N  N   . MET A 240 ? 0.2049 0.1289 0.1333 0.0052  0.0568  0.0172  241 MET A N   
1984 C  CA  . MET A 240 ? 0.2101 0.1383 0.1124 0.0074  0.0474  0.0010  241 MET A CA  
1985 C  C   . MET A 240 ? 0.1676 0.1301 0.0891 0.0164  0.0115  0.0099  241 MET A C   
1986 O  O   . MET A 240 ? 0.1918 0.1341 0.1103 0.0326  0.0173  0.0000  241 MET A O   
1987 C  CB  . MET A 240 ? 0.2293 0.1263 0.1141 0.0076  0.0390  -0.0104 241 MET A CB  
1988 C  CG  . MET A 240 ? 0.2458 0.1466 0.1148 0.0311  0.0505  0.0082  241 MET A CG  
1989 S  SD  . MET A 240 ? 0.2350 0.1216 0.1562 0.0280  0.0335  -0.0063 241 MET A SD  
1990 C  CE  . MET A 240 ? 0.2099 0.1306 0.1944 0.0164  0.0573  -0.0333 241 MET A CE  
1991 N  N   . VAL A 241 ? 0.2044 0.1085 0.1009 0.0275  0.0318  0.0245  242 VAL A N   
1992 C  CA  . VAL A 241 ? 0.1756 0.1005 0.0961 0.0306  0.0522  0.0136  242 VAL A CA  
1993 C  C   . VAL A 241 ? 0.1657 0.0965 0.1040 0.0271  0.0304  0.0160  242 VAL A C   
1994 O  O   . VAL A 241 ? 0.1702 0.1291 0.1005 0.0241  0.0386  0.0124  242 VAL A O   
1995 C  CB  . VAL A 241 ? 0.1740 0.1099 0.1112 0.0168  0.0373  0.0184  242 VAL A CB  
1996 C  CG1 . VAL A 241 ? 0.2223 0.1362 0.1445 0.0560  0.0337  0.0340  242 VAL A CG1 
1997 C  CG2 . VAL A 241 ? 0.2166 0.1148 0.1351 0.0028  0.0443  0.0269  242 VAL A CG2 
1998 N  N   . ASP A 242 ? 0.1642 0.0965 0.1054 0.0137  0.0313  0.0168  243 ASP A N   
1999 C  CA  . ASP A 242 ? 0.1325 0.0975 0.1036 -0.0068 0.0126  0.0200  243 ASP A CA  
2000 C  C   . ASP A 242 ? 0.1413 0.1085 0.1048 0.0324  0.0296  0.0083  243 ASP A C   
2001 O  O   . ASP A 242 ? 0.1555 0.0966 0.1464 0.0230  0.0188  0.0187  243 ASP A O   
2002 C  CB  . ASP A 242 ? 0.1523 0.1092 0.1177 0.0192  0.0348  0.0164  243 ASP A CB  
2003 C  CG  . ASP A 242 ? 0.1510 0.1046 0.1268 0.0060  0.0256  0.0269  243 ASP A CG  
2004 O  OD1 . ASP A 242 ? 0.1459 0.0913 0.1256 -0.0008 0.0263  0.0127  243 ASP A OD1 
2005 O  OD2 . ASP A 242 ? 0.1691 0.1103 0.1864 0.0092  0.0405  0.0372  243 ASP A OD2 
2006 N  N   . ASN A 243 ? 0.1525 0.0788 0.1036 0.0147  0.0230  0.0119  244 ASN A N   
2007 C  CA  . ASN A 243 ? 0.1483 0.0816 0.1112 0.0162  0.0214  0.0198  244 ASN A CA  
2008 C  C   . ASN A 243 ? 0.1191 0.0771 0.1049 0.0132  0.0221  0.0041  244 ASN A C   
2009 O  O   . ASN A 243 ? 0.1484 0.0992 0.1037 -0.0062 0.0190  0.0024  244 ASN A O   
2010 C  CB  . ASN A 243 ? 0.1605 0.0920 0.1030 0.0185  0.0232  -0.0015 244 ASN A CB  
2011 C  CG  . ASN A 243 ? 0.1509 0.0916 0.1054 0.0434  0.0176  0.0076  244 ASN A CG  
2012 O  OD1 . ASN A 243 ? 0.1293 0.1032 0.1444 0.0207  0.0114  -0.0214 244 ASN A OD1 
2013 N  ND2 . ASN A 243 ? 0.2116 0.1676 0.1567 0.0586  -0.0132 -0.0665 244 ASN A ND2 
2014 N  N   . TRP A 244 ? 0.1150 0.0838 0.0960 0.0027  0.0071  0.0168  245 TRP A N   
2015 C  CA  . TRP A 244 ? 0.1062 0.0930 0.0900 -0.0024 0.0118  0.0122  245 TRP A CA  
2016 C  C   . TRP A 244 ? 0.1094 0.0776 0.1089 0.0037  0.0238  0.0080  245 TRP A C   
2017 O  O   . TRP A 244 ? 0.1208 0.1070 0.1327 -0.0153 0.0100  0.0271  245 TRP A O   
2018 C  CB  . TRP A 244 ? 0.1027 0.0863 0.0962 0.0082  0.0225  0.0076  245 TRP A CB  
2019 C  CG  . TRP A 244 ? 0.0945 0.0820 0.0966 0.0048  0.0076  0.0060  245 TRP A CG  
2020 C  CD1 . TRP A 244 ? 0.1105 0.0926 0.0995 0.0082  0.0256  0.0088  245 TRP A CD1 
2021 C  CD2 . TRP A 244 ? 0.1064 0.0898 0.1058 0.0057  0.0163  0.0059  245 TRP A CD2 
2022 N  NE1 . TRP A 244 ? 0.1268 0.0894 0.1061 0.0078  0.0216  0.0087  245 TRP A NE1 
2023 C  CE2 . TRP A 244 ? 0.1196 0.0907 0.1253 0.0027  0.0130  0.0040  245 TRP A CE2 
2024 C  CE3 . TRP A 244 ? 0.1254 0.1063 0.1178 0.0070  0.0162  0.0024  245 TRP A CE3 
2025 C  CZ2 . TRP A 244 ? 0.1462 0.1014 0.1391 0.0000  0.0190  0.0015  245 TRP A CZ2 
2026 C  CZ3 . TRP A 244 ? 0.1554 0.1092 0.1511 -0.0083 0.0087  0.0076  245 TRP A CZ3 
2027 C  CH2 . TRP A 244 ? 0.1350 0.1159 0.1451 -0.0097 0.0012  0.0055  245 TRP A CH2 
2028 N  N   . ARG A 245 ? 0.0943 0.0888 0.1049 0.0013  0.0092  0.0209  246 ARG A N   
2029 C  CA  . ARG A 245 ? 0.0732 0.0995 0.1045 0.0005  0.0065  0.0141  246 ARG A CA  
2030 C  C   . ARG A 245 ? 0.0750 0.0945 0.1041 -0.0031 -0.0048 0.0288  246 ARG A C   
2031 O  O   . ARG A 245 ? 0.0842 0.1062 0.1171 -0.0003 -0.0010 0.0142  246 ARG A O   
2032 C  CB  . ARG A 245 ? 0.0799 0.0970 0.1206 0.0013  0.0070  0.0185  246 ARG A CB  
2033 C  CG  . ARG A 245 ? 0.0749 0.1024 0.1427 0.0065  0.0099  0.0208  246 ARG A CG  
2034 C  CD  . ARG A 245 ? 0.0643 0.1136 0.1418 0.0160  -0.0006 0.0281  246 ARG A CD  
2035 N  NE  . ARG A 245 ? 0.0720 0.1121 0.1526 0.0168  0.0115  0.0310  246 ARG A NE  
2036 C  CZ  . ARG A 245 ? 0.0816 0.1084 0.1352 0.0204  0.0082  0.0097  246 ARG A CZ  
2037 N  NH1 . ARG A 245 ? 0.1009 0.1154 0.1437 0.0188  0.0082  0.0231  246 ARG A NH1 
2038 N  NH2 . ARG A 245 ? 0.0833 0.1438 0.1712 0.0302  0.0089  0.0274  246 ARG A NH2 
2039 N  N   A PRO A 246 ? 0.0987 0.1026 0.1195 -0.0081 0.0041  0.0003  247 PRO A N   
2040 N  N   B PRO A 246 ? 0.1032 0.1077 0.1202 -0.0059 0.0010  -0.0010 247 PRO A N   
2041 C  CA  A PRO A 246 ? 0.1124 0.0942 0.1112 -0.0132 0.0051  0.0057  247 PRO A CA  
2042 C  CA  B PRO A 246 ? 0.1154 0.1002 0.1123 -0.0120 0.0065  0.0030  247 PRO A CA  
2043 C  C   A PRO A 246 ? 0.1098 0.0905 0.1014 -0.0074 -0.0060 0.0003  247 PRO A C   
2044 C  C   B PRO A 246 ? 0.1146 0.0927 0.1008 -0.0060 -0.0140 0.0000  247 PRO A C   
2045 O  O   A PRO A 246 ? 0.0960 0.1017 0.1093 -0.0065 -0.0031 0.0043  247 PRO A O   
2046 O  O   B PRO A 246 ? 0.1037 0.1042 0.1127 -0.0017 -0.0024 0.0071  247 PRO A O   
2047 C  CB  A PRO A 246 ? 0.1466 0.1309 0.1342 -0.0478 0.0142  -0.0086 247 PRO A CB  
2048 C  CB  B PRO A 246 ? 0.1569 0.1342 0.1647 -0.0467 -0.0023 0.0026  247 PRO A CB  
2049 C  CG  A PRO A 246 ? 0.1318 0.1670 0.1529 -0.0696 0.0460  -0.0309 247 PRO A CG  
2050 C  CG  B PRO A 246 ? 0.1422 0.1852 0.2296 -0.0564 0.0065  -0.0454 247 PRO A CG  
2051 C  CD  A PRO A 246 ? 0.0947 0.1328 0.1711 -0.0222 0.0120  -0.0162 247 PRO A CD  
2052 C  CD  B PRO A 246 ? 0.1096 0.1485 0.1838 -0.0373 0.0094  -0.0136 247 PRO A CD  
2053 N  N   . ALA A 247 ? 0.1083 0.1028 0.1089 -0.0135 -0.0001 0.0012  248 ALA A N   
2054 C  CA  . ALA A 247 ? 0.1062 0.0979 0.1175 -0.0154 -0.0085 -0.0001 248 ALA A CA  
2055 C  C   . ALA A 247 ? 0.0970 0.1084 0.1106 -0.0206 -0.0077 -0.0017 248 ALA A C   
2056 O  O   . ALA A 247 ? 0.1162 0.1341 0.1423 -0.0417 -0.0210 0.0019  248 ALA A O   
2057 C  CB  . ALA A 247 ? 0.1513 0.1394 0.1141 0.0001  0.0148  0.0000  248 ALA A CB  
2058 N  N   . GLN A 248 ? 0.0967 0.1036 0.1222 -0.0055 -0.0113 0.0003  249 GLN A N   
2059 C  CA  . GLN A 248 ? 0.0921 0.1277 0.1325 -0.0209 -0.0119 0.0017  249 GLN A CA  
2060 C  C   . GLN A 248 ? 0.0872 0.1233 0.1421 -0.0137 -0.0229 -0.0190 249 GLN A C   
2061 O  O   . GLN A 248 ? 0.1186 0.1245 0.1316 -0.0109 -0.0035 -0.0102 249 GLN A O   
2062 C  CB  . GLN A 248 ? 0.1125 0.1215 0.1354 0.0015  -0.0244 0.0120  249 GLN A CB  
2063 C  CG  . GLN A 248 ? 0.1173 0.1243 0.1238 0.0127  -0.0250 -0.0109 249 GLN A CG  
2064 C  CD  . GLN A 248 ? 0.1058 0.1618 0.1521 0.0094  -0.0157 -0.0093 249 GLN A CD  
2065 O  OE1 . GLN A 248 ? 0.1058 0.2164 0.1964 0.0271  -0.0080 0.0430  249 GLN A OE1 
2066 N  NE2 . GLN A 248 ? 0.1515 0.1583 0.1519 -0.0028 -0.0129 0.0151  249 GLN A NE2 
2067 N  N   . PRO A 249 ? 0.1220 0.1571 0.1445 -0.0315 -0.0322 0.0094  250 PRO A N   
2068 C  CA  . PRO A 249 ? 0.1636 0.2000 0.1393 -0.0714 -0.0313 0.0035  250 PRO A CA  
2069 C  C   . PRO A 249 ? 0.1449 0.1460 0.1263 -0.0266 -0.0441 -0.0032 250 PRO A C   
2070 O  O   . PRO A 249 ? 0.1350 0.1537 0.1374 -0.0339 -0.0304 -0.0097 250 PRO A O   
2071 C  CB  . PRO A 249 ? 0.1404 0.2772 0.1726 -0.0838 -0.0581 0.0313  250 PRO A CB  
2072 C  CG  . PRO A 249 ? 0.1712 0.2980 0.1673 -0.0653 -0.0595 0.0189  250 PRO A CG  
2073 C  CD  . PRO A 249 ? 0.1245 0.2450 0.1727 -0.0582 -0.0579 0.0496  250 PRO A CD  
2074 N  N   . LEU A 250 ? 0.1676 0.1498 0.1234 -0.0483 -0.0219 -0.0093 251 LEU A N   
2075 C  CA  . LEU A 250 ? 0.1684 0.1202 0.1137 -0.0215 -0.0131 0.0020  251 LEU A CA  
2076 C  C   . LEU A 250 ? 0.1303 0.1234 0.1377 -0.0218 -0.0270 -0.0105 251 LEU A C   
2077 O  O   . LEU A 250 ? 0.1509 0.1313 0.1289 -0.0200 -0.0337 0.0063  251 LEU A O   
2078 C  CB  . LEU A 250 ? 0.2035 0.1271 0.1312 -0.0159 -0.0066 -0.0151 251 LEU A CB  
2079 C  CG  . LEU A 250 ? 0.2137 0.1513 0.1402 0.0157  0.0408  0.0201  251 LEU A CG  
2080 C  CD1 . LEU A 250 ? 0.1665 0.1886 0.1359 0.0215  -0.0027 0.0113  251 LEU A CD1 
2081 C  CD2 . LEU A 250 ? 0.2599 0.1859 0.1876 0.0282  0.0515  0.0187  251 LEU A CD2 
2082 N  N   A LYS A 251 ? 0.1831 0.1670 0.1218 -0.0456 -0.0538 0.0109  252 LYS A N   
2083 N  N   B LYS A 251 ? 0.1850 0.1713 0.1193 -0.0458 -0.0542 0.0098  252 LYS A N   
2084 C  CA  A LYS A 251 ? 0.1733 0.1920 0.1421 -0.0575 -0.0527 0.0225  252 LYS A CA  
2085 C  CA  B LYS A 251 ? 0.1761 0.1990 0.1480 -0.0553 -0.0507 0.0269  252 LYS A CA  
2086 C  C   A LYS A 251 ? 0.1805 0.1842 0.1474 -0.0237 -0.0438 0.0195  252 LYS A C   
2087 C  C   B LYS A 251 ? 0.1797 0.1856 0.1546 -0.0232 -0.0432 0.0186  252 LYS A C   
2088 O  O   A LYS A 251 ? 0.2254 0.2046 0.1642 -0.0010 0.0000  0.0184  252 LYS A O   
2089 O  O   B LYS A 251 ? 0.2234 0.2079 0.1615 -0.0035 -0.0030 0.0125  252 LYS A O   
2090 C  CB  A LYS A 251 ? 0.2141 0.1941 0.1771 -0.0092 -0.0566 0.0412  252 LYS A CB  
2091 C  CB  B LYS A 251 ? 0.2161 0.1961 0.1744 -0.0097 -0.0573 0.0471  252 LYS A CB  
2092 C  CG  A LYS A 251 ? 0.2314 0.2429 0.2250 -0.0313 -0.0432 0.0505  252 LYS A CG  
2093 C  CG  B LYS A 251 ? 0.2531 0.2326 0.2282 -0.0304 -0.0285 0.0522  252 LYS A CG  
2094 C  CD  A LYS A 251 ? 0.2282 0.3118 0.2666 -0.0710 0.0051  -0.0140 252 LYS A CD  
2095 C  CD  B LYS A 251 ? 0.2509 0.3212 0.2551 -0.0434 -0.0208 -0.0274 252 LYS A CD  
2096 C  CE  A LYS A 251 ? 0.2078 0.3030 0.3982 -0.0722 0.0231  -0.0386 252 LYS A CE  
2097 C  CE  B LYS A 251 ? 0.2953 0.3230 0.3867 -0.0927 -0.0015 0.0091  252 LYS A CE  
2098 N  NZ  A LYS A 251 ? 0.2437 0.2967 0.2490 -0.0838 -0.0035 -0.0320 252 LYS A NZ  
2099 N  NZ  B LYS A 251 ? 0.4223 0.2908 0.4489 -0.0149 0.0914  -0.1847 252 LYS A NZ  
2100 N  N   . ASN A 252 ? 0.1912 0.1923 0.1448 -0.0315 -0.0452 0.0432  253 ASN A N   
2101 C  CA  . ASN A 252 ? 0.2017 0.3330 0.2047 -0.0741 -0.0476 0.0979  253 ASN A CA  
2102 C  C   . ASN A 252 ? 0.2188 0.2833 0.2397 -0.0542 -0.0698 0.0423  253 ASN A C   
2103 O  O   . ASN A 252 ? 0.2910 0.2703 0.2691 -0.0812 -0.0194 0.0636  253 ASN A O   
2104 C  CB  . ASN A 252 ? 0.2125 0.3966 0.3064 -0.0483 -0.0830 0.1801  253 ASN A CB  
2105 C  CG  . ASN A 252 ? 0.3188 0.3614 0.3228 -0.1138 -0.0116 0.1085  253 ASN A CG  
2106 O  OD1 . ASN A 252 ? 0.6772 0.7142 0.4666 -0.0120 0.0764  -0.1177 253 ASN A OD1 
2107 N  ND2 . ASN A 252 ? 0.3889 0.3088 0.3662 -0.0746 -0.0588 0.0942  253 ASN A ND2 
2108 N  N   . ARG A 253 ? 0.1523 0.2815 0.1023 -0.0395 -0.0077 -0.0161 254 ARG A N   
2109 C  CA  . ARG A 253 ? 0.1542 0.1588 0.1085 -0.0337 -0.0174 0.0088  254 ARG A CA  
2110 C  C   . ARG A 253 ? 0.1832 0.1659 0.1133 -0.0227 0.0086  0.0208  254 ARG A C   
2111 O  O   . ARG A 253 ? 0.2408 0.1826 0.2786 -0.0687 0.0842  -0.0592 254 ARG A O   
2112 C  CB  . ARG A 253 ? 0.1700 0.1389 0.0904 -0.0305 -0.0031 0.0057  254 ARG A CB  
2113 C  CG  . ARG A 253 ? 0.1667 0.1296 0.0886 -0.0131 -0.0006 0.0153  254 ARG A CG  
2114 C  CD  . ARG A 253 ? 0.1362 0.1238 0.0992 -0.0171 -0.0070 0.0049  254 ARG A CD  
2115 N  NE  . ARG A 253 ? 0.1275 0.1222 0.0982 -0.0218 -0.0217 0.0030  254 ARG A NE  
2116 C  CZ  . ARG A 253 ? 0.1068 0.1035 0.0948 0.0038  -0.0151 -0.0013 254 ARG A CZ  
2117 N  NH1 . ARG A 253 ? 0.0842 0.1132 0.1066 0.0021  -0.0272 -0.0024 254 ARG A NH1 
2118 N  NH2 . ARG A 253 ? 0.1071 0.1071 0.1049 -0.0132 -0.0282 0.0085  254 ARG A NH2 
2119 N  N   . GLN A 254 ? 0.1513 0.1627 0.1287 -0.0216 -0.0119 0.0441  255 GLN A N   
2120 C  CA  . GLN A 254 ? 0.1949 0.2215 0.1121 0.0000  -0.0114 0.0285  255 GLN A CA  
2121 C  C   . GLN A 254 ? 0.1612 0.1665 0.1211 0.0017  -0.0099 -0.0087 255 GLN A C   
2122 O  O   . GLN A 254 ? 0.2082 0.1588 0.1941 0.0082  -0.0606 -0.0092 255 GLN A O   
2123 C  CB  . GLN A 254 ? 0.1935 0.3612 0.1439 -0.0027 0.0065  0.0851  255 GLN A CB  
2124 C  CG  . GLN A 254 ? 0.3106 0.5691 0.2411 0.0434  0.0822  0.0612  255 GLN A CG  
2125 C  CD  . GLN A 254 ? 0.5120 0.9602 0.6112 -0.2339 0.1990  -0.3822 255 GLN A CD  
2126 O  OE1 . GLN A 254 ? 0.5727 1.0192 0.3197 -0.1738 -0.1893 0.0450  255 GLN A OE1 
2127 N  NE2 . GLN A 254 ? 1.9153 0.9089 2.0576 -0.4117 1.6821  -0.6445 255 GLN A NE2 
2128 N  N   . ILE A 255 ? 0.1361 0.1406 0.1103 -0.0051 -0.0003 -0.0038 256 ILE A N   
2129 C  CA  . ILE A 255 ? 0.1359 0.1411 0.0865 -0.0164 0.0066  -0.0147 256 ILE A CA  
2130 C  C   . ILE A 255 ? 0.1484 0.1186 0.1010 -0.0163 0.0065  -0.0171 256 ILE A C   
2131 O  O   . ILE A 255 ? 0.1617 0.1490 0.1280 -0.0267 0.0223  -0.0434 256 ILE A O   
2132 C  CB  . ILE A 255 ? 0.1308 0.1178 0.1303 -0.0126 -0.0054 -0.0109 256 ILE A CB  
2133 C  CG1 . ILE A 255 ? 0.1296 0.1344 0.1277 -0.0225 0.0008  0.0024  256 ILE A CG1 
2134 C  CG2 . ILE A 255 ? 0.1341 0.1747 0.1247 0.0105  -0.0076 -0.0026 256 ILE A CG2 
2135 C  CD1 . ILE A 255 ? 0.1647 0.1397 0.1449 -0.0135 0.0282  0.0020  256 ILE A CD1 
2136 N  N   . LYS A 256 ? 0.1272 0.1481 0.0860 -0.0031 0.0003  -0.0146 257 LYS A N   
2137 C  CA  . LYS A 256 ? 0.1412 0.1504 0.0899 -0.0086 0.0274  -0.0300 257 LYS A CA  
2138 C  C   . LYS A 256 ? 0.1279 0.1455 0.0914 0.0006  0.0181  -0.0125 257 LYS A C   
2139 O  O   . LYS A 256 ? 0.1520 0.1849 0.0926 0.0381  0.0208  -0.0054 257 LYS A O   
2140 C  CB  . LYS A 256 ? 0.1606 0.1445 0.1243 -0.0086 0.0216  0.0131  257 LYS A CB  
2141 C  CG  . LYS A 256 ? 0.2418 0.2052 0.1899 0.0297  0.0098  0.0275  257 LYS A CG  
2142 C  CD  . LYS A 256 ? 0.4282 0.1909 0.2921 -0.0131 -0.0920 0.0252  257 LYS A CD  
2143 C  CE  . LYS A 256 ? 0.5016 0.4541 0.3569 0.1402  -0.0078 0.2362  257 LYS A CE  
2144 N  NZ  . LYS A 256 ? 0.3470 0.4257 0.6786 0.0953  0.2091  0.2117  257 LYS A NZ  
2145 N  N   . ALA A 257 ? 0.1155 0.1737 0.0938 0.0001  0.0297  -0.0046 258 ALA A N   
2146 C  CA  . ALA A 257 ? 0.0984 0.1664 0.1289 -0.0008 0.0003  -0.0274 258 ALA A CA  
2147 C  C   . ALA A 257 ? 0.1200 0.1555 0.1242 0.0125  0.0027  -0.0082 258 ALA A C   
2148 O  O   . ALA A 257 ? 0.1365 0.1939 0.1103 -0.0063 0.0331  0.0038  258 ALA A O   
2149 C  CB  . ALA A 257 ? 0.1441 0.1543 0.1695 0.0263  0.0043  -0.0226 258 ALA A CB  
2150 N  N   . SER A 258 ? 0.1071 0.1414 0.1306 0.0068  0.0175  -0.0115 259 SER A N   
2151 C  CA  . SER A 258 ? 0.1250 0.2000 0.1492 -0.0008 0.0340  -0.0129 259 SER A CA  
2152 C  C   . SER A 258 ? 0.0961 0.2138 0.1798 0.0049  0.0513  -0.0052 259 SER A C   
2153 O  O   . SER A 258 ? 0.1387 0.3129 0.1897 -0.0100 0.0546  -0.0164 259 SER A O   
2154 C  CB  . SER A 258 ? 0.1350 0.1752 0.1594 0.0000  -0.0165 -0.0020 259 SER A CB  
2155 O  OG  . SER A 258 ? 0.1123 0.1881 0.1407 -0.0043 0.0238  -0.0065 259 SER A OG  
2156 N  N   . PHE A 259 ? 0.1542 0.2014 0.1846 0.0255  0.0526  -0.0181 260 PHE A N   
2157 C  CA  . PHE A 259 ? 0.2117 0.2035 0.1966 0.0491  0.0833  -0.0260 260 PHE A CA  
2158 C  C   . PHE A 259 ? 0.2328 0.2651 0.2419 0.0399  0.0634  -0.0417 260 PHE A C   
2159 O  O   . PHE A 259 ? 0.3107 0.2308 0.2249 0.0368  0.0379  -0.0885 260 PHE A O   
2160 C  CB  . PHE A 259 ? 0.1746 0.2259 0.2246 0.0226  0.0586  0.0127  260 PHE A CB  
2161 C  CG  . PHE A 259 ? 0.1621 0.1708 0.2004 0.0359  0.0024  -0.0252 260 PHE A CG  
2162 C  CD1 . PHE A 259 ? 0.1737 0.1518 0.1763 0.0348  -0.0013 -0.0027 260 PHE A CD1 
2163 C  CD2 . PHE A 259 ? 0.2477 0.1739 0.3082 0.0337  0.0593  -0.0329 260 PHE A CD2 
2164 C  CE1 . PHE A 259 ? 0.1668 0.1846 0.1881 0.0149  0.0024  0.0027  260 PHE A CE1 
2165 C  CE2 . PHE A 259 ? 0.2459 0.1861 0.2962 0.0093  0.0085  -0.0454 260 PHE A CE2 
2166 C  CZ  . PHE A 259 ? 0.2118 0.1713 0.2700 0.0309  0.0000  0.0071  260 PHE A CZ  
2167 N  N   . LYS A 260 ? 0.3465 0.5153 0.3957 0.1102  0.1162  -0.2381 261 LYS A N   
2168 C  CA  . LYS A 260 ? 0.7400 0.4219 0.9176 0.0621  -0.0421 -0.3603 261 LYS A CA  
2169 C  C   . LYS A 260 ? 1.6258 0.9700 1.2462 0.6115  -0.9987 -0.5195 261 LYS A C   
2170 O  O   . LYS A 260 ? 1.1585 1.0569 1.5762 0.6854  -0.9821 -0.6646 261 LYS A O   
2171 C  CB  . LYS A 260 ? 0.6633 0.4059 0.4918 0.1713  -0.0364 -0.2286 261 LYS A CB  
2172 C  CG  . LYS A 260 ? 0.5126 0.3248 0.6025 0.2234  0.1347  0.0104  261 LYS A CG  
2173 O  OXT . LYS A 260 ? 1.9347 1.4198 1.9193 0.9560  -1.6930 -1.2331 261 LYS A OXT 
2174 N  N   . HIS B 3   ? 0.2691 0.4544 0.2050 0.0529  -0.0190 0.0051  3   HIS B N   
2175 C  CA  . HIS B 3   ? 0.2689 0.4296 0.2544 -0.0063 -0.0688 0.0644  3   HIS B CA  
2176 C  C   . HIS B 3   ? 0.3657 0.4327 0.3653 0.1544  -0.0120 0.0662  3   HIS B C   
2177 O  O   . HIS B 3   ? 0.5012 0.5358 0.4104 -0.0675 -0.2037 -0.0322 3   HIS B O   
2178 C  CB  . HIS B 3   ? 0.3248 0.3208 0.4769 -0.0537 -0.1260 0.1291  3   HIS B CB  
2179 C  CG  . HIS B 3   ? 0.3009 0.3864 0.5077 -0.1754 -0.1626 0.1662  3   HIS B CG  
2180 N  ND1 . HIS B 3   ? 0.5468 0.5372 0.4467 -0.2578 -0.1668 0.2987  3   HIS B ND1 
2181 C  CD2 . HIS B 3   ? 0.2213 0.4092 0.4821 -0.0864 -0.0560 0.0130  3   HIS B CD2 
2182 C  CE1 . HIS B 3   ? 0.3562 0.4023 0.4079 -0.1526 -0.0108 0.0922  3   HIS B CE1 
2183 N  NE2 . HIS B 3   ? 0.4404 0.5088 0.6137 -0.1597 0.2508  0.0283  3   HIS B NE2 
2184 N  N   . HIS B 4   ? 0.2590 0.4066 0.3237 0.0308  0.0825  0.1642  4   HIS B N   
2185 C  CA  . HIS B 4   ? 0.4733 0.2973 0.8288 0.0275  0.4499  0.1969  4   HIS B CA  
2186 C  C   . HIS B 4   ? 0.2231 0.2714 0.2820 -0.0544 0.0612  0.0535  4   HIS B C   
2187 O  O   . HIS B 4   ? 0.2124 0.2908 0.2890 -0.0372 0.0727  0.0239  4   HIS B O   
2188 C  CB  . HIS B 4   ? 0.4968 1.1263 1.4437 0.4806  0.4550  0.5939  4   HIS B CB  
2189 C  CG  . HIS B 4   ? 0.2960 1.3858 1.9997 0.2996  0.3210  0.8848  4   HIS B CG  
2190 N  ND1 . HIS B 4   ? 0.4063 1.7867 2.4168 -0.2099 0.1811  -0.2167 4   HIS B ND1 
2191 C  CD2 . HIS B 4   ? 0.5715 1.0713 2.0913 0.3907  -0.2293 0.7799  4   HIS B CD2 
2192 C  CE1 . HIS B 4   ? 0.5573 1.4092 2.2396 0.2716  0.1255  0.0010  4   HIS B CE1 
2193 N  NE2 . HIS B 4   ? 0.5845 1.7796 2.2053 0.3481  -0.4611 0.5113  4   HIS B NE2 
2194 N  N   . TRP B 5   ? 0.2556 0.2477 0.3222 -0.0577 0.1174  0.0296  5   TRP B N   
2195 C  CA  . TRP B 5   ? 0.1635 0.1696 0.2734 -0.0221 0.0756  0.0241  5   TRP B CA  
2196 C  C   . TRP B 5   ? 0.1968 0.1889 0.2439 -0.0105 0.1184  0.0052  5   TRP B C   
2197 O  O   . TRP B 5   ? 0.2299 0.1993 0.2407 -0.0351 0.0812  0.0068  5   TRP B O   
2198 C  CB  . TRP B 5   ? 0.1587 0.1758 0.2536 -0.0074 0.0454  0.0054  5   TRP B CB  
2199 C  CG  . TRP B 5   ? 0.1748 0.1754 0.1978 -0.0302 0.0557  0.0179  5   TRP B CG  
2200 C  CD1 . TRP B 5   ? 0.2090 0.1879 0.2067 0.0000  0.0599  0.0317  5   TRP B CD1 
2201 C  CD2 . TRP B 5   ? 0.1685 0.1956 0.1564 -0.0093 0.0381  -0.0013 5   TRP B CD2 
2202 N  NE1 . TRP B 5   ? 0.2153 0.1952 0.1905 0.0010  0.0379  0.0185  5   TRP B NE1 
2203 C  CE2 . TRP B 5   ? 0.2184 0.2019 0.1814 0.0149  0.0351  0.0206  5   TRP B CE2 
2204 C  CE3 . TRP B 5   ? 0.1535 0.1975 0.1843 -0.0227 0.0465  -0.0300 5   TRP B CE3 
2205 C  CZ2 . TRP B 5   ? 0.2369 0.2653 0.1398 0.0233  0.0027  0.0083  5   TRP B CZ2 
2206 C  CZ3 . TRP B 5   ? 0.1598 0.2317 0.1544 -0.0027 0.0379  -0.0379 5   TRP B CZ3 
2207 C  CH2 . TRP B 5   ? 0.1762 0.2506 0.1939 0.0151  -0.0068 -0.0675 5   TRP B CH2 
2208 N  N   . GLY B 6   ? 0.1688 0.1551 0.2339 -0.0104 0.0825  -0.0087 6   GLY B N   
2209 C  CA  . GLY B 6   ? 0.2030 0.1432 0.2304 -0.0364 0.0807  -0.0204 6   GLY B CA  
2210 C  C   . GLY B 6   ? 0.1844 0.1386 0.2488 -0.0020 0.0970  -0.0034 6   GLY B C   
2211 O  O   . GLY B 6   ? 0.1562 0.1662 0.2311 0.0264  0.0749  0.0241  6   GLY B O   
2212 N  N   A TYR B 7   ? 0.1236 0.1293 0.3260 0.0263  0.1013  -0.0300 7   TYR B N   
2213 N  N   B TYR B 7   ? 0.1152 0.1288 0.1847 0.0395  0.0542  0.0295  7   TYR B N   
2214 C  CA  A TYR B 7   ? 0.1383 0.1367 0.2154 -0.0344 0.0041  -0.0489 7   TYR B CA  
2215 C  CA  B TYR B 7   ? 0.1013 0.1251 0.1658 -0.0082 -0.0015 -0.0083 7   TYR B CA  
2216 C  C   A TYR B 7   ? 0.0956 0.1798 0.2574 -0.0240 0.0102  -0.0737 7   TYR B C   
2217 C  C   B TYR B 7   ? 0.1112 0.1193 0.2369 -0.0120 0.0186  0.0034  7   TYR B C   
2218 O  O   A TYR B 7   ? 0.1108 0.1613 0.3914 -0.0313 0.0516  -0.0870 7   TYR B O   
2219 O  O   B TYR B 7   ? 0.1157 0.1128 0.4268 0.0110  0.0494  -0.0104 7   TYR B O   
2220 C  CB  A TYR B 7   ? 0.1071 0.1993 0.2037 0.0172  0.0071  -0.0535 7   TYR B CB  
2221 C  CB  B TYR B 7   ? 0.1015 0.1080 0.1583 -0.0111 0.0121  -0.0113 7   TYR B CB  
2222 C  CG  A TYR B 7   ? 0.1240 0.1523 0.1098 0.0003  -0.0153 -0.0516 7   TYR B CG  
2223 C  CG  B TYR B 7   ? 0.0847 0.1218 0.0938 -0.0041 0.0026  0.0082  7   TYR B CG  
2224 C  CD1 A TYR B 7   ? 0.1439 0.1386 0.1295 0.0063  0.0027  -0.0263 7   TYR B CD1 
2225 C  CD1 B TYR B 7   ? 0.1087 0.1211 0.0992 -0.0166 0.0242  -0.0021 7   TYR B CD1 
2226 C  CD2 A TYR B 7   ? 0.1563 0.1752 0.1245 0.0028  0.0212  -0.0243 7   TYR B CD2 
2227 C  CD2 B TYR B 7   ? 0.1054 0.0958 0.1284 -0.0107 -0.0060 0.0140  7   TYR B CD2 
2228 C  CE1 A TYR B 7   ? 0.0923 0.1130 0.1782 -0.0244 0.0097  -0.0243 7   TYR B CE1 
2229 C  CE1 B TYR B 7   ? 0.1063 0.1115 0.0860 -0.0104 0.0089  0.0003  7   TYR B CE1 
2230 C  CE2 A TYR B 7   ? 0.1611 0.1471 0.1280 -0.0104 0.0228  -0.0077 7   TYR B CE2 
2231 C  CE2 B TYR B 7   ? 0.1108 0.1304 0.1272 -0.0087 0.0227  0.0144  7   TYR B CE2 
2232 C  CZ  A TYR B 7   ? 0.1150 0.1240 0.1398 -0.0172 0.0254  -0.0379 7   TYR B CZ  
2233 C  CZ  B TYR B 7   ? 0.0920 0.1152 0.1372 0.0003  0.0170  0.0023  7   TYR B CZ  
2234 O  OH  A TYR B 7   ? 0.1466 0.1157 0.1146 -0.0062 0.0303  -0.0164 7   TYR B OH  
2235 O  OH  B TYR B 7   ? 0.1236 0.1287 0.1556 0.0142  -0.0006 -0.0179 7   TYR B OH  
2236 N  N   A GLY B 8   ? 0.1489 0.1517 0.2298 0.0200  0.0357  -0.0071 8   GLY B N   
2237 N  N   B GLY B 8   ? 0.1031 0.1266 0.2046 0.0017  0.0245  0.0059  8   GLY B N   
2238 C  CA  A GLY B 8   ? 0.1220 0.1468 0.2330 -0.0015 0.0394  -0.0043 8   GLY B CA  
2239 C  CA  B GLY B 8   ? 0.1529 0.1309 0.2452 0.0309  -0.0154 -0.0115 8   GLY B CA  
2240 C  C   A GLY B 8   ? 0.0715 0.2304 0.2407 -0.0384 0.0070  -0.0724 8   GLY B C   
2241 C  C   B GLY B 8   ? 0.1816 0.2038 0.1344 0.0467  -0.0348 -0.0684 8   GLY B C   
2242 O  O   A GLY B 8   ? 0.2048 0.1893 0.2833 -0.0892 0.1697  -0.1041 8   GLY B O   
2243 O  O   B GLY B 8   ? 0.1439 0.1553 0.1474 0.0377  0.0093  -0.0326 8   GLY B O   
2244 N  N   A LYS B 9   ? 0.1683 0.1756 0.2777 -0.0141 -0.0027 -0.0434 9   LYS B N   
2245 N  N   B LYS B 9   ? 0.1465 0.1395 0.1400 0.0148  -0.0054 -0.0197 9   LYS B N   
2246 C  CA  A LYS B 9   ? 0.1310 0.2074 0.2935 -0.0414 0.0043  -0.0109 9   LYS B CA  
2247 C  CA  B LYS B 9   ? 0.1385 0.2149 0.1447 0.0318  -0.0353 -0.0445 9   LYS B CA  
2248 C  C   A LYS B 9   ? 0.1404 0.1500 0.2299 -0.0177 0.0252  -0.0087 9   LYS B C   
2249 C  C   B LYS B 9   ? 0.1880 0.1767 0.1190 -0.0187 -0.0051 0.0091  9   LYS B C   
2250 O  O   A LYS B 9   ? 0.1292 0.2770 0.2552 -0.0305 0.0555  -0.0474 9   LYS B O   
2251 O  O   B LYS B 9   ? 0.1284 0.2075 0.1493 -0.0037 0.0008  -0.0152 9   LYS B O   
2252 C  CB  A LYS B 9   ? 0.2145 0.1191 0.3953 -0.0189 0.0120  0.0320  9   LYS B CB  
2253 C  CB  B LYS B 9   ? 0.1987 0.2097 0.1669 0.0706  -0.0662 -0.0483 9   LYS B CB  
2254 C  CG  A LYS B 9   ? 0.2114 0.2072 0.4481 0.0604  0.0384  0.0661  9   LYS B CG  
2255 C  CG  B LYS B 9   ? 0.3280 0.1807 0.2405 0.0384  -0.0342 -0.1437 9   LYS B CG  
2256 N  N   A HIS B 10  ? 0.1042 0.1647 0.1871 0.0198  0.0233  -0.0296 10  HIS B N   
2257 N  N   B HIS B 10  ? 0.1013 0.1683 0.1800 0.0034  0.0027  0.0052  10  HIS B N   
2258 C  CA  A HIS B 10  ? 0.1010 0.1908 0.1787 0.0032  0.0296  -0.0373 10  HIS B CA  
2259 C  CA  B HIS B 10  ? 0.0718 0.2046 0.1378 0.0183  -0.0201 -0.0143 10  HIS B CA  
2260 C  C   A HIS B 10  ? 0.1845 0.1529 0.1555 -0.0174 0.0641  -0.0264 10  HIS B C   
2261 C  C   B HIS B 10  ? 0.0703 0.2267 0.1671 0.0318  -0.0406 -0.0643 10  HIS B C   
2262 O  O   A HIS B 10  ? 0.1279 0.2127 0.2061 0.0285  -0.0006 -0.0487 10  HIS B O   
2263 O  O   B HIS B 10  ? 0.0323 0.2544 0.2392 0.0169  -0.0381 -0.1240 10  HIS B O   
2264 C  CB  A HIS B 10  ? 0.0544 0.2194 0.2188 0.0099  0.0220  -0.0132 10  HIS B CB  
2265 C  CB  B HIS B 10  ? 0.0320 0.2439 0.2181 0.0143  0.0078  -0.0640 10  HIS B CB  
2266 C  CG  A HIS B 10  ? 0.0891 0.2310 0.1557 0.0012  0.0217  -0.0344 10  HIS B CG  
2267 C  CG  B HIS B 10  ? 0.1028 0.1943 0.1510 -0.0098 0.0232  -0.0461 10  HIS B CG  
2268 N  ND1 A HIS B 10  ? 0.0925 0.1752 0.2321 0.0097  0.0131  -0.0449 10  HIS B ND1 
2269 N  ND1 B HIS B 10  ? 0.1576 0.1689 0.1780 0.0274  -0.0031 -0.0458 10  HIS B ND1 
2270 C  CD2 A HIS B 10  ? 0.1729 0.1923 0.2623 -0.0057 0.0057  -0.0386 10  HIS B CD2 
2271 C  CD2 B HIS B 10  ? 0.1166 0.2316 0.1676 -0.0031 -0.0116 -0.0635 10  HIS B CD2 
2272 C  CE1 A HIS B 10  ? 0.1825 0.1858 0.2527 0.0533  0.0122  -0.0595 10  HIS B CE1 
2273 C  CE1 B HIS B 10  ? 0.1080 0.1777 0.2273 -0.0130 0.0397  -0.0732 10  HIS B CE1 
2274 N  NE2 A HIS B 10  ? 0.2141 0.1526 0.2233 0.0082  0.0397  -0.0386 10  HIS B NE2 
2275 N  NE2 B HIS B 10  ? 0.1692 0.1950 0.2190 -0.0024 0.0377  -0.0940 10  HIS B NE2 
2276 N  N   . ASN B 11  ? 0.1659 0.2257 0.3736 0.0621  0.1581  0.0494  11  ASN B N   
2277 C  CA  . ASN B 11  ? 0.1625 0.2060 0.3156 0.0557  0.1088  0.0195  11  ASN B CA  
2278 C  C   . ASN B 11  ? 0.1870 0.1862 0.2791 0.0582  0.1310  0.0395  11  ASN B C   
2279 O  O   . ASN B 11  ? 0.1770 0.2138 0.2693 0.0663  0.1195  0.0370  11  ASN B O   
2280 C  CB  . ASN B 11  ? 0.1564 0.2020 0.2703 0.0366  0.1077  0.0441  11  ASN B CB  
2281 C  CG  . ASN B 11  ? 0.1947 0.2025 0.2926 0.0216  0.1324  -0.0049 11  ASN B CG  
2282 O  OD1 . ASN B 11  ? 0.2522 0.2275 0.3301 -0.0003 0.1092  0.0434  11  ASN B OD1 
2283 N  ND2 . ASN B 11  ? 0.2283 0.2013 0.2917 0.0226  0.1132  0.0148  11  ASN B ND2 
2284 N  N   . GLY B 12  ? 0.1512 0.1908 0.2412 0.0324  0.0983  0.0243  12  GLY B N   
2285 C  CA  . GLY B 12  ? 0.0943 0.2126 0.2542 0.0474  0.0725  0.0168  12  GLY B CA  
2286 C  C   . GLY B 12  ? 0.1180 0.1758 0.2469 0.0293  0.0619  0.0344  12  GLY B C   
2287 O  O   . GLY B 12  ? 0.1132 0.1624 0.2350 0.0275  0.0417  0.0355  12  GLY B O   
2288 N  N   . PRO B 13  ? 0.1193 0.1229 0.2418 0.0052  0.0723  -0.0074 13  PRO B N   
2289 C  CA  . PRO B 13  ? 0.1225 0.1227 0.2554 0.0096  0.0634  -0.0023 13  PRO B CA  
2290 C  C   . PRO B 13  ? 0.1932 0.1173 0.1934 0.0100  0.0744  0.0020  13  PRO B C   
2291 O  O   . PRO B 13  ? 0.1081 0.1717 0.2351 -0.0100 0.0441  -0.0178 13  PRO B O   
2292 C  CB  . PRO B 13  ? 0.1420 0.1393 0.2199 -0.0048 0.0844  -0.0129 13  PRO B CB  
2293 C  CG  . PRO B 13  ? 0.1650 0.1597 0.2261 -0.0277 0.0750  -0.0318 13  PRO B CG  
2294 C  CD  . PRO B 13  ? 0.1368 0.1696 0.2187 0.0215  0.0693  0.0024  13  PRO B CD  
2295 N  N   . GLU B 14  ? 0.1712 0.1314 0.2228 0.0130  0.0701  0.0054  14  GLU B N   
2296 C  CA  . GLU B 14  ? 0.2016 0.1970 0.2540 0.0414  0.0873  0.0262  14  GLU B CA  
2297 C  C   . GLU B 14  ? 0.1624 0.1869 0.2653 0.0780  0.0527  0.0416  14  GLU B C   
2298 O  O   . GLU B 14  ? 0.1841 0.1985 0.2833 0.0881  0.0706  0.0759  14  GLU B O   
2299 C  CB  . GLU B 14  ? 0.3486 0.2094 0.2752 0.0780  0.0304  0.0194  14  GLU B CB  
2300 C  CG  . GLU B 14  ? 0.1658 0.3093 0.2910 0.0339  -0.0306 -0.0337 14  GLU B CG  
2301 C  CD  . GLU B 14  ? 0.2563 0.2700 0.2569 0.0441  -0.0168 -0.0083 14  GLU B CD  
2302 O  OE1 . GLU B 14  ? 0.2642 0.2161 0.2698 0.0873  -0.0720 -0.0636 14  GLU B OE1 
2303 O  OE2 . GLU B 14  ? 0.5494 0.1999 0.2845 0.0154  0.1316  -0.0186 14  GLU B OE2 
2304 N  N   . HIS B 15  ? 0.1044 0.1448 0.2601 0.0310  0.0461  0.0171  15  HIS B N   
2305 C  CA  . HIS B 15  ? 0.1018 0.1618 0.2527 0.0362  0.0434  0.0156  15  HIS B CA  
2306 C  C   . HIS B 15  ? 0.0913 0.1669 0.2572 0.0315  0.0406  0.0156  15  HIS B C   
2307 O  O   . HIS B 15  ? 0.0737 0.1756 0.3072 0.0152  0.0372  0.0423  15  HIS B O   
2308 C  CB  . HIS B 15  ? 0.1193 0.1925 0.2892 0.0509  0.0627  0.0368  15  HIS B CB  
2309 C  CG  . HIS B 15  ? 0.1402 0.2278 0.2682 0.0789  0.0680  0.0759  15  HIS B CG  
2310 N  ND1 . HIS B 15  ? 0.1838 0.3368 0.2572 0.1321  0.0529  0.0362  15  HIS B ND1 
2311 C  CD2 . HIS B 15  ? 0.2366 0.2143 0.2459 0.1101  0.0824  0.0260  15  HIS B CD2 
2312 C  CE1 . HIS B 15  ? 0.2603 0.3846 0.2443 0.2004  0.0263  0.0252  15  HIS B CE1 
2313 N  NE2 . HIS B 15  ? 0.3037 0.2565 0.2455 0.1595  0.0856  0.0186  15  HIS B NE2 
2314 N  N   . TRP B 16  ? 0.0804 0.1451 0.2407 0.0184  0.0175  0.0189  16  TRP B N   
2315 C  CA  . TRP B 16  ? 0.0568 0.1286 0.2551 0.0126  0.0132  -0.0097 16  TRP B CA  
2316 C  C   . TRP B 16  ? 0.0832 0.1430 0.2184 0.0078  0.0098  0.0291  16  TRP B C   
2317 O  O   . TRP B 16  ? 0.0822 0.1395 0.2648 0.0055  -0.0087 0.0153  16  TRP B O   
2318 C  CB  . TRP B 16  ? 0.0676 0.1412 0.2390 0.0164  0.0208  -0.0124 16  TRP B CB  
2319 C  CG  . TRP B 16  ? 0.1053 0.1136 0.1851 -0.0097 0.0120  0.0046  16  TRP B CG  
2320 C  CD1 . TRP B 16  ? 0.1222 0.1545 0.1536 0.0208  0.0406  0.0241  16  TRP B CD1 
2321 C  CD2 . TRP B 16  ? 0.0998 0.0995 0.1982 0.0000  0.0276  0.0111  16  TRP B CD2 
2322 N  NE1 . TRP B 16  ? 0.0910 0.1433 0.2005 0.0097  0.0337  -0.0015 16  TRP B NE1 
2323 C  CE2 . TRP B 16  ? 0.1032 0.1076 0.1850 0.0113  0.0364  -0.0023 16  TRP B CE2 
2324 C  CE3 . TRP B 16  ? 0.0760 0.1198 0.2046 0.0044  0.0291  0.0043  16  TRP B CE3 
2325 C  CZ2 . TRP B 16  ? 0.0913 0.1070 0.1785 0.0026  0.0259  -0.0008 16  TRP B CZ2 
2326 C  CZ3 . TRP B 16  ? 0.0829 0.1393 0.1898 0.0017  0.0331  -0.0071 16  TRP B CZ3 
2327 C  CH2 . TRP B 16  ? 0.0976 0.1362 0.1854 0.0026  0.0322  -0.0159 16  TRP B CH2 
2328 N  N   . HIS B 17  ? 0.0700 0.1630 0.2318 0.0054  -0.0043 -0.0148 17  HIS B N   
2329 C  CA  . HIS B 17  ? 0.0687 0.1849 0.2414 0.0013  0.0059  0.0285  17  HIS B CA  
2330 C  C   . HIS B 17  ? 0.0688 0.1626 0.3027 -0.0066 -0.0153 0.0293  17  HIS B C   
2331 O  O   . HIS B 17  ? 0.0764 0.1947 0.3140 -0.0019 -0.0121 0.0149  17  HIS B O   
2332 C  CB  . HIS B 17  ? 0.0830 0.1964 0.2540 0.0151  -0.0017 0.0269  17  HIS B CB  
2333 C  CG  . HIS B 17  ? 0.0817 0.2067 0.2836 0.0217  -0.0221 0.0701  17  HIS B CG  
2334 N  ND1 . HIS B 17  ? 0.1000 0.2899 0.3276 0.0105  -0.0241 0.0847  17  HIS B ND1 
2335 C  CD2 . HIS B 17  ? 0.1184 0.1993 0.3767 0.0584  0.0182  0.0984  17  HIS B CD2 
2336 C  CE1 . HIS B 17  ? 0.1132 0.2383 0.3573 0.0318  0.0272  0.0790  17  HIS B CE1 
2337 N  NE2 . HIS B 17  ? 0.1209 0.1962 0.3443 0.0414  0.0248  0.0976  17  HIS B NE2 
2338 N  N   . LYS B 18  ? 0.0601 0.1821 0.2838 0.0017  -0.0057 0.0498  18  LYS B N   
2339 C  CA  . LYS B 18  ? 0.0593 0.2293 0.3504 0.0066  0.0005  0.0584  18  LYS B CA  
2340 C  C   . LYS B 18  ? 0.0604 0.2318 0.4122 -0.0074 -0.0164 0.0511  18  LYS B C   
2341 O  O   . LYS B 18  ? 0.1272 0.2389 0.5493 -0.0619 -0.0621 0.1368  18  LYS B O   
2342 C  CB  . LYS B 18  ? 0.0734 0.2712 0.3034 0.0099  0.0003  0.0868  18  LYS B CB  
2343 C  CG  . LYS B 18  ? 0.1133 0.2739 0.3192 0.0441  0.0098  0.0785  18  LYS B CG  
2344 C  CD  . LYS B 18  ? 0.0826 0.2849 0.3364 0.0570  0.0311  0.1234  18  LYS B CD  
2345 C  CE  . LYS B 18  ? 0.0910 0.2739 0.3310 0.0533  0.0265  0.0935  18  LYS B CE  
2346 N  NZ  . LYS B 18  ? 0.0918 0.2910 0.3219 0.0842  0.0697  0.1431  18  LYS B NZ  
2347 N  N   . ASP B 19  ? 0.0876 0.2189 0.2903 0.0070  0.0223  0.0644  19  ASP B N   
2348 C  CA  . ASP B 19  ? 0.0974 0.2176 0.3734 0.0060  0.0122  0.0768  19  ASP B CA  
2349 C  C   . ASP B 19  ? 0.0891 0.1699 0.3598 -0.0148 0.0094  0.0635  19  ASP B C   
2350 O  O   . ASP B 19  ? 0.1424 0.1647 0.3526 -0.0269 0.0351  0.0522  19  ASP B O   
2351 C  CB  . ASP B 19  ? 0.1555 0.2887 0.3323 0.0715  0.0335  0.0537  19  ASP B CB  
2352 C  CG  . ASP B 19  ? 0.2333 0.4111 0.3878 0.0000  0.1002  -0.0266 19  ASP B CG  
2353 O  OD1 . ASP B 19  ? 0.2567 0.4172 0.4029 -0.0381 0.1036  0.0599  19  ASP B OD1 
