data_5LLG
# 
_entry.id   5LLG 
# 
_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   5LLG         pdb_00005llg 10.2210/pdb5llg/pdb 
WWPDB D_1200000953 ?            ?                   
# 
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 2017-08-16 
2 'Structure model' 1 1 2018-05-16 
3 'Structure model' 1 2 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' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 3 'Structure model' Advisory                 
4 3 'Structure model' 'Data collection'        
5 3 'Structure model' 'Database references'    
6 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation                      
2 2 'Structure model' citation_author               
3 3 'Structure model' chem_comp_atom                
4 3 'Structure model' chem_comp_bond                
5 3 'Structure model' database_2                    
6 3 'Structure model' diffrn_radiation_wavelength   
7 3 'Structure model' pdbx_initial_refinement_model 
8 3 'Structure model' pdbx_unobs_or_zero_occ_atoms  
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                   
2  2 'Structure model' '_citation.journal_abbrev'            
3  2 'Structure model' '_citation.journal_id_CSD'            
4  2 'Structure model' '_citation.journal_id_ISSN'           
5  2 'Structure model' '_citation.journal_volume'            
6  2 'Structure model' '_citation.page_first'                
7  2 'Structure model' '_citation.page_last'                 
8  2 'Structure model' '_citation.pdbx_database_id_DOI'      
9  2 'Structure model' '_citation.pdbx_database_id_PubMed'   
10 2 'Structure model' '_citation.title'                     
11 2 'Structure model' '_citation.year'                      
12 3 'Structure model' '_database_2.pdbx_DOI'                
13 3 'Structure model' '_database_2.pdbx_database_accession' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5LLG 
_pdbx_database_status.recvd_initial_deposition_date   2016-07-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            PeerJ 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2167-8359 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            6 
_citation.language                  ? 
_citation.page_first                e4412 
_citation.page_last                 e4412 
_citation.title                     
'Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding.' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.7717/peerj.4412 
_citation.pdbx_database_id_PubMed   29503769 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnov, A.'  1 ? 
primary 'Zubriene, A.' 2 ? 
primary 'Manakova, E.' 3 ? 
primary 'Grazulis, S.' 4 ? 
primary 'Matulis, D.'  5 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                 29289.062 1   4.2.1.1 ? 'human carbonic anhydrase II'  ? 
2 non-polymer syn 'ZINC ION'                             65.409    1   ?       ? 4-Propylthiobenzenesulfonamide ? 
3 non-polymer syn '4-(propylsulfanyl)benzenesulfonamide' 231.335   2   ?       ? Zn                             ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                   78.133    2   ?       ? DMS                            ? 
5 non-polymer syn BICINE                                 163.172   1   ?       ? BCN                            ? 
6 water       nat water                                  18.015    306 ?       ? ?                              ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                             ZN  
3 '4-(propylsulfanyl)benzenesulfonamide' VD9 
4 'DIMETHYL SULFOXIDE'                   DMS 
5 BICINE                                 BCN 
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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                        ? 'C4 H7 N O4'     133.103 
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 
VD9 non-polymer         . '4-(propylsulfanyl)benzenesulfonamide' ? 'C9 H13 N O2 S2' 231.335 
ZN  non-polymer         . 'ZINC ION'                             ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 VD9 1   302 1   VD9 VD9 A . 
D 3 VD9 1   303 2   VD9 VD9 A . 
E 4 DMS 1   304 1   DMS DMS A . 
F 5 BCN 1   305 2   BCN BCN A . 
G 4 DMS 1   306 3   DMS DMS A . 
H 6 HOH 1   401 222 HOH HOH A . 
H 6 HOH 2   402 301 HOH HOH A . 
H 6 HOH 3   403 280 HOH HOH A . 
H 6 HOH 4   404 204 HOH HOH A . 
H 6 HOH 5   405 299 HOH HOH A . 
H 6 HOH 6   406 147 HOH HOH A . 
H 6 HOH 7   407 141 HOH HOH A . 
H 6 HOH 8   408 172 HOH HOH A . 
H 6 HOH 9   409 164 HOH HOH A . 
H 6 HOH 10  410 203 HOH HOH A . 
H 6 HOH 11  411 297 HOH HOH A . 
H 6 HOH 12  412 157 HOH HOH A . 
H 6 HOH 13  413 138 HOH HOH A . 
H 6 HOH 14  414 182 HOH HOH A . 
H 6 HOH 15  415 255 HOH HOH A . 
H 6 HOH 16  416 286 HOH HOH A . 
H 6 HOH 17  417 29  HOH HOH A . 
H 6 HOH 18  418 189 HOH HOH A . 
H 6 HOH 19  419 283 HOH HOH A . 
H 6 HOH 20  420 262 HOH HOH A . 
H 6 HOH 21  421 36  HOH HOH A . 
H 6 HOH 22  422 220 HOH HOH A . 
H 6 HOH 23  423 231 HOH HOH A . 
H 6 HOH 24  424 240 HOH HOH A . 
H 6 HOH 25  425 71  HOH HOH A . 
H 6 HOH 26  426 123 HOH HOH A . 
H 6 HOH 27  427 49  HOH HOH A . 
H 6 HOH 28  428 288 HOH HOH A . 
H 6 HOH 29  429 194 HOH HOH A . 
H 6 HOH 30  430 304 HOH HOH A . 
H 6 HOH 31  431 260 HOH HOH A . 
H 6 HOH 32  432 15  HOH HOH A . 
H 6 HOH 33  433 252 HOH HOH A . 
H 6 HOH 34  434 3   HOH HOH A . 
H 6 HOH 35  435 6   HOH HOH A . 
H 6 HOH 36  436 21  HOH HOH A . 
H 6 HOH 37  437 25  HOH HOH A . 
H 6 HOH 38  438 68  HOH HOH A . 
H 6 HOH 39  439 151 HOH HOH A . 
H 6 HOH 40  440 162 HOH HOH A . 
H 6 HOH 41  441 80  HOH HOH A . 
H 6 HOH 42  442 89  HOH HOH A . 
H 6 HOH 43  443 140 HOH HOH A . 
H 6 HOH 44  444 105 HOH HOH A . 
H 6 HOH 45  445 66  HOH HOH A . 
H 6 HOH 46  446 27  HOH HOH A . 
H 6 HOH 47  447 108 HOH HOH A . 
H 6 HOH 48  448 134 HOH HOH A . 
H 6 HOH 49  449 217 HOH HOH A . 
H 6 HOH 50  450 52  HOH HOH A . 
H 6 HOH 51  451 200 HOH HOH A . 
H 6 HOH 52  452 107 HOH HOH A . 
H 6 HOH 53  453 174 HOH HOH A . 
H 6 HOH 54  454 30  HOH HOH A . 
H 6 HOH 55  455 32  HOH HOH A . 
H 6 HOH 56  456 77  HOH HOH A . 
H 6 HOH 57  457 160 HOH HOH A . 
H 6 HOH 58  458 17  HOH HOH A . 
H 6 HOH 59  459 210 HOH HOH A . 
H 6 HOH 60  460 91  HOH HOH A . 
H 6 HOH 61  461 37  HOH HOH A . 
H 6 HOH 62  462 256 HOH HOH A . 
H 6 HOH 63  463 276 HOH HOH A . 
H 6 HOH 64  464 169 HOH HOH A . 
H 6 HOH 65  465 100 HOH HOH A . 
H 6 HOH 66  466 110 HOH HOH A . 
H 6 HOH 67  467 34  HOH HOH A . 
H 6 HOH 68  468 81  HOH HOH A . 
H 6 HOH 69  469 61  HOH HOH A . 
H 6 HOH 70  470 227 HOH HOH A . 
H 6 HOH 71  471 137 HOH HOH A . 
H 6 HOH 72  472 124 HOH HOH A . 
H 6 HOH 73  473 279 HOH HOH A . 
H 6 HOH 74  474 183 HOH HOH A . 
H 6 HOH 75  475 196 HOH HOH A . 
H 6 HOH 76  476 98  HOH HOH A . 
H 6 HOH 77  477 4   HOH HOH A . 
H 6 HOH 78  478 58  HOH HOH A . 
H 6 HOH 79  479 192 HOH HOH A . 
H 6 HOH 80  480 199 HOH HOH A . 
H 6 HOH 81  481 94  HOH HOH A . 
H 6 HOH 82  482 139 HOH HOH A . 
H 6 HOH 83  483 16  HOH HOH A . 
H 6 HOH 84  484 112 HOH HOH A . 
H 6 HOH 85  485 209 HOH HOH A . 
H 6 HOH 86  486 14  HOH HOH A . 
H 6 HOH 87  487 186 HOH HOH A . 
H 6 HOH 88  488 2   HOH HOH A . 
H 6 HOH 89  489 48  HOH HOH A . 
H 6 HOH 90  490 149 HOH HOH A . 
H 6 HOH 91  491 75  HOH HOH A . 
H 6 HOH 92  492 106 HOH HOH A . 
H 6 HOH 93  493 50  HOH HOH A . 
H 6 HOH 94  494 253 HOH HOH A . 
H 6 HOH 95  495 8   HOH HOH A . 
H 6 HOH 96  496 126 HOH HOH A . 
H 6 HOH 97  497 47  HOH HOH A . 
H 6 HOH 98  498 42  HOH HOH A . 
H 6 HOH 99  499 121 HOH HOH A . 
H 6 HOH 100 500 127 HOH HOH A . 
H 6 HOH 101 501 150 HOH HOH A . 
H 6 HOH 102 502 113 HOH HOH A . 
H 6 HOH 103 503 87  HOH HOH A . 
H 6 HOH 104 504 70  HOH HOH A . 
H 6 HOH 105 505 278 HOH HOH A . 
H 6 HOH 106 506 266 HOH HOH A . 
H 6 HOH 107 507 267 HOH HOH A . 
H 6 HOH 108 508 155 HOH HOH A . 
H 6 HOH 109 509 24  HOH HOH A . 
H 6 HOH 110 510 59  HOH HOH A . 
H 6 HOH 111 511 243 HOH HOH A . 
H 6 HOH 112 512 44  HOH HOH A . 
H 6 HOH 113 513 95  HOH HOH A . 
H 6 HOH 114 514 119 HOH HOH A . 
H 6 HOH 115 515 33  HOH HOH A . 
H 6 HOH 116 516 170 HOH HOH A . 
H 6 HOH 117 517 184 HOH HOH A . 
H 6 HOH 118 518 235 HOH HOH A . 
H 6 HOH 119 519 7   HOH HOH A . 
H 6 HOH 120 520 9   HOH HOH A . 
H 6 HOH 121 521 22  HOH HOH A . 
H 6 HOH 122 522 293 HOH HOH A . 
H 6 HOH 123 523 84  HOH HOH A . 
H 6 HOH 124 524 117 HOH HOH A . 
H 6 HOH 125 525 275 HOH HOH A . 
H 6 HOH 126 526 224 HOH HOH A . 
H 6 HOH 127 527 167 HOH HOH A . 
H 6 HOH 128 528 10  HOH HOH A . 
H 6 HOH 129 529 51  HOH HOH A . 
H 6 HOH 130 530 114 HOH HOH A . 
H 6 HOH 131 531 207 HOH HOH A . 
H 6 HOH 132 532 103 HOH HOH A . 
H 6 HOH 133 533 178 HOH HOH A . 
H 6 HOH 134 534 73  HOH HOH A . 
H 6 HOH 135 535 118 HOH HOH A . 
H 6 HOH 136 536 216 HOH HOH A . 
H 6 HOH 137 537 83  HOH HOH A . 
H 6 HOH 138 538 120 HOH HOH A . 
H 6 HOH 139 539 273 HOH HOH A . 
H 6 HOH 140 540 78  HOH HOH A . 
H 6 HOH 141 541 1   HOH HOH A . 
H 6 HOH 142 542 96  HOH HOH A . 
H 6 HOH 143 543 67  HOH HOH A . 
H 6 HOH 144 544 90  HOH HOH A . 
H 6 HOH 145 545 211 HOH HOH A . 
H 6 HOH 146 546 300 HOH HOH A . 
H 6 HOH 147 547 156 HOH HOH A . 
H 6 HOH 148 548 46  HOH HOH A . 
H 6 HOH 149 549 187 HOH HOH A . 
H 6 HOH 150 550 254 HOH HOH A . 
H 6 HOH 151 551 19  HOH HOH A . 
H 6 HOH 152 552 64  HOH HOH A . 
H 6 HOH 153 553 28  HOH HOH A . 
H 6 HOH 154 554 244 HOH HOH A . 
H 6 HOH 155 555 104 HOH HOH A . 
H 6 HOH 156 556 173 HOH HOH A . 
H 6 HOH 157 557 251 HOH HOH A . 
H 6 HOH 158 558 115 HOH HOH A . 
H 6 HOH 159 559 56  HOH HOH A . 
H 6 HOH 160 560 132 HOH HOH A . 
H 6 HOH 161 561 212 HOH HOH A . 
H 6 HOH 162 562 271 HOH HOH A . 
H 6 HOH 163 563 43  HOH HOH A . 
H 6 HOH 164 564 20  HOH HOH A . 
H 6 HOH 165 565 53  HOH HOH A . 
H 6 HOH 166 566 171 HOH HOH A . 
H 6 HOH 167 567 128 HOH HOH A . 
H 6 HOH 168 568 168 HOH HOH A . 
H 6 HOH 169 569 179 HOH HOH A . 
H 6 HOH 170 570 12  HOH HOH A . 
H 6 HOH 171 571 11  HOH HOH A . 
H 6 HOH 172 572 239 HOH HOH A . 
H 6 HOH 173 573 72  HOH HOH A . 
H 6 HOH 174 574 303 HOH HOH A . 
H 6 HOH 175 575 55  HOH HOH A . 
H 6 HOH 176 576 39  HOH HOH A . 
H 6 HOH 177 577 62  HOH HOH A . 
H 6 HOH 178 578 40  HOH HOH A . 
H 6 HOH 179 579 136 HOH HOH A . 
H 6 HOH 180 580 85  HOH HOH A . 
H 6 HOH 181 581 76  HOH HOH A . 
H 6 HOH 182 582 88  HOH HOH A . 
H 6 HOH 183 583 18  HOH HOH A . 
H 6 HOH 184 584 277 HOH HOH A . 
H 6 HOH 185 585 99  HOH HOH A . 
H 6 HOH 186 586 69  HOH HOH A . 
H 6 HOH 187 587 92  HOH HOH A . 
H 6 HOH 188 588 13  HOH HOH A . 
H 6 HOH 189 589 82  HOH HOH A . 
H 6 HOH 190 590 116 HOH HOH A . 
H 6 HOH 191 591 111 HOH HOH A . 
H 6 HOH 192 592 238 HOH HOH A . 
H 6 HOH 193 593 285 HOH HOH A . 
H 6 HOH 194 594 54  HOH HOH A . 
H 6 HOH 195 595 295 HOH HOH A . 
H 6 HOH 196 596 144 HOH HOH A . 
H 6 HOH 197 597 5   HOH HOH A . 
H 6 HOH 198 598 232 HOH HOH A . 
H 6 HOH 199 599 257 HOH HOH A . 
H 6 HOH 200 600 165 HOH HOH A . 
H 6 HOH 201 601 281 HOH HOH A . 
H 6 HOH 202 602 23  HOH HOH A . 
H 6 HOH 203 603 135 HOH HOH A . 
H 6 HOH 204 604 195 HOH HOH A . 
H 6 HOH 205 605 35  HOH HOH A . 
H 6 HOH 206 606 215 HOH HOH A . 
H 6 HOH 207 607 65  HOH HOH A . 
H 6 HOH 208 608 226 HOH HOH A . 
H 6 HOH 209 609 26  HOH HOH A . 
H 6 HOH 210 610 175 HOH HOH A . 
H 6 HOH 211 611 177 HOH HOH A . 
H 6 HOH 212 612 45  HOH HOH A . 
H 6 HOH 213 613 208 HOH HOH A . 
H 6 HOH 214 614 60  HOH HOH A . 
H 6 HOH 215 615 166 HOH HOH A . 
H 6 HOH 216 616 272 HOH HOH A . 
H 6 HOH 217 617 206 HOH HOH A . 
H 6 HOH 218 618 122 HOH HOH A . 
H 6 HOH 219 619 86  HOH HOH A . 
H 6 HOH 220 620 306 HOH HOH A . 
H 6 HOH 221 621 154 HOH HOH A . 
H 6 HOH 222 622 290 HOH HOH A . 
H 6 HOH 223 623 152 HOH HOH A . 
H 6 HOH 224 624 190 HOH HOH A . 
H 6 HOH 225 625 143 HOH HOH A . 
H 6 HOH 226 626 298 HOH HOH A . 
H 6 HOH 227 627 296 HOH HOH A . 
H 6 HOH 228 628 250 HOH HOH A . 
H 6 HOH 229 629 131 HOH HOH A . 
H 6 HOH 230 630 246 HOH HOH A . 
H 6 HOH 231 631 219 HOH HOH A . 
H 6 HOH 232 632 93  HOH HOH A . 
H 6 HOH 233 633 31  HOH HOH A . 
H 6 HOH 234 634 205 HOH HOH A . 
H 6 HOH 235 635 302 HOH HOH A . 
H 6 HOH 236 636 97  HOH HOH A . 
H 6 HOH 237 637 241 HOH HOH A . 
H 6 HOH 238 638 74  HOH HOH A . 
H 6 HOH 239 639 133 HOH HOH A . 
H 6 HOH 240 640 263 HOH HOH A . 
H 6 HOH 241 641 163 HOH HOH A . 
H 6 HOH 242 642 79  HOH HOH A . 
H 6 HOH 243 643 146 HOH HOH A . 
H 6 HOH 244 644 292 HOH HOH A . 
H 6 HOH 245 645 161 HOH HOH A . 
H 6 HOH 246 646 176 HOH HOH A . 
H 6 HOH 247 647 63  HOH HOH A . 
H 6 HOH 248 648 230 HOH HOH A . 
H 6 HOH 249 649 236 HOH HOH A . 
H 6 HOH 250 650 294 HOH HOH A . 
H 6 HOH 251 651 57  HOH HOH A . 
H 6 HOH 252 652 233 HOH HOH A . 
H 6 HOH 253 653 213 HOH HOH A . 
H 6 HOH 254 654 225 HOH HOH A . 
H 6 HOH 255 655 242 HOH HOH A . 
H 6 HOH 256 656 268 HOH HOH A . 
H 6 HOH 257 657 197 HOH HOH A . 
H 6 HOH 258 658 125 HOH HOH A . 
H 6 HOH 259 659 291 HOH HOH A . 
H 6 HOH 260 660 185 HOH HOH A . 
H 6 HOH 261 661 159 HOH HOH A . 
H 6 HOH 262 662 101 HOH HOH A . 
H 6 HOH 263 663 193 HOH HOH A . 
H 6 HOH 264 664 130 HOH HOH A . 
H 6 HOH 265 665 180 HOH HOH A . 
H 6 HOH 266 666 247 HOH HOH A . 
H 6 HOH 267 667 249 HOH HOH A . 
H 6 HOH 268 668 158 HOH HOH A . 
H 6 HOH 269 669 287 HOH HOH A . 
H 6 HOH 270 670 274 HOH HOH A . 
H 6 HOH 271 671 261 HOH HOH A . 
H 6 HOH 272 672 142 HOH HOH A . 
H 6 HOH 273 673 265 HOH HOH A . 
H 6 HOH 274 674 245 HOH HOH A . 
H 6 HOH 275 675 188 HOH HOH A . 
H 6 HOH 276 676 282 HOH HOH A . 
H 6 HOH 277 677 305 HOH HOH A . 
H 6 HOH 278 678 237 HOH HOH A . 
H 6 HOH 279 679 181 HOH HOH A . 
H 6 HOH 280 680 229 HOH HOH A . 
H 6 HOH 281 681 234 HOH HOH A . 
H 6 HOH 282 682 258 HOH HOH A . 
H 6 HOH 283 683 201 HOH HOH A . 
H 6 HOH 284 684 198 HOH HOH A . 
H 6 HOH 285 685 41  HOH HOH A . 
H 6 HOH 286 686 202 HOH HOH A . 
H 6 HOH 287 687 191 HOH HOH A . 
H 6 HOH 288 688 289 HOH HOH A . 
H 6 HOH 289 689 153 HOH HOH A . 
H 6 HOH 290 690 228 HOH HOH A . 
H 6 HOH 291 691 145 HOH HOH A . 
H 6 HOH 292 692 284 HOH HOH A . 
H 6 HOH 293 693 221 HOH HOH A . 
H 6 HOH 294 694 38  HOH HOH A . 
H 6 HOH 295 695 129 HOH HOH A . 
H 6 HOH 296 696 248 HOH HOH A . 
H 6 HOH 297 697 223 HOH HOH A . 
H 6 HOH 298 698 269 HOH HOH A . 
H 6 HOH 299 699 264 HOH HOH A . 
H 6 HOH 300 700 109 HOH HOH A . 
H 6 HOH 301 701 218 HOH HOH A . 
H 6 HOH 302 702 214 HOH HOH A . 
H 6 HOH 303 703 270 HOH HOH A . 
H 6 HOH 304 704 102 HOH HOH A . 
H 6 HOH 305 705 148 HOH HOH A . 
H 6 HOH 306 706 259 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
3  1 Y 0 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 ? CD  ? A LYS 158 CD  
7  1 Y 1 A LYS 159 ? CE  ? A LYS 158 CE  
8  1 Y 1 A LYS 159 ? NZ  ? A LYS 158 NZ  
9  1 Y 1 A LYS 228 ? CE  ? A LYS 227 CE  
10 1 Y 1 A LYS 228 ? NZ  ? A LYS 227 NZ  
11 1 Y 1 A GLU 239 ? CD  ? A GLU 238 CD  
12 1 Y 1 A GLU 239 ? OE1 ? A GLU 238 OE1 
13 1 Y 1 A GLU 239 ? OE2 ? A GLU 238 OE2 
14 1 Y 1 A GLN 255 ? CD  ? A GLN 254 CD  
15 1 Y 1 A GLN 255 ? OE1 ? A GLN 254 OE1 
16 1 Y 1 A GLN 255 ? NE2 ? A GLN 254 NE2 
17 1 Y 1 A LYS 257 ? CD  ? A LYS 256 CD  
18 1 Y 1 A LYS 257 ? CE  ? A LYS 256 CE  
19 1 Y 1 A LYS 257 ? NZ  ? A LYS 256 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.240 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5LLG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.116 
_cell.length_a_esd                 ? 
_cell.length_b                     41.129 
_cell.length_b_esd                 ? 
_cell.length_c                     71.824 
_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                         5LLG 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5LLG 
_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         38.4 
_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 
_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), 0.2M ammonium sulfate and 2M sodium malonate (pH 7)' 
_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-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-01-07 
# 
_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 P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            10.684 
_reflns.entry_id                         5LLG 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.120 
_reflns.d_resolution_low                 40.821 
_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                       ? 
_reflns.number_obs                       83155 
_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             91.500 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.600 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.068 
_reflns.pdbx_netI_over_av_sigmaI         3.881 
_reflns.pdbx_netI_over_sigmaI            11.200 
_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                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_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 
1.120 1.180  ? 1.800  ? ? ? ? ? 67.000 ? ? ? ? 0.400 ? ? ? ? ? ? ? ? 5.500 ? ? ? ? ? ? ? 1  1 ? ? 
1.180 1.250  ? 2.300  ? ? ? ? ? 92.100 ? ? ? ? 0.309 ? ? ? ? ? ? ? ? 6.300 ? ? ? ? ? ? ? 2  1 ? ? 
1.250 1.340  ? 3.100  ? ? ? ? ? 94.700 ? ? ? ? 0.224 ? ? ? ? ? ? ? ? 6.800 ? ? ? ? ? ? ? 3  1 ? ? 
1.340 1.450  ? 4.500  ? ? ? ? ? 94.800 ? ? ? ? 0.153 ? ? ? ? ? ? ? ? 6.800 ? ? ? ? ? ? ? 4  1 ? ? 
1.450 1.590  ? 6.300  ? ? ? ? ? 95.900 ? ? ? ? 0.106 ? ? ? ? ? ? ? ? 6.800 ? ? ? ? ? ? ? 5  1 ? ? 
1.590 1.770  ? 7.800  ? ? ? ? ? 96.600 ? ? ? ? 0.083 ? ? ? ? ? ? ? ? 6.800 ? ? ? ? ? ? ? 6  1 ? ? 
1.770 2.050  ? 8.900  ? ? ? ? ? 98.000 ? ? ? ? 0.069 ? ? ? ? ? ? ? ? 7.000 ? ? ? ? ? ? ? 7  1 ? ? 
2.050 2.510  ? 10.300 ? ? ? ? ? 98.300 ? ? ? ? 0.063 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 8  1 ? ? 
2.510 3.550  ? 10.100 ? ? ? ? ? 99.200 ? ? ? ? 0.059 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 9  1 ? ? 