2354 O  OD2 . ASP B 19  ? 0.6676 0.6887 0.5059 0.1033  0.2022  -0.1950 19  ASP B OD2 
2355 N  N   . PHE B 20  ? 0.0729 0.1669 0.2737 -0.0023 -0.0027 0.0353  20  PHE B N   
2356 C  CA  . PHE B 20  ? 0.0703 0.1679 0.2867 -0.0131 0.0088  0.0293  20  PHE B CA  
2357 C  C   . PHE B 20  ? 0.0790 0.1560 0.2854 -0.0267 0.0059  -0.0074 20  PHE B C   
2358 O  O   . PHE B 20  ? 0.0992 0.1427 0.2596 -0.0093 -0.0052 0.0066  20  PHE B O   
2359 C  CB  . PHE B 20  ? 0.1054 0.1631 0.2590 -0.0311 -0.0013 0.0147  20  PHE B CB  
2360 C  CG  . PHE B 20  ? 0.0931 0.2100 0.2763 -0.0331 0.0043  0.0675  20  PHE B CG  
2361 C  CD1 . PHE B 20  ? 0.1084 0.2213 0.3190 -0.0157 0.0377  0.0741  20  PHE B CD1 
2362 C  CD2 . PHE B 20  ? 0.1098 0.2897 0.2784 -0.0509 0.0093  0.0379  20  PHE B CD2 
2363 C  CE1 . PHE B 20  ? 0.1509 0.2960 0.2984 0.0142  0.0198  0.1002  20  PHE B CE1 
2364 C  CE2 . PHE B 20  ? 0.1280 0.3291 0.2904 -0.0331 0.0076  0.0634  20  PHE B CE2 
2365 C  CZ  . PHE B 20  ? 0.1001 0.3300 0.3039 -0.0287 0.0282  0.0775  20  PHE B CZ  
2366 N  N   . PRO B 21  ? 0.0846 0.1688 0.2887 -0.0249 -0.0100 0.0008  21  PRO B N   
2367 C  CA  . PRO B 21  ? 0.0869 0.2124 0.3052 -0.0537 -0.0204 0.0000  21  PRO B CA  
2368 C  C   . PRO B 21  ? 0.1037 0.1683 0.2522 -0.0275 -0.0524 -0.0093 21  PRO B C   
2369 O  O   . PRO B 21  ? 0.0952 0.1941 0.2459 -0.0190 -0.0432 0.0015  21  PRO B O   
2370 C  CB  . PRO B 21  ? 0.1004 0.2836 0.2940 -0.0784 -0.0315 0.0115  21  PRO B CB  
2371 C  CG  . PRO B 21  ? 0.3614 0.4070 0.3813 -0.2250 -0.1423 0.0812  21  PRO B CG  
2372 C  CD  . PRO B 21  ? 0.1379 0.2319 0.3066 -0.0666 -0.0337 0.0531  21  PRO B CD  
2373 N  N   A ILE B 22  ? 0.0860 0.1184 0.2511 -0.0599 -0.0509 -0.0082 22  ILE B N   
2374 N  N   B ILE B 22  ? 0.0778 0.1888 0.2132 -0.0184 -0.0231 -0.0038 22  ILE B N   
2375 C  CA  A ILE B 22  ? 0.1177 0.1229 0.1691 -0.0175 -0.0394 -0.0231 22  ILE B CA  
2376 C  CA  B ILE B 22  ? 0.0445 0.1752 0.2605 -0.0096 -0.0326 0.0098  22  ILE B CA  
2377 C  C   A ILE B 22  ? 0.0820 0.1150 0.1923 -0.0098 -0.0342 -0.0140 22  ILE B C   
2378 C  C   B ILE B 22  ? 0.0766 0.1679 0.1802 -0.0157 -0.0471 -0.0251 22  ILE B C   
2379 O  O   A ILE B 22  ? 0.0982 0.1359 0.1674 0.0176  -0.0201 0.0111  22  ILE B O   
2380 O  O   B ILE B 22  ? 0.0854 0.1148 0.2164 -0.0219 -0.0280 -0.0161 22  ILE B O   
2381 C  CB  A ILE B 22  ? 0.1010 0.1342 0.1453 -0.0043 -0.0272 -0.0157 22  ILE B CB  
2382 C  CB  B ILE B 22  ? 0.0604 0.1465 0.1844 -0.0351 -0.0261 0.0207  22  ILE B CB  
2383 C  CG1 A ILE B 22  ? 0.1352 0.1395 0.1912 -0.0041 0.0085  -0.0370 22  ILE B CG1 
2384 C  CG1 B ILE B 22  ? 0.1253 0.1398 0.1693 -0.0278 -0.0041 -0.0142 22  ILE B CG1 
2385 C  CG2 A ILE B 22  ? 0.1445 0.1425 0.1037 0.0083  -0.0300 0.0127  22  ILE B CG2 
2386 C  CG2 B ILE B 22  ? 0.0839 0.1492 0.1773 -0.0410 -0.0214 0.0023  22  ILE B CG2 
2387 C  CD1 A ILE B 22  ? 0.1313 0.2996 0.2330 -0.0329 0.0114  -0.0370 22  ILE B CD1 
2388 C  CD1 B ILE B 22  ? 0.1110 0.1242 0.2144 -0.0148 -0.0108 -0.0230 22  ILE B CD1 
2389 N  N   . ALA B 23  ? 0.1037 0.1395 0.1854 -0.0087 -0.0088 -0.0026 23  ALA B N   
2390 C  CA  . ALA B 23  ? 0.0989 0.1370 0.1938 -0.0324 -0.0085 -0.0178 23  ALA B CA  
2391 C  C   . ALA B 23  ? 0.0689 0.1539 0.2134 -0.0076 -0.0086 -0.0274 23  ALA B C   
2392 O  O   . ALA B 23  ? 0.0969 0.1404 0.2032 -0.0137 -0.0130 -0.0176 23  ALA B O   
2393 C  CB  . ALA B 23  ? 0.0816 0.1407 0.2178 0.0063  -0.0313 -0.0318 23  ALA B CB  
2394 N  N   . LYS B 24  ? 0.1059 0.1492 0.2145 -0.0062 -0.0252 -0.0082 24  LYS B N   
2395 C  CA  . LYS B 24  ? 0.1036 0.1668 0.2220 -0.0163 -0.0397 0.0105  24  LYS B CA  
2396 C  C   . LYS B 24  ? 0.1278 0.1906 0.2213 -0.0177 -0.0630 -0.0284 24  LYS B C   
2397 O  O   . LYS B 24  ? 0.1506 0.2291 0.2495 -0.0189 -0.0777 -0.0030 24  LYS B O   
2398 C  CB  . LYS B 24  ? 0.1072 0.2181 0.2342 -0.0013 -0.0289 0.0057  24  LYS B CB  
2399 C  CG  . LYS B 24  ? 0.1429 0.2158 0.2490 0.0362  -0.0308 0.0121  24  LYS B CG  
2400 C  CD  . LYS B 24  ? 0.1429 0.3364 0.2856 0.0478  -0.0188 0.0165  24  LYS B CD  
2401 C  CE  . LYS B 24  ? 0.1526 0.3163 0.3492 0.0476  -0.0126 0.0258  24  LYS B CE  
2402 N  NZ  . LYS B 24  ? 0.3251 0.3350 0.4727 0.0476  0.1129  -0.0012 24  LYS B NZ  
2403 N  N   . GLY B 25  ? 0.1171 0.1668 0.2074 0.0005  -0.0465 -0.0297 25  GLY B N   
2404 C  CA  . GLY B 25  ? 0.1151 0.1808 0.2653 -0.0168 -0.0240 -0.0621 25  GLY B CA  
2405 C  C   . GLY B 25  ? 0.1199 0.1870 0.1835 -0.0104 -0.0443 -0.0439 25  GLY B C   
2406 O  O   . GLY B 25  ? 0.1230 0.2295 0.1729 -0.0135 -0.0267 -0.0261 25  GLY B O   
2407 N  N   . GLU B 26  ? 0.1234 0.2400 0.1526 -0.0020 -0.0516 -0.0551 26  GLU B N   
2408 C  CA  . GLU B 26  ? 0.1643 0.2368 0.1200 -0.0218 -0.0386 -0.0366 26  GLU B CA  
2409 C  C   . GLU B 26  ? 0.1462 0.1847 0.1292 0.0120  -0.0274 -0.0283 26  GLU B C   
2410 O  O   . GLU B 26  ? 0.1722 0.2371 0.1227 0.0019  -0.0516 -0.0178 26  GLU B O   
2411 C  CB  . GLU B 26  ? 0.2060 0.3226 0.1821 -0.0215 -0.0759 -0.1066 26  GLU B CB  
2412 C  CG  . GLU B 26  ? 0.2101 0.3407 0.2540 -0.0007 -0.0909 -0.1033 26  GLU B CG  
2413 C  CD  . GLU B 26  ? 0.4002 0.3880 0.2490 0.0425  -0.1220 -0.0732 26  GLU B CD  
2414 O  OE1 . GLU B 26  ? 0.3616 0.5425 0.3001 -0.0460 -0.1431 -0.0270 26  GLU B OE1 
2415 O  OE2 . GLU B 26  ? 0.3459 0.4973 0.5756 0.1176  -0.1772 -0.0353 26  GLU B OE2 
2416 N  N   . ARG B 27  ? 0.1360 0.1308 0.1215 0.0000  -0.0370 -0.0357 27  ARG B N   
2417 C  CA  . ARG B 27  ? 0.1083 0.1132 0.1094 -0.0052 -0.0256 -0.0182 27  ARG B CA  
2418 C  C   . ARG B 27  ? 0.0918 0.1089 0.1080 -0.0037 -0.0032 -0.0208 27  ARG B C   
2419 O  O   . ARG B 27  ? 0.1027 0.1221 0.1075 0.0078  -0.0198 -0.0161 27  ARG B O   
2420 C  CB  . ARG B 27  ? 0.1875 0.1395 0.1301 0.0115  -0.0240 -0.0432 27  ARG B CB  
2421 C  CG  . ARG B 27  ? 0.1870 0.1875 0.1768 -0.0032 0.0015  -0.0270 27  ARG B CG  
2422 C  CD  . ARG B 27  ? 0.2502 0.2261 0.1675 0.0494  -0.0520 -0.0076 27  ARG B CD  
2423 N  NE  . ARG B 27  ? 0.2396 0.1448 0.1480 -0.0003 0.0100  -0.0281 27  ARG B NE  
2424 C  CZ  . ARG B 27  ? 0.1744 0.1623 0.1076 0.0256  -0.0065 0.0120  27  ARG B CZ  
2425 N  NH1 . ARG B 27  ? 0.1569 0.2556 0.1988 0.0430  -0.0153 -0.1385 27  ARG B NH1 
2426 N  NH2 . ARG B 27  ? 0.1606 0.1717 0.1687 -0.0147 -0.0197 -0.0366 27  ARG B NH2 
2427 N  N   . GLN B 28  ? 0.1130 0.1005 0.1015 -0.0046 -0.0182 -0.0250 28  GLN B N   
2428 C  CA  . GLN B 28  ? 0.0772 0.1096 0.1041 -0.0103 -0.0138 -0.0132 28  GLN B CA  
2429 C  C   . GLN B 28  ? 0.0956 0.0908 0.0962 -0.0005 -0.0097 -0.0063 28  GLN B C   
2430 O  O   . GLN B 28  ? 0.1123 0.1096 0.0944 -0.0092 -0.0155 -0.0108 28  GLN B O   
2431 C  CB  . GLN B 28  ? 0.0741 0.1141 0.1343 -0.0057 -0.0176 -0.0189 28  GLN B CB  
2432 C  CG  . GLN B 28  ? 0.0894 0.1139 0.1245 -0.0010 -0.0087 -0.0274 28  GLN B CG  
2433 C  CD  . GLN B 28  ? 0.0769 0.1125 0.1262 -0.0146 -0.0187 -0.0238 28  GLN B CD  
2434 O  OE1 . GLN B 28  ? 0.0908 0.1055 0.1277 -0.0174 -0.0096 -0.0129 28  GLN B OE1 
2435 N  NE2 . GLN B 28  ? 0.0835 0.1087 0.1440 -0.0083 -0.0212 -0.0265 28  GLN B NE2 
2436 N  N   . SER B 29  ? 0.0856 0.0964 0.0892 0.0038  -0.0076 -0.0179 29  SER B N   
2437 C  CA  . SER B 29  ? 0.0672 0.0806 0.1092 0.0017  -0.0107 -0.0153 29  SER B CA  
2438 C  C   . SER B 29  ? 0.0674 0.0873 0.0992 -0.0024 -0.0065 -0.0074 29  SER B C   
2439 O  O   . SER B 29  ? 0.0742 0.0922 0.1112 -0.0098 0.0049  -0.0096 29  SER B O   
2440 C  CB  . SER B 29  ? 0.0658 0.0847 0.1036 0.0088  -0.0080 -0.0197 29  SER B CB  
2441 O  OG  . SER B 29  ? 0.0819 0.0864 0.1014 0.0035  -0.0020 -0.0187 29  SER B OG  
2442 N  N   . PRO B 30  ? 0.0657 0.0764 0.0945 -0.0010 -0.0031 -0.0140 30  PRO B N   
2443 C  CA  . PRO B 30  ? 0.0724 0.0808 0.1031 0.0008  -0.0035 -0.0060 30  PRO B CA  
2444 C  C   . PRO B 30  ? 0.0696 0.0772 0.0948 0.0019  0.0060  -0.0098 30  PRO B C   
2445 O  O   . PRO B 30  ? 0.0837 0.0930 0.1027 0.0017  -0.0087 -0.0057 30  PRO B O   
2446 C  CB  . PRO B 30  ? 0.0775 0.0777 0.0930 -0.0019 0.0027  -0.0141 30  PRO B CB  
2447 C  CG  . PRO B 30  ? 0.0821 0.0953 0.1005 -0.0003 0.0082  -0.0185 30  PRO B CG  
2448 C  CD  . PRO B 30  ? 0.0908 0.0920 0.1028 0.0012  0.0103  -0.0116 30  PRO B CD  
2449 N  N   . VAL B 31  ? 0.0965 0.0817 0.0908 0.0038  -0.0057 0.0015  31  VAL B N   
2450 C  CA  . VAL B 31  ? 0.0939 0.0993 0.0797 0.0060  0.0007  0.0062  31  VAL B CA  
2451 C  C   . VAL B 31  ? 0.0917 0.0829 0.1001 0.0089  -0.0070 -0.0013 31  VAL B C   
2452 O  O   . VAL B 31  ? 0.1017 0.0938 0.1005 -0.0015 -0.0130 0.0100  31  VAL B O   
2453 C  CB  . VAL B 31  ? 0.1092 0.0896 0.1068 0.0038  -0.0060 -0.0043 31  VAL B CB  
2454 C  CG1 . VAL B 31  ? 0.1410 0.1040 0.1102 -0.0089 0.0031  -0.0087 31  VAL B CG1 
2455 C  CG2 . VAL B 31  ? 0.1019 0.0952 0.1227 0.0003  0.0122  -0.0026 31  VAL B CG2 
2456 N  N   . ASP B 32  ? 0.1103 0.0901 0.0891 0.0076  -0.0052 0.0097  32  ASP B N   
2457 C  CA  . ASP B 32  ? 0.1079 0.0852 0.0995 0.0049  -0.0008 0.0088  32  ASP B CA  
2458 C  C   . ASP B 32  ? 0.1076 0.1001 0.0901 0.0102  -0.0043 0.0098  32  ASP B C   
2459 O  O   . ASP B 32  ? 0.1259 0.1400 0.1194 0.0020  -0.0124 -0.0195 32  ASP B O   
2460 C  CB  . ASP B 32  ? 0.1436 0.0993 0.1123 0.0195  -0.0051 0.0173  32  ASP B CB  
2461 C  CG  . ASP B 32  ? 0.1446 0.0983 0.1116 0.0071  -0.0062 0.0208  32  ASP B CG  
2462 O  OD1 . ASP B 32  ? 0.1343 0.1080 0.1189 0.0043  -0.0126 0.0110  32  ASP B OD1 
2463 O  OD2 . ASP B 32  ? 0.2258 0.1238 0.1182 -0.0203 -0.0110 0.0337  32  ASP B OD2 
2464 N  N   . ILE B 33  ? 0.1072 0.0967 0.0900 0.0060  0.0092  0.0125  33  ILE B N   
2465 C  CA  . ILE B 33  ? 0.1190 0.0996 0.0951 0.0129  0.0103  0.0020  33  ILE B CA  
2466 C  C   . ILE B 33  ? 0.1411 0.1096 0.0916 0.0233  0.0307  0.0170  33  ILE B C   
2467 O  O   . ILE B 33  ? 0.1410 0.1145 0.1255 0.0038  0.0137  0.0264  33  ILE B O   
2468 C  CB  . ILE B 33  ? 0.1125 0.1080 0.1173 0.0094  0.0082  0.0156  33  ILE B CB  
2469 C  CG1 . ILE B 33  ? 0.1248 0.1036 0.1293 0.0100  -0.0131 0.0306  33  ILE B CG1 
2470 C  CG2 . ILE B 33  ? 0.1263 0.1504 0.1416 0.0178  0.0151  0.0092  33  ILE B CG2 
2471 C  CD1 . ILE B 33  ? 0.1105 0.1474 0.1501 -0.0043 -0.0131 0.0432  33  ILE B CD1 
2472 N  N   . ASP B 34  ? 0.1720 0.1377 0.1042 0.0241  0.0184  0.0259  34  ASP B N   
2473 C  CA  . ASP B 34  ? 0.1755 0.1606 0.1081 0.0384  0.0243  0.0568  34  ASP B CA  
2474 C  C   . ASP B 34  ? 0.2150 0.1493 0.1132 0.0663  0.0410  0.0601  34  ASP B C   
2475 O  O   . ASP B 34  ? 0.2441 0.1722 0.1343 0.0595  0.0535  0.0320  34  ASP B O   
2476 C  CB  . ASP B 34  ? 0.2506 0.1631 0.1132 0.0403  0.0181  0.0348  34  ASP B CB  
2477 C  CG  . ASP B 34  ? 0.2766 0.2813 0.2137 0.0107  -0.0317 0.1361  34  ASP B CG  
2478 O  OD1 . ASP B 34  ? 0.3371 0.2294 0.2433 0.0643  0.0931  0.0974  34  ASP B OD1 
2479 O  OD2 . ASP B 34  ? 0.3242 0.4286 0.4424 0.0498  -0.0635 0.2605  34  ASP B OD2 
2480 N  N   . THR B 35  ? 0.1988 0.1789 0.1420 0.0515  0.0498  0.0724  35  THR B N   
2481 C  CA  . THR B 35  ? 0.1946 0.1977 0.1392 0.0844  0.0516  0.0619  35  THR B CA  
2482 C  C   . THR B 35  ? 0.2289 0.1599 0.1476 0.0658  0.0606  0.0540  35  THR B C   
2483 O  O   . THR B 35  ? 0.2931 0.1932 0.1591 0.0954  0.0640  0.0679  35  THR B O   
2484 C  CB  . THR B 35  ? 0.1692 0.2223 0.1878 0.0573  0.0310  0.0694  35  THR B CB  
2485 O  OG1 . THR B 35  ? 0.2157 0.2089 0.1880 0.0384  0.0597  0.0588  35  THR B OG1 
2486 C  CG2 . THR B 35  ? 0.2098 0.2872 0.1950 0.0861  0.0737  0.0907  35  THR B CG2 
2487 N  N   . HIS B 36  ? 0.2716 0.1915 0.1247 0.0636  0.0597  0.0672  36  HIS B N   
2488 C  CA  . HIS B 36  ? 0.3249 0.2064 0.1180 0.0339  0.0904  0.0489  36  HIS B CA  
2489 C  C   . HIS B 36  ? 0.3154 0.2266 0.1342 0.0577  0.0439  0.0688  36  HIS B C   
2490 O  O   . HIS B 36  ? 0.3215 0.3368 0.1291 0.0883  0.0205  0.0339  36  HIS B O   
2491 C  CB  . HIS B 36  ? 0.3048 0.2411 0.1485 0.0322  0.0188  0.1058  36  HIS B CB  
2492 C  CG  . HIS B 36  ? 0.3704 0.1632 0.1467 0.0410  -0.0331 0.0593  36  HIS B CG  
2493 N  ND1 . HIS B 36  ? 0.3804 0.2870 0.2189 -0.0093 -0.0816 0.0447  36  HIS B ND1 
2494 C  CD2 . HIS B 36  ? 0.3883 0.1756 0.1955 0.0656  -0.0935 0.0643  36  HIS B CD2 
2495 C  CE1 . HIS B 36  ? 0.3125 0.2937 0.2298 -0.0241 -0.0581 0.0445  36  HIS B CE1 
2496 N  NE2 . HIS B 36  ? 0.3759 0.2745 0.3165 0.0597  0.0306  0.1033  36  HIS B NE2 
2497 N  N   . THR B 37  ? 0.3664 0.1587 0.2018 0.0753  0.0785  0.0513  37  THR B N   
2498 C  CA  . THR B 37  ? 0.3842 0.1871 0.1588 0.0966  0.0480  0.0848  37  THR B CA  
2499 C  C   . THR B 37  ? 0.2809 0.2094 0.1572 0.1130  0.0617  0.0322  37  THR B C   
2500 O  O   . THR B 37  ? 0.3641 0.2662 0.1741 0.1246  -0.0113 0.0162  37  THR B O   
2501 C  CB  . THR B 37  ? 0.3932 0.1948 0.4776 0.0956  -0.1413 0.0590  37  THR B CB  
2502 O  OG1 . THR B 37  ? 0.6970 0.2975 0.8500 0.1014  -0.3028 0.2072  37  THR B OG1 
2503 C  CG2 . THR B 37  ? 0.3948 0.3206 0.1871 0.0988  -0.0465 0.0617  37  THR B CG2 
2504 N  N   . ALA B 38  ? 0.2736 0.1805 0.1164 0.0500  0.0505  0.0478  38  ALA B N   
2505 C  CA  . ALA B 38  ? 0.2241 0.1856 0.1218 0.0579  0.0392  0.0384  38  ALA B CA  
2506 C  C   . ALA B 38  ? 0.2960 0.1816 0.1797 0.0750  0.0974  0.0832  38  ALA B C   
2507 O  O   . ALA B 38  ? 0.3328 0.2070 0.3082 0.1004  0.1765  0.0727  38  ALA B O   
2508 C  CB  . ALA B 38  ? 0.2202 0.1844 0.1609 0.0526  0.0103  0.0164  38  ALA B CB  
2509 N  N   . LYS B 39  ? 0.2298 0.2126 0.1442 0.0957  0.0130  0.0007  39  LYS B N   
2510 C  CA  . LYS B 39  ? 0.3334 0.3808 0.0857 0.1969  0.0001  0.0082  39  LYS B CA  
2511 C  C   . LYS B 39  ? 0.1969 0.2746 0.1148 0.0942  0.0288  0.0046  39  LYS B C   
2512 O  O   . LYS B 39  ? 0.1890 0.2531 0.1132 0.0702  0.0164  0.0093  39  LYS B O   
2513 C  CB  . LYS B 39  ? 0.2973 0.5960 0.2637 0.2721  -0.1196 -0.1639 39  LYS B CB  
2514 C  CG  . LYS B 39  ? 0.3465 0.6227 0.2151 0.3034  -0.1053 -0.1220 39  LYS B CG  
2515 C  CD  . LYS B 39  ? 0.3440 0.3973 0.2158 0.0876  -0.0425 0.0397  39  LYS B CD  
2516 C  CE  . LYS B 39  ? 0.4904 0.3756 0.2691 0.0544  0.1137  0.0386  39  LYS B CE  
2517 N  NZ  . LYS B 39  ? 0.2928 0.5177 0.3389 0.1493  0.0524  0.1943  39  LYS B NZ  
2518 N  N   . TYR B 40  ? 0.2585 0.2617 0.1500 0.0891  0.0676  0.0304  40  TYR B N   
2519 C  CA  . TYR B 40  ? 0.2284 0.1924 0.1595 0.0205  0.0778  0.0181  40  TYR B CA  
2520 C  C   . TYR B 40  ? 0.1771 0.2219 0.1132 0.0055  0.0253  0.0188  40  TYR B C   
2521 O  O   . TYR B 40  ? 0.2185 0.3018 0.1143 0.0581  0.0242  -0.0020 40  TYR B O   
2522 C  CB  . TYR B 40  ? 0.3036 0.3106 0.1931 -0.0500 0.1127  0.0226  40  TYR B CB  
2523 C  CG  . TYR B 40  ? 0.2601 0.2939 0.1923 -0.1094 0.0991  -0.0089 40  TYR B CG  
2524 C  CD1 . TYR B 40  ? 0.2339 0.2960 0.1829 -0.0648 0.0604  -0.0275 40  TYR B CD1 
2525 C  CD2 . TYR B 40  ? 0.3898 0.4485 0.2375 0.0175  0.1530  0.0092  40  TYR B CD2 
2526 C  CE1 . TYR B 40  ? 0.1852 0.4034 0.2058 -0.0535 0.0436  -0.0307 40  TYR B CE1 
2527 C  CE2 . TYR B 40  ? 0.2802 0.6534 0.1791 0.0220  0.0666  -0.0216 40  TYR B CE2 
2528 C  CZ  . TYR B 40  ? 0.1887 0.6075 0.1984 -0.0293 0.0454  -0.0190 40  TYR B CZ  
2529 O  OH  . TYR B 40  ? 0.2383 0.6233 0.3524 0.0456  0.0727  -0.0715 40  TYR B OH  
2530 N  N   . ASP B 41  ? 0.1624 0.1937 0.1599 0.0381  0.0423  0.0113  41  ASP B N   
2531 C  CA  . ASP B 41  ? 0.1525 0.2055 0.1675 -0.0027 0.0021  -0.0240 41  ASP B CA  
2532 C  C   . ASP B 41  ? 0.1881 0.2752 0.1562 0.0370  0.0220  -0.0239 41  ASP B C   
2533 O  O   . ASP B 41  ? 0.1785 0.2494 0.1703 0.0405  0.0040  -0.0063 41  ASP B O   
2534 C  CB  . ASP B 41  ? 0.2427 0.2153 0.2005 -0.0269 0.0097  -0.0515 41  ASP B CB  
2535 C  CG  . ASP B 41  ? 0.2739 0.2506 0.2340 -0.0527 -0.0247 -0.0876 41  ASP B CG  
2536 O  OD1 . ASP B 41  ? 0.2673 0.2725 0.2642 0.0136  -0.0344 -0.1128 41  ASP B OD1 
2537 O  OD2 . ASP B 41  ? 0.3120 0.3100 0.3353 -0.0984 -0.0900 -0.0425 41  ASP B OD2 
2538 N  N   . PRO B 42  ? 0.1939 0.3481 0.1640 0.0688  0.0366  -0.0264 42  PRO B N   
2539 C  CA  . PRO B 42  ? 0.2004 0.4147 0.2509 0.0863  0.0728  0.0164  42  PRO B CA  
2540 C  C   . PRO B 42  ? 0.2696 0.3912 0.2542 0.1366  0.0715  0.0035  42  PRO B C   
2541 O  O   . PRO B 42  ? 0.3095 0.6513 0.2890 0.2137  0.0649  0.0142  42  PRO B O   
2542 C  CB  . PRO B 42  ? 0.2922 0.5802 0.2336 0.1682  0.0931  0.0666  42  PRO B CB  
2543 C  CG  . PRO B 42  ? 0.2845 0.5224 0.2590 0.1264  0.0820  -0.0359 42  PRO B CG  
2544 C  CD  . PRO B 42  ? 0.2732 0.4074 0.1532 0.0978  0.0720  -0.0183 42  PRO B CD  
2545 N  N   . SER B 43  ? 0.3088 0.3395 0.1915 0.1022  0.0392  -0.0355 43  SER B N   
2546 C  CA  . SER B 43  ? 0.3851 0.3325 0.2502 0.1383  -0.0375 -0.0529 43  SER B CA  
2547 C  C   . SER B 43  ? 0.2799 0.2991 0.2608 0.1209  -0.0210 -0.0285 43  SER B C   
2548 O  O   . SER B 43  ? 0.4453 0.2994 0.3016 0.2039  -0.0718 -0.0375 43  SER B O   
2549 C  CB  . SER B 43  ? 0.3287 0.3115 0.2603 0.0467  0.0309  -0.0670 43  SER B CB  
2550 O  OG  . SER B 43  ? 0.3492 0.2552 0.3364 -0.0082 -0.0524 -0.0546 43  SER B OG  
2551 N  N   . LEU B 44  ? 0.3339 0.3235 0.2080 0.1010  -0.0260 -0.0546 44  LEU B N   
2552 C  CA  . LEU B 44  ? 0.2570 0.2380 0.2081 0.0285  -0.0410 -0.0015 44  LEU B CA  
2553 C  C   . LEU B 44  ? 0.2029 0.2536 0.2170 0.0362  0.0263  0.0253  44  LEU B C   
2554 O  O   . LEU B 44  ? 0.1571 0.5110 0.3023 -0.0017 0.0074  0.1321  44  LEU B O   
2555 C  CB  . LEU B 44  ? 0.1926 0.2885 0.1458 -0.0092 0.0156  -0.0078 44  LEU B CB  
2556 C  CG  . LEU B 44  ? 0.1808 0.2545 0.1589 -0.0193 -0.0098 0.0329  44  LEU B CG  
2557 C  CD1 . LEU B 44  ? 0.2293 0.2225 0.1770 -0.0071 0.0043  0.0046  44  LEU B CD1 
2558 C  CD2 . LEU B 44  ? 0.1904 0.2222 0.1879 -0.0170 -0.0013 0.0197  44  LEU B CD2 
2559 N  N   . LYS B 45  ? 0.2515 0.2644 0.2001 0.0553  -0.0208 -0.0107 45  LYS B N   
2560 C  CA  . LYS B 45  ? 0.1914 0.2215 0.2775 0.0384  -0.0162 -0.0098 45  LYS B CA  
2561 C  C   . LYS B 45  ? 0.1622 0.2750 0.2074 0.0619  0.0302  -0.0131 45  LYS B C   
2562 O  O   . LYS B 45  ? 0.1668 0.2270 0.2705 0.0417  0.0163  -0.0006 45  LYS B O   
2563 C  CB  . LYS B 45  ? 0.2230 0.2249 0.2336 0.0705  -0.0020 0.0082  45  LYS B CB  
2564 C  CG  . LYS B 45  ? 0.2180 0.3815 0.2966 0.0131  -0.0210 -0.0485 45  LYS B CG  
2565 C  CD  . LYS B 45  ? 0.3023 0.3889 0.3623 -0.0082 0.0070  -0.0377 45  LYS B CD  
2566 C  CE  . LYS B 45  ? 0.4544 0.4636 0.5788 -0.0109 0.0229  -0.1694 45  LYS B CE  
2567 N  NZ  . LYS B 45  ? 0.5285 0.6581 0.6514 0.1606  0.1384  -0.1336 45  LYS B NZ  
2568 N  N   . PRO B 46  ? 0.1412 0.2214 0.2667 -0.0062 0.0296  -0.0001 46  PRO B N   
2569 C  CA  . PRO B 46  ? 0.1665 0.2768 0.2138 0.0000  0.0218  0.0044  46  PRO B CA  
2570 C  C   . PRO B 46  ? 0.1114 0.2012 0.2061 -0.0026 0.0122  -0.0063 46  PRO B C   
2571 O  O   . PRO B 46  ? 0.1080 0.2154 0.2712 -0.0115 -0.0203 0.0236  46  PRO B O   
2572 C  CB  . PRO B 46  ? 0.1626 0.3212 0.2698 -0.0120 0.0097  0.0211  46  PRO B CB  
2573 C  CG  . PRO B 46  ? 0.1277 0.4801 0.3170 0.0384  -0.0076 -0.0210 46  PRO B CG  
2574 C  CD  . PRO B 46  ? 0.1626 0.3025 0.3210 0.0348  0.0193  -0.0245 46  PRO B CD  
2575 N  N   . LEU B 47  ? 0.1606 0.2576 0.2197 0.0218  0.0174  0.0264  47  LEU B N   
2576 C  CA  . LEU B 47  ? 0.1027 0.2344 0.2093 -0.0080 0.0027  0.0109  47  LEU B CA  
2577 C  C   . LEU B 47  ? 0.0716 0.2504 0.3361 -0.0423 -0.0254 0.0939  47  LEU B C   
2578 O  O   . LEU B 47  ? 0.1254 0.2892 0.4309 -0.0790 -0.0833 0.1528  47  LEU B O   
2579 C  CB  . LEU B 47  ? 0.1735 0.2339 0.3027 0.0544  0.0375  0.0300  47  LEU B CB  
2580 C  CG  . LEU B 47  ? 0.1397 0.2887 0.3531 -0.0357 0.0259  -0.0754 47  LEU B CG  
2581 C  CD1 . LEU B 47  ? 0.0851 0.3438 0.4742 -0.0640 0.0046  -0.0353 47  LEU B CD1 
2582 C  CD2 . LEU B 47  ? 0.1240 0.3097 0.3643 0.0381  -0.0020 -0.0696 47  LEU B CD2 
2583 N  N   . SER B 48  ? 0.1066 0.1990 0.2160 -0.0291 0.0008  0.0564  48  SER B N   
2584 C  CA  . SER B 48  ? 0.1483 0.2205 0.1949 -0.0132 -0.0276 0.0377  48  SER B CA  
2585 C  C   . SER B 48  ? 0.1033 0.2081 0.2131 -0.0127 -0.0205 0.0461  48  SER B C   
2586 O  O   . SER B 48  ? 0.1292 0.2013 0.2207 -0.0375 -0.0015 0.0080  48  SER B O   
2587 C  CB  . SER B 48  ? 0.1307 0.2364 0.2718 0.0087  0.0000  0.0559  48  SER B CB  
2588 O  OG  . SER B 48  ? 0.1844 0.2648 0.3118 0.0491  0.0351  0.0945  48  SER B OG  
2589 N  N   . VAL B 49  ? 0.1809 0.2137 0.2001 -0.0724 -0.0222 0.0498  49  VAL B N   
2590 C  CA  . VAL B 49  ? 0.1704 0.2003 0.2369 -0.0910 -0.0171 -0.0161 49  VAL B CA  
2591 C  C   . VAL B 49  ? 0.1885 0.2369 0.2247 -0.0944 -0.0299 -0.0104 49  VAL B C   
2592 O  O   . VAL B 49  ? 0.2258 0.4453 0.2576 -0.1994 -0.0724 0.0381  49  VAL B O   
2593 C  CB  . VAL B 49  ? 0.2761 0.2054 0.2405 -0.0910 0.0284  -0.0111 49  VAL B CB  
2594 C  CG1 . VAL B 49  ? 0.3844 0.2479 0.3005 -0.0615 0.0988  -0.0346 49  VAL B CG1 
2595 C  CG2 . VAL B 49  ? 0.2140 0.2350 0.3768 -0.0430 0.0370  0.0445  49  VAL B CG2 
2596 N  N   . SER B 50  ? 0.1484 0.2318 0.2398 -0.0676 -0.0299 -0.0041 50  SER B N   
2597 C  CA  . SER B 50  ? 0.1599 0.3107 0.2784 -0.0368 -0.0346 0.0209  50  SER B CA  
2598 C  C   . SER B 50  ? 0.1291 0.2484 0.2734 -0.0203 -0.0546 0.0299  50  SER B C   
2599 O  O   . SER B 50  ? 0.1896 0.2353 0.2680 -0.0463 -0.0522 0.0368  50  SER B O   
2600 C  CB  . SER B 50  ? 0.1479 0.3495 0.3212 0.0080  -0.0408 0.0227  50  SER B CB  
2601 O  OG  . SER B 50  ? 0.3837 0.3160 0.3619 -0.0241 0.0008  -0.0063 50  SER B OG  
2602 N  N   . TYR B 51  ? 0.1538 0.2295 0.2951 -0.0460 -0.0427 0.0031  51  TYR B N   
2603 C  CA  . TYR B 51  ? 0.1200 0.1861 0.2917 -0.0263 -0.0723 0.0505  51  TYR B CA  
2604 C  C   . TYR B 51  ? 0.1398 0.2291 0.3206 -0.0353 -0.0546 0.0736  51  TYR B C   
2605 O  O   . TYR B 51  ? 0.2419 0.2682 0.2714 -0.0159 -0.0957 0.0619  51  TYR B O   
2606 C  CB  . TYR B 51  ? 0.1518 0.1743 0.2612 -0.0386 -0.0712 0.0317  51  TYR B CB  
2607 C  CG  . TYR B 51  ? 0.1551 0.1959 0.1703 -0.0604 -0.0661 0.0384  51  TYR B CG  
2608 C  CD1 . TYR B 51  ? 0.1851 0.1537 0.2409 -0.0443 -0.0817 0.0344  51  TYR B CD1 
2609 C  CD2 . TYR B 51  ? 0.1605 0.1659 0.1484 -0.0348 -0.0261 0.0211  51  TYR B CD2 
2610 C  CE1 . TYR B 51  ? 0.1332 0.1557 0.1624 -0.0419 -0.0364 0.0322  51  TYR B CE1 
2611 C  CE2 . TYR B 51  ? 0.1518 0.1655 0.1582 -0.0480 -0.0450 0.0083  51  TYR B CE2 
2612 C  CZ  . TYR B 51  ? 0.1409 0.1350 0.1651 -0.0262 -0.0197 0.0031  51  TYR B CZ  
2613 O  OH  . TYR B 51  ? 0.1395 0.1295 0.1815 -0.0161 -0.0370 -0.0015 51  TYR B OH  
2614 N  N   . ASP B 52  ? 0.1511 0.3050 0.3088 -0.0564 -0.0785 0.0734  52  ASP B N   
2615 C  CA  . ASP B 52  ? 0.1625 0.3334 0.3474 -0.0443 -0.0879 0.1253  52  ASP B CA  
2616 C  C   . ASP B 52  ? 0.1921 0.3177 0.3641 -0.0375 -0.0992 0.1190  52  ASP B C   
2617 O  O   . ASP B 52  ? 0.2779 0.3673 0.3467 -0.0216 -0.1252 0.1001  52  ASP B O   
2618 C  CB  . ASP B 52  ? 0.1580 0.3781 0.5629 0.0494  -0.0882 0.1344  52  ASP B CB  
2619 C  CG  . ASP B 52  ? 0.4277 0.2354 0.9153 0.0295  0.1448  -0.0185 52  ASP B CG  
2620 O  OD1 . ASP B 52  ? 0.4952 0.6403 0.8310 -0.0130 0.1747  0.0905  52  ASP B OD1 
2621 O  OD2 . ASP B 52  ? 0.7933 0.5099 1.0499 0.2405  0.2858  0.4533  52  ASP B OD2 
2622 N  N   . GLN B 53  ? 0.2074 0.2603 0.4083 -0.0135 -0.0785 0.1244  53  GLN B N   
2623 C  CA  . GLN B 53  ? 0.2000 0.2899 0.4275 -0.0313 -0.0516 0.1033  53  GLN B CA  
2624 C  C   . GLN B 53  ? 0.2263 0.2025 0.2781 -0.0342 -0.0648 0.0461  53  GLN B C   
2625 O  O   . GLN B 53  ? 0.2400 0.2134 0.3043 -0.0285 -0.0359 0.0474  53  GLN B O   
2626 C  CB  . GLN B 53  ? 0.3431 0.2998 0.4625 0.0252  -0.1206 0.1427  53  GLN B CB  
2627 C  CG  . GLN B 53  ? 0.3377 0.3244 0.7498 0.0361  -0.0088 0.1617  53  GLN B CG  
2628 C  CD  . GLN B 53  ? 0.5580 0.7602 0.9810 0.1650  -0.1204 0.2815  53  GLN B CD  
2629 O  OE1 . GLN B 53  ? 0.3564 0.8758 1.0657 0.0636  -0.0719 0.2680  53  GLN B OE1 
2630 N  NE2 . GLN B 53  ? 1.0212 0.3700 1.6583 -0.3244 -0.1023 0.4013  53  GLN B NE2 
2631 N  N   . ALA B 54  ? 0.2321 0.1835 0.2991 -0.0439 -0.0762 0.0566  54  ALA B N   
2632 C  CA  . ALA B 54  ? 0.2185 0.1651 0.2486 -0.0099 -0.0658 -0.0416 54  ALA B CA  
2633 C  C   . ALA B 54  ? 0.2632 0.1785 0.2146 -0.0419 -0.0505 -0.0461 54  ALA B C   
2634 O  O   . ALA B 54  ? 0.2754 0.3291 0.3097 -0.0603 -0.0881 -0.1086 54  ALA B O   
2635 C  CB  . ALA B 54  ? 0.2468 0.1685 0.2921 -0.0252 -0.0383 0.0049  54  ALA B CB  
2636 N  N   . THR B 55  ? 0.2125 0.1506 0.1816 0.0098  -0.0467 0.0040  55  THR B N   
2637 C  CA  . THR B 55  ? 0.2818 0.1800 0.1634 0.0693  -0.0843 0.0292  55  THR B CA  
2638 C  C   . THR B 55  ? 0.2725 0.1157 0.1213 0.0001  -0.0702 0.0060  55  THR B C   
2639 O  O   . THR B 55  ? 0.2754 0.1155 0.1598 0.0015  -0.0650 0.0218  55  THR B O   
2640 C  CB  . THR B 55  ? 0.4104 0.2448 0.2354 0.0681  -0.0076 0.1058  55  THR B CB  
2641 O  OG1 . THR B 55  ? 0.4494 0.2157 0.4753 0.0273  -0.2107 0.0406  55  THR B OG1 
2642 C  CG2 . THR B 55  ? 0.4833 0.3059 0.2148 0.1932  0.0262  0.1027  55  THR B CG2 
2643 N  N   . SER B 56  ? 0.2885 0.1309 0.1481 0.0445  -0.0803 0.0026  56  SER B N   
2644 C  CA  . SER B 56  ? 0.2630 0.1309 0.1187 0.0024  -0.0430 0.0059  56  SER B CA  
2645 C  C   . SER B 56  ? 0.2232 0.1469 0.1509 0.0362  -0.0199 0.0296  56  SER B C   
2646 O  O   . SER B 56  ? 0.3521 0.1560 0.1629 0.0463  -0.0868 0.0259  56  SER B O   
2647 C  CB  . SER B 56  ? 0.3355 0.1326 0.1184 0.0089  -0.0857 0.0007  56  SER B CB  
2648 O  OG  . SER B 56  ? 0.3626 0.1403 0.1509 -0.0083 -0.1168 0.0285  56  SER B OG  
2649 N  N   . LEU B 57  ? 0.2289 0.1184 0.1033 0.0198  -0.0252 0.0264  57  LEU B N   
2650 C  CA  . LEU B 57  ? 0.2358 0.1220 0.1763 0.0284  -0.0178 0.0445  57  LEU B CA  
2651 C  C   . LEU B 57  ? 0.2655 0.1298 0.1295 0.0179  -0.0155 0.0114  57  LEU B C   
2652 O  O   . LEU B 57  ? 0.3395 0.1680 0.1218 0.0370  -0.0373 0.0445  57  LEU B O   
2653 C  CB  . LEU B 57  ? 0.4350 0.1430 0.1755 -0.0212 0.0082  0.0225  57  LEU B CB  
2654 C  CG  . LEU B 57  ? 0.5832 0.1590 0.2030 0.0153  -0.0588 -0.0214 57  LEU B CG  
2655 C  CD1 . LEU B 57  ? 0.6717 0.1923 0.2380 -0.0593 -0.0209 -0.0121 57  LEU B CD1 
2656 C  CD2 . LEU B 57  ? 0.8730 0.3418 0.3034 0.1094  -0.1605 -0.1098 57  LEU B CD2 
2657 N  N   . ARG B 58  ? 0.3079 0.1344 0.1527 0.0577  -0.0048 0.0255  58  ARG B N   
2658 C  CA  . ARG B 58  ? 0.2709 0.1292 0.1494 0.0000  -0.0355 0.0443  58  ARG B CA  
2659 C  C   . ARG B 58  ? 0.2401 0.1458 0.0961 -0.0119 -0.0119 0.0384  58  ARG B C   
2660 O  O   . ARG B 58  ? 0.3023 0.1353 0.0973 0.0126  -0.0020 0.0249  58  ARG B O   
2661 C  CB  . ARG B 58  ? 0.1885 0.2075 0.1520 0.0027  -0.0046 0.0164  58  ARG B CB  
2662 C  CG  . ARG B 58  ? 0.1884 0.1815 0.2623 -0.0428 0.0178  0.1054  58  ARG B CG  
2663 C  CD  . ARG B 58  ? 0.2261 0.2301 0.1868 -0.0740 -0.0238 0.0379  58  ARG B CD  
2664 N  NE  . ARG B 58  ? 0.1888 0.2013 0.1728 -0.0348 -0.0003 0.0107  58  ARG B NE  
2665 C  CZ  . ARG B 58  ? 0.1932 0.2011 0.1491 -0.0573 0.0032  0.0207  58  ARG B CZ  
2666 N  NH1 . ARG B 58  ? 0.2587 0.2203 0.1891 -0.0772 0.0373  0.0372  58  ARG B NH1 
2667 N  NH2 . ARG B 58  ? 0.2351 0.1458 0.1668 -0.0357 0.0148  0.0052  58  ARG B NH2 
2668 N  N   . ILE B 59  ? 0.2576 0.1215 0.1054 0.0040  -0.0119 0.0142  59  ILE B N   
2669 C  CA  . ILE B 59  ? 0.2020 0.1344 0.1239 -0.0125 -0.0215 0.0211  59  ILE B CA  
2670 C  C   . ILE B 59  ? 0.2294 0.1079 0.1087 0.0115  -0.0507 0.0212  59  ILE B C   
2671 O  O   . ILE B 59  ? 0.3183 0.1865 0.0819 0.0242  -0.0397 0.0209  59  ILE B O   
2672 C  CB  . ILE B 59  ? 0.3009 0.1141 0.0997 -0.0023 -0.0333 0.0141  59  ILE B CB  
2673 C  CG1 . ILE B 59  ? 0.2718 0.1286 0.0834 -0.0141 -0.0447 0.0102  59  ILE B CG1 
2674 C  CG2 . ILE B 59  ? 0.2865 0.1451 0.0887 -0.0148 -0.0491 0.0083  59  ILE B CG2 
2675 C  CD1 . ILE B 59  ? 0.2842 0.1363 0.1202 -0.0209 -0.0500 0.0189  59  ILE B CD1 
2676 N  N   . LEU B 60  ? 0.1805 0.1280 0.1388 -0.0167 -0.0197 0.0121  60  LEU B N   
2677 C  CA  . LEU B 60  ? 0.2115 0.1077 0.0966 0.0031  -0.0373 0.0114  60  LEU B CA  
2678 C  C   . LEU B 60  ? 0.2327 0.0993 0.1218 -0.0103 -0.0215 0.0055  60  LEU B C   
2679 O  O   . LEU B 60  ? 0.2201 0.1366 0.0930 -0.0265 -0.0093 0.0220  60  LEU B O   
2680 C  CB  . LEU B 60  ? 0.1715 0.1166 0.1657 -0.0304 0.0115  0.0085  60  LEU B CB  
2681 C  CG  . LEU B 60  ? 0.2192 0.1243 0.1453 -0.0192 0.0104  0.0368  60  LEU B CG  
2682 C  CD1 . LEU B 60  ? 0.1721 0.1577 0.1676 -0.0104 0.0114  0.0232  60  LEU B CD1 
2683 C  CD2 . LEU B 60  ? 0.2186 0.0967 0.2021 -0.0089 -0.0163 0.0077  60  LEU B CD2 
2684 N  N   . ASN B 61  ? 0.2011 0.0974 0.1363 -0.0092 -0.0055 0.0255  61  ASN B N   
2685 C  CA  . ASN B 61  ? 0.2448 0.1312 0.1045 -0.0339 0.0038  -0.0146 61  ASN B CA  
2686 C  C   . ASN B 61  ? 0.2208 0.1242 0.1010 -0.0478 0.0030  -0.0001 61  ASN B C   
2687 O  O   . ASN B 61  ? 0.2500 0.1474 0.1463 -0.0463 0.0254  0.0353  61  ASN B O   
2688 C  CB  . ASN B 61  ? 0.2099 0.1148 0.1225 -0.0032 0.0175  0.0151  61  ASN B CB  
2689 C  CG  . ASN B 61  ? 0.2008 0.1401 0.0938 -0.0452 0.0253  -0.0201 61  ASN B CG  
2690 O  OD1 . ASN B 61  ? 0.2504 0.1386 0.1272 -0.0476 0.0105  -0.0021 61  ASN B OD1 
2691 N  ND2 . ASN B 61  ? 0.2599 0.1356 0.1124 -0.0355 0.0267  0.0020  61  ASN B ND2 
2692 N  N   . ASN B 62  ? 0.2630 0.1264 0.1146 -0.0362 -0.0070 0.0030  62  ASN B N   
2693 C  CA  . ASN B 62  ? 0.2890 0.1203 0.1715 -0.0038 -0.0553 0.0001  62  ASN B CA  
2694 C  C   . ASN B 62  ? 0.2811 0.1564 0.1387 -0.1023 -0.0021 0.0226  62  ASN B C   
2695 O  O   . ASN B 62  ? 0.4011 0.2098 0.2157 -0.1641 -0.0304 0.0054  62  ASN B O   
2696 C  CB  . ASN B 62  ? 0.3675 0.1643 0.1771 -0.0283 -0.0329 0.0110  62  ASN B CB  
2697 C  CG  . ASN B 62  ? 0.3952 0.2134 0.1360 -0.0294 -0.0121 -0.0582 62  ASN B CG  
2698 O  OD1 . ASN B 62  ? 0.2621 0.1704 0.1483 -0.0538 -0.0003 -0.0063 62  ASN B OD1 
2699 N  ND2 . ASN B 62  ? 0.4990 0.4327 0.3012 0.1592  0.0432  -0.0683 62  ASN B ND2 
2700 N  N   . GLY B 63  ? 0.1969 0.1677 0.1438 -0.0417 0.0000  0.0397  63  GLY B N   
2701 C  CA  . GLY B 63  ? 0.1860 0.2018 0.1190 -0.0619 0.0054  0.0186  63  GLY B CA  
2702 C  C   . GLY B 63  ? 0.2497 0.1306 0.1938 -0.0017 0.0326  -0.0057 63  GLY B C   
2703 O  O   . GLY B 63  ? 0.2071 0.1817 0.2533 -0.0308 0.0524  0.0469  63  GLY B O   
2704 N  N   . HIS B 64  ? 0.2026 0.1674 0.1347 -0.0546 0.0197  0.0295  64  HIS B N   
2705 C  CA  . HIS B 64  ? 0.2231 0.2441 0.1710 -0.0553 0.0232  0.0759  64  HIS B CA  
2706 C  C   . HIS B 64  ? 0.1897 0.1956 0.1776 -0.0597 0.0247  0.0634  64  HIS B C   
2707 O  O   . HIS B 64  ? 0.1826 0.2187 0.2515 -0.0211 0.0226  0.1071  64  HIS B O   
2708 C  CB  . HIS B 64  ? 0.2037 0.3204 0.1387 -0.0684 0.0201  0.0570  64  HIS B CB  
2709 C  CG  . HIS B 64  ? 0.2186 0.3727 0.1199 -0.0581 0.0192  -0.0006 64  HIS B CG  
2710 N  ND1 . HIS B 64  ? 0.2171 0.4088 0.2266 -0.0847 0.0395  -0.0693 64  HIS B ND1 
2711 C  CD2 . HIS B 64  ? 0.2504 0.3183 0.2197 -0.1030 0.0684  -0.0408 64  HIS B CD2 
2712 C  CE1 . HIS B 64  ? 0.2317 0.3422 0.2257 -0.0879 0.0672  -0.0617 64  HIS B CE1 
2713 N  NE2 . HIS B 64  ? 0.2419 0.3637 0.2533 -0.0834 0.0759  -0.0688 64  HIS B NE2 
2714 N  N   . ALA B 65  ? 0.2195 0.1506 0.1614 -0.0395 0.0127  0.0498  65  ALA B N   
2715 C  CA  . ALA B 65  ? 0.2159 0.1479 0.1282 -0.0315 0.0104  0.0320  65  ALA B CA  
2716 C  C   . ALA B 65  ? 0.2362 0.1141 0.0750 -0.0296 -0.0044 0.0100  65  ALA B C   
2717 O  O   . ALA B 65  ? 0.2353 0.1498 0.1186 -0.0342 0.0162  0.0303  65  ALA B O   
2718 C  CB  . ALA B 65  ? 0.2222 0.2072 0.1159 -0.0364 -0.0017 0.0416  65  ALA B CB  
2719 N  N   . PHE B 66  ? 0.2166 0.1233 0.1281 -0.0297 -0.0173 0.0082  66  PHE B N   
2720 C  CA  . PHE B 66  ? 0.2226 0.0962 0.0901 -0.0074 0.0046  0.0167  66  PHE B CA  
2721 C  C   . PHE B 66  ? 0.2018 0.1112 0.0912 -0.0181 -0.0153 0.0104  66  PHE B C   
2722 O  O   . PHE B 66  ? 0.2407 0.1155 0.0822 -0.0244 -0.0044 0.0077  66  PHE B O   
2723 C  CB  . PHE B 66  ? 0.2544 0.1409 0.0903 -0.0357 -0.0216 0.0038  66  PHE B CB  
2724 C  CG  . PHE B 66  ? 0.2295 0.1216 0.0734 -0.0274 -0.0284 -0.0031 66  PHE B CG  
2725 C  CD1 . PHE B 66  ? 0.2122 0.1633 0.0863 0.0032  -0.0370 -0.0015 66  PHE B CD1 