3.550 40.821 ? 8.900  ? ? ? ? ? 98.200 ? ? ? ? 0.058 ? ? ? ? ? ? ? ? 6.600 ? ? ? ? ? ? ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            0.3500 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0600 
_refine.aniso_B[2][2]                            -0.5100 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.1900 
_refine.B_iso_max                                113.050 
_refine.B_iso_mean                               17.7870 
_refine.B_iso_min                                6.970 
_refine.correlation_coeff_Fo_to_Fc               0.9800 
_refine.correlation_coeff_Fo_to_Fc_free          0.9730 
_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                                 5LLG 
_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                            1.1200 
_refine.ls_d_res_low                             39.7400 
_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                     74815 
_refine.ls_number_reflns_R_free                  8316 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.1500 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1409 
_refine.ls_R_factor_R_free                       0.1671 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1380 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4HT0 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0360 
_refine.pdbx_overall_ESU_R_Free                  0.0370 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.0361 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.1200 
_refine_hist.d_res_low                        39.7400 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.number_atoms_solvent             306 
_refine_hist.number_atoms_total               2403 
_refine_hist.pdbx_number_residues_total       257 
_refine_hist.pdbx_B_iso_mean_ligand           26.53 
_refine_hist.pdbx_B_iso_mean_solvent          29.40 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
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' ? 0.024  0.020  2262 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.307  1.967  3092 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.753  5.000  283  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.459 24.700 100  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 11.900 15.000 359  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 20.942 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.173  0.200  320  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.021  1777 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 9.243  3.000  2262 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 22.972 5.000  307  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 12.711 5.000  2187 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.1220 
_refine_ls_shell.d_res_low                        1.1510 
_refine_ls_shell.number_reflns_all                3626 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             369 
_refine_ls_shell.number_reflns_R_work             3257 
_refine_ls_shell.percent_reflns_obs               53.7700 
_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                  0.2610 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2520 
_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                     5LLG 
_struct.title                        'Crystal structure of human carbonic anhydrase isozyme II with 4-Propylthiobenzenesulfonamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        5LLG 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 4 ? 
H N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              5LLG 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 710   ? 
1 MORE         4     ? 
1 'SSA (A^2)'  11440 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C VD9 . N3 ? ? A ZN  301 A VD9 302 1_555 ? ? ? ? ? ? ? 1.892 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 104.0 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 111.4 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.2  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N3  ? C VD9 .   ? A VD9 302 ? 1_555 110.8 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N3  ? C VD9 .   ? A VD9 302 ? 1_555 113.4 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N3  ? C VD9 .   ? A VD9 302 ? 1_555 116.9 ? 
# 
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 -1.96 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 9.17  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  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 
# 
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 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A VD9 302 ? 10 'binding site for residue VD9 A 302' 
AC3 Software A VD9 303 ? 12 'binding site for residue VD9 A 303' 
AC4 Software A DMS 304 ? 3  'binding site for residue DMS A 304' 
AC5 Software A BCN 305 ? 8  'binding site for residue BCN A 305' 
AC6 Software A DMS 306 ? 5  'binding site for residue DMS A 306' 
# 
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  VD9 C .   ? VD9 A 302 . ? 1_555 ? 
5  AC2 10 HIS A 94  ? HIS A 94  . ? 1_555 ? 
6  AC2 10 HIS A 96  ? HIS A 96  . ? 1_555 ? 
7  AC2 10 HIS A 119 ? HIS A 119 . ? 1_555 ? 
8  AC2 10 LEU A 197 ? LEU A 198 . ? 1_555 ? 
9  AC2 10 THR A 198 ? THR A 199 . ? 1_555 ? 
10 AC2 10 THR A 199 ? THR A 200 . ? 1_555 ? 
11 AC2 10 TRP A 208 ? TRP A 209 . ? 1_555 ? 
12 AC2 10 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
13 AC2 10 DMS G .   ? DMS A 306 . ? 1_555 ? 
14 AC2 10 HOH H .   ? HOH A 612 . ? 1_555 ? 
15 AC3 12 HIS A 4   ? HIS A 4   . ? 1_555 ? 
16 AC3 12 TRP A 5   ? TRP A 5   . ? 1_555 ? 
17 AC3 12 HIS A 10  ? HIS A 10  . ? 1_555 ? 
18 AC3 12 ASN A 11  ? ASN A 11  . ? 1_555 ? 
19 AC3 12 HIS A 15  ? HIS A 15  . ? 1_555 ? 
20 AC3 12 TRP A 16  ? TRP A 16  . ? 1_555 ? 
21 AC3 12 ASP A 19  ? ASP A 19  . ? 1_555 ? 
22 AC3 12 PHE A 20  ? PHE A 20  . ? 1_555 ? 
23 AC3 12 ASP A 179 ? ASP A 180 . ? 1_655 ? 
24 AC3 12 ARG A 181 ? ARG A 182 . ? 1_655 ? 
25 AC3 12 GLY A 182 ? GLY A 183 . ? 1_655 ? 
26 AC3 12 HOH H .   ? HOH A 472 . ? 1_555 ? 
27 AC4 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
28 AC4 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
29 AC4 3  PRO A 246 ? PRO A 247 . ? 1_555 ? 
30 AC5 8  LYS A 148 ? LYS A 149 . ? 1_555 ? 
31 AC5 8  LYS A 212 ? LYS A 213 . ? 1_555 ? 
32 AC5 8  GLU A 213 ? GLU A 214 . ? 1_555 ? 
33 AC5 8  PRO A 214 ? PRO A 215 . ? 1_555 ? 
34 AC5 8  HOH H .   ? HOH A 444 . ? 1_555 ? 
35 AC5 8  HOH H .   ? HOH A 455 . ? 1_555 ? 
36 AC5 8  HOH H .   ? HOH A 470 . ? 1_555 ? 
37 AC5 8  HOH H .   ? HOH A 584 . ? 1_555 ? 
38 AC6 5  ILE A 91  ? ILE A 91  . ? 1_555 ? 
39 AC6 5  GLN A 92  ? GLN A 92  . ? 1_555 ? 
40 AC6 5  PHE A 130 ? PHE A 131 . ? 1_555 ? 
41 AC6 5  VD9 C .   ? VD9 A 302 . ? 1_555 ? 
42 AC6 5  HOH H .   ? HOH A 617 . ? 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 O   A LYS 76  ? ? O A HOH 401 ? ? 1.77 
2 1 NE2 A GLN 137 ? ? O A HOH 402 ? ? 1.87 
3 1 O   A HOH 404 ? ? O A HOH 410 ? ? 1.89 
4 1 OE1 A GLU 238 ? ? O A HOH 403 ? ? 2.05 
5 1 NE2 A HIS 64  ? B O A HOH 404 ? ? 2.05 
6 1 O   A HOH 409 ? ? O A HOH 439 ? ? 2.16 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OG 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    SER 
_pdbx_validate_symm_contact.auth_seq_id_1     73 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     409 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_565 
_pdbx_validate_symm_contact.dist              2.18 
# 
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 15 ? ? CD2 A HIS 15 ? ? 1.412 1.354 0.058 0.009 N 
2 1 CG A HIS 36 ? ? CD2 A HIS 36 ? ? 1.412 1.354 0.058 0.009 N 
3 1 CG A HIS 64 ? B CD2 A HIS 64 ? B 1.450 1.354 0.096 0.009 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -142.39 55.87   
2 1 ALA A 65  ? ? -167.59 -169.43 
3 1 LYS A 111 ? ? 72.88   -0.25   
4 1 PHE A 176 ? ? -150.00 73.12   
5 1 ASN A 244 ? ? -94.17  47.71   
6 1 LYS A 252 ? ? 53.77   -138.56 
# 
_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                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       706 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.54 
_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 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
LEU N    N  N N 217 
LEU CA   C  N S 218 
LEU C    C  N N 219 
LEU O    O  N N 220 
LEU CB   C  N N 221 
LEU CG   C  N N 222 
LEU CD1  C  N N 223 
LEU CD2  C  N N 224 
LEU OXT  O  N N 225 
LEU H    H  N N 226 
LEU H2   H  N N 227 
LEU HA   H  N N 228 
LEU HB2  H  N N 229 
LEU HB3  H  N N 230 
LEU HG   H  N N 231 
LEU HD11 H  N N 232 
LEU HD12 H  N N 233 
LEU HD13 H  N N 234 
LEU HD21 H  N N 235 
LEU HD22 H  N N 236 
LEU HD23 H  N N 237 
LEU HXT  H  N N 238 
LYS N    N  N N 239 
LYS CA   C  N S 240 
LYS C    C  N N 241 
LYS O    O  N N 242 
LYS CB   C  N N 243 
LYS CG   C  N N 244 
LYS CD   C  N N 245 
LYS CE   C  N N 246 
LYS NZ   N  N N 247 
LYS OXT  O  N N 248 
LYS H    H  N N 249 
LYS H2   H  N N 250 
LYS HA   H  N N 251 
LYS HB2  H  N N 252 
LYS HB3  H  N N 253 
LYS HG2  H  N N 254 
LYS HG3  H  N N 255 
LYS HD2  H  N N 256 
LYS HD3  H  N N 257 
LYS HE2  H  N N 258 
LYS HE3  H  N N 259 
LYS HZ1  H  N N 260 
LYS HZ2  H  N N 261 
LYS HZ3  H  N N 262 
LYS HXT  H  N N 263 
MET N    N  N N 264 
MET CA   C  N S 265 
MET C    C  N N 266 
MET O    O  N N 267 
MET CB   C  N N 268 
MET CG   C  N N 269 
MET SD   S  N N 270 
MET CE   C  N N 271 
MET OXT  O  N N 272 
MET H    H  N N 273 
MET H2   H  N N 274 
MET HA   H  N N 275 
MET HB2  H  N N 276 
MET HB3  H  N N 277 
MET HG2  H  N N 278 
MET HG3  H  N N 279 
MET HE1  H  N N 280 
MET HE2  H  N N 281 
MET HE3  H  N N 282 
MET HXT  H  N N 283 
PHE N    N  N N 284 
PHE CA   C  N S 285 
PHE C    C  N N 286 
PHE O    O  N N 287 
PHE CB   C  N N 288 
PHE CG   C  Y N 289 
PHE CD1  C  Y N 290 
PHE CD2  C  Y N 291 
PHE CE1  C  Y N 292 
PHE CE2  C  Y N 293 
PHE CZ   C  Y N 294 
PHE OXT  O  N N 295 
PHE H    H  N N 296 
PHE H2   H  N N 297 
PHE HA   H  N N 298 
PHE HB2  H  N N 299 
PHE HB3  H  N N 300 
PHE HD1  H  N N 301 
PHE HD2  H  N N 302 
PHE HE1  H  N N 303 
PHE HE2  H  N N 304 
PHE HZ   H  N N 305 
PHE HXT  H  N N 306 
PRO N    N  N N 307 
PRO CA   C  N S 308 
PRO C    C  N N 309 
PRO O    O  N N 310 
PRO CB   C  N N 311 
PRO CG   C  N N 312 
PRO CD   C  N N 313 
PRO OXT  O  N N 314 
PRO H    H  N N 315 
PRO HA   H  N N 316 
PRO HB2  H  N N 317 
PRO HB3  H  N N 318 
PRO HG2  H  N N 319 
PRO HG3  H  N N 320 
PRO HD2  H  N N 321 
PRO HD3  H  N N 322 
PRO HXT  H  N N 323 
SER N    N  N N 324 
SER CA   C  N S 325 
SER C    C  N N 326 
SER O    O  N N 327 
SER CB   C  N N 328 
SER OG   O  N N 329 
SER OXT  O  N N 330 
SER H    H  N N 331 
SER H2   H  N N 332 
SER HA   H  N N 333 
SER HB2  H  N N 334 
SER HB3  H  N N 335 
SER HG   H  N N 336 
SER HXT  H  N N 337 
THR N    N  N N 338 
THR CA   C  N S 339 
THR C    C  N N 340 
THR O    O  N N 341 
THR CB   C  N R 342 
THR OG1  O  N N 343 
THR CG2  C  N N 344 
THR OXT  O  N N 345 
THR H    H  N N 346 
THR H2   H  N N 347 
THR HA   H  N N 348 
THR HB   H  N N 349 
THR HG1  H  N N 350 
THR HG21 H  N N 351 
THR HG22 H  N N 352 
THR HG23 H  N N 353 
THR HXT  H  N N 354 
TRP N    N  N N 355 
TRP CA   C  N S 356 
TRP C    C  N N 357 
TRP O    O  N N 358 
TRP CB   C  N N 359 
TRP CG   C  Y N 360 
TRP CD1  C  Y N 361 
TRP CD2  C  Y N 362 
TRP NE1  N  Y N 363 
TRP CE2  C  Y N 364 
TRP CE3  C  Y N 365 
TRP CZ2  C  Y N 366 
TRP CZ3  C  Y N 367 
TRP CH2  C  Y N 368 
TRP OXT  O  N N 369 
TRP H    H  N N 370 
TRP H2   H  N N 371 
TRP HA   H  N N 372 
TRP HB2  H  N N 373 
TRP HB3  H  N N 374 
TRP HD1  H  N N 375 
TRP HE1  H  N N 376 
TRP HE3  H  N N 377 
TRP HZ2  H  N N 378 
TRP HZ3  H  N N 379 
TRP HH2  H  N N 380 
TRP HXT  H  N N 381 
TYR N    N  N N 382 
TYR CA   C  N S 383 
TYR C    C  N N 384 
TYR O    O  N N 385 
TYR CB   C  N N 386 
TYR CG   C  Y N 387 
TYR CD1  C  Y N 388 
TYR CD2  C  Y N 389 
TYR CE1  C  Y N 390 
TYR CE2  C  Y N 391 
TYR CZ   C  Y N 392 
TYR OH   O  N N 393 
TYR OXT  O  N N 394 
TYR H    H  N N 395 
TYR H2   H  N N 396 
TYR HA   H  N N 397 
TYR HB2  H  N N 398 
TYR HB3  H  N N 399 
TYR HD1  H  N N 400 
TYR HD2  H  N N 401 
TYR HE1  H  N N 402 
TYR HE2  H  N N 403 
TYR HH   H  N N 404 
TYR HXT  H  N N 405 
VAL N    N  N N 406 
VAL CA   C  N S 407 
VAL C    C  N N 408 
VAL O    O  N N 409 
VAL CB   C  N N 410 
VAL CG1  C  N N 411 
VAL CG2  C  N N 412 
VAL OXT  O  N N 413 
VAL H    H  N N 414 
VAL H2   H  N N 415 
VAL HA   H  N N 416 
VAL HB   H  N N 417 
VAL HG11 H  N N 418 
VAL HG12 H  N N 419 
VAL HG13 H  N N 420 
VAL HG21 H  N N 421 
VAL HG22 H  N N 422 
VAL HG23 H  N N 423 
VAL HXT  H  N N 424 
VD9 O4   O  N N 425 
VD9 S2   S  N N 426 
VD9 O1   O  N N 427 
VD9 N3   N  N N 428 
VD9 C5   C  Y N 429 
VD9 C10  C  Y N 430 
VD9 C9   C  Y N 431 
VD9 C8   C  Y N 432 
VD9 C7   C  Y N 433 
VD9 C6   C  Y N 434 
VD9 S11  S  N N 435 
VD9 C12  C  N N 436 
VD9 C13  C  N N 437 
VD9 C14  C  N N 438 
VD9 H1   H  N N 439 
VD9 H2   H  N N 440 
VD9 H3   H  N N 441 
VD9 H4   H  N N 442 
VD9 H5   H  N N 443 
VD9 H6   H  N N 444 
VD9 H7   H  N N 445 
VD9 H8   H  N N 446 
VD9 H9   H  N N 447 
VD9 H10  H  N N 448 
VD9 H11  H  N N 449 
VD9 H12  H  N N 450 
VD9 H13  H  N N 451 
ZN  ZN   ZN N N 452 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
GLN N   CA   sing N N 115 
GLN N   H    sing N N 116 
GLN N   H2   sing N N 117 
GLN CA  C    sing N N 118 
GLN CA  CB   sing N N 119 
GLN CA  HA   sing N N 120 
GLN C   O    doub N N 121 
GLN C   OXT  sing N N 122 
GLN CB  CG   sing N N 123 
GLN CB  HB2  sing N N 124 
GLN CB  HB3  sing N N 125 
GLN CG  CD   sing N N 126 
GLN CG  HG2  sing N N 127 
GLN CG  HG3  sing N N 128 
GLN CD  OE1  doub N N 129 
GLN CD  NE2  sing N N 130 
GLN NE2 HE21 sing N N 131 
GLN NE2 HE22 sing N N 132 
GLN OXT HXT  sing N N 133 
GLU N   CA   sing N N 134 
GLU N   H    sing N N 135 
GLU N   H2   sing N N 136 
GLU CA  C    sing N N 137 
GLU CA  CB   sing N N 138 
GLU CA  HA   sing N N 139 
GLU C   O    doub N N 140 
GLU C   OXT  sing N N 141 
GLU CB  CG   sing N N 142 
GLU CB  HB2  sing N N 143 
GLU CB  HB3  sing N N 144 
GLU CG  CD   sing N N 145 
GLU CG  HG2  sing N N 146 
GLU CG  HG3  sing N N 147 
GLU CD  OE1  doub N N 148 
GLU CD  OE2  sing N N 149 
GLU OE2 HE2  sing N N 150 
GLU OXT HXT  sing N N 151 
GLY N   CA   sing N N 152 
GLY N   H    sing N N 153 
GLY N   H2   sing N N 154 
GLY CA  C    sing N N 155 
GLY CA  HA2  sing N N 156 
GLY CA  HA3  sing N N 157 
GLY C   O    doub N N 158 
GLY C   OXT  sing N N 159 
GLY OXT HXT  sing N N 160 
HIS N   CA   sing N N 161 
HIS N   H    sing N N 162 
HIS N   H2   sing N N 163 
HIS CA  C    sing N N 164 
HIS CA  CB   sing N N 165 
HIS CA  HA   sing N N 166 
HIS C   O    doub N N 167 
HIS C   OXT  sing N N 168 
HIS CB  CG   sing N N 169 
HIS CB  HB2  sing N N 170 
HIS CB  HB3  sing N N 171 
HIS CG  ND1  sing Y N 172 
HIS CG  CD2  doub Y N 173 
HIS ND1 CE1  doub Y N 174 
HIS ND1 HD1  sing N N 175 
HIS CD2 NE2  sing Y N 176 
HIS CD2 HD2  sing N N 177 
HIS CE1 NE2  sing Y N 178 
HIS CE1 HE1  sing N N 179 
HIS NE2 HE2  sing N N 180 
HIS OXT HXT  sing N N 181 
HOH O   H1   sing N N 182 
HOH O   H2   sing N N 183 
ILE N   CA   sing N N 184 
ILE N   H    sing N N 185 
ILE N   H2   sing N N 186 
ILE CA  C    sing N N 187 
ILE CA  CB   sing N N 188 
ILE CA  HA   sing N N 189 
ILE C   O    doub N N 190 
ILE C   OXT  sing N N 191 
ILE CB  CG1  sing N N 192 
ILE CB  CG2  sing N N 193 
ILE CB  HB   sing N N 194 
ILE CG1 CD1  sing N N 195 
ILE CG1 HG12 sing N N 196 
ILE CG1 HG13 sing N N 197 
ILE CG2 HG21 sing N N 198 
ILE CG2 HG22 sing N N 199 
ILE CG2 HG23 sing N N 200 
ILE CD1 HD11 sing N N 201 
ILE CD1 HD12 sing N N 202 
ILE CD1 HD13 sing N N 203 
ILE OXT HXT  sing N N 204 
LEU N   CA   sing N N 205 
LEU N   H    sing N N 206 
LEU N   H2   sing N N 207 
LEU CA  C    sing N N 208 
LEU CA  CB   sing N N 209 
LEU CA  HA   sing N N 210 
LEU C   O    doub N N 211 
LEU C   OXT  sing N N 212 
LEU CB  CG   sing N N 213 
LEU CB  HB2  sing N N 214 
LEU CB  HB3  sing N N 215 
LEU CG  CD1  sing N N 216 
LEU CG  CD2  sing N N 217 
LEU CG  HG   sing N N 218 
LEU CD1 HD11 sing N N 219 
LEU CD1 HD12 sing N N 220 
LEU CD1 HD13 sing N N 221 
LEU CD2 HD21 sing N N 222 
LEU CD2 HD22 sing N N 223 
LEU CD2 HD23 sing N N 224 
LEU OXT HXT  sing N N 225 
LYS N   CA   sing N N 226 
LYS N   H    sing N N 227 
LYS N   H2   sing N N 228 
LYS CA  C    sing N N 229 
LYS CA  CB   sing N N 230 
LYS CA  HA   sing N N 231 
LYS C   O    doub N N 232 
LYS C   OXT  sing N N 233 
LYS CB  CG   sing N N 234 
LYS CB  HB2  sing N N 235 
LYS CB  HB3  sing N N 236 
LYS CG  CD   sing N N 237 
LYS CG  HG2  sing N N 238 
LYS CG  HG3  sing N N 239 
LYS CD  CE   sing N N 240 
LYS CD  HD2  sing N N 241 
LYS CD  HD3  sing N N 242 
LYS CE  NZ   sing N N 243 
LYS CE  HE2  sing N N 244 
LYS CE  HE3  sing N N 245 
LYS NZ  HZ1  sing N N 246 
LYS NZ  HZ2  sing N N 247 
LYS NZ  HZ3  sing N N 248 
LYS OXT HXT  sing N N 249 
MET N   CA   sing N N 250 
MET N   H    sing N N 251 
MET N   H2   sing N N 252 
MET CA  C    sing N N 253 
MET CA  CB   sing N N 254 
MET CA  HA   sing N N 255 
MET C   O    doub N N 256 
MET C   OXT  sing N N 257 
MET CB  CG   sing N N 258 
MET CB  HB2  sing N N 259 
MET CB  HB3  sing N N 260 
MET CG  SD   sing N N 261 
MET CG  HG2  sing N N 262 
MET CG  HG3  sing N N 263 
MET SD  CE   sing N N 264 
MET CE  HE1  sing N N 265 
MET CE  HE2  sing N N 266 
MET CE  HE3  sing N N 267 
MET OXT HXT  sing N N 268 
PHE N   CA   sing N N 269 
PHE N   H    sing N N 270 
PHE N   H2   sing N N 271 
PHE CA  C    sing N N 272 
PHE CA  CB   sing N N 273 
PHE CA  HA   sing N N 274 
PHE C   O    doub N N 275 
PHE C   OXT  sing N N 276 
PHE CB  CG   sing N N 277 
PHE CB  HB2  sing N N 278 
PHE CB  HB3  sing N N 279 
PHE CG  CD1  doub Y N 280 
PHE CG  CD2  sing Y N 281 
PHE CD1 CE1  sing Y N 282 
PHE CD1 HD1  sing N N 283 
PHE CD2 CE2  doub Y N 284 
PHE CD2 HD2  sing N N 285 
PHE CE1 CZ   doub Y N 286 
PHE CE1 HE1  sing N N 287 
PHE CE2 CZ   sing Y N 288 
PHE CE2 HE2  sing N N 289 
PHE CZ  HZ   sing N N 290 
PHE OXT HXT  sing N N 291 
PRO N   CA   sing N N 292 
PRO N   CD   sing N N 293 
PRO N   H    sing N N 294 
PRO CA  C    sing N N 295 
PRO CA  CB   sing N N 296 
PRO CA  HA   sing N N 297 
PRO C   O    doub N N 298 
PRO C   OXT  sing N N 299 
PRO CB  CG   sing N N 300 
PRO CB  HB2  sing N N 301 
PRO CB  HB3  sing N N 302 
PRO CG  CD   sing N N 303 
PRO CG  HG2  sing N N 304 
PRO CG  HG3  sing N N 305 
PRO CD  HD2  sing N N 306 
PRO CD  HD3  sing N N 307 
PRO OXT HXT  sing N N 308 
SER N   CA   sing N N 309 
SER N   H    sing N N 310 
SER N   H2   sing N N 311 
SER CA  C    sing N N 312 
SER CA  CB   sing N N 313 
SER CA  HA   sing N N 314 
SER C   O    doub N N 315 
SER C   OXT  sing N N 316 
SER CB  OG   sing N N 317 
SER CB  HB2  sing N N 318 
SER CB  HB3  sing N N 319 
SER OG  HG   sing N N 320 
SER OXT HXT  sing N N 321 
THR N   CA   sing N N 322 
THR N   H    sing N N 323 
THR N   H2   sing N N 324 
THR CA  C    sing N N 325 
THR CA  CB   sing N N 326 
THR CA  HA   sing N N 327 
THR C   O    doub N N 328 
THR C   OXT  sing N N 329 
THR CB  OG1  sing N N 330 
THR CB  CG2  sing N N 331 
THR CB  HB   sing N N 332 
THR OG1 HG1  sing N N 333 
THR CG2 HG21 sing N N 334 
THR CG2 HG22 sing N N 335 
THR CG2 HG23 sing N N 336 
THR OXT HXT  sing N N 337 
TRP N   CA   sing N N 338 
TRP N   H    sing N N 339 
TRP N   H2   sing N N 340 
TRP CA  C    sing N N 341 
TRP CA  CB   sing N N 342 
TRP CA  HA   sing N N 343 
TRP C   O    doub N N 344 
TRP C   OXT  sing N N 345 
TRP CB  CG   sing N N 346 
TRP CB  HB2  sing N N 347 
TRP CB  HB3  sing N N 348 
TRP CG  CD1  doub Y N 349 
TRP CG  CD2  sing Y N 350 
TRP CD1 NE1  sing Y N 351 
TRP CD1 HD1  sing N N 352 
TRP CD2 CE2  doub Y N 353 
TRP CD2 CE3  sing Y N 354 
TRP NE1 CE2  sing Y N 355 
TRP NE1 HE1  sing N N 356 
TRP CE2 CZ2  sing Y N 357 
TRP CE3 CZ3  doub Y N 358 
TRP CE3 HE3  sing N N 359 
TRP CZ2 CH2  doub Y N 360 
TRP CZ2 HZ2  sing N N 361 
TRP CZ3 CH2  sing Y N 362 
TRP CZ3 HZ3  sing N N 363 
TRP CH2 HH2  sing N N 364 
TRP OXT HXT  sing N N 365 
TYR N   CA   sing N N 366 
TYR N   H    sing N N 367 
TYR N   H2   sing N N 368 
TYR CA  C    sing N N 369 
TYR CA  CB   sing N N 370 
TYR CA  HA   sing N N 371 
TYR C   O    doub N N 372 
TYR C   OXT  sing N N 373 
TYR CB  CG   sing N N 374 
TYR CB  HB2  sing N N 375 
TYR CB  HB3  sing N N 376 
TYR CG  CD1  doub Y N 377 
TYR CG  CD2  sing Y N 378 
TYR CD1 CE1  sing Y N 379 
TYR CD1 HD1  sing N N 380 
TYR CD2 CE2  doub Y N 381 
TYR CD2 HD2  sing N N 382 
TYR CE1 CZ   doub Y N 383 
TYR CE1 HE1  sing N N 384 
TYR CE2 CZ   sing Y N 385 
TYR CE2 HE2  sing N N 386 
TYR CZ  OH   sing N N 387 
TYR OH  HH   sing N N 388 
TYR OXT HXT  sing N N 389 
VAL N   CA   sing N N 390 
VAL N   H    sing N N 391 
VAL N   H2   sing N N 392 
VAL CA  C    sing N N 393 
VAL CA  CB   sing N N 394 
VAL CA  HA   sing N N 395 
VAL C   O    doub N N 396 
VAL C   OXT  sing N N 397 
VAL CB  CG1  sing N N 398 
VAL CB  CG2  sing N N 399 
VAL CB  HB   sing N N 400 
VAL CG1 HG11 sing N N 401 
VAL CG1 HG12 sing N N 402 
VAL CG1 HG13 sing N N 403 
VAL CG2 HG21 sing N N 404 
VAL CG2 HG22 sing N N 405 
VAL CG2 HG23 sing N N 406 
VAL OXT HXT  sing N N 407 
VD9 C14 C13  sing N N 408 
VD9 O4  S2   doub N N 409 
VD9 C13 C12  sing N N 410 
VD9 S2  O1   doub N N 411 
VD9 S2  C5   sing N N 412 
VD9 S2  N3   sing N N 413 
VD9 C10 C5   doub Y N 414 
VD9 C10 C9   sing Y N 415 
VD9 C5  C6   sing Y N 416 
VD9 C12 S11  sing N N 417 
VD9 C9  C8   doub Y N 418 
VD9 C6  C7   doub Y N 419 
VD9 C8  C7   sing Y N 420 
VD9 C8  S11  sing N N 421 
VD9 N3  H1   sing N N 422 
VD9 N3  H2   sing N N 423 
VD9 C10 H3   sing N N 424 
VD9 C9  H4   sing N N 425 
VD9 C7  H5   sing N N 426 
VD9 C6  H6   sing N N 427 
VD9 C12 H7   sing N N 428 
VD9 C12 H8   sing N N 429 
VD9 C13 H9   sing N N 430 
VD9 C13 H10  sing N N 431 
VD9 C14 H11  sing N N 432 
VD9 C14 H12  sing N N 433 
VD9 C14 H13  sing N N 434 
# 
_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   4HT0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    5LLG 
_atom_sites.fract_transf_matrix[1][1]   0.023744 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006028 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024314 
_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]   0.014365 
_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  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 11.033  -0.330  8.009   1.00 32.44  ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 9.836   0.147   8.674   1.00 27.89  ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.124   -0.940  9.419   1.00 22.31  ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.326   -2.155  9.177   1.00 23.00  ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 8.920   0.851   7.712   1.00 41.03  ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 8.546   2.209   8.174   1.00 44.05  ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 7.826   3.052   7.417   1.00 69.18  ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 8.805   2.869   9.370   1.00 53.56  ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 7.626   4.205   8.094   1.00 87.79  ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 8.222   4.091   9.293   1.00 85.51  ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.276   -0.562  10.338  1.00 17.67  ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.616   -1.533  11.188  1.00 15.20  ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.621   -2.351  10.389  1.00 15.49  ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.042   -1.866  9.393   1.00 17.90  ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 6.980   -0.842  12.392  1.00 14.96  ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 5.813   0.014   12.030  1.00 13.50  ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 5.781   1.359   11.731  1.00 15.35  ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.436   -0.437  11.974  1.00 13.14  ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.516   1.779   11.478  1.00 15.99  ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.670   0.693   11.574  1.00 14.54  ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 3.797   -1.653  12.188  1.00 14.02  ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.301   0.638   11.455  1.00 15.28  ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.423   -1.727  12.009  1.00 14.43  ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.703   -0.584  11.667  1.00 16.06  ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.315   -3.555  10.895  1.00 14.61  ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.271   -4.342  10.250  1.00 15.12  ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 4.985   -5.486  11.180  1.00 14.55  ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 4.977   -5.382  12.403  1.00 14.24  ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 4.667   -6.644  10.557  1.00 16.54  ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.205   -7.826  11.332  1.00 18.03  ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.127   -9.031  11.047  1.00 25.62  ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 4.797   -10.147 11.513  1.00 40.39  ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 2.758   -8.158  11.081  1.00 16.57  ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 1.925   -7.032  11.660  1.00 12.94  ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.532   -7.085  13.041  1.00 12.51  ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.429   -6.013  10.866  1.00 13.89  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 0.705   -6.085  13.547  1.00 11.65  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.593   -5.065  11.379  1.00 12.89  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.244   -5.115  12.730  1.00 11.63  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.604  -4.163  13.179  1.00 12.84  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.229   -8.810  10.330  1.00 23.81  ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.138   -9.941  10.070  1.00 29.16  ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.080   -10.307 11.222  1.00 24.19  ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.289   -9.672  12.325  1.00 28.50  ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 8.923   -11.240 10.860  1.00 36.76  ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 9.941   -11.696 11.830  1.00 36.99  ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 10.912  -10.601 12.019  1.00 35.06  ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.466  -10.361 13.166  1.00 32.03  ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 10.694  -12.937 11.315  1.00 51.05  ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 11.705  -13.448 12.314  1.00 40.22  ? 9   LYS A CG  1 
ATOM   51   N  NZ  . LYS A 1 9   ? 14.161  -15.191 13.360  0.00 70.78  ? 9   LYS A NZ  1 
ATOM   52   N  N   . HIS A 1 10  ? 11.166  -9.850  10.935  1.00 20.24  ? 10  HIS A N   1 
ATOM   53   C  CA  . HIS A 1 10  ? 12.164  -8.882  11.181  1.00 19.37  ? 10  HIS A CA  1 
ATOM   54   C  C   . HIS A 1 10  ? 11.709  -7.552  11.638  1.00 19.16  ? 10  HIS A C   1 
ATOM   55   O  O   . HIS A 1 10  ? 12.551  -6.762  12.050  1.00 23.17  ? 10  HIS A O   1 
ATOM   56   C  CB  . HIS A 1 10  ? 13.065  -8.832  9.964   1.00 20.74  ? 10  HIS A CB  1 
ATOM   57   C  CG  . HIS A 1 10  ? 13.628  -10.214 9.621   1.00 19.10  ? 10  HIS A CG  1 
ATOM   58   N  ND1 . HIS A 1 10  ? 14.506  -10.853 10.423  1.00 22.22  ? 10  HIS A ND1 1 
ATOM   59   C  CD2 . HIS A 1 10  ? 13.325  -11.107 8.590   1.00 23.89  ? 10  HIS A CD2 1 
ATOM   60   C  CE1 . HIS A 1 10  ? 14.792  -12.067 9.907   1.00 18.35  ? 10  HIS A CE1 1 
ATOM   61   N  NE2 . HIS A 1 10  ? 14.071  -12.222 8.786   1.00 27.22  ? 10  HIS A NE2 1 
ATOM   62   N  N   . ASN A 1 11  ? 10.409  -7.255  11.560  1.00 18.53  ? 11  ASN A N   1 
ATOM   63   C  CA  . ASN A 1 11  ? 9.924   -5.931  11.848  1.00 16.81  ? 11  ASN A CA  1 
ATOM   64   C  C   . ASN A 1 11  ? 8.655   -5.925  12.652  1.00 14.73  ? 11  ASN A C   1 
ATOM   65   O  O   . ASN A 1 11  ? 8.006   -4.892  12.785  1.00 15.63  ? 11  ASN A O   1 
ATOM   66   C  CB  . ASN A 1 11  ? 9.730   -5.151  10.589  1.00 16.44  ? 11  ASN A CB  1 
ATOM   67   C  CG  . ASN A 1 11  ? 8.655   -5.685  9.665   1.00 17.57  ? 11  ASN A CG  1 
ATOM   68   O  OD1 . ASN A 1 11  ? 8.081   -6.757  9.931   1.00 18.29  ? 11  ASN A OD1 1 
ATOM   69   N  ND2 . ASN A 1 11  ? 8.371   -4.983  8.581   1.00 20.96  ? 11  ASN A ND2 1 
ATOM   70   N  N   . GLY A 1 12  ? 8.356   -7.053  13.315  1.00 15.91  ? 12  GLY A N   1 
ATOM   71   C  CA  . GLY A 1 12  ? 7.076   -7.191  13.979  1.00 14.91  ? 12  GLY A CA  1 
ATOM   72   C  C   . GLY A 1 12  ? 7.087   -6.684  15.385  1.00 13.40  ? 12  GLY A C   1 
ATOM   73   O  O   . GLY A 1 12  ? 8.021   -5.951  15.827  1.00 13.93  ? 12  GLY A O   1 
ATOM   74   N  N   . PRO A 1 13  ? 6.002   -6.901  16.138  1.00 12.25  ? 13  PRO A N   1 
ATOM   75   C  CA  . PRO A 1 13  ? 5.780   -6.364  17.469  1.00 13.40  ? 13  PRO A CA  1 
ATOM   76   C  C   . PRO A 1 13  ? 6.917   -6.387  18.435  1.00 12.62  ? 13  PRO A C   1 
ATOM   77   O  O   . PRO A 1 13  ? 7.091   -5.432  19.236  1.00 13.69  ? 13  PRO A O   1 
ATOM   78   C  CB  . PRO A 1 13  ? 4.573   -7.158  17.982  1.00 14.36  ? 13  PRO A CB  1 
ATOM   79   C  CG  . PRO A 1 13  ? 3.778   -7.404  16.768  1.00 13.19  ? 13  PRO A CG  1 
ATOM   80   C  CD  . PRO A 1 13  ? 4.815   -7.663  15.685  1.00 13.92  ? 13  PRO A CD  1 
ATOM   81   N  N   . GLU A 1 14  ? 7.731   -7.425  18.429  1.00 13.98  ? 14  GLU A N   1 
ATOM   82   C  CA  . GLU A 1 14  ? 8.829   -7.461  19.350  1.00 16.05  ? 14  GLU A CA  1 
ATOM   83   C  C   . GLU A 1 14  ? 9.950   -6.459  19.015  1.00 14.73  ? 14  GLU A C   1 
ATOM   84   O  O   . GLU A 1 14  ? 10.802  -6.212  19.870  1.00 16.34  ? 14  GLU A O   1 
ATOM   85   C  CB  . GLU A 1 14  ? 9.336   -8.882  19.417  1.00 22.81  ? 14  GLU A CB  1 
ATOM   86   C  CG  . GLU A 1 14  ? 9.941   -9.398  18.091  1.00 26.97  ? 14  GLU A CG  1 
ATOM   87   C  CD  . GLU A 1 14  ? 9.110   -9.978  16.867  1.00 30.70  ? 14  GLU A CD  1 
ATOM   88   O  OE1 . GLU A 1 14  ? 7.932   -9.593  16.710  1.00 24.54  ? 14  GLU A OE1 1 
ATOM   89   O  OE2 . GLU A 1 14  ? 9.664   -10.798 16.106  1.00 27.96  ? 14  GLU A OE2 1 
ATOM   90   N  N   . HIS A 1 15  ? 9.937   -5.910  17.816  1.00 13.67  ? 15  HIS A N   1 
ATOM   91   C  CA  . HIS A 1 15  ? 10.928  -4.897  17.406  1.00 13.35  ? 15  HIS A CA  1 
ATOM   92   C  C   . HIS A 1 15  ? 10.468  -3.476  17.584  1.00 12.57  ? 15  HIS A C   1 
ATOM   93   O  O   . HIS A 1 15  ? 11.305  -2.555  17.523  1.00 13.85  ? 15  HIS A O   1 
ATOM   94   C  CB  . HIS A 1 15  ? 11.269  -5.079  15.931  1.00 15.17  ? 15  HIS A CB  1 
ATOM   95   C  CG  . HIS A 1 15  ? 11.977  -6.350  15.683  1.00 17.13  ? 15  HIS A CG  1 
ATOM   96   N  ND1 . HIS A 1 15  ? 13.353  -6.442  15.787  1.00 20.48  ? 15  HIS A ND1 1 
ATOM   97   C  CD2 . HIS A 1 15  ? 11.493  -7.608  15.264  1.00 18.20  ? 15  HIS A CD2 1 
ATOM   98   C  CE1 . HIS A 1 15  ? 13.675  -7.716  15.583  1.00 27.51  ? 15  HIS A CE1 1 
ATOM   99   N  NE2 . HIS A 1 15  ? 12.590  -8.412  15.184  1.00 23.80  ? 15  HIS A NE2 1 
ATOM   100  N  N   . TRP A 1 16  ? 9.181   -3.225  17.754  1.00 12.61  ? 16  TRP A N   1 
ATOM   101  C  CA  . TRP A 1 16  ? 8.650   -1.884  17.675  1.00 11.61  ? 16  TRP A CA  1 
ATOM   102  C  C   . TRP A 1 16  ? 9.223   -0.922  18.694  1.00 12.31  ? 16  TRP A C   1 
ATOM   103  O  O   . TRP A 1 16  ? 9.362   0.280   18.449  1.00 12.98  ? 16  TRP A O   1 
ATOM   104  C  CB  . TRP A 1 16  ? 7.136   -1.935  17.829  1.00 11.30  ? 16  TRP A CB  1 
ATOM   105  C  CG  . TRP A 1 16  ? 6.436   -2.616  16.693  1.00 10.64  ? 16  TRP A CG  1 
ATOM   106  C  CD1 . TRP A 1 16  ? 6.938   -3.037  15.492  1.00 11.76  ? 16  TRP A CD1 1 
ATOM   107  C  CD2 . TRP A 1 16  ? 5.008   -2.920  16.664  1.00 11.29  ? 16  TRP A CD2 1 
ATOM   108  N  NE1 . TRP A 1 16  ? 5.950   -3.643  14.754  1.00 12.43  ? 16  TRP A NE1 1 
ATOM   109  C  CE2 . TRP A 1 16  ? 4.743   -3.555  15.411  1.00 11.43  ? 16  TRP A CE2 1 
ATOM   110  C  CE3 . TRP A 1 16  ? 3.982   -2.746  17.584  1.00 11.15  ? 16  TRP A CE3 1 
ATOM   111  C  CZ2 . TRP A 1 16  ? 3.489   -4.008  15.052  1.00 10.93  ? 16  TRP A CZ2 1 
ATOM   112  C  CZ3 . TRP A 1 16  ? 2.719   -3.161  17.210  1.00 10.66  ? 16  TRP A CZ3 1 
ATOM   113  C  CH2 . TRP A 1 16  ? 2.477   -3.747  15.966  1.00 11.65  ? 16  TRP A CH2 1 
ATOM   114  N  N   . HIS A 1 17  ? 9.610   -1.424  19.867  1.00 11.69  ? 17  HIS A N   1 
ATOM   115  C  CA  . HIS A 1 17  ? 10.102  -0.612  20.921  1.00 12.31  ? 17  HIS A CA  1 
ATOM   116  C  C   . HIS A 1 17  ? 11.356  0.185   20.561  1.00 13.30  ? 17  HIS A C   1 
ATOM   117  O  O   . HIS A 1 17  ? 11.624  1.249   21.134  1.00 14.05  ? 17  HIS A O   1 
ATOM   118  C  CB  . HIS A 1 17  ? 10.375  -1.364  22.222  1.00 13.37  ? 17  HIS A CB  1 
ATOM   119  C  CG  . HIS A 1 17  ? 11.566  -2.233  22.130  1.00 14.32  ? 17  HIS A CG  1 
ATOM   120  N  ND1 . HIS A 1 17  ? 12.771  -1.836  22.617  1.00 16.07  ? 17  HIS A ND1 1 
ATOM   121  C  CD2 . HIS A 1 17  ? 11.747  -3.448  21.527  1.00 15.48  ? 17  HIS A CD2 1 
ATOM   122  C  CE1 . HIS A 1 17  ? 13.660  -2.767  22.368  1.00 17.05  ? 17  HIS A CE1 1 
ATOM   123  N  NE2 . HIS A 1 17  ? 13.076  -3.786  21.723  1.00 16.92  ? 17  HIS A NE2 1 
ATOM   124  N  N   . LYS A 1 18  ? 12.118  -0.315  19.583  1.00 14.01  ? 18  LYS A N   1 
ATOM   125  C  CA  . LYS A 1 18  ? 13.362  0.387   19.263  1.00 15.38  ? 18  LYS A CA  1 
ATOM   126  C  C   . LYS A 1 18  ? 13.058  1.717   18.564  1.00 15.22  ? 18  LYS A C   1 
ATOM   127  O  O   . LYS A 1 18  ? 13.846  2.631   18.643  1.00 20.26  ? 18  LYS A O   1 
ATOM   128  C  CB  . LYS A 1 18  ? 14.182  -0.505  18.336  1.00 15.99  ? 18  LYS A CB  1 
ATOM   129  C  CG  . LYS A 1 18  ? 14.759  -1.716  19.060  1.00 17.76  ? 18  LYS A CG  1 