2726 C  CD2 . PHE B 66  ? 0.2423 0.1407 0.0920 -0.0217 -0.0239 -0.0131 66  PHE B CD2 
2727 C  CE1 . PHE B 66  ? 0.2596 0.1392 0.1092 -0.0432 -0.0538 0.0054  66  PHE B CE1 
2728 C  CE2 . PHE B 66  ? 0.2340 0.1190 0.0940 -0.0333 -0.0311 -0.0060 66  PHE B CE2 
2729 C  CZ  . PHE B 66  ? 0.2094 0.1613 0.1132 -0.0133 -0.0412 -0.0260 66  PHE B CZ  
2730 N  N   . ASN B 67  ? 0.2247 0.1096 0.0983 -0.0146 -0.0226 0.0236  67  ASN B N   
2731 C  CA  . ASN B 67  ? 0.2124 0.1020 0.0974 -0.0131 -0.0066 -0.0017 67  ASN B CA  
2732 C  C   . ASN B 67  ? 0.1842 0.0886 0.1115 -0.0163 -0.0335 0.0104  67  ASN B C   
2733 O  O   . ASN B 67  ? 0.2167 0.1448 0.1002 -0.0251 -0.0205 0.0346  67  ASN B O   
2734 C  CB  . ASN B 67  ? 0.1794 0.1324 0.1402 -0.0215 -0.0060 -0.0236 67  ASN B CB  
2735 C  CG  . ASN B 67  ? 0.3075 0.1300 0.1995 -0.0516 -0.0555 -0.0027 67  ASN B CG  
2736 O  OD1 . ASN B 67  ? 0.2469 0.1785 0.1512 -0.0324 -0.0465 -0.0012 67  ASN B OD1 
2737 N  ND2 . ASN B 67  ? 0.2549 0.1825 0.3043 -0.0474 -0.0989 -0.0322 67  ASN B ND2 
2738 N  N   . VAL B 68  ? 0.2205 0.1001 0.1013 -0.0034 -0.0262 0.0118  68  VAL B N   
2739 C  CA  . VAL B 68  ? 0.2466 0.1216 0.0944 0.0313  -0.0401 0.0074  68  VAL B CA  
2740 C  C   . VAL B 68  ? 0.2197 0.1089 0.1057 0.0236  -0.0346 0.0103  68  VAL B C   
2741 O  O   . VAL B 68  ? 0.2504 0.0956 0.0908 0.0137  -0.0164 0.0142  68  VAL B O   
2742 C  CB  . VAL B 68  ? 0.2376 0.0873 0.1448 -0.0038 -0.0234 0.0094  68  VAL B CB  
2743 C  CG1 . VAL B 68  ? 0.2337 0.1762 0.1200 0.0231  -0.0555 -0.0115 68  VAL B CG1 
2744 C  CG2 . VAL B 68  ? 0.2619 0.1511 0.1324 0.0152  -0.0311 -0.0373 68  VAL B CG2 
2745 N  N   . GLU B 69  ? 0.2107 0.1145 0.1028 0.0105  -0.0088 0.0153  69  GLU B N   
2746 C  CA  . GLU B 69  ? 0.2198 0.1204 0.1076 -0.0001 0.0049  -0.0023 69  GLU B CA  
2747 C  C   . GLU B 69  ? 0.2098 0.1184 0.0969 0.0186  -0.0109 0.0239  69  GLU B C   
2748 O  O   . GLU B 69  ? 0.2415 0.1225 0.1402 0.0146  -0.0379 0.0120  69  GLU B O   
2749 C  CB  . GLU B 69  ? 0.1455 0.1498 0.1630 -0.0048 0.0170  0.0006  69  GLU B CB  
2750 C  CG  . GLU B 69  ? 0.1361 0.2092 0.1589 -0.0142 0.0172  0.0322  69  GLU B CG  
2751 C  CD  . GLU B 69  ? 0.1772 0.1365 0.1886 -0.0028 0.0255  0.0156  69  GLU B CD  
2752 O  OE1 . GLU B 69  ? 0.1832 0.1701 0.1946 -0.0226 0.0046  0.0425  69  GLU B OE1 
2753 O  OE2 . GLU B 69  ? 0.1703 0.1668 0.2132 -0.0208 0.0243  0.0208  69  GLU B OE2 
2754 N  N   . PHE B 70  ? 0.2506 0.1163 0.1075 0.0040  -0.0262 0.0120  70  PHE B N   
2755 C  CA  . PHE B 70  ? 0.2277 0.1040 0.1439 0.0201  -0.0601 0.0281  70  PHE B CA  
2756 C  C   . PHE B 70  ? 0.2169 0.1076 0.1383 0.0054  -0.0417 -0.0037 70  PHE B C   
2757 O  O   . PHE B 70  ? 0.2614 0.1067 0.1805 0.0054  -0.0680 0.0328  70  PHE B O   
2758 C  CB  . PHE B 70  ? 0.2461 0.1089 0.1173 0.0127  -0.0610 0.0052  70  PHE B CB  
2759 C  CG  . PHE B 70  ? 0.2506 0.1018 0.1106 0.0255  -0.0201 0.0229  70  PHE B CG  
2760 C  CD1 . PHE B 70  ? 0.2423 0.1121 0.1245 0.0252  -0.0278 0.0306  70  PHE B CD1 
2761 C  CD2 . PHE B 70  ? 0.2192 0.1123 0.1247 0.0175  -0.0441 0.0059  70  PHE B CD2 
2762 C  CE1 . PHE B 70  ? 0.2791 0.1218 0.1544 0.0264  -0.0230 0.0465  70  PHE B CE1 
2763 C  CE2 . PHE B 70  ? 0.2531 0.1087 0.1403 0.0152  -0.0428 0.0263  70  PHE B CE2 
2764 C  CZ  . PHE B 70  ? 0.2829 0.1061 0.1282 0.0203  -0.0175 0.0136  70  PHE B CZ  
2765 N  N   . ASP B 71  ? 0.2786 0.1080 0.1811 0.0278  -0.0842 0.0395  71  ASP B N   
2766 C  CA  . ASP B 71  ? 0.2802 0.1046 0.2248 0.0237  -0.0666 0.0452  71  ASP B CA  
2767 C  C   . ASP B 71  ? 0.2261 0.0844 0.2585 -0.0173 -0.0138 0.0176  71  ASP B C   
2768 O  O   . ASP B 71  ? 0.2387 0.1655 0.3932 -0.0302 0.0124  -0.0100 71  ASP B O   
2769 C  CB  . ASP B 71  ? 0.4352 0.1186 0.3937 -0.0035 -0.2104 0.0876  71  ASP B CB  
2770 C  CG  . ASP B 71  ? 0.4753 0.1607 0.4050 -0.0601 -0.1855 0.0357  71  ASP B CG  
2771 O  OD1 . ASP B 71  ? 0.3946 0.1204 0.3781 0.0359  -0.1274 0.0553  71  ASP B OD1 
2772 O  OD2 . ASP B 71  ? 1.0857 0.1917 1.4799 0.1044  -0.7204 0.3170  71  ASP B OD2 
2773 N  N   . ASP B 72  ? 0.2194 0.0860 0.2325 -0.0091 -0.0233 0.0193  72  ASP B N   
2774 C  CA  . ASP B 72  ? 0.2254 0.0957 0.2423 -0.0249 0.0280  -0.0082 72  ASP B CA  
2775 C  C   . ASP B 72  ? 0.2473 0.0982 0.2490 -0.0239 0.0593  0.0227  72  ASP B C   
2776 O  O   . ASP B 72  ? 0.3447 0.1124 0.2316 -0.0310 0.0586  -0.0149 72  ASP B O   
2777 C  CB  . ASP B 72  ? 0.2480 0.1032 0.2003 -0.0080 0.0286  0.0119  72  ASP B CB  
2778 C  CG  . ASP B 72  ? 0.2173 0.1754 0.1438 -0.0183 -0.0060 0.0076  72  ASP B CG  
2779 O  OD1 . ASP B 72  ? 0.2318 0.2867 0.1851 -0.0483 -0.0381 0.0731  72  ASP B OD1 
2780 O  OD2 . ASP B 72  ? 0.2763 0.2240 0.1454 -0.0527 -0.0346 0.0248  72  ASP B OD2 
2781 N  N   . SER B 73  ? 0.2610 0.0794 0.2955 0.0074  0.0186  0.0522  73  SER B N   
2782 C  CA  . SER B 73  ? 0.3371 0.1033 0.3398 -0.0379 0.0190  -0.0010 73  SER B CA  
2783 C  C   . SER B 73  ? 0.3330 0.0949 0.3714 -0.0222 0.0653  -0.0313 73  SER B C   
2784 O  O   . SER B 73  ? 0.3082 0.0935 0.3213 0.0020  0.0132  0.0174  73  SER B O   
2785 C  CB  . SER B 73  ? 0.4659 0.1923 0.3564 -0.0049 0.0225  0.0854  73  SER B CB  
2786 O  OG  . SER B 73  ? 0.4535 0.1231 0.2800 0.0472  0.0630  0.0781  73  SER B OG  
2787 N  N   . GLN B 74  ? 0.3134 0.0988 0.4496 0.0148  0.0993  -0.0096 74  GLN B N   
2788 C  CA  . GLN B 74  ? 0.3303 0.1400 0.5126 -0.0135 0.1120  -0.0175 74  GLN B CA  
2789 C  C   . GLN B 74  ? 0.3454 0.1477 0.3483 -0.0553 0.0505  -0.0631 74  GLN B C   
2790 O  O   . GLN B 74  ? 0.2606 0.1516 0.2515 -0.0544 -0.0549 0.0278  74  GLN B O   
2791 C  CB  . GLN B 74  ? 0.3127 0.1647 0.6147 0.0026  0.0904  0.0361  74  GLN B CB  
2792 C  CG  . GLN B 74  ? 0.1958 0.2361 0.7373 0.0237  0.0887  0.1163  74  GLN B CG  
2793 C  CD  . GLN B 74  ? 0.2770 0.4778 0.5109 -0.1254 -0.0568 0.1660  74  GLN B CD  
2794 O  OE1 . GLN B 74  ? 0.6995 0.6259 0.6934 -0.1061 0.2178  0.2019  74  GLN B OE1 
2795 N  NE2 . GLN B 74  ? 0.3278 0.3905 0.4050 0.0471  -0.0502 0.1894  74  GLN B NE2 
2796 N  N   A ASP B 75  ? 0.3718 0.4079 0.3700 -0.0751 0.0838  -0.0687 75  ASP B N   
2797 N  N   B ASP B 75  ? 0.2791 0.1674 0.1939 -0.0979 -0.0249 -0.0190 75  ASP B N   
2798 C  CA  A ASP B 75  ? 0.2012 0.3943 0.3481 0.0130  -0.0851 -0.0260 75  ASP B CA  
2799 C  CA  B ASP B 75  ? 0.4196 0.0864 0.1870 -0.0381 -0.0469 0.0348  75  ASP B CA  
2800 C  C   A ASP B 75  ? 0.1762 0.4011 0.3650 0.0153  -0.0520 0.0342  75  ASP B C   
2801 C  C   B ASP B 75  ? 0.3470 0.2430 0.2301 -0.0653 -0.1164 0.0097  75  ASP B C   
2802 O  O   A ASP B 75  ? 0.2554 0.8511 0.5345 -0.0966 0.1710  0.0790  75  ASP B O   
2803 O  O   B ASP B 75  ? 0.3691 0.2022 0.3844 0.0034  -0.1740 0.0513  75  ASP B O   
2804 C  CB  A ASP B 75  ? 0.1744 0.4837 0.3603 -0.0262 0.0265  0.0046  75  ASP B CB  
2805 C  CB  B ASP B 75  ? 0.4214 0.2100 0.1530 -0.0909 0.0261  0.0103  75  ASP B CB  
2806 C  CG  A ASP B 75  ? 0.1758 0.3443 0.2552 0.0631  0.1147  -0.0156 75  ASP B CG  
2807 C  CG  B ASP B 75  ? 0.4948 0.2815 0.1948 -0.0998 -0.0038 0.1044  75  ASP B CG  
2808 O  OD1 A ASP B 75  ? 0.1277 0.2829 0.1997 -0.0250 0.0241  0.0674  75  ASP B OD1 
2809 O  OD1 B ASP B 75  ? 0.6337 0.2919 0.3043 -0.0059 0.0670  0.1262  75  ASP B OD1 
2810 O  OD2 A ASP B 75  ? 0.4205 0.3892 0.2594 0.0328  0.1169  -0.0264 75  ASP B OD2 
2811 O  OD2 B ASP B 75  ? 0.1643 0.3454 0.3801 -0.0984 -0.0650 0.2265  75  ASP B OD2 
2812 N  N   . LYS B 76  ? 0.3066 0.1946 0.3359 -0.0631 -0.1059 0.1028  76  LYS B N   
2813 C  CA  . LYS B 76  ? 0.2951 0.1497 0.5404 -0.0375 -0.0559 0.0637  76  LYS B CA  
2814 C  C   . LYS B 76  ? 0.2818 0.2222 0.8191 -0.0681 -0.2193 0.1882  76  LYS B C   
2815 O  O   . LYS B 76  ? 0.2973 0.4787 0.6218 -0.1556 -0.1792 0.0826  76  LYS B O   
2816 C  CB  . LYS B 76  ? 0.4029 0.1635 0.3743 -0.0644 -0.2111 0.0588  76  LYS B CB  
2817 C  CG  . LYS B 76  ? 1.0132 0.2711 0.4302 -0.0667 -0.4023 0.1128  76  LYS B CG  
2818 C  CD  . LYS B 76  ? 1.3565 0.2942 0.4088 -0.3037 -0.5853 0.1915  76  LYS B CD  
2819 C  CE  . LYS B 76  ? 0.8557 0.7027 0.9067 0.0326  -0.3605 0.5192  76  LYS B CE  
2820 N  NZ  . LYS B 76  ? 0.6844 0.2567 0.8465 -0.0804 -0.3080 0.1439  76  LYS B NZ  
2821 N  N   . ALA B 77  ? 0.3806 0.5500 0.8213 -0.0419 -0.3265 0.2980  77  ALA B N   
2822 C  CA  . ALA B 77  ? 0.2115 0.3048 0.2567 -0.0263 -0.1093 -0.0125 77  ALA B CA  
2823 C  C   . ALA B 77  ? 0.1259 0.2102 0.2784 -0.0294 -0.0812 -0.0027 77  ALA B C   
2824 O  O   . ALA B 77  ? 0.1508 0.4426 0.2926 -0.0263 -0.0648 -0.1155 77  ALA B O   
2825 C  CB  . ALA B 77  ? 0.2540 0.2137 0.2700 -0.0337 -0.1097 0.0590  77  ALA B CB  
2826 N  N   . VAL B 78  ? 0.1860 0.1509 0.2133 -0.0262 -0.0662 0.0307  78  VAL B N   
2827 C  CA  . VAL B 78  ? 0.2436 0.1191 0.2294 -0.0348 -0.0808 0.0221  78  VAL B CA  
2828 C  C   . VAL B 78  ? 0.1491 0.1242 0.2260 -0.0132 -0.0362 0.0055  78  VAL B C   
2829 O  O   . VAL B 78  ? 0.1674 0.1567 0.2737 -0.0450 -0.0781 0.0368  78  VAL B O   
2830 C  CB  . VAL B 78  ? 0.3310 0.1744 0.2651 0.0331  -0.1002 -0.0164 78  VAL B CB  
2831 C  CG1 . VAL B 78  ? 0.3555 0.1351 0.3713 0.0364  -0.1036 0.0174  78  VAL B CG1 
2832 C  CG2 . VAL B 78  ? 0.3212 0.2226 0.3528 0.0031  -0.0315 -0.0065 78  VAL B CG2 
2833 N  N   . LEU B 79  ? 0.1288 0.1164 0.1920 -0.0111 -0.0281 0.0151  79  LEU B N   
2834 C  CA  . LEU B 79  ? 0.1406 0.1318 0.1687 -0.0124 -0.0091 0.0153  79  LEU B CA  
2835 C  C   . LEU B 79  ? 0.1254 0.1428 0.1720 -0.0093 0.0037  0.0031  79  LEU B C   
2836 O  O   . LEU B 79  ? 0.1444 0.1615 0.1956 -0.0242 0.0137  -0.0115 79  LEU B O   
2837 C  CB  . LEU B 79  ? 0.1427 0.1501 0.2117 -0.0148 -0.0313 0.0130  79  LEU B CB  
2838 C  CG  . LEU B 79  ? 0.1662 0.1577 0.1737 0.0157  -0.0175 0.0126  79  LEU B CG  
2839 C  CD1 . LEU B 79  ? 0.1664 0.1572 0.4079 -0.0124 0.0007  0.0834  79  LEU B CD1 
2840 C  CD2 . LEU B 79  ? 0.1371 0.1665 0.1895 0.0092  -0.0104 0.0152  79  LEU B CD2 
2841 N  N   . LYS B 80  ? 0.1398 0.1709 0.1897 -0.0201 0.0184  -0.0041 80  LYS B N   
2842 C  CA  . LYS B 80  ? 0.1678 0.1486 0.2052 -0.0048 0.0259  0.0007  80  LYS B CA  
2843 C  C   . LYS B 80  ? 0.1133 0.1891 0.2215 0.0089  0.0461  0.0280  80  LYS B C   
2844 O  O   . LYS B 80  ? 0.1359 0.1603 0.2166 -0.0093 0.0049  0.0219  80  LYS B O   
2845 C  CB  . LYS B 80  ? 0.2425 0.1811 0.2328 0.0489  0.0414  -0.0010 80  LYS B CB  
2846 C  CG  . LYS B 80  ? 0.2178 0.2043 0.2944 0.0640  0.0342  0.0223  80  LYS B CG  
2847 C  CD  . LYS B 80  ? 0.2854 0.2502 0.3501 0.1008  0.0161  0.0443  80  LYS B CD  
2848 C  CE  . LYS B 80  ? 0.2998 0.4729 0.4875 0.1960  -0.1191 -0.1457 80  LYS B CE  
2849 N  NZ  . LYS B 80  ? 1.0458 0.5691 0.7710 -0.0772 -0.2795 -0.3565 80  LYS B NZ  
2850 N  N   . GLY B 81  ? 0.1651 0.1673 0.2170 0.0210  0.0423  0.0087  81  GLY B N   
2851 C  CA  . GLY B 81  ? 0.1783 0.1898 0.2261 0.0227  0.0652  0.0392  81  GLY B CA  
2852 C  C   . GLY B 81  ? 0.1516 0.1800 0.2340 0.0252  0.0548  0.0210  81  GLY B C   
2853 O  O   . GLY B 81  ? 0.1441 0.1756 0.2144 -0.0238 0.0223  -0.0263 81  GLY B O   
2854 N  N   . GLY B 82  ? 0.1642 0.2044 0.3734 -0.0155 0.0666  0.0685  82  GLY B N   
2855 C  CA  . GLY B 82  ? 0.2072 0.1987 0.3499 -0.0342 0.0132  0.0383  82  GLY B CA  
2856 C  C   . GLY B 82  ? 0.1684 0.1922 0.2441 0.0540  0.0483  0.0615  82  GLY B C   
2857 O  O   . GLY B 82  ? 0.2384 0.3555 0.2529 0.1244  0.0679  0.0324  82  GLY B O   
2858 N  N   . PRO B 83  ? 0.1694 0.1655 0.2601 0.0299  0.0584  0.0463  83  PRO B N   
2859 C  CA  . PRO B 83  ? 0.2290 0.1854 0.1907 0.0776  0.0467  0.0458  83  PRO B CA  
2860 C  C   . PRO B 83  ? 0.1412 0.2233 0.1877 0.0476  -0.0041 -0.0164 83  PRO B C   
2861 O  O   . PRO B 83  ? 0.2441 0.2036 0.2124 0.0231  -0.0537 -0.0057 83  PRO B O   
2862 C  CB  . PRO B 83  ? 0.1803 0.2091 0.2078 0.0608  0.0057  0.0250  83  PRO B CB  
2863 C  CG  . PRO B 83  ? 0.1683 0.1686 0.2238 0.0450  0.0329  0.0450  83  PRO B CG  
2864 C  CD  . PRO B 83  ? 0.1519 0.1424 0.2757 0.0171  0.0361  0.0127  83  PRO B CD  
2865 N  N   . LEU B 84  ? 0.1444 0.1571 0.1888 0.0313  0.0255  -0.0049 84  LEU B N   
2866 C  CA  . LEU B 84  ? 0.1802 0.1334 0.1796 0.0231  0.0261  -0.0179 84  LEU B CA  
2867 C  C   . LEU B 84  ? 0.1732 0.1779 0.2211 0.0546  0.0032  -0.0212 84  LEU B C   
2868 O  O   . LEU B 84  ? 0.1942 0.1764 0.2619 0.0441  0.0335  -0.0548 84  LEU B O   
2869 C  CB  . LEU B 84  ? 0.1442 0.1229 0.1809 0.0093  0.0259  -0.0151 84  LEU B CB  
2870 C  CG  . LEU B 84  ? 0.1146 0.1087 0.1697 0.0083  0.0351  0.0057  84  LEU B CG  
2871 C  CD1 . LEU B 84  ? 0.1322 0.1524 0.1491 0.0364  0.0148  0.0063  84  LEU B CD1 
2872 C  CD2 . LEU B 84  ? 0.1074 0.1287 0.2074 0.0068  0.0217  -0.0210 84  LEU B CD2 
2873 N  N   . ASP B 85  ? 0.2411 0.1624 0.2208 0.0295  0.0212  -0.0674 85  ASP B N   
2874 C  CA  . ASP B 85  ? 0.3073 0.1552 0.2436 -0.0302 0.0697  -0.0967 85  ASP B CA  
2875 C  C   . ASP B 85  ? 0.2353 0.1218 0.3332 0.0162  0.0310  0.0098  85  ASP B C   
2876 O  O   . ASP B 85  ? 0.3459 0.2635 0.3023 0.0115  0.0794  -0.0452 85  ASP B O   
2877 C  CB  . ASP B 85  ? 0.3980 0.1625 0.2390 0.0135  0.0538  -0.0599 85  ASP B CB  
2878 C  CG  . ASP B 85  ? 0.4072 0.3420 0.3551 0.0754  0.2154  0.0248  85  ASP B CG  
2879 O  OD1 . ASP B 85  ? 0.5167 0.5497 0.2793 -0.0973 0.1336  -0.0127 85  ASP B OD1 
2880 O  OD2 . ASP B 85  ? 0.4492 0.6169 0.6568 -0.1957 0.1009  -0.0282 85  ASP B OD2 
2881 N  N   . GLY B 86  ? 0.3186 0.2500 0.3161 -0.0197 -0.0408 0.0653  86  GLY B N   
2882 C  CA  . GLY B 86  ? 0.3623 0.2685 0.2293 -0.0133 0.0032  0.0403  86  GLY B CA  
2883 C  C   . GLY B 86  ? 0.3036 0.2730 0.2182 -0.0864 -0.0384 0.0555  86  GLY B C   
2884 O  O   . GLY B 86  ? 0.3819 0.3544 0.2439 -0.1753 -0.0034 0.0483  86  GLY B O   
2885 N  N   A THR B 87  ? 0.2441 0.1220 0.2113 -0.0015 0.0364  -0.0129 87  THR B N   
2886 N  N   B THR B 87  ? 0.1732 0.1805 0.2035 0.0302  0.0136  -0.0034 87  THR B N   
2887 C  CA  A THR B 87  ? 0.1441 0.1404 0.2667 0.0129  0.0185  -0.0395 87  THR B CA  
2888 C  CA  B THR B 87  ? 0.1474 0.1581 0.2373 0.0238  0.0152  -0.0181 87  THR B CA  
2889 C  C   A THR B 87  ? 0.1318 0.1041 0.2316 0.0149  0.0179  -0.0068 87  THR B C   
2890 C  C   B THR B 87  ? 0.1019 0.1345 0.2626 0.0242  -0.0065 -0.0557 87  THR B C   
2891 O  O   A THR B 87  ? 0.1441 0.0922 0.1403 0.0118  0.0043  0.0088  87  THR B O   
2892 O  O   B THR B 87  ? 0.1905 0.1064 0.1870 0.0000  -0.0498 -0.0085 87  THR B O   
2893 C  CB  A THR B 87  ? 0.1702 0.1840 0.3384 0.0610  -0.0428 -0.0684 87  THR B CB  
2894 C  CB  B THR B 87  ? 0.1004 0.1548 0.2346 0.0185  0.0410  -0.0210 87  THR B CB  
2895 O  OG1 A THR B 87  ? 0.2287 0.2364 0.3382 0.0406  0.0087  -0.0707 87  THR B OG1 
2896 O  OG1 B THR B 87  ? 0.1491 0.1388 0.2131 0.0116  0.0137  0.0295  87  THR B OG1 
2897 C  CG2 A THR B 87  ? 0.2278 0.2224 0.2836 0.0839  -0.0834 -0.0130 87  THR B CG2 
2898 C  CG2 B THR B 87  ? 0.1028 0.1643 0.2698 0.0452  0.0529  -0.0052 87  THR B CG2 
2899 N  N   . TYR B 88  ? 0.1075 0.1058 0.2115 0.0162  -0.0003 -0.0122 88  TYR B N   
2900 C  CA  . TYR B 88  ? 0.1157 0.1022 0.1703 0.0055  -0.0060 -0.0006 88  TYR B CA  
2901 C  C   . TYR B 88  ? 0.1132 0.1063 0.1648 -0.0005 -0.0300 -0.0006 88  TYR B C   
2902 O  O   . TYR B 88  ? 0.1365 0.2011 0.2057 -0.0498 -0.0469 0.0225  88  TYR B O   
2903 C  CB  . TYR B 88  ? 0.1146 0.0975 0.1974 0.0032  -0.0315 -0.0110 88  TYR B CB  
2904 C  CG  . TYR B 88  ? 0.1032 0.0932 0.1587 0.0074  -0.0071 0.0028  88  TYR B CG  
2905 C  CD1 . TYR B 88  ? 0.1014 0.1227 0.1732 0.0038  0.0231  -0.0074 88  TYR B CD1 
2906 C  CD2 . TYR B 88  ? 0.1182 0.0909 0.1307 0.0118  0.0003  -0.0068 88  TYR B CD2 
2907 C  CE1 . TYR B 88  ? 0.1209 0.1208 0.1506 0.0089  0.0216  -0.0082 88  TYR B CE1 
2908 C  CE2 . TYR B 88  ? 0.1145 0.0724 0.1361 0.0000  0.0129  -0.0007 88  TYR B CE2 
2909 C  CZ  . TYR B 88  ? 0.1119 0.0913 0.1323 -0.0020 0.0037  -0.0115 88  TYR B CZ  
2910 O  OH  . TYR B 88  ? 0.1166 0.1079 0.1448 0.0021  -0.0037 -0.0261 88  TYR B OH  
2911 N  N   . ARG B 89  ? 0.1159 0.0988 0.1511 0.0051  -0.0198 -0.0177 89  ARG B N   
2912 C  CA  . ARG B 89  ? 0.1359 0.0900 0.1615 0.0068  -0.0342 -0.0006 89  ARG B CA  
2913 C  C   . ARG B 89  ? 0.1377 0.0753 0.1157 -0.0122 -0.0274 0.0236  89  ARG B C   
2914 O  O   . ARG B 89  ? 0.1283 0.0825 0.1187 -0.0088 -0.0187 0.0105  89  ARG B O   
2915 C  CB  . ARG B 89  ? 0.2282 0.0839 0.2115 0.0135  -0.0724 0.0214  89  ARG B CB  
2916 C  CG  . ARG B 89  ? 0.2146 0.1270 0.1767 -0.0068 -0.0364 0.0280  89  ARG B CG  
2917 C  CD  . ARG B 89  ? 0.2418 0.1125 0.2201 0.0210  -0.0196 0.0119  89  ARG B CD  
2918 N  NE  . ARG B 89  ? 0.2976 0.1058 0.2029 -0.0060 -0.0408 0.0417  89  ARG B NE  
2919 C  CZ  . ARG B 89  ? 0.2506 0.1123 0.1714 -0.0370 0.0035  -0.0059 89  ARG B CZ  
2920 N  NH1 . ARG B 89  ? 0.2078 0.1811 0.2815 0.0157  0.0474  0.0767  89  ARG B NH1 
2921 N  NH2 . ARG B 89  ? 0.2761 0.1172 0.2310 0.0307  -0.0074 0.0141  89  ARG B NH2 
2922 N  N   . LEU B 90  ? 0.1438 0.0852 0.1236 -0.0161 -0.0335 0.0184  90  LEU B N   
2923 C  CA  . LEU B 90  ? 0.1454 0.0812 0.1172 -0.0148 -0.0242 0.0104  90  LEU B CA  
2924 C  C   . LEU B 90  ? 0.1771 0.0957 0.1202 -0.0104 -0.0439 0.0281  90  LEU B C   
2925 O  O   . LEU B 90  ? 0.1834 0.1305 0.1482 -0.0148 -0.0425 0.0417  90  LEU B O   
2926 C  CB  . LEU B 90  ? 0.1635 0.0978 0.1150 -0.0331 -0.0237 0.0141  90  LEU B CB  
2927 C  CG  . LEU B 90  ? 0.2087 0.1008 0.1297 -0.0386 -0.0311 0.0034  90  LEU B CG  
2928 C  CD1 . LEU B 90  ? 0.2091 0.0942 0.1488 -0.0245 -0.0333 -0.0041 90  LEU B CD1 
2929 C  CD2 . LEU B 90  ? 0.2257 0.1587 0.1446 -0.0643 -0.0584 -0.0012 90  LEU B CD2 
2930 N  N   . ILE B 91  ? 0.1793 0.0846 0.0922 -0.0030 -0.0074 0.0013  91  ILE B N   
2931 C  CA  . ILE B 91  ? 0.2008 0.0873 0.0988 -0.0119 -0.0146 0.0070  91  ILE B CA  
2932 C  C   . ILE B 91  ? 0.1675 0.0786 0.0943 -0.0205 -0.0126 0.0046  91  ILE B C   
2933 O  O   . ILE B 91  ? 0.2150 0.0815 0.0939 -0.0178 -0.0156 0.0148  91  ILE B O   
2934 C  CB  . ILE B 91  ? 0.1917 0.0778 0.1050 -0.0228 -0.0131 -0.0060 91  ILE B CB  
2935 C  CG1 . ILE B 91  ? 0.2241 0.1578 0.1099 -0.0688 -0.0030 0.0063  91  ILE B CG1 
2936 C  CG2 . ILE B 91  ? 0.2096 0.0982 0.1163 -0.0296 -0.0231 0.0070  91  ILE B CG2 
2937 C  CD1 . ILE B 91  ? 0.2318 0.1962 0.1475 -0.0834 -0.0062 -0.0017 91  ILE B CD1 
2938 N  N   . GLN B 92  ? 0.1764 0.0658 0.1009 -0.0196 -0.0086 0.0129  92  GLN B N   
2939 C  CA  . GLN B 92  ? 0.1808 0.0716 0.1000 -0.0104 -0.0137 0.0104  92  GLN B CA  
2940 C  C   . GLN B 92  ? 0.1564 0.0803 0.0967 -0.0035 -0.0144 0.0097  92  GLN B C   
2941 O  O   . GLN B 92  ? 0.1948 0.0771 0.0817 -0.0096 -0.0184 0.0065  92  GLN B O   
2942 C  CB  . GLN B 92  ? 0.2101 0.0993 0.1150 -0.0092 -0.0273 0.0167  92  GLN B CB  
2943 C  CG  . GLN B 92  ? 0.1871 0.1040 0.1568 -0.0012 -0.0197 0.0130  92  GLN B CG  
2944 C  CD  . GLN B 92  ? 0.1969 0.1040 0.1439 -0.0190 0.0065  0.0280  92  GLN B CD  
2945 O  OE1 . GLN B 92  ? 0.2019 0.0834 0.1581 -0.0066 -0.0304 0.0254  92  GLN B OE1 
2946 N  NE2 . GLN B 92  ? 0.2317 0.1503 0.4348 0.0048  0.0864  0.0771  92  GLN B NE2 
2947 N  N   . PHE B 93  ? 0.1712 0.0689 0.0869 -0.0083 -0.0089 0.0054  93  PHE B N   
2948 C  CA  . PHE B 93  ? 0.1752 0.0672 0.0983 0.0043  -0.0326 0.0055  93  PHE B CA  
2949 C  C   . PHE B 93  ? 0.1640 0.0710 0.0873 -0.0136 -0.0302 0.0144  93  PHE B C   
2950 O  O   . PHE B 93  ? 0.2154 0.0908 0.0816 0.0027  -0.0276 0.0120  93  PHE B O   
2951 C  CB  . PHE B 93  ? 0.1548 0.0938 0.1013 -0.0160 -0.0465 0.0149  93  PHE B CB  
2952 C  CG  . PHE B 93  ? 0.1675 0.0778 0.1094 -0.0087 -0.0410 0.0080  93  PHE B CG  
2953 C  CD1 . PHE B 93  ? 0.2046 0.0857 0.0947 -0.0001 -0.0370 -0.0085 93  PHE B CD1 
2954 C  CD2 . PHE B 93  ? 0.1844 0.0901 0.1230 -0.0037 -0.0546 0.0124  93  PHE B CD2 
2955 C  CE1 . PHE B 93  ? 0.2046 0.0860 0.1269 0.0070  -0.0570 -0.0049 93  PHE B CE1 
2956 C  CE2 . PHE B 93  ? 0.2301 0.1125 0.1182 0.0187  -0.0724 -0.0087 93  PHE B CE2 
2957 C  CZ  . PHE B 93  ? 0.2242 0.0930 0.1401 0.0136  -0.0830 -0.0115 93  PHE B CZ  
2958 N  N   . HIS B 94  ? 0.1676 0.0653 0.0878 -0.0087 -0.0168 0.0031  94  HIS B N   
2959 C  CA  . HIS B 94  ? 0.1708 0.0701 0.0807 -0.0074 -0.0174 0.0023  94  HIS B CA  
2960 C  C   . HIS B 94  ? 0.1416 0.0720 0.0747 -0.0241 -0.0218 0.0041  94  HIS B C   
2961 O  O   . HIS B 94  ? 0.1521 0.0833 0.0736 -0.0063 -0.0017 0.0074  94  HIS B O   
2962 C  CB  . HIS B 94  ? 0.1650 0.0896 0.0816 -0.0185 -0.0149 0.0076  94  HIS B CB  
2963 C  CG  . HIS B 94  ? 0.1336 0.0790 0.0873 -0.0278 -0.0051 0.0088  94  HIS B CG  
2964 N  ND1 . HIS B 94  ? 0.1448 0.0808 0.0905 -0.0241 -0.0179 0.0024  94  HIS B ND1 
2965 C  CD2 . HIS B 94  ? 0.1339 0.0916 0.0707 -0.0167 -0.0119 -0.0049 94  HIS B CD2 
2966 C  CE1 . HIS B 94  ? 0.1270 0.0813 0.0956 -0.0005 -0.0167 0.0104  94  HIS B CE1 
2967 N  NE2 . HIS B 94  ? 0.1363 0.0724 0.0921 -0.0193 -0.0073 0.0046  94  HIS B NE2 
2968 N  N   . PHE B 95  ? 0.1317 0.0825 0.0781 -0.0098 -0.0096 0.0074  95  PHE B N   
2969 C  CA  . PHE B 95  ? 0.1340 0.0817 0.0905 -0.0035 -0.0188 0.0113  95  PHE B CA  
2970 C  C   . PHE B 95  ? 0.1397 0.0782 0.0654 -0.0261 0.0006  -0.0015 95  PHE B C   
2971 O  O   . PHE B 95  ? 0.1287 0.0979 0.0945 -0.0183 -0.0065 0.0107  95  PHE B O   
2972 C  CB  . PHE B 95  ? 0.1468 0.0714 0.0962 -0.0054 -0.0170 -0.0035 95  PHE B CB  
2973 C  CG  . PHE B 95  ? 0.1395 0.0729 0.0864 -0.0163 -0.0265 -0.0099 95  PHE B CG  
2974 C  CD1 . PHE B 95  ? 0.2013 0.0907 0.0860 -0.0038 -0.0377 -0.0098 95  PHE B CD1 
2975 C  CD2 . PHE B 95  ? 0.1467 0.1053 0.0890 -0.0231 -0.0258 -0.0155 95  PHE B CD2 
2976 C  CE1 . PHE B 95  ? 0.1696 0.1157 0.1058 -0.0222 -0.0342 -0.0020 95  PHE B CE1 
2977 C  CE2 . PHE B 95  ? 0.1607 0.0929 0.1180 -0.0098 -0.0351 -0.0273 95  PHE B CE2 
2978 C  CZ  . PHE B 95  ? 0.1636 0.1017 0.1202 -0.0049 -0.0432 -0.0307 95  PHE B CZ  
2979 N  N   . HIS B 96  ? 0.1207 0.0784 0.0904 -0.0062 -0.0097 -0.0031 96  HIS B N   
2980 C  CA  . HIS B 96  ? 0.1178 0.0780 0.0828 -0.0109 0.0027  -0.0049 96  HIS B CA  
2981 C  C   . HIS B 96  ? 0.1233 0.0865 0.0816 -0.0153 0.0006  0.0041  96  HIS B C   
2982 O  O   . HIS B 96  ? 0.1245 0.0846 0.0895 -0.0178 0.0104  -0.0024 96  HIS B O   
2983 C  CB  . HIS B 96  ? 0.1570 0.0753 0.0847 -0.0107 -0.0151 -0.0096 96  HIS B CB  
2984 C  CG  . HIS B 96  ? 0.1143 0.0932 0.0797 -0.0074 -0.0109 -0.0076 96  HIS B CG  
2985 N  ND1 . HIS B 96  ? 0.1193 0.0901 0.1050 -0.0035 0.0015  0.0015  96  HIS B ND1 
2986 C  CD2 . HIS B 96  ? 0.1181 0.0828 0.0807 -0.0115 0.0021  -0.0113 96  HIS B CD2 
2987 C  CE1 . HIS B 96  ? 0.1171 0.0825 0.1071 -0.0032 -0.0006 -0.0012 96  HIS B CE1 
2988 N  NE2 . HIS B 96  ? 0.1049 0.0825 0.0837 -0.0085 0.0005  -0.0006 96  HIS B NE2 
2989 N  N   . TRP B 97  ? 0.1207 0.0784 0.0847 -0.0043 0.0035  -0.0028 97  TRP B N   
2990 C  CA  . TRP B 97  ? 0.1326 0.0813 0.0952 -0.0119 0.0000  -0.0055 97  TRP B CA  
2991 C  C   . TRP B 97  ? 0.1272 0.0850 0.0723 -0.0031 0.0054  -0.0153 97  TRP B C   
2992 O  O   . TRP B 97  ? 0.1306 0.0887 0.1058 -0.0200 0.0120  -0.0081 97  TRP B O   
2993 C  CB  . TRP B 97  ? 0.1500 0.0964 0.0912 -0.0259 0.0054  -0.0076 97  TRP B CB  
2994 C  CG  . TRP B 97  ? 0.1551 0.0869 0.0966 -0.0205 -0.0135 -0.0076 97  TRP B CG  
2995 C  CD1 . TRP B 97  ? 0.1728 0.0952 0.0882 -0.0258 0.0041  -0.0126 97  TRP B CD1 
2996 C  CD2 . TRP B 97  ? 0.1691 0.0876 0.0848 -0.0318 -0.0052 -0.0122 97  TRP B CD2 
2997 N  NE1 . TRP B 97  ? 0.1992 0.0907 0.0917 -0.0259 0.0108  -0.0168 97  TRP B NE1 
2998 C  CE2 . TRP B 97  ? 0.1991 0.0926 0.0728 -0.0251 0.0034  -0.0162 97  TRP B CE2 
2999 C  CE3 . TRP B 97  ? 0.1495 0.0929 0.0842 -0.0043 -0.0190 -0.0008 97  TRP B CE3 
3000 C  CZ2 . TRP B 97  ? 0.1997 0.0995 0.0877 -0.0241 -0.0024 -0.0008 97  TRP B CZ2 
3001 C  CZ3 . TRP B 97  ? 0.1729 0.0916 0.0995 -0.0231 0.0020  -0.0006 97  TRP B CZ3 
3002 C  CH2 . TRP B 97  ? 0.2234 0.0993 0.0907 -0.0293 0.0048  0.0001  97  TRP B CH2 
3003 N  N   . GLY B 98  ? 0.1583 0.0772 0.0936 -0.0082 0.0183  -0.0085 98  GLY B N   
3004 C  CA  . GLY B 98  ? 0.1369 0.0975 0.0932 -0.0062 0.0052  -0.0035 98  GLY B CA  
3005 C  C   . GLY B 98  ? 0.1580 0.0790 0.1103 -0.0057 0.0105  -0.0188 98  GLY B C   
3006 O  O   . GLY B 98  ? 0.1766 0.0876 0.1119 -0.0189 0.0085  -0.0192 98  GLY B O   
3007 N  N   . SER B 99  ? 0.1703 0.0887 0.1080 -0.0116 0.0170  -0.0221 99  SER B N   
3008 C  CA  . SER B 99  ? 0.1881 0.1039 0.1220 -0.0136 0.0076  -0.0333 99  SER B CA  
3009 C  C   . SER B 99  ? 0.2046 0.1002 0.1465 0.0035  0.0063  -0.0439 99  SER B C   
3010 O  O   . SER B 99  ? 0.2264 0.1298 0.1648 -0.0111 -0.0054 -0.0472 99  SER B O   
3011 C  CB  . SER B 99  ? 0.1957 0.1166 0.1532 -0.0017 0.0107  -0.0485 99  SER B CB  
3012 O  OG  . SER B 99  ? 0.1553 0.1042 0.1997 0.0105  0.0161  -0.0283 99  SER B OG  
3013 N  N   . LEU B 100 ? 0.1655 0.1050 0.1659 -0.0129 0.0193  -0.0386 100 LEU B N   
3014 C  CA  . LEU B 100 ? 0.1723 0.0791 0.2168 0.0119  0.0230  -0.0318 100 LEU B CA  
3015 C  C   . LEU B 100 ? 0.1669 0.0870 0.1787 -0.0282 0.0063  -0.0189 100 LEU B C   
3016 O  O   . LEU B 100 ? 0.1720 0.0888 0.1668 -0.0178 -0.0008 -0.0165 100 LEU B O   
3017 C  CB  . LEU B 100 ? 0.2906 0.1605 0.1914 0.0540  0.0452  0.0076  100 LEU B CB  
3018 C  CG  . LEU B 100 ? 0.2955 0.2222 0.2640 0.0498  0.0077  -0.0658 100 LEU B CG  
3019 C  CD1 . LEU B 100 ? 0.3055 0.3305 0.3131 0.1292  0.0348  -0.0300 100 LEU B CD1 
3020 C  CD2 . LEU B 100 ? 0.3149 0.2583 0.3224 0.0584  0.0781  -0.1275 100 LEU B CD2 
3021 N  N   . ASP B 101 ? 0.1582 0.0998 0.1949 -0.0209 -0.0046 -0.0254 101 ASP B N   
3022 C  CA  . ASP B 101 ? 0.1639 0.0903 0.1577 -0.0280 0.0148  0.0046  101 ASP B CA  
3023 C  C   . ASP B 101 ? 0.1509 0.0768 0.1767 -0.0109 0.0044  0.0023  101 ASP B C   
3024 O  O   . ASP B 101 ? 0.1939 0.1150 0.1686 0.0041  0.0080  0.0055  101 ASP B O   
3025 C  CB  . ASP B 101 ? 0.1685 0.1041 0.2005 -0.0190 -0.0152 0.0274  101 ASP B CB  
3026 C  CG  . ASP B 101 ? 0.1824 0.1168 0.2205 -0.0298 -0.0182 0.0384  101 ASP B CG  
3027 O  OD1 . ASP B 101 ? 0.2232 0.1475 0.1617 -0.0335 0.0044  -0.0135 101 ASP B OD1 
3028 O  OD2 . ASP B 101 ? 0.2592 0.1930 0.2045 -0.1023 -0.0388 0.0143  101 ASP B OD2 
3029 N  N   . GLY B 102 ? 0.1797 0.0930 0.1747 -0.0227 -0.0059 0.0251  102 GLY B N   
3030 C  CA  . GLY B 102 ? 0.2090 0.1173 0.1785 -0.0366 -0.0127 0.0351  102 GLY B CA  
3031 C  C   . GLY B 102 ? 0.1582 0.1049 0.1612 -0.0006 0.0044  0.0230  102 GLY B C   
3032 O  O   . GLY B 102 ? 0.1777 0.1177 0.1614 -0.0052 0.0200  0.0241  102 GLY B O   
3033 N  N   . GLN B 103 ? 0.1534 0.0888 0.1421 -0.0118 0.0063  0.0083  103 GLN B N   
3034 C  CA  . GLN B 103 ? 0.1360 0.0931 0.1107 0.0074  0.0055  -0.0010 103 GLN B CA  
3035 C  C   . GLN B 103 ? 0.1229 0.0769 0.1106 -0.0103 0.0181  -0.0043 103 GLN B C   
3036 O  O   . GLN B 103 ? 0.1474 0.0882 0.1045 -0.0137 -0.0020 -0.0091 103 GLN B O   
3037 C  CB  . GLN B 103 ? 0.1553 0.0966 0.1350 0.0049  0.0225  0.0091  103 GLN B CB  
3038 C  CG  . GLN B 103 ? 0.1774 0.1157 0.1368 0.0201  0.0274  0.0000  103 GLN B CG  
3039 C  CD  . GLN B 103 ? 0.2099 0.1077 0.1985 0.0395  0.0456  0.0340  103 GLN B CD  
3040 O  OE1 . GLN B 103 ? 0.2761 0.2851 0.3368 0.1564  0.1234  0.1711  103 GLN B OE1 
3041 N  NE2 . GLN B 103 ? 0.1611 0.1335 0.2136 0.0272  0.0324  0.0241  103 GLN B NE2 
3042 N  N   . GLY B 104 ? 0.1177 0.0894 0.0918 -0.0024 0.0048  -0.0031 104 GLY B N   
3043 C  CA  . GLY B 104 ? 0.1227 0.0799 0.0847 -0.0092 0.0051  0.0017  104 GLY B CA  
3044 C  C   . GLY B 104 ? 0.1004 0.0819 0.1039 -0.0107 -0.0138 0.0089  104 GLY B C   
3045 O  O   . GLY B 104 ? 0.1173 0.0839 0.1107 -0.0129 0.0052  0.0032  104 GLY B O   
3046 N  N   . SER B 105 ? 0.1019 0.0894 0.0951 -0.0142 0.0027  -0.0046 105 SER B N   
3047 C  CA  . SER B 105 ? 0.0954 0.0768 0.1017 -0.0119 -0.0017 -0.0087 105 SER B CA  
3048 C  C   . SER B 105 ? 0.0991 0.0747 0.0854 -0.0137 -0.0007 0.0023  105 SER B C   
3049 O  O   . SER B 105 ? 0.1080 0.0832 0.1040 -0.0028 -0.0071 -0.0065 105 SER B O   
3050 C  CB  . SER B 105 ? 0.1018 0.0758 0.1001 -0.0082 0.0055  0.0076  105 SER B CB  
3051 O  OG  . SER B 105 ? 0.1123 0.0733 0.1000 -0.0107 0.0026  0.0074  105 SER B OG  
3052 N  N   . GLU B 106 ? 0.0914 0.0732 0.0868 -0.0054 -0.0012 -0.0040 106 GLU B N   
3053 C  CA  . GLU B 106 ? 0.1071 0.0807 0.0839 -0.0142 -0.0096 -0.0063 106 GLU B CA  
3054 C  C   . GLU B 106 ? 0.0856 0.0758 0.0948 -0.0035 -0.0118 -0.0040 106 GLU B C   
3055 O  O   . GLU B 106 ? 0.0895 0.0882 0.0929 -0.0026 -0.0078 0.0000  106 GLU B O   
3056 C  CB  . GLU B 106 ? 0.1014 0.0825 0.0834 -0.0159 -0.0017 0.0103  106 GLU B CB  
3057 C  CG  . GLU B 106 ? 0.1626 0.0882 0.0991 -0.0205 0.0166  0.0005  106 GLU B CG  
3058 C  CD  . GLU B 106 ? 0.1139 0.0901 0.0865 -0.0107 -0.0028 -0.0082 106 GLU B CD  
3059 O  OE1 . GLU B 106 ? 0.0851 0.0851 0.1090 -0.0100 0.0005  -0.0024 106 GLU B OE1 
3060 O  OE2 . GLU B 106 ? 0.1081 0.1040 0.1231 -0.0023 0.0140  -0.0181 106 GLU B OE2 
3061 N  N   . HIS B 107 ? 0.0936 0.0731 0.0882 -0.0030 -0.0038 0.0087  107 HIS B N   
3062 C  CA  . HIS B 107 ? 0.0882 0.0793 0.0759 -0.0017 -0.0068 0.0027  107 HIS B CA  
3063 C  C   . HIS B 107 ? 0.0785 0.0790 0.0759 0.0031  0.0024  0.0076  107 HIS B C   
3064 O  O   . HIS B 107 ? 0.1018 0.0810 0.0839 -0.0040 -0.0019 0.0049  107 HIS B O   
3065 C  CB  . HIS B 107 ? 0.0873 0.0856 0.0785 -0.0001 0.0015  -0.0021 107 HIS B CB  
3066 C  CG  . HIS B 107 ? 0.0759 0.0738 0.0888 0.0038  -0.0024 0.0031  107 HIS B CG  
3067 N  ND1 . HIS B 107 ? 0.0939 0.0724 0.0873 0.0015  -0.0086 -0.0027 107 HIS B ND1 
3068 C  CD2 . HIS B 107 ? 0.0830 0.0785 0.0970 0.0176  -0.0081 -0.0059 107 HIS B CD2 
3069 C  CE1 . HIS B 107 ? 0.1041 0.0719 0.1076 0.0131  -0.0044 -0.0060 107 HIS B CE1 
3070 N  NE2 . HIS B 107 ? 0.0758 0.0857 0.0926 0.0074  -0.0068 -0.0062 107 HIS B NE2 
3071 N  N   . THR B 108 ? 0.0960 0.0841 0.0982 -0.0059 -0.0019 0.0082  108 THR B N   
3072 C  CA  . THR B 108 ? 0.1208 0.0671 0.0909 0.0024  -0.0023 0.0023  108 THR B CA  
3073 C  C   . THR B 108 ? 0.1245 0.0710 0.0931 -0.0001 -0.0140 0.0107  108 THR B C   
3074 O  O   . THR B 108 ? 0.1130 0.0927 0.0961 0.0102  -0.0080 0.0098  108 THR B O   
3075 C  CB  . THR B 108 ? 0.1259 0.0900 0.0951 0.0098  -0.0168 0.0060  108 THR B CB  
3076 O  OG1 . THR B 108 ? 0.1127 0.0962 0.1111 0.0121  -0.0183 0.0006  108 THR B OG1 
3077 C  CG2 . THR B 108 ? 0.1139 0.1098 0.1206 0.0256  -0.0017 0.0032  108 THR B CG2 
3078 N  N   . VAL B 109 ? 0.1026 0.0913 0.1103 -0.0054 0.0008  0.0148  109 VAL B N   
3079 C  CA  . VAL B 109 ? 0.1182 0.0997 0.1064 -0.0110 0.0114  0.0308  109 VAL B CA  
3080 C  C   . VAL B 109 ? 0.1224 0.0908 0.1274 -0.0176 0.0097  0.0272  109 VAL B C   
3081 O  O   . VAL B 109 ? 0.1448 0.0777 0.1337 -0.0010 0.0063  0.0261  109 VAL B O   
3082 C  CB  . VAL B 109 ? 0.1108 0.1111 0.1245 0.0035  0.0037  0.0303  109 VAL B CB  
3083 C  CG1 . VAL B 109 ? 0.1377 0.1233 0.1500 -0.0017 0.0221  0.0366  109 VAL B CG1 
3084 C  CG2 . VAL B 109 ? 0.1448 0.1182 0.1422 0.0183  -0.0048 0.0335  109 VAL B CG2 
3085 N  N   . ASP B 110 ? 0.1376 0.0996 0.1199 0.0115  0.0099  0.0315  110 ASP B N   
3086 C  CA  . ASP B 110 ? 0.1836 0.1033 0.1544 0.0143  0.0280  0.0505  110 ASP B CA  
3087 C  C   . ASP B 110 ? 0.1973 0.0812 0.1251 0.0201  0.0076  0.0361  110 ASP B C   
3088 O  O   . ASP B 110 ? 0.1800 0.0983 0.1289 0.0109  -0.0010 0.0252  110 ASP B O   
3089 C  CB  . ASP B 110 ? 0.2034 0.1168 0.1407 0.0098  0.0304  0.0487  110 ASP B CB  
3090 C  CG  . ASP B 110 ? 0.2020 0.1379 0.1577 -0.0034 0.0324  0.0524  110 ASP B CG  
3091 O  OD1 . ASP B 110 ? 0.2173 0.1564 0.1692 0.0416  0.0469  0.0575  110 ASP B OD1 
3092 O  OD2 . ASP B 110 ? 0.1842 0.2407 0.1794 0.0157  0.0373  0.0469  110 ASP B OD2 
3093 N  N   . LYS B 111 ? 0.1405 0.0944 0.1151 0.0083  -0.0062 0.0175  111 LYS B N   
3094 C  CA  . LYS B 111 ? 0.1523 0.0931 0.1260 0.0206  0.0043  0.0188  111 LYS B CA  
3095 C  C   . LYS B 111 ? 0.1664 0.1008 0.1148 0.0019  0.0015  0.0146  111 LYS B C   
3096 O  O   . LYS B 111 ? 0.1657 0.1361 0.1238 0.0076  0.0121  0.0013  111 LYS B O   
3097 C  CB  . LYS B 111 ? 0.1664 0.1542 0.1272 0.0491  -0.0272 0.0166  111 LYS B CB  
3098 C  CG  . LYS B 111 ? 0.2021 0.2060 0.1648 0.0992  -0.0252 0.0035  111 LYS B CG  
3099 C  CD  . LYS B 111 ? 0.2295 0.2375 0.2275 0.0310  -0.0865 -0.0562 111 LYS B CD  
3100 C  CE  . LYS B 111 ? 0.2899 0.3382 0.2901 0.0524  -0.1324 -0.0625 111 LYS B CE  
3101 N  NZ  . LYS B 111 ? 0.2856 0.3458 0.2558 -0.0038 -0.0798 0.0306  111 LYS B NZ  
3102 N  N   . LYS B 112 ? 0.1534 0.0900 0.1068 -0.0026 -0.0065 0.0121  112 LYS B N   
3103 C  CA  . LYS B 112 ? 0.1526 0.0885 0.1132 -0.0031 0.0024  -0.0027 112 LYS B CA  
3104 C  C   . LYS B 112 ? 0.1211 0.0820 0.1222 0.0044  -0.0138 0.0059  112 LYS B C   
3105 O  O   . LYS B 112 ? 0.1272 0.0785 0.1251 -0.0044 -0.0024 -0.0020 112 LYS B O   
3106 C  CB  . LYS B 112 ? 0.1403 0.1265 0.1439 -0.0535 0.0052  0.0000  112 LYS B CB  
3107 C  CG  . LYS B 112 ? 0.1474 0.1345 0.1785 -0.0344 -0.0043 -0.0243 112 LYS B CG  
3108 C  CD  . LYS B 112 ? 0.1562 0.2071 0.2052 -0.0183 -0.0217 0.0265  112 LYS B CD  
3109 C  CE  . LYS B 112 ? 0.2540 0.1740 0.1888 -0.0190 -0.0412 0.0113  112 LYS B CE  
3110 N  NZ  . LYS B 112 ? 0.2561 0.1683 0.1833 -0.0203 -0.0692 0.0283  112 LYS B NZ  
3111 N  N   A LYS B 113 ? 0.1635 0.0763 0.1058 0.0170  -0.0070 0.0060  113 LYS B N   
3112 N  N   B LYS B 113 ? 0.1213 0.0935 0.1213 0.0017  -0.0153 -0.0013 113 LYS B N   
3113 C  CA  A LYS B 113 ? 0.1620 0.0759 0.1005 0.0028  0.0192  -0.0019 113 LYS B CA  
3114 C  CA  B LYS B 113 ? 0.1186 0.0958 0.1125 0.0273  -0.0298 0.0165  113 LYS B CA  
3115 C  C   A LYS B 113 ? 0.1362 0.0668 0.1155 0.0019  0.0252  0.0159  113 LYS B C   
3116 C  C   B LYS B 113 ? 0.1255 0.0935 0.1175 0.0078  -0.0264 -0.0152 113 LYS B C   
3117 O  O   A LYS B 113 ? 0.1552 0.0503 0.1606 0.0001  0.0252  0.0210  113 LYS B O   
3118 O  O   B LYS B 113 ? 0.1277 0.0934 0.1212 0.0071  -0.0115 -0.0238 113 LYS B O   
3119 C  CB  A LYS B 113 ? 0.1299 0.0789 0.1172 -0.0148 0.0098  0.0046  113 LYS B CB  
3120 C  CB  B LYS B 113 ? 0.1193 0.1310 0.1527 0.0362  -0.0244 -0.0080 113 LYS B CB  
3121 C  CG  A LYS B 113 ? 0.1177 0.1098 0.1414 0.0038  0.0098  -0.0013 113 LYS B CG  
3122 C  CG  B LYS B 113 ? 0.1055 0.1773 0.1139 0.0217  -0.0147 -0.0024 113 LYS B CG  
3123 C  CD  A LYS B 113 ? 0.1342 0.1250 0.1508 -0.0051 0.0263  -0.0248 113 LYS B CD  
3124 C  CD  B LYS B 113 ? 0.1300 0.1018 0.1917 0.0368  -0.0151 -0.0076 113 LYS B CD  
3125 C  CE  A LYS B 113 ? 0.1859 0.1253 0.1429 -0.0185 0.0071  -0.0441 113 LYS B CE  
3126 C  CE  B LYS B 113 ? 0.1101 0.2433 0.2259 0.0239  -0.0584 -0.0138 113 LYS B CE  
3127 N  NZ  A LYS B 113 ? 0.0930 0.1955 0.2107 0.0252  -0.0410 -0.0329 113 LYS B NZ  
3128 N  NZ  B LYS B 113 ? 0.1542 0.2554 0.1877 0.0458  -0.0043 0.0013  113 LYS B NZ  
3129 N  N   . TYR B 114 ? 0.1282 0.0824 0.1045 -0.0028 -0.0120 0.0020  114 TYR B N   
3130 C  CA  . TYR B 114 ? 0.1008 0.0771 0.1220 -0.0165 -0.0115 0.0116  114 TYR B CA  
3131 C  C   . TYR B 114 ? 0.1173 0.0634 0.1114 -0.0115 -0.0091 -0.0003 114 TYR B C   
3132 O  O   . TYR B 114 ? 0.1139 0.0851 0.1202 -0.0068 0.0027  -0.0063 114 TYR B O   
3133 C  CB  . TYR B 114 ? 0.0960 0.0778 0.1209 -0.0091 -0.0010 0.0059  114 TYR B CB  
3134 C  CG  . TYR B 114 ? 0.1169 0.0816 0.1220 0.0024  0.0031  0.0104  114 TYR B CG  
3135 C  CD1 . TYR B 114 ? 0.1412 0.0887 0.1423 0.0093  0.0015  0.0049  114 TYR B CD1 
3136 C  CD2 . TYR B 114 ? 0.1293 0.0939 0.1546 -0.0142 0.0000  0.0212  114 TYR B CD2 
3137 C  CE1 . TYR B 114 ? 0.2161 0.1053 0.1350 0.0190  0.0234  0.0215  114 TYR B CE1 
3138 C  CE2 . TYR B 114 ? 0.1721 0.1163 0.1794 -0.0124 0.0388  -0.0051 114 TYR B CE2 
3139 C  CZ  . TYR B 114 ? 0.1960 0.1146 0.1842 -0.0245 0.0685  0.0143  114 TYR B CZ  
3140 O  OH  . TYR B 114 ? 0.2488 0.2067 0.2247 0.0020  0.0979  0.0121  114 TYR B OH  
3141 N  N   . ALA B 115 ? 0.1441 0.0740 0.1141 -0.0190 -0.0167 0.0035  115 ALA B N   
3142 C  CA  . ALA B 115 ? 0.1186 0.0705 0.1202 -0.0135 -0.0065 0.0000  115 ALA B CA  
3143 C  C   . ALA B 115 ? 0.1412 0.0817 0.0925 -0.0188 -0.0102 -0.0005 115 ALA B C   
3144 O  O   . ALA B 115 ? 0.1375 0.0766 0.1169 -0.0146 0.0028  -0.0057 115 ALA B O   
3145 C  CB  . ALA B 115 ? 0.1596 0.0907 0.1316 -0.0280 -0.0140 -0.0120 115 ALA B CB  
3146 N  N   . ALA B 116 ? 0.1289 0.0754 0.1032 -0.0146 -0.0081 -0.0017 116 ALA B N   
3147 C  CA  . ALA B 116 ? 0.1498 0.0692 0.0903 -0.0093 -0.0182 0.0049  116 ALA B CA  
3148 C  C   . ALA B 116 ? 0.1010 0.0675 0.1024 -0.0071 -0.0170 0.0010  116 ALA B C   
3149 O  O   . ALA B 116 ? 0.1182 0.0724 0.1030 -0.0114 -0.0024 0.0070  116 ALA B O   
3150 C  CB  . ALA B 116 ? 0.1528 0.0841 0.0974 -0.0234 -0.0027 0.0017  116 ALA B CB  
3151 N  N   . GLU B 117 ? 0.1130 0.0639 0.0883 -0.0054 -0.0054 -0.0052 117 GLU B N   
3152 C  CA  . GLU B 117 ? 0.1070 0.0714 0.0781 -0.0091 -0.0020 -0.0052 117 GLU B CA  
3153 C  C   . GLU B 117 ? 0.1254 0.0684 0.0768 -0.0179 -0.0097 0.0051  117 GLU B C   
3154 O  O   . GLU B 117 ? 0.1195 0.0879 0.1103 -0.0093 0.0015  0.0204  117 GLU B O   
3155 C  CB  . GLU B 117 ? 0.0970 0.0882 0.0861 -0.0109 -0.0116 0.0013  117 GLU B CB  
3156 C  CG  . GLU B 117 ? 0.1175 0.0771 0.0921 0.0023  -0.0182 -0.0003 117 GLU B CG  
3157 C  CD  . GLU B 117 ? 0.1041 0.0764 0.0784 -0.0043 0.0027  -0.0010 117 GLU B CD  
3158 O  OE1 . GLU B 117 ? 0.0954 0.0961 0.0983 0.0049  -0.0034 0.0005  117 GLU B OE1 
3159 O  OE2 . GLU B 117 ? 0.1255 0.0803 0.0917 -0.0035 -0.0242 -0.0027 117 GLU B OE2 
3160 N  N   . LEU B 118 ? 0.1112 0.0678 0.0930 -0.0078 -0.0222 -0.0030 118 LEU B N   
3161 C  CA  . LEU B 118 ? 0.1213 0.0610 0.0901 -0.0049 -0.0181 0.0030  118 LEU B CA  
3162 C  C   . LEU B 118 ? 0.1124 0.0613 0.0944 -0.0001 -0.0211 -0.0020 118 LEU B C   
3163 O  O   . LEU B 118 ? 0.1181 0.0694 0.0825 -0.0068 -0.0097 0.0015  118 LEU B O   
3164 C  CB  . LEU B 118 ? 0.1243 0.0798 0.0969 -0.0065 -0.0289 -0.0023 118 LEU B CB  
3165 C  CG  . LEU B 118 ? 0.1410 0.0900 0.0913 -0.0049 -0.0350 0.0071  118 LEU B CG  
3166 C  CD1 . LEU B 118 ? 0.1617 0.0848 0.1075 -0.0044 -0.0392 0.0198  118 LEU B CD1 
3167 C  CD2 . LEU B 118 ? 0.1339 0.1220 0.1375 -0.0057 -0.0414 0.0031  118 LEU B CD2 
3168 N  N   . HIS B 119 ? 0.1175 0.0605 0.0877 -0.0046 -0.0195 0.0010  119 HIS B N   
3169 C  CA  . HIS B 119 ? 0.1239 0.0689 0.0751 -0.0057 -0.0225 0.0006  119 HIS B CA  
3170 C  C   . HIS B 119 ? 0.1145 0.0643 0.0782 -0.0098 -0.0229 0.0055  119 HIS B C   
3171 O  O   . HIS B 119 ? 0.1324 0.0808 0.0850 -0.0043 -0.0121 0.0087  119 HIS B O   
3172 C  CB  . HIS B 119 ? 0.0964 0.0634 0.0872 -0.0027 -0.0149 0.0049  119 HIS B CB  
3173 C  CG  . HIS B 119 ? 0.0995 0.0802 0.0696 -0.0097 -0.0074 -0.0013 119 HIS B CG  
3174 N  ND1 . HIS B 119 ? 0.1018 0.0728 0.0741 -0.0074 0.0005  0.0052  119 HIS B ND1 
3175 C  CD2 . HIS B 119 ? 0.1101 0.0793 0.0769 -0.0019 -0.0076 0.0003  119 HIS B CD2 
3176 C  CE1 . HIS B 119 ? 0.1181 0.0798 0.0804 -0.0019 -0.0054 -0.0093 119 HIS B CE1 
3177 N  NE2 . HIS B 119 ? 0.0952 0.0922 0.0825 -0.0024 -0.0126 0.0049  119 HIS B NE2 
3178 N  N   . LEU B 120 ? 0.1211 0.0617 0.0905 -0.0031 -0.0174 0.0060  120 LEU B N   
3179 C  CA  . LEU B 120 ? 0.1213 0.0688 0.0992 0.0074  -0.0243 0.0034  120 LEU B CA  
3180 C  C   . LEU B 120 ? 0.1184 0.0621 0.0856 0.0049  -0.0156 0.0167  120 LEU B C   
3181 O  O   . LEU B 120 ? 0.1128 0.0716 0.0876 -0.0070 -0.0193 0.0060  120 LEU B O   
3182 C  CB  . LEU B 120 ? 0.1124 0.0817 0.1093 0.0015  -0.0381 0.0017  120 LEU B CB  
3183 C  CG  . LEU B 120 ? 0.1513 0.0943 0.1067 -0.0165 -0.0417 0.0015  120 LEU B CG  
3184 C  CD1 . LEU B 120 ? 0.2540 0.1350 0.1442 -0.0975 -0.0030 -0.0005 120 LEU B CD1 
3185 C  CD2 . LEU B 120 ? 0.1586 0.1545 0.1357 0.0151  -0.0542 -0.0159 120 LEU B CD2 
3186 N  N   . VAL B 121 ? 0.1288 0.0715 0.0834 -0.0098 -0.0148 0.0077  121 VAL B N   
3187 C  CA  . VAL B 121 ? 0.1379 0.0683 0.0989 -0.0135 -0.0057 0.0151  121 VAL B CA  
3188 C  C   . VAL B 121 ? 0.1368 0.0610 0.1032 -0.0109 -0.0135 0.0006  121 VAL B C   
3189 O  O   . VAL B 121 ? 0.1520 0.0729 0.0973 0.0043  -0.0185 0.0113  121 VAL B O   
3190 C  CB  . VAL B 121 ? 0.1454 0.0745 0.1096 -0.0178 -0.0041 0.0006  121 VAL B CB  
3191 C  CG1 . VAL B 121 ? 0.1286 0.1098 0.1177 -0.0148 0.0024  -0.0065 121 VAL B CG1 
3192 C  CG2 . VAL B 121 ? 0.1511 0.0832 0.1234 -0.0055 0.0013  -0.0068 121 VAL B CG2 
3193 N  N   . HIS B 122 ? 0.1184 0.0706 0.1009 -0.0124 -0.0163 0.0109  122 HIS B N   
3194 C  CA  . HIS B 122 ? 0.1278 0.0625 0.1014 -0.0080 -0.0107 0.0031  122 HIS B CA  
3195 C  C   . HIS B 122 ? 0.1152 0.0671 0.1033 0.0023  -0.0186 0.0028  122 HIS B C   
3196 O  O   . HIS B 122 ? 0.1433 0.0685 0.1145 -0.0111 -0.0239 0.0059  122 HIS B O   
3197 C  CB  . HIS B 122 ? 0.1202 0.0684 0.1234 -0.0060 -0.0111 -0.0003 122 HIS B CB  
3198 C  CG  . HIS B 122 ? 0.1164 0.0775 0.1102 -0.0073 -0.0054 0.0093  122 HIS B CG  
3199 N  ND1 . HIS B 122 ? 0.1040 0.0790 0.1123 -0.0046 -0.0160 0.0073  122 HIS B ND1 
3200 C  CD2 . HIS B 122 ? 0.1089 0.0976 0.1160 -0.0115 -0.0165 -0.0031 122 HIS B CD2 
3201 C  CE1 . HIS B 122 ? 0.0944 0.0910 0.1380 -0.0109 -0.0060 0.0057  122 HIS B CE1 
3202 N  NE2 . HIS B 122 ? 0.1171 0.0960 0.1360 -0.0110 -0.0192 0.0052  122 HIS B NE2 
3203 N  N   . TRP B 123 ? 0.1191 0.0608 0.1168 -0.0077 -0.0160 -0.0044 123 TRP B N   
3204 C  CA  . TRP B 123 ? 0.1203 0.0714 0.1035 -0.0013 -0.0091 -0.0003 123 TRP B CA  
3205 C  C   . TRP B 123 ? 0.1089 0.0609 0.1290 -0.0160 -0.0071 -0.0098 123 TRP B C   
3206 O  O   . TRP B 123 ? 0.1102 0.0859 0.1325 0.0017  -0.0157 -0.0066 123 TRP B O   
3207 C  CB  . TRP B 123 ? 0.1617 0.1067 0.1052 -0.0359 -0.0119 -0.0015 123 TRP B CB  
3208 C  CG  . TRP B 123 ? 0.1535 0.0917 0.1245 -0.0328 -0.0051 -0.0007 123 TRP B CG  
3209 C  CD1 . TRP B 123 ? 0.1974 0.0966 0.1227 -0.0296 -0.0003 0.0005  123 TRP B CD1 
3210 C  CD2 . TRP B 123 ? 0.1897 0.0750 0.1268 -0.0310 -0.0109 0.0111  123 TRP B CD2 
3211 N  NE1 . TRP B 123 ? 0.2429 0.0790 0.1340 -0.0232 -0.0193 0.0034  123 TRP B NE1 
3212 C  CE2 . TRP B 123 ? 0.2412 0.0794 0.1342 -0.0252 -0.0274 0.0121  123 TRP B CE2 
3213 C  CE3 . TRP B 123 ? 0.2261 0.0681 0.1413 -0.0428 0.0122  0.0115  123 TRP B CE3 
3214 C  CZ2 . TRP B 123 ? 0.3021 0.0751 0.1747 -0.0136 -0.0205 0.0083  123 TRP B CZ2 
3215 C  CZ3 . TRP B 123 ? 0.2994 0.0848 0.1401 -0.0346 0.0054  -0.0028 123 TRP B CZ3 
3216 C  CH2 . TRP B 123 ? 0.3052 0.0799 0.1534 0.0026  -0.0003 0.0143  123 TRP B CH2 
3217 N  N   . ASN B 124 ? 0.1139 0.0687 0.1225 -0.0038 -0.0041 -0.0052 124 ASN B N   
3218 C  CA  . ASN B 124 ? 0.1384 0.0732 0.1212 0.0073  0.0012  -0.0208 124 ASN B CA  
3219 C  C   . ASN B 124 ? 0.1332 0.0851 0.1344 0.0093  -0.0060 -0.0329 124 ASN B C   
3220 O  O   . ASN B 124 ? 0.1367 0.0876 0.1238 0.0098  -0.0037 -0.0043 124 ASN B O   
3221 C  CB  . ASN B 124 ? 0.1463 0.0852 0.1261 0.0012  0.0127  -0.0121 124 ASN B CB  
3222 C  CG  . ASN B 124 ? 0.1636 0.0751 0.1342 -0.0093 0.0154  -0.0178 124 ASN B CG  
3223 O  OD1 . ASN B 124 ? 0.1685 0.0855 0.1675 0.0185  0.0204  -0.0207 124 ASN B OD1 
3224 N  ND2 . ASN B 124 ? 0.2102 0.0966 0.1290 -0.0065 0.0040  -0.0201 124 ASN B ND2 
3225 N  N   . THR B 125 ? 0.1438 0.0843 0.1484 0.0132  -0.0148 -0.0159 125 THR B N   
3226 C  CA  . THR B 125 ? 0.1668 0.0873 0.1956 0.0302  -0.0147 -0.0046 125 THR B CA  
3227 C  C   . THR B 125 ? 0.1967 0.0750 0.2158 0.0296  -0.0233 0.0074  125 THR B C   
3228 O  O   . THR B 125 ? 0.1853 0.1001 0.1917 0.0166  -0.0118 0.0046  125 THR B O   
3229 C  CB  . THR B 125 ? 0.1503 0.1265 0.2472 0.0350  -0.0198 0.0197  125 THR B CB  
3230 O  OG1 . THR B 125 ? 0.1937 0.1729 0.3336 0.0705  0.0515  0.0173  125 THR B OG1 
3231 C  CG2 . THR B 125 ? 0.2043 0.1275 0.3007 -0.0037 -0.0974 0.0133  125 THR B CG2 
3232 N  N   A LYS B 126 ? 0.1738 0.1052 0.1875 0.0434  0.0178  -0.0071 127 LYS B N   
3233 N  N   B LYS B 126 ? 0.1841 0.0403 0.1613 0.0142  -0.0308 0.0010  127 LYS B N   
3234 C  CA  A LYS B 126 ? 0.2303 0.1483 0.1844 -0.0137 0.0297  -0.0335 127 LYS B CA  
3235 C  CA  B LYS B 126 ? 0.2113 0.0586 0.1632 -0.0059 0.0080  -0.0217 127 LYS B CA  
3236 C  C   A LYS B 126 ? 0.2436 0.0460 0.1372 -0.0059 0.0041  0.0049  127 LYS B C   
3237 C  C   B LYS B 126 ? 0.2270 0.0873 0.1527 0.0068  -0.0086 -0.0216 127 LYS B C   
3238 O  O   A LYS B 126 ? 0.2249 0.0663 0.1270 -0.0086 -0.0055 -0.0078 127 LYS B O   
3239 O  O   B LYS B 126 ? 0.2432 0.1094 0.1873 -0.0167 -0.0419 -0.0427 127 LYS B O   
3240 C  CB  A LYS B 126 ? 0.2084 0.1178 0.1583 -0.0071 -0.0027 -0.0157 127 LYS B CB  
3241 C  CB  B LYS B 126 ? 0.1879 0.1055 0.1508 0.0023  0.0027  -0.0186 127 LYS B CB  
3242 C  CG  A LYS B 126 ? 0.1595 0.1859 0.1588 -0.0122 -0.0527 -0.0263 127 LYS B CG  
3243 C  CG  B LYS B 126 ? 0.2019 0.1080 0.1777 0.0303  0.0480  0.0211  127 LYS B CG  
3244 C  CD  A LYS B 126 ? 0.1577 0.2331 0.1749 -0.0031 0.0085  -0.0397 127 LYS B CD  
3245 C  CD  B LYS B 126 ? 0.2308 0.1592 0.1641 0.0206  0.0137  0.0277  127 LYS B CD  
3246 C  CE  A LYS B 126 ? 0.1554 0.2224 0.1818 -0.0491 -0.0136 0.0017  127 LYS B CE  
3247 C  CE  B LYS B 126 ? 0.3503 0.1415 0.1803 0.0252  0.0078  0.0326  127 LYS B CE  
3248 N  NZ  A LYS B 126 ? 0.2754 0.2320 0.1474 0.0551  0.0001  -0.0076 127 LYS B NZ  
3249 N  NZ  B LYS B 126 ? 0.2327 0.2375 0.1827 0.0247  -0.0100 0.0460  127 LYS B NZ  
3250 N  N   . TYR B 127 ? 0.1962 0.0782 0.1307 -0.0052 0.0019  -0.0006 128 TYR B N   
3251 C  CA  . TYR B 127 ? 0.2152 0.0710 0.1509 -0.0040 -0.0186 -0.0063 128 TYR B CA  
3252 C  C   . TYR B 127 ? 0.1686 0.0846 0.1475 -0.0146 0.0003  -0.0048 128 TYR B C   
3253 O  O   . TYR B 127 ? 0.1819 0.0916 0.1612 -0.0122 -0.0089 -0.0026 128 TYR B O   
3254 C  CB  . TYR B 127 ? 0.2010 0.0887 0.1732 -0.0027 -0.0151 -0.0108 128 TYR B CB  
3255 C  CG  . TYR B 127 ? 0.1550 0.0876 0.1592 -0.0065 -0.0223 -0.0118 128 TYR B CG  
3256 C  CD1 . TYR B 127 ? 0.1863 0.0992 0.1826 0.0003  -0.0458 -0.0186 128 TYR B CD1 
3257 C  CD2 . TYR B 127 ? 0.1509 0.0976 0.1333 -0.0044 -0.0141 -0.0076 128 TYR B CD2 
3258 C  CE1 . TYR B 127 ? 0.1985 0.0992 0.1598 0.0035  -0.0196 -0.0223 128 TYR B CE1 
3259 C  CE2 . TYR B 127 ? 0.1460 0.1058 0.1436 0.0003  -0.0020 -0.0344 128 TYR B CE2 
3260 C  CZ  . TYR B 127 ? 0.1561 0.1146 0.1502 0.0182  -0.0193 -0.0155 128 TYR B CZ  
3261 O  OH  . TYR B 127 ? 0.2351 0.1342 0.1449 0.0232  -0.0294 -0.0384 128 TYR B OH  
3262 N  N   . GLY B 128 ? 0.1683 0.0905 0.1482 -0.0186 -0.0197 0.0043  129 GLY B N   
3263 C  CA  . GLY B 128 ? 0.2448 0.0793 0.1624 -0.0326 0.0130  0.0147  129 GLY B CA  
3264 C  C   . GLY B 128 ? 0.2278 0.0916 0.1367 -0.0015 -0.0093 0.0184  129 GLY B C   
3265 O  O   . GLY B 128 ? 0.2897 0.1074 0.1435 -0.0126 -0.0370 0.0329  129 GLY B O   
3266 N  N   . ASP B 129 ? 0.2520 0.1049 0.1166 0.0151  -0.0071 -0.0015 130 ASP B N   
3267 C  CA  . ASP B 129 ? 0.3294 0.0948 0.1314 -0.0071 0.0097  0.0035  130 ASP B CA  
3268 C  C   . ASP B 129 ? 0.3043 0.1061 0.1368 -0.0041 -0.0296 0.0068  130 ASP B C   
3269 O  O   . ASP B 129 ? 0.3481 0.1044 0.1141 0.0270  0.0010  0.0037  130 ASP B O   
3270 C  CB  . ASP B 129 ? 0.2606 0.1600 0.1946 -0.0197 0.0267  0.0274  130 ASP B CB  
3271 C  CG  . ASP B 129 ? 0.2556 0.0996 0.1378 0.0114  0.0108  0.0156  130 ASP B CG  
3272 O  OD1 . ASP B 129 ? 0.3140 0.2166 0.2318 0.0023  -0.0489 -0.0533 130 ASP B OD1 
3273 O  OD2 . ASP B 129 ? 0.3289 0.1583 0.2215 -0.0109 0.1019  0.0216  130 ASP B OD2 
3274 N  N   . PHE B 130 ? 0.2881 0.1018 0.1181 0.0048  0.0245  0.0071  131 PHE B N   
3275 C  CA  . PHE B 130 ? 0.2504 0.1057 0.1031 -0.0044 0.0012  0.0059  131 PHE B CA  
3276 C  C   . PHE B 130 ? 0.2293 0.1030 0.1414 -0.0187 0.0351  0.0126  131 PHE B C   
3277 O  O   . PHE B 130 ? 0.2020 0.1106 0.1248 -0.0231 0.0315  0.0006  131 PHE B O   
3278 C  CB  . PHE B 130 ? 0.2418 0.1092 0.1421 -0.0001 0.0233  -0.0148 131 PHE B CB  
3279 C  CG  . PHE B 130 ? 0.2048 0.1026 0.1685 0.0027  0.0282  -0.0156 131 PHE B CG  
3280 C  CD1 . PHE B 130 ? 0.2152 0.1191 0.1381 -0.0240 0.0098  -0.0182 131 PHE B CD1 
3281 C  CD2 . PHE B 130 ? 0.2531 0.1263 0.1673 -0.0260 0.0401  -0.0340 131 PHE B CD2 
3282 C  CE1 . PHE B 130 ? 0.2143 0.1411 0.1720 -0.0364 0.0007  -0.0263 131 PHE B CE1 
3283 C  CE2 . PHE B 130 ? 0.2134 0.1801 0.2159 0.0035  0.0076  -0.0399 131 PHE B CE2 
3284 C  CZ  . PHE B 130 ? 0.2231 0.1653 0.2455 -0.0243 -0.0172 -0.0504 131 PHE B CZ  
3285 N  N   . GLY B 131 ? 0.2667 0.1404 0.1536 -0.0452 0.0522  0.0065  132 GLY B N   
3286 C  CA  . GLY B 131 ? 0.2639 0.1718 0.1483 -0.0562 0.0773  0.0261  132 GLY B CA  
3287 C  C   . GLY B 131 ? 0.2418 0.1825 0.1765 -0.0571 0.0728  0.0286  132 GLY B C   
3288 O  O   . GLY B 131 ? 0.2362 0.1305 0.2741 -0.0483 0.0357  -0.0121 132 GLY B O   
3289 N  N   . LYS B 132 ? 0.2140 0.1189 0.1890 -0.0480 0.0359  0.0114  133 LYS B N   
3290 C  CA  . LYS B 132 ? 0.2063 0.1074 0.1840 -0.0397 0.0151  0.0148  133 LYS B CA  
3291 C  C   . LYS B 132 ? 0.2043 0.1036 0.1708 -0.0666 0.0188  -0.0107 133 LYS B C   
3292 O  O   . LYS B 132 ? 0.1692 0.1301 0.1703 -0.0436 0.0023  -0.0219 133 LYS B O   
3293 C  CB  . LYS B 132 ? 0.1967 0.1112 0.2004 -0.0315 -0.0087 -0.0082 133 LYS B CB  
3294 C  CG  . LYS B 132 ? 0.1938 0.1474 0.3887 -0.0333 -0.0023 0.0489  133 LYS B CG  
3295 C  CD  . LYS B 132 ? 0.3348 0.3621 0.9961 -0.1765 -0.2951 0.3903  133 LYS B CD  
3296 C  CE  . LYS B 132 ? 0.3397 0.2060 0.6643 -0.1127 -0.1741 0.0513  133 LYS B CE  
3297 N  NZ  . LYS B 132 ? 0.5314 0.4932 0.4679 -0.0918 -0.1747 -0.0829 133 LYS B NZ  
3298 N  N   . ALA B 133 ? 0.1680 0.1133 0.1483 -0.0472 0.0187  -0.0012 134 ALA B N   
3299 C  CA  . ALA B 133 ? 0.1509 0.1094 0.1259 -0.0359 0.0024  0.0041  134 ALA B CA  
3300 C  C   . ALA B 133 ? 0.1524 0.1139 0.1168 -0.0432 0.0109  -0.0066 134 ALA B C   
3301 O  O   . ALA B 133 ? 0.1358 0.1333 0.1130 -0.0377 0.0126  -0.0081 134 ALA B O   
3302 C  CB  . ALA B 133 ? 0.1457 0.1263 0.1077 -0.0390 -0.0035 0.0027  134 ALA B CB  
3303 N  N   . VAL B 134 ? 0.1721 0.1027 0.1348 -0.0346 0.0384  -0.0046 135 VAL B N   
3304 C  CA  . VAL B 134 ? 0.1847 0.1168 0.1388 -0.0359 0.0348  0.0062  135 VAL B CA  
3305 C  C   . VAL B 134 ? 0.1557 0.1238 0.1598 -0.0264 0.0362  -0.0148 135 VAL B C   
3306 O  O   . VAL B 134 ? 0.1671 0.1304 0.1748 -0.0199 0.0456  -0.0078 135 VAL B O   
3307 C  CB  . VAL B 134 ? 0.2037 0.1202 0.1606 -0.0331 0.0307  -0.0153 135 VAL B CB  
3308 C  CG1 . VAL B 134 ? 0.2414 0.1650 0.1807 -0.0421 0.0115  -0.0208 135 VAL B CG1 
3309 C  CG2 . VAL B 134 ? 0.2021 0.1450 0.1819 -0.0355 0.0640  -0.0192 135 VAL B CG2 
3310 N  N   . GLN B 135 ? 0.1721 0.1159 0.1586 -0.0274 0.0239  -0.0115 136 GLN B N   
3311 C  CA  . GLN B 135 ? 0.1700 0.1360 0.2029 -0.0414 0.0038  -0.0197 136 GLN B CA  
3312 C  C   . GLN B 135 ? 0.1331 0.1343 0.1825 -0.0195 -0.0137 -0.0195 136 GLN B C   
3313 O  O   . GLN B 135 ? 0.1590 0.1939 0.1977 -0.0502 -0.0153 -0.0399 136 GLN B O   
3314 C  CB  . GLN B 135 ? 0.2035 0.1620 0.1895 -0.0628 0.0073  0.0083  136 GLN B CB  
3315 C  CG  . GLN B 135 ? 0.2289 0.2193 0.2444 -0.0971 0.0449  0.0326  136 GLN B CG  
3316 C  CD  . GLN B 135 ? 0.1988 0.2378 0.3806 -0.0599 0.0318  0.0697  136 GLN B CD  
3317 O  OE1 . GLN B 135 ? 0.2998 0.3930 0.4298 -0.0922 -0.0581 0.1297  136 GLN B OE1 
3318 N  NE2 . GLN B 135 ? 0.2958 0.2640 0.3932 -0.1272 -0.0017 0.1030  136 GLN B NE2 
3319 N  N   . GLN B 136 ? 0.1284 0.1277 0.1545 -0.0147 -0.0030 -0.0166 137 GLN B N   
3320 C  CA  . GLN B 136 ? 0.1474 0.1383 0.1190 -0.0176 -0.0102 -0.0368 137 GLN B CA  
3321 C  C   . GLN B 136 ? 0.1396 0.1325 0.1175 -0.0105 -0.0193 -0.0174 137 GLN B C   
3322 O  O   . GLN B 136 ? 0.1476 0.1182 0.1062 -0.0148 -0.0052 -0.0166 137 GLN B O   
3323 C  CB  . GLN B 136 ? 0.1528 0.1166 0.1696 -0.0051 -0.0226 -0.0175 137 GLN B CB  
3324 C  CG  . GLN B 136 ? 0.2671 0.1432 0.1529 0.0140  -0.0122 -0.0034 137 GLN B CG  
3325 C  CD  . GLN B 136 ? 0.2153 0.1720 0.2322 0.0241  0.0137  -0.0001 137 GLN B CD  
3326 O  OE1 . GLN B 136 ? 0.2197 0.1607 0.2472 -0.0135 0.0126  -0.0820 137 GLN B OE1 
3327 N  NE2 . GLN B 136 ? 0.3048 0.2348 0.2136 -0.0243 0.0348  -0.0329 137 GLN B NE2 
3328 N  N   . PRO B 137 ? 0.1181 0.1570 0.1191 -0.0010 -0.0098 -0.0249 138 PRO B N   
3329 C  CA  . PRO B 137 ? 0.1398 0.1554 0.1023 0.0132  -0.0113 0.0119  138 PRO B CA  
3330 C  C   . PRO B 137 ? 0.1333 0.1589 0.1067 0.0083  -0.0196 -0.0006 138 PRO B C   
3331 O  O   . PRO B 137 ? 0.2034 0.1430 0.1849 0.0196  -0.0068 0.0253  138 PRO B O   
3332 C  CB  . PRO B 137 ? 0.1711 0.2325 0.0992 0.0070  -0.0146 0.0110  138 PRO B CB  
3333 C  CG  . PRO B 137 ? 0.4275 0.2989 0.1312 -0.0575 -0.0590 -0.0302 138 PRO B CG  
3334 C  CD  . PRO B 137 ? 0.1877 0.2384 0.1124 -0.0487 -0.0124 -0.0537 138 PRO B CD  
3335 N  N   . ASP B 138 ? 0.1518 0.1421 0.0930 0.0097  -0.0148 -0.0147 139 ASP B N   
3336 C  CA  . ASP B 138 ? 0.1479 0.1272 0.0970 -0.0044 -0.0012 -0.0103 139 ASP B CA  
3337 C  C   . ASP B 138 ? 0.1182 0.1054 0.1031 -0.0065 -0.0070 -0.0054 139 ASP B C   
3338 O  O   . ASP B 138 ? 0.1335 0.1114 0.1204 0.0015  0.0024  -0.0035 139 ASP B O   
3339 C  CB  . ASP B 138 ? 0.1933 0.1465 0.1193 -0.0082 0.0115  -0.0219 139 ASP B CB  
3340 C  CG  . ASP B 138 ? 0.1811 0.1743 0.1196 0.0221  0.0057  -0.0260 139 ASP B CG  
3341 O  OD1 . ASP B 138 ? 0.1995 0.1243 0.1393 0.0119  -0.0041 -0.0388 139 ASP B OD1 
3342 O  OD2 . ASP B 138 ? 0.2163 0.1961 0.1623 0.0428  0.0148  -0.0465 139 ASP B OD2 
3343 N  N   . GLY B 139 ? 0.1319 0.0874 0.0938 -0.0055 -0.0001 -0.0121 140 GLY B N   
3344 C  CA  . GLY B 139 ? 0.1473 0.0912 0.0881 -0.0098 -0.0092 0.0003  140 GLY B CA  
3345 C  C   . GLY B 139 ? 0.1182 0.0755 0.0970 -0.0088 -0.0049 -0.0027 140 GLY B C   
3346 O  O   . GLY B 139 ? 0.1191 0.0832 0.1023 0.0063  -0.0057 0.0017  140 GLY B O   
3347 N  N   . LEU B 140 ? 0.0944 0.0732 0.1036 -0.0027 -0.0080 -0.0015 141 LEU B N   
3348 C  CA  . LEU B 140 ? 0.0984 0.0705 0.1155 -0.0035 0.0008  -0.0120 141 LEU B CA  
3349 C  C   . LEU B 140 ? 0.0892 0.0662 0.0980 0.0046  -0.0010 -0.0048 141 LEU B C   
3350 O  O   . LEU B 140 ? 0.1036 0.0747 0.0947 -0.0060 -0.0063 0.0077  141 LEU B O   
3351 C  CB  . LEU B 140 ? 0.1108 0.0864 0.1075 0.0010  0.0062  -0.0062 141 LEU B CB  
3352 C  CG  . LEU B 140 ? 0.1211 0.1023 0.1250 0.0074  0.0099  0.0115  141 LEU B CG  
3353 C  CD1 . LEU B 140 ? 0.1194 0.1111 0.1263 0.0115  0.0175  -0.0049 141 LEU B CD1 
3354 C  CD2 . LEU B 140 ? 0.1484 0.1148 0.1544 0.0131  0.0201  0.0214  141 LEU B CD2 
3355 N  N   . ALA B 141 ? 0.0917 0.0667 0.1049 -0.0092 -0.0082 0.0027  142 ALA B N   
3356 C  CA  . ALA B 141 ? 0.1119 0.0648 0.1068 -0.0142 0.0024  -0.0024 142 ALA B CA  
3357 C  C   . ALA B 141 ? 0.1024 0.0710 0.0967 -0.0141 -0.0012 0.0118  142 ALA B C   
3358 O  O   . ALA B 141 ? 0.1262 0.0797 0.1005 -0.0049 -0.0177 0.0057  142 ALA B O   
3359 C  CB  . ALA B 141 ? 0.1052 0.0913 0.1227 -0.0110 0.0041  0.0085  142 ALA B CB  
3360 N  N   . VAL B 142 ? 0.0984 0.0619 0.0948 -0.0057 -0.0068 0.0013  143 VAL B N   
3361 C  CA  . VAL B 142 ? 0.1058 0.0724 0.0877 0.0010  -0.0109 0.0057  143 VAL B CA  
3362 C  C   . VAL B 142 ? 0.1081 0.0728 0.0738 0.0010  -0.0005 -0.0063 143 VAL B C   
3363 O  O   . VAL B 142 ? 0.1058 0.0790 0.0829 -0.0049 -0.0115 0.0124  143 VAL B O   
3364 C  CB  . VAL B 142 ? 0.1074 0.0829 0.0913 0.0078  -0.0137 0.0065  143 VAL B CB  
3365 C  CG1 . VAL B 142 ? 0.1208 0.1061 0.0872 0.0099  -0.0170 -0.0065 143 VAL B CG1 
3366 C  CG2 . VAL B 142 ? 0.1079 0.1211 0.0964 -0.0157 -0.0043 0.0182  143 VAL B CG2 
3367 N  N   . LEU B 143 ? 0.1032 0.0588 0.0974 -0.0085 -0.0164 0.0104  144 LEU B N   
3368 C  CA  . LEU B 143 ? 0.0935 0.0749 0.1028 -0.0082 -0.0243 0.0107  144 LEU B CA  
3369 C  C   . LEU B 143 ? 0.0877 0.0772 0.0942 -0.0153 -0.0155 0.0068  144 LEU B C   
3370 O  O   . LEU B 143 ? 0.1172 0.0874 0.0888 -0.0043 -0.0074 0.0040  144 LEU B O   
3371 C  CB  . LEU B 143 ? 0.1083 0.0989 0.1175 -0.0136 -0.0184 0.0105  144 LEU B CB  
3372 C  CG  . LEU B 143 ? 0.1031 0.1096 0.1512 -0.0065 -0.0159 0.0037  144 LEU B CG  
3373 C  CD1 . LEU B 143 ? 0.1123 0.1526 0.1789 -0.0291 -0.0212 0.0489  144 LEU B CD1 
3374 C  CD2 . LEU B 143 ? 0.1023 0.1733 0.1650 -0.0146 -0.0250 0.0154  144 LEU B CD2 
3375 N  N   . GLY B 144 ? 0.0857 0.0714 0.0913 -0.0125 -0.0164 0.0032  145 GLY B N   
3376 C  CA  . GLY B 144 ? 0.1001 0.0740 0.0900 -0.0074 -0.0068 -0.0057 145 GLY B CA  
3377 C  C   . GLY B 144 ? 0.1032 0.0668 0.0839 -0.0060 -0.0093 0.0027  145 GLY B C   
3378 O  O   . GLY B 144 ? 0.1046 0.0904 0.0940 -0.0183 -0.0003 -0.0031 145 GLY B O   
3379 N  N   . ILE B 145 ? 0.0961 0.0706 0.0887 -0.0099 -0.0136 -0.0024 146 ILE B N   
3380 C  CA  . ILE B 145 ? 0.0878 0.0648 0.1090 -0.0071 -0.0226 0.0059  146 ILE B CA  
3381 C  C   . ILE B 145 ? 0.0957 0.0780 0.0869 -0.0153 -0.0212 0.0032  146 ILE B C   
3382 O  O   . ILE B 145 ? 0.1200 0.0680 0.1046 -0.0104 -0.0081 0.0021  146 ILE B O   
3383 C  CB  . ILE B 145 ? 0.1083 0.0793 0.1229 -0.0005 -0.0403 -0.0015 146 ILE B CB  
3384 C  CG1 . ILE B 145 ? 0.1356 0.0930 0.1529 0.0201  -0.0445 0.0046  146 ILE B CG1 
3385 C  CG2 . ILE B 145 ? 0.1067 0.1064 0.1556 -0.0238 -0.0476 0.0012  146 ILE B CG2 
3386 C  CD1 . ILE B 145 ? 0.1222 0.1064 0.1509 -0.0023 -0.0445 0.0175  146 ILE B CD1 
3387 N  N   . PHE B 146 ? 0.0944 0.0697 0.0923 -0.0057 -0.0137 0.0035  147 PHE B N   
3388 C  CA  . PHE B 146 ? 0.1098 0.0634 0.0939 -0.0007 -0.0132 0.0017  147 PHE B CA  
3389 C  C   . PHE B 146 ? 0.0989 0.0776 0.0974 -0.0192 -0.0103 0.0007  147 PHE B C   
3390 O  O   . PHE B 146 ? 0.1112 0.0872 0.1200 -0.0065 -0.0239 -0.0060 147 PHE B O   
3391 C  CB  . PHE B 146 ? 0.1044 0.0740 0.1066 -0.0080 -0.0252 0.0126  147 PHE B CB  
3392 C  CG  . PHE B 146 ? 0.0887 0.0746 0.0925 0.0000  -0.0163 0.0155  147 PHE B CG  
3393 C  CD1 . PHE B 146 ? 0.0964 0.0798 0.1042 0.0099  -0.0199 0.0055  147 PHE B CD1 
3394 C  CD2 . PHE B 146 ? 0.1130 0.0737 0.1154 -0.0020 -0.0124 0.0241  147 PHE B CD2 
3395 C  CE1 . PHE B 146 ? 0.1076 0.0800 0.1142 -0.0087 -0.0120 0.0063  147 PHE B CE1 
3396 C  CE2 . PHE B 146 ? 0.0996 0.0877 0.1106 -0.0085 -0.0097 0.0094  147 PHE B CE2 
3397 C  CZ  . PHE B 146 ? 0.0938 0.0815 0.1062 -0.0046 -0.0076 0.0063  147 PHE B CZ  
3398 N  N   . LEU B 147 ? 0.1142 0.0731 0.1045 -0.0189 -0.0078 -0.0035 148 LEU B N   
3399 C  CA  . LEU B 147 ? 0.1387 0.0781 0.0925 -0.0277 -0.0203 -0.0071 148 LEU B CA  
3400 C  C   . LEU B 147 ? 0.1255 0.0746 0.1067 -0.0120 -0.0068 -0.0024 148 LEU B C   
3401 O  O   . LEU B 147 ? 0.1221 0.0844 0.1196 -0.0049 -0.0073 0.0031  148 LEU B O   
3402 C  CB  . LEU B 147 ? 0.1512 0.0804 0.1087 -0.0108 -0.0251 -0.0010 148 LEU B CB  
3403 C  CG  . LEU B 147 ? 0.1555 0.0806 0.1134 -0.0192 -0.0340 -0.0074 148 LEU B CG  
3404 C  CD1 . LEU B 147 ? 0.1967 0.0819 0.1160 -0.0138 -0.0269 -0.0038 148 LEU B CD1 
3405 C  CD2 . LEU B 147 ? 0.1814 0.1009 0.1064 -0.0177 -0.0241 0.0010  148 LEU B CD2 
3406 N  N   . LYS B 148 ? 0.1430 0.0618 0.1307 -0.0197 -0.0206 -0.0054 149 LYS B N   
3407 C  CA  . LYS B 148 ? 0.1583 0.0688 0.1413 -0.0148 -0.0189 -0.0057 149 LYS B CA  
3408 C  C   . LYS B 148 ? 0.1316 0.0812 0.1587 -0.0146 -0.0276 -0.0038 149 LYS B C   
3409 O  O   . LYS B 148 ? 0.1633 0.1211 0.1381 0.0236  -0.0370 -0.0230 149 LYS B O   
3410 C  CB  . LYS B 148 ? 0.1606 0.1063 0.1283 -0.0258 -0.0182 0.0041  149 LYS B CB  
3411 C  CG  . LYS B 148 ? 0.1731 0.1272 0.1474 -0.0239 -0.0015 0.0241  149 LYS B CG  
3412 C  CD  . LYS B 148 ? 0.2430 0.2152 0.2193 -0.0593 0.0586  0.0197  149 LYS B CD  
3413 C  CE  . LYS B 148 ? 0.2606 0.3181 0.3537 -0.0267 0.1101  0.0641  149 LYS B CE  
3414 N  NZ  . LYS B 148 ? 0.6560 0.6110 0.4783 -0.2825 0.1081  0.2128  149 LYS B NZ  
3415 N  N   . VAL B 149 ? 0.1609 0.0841 0.1647 0.0013  -0.0342 -0.0209 150 VAL B N   
3416 C  CA  . VAL B 149 ? 0.1675 0.0778 0.1669 -0.0044 -0.0237 -0.0269 150 VAL B CA  
3417 C  C   . VAL B 149 ? 0.1772 0.0825 0.1447 -0.0041 -0.0063 -0.0076 150 VAL B C   
3418 O  O   . VAL B 149 ? 0.1911 0.1061 0.1631 -0.0074 -0.0256 0.0006  150 VAL B O   
3419 C  CB  . VAL B 149 ? 0.1559 0.1001 0.1678 -0.0005 -0.0156 -0.0194 150 VAL B CB  
3420 C  CG1 . VAL B 149 ? 0.1542 0.1342 0.1643 -0.0052 -0.0098 -0.0220 150 VAL B CG1 
3421 C  CG2 . VAL B 149 ? 0.1713 0.1393 0.1737 -0.0183 -0.0008 -0.0015 150 VAL B CG2 
3422 N  N   . GLY B 150 ? 0.1717 0.0978 0.1548 -0.0274 -0.0406 -0.0076 151 GLY B N   
3423 C  CA  . GLY B 150 ? 0.1772 0.1196 0.1678 -0.0410 -0.0509 0.0179  151 GLY B CA  
3424 C  C   . GLY B 150 ? 0.1845 0.1076 0.1513 -0.0548 -0.0434 -0.0003 151 GLY B C   
3425 O  O   . GLY B 150 ? 0.2067 0.1273 0.1773 -0.0278 -0.0344 -0.0242 151 GLY B O   
3426 N  N   . SER B 151 ? 0.1727 0.1407 0.1915 -0.0386 -0.0335 -0.0167 152 SER B N   
3427 C  CA  . SER B 151 ? 0.1794 0.1354 0.2127 -0.0397 -0.0684 -0.0148 152 SER B CA  
3428 C  C   . SER B 151 ? 0.1746 0.1194 0.1537 -0.0127 -0.0344 -0.0285 152 SER B C   
3429 O  O   . SER B 151 ? 0.1967 0.1245 0.1615 -0.0346 -0.0452 -0.0182 152 SER B O   
3430 C  CB  . SER B 151 ? 0.1774 0.3005 0.2682 -0.0307 -0.0397 -0.0019 152 SER B CB  
3431 O  OG  . SER B 151 ? 0.3009 0.4287 0.3587 -0.1344 0.0130  -0.0031 152 SER B OG  
3432 N  N   . ALA B 152 ? 0.2154 0.1254 0.1861 -0.0166 -0.0804 -0.0122 153 ALA B N   
3433 C  CA  . ALA B 152 ? 0.1862 0.1177 0.1407 -0.0081 -0.0318 -0.0260 153 ALA B CA  
3434 C  C   . ALA B 152 ? 0.2152 0.1281 0.1498 0.0015  -0.0597 -0.0232 153 ALA B C   
3435 O  O   . ALA B 152 ? 0.2131 0.1396 0.2009 0.0046  -0.0337 -0.0253 153 ALA B O   
3436 C  CB  . ALA B 152 ? 0.2930 0.1627 0.1694 0.0019  -0.0864 -0.0373 153 ALA B CB  
3437 N  N   . LYS B 153 ? 0.2581 0.1085 0.1565 -0.0130 -0.0753 -0.0051 154 LYS B N   
3438 C  CA  . LYS B 153 ? 0.2106 0.1259 0.1890 0.0193  -0.0662 -0.0032 154 LYS B CA  
3439 C  C   . LYS B 153 ? 0.1825 0.1268 0.1816 0.0085  -0.0461 -0.0144 154 LYS B C   
3440 O  O   . LYS B 153 ? 0.2014 0.1386 0.1509 -0.0007 -0.0769 -0.0205 154 LYS B O   
3441 C  CB  . LYS B 153 ? 0.2888 0.1211 0.1870 -0.0240 -0.0953 0.0013  154 LYS B CB  
3442 C  CG  . LYS B 153 ? 0.3264 0.1115 0.2328 -0.0308 -0.0895 -0.0263 154 LYS B CG  
3443 C  CD  . LYS B 153 ? 0.3497 0.1298 0.2405 0.0060  -0.1208 -0.0087 154 LYS B CD  
3444 C  CE  . LYS B 153 ? 0.3136 0.1800 0.1896 0.0037  -0.0719 -0.0115 154 LYS B CE  
3445 N  NZ  . LYS B 153 ? 0.2287 0.2321 0.2953 -0.0346 -0.0278 -0.0793 154 LYS B NZ  
3446 N  N   . PRO B 154 ? 0.2231 0.1356 0.1891 0.0071  -0.0738 -0.0093 155 PRO B N   
3447 C  CA  . PRO B 154 ? 0.2343 0.1532 0.2035 -0.0032 -0.0995 -0.0059 155 PRO B CA  
3448 C  C   . PRO B 154 ? 0.2387 0.1798 0.1700 0.0197  -0.1062 -0.0093 155 PRO B C   
3449 O  O   . PRO B 154 ? 0.2984 0.1761 0.1745 -0.0096 -0.1063 0.0088  155 PRO B O   
3450 C  CB  . PRO B 154 ? 0.2215 0.1975 0.2184 0.0252  -0.0744 -0.0060 155 PRO B CB  
3451 C  CG  . PRO B 154 ? 0.2434 0.2451 0.2461 -0.0104 -0.0734 0.0048  155 PRO B CG  
3452 C  CD  . PRO B 154 ? 0.2125 0.1835 0.2117 -0.0062 -0.0507 0.0137  155 PRO B CD  
3453 N  N   . GLY B 155 ? 0.2520 0.1435 0.1828 0.0406  -0.0776 -0.0172 156 GLY B N   
3454 C  CA  . GLY B 155 ? 0.2542 0.1236 0.2578 0.0027  -0.0758 -0.0194 156 GLY B CA  
3455 C  C   . GLY B 155 ? 0.2808 0.1048 0.1797 -0.0031 -0.0773 0.0142  156 GLY B C   
3456 O  O   . GLY B 155 ? 0.2827 0.1166 0.2784 0.0113  -0.0577 0.0278  156 GLY B O   
3457 N  N   . LEU B 156 ? 0.2365 0.1360 0.1598 -0.0108 -0.0745 -0.0006 157 LEU B N   
3458 C  CA  . LEU B 156 ? 0.2319 0.1172 0.1371 -0.0162 -0.0666 -0.0142 157 LEU B CA  
3459 C  C   . LEU B 156 ? 0.2531 0.1083 0.1622 -0.0078 -0.0782 -0.0176 157 LEU B C   
3460 O  O   . LEU B 156 ? 0.2500 0.1259 0.1422 -0.0175 -0.0732 -0.0153 157 LEU B O   
3461 C  CB  . LEU B 156 ? 0.2089 0.1300 0.1709 -0.0329 -0.0870 0.0159  157 LEU B CB  
3462 C  CG  . LEU B 156 ? 0.2458 0.1286 0.1303 -0.0270 -0.0568 0.0076  157 LEU B CG  
3463 C  CD1 . LEU B 156 ? 0.2608 0.1801 0.1603 -0.0637 -0.0892 -0.0076 157 LEU B CD1 
3464 C  CD2 . LEU B 156 ? 0.1943 0.1425 0.1759 0.0019  -0.0612 -0.0076 157 LEU B CD2 
3465 N  N   . GLN B 157 ? 0.2757 0.1265 0.1720 -0.0104 -0.1036 -0.0085 158 GLN B N   
3466 C  CA  . GLN B 157 ? 0.2917 0.1516 0.1477 -0.0494 -0.0828 -0.0201 158 GLN B CA  
3467 C  C   . GLN B 157 ? 0.2387 0.1418 0.1404 -0.0292 -0.0918 -0.0115 158 GLN B C   