ATOM   130  C  CD  . LYS A 1 18  ? 15.470  -2.679  18.131  1.00 16.86  ? 18  LYS A CD  1 
ATOM   131  C  CE  . LYS A 1 18  ? 14.523  -3.641  17.415  1.00 17.01  ? 18  LYS A CE  1 
ATOM   132  N  NZ  . LYS A 1 18  ? 15.227  -4.423  16.322  1.00 18.18  ? 18  LYS A NZ  1 
ATOM   133  N  N   . ASP A 1 19  ? 11.977  1.834   17.767  1.00 14.24  ? 19  ASP A N   1 
ATOM   134  C  CA  . ASP A 1 19  ? 11.584  3.101   17.184  1.00 14.43  ? 19  ASP A CA  1 
ATOM   135  C  C   . ASP A 1 19  ? 10.505  3.820   17.954  1.00 14.30  ? 19  ASP A C   1 
ATOM   136  O  O   . ASP A 1 19  ? 10.375  5.021   17.828  1.00 16.68  ? 19  ASP A O   1 
ATOM   137  C  CB  . ASP A 1 19  ? 11.258  2.915   15.680  1.00 16.14  ? 19  ASP A CB  1 
ATOM   138  C  CG  . ASP A 1 19  ? 12.523  2.738   14.890  1.00 22.08  ? 19  ASP A CG  1 
ATOM   139  O  OD1 . ASP A 1 19  ? 13.269  3.705   14.679  1.00 21.47  ? 19  ASP A OD1 1 
ATOM   140  O  OD2 . ASP A 1 19  ? 12.907  1.565   14.696  1.00 26.22  ? 19  ASP A OD2 1 
ATOM   141  N  N   . PHE A 1 20  ? 9.804   3.054   18.790  1.00 13.82  ? 20  PHE A N   1 
ATOM   142  C  CA  . PHE A 1 20  ? 8.665   3.625   19.491  1.00 14.00  ? 20  PHE A CA  1 
ATOM   143  C  C   . PHE A 1 20  ? 8.755   3.126   20.966  1.00 13.26  ? 20  PHE A C   1 
ATOM   144  O  O   . PHE A 1 20  ? 8.094   2.145   21.327  1.00 13.26  ? 20  PHE A O   1 
ATOM   145  C  CB  . PHE A 1 20  ? 7.359   3.124   18.844  1.00 13.55  ? 20  PHE A CB  1 
ATOM   146  C  CG  . PHE A 1 20  ? 7.284   3.492   17.406  1.00 13.53  ? 20  PHE A CG  1 
ATOM   147  C  CD1 . PHE A 1 20  ? 6.867   4.768   17.052  1.00 15.82  ? 20  PHE A CD1 1 
ATOM   148  C  CD2 . PHE A 1 20  ? 7.713   2.578   16.394  1.00 15.73  ? 20  PHE A CD2 1 
ATOM   149  C  CE1 . PHE A 1 20  ? 6.918   5.106   15.706  1.00 17.05  ? 20  PHE A CE1 1 
ATOM   150  C  CE2 . PHE A 1 20  ? 7.743   2.884   15.070  1.00 16.44  ? 20  PHE A CE2 1 
ATOM   151  C  CZ  . PHE A 1 20  ? 7.307   4.181   14.697  1.00 17.40  ? 20  PHE A CZ  1 
ATOM   152  N  N   . PRO A 1 21  ? 9.641   3.733   21.772  1.00 14.61  ? 21  PRO A N   1 
ATOM   153  C  CA  . PRO A 1 21  ? 9.898   3.210   23.083  1.00 14.30  ? 21  PRO A CA  1 
ATOM   154  C  C   . PRO A 1 21  ? 8.678   3.159   24.017  1.00 13.86  ? 21  PRO A C   1 
ATOM   155  O  O   . PRO A 1 21  ? 8.690   2.386   24.992  1.00 13.82  ? 21  PRO A O   1 
ATOM   156  C  CB  . PRO A 1 21  ? 11.011  4.103   23.729  1.00 19.30  ? 21  PRO A CB  1 
ATOM   157  C  CG  . PRO A 1 21  ? 11.167  5.201   22.741  1.00 24.28  ? 21  PRO A CG  1 
ATOM   158  C  CD  . PRO A 1 21  ? 10.564  4.828   21.422  1.00 16.97  ? 21  PRO A CD  1 
ATOM   159  N  N   A ILE A 1 22  ? 7.611   3.915   23.730  0.50 12.88  ? 22  ILE A N   1 
ATOM   160  N  N   B ILE A 1 22  ? 7.612   3.921   23.734  0.50 12.96  ? 22  ILE A N   1 
ATOM   161  C  CA  A ILE A 1 22  ? 6.357   3.795   24.495  0.50 13.11  ? 22  ILE A CA  1 
ATOM   162  C  CA  B ILE A 1 22  ? 6.345   3.811   24.490  0.50 13.08  ? 22  ILE A CA  1 
ATOM   163  C  C   A ILE A 1 22  ? 5.744   2.377   24.407  0.50 11.71  ? 22  ILE A C   1 
ATOM   164  C  C   B ILE A 1 22  ? 5.742   2.381   24.406  0.50 11.65  ? 22  ILE A C   1 
ATOM   165  O  O   A ILE A 1 22  ? 4.870   2.025   25.172  0.50 12.30  ? 22  ILE A O   1 
ATOM   166  O  O   B ILE A 1 22  ? 4.872   2.026   25.175  0.50 12.51  ? 22  ILE A O   1 
ATOM   167  C  CB  A ILE A 1 22  ? 5.369   4.875   24.070  0.50 12.40  ? 22  ILE A CB  1 
ATOM   168  C  CB  B ILE A 1 22  ? 5.358   4.885   24.031  0.50 13.15  ? 22  ILE A CB  1 
ATOM   169  C  CG1 A ILE A 1 22  ? 4.339   5.166   25.146  0.50 14.62  ? 22  ILE A CG1 1 
ATOM   170  C  CG1 B ILE A 1 22  ? 4.272   5.166   25.061  0.50 16.01  ? 22  ILE A CG1 1 
ATOM   171  C  CG2 A ILE A 1 22  ? 4.774   4.517   22.718  0.50 13.40  ? 22  ILE A CG2 1 
ATOM   172  C  CG2 B ILE A 1 22  ? 4.799   4.491   22.681  0.50 13.13  ? 22  ILE A CG2 1 
ATOM   173  C  CD1 A ILE A 1 22  ? 3.399   6.287   24.744  0.50 13.69  ? 22  ILE A CD1 1 
ATOM   174  C  CD1 B ILE A 1 22  ? 4.785   5.790   26.338  0.50 19.22  ? 22  ILE A CD1 1 
ATOM   175  N  N   . ALA A 1 23  ? 6.269   1.533   23.501  1.00 12.21  ? 23  ALA A N   1 
ATOM   176  C  CA  . ALA A 1 23  ? 5.818   0.167   23.388  1.00 11.96  ? 23  ALA A CA  1 
ATOM   177  C  C   . ALA A 1 23  ? 5.915   -0.555  24.724  1.00 12.34  ? 23  ALA A C   1 
ATOM   178  O  O   . ALA A 1 23  ? 5.224   -1.560  24.885  1.00 11.95  ? 23  ALA A O   1 
ATOM   179  C  CB  . ALA A 1 23  ? 6.694   -0.577  22.374  1.00 12.64  ? 23  ALA A CB  1 
ATOM   180  N  N   . LYS A 1 24  ? 6.846   -0.140  25.608  1.00 13.39  ? 24  LYS A N   1 
ATOM   181  C  CA  . LYS A 1 24  ? 7.074   -0.718  26.923  1.00 13.50  ? 24  LYS A CA  1 
ATOM   182  C  C   . LYS A 1 24  ? 6.456   0.163   27.985  1.00 15.26  ? 24  LYS A C   1 
ATOM   183  O  O   . LYS A 1 24  ? 6.847   0.072   29.154  1.00 16.82  ? 24  LYS A O   1 
ATOM   184  C  CB  . LYS A 1 24  ? 8.546   -1.010  27.191  1.00 15.28  ? 24  LYS A CB  1 
ATOM   185  C  CG  . LYS A 1 24  ? 9.149   -2.005  26.231  1.00 17.03  ? 24  LYS A CG  1 
ATOM   186  C  CD  . LYS A 1 24  ? 10.647  -2.169  26.584  1.00 21.35  ? 24  LYS A CD  1 
ATOM   187  C  CE  . LYS A 1 24  ? 11.374  -3.136  25.675  1.00 25.43  ? 24  LYS A CE  1 
ATOM   188  N  NZ  . LYS A 1 24  ? 11.014  -4.530  25.998  1.00 39.34  ? 24  LYS A NZ  1 
ATOM   189  N  N   . GLY A 1 25  ? 5.427   0.965   27.635  1.00 13.85  ? 25  GLY A N   1 
ATOM   190  C  CA  . GLY A 1 25  ? 4.812   1.943   28.544  1.00 15.80  ? 25  GLY A CA  1 
ATOM   191  C  C   . GLY A 1 25  ? 3.851   1.279   29.543  1.00 13.29  ? 25  GLY A C   1 
ATOM   192  O  O   . GLY A 1 25  ? 3.667   0.046   29.630  1.00 14.34  ? 25  GLY A O   1 
ATOM   193  N  N   . GLU A 1 26  ? 3.193   2.168   30.262  1.00 14.08  ? 26  GLU A N   1 
ATOM   194  C  CA  . GLU A 1 26  ? 2.369   1.816   31.350  1.00 14.88  ? 26  GLU A CA  1 
ATOM   195  C  C   . GLU A 1 26  ? 0.917   1.559   30.975  1.00 13.41  ? 26  GLU A C   1 
ATOM   196  O  O   . GLU A 1 26  ? 0.177   1.046   31.805  1.00 14.73  ? 26  GLU A O   1 
ATOM   197  C  CB  . GLU A 1 26  ? 2.370   2.927   32.442  1.00 19.82  ? 26  GLU A CB  1 
ATOM   198  C  CG  . GLU A 1 26  ? 3.791   3.158   33.008  1.00 20.70  ? 26  GLU A CG  1 
ATOM   199  C  CD  . GLU A 1 26  ? 4.359   1.883   33.663  1.00 28.30  ? 26  GLU A CD  1 
ATOM   200  O  OE1 . GLU A 1 26  ? 3.673   1.236   34.531  1.00 32.39  ? 26  GLU A OE1 1 
ATOM   201  O  OE2 . GLU A 1 26  ? 5.484   1.518   33.292  1.00 40.15  ? 26  GLU A OE2 1 
ATOM   202  N  N   . ARG A 1 27  ? 0.510   1.895   29.756  1.00 11.44  ? 27  ARG A N   1 
ATOM   203  C  CA  . ARG A 1 27  ? -0.853  1.653   29.380  1.00 10.35  ? 27  ARG A CA  1 
ATOM   204  C  C   . ARG A 1 27  ? -0.960  1.200   27.909  1.00 9.71   ? 27  ARG A C   1 
ATOM   205  O  O   . ARG A 1 27  ? -1.683  1.807   27.109  1.00 9.96   ? 27  ARG A O   1 
ATOM   206  C  CB  . ARG A 1 27  ? -1.786  2.868   29.672  1.00 13.18  ? 27  ARG A CB  1 
ATOM   207  C  CG  . ARG A 1 27  ? -1.473  4.199   29.113  1.00 16.00  ? 27  ARG A CG  1 
ATOM   208  C  CD  . ARG A 1 27  ? -2.515  5.301   29.317  1.00 20.47  ? 27  ARG A CD  1 
ATOM   209  N  NE  . ARG A 1 27  ? -3.660  5.236   28.407  1.00 15.27  ? 27  ARG A NE  1 
ATOM   210  C  CZ  . ARG A 1 27  ? -4.573  6.196   28.291  1.00 14.13  ? 27  ARG A CZ  1 
ATOM   211  N  NH1 . ARG A 1 27  ? -4.474  7.294   29.019  1.00 17.55  ? 27  ARG A NH1 1 
ATOM   212  N  NH2 . ARG A 1 27  ? -5.585  6.059   27.445  1.00 15.31  ? 27  ARG A NH2 1 
ATOM   213  N  N   . GLN A 1 28  ? -0.228  0.125   27.619  1.00 9.26   ? 28  GLN A N   1 
ATOM   214  C  CA  . GLN A 1 28  ? -0.227  -0.395  26.276  1.00 9.10   ? 28  GLN A CA  1 
ATOM   215  C  C   . GLN A 1 28  ? -1.392  -1.365  26.011  1.00 8.82   ? 28  GLN A C   1 
ATOM   216  O  O   . GLN A 1 28  ? -1.891  -2.041  26.910  1.00 9.72   ? 28  GLN A O   1 
ATOM   217  C  CB  . GLN A 1 28  ? 1.122   -1.063  26.009  1.00 9.96   ? 28  GLN A CB  1 
ATOM   218  C  CG  . GLN A 1 28  ? 2.267   -0.026  25.913  1.00 10.49  ? 28  GLN A CG  1 
ATOM   219  C  CD  . GLN A 1 28  ? 2.133   0.770   24.632  1.00 10.42  ? 28  GLN A CD  1 
ATOM   220  O  OE1 . GLN A 1 28  ? 2.293   0.237   23.544  1.00 10.04  ? 28  GLN A OE1 1 
ATOM   221  N  NE2 . GLN A 1 28  ? 1.793   2.069   24.738  1.00 9.87   ? 28  GLN A NE2 1 
ATOM   222  N  N   . SER A 1 29  ? -1.770  -1.439  24.730  1.00 8.28   ? 29  SER A N   1 
ATOM   223  C  CA  . SER A 1 29  ? -2.816  -2.319  24.278  1.00 8.24   ? 29  SER A CA  1 
ATOM   224  C  C   . SER A 1 29  ? -2.277  -3.206  23.143  1.00 8.26   ? 29  SER A C   1 
ATOM   225  O  O   . SER A 1 29  ? -1.349  -2.841  22.441  1.00 8.85   ? 29  SER A O   1 
ATOM   226  C  CB  . SER A 1 29  ? -3.943  -1.448  23.729  1.00 8.76   ? 29  SER A CB  1 
ATOM   227  O  OG  . SER A 1 29  ? -4.568  -0.747  24.798  1.00 8.58   ? 29  SER A OG  1 
ATOM   228  N  N   . PRO A 1 30  ? -2.945  -4.344  22.899  1.00 8.18   ? 30  PRO A N   1 
ATOM   229  C  CA  . PRO A 1 30  ? -4.110  -4.879  23.603  1.00 8.14   ? 30  PRO A CA  1 
ATOM   230  C  C   . PRO A 1 30  ? -3.686  -5.523  24.923  1.00 8.05   ? 30  PRO A C   1 
ATOM   231  O  O   . PRO A 1 30  ? -2.501  -5.581  25.249  1.00 8.78   ? 30  PRO A O   1 
ATOM   232  C  CB  . PRO A 1 30  ? -4.660  -5.918  22.623  1.00 8.37   ? 30  PRO A CB  1 
ATOM   233  C  CG  . PRO A 1 30  ? -3.360  -6.473  22.004  1.00 9.01   ? 30  PRO A CG  1 
ATOM   234  C  CD  . PRO A 1 30  ? -2.472  -5.252  21.847  1.00 9.05   ? 30  PRO A CD  1 
ATOM   235  N  N   . VAL A 1 31  ? -4.674  -6.082  25.612  1.00 8.72   ? 31  VAL A N   1 
ATOM   236  C  CA  . VAL A 1 31  ? -4.494  -6.827  26.850  1.00 8.65   ? 31  VAL A CA  1 
ATOM   237  C  C   . VAL A 1 31  ? -5.374  -8.040  26.796  1.00 9.36   ? 31  VAL A C   1 
ATOM   238  O  O   . VAL A 1 31  ? -6.363  -8.099  26.041  1.00 9.68   ? 31  VAL A O   1 
ATOM   239  C  CB  . VAL A 1 31  ? -4.811  -5.997  28.116  1.00 10.04  ? 31  VAL A CB  1 
ATOM   240  C  CG1 . VAL A 1 31  ? -3.859  -4.795  28.174  1.00 10.76  ? 31  VAL A CG1 1 
ATOM   241  C  CG2 . VAL A 1 31  ? -6.268  -5.566  28.169  1.00 10.59  ? 31  VAL A CG2 1 
ATOM   242  N  N   . ASP A 1 32  ? -5.056  -9.037  27.654  1.00 9.53   ? 32  ASP A N   1 
ATOM   243  C  CA  . ASP A 1 32  ? -5.935  -10.126 27.938  1.00 9.85   ? 32  ASP A CA  1 
ATOM   244  C  C   . ASP A 1 32  ? -7.000  -9.614  28.912  1.00 10.19  ? 32  ASP A C   1 
ATOM   245  O  O   . ASP A 1 32  ? -6.687  -8.949  29.902  1.00 11.45  ? 32  ASP A O   1 
ATOM   246  C  CB  . ASP A 1 32  ? -5.205  -11.295 28.534  1.00 11.02  ? 32  ASP A CB  1 
ATOM   247  C  CG  . ASP A 1 32  ? -6.146  -12.449 28.834  1.00 11.02  ? 32  ASP A CG  1 
ATOM   248  O  OD1 . ASP A 1 32  ? -6.836  -12.917 27.921  1.00 11.02  ? 32  ASP A OD1 1 
ATOM   249  O  OD2 . ASP A 1 32  ? -6.223  -12.874 30.033  1.00 14.03  ? 32  ASP A OD2 1 
ATOM   250  N  N   . ILE A 1 33  ? -8.254  -9.915  28.610  1.00 9.40   ? 33  ILE A N   1 
ATOM   251  C  CA  . ILE A 1 33  ? -9.380  -9.542  29.482  1.00 10.46  ? 33  ILE A CA  1 
ATOM   252  C  C   . ILE A 1 33  ? -9.679  -10.794 30.325  1.00 10.97  ? 33  ILE A C   1 
ATOM   253  O  O   . ILE A 1 33  ? -10.226 -11.774 29.859  1.00 12.10  ? 33  ILE A O   1 
ATOM   254  C  CB  . ILE A 1 33  ? -10.586 -9.118  28.666  1.00 10.59  ? 33  ILE A CB  1 
ATOM   255  C  CG1 . ILE A 1 33  ? -10.228 -7.896  27.835  1.00 10.99  ? 33  ILE A CG1 1 
ATOM   256  C  CG2 . ILE A 1 33  ? -11.789 -8.863  29.582  1.00 13.55  ? 33  ILE A CG2 1 
ATOM   257  C  CD1 . ILE A 1 33  ? -11.292 -7.565  26.719  1.00 13.21  ? 33  ILE A CD1 1 
ATOM   258  N  N   A ASP A 1 34  ? -9.293  -10.739 31.588  0.50 13.15  ? 34  ASP A N   1 
ATOM   259  N  N   B ASP A 1 34  ? -9.319  -10.678 31.606  0.50 11.75  ? 34  ASP A N   1 
ATOM   260  C  CA  A ASP A 1 34  ? -9.581  -11.846 32.499  0.50 13.29  ? 34  ASP A CA  1 
ATOM   261  C  CA  B ASP A 1 34  ? -9.611  -11.717 32.620  0.50 12.60  ? 34  ASP A CA  1 
ATOM   262  C  C   A ASP A 1 34  ? -10.960 -11.540 33.063  0.50 14.34  ? 34  ASP A C   1 
ATOM   263  C  C   B ASP A 1 34  ? -11.062 -11.478 33.054  0.50 12.53  ? 34  ASP A C   1 
ATOM   264  O  O   A ASP A 1 34  ? -11.086 -10.584 33.892  0.50 17.13  ? 34  ASP A O   1 
ATOM   265  O  O   B ASP A 1 34  ? -11.395 -10.519 33.762  0.50 13.25  ? 34  ASP A O   1 
ATOM   266  C  CB  A ASP A 1 34  ? -8.513  -11.922 33.588  0.50 13.73  ? 34  ASP A CB  1 
ATOM   267  C  CB  B ASP A 1 34  ? -8.617  -11.614 33.792  0.50 15.80  ? 34  ASP A CB  1 
ATOM   268  C  CG  A ASP A 1 34  ? -8.707  -13.123 34.486  0.50 17.92  ? 34  ASP A CG  1 
ATOM   269  C  CG  B ASP A 1 34  ? -8.812  -12.730 34.821  0.50 16.09  ? 34  ASP A CG  1 
ATOM   270  O  OD1 A ASP A 1 34  ? -9.318  -12.983 35.561  0.50 21.15  ? 34  ASP A OD1 1 
ATOM   271  O  OD1 B ASP A 1 34  ? -9.955  -13.187 34.963  0.50 14.15  ? 34  ASP A OD1 1 
ATOM   272  O  OD2 A ASP A 1 34  ? -8.274  -14.190 34.061  0.50 22.44  ? 34  ASP A OD2 1 
ATOM   273  O  OD2 B ASP A 1 34  ? -7.807  -13.080 35.471  0.50 20.51  ? 34  ASP A OD2 1 
ATOM   274  N  N   . THR A 1 35  ? -11.980 -12.283 32.599  1.00 14.95  ? 35  THR A N   1 
ATOM   275  C  CA  . THR A 1 35  ? -13.325 -11.947 32.819  1.00 14.43  ? 35  THR A CA  1 
ATOM   276  C  C   . THR A 1 35  ? -13.759 -12.118 34.246  1.00 14.23  ? 35  THR A C   1 
ATOM   277  O  O   . THR A 1 35  ? -14.665 -11.398 34.708  1.00 18.23  ? 35  THR A O   1 
ATOM   278  C  CB  . THR A 1 35  ? -14.280 -12.839 32.010  1.00 16.59  ? 35  THR A CB  1 
ATOM   279  O  OG1 . THR A 1 35  ? -14.122 -14.188 32.455  1.00 17.90  ? 35  THR A OG1 1 
ATOM   280  C  CG2 . THR A 1 35  ? -14.031 -12.702 30.537  1.00 18.07  ? 35  THR A CG2 1 
ATOM   281  N  N   . HIS A 1 36  ? -13.089 -12.998 34.998  1.00 16.82  ? 36  HIS A N   1 
ATOM   282  C  CA  . HIS A 1 36  ? -13.341 -13.122 36.366  1.00 17.24  ? 36  HIS A CA  1 
ATOM   283  C  C   . HIS A 1 36  ? -12.824 -11.979 37.179  1.00 18.90  ? 36  HIS A C   1 
ATOM   284  O  O   . HIS A 1 36  ? -13.499 -11.694 38.197  1.00 20.49  ? 36  HIS A O   1 
ATOM   285  C  CB  . HIS A 1 36  ? -12.839 -14.567 36.772  1.00 21.29  ? 36  HIS A CB  1 
ATOM   286  C  CG  . HIS A 1 36  ? -13.866 -15.683 36.337  1.00 18.50  ? 36  HIS A CG  1 
ATOM   287  N  ND1 . HIS A 1 36  ? -13.622 -16.641 35.319  1.00 22.67  ? 36  HIS A ND1 1 
ATOM   288  C  CD2 . HIS A 1 36  ? -15.244 -15.758 36.636  1.00 20.87  ? 36  HIS A CD2 1 
ATOM   289  C  CE1 . HIS A 1 36  ? -14.801 -17.320 35.110  1.00 26.93  ? 36  HIS A CE1 1 
ATOM   290  N  NE2 . HIS A 1 36  ? -15.766 -16.796 35.926  1.00 36.01  ? 36  HIS A NE2 1 
ATOM   291  N  N   . THR A 1 37  ? -11.690 -11.317 36.803  1.00 18.99  ? 37  THR A N   1 
ATOM   292  C  CA  . THR A 1 37  ? -11.146 -10.183 37.579  1.00 18.35  ? 37  THR A CA  1 
ATOM   293  C  C   . THR A 1 37  ? -11.685 -8.788  37.128  1.00 16.69  ? 37  THR A C   1 
ATOM   294  O  O   . THR A 1 37  ? -11.495 -7.808  37.825  1.00 20.77  ? 37  THR A O   1 
ATOM   295  C  CB  . THR A 1 37  ? -9.606  -10.165 37.550  1.00 23.79  ? 37  THR A CB  1 
ATOM   296  O  OG1 . THR A 1 37  ? -9.150  -10.147 36.191  1.00 28.27  ? 37  THR A OG1 1 
ATOM   297  C  CG2 . THR A 1 37  ? -9.045  -11.393 38.251  1.00 26.39  ? 37  THR A CG2 1 
ATOM   298  N  N   . ALA A 1 38  ? -12.347 -8.750  35.979  1.00 16.89  ? 38  ALA A N   1 
ATOM   299  C  CA  . ALA A 1 38  ? -12.968 -7.503  35.550  1.00 15.62  ? 38  ALA A CA  1 
ATOM   300  C  C   . ALA A 1 38  ? -14.095 -7.182  36.532  1.00 18.44  ? 38  ALA A C   1 
ATOM   301  O  O   . ALA A 1 38  ? -14.853 -8.020  36.905  1.00 25.83  ? 38  ALA A O   1 
ATOM   302  C  CB  . ALA A 1 38  ? -13.508 -7.652  34.175  1.00 15.10  ? 38  ALA A CB  1 
ATOM   303  N  N   A LYS A 1 39  ? -14.121 -5.920  36.928  0.50 18.43  ? 39  LYS A N   1 
ATOM   304  N  N   B LYS A 1 39  ? -14.175 -5.977  37.025  0.50 19.54  ? 39  LYS A N   1 
ATOM   305  C  CA  A LYS A 1 39  ? -15.008 -5.355  37.996  0.50 16.47  ? 39  LYS A CA  1 
ATOM   306  C  CA  B LYS A 1 39  ? -15.296 -5.791  37.947  0.50 21.05  ? 39  LYS A CA  1 
ATOM   307  C  C   A LYS A 1 39  ? -16.371 -4.922  37.339  0.50 16.99  ? 39  LYS A C   1 
ATOM   308  C  C   B LYS A 1 39  ? -16.397 -5.070  37.261  0.50 15.58  ? 39  LYS A C   1 
ATOM   309  O  O   A LYS A 1 39  ? -16.346 -3.980  36.555  0.50 15.31  ? 39  LYS A O   1 
ATOM   310  O  O   B LYS A 1 39  ? -16.234 -4.059  36.578  0.50 14.68  ? 39  LYS A O   1 
ATOM   311  C  CB  A LYS A 1 39  ? -14.278 -4.125  38.568  0.50 15.99  ? 39  LYS A CB  1 
ATOM   312  C  CB  B LYS A 1 39  ? -14.952 -5.020  39.198  0.50 19.21  ? 39  LYS A CB  1 
ATOM   313  C  CG  A LYS A 1 39  ? -14.954 -3.357  39.686  0.50 19.52  ? 39  LYS A CG  1 
ATOM   314  C  CG  B LYS A 1 39  ? -15.875 -5.078  40.419  0.50 18.72  ? 39  LYS A CG  1 
ATOM   315  C  CD  A LYS A 1 39  ? -15.324 -4.227  40.860  0.50 18.49  ? 39  LYS A CD  1 
ATOM   316  C  CD  B LYS A 1 39  ? -15.371 -4.006  41.386  0.50 23.03  ? 39  LYS A CD  1 
ATOM   317  C  CE  A LYS A 1 39  ? -15.839 -3.304  41.946  0.50 22.39  ? 39  LYS A CE  1 
ATOM   318  C  CE  B LYS A 1 39  ? -16.386 -3.594  42.447  0.50 30.83  ? 39  LYS A CE  1 