3468 O  O   . GLN B 157 ? 0.2337 0.1465 0.1648 -0.0258 -0.0662 -0.0256 158 GLN B O   
3469 C  CB  . GLN B 157 ? 0.3201 0.1635 0.1765 -0.0557 -0.1062 -0.0027 158 GLN B CB  
3470 C  CG  . GLN B 157 ? 0.3497 0.1437 0.1773 -0.0248 -0.1019 -0.0344 158 GLN B CG  
3471 C  CD  . GLN B 157 ? 0.3172 0.1416 0.1601 -0.0379 -0.0736 -0.0167 158 GLN B CD  
3472 O  OE1 . GLN B 157 ? 0.3580 0.1422 0.1702 -0.0074 -0.1074 -0.0126 158 GLN B OE1 
3473 N  NE2 . GLN B 157 ? 0.3923 0.1846 0.1546 -0.0776 -0.0738 -0.0465 158 GLN B NE2 
3474 N  N   . LYS B 158 ? 0.2964 0.1186 0.1554 -0.0286 -0.1001 0.0052  159 LYS B N   
3475 C  CA  . LYS B 158 ? 0.2978 0.1383 0.1661 -0.0274 -0.0992 0.0153  159 LYS B CA  
3476 C  C   . LYS B 158 ? 0.2946 0.1428 0.1363 -0.0093 -0.0782 0.0015  159 LYS B C   
3477 O  O   . LYS B 158 ? 0.3260 0.1477 0.1580 -0.0348 -0.0807 -0.0012 159 LYS B O   
3478 C  CB  . LYS B 158 ? 0.3483 0.1393 0.1988 0.0054  -0.0834 0.0375  159 LYS B CB  
3479 C  CG  . LYS B 158 ? 0.3882 0.2301 0.2286 -0.0051 -0.1081 0.0646  159 LYS B CG  
3480 C  CD  . LYS B 158 ? 0.6085 0.3709 0.5569 0.1721  -0.0725 0.1077  159 LYS B CD  
3481 C  CE  . LYS B 158 ? 1.2048 0.6696 0.5238 -0.2193 -0.0185 -0.0628 159 LYS B CE  
3482 N  NZ  . LYS B 158 ? 2.2392 0.9884 0.3980 0.4842  -0.1837 -0.0008 159 LYS B NZ  
3483 N  N   . VAL B 159 ? 0.2942 0.1309 0.1279 -0.0164 -0.0650 -0.0219 160 VAL B N   
3484 C  CA  . VAL B 159 ? 0.2648 0.1169 0.1046 -0.0315 -0.0381 0.0074  160 VAL B CA  
3485 C  C   . VAL B 159 ? 0.2714 0.1273 0.1198 -0.0099 -0.0604 -0.0082 160 VAL B C   
3486 O  O   . VAL B 159 ? 0.2879 0.1273 0.1379 -0.0190 -0.0645 -0.0081 160 VAL B O   
3487 C  CB  . VAL B 159 ? 0.2490 0.1271 0.1103 -0.0126 -0.0654 -0.0102 160 VAL B CB  
3488 C  CG1 . VAL B 159 ? 0.2660 0.1609 0.1310 -0.0310 -0.0654 0.0245  160 VAL B CG1 
3489 C  CG2 . VAL B 159 ? 0.2433 0.1754 0.1182 -0.0126 -0.0452 -0.0183 160 VAL B CG2 
3490 N  N   . VAL B 160 ? 0.2865 0.0970 0.1428 -0.0092 -0.0658 -0.0199 161 VAL B N   
3491 C  CA  . VAL B 160 ? 0.3138 0.1045 0.1507 0.0023  -0.0665 -0.0044 161 VAL B CA  
3492 C  C   . VAL B 160 ? 0.2878 0.1203 0.1737 -0.0108 -0.0287 -0.0469 161 VAL B C   
3493 O  O   . VAL B 160 ? 0.2912 0.1444 0.1625 -0.0154 -0.0162 -0.0307 161 VAL B O   
3494 C  CB  . VAL B 160 ? 0.3285 0.1545 0.1506 -0.0263 -0.0156 -0.0133 161 VAL B CB  
3495 C  CG1 . VAL B 160 ? 0.3188 0.1703 0.2320 -0.0452 -0.0522 -0.0131 161 VAL B CG1 
3496 C  CG2 . VAL B 160 ? 0.3107 0.1494 0.1809 -0.0003 -0.0271 0.0132  161 VAL B CG2 
3497 N  N   . ASP B 161 ? 0.3287 0.1437 0.1317 -0.0344 -0.0703 -0.0177 162 ASP B N   
3498 C  CA  . ASP B 161 ? 0.3955 0.1941 0.1462 -0.0709 -0.1076 -0.0087 162 ASP B CA  
3499 C  C   . ASP B 161 ? 0.3944 0.2063 0.1431 -0.0772 -0.0905 -0.0189 162 ASP B C   
3500 O  O   . ASP B 161 ? 0.5349 0.2908 0.1572 -0.1256 -0.0115 -0.0285 162 ASP B O   
3501 C  CB  . ASP B 161 ? 0.4918 0.2242 0.1430 -0.0599 -0.0930 -0.0271 162 ASP B CB  
3502 C  CG  . ASP B 161 ? 0.3838 0.2286 0.1424 -0.0474 0.0012  -0.0467 162 ASP B CG  
3503 O  OD1 . ASP B 161 ? 0.4929 0.2533 0.1970 -0.0921 -0.0901 -0.0333 162 ASP B OD1 
3504 O  OD2 . ASP B 161 ? 0.4029 0.3018 0.2565 -0.0447 -0.0830 -0.0759 162 ASP B OD2 
3505 N  N   . VAL B 162 ? 0.3603 0.1498 0.1469 -0.0485 -0.0891 0.0040  163 VAL B N   
3506 C  CA  . VAL B 162 ? 0.3066 0.1869 0.1607 -0.0211 -0.0498 -0.0062 163 VAL B CA  
3507 C  C   . VAL B 162 ? 0.3438 0.1521 0.1094 -0.0615 -0.0252 0.0289  163 VAL B C   
3508 O  O   . VAL B 162 ? 0.3494 0.1798 0.1180 -0.0463 -0.0163 0.0074  163 VAL B O   
3509 C  CB  . VAL B 162 ? 0.3226 0.1682 0.1615 0.0006  -0.0373 -0.0052 163 VAL B CB  
3510 C  CG1 . VAL B 162 ? 0.3522 0.1679 0.1841 -0.0103 -0.0458 -0.0008 163 VAL B CG1 
3511 C  CG2 . VAL B 162 ? 0.2601 0.2146 0.1878 -0.0076 -0.0013 0.0340  163 VAL B CG2 
3512 N  N   . LEU B 163 ? 0.2490 0.1666 0.1444 -0.0383 -0.0511 0.0152  164 LEU B N   
3513 C  CA  . LEU B 163 ? 0.2772 0.1200 0.1264 -0.0355 0.0175  0.0068  164 LEU B CA  
3514 C  C   . LEU B 163 ? 0.3066 0.1536 0.1641 -0.0205 0.0152  -0.0098 164 LEU B C   
3515 O  O   . LEU B 163 ? 0.3021 0.1788 0.1094 0.0010  0.0152  0.0173  164 LEU B O   
3516 C  CB  . LEU B 163 ? 0.2858 0.1326 0.1245 -0.0370 -0.0024 -0.0021 164 LEU B CB  
3517 C  CG  . LEU B 163 ? 0.3161 0.1290 0.1200 -0.0149 -0.0383 0.0049  164 LEU B CG  
3518 C  CD1 . LEU B 163 ? 0.2723 0.1282 0.1718 -0.0211 -0.0220 0.0163  164 LEU B CD1 
3519 C  CD2 . LEU B 163 ? 0.3014 0.1582 0.1134 -0.0214 -0.0372 -0.0082 164 LEU B CD2 
3520 N  N   . ASP B 164 ? 0.4079 0.1664 0.1247 -0.0368 -0.0040 -0.0348 165 ASP B N   
3521 C  CA  . ASP B 164 ? 0.5429 0.1967 0.1312 -0.0564 0.0337  -0.0544 165 ASP B CA  
3522 C  C   . ASP B 164 ? 0.3989 0.2874 0.1098 0.0015  0.0193  0.0194  165 ASP B C   
3523 O  O   . ASP B 164 ? 0.4763 0.2457 0.2129 0.0126  0.0798  -0.0032 165 ASP B O   
3524 C  CB  . ASP B 164 ? 0.8995 0.3488 0.3885 -0.1207 -0.2565 -0.0308 165 ASP B CB  
3525 C  CG  . ASP B 164 ? 0.8305 0.3129 0.5828 -0.1518 -0.2657 -0.2865 165 ASP B CG  
3526 O  OD1 . ASP B 164 ? 0.8411 0.6563 0.2705 -0.3246 -0.0461 0.0197  165 ASP B OD1 
3527 O  OD2 . ASP B 164 ? 1.2085 2.0436 0.8895 -0.1062 0.2669  -0.7484 165 ASP B OD2 
3528 N  N   . SER B 165 ? 0.3919 0.2044 0.1259 -0.0366 -0.0522 0.0087  166 SER B N   
3529 C  CA  . SER B 165 ? 0.3447 0.2328 0.1263 -0.0204 -0.0247 0.0043  166 SER B CA  
3530 C  C   . SER B 165 ? 0.3458 0.1870 0.1074 -0.0342 -0.0178 0.0120  166 SER B C   
3531 O  O   . SER B 165 ? 0.4223 0.1976 0.1178 -0.0403 -0.0020 0.0500  166 SER B O   
3532 C  CB  . SER B 165 ? 0.4313 0.2500 0.1430 -0.0007 0.0071  0.0582  166 SER B CB  
3533 O  OG  . SER B 165 ? 0.4647 0.2333 0.1563 -0.0212 -0.0174 0.0328  166 SER B OG  
3534 N  N   . ILE B 166 ? 0.2987 0.1624 0.1101 -0.0294 -0.0219 0.0155  167 ILE B N   
3535 C  CA  . ILE B 166 ? 0.2386 0.1371 0.1272 -0.0153 0.0065  0.0315  167 ILE B CA  
3536 C  C   . ILE B 166 ? 0.2723 0.1517 0.1018 -0.0250 -0.0083 -0.0181 167 ILE B C   
3537 O  O   . ILE B 166 ? 0.2746 0.1436 0.1031 -0.0163 0.0063  0.0017  167 ILE B O   
3538 C  CB  . ILE B 166 ? 0.3063 0.1316 0.1121 -0.0307 0.0013  -0.0015 167 ILE B CB  
3539 C  CG1 . ILE B 166 ? 0.2827 0.1789 0.0987 -0.0366 -0.0086 -0.0129 167 ILE B CG1 
3540 C  CG2 . ILE B 166 ? 0.3287 0.1571 0.1694 -0.0091 -0.0346 0.0144  167 ILE B CG2 
3541 C  CD1 . ILE B 166 ? 0.3091 0.1772 0.1049 -0.0335 0.0225  -0.0309 167 ILE B CD1 
3542 N  N   . LYS B 167 ? 0.2328 0.1541 0.1289 0.0038  -0.0019 0.0194  168 LYS B N   
3543 C  CA  . LYS B 167 ? 0.2369 0.1764 0.1182 -0.0055 0.0068  -0.0386 168 LYS B CA  
3544 C  C   . LYS B 167 ? 0.2405 0.1523 0.1125 -0.0063 0.0339  0.0249  168 LYS B C   
3545 O  O   . LYS B 167 ? 0.2423 0.1393 0.1213 -0.0326 -0.0034 -0.0043 168 LYS B O   
3546 C  CB  . LYS B 167 ? 0.2770 0.1536 0.1532 -0.0049 -0.0119 -0.0324 168 LYS B CB  
3547 C  CG  . LYS B 167 ? 0.2567 0.1869 0.1735 0.0059  -0.0031 -0.0261 168 LYS B CG  
3548 C  CD  . LYS B 167 ? 0.3781 0.2001 0.2619 0.0008  -0.0295 -0.0775 168 LYS B CD  
3549 C  CE  . LYS B 167 ? 0.5654 0.4232 0.2825 0.1826  -0.1365 -0.1208 168 LYS B CE  
3550 N  NZ  . LYS B 167 ? 0.6263 0.6165 0.4422 0.1997  -0.0932 -0.3156 168 LYS B NZ  
3551 N  N   . THR B 168 ? 0.1941 0.1644 0.1236 -0.0174 0.0104  0.0115  169 THR B N   
3552 C  CA  . THR B 168 ? 0.1916 0.1571 0.1352 0.0100  0.0340  0.0326  169 THR B CA  
3553 C  C   . THR B 168 ? 0.1827 0.1899 0.0936 0.0156  0.0085  0.0130  169 THR B C   
3554 O  O   . THR B 168 ? 0.2354 0.1535 0.1305 -0.0093 0.0375  0.0228  169 THR B O   
3555 C  CB  . THR B 168 ? 0.2596 0.1766 0.1449 0.0154  0.0278  0.0163  169 THR B CB  
3556 O  OG1 . THR B 168 ? 0.2940 0.1870 0.1281 0.0113  0.0412  0.0186  169 THR B OG1 
3557 C  CG2 . THR B 168 ? 0.2592 0.1557 0.1644 -0.0274 0.0438  -0.0120 169 THR B CG2 
3558 N  N   . LYS B 169 ? 0.2412 0.1598 0.1400 -0.0315 0.0529  0.0221  170 LYS B N   
3559 C  CA  . LYS B 169 ? 0.2012 0.1475 0.1495 -0.0233 0.0223  0.0172  170 LYS B CA  
3560 C  C   . LYS B 169 ? 0.2472 0.1792 0.1596 0.0010  0.0408  0.0763  170 LYS B C   
3561 O  O   . LYS B 169 ? 0.2989 0.2017 0.1439 -0.0597 0.0388  0.0340  170 LYS B O   
3562 C  CB  . LYS B 169 ? 0.1976 0.1396 0.1625 0.0103  0.0463  0.0245  170 LYS B CB  
3563 C  CG  . LYS B 169 ? 0.2432 0.1667 0.1752 -0.0110 0.0340  0.0240  170 LYS B CG  
3564 C  CD  . LYS B 169 ? 0.3086 0.1987 0.2044 -0.0280 0.0383  0.0564  170 LYS B CD  
3565 C  CE  . LYS B 169 ? 0.2770 0.4724 0.2597 -0.0346 0.0603  0.0800  170 LYS B CE  
3566 N  NZ  . LYS B 169 ? 0.3402 0.4751 0.4341 -0.0548 -0.0317 0.1026  170 LYS B NZ  
3567 N  N   . GLY B 170 ? 0.2391 0.1282 0.2075 -0.0344 0.0163  0.0124  171 GLY B N   
3568 C  CA  . GLY B 170 ? 0.2664 0.1334 0.2346 -0.0480 -0.0147 0.0706  171 GLY B CA  
3569 C  C   . GLY B 170 ? 0.2488 0.1608 0.1710 -0.0087 0.0059  0.0456  171 GLY B C   
3570 O  O   . GLY B 170 ? 0.3759 0.1596 0.2387 -0.0527 0.0065  0.0876  171 GLY B O   
3571 N  N   . LYS B 171 ? 0.2861 0.1398 0.1659 -0.0299 0.0333  0.0509  172 LYS B N   
3572 C  CA  . LYS B 171 ? 0.2630 0.1282 0.1974 -0.0190 0.0209  0.0476  172 LYS B CA  
3573 C  C   . LYS B 171 ? 0.2540 0.1615 0.1074 0.0054  0.0251  0.0207  172 LYS B C   
3574 O  O   . LYS B 171 ? 0.2827 0.1568 0.0970 -0.0265 0.0247  0.0211  172 LYS B O   
3575 C  CB  . LYS B 171 ? 0.3253 0.1724 0.1133 -0.0390 0.0297  0.0353  172 LYS B CB  
3576 C  CG  . LYS B 171 ? 0.2881 0.2506 0.1368 -0.0498 0.0417  0.0091  172 LYS B CG  
3577 C  CD  . LYS B 171 ? 0.4559 0.2194 0.2081 0.0372  -0.0379 -0.0148 172 LYS B CD  
3578 C  CE  . LYS B 171 ? 0.5198 0.4620 0.2300 0.1212  0.0485  -0.0965 172 LYS B CE  
3579 N  NZ  . LYS B 171 ? 1.2165 0.3438 0.2163 -0.1714 -0.0083 -0.0252 172 LYS B NZ  
3580 N  N   . SER B 172 ? 0.2289 0.1721 0.1683 -0.0024 -0.0118 0.0900  173 SER B N   
3581 C  CA  . SER B 172 ? 0.2161 0.1877 0.2047 0.0038  0.0241  0.0229  173 SER B CA  
3582 C  C   . SER B 172 ? 0.2612 0.1946 0.1388 0.0249  0.0098  0.0511  173 SER B C   
3583 O  O   . SER B 172 ? 0.3946 0.2205 0.0921 0.0537  -0.0091 0.0234  173 SER B O   
3584 C  CB  . SER B 172 ? 0.3346 0.1767 0.1544 0.0111  0.0425  0.0252  173 SER B CB  
3585 O  OG  . SER B 172 ? 0.5223 0.1668 0.2098 0.0322  0.0870  0.0593  173 SER B OG  
3586 N  N   . ALA B 173 ? 0.2955 0.2265 0.1166 0.0762  -0.0120 0.0206  174 ALA B N   
3587 C  CA  . ALA B 173 ? 0.2511 0.2818 0.1280 0.0417  -0.0253 0.0776  174 ALA B CA  
3588 C  C   . ALA B 173 ? 0.2032 0.2386 0.1314 0.0013  -0.0317 0.0555  174 ALA B C   
3589 O  O   . ALA B 173 ? 0.2721 0.1959 0.1061 0.0233  -0.0197 0.0331  174 ALA B O   
3590 C  CB  . ALA B 173 ? 0.3961 0.2454 0.1411 0.0573  -0.0068 -0.0005 174 ALA B CB  
3591 N  N   . ASP B 174 ? 0.2154 0.2671 0.1368 0.0205  -0.0109 0.0625  175 ASP B N   
3592 C  CA  . ASP B 174 ? 0.2949 0.2608 0.1301 0.0645  0.0000  0.0540  175 ASP B CA  
3593 C  C   . ASP B 174 ? 0.2982 0.2178 0.1266 0.0331  -0.0471 -0.0021 175 ASP B C   
3594 O  O   . ASP B 174 ? 0.3262 0.2754 0.1671 0.0262  0.0015  -0.0445 175 ASP B O   
3595 C  CB  . ASP B 174 ? 0.2270 0.4083 0.2752 0.0115  -0.0850 0.1108  175 ASP B CB  
3596 C  CG  . ASP B 174 ? 0.4918 0.6252 0.2284 0.0856  0.0129  0.2621  175 ASP B CG  
3597 O  OD1 . ASP B 174 ? 1.3276 1.2387 0.2606 0.0498  -0.5213 -0.1449 175 ASP B OD1 
3598 O  OD2 . ASP B 174 ? 0.5382 0.6851 0.2290 -0.1930 -0.0758 0.1190  175 ASP B OD2 
3599 N  N   . PHE B 175 ? 0.2606 0.1791 0.1385 0.0178  -0.0057 0.0114  176 PHE B N   
3600 C  CA  . PHE B 175 ? 0.2563 0.1884 0.1683 0.0133  -0.0370 0.0324  176 PHE B CA  
3601 C  C   . PHE B 175 ? 0.2743 0.1186 0.1861 0.0219  -0.0564 0.0041  176 PHE B C   
3602 O  O   . PHE B 175 ? 0.3499 0.2169 0.1351 0.0621  -0.0948 -0.0107 176 PHE B O   
3603 C  CB  . PHE B 175 ? 0.3034 0.1632 0.1630 0.0093  -0.0461 0.0322  176 PHE B CB  
3604 C  CG  . PHE B 175 ? 0.3023 0.1412 0.1643 0.0405  -0.0280 -0.0142 176 PHE B CG  
3605 C  CD1 . PHE B 175 ? 0.4025 0.1343 0.2175 0.0324  -0.0386 -0.0162 176 PHE B CD1 
3606 C  CD2 . PHE B 175 ? 0.3882 0.1603 0.1475 0.0296  -0.0885 0.0184  176 PHE B CD2 
3607 C  CE1 . PHE B 175 ? 0.5120 0.1394 0.1724 0.0401  -0.0476 -0.0173 176 PHE B CE1 
3608 C  CE2 . PHE B 175 ? 0.3761 0.1507 0.1609 0.0496  -0.0603 0.0227  176 PHE B CE2 
3609 C  CZ  . PHE B 175 ? 0.4122 0.1172 0.2000 0.0262  -0.0553 -0.0006 176 PHE B CZ  
3610 N  N   . THR B 176 ? 0.3348 0.1809 0.1182 0.0277  -0.0848 0.0414  177 THR B N   
3611 C  CA  . THR B 176 ? 0.2608 0.1446 0.1207 0.0289  -0.0419 0.0218  177 THR B CA  
3612 C  C   . THR B 176 ? 0.2466 0.1293 0.1468 -0.0017 -0.0750 0.0509  177 THR B C   
3613 O  O   . THR B 176 ? 0.3406 0.1304 0.1386 -0.0204 -0.0904 0.0267  177 THR B O   
3614 C  CB  . THR B 176 ? 0.4176 0.2196 0.1967 -0.0302 -0.1561 0.0785  177 THR B CB  
3615 O  OG1 . THR B 176 ? 2.1493 0.3352 1.3956 0.2653  -1.4234 -0.2615 177 THR B OG1 
3616 C  CG2 . THR B 176 ? 0.4476 0.2989 0.4810 -0.0599 -0.1412 0.2093  177 THR B CG2 
3617 N  N   . ASN B 177 ? 0.3190 0.1693 0.1145 0.0331  -0.0785 0.0217  178 ASN B N   
3618 C  CA  . ASN B 177 ? 0.3057 0.1723 0.1430 -0.0220 -0.0715 0.0524  178 ASN B CA  
3619 C  C   . ASN B 177 ? 0.3292 0.1577 0.1509 -0.0035 -0.0819 0.0381  178 ASN B C   
3620 O  O   . ASN B 177 ? 0.3632 0.1992 0.2865 -0.0342 -0.1248 0.1181  178 ASN B O   
3621 C  CB  . ASN B 177 ? 0.3639 0.1550 0.1958 -0.0140 -0.1353 0.0524  178 ASN B CB  
3622 C  CG  . ASN B 177 ? 0.3571 0.1592 0.1594 0.0353  -0.1040 0.0091  178 ASN B CG  
3623 O  OD1 . ASN B 177 ? 0.3925 0.1629 0.2173 0.0474  -0.0472 0.0324  178 ASN B OD1 
3624 N  ND2 . ASN B 177 ? 0.3531 0.1647 0.1563 0.0355  -0.0908 0.0355  178 ASN B ND2 
3625 N  N   . PHE B 178 ? 0.3418 0.1296 0.1291 0.0137  -0.0899 0.0175  179 PHE B N   
3626 C  CA  . PHE B 178 ? 0.3258 0.1240 0.1427 -0.0027 -0.0671 0.0329  179 PHE B CA  
3627 C  C   . PHE B 178 ? 0.3113 0.1166 0.1279 -0.0070 -0.0895 0.0208  179 PHE B C   
3628 O  O   . PHE B 178 ? 0.3070 0.1437 0.1248 -0.0114 -0.0652 0.0175  179 PHE B O   
3629 C  CB  . PHE B 178 ? 0.3334 0.1313 0.1184 0.0121  -0.0318 0.0220  179 PHE B CB  
3630 C  CG  . PHE B 178 ? 0.2608 0.1213 0.1448 -0.0044 -0.0571 0.0320  179 PHE B CG  
3631 C  CD1 . PHE B 178 ? 0.3169 0.1134 0.1397 0.0175  -0.0425 0.0183  179 PHE B CD1 
3632 C  CD2 . PHE B 178 ? 0.2267 0.1272 0.1337 0.0003  -0.0553 0.0175  179 PHE B CD2 
3633 C  CE1 . PHE B 178 ? 0.3292 0.1171 0.1685 -0.0037 -0.0590 0.0313  179 PHE B CE1 
3634 C  CE2 . PHE B 178 ? 0.2110 0.1287 0.1462 -0.0038 -0.0277 0.0234  179 PHE B CE2 
3635 C  CZ  . PHE B 178 ? 0.2815 0.1224 0.1402 0.0115  -0.0322 0.0198  179 PHE B CZ  
3636 N  N   . ASP B 179 ? 0.2750 0.1384 0.1546 0.0148  -0.0956 0.0395  180 ASP B N   
3637 C  CA  . ASP B 179 ? 0.2375 0.1668 0.1500 0.0109  -0.0857 0.0137  180 ASP B CA  
3638 C  C   . ASP B 179 ? 0.2125 0.1199 0.1431 -0.0008 -0.0636 0.0074  180 ASP B C   
3639 O  O   . ASP B 179 ? 0.2334 0.1227 0.1583 -0.0118 -0.0719 0.0153  180 ASP B O   
3640 C  CB  . ASP B 179 ? 0.2260 0.2230 0.2234 0.0077  -0.1212 0.0359  180 ASP B CB  
3641 C  CG  . ASP B 179 ? 0.2035 0.2382 0.2711 0.0057  -0.1097 0.0362  180 ASP B CG  
3642 O  OD1 . ASP B 179 ? 0.2465 0.1616 0.2090 0.0115  -0.0885 0.0397  180 ASP B OD1 
3643 O  OD2 . ASP B 179 ? 0.2031 0.4347 0.3697 0.0017  -0.1141 -0.0152 180 ASP B OD2 
3644 N  N   . PRO B 180 ? 0.1958 0.1128 0.1273 -0.0031 -0.0568 0.0142  181 PRO B N   
3645 C  CA  . PRO B 180 ? 0.1643 0.1266 0.1395 0.0043  -0.0544 0.0210  181 PRO B CA  
3646 C  C   . PRO B 180 ? 0.1653 0.1252 0.1363 0.0121  -0.0542 0.0193  181 PRO B C   
3647 O  O   . PRO B 180 ? 0.1826 0.1316 0.1368 -0.0085 -0.0524 0.0274  181 PRO B O   
3648 C  CB  . PRO B 180 ? 0.2018 0.1494 0.1450 -0.0194 -0.0617 0.0197  181 PRO B CB  
3649 C  CG  . PRO B 180 ? 0.2046 0.1576 0.1474 -0.0167 -0.0711 0.0227  181 PRO B CG  
3650 C  CD  . PRO B 180 ? 0.2267 0.1327 0.1283 -0.0023 -0.0727 0.0089  181 PRO B CD  
3651 N  N   . ARG B 181 ? 0.1729 0.1406 0.1334 0.0078  -0.0505 0.0167  182 ARG B N   
3652 C  CA  . ARG B 181 ? 0.1597 0.1501 0.1580 -0.0247 -0.0344 0.0099  182 ARG B CA  
3653 C  C   . ARG B 181 ? 0.1577 0.1550 0.1849 -0.0031 -0.0754 0.0322  182 ARG B C   
3654 O  O   . ARG B 181 ? 0.2090 0.1368 0.2078 -0.0215 -0.0634 0.0417  182 ARG B O   
3655 C  CB  . ARG B 181 ? 0.1632 0.1556 0.1914 -0.0024 -0.0522 0.0211  182 ARG B CB  
3656 C  CG  . ARG B 181 ? 0.1933 0.1544 0.2089 0.0020  -0.0287 0.0071  182 ARG B CG  
3657 C  CD  . ARG B 181 ? 0.1884 0.2079 0.2346 0.0137  0.0043  0.0302  182 ARG B CD  
3658 N  NE  . ARG B 181 ? 0.2342 0.1981 0.2723 -0.0151 -0.0498 0.0820  182 ARG B NE  
3659 C  CZ  . ARG B 181 ? 0.2124 0.3522 0.3477 0.0582  0.0838  0.2102  182 ARG B CZ  
3660 N  NH1 . ARG B 181 ? 0.2196 0.3310 0.4652 0.0324  0.0247  0.1467  182 ARG B NH1 
3661 N  NH2 . ARG B 181 ? 0.2158 0.3217 0.4063 0.0299  -0.0144 0.1686  182 ARG B NH2 
3662 N  N   . GLY B 182 ? 0.2029 0.1565 0.1689 -0.0006 -0.0997 0.0165  183 GLY B N   
3663 C  CA  . GLY B 182 ? 0.1968 0.1391 0.2567 -0.0171 -0.1020 0.0274  183 GLY B CA  
3664 C  C   . GLY B 182 ? 0.2447 0.1271 0.1947 0.0081  -0.1049 0.0153  183 GLY B C   
3665 O  O   . GLY B 182 ? 0.2779 0.1318 0.2637 -0.0137 -0.1242 0.0021  183 GLY B O   
3666 N  N   . LEU B 183 ? 0.2207 0.1245 0.1380 -0.0015 -0.0812 0.0017  184 LEU B N   
3667 C  CA  . LEU B 183 ? 0.1879 0.1107 0.1617 0.0156  -0.0494 0.0071  184 LEU B CA  
3668 C  C   . LEU B 183 ? 0.1944 0.1220 0.1513 -0.0060 -0.0816 0.0126  184 LEU B C   
3669 O  O   . LEU B 183 ? 0.2150 0.1597 0.1583 0.0082  -0.0615 0.0285  184 LEU B O   
3670 C  CB  . LEU B 183 ? 0.1957 0.1401 0.1261 0.0219  -0.0489 0.0032  184 LEU B CB  
3671 C  CG  . LEU B 183 ? 0.2207 0.1597 0.1273 0.0322  -0.0656 0.0087  184 LEU B CG  
3672 C  CD1 . LEU B 183 ? 0.2053 0.2404 0.1483 0.0384  -0.0359 0.0335  184 LEU B CD1 
3673 C  CD2 . LEU B 183 ? 0.3048 0.1756 0.1422 0.0329  -0.0276 -0.0194 184 LEU B CD2 
3674 N  N   . LEU B 184 ? 0.2045 0.1362 0.1749 0.0037  -0.0641 0.0262  185 LEU B N   
3675 C  CA  . LEU B 184 ? 0.1507 0.1381 0.1761 -0.0357 -0.0630 0.0353  185 LEU B CA  
3676 C  C   . LEU B 184 ? 0.2542 0.1641 0.1914 -0.0935 -0.1138 0.0434  185 LEU B C   
3677 O  O   . LEU B 184 ? 0.2369 0.2178 0.2443 -0.0916 -0.1186 0.0834  185 LEU B O   
3678 C  CB  . LEU B 184 ? 0.1090 0.1511 0.1977 -0.0200 -0.0417 0.0308  185 LEU B CB  
3679 C  CG  . LEU B 184 ? 0.1024 0.1501 0.1615 -0.0057 -0.0344 0.0264  185 LEU B CG  
3680 C  CD1 . LEU B 184 ? 0.1277 0.2003 0.1792 0.0274  0.0135  0.0184  185 LEU B CD1 
3681 C  CD2 . LEU B 184 ? 0.0971 0.1697 0.2348 -0.0212 -0.0350 0.0210  185 LEU B CD2 
3682 N  N   . PRO B 185 ? 0.1377 0.1465 0.1774 -0.0250 -0.0636 0.0263  186 PRO B N   
3683 C  CA  . PRO B 185 ? 0.1745 0.1308 0.1898 -0.0263 -0.0654 0.0364  186 PRO B CA  
3684 C  C   . PRO B 185 ? 0.1464 0.1325 0.2339 -0.0287 -0.0753 0.0491  186 PRO B C   
3685 O  O   . PRO B 185 ? 0.1066 0.1389 0.3774 -0.0208 -0.0768 0.0732  186 PRO B O   
3686 C  CB  . PRO B 185 ? 0.1400 0.1341 0.1712 -0.0032 -0.0208 0.0335  186 PRO B CB  
3687 C  CG  . PRO B 185 ? 0.1218 0.1398 0.1400 0.0138  -0.0309 0.0121  186 PRO B CG  
3688 C  CD  . PRO B 185 ? 0.1412 0.1186 0.1193 0.0024  -0.0339 0.0015  186 PRO B CD  
3689 N  N   . GLU B 186 ? 0.1360 0.1152 0.1447 -0.0071 -0.0406 0.0218  187 GLU B N   
3690 C  CA  . GLU B 186 ? 0.1191 0.1386 0.1913 -0.0010 0.0142  0.0267  187 GLU B CA  
3691 C  C   . GLU B 186 ? 0.1160 0.1321 0.1923 -0.0085 -0.0023 0.0553  187 GLU B C   
3692 O  O   . GLU B 186 ? 0.1252 0.2116 0.1494 0.0143  0.0318  0.0269  187 GLU B O   
3693 C  CB  . GLU B 186 ? 0.0425 0.2049 0.2216 -0.0350 0.0049  0.0038  187 GLU B CB  
3694 C  CG  . GLU B 186 ? 0.1776 0.2105 0.2441 -0.0733 -0.0747 0.0313  187 GLU B CG  
3695 C  CD  . GLU B 186 ? 0.1001 0.2419 0.2969 -0.0769 0.0052  -0.0230 187 GLU B CD  
3696 O  OE1 . GLU B 186 ? 0.2354 0.2009 0.3005 -0.1203 0.0091  0.0520  187 GLU B OE1 
3697 O  OE2 . GLU B 186 ? 0.2861 0.2946 0.3510 -0.1123 -0.0551 -0.0489 187 GLU B OE2 
3698 N  N   . SER B 187 ? 0.0939 0.1574 0.2439 -0.0242 -0.0328 0.0320  188 SER B N   
3699 C  CA  . SER B 187 ? 0.0949 0.1500 0.2940 -0.0219 -0.0264 0.0416  188 SER B CA  
3700 C  C   . SER B 187 ? 0.1030 0.1438 0.2316 -0.0149 -0.0114 0.0432  188 SER B C   
3701 O  O   . SER B 187 ? 0.1017 0.1958 0.2337 -0.0373 -0.0041 -0.0120 188 SER B O   
3702 C  CB  . SER B 187 ? 0.1693 0.1730 0.2477 -0.0419 -0.0333 0.0533  188 SER B CB  
3703 O  OG  . SER B 187 ? 0.1315 0.1953 0.2574 -0.0331 -0.0076 0.0425  188 SER B OG  
3704 N  N   . LEU B 188 ? 0.0989 0.1378 0.2185 -0.0159 -0.0182 0.0256  189 LEU B N   
3705 C  CA  . LEU B 188 ? 0.1046 0.1498 0.2254 -0.0089 -0.0212 0.0103  189 LEU B CA  
3706 C  C   . LEU B 188 ? 0.1121 0.1380 0.2064 -0.0184 0.0062  -0.0126 189 LEU B C   
3707 O  O   . LEU B 188 ? 0.1367 0.1648 0.2069 -0.0178 -0.0031 -0.0263 189 LEU B O   
3708 C  CB  . LEU B 188 ? 0.1272 0.1852 0.2653 -0.0167 -0.0355 0.0445  189 LEU B CB  
3709 C  CG  . LEU B 188 ? 0.1247 0.2011 0.3131 -0.0220 -0.0122 0.0745  189 LEU B CG  
3710 C  CD1 . LEU B 188 ? 0.1368 0.2075 0.3824 -0.0153 -0.0040 0.1111  189 LEU B CD1 
3711 C  CD2 . LEU B 188 ? 0.1488 0.3652 0.2344 -0.0240 -0.0432 0.0830  189 LEU B CD2 
3712 N  N   . ASP B 189 ? 0.0741 0.1620 0.1888 -0.0076 0.0088  -0.0088 190 ASP B N   
3713 C  CA  . ASP B 189 ? 0.0826 0.1729 0.1926 -0.0232 0.0052  0.0027  190 ASP B CA  
3714 C  C   . ASP B 189 ? 0.1004 0.1263 0.1446 -0.0141 0.0124  -0.0027 190 ASP B C   
3715 O  O   . ASP B 189 ? 0.0930 0.1332 0.1395 -0.0082 0.0094  -0.0024 190 ASP B O   
3716 C  CB  . ASP B 189 ? 0.1177 0.2179 0.2020 -0.0581 0.0167  0.0351  190 ASP B CB  
3717 C  CG  . ASP B 189 ? 0.1493 0.3438 0.1918 -0.0696 0.0164  0.0348  190 ASP B CG  
3718 O  OD1 . ASP B 189 ? 0.1493 0.5392 0.3862 -0.0423 0.1011  -0.0749 190 ASP B OD1 
3719 O  OD2 . ASP B 189 ? 0.2274 0.5210 0.2964 -0.1923 -0.0043 0.1129  190 ASP B OD2 
3720 N  N   . TYR B 190 ? 0.0873 0.1293 0.1389 -0.0116 0.0085  0.0192  191 TYR B N   
3721 C  CA  . TYR B 190 ? 0.0979 0.1236 0.1150 -0.0181 -0.0063 0.0074  191 TYR B CA  
3722 C  C   . TYR B 190 ? 0.0798 0.1098 0.1164 -0.0099 0.0074  0.0126  191 TYR B C   
3723 O  O   . TYR B 190 ? 0.1114 0.1324 0.1054 -0.0115 0.0230  0.0057  191 TYR B O   
3724 C  CB  . TYR B 190 ? 0.1080 0.1208 0.1281 -0.0209 0.0013  0.0060  191 TYR B CB  
3725 C  CG  . TYR B 190 ? 0.0978 0.1227 0.1263 -0.0220 0.0098  0.0186  191 TYR B CG  
3726 C  CD1 . TYR B 190 ? 0.1123 0.1299 0.1335 -0.0153 0.0148  0.0192  191 TYR B CD1 
3727 C  CD2 . TYR B 190 ? 0.1054 0.1398 0.1486 -0.0066 0.0105  0.0132  191 TYR B CD2 
3728 C  CE1 . TYR B 190 ? 0.1216 0.1375 0.1385 -0.0071 0.0027  0.0241  191 TYR B CE1 
3729 C  CE2 . TYR B 190 ? 0.1061 0.1481 0.1761 -0.0063 0.0046  0.0165  191 TYR B CE2 
3730 C  CZ  . TYR B 190 ? 0.1247 0.1238 0.1614 -0.0052 0.0174  0.0051  191 TYR B CZ  
3731 O  OH  . TYR B 190 ? 0.1499 0.1420 0.1775 0.0211  -0.0006 -0.0116 191 TYR B OH  
3732 N  N   . TRP B 191 ? 0.0895 0.0961 0.1071 -0.0024 -0.0068 0.0063  192 TRP B N   
3733 C  CA  . TRP B 191 ? 0.0948 0.0987 0.1087 0.0006  0.0126  0.0019  192 TRP B CA  
3734 C  C   . TRP B 191 ? 0.0886 0.1062 0.0804 0.0076  0.0015  -0.0031 192 TRP B C   
3735 O  O   . TRP B 191 ? 0.1202 0.1277 0.0788 -0.0197 0.0060  0.0006  192 TRP B O   
3736 C  CB  . TRP B 191 ? 0.1059 0.1085 0.1067 -0.0028 0.0168  0.0038  192 TRP B CB  
3737 C  CG  . TRP B 191 ? 0.1031 0.1054 0.1087 0.0071  0.0129  0.0129  192 TRP B CG  
3738 C  CD1 . TRP B 191 ? 0.1446 0.1125 0.1209 0.0076  0.0240  0.0129  192 TRP B CD1 
3739 C  CD2 . TRP B 191 ? 0.0842 0.0966 0.1459 0.0052  -0.0062 0.0098  192 TRP B CD2 
3740 N  NE1 . TRP B 191 ? 0.1703 0.1015 0.1398 0.0073  0.0207  0.0329  192 TRP B NE1 
3741 C  CE2 . TRP B 191 ? 0.1512 0.1072 0.1335 0.0110  0.0136  0.0142  192 TRP B CE2 
3742 C  CE3 . TRP B 191 ? 0.0979 0.1440 0.1116 0.0096  0.0099  -0.0007 192 TRP B CE3 
3743 C  CZ2 . TRP B 191 ? 0.1324 0.1085 0.1762 -0.0044 -0.0143 0.0110  192 TRP B CZ2 
3744 C  CZ3 . TRP B 191 ? 0.0881 0.1343 0.1645 0.0015  -0.0005 -0.0195 192 TRP B CZ3 
3745 C  CH2 . TRP B 191 ? 0.1222 0.1150 0.1878 0.0085  -0.0177 -0.0030 192 TRP B CH2 
3746 N  N   . THR B 192 ? 0.0964 0.1030 0.0799 -0.0086 0.0003  0.0081  193 THR B N   
3747 C  CA  . THR B 192 ? 0.0886 0.1032 0.0842 -0.0049 0.0043  0.0000  193 THR B CA  
3748 C  C   . THR B 192 ? 0.0909 0.1011 0.0834 -0.0060 0.0137  0.0060  193 THR B C   
3749 O  O   . THR B 192 ? 0.1046 0.1281 0.0804 -0.0043 0.0081  0.0076  193 THR B O   
3750 C  CB  . THR B 192 ? 0.1000 0.0970 0.1059 0.0000  0.0121  0.0062  193 THR B CB  
3751 O  OG1 . THR B 192 ? 0.1015 0.0995 0.1036 0.0068  0.0068  0.0000  193 THR B OG1 
3752 C  CG2 . THR B 192 ? 0.1178 0.1282 0.1015 0.0217  0.0242  -0.0030 193 THR B CG2 
3753 N  N   . TYR B 193 ? 0.0847 0.0974 0.0932 0.0051  -0.0160 -0.0097 194 TYR B N   
3754 C  CA  . TYR B 193 ? 0.0914 0.1148 0.0776 0.0068  0.0012  -0.0038 194 TYR B CA  
3755 C  C   . TYR B 193 ? 0.0909 0.0942 0.0756 0.0020  -0.0057 -0.0044 194 TYR B C   
3756 O  O   . TYR B 193 ? 0.0947 0.1050 0.0837 -0.0012 -0.0096 -0.0005 194 TYR B O   
3757 C  CB  . TYR B 193 ? 0.1199 0.1049 0.0709 0.0137  -0.0052 -0.0041 194 TYR B CB  
3758 C  CG  . TYR B 193 ? 0.1017 0.0839 0.0925 0.0034  -0.0126 -0.0020 194 TYR B CG  
3759 C  CD1 . TYR B 193 ? 0.0936 0.0850 0.0899 0.0094  -0.0098 0.0006  194 TYR B CD1 
3760 C  CD2 . TYR B 193 ? 0.0947 0.0970 0.0949 0.0132  -0.0164 -0.0020 194 TYR B CD2 
3761 C  CE1 . TYR B 193 ? 0.0896 0.0834 0.1002 -0.0020 -0.0109 -0.0057 194 TYR B CE1 
3762 C  CE2 . TYR B 193 ? 0.0970 0.0982 0.0926 0.0019  -0.0124 -0.0074 194 TYR B CE2 
3763 C  CZ  . TYR B 193 ? 0.0936 0.0771 0.0860 0.0019  -0.0024 0.0000  194 TYR B CZ  
3764 O  OH  . TYR B 193 ? 0.0890 0.0861 0.0979 0.0006  -0.0034 -0.0057 194 TYR B OH  
3765 N  N   . PRO B 194 ? 0.0908 0.1142 0.0793 0.0034  -0.0015 -0.0085 195 PRO B N   
3766 C  CA  . PRO B 194 ? 0.0967 0.0903 0.1072 0.0046  0.0000  -0.0175 195 PRO B CA  
3767 C  C   . PRO B 194 ? 0.0842 0.0879 0.0971 -0.0021 -0.0160 -0.0121 195 PRO B C   
3768 O  O   . PRO B 194 ? 0.0903 0.1169 0.0920 0.0159  -0.0156 -0.0007 195 PRO B O   
3769 C  CB  . PRO B 194 ? 0.1121 0.1300 0.0998 -0.0031 -0.0052 -0.0259 195 PRO B CB  
3770 C  CG  . PRO B 194 ? 0.1315 0.1545 0.0922 -0.0159 0.0013  -0.0236 195 PRO B CG  
3771 C  CD  . PRO B 194 ? 0.1325 0.1482 0.0785 -0.0250 -0.0111 -0.0098 195 PRO B CD  
3772 N  N   . GLY B 195 ? 0.0802 0.0890 0.0939 0.0027  -0.0102 -0.0097 196 GLY B N   
3773 C  CA  . GLY B 195 ? 0.0930 0.0874 0.0989 0.0093  0.0010  -0.0030 196 GLY B CA  
3774 C  C   . GLY B 195 ? 0.0842 0.0824 0.0855 -0.0019 -0.0060 -0.0121 196 GLY B C   
3775 O  O   . GLY B 195 ? 0.1058 0.0828 0.0917 -0.0076 -0.0024 -0.0125 196 GLY B O   
3776 N  N   . SER B 196 ? 0.0802 0.0870 0.0835 -0.0049 -0.0065 -0.0092 197 SER B N   
3777 C  CA  . SER B 196 ? 0.0830 0.0888 0.0900 -0.0115 0.0024  -0.0165 197 SER B CA  
3778 C  C   . SER B 196 ? 0.0662 0.0760 0.0935 -0.0008 0.0044  -0.0017 197 SER B C   
3779 O  O   . SER B 196 ? 0.0720 0.0903 0.0976 -0.0126 0.0017  -0.0077 197 SER B O   
3780 C  CB  . SER B 196 ? 0.0813 0.0970 0.1085 -0.0097 -0.0099 -0.0125 197 SER B CB  
3781 O  OG  . SER B 196 ? 0.0759 0.0833 0.1200 -0.0021 -0.0093 -0.0081 197 SER B OG  
3782 N  N   . LEU B 197 ? 0.0802 0.0794 0.1001 -0.0035 0.0116  -0.0115 198 LEU B N   
3783 C  CA  . LEU B 197 ? 0.0952 0.0855 0.0829 -0.0093 0.0026  -0.0136 198 LEU B CA  
3784 C  C   . LEU B 197 ? 0.0728 0.0934 0.1107 -0.0137 -0.0020 -0.0125 198 LEU B C   
3785 O  O   . LEU B 197 ? 0.0701 0.1062 0.1111 -0.0119 0.0010  -0.0188 198 LEU B O   
3786 C  CB  . LEU B 197 ? 0.1039 0.1018 0.1054 -0.0081 0.0087  -0.0148 198 LEU B CB  
3787 C  CG  . LEU B 197 ? 0.1413 0.1141 0.1431 0.0027  0.0148  0.0124  198 LEU B CG  
3788 C  CD1 . LEU B 197 ? 0.2081 0.1277 0.2176 -0.0496 -0.0049 0.0439  198 LEU B CD1 
3789 C  CD2 . LEU B 197 ? 0.1439 0.1518 0.1946 0.0233  0.0676  0.0472  198 LEU B CD2 
3790 N  N   . THR B 198 ? 0.0956 0.0908 0.1009 -0.0035 0.0000  -0.0151 199 THR B N   
3791 C  CA  . THR B 198 ? 0.0769 0.1045 0.1180 0.0032  -0.0148 -0.0221 199 THR B CA  
3792 C  C   . THR B 198 ? 0.0789 0.1014 0.1273 -0.0024 -0.0051 -0.0189 199 THR B C   
3793 O  O   . THR B 198 ? 0.0815 0.1089 0.1588 0.0005  0.0093  -0.0230 199 THR B O   
3794 C  CB  . THR B 198 ? 0.0957 0.0894 0.0825 0.0012  -0.0114 -0.0120 199 THR B CB  
3795 O  OG1 . THR B 198 ? 0.0991 0.0864 0.1019 -0.0104 0.0008  0.0032  199 THR B OG1 
3796 C  CG2 . THR B 198 ? 0.0975 0.1146 0.0965 0.0024  0.0096  -0.0074 199 THR B CG2 
3797 N  N   . THR B 199 ? 0.1225 0.1154 0.1359 -0.0160 0.0205  -0.0131 200 THR B N   
3798 C  CA  . THR B 199 ? 0.1238 0.1312 0.1309 -0.0200 0.0283  -0.0175 200 THR B CA  
3799 C  C   . THR B 199 ? 0.1256 0.1272 0.1265 -0.0254 0.0208  -0.0166 200 THR B C   
3800 O  O   . THR B 199 ? 0.1202 0.1169 0.1411 -0.0272 0.0227  -0.0207 200 THR B O   
3801 C  CB  . THR B 199 ? 0.1653 0.1581 0.1383 -0.0192 0.0017  -0.0267 200 THR B CB  
3802 O  OG1 . THR B 199 ? 0.2561 0.1404 0.2313 -0.0204 -0.0522 -0.0142 200 THR B OG1 
3803 C  CG2 . THR B 199 ? 0.2397 0.1636 0.1999 -0.0650 0.0098  -0.0278 200 THR B CG2 
3804 N  N   . PRO B 200 ? 0.1316 0.1348 0.1476 -0.0221 0.0362  -0.0136 201 PRO B N   
3805 C  CA  . PRO B 200 ? 0.1218 0.1447 0.1510 -0.0269 0.0264  -0.0174 201 PRO B CA  
3806 C  C   . PRO B 200 ? 0.1392 0.1508 0.1645 -0.0303 0.0296  -0.0062 201 PRO B C   
3807 O  O   . PRO B 200 ? 0.1697 0.1679 0.1455 -0.0163 0.0124  0.0094  201 PRO B O   
3808 C  CB  . PRO B 200 ? 0.1175 0.1889 0.2011 -0.0408 0.0401  -0.0020 201 PRO B CB  
3809 C  CG  . PRO B 200 ? 0.1527 0.1685 0.1641 -0.0254 0.0368  -0.0228 201 PRO B CG  
3810 C  CD  . PRO B 200 ? 0.1422 0.1818 0.1625 -0.0096 0.0283  -0.0392 201 PRO B CD  
3811 N  N   . PRO B 201 ? 0.1381 0.1340 0.1564 -0.0309 0.0197  0.0093  202 PRO B N   
3812 C  CA  . PRO B 201 ? 0.1577 0.1502 0.1436 -0.0472 0.0254  -0.0161 202 PRO B CA  
3813 C  C   . PRO B 201 ? 0.1162 0.1242 0.1509 -0.0239 0.0225  -0.0065 202 PRO B C   
3814 O  O   . PRO B 201 ? 0.1071 0.1263 0.1761 -0.0274 0.0166  0.0049  202 PRO B O   
3815 C  CB  . PRO B 201 ? 0.2037 0.1472 0.2167 -0.0507 0.0337  0.0302  202 PRO B CB  
3816 C  CG  . PRO B 201 ? 0.2207 0.1357 0.2266 -0.0267 0.0289  -0.0049 202 PRO B CG  
3817 C  CD  . PRO B 201 ? 0.2061 0.1439 0.1523 -0.0044 0.0005  0.0186  202 PRO B CD  
3818 N  N   . LEU B 202 ? 0.1072 0.1089 0.1441 -0.0185 0.0161  -0.0019 203 LEU B N   
3819 C  CA  . LEU B 202 ? 0.0864 0.1064 0.1554 -0.0032 0.0066  -0.0071 203 LEU B CA  
3820 C  C   . LEU B 202 ? 0.0852 0.1018 0.1398 -0.0140 0.0031  -0.0068 203 LEU B C   
3821 O  O   . LEU B 202 ? 0.0895 0.1023 0.1498 -0.0113 -0.0041 -0.0196 203 LEU B O   
3822 C  CB  . LEU B 202 ? 0.0769 0.1190 0.1535 0.0006  0.0052  -0.0140 203 LEU B CB  
3823 C  CG  . LEU B 202 ? 0.0873 0.1181 0.1424 0.0000  0.0126  -0.0287 203 LEU B CG  
3824 C  CD1 . LEU B 202 ? 0.0980 0.1354 0.1940 0.0031  -0.0129 -0.0283 203 LEU B CD1 
3825 C  CD2 . LEU B 202 ? 0.0898 0.1142 0.1737 -0.0156 0.0049  -0.0340 203 LEU B CD2 
3826 N  N   . LEU B 203 ? 0.0873 0.0993 0.1491 -0.0073 0.0017  -0.0114 204 LEU B N   
3827 C  CA  . LEU B 203 ? 0.0954 0.0965 0.1638 -0.0157 0.0020  -0.0165 204 LEU B CA  
3828 C  C   . LEU B 203 ? 0.0974 0.0684 0.1473 -0.0126 0.0000  -0.0076 204 LEU B C   
3829 O  O   . LEU B 203 ? 0.0979 0.0934 0.1282 -0.0143 -0.0015 -0.0154 204 LEU B O   
3830 C  CB  . LEU B 203 ? 0.1124 0.0979 0.1747 -0.0105 0.0186  0.0032  204 LEU B CB  
3831 C  CG  . LEU B 203 ? 0.1676 0.1168 0.2028 -0.0028 0.0531  0.0149  204 LEU B CG  
3832 C  CD1 . LEU B 203 ? 0.1732 0.1404 0.2574 0.0204  0.0798  0.0452  204 LEU B CD1 
3833 C  CD2 . LEU B 203 ? 0.1437 0.1791 0.3481 -0.0816 0.0489  0.0192  204 LEU B CD2 
3834 N  N   . GLU B 204 ? 0.0914 0.1048 0.1391 -0.0178 0.0031  -0.0310 205 GLU B N   
3835 C  CA  . GLU B 204 ? 0.1101 0.0974 0.1380 -0.0070 -0.0209 -0.0280 205 GLU B CA  
3836 C  C   . GLU B 204 ? 0.0939 0.0967 0.1351 -0.0133 -0.0217 -0.0241 205 GLU B C   
3837 O  O   . GLU B 204 ? 0.1432 0.1459 0.1449 0.0322  -0.0386 -0.0571 205 GLU B O   
3838 C  CB  . GLU B 204 ? 0.1010 0.1271 0.1465 0.0110  -0.0472 -0.0370 205 GLU B CB  
3839 C  CG  . GLU B 204 ? 0.1023 0.1216 0.1554 -0.0008 -0.0315 -0.0322 205 GLU B CG  
3840 C  CD  . GLU B 204 ? 0.1465 0.1342 0.1530 0.0003  -0.0441 -0.0288 205 GLU B CD  
3841 O  OE1 . GLU B 204 ? 0.1553 0.1502 0.2258 0.0167  -0.0954 -0.0592 205 GLU B OE1 
3842 O  OE2 . GLU B 204 ? 0.1107 0.1243 0.1755 -0.0041 -0.0478 -0.0157 205 GLU B OE2 
3843 N  N   . CYS B 205 ? 0.0917 0.0833 0.1318 -0.0063 -0.0141 -0.0159 206 CYS B N   
3844 C  CA  . CYS B 205 ? 0.1145 0.0812 0.1204 -0.0055 -0.0115 -0.0031 206 CYS B CA  
3845 C  C   . CYS B 205 ? 0.0954 0.0900 0.1006 -0.0003 -0.0077 -0.0204 206 CYS B C   
3846 O  O   . CYS B 205 ? 0.1111 0.0859 0.1573 0.0020  -0.0299 -0.0060 206 CYS B O   
3847 C  CB  . CYS B 205 ? 0.1334 0.0942 0.1292 -0.0130 0.0099  -0.0049 206 CYS B CB  
3848 S  SG  . CYS B 205 ? 0.1351 0.1048 0.1254 -0.0041 -0.0038 -0.0062 206 CYS B SG  
3849 N  N   . VAL B 206 ? 0.0944 0.0776 0.1031 -0.0043 -0.0107 -0.0071 207 VAL B N   
3850 C  CA  . VAL B 206 ? 0.0892 0.0759 0.1048 -0.0052 -0.0031 -0.0015 207 VAL B CA  
3851 C  C   . VAL B 206 ? 0.0839 0.0764 0.1059 -0.0005 -0.0129 0.0005  207 VAL B C   
3852 O  O   . VAL B 206 ? 0.0940 0.1079 0.1175 0.0008  -0.0144 0.0120  207 VAL B O   
3853 C  CB  . VAL B 206 ? 0.0891 0.0899 0.1031 -0.0006 -0.0006 -0.0010 207 VAL B CB  
3854 C  CG1 . VAL B 206 ? 0.0886 0.0820 0.1212 0.0003  -0.0108 -0.0114 207 VAL B CG1 
3855 C  CG2 . VAL B 206 ? 0.0912 0.1027 0.1220 0.0019  0.0048  -0.0063 207 VAL B CG2 
3856 N  N   . THR B 207 ? 0.0851 0.0693 0.0944 -0.0026 -0.0048 -0.0049 208 THR B N   
3857 C  CA  . THR B 207 ? 0.1062 0.0738 0.0934 -0.0041 -0.0057 0.0017  208 THR B CA  
3858 C  C   . THR B 207 ? 0.0879 0.0759 0.0872 -0.0066 0.0007  -0.0006 208 THR B C   
3859 O  O   . THR B 207 ? 0.1023 0.0822 0.0991 0.0032  -0.0160 -0.0027 208 THR B O   
3860 C  CB  . THR B 207 ? 0.0998 0.0825 0.1171 -0.0026 0.0043  -0.0125 208 THR B CB  
3861 O  OG1 . THR B 207 ? 0.1202 0.0939 0.1143 0.0007  -0.0013 -0.0170 208 THR B OG1 
3862 C  CG2 . THR B 207 ? 0.1023 0.1014 0.1325 -0.0057 0.0063  -0.0052 208 THR B CG2 
3863 N  N   . TRP B 208 ? 0.0894 0.0692 0.0870 -0.0048 0.0000  -0.0024 209 TRP B N   
3864 C  CA  . TRP B 208 ? 0.0882 0.0789 0.0813 0.0000  -0.0003 0.0000  209 TRP B CA  
3865 C  C   . TRP B 208 ? 0.0781 0.0724 0.0913 0.0003  -0.0046 -0.0006 209 TRP B C   
3866 O  O   . TRP B 208 ? 0.0882 0.0980 0.0798 -0.0043 0.0024  0.0020  209 TRP B O   
3867 C  CB  . TRP B 208 ? 0.0886 0.0835 0.0978 0.0003  0.0015  0.0035  209 TRP B CB  
3868 C  CG  . TRP B 208 ? 0.0753 0.0780 0.0907 0.0068  -0.0089 -0.0015 209 TRP B CG  
3869 C  CD1 . TRP B 208 ? 0.0888 0.0813 0.1081 0.0023  -0.0088 -0.0020 209 TRP B CD1 
3870 C  CD2 . TRP B 208 ? 0.0648 0.0737 0.1074 0.0017  -0.0068 -0.0110 209 TRP B CD2 
3871 N  NE1 . TRP B 208 ? 0.0798 0.0920 0.1187 -0.0035 -0.0070 -0.0020 209 TRP B NE1 
3872 C  CE2 . TRP B 208 ? 0.0847 0.0754 0.1141 0.0034  -0.0149 0.0012  209 TRP B CE2 
3873 C  CE3 . TRP B 208 ? 0.0741 0.0825 0.0966 0.0051  -0.0103 0.0037  209 TRP B CE3 
3874 C  CZ2 . TRP B 208 ? 0.0839 0.0930 0.1239 0.0184  0.0115  -0.0154 209 TRP B CZ2 
3875 C  CZ3 . TRP B 208 ? 0.1031 0.0926 0.0996 0.0124  -0.0034 -0.0097 209 TRP B CZ3 
3876 C  CH2 . TRP B 208 ? 0.1198 0.0851 0.1123 0.0174  0.0013  0.0013  209 TRP B CH2 
3877 N  N   . ILE B 209 ? 0.0760 0.0732 0.0949 0.0000  0.0007  0.0013  210 ILE B N   
3878 C  CA  . ILE B 209 ? 0.0734 0.0813 0.0974 -0.0048 0.0035  -0.0024 210 ILE B CA  
3879 C  C   . ILE B 209 ? 0.0815 0.0696 0.0898 -0.0054 -0.0054 0.0054  210 ILE B C   
3880 O  O   . ILE B 209 ? 0.1229 0.0882 0.0794 -0.0032 -0.0087 0.0041  210 ILE B O   
3881 C  CB  . ILE B 209 ? 0.0838 0.0800 0.1337 0.0000  0.0052  0.0000  210 ILE B CB  
3882 C  CG1 . ILE B 209 ? 0.1001 0.0960 0.1606 0.0109  -0.0032 -0.0186 210 ILE B CG1 
3883 C  CG2 . ILE B 209 ? 0.0832 0.1250 0.1471 -0.0030 -0.0003 0.0126  210 ILE B CG2 
3884 C  CD1 . ILE B 209 ? 0.1148 0.1013 0.2239 0.0162  0.0086  -0.0017 210 ILE B CD1 
3885 N  N   . VAL B 210 ? 0.0737 0.0724 0.1000 0.0001  0.0001  0.0057  211 VAL B N   
3886 C  CA  . VAL B 210 ? 0.0789 0.0825 0.0926 -0.0083 -0.0049 0.0055  211 VAL B CA  
3887 C  C   . VAL B 210 ? 0.0860 0.0719 0.0898 -0.0028 0.0003  0.0021  211 VAL B C   
3888 O  O   . VAL B 210 ? 0.0945 0.1026 0.0894 -0.0219 -0.0001 0.0083  211 VAL B O   
3889 C  CB  . VAL B 210 ? 0.0869 0.0908 0.0982 0.0000  -0.0115 0.0003  211 VAL B CB  
3890 C  CG1 . VAL B 210 ? 0.1168 0.0829 0.1243 -0.0008 -0.0006 0.0055  211 VAL B CG1 
3891 C  CG2 . VAL B 210 ? 0.1036 0.0925 0.1168 -0.0085 0.0021  -0.0015 211 VAL B CG2 
3892 N  N   . LEU B 211 ? 0.0722 0.0992 0.1032 -0.0162 -0.0052 -0.0020 212 LEU B N   
3893 C  CA  . LEU B 211 ? 0.0856 0.1046 0.1146 -0.0121 -0.0076 0.0057  212 LEU B CA  
3894 C  C   . LEU B 211 ? 0.0785 0.1036 0.1080 -0.0178 -0.0032 -0.0030 212 LEU B C   
3895 O  O   . LEU B 211 ? 0.0962 0.1041 0.1054 -0.0161 0.0010  0.0065  212 LEU B O   
3896 C  CB  . LEU B 211 ? 0.0750 0.1238 0.1303 -0.0103 -0.0081 0.0151  212 LEU B CB  
3897 C  CG  . LEU B 211 ? 0.0916 0.1141 0.1416 -0.0094 -0.0166 0.0104  212 LEU B CG  
3898 C  CD1 . LEU B 211 ? 0.0961 0.1810 0.1683 -0.0136 -0.0412 0.0401  212 LEU B CD1 
3899 C  CD2 . LEU B 211 ? 0.1024 0.1127 0.1614 0.0074  0.0013  0.0019  212 LEU B CD2 
3900 N  N   . LYS B 212 ? 0.0947 0.1120 0.1187 -0.0259 -0.0119 0.0130  213 LYS B N   
3901 C  CA  . LYS B 212 ? 0.1150 0.1187 0.1307 -0.0315 -0.0080 0.0208  213 LYS B CA  
3902 C  C   . LYS B 212 ? 0.0988 0.0939 0.1261 -0.0152 0.0031  0.0172  213 LYS B C   
3903 O  O   . LYS B 212 ? 0.1168 0.1159 0.1687 -0.0133 -0.0271 0.0203  213 LYS B O   
3904 C  CB  . LYS B 212 ? 0.1521 0.1502 0.1166 -0.0570 0.0059  0.0138  213 LYS B CB  
3905 C  CG  . LYS B 212 ? 0.2524 0.1885 0.1718 -0.0661 -0.0174 0.0590  213 LYS B CG  
3906 C  CD  . LYS B 212 ? 0.4113 0.2368 0.1829 -0.1439 0.0256  0.0220  213 LYS B CD  
3907 C  CE  . LYS B 212 ? 0.5924 0.2966 0.2813 -0.0731 0.1448  0.0942  213 LYS B CE  
3908 N  NZ  . LYS B 212 ? 0.6417 0.6334 0.3677 -0.1652 0.1450  0.1846  213 LYS B NZ  
3909 N  N   . GLU B 213 ? 0.0895 0.0997 0.1300 -0.0184 -0.0148 0.0087  214 GLU B N   
3910 C  CA  . GLU B 213 ? 0.1074 0.1209 0.1324 -0.0271 -0.0092 0.0049  214 GLU B CA  
3911 C  C   . GLU B 213 ? 0.0908 0.1015 0.1394 -0.0216 -0.0190 0.0147  214 GLU B C   
3912 O  O   . GLU B 213 ? 0.1080 0.1035 0.1330 -0.0094 -0.0168 0.0183  214 GLU B O   
3913 C  CB  . GLU B 213 ? 0.0807 0.1429 0.1557 -0.0252 -0.0177 0.0220  214 GLU B CB  
3914 C  CG  . GLU B 213 ? 0.1278 0.1533 0.2337 -0.0439 -0.0621 0.0032  214 GLU B CG  
3915 C  CD  . GLU B 213 ? 0.1463 0.2554 0.2205 -0.0474 -0.0657 -0.0078 214 GLU B CD  
3916 O  OE1 . GLU B 213 ? 0.1216 0.1676 0.3120 -0.0302 -0.0636 0.0472  214 GLU B OE1 
3917 O  OE2 . GLU B 213 ? 0.1932 0.4207 0.4124 -0.0719 -0.0800 -0.1234 214 GLU B OE2 
3918 N  N   A PRO B 214 ? 0.1278 0.0865 0.1209 -0.0164 -0.0179 0.0129  215 PRO B N   
3919 N  N   B PRO B 214 ? 0.1381 0.1011 0.1273 -0.0163 -0.0155 0.0070  215 PRO B N   
3920 C  CA  A PRO B 214 ? 0.1024 0.1022 0.1154 -0.0103 -0.0137 0.0043  215 PRO B CA  
3921 C  CA  B PRO B 214 ? 0.1087 0.1074 0.1184 -0.0098 -0.0148 0.0062  215 PRO B CA  
3922 C  C   A PRO B 214 ? 0.1231 0.1027 0.1342 -0.0307 -0.0386 -0.0027 215 PRO B C   
3923 C  C   B PRO B 214 ? 0.1321 0.1080 0.1377 -0.0303 -0.0386 -0.0027 215 PRO B C   
3924 O  O   A PRO B 214 ? 0.1240 0.1577 0.1347 -0.0428 -0.0403 0.0052  215 PRO B O   
3925 O  O   B PRO B 214 ? 0.1299 0.1630 0.1429 -0.0399 -0.0447 0.0030  215 PRO B O   
3926 C  CB  A PRO B 214 ? 0.1182 0.0900 0.1523 -0.0110 -0.0063 0.0066  215 PRO B CB  
3927 C  CB  B PRO B 214 ? 0.1277 0.0957 0.1708 -0.0105 -0.0115 -0.0041 215 PRO B CB  
3928 C  CG  A PRO B 214 ? 0.1184 0.0754 0.1596 -0.0130 -0.0076 0.0071  215 PRO B CG  
3929 C  CG  B PRO B 214 ? 0.2113 0.1639 0.1867 -0.0010 0.0313  0.0205  215 PRO B CG  
3930 C  CD  A PRO B 214 ? 0.1268 0.0741 0.1297 -0.0271 -0.0051 0.0102  215 PRO B CD  
3931 C  CD  B PRO B 214 ? 0.1946 0.1146 0.1906 0.0098  0.0149  0.0291  215 PRO B CD  
3932 N  N   . ILE B 215 ? 0.1247 0.1075 0.1151 -0.0044 -0.0244 -0.0131 216 ILE B N   
3933 C  CA  . ILE B 215 ? 0.1410 0.0991 0.1239 0.0013  -0.0416 -0.0208 216 ILE B CA  
3934 C  C   . ILE B 215 ? 0.1230 0.0948 0.1328 -0.0172 -0.0288 -0.0081 216 ILE B C   
3935 O  O   . ILE B 215 ? 0.1279 0.1018 0.1721 -0.0113 -0.0284 -0.0190 216 ILE B O   
3936 C  CB  . ILE B 215 ? 0.1509 0.1075 0.1459 -0.0037 -0.0289 -0.0221 216 ILE B CB  
3937 C  CG1 . ILE B 215 ? 0.1924 0.1275 0.1120 0.0041  -0.0212 0.0078  216 ILE B CG1 
3938 C  CG2 . ILE B 215 ? 0.1912 0.1227 0.1466 0.0232  -0.0533 -0.0153 216 ILE B CG2 
3939 C  CD1 . ILE B 215 ? 0.2204 0.1296 0.1295 0.0059  -0.0305 0.0151  216 ILE B CD1 
3940 N  N   . SER B 216 ? 0.1344 0.1148 0.1588 -0.0115 -0.0340 -0.0238 217 SER B N   
3941 C  CA  . SER B 216 ? 0.1410 0.1112 0.1348 -0.0083 -0.0329 -0.0221 217 SER B CA  
3942 C  C   . SER B 216 ? 0.1559 0.0905 0.1437 -0.0118 -0.0476 -0.0121 217 SER B C   
3943 O  O   . SER B 216 ? 0.1418 0.1395 0.1641 -0.0063 -0.0509 -0.0063 217 SER B O   
3944 C  CB  . SER B 216 ? 0.3001 0.0970 0.1668 -0.0522 0.0260  -0.0171 217 SER B CB  
3945 O  OG  . SER B 216 ? 0.2777 0.1943 0.2073 -0.0852 -0.0199 -0.0038 217 SER B OG  
3946 N  N   . VAL B 217 ? 0.1544 0.0952 0.1409 -0.0156 -0.0372 -0.0161 218 VAL B N   
3947 C  CA  . VAL B 217 ? 0.1935 0.0886 0.1283 -0.0255 -0.0419 -0.0086 218 VAL B CA  
3948 C  C   . VAL B 217 ? 0.1527 0.0847 0.1537 -0.0249 -0.0284 -0.0032 218 VAL B C   
3949 O  O   . VAL B 217 ? 0.1700 0.0953 0.1349 -0.0264 -0.0282 -0.0097 218 VAL B O   
3950 C  CB  . VAL B 217 ? 0.1650 0.0882 0.1713 -0.0280 -0.0412 -0.0175 218 VAL B CB  
3951 C  CG1 . VAL B 217 ? 0.1955 0.1036 0.1641 -0.0375 -0.0285 -0.0186 218 VAL B CG1 
3952 C  CG2 . VAL B 217 ? 0.1607 0.0952 0.2094 -0.0212 -0.0425 -0.0160 218 VAL B CG2 
3953 N  N   . SER B 218 ? 0.1685 0.0969 0.1412 -0.0262 -0.0375 -0.0320 219 SER B N   
3954 C  CA  . SER B 218 ? 0.1765 0.0856 0.1465 -0.0124 -0.0200 -0.0198 219 SER B CA  
3955 C  C   . SER B 218 ? 0.1979 0.0808 0.1386 -0.0225 -0.0131 -0.0068 219 SER B C   
3956 O  O   . SER B 218 ? 0.2018 0.0855 0.1314 -0.0190 -0.0326 0.0015  219 SER B O   
3957 C  CB  . SER B 218 ? 0.2257 0.0978 0.1501 -0.0190 -0.0500 -0.0219 219 SER B CB  
3958 O  OG  . SER B 218 ? 0.2361 0.1184 0.1526 -0.0355 -0.0520 -0.0052 219 SER B OG  
3959 N  N   A SER B 219 ? 0.1890 0.0901 0.1479 -0.0163 -0.0276 -0.0094 220 SER B N   
3960 N  N   B SER B 219 ? 0.1844 0.0838 0.1511 -0.0142 -0.0239 0.0030  220 SER B N   
3961 C  CA  A SER B 219 ? 0.2101 0.1077 0.1739 -0.0098 -0.0250 -0.0200 220 SER B CA  
3962 C  CA  B SER B 219 ? 0.1992 0.0715 0.1780 -0.0251 -0.0116 0.0159  220 SER B CA  
3963 C  C   A SER B 219 ? 0.2040 0.1413 0.1620 -0.0527 -0.0083 -0.0355 220 SER B C   
3964 C  C   B SER B 219 ? 0.1879 0.0710 0.1885 0.0137  0.0091  0.0113  220 SER B C   
3965 O  O   A SER B 219 ? 0.1785 0.1254 0.1395 0.0062  0.0060  -0.0310 220 SER B O   
3966 O  O   B SER B 219 ? 0.2258 0.0952 0.2014 -0.0346 0.0165  0.0135  220 SER B O   
3967 C  CB  A SER B 219 ? 0.2472 0.1072 0.2380 -0.0485 0.0218  -0.0386 220 SER B CB  
3968 C  CB  B SER B 219 ? 0.2445 0.0728 0.2275 0.0144  -0.0074 0.0478  220 SER B CB  
3969 O  OG  A SER B 219 ? 0.2479 0.0772 0.2230 -0.0164 0.0019  -0.0082 220 SER B OG  
3970 O  OG  B SER B 219 ? 0.2222 0.1092 0.1879 -0.0038 -0.0291 -0.0119 220 SER B OG  
3971 N  N   . GLU B 220 ? 0.2222 0.0922 0.1493 -0.0121 -0.0131 -0.0108 221 GLU B N   
3972 C  CA  . GLU B 220 ? 0.2843 0.1022 0.1616 -0.0241 -0.0037 -0.0063 221 GLU B CA  
3973 C  C   . GLU B 220 ? 0.2608 0.1036 0.1293 -0.0170 0.0074  0.0083  221 GLU B C   
3974 O  O   . GLU B 220 ? 0.2535 0.1279 0.1491 -0.0057 0.0126  -0.0077 221 GLU B O   
3975 C  CB  . GLU B 220 ? 0.3842 0.1854 0.1650 -0.0557 -0.0560 -0.0542 221 GLU B CB  
3976 C  CG  . GLU B 220 ? 0.4167 0.2143 0.1818 0.0035  -0.0895 -0.0821 221 GLU B CG  
3977 C  CD  . GLU B 220 ? 0.5726 0.2840 0.2784 -0.0581 0.0406  -0.1010 221 GLU B CD  
3978 O  OE1 . GLU B 220 ? 0.3314 0.1976 0.2935 -0.0979 -0.0097 -0.0362 221 GLU B OE1 
3979 O  OE2 . GLU B 220 ? 1.6725 1.1247 0.8442 0.0000  0.1071  -0.3835 221 GLU B OE2 
3980 N  N   . GLN B 221 ? 0.2199 0.0908 0.1430 -0.0087 -0.0324 -0.0085 222 GLN B N   
3981 C  CA  . GLN B 221 ? 0.2043 0.0922 0.1431 -0.0197 -0.0104 -0.0094 222 GLN B CA  
3982 C  C   . GLN B 221 ? 0.1938 0.0868 0.1378 -0.0100 -0.0219 0.0074  222 GLN B C   
3983 O  O   . GLN B 221 ? 0.2222 0.1182 0.1238 -0.0322 -0.0065 0.0110  222 GLN B O   
3984 C  CB  . GLN B 221 ? 0.2151 0.1017 0.1076 -0.0153 -0.0315 -0.0091 222 GLN B CB  
3985 C  CG  . GLN B 221 ? 0.1967 0.1130 0.1337 -0.0238 -0.0474 -0.0092 222 GLN B CG  
3986 C  CD  . GLN B 221 ? 0.1937 0.0930 0.1425 -0.0201 -0.0430 -0.0080 222 GLN B CD  
3987 O  OE1 . GLN B 221 ? 0.1985 0.1094 0.1400 -0.0148 -0.0390 -0.0113 222 GLN B OE1 
3988 N  NE2 . GLN B 221 ? 0.2224 0.1087 0.1588 -0.0156 -0.0560 -0.0098 222 GLN B NE2 
3989 N  N   . VAL B 222 ? 0.2074 0.1028 0.1365 -0.0212 -0.0229 0.0041  223 VAL B N   
3990 C  CA  . VAL B 222 ? 0.1580 0.1303 0.1500 -0.0164 -0.0097 0.0156  223 VAL B CA  
3991 C  C   . VAL B 222 ? 0.1824 0.1159 0.1564 -0.0232 -0.0062 0.0153  223 VAL B C   
3992 O  O   . VAL B 222 ? 0.2195 0.1321 0.1512 -0.0351 -0.0181 0.0274  223 VAL B O   
3993 C  CB  . VAL B 222 ? 0.1744 0.1624 0.1756 -0.0230 -0.0200 0.0410  223 VAL B CB  
3994 C  CG1 . VAL B 222 ? 0.2256 0.1870 0.2114 -0.0500 -0.0494 0.0590  223 VAL B CG1 
3995 C  CG2 . VAL B 222 ? 0.2606 0.1782 0.1758 -0.0449 -0.0458 0.0041  223 VAL B CG2 
3996 N  N   . LEU B 223 ? 0.1960 0.1227 0.1620 -0.0203 0.0127  0.0015  224 LEU B N   
3997 C  CA  . LEU B 223 ? 0.2687 0.1362 0.1912 -0.0427 0.0282  -0.0087 224 LEU B CA  
3998 C  C   . LEU B 223 ? 0.2215 0.1362 0.1284 -0.0318 -0.0007 -0.0151 224 LEU B C   
3999 O  O   . LEU B 223 ? 0.2400 0.1523 0.1782 -0.0212 0.0278  -0.0143 224 LEU B O   
4000 C  CB  . LEU B 223 ? 0.2763 0.1328 0.2414 -0.0320 0.0274  -0.0432 224 LEU B CB  
4001 C  CG  . LEU B 223 ? 0.3075 0.1397 0.2400 -0.0263 0.0307  0.0000  224 LEU B CG  
4002 C  CD1 . LEU B 223 ? 0.4537 0.1836 0.2885 -0.0644 -0.0707 0.0000  224 LEU B CD1 
4003 C  CD2 . LEU B 223 ? 0.3183 0.2056 0.2894 0.0052  -0.0623 -0.0487 224 LEU B CD2 
4004 N  N   . LYS B 224 ? 0.2416 0.1280 0.1360 -0.0307 -0.0093 -0.0094 225 LYS B N   
4005 C  CA  . LYS B 224 ? 0.2393 0.1480 0.1447 -0.0148 0.0081  -0.0092 225 LYS B CA  
4006 C  C   . LYS B 224 ? 0.2522 0.1384 0.1098 -0.0210 0.0030  0.0143  225 LYS B C   
4007 O  O   . LYS B 224 ? 0.2398 0.1500 0.1119 -0.0296 0.0113  0.0066  225 LYS B O   
4008 C  CB  . LYS B 224 ? 0.2642 0.2161 0.1650 -0.0256 -0.0483 0.0361  225 LYS B CB  
4009 C  CG  . LYS B 224 ? 0.3197 0.2585 0.2064 -0.0142 -0.0637 -0.0208 225 LYS B CG  
4010 C  CD  . LYS B 224 ? 0.3822 0.1849 0.2700 -0.0192 -0.1066 -0.0284 225 LYS B CD  
4011 C  CE  . LYS B 224 ? 0.3540 0.3747 0.3260 -0.0606 -0.0842 -0.1375 225 LYS B CE  
4012 N  NZ  . LYS B 224 ? 0.4217 0.2500 0.3815 -0.0491 -0.0564 -0.0896 225 LYS B NZ  
4013 N  N   . PHE B 225 ? 0.2151 0.1137 0.1162 -0.0120 0.0065  0.0024  226 PHE B N   
4014 C  CA  . PHE B 225 ? 0.2134 0.1094 0.1336 -0.0151 0.0233  0.0026  226 PHE B CA  
4015 C  C   . PHE B 225 ? 0.2405 0.1164 0.1039 -0.0434 0.0043  0.0085  226 PHE B C   
4016 O  O   . PHE B 225 ? 0.2251 0.1313 0.1028 -0.0259 0.0230  -0.0210 226 PHE B O   
4017 C  CB  . PHE B 225 ? 0.2416 0.1018 0.1121 -0.0173 0.0274  -0.0032 226 PHE B CB  
4018 C  CG  . PHE B 225 ? 0.2052 0.0886 0.1331 -0.0480 0.0229  -0.0322 226 PHE B CG  
4019 C  CD1 . PHE B 225 ? 0.2653 0.1601 0.1732 0.0196  0.0054  0.0046  226 PHE B CD1 
4020 C  CD2 . PHE B 225 ? 0.2208 0.2037 0.1699 -0.0500 0.0270  -0.0653 226 PHE B CD2 
4021 C  CE1 . PHE B 225 ? 0.3048 0.1421 0.1687 0.0074  0.0216  0.0098  226 PHE B CE1 
4022 C  CE2 . PHE B 225 ? 0.2405 0.2126 0.1587 -0.0259 0.0005  -0.0847 226 PHE B CE2 
4023 C  CZ  . PHE B 225 ? 0.1957 0.1483 0.2073 -0.0362 -0.0138 -0.0595 226 PHE B CZ  
4024 N  N   . ARG B 226 ? 0.1982 0.1154 0.1177 -0.0057 0.0147  -0.0006 227 ARG B N   
4025 C  CA  . ARG B 226 ? 0.2223 0.1310 0.1032 -0.0379 -0.0113 0.0013  227 ARG B CA  
4026 C  C   . ARG B 226 ? 0.2295 0.1128 0.1280 -0.0193 0.0304  -0.0038 227 ARG B C   
4027 O  O   . ARG B 226 ? 0.2213 0.1479 0.1454 -0.0186 0.0217  -0.0132 227 ARG B O   
4028 C  CB  . ARG B 226 ? 0.2486 0.1049 0.1308 -0.0296 0.0049  -0.0049 227 ARG B CB  
4029 C  CG  . ARG B 226 ? 0.2189 0.1148 0.1333 -0.0439 0.0102  0.0149  227 ARG B CG  
4030 C  CD  . ARG B 226 ? 0.2626 0.1344 0.1409 -0.0027 0.0010  0.0093  227 ARG B CD  
4031 N  NE  . ARG B 226 ? 0.2393 0.1123 0.1275 -0.0538 -0.0113 -0.0070 227 ARG B NE  
4032 C  CZ  . ARG B 226 ? 0.2375 0.1182 0.1216 -0.0465 -0.0077 -0.0170 227 ARG B CZ  
4033 N  NH1 . ARG B 226 ? 0.2745 0.1503 0.1944 -0.0816 -0.0100 -0.0469 227 ARG B NH1 
4034 N  NH2 . ARG B 226 ? 0.2538 0.1286 0.1524 -0.0762 0.0155  -0.0057 227 ARG B NH2 
4035 N  N   . LYS B 227 ? 0.2184 0.1180 0.1227 -0.0329 0.0192  -0.0141 228 LYS B N   
4036 C  CA  . LYS B 227 ? 0.2737 0.1456 0.1018 -0.0671 0.0240  -0.0226 228 LYS B CA  
4037 C  C   . LYS B 227 ? 0.2364 0.1442 0.0920 -0.0324 0.0173  -0.0225 228 LYS B C   
4038 O  O   . LYS B 227 ? 0.3161 0.1666 0.0970 -0.0692 0.0381  -0.0329 228 LYS B O   
4039 C  CB  . LYS B 227 ? 0.2761 0.1991 0.1098 -0.0649 0.0186  -0.0428 228 LYS B CB  
4040 C  CG  . LYS B 227 ? 0.2845 0.1990 0.1573 -0.0918 0.0259  -0.0401 228 LYS B CG  
4041 C  CD  . LYS B 227 ? 0.4178 0.2752 0.2180 -0.1451 -0.0476 -0.0262 228 LYS B CD  
4042 C  CE  . LYS B 227 ? 0.5486 0.7059 0.2231 -0.2276 -0.0318 -0.1212 228 LYS B CE  
4043 N  NZ  . LYS B 227 ? 1.0549 0.7196 0.3749 -0.3271 -0.2594 -0.0028 228 LYS B NZ  
4044 N  N   . LEU B 228 ? 0.2310 0.1300 0.0938 -0.0531 0.0281  -0.0230 229 LEU B N   
4045 C  CA  . LEU B 228 ? 0.1923 0.1498 0.1413 -0.0533 0.0027  -0.0151 229 LEU B CA  
4046 C  C   . LEU B 228 ? 0.2764 0.0974 0.0965 -0.0318 0.0230  -0.0038 229 LEU B C   
4047 O  O   . LEU B 228 ? 0.2071 0.1372 0.1247 -0.0192 0.0361  -0.0238 229 LEU B O   
4048 C  CB  . LEU B 228 ? 0.2455 0.1121 0.0947 -0.0436 0.0211  -0.0120 229 LEU B CB  
4049 C  CG  . LEU B 228 ? 0.2052 0.1659 0.1075 -0.0080 0.0000  -0.0055 229 LEU B CG  
4050 C  CD1 . LEU B 228 ? 0.2852 0.1664 0.1055 -0.0406 0.0173  -0.0366 229 LEU B CD1 
4051 C  CD2 . LEU B 228 ? 0.2858 0.1500 0.1358 -0.0152 0.0052  0.0190  229 LEU B CD2 
4052 N  N   . ASN B 229 ? 0.2052 0.1454 0.1245 -0.0259 0.0138  0.0003  230 ASN B N   
4053 C  CA  . ASN B 229 ? 0.2047 0.1282 0.1130 -0.0013 0.0187  -0.0131 230 ASN B CA  
4054 C  C   . ASN B 229 ? 0.1677 0.1508 0.1191 0.0225  0.0372  0.0206  230 ASN B C   
4055 O  O   . ASN B 229 ? 0.2213 0.1484 0.1372 -0.0249 0.0261  0.0035  230 ASN B O   
4056 C  CB  . ASN B 229 ? 0.2590 0.1694 0.1143 -0.0164 0.0472  0.0060  230 ASN B CB  
4057 C  CG  . ASN B 229 ? 0.2709 0.1870 0.1022 -0.0362 0.0252  -0.0160 230 ASN B CG  
4058 O  OD1 . ASN B 229 ? 0.3418 0.1905 0.1200 -0.0010 0.0493  -0.0137 230 ASN B OD1 
4059 N  ND2 . ASN B 229 ? 0.2942 0.1689 0.1440 -0.0395 0.0423  -0.0355 230 ASN B ND2 
4060 N  N   . PHE B 230 ? 0.1823 0.1247 0.1495 -0.0210 0.0531  0.0060  231 PHE B N   
4061 C  CA  . PHE B 230 ? 0.1750 0.1422 0.1456 -0.0230 0.0074  0.0164  231 PHE B CA  
4062 C  C   . PHE B 230 ? 0.2852 0.1360 0.1518 -0.0472 0.0324  -0.0031 231 PHE B C   
4063 O  O   . PHE B 230 ? 0.2639 0.1948 0.1622 -0.1001 0.0588  -0.0183 231 PHE B O   
4064 C  CB  . PHE B 230 ? 0.1649 0.1307 0.1898 -0.0357 0.0329  0.0074  231 PHE B CB  
4065 C  CG  . PHE B 230 ? 0.2138 0.1193 0.1268 -0.0406 0.0255  -0.0157 231 PHE B CG  
4066 C  CD1 . PHE B 230 ? 0.1609 0.1671 0.1520 -0.0179 0.0162  0.0023  231 PHE B CD1 
4067 C  CD2 . PHE B 230 ? 0.1783 0.1729 0.1173 0.0242  0.0173  -0.0226 231 PHE B CD2 
4068 C  CE1 . PHE B 230 ? 0.2064 0.1639 0.1573 -0.0284 0.0520  0.0054  231 PHE B CE1 
4069 C  CE2 . PHE B 230 ? 0.2005 0.1624 0.1395 -0.0254 0.0203  -0.0007 231 PHE B CE2 
4070 C  CZ  . PHE B 230 ? 0.1536 0.1854 0.1352 -0.0377 0.0186  -0.0038 231 PHE B CZ  
4071 N  N   . ASN B 231 ? 0.2321 0.1732 0.1307 -0.0408 0.0397  0.0124  232 ASN B N   
4072 C  CA  . ASN B 231 ? 0.2504 0.1782 0.1621 -0.0115 0.0518  -0.0017 232 ASN B CA  
4073 C  C   . ASN B 231 ? 0.1669 0.1941 0.1076 0.0244  0.0173  0.0126  232 ASN B C   
4074 O  O   . ASN B 231 ? 0.2161 0.1887 0.1840 0.0008  0.0377  -0.0057 232 ASN B O   
4075 C  CB  . ASN B 231 ? 0.2384 0.1650 0.1837 -0.0065 0.0740  0.0163  232 ASN B CB  
4076 C  CG  . ASN B 231 ? 0.2133 0.1613 0.2176 0.0173  0.0493  0.0244  232 ASN B CG  
4077 O  OD1 . ASN B 231 ? 0.2926 0.1562 0.1744 0.0035  0.0781  -0.0041 232 ASN B OD1 
4078 N  ND2 . ASN B 231 ? 0.2924 0.1931 0.1781 -0.0020 0.0812  -0.0081 232 ASN B ND2 
4079 N  N   . GLY B 232 ? 0.2533 0.1729 0.1696 -0.0031 0.0740  0.0219  233 GLY B N   
4080 C  CA  . GLY B 232 ? 0.2779 0.1706 0.1578 -0.0097 0.0535  0.0348  233 GLY B CA  
4081 C  C   . GLY B 232 ? 0.1990 0.1568 0.2061 0.0184  -0.0109 0.0306  233 GLY B C   
4082 O  O   . GLY B 232 ? 0.2551 0.2458 0.1841 0.0678  0.0900  0.0868  233 GLY B O   
4083 N  N   . GLU B 233 ? 0.2013 0.1993 0.1700 0.0241  0.0443  0.0258  234 GLU B N   
4084 C  CA  . GLU B 233 ? 0.2029 0.2073 0.1600 0.0487  0.0375  0.0052  234 GLU B CA  
4085 C  C   . GLU B 233 ? 0.1992 0.2197 0.1964 0.0610  0.0496  0.0427  234 GLU B C   
4086 O  O   . GLU B 233 ? 0.2475 0.2852 0.1993 -0.0109 0.0542  0.0472  234 GLU B O   
4087 C  CB  . GLU B 233 ? 0.2463 0.2002 0.1623 0.0531  0.0209  0.0441  234 GLU B CB  
4088 C  CG  . GLU B 233 ? 0.3499 0.2730 0.1447 -0.0375 0.0012  0.0518  234 GLU B CG  
4089 C  CD  . GLU B 233 ? 0.3111 0.4043 0.2104 0.0956  0.0715  0.0274  234 GLU B CD  
4090 O  OE1 . GLU B 233 ? 0.3488 0.3289 0.2815 0.0144  0.1067  0.0469  234 GLU B OE1 
4091 O  OE2 . GLU B 233 ? 0.3822 0.3285 0.2205 0.0107  -0.0006 0.0232  234 GLU B OE2 
4092 N  N   . GLY B 234 ? 0.3540 0.2635 0.1907 0.0419  0.1233  -0.0108 235 GLY B N   
4093 C  CA  . GLY B 234 ? 0.3134 0.2549 0.1845 0.0670  0.0720  0.0372  235 GLY B CA  
4094 C  C   . GLY B 234 ? 0.2797 0.3452 0.2398 0.0690  0.0759  0.1107  235 GLY B C   
4095 O  O   . GLY B 234 ? 0.3086 0.4596 0.2694 0.1238  0.1457  0.1251  235 GLY B O   
4096 N  N   . GLU B 235 ? 0.2487 0.1933 0.2336 0.0460  0.0518  0.0436  236 GLU B N   
4097 C  CA  . GLU B 235 ? 0.2324 0.1645 0.2224 0.0357  0.0368  0.0427  236 GLU B CA  
4098 C  C   . GLU B 235 ? 0.2405 0.2111 0.2517 0.0306  0.1093  0.0671  236 GLU B C   
4099 O  O   . GLU B 235 ? 0.2488 0.2336 0.2590 0.0132  0.0772  0.0217  236 GLU B O   
4100 C  CB  . GLU B 235 ? 0.2662 0.1877 0.2230 0.0146  0.0966  0.0096  236 GLU B CB  
4101 C  CG  . GLU B 235 ? 0.2531 0.2237 0.2304 -0.0154 0.0178  0.0243  236 GLU B CG  
4102 C  CD  . GLU B 235 ? 0.4659 0.2187 0.2942 -0.0496 0.1518  0.0100  236 GLU B CD  
4103 O  OE1 . GLU B 235 ? 0.2689 0.2458 0.2612 -0.0212 0.0675  0.0340  236 GLU B OE1 
4104 O  OE2 . GLU B 235 ? 0.4902 0.2711 0.4020 -0.0974 0.1448  0.0183  236 GLU B OE2 
4105 N  N   . PRO B 236 ? 0.2280 0.2079 0.2250 0.0406  0.0790  0.0736  237 PRO B N   
4106 C  CA  . PRO B 236 ? 0.2750 0.1914 0.2581 0.0794  0.1225  0.0601  237 PRO B CA  
4107 C  C   . PRO B 236 ? 0.2515 0.1556 0.1939 -0.0021 0.0898  0.0086  237 PRO B C   
4108 O  O   . PRO B 236 ? 0.2538 0.1985 0.2270 -0.0140 0.1239  -0.0208 237 PRO B O   
4109 C  CB  . PRO B 236 ? 0.2811 0.1856 0.2635 0.0586  0.0898  0.0776  237 PRO B CB  
4110 C  CG  . PRO B 236 ? 0.2658 0.2202 0.3589 0.0292  0.0483  0.1357  237 PRO B CG  
4111 C  CD  . PRO B 236 ? 0.2228 0.2143 0.3262 -0.0153 0.0772  0.0412  237 PRO B CD  
4112 N  N   . GLU B 237 ? 0.3321 0.1548 0.2104 -0.0166 0.1158  -0.0076 238 GLU B N   
4113 C  CA  . GLU B 237 ? 0.3287 0.2023 0.1422 -0.0296 0.0597  -0.0331 238 GLU B CA  
4114 C  C   . GLU B 237 ? 0.2299 0.1598 0.2054 0.0120  0.0712  0.0087  238 GLU B C   
4115 O  O   . GLU B 237 ? 0.2011 0.2050 0.1518 0.0276  0.0274  -0.0024 238 GLU B O   
4116 C  CB  . GLU B 237 ? 0.2894 0.1852 0.2107 -0.0291 0.0292  -0.0461 238 GLU B CB  
4117 C  CG  . GLU B 237 ? 0.3089 0.2354 0.3016 -0.0441 0.0712  -0.0797 238 GLU B CG  
4118 C  CD  . GLU B 237 ? 0.3235 0.1982 0.2664 -0.0267 0.0476  -0.1066 238 GLU B CD  
4119 O  OE1 . GLU B 237 ? 0.3088 0.2579 0.5098 0.0487  -0.0759 -0.1309 238 GLU B OE1 
4120 O  OE2 . GLU B 237 ? 0.3359 0.1930 0.2089 -0.0099 0.0373  -0.0573 238 GLU B OE2 
4121 N  N   . GLU B 238 ? 0.2270 0.1967 0.1398 -0.0505 0.0566  -0.0263 239 GLU B N   
4122 C  CA  . GLU B 238 ? 0.1656 0.2078 0.1645 -0.0364 0.0401  -0.0238 239 GLU B CA  
4123 C  C   . GLU B 238 ? 0.1523 0.1907 0.1154 0.0147  0.0348  0.0005  239 GLU B C   
4124 O  O   . GLU B 238 ? 0.2669 0.1553 0.1747 -0.0219 0.0573  -0.0111 239 GLU B O   
4125 C  CB  . GLU B 238 ? 0.2682 0.2299 0.2011 -0.0683 0.0242  -0.0121 239 GLU B CB  
4126 C  CG  . GLU B 238 ? 0.2910 0.2831 0.2922 0.0167  0.0516  -0.0425 239 GLU B CG  
4127 C  CD  . GLU B 238 ? 0.6758 0.4828 0.2199 -0.3240 0.0284  -0.0038 239 GLU B CD  
4128 O  OE1 . GLU B 238 ? 0.4943 0.4869 0.2649 -0.0984 0.0146  0.0483  239 GLU B OE1 
4129 O  OE2 . GLU B 238 ? 0.8708 0.6209 0.9075 -0.3941 0.2799  0.1893  239 GLU B OE2 
4130 N  N   . LEU B 239 ? 0.1735 0.1907 0.1116 -0.0529 0.0353  -0.0177 240 LEU B N   
4131 C  CA  . LEU B 239 ? 0.1773 0.1467 0.1280 -0.0315 0.0366  -0.0105 240 LEU B CA  
4132 C  C   . LEU B 239 ? 0.2066 0.1571 0.0857 -0.0465 0.0247  0.0142  240 LEU B C   
4133 O  O   . LEU B 239 ? 0.2115 0.1508 0.1209 -0.0240 0.0491  -0.0083 240 LEU B O   
4134 C  CB  . LEU B 239 ? 0.1843 0.1391 0.1568 -0.0137 0.0342  -0.0137 240 LEU B CB  
4135 C  CG  . LEU B 239 ? 0.1526 0.1567 0.1826 -0.0148 0.0174  -0.0368 240 LEU B CG  
4136 C  CD1 . LEU B 239 ? 0.2809 0.1186 0.2958 -0.0030 -0.0143 -0.0170 240 LEU B CD1 
4137 C  CD2 . LEU B 239 ? 0.2071 0.1697 0.1658 0.0207  0.0060  -0.0218 240 LEU B CD2 
4138 N  N   . MET B 240 ? 0.2172 0.1280 0.1160 -0.0104 0.0549  -0.0082 241 MET B N   
4139 C  CA  . MET B 240 ? 0.2168 0.1336 0.1053 0.0020  0.0652  0.0013  241 MET B CA  
4140 C  C   . MET B 240 ? 0.1794 0.1277 0.0800 -0.0120 0.0017  -0.0143 241 MET B C   
4141 O  O   . MET B 240 ? 0.1825 0.1366 0.1037 -0.0250 0.0298  -0.0111 241 MET B O   
4142 C  CB  . MET B 240 ? 0.2066 0.1245 0.1102 -0.0049 0.0313  0.0120  241 MET B CB  
4143 C  CG  . MET B 240 ? 0.2256 0.1561 0.1107 -0.0295 0.0582  -0.0186 241 MET B CG  
4144 S  SD  . MET B 240 ? 0.2255 0.1247 0.1504 -0.0171 0.0342  0.0074  241 MET B SD  
4145 C  CE  . MET B 240 ? 0.2865 0.1230 0.1783 -0.0292 0.1048  0.0120  241 MET B CE  
4146 N  N   . VAL B 241 ? 0.1879 0.1089 0.1076 -0.0328 0.0438  -0.0313 242 VAL B N   
4147 C  CA  . VAL B 241 ? 0.1816 0.1006 0.0995 -0.0313 0.0362  -0.0226 242 VAL B CA  
4148 C  C   . VAL B 241 ? 0.1684 0.0993 0.0947 -0.0229 0.0258  -0.0218 242 VAL B C   
4149 O  O   . VAL B 241 ? 0.1573 0.1262 0.1115 -0.0237 0.0324  -0.0172 242 VAL B O   
4150 C  CB  . VAL B 241 ? 0.1749 0.1139 0.1141 -0.0239 0.0355  -0.0208 242 VAL B CB  
4151 C  CG1 . VAL B 241 ? 0.2357 0.1230 0.1386 -0.0529 0.0100  -0.0428 242 VAL B CG1 
4152 C  CG2 . VAL B 241 ? 0.1985 0.1175 0.1366 -0.0181 0.0430  -0.0399 242 VAL B CG2 
4153 N  N   . ASP B 242 ? 0.1553 0.0966 0.0856 -0.0155 0.0240  -0.0173 243 ASP B N   
4154 C  CA  . ASP B 242 ? 0.1544 0.0943 0.0998 0.0010  0.0212  -0.0177 243 ASP B CA  
4155 C  C   . ASP B 242 ? 0.1431 0.1137 0.0987 -0.0296 0.0190  -0.0108 243 ASP B C   
4156 O  O   . ASP B 242 ? 0.1511 0.1049 0.1486 -0.0162 0.0126  -0.0184 243 ASP B O   
4157 C  CB  . ASP B 242 ? 0.1490 0.1052 0.1220 -0.0098 0.0164  -0.0104 243 ASP B CB  
4158 C  CG  . ASP B 242 ? 0.1428 0.1042 0.1193 -0.0155 0.0152  -0.0329 243 ASP B CG  
4159 O  OD1 . ASP B 242 ? 0.1468 0.0979 0.1273 -0.0037 0.0242  -0.0108 243 ASP B OD1 
4160 O  OD2 . ASP B 242 ? 0.1805 0.1123 0.1656 -0.0091 0.0300  -0.0361 243 ASP B OD2 
4161 N  N   . ASN B 243 ? 0.1393 0.0851 0.1046 -0.0104 0.0283  -0.0164 244 ASN B N   
4162 C  CA  . ASN B 243 ? 0.1388 0.0832 0.1150 -0.0142 0.0313  -0.0140 244 ASN B CA  
4163 C  C   . ASN B 243 ? 0.1090 0.0860 0.0976 -0.0031 0.0080  -0.0006 244 ASN B C   
4164 O  O   . ASN B 243 ? 0.1528 0.1009 0.0988 0.0133  0.0263  0.0038  244 ASN B O   
4165 C  CB  . ASN B 243 ? 0.1717 0.0962 0.0932 -0.0162 0.0333  -0.0035 244 ASN B CB  
4166 C  CG  . ASN B 243 ? 0.1322 0.0894 0.1196 -0.0324 0.0148  0.0017  244 ASN B CG  
4167 O  OD1 . ASN B 243 ? 0.1419 0.1017 0.1427 -0.0226 0.0120  0.0184  244 ASN B OD1 
4168 N  ND2 . ASN B 243 ? 0.1911 0.1544 0.1579 -0.0480 -0.0136 0.0559  244 ASN B ND2 
4169 N  N   . TRP B 244 ? 0.1121 0.0798 0.1022 -0.0030 0.0054  -0.0151 245 TRP B N   
4170 C  CA  . TRP B 244 ? 0.1137 0.0939 0.0798 0.0030  0.0108  -0.0182 245 TRP B CA  
4171 C  C   . TRP B 244 ? 0.1093 0.0892 0.0942 -0.0066 0.0206  -0.0077 245 TRP B C   
4172 O  O   . TRP B 244 ? 0.1177 0.1085 0.1326 0.0105  -0.0020 -0.0296 245 TRP B O   
4173 C  CB  . TRP B 244 ? 0.1155 0.0813 0.1008 -0.0154 0.0140  -0.0105 245 TRP B CB  
4174 C  CG  . TRP B 244 ? 0.1005 0.0878 0.0992 -0.0111 0.0109  -0.0098 245 TRP B CG  
4175 C  CD1 . TRP B 244 ? 0.1290 0.0834 0.0956 -0.0118 0.0289  -0.0127 245 TRP B CD1 
4176 C  CD2 . TRP B 244 ? 0.1041 0.0904 0.1116 -0.0048 0.0110  0.0017  245 TRP B CD2 
4177 N  NE1 . TRP B 244 ? 0.1173 0.0882 0.1083 -0.0043 0.0236  -0.0089 245 TRP B NE1 
4178 C  CE2 . TRP B 244 ? 0.1233 0.0908 0.1195 -0.0028 0.0182  -0.0037 245 TRP B CE2 
4179 C  CE3 . TRP B 244 ? 0.1335 0.1137 0.1044 -0.0105 0.0063  -0.0057 245 TRP B CE3 
4180 C  CZ2 . TRP B 244 ? 0.1438 0.1018 0.1314 0.0000  0.0179  -0.0034 245 TRP B CZ2 
4181 C  CZ3 . TRP B 244 ? 0.1523 0.1001 0.1497 0.0054  0.0034  0.0051  245 TRP B CZ3 
4182 C  CH2 . TRP B 244 ? 0.1248 0.1272 0.1440 0.0041  0.0068  0.0000  245 TRP B CH2 
4183 N  N   . ARG B 245 ? 0.0923 0.0962 0.1024 -0.0027 0.0147  -0.0219 246 ARG B N   
4184 C  CA  . ARG B 245 ? 0.0851 0.1027 0.0986 -0.0017 0.0038  -0.0192 246 ARG B CA  
4185 C  C   . ARG B 245 ? 0.0776 0.0986 0.1057 0.0076  0.0017  -0.0307 246 ARG B C   
4186 O  O   . ARG B 245 ? 0.0847 0.1072 0.1164 0.0054  0.0013  -0.0230 246 ARG B O   
4187 C  CB  . ARG B 245 ? 0.0879 0.1058 0.1187 -0.0065 -0.0020 -0.0238 246 ARG B CB  
4188 C  CG  . ARG B 245 ? 0.0793 0.1115 0.1351 -0.0048 0.0037  -0.0258 246 ARG B CG  
4189 C  CD  . ARG B 245 ? 0.0693 0.1184 0.1318 -0.0103 -0.0001 -0.0342 246 ARG B CD  
4190 N  NE  . ARG B 245 ? 0.0898 0.1187 0.1400 -0.0186 0.0038  -0.0272 246 ARG B NE  
4191 C  CZ  . ARG B 245 ? 0.0931 0.1110 0.1292 -0.0263 0.0013  -0.0187 246 ARG B CZ  
4192 N  NH1 . ARG B 245 ? 0.0970 0.1191 0.1389 -0.0178 0.0098  -0.0353 246 ARG B NH1 
4193 N  NH2 . ARG B 245 ? 0.0872 0.1494 0.1687 -0.0284 0.0083  -0.0195 246 ARG B NH2 
4194 N  N   A PRO B 246 ? 0.0944 0.1080 0.1058 0.0023  0.0077  -0.0001 247 PRO B N   
4195 N  N   B PRO B 246 ? 0.1023 0.1049 0.1096 0.0130  0.0109  -0.0127 247 PRO B N   
4196 C  CA  A PRO B 246 ? 0.1105 0.1089 0.1022 0.0068  0.0060  -0.0006 247 PRO B CA  
4197 C  CA  B PRO B 246 ? 0.1103 0.1080 0.1101 0.0076  -0.0034 -0.0065 247 PRO B CA  
4198 C  C   A PRO B 246 ? 0.1225 0.0888 0.0987 0.0136  -0.0189 0.0035  247 PRO B C   
4199 C  C   B PRO B 246 ? 0.1263 0.0934 0.1057 0.0116  -0.0126 0.0020  247 PRO B C   
4200 O  O   A PRO B 246 ? 0.1066 0.1045 0.1071 0.0068  -0.0003 -0.0087 247 PRO B O   
4201 O  O   B PRO B 246 ? 0.1130 0.1061 0.1132 0.0109  -0.0037 -0.0081 247 PRO B O   
4202 C  CB  A PRO B 246 ? 0.1412 0.1265 0.1377 0.0295  0.0089  -0.0040 247 PRO B CB  
4203 C  CB  B PRO B 246 ? 0.1544 0.1301 0.1767 0.0427  -0.0059 -0.0239 247 PRO B CB  
4204 C  CG  A PRO B 246 ? 0.1157 0.0874 0.1510 0.0019  0.0265  -0.0115 247 PRO B CG  
4205 C  CG  B PRO B 246 ? 0.1145 0.1362 0.2000 0.0494  -0.0078 -0.0225 247 PRO B CG  
4206 C  CD  A PRO B 246 ? 0.0872 0.0865 0.1537 0.0003  0.0062  0.0013  247 PRO B CD  
4207 C  CD  B PRO B 246 ? 0.1045 0.1489 0.1388 0.0461  -0.0003 -0.0390 247 PRO B CD  
4208 N  N   . ALA B 247 ? 0.1037 0.1049 0.1107 0.0076  -0.0010 -0.0082 248 ALA B N   
4209 C  CA  . ALA B 247 ? 0.1076 0.1094 0.1204 0.0088  -0.0006 -0.0089 248 ALA B CA  
4210 C  C   . ALA B 247 ? 0.1024 0.1145 0.1189 0.0178  -0.0147 0.0065  248 ALA B C   