ATOM   319  N  NZ  A LYS A 1 39  ? -16.226 -4.096  43.114  0.50 26.68  ? 39  LYS A NZ  1 
ATOM   320  N  NZ  B LYS A 1 39  ? -16.816 -4.773  43.252  0.50 43.45  ? 39  LYS A NZ  1 
ATOM   321  N  N   . TYR A 1 40  ? -17.556 -5.489  37.674  1.00 18.26  ? 40  TYR A N   1 
ATOM   322  C  CA  . TYR A 1 40  ? -18.790 -4.884  37.235  1.00 16.84  ? 40  TYR A CA  1 
ATOM   323  C  C   . TYR A 1 40  ? -18.867 -3.493  37.827  1.00 16.37  ? 40  TYR A C   1 
ATOM   324  O  O   . TYR A 1 40  ? -18.697 -3.302  39.071  1.00 17.36  ? 40  TYR A O   1 
ATOM   325  C  CB  . TYR A 1 40  ? -20.001 -5.722  37.598  1.00 21.49  ? 40  TYR A CB  1 
ATOM   326  C  CG  . TYR A 1 40  ? -21.262 -4.939  37.485  1.00 22.70  ? 40  TYR A CG  1 
ATOM   327  C  CD1 . TYR A 1 40  ? -21.694 -4.499  36.246  1.00 20.07  ? 40  TYR A CD1 1 
ATOM   328  C  CD2 . TYR A 1 40  ? -22.115 -4.760  38.576  1.00 31.59  ? 40  TYR A CD2 1 
ATOM   329  C  CE1 . TYR A 1 40  ? -22.917 -3.809  36.081  1.00 24.62  ? 40  TYR A CE1 1 
ATOM   330  C  CE2 . TYR A 1 40  ? -23.320 -4.056  38.409  1.00 30.91  ? 40  TYR A CE2 1 
ATOM   331  C  CZ  . TYR A 1 40  ? -23.730 -3.578  37.173  1.00 28.02  ? 40  TYR A CZ  1 
ATOM   332  O  OH  . TYR A 1 40  ? -24.944 -2.924  37.005  1.00 30.62  ? 40  TYR A OH  1 
ATOM   333  N  N   . ASP A 1 41  ? -19.118 -2.494  37.005  1.00 14.81  ? 41  ASP A N   1 
ATOM   334  C  CA  . ASP A 1 41  ? -19.193 -1.088  37.521  1.00 15.51  ? 41  ASP A CA  1 
ATOM   335  C  C   . ASP A 1 41  ? -20.591 -0.570  37.257  1.00 17.31  ? 41  ASP A C   1 
ATOM   336  O  O   . ASP A 1 41  ? -20.913 -0.261  36.128  1.00 17.78  ? 41  ASP A O   1 
ATOM   337  C  CB  . ASP A 1 41  ? -18.151 -0.232  36.793  1.00 19.42  ? 41  ASP A CB  1 
ATOM   338  C  CG  . ASP A 1 41  ? -18.096 1.179   37.282  1.00 21.02  ? 41  ASP A CG  1 
ATOM   339  O  OD1 . ASP A 1 41  ? -18.992 1.567   38.081  1.00 22.43  ? 41  ASP A OD1 1 
ATOM   340  O  OD2 . ASP A 1 41  ? -17.093 1.886   36.934  1.00 24.63  ? 41  ASP A OD2 1 
ATOM   341  N  N   . PRO A 1 42  ? -21.444 -0.512  38.311  1.00 20.27  ? 42  PRO A N   1 
ATOM   342  C  CA  . PRO A 1 42  ? -22.805 -0.083  38.106  1.00 22.21  ? 42  PRO A CA  1 
ATOM   343  C  C   . PRO A 1 42  ? -22.888 1.382   37.699  1.00 23.11  ? 42  PRO A C   1 
ATOM   344  O  O   . PRO A 1 42  ? -23.956 1.848   37.281  1.00 31.55  ? 42  PRO A O   1 
ATOM   345  C  CB  . PRO A 1 42  ? -23.454 -0.353  39.475  1.00 35.81  ? 42  PRO A CB  1 
ATOM   346  C  CG  . PRO A 1 42  ? -22.328 -0.309  40.442  1.00 36.68  ? 42  PRO A CG  1 
ATOM   347  C  CD  . PRO A 1 42  ? -21.175 -0.911  39.695  1.00 24.04  ? 42  PRO A CD  1 
ATOM   348  N  N   . SER A 1 43  ? -21.807 2.151   37.805  1.00 22.44  ? 43  SER A N   1 
ATOM   349  C  CA  . SER A 1 43  ? -21.771 3.590   37.340  1.00 26.49  ? 43  SER A CA  1 
ATOM   350  C  C   . SER A 1 43  ? -21.571 3.724   35.820  1.00 21.02  ? 43  SER A C   1 
ATOM   351  O  O   . SER A 1 43  ? -21.748 4.825   35.225  1.00 30.19  ? 43  SER A O   1 
ATOM   352  C  CB  . SER A 1 43  ? -20.648 4.404   38.030  1.00 23.07  ? 43  SER A CB  1 
ATOM   353  O  OG  . SER A 1 43  ? -19.332 4.100   37.606  1.00 27.80  ? 43  SER A OG  1 
ATOM   354  N  N   . LEU A 1 44  ? -21.169 2.631   35.169  1.00 22.05  ? 44  LEU A N   1 
ATOM   355  C  CA  . LEU A 1 44  ? -20.993 2.672   33.699  1.00 19.54  ? 44  LEU A CA  1 
ATOM   356  C  C   . LEU A 1 44  ? -22.339 2.833   33.024  1.00 19.54  ? 44  LEU A C   1 
ATOM   357  O  O   . LEU A 1 44  ? -23.303 2.195   33.407  1.00 27.67  ? 44  LEU A O   1 
ATOM   358  C  CB  . LEU A 1 44  ? -20.272 1.422   33.186  1.00 17.71  ? 44  LEU A CB  1 
ATOM   359  C  CG  . LEU A 1 44  ? -18.819 1.411   33.421  1.00 16.21  ? 44  LEU A CG  1 
ATOM   360  C  CD1 . LEU A 1 44  ? -18.354 0.029   33.037  1.00 17.75  ? 44  LEU A CD1 1 
ATOM   361  C  CD2 . LEU A 1 44  ? -18.067 2.518   32.669  1.00 18.04  ? 44  LEU A CD2 1 
ATOM   362  N  N   . LYS A 1 45  ? -22.404 3.649   31.970  1.00 20.23  ? 45  LYS A N   1 
ATOM   363  C  CA  . LYS A 1 45  ? -23.682 3.848   31.291  1.00 20.12  ? 45  LYS A CA  1 
ATOM   364  C  C   . LYS A 1 45  ? -23.703 2.974   30.058  1.00 18.87  ? 45  LYS A C   1 
ATOM   365  O  O   . LYS A 1 45  ? -22.682 2.471   29.557  1.00 17.93  ? 45  LYS A O   1 
ATOM   366  C  CB  . LYS A 1 45  ? -23.800 5.234   30.826  1.00 19.96  ? 45  LYS A CB  1 
ATOM   367  C  CG  . LYS A 1 45  ? -23.443 6.313   31.817  1.00 26.42  ? 45  LYS A CG  1 
ATOM   368  C  CD  . LYS A 1 45  ? -24.298 7.550   31.665  1.00 47.98  ? 45  LYS A CD  1 
ATOM   369  N  N   . PRO A 1 46  ? -24.926 2.769   29.519  1.00 18.78  ? 46  PRO A N   1 
ATOM   370  C  CA  . PRO A 1 46  ? -25.025 2.090   28.187  1.00 18.80  ? 46  PRO A CA  1 
ATOM   371  C  C   . PRO A 1 46  ? -24.248 2.854   27.165  1.00 14.39  ? 46  PRO A C   1 
ATOM   372  O  O   . PRO A 1 46  ? -24.191 4.076   27.265  1.00 16.09  ? 46  PRO A O   1 
ATOM   373  C  CB  . PRO A 1 46  ? -26.535 2.155   27.875  1.00 18.53  ? 46  PRO A CB  1 
ATOM   374  C  CG  . PRO A 1 46  ? -27.246 2.327   29.183  1.00 24.65  ? 46  PRO A CG  1 
ATOM   375  C  CD  . PRO A 1 46  ? -26.272 3.112   30.032  1.00 20.69  ? 46  PRO A CD  1 
ATOM   376  N  N   . LEU A 1 47  ? -23.652 2.110   26.272  1.00 17.12  ? 47  LEU A N   1 
ATOM   377  C  CA  . LEU A 1 47  ? -22.938 2.741   25.205  1.00 14.50  ? 47  LEU A CA  1 
ATOM   378  C  C   . LEU A 1 47  ? -23.983 3.372   24.238  1.00 16.26  ? 47  LEU A C   1 
ATOM   379  O  O   . LEU A 1 47  ? -24.978 2.687   23.948  1.00 21.45  ? 47  LEU A O   1 
ATOM   380  C  CB  . LEU A 1 47  ? -22.139 1.669   24.483  1.00 19.02  ? 47  LEU A CB  1 
ATOM   381  C  CG  . LEU A 1 47  ? -21.093 2.001   23.592  1.00 19.56  ? 47  LEU A CG  1 
ATOM   382  C  CD1 . LEU A 1 47  ? -20.032 2.912   24.331  1.00 24.11  ? 47  LEU A CD1 1 
ATOM   383  C  CD2 . LEU A 1 47  ? -20.455 0.746   22.968  1.00 20.83  ? 47  LEU A CD2 1 
ATOM   384  N  N   . SER A 1 48  ? -23.713 4.565   23.704  1.00 14.49  ? 48  SER A N   1 
ATOM   385  C  CA  . SER A 1 48  ? -24.563 5.189   22.706  1.00 13.94  ? 48  SER A CA  1 
ATOM   386  C  C   . SER A 1 48  ? -23.779 5.230   21.416  1.00 14.58  ? 48  SER A C   1 
ATOM   387  O  O   . SER A 1 48  ? -22.761 5.946   21.284  1.00 15.52  ? 48  SER A O   1 
ATOM   388  C  CB  . SER A 1 48  ? -24.903 6.592   23.147  1.00 16.83  ? 48  SER A CB  1 
ATOM   389  O  OG  . SER A 1 48  ? -25.579 7.322   22.147  1.00 20.79  ? 48  SER A OG  1 
ATOM   390  N  N   . VAL A 1 49  ? -24.199 4.436   20.475  1.00 15.54  ? 49  VAL A N   1 
ATOM   391  C  CA  . VAL A 1 49  ? -23.616 4.394   19.156  1.00 16.45  ? 49  VAL A CA  1 
ATOM   392  C  C   . VAL A 1 49  ? -24.608 5.021   18.174  1.00 17.10  ? 49  VAL A C   1 
ATOM   393  O  O   . VAL A 1 49  ? -25.715 4.474   17.999  1.00 21.40  ? 49  VAL A O   1 
ATOM   394  C  CB  . VAL A 1 49  ? -23.385 2.911   18.740  1.00 17.97  ? 49  VAL A CB  1 
ATOM   395  C  CG1 . VAL A 1 49  ? -22.793 2.869   17.368  1.00 23.79  ? 49  VAL A CG1 1 
ATOM   396  C  CG2 . VAL A 1 49  ? -22.493 2.196   19.784  1.00 20.06  ? 49  VAL A CG2 1 
ATOM   397  N  N   . SER A 1 50  ? -24.256 6.138   17.565  1.00 16.39  ? 50  SER A N   1 
ATOM   398  C  CA  . SER A 1 50  ? -25.210 6.843   16.724  1.00 17.82  ? 50  SER A CA  1 
ATOM   399  C  C   . SER A 1 50  ? -24.582 6.950   15.371  1.00 17.51  ? 50  SER A C   1 
ATOM   400  O  O   . SER A 1 50  ? -23.922 7.921   15.053  1.00 17.81  ? 50  SER A O   1 
ATOM   401  C  CB  . SER A 1 50  ? -25.536 8.206   17.331  1.00 22.71  ? 50  SER A CB  1 
ATOM   402  O  OG  . SER A 1 50  ? -26.204 8.039   18.559  1.00 27.37  ? 50  SER A OG  1 
ATOM   403  N  N   . TYR A 1 51  ? -24.829 5.924   14.529  1.00 16.04  ? 51  TYR A N   1 
ATOM   404  C  CA  . TYR A 1 51  ? -24.207 5.833   13.243  1.00 15.49  ? 51  TYR A CA  1 
ATOM   405  C  C   . TYR A 1 51  ? -25.202 6.071   12.087  1.00 18.01  ? 51  TYR A C   1 
ATOM   406  O  O   . TYR A 1 51  ? -24.827 5.903   10.954  1.00 17.20  ? 51  TYR A O   1 
ATOM   407  C  CB  . TYR A 1 51  ? -23.559 4.473   13.034  1.00 16.03  ? 51  TYR A CB  1 
ATOM   408  C  CG  . TYR A 1 51  ? -22.303 4.199   13.821  1.00 14.39  ? 51  TYR A CG  1 
ATOM   409  C  CD1 . TYR A 1 51  ? -21.550 5.214   14.491  1.00 14.81  ? 51  TYR A CD1 1 
ATOM   410  C  CD2 . TYR A 1 51  ? -21.822 2.891   13.885  1.00 13.76  ? 51  TYR A CD2 1 
ATOM   411  C  CE1 . TYR A 1 51  ? -20.376 4.865   15.162  1.00 12.66  ? 51  TYR A CE1 1 
ATOM   412  C  CE2 . TYR A 1 51  ? -20.656 2.540   14.522  1.00 13.05  ? 51  TYR A CE2 1 
ATOM   413  C  CZ  . TYR A 1 51  ? -19.922 3.552   15.173  1.00 12.44  ? 51  TYR A CZ  1 
ATOM   414  O  OH  . TYR A 1 51  ? -18.804 3.157   15.844  1.00 13.07  ? 51  TYR A OH  1 
ATOM   415  N  N   A ASP A 1 52  ? -26.428 6.501   12.364  0.50 19.02  ? 52  ASP A N   1 
ATOM   416  N  N   B ASP A 1 52  ? -26.418 6.513   12.384  0.50 19.08  ? 52  ASP A N   1 
ATOM   417  C  CA  A ASP A 1 52  ? -27.433 6.733   11.326  0.50 20.95  ? 52  ASP A CA  1 
ATOM   418  C  CA  B ASP A 1 52  ? -27.454 6.782   11.375  0.50 21.12  ? 52  ASP A CA  1 
ATOM   419  C  C   A ASP A 1 52  ? -26.996 7.683   10.203  0.50 21.95  ? 52  ASP A C   1 
ATOM   420  C  C   B ASP A 1 52  ? -27.003 7.689   10.225  0.50 21.94  ? 52  ASP A C   1 
ATOM   421  O  O   A ASP A 1 52  ? -27.441 7.515   9.030   0.50 23.90  ? 52  ASP A O   1 
ATOM   422  O  O   B ASP A 1 52  ? -27.422 7.490   9.071   0.50 24.40  ? 52  ASP A O   1 
ATOM   423  C  CB  A ASP A 1 52  ? -28.736 7.225   11.953  0.50 22.29  ? 52  ASP A CB  1 
ATOM   424  C  CB  B ASP A 1 52  ? -28.684 7.392   12.039  0.50 24.96  ? 52  ASP A CB  1 
ATOM   425  C  CG  A ASP A 1 52  ? -28.501 8.261   13.118  0.50 34.61  ? 52  ASP A CG  1 
ATOM   426  C  CG  B ASP A 1 52  ? -29.817 7.575   11.089  0.50 33.28  ? 52  ASP A CG  1 
ATOM   427  O  OD1 A ASP A 1 52  ? -27.863 7.932   14.180  0.50 35.44  ? 52  ASP A OD1 1 
ATOM   428  O  OD1 B ASP A 1 52  ? -30.282 6.534   10.598  0.50 37.29  ? 52  ASP A OD1 1 
ATOM   429  O  OD2 A ASP A 1 52  ? -28.972 9.409   12.969  0.50 49.47  ? 52  ASP A OD2 1 
ATOM   430  O  OD2 B ASP A 1 52  ? -30.238 8.725   10.814  0.50 52.17  ? 52  ASP A OD2 1 
ATOM   431  N  N   . GLN A 1 53  ? -26.148 8.661   10.505  1.00 21.97  ? 53  GLN A N   1 
ATOM   432  C  CA  . GLN A 1 53  ? -25.742 9.606   9.430   1.00 24.29  ? 53  GLN A CA  1 
ATOM   433  C  C   . GLN A 1 53  ? -24.295 9.385   8.993   1.00 18.44  ? 53  GLN A C   1 
ATOM   434  O  O   . GLN A 1 53  ? -23.699 10.235  8.352   1.00 20.20  ? 53  GLN A O   1 
ATOM   435  C  CB  . GLN A 1 53  ? -25.938 11.097  9.837   1.00 26.50  ? 53  GLN A CB  1 
ATOM   436  C  CG  . GLN A 1 53  ? -27.414 11.513  9.853   1.00 34.60  ? 53  GLN A CG  1 
ATOM   437  C  CD  . GLN A 1 53  ? -28.090 11.468  8.453   1.00 64.75  ? 53  GLN A CD  1 
ATOM   438  O  OE1 . GLN A 1 53  ? -27.572 11.997  7.438   1.00 71.12  ? 53  GLN A OE1 1 
ATOM   439  N  NE2 . GLN A 1 53  ? -29.243 10.811  8.397   1.00 88.14  ? 53  GLN A NE2 1 
ATOM   440  N  N   . ALA A 1 54  ? -23.736 8.254   9.307   1.00 18.97  ? 54  ALA A N   1 
ATOM   441  C  CA  . ALA A 1 54  ? -22.373 7.977   8.880   1.00 16.30  ? 54  ALA A CA  1 
ATOM   442  C  C   . ALA A 1 54  ? -22.177 8.068   7.394   1.00 17.17  ? 54  ALA A C   1 
ATOM   443  O  O   . ALA A 1 54  ? -23.028 7.611   6.596   1.00 23.78  ? 54  ALA A O   1 
ATOM   444  C  CB  . ALA A 1 54  ? -21.921 6.585   9.371   1.00 18.70  ? 54  ALA A CB  1 
ATOM   445  N  N   . THR A 1 55  ? -21.092 8.701   6.975   1.00 15.68  ? 55  THR A N   1 
ATOM   446  C  CA  . THR A 1 55  ? -20.739 8.887   5.592   1.00 16.42  ? 55  THR A CA  1 
ATOM   447  C  C   . THR A 1 55  ? -19.408 8.332   5.281   1.00 13.89  ? 55  THR A C   1 
ATOM   448  O  O   . THR A 1 55  ? -18.373 8.927   5.534   1.00 14.69  ? 55  THR A O   1 
ATOM   449  C  CB  . THR A 1 55  ? -20.657 10.410  5.151   1.00 21.13  ? 55  THR A CB  1 
ATOM   450  O  OG1 . THR A 1 55  ? -21.893 11.071  5.349   1.00 28.97  ? 55  THR A OG1 1 
ATOM   451  C  CG2 . THR A 1 55  ? -20.377 10.431  3.690   1.00 24.58  ? 55  THR A CG2 1 
ATOM   452  N  N   . SER A 1 56  ? -19.402 7.109   4.782   1.00 15.40  ? 56  SER A N   1 
ATOM   453  C  CA  . SER A 1 56  ? -18.141 6.501   4.399   1.00 16.55  ? 56  SER A CA  1 
ATOM   454  C  C   . SER A 1 56  ? -17.768 7.157   3.132   1.00 17.70  ? 56  SER A C   1 
ATOM   455  O  O   . SER A 1 56  ? -18.570 7.597   2.322   1.00 18.46  ? 56  SER A O   1 
ATOM   456  C  CB  . SER A 1 56  ? -18.192 4.980   4.204   1.00 16.67  ? 56  SER A CB  1 
ATOM   457  O  OG  . SER A 1 56  ? -19.069 4.616   3.120   1.00 17.89  ? 56  SER A OG  1 
ATOM   458  N  N   . LEU A 1 57  ? -16.469 7.214   2.910   1.00 14.33  ? 57  LEU A N   1 
ATOM   459  C  CA  . LEU A 1 57  ? -15.965 7.775   1.696   1.00 16.21  ? 57  LEU A CA  1 
ATOM   460  C  C   . LEU A 1 57  ? -15.099 6.832   0.868   1.00 14.55  ? 57  LEU A C   1 
ATOM   461  O  O   . LEU A 1 57  ? -15.093 6.914   -0.342  1.00 17.12  ? 57  LEU A O   1 
ATOM   462  C  CB  . LEU A 1 57  ? -15.112 8.928   2.084   1.00 20.11  ? 57  LEU A CB  1 
ATOM   463  C  CG  . LEU A 1 57  ? -15.931 10.131  2.687   1.00 21.04  ? 57  LEU A CG  1 
ATOM   464  C  CD1 . LEU A 1 57  ? -14.909 11.177  3.120   1.00 27.86  ? 57  LEU A CD1 1 
ATOM   465  C  CD2 . LEU A 1 57  ? -17.034 10.739  1.757   1.00 25.63  ? 57  LEU A CD2 1 
ATOM   466  N  N   . ARG A 1 58  ? -14.204 6.081   1.516   1.00 16.33  ? 58  ARG A N   1 
ATOM   467  C  CA  . ARG A 1 58  ? -13.148 5.400   0.760   1.00 15.64  ? 58  ARG A CA  1 
ATOM   468  C  C   . ARG A 1 58  ? -12.630 4.264   1.586   1.00 14.14  ? 58  ARG A C   1 
ATOM   469  O  O   . ARG A 1 58  ? -12.751 4.263   2.800   1.00 14.91  ? 58  ARG A O   1 
ATOM   470  C  CB  . ARG A 1 58  ? -12.032 6.429   0.618   1.00 17.04  ? 58  ARG A CB  1 
ATOM   471  C  CG  . ARG A 1 58  ? -10.971 6.104   -0.255  1.00 17.93  ? 58  ARG A CG  1 
ATOM   472  C  CD  . ARG A 1 58  ? -9.938  7.120   -0.514  1.00 21.26  ? 58  ARG A CD  1 
ATOM   473  N  NE  . ARG A 1 58  ? -9.050  7.149   0.649   1.00 18.22  ? 58  ARG A NE  1 
ATOM   474  C  CZ  . ARG A 1 58  ? -7.738  7.370   0.634   1.00 18.05  ? 58  ARG A CZ  1 
ATOM   475  N  NH1 . ARG A 1 58  ? -7.088  7.604   -0.499  1.00 20.72  ? 58  ARG A NH1 1 
ATOM   476  N  NH2 . ARG A 1 58  ? -7.068  7.346   1.778   1.00 17.62  ? 58  ARG A NH2 1 
ATOM   477  N  N   . ILE A 1 59  ? -12.010 3.304   0.911   1.00 14.33  ? 59  ILE A N   1 
ATOM   478  C  CA  . ILE A 1 59  ? -11.377 2.199   1.584   1.00 16.05  ? 59  ILE A CA  1 
ATOM   479  C  C   . ILE A 1 59  ? -9.936  2.215   1.064   1.00 13.26  ? 59  ILE A C   1 
ATOM   480  O  O   . ILE A 1 59  ? -9.656  2.365   -0.144  1.00 15.79  ? 59  ILE A O   1 
ATOM   481  C  CB  . ILE A 1 59  ? -12.115 0.885   1.318   1.00 13.63  ? 59  ILE A CB  1 
ATOM   482  C  CG1 . ILE A 1 59  ? -11.478 -0.255  2.179   1.00 15.13  ? 59  ILE A CG1 1 
ATOM   483  C  CG2 . ILE A 1 59  ? -12.104 0.470   -0.171  1.00 16.44  ? 59  ILE A CG2 1 
ATOM   484  C  CD1 . ILE A 1 59  ? -12.300 -1.503  2.116   1.00 15.65  ? 59  ILE A CD1 1 
ATOM   485  N  N   . LEU A 1 60  ? -8.966  1.999   1.973   1.00 14.59  ? 60  LEU A N   1 
ATOM   486  C  CA  . LEU A 1 60  ? -7.588  2.118   1.723   1.00 13.87  ? 60  LEU A CA  1 
ATOM   487  C  C   . LEU A 1 60  ? -6.748  0.927   2.259   1.00 13.15  ? 60  LEU A C   1 
ATOM   488  O  O   . LEU A 1 60  ? -6.911  0.607   3.405   1.00 12.69  ? 60  LEU A O   1 
ATOM   489  C  CB  . LEU A 1 60  ? -7.047  3.419   2.381   1.00 14.58  ? 60  LEU A CB  1 
ATOM   490  C  CG  . LEU A 1 60  ? -5.546  3.550   2.365   1.00 15.43  ? 60  LEU A CG  1 
ATOM   491  C  CD1 . LEU A 1 60  ? -4.950  3.800   0.912   1.00 16.81  ? 60  LEU A CD1 1 
ATOM   492  C  CD2 . LEU A 1 60  ? -5.027  4.654   3.341   1.00 17.46  ? 60  LEU A CD2 1 
ATOM   493  N  N   . ASN A 1 61  ? -5.913  0.318   1.432   1.00 12.65  ? 61  ASN A N   1 
ATOM   494  C  CA  . ASN A 1 61  ? -4.890  -0.612  1.879   1.00 14.05  ? 61  ASN A CA  1 
ATOM   495  C  C   . ASN A 1 61  ? -3.634  0.174   2.279   1.00 13.68  ? 61  ASN A C   1 
ATOM   496  O  O   . ASN A 1 61  ? -3.024  0.709   1.403   1.00 15.24  ? 61  ASN A O   1 
ATOM   497  C  CB  . ASN A 1 61  ? -4.625  -1.672  0.812   1.00 14.46  ? 61  ASN A CB  1 
ATOM   498  C  CG  . ASN A 1 61  ? -3.548  -2.661  1.221   1.00 13.89  ? 61  ASN A CG  1 
ATOM   499  O  OD1 . ASN A 1 61  ? -2.613  -2.418  2.093   1.00 15.05  ? 61  ASN A OD1 1 
ATOM   500  N  ND2 . ASN A 1 61  ? -3.614  -3.859  0.611   1.00 14.86  ? 61  ASN A ND2 1 
ATOM   501  N  N   . ASN A 1 62  ? -3.363  0.257   3.555   1.00 13.99  ? 62  ASN A N   1 
ATOM   502  C  CA  . ASN A 1 62  ? -2.287  1.099   4.030   1.00 14.71  ? 62  ASN A CA  1 
ATOM   503  C  C   . ASN A 1 62  ? -1.017  0.308   4.244   1.00 14.43  ? 62  ASN A C   1 
ATOM   504  O  O   . ASN A 1 62  ? 0.001   0.756   4.836   1.00 18.16  ? 62  ASN A O   1 
ATOM   505  C  CB  . ASN A 1 62  ? -2.657  1.920   5.275   1.00 16.15  ? 62  ASN A CB  1 
ATOM   506  C  CG  . ASN A 1 62  ? -2.893  1.022   6.463   1.00 16.94  ? 62  ASN A CG  1 