4211 O  O   . ALA B 247 ? 0.1306 0.1303 0.1407 0.0438  -0.0142 0.0031  248 ALA B O   
4212 C  CB  . ALA B 247 ? 0.1454 0.1365 0.1203 -0.0078 0.0160  0.0068  248 ALA B CB  
4213 N  N   . GLN B 248 ? 0.1032 0.1055 0.1157 0.0035  -0.0109 0.0000  249 GLN B N   
4214 C  CA  . GLN B 248 ? 0.1028 0.1392 0.1070 0.0073  -0.0028 -0.0040 249 GLN B CA  
4215 C  C   . GLN B 248 ? 0.1132 0.1309 0.1227 0.0299  -0.0245 0.0135  249 GLN B C   
4216 O  O   . GLN B 248 ? 0.1283 0.1342 0.1159 0.0151  0.0020  0.0073  249 GLN B O   
4217 C  CB  . GLN B 248 ? 0.1260 0.1142 0.1486 0.0013  -0.0256 -0.0076 249 GLN B CB  
4218 C  CG  . GLN B 248 ? 0.1280 0.1266 0.1259 -0.0104 -0.0292 0.0082  249 GLN B CG  
4219 C  CD  . GLN B 248 ? 0.0982 0.1576 0.1449 -0.0163 -0.0127 0.0115  249 GLN B CD  
4220 O  OE1 . GLN B 248 ? 0.1081 0.2205 0.1685 -0.0416 -0.0152 -0.0239 249 GLN B OE1 
4221 N  NE2 . GLN B 248 ? 0.1225 0.1718 0.1466 -0.0153 -0.0174 -0.0171 249 GLN B NE2 
4222 N  N   . PRO B 249 ? 0.1413 0.1599 0.1404 0.0474  -0.0355 -0.0121 250 PRO B N   
4223 C  CA  . PRO B 249 ? 0.1594 0.2120 0.1261 0.0627  -0.0281 -0.0096 250 PRO B CA  
4224 C  C   . PRO B 249 ? 0.1445 0.1543 0.1085 0.0373  -0.0225 0.0060  250 PRO B C   
4225 O  O   . PRO B 249 ? 0.1334 0.1641 0.1298 0.0366  -0.0252 0.0102  250 PRO B O   
4226 C  CB  . PRO B 249 ? 0.1590 0.2824 0.1727 0.0895  -0.0615 -0.0302 250 PRO B CB  
4227 C  CG  . PRO B 249 ? 0.2073 0.3292 0.1675 0.0927  -0.0688 -0.0313 250 PRO B CG  
4228 C  CD  . PRO B 249 ? 0.1074 0.2382 0.1847 0.0610  -0.0520 -0.0531 250 PRO B CD  
4229 N  N   . LEU B 250 ? 0.1568 0.1521 0.1177 0.0445  -0.0220 0.0041  251 LEU B N   
4230 C  CA  . LEU B 250 ? 0.1474 0.1317 0.1075 0.0259  -0.0087 -0.0103 251 LEU B CA  
4231 C  C   . LEU B 250 ? 0.1518 0.1304 0.1200 0.0229  -0.0229 0.0098  251 LEU B C   
4232 O  O   . LEU B 250 ? 0.1502 0.1324 0.1289 0.0223  -0.0307 -0.0162 251 LEU B O   
4233 C  CB  . LEU B 250 ? 0.2166 0.1462 0.1263 0.0113  0.0065  0.0020  251 LEU B CB  
4234 C  CG  . LEU B 250 ? 0.2013 0.1421 0.1480 -0.0085 0.0217  -0.0197 251 LEU B CG  
4235 C  CD1 . LEU B 250 ? 0.1701 0.2043 0.1375 -0.0342 -0.0049 -0.0027 251 LEU B CD1 
4236 C  CD2 . LEU B 250 ? 0.2651 0.1845 0.1841 -0.0359 0.0439  -0.0318 251 LEU B CD2 
4237 N  N   A LYS B 251 ? 0.1791 0.1782 0.1154 0.0397  -0.0423 -0.0012 252 LYS B N   
4238 N  N   B LYS B 251 ? 0.1888 0.1790 0.1014 0.0379  -0.0476 -0.0111 252 LYS B N   
4239 C  CA  A LYS B 251 ? 0.1372 0.2167 0.1168 0.0355  -0.0357 0.0041  252 LYS B CA  
4240 C  CA  B LYS B 251 ? 0.1598 0.2212 0.1155 0.0379  -0.0458 -0.0163 252 LYS B CA  
4241 C  C   A LYS B 251 ? 0.1344 0.2152 0.1669 0.0209  -0.0375 -0.0177 252 LYS B C   
4242 C  C   B LYS B 251 ? 0.1353 0.2158 0.1480 0.0082  -0.0531 -0.0308 252 LYS B C   
4243 O  O   A LYS B 251 ? 0.2081 0.2132 0.1916 0.0250  0.0094  -0.0038 252 LYS B O   
4244 O  O   B LYS B 251 ? 0.2136 0.2069 0.1651 0.0105  0.0146  -0.0346 252 LYS B O   
4245 C  CB  A LYS B 251 ? 0.2016 0.2143 0.1755 0.0168  -0.0092 0.0175  252 LYS B CB  
4246 C  CB  B LYS B 251 ? 0.2138 0.1808 0.1457 0.0028  -0.0601 -0.0478 252 LYS B CB  
4247 C  CG  A LYS B 251 ? 0.0992 0.4273 0.1912 0.0383  -0.0750 -0.0447 252 LYS B CG  
4248 C  CG  B LYS B 251 ? 0.2518 0.2188 0.1920 0.0032  -0.0199 -0.0653 252 LYS B CG  
4249 C  CD  A LYS B 251 ? 0.1141 0.4959 0.2375 0.0359  -0.0183 -0.0076 252 LYS B CD  
4250 C  CD  B LYS B 251 ? 0.1926 0.2061 0.1724 -0.0107 -0.0755 -0.0513 252 LYS B CD  
4251 C  CE  A LYS B 251 ? 0.1333 0.2205 0.3648 0.0538  -0.0141 -0.0333 252 LYS B CE  
4252 C  CE  B LYS B 251 ? 0.1576 0.2946 0.3242 -0.0250 -0.1247 -0.0538 252 LYS B CE  
4253 N  NZ  A LYS B 251 ? 0.1972 0.3082 0.2876 0.0392  -0.0313 0.0832  252 LYS B NZ  
4254 N  NZ  B LYS B 251 ? 0.3100 0.5049 0.3544 0.0322  -0.1326 0.0160  252 LYS B NZ  
4255 N  N   . ASN B 252 ? 0.1907 0.2061 0.1254 0.0410  -0.0553 -0.0472 253 ASN B N   
4256 C  CA  . ASN B 252 ? 0.2031 0.3752 0.1805 0.0450  -0.0375 -0.0938 253 ASN B CA  
4257 C  C   . ASN B 252 ? 0.2274 0.2393 0.1812 0.0628  -0.0214 -0.0242 253 ASN B C   
4258 O  O   . ASN B 252 ? 0.2599 0.2452 0.2217 0.0450  -0.0001 -0.0052 253 ASN B O   
4259 C  CB  . ASN B 252 ? 0.2883 0.3914 0.2587 0.0559  -0.0685 -0.1492 253 ASN B CB  
4260 C  CG  . ASN B 252 ? 0.3682 0.2885 0.3578 0.1072  0.0538  -0.0780 253 ASN B CG  
4261 O  OD1 . ASN B 252 ? 0.7573 0.4945 0.4241 -0.0416 0.1993  -0.0092 253 ASN B OD1 
4262 N  ND2 . ASN B 252 ? 0.3134 0.3122 0.5430 -0.0239 -0.0496 -0.1702 253 ASN B ND2 
4263 N  N   . ARG B 253 ? 0.1630 0.3014 0.1071 0.0408  -0.0184 0.0114  254 ARG B N   
4264 C  CA  . ARG B 253 ? 0.1511 0.1782 0.0935 0.0395  -0.0126 -0.0104 254 ARG B CA  
4265 C  C   . ARG B 253 ? 0.1719 0.1748 0.0984 0.0266  0.0148  -0.0185 254 ARG B C   
4266 O  O   . ARG B 253 ? 0.2815 0.1756 0.2973 0.0694  0.1310  0.0551  254 ARG B O   
4267 C  CB  . ARG B 253 ? 0.1421 0.1518 0.0860 0.0154  -0.0087 -0.0195 254 ARG B CB  
4268 C  CG  . ARG B 253 ? 0.1559 0.1231 0.1033 0.0024  -0.0054 -0.0155 254 ARG B CG  
4269 C  CD  . ARG B 253 ? 0.1597 0.1040 0.0920 0.0129  -0.0043 -0.0024 254 ARG B CD  
4270 N  NE  . ARG B 253 ? 0.1218 0.1182 0.1010 0.0111  -0.0164 0.0048  254 ARG B NE  
4271 C  CZ  . ARG B 253 ? 0.0895 0.1077 0.0854 -0.0015 -0.0127 -0.0015 254 ARG B CZ  
4272 N  NH1 . ARG B 253 ? 0.0834 0.1150 0.0944 -0.0046 -0.0206 -0.0057 254 ARG B NH1 
4273 N  NH2 . ARG B 253 ? 0.1137 0.1101 0.0995 0.0098  -0.0287 -0.0071 254 ARG B NH2 
4274 N  N   . GLN B 254 ? 0.1483 0.1700 0.1357 0.0109  -0.0023 -0.0489 255 GLN B N   
4275 C  CA  . GLN B 254 ? 0.1576 0.2027 0.1307 0.0065  -0.0003 -0.0417 255 GLN B CA  
4276 C  C   . GLN B 254 ? 0.1826 0.1641 0.1236 -0.0027 -0.0081 -0.0010 255 GLN B C   
4277 O  O   . GLN B 254 ? 0.2382 0.1543 0.2225 -0.0021 -0.0737 0.0015  255 GLN B O   
4278 C  CB  . GLN B 254 ? 0.2008 0.3359 0.1421 0.0043  0.0074  -0.0869 255 GLN B CB  
4279 C  CG  . GLN B 254 ? 0.4020 0.4327 0.4347 -0.0535 0.1164  -0.0891 255 GLN B CG  
4280 N  N   . ILE B 255 ? 0.1375 0.1428 0.1108 0.0196  -0.0017 -0.0054 256 ILE B N   
4281 C  CA  . ILE B 255 ? 0.1278 0.1402 0.1062 0.0060  0.0019  0.0071  256 ILE B CA  
4282 C  C   . ILE B 255 ? 0.1414 0.1431 0.0945 0.0320  0.0157  0.0183  256 ILE B C   
4283 O  O   . ILE B 255 ? 0.1638 0.1616 0.1278 0.0216  0.0160  0.0511  256 ILE B O   
4284 C  CB  . ILE B 255 ? 0.1330 0.1288 0.1053 0.0140  0.0046  0.0019  256 ILE B CB  
4285 C  CG1 . ILE B 255 ? 0.1274 0.1360 0.1368 0.0167  -0.0027 0.0054  256 ILE B CG1 
4286 C  CG2 . ILE B 255 ? 0.1442 0.1761 0.1213 -0.0219 -0.0107 0.0082  256 ILE B CG2 
4287 C  CD1 . ILE B 255 ? 0.1854 0.1383 0.1401 0.0046  0.0236  -0.0096 256 ILE B CD1 
4288 N  N   . LYS B 256 ? 0.1242 0.1542 0.0886 0.0057  0.0035  0.0189  257 LYS B N   
4289 C  CA  . LYS B 256 ? 0.1280 0.1479 0.1028 0.0083  0.0186  0.0333  257 LYS B CA  
4290 C  C   . LYS B 256 ? 0.1263 0.1389 0.0935 0.0074  -0.0046 0.0114  257 LYS B C   
4291 O  O   . LYS B 256 ? 0.1579 0.1894 0.0905 -0.0428 0.0140  0.0094  257 LYS B O   
4292 C  CB  . LYS B 256 ? 0.1464 0.1509 0.1139 -0.0024 -0.0012 -0.0238 257 LYS B CB  
4293 C  CG  . LYS B 256 ? 0.2161 0.2028 0.2202 -0.0003 -0.0038 -0.0423 257 LYS B CG  
4294 C  CD  . LYS B 256 ? 0.3567 0.2432 0.2556 0.0274  -0.0410 -0.0471 257 LYS B CD  
4295 C  CE  . LYS B 256 ? 0.4050 0.4968 0.3282 -0.1341 -0.0065 -0.1837 257 LYS B CE  
4296 N  NZ  . LYS B 256 ? 0.4887 0.4490 0.2405 -0.1044 -0.0973 -0.0465 257 LYS B NZ  
4297 N  N   . ALA B 257 ? 0.1196 0.1572 0.1050 -0.0040 0.0232  0.0138  258 ALA B N   
4298 C  CA  . ALA B 257 ? 0.1254 0.1570 0.1114 -0.0027 0.0027  0.0080  258 ALA B CA  
4299 C  C   . ALA B 257 ? 0.1134 0.1594 0.1157 -0.0186 0.0043  0.0105  258 ALA B C   
4300 O  O   . ALA B 257 ? 0.1504 0.1838 0.1121 -0.0119 0.0333  -0.0044 258 ALA B O   
4301 C  CB  . ALA B 257 ? 0.1550 0.1500 0.1687 -0.0115 0.0260  0.0035  258 ALA B CB  
4302 N  N   . SER B 258 ? 0.1171 0.1384 0.1195 0.0003  0.0126  0.0052  259 SER B N   
4303 C  CA  . SER B 258 ? 0.1360 0.1625 0.1527 -0.0035 0.0214  -0.0041 259 SER B CA  
4304 C  C   . SER B 258 ? 0.1119 0.1926 0.1679 -0.0100 0.0386  -0.0091 259 SER B C   
4305 O  O   . SER B 258 ? 0.1341 0.2851 0.1977 0.0187  0.0489  0.0195  259 SER B O   
4306 C  CB  . SER B 258 ? 0.1449 0.1821 0.1424 -0.0148 -0.0108 0.0074  259 SER B CB  
4307 O  OG  . SER B 258 ? 0.1132 0.2009 0.1256 0.0034  0.0217  0.0012  259 SER B OG  
4308 N  N   . PHE B 259 ? 0.1406 0.1966 0.1644 -0.0199 0.0430  0.0107  260 PHE B N   
4309 C  CA  . PHE B 259 ? 0.1748 0.2195 0.2013 -0.0476 0.0649  0.0340  260 PHE B CA  
4310 C  C   . PHE B 259 ? 0.2329 0.2334 0.1973 -0.0710 0.0568  0.0240  260 PHE B C   
4311 O  O   . PHE B 259 ? 0.2876 0.2281 0.2269 -0.0625 0.0062  0.0944  260 PHE B O   
4312 C  CB  . PHE B 259 ? 0.1705 0.2252 0.1932 -0.0498 0.0370  0.0120  260 PHE B CB  
4313 C  CG  . PHE B 259 ? 0.1715 0.1675 0.2053 -0.0432 0.0221  0.0197  260 PHE B CG  
4314 C  CD1 . PHE B 259 ? 0.1480 0.1861 0.1454 -0.0447 0.0027  0.0055  260 PHE B CD1 
4315 C  CD2 . PHE B 259 ? 0.2425 0.1701 0.2703 -0.0436 0.0505  0.0142  260 PHE B CD2 
4316 C  CE1 . PHE B 259 ? 0.1497 0.1897 0.1967 -0.0251 -0.0114 0.0007  260 PHE B CE1 
4317 C  CE2 . PHE B 259 ? 0.2436 0.1767 0.2976 -0.0159 0.0164  0.0243  260 PHE B CE2 
4318 C  CZ  . PHE B 259 ? 0.2556 0.1785 0.2703 -0.0414 0.0239  -0.0124 260 PHE B CZ  
4319 N  N   . LYS B 260 ? 0.4305 0.7017 0.4113 -0.2696 0.0936  0.1578  261 LYS B N   
4320 C  CA  . LYS B 260 ? 0.6280 0.5587 0.3964 -0.1006 0.1140  0.1340  261 LYS B CA  
4321 C  C   . LYS B 260 ? 1.0088 0.8668 0.4348 -0.2971 0.1326  0.4099  261 LYS B C   
4322 O  O   . LYS B 260 ? 0.7362 0.5522 1.1959 -0.1844 -0.1436 0.1280  261 LYS B O   
4323 C  CB  . LYS B 260 ? 0.9368 0.4359 0.4523 -0.1817 0.1324  0.1562  261 LYS B CB  
4324 C  CG  . LYS B 260 ? 0.8762 0.3842 0.6484 -0.3578 0.1947  -0.0017 261 LYS B CG  
4325 C  CD  . LYS B 260 ? 1.2328 0.4711 0.7598 -0.3278 -0.1940 -0.1731 261 LYS B CD  
4326 C  CE  . LYS B 260 ? 1.2354 0.3300 0.3919 -0.2012 -0.3120 0.1368  261 LYS B CE  
4327 N  NZ  . LYS B 260 ? 1.7396 0.3691 0.3607 -0.0745 0.1412  0.0086  261 LYS B NZ  
4328 O  OXT . LYS B 260 ? 1.0803 0.6128 1.3137 -0.2023 0.0065  0.2078  261 LYS B OXT 
4329 ZN ZN  . ZN  C .   ? 0.1050 0.0769 0.0872 0.0108  -0.0057 -0.0024 301 ZN  A ZN  
4330 N  N1  . BCN D .   ? 0.3630 0.2967 0.2714 0.0200  -0.0216 0.0298  302 BCN A N1  
4331 C  C1  . BCN D .   ? 0.2041 0.4293 0.3278 0.1685  -0.0614 -0.0637 302 BCN A C1  
4332 C  C2  . BCN D .   ? 0.2910 0.3639 0.4007 0.1207  0.0241  -0.0531 302 BCN A C2  
4333 O  O21 . BCN D .   ? 0.3707 0.3440 0.4296 0.0566  -0.0121 -0.0986 302 BCN A O21 
4334 O  O22 . BCN D .   ? 0.3919 0.4377 0.4855 0.1902  -0.1282 -0.1834 302 BCN A O22 
4335 C  C3  . BCN D .   ? 0.2603 0.1890 0.3522 0.0463  0.0073  -0.0348 302 BCN A C3  
4336 C  C4  . BCN D .   ? 0.4058 0.3427 0.3991 -0.0359 0.0472  0.0610  302 BCN A C4  
4337 O  O4  . BCN D .   ? 0.4471 0.2939 0.3465 0.0148  0.1519  -0.0057 302 BCN A O4  
4338 C  C5  . BCN D .   ? 0.2222 0.1460 0.2955 0.0390  0.0284  -0.0313 302 BCN A C5  
4339 C  C6  . BCN D .   ? 0.4298 0.3639 0.3754 0.1035  -0.0377 0.0364  302 BCN A C6  
4340 O  O6  . BCN D .   ? 0.7026 0.3413 0.4774 0.2255  0.1529  0.0375  302 BCN A O6  
4341 S  S   . DMS E .   ? 0.2633 0.2452 0.2640 0.0238  0.0299  0.0233  303 DMS A S   
4342 O  O   . DMS E .   ? 0.4550 0.3107 0.2928 -0.0229 0.1004  0.1209  303 DMS A O   
4343 C  C1  . DMS E .   ? 0.2039 0.2462 0.2409 0.0062  0.0436  0.0815  303 DMS A C1  
4344 C  C2  . DMS E .   ? 0.3215 0.2027 0.3425 0.0140  0.0529  0.0423  303 DMS A C2  
4345 F  F13 . 5DU F .   ? 0.7222 0.5375 0.3594 -0.1186 0.1952  -0.0322 304 5DU A F13 
4346 C  C9  . 5DU F .   ? 0.3655 0.2786 0.3339 -0.0866 0.0218  0.0081  304 5DU A C9  
4347 C  C8  . 5DU F .   ? 0.4422 0.2289 0.2858 -0.0107 0.1242  -0.0658 304 5DU A C8  
4348 S  S24 . 5DU F .   ? 0.5809 0.3154 0.4908 0.0146  0.0295  -0.1107 304 5DU A S24 
4349 C  C25 . 5DU F .   ? 0.3039 0.2788 0.1236 0.0746  0.0054  -0.0003 304 5DU A C25 
4350 C  C26 . 5DU F .   ? 0.5583 0.2705 0.2991 0.0395  -0.0454 -0.0183 304 5DU A C26 
4351 O  O27 . 5DU F .   ? 0.6359 0.6618 0.3869 0.0471  0.0615  -0.2897 304 5DU A O27 
4352 C  C7  . 5DU F .   ? 0.2560 0.1871 0.2615 -0.0408 0.0094  -0.0305 304 5DU A C7  
4353 F  F12 . 5DU F .   ? 0.3352 0.2125 0.3271 -0.0579 -0.0215 -0.0175 304 5DU A F12 
4354 C  C6  . 5DU F .   ? 0.2487 0.1713 0.2231 0.0026  -0.0031 -0.0313 304 5DU A C6  
4355 F  F11 . 5DU F .   ? 0.2955 0.2506 0.2462 0.0505  -0.0143 -0.0124 304 5DU A F11 
4356 C  C10 . 5DU F .   ? 0.2494 0.2795 0.2549 0.0041  0.0370  -0.0324 304 5DU A C10 
4357 C  C5  . 5DU F .   ? 0.2477 0.1546 0.2899 -0.0057 -0.0697 0.0081  304 5DU A C5  
4358 S  S1  . 5DU F .   ? 0.2390 0.1768 0.1987 0.0439  -0.0423 -0.0087 304 5DU A S1  
4359 O  O3  . 5DU F .   ? 0.2249 0.1911 0.2083 0.0318  -0.0395 0.0252  304 5DU A O3  
4360 N  N4  . 5DU F .   ? 0.1635 0.1343 0.1563 0.0531  -0.0405 0.0286  304 5DU A N4  
4361 O  O2  . 5DU F .   ? 0.1213 0.1465 0.1616 0.0021  -0.0209 0.0136  304 5DU A O2  
4362 N  N14 . 5DU F .   ? 0.2949 0.3043 0.5138 0.0373  0.1268  0.0603  304 5DU A N14 
4363 C  C15 . 5DU F .   ? 0.2222 0.2829 0.3406 0.0256  0.0283  -0.0548 304 5DU A C15 
4364 C  C19 . 5DU F .   ? 0.2429 0.2755 0.2045 0.0148  0.0670  -0.0428 304 5DU A C19 
4365 C  C20 . 5DU F .   ? 0.2601 0.2434 0.3195 -0.0351 0.1155  -0.0566 304 5DU A C20 
4366 C  C21 . 5DU F .   ? 0.3271 0.2980 0.2786 -0.0817 0.0778  0.0149  304 5DU A C21 
4367 C  C22 . 5DU F .   ? 0.2572 0.2752 0.1436 -0.0472 -0.0253 0.0601  304 5DU A C22 
4368 C  C23 . 5DU F .   ? 0.2908 0.2939 0.2340 -0.0640 0.0377  0.0097  304 5DU A C23 
4369 C  C18 . 5DU F .   ? 0.2384 0.2590 0.2879 -0.0310 -0.0038 0.0311  304 5DU A C18 
4370 C  C17 . 5DU F .   ? 0.3201 0.2793 0.3935 -0.0223 -0.0623 -0.0082 304 5DU A C17 
4371 C  C16 . 5DU F .   ? 0.2278 0.3461 0.4146 0.0293  0.0685  0.0000  304 5DU A C16 
4372 ZN ZN  . ZN  G .   ? 0.1045 0.0789 0.0856 -0.0109 -0.0071 0.0000  301 ZN  B ZN  
4373 N  N1  . BCN H .   ? 0.3237 0.2890 0.3578 0.0108  -0.0020 -0.0498 302 BCN B N1  
4374 C  C1  . BCN H .   ? 0.2576 0.4029 0.3237 -0.1079 -0.0342 0.0256  302 BCN B C1  
4375 C  C2  . BCN H .   ? 0.6169 0.4620 0.4839 -0.0131 -0.0623 0.1063  302 BCN B C2  
4376 O  O21 . BCN H .   ? 0.8088 0.7235 0.5813 -0.2953 -0.3307 0.0456  302 BCN B O21 
4377 O  O22 . BCN H .   ? 0.4338 0.3350 0.5134 -0.1287 0.1448  -0.0163 302 BCN B O22 
4378 C  C3  . BCN H .   ? 0.1715 0.1722 0.3217 -0.0251 0.0315  0.0035  302 BCN B C3  
4379 C  C4  . BCN H .   ? 0.5066 0.3684 0.4165 -0.1228 -0.0275 -0.0340 302 BCN B C4  
4380 O  O4  . BCN H .   ? 0.5861 0.6729 0.6243 -0.3102 -0.1581 0.2485  302 BCN B O4  
4381 C  C5  . BCN H .   ? 0.1990 0.2161 0.2913 -0.0339 0.0351  0.0375  302 BCN B C5  
4382 C  C6  . BCN H .   ? 0.5857 0.4569 0.4758 0.0684  0.1787  -0.1554 302 BCN B C6  
4383 O  O6  . BCN H .   ? 0.3411 0.3436 0.3716 -0.0355 0.0775  -0.0489 302 BCN B O6  
4384 S  S   . DMS I .   ? 0.2779 0.2481 0.2628 -0.0322 0.0271  -0.0417 303 DMS B S   
4385 O  O   . DMS I .   ? 0.4625 0.2930 0.3289 0.0239  0.1404  -0.1129 303 DMS B O   
4386 C  C1  . DMS I .   ? 0.2459 0.2585 0.2558 -0.0152 0.0718  -0.0996 303 DMS B C1  
4387 C  C2  . DMS I .   ? 0.2872 0.1952 0.3057 -0.0046 0.0434  -0.0284 303 DMS B C2  
4388 F  F13 . 5DU J .   ? 0.3652 0.3217 0.2766 0.0324  0.0368  0.0035  304 5DU B F13 
4389 C  C9  . 5DU J .   ? 0.2398 0.2339 0.2351 0.0013  0.0063  -0.0136 304 5DU B C9  
4390 C  C8  . 5DU J .   ? 0.2689 0.2161 0.2192 0.0003  -0.0083 0.0163  304 5DU B C8  
4391 S  S24 . 5DU J .   ? 0.3106 0.2741 0.2831 0.0153  -0.0174 0.0024  304 5DU B S24 
4392 C  C25 . 5DU J .   ? 0.4205 0.3860 0.3303 -0.0780 0.0467  0.0157  304 5DU B C25 
4393 C  C26 . 5DU J .   ? 0.3978 0.3621 0.3503 0.0322  0.0015  0.0307  304 5DU B C26 
4394 O  O27 . 5DU J .   ? 0.3519 0.4487 0.3562 -0.0217 -0.0051 0.0148  304 5DU B O27 
4395 C  C7  . 5DU J .   ? 0.2430 0.1900 0.2264 0.0364  0.0096  0.0237  304 5DU B C7  
4396 F  F12 . 5DU J .   ? 0.2678 0.2193 0.2739 0.0291  -0.0038 -0.0031 304 5DU B F12 
4397 C  C6  . 5DU J .   ? 0.2451 0.1684 0.2066 -0.0100 -0.0020 0.0208  304 5DU B C6  
4398 F  F11 . 5DU J .   ? 0.2476 0.2397 0.2232 -0.0142 -0.0007 0.0003  304 5DU B F11 
4399 C  C10 . 5DU J .   ? 0.2648 0.2531 0.2364 -0.0068 -0.0066 0.0115  304 5DU B C10 
4400 C  C5  . 5DU J .   ? 0.2425 0.1833 0.2569 0.0104  -0.0944 -0.0138 304 5DU B C5  
4401 S  S1  . 5DU J .   ? 0.2414 0.1608 0.2275 -0.0024 -0.0940 -0.0212 304 5DU B S1  
4402 O  O3  . 5DU J .   ? 0.3328 0.1969 0.2716 0.0362  -0.1712 -0.0878 304 5DU B O3  
4403 N  N4  . 5DU J .   ? 0.2980 0.1233 0.2569 -0.1182 -0.1451 0.0328  304 5DU B N4  
4404 O  O2  . 5DU J .   ? 0.4307 0.2483 0.2150 -0.0661 0.0405  0.0006  304 5DU B O2  
4405 N  N14 . 5DU J .   ? 0.3512 0.3043 0.2772 0.0197  -0.0059 -0.0057 304 5DU B N14 
4406 C  C15 . 5DU J .   ? 0.2249 0.2402 0.2746 0.0076  0.0046  0.0441  304 5DU B C15 
4407 C  C19 . 5DU J .   ? 0.2305 0.2380 0.2073 -0.0044 0.0460  0.0031  304 5DU B C19 
4408 C  C20 . 5DU J .   ? 0.2274 0.2346 0.2310 0.0146  0.0649  0.0292  304 5DU B C20 
4409 C  C21 . 5DU J .   ? 0.2687 0.2255 0.2233 0.0023  0.0231  -0.0046 304 5DU B C21 
4410 C  C22 . 5DU J .   ? 0.1902 0.2466 0.2093 0.0381  -0.0114 -0.0603 304 5DU B C22 
4411 C  C23 . 5DU J .   ? 0.2587 0.2484 0.2190 0.0320  0.0093  -0.0195 304 5DU B C23 
4412 C  C18 . 5DU J .   ? 0.2346 0.2142 0.2601 0.0209  0.0055  -0.0237 304 5DU B C18 
4413 C  C17 . 5DU J .   ? 0.2696 0.2498 0.2757 -0.0131 -0.0386 -0.0533 304 5DU B C17 
4414 C  C16 . 5DU J .   ? 0.2606 0.3151 0.3898 0.0010  0.0141  -0.0288 304 5DU B C16 
4415 O  O   . HOH K .   ? 0.1900 0.3770 0.3032 0.0148  -0.0533 -0.0447 401 HOH A O   
4416 O  O   . HOH K .   ? 0.4167 0.4524 0.4162 -0.0115 -0.0606 0.0529  402 HOH A O   
4417 O  O   . HOH K .   ? 0.4156 0.1513 0.5358 0.0229  -0.1387 0.0351  403 HOH A O   
4418 O  O   . HOH K .   ? 0.3574 0.3980 0.2393 -0.0229 -0.0122 -0.0467 404 HOH A O   
4419 O  O   . HOH K .   ? 0.7512 0.3619 0.2216 0.1960  0.0195  0.0778  405 HOH A O   
4420 O  O   . HOH K .   ? 0.5275 0.4900 0.9711 0.0892  -0.1809 -0.0192 406 HOH A O   
4421 O  O   . HOH K .   ? 0.4034 0.4002 0.7917 0.1389  0.0898  0.0454  407 HOH A O   
4422 O  O   . HOH K .   ? 1.8532 0.6281 0.5541 -0.1831 0.2894  -0.0074 408 HOH A O   
4423 O  O   . HOH K .   ? 0.4650 0.2682 0.4854 0.0164  0.1203  -0.1027 409 HOH A O   
4424 O  O   . HOH K .   ? 0.4621 0.4221 0.6977 -0.0240 -0.3037 -0.1820 410 HOH A O   
4425 O  O   . HOH K .   ? 0.3776 0.2463 0.2989 0.0822  0.1137  0.0822  411 HOH A O   
4426 O  O   . HOH K .   ? 0.3524 0.2606 0.2840 -0.0447 0.0507  -0.0653 412 HOH A O   
4427 O  O   . HOH K .   ? 0.2249 0.2064 0.3248 -0.0248 0.0221  -0.0013 413 HOH A O   
4428 O  O   . HOH K .   ? 0.1106 0.1157 0.1414 0.0066  0.0236  0.0243  414 HOH A O   
4429 O  O   . HOH K .   ? 0.2425 0.2628 0.3862 0.0549  -0.0082 0.0082  415 HOH A O   
4430 O  O   . HOH K .   ? 0.4580 0.3291 0.6481 0.1006  0.0577  -0.0311 416 HOH A O   
4431 O  O   . HOH K .   ? 0.3201 0.4198 0.3603 -0.1053 0.1587  -0.0258 417 HOH A O   
4432 O  O   . HOH K .   ? 0.5266 0.4876 0.2405 0.1247  0.0412  0.0344  418 HOH A O   
4433 O  O   . HOH K .   ? 0.5916 0.9889 0.6129 -0.0256 0.0227  0.0421  419 HOH A O   
4434 O  O   . HOH K .   ? 0.4630 0.4250 0.3122 0.2283  0.1802  0.1897  420 HOH A O   
4435 O  O   . HOH K .   ? 1.3058 0.9195 0.7072 0.6433  0.0961  0.6688  421 HOH A O   
4436 O  O   . HOH K .   ? 0.4284 0.2504 0.3499 -0.0054 0.1774  0.0276  422 HOH A O   
4437 O  O   . HOH K .   ? 0.5180 0.3127 0.1155 0.0120  -0.0144 -0.0098 423 HOH A O   
4438 O  O   . HOH K .   ? 0.5673 0.4361 0.2481 0.0384  -0.1437 -0.0443 424 HOH A O   
4439 O  O   . HOH K .   ? 0.5643 0.2897 0.1854 0.0551  0.1191  0.0467  425 HOH A O   
4440 O  O   . HOH K .   ? 0.3260 0.5828 0.6119 -0.0189 -0.0005 0.0816  426 HOH A O   
4441 O  O   . HOH K .   ? 0.2621 0.2173 0.4282 -0.0182 0.0452  -0.0658 427 HOH A O   
4442 O  O   . HOH K .   ? 0.5731 0.2547 0.5274 0.0992  -0.0907 0.1151  428 HOH A O   
4443 O  O   . HOH K .   ? 0.3003 0.5004 0.2318 -0.0388 -0.0031 0.0965  429 HOH A O   
4444 O  O   . HOH K .   ? 0.3456 0.3461 0.3366 0.0974  0.1518  0.2002  430 HOH A O   
4445 O  O   . HOH K .   ? 0.2259 0.3240 0.2472 0.0364  0.0553  -0.0370 431 HOH A O   
4446 O  O   . HOH K .   ? 0.2843 0.4262 0.7171 0.0932  0.2173  0.0516  432 HOH A O   
4447 O  O   . HOH K .   ? 0.3741 0.4591 0.1624 0.1314  -0.1174 -0.0507 433 HOH A O   
4448 O  O   . HOH K .   ? 0.1855 0.1139 0.0829 0.0270  -0.0065 -0.0081 434 HOH A O   
4449 O  O   . HOH K .   ? 0.2026 0.2012 0.2118 -0.0125 -0.0425 0.0086  435 HOH A O   
4450 O  O   . HOH K .   ? 0.1428 1.1057 0.9210 -0.2016 0.1990  0.2989  436 HOH A O   
4451 O  O   . HOH K .   ? 0.4180 0.2667 0.3722 0.0379  -0.0230 0.0256  437 HOH A O   
4452 O  O   . HOH K .   ? 0.2133 0.7741 0.3774 -0.0970 0.0103  0.0031  438 HOH A O   
4453 O  O   . HOH K .   ? 0.4187 0.7888 0.2222 0.0631  0.1158  0.0172  439 HOH A O   
4454 O  O   . HOH K .   ? 0.4508 0.7174 1.5856 -0.0008 -0.0835 -0.4404 440 HOH A O   
4455 O  O   . HOH K .   ? 0.5472 0.3310 0.6305 0.0806  0.1213  0.0267  441 HOH A O   
4456 O  O   . HOH K .   ? 0.2107 0.1649 0.2513 0.0388  -0.0340 -0.0403 442 HOH A O   
4457 O  O   . HOH K .   ? 0.5418 0.4138 0.4819 0.2520  -0.2646 -0.1752 443 HOH A O   
4458 O  O   . HOH K .   ? 0.2811 0.2285 0.2383 0.0480  -0.0099 0.0089  444 HOH A O   
4459 O  O   . HOH K .   ? 0.3075 0.1834 0.2285 0.0829  -0.0505 0.0003  445 HOH A O   
4460 O  O   . HOH K .   ? 0.2178 0.2578 0.2703 -0.0195 -0.0054 -0.0348 446 HOH A O   
4461 O  O   . HOH K .   ? 0.3772 0.6389 0.4458 0.1167  0.0388  -0.3158 447 HOH A O   
4462 O  O   . HOH K .   ? 0.3009 0.1643 0.2836 0.0003  0.0308  -0.0658 448 HOH A O   
4463 O  O   . HOH K .   ? 0.2919 0.5245 0.3959 -0.0773 0.0920  -0.0969 449 HOH A O   
4464 O  O   . HOH K .   ? 0.1974 0.1958 0.2728 0.0000  -0.1289 0.0351  450 HOH A O   
4465 O  O   . HOH K .   ? 0.3533 0.1911 0.2791 0.0555  -0.0886 -0.0509 451 HOH A O   
4466 O  O   . HOH K .   ? 0.2167 0.2097 0.2808 -0.0496 0.0465  -0.0652 452 HOH A O   
4467 O  O   . HOH K .   ? 0.1403 0.1037 0.1220 0.0088  0.0035  0.0113  453 HOH A O   
4468 O  O   . HOH K .   ? 0.2081 0.3790 0.6010 0.0013  -0.0900 0.0527  454 HOH A O   
4469 O  O   . HOH K .   ? 0.6150 0.2354 0.1676 0.1093  -0.0417 -0.0820 455 HOH A O   
4470 O  O   . HOH K .   ? 0.4356 0.2400 0.4860 0.1648  -0.0211 -0.0197 456 HOH A O   
4471 O  O   . HOH K .   ? 0.2919 0.6419 0.2493 -0.1257 -0.0427 -0.0335 457 HOH A O   
4472 O  O   . HOH K .   ? 0.1255 0.1511 0.1269 -0.0046 -0.0315 -0.0077 458 HOH A O   
4473 O  O   . HOH K .   ? 0.1595 0.1123 0.1200 0.0115  0.0082  0.0135  459 HOH A O   
4474 O  O   . HOH K .   ? 0.4435 0.3400 0.3634 0.0454  0.0399  0.0485  460 HOH A O   
4475 O  O   . HOH K .   ? 0.2836 0.2992 0.2081 -0.0555 0.0753  0.0193  461 HOH A O   
4476 O  O   . HOH K .   ? 0.1928 0.3179 0.4052 -0.0636 -0.0493 0.0026  462 HOH A O   
4477 O  O   . HOH K .   ? 0.1730 0.1028 0.1564 0.0185  -0.0092 -0.0110 463 HOH A O   
4478 O  O   . HOH K .   ? 0.2913 0.4589 0.7933 -0.0209 0.0031  -0.2427 464 HOH A O   
4479 O  O   . HOH K .   ? 0.2854 0.4995 0.2319 0.0964  0.0151  -0.0573 465 HOH A O   
4480 O  O   . HOH K .   ? 0.3361 0.2408 0.1615 0.0006  -0.0586 0.0126  466 HOH A O   
4481 O  O   . HOH K .   ? 0.3646 0.2671 0.1940 0.0516  0.0644  0.0791  467 HOH A O   
4482 O  O   . HOH K .   ? 0.3106 1.1101 0.4099 -0.1582 0.1145  0.0953  468 HOH A O   
4483 O  O   . HOH K .   ? 0.5835 0.2642 0.1451 0.0092  -0.0445 0.0412  469 HOH A O   
4484 O  O   . HOH K .   ? 0.5370 0.3977 0.3300 0.1270  -0.0078 0.0164  470 HOH A O   
4485 O  O   . HOH K .   ? 0.2612 0.1814 0.1543 0.0080  0.0366  -0.0337 471 HOH A O   
4486 O  O   . HOH K .   ? 0.4580 0.4325 0.2171 -0.0333 -0.0718 -0.0274 472 HOH A O   
4487 O  O   . HOH K .   ? 0.4835 0.3653 0.3145 -0.0472 0.1380  -0.1216 473 HOH A O   
4488 O  O   . HOH K .   ? 0.6895 0.2337 0.1586 -0.0196 0.0171  -0.0160 474 HOH A O   
4489 O  O   . HOH K .   ? 1.6277 1.1143 0.2046 -0.3468 -0.2897 0.3634  475 HOH A O   
4490 O  O   . HOH K .   ? 0.3842 0.5044 0.7390 0.0340  -0.1571 -0.0724 476 HOH A O   
4491 O  O   . HOH K .   ? 0.2851 0.3899 0.3481 0.0794  -0.1221 -0.0472 477 HOH A O   
4492 O  O   . HOH K .   ? 0.4217 0.1961 0.3188 -0.1071 -0.0886 0.0179  478 HOH A O   
4493 O  O   . HOH K .   ? 0.2802 0.2651 0.1841 0.0419  0.0195  0.0408  479 HOH A O   
4494 O  O   . HOH K .   ? 1.1158 0.3772 0.6565 0.0529  0.1306  -0.0441 480 HOH A O   
4495 O  O   . HOH K .   ? 0.5475 0.2870 0.2391 0.1370  -0.1638 -0.0115 481 HOH A O   
4496 O  O   . HOH K .   ? 0.5407 0.2513 0.2257 0.0129  -0.0568 -0.1344 482 HOH A O   
4497 O  O   . HOH K .   ? 0.1031 0.1019 0.1236 0.0093  0.0052  -0.0020 483 HOH A O   
4498 O  O   . HOH K .   ? 0.2820 0.3066 0.3425 0.1013  -0.0544 -0.0253 484 HOH A O   
4499 O  O   . HOH K .   ? 0.1456 0.1527 0.3350 0.0304  -0.0643 -0.0205 485 HOH A O   
4500 O  O   . HOH K .   ? 0.1969 0.1777 0.3037 -0.0118 0.0474  -0.0073 486 HOH A O   
4501 O  O   . HOH K .   ? 0.4879 0.2872 0.7555 -0.0408 0.0357  -0.0335 487 HOH A O   
4502 O  O   . HOH K .   ? 0.3379 0.3389 0.2364 0.1124  -0.0156 0.0724  488 HOH A O   
4503 O  O   . HOH K .   ? 0.2060 0.1483 0.1912 0.0065  -0.0615 -0.0110 489 HOH A O   
4504 O  O   . HOH K .   ? 0.2576 0.1979 0.3039 0.0049  0.0271  0.0439  490 HOH A O   
4505 O  O   . HOH K .   ? 0.1054 0.1166 0.1155 -0.0195 -0.0098 0.0060  491 HOH A O   
4506 O  O   . HOH K .   ? 0.0807 0.8687 1.0605 -0.1627 -0.1308 0.6777  492 HOH A O   
4507 O  O   . HOH K .   ? 0.7799 0.3298 0.4510 0.1253  0.2926  0.0546  493 HOH A O   
4508 O  O   . HOH K .   ? 0.3637 0.5271 0.3691 0.0109  -0.1306 0.0625  494 HOH A O   
4509 O  O   . HOH K .   ? 0.2673 0.2257 0.3592 0.0258  -0.0923 0.0266  495 HOH A O   
4510 O  O   . HOH K .   ? 0.2176 0.2264 0.2108 0.0073  -0.0714 -0.0417 496 HOH A O   
4511 O  O   . HOH K .   ? 0.1295 0.0989 0.1222 -0.0089 -0.0113 0.0108  497 HOH A O   
4512 O  O   . HOH K .   ? 0.3591 0.3343 0.2657 -0.0196 0.0046  0.0496  498 HOH A O   
4513 O  O   . HOH K .   ? 0.2124 0.1254 0.1787 0.0381  -0.0114 0.0012  499 HOH A O   
4514 O  O   . HOH K .   ? 0.2080 0.3104 0.1838 0.0278  -0.0240 0.0776  500 HOH A O   
4515 O  O   . HOH K .   ? 0.4293 0.3677 0.4110 -0.1756 -0.1288 0.0966  501 HOH A O   
4516 O  O   . HOH K .   ? 0.2712 0.1634 0.2258 0.0174  -0.0615 0.0115  502 HOH A O   
4517 O  O   . HOH K .   ? 0.2818 0.2153 0.2757 -0.0027 -0.0509 -0.0606 503 HOH A O   
4518 O  O   . HOH K .   ? 0.3237 0.4584 0.2445 0.0597  -0.1262 -0.1342 504 HOH A O   
4519 O  O   . HOH K .   ? 0.2372 0.1758 0.2402 0.0094  -0.0196 0.0233  505 HOH A O   
4520 O  O   . HOH K .   ? 0.2590 0.1929 0.1942 -0.0040 0.0832  0.0167  506 HOH A O   
4521 O  O   . HOH K .   ? 0.2108 0.6179 0.3046 0.0041  -0.0212 -0.1738 507 HOH A O   
4522 O  O   . HOH K .   ? 0.0957 0.1371 0.2188 -0.0037 -0.0179 0.0318  508 HOH A O   
4523 O  O   . HOH K .   ? 0.4445 0.3039 0.4941 -0.0280 0.1468  -0.0395 509 HOH A O   
4524 O  O   . HOH K .   ? 0.5120 0.2617 0.2157 -0.0555 -0.0242 -0.0175 510 HOH A O   
4525 O  O   . HOH K .   ? 0.2795 0.3628 0.4690 -0.0082 0.2019  -0.0414 511 HOH A O   
4526 O  O   . HOH K .   ? 0.2014 0.1353 0.1464 0.0211  0.0001  -0.0078 512 HOH A O   
4527 O  O   . HOH K .   ? 0.2450 0.1344 0.1556 -0.0186 -0.0280 0.0000  513 HOH A O   
4528 O  O   . HOH K .   ? 0.3582 0.3355 0.4483 0.1009  -0.1181 -0.0586 514 HOH A O   
4529 O  O   . HOH K .   ? 0.1612 0.3761 0.3149 -0.0384 -0.0049 -0.1614 515 HOH A O   
4530 O  O   . HOH K .   ? 0.2472 0.2074 0.3190 -0.0267 0.0570  -0.0812 516 HOH A O   
4531 O  O   . HOH K .   ? 0.2655 0.3003 0.4131 -0.0571 0.0222  -0.0310 517 HOH A O   
4532 O  O   . HOH K .   ? 0.1993 0.2915 0.2231 0.0239  -0.0447 0.0044  518 HOH A O   
4533 O  O   . HOH K .   ? 0.1829 0.1640 0.1597 0.0060  -0.0078 -0.0093 519 HOH A O   
4534 O  O   . HOH K .   ? 0.4304 0.3851 0.5928 0.0750  -0.0326 -0.0693 520 HOH A O   
4535 O  O   . HOH K .   ? 0.1747 0.1245 0.1748 -0.0275 0.0107  -0.0242 521 HOH A O   
4536 O  O   . HOH K .   ? 0.4323 0.2418 0.2066 0.0971  0.1274  0.0773  522 HOH A O   
4537 O  O   . HOH K .   ? 0.2387 0.2081 0.1542 -0.0370 -0.0093 0.0234  523 HOH A O   
4538 O  O   . HOH K .   ? 0.2793 0.1843 0.2423 -0.0153 -0.0976 0.0355  524 HOH A O   
4539 O  O   . HOH K .   ? 0.3801 0.1456 0.1962 0.0102  -0.1341 -0.0167 525 HOH A O   
4540 O  O   . HOH K .   ? 1.4294 1.7203 0.1225 0.1374  0.2203  -0.1512 526 HOH A O   
4541 O  O   . HOH K .   ? 0.3077 0.2045 0.2016 -0.0179 0.0209  -0.0052 527 HOH A O   
4542 O  O   . HOH K .   ? 0.1729 0.9186 0.8187 0.1932  0.0423  0.0803  528 HOH A O   
4543 O  O   . HOH K .   ? 0.1476 0.1739 0.2011 -0.0286 -0.0153 -0.0261 529 HOH A O   
4544 O  O   . HOH K .   ? 0.3416 0.6922 0.3023 -0.0744 0.1167  -0.0904 530 HOH A O   
4545 O  O   . HOH K .   ? 0.1184 0.1789 0.2494 0.0102  -0.0041 -0.0232 531 HOH A O   
4546 O  O   . HOH K .   ? 1.0421 0.6162 0.5282 0.1058  -0.2425 -0.1375 532 HOH A O   
4547 O  O   . HOH K .   ? 0.1227 0.1224 0.1450 -0.0163 -0.0241 -0.0142 533 HOH A O   
4548 O  O   . HOH K .   ? 0.3032 0.1264 0.2342 -0.0057 -0.1176 -0.0028 534 HOH A O   
4549 O  O   . HOH K .   ? 0.2576 0.1844 0.2303 -0.0513 0.0623  -0.1039 535 HOH A O   
4550 O  O   . HOH K .   ? 0.5519 0.4419 0.3499 -0.2143 0.0165  0.0390  536 HOH A O   
4551 O  O   . HOH K .   ? 0.2833 0.1212 0.2098 0.0274  -0.0217 -0.0133 537 HOH A O   
4552 O  O   . HOH K .   ? 0.7261 0.3041 0.5194 0.0483  -0.0920 0.1430  538 HOH A O   
4553 O  O   . HOH K .   ? 0.1242 0.2924 0.3792 0.0322  -0.0441 -0.0665 539 HOH A O   
4554 O  O   . HOH K .   ? 0.6680 1.2553 0.2614 -0.2513 -0.1962 -0.0879 540 HOH A O   
4555 O  O   . HOH K .   ? 0.2127 0.1544 0.2671 -0.0467 -0.0057 0.0439  541 HOH A O   
4556 O  O   . HOH K .   ? 0.3215 0.1439 0.1867 0.0142  -0.0160 0.0220  542 HOH A O   
4557 O  O   . HOH K .   ? 0.2454 0.1347 0.1967 -0.0142 -0.0253 -0.0226 543 HOH A O   
4558 O  O   . HOH K .   ? 0.2348 0.2344 0.1878 -0.0494 0.0017  -0.0220 544 HOH A O   
4559 O  O   . HOH K .   ? 0.6108 0.2705 0.2276 0.1181  0.0071  0.0863  545 HOH A O   
4560 O  O   . HOH K .   ? 0.2430 0.2053 0.3729 0.0089  0.0280  0.1041  546 HOH A O   
4561 O  O   . HOH K .   ? 0.3273 0.2047 0.5957 -0.0096 -0.1516 -0.0472 547 HOH A O   
4562 O  O   . HOH K .   ? 0.3355 0.1565 0.3325 0.0197  -0.0817 0.0116  548 HOH A O   
4563 O  O   . HOH K .   ? 0.1483 0.1429 0.2283 0.0160  0.0241  0.0013  549 HOH A O   
4564 O  O   . HOH K .   ? 0.3941 0.2971 0.4962 -0.0335 -0.1464 0.0516  550 HOH A O   
4565 O  O   . HOH K .   ? 0.0833 0.1967 0.2340 -0.0111 0.0185  0.0373  551 HOH A O   
4566 O  O   . HOH K .   ? 0.2414 0.1972 0.2861 -0.0157 -0.0882 0.0870  552 HOH A O   
4567 O  O   . HOH K .   ? 0.4106 0.4605 0.2906 0.0285  -0.0469 0.0103  553 HOH A O   
4568 O  O   . HOH K .   ? 0.6004 0.3616 0.3091 0.0310  -0.1625 0.1036  554 HOH A O   
4569 O  O   . HOH K .   ? 0.2601 0.3648 0.5814 0.1556  -0.0754 -0.1381 555 HOH A O   
4570 O  O   . HOH K .   ? 0.4987 0.3433 0.2072 -0.2393 -0.0608 0.0137  556 HOH A O   
4571 O  O   . HOH K .   ? 0.4756 0.3416 0.3440 -0.0837 -0.0599 0.0485  557 HOH A O   
4572 O  O   . HOH K .   ? 0.2308 0.1750 0.3136 0.0838  -0.0643 0.0310  558 HOH A O   
4573 O  O   . HOH K .   ? 0.3161 0.1544 0.2766 -0.0162 -0.0824 0.0289  559 HOH A O   
4574 O  O   . HOH K .   ? 0.4440 0.3447 0.3082 0.1147  0.0105  0.0465  560 HOH A O   
4575 O  O   . HOH K .   ? 0.1242 0.3461 0.4566 -0.0074 -0.0555 -0.1356 561 HOH A O   
4576 O  O   . HOH K .   ? 0.2066 0.2711 0.2520 0.0342  0.0252  0.0000  562 HOH A O   
4577 O  O   . HOH K .   ? 0.6200 0.3156 0.3987 0.0381  0.0381  0.1427  563 HOH A O   
4578 O  O   . HOH K .   ? 0.3591 0.3072 0.6039 0.0870  0.1251  -0.0195 564 HOH A O   
4579 O  O   . HOH K .   ? 0.1552 0.2664 0.3934 -0.0608 0.0703  -0.0233 565 HOH A O   
4580 O  O   . HOH K .   ? 0.3982 0.2504 0.4102 -0.1322 -0.0350 0.0406  566 HOH A O   
4581 O  O   . HOH K .   ? 0.3583 0.2280 0.4135 -0.0088 0.0456  -0.1216 567 HOH A O   