ATOM   507  O  OD1 . ASN A 1 62  ? -2.562  -0.183  6.476   1.00 15.30  ? 62  ASN A OD1 1 
ATOM   508  N  ND2 . ASN A 1 62  ? -3.417  1.594   7.465   1.00 23.74  ? 62  ASN A ND2 1 
ATOM   509  N  N   . GLY A 1 63  ? -1.030  -0.981  3.824   1.00 15.08  ? 63  GLY A N   1 
ATOM   510  C  CA  . GLY A 1 63  ? 0.123   -1.790  4.018   1.00 14.81  ? 63  GLY A CA  1 
ATOM   511  C  C   . GLY A 1 63  ? 0.172   -2.592  5.327   1.00 14.20  ? 63  GLY A C   1 
ATOM   512  O  O   . GLY A 1 63  ? 1.090   -3.420  5.536   1.00 15.94  ? 63  GLY A O   1 
ATOM   513  N  N   A HIS A 1 64  ? -0.752  -2.324  6.194   0.50 12.61  ? 64  HIS A N   1 
ATOM   514  N  N   B HIS A 1 64  ? -0.677  -2.272  6.278   0.50 14.52  ? 64  HIS A N   1 
ATOM   515  C  CA  A HIS A 1 64  ? -0.816  -2.990  7.508   0.50 12.76  ? 64  HIS A CA  1 
ATOM   516  C  CA  B HIS A 1 64  ? -0.831  -3.078  7.562   0.50 15.74  ? 64  HIS A CA  1 
ATOM   517  C  C   A HIS A 1 64  ? -2.154  -3.701  7.581   0.50 13.26  ? 64  HIS A C   1 
ATOM   518  C  C   B HIS A 1 64  ? -2.224  -3.573  7.847   0.50 12.28  ? 64  HIS A C   1 
ATOM   519  O  O   A HIS A 1 64  ? -2.210  -4.916  7.951   0.50 12.83  ? 64  HIS A O   1 
ATOM   520  O  O   B HIS A 1 64  ? -2.407  -4.487  8.678   0.50 12.96  ? 64  HIS A O   1 
ATOM   521  C  CB  A HIS A 1 64  ? -0.578  -1.944  8.608   0.50 10.87  ? 64  HIS A CB  1 
ATOM   522  C  CB  B HIS A 1 64  ? -0.296  -2.382  8.827   0.50 16.58  ? 64  HIS A CB  1 
ATOM   523  C  CG  A HIS A 1 64  ? 0.737   -1.195  8.446   0.50 12.91  ? 64  HIS A CG  1 
ATOM   524  C  CG  B HIS A 1 64  ? -0.758  -0.922  9.038   0.50 20.25  ? 64  HIS A CG  1 
ATOM   525  N  ND1 A HIS A 1 64  ? 1.951   -1.824  8.510   0.50 14.46  ? 64  HIS A ND1 1 
ATOM   526  N  ND1 B HIS A 1 64  ? -0.040  0.103   8.542   0.50 21.16  ? 64  HIS A ND1 1 
ATOM   527  C  CD2 A HIS A 1 64  ? 0.987   0.114   8.210   0.50 13.12  ? 64  HIS A CD2 1 
ATOM   528  C  CD2 B HIS A 1 64  ? -1.747  -0.332  9.919   0.50 20.37  ? 64  HIS A CD2 1 
ATOM   529  C  CE1 A HIS A 1 64  ? 2.920   -0.926  8.383   0.50 15.55  ? 64  HIS A CE1 1 
ATOM   530  C  CE1 B HIS A 1 64  ? -0.558  1.263   8.954   0.50 20.36  ? 64  HIS A CE1 1 
ATOM   531  N  NE2 A HIS A 1 64  ? 2.326   0.265   8.146   0.50 16.28  ? 64  HIS A NE2 1 
ATOM   532  N  NE2 B HIS A 1 64  ? -1.583  1.008   9.808   0.50 26.00  ? 64  HIS A NE2 1 
ATOM   533  N  N   . ALA A 1 65  ? -3.202  -2.967  7.186   1.00 12.80  ? 65  ALA A N   1 
ATOM   534  C  CA  . ALA A 1 65  ? -4.580  -3.397  7.203   1.00 12.42  ? 65  ALA A CA  1 
ATOM   535  C  C   . ALA A 1 65  ? -5.348  -2.642  6.077   1.00 11.64  ? 65  ALA A C   1 
ATOM   536  O  O   . ALA A 1 65  ? -4.664  -1.982  5.243   1.00 14.33  ? 65  ALA A O   1 
ATOM   537  C  CB  . ALA A 1 65  ? -5.225  -3.210  8.579   1.00 14.75  ? 65  ALA A CB  1 
ATOM   538  N  N   . PHE A 1 66  ? -6.639  -2.728  6.057   1.00 11.59  ? 66  PHE A N   1 
ATOM   539  C  CA  . PHE A 1 66  ? -7.402  -1.767  5.275   1.00 12.62  ? 66  PHE A CA  1 
ATOM   540  C  C   . PHE A 1 66  ? -8.241  -0.928  6.151   1.00 12.29  ? 66  PHE A C   1 
ATOM   541  O  O   . PHE A 1 66  ? -8.847  -1.391  7.115   1.00 12.52  ? 66  PHE A O   1 
ATOM   542  C  CB  . PHE A 1 66  ? -8.193  -2.458  4.165   1.00 13.20  ? 66  PHE A CB  1 
ATOM   543  C  CG  . PHE A 1 66  ? -9.238  -3.407  4.629   1.00 13.78  ? 66  PHE A CG  1 
ATOM   544  C  CD1 . PHE A 1 66  ? -10.461 -2.921  5.015   1.00 14.47  ? 66  PHE A CD1 1 
ATOM   545  C  CD2 . PHE A 1 66  ? -8.945  -4.784  4.809   1.00 13.44  ? 66  PHE A CD2 1 
ATOM   546  C  CE1 . PHE A 1 66  ? -11.426 -3.796  5.499   1.00 13.35  ? 66  PHE A CE1 1 
ATOM   547  C  CE2 . PHE A 1 66  ? -9.933  -5.675  5.317   1.00 14.19  ? 66  PHE A CE2 1 
ATOM   548  C  CZ  . PHE A 1 66  ? -11.186 -5.177  5.648   1.00 14.51  ? 66  PHE A CZ  1 
ATOM   549  N  N   . ASN A 1 67  ? -8.329  0.364   5.803   1.00 13.10  ? 67  ASN A N   1 
ATOM   550  C  CA  . ASN A 1 67  ? -9.182  1.283   6.570   1.00 12.05  ? 67  ASN A CA  1 
ATOM   551  C  C   . ASN A 1 67  ? -10.411 1.726   5.781   1.00 11.39  ? 67  ASN A C   1 
ATOM   552  O  O   . ASN A 1 67  ? -10.245 2.152   4.593   1.00 13.85  ? 67  ASN A O   1 
ATOM   553  C  CB  . ASN A 1 67  ? -8.459  2.555   6.952   1.00 14.53  ? 67  ASN A CB  1 
ATOM   554  C  CG  . ASN A 1 67  ? -7.330  2.334   7.901   1.00 14.78  ? 67  ASN A CG  1 
ATOM   555  O  OD1 . ASN A 1 67  ? -7.160  1.289   8.533   1.00 17.07  ? 67  ASN A OD1 1 
ATOM   556  N  ND2 . ASN A 1 67  ? -6.553  3.374   8.069   1.00 19.76  ? 67  ASN A ND2 1 
ATOM   557  N  N   . VAL A 1 68  ? -11.579 1.612   6.320   1.00 11.93  ? 68  VAL A N   1 
ATOM   558  C  CA  . VAL A 1 68  ? -12.769 2.218   5.721   1.00 12.20  ? 68  VAL A CA  1 
ATOM   559  C  C   . VAL A 1 68  ? -12.838 3.608   6.403   1.00 13.97  ? 68  VAL A C   1 
ATOM   560  O  O   . VAL A 1 68  ? -12.968 3.684   7.648   1.00 12.63  ? 68  VAL A O   1 
ATOM   561  C  CB  . VAL A 1 68  ? -14.018 1.384   5.917   1.00 13.54  ? 68  VAL A CB  1 
ATOM   562  C  CG1 . VAL A 1 68  ? -15.271 2.183   5.502   1.00 14.85  ? 68  VAL A CG1 1 
ATOM   563  C  CG2 . VAL A 1 68  ? -13.879 0.067   5.139   1.00 15.19  ? 68  VAL A CG2 1 
ATOM   564  N  N   . GLU A 1 69  ? -12.802 4.671   5.631   1.00 14.79  ? 69  GLU A N   1 
ATOM   565  C  CA  . GLU A 1 69  ? -12.735 6.038   6.127   1.00 14.21  ? 69  GLU A CA  1 
ATOM   566  C  C   . GLU A 1 69  ? -14.091 6.701   6.048   1.00 13.89  ? 69  GLU A C   1 
ATOM   567  O  O   . GLU A 1 69  ? -14.861 6.499   5.070   1.00 15.25  ? 69  GLU A O   1 
ATOM   568  C  CB  . GLU A 1 69  ? -11.839 6.772   5.220   1.00 15.23  ? 69  GLU A CB  1 
ATOM   569  C  CG  . GLU A 1 69  ? -10.469 6.214   5.272   1.00 15.07  ? 69  GLU A CG  1 
ATOM   570  C  CD  . GLU A 1 69  ? -9.589  6.697   4.157   1.00 18.65  ? 69  GLU A CD  1 
ATOM   571  O  OE1 . GLU A 1 69  ? -10.083 7.435   3.238   1.00 18.27  ? 69  GLU A OE1 1 
ATOM   572  O  OE2 . GLU A 1 69  ? -8.342  6.399   4.137   1.00 19.97  ? 69  GLU A OE2 1 
ATOM   573  N  N   . PHE A 1 70  ? -14.277 7.622   6.974   1.00 13.90  ? 70  PHE A N   1 
ATOM   574  C  CA  . PHE A 1 70  ? -15.525 8.360   7.074   1.00 12.68  ? 70  PHE A CA  1 
ATOM   575  C  C   . PHE A 1 70  ? -15.310 9.838   7.011   1.00 14.00  ? 70  PHE A C   1 
ATOM   576  O  O   . PHE A 1 70  ? -14.216 10.326  7.377   1.00 15.04  ? 70  PHE A O   1 
ATOM   577  C  CB  . PHE A 1 70  ? -16.228 8.015   8.379   1.00 12.93  ? 70  PHE A CB  1 
ATOM   578  C  CG  . PHE A 1 70  ? -16.782 6.605   8.351   1.00 13.57  ? 70  PHE A CG  1 
ATOM   579  C  CD1 . PHE A 1 70  ? -15.962 5.511   8.566   1.00 13.46  ? 70  PHE A CD1 1 
ATOM   580  C  CD2 . PHE A 1 70  ? -18.104 6.404   8.020   1.00 13.70  ? 70  PHE A CD2 1 
ATOM   581  C  CE1 . PHE A 1 70  ? -16.459 4.256   8.436   1.00 14.39  ? 70  PHE A CE1 1 
ATOM   582  C  CE2 . PHE A 1 70  ? -18.630 5.109   7.879   1.00 14.87  ? 70  PHE A CE2 1 
ATOM   583  C  CZ  . PHE A 1 70  ? -17.786 4.028   8.111   1.00 14.36  ? 70  PHE A CZ  1 
ATOM   584  N  N   . ASP A 1 71  ? -16.289 10.576  6.522   1.00 16.38  ? 71  ASP A N   1 
ATOM   585  C  CA  . ASP A 1 71  ? -16.213 12.024  6.611   1.00 16.81  ? 71  ASP A CA  1 
ATOM   586  C  C   . ASP A 1 71  ? -16.495 12.343  8.056   1.00 16.28  ? 71  ASP A C   1 
ATOM   587  O  O   . ASP A 1 71  ? -17.586 12.186  8.534   1.00 22.15  ? 71  ASP A O   1 
ATOM   588  C  CB  . ASP A 1 71  ? -17.290 12.566  5.729   1.00 21.96  ? 71  ASP A CB  1 
ATOM   589  C  CG  . ASP A 1 71  ? -17.499 14.070  5.921   1.00 27.61  ? 71  ASP A CG  1 
ATOM   590  O  OD1 . ASP A 1 71  ? -16.627 14.753  6.478   1.00 24.02  ? 71  ASP A OD1 1 
ATOM   591  O  OD2 . ASP A 1 71  ? -18.587 14.598  5.610   1.00 35.51  ? 71  ASP A OD2 1 
ATOM   592  N  N   . ASP A 1 72  ? -15.496 12.899  8.735   1.00 14.93  ? 72  ASP A N   1 
ATOM   593  C  CA  . ASP A 1 72  ? -15.580 13.275  10.141  1.00 16.30  ? 72  ASP A CA  1 
ATOM   594  C  C   . ASP A 1 72  ? -15.540 14.786  10.284  1.00 19.92  ? 72  ASP A C   1 
ATOM   595  O  O   . ASP A 1 72  ? -15.152 15.317  11.313  1.00 22.28  ? 72  ASP A O   1 
ATOM   596  C  CB  . ASP A 1 72  ? -14.480 12.608  10.973  1.00 16.70  ? 72  ASP A CB  1 
ATOM   597  C  CG  . ASP A 1 72  ? -13.136 13.142  10.615  1.00 16.78  ? 72  ASP A CG  1 
ATOM   598  O  OD1 . ASP A 1 72  ? -12.972 13.776  9.485   1.00 19.06  ? 72  ASP A OD1 1 
ATOM   599  O  OD2 . ASP A 1 72  ? -12.221 12.888  11.392  1.00 17.74  ? 72  ASP A OD2 1 
ATOM   600  N  N   . SER A 1 73  ? -15.988 15.517  9.250   1.00 18.27  ? 73  SER A N   1 
ATOM   601  C  CA  . SER A 1 73  ? -15.960 17.037  9.257   1.00 21.16  ? 73  SER A CA  1 
ATOM   602  C  C   . SER A 1 73  ? -17.298 17.591  9.811   1.00 21.88  ? 73  SER A C   1 
ATOM   603  O  O   . SER A 1 73  ? -17.415 18.806  9.981   1.00 20.74  ? 73  SER A O   1 
ATOM   604  C  CB  . SER A 1 73  ? -15.656 17.491  7.855   1.00 25.42  ? 73  SER A CB  1 
ATOM   605  O  OG  . SER A 1 73  ? -16.830 17.374  7.088   1.00 22.44  ? 73  SER A OG  1 
ATOM   606  N  N   . GLN A 1 74  ? -18.258 16.764  10.145  1.00 23.34  ? 74  GLN A N   1 
ATOM   607  C  CA  . GLN A 1 74  ? -19.454 17.223  10.816  1.00 27.63  ? 74  GLN A CA  1 
ATOM   608  C  C   . GLN A 1 74  ? -19.792 16.225  11.870  1.00 22.66  ? 74  GLN A C   1 
ATOM   609  O  O   . GLN A 1 74  ? -19.268 15.097  11.861  1.00 18.58  ? 74  GLN A O   1 
ATOM   610  C  CB  . GLN A 1 74  ? -20.691 17.197  9.887   1.00 29.39  ? 74  GLN A CB  1 
ATOM   611  C  CG  . GLN A 1 74  ? -20.541 18.193  8.793   1.00 35.61  ? 74  GLN A CG  1 
ATOM   612  C  CD  . GLN A 1 74  ? -21.786 18.310  7.963   1.00 42.51  ? 74  GLN A CD  1 
ATOM   613  O  OE1 . GLN A 1 74  ? -22.842 18.625  8.481   1.00 68.16  ? 74  GLN A OE1 1 
ATOM   614  N  NE2 . GLN A 1 74  ? -21.660 18.076  6.659   1.00 40.69  ? 74  GLN A NE2 1 
ATOM   615  N  N   . ASP A 1 75  ? -20.678 16.637  12.748  1.00 27.98  ? 75  ASP A N   1 
ATOM   616  C  CA  . ASP A 1 75  ? -21.159 15.758  13.679  1.00 21.51  ? 75  ASP A CA  1 
ATOM   617  C  C   . ASP A 1 75  ? -22.139 14.699  13.188  1.00 23.49  ? 75  ASP A C   1 
ATOM   618  O  O   . ASP A 1 75  ? -23.388 14.936  13.130  1.00 27.86  ? 75  ASP A O   1 
ATOM   619  C  CB  . ASP A 1 75  ? -21.740 16.525  14.839  1.00 29.54  ? 75  ASP A CB  1 
ATOM   620  C  CG  . ASP A 1 75  ? -21.491 15.835  16.160  1.00 30.39  ? 75  ASP A CG  1 
ATOM   621  O  OD1 . ASP A 1 75  ? -20.327 15.929  16.623  1.00 33.90  ? 75  ASP A OD1 1 
ATOM   622  O  OD2 . ASP A 1 75  ? -22.402 15.125  16.689  1.00 32.52  ? 75  ASP A OD2 1 
ATOM   623  N  N   . LYS A 1 76  ? -21.638 13.533  12.800  1.00 20.10  ? 76  LYS A N   1 
ATOM   624  C  CA  . LYS A 1 76  ? -22.450 12.546  12.012  1.00 20.53  ? 76  LYS A CA  1 
ATOM   625  C  C   . LYS A 1 76  ? -22.633 11.073  12.532  1.00 29.32  ? 76  LYS A C   1 
ATOM   626  O  O   . LYS A 1 76  ? -23.677 10.485  12.533  1.00 38.56  ? 76  LYS A O   1 
ATOM   627  C  CB  . LYS A 1 76  ? -21.891 12.481  10.584  1.00 21.50  ? 76  LYS A CB  1 
ATOM   628  C  CG  . LYS A 1 76  ? -22.276 13.608  9.657   1.00 30.83  ? 76  LYS A CG  1 
ATOM   629  C  CD  . LYS A 1 76  ? -21.640 13.360  8.296   1.00 34.66  ? 76  LYS A CD  1 
ATOM   630  C  CE  . LYS A 1 76  ? -22.220 14.297  7.246   1.00 34.63  ? 76  LYS A CE  1 
ATOM   631  N  NZ  . LYS A 1 76  ? -21.560 14.047  5.934   1.00 33.90  ? 76  LYS A NZ  1 
ATOM   632  N  N   . ALA A 1 77  ? -21.549 10.473  12.945  1.00 24.69  ? 77  ALA A N   1 
ATOM   633  C  CA  . ALA A 1 77  ? -21.380 9.060   13.431  1.00 16.69  ? 77  ALA A CA  1 
ATOM   634  C  C   . ALA A 1 77  ? -20.618 9.223   14.720  1.00 15.88  ? 77  ALA A C   1 
ATOM   635  O  O   . ALA A 1 77  ? -19.403 9.445   14.737  1.00 22.26  ? 77  ALA A O   1 
ATOM   636  C  CB  . ALA A 1 77  ? -20.557 8.366   12.405  1.00 16.56  ? 77  ALA A CB  1 
ATOM   637  N  N   . VAL A 1 78  ? -21.310 9.162   15.816  1.00 13.92  ? 78  VAL A N   1 
ATOM   638  C  CA  . VAL A 1 78  ? -20.679 9.469   17.099  1.00 15.32  ? 78  VAL A CA  1 
ATOM   639  C  C   . VAL A 1 78  ? -20.933 8.385   18.121  1.00 14.47  ? 78  VAL A C   1 
ATOM   640  O  O   . VAL A 1 78  ? -21.960 7.690   18.168  1.00 16.10  ? 78  VAL A O   1 
ATOM   641  C  CB  . VAL A 1 78  ? -21.022 10.812  17.617  1.00 19.72  ? 78  VAL A CB  1 
ATOM   642  C  CG1 . VAL A 1 78  ? -20.738 11.989  16.685  1.00 22.80  ? 78  VAL A CG1 1 
ATOM   643  C  CG2 . VAL A 1 78  ? -22.388 10.771  18.024  1.00 22.62  ? 78  VAL A CG2 1 
ATOM   644  N  N   . LEU A 1 79  ? -19.913 8.235   18.939  1.00 13.45  ? 79  LEU A N   1 
ATOM   645  C  CA  . LEU A 1 79  ? -19.934 7.352   20.097  1.00 14.45  ? 79  LEU A CA  1 
ATOM   646  C  C   . LEU A 1 79  ? -19.952 8.207   21.348  1.00 12.67  ? 79  LEU A C   1 
ATOM   647  O  O   . LEU A 1 79  ? -19.091 9.137   21.470  1.00 14.09  ? 79  LEU A O   1 
ATOM   648  C  CB  . LEU A 1 79  ? -18.671 6.441   20.037  1.00 14.68  ? 79  LEU A CB  1 
ATOM   649  C  CG  . LEU A 1 79  ? -18.550 5.399   21.072  1.00 14.27  ? 79  LEU A CG  1 
ATOM   650  C  CD1 . LEU A 1 79  ? -19.585 4.300   20.860  1.00 20.78  ? 79  LEU A CD1 1 
ATOM   651  C  CD2 . LEU A 1 79  ? -17.184 4.730   21.033  1.00 13.98  ? 79  LEU A CD2 1 
ATOM   652  N  N   . LYS A 1 80  ? -20.774 7.870   22.304  1.00 14.37  ? 80  LYS A N   1 
ATOM   653  C  CA  . LYS A 1 80  ? -20.837 8.580   23.588  1.00 15.27  ? 80  LYS A CA  1 
ATOM   654  C  C   . LYS A 1 80  ? -21.377 7.653   24.654  1.00 14.80  ? 80  LYS A C   1 
ATOM   655  O  O   . LYS A 1 80  ? -21.678 6.488   24.329  1.00 14.36  ? 80  LYS A O   1 
ATOM   656  C  CB  . LYS A 1 80  ? -21.580 9.891   23.522  1.00 19.21  ? 80  LYS A CB  1 
ATOM   657  C  CG  . LYS A 1 80  ? -22.994 9.670   23.314  1.00 19.89  ? 80  LYS A CG  1 
ATOM   658  C  CD  . LYS A 1 80  ? -23.706 11.007  22.996  1.00 27.24  ? 80  LYS A CD  1 
ATOM   659  C  CE  . LYS A 1 80  ? -22.859 11.658  21.924  1.00 42.48  ? 80  LYS A CE  1 
ATOM   660  N  NZ  . LYS A 1 80  ? -23.555 12.510  20.903  1.00 66.04  ? 80  LYS A NZ  1 
ATOM   661  N  N   . GLY A 1 81  ? -21.496 8.123   25.894  1.00 15.42  ? 81  GLY A N   1 
ATOM   662  C  CA  . GLY A 1 81  ? -21.929 7.279   26.967  1.00 15.72  ? 81  GLY A CA  1 
ATOM   663  C  C   . GLY A 1 81  ? -20.956 6.241   27.245  1.00 15.36  ? 81  GLY A C   1 
ATOM   664  O  O   . GLY A 1 81  ? -19.757 6.462   27.073  1.00 14.96  ? 81  GLY A O   1 
ATOM   665  N  N   . GLY A 1 82  ? -21.424 5.129   27.757  1.00 18.92  ? 82  GLY A N   1 
ATOM   666  C  CA  . GLY A 1 82  ? -20.451 4.162   28.168  1.00 19.95  ? 82  GLY A CA  1 
ATOM   667  C  C   . GLY A 1 82  ? -19.618 4.750   29.274  1.00 18.01  ? 82  GLY A C   1 
ATOM   668  O  O   . GLY A 1 82  ? -20.106 5.436   30.181  1.00 23.07  ? 82  GLY A O   1 
ATOM   669  N  N   . PRO A 1 83  ? -18.274 4.553   29.184  1.00 16.67  ? 83  PRO A N   1 
ATOM   670  C  CA  . PRO A 1 83  ? -17.367 5.128   30.129  1.00 15.81  ? 83  PRO A CA  1 
ATOM   671  C  C   . PRO A 1 83  ? -16.947 6.543   29.740  1.00 16.53  ? 83  PRO A C   1 
ATOM   672  O  O   . PRO A 1 83  ? -16.122 7.140   30.440  1.00 18.81  ? 83  PRO A O   1 
ATOM   673  C  CB  . PRO A 1 83  ? -16.067 4.205   29.973  1.00 16.35  ? 83  PRO A CB  1 
ATOM   674  C  CG  . PRO A 1 83  ? -16.069 3.930   28.510  1.00 15.16  ? 83  PRO A CG  1 
ATOM   675  C  CD  . PRO A 1 83  ? -17.554 3.735   28.182  1.00 14.58  ? 83  PRO A CD  1 
ATOM   676  N  N   . LEU A 1 84  ? -17.454 7.068   28.621  1.00 13.91  ? 84  LEU A N   1 
ATOM   677  C  CA  . LEU A 1 84  ? -16.900 8.281   28.028  1.00 13.73  ? 84  LEU A CA  1 
ATOM   678  C  C   . LEU A 1 84  ? -17.517 9.538   28.606  1.00 14.97  ? 84  LEU A C   1 
ATOM   679  O  O   . LEU A 1 84  ? -18.700 9.571   28.898  1.00 18.02  ? 84  LEU A O   1 
ATOM   680  C  CB  . LEU A 1 84  ? -17.158 8.282   26.541  1.00 12.15  ? 84  LEU A CB  1 
ATOM   681  C  CG  . LEU A 1 84  ? -16.554 7.026   25.809  1.00 12.04  ? 84  LEU A CG  1 
ATOM   682  C  CD1 . LEU A 1 84  ? -17.020 7.014   24.361  1.00 13.22  ? 84  LEU A CD1 1 
ATOM   683  C  CD2 . LEU A 1 84  ? -15.019 6.991   25.922  1.00 12.62  ? 84  LEU A CD2 1 
ATOM   684  N  N   . ASP A 1 85  ? -16.770 10.624  28.627  1.00 17.09  ? 85  ASP A N   1 
ATOM   685  C  CA  . ASP A 1 85  ? -17.263 11.994  28.870  1.00 20.00  ? 85  ASP A CA  1 
ATOM   686  C  C   . ASP A 1 85  ? -17.226 12.586  27.493  1.00 20.23  ? 85  ASP A C   1 
ATOM   687  O  O   . ASP A 1 85  ? -16.206 12.579  26.792  1.00 26.42  ? 85  ASP A O   1 
ATOM   688  C  CB  . ASP A 1 85  ? -16.283 12.673  29.845  1.00 26.47  ? 85  ASP A CB  1 
ATOM   689  C  CG  . ASP A 1 85  ? -16.404 12.146  31.253  1.00 30.21  ? 85  ASP A CG  1 
ATOM   690  O  OD1 . ASP A 1 85  ? -17.504 11.579  31.640  1.00 44.99  ? 85  ASP A OD1 1 
ATOM   691  O  OD2 . ASP A 1 85  ? -15.387 12.342  32.013  1.00 48.17  ? 85  ASP A OD2 1 
ATOM   692  N  N   . GLY A 1 86  ? -18.273 13.228  27.081  1.00 26.09  ? 86  GLY A N   1 
ATOM   693  C  CA  . GLY A 1 86  ? -18.215 13.820  25.824  1.00 25.49  ? 86  GLY A CA  1 
ATOM   694  C  C   . GLY A 1 86  ? -18.460 12.904  24.621  1.00 23.02  ? 86  GLY A C   1 
ATOM   695  O  O   . GLY A 1 86  ? -18.948 11.765  24.670  1.00 27.73  ? 86  GLY A O   1 
ATOM   696  N  N   A THR A 1 87  ? -18.179 13.527  23.482  0.50 16.00  ? 87  THR A N   1 
ATOM   697  N  N   B THR A 1 87  ? -18.133 13.450  23.496  0.50 14.65  ? 87  THR A N   1 
ATOM   698  C  CA  A THR A 1 87  ? -18.582 13.036  22.129  0.50 18.27  ? 87  THR A CA  1 
ATOM   699  C  CA  B THR A 1 87  ? -18.558 12.783  22.295  0.50 14.11  ? 87  THR A CA  1 
ATOM   700  C  C   A THR A 1 87  ? -17.390 12.667  21.257  0.50 15.03  ? 87  THR A C   1 
ATOM   701  C  C   B THR A 1 87  ? -17.384 12.588  21.400  0.50 12.68  ? 87  THR A C   1 
ATOM   702  O  O   A THR A 1 87  ? -16.454 13.474  21.094  0.50 14.82  ? 87  THR A O   1 
ATOM   703  O  O   B THR A 1 87  ? -16.476 13.429  21.360  0.50 13.47  ? 87  THR A O   1 
ATOM   704  C  CB  A THR A 1 87  ? -19.357 14.143  21.346  0.50 18.08  ? 87  THR A CB  1 
ATOM   705  C  CB  B THR A 1 87  ? -19.602 13.675  21.602  0.50 14.70  ? 87  THR A CB  1 
ATOM   706  O  OG1 A THR A 1 87  ? -20.605 14.425  21.976  0.50 22.25  ? 87  THR A OG1 1 
ATOM   707  O  OG1 B THR A 1 87  ? -19.021 14.969  21.421  0.50 15.00  ? 87  THR A OG1 1 
ATOM   708  C  CG2 A THR A 1 87  ? -19.600 13.783  19.908  0.50 19.73  ? 87  THR A CG2 1 
ATOM   709  C  CG2 B THR A 1 87  ? -20.783 13.849  22.478  0.50 16.78  ? 87  THR A CG2 1 
ATOM   710  N  N   . TYR A 1 88  ? -17.436 11.455  20.736  1.00 12.17  ? 88  TYR A N   1 
ATOM   711  C  CA  . TYR A 1 88  ? -16.297 10.974  19.934  1.00 11.58  ? 88  TYR A CA  1 
ATOM   712  C  C   . TYR A 1 88  ? -16.773 10.675  18.531  1.00 11.36  ? 88  TYR A C   1 
ATOM   713  O  O   . TYR A 1 88  ? -17.774 9.942   18.372  1.00 15.52  ? 88  TYR A O   1 
ATOM   714  C  CB  . TYR A 1 88  ? -15.654 9.740   20.542  1.00 11.30  ? 88  TYR A CB  1 
ATOM   715  C  CG  . TYR A 1 88  ? -14.941 9.964   21.850  1.00 10.36  ? 88  TYR A CG  1 
ATOM   716  C  CD1 . TYR A 1 88  ? -15.605 10.282  23.047  1.00 11.86  ? 88  TYR A CD1 1 
ATOM   717  C  CD2 . TYR A 1 88  ? -13.535 9.833   21.892  1.00 10.11  ? 88  TYR A CD2 1 
ATOM   718  C  CE1 . TYR A 1 88  ? -14.896 10.479  24.227  1.00 11.47  ? 88  TYR A CE1 1 
ATOM   719  C  CE2 . TYR A 1 88  ? -12.844 9.955   23.081  1.00 10.00  ? 88  TYR A CE2 1 
ATOM   720  C  CZ  . TYR A 1 88  ? -13.518 10.254  24.258  1.00 10.80  ? 88  TYR A CZ  1 
ATOM   721  O  OH  . TYR A 1 88  ? -12.793 10.374  25.417  1.00 11.08  ? 88  TYR A OH  1 
ATOM   722  N  N   . ARG A 1 89  ? -16.141 11.179  17.510  1.00 10.71  ? 89  ARG A N   1 
ATOM   723  C  CA  . ARG A 1 89  ? -16.585 11.051  16.135  1.00 11.83  ? 89  ARG A CA  1 
ATOM   724  C  C   . ARG A 1 89  ? -15.814 9.968   15.424  1.00 9.80   ? 89  ARG A C   1 
ATOM   725  O  O   . ARG A 1 89  ? -14.593 9.877   15.496  1.00 9.94   ? 89  ARG A O   1 
ATOM   726  C  CB  . ARG A 1 89  ? -16.239 12.383  15.468  1.00 14.57  ? 89  ARG A CB  1 
ATOM   727  C  CG  . ARG A 1 89  ? -17.082 12.506  14.232  1.00 16.94  ? 89  ARG A CG  1 
ATOM   728  C  CD  . ARG A 1 89  ? -16.885 13.923  13.699  1.00 18.24  ? 89  ARG A CD  1 
ATOM   729  N  NE  . ARG A 1 89  ? -17.531 14.955  14.512  1.00 19.97  ? 89  ARG A NE  1 
ATOM   730  C  CZ  . ARG A 1 89  ? -17.380 16.266  14.335  1.00 16.43  ? 89  ARG A CZ  1 
ATOM   731  N  NH1 . ARG A 1 89  ? -16.605 16.734  13.367  1.00 21.38  ? 89  ARG A NH1 1 
ATOM   732  N  NH2 . ARG A 1 89  ? -18.009 17.116  15.135  1.00 19.54  ? 89  ARG A NH2 1 
ATOM   733  N  N   . LEU A 1 90  ? -16.584 9.145   14.702  1.00 10.44  ? 90  LEU A N   1 
ATOM   734  C  CA  . LEU A 1 90  ? -15.988 8.055   13.914  1.00 10.21  ? 90  LEU A CA  1 
ATOM   735  C  C   . LEU A 1 90  ? -15.146 8.606   12.767  1.00 10.66  ? 90  LEU A C   1 
ATOM   736  O  O   . LEU A 1 90  ? -15.634 9.405   11.933  1.00 12.45  ? 90  LEU A O   1 
ATOM   737  C  CB  . LEU A 1 90  ? -17.084 7.200   13.343  1.00 11.55  ? 90  LEU A CB  1 
ATOM   738  C  CG  . LEU A 1 90  ? -16.670 6.018   12.451  1.00 11.81  ? 90  LEU A CG  1 
ATOM   739  C  CD1 . LEU A 1 90  ? -15.909 4.941   13.274  1.00 12.01  ? 90  LEU A CD1 1 
ATOM   740  C  CD2 . LEU A 1 90  ? -17.886 5.356   11.802  1.00 14.09  ? 90  LEU A CD2 1 
ATOM   741  N  N   . ILE A 1 91  ? -13.926 8.167   12.670  1.00 10.04  ? 91  ILE A N   1 
ATOM   742  C  CA  . ILE A 1 91  ? -13.052 8.503   11.561  1.00 10.48  ? 91  ILE A CA  1 
ATOM   743  C  C   . ILE A 1 91  ? -12.770 7.357   10.636  1.00 9.33   ? 91  ILE A C   1 
ATOM   744  O  O   . ILE A 1 91  ? -12.637 7.519   9.429   1.00 10.55  ? 91  ILE A O   1 
ATOM   745  C  CB  . ILE A 1 91  ? -11.731 9.188   12.077  1.00 11.50  ? 91  ILE A CB  1 
ATOM   746  C  CG1 . ILE A 1 91  ? -10.806 9.553   10.869  1.00 14.32  ? 91  ILE A CG1 1 
ATOM   747  C  CG2 . ILE A 1 91  ? -10.983 8.362   13.135  1.00 12.11  ? 91  ILE A CG2 1 
ATOM   748  C  CD1 . ILE A 1 91  ? -9.716  10.542  11.264  1.00 16.27  ? 91  ILE A CD1 1 
ATOM   749  N  N   . GLN A 1 92  ? -12.594 6.117   11.176  1.00 10.22  ? 92  GLN A N   1 
ATOM   750  C  CA  . GLN A 1 92  ? -12.279 4.954   10.320  1.00 10.59  ? 92  GLN A CA  1 
ATOM   751  C  C   . GLN A 1 92  ? -12.522 3.713   11.100  1.00 9.16   ? 92  GLN A C   1 
ATOM   752  O  O   . GLN A 1 92  ? -12.599 3.731   12.323  1.00 9.43   ? 92  GLN A O   1 
ATOM   753  C  CB  . GLN A 1 92  ? -10.847 4.983   9.819   1.00 11.78  ? 92  GLN A CB  1 
ATOM   754  C  CG  . GLN A 1 92  ? -9.759  5.102   10.936  1.00 12.80  ? 92  GLN A CG  1 
ATOM   755  C  CD  . GLN A 1 92  ? -8.997  3.831   11.198  1.00 11.72  ? 92  GLN A CD  1 
ATOM   756  O  OE1 . GLN A 1 92  ? -9.554  2.709   11.164  1.00 11.70  ? 92  GLN A OE1 1 
ATOM   757  N  NE2 . GLN A 1 92  ? -7.758  3.987   11.603  1.00 13.77  ? 92  GLN A NE2 1 
ATOM   758  N  N   . PHE A 1 93  ? -12.688 2.595   10.372  1.00 9.65   ? 93  PHE A N   1 
ATOM   759  C  CA  . PHE A 1 93  ? -12.585 1.299   10.983  1.00 9.81   ? 93  PHE A CA  1 
ATOM   760  C  C   . PHE A 1 93  ? -11.627 0.480   10.185  1.00 9.50   ? 93  PHE A C   1 
ATOM   761  O  O   . PHE A 1 93  ? -11.393 0.657   8.970   1.00 11.31  ? 93  PHE A O   1 
ATOM   762  C  CB  . PHE A 1 93  ? -13.935 0.617   11.199  1.00 9.92   ? 93  PHE A CB  1 
ATOM   763  C  CG  . PHE A 1 93  ? -14.676 0.135   9.978   1.00 10.55  ? 93  PHE A CG  1 
ATOM   764  C  CD1 . PHE A 1 93  ? -14.309 -1.006  9.312   1.00 11.81  ? 93  PHE A CD1 1 
ATOM   765  C  CD2 . PHE A 1 93  ? -15.786 0.874   9.543   1.00 12.09  ? 93  PHE A CD2 1 
ATOM   766  C  CE1 . PHE A 1 93  ? -14.996 -1.435  8.186   1.00 12.14  ? 93  PHE A CE1 1 
ATOM   767  C  CE2 . PHE A 1 93  ? -16.555 0.400   8.431   1.00 12.96  ? 93  PHE A CE2 1 
ATOM   768  C  CZ  . PHE A 1 93  ? -16.151 -0.748  7.777   1.00 12.89  ? 93  PHE A CZ  1 
ATOM   769  N  N   . HIS A 1 94  ? -11.110 -0.580  10.854  1.00 9.69   ? 94  HIS A N   1 
ATOM   770  C  CA  . HIS A 1 94  ? -10.218 -1.528  10.231  1.00 9.16   ? 94  HIS A CA  1 
ATOM   771  C  C   . HIS A 1 94  ? -10.300 -2.822  11.069  1.00 8.53   ? 94  HIS A C   1 
ATOM   772  O  O   . HIS A 1 94  ? -10.904 -2.832  12.131  1.00 8.68   ? 94  HIS A O   1 
ATOM   773  C  CB  . HIS A 1 94  ? -8.785  -1.042  10.190  1.00 9.44   ? 94  HIS A CB  1 
ATOM   774  C  CG  . HIS A 1 94  ? -8.249  -0.762  11.547  1.00 9.16   ? 94  HIS A CG  1 
ATOM   775  N  ND1 . HIS A 1 94  ? -8.382  0.437   12.188  1.00 9.45   ? 94  HIS A ND1 1 
ATOM   776  C  CD2 . HIS A 1 94  ? -7.601  -1.585  12.457  1.00 9.51   ? 94  HIS A CD2 1 
ATOM   777  C  CE1 . HIS A 1 94  ? -7.964  0.328   13.415  1.00 8.79   ? 94  HIS A CE1 1 
ATOM   778  N  NE2 . HIS A 1 94  ? -7.434  -0.908  13.634  1.00 8.92   ? 94  HIS A NE2 1 
ATOM   779  N  N   . PHE A 1 95  ? -9.616  -3.849  10.602  1.00 9.45   ? 95  PHE A N   1 
ATOM   780  C  CA  . PHE A 1 95  ? -9.559  -5.152  11.287  1.00 8.98   ? 95  PHE A CA  1 
ATOM   781  C  C   . PHE A 1 95  ? -8.121  -5.567  11.488  1.00 8.84   ? 95  PHE A C   1 
ATOM   782  O  O   . PHE A 1 95  ? -7.209  -5.117  10.800  1.00 9.81   ? 95  PHE A O   1 
ATOM   783  C  CB  . PHE A 1 95  ? -10.307 -6.246  10.439  1.00 9.80   ? 95  PHE A CB  1 
ATOM   784  C  CG  . PHE A 1 95  ? -11.722 -5.943  10.142  1.00 9.51   ? 95  PHE A CG  1 
ATOM   785  C  CD1 . PHE A 1 95  ? -12.052 -5.085  9.084   1.00 10.94  ? 95  PHE A CD1 1 
ATOM   786  C  CD2 . PHE A 1 95  ? -12.753 -6.586  10.802  1.00 10.02  ? 95  PHE A CD2 1 
ATOM   787  C  CE1 . PHE A 1 95  ? -13.336 -4.878  8.718   1.00 11.77  ? 95  PHE A CE1 1 
ATOM   788  C  CE2 . PHE A 1 95  ? -14.072 -6.389  10.465  1.00 11.13  ? 95  PHE A CE2 1 
ATOM   789  C  CZ  . PHE A 1 95  ? -14.375 -5.533  9.383   1.00 11.75  ? 95  PHE A CZ  1 
ATOM   790  N  N   . HIS A 1 96  ? -7.986  -6.545  12.400  1.00 8.54   ? 96  HIS A N   1 
ATOM   791  C  CA  . HIS A 1 96  ? -6.783  -7.357  12.568  1.00 9.15   ? 96  HIS A CA  1 
ATOM   792  C  C   . HIS A 1 96  ? -7.221  -8.808  12.447  1.00 8.57   ? 96  HIS A C   1 
ATOM   793  O  O   . HIS A 1 96  ? -8.287  -9.137  12.948  1.00 9.12   ? 96  HIS A O   1 
ATOM   794  C  CB  . HIS A 1 96  ? -6.128  -7.121  13.940  1.00 8.60   ? 96  HIS A CB  1 
ATOM   795  C  CG  . HIS A 1 96  ? -5.801  -5.688  14.199  1.00 8.64   ? 96  HIS A CG  1 
ATOM   796  N  ND1 . HIS A 1 96  ? -4.597  -5.133  14.038  1.00 9.64   ? 96  HIS A ND1 1 
ATOM   797  C  CD2 . HIS A 1 96  ? -6.649  -4.654  14.604  1.00 8.46   ? 96  HIS A CD2 1 
ATOM   798  C  CE1 . HIS A 1 96  ? -4.657  -3.806  14.334  1.00 10.28  ? 96  HIS A CE1 1 
ATOM   799  N  NE2 . HIS A 1 96  ? -5.912  -3.493  14.658  1.00 8.54   ? 96  HIS A NE2 1 
ATOM   800  N  N   . TRP A 1 97  ? -6.442  -9.656  11.776  1.00 8.35   ? 97  TRP A N   1 
ATOM   801  C  CA  . TRP A 1 97  ? -6.850  -11.037 11.592  1.00 9.14   ? 97  TRP A CA  1 
ATOM   802  C  C   . TRP A 1 97  ? -5.657  -11.949 11.444  1.00 9.09   ? 97  TRP A C   1 
ATOM   803  O  O   . TRP A 1 97  ? -4.493  -11.500 11.351  1.00 9.66   ? 97  TRP A O   1 
ATOM   804  C  CB  . TRP A 1 97  ? -7.778  -11.114 10.352  1.00 9.77   ? 97  TRP A CB  1 
ATOM   805  C  CG  . TRP A 1 97  ? -7.118  -10.746 9.041   1.00 9.65   ? 97  TRP A CG  1 
ATOM   806  C  CD1 . TRP A 1 97  ? -6.434  -11.548 8.193   1.00 10.60  ? 97  TRP A CD1 1 
ATOM   807  C  CD2 . TRP A 1 97  ? -7.055  -9.433  8.470   1.00 10.06  ? 97  TRP A CD2 1 
ATOM   808  N  NE1 . TRP A 1 97  ? -5.999  -10.837 7.075   1.00 11.52  ? 97  TRP A NE1 1 
ATOM   809  C  CE2 . TRP A 1 97  ? -6.361  -9.526  7.243   1.00 10.87  ? 97  TRP A CE2 1 
ATOM   810  C  CE3 . TRP A 1 97  ? -7.543  -8.160  8.873   1.00 9.89   ? 97  TRP A CE3 1 
ATOM   811  C  CZ2 . TRP A 1 97  ? -6.156  -8.428  6.406   1.00 11.53  ? 97  TRP A CZ2 1 
ATOM   812  C  CZ3 . TRP A 1 97  ? -7.322  -7.052  8.036   1.00 11.07  ? 97  TRP A CZ3 1 
ATOM   813  C  CH2 . TRP A 1 97  ? -6.659  -7.191  6.808   1.00 11.25  ? 97  TRP A CH2 1 
ATOM   814  N  N   . GLY A 1 98  ? -5.948  -13.253 11.440  1.00 9.57   ? 98  GLY A N   1 
ATOM   815  C  CA  . GLY A 1 98  ? -4.908  -14.237 11.486  1.00 10.36  ? 98  GLY A CA  1 
ATOM   816  C  C   . GLY A 1 98  ? -4.714  -14.947 10.157  1.00 10.10  ? 98  GLY A C   1 
ATOM   817  O  O   . GLY A 1 98  ? -5.443  -14.788 9.186   1.00 11.52  ? 98  GLY A O   1 
ATOM   818  N  N   . SER A 1 99  ? -3.682  -15.795 10.166  1.00 10.98  ? 99  SER A N   1 
ATOM   819  C  CA  . SER A 1 99  ? -3.460  -16.751 9.064   1.00 12.74  ? 99  SER A CA  1 
ATOM   820  C  C   . SER A 1 99  ? -4.334  -17.987 9.191   1.00 13.43  ? 99  SER A C   1 
ATOM   821  O  O   . SER A 1 99  ? -4.462  -18.708 8.205   1.00 15.99  ? 99  SER A O   1 
ATOM   822  C  CB  . SER A 1 99  ? -2.024  -17.109 9.023   1.00 14.60  ? 99  SER A CB  1 
ATOM   823  O  OG  . SER A 1 99  ? -1.564  -17.630 10.280  1.00 14.31  ? 99  SER A OG  1 
ATOM   824  N  N   . LEU A 1 100 ? -4.943  -18.187 10.353  1.00 12.76  ? 100 LEU A N   1 
ATOM   825  C  CA  . LEU A 1 100 ? -5.726  -19.364 10.684  1.00 14.18  ? 100 LEU A CA  1 
ATOM   826  C  C   . LEU A 1 100 ? -6.853  -18.898 11.523  1.00 12.96  ? 100 LEU A C   1 
ATOM   827  O  O   . LEU A 1 100 ? -6.693  -17.876 12.223  1.00 12.44  ? 100 LEU A O   1 
ATOM   828  C  CB  . LEU A 1 100 ? -4.870  -20.331 11.626  1.00 20.12  ? 100 LEU A CB  1 
ATOM   829  C  CG  . LEU A 1 100 ? -3.553  -20.752 11.031  1.00 21.79  ? 100 LEU A CG  1 
ATOM   830  C  CD1 . LEU A 1 100 ? -2.579  -21.275 12.082  1.00 31.07  ? 100 LEU A CD1 1 
ATOM   831  C  CD2 . LEU A 1 100 ? -3.933  -21.812 9.977   1.00 30.55  ? 100 LEU A CD2 1 
ATOM   832  N  N   . ASP A 1 101 ? -7.970  -19.577 11.528  1.00 13.32  ? 101 ASP A N   1 
ATOM   833  C  CA  . ASP A 1 101 ? -9.124  -19.158 12.352  1.00 12.66  ? 101 ASP A CA  1 
ATOM   834  C  C   . ASP A 1 101 ? -8.878  -19.055 13.840  1.00 12.80  ? 101 ASP A C   1 
ATOM   835  O  O   . ASP A 1 101 ? -9.546  -18.351 14.528  1.00 15.03  ? 101 ASP A O   1 
ATOM   836  C  CB  . ASP A 1 101 ? -10.338 -20.077 12.127  1.00 13.91  ? 101 ASP A CB  1 
ATOM   837  C  CG  . ASP A 1 101 ? -10.831 -20.080 10.682  1.00 16.28  ? 101 ASP A CG  1 
ATOM   838  O  OD1 . ASP A 1 101 ? -10.428 -19.209 9.887   1.00 15.79  ? 101 ASP A OD1 1 
ATOM   839  O  OD2 . ASP A 1 101 ? -11.644 -20.972 10.353  1.00 20.42  ? 101 ASP A OD2 1 
ATOM   840  N  N   . GLY A 1 102 ? -7.865  -19.823 14.317  1.00 13.52  ? 102 GLY A N   1 
ATOM   841  C  CA  . GLY A 1 102 ? -7.602  -19.840 15.722  1.00 15.01  ? 102 GLY A CA  1 
ATOM   842  C  C   . GLY A 1 102 ? -6.755  -18.671 16.258  1.00 13.19  ? 102 GLY A C   1 
ATOM   843  O  O   . GLY A 1 102 ? -6.416  -18.687 17.446  1.00 13.80  ? 102 GLY A O   1 
ATOM   844  N  N   . GLN A 1 103 ? -6.462  -17.653 15.454  1.00 11.44  ? 103 GLN A N   1 
ATOM   845  C  CA  . GLN A 1 103 ? -5.744  -16.506 15.930  1.00 10.92  ? 103 GLN A CA  1 
ATOM   846  C  C   . GLN A 1 103 ? -6.139  -15.334 15.088  1.00 10.16  ? 103 GLN A C   1 
ATOM   847  O  O   . GLN A 1 103 ? -6.667  -15.513 13.996  1.00 10.95  ? 103 GLN A O   1 
ATOM   848  C  CB  . GLN A 1 103 ? -4.228  -16.718 15.968  1.00 11.90  ? 103 GLN A CB  1 
ATOM   849  C  CG  . GLN A 1 103 ? -3.654  -16.903 14.563  1.00 12.60  ? 103 GLN A CG  1 
ATOM   850  C  CD  . GLN A 1 103 ? -2.264  -17.509 14.599  1.00 15.83  ? 103 GLN A CD  1 
ATOM   851  O  OE1 . GLN A 1 103 ? -2.126  -18.510 15.280  1.00 26.36  ? 103 GLN A OE1 1 
ATOM   852  N  NE2 . GLN A 1 103 ? -1.369  -17.047 13.868  1.00 15.89  ? 103 GLN A NE2 1 
ATOM   853  N  N   . GLY A 1 104 ? -5.817  -14.121 15.556  1.00 9.55   ? 104 GLY A N   1 
ATOM   854  C  CA  . GLY A 1 104 ? -6.107  -12.913 14.774  1.00 9.70   ? 104 GLY A CA  1 
ATOM   855  C  C   . GLY A 1 104 ? -6.571  -11.757 15.612  1.00 8.90   ? 104 GLY A C   1 
ATOM   856  O  O   . GLY A 1 104 ? -6.270  -10.608 15.270  1.00 9.95   ? 104 GLY A O   1 
ATOM   857  N  N   . SER A 1 105 ? -7.252  -12.004 16.736  1.00 8.72   ? 105 SER A N   1 
ATOM   858  C  CA  . SER A 1 105 ? -7.648  -10.884 17.560  1.00 8.70   ? 105 SER A CA  1 
ATOM   859  C  C   . SER A 1 105 ? -6.414  -10.338 18.315  1.00 7.47   ? 105 SER A C   1 
ATOM   860  O  O   . SER A 1 105 ? -5.407  -11.017 18.533  1.00 9.29   ? 105 SER A O   1 
ATOM   861  C  CB  . SER A 1 105 ? -8.771  -11.230 18.498  1.00 8.89   ? 105 SER A CB  1 
ATOM   862  O  OG  . SER A 1 105 ? -8.428  -12.195 19.487  1.00 9.57   ? 105 SER A OG  1 
ATOM   863  N  N   . GLU A 1 106 ? -6.575  -9.087  18.722  1.00 8.01   ? 106 GLU A N   1 
ATOM   864  C  CA  . GLU A 1 106 ? -5.561  -8.377  19.536  1.00 7.91   ? 106 GLU A CA  1 
ATOM   865  C  C   . GLU A 1 106 ? -5.905  -8.540  21.011  1.00 7.70   ? 106 GLU A C   1 
ATOM   866  O  O   . GLU A 1 106 ? -5.091  -9.136  21.780  1.00 8.81   ? 106 GLU A O   1 
ATOM   867  C  CB  . GLU A 1 106 ? -5.496  -6.913  19.101  1.00 7.92   ? 106 GLU A CB  1 
ATOM   868  C  CG  . GLU A 1 106 ? -5.071  -6.803  17.695  1.00 9.55   ? 106 GLU A CG  1 
ATOM   869  C  CD  . GLU A 1 106 ? -4.356  -5.524  17.391  1.00 9.05   ? 106 GLU A CD  1 
ATOM   870  O  OE1 . GLU A 1 106 ? -4.969  -4.454  17.633  1.00 8.48   ? 106 GLU A OE1 1 
ATOM   871  O  OE2 . GLU A 1 106 ? -3.208  -5.564  16.920  1.00 10.55  ? 106 GLU A OE2 1 
ATOM   872  N  N   . HIS A 1 107 ? -7.069  -8.113  21.449  1.00 8.01   ? 107 HIS A N   1 
ATOM   873  C  CA  . HIS A 1 107 ? -7.527  -8.483  22.741  1.00 7.92   ? 107 HIS A CA  1 
ATOM   874  C  C   . HIS A 1 107 ? -7.800  -10.014 22.754  1.00 7.75   ? 107 HIS A C   1 
ATOM   875  O  O   . HIS A 1 107 ? -8.165  -10.596 21.733  1.00 8.65   ? 107 HIS A O   1 
ATOM   876  C  CB  . HIS A 1 107 ? -8.785  -7.686  23.137  1.00 8.53   ? 107 HIS A CB  1 
ATOM   877  C  CG  . HIS A 1 107 ? -8.469  -6.235  23.283  1.00 8.04   ? 107 HIS A CG  1 
ATOM   878  N  ND1 . HIS A 1 107 ? -8.535  -5.339  22.228  1.00 8.54   ? 107 HIS A ND1 1 
ATOM   879  C  CD2 . HIS A 1 107 ? -7.992  -5.528  24.355  1.00 8.10   ? 107 HIS A CD2 1 
ATOM   880  C  CE1 . HIS A 1 107 ? -8.041  -4.145  22.667  1.00 8.54   ? 107 HIS A CE1 1 
ATOM   881  N  NE2 . HIS A 1 107 ? -7.772  -4.225  23.953  1.00 8.02   ? 107 HIS A NE2 1 
ATOM   882  N  N   . THR A 1 108 ? -7.715  -10.561 23.952  1.00 8.92   ? 108 THR A N   1 
ATOM   883  C  CA  . THR A 1 108 ? -8.104  -11.932 24.220  1.00 8.55   ? 108 THR A CA  1 