4582 O  O   . HOH K .   ? 0.3971 0.1761 0.2727 -0.0759 -0.0777 0.0348  568 HOH A O   
4583 O  O   . HOH K .   ? 0.1671 0.2187 0.2423 0.0068  -0.0142 0.0259  569 HOH A O   
4584 O  O   . HOH K .   ? 0.4779 0.2129 0.2980 -0.0776 0.0507  -0.0386 570 HOH A O   
4585 O  O   . HOH K .   ? 0.4309 0.1808 0.2797 -0.0631 -0.0110 -0.0654 571 HOH A O   
4586 O  O   . HOH K .   ? 0.2975 0.2480 0.1819 -0.0864 0.0131  0.0201  572 HOH A O   
4587 O  O   . HOH K .   ? 0.2933 0.1500 0.1897 -0.0153 -0.0137 0.0107  573 HOH A O   
4588 O  O   . HOH K .   ? 0.2018 0.5142 0.3664 0.0285  0.0264  -0.1247 574 HOH A O   
4589 O  O   . HOH K .   ? 0.2484 0.2027 0.3357 -0.0888 -0.0447 0.0504  575 HOH A O   
4590 O  O   . HOH K .   ? 0.2581 0.2316 0.3359 -0.0531 0.0249  -0.0173 576 HOH A O   
4591 O  O   . HOH K .   ? 0.2531 0.4674 0.3937 0.0142  0.0000  0.0107  577 HOH A O   
4592 O  O   . HOH K .   ? 0.1175 0.2459 0.1768 0.0186  -0.0507 -0.0593 578 HOH A O   
4593 O  O   . HOH K .   ? 0.4607 0.2081 0.2057 0.1049  -0.1331 -0.0142 579 HOH A O   
4594 O  O   . HOH K .   ? 0.2342 1.2535 1.3727 0.3479  0.4864  0.4376  580 HOH A O   
4595 O  O   . HOH K .   ? 0.4717 0.3472 0.6701 -0.0399 -0.0060 0.1967  581 HOH A O   
4596 O  O   . HOH K .   ? 0.3346 0.2050 0.1988 -0.0289 -0.0483 -0.0403 582 HOH A O   
4597 O  O   . HOH K .   ? 0.2750 0.2052 0.2027 -0.0509 -0.0142 -0.0522 583 HOH A O   
4598 O  O   . HOH K .   ? 0.3222 0.3819 0.2594 0.0063  0.0401  0.0087  584 HOH A O   
4599 O  O   . HOH K .   ? 0.3147 0.2903 0.3064 0.0361  -0.1268 0.0104  585 HOH A O   
4600 O  O   . HOH K .   ? 0.3589 0.4106 0.1527 -0.0885 -0.0542 0.0060  586 HOH A O   
4601 O  O   . HOH K .   ? 0.1994 0.2597 0.3111 -0.0812 -0.1002 0.0654  587 HOH A O   
4602 O  O   . HOH K .   ? 0.2008 0.1900 0.7620 -0.0116 0.0692  0.1193  588 HOH A O   
4603 O  O   . HOH K .   ? 0.3235 0.3415 0.3596 -0.1394 0.0754  -0.0551 589 HOH A O   
4604 O  O   . HOH K .   ? 0.3623 0.2847 0.2157 -0.0164 0.1037  0.0185  590 HOH A O   
4605 O  O   . HOH K .   ? 0.1198 0.1062 0.1574 -0.0144 -0.0121 0.0017  591 HOH A O   
4606 O  O   . HOH K .   ? 0.2831 0.5773 0.4801 -0.0894 -0.0856 -0.0175 592 HOH A O   
4607 O  O   . HOH K .   ? 0.8274 0.8174 1.1813 -0.1915 0.3287  -0.6970 593 HOH A O   
4608 O  O   . HOH K .   ? 0.1087 0.1779 0.3201 0.0127  -0.0119 0.0038  594 HOH A O   
4609 O  O   . HOH K .   ? 0.2372 0.2881 0.8037 0.1160  0.1257  -0.0724 595 HOH A O   
4610 O  O   . HOH K .   ? 1.6526 0.7480 0.4293 -0.3896 0.3239  -0.5397 596 HOH A O   
4611 O  O   . HOH K .   ? 0.2267 0.2243 0.4433 -0.0502 0.0175  -0.0366 597 HOH A O   
4612 O  O   . HOH K .   ? 1.6466 1.5049 1.0240 -0.6615 -0.5536 0.5192  598 HOH A O   
4613 O  O   . HOH K .   ? 0.1759 0.3352 0.4650 -0.0307 0.0364  -0.1483 599 HOH A O   
4614 O  O   . HOH K .   ? 0.3019 0.2137 0.2676 -0.0930 0.0763  -0.0487 600 HOH A O   
4615 O  O   . HOH K .   ? 0.2276 0.4232 0.2264 -0.0562 -0.0313 0.0712  601 HOH A O   
4616 O  O   . HOH K .   ? 0.4016 0.3179 0.1905 0.0276  -0.0698 0.0015  602 HOH A O   
4617 O  O   . HOH K .   ? 0.3556 0.1924 0.3088 0.0377  -0.0610 -0.0285 603 HOH A O   
4618 O  O   . HOH K .   ? 0.1993 1.8216 0.8984 0.1425  0.1926  -0.0142 604 HOH A O   
4619 O  O   . HOH K .   ? 0.3522 1.9424 1.7266 0.2626  -0.0186 0.1044  605 HOH A O   
4620 O  O   . HOH K .   ? 0.3251 0.2476 0.7042 -0.0882 0.1375  -0.1365 606 HOH A O   
4621 O  O   . HOH K .   ? 0.4478 0.3736 0.4058 0.0264  0.0705  -0.1213 607 HOH A O   
4622 O  O   . HOH K .   ? 0.3817 0.4431 0.2448 0.1085  0.0403  -0.0318 608 HOH A O   
4623 O  O   . HOH K .   ? 0.5097 0.2344 0.4901 -0.0610 0.2395  -0.0790 609 HOH A O   
4624 O  O   . HOH K .   ? 0.6219 0.3039 0.2849 0.1102  0.1358  -0.1319 610 HOH A O   
4625 O  O   . HOH K .   ? 0.2484 0.6140 0.2763 -0.0386 0.0441  0.0421  611 HOH A O   
4626 O  O   . HOH K .   ? 1.0758 0.1641 1.7591 0.0520  -0.2536 0.0137  612 HOH A O   
4627 O  O   . HOH K .   ? 0.5841 1.1964 0.4451 -0.0922 0.0390  -0.0852 613 HOH A O   
4628 O  O   . HOH K .   ? 0.4528 0.2693 0.2630 -0.0483 0.0031  -0.0366 614 HOH A O   
4629 O  O   . HOH K .   ? 0.2739 0.2576 0.5546 0.0103  0.1098  -0.0040 615 HOH A O   
4630 O  O   . HOH K .   ? 0.4787 0.3027 0.2549 -0.1359 -0.1554 -0.0103 616 HOH A O   
4631 O  O   . HOH K .   ? 0.1701 0.1076 0.1738 0.0094  -0.0315 -0.0070 617 HOH A O   
4632 O  O   . HOH K .   ? 0.5299 0.6241 0.6729 -0.2655 0.1384  -0.4347 618 HOH A O   
4633 O  O   . HOH K .   ? 0.3844 0.5490 0.5702 -0.1118 -0.0834 0.1860  619 HOH A O   
4634 O  O   . HOH K .   ? 0.5436 0.2770 1.0753 0.0088  0.2326  0.0116  620 HOH A O   
4635 O  O   . HOH K .   ? 0.3865 0.2759 0.3495 -0.0515 -0.1366 0.0617  621 HOH A O   
4636 O  O   . HOH K .   ? 0.4559 0.3282 0.3759 -0.0747 0.0529  -0.0560 622 HOH A O   
4637 O  O   . HOH K .   ? 0.3203 0.3411 0.3844 -0.0335 0.1686  0.0907  623 HOH A O   
4638 O  O   . HOH K .   ? 0.5626 0.1808 0.3519 0.0258  0.0658  -0.0724 624 HOH A O   
4639 O  O   . HOH K .   ? 0.3921 0.4244 0.5490 -0.0491 0.1446  0.1673  625 HOH A O   
4640 O  O   . HOH K .   ? 0.2383 0.1092 0.1853 -0.0062 -0.0174 0.0017  626 HOH A O   
4641 O  O   . HOH K .   ? 0.2856 0.3418 0.6456 -0.1332 -0.1730 0.1454  627 HOH A O   
4642 O  O   . HOH K .   ? 0.3237 0.1947 0.3605 -0.0573 -0.1899 0.0328  628 HOH A O   
4643 O  O   . HOH K .   ? 0.2768 0.2648 0.2739 -0.0083 -0.0273 -0.0210 629 HOH A O   
4644 O  O   . HOH K .   ? 0.6044 0.4501 0.4099 -0.0509 0.2612  -0.1050 630 HOH A O   
4645 O  O   . HOH K .   ? 0.3152 0.9366 0.3948 -0.1422 -0.0900 -0.0614 631 HOH A O   
4646 O  O   . HOH K .   ? 0.3553 0.7777 0.4101 0.1915  -0.0773 -0.1986 632 HOH A O   
4647 O  O   . HOH K .   ? 0.2436 1.4399 1.7798 -0.2407 0.1310  -0.8719 633 HOH A O   
4648 O  O   . HOH K .   ? 0.4420 1.0502 2.6057 0.5772  -0.9781 -1.1022 634 HOH A O   
4649 O  O   . HOH K .   ? 0.3587 0.2922 0.3711 -0.1133 -0.1266 0.0074  635 HOH A O   
4650 O  O   . HOH K .   ? 0.2346 0.2504 0.4063 -0.0043 -0.0876 -0.0283 636 HOH A O   
4651 O  O   . HOH K .   ? 0.3711 0.3411 0.2400 0.1067  0.0085  -0.0197 637 HOH A O   
4652 O  O   . HOH K .   ? 0.5080 0.2739 0.1821 0.0932  0.0310  0.0784  638 HOH A O   
4653 O  O   . HOH K .   ? 0.2745 0.3154 0.3531 0.1041  -0.0271 0.0333  639 HOH A O   
4654 O  O   . HOH K .   ? 0.2614 0.4187 0.2526 0.0065  0.0824  0.0454  640 HOH A O   
4655 O  O   . HOH K .   ? 0.2222 1.3062 0.6119 0.0921  0.1319  0.1895  641 HOH A O   
4656 O  O   . HOH K .   ? 0.4487 0.2790 0.2702 -0.1198 -0.0264 0.0657  642 HOH A O   
4657 O  O   . HOH K .   ? 0.4844 0.3452 0.4686 -0.0938 -0.0754 -0.1336 643 HOH A O   
4658 O  O   . HOH K .   ? 0.2978 0.5357 0.2437 -0.0228 0.0046  -0.0828 644 HOH A O   
4659 O  O   . HOH K .   ? 0.6043 0.5479 0.2915 0.0920  0.0218  0.1419  645 HOH A O   
4660 O  O   . HOH K .   ? 0.3662 0.2858 0.2134 -0.0674 0.0308  0.0515  646 HOH A O   
4661 O  O   . HOH K .   ? 0.5325 0.3147 0.3080 0.1168  -0.1836 -0.0137 647 HOH A O   
4662 O  O   . HOH K .   ? 0.5436 0.5297 0.5386 -0.2398 0.0219  -0.1150 648 HOH A O   
4663 O  O   . HOH K .   ? 0.2275 0.2639 0.5633 0.0658  0.0878  0.1005  649 HOH A O   
4664 O  O   . HOH K .   ? 0.3621 0.3831 0.5127 -0.0746 -0.0562 0.0399  650 HOH A O   
4665 O  O   . HOH K .   ? 0.3882 0.2942 0.4693 -0.0041 -0.0254 -0.0662 651 HOH A O   
4666 O  O   . HOH K .   ? 0.4700 0.2190 0.3605 -0.0256 -0.1041 -0.0076 652 HOH A O   
4667 O  O   . HOH K .   ? 0.6991 0.2870 0.4975 -0.1824 -0.1162 0.0688  653 HOH A O   
4668 O  O   . HOH K .   ? 0.4733 0.2590 0.3948 0.0447  0.1665  0.1225  654 HOH A O   
4669 O  O   . HOH K .   ? 0.6155 0.5436 0.2603 0.0105  -0.0537 -0.0684 655 HOH A O   
4670 O  O   . HOH K .   ? 0.7113 0.2653 0.4386 -0.0228 -0.0627 -0.0817 656 HOH A O   
4671 O  O   . HOH K .   ? 0.7505 0.2084 0.5018 0.0261  -0.1694 -0.0493 657 HOH A O   
4672 O  O   . HOH K .   ? 0.6639 0.3544 0.2975 0.0017  -0.0254 0.1438  658 HOH A O   
4673 O  O   . HOH K .   ? 0.2073 0.1987 0.2105 -0.0245 -0.0474 -0.0214 659 HOH A O   
4674 O  O   . HOH K .   ? 0.3016 0.2707 0.3767 -0.0329 -0.0388 0.1465  660 HOH A O   
4675 O  O   . HOH K .   ? 0.5455 0.2800 0.3853 0.1142  0.0207  0.0702  661 HOH A O   
4676 O  O   . HOH K .   ? 0.4137 0.2044 0.5672 -0.0434 0.1326  -0.0979 662 HOH A O   
4677 O  O   . HOH K .   ? 0.3495 0.9599 1.0494 0.2887  0.1042  -0.2049 663 HOH A O   
4678 O  O   . HOH K .   ? 0.6815 0.2980 0.3271 -0.0604 0.0847  0.0373  664 HOH A O   
4679 O  O   . HOH K .   ? 0.2264 0.2621 0.2813 -0.0077 -0.0024 -0.0118 665 HOH A O   
4680 O  O   . HOH K .   ? 0.2883 0.1292 0.3860 0.0094  0.1172  0.0141  666 HOH A O   
4681 O  O   . HOH K .   ? 0.4158 0.6129 0.8152 0.0081  -0.3594 0.1985  667 HOH A O   
4682 O  O   . HOH K .   ? 0.2155 0.1671 0.2597 -0.0425 -0.0232 0.0344  668 HOH A O   
4683 O  O   . HOH K .   ? 0.2651 0.3776 0.5539 -0.0416 0.0675  -0.0006 669 HOH A O   
4684 O  O   . HOH K .   ? 0.3993 0.4503 0.2973 -0.0216 -0.0071 -0.0373 670 HOH A O   
4685 O  O   . HOH K .   ? 0.5936 0.4120 0.6312 0.0568  0.0579  0.2899  671 HOH A O   
4686 O  O   . HOH K .   ? 0.2443 0.3224 0.5447 0.1085  -0.0270 0.0772  672 HOH A O   
4687 O  O   . HOH K .   ? 0.3650 0.3975 0.4905 0.0419  -0.0410 -0.0878 673 HOH A O   
4688 O  O   . HOH L .   ? 0.2845 0.3713 0.3519 -0.0133 0.0557  -0.0127 401 HOH B O   
4689 O  O   . HOH L .   ? 0.3411 0.3600 0.5153 0.0077  -0.1834 0.0755  402 HOH B O   
4690 O  O   . HOH L .   ? 0.3131 0.1680 0.4623 -0.0204 -0.1005 0.0104  403 HOH B O   
4691 O  O   . HOH L .   ? 0.3776 0.4350 0.2217 -0.0297 0.0441  0.0285  404 HOH B O   
4692 O  O   . HOH L .   ? 0.5153 0.3501 0.3630 -0.0196 -0.0615 0.0126  405 HOH B O   
4693 O  O   . HOH L .   ? 1.1488 0.3231 0.3510 -0.2588 0.3014  -0.0794 406 HOH B O   
4694 O  O   . HOH L .   ? 0.3389 0.5967 0.7116 -0.1545 0.0469  0.1404  407 HOH B O   
4695 O  O   . HOH L .   ? 0.4480 0.2348 0.3549 0.0992  -0.0610 -0.0355 408 HOH B O   
4696 O  O   . HOH L .   ? 0.3395 0.3163 0.4128 0.0175  0.1376  0.0597  409 HOH B O   
4697 O  O   . HOH L .   ? 0.3619 0.3023 0.2705 0.0093  0.0571  0.0789  410 HOH B O   
4698 O  O   . HOH L .   ? 0.6520 0.3070 0.7718 0.1212  0.4431  -0.0263 411 HOH B O   
4699 O  O   . HOH L .   ? 0.3235 0.1463 0.2087 -0.0278 -0.0137 -0.0040 412 HOH B O   
4700 O  O   . HOH L .   ? 0.5133 0.2063 0.5203 0.0573  0.0582  0.0847  413 HOH B O   
4701 O  O   . HOH L .   ? 0.4679 0.4616 0.3529 -0.0636 0.1419  -0.0970 414 HOH B O   
4702 O  O   . HOH L .   ? 1.0821 1.6471 0.0539 -0.3006 0.1164  -0.1886 415 HOH B O   
4703 O  O   . HOH L .   ? 0.4307 0.1421 0.1867 0.0364  -0.1634 -0.0027 416 HOH B O   
4704 O  O   . HOH L .   ? 0.4607 0.4835 0.4526 -0.0296 0.0608  -0.0581 417 HOH B O   
4705 O  O   . HOH L .   ? 0.4187 0.2458 0.4535 -0.1665 -0.0188 0.0361  418 HOH B O   
4706 O  O   . HOH L .   ? 0.3212 0.4381 0.3361 0.1283  0.1076  -0.0303 419 HOH B O   
4707 O  O   . HOH L .   ? 0.3574 0.4959 0.8156 -0.0478 -0.2056 0.0357  420 HOH B O   
4708 O  O   . HOH L .   ? 0.2205 0.2096 0.3528 0.0087  0.0119  -0.0006 421 HOH B O   
4709 O  O   . HOH L .   ? 0.2901 0.3912 0.2928 -0.0628 0.0820  -0.1826 422 HOH B O   
4710 O  O   . HOH L .   ? 0.1962 0.2439 0.4945 -0.0277 -0.0322 0.0670  423 HOH B O   
4711 O  O   . HOH L .   ? 0.2881 0.1323 0.2193 -0.0298 -0.0013 0.0054  424 HOH B O   
4712 O  O   . HOH L .   ? 0.3569 0.2640 0.3255 -0.0886 0.1306  -0.1055 425 HOH B O   
4713 O  O   . HOH L .   ? 0.1227 0.1155 0.1307 -0.0161 0.0164  -0.0204 426 HOH B O   
4714 O  O   . HOH L .   ? 0.4666 0.2743 0.5052 -0.0392 0.0233  -0.0627 427 HOH B O   
4715 O  O   . HOH L .   ? 1.8698 0.7210 0.5619 -0.0274 -0.1036 -0.0151 428 HOH B O   
4716 O  O   . HOH L .   ? 0.3925 0.7084 0.2233 0.1052  -0.0671 -0.1612 429 HOH B O   
4717 O  O   . HOH L .   ? 0.4056 1.4033 1.4663 0.0263  0.0055  0.1884  430 HOH B O   
4718 O  O   . HOH L .   ? 0.2047 0.2197 0.2716 0.0026  0.0000  0.0148  431 HOH B O   
4719 O  O   . HOH L .   ? 0.2005 0.1189 0.0741 -0.0353 -0.0183 0.0060  432 HOH B O   
4720 O  O   . HOH L .   ? 0.4602 0.2815 0.1300 -0.0068 -0.0295 0.0024  433 HOH B O   
4721 O  O   . HOH L .   ? 0.2578 0.2858 0.2515 -0.0173 0.0621  0.0546  434 HOH B O   
4722 O  O   . HOH L .   ? 0.2265 0.5975 0.5314 -0.0355 -0.1181 0.1323  435 HOH B O   
4723 O  O   . HOH L .   ? 0.1973 0.2072 0.2111 0.0151  -0.0379 -0.0007 436 HOH B O   
4724 O  O   . HOH L .   ? 0.2655 0.3948 0.2549 0.0430  -0.0027 0.0126  437 HOH B O   
4725 O  O   . HOH L .   ? 0.4016 0.4465 0.2587 -0.0531 -0.0516 0.0998  438 HOH B O   
4726 O  O   . HOH L .   ? 0.2411 0.2833 0.3937 -0.0679 0.0254  -0.0307 439 HOH B O   
4727 O  O   . HOH L .   ? 0.4980 0.2437 0.5422 0.0798  0.0270  0.0196  440 HOH B O   
4728 O  O   . HOH L .   ? 0.5611 0.2730 0.1995 0.0046  0.0590  -0.0803 441 HOH B O   
4729 O  O   . HOH L .   ? 0.5390 0.4273 0.2732 0.0189  -0.0579 -0.0098 442 HOH B O   
4730 O  O   . HOH L .   ? 0.2477 0.3754 0.5990 0.0031  0.1733  0.0291  443 HOH B O   
4731 O  O   . HOH L .   ? 0.8907 0.5188 2.4393 -0.1053 -0.8386 -0.3540 444 HOH B O   
4732 O  O   . HOH L .   ? 0.4984 0.2565 0.2703 -0.1079 0.0930  0.0043  445 HOH B O   
4733 O  O   . HOH L .   ? 0.1386 0.1033 0.1209 -0.0063 0.0142  -0.0099 446 HOH B O   
4734 O  O   . HOH L .   ? 0.3574 0.4711 0.3208 0.0052  0.0311  0.1957  447 HOH B O   
4735 O  O   . HOH L .   ? 1.3080 1.3388 0.3804 0.7465  -0.1661 -0.1606 448 HOH B O   
4736 O  O   . HOH L .   ? 0.4336 0.3910 0.4907 -0.1130 0.1517  -0.0342 449 HOH B O   
4737 O  O   . HOH L .   ? 0.6536 0.2138 0.1680 -0.0989 -0.0142 0.0681  450 HOH B O   
4738 O  O   . HOH L .   ? 0.3497 0.1958 0.3093 -0.0800 -0.0998 0.0394  451 HOH B O   
4739 O  O   . HOH L .   ? 0.4553 0.5024 0.2793 0.1777  -0.0747 0.0868  452 HOH B O   
4740 O  O   . HOH L .   ? 0.2901 0.6765 0.4566 -0.1035 -0.0040 0.3323  453 HOH B O   
4741 O  O   . HOH L .   ? 0.4307 0.2502 0.1964 -0.1089 0.1238  -0.0731 454 HOH B O   
4742 O  O   . HOH L .   ? 0.3152 0.1905 0.2269 -0.0829 -0.0518 -0.0151 455 HOH B O   
4743 O  O   . HOH L .   ? 0.2119 0.2109 0.3118 0.0066  -0.1458 -0.0617 456 HOH B O   
4744 O  O   . HOH L .   ? 0.3427 0.6955 0.5077 0.2071  0.1372  -0.0505 457 HOH B O   
4745 O  O   . HOH L .   ? 0.2628 0.2387 0.1782 -0.0088 -0.0311 0.0130  458 HOH B O   
4746 O  O   . HOH L .   ? 0.5985 0.2833 0.1335 -0.0414 -0.0346 -0.0370 459 HOH B O   
4747 O  O   . HOH L .   ? 0.2949 0.1811 0.2509 0.0046  0.0007  0.0412  460 HOH B O   
4748 O  O   . HOH L .   ? 0.1269 0.1495 0.1240 0.0024  -0.0234 0.0155  461 HOH B O   
4749 O  O   . HOH L .   ? 0.1638 0.1077 0.1326 -0.0144 0.0054  -0.0149 462 HOH B O   
4750 O  O   . HOH L .   ? 0.2143 0.1879 0.2736 0.0021  0.0322  -0.0013 463 HOH B O   
4751 O  O   . HOH L .   ? 0.2820 0.3684 0.4832 0.1305  0.1480  0.1253  464 HOH B O   
4752 O  O   . HOH L .   ? 0.2089 0.4140 0.3504 -0.1092 -0.0296 -0.0719 465 HOH B O   
4753 O  O   . HOH L .   ? 0.3217 0.1939 0.2358 0.0111  -0.0662 0.0108  466 HOH B O   
4754 O  O   . HOH L .   ? 0.3792 0.2427 0.3497 0.0342  0.1333  -0.0239 467 HOH B O   
4755 O  O   . HOH L .   ? 0.3102 0.3515 0.2992 -0.0073 -0.0159 -0.0617 468 HOH B O   
4756 O  O   . HOH L .   ? 0.1324 0.3018 0.3610 -0.0401 -0.0614 0.0756  469 HOH B O   
4757 O  O   . HOH L .   ? 0.1719 0.2694 0.4474 0.0568  -0.0129 0.0619  470 HOH B O   
4758 O  O   . HOH L .   ? 0.2558 0.2450 0.3440 -0.0439 -0.0829 -0.0046 471 HOH B O   
4759 O  O   . HOH L .   ? 0.5776 0.3052 0.4158 0.0837  0.0211  -0.0851 472 HOH B O   
4760 O  O   . HOH L .   ? 0.2368 0.1820 0.1730 -0.0120 0.0388  0.0275  473 HOH B O   
4761 O  O   . HOH L .   ? 1.8273 0.3303 0.3267 -0.2117 -0.0087 -0.1600 474 HOH B O   
4762 O  O   . HOH L .   ? 0.2425 0.1768 0.2360 -0.0044 -0.0277 -0.0282 475 HOH B O   
4763 O  O   . HOH L .   ? 0.2405 0.4146 0.3826 0.0159  -0.0273 -0.1816 476 HOH B O   
4764 O  O   . HOH L .   ? 0.3892 0.2073 0.3589 -0.0824 0.0505  -0.0864 477 HOH B O   
4765 O  O   . HOH L .   ? 0.2201 0.2712 0.1935 -0.0335 -0.0170 -0.0702 478 HOH B O   
4766 O  O   . HOH L .   ? 0.1124 0.1265 0.1118 0.0250  -0.0037 -0.0040 479 HOH B O   
4767 O  O   . HOH L .   ? 0.1614 0.5170 0.3488 -0.0370 0.0226  0.0769  480 HOH B O   
4768 O  O   . HOH L .   ? 0.2150 0.2088 0.2080 -0.0248 -0.0702 0.0242  481 HOH B O   
4769 O  O   . HOH L .   ? 0.2736 0.3646 0.3774 -0.0615 0.1045  0.0253  482 HOH B O   
4770 O  O   . HOH L .   ? 0.4496 0.2053 0.3027 0.1323  -0.1295 -0.0584 483 HOH B O   
4771 O  O   . HOH L .   ? 0.6854 0.2275 0.1656 0.0432  0.0231  0.0282  484 HOH B O   
4772 O  O   . HOH L .   ? 0.2196 0.2076 0.3564 0.0174  0.0649  0.0800  485 HOH B O   
4773 O  O   . HOH L .   ? 0.1093 0.1067 0.1225 -0.0140 0.0021  0.0000  486 HOH B O   
4774 O  O   . HOH L .   ? 0.3781 0.3219 0.2210 -0.1358 0.0129  -0.1018 487 HOH B O   
4775 O  O   . HOH L .   ? 0.2461 0.3221 0.2285 0.0226  0.0855  -0.0267 488 HOH B O   
4776 O  O   . HOH L .   ? 0.1166 0.0957 0.1141 0.0076  -0.0062 -0.0092 489 HOH B O   
4777 O  O   . HOH L .   ? 0.2948 1.2266 0.6527 0.1994  -0.0005 -0.5411 490 HOH B O   
4778 O  O   . HOH L .   ? 0.2187 0.1360 0.1530 -0.0248 -0.0174 0.0188  491 HOH B O   
4779 O  O   . HOH L .   ? 0.1982 0.2011 0.2901 0.0127  0.0059  0.0469  492 HOH B O   
4780 O  O   . HOH L .   ? 0.4390 0.2476 0.2426 -0.0516 0.1341  -0.0851 493 HOH B O   
4781 O  O   . HOH L .   ? 0.0806 0.1582 0.2164 0.0003  -0.0165 -0.0416 494 HOH B O   
4782 O  O   . HOH L .   ? 0.2700 0.1942 0.1806 0.0041  0.0694  -0.0256 495 HOH B O   
4783 O  O   . HOH L .   ? 0.1509 0.3666 0.2511 -0.0083 -0.0185 0.1184  496 HOH B O   
4784 O  O   . HOH L .   ? 0.3228 0.6599 0.3564 -0.0364 0.1378  0.0631  497 HOH B O   
4785 O  O   . HOH L .   ? 0.2676 0.6074 0.6431 -0.0439 0.1808  0.1209  498 HOH B O   
4786 O  O   . HOH L .   ? 0.1524 0.1585 0.3449 -0.0337 -0.0627 0.0212  499 HOH B O   
4787 O  O   . HOH L .   ? 0.3050 0.4997 0.1895 -0.0463 -0.1026 0.1039  500 HOH B O   
4788 O  O   . HOH L .   ? 0.2703 0.1897 0.1939 -0.0164 -0.0817 -0.0003 501 HOH B O   
4789 O  O   . HOH L .   ? 0.2159 0.1238 0.1818 -0.0351 -0.0249 0.0010  502 HOH B O   
4790 O  O   . HOH L .   ? 0.2477 0.2196 0.1891 0.0252  -0.0076 0.0245  503 HOH B O   
4791 O  O   . HOH L .   ? 0.1984 0.3186 0.2254 -0.0173 -0.0557 -0.0088 504 HOH B O   
4792 O  O   . HOH L .   ? 0.5378 0.3177 0.3497 -0.0003 0.0197  -0.0604 505 HOH B O   
4793 O  O   . HOH L .   ? 0.1332 0.1199 0.1562 0.0201  -0.0174 0.0160  506 HOH B O   
4794 O  O   . HOH L .   ? 0.1773 0.1277 0.1762 0.0231  0.0153  0.0119  507 HOH B O   
4795 O  O   . HOH L .   ? 0.2962 0.3395 0.3337 0.0326  -0.0452 0.0553  508 HOH B O   
4796 O  O   . HOH L .   ? 0.1448 0.1801 0.1941 0.0303  -0.0218 0.0197  509 HOH B O   
4797 O  O   . HOH L .   ? 0.3634 0.2169 0.2246 -0.0359 -0.0083 -0.0210 510 HOH B O   
4798 O  O   . HOH L .   ? 0.5134 0.5892 0.1834 -0.0829 0.0293  0.0832  511 HOH B O   
4799 O  O   . HOH L .   ? 0.2153 0.1379 0.1845 -0.0012 -0.0553 -0.0054 512 HOH B O   
4800 O  O   . HOH L .   ? 0.3167 0.1761 0.2730 0.0116  -0.1250 -0.0474 513 HOH B O   
4801 O  O   . HOH L .   ? 0.2879 0.4232 0.3190 -0.0727 -0.1391 0.0388  514 HOH B O   
4802 O  O   . HOH L .   ? 0.2551 0.2840 0.1967 -0.0601 0.0383  -0.0283 515 HOH B O   
4803 O  O   . HOH L .   ? 0.2536 0.6735 0.4731 -0.1749 0.0810  -0.1105 516 HOH B O   
4804 O  O   . HOH L .   ? 0.3226 0.1753 0.3186 -0.0181 -0.0688 -0.0277 517 HOH B O   
4805 O  O   . HOH L .   ? 0.2845 0.1838 0.2082 0.0507  0.0612  0.0917  518 HOH B O   
4806 O  O   . HOH L .   ? 0.2985 0.1278 0.2046 0.0133  -0.0763 -0.0035 519 HOH B O   
4807 O  O   . HOH L .   ? 0.3946 0.1565 0.1738 -0.0077 -0.1238 0.0160  520 HOH B O   
4808 O  O   . HOH L .   ? 0.3366 2.0437 0.3926 -0.2319 0.2754  0.2727  521 HOH B O   
4809 O  O   . HOH L .   ? 0.3160 0.1590 0.1791 -0.0131 -0.0216 -0.0303 522 HOH B O   
4810 O  O   . HOH L .   ? 0.3016 0.1674 0.1975 0.0162  -0.0483 -0.0160 523 HOH B O   
4811 O  O   . HOH L .   ? 0.2389 0.2034 0.3021 -0.0143 0.0222  -0.0690 524 HOH B O   
4812 O  O   . HOH L .   ? 0.4449 0.2560 0.2242 0.0729  0.0127  0.0351  525 HOH B O   
4813 O  O   . HOH L .   ? 0.2791 0.2639 0.6212 -0.1319 -0.0509 0.0830  526 HOH B O   
4814 O  O   . HOH L .   ? 0.1497 0.1729 0.2520 -0.0010 -0.0059 0.0170  527 HOH B O   
4815 O  O   . HOH L .   ? 0.5832 0.2903 0.5917 0.0549  -0.3454 -0.0709 528 HOH B O   
4816 O  O   . HOH L .   ? 0.6162 0.4577 0.3382 0.0127  0.0636  -0.0161 529 HOH B O   
4817 O  O   . HOH L .   ? 0.2061 0.1485 0.2603 0.0236  0.0027  -0.0335 530 HOH B O   
4818 O  O   . HOH L .   ? 0.2380 0.1480 0.1888 0.0000  -0.0357 0.0154  531 HOH B O   
4819 O  O   . HOH L .   ? 0.2576 0.2167 0.1474 0.0125  -0.0197 -0.0109 532 HOH B O   
4820 O  O   . HOH L .   ? 0.3226 0.2140 0.6603 -0.0483 -0.1221 0.0921  533 HOH B O   
4821 O  O   . HOH L .   ? 0.2477 0.5762 0.2815 -0.0392 -0.0564 0.1286  534 HOH B O   
4822 O  O   . HOH L .   ? 0.5494 0.2712 0.2145 -0.0509 -0.0575 -0.0868 535 HOH B O   
4823 O  O   . HOH L .   ? 0.2588 0.2603 0.2942 0.0829  0.0584  0.0083  536 HOH B O   
4824 O  O   . HOH L .   ? 0.1976 0.6984 0.3935 0.0249  0.0454  -0.0126 537 HOH B O   
4825 O  O   . HOH L .   ? 0.3264 0.2199 0.2070 0.0335  0.0007  -0.0109 538 HOH B O   
4826 O  O   . HOH L .   ? 0.2484 0.1333 0.1580 0.0137  -0.0116 0.0144  539 HOH B O   
4827 O  O   . HOH L .   ? 0.4176 0.3255 0.3269 -0.1159 -0.0178 -0.0485 540 HOH B O   
4828 O  O   . HOH L .   ? 0.6079 0.3686 0.3030 -0.1237 0.1325  -0.0212 541 HOH B O   
4829 O  O   . HOH L .   ? 0.8088 0.6245 0.6044 -0.0186 -0.0126 0.1753  542 HOH B O   
4830 O  O   . HOH L .   ? 0.2930 0.2182 0.3765 -0.0124 0.0353  -0.1120 543 HOH B O   
4831 O  O   . HOH L .   ? 0.1719 0.3386 0.4476 0.0478  0.0482  0.0935  544 HOH B O   
4832 O  O   . HOH L .   ? 0.1591 0.1450 0.2476 -0.0151 0.0147  0.0032  545 HOH B O   
4833 O  O   . HOH L .   ? 0.6383 0.2475 0.3490 0.0302  -0.0147 -0.0957 546 HOH B O   
4834 O  O   . HOH L .   ? 0.0854 0.2230 0.2398 0.0015  0.0195  -0.0518 547 HOH B O   
4835 O  O   . HOH L .   ? 0.2096 0.2491 0.2865 -0.0342 0.0040  0.0175  548 HOH B O   
4836 O  O   . HOH L .   ? 0.9789 0.3404 0.8021 0.3984  -0.2926 -0.4417 549 HOH B O   
4837 O  O   . HOH L .   ? 0.4708 0.3285 0.2099 0.2318  -0.0728 -0.0027 550 HOH B O   
4838 O  O   . HOH L .   ? 0.1300 0.3474 0.4715 0.0126  -0.0571 0.1385  551 HOH B O   
4839 O  O   . HOH L .   ? 0.5311 0.3903 0.3151 -0.0597 -0.1124 -0.1421 552 HOH B O   
4840 O  O   . HOH L .   ? 0.2208 0.1797 0.3063 -0.0923 -0.0300 -0.0472 553 HOH B O   
4841 O  O   . HOH L .   ? 0.3305 0.2283 0.1836 0.0194  -0.0226 0.0328  554 HOH B O   
4842 O  O   . HOH L .   ? 0.2339 0.1879 0.2421 -0.0192 -0.0329 -0.0753 555 HOH B O   
4843 O  O   . HOH L .   ? 0.3188 0.4271 0.3603 0.0359  -0.0650 -0.0905 556 HOH B O   
4844 O  O   . HOH L .   ? 0.3573 0.1685 0.2655 0.0023  -0.0788 -0.0277 557 HOH B O   
4845 O  O   . HOH L .   ? 0.3440 1.5769 1.1612 0.0320  -0.1084 -0.1534 558 HOH B O   
4846 O  O   . HOH L .   ? 0.2944 0.3170 0.7965 -0.0927 -0.0456 0.2973  559 HOH B O   
4847 O  O   . HOH L .   ? 0.1448 0.2347 0.1590 -0.0214 -0.0568 0.0582  560 HOH B O   
4848 O  O   . HOH L .   ? 0.2804 0.3456 0.3249 0.0706  0.0109  -0.0904 561 HOH B O   
4849 O  O   . HOH L .   ? 0.1755 0.2134 0.2433 -0.0088 -0.0107 -0.0198 562 HOH B O   
4850 O  O   . HOH L .   ? 0.2142 0.2132 0.3630 0.0878  -0.0237 -0.0482 563 HOH B O   
4851 O  O   . HOH L .   ? 0.3705 0.6359 0.5554 -0.0566 0.1879  -0.1063 564 HOH B O   
4852 O  O   . HOH L .   ? 0.2376 0.2433 0.1972 0.0403  0.0074  0.0666  565 HOH B O   
4853 O  O   . HOH L .   ? 0.3759 0.2569 0.2328 0.0855  0.0659  0.0458  566 HOH B O   
4854 O  O   . HOH L .   ? 0.5162 0.2560 0.4919 0.0794  -0.0632 0.0392  567 HOH B O   
4855 O  O   . HOH L .   ? 0.4034 0.1914 0.2621 0.0755  -0.0299 -0.0505 568 HOH B O   
4856 O  O   . HOH L .   ? 0.8305 0.4347 0.5464 0.2439  0.3208  0.2518  569 HOH B O   
4857 O  O   . HOH L .   ? 0.1914 0.1784 0.6297 0.0160  0.0285  -0.0957 570 HOH B O   
4858 O  O   . HOH L .   ? 0.4860 0.1967 0.2264 -0.1196 -0.1298 0.0153  571 HOH B O   
4859 O  O   . HOH L .   ? 0.1388 0.1553 0.3219 -0.0151 -0.0085 0.0055  572 HOH B O   
4860 O  O   . HOH L .   ? 0.2980 0.4648 0.4347 0.0551  -0.1013 -0.1009 573 HOH B O   
4861 O  O   . HOH L .   ? 0.1336 0.1039 0.1474 0.0131  -0.0125 -0.0048 574 HOH B O   
4862 O  O   . HOH L .   ? 0.3560 0.2545 0.2924 -0.0711 -0.0500 -0.0491 575 HOH B O   
4863 O  O   . HOH L .   ? 0.2802 0.3925 0.3420 0.1124  0.0342  0.0582  576 HOH B O   
4864 O  O   . HOH L .   ? 0.4147 0.3905 0.1615 0.0625  -0.0443 0.0172  577 HOH B O   
4865 O  O   . HOH L .   ? 0.4122 0.4436 0.5978 0.2494  -0.0163 0.0362  578 HOH B O   
4866 O  O   . HOH L .   ? 0.4410 0.1591 0.2901 0.0649  0.0304  0.0447  579 HOH B O   
4867 O  O   . HOH L .   ? 0.3151 0.2276 0.1835 0.0718  0.0232  -0.0228 580 HOH B O   
4868 O  O   . HOH L .   ? 0.2477 0.5236 0.4052 -0.0913 -0.0127 0.0205  581 HOH B O   
4869 O  O   . HOH L .   ? 0.1941 0.3075 0.3274 0.0778  -0.1000 -0.0666 582 HOH B O   
4870 O  O   . HOH L .   ? 0.2991 0.5845 0.4853 0.1741  0.0469  0.1896  583 HOH B O   
4871 O  O   . HOH L .   ? 0.2606 0.2021 0.4332 0.0577  0.0500  0.0307  584 HOH B O   
4872 O  O   . HOH L .   ? 0.3759 0.6335 0.3037 0.2028  0.0388  0.1404  585 HOH B O   
4873 O  O   . HOH L .   ? 0.3695 0.3048 0.1970 -0.0803 -0.0645 -0.0020 586 HOH B O   
4874 O  O   . HOH L .   ? 0.3332 0.4167 0.5489 -0.0984 0.0689  0.0575  587 HOH B O   
4875 O  O   . HOH L .   ? 0.3510 0.2062 0.2802 0.0024  -0.0340 0.0197  588 HOH B O   
4876 O  O   . HOH L .   ? 0.4695 0.3806 0.7433 -0.1240 -0.0085 -0.0518 589 HOH B O   
4877 O  O   . HOH L .   ? 0.3179 0.2266 0.2554 0.0856  0.0375  0.0175  590 HOH B O   
4878 O  O   . HOH L .   ? 0.3723 0.4339 0.2143 0.0141  0.0344  0.1777  591 HOH B O   
4879 O  O   . HOH L .   ? 0.3574 0.3517 0.3882 0.1403  0.0811  0.1351  592 HOH B O   
4880 O  O   . HOH L .   ? 0.3420 0.4022 0.4162 0.1332  0.1509  0.1854  593 HOH B O   
4881 O  O   . HOH L .   ? 0.4183 0.4749 0.2960 0.0322  -0.0151 0.0952  594 HOH B O   
4882 O  O   . HOH L .   ? 0.4740 0.1366 0.2000 -0.0313 -0.1820 -0.0052 595 HOH B O   
4883 O  O   . HOH L .   ? 0.3537 0.4287 0.3027 -0.0097 -0.0175 0.0346  596 HOH B O   
4884 O  O   . HOH L .   ? 0.3697 0.3273 2.0078 -0.2208 0.2354  0.3190  597 HOH B O   
4885 O  O   . HOH L .   ? 1.3228 0.0962 1.5809 -0.1290 0.5044  0.1020  598 HOH B O   
4886 O  O   . HOH L .   ? 0.3693 0.3125 0.3348 0.1376  -0.0142 -0.0449 599 HOH B O   
4887 O  O   . HOH L .   ? 0.6104 0.2818 0.2962 -0.0825 0.1570  0.0882  600 HOH B O   
4888 O  O   . HOH L .   ? 0.6046 0.2526 0.2461 0.0873  -0.0076 0.0189  601 HOH B O   
4889 O  O   . HOH L .   ? 0.2601 0.5081 0.3215 -0.0153 0.0340  0.0054  602 HOH B O   
4890 O  O   . HOH L .   ? 1.7280 1.2749 0.8726 -0.9038 0.5855  -0.3145 603 HOH B O   
4891 O  O   . HOH L .   ? 0.1710 0.1155 0.1660 -0.0068 -0.0366 -0.0076 604 HOH B O   
4892 O  O   . HOH L .   ? 0.5137 0.4539 0.5626 0.0776  -0.0381 0.1937  605 HOH B O   
4893 O  O   . HOH L .   ? 0.3831 0.8481 0.4986 -0.2739 -0.1156 0.1719  606 HOH B O   
4894 O  O   . HOH L .   ? 0.3707 0.2861 0.2825 -0.0212 -0.0797 0.0041  607 HOH B O   
4895 O  O   . HOH L .   ? 0.3244 0.3477 0.7073 -0.0991 -0.1748 0.1149  608 HOH B O   
4896 O  O   . HOH L .   ? 0.4456 0.4819 0.5098 -0.1532 -0.2240 0.1412  609 HOH B O   
4897 O  O   . HOH L .   ? 0.5286 0.9660 0.2913 0.2343  0.0454  0.0491  610 HOH B O   
4898 O  O   . HOH L .   ? 0.3147 0.4887 0.5309 -0.0838 0.0125  -0.0878 611 HOH B O   
4899 O  O   . HOH L .   ? 0.2380 0.1048 0.1888 -0.0019 -0.0083 -0.0091 612 HOH B O   
4900 O  O   . HOH L .   ? 0.3555 0.5500 0.5457 0.0288  0.1306  -0.2363 613 HOH B O   
4901 O  O   . HOH L .   ? 0.5669 0.6596 0.2587 0.1145  0.0241  -0.0509 614 HOH B O   
4902 O  O   . HOH L .   ? 0.3591 0.8691 0.9293 0.2216  0.2324  0.2123  615 HOH B O   
4903 O  O   . HOH L .   ? 0.5282 0.2689 0.1826 -0.1238 -0.0144 -0.0644 616 HOH B O   
4904 O  O   . HOH L .   ? 0.2444 0.7415 0.2836 0.1186  -0.0615 0.0694  617 HOH B O   
4905 O  O   . HOH L .   ? 0.3147 0.2021 0.3702 0.0630  -0.1947 -0.0577 618 HOH B O   
4906 O  O   . HOH L .   ? 0.2815 0.2648 0.2682 0.0104  -0.0160 0.0201  619 HOH B O   
4907 O  O   . HOH L .   ? 0.2991 0.7012 0.2669 0.0724  0.0307  0.0652  620 HOH B O   
4908 O  O   . HOH L .   ? 0.2982 0.3567 0.3957 0.0768  0.1315  -0.0511 621 HOH B O   
4909 O  O   . HOH L .   ? 0.3668 0.3233 0.2556 -0.1026 -0.0068 0.0423  622 HOH B O   
4910 O  O   . HOH L .   ? 0.5365 0.5232 0.3312 0.1295  0.0295  0.1295  623 HOH B O   
4911 O  O   . HOH L .   ? 0.2290 0.2635 0.3237 0.0357  -0.0756 -0.0406 624 HOH B O   
4912 O  O   . HOH L .   ? 0.3741 0.5110 0.6136 0.1547  0.0744  0.3014  625 HOH B O   
4913 O  O   . HOH L .   ? 0.2874 0.3395 0.2791 -0.1343 -0.0063 -0.0280 626 HOH B O   
4914 O  O   . HOH L .   ? 0.1803 0.2556 0.3777 0.0649  0.0974  0.0392  627 HOH B O   
4915 O  O   . HOH L .   ? 0.4226 0.8985 0.7335 -0.2775 -0.0127 0.3492  628 HOH B O   
4916 O  O   . HOH L .   ? 0.3479 0.3204 0.3565 0.1341  -0.1520 -0.0781 629 HOH B O   
4917 O  O   . HOH L .   ? 0.4248 0.6812 0.3648 0.1456  -0.0793 0.0373  630 HOH B O   
4918 O  O   . HOH L .   ? 0.2476 0.3332 0.2441 -0.0439 0.0593  -0.0412 631 HOH B O   
4919 O  O   . HOH L .   ? 0.2714 0.2962 0.5220 -0.0165 0.0186  0.1216  632 HOH B O   
4920 O  O   . HOH L .   ? 0.6503 0.6689 0.7207 0.4557  0.2806  0.3158  633 HOH B O   
4921 O  O   . HOH L .   ? 0.4966 0.5277 0.2969 -0.0028 0.0917  -0.1115 634 HOH B O   
4922 O  O   . HOH L .   ? 0.2155 0.1398 0.1915 -0.0078 -0.0209 -0.0012 635 HOH B O   
4923 O  O   . HOH L .   ? 0.4462 0.2646 0.1972 -0.0148 -0.0557 0.0324  636 HOH B O   
4924 O  O   . HOH L .   ? 1.0376 1.6170 0.4718 0.4543  -0.6411 -0.0511 637 HOH B O   
4925 O  O   . HOH L .   ? 0.2292 0.2707 0.5820 -0.0493 0.0671  -0.0918 638 HOH B O   
4926 O  O   . HOH L .   ? 0.3589 0.4894 0.2755 0.0640  -0.0087 0.0838  639 HOH B O   
4927 O  O   . HOH L .   ? 0.3508 0.5415 0.3296 0.0204  -0.0472 0.0905  640 HOH B O   
4928 O  O   . HOH L .   ? 0.5321 0.3740 0.2890 -0.1004 -0.1587 -0.0008 641 HOH B O   
4929 O  O   . HOH L .   ? 0.2763 0.4264 0.4738 0.0344  0.0394  0.1316  642 HOH B O   
4930 O  O   . HOH L .   ? 0.3750 0.3140 0.2219 0.0430  0.0264  -0.0806 643 HOH B O   
4931 O  O   . HOH L .   ? 0.4275 0.2592 0.5848 -0.0098 -0.0546 -0.0322 644 HOH B O   
4932 O  O   . HOH L .   ? 0.1937 0.1030 0.1709 -0.0207 -0.0152 -0.0021 645 HOH B O   
4933 O  O   . HOH L .   ? 0.4559 0.2939 0.3226 -0.0483 0.0989  -0.1193 646 HOH B O   
4934 O  O   . HOH L .   ? 0.6079 0.2354 0.3303 -0.0055 -0.0668 0.0430  647 HOH B O   
4935 O  O   . HOH L .   ? 0.3609 0.2533 0.4958 0.0175  -0.0026 0.0428  648 HOH B O   
4936 O  O   . HOH L .   ? 0.6047 0.3472 0.1811 0.1052  -0.0252 -0.0684 649 HOH B O   
4937 O  O   . HOH L .   ? 0.3806 0.2716 0.6179 -0.0063 0.1485  0.1316  650 HOH B O   
4938 O  O   . HOH L .   ? 0.2034 0.1837 0.2412 0.0284  -0.0493 0.0032  651 HOH B O   
4939 O  O   . HOH L .   ? 0.2806 0.3059 0.4095 0.0458  -0.0781 -0.1896 652 HOH B O   
4940 O  O   . HOH L .   ? 0.6916 0.2845 0.3506 -0.1626 0.0425  -0.0573 653 HOH B O   
4941 O  O   . HOH L .   ? 0.1984 0.3842 0.9571 -0.0676 -0.0922 -0.0188 654 HOH B O   
4942 O  O   . HOH L .   ? 0.5238 0.4652 1.3355 0.1377  -0.1538 0.2669  655 HOH B O   
4943 O  O   . HOH L .   ? 0.3837 0.3919 0.4605 0.0480  -0.1289 -0.0976 656 HOH B O   
4944 O  O   . HOH L .   ? 0.2187 0.2924 0.2504 0.0052  0.0055  0.0129  657 HOH B O   
4945 O  O   . HOH L .   ? 0.2955 0.1313 0.4339 -0.0239 0.1342  -0.0074 658 HOH B O   
4946 O  O   . HOH L .   ? 0.2348 0.4289 0.3975 -0.0379 0.0575  0.0292  659 HOH B O   
4947 O  O   . HOH L .   ? 0.3970 0.3754 0.3603 -0.0184 -0.0308 0.0588  660 HOH B O   
4948 O  O   . HOH L .   ? 0.3652 0.6080 0.6696 -0.1057 -0.1193 -0.0860 661 HOH B O   
4949 O  O   . HOH L .   ? 0.6632 0.2908 0.2820 0.0711  -0.1089 -0.0102 662 HOH B O   
4950 O  O   . HOH L .   ? 0.1949 0.3210 0.4890 -0.0661 -0.0286 -0.0864 663 HOH B O   
4951 O  O   . HOH L .   ? 0.4630 0.6668 0.4952 -0.1106 -0.0483 -0.0571 664 HOH B O   
4952 O  O   . HOH L .   ? 0.4244 0.5709 0.9556 0.0914  0.0672  0.1400  665 HOH B O   
# 