ATOM   884  C  C   . THR A 1 108 ? -9.019  -11.947 25.415  1.00 8.36   ? 108 THR A C   1 
ATOM   885  O  O   . THR A 1 108 ? -9.040  -10.976 26.201  1.00 9.46   ? 108 THR A O   1 
ATOM   886  C  CB  . THR A 1 108 ? -6.853  -12.852 24.399  1.00 9.51   ? 108 THR A CB  1 
ATOM   887  O  OG1 . THR A 1 108 ? -6.009  -12.348 25.449  1.00 10.29  ? 108 THR A OG1 1 
ATOM   888  C  CG2 . THR A 1 108 ? -6.094  -12.887 23.109  1.00 10.35  ? 108 THR A CG2 1 
ATOM   889  N  N   . VAL A 1 109 ? -9.796  -13.014 25.560  1.00 9.37   ? 109 VAL A N   1 
ATOM   890  C  CA  . VAL A 1 109 ? -10.796 -13.119 26.639  1.00 9.86   ? 109 VAL A CA  1 
ATOM   891  C  C   . VAL A 1 109 ? -10.438 -14.395 27.371  1.00 10.44  ? 109 VAL A C   1 
ATOM   892  O  O   . VAL A 1 109 ? -10.620 -15.501 26.823  1.00 10.88  ? 109 VAL A O   1 
ATOM   893  C  CB  . VAL A 1 109 ? -12.233 -13.121 26.092  1.00 10.81  ? 109 VAL A CB  1 
ATOM   894  C  CG1 . VAL A 1 109 ? -13.226 -13.247 27.210  1.00 12.09  ? 109 VAL A CG1 1 
ATOM   895  C  CG2 . VAL A 1 109 ? -12.491 -11.838 25.258  1.00 12.51  ? 109 VAL A CG2 1 
ATOM   896  N  N   . ASP A 1 110 ? -9.957  -14.278 28.600  1.00 11.21  ? 110 ASP A N   1 
ATOM   897  C  CA  . ASP A 1 110 ? -9.464  -15.501 29.313  1.00 12.12  ? 110 ASP A CA  1 
ATOM   898  C  C   . ASP A 1 110 ? -8.532  -16.307 28.409  1.00 11.97  ? 110 ASP A C   1 
ATOM   899  O  O   . ASP A 1 110 ? -8.594  -17.513 28.361  1.00 12.43  ? 110 ASP A O   1 
ATOM   900  C  CB  . ASP A 1 110 ? -10.621 -16.340 29.797  1.00 14.50  ? 110 ASP A CB  1 
ATOM   901  C  CG  . ASP A 1 110 ? -11.502 -15.571 30.809  1.00 14.84  ? 110 ASP A CG  1 
ATOM   902  O  OD1 . ASP A 1 110 ? -10.915 -14.699 31.542  1.00 15.99  ? 110 ASP A OD1 1 
ATOM   903  O  OD2 . ASP A 1 110 ? -12.671 -15.830 30.907  1.00 18.08  ? 110 ASP A OD2 1 
ATOM   904  N  N   . LYS A 1 111 ? -7.660  -15.569 27.720  1.00 10.98  ? 111 LYS A N   1 
ATOM   905  C  CA  . LYS A 1 111 ? -6.613  -16.092 26.827  1.00 11.50  ? 111 LYS A CA  1 
ATOM   906  C  C   . LYS A 1 111 ? -7.193  -16.643 25.508  1.00 11.07  ? 111 LYS A C   1 
ATOM   907  O  O   . LYS A 1 111 ? -6.403  -16.985 24.607  1.00 12.48  ? 111 LYS A O   1 
ATOM   908  C  CB  . LYS A 1 111 ? -5.685  -17.159 27.489  1.00 13.37  ? 111 LYS A CB  1 
ATOM   909  C  CG  . LYS A 1 111 ? -5.013  -16.624 28.747  1.00 18.05  ? 111 LYS A CG  1 
ATOM   910  C  CD  . LYS A 1 111 ? -4.102  -15.413 28.401  1.00 20.56  ? 111 LYS A CD  1 
ATOM   911  C  CE  . LYS A 1 111 ? -3.261  -14.814 29.543  1.00 23.56  ? 111 LYS A CE  1 
ATOM   912  N  NZ  . LYS A 1 111 ? -2.148  -15.718 29.762  1.00 25.97  ? 111 LYS A NZ  1 
ATOM   913  N  N   . LYS A 1 112 ? -8.509  -16.601 25.315  1.00 10.55  ? 112 LYS A N   1 
ATOM   914  C  CA  . LYS A 1 112 ? -9.055  -16.995 24.021  1.00 11.64  ? 112 LYS A CA  1 
ATOM   915  C  C   . LYS A 1 112 ? -8.717  -15.964 22.953  1.00 10.03  ? 112 LYS A C   1 
ATOM   916  O  O   . LYS A 1 112 ? -9.020  -14.747 23.140  1.00 10.60  ? 112 LYS A O   1 
ATOM   917  C  CB  . LYS A 1 112 ? -10.607 -17.085 24.093  1.00 12.33  ? 112 LYS A CB  1 
ATOM   918  C  CG  . LYS A 1 112 ? -11.308 -17.434 22.757  1.00 14.08  ? 112 LYS A CG  1 
ATOM   919  C  CD  . LYS A 1 112 ? -12.810 -17.369 22.858  1.00 16.59  ? 112 LYS A CD  1 
ATOM   920  C  CE  . LYS A 1 112 ? -13.455 -17.637 21.523  1.00 18.15  ? 112 LYS A CE  1 
ATOM   921  N  NZ  . LYS A 1 112 ? -13.253 -18.960 21.058  1.00 17.46  ? 112 LYS A NZ  1 
ATOM   922  N  N   A LYS A 1 113 ? -8.192  -16.406 21.842  0.50 10.05  ? 113 LYS A N   1 
ATOM   923  N  N   B LYS A 1 113 ? -8.247  -16.432 21.817  0.50 10.39  ? 113 LYS A N   1 
ATOM   924  C  CA  A LYS A 1 113 ? -8.060  -15.600 20.646  0.50 10.35  ? 113 LYS A CA  1 
ATOM   925  C  CA  B LYS A 1 113 ? -8.012  -15.633 20.606  0.50 10.72  ? 113 LYS A CA  1 
ATOM   926  C  C   A LYS A 1 113 ? -9.255  -15.854 19.757  0.50 9.60   ? 113 LYS A C   1 
ATOM   927  C  C   B LYS A 1 113 ? -9.079  -15.869 19.555  0.50 10.48  ? 113 LYS A C   1 
ATOM   928  O  O   A LYS A 1 113 ? -9.729  -16.994 19.612  0.50 10.11  ? 113 LYS A O   1 
ATOM   929  O  O   B LYS A 1 113 ? -9.340  -17.027 19.154  0.50 9.08   ? 113 LYS A O   1 
ATOM   930  C  CB  A LYS A 1 113 ? -6.800  -16.024 19.890  0.50 10.21  ? 113 LYS A CB  1 
ATOM   931  C  CB  B LYS A 1 113 ? -6.663  -16.018 20.000  0.50 11.43  ? 113 LYS A CB  1 
ATOM   932  C  CG  A LYS A 1 113 ? -5.474  -15.847 20.625  0.50 10.13  ? 113 LYS A CG  1 
ATOM   933  C  CG  B LYS A 1 113 ? -5.452  -15.573 20.793  0.50 12.39  ? 113 LYS A CG  1 
ATOM   934  C  CD  A LYS A 1 113 ? -4.292  -16.384 19.844  0.50 12.24  ? 113 LYS A CD  1 
ATOM   935  C  CD  B LYS A 1 113 ? -4.202  -16.260 20.299  0.50 12.53  ? 113 LYS A CD  1 
ATOM   936  C  CE  A LYS A 1 113 ? -2.968  -15.889 20.454  0.50 12.90  ? 113 LYS A CE  1 
ATOM   937  C  CE  B LYS A 1 113 ? -3.004  -15.605 20.989  0.50 15.79  ? 113 LYS A CE  1 
ATOM   938  N  NZ  A LYS A 1 113 ? -2.562  -16.479 21.789  0.50 15.79  ? 113 LYS A NZ  1 
ATOM   939  N  NZ  B LYS A 1 113 ? -1.809  -16.455 20.728  0.50 16.77  ? 113 LYS A NZ  1 
ATOM   940  N  N   . TYR A 1 114 ? -9.744  -14.788 19.135  1.00 9.30   ? 114 TYR A N   1 
ATOM   941  C  CA  . TYR A 1 114 ? -10.731 -14.834 18.122  1.00 9.46   ? 114 TYR A CA  1 
ATOM   942  C  C   . TYR A 1 114 ? -10.045 -14.792 16.710  1.00 9.22   ? 114 TYR A C   1 
ATOM   943  O  O   . TYR A 1 114 ? -8.849  -14.483 16.615  1.00 10.03  ? 114 TYR A O   1 
ATOM   944  C  CB  . TYR A 1 114 ? -11.791 -13.737 18.218  1.00 9.70   ? 114 TYR A CB  1 
ATOM   945  C  CG  . TYR A 1 114 ? -12.752 -13.944 19.377  1.00 9.68   ? 114 TYR A CG  1 
ATOM   946  C  CD1 . TYR A 1 114 ? -12.438 -13.536 20.676  1.00 11.08  ? 114 TYR A CD1 1 
ATOM   947  C  CD2 . TYR A 1 114 ? -13.973 -14.555 19.166  1.00 11.17  ? 114 TYR A CD2 1 
ATOM   948  C  CE1 . TYR A 1 114 ? -13.327 -13.729 21.719  1.00 13.10  ? 114 TYR A CE1 1 
ATOM   949  C  CE2 . TYR A 1 114 ? -14.862 -14.751 20.201  1.00 13.36  ? 114 TYR A CE2 1 
ATOM   950  C  CZ  . TYR A 1 114 ? -14.535 -14.337 21.477  1.00 13.93  ? 114 TYR A CZ  1 
ATOM   951  O  OH  . TYR A 1 114 ? -15.407 -14.518 22.532  1.00 19.14  ? 114 TYR A OH  1 
ATOM   952  N  N   . ALA A 1 115 ? -10.810 -15.095 15.669  1.00 9.59   ? 115 ALA A N   1 
ATOM   953  C  CA  . ALA A 1 115 ? -10.269 -15.111 14.320  1.00 9.20   ? 115 ALA A CA  1 
ATOM   954  C  C   . ALA A 1 115 ? -9.870  -13.712 13.840  1.00 9.43   ? 115 ALA A C   1 
ATOM   955  O  O   . ALA A 1 115 ? -9.055  -13.573 12.939  1.00 9.98   ? 115 ALA A O   1 
ATOM   956  C  CB  . ALA A 1 115 ? -11.304 -15.699 13.379  1.00 11.16  ? 115 ALA A CB  1 
ATOM   957  N  N   . ALA A 1 116 ? -10.552 -12.673 14.370  1.00 9.52   ? 116 ALA A N   1 
ATOM   958  C  CA  . ALA A 1 116 ? -10.250 -11.315 13.920  1.00 9.33   ? 116 ALA A CA  1 
ATOM   959  C  C   . ALA A 1 116 ? -10.866 -10.404 14.954  1.00 8.26   ? 116 ALA A C   1 
ATOM   960  O  O   . ALA A 1 116 ? -11.581 -10.774 15.860  1.00 8.57   ? 116 ALA A O   1 
ATOM   961  C  CB  . ALA A 1 116 ? -10.743 -11.052 12.487  1.00 10.03  ? 116 ALA A CB  1 
ATOM   962  N  N   . GLU A 1 117 ? -10.521 -9.104  14.788  1.00 8.66   ? 117 GLU A N   1 
ATOM   963  C  CA  . GLU A 1 117 ? -11.040 -8.067  15.666  1.00 8.80   ? 117 GLU A CA  1 
ATOM   964  C  C   . GLU A 1 117 ? -11.233 -6.778  14.810  1.00 8.16   ? 117 GLU A C   1 
ATOM   965  O  O   . GLU A 1 117 ? -10.320 -6.380  14.102  1.00 9.52   ? 117 GLU A O   1 
ATOM   966  C  CB  . GLU A 1 117 ? -10.078 -7.796  16.803  1.00 8.94   ? 117 GLU A CB  1 
ATOM   967  C  CG  . GLU A 1 117 ? -10.591 -6.866  17.859  1.00 9.32   ? 117 GLU A CG  1 
ATOM   968  C  CD  . GLU A 1 117 ? -9.699  -6.800  19.124  1.00 8.26   ? 117 GLU A CD  1 
ATOM   969  O  OE1 . GLU A 1 117 ? -9.012  -7.812  19.398  1.00 9.45   ? 117 GLU A OE1 1 
ATOM   970  O  OE2 . GLU A 1 117 ? -9.628  -5.710  19.755  1.00 9.77   ? 117 GLU A OE2 1 
ATOM   971  N  N   . LEU A 1 118 ? -12.406 -6.206  14.931  1.00 8.10   ? 118 LEU A N   1 
ATOM   972  C  CA  . LEU A 1 118 ? -12.821 -4.973  14.282  1.00 8.14   ? 118 LEU A CA  1 
ATOM   973  C  C   . LEU A 1 118 ? -12.562 -3.828  15.277  1.00 7.65   ? 118 LEU A C   1 
ATOM   974  O  O   . LEU A 1 118 ? -12.967 -3.898  16.439  1.00 7.80   ? 118 LEU A O   1 
ATOM   975  C  CB  . LEU A 1 118 ? -14.270 -5.054  13.943  1.00 9.25   ? 118 LEU A CB  1 
ATOM   976  C  CG  . LEU A 1 118 ? -15.000 -3.765  13.568  1.00 9.37   ? 118 LEU A CG  1 
ATOM   977  C  CD1 . LEU A 1 118 ? -14.427 -3.114  12.319  1.00 10.86  ? 118 LEU A CD1 1 
ATOM   978  C  CD2 . LEU A 1 118 ? -16.447 -4.092  13.322  1.00 11.14  ? 118 LEU A CD2 1 
ATOM   979  N  N   . HIS A 1 119 ? -11.932 -2.751  14.792  1.00 7.80   ? 119 HIS A N   1 
ATOM   980  C  CA  . HIS A 1 119 ? -11.706 -1.525  15.543  1.00 7.77   ? 119 HIS A CA  1 
ATOM   981  C  C   . HIS A 1 119 ? -12.405 -0.356  14.856  1.00 7.97   ? 119 HIS A C   1 
ATOM   982  O  O   . HIS A 1 119 ? -12.008 -0.004  13.728  1.00 8.78   ? 119 HIS A O   1 
ATOM   983  C  CB  . HIS A 1 119 ? -10.208 -1.258  15.646  1.00 8.11   ? 119 HIS A CB  1 
ATOM   984  C  CG  . HIS A 1 119 ? -9.488  -2.221  16.530  1.00 7.49   ? 119 HIS A CG  1 
ATOM   985  N  ND1 . HIS A 1 119 ? -8.196  -2.446  16.529  1.00 7.73   ? 119 HIS A ND1 1 
ATOM   986  C  CD2 . HIS A 1 119 ? -10.037 -3.050  17.480  1.00 7.84   ? 119 HIS A CD2 1 
ATOM   987  C  CE1 . HIS A 1 119 ? -7.870  -3.360  17.421  1.00 8.62   ? 119 HIS A CE1 1 
ATOM   988  N  NE2 . HIS A 1 119 ? -8.979  -3.753  18.038  1.00 8.45   ? 119 HIS A NE2 1 
ATOM   989  N  N   . LEU A 1 120 ? -13.381 0.203   15.530  1.00 8.26   ? 120 LEU A N   1 
ATOM   990  C  CA  . LEU A 1 120 ? -14.082 1.430   15.083  1.00 8.75   ? 120 LEU A CA  1 
ATOM   991  C  C   . LEU A 1 120 ? -13.409 2.566   15.861  1.00 6.97   ? 120 LEU A C   1 
ATOM   992  O  O   . LEU A 1 120 ? -13.542 2.612   17.093  1.00 8.15   ? 120 LEU A O   1 
ATOM   993  C  CB  . LEU A 1 120 ? -15.559 1.335   15.299  1.00 9.28   ? 120 LEU A CB  1 
ATOM   994  C  CG  . LEU A 1 120 ? -16.248 0.255   14.424  1.00 10.43  ? 120 LEU A CG  1 
ATOM   995  C  CD1 . LEU A 1 120 ? -17.126 -0.621  15.229  1.00 14.05  ? 120 LEU A CD1 1 
ATOM   996  C  CD2 . LEU A 1 120 ? -17.075 0.925   13.324  1.00 12.80  ? 120 LEU A CD2 1 
ATOM   997  N  N   . VAL A 1 121 ? -12.726 3.451   15.147  1.00 8.70   ? 121 VAL A N   1 
ATOM   998  C  CA  . VAL A 1 121 ? -11.861 4.465   15.786  1.00 8.55   ? 121 VAL A CA  1 
ATOM   999  C  C   . VAL A 1 121 ? -12.575 5.814   15.810  1.00 8.74   ? 121 VAL A C   1 
ATOM   1000 O  O   . VAL A 1 121 ? -13.008 6.290   14.744  1.00 9.38   ? 121 VAL A O   1 
ATOM   1001 C  CB  . VAL A 1 121 ? -10.562 4.564   14.961  1.00 9.09   ? 121 VAL A CB  1 
ATOM   1002 C  CG1 . VAL A 1 121 ? -9.602  5.596   15.558  1.00 10.47  ? 121 VAL A CG1 1 
ATOM   1003 C  CG2 . VAL A 1 121 ? -9.891  3.177   14.817  1.00 9.36   ? 121 VAL A CG2 1 
ATOM   1004 N  N   . HIS A 1 122 ? -12.635 6.391   16.992  1.00 8.79   ? 122 HIS A N   1 
ATOM   1005 C  CA  . HIS A 1 122 ? -13.344 7.667   17.188  1.00 9.01   ? 122 HIS A CA  1 
ATOM   1006 C  C   . HIS A 1 122 ? -12.472 8.650   17.930  1.00 9.32   ? 122 HIS A C   1 
ATOM   1007 O  O   . HIS A 1 122 ? -11.700 8.254   18.814  1.00 9.77   ? 122 HIS A O   1 
ATOM   1008 C  CB  . HIS A 1 122 ? -14.598 7.478   18.010  1.00 9.42   ? 122 HIS A CB  1 
ATOM   1009 C  CG  . HIS A 1 122 ? -15.485 6.369   17.599  1.00 9.40   ? 122 HIS A CG  1 
ATOM   1010 N  ND1 . HIS A 1 122 ? -15.166 5.056   17.865  1.00 9.49   ? 122 HIS A ND1 1 
ATOM   1011 C  CD2 . HIS A 1 122 ? -16.692 6.308   16.971  1.00 10.60  ? 122 HIS A CD2 1 
ATOM   1012 C  CE1 . HIS A 1 122 ? -16.147 4.260   17.432  1.00 9.50   ? 122 HIS A CE1 1 
ATOM   1013 N  NE2 . HIS A 1 122 ? -17.121 5.000   16.875  1.00 9.87   ? 122 HIS A NE2 1 
ATOM   1014 N  N   . TRP A 1 123 ? -12.569 9.960   17.615  1.00 9.12   ? 123 TRP A N   1 
ATOM   1015 C  CA  . TRP A 1 123 ? -11.739 10.971  18.322  1.00 9.51   ? 123 TRP A CA  1 
ATOM   1016 C  C   . TRP A 1 123 ? -12.643 11.926  19.040  1.00 9.00   ? 123 TRP A C   1 
ATOM   1017 O  O   . TRP A 1 123 ? -13.766 12.286  18.636  1.00 10.11  ? 123 TRP A O   1 
ATOM   1018 C  CB  . TRP A 1 123 ? -10.768 11.660  17.337  1.00 11.43  ? 123 TRP A CB  1 
ATOM   1019 C  CG  . TRP A 1 123 ? -11.460 12.325  16.179  1.00 11.34  ? 123 TRP A CG  1 
ATOM   1020 C  CD1 . TRP A 1 123 ? -11.696 11.716  14.943  1.00 12.04  ? 123 TRP A CD1 1 
ATOM   1021 C  CD2 . TRP A 1 123 ? -11.926 13.667  16.048  1.00 12.54  ? 123 TRP A CD2 1 
ATOM   1022 N  NE1 . TRP A 1 123 ? -12.297 12.579  14.088  1.00 12.69  ? 123 TRP A NE1 1 
ATOM   1023 C  CE2 . TRP A 1 123 ? -12.453 13.805  14.713  1.00 13.78  ? 123 TRP A CE2 1 
ATOM   1024 C  CE3 . TRP A 1 123 ? -11.985 14.798  16.912  1.00 14.69  ? 123 TRP A CE3 1 
ATOM   1025 C  CZ2 . TRP A 1 123 ? -13.023 14.970  14.249  1.00 15.75  ? 123 TRP A CZ2 1 
ATOM   1026 C  CZ3 . TRP A 1 123 ? -12.522 15.960  16.420  1.00 15.71  ? 123 TRP A CZ3 1 
ATOM   1027 C  CH2 . TRP A 1 123 ? -13.005 16.035  15.093  1.00 16.85  ? 123 TRP A CH2 1 
ATOM   1028 N  N   . ASN A 1 124 ? -12.111 12.399  20.183  1.00 9.61   ? 124 ASN A N   1 
ATOM   1029 C  CA  . ASN A 1 124 ? -12.864 13.288  21.070  1.00 10.16  ? 124 ASN A CA  1 
ATOM   1030 C  C   . ASN A 1 124 ? -12.989 14.670  20.468  1.00 10.52  ? 124 ASN A C   1 
ATOM   1031 O  O   . ASN A 1 124 ? -11.970 15.333  20.225  1.00 10.47  ? 124 ASN A O   1 
ATOM   1032 C  CB  . ASN A 1 124 ? -12.070 13.329  22.373  1.00 11.18  ? 124 ASN A CB  1 
ATOM   1033 C  CG  . ASN A 1 124 ? -12.843 13.943  23.495  1.00 10.72  ? 124 ASN A CG  1 
ATOM   1034 O  OD1 . ASN A 1 124 ? -13.685 14.845  23.283  1.00 12.45  ? 124 ASN A OD1 1 
ATOM   1035 N  ND2 . ASN A 1 124 ? -12.571 13.501  24.718  1.00 13.13  ? 124 ASN A ND2 1 
ATOM   1036 N  N   . THR A 1 125 ? -14.229 15.092  20.277  1.00 11.17  ? 125 THR A N   1 
ATOM   1037 C  CA  . THR A 1 125 ? -14.479 16.363  19.550  1.00 12.76  ? 125 THR A CA  1 
ATOM   1038 C  C   . THR A 1 125 ? -13.901 17.542  20.300  1.00 13.22  ? 125 THR A C   1 
ATOM   1039 O  O   . THR A 1 125 ? -13.726 18.598  19.706  1.00 14.61  ? 125 THR A O   1 
ATOM   1040 C  CB  . THR A 1 125 ? -15.964 16.495  19.206  1.00 14.88  ? 125 THR A CB  1 
ATOM   1041 O  OG1 . THR A 1 125 ? -16.695 16.501  20.431  1.00 20.08  ? 125 THR A OG1 1 
ATOM   1042 C  CG2 . THR A 1 125 ? -16.356 15.393  18.190  1.00 17.03  ? 125 THR A CG2 1 
ATOM   1043 N  N   . LYS A 1 126 ? -13.652 17.445  21.639  1.00 12.41  ? 127 LYS A N   1 
ATOM   1044 C  CA  . LYS A 1 126 ? -13.115 18.550  22.377  1.00 13.68  ? 127 LYS A CA  1 
ATOM   1045 C  C   . LYS A 1 126 ? -11.692 18.909  21.880  1.00 12.31  ? 127 LYS A C   1 
ATOM   1046 O  O   . LYS A 1 126 ? -11.212 19.995  22.215  1.00 15.44  ? 127 LYS A O   1 
ATOM   1047 C  CB  . LYS A 1 126 ? -13.217 18.346  23.828  1.00 14.89  ? 127 LYS A CB  1 
ATOM   1048 C  CG  . LYS A 1 126 ? -12.124 17.492  24.375  1.00 15.92  ? 127 LYS A CG  1 
ATOM   1049 C  CD  . LYS A 1 126 ? -12.516 17.144  25.806  1.00 20.10  ? 127 LYS A CD  1 
ATOM   1050 C  CE  . LYS A 1 126 ? -11.495 16.380  26.529  1.00 21.13  ? 127 LYS A CE  1 
ATOM   1051 N  NZ  . LYS A 1 126 ? -12.040 15.853  27.837  1.00 29.92  ? 127 LYS A NZ  1 
ATOM   1052 N  N   . TYR A 1 127 ? -11.042 18.033  21.103  1.00 11.85  ? 128 TYR A N   1 
ATOM   1053 C  CA  . TYR A 1 127 ? -9.692  18.322  20.612  1.00 12.10  ? 128 TYR A CA  1 
ATOM   1054 C  C   . TYR A 1 127 ? -9.672  18.728  19.129  1.00 12.03  ? 128 TYR A C   1 
ATOM   1055 O  O   . TYR A 1 127 ? -8.579  18.946  18.590  1.00 12.76  ? 128 TYR A O   1 
ATOM   1056 C  CB  . TYR A 1 127 ? -8.726  17.162  20.878  1.00 12.54  ? 128 TYR A CB  1 
ATOM   1057 C  CG  . TYR A 1 127 ? -8.618  16.851  22.312  1.00 11.89  ? 128 TYR A CG  1 
ATOM   1058 C  CD1 . TYR A 1 127 ? -8.204  17.854  23.248  1.00 12.56  ? 128 TYR A CD1 1 
ATOM   1059 C  CD2 . TYR A 1 127 ? -8.959  15.576  22.822  1.00 11.55  ? 128 TYR A CD2 1 
ATOM   1060 C  CE1 . TYR A 1 127 ? -8.151  17.544  24.595  1.00 12.90  ? 128 TYR A CE1 1 
ATOM   1061 C  CE2 . TYR A 1 127 ? -8.857  15.300  24.168  1.00 12.16  ? 128 TYR A CE2 1 
ATOM   1062 C  CZ  . TYR A 1 127 ? -8.448  16.307  25.044  1.00 12.33  ? 128 TYR A CZ  1 
ATOM   1063 O  OH  . TYR A 1 127 ? -8.389  16.084  26.362  1.00 14.60  ? 128 TYR A OH  1 
ATOM   1064 N  N   . GLY A 1 128 ? -10.845 18.847  18.506  1.00 11.64  ? 129 GLY A N   1 
ATOM   1065 C  CA  . GLY A 1 128 ? -10.934 19.500  17.225  1.00 13.16  ? 129 GLY A CA  1 
ATOM   1066 C  C   . GLY A 1 128 ? -10.585 18.658  15.993  1.00 12.52  ? 129 GLY A C   1 
ATOM   1067 O  O   . GLY A 1 128 ? -11.214 18.786  14.959  1.00 15.02  ? 129 GLY A O   1 
ATOM   1068 N  N   . ASP A 1 129 ? -9.536  17.827  16.099  1.00 13.48  ? 130 ASP A N   1 
ATOM   1069 C  CA  . ASP A 1 129 ? -9.294  16.902  14.993  1.00 15.10  ? 130 ASP A CA  1 
ATOM   1070 C  C   . ASP A 1 129 ? -8.528  15.704  15.550  1.00 14.35  ? 130 ASP A C   1 
ATOM   1071 O  O   . ASP A 1 129 ? -8.047  15.679  16.690  1.00 15.15  ? 130 ASP A O   1 
ATOM   1072 C  CB  . ASP A 1 129 ? -8.710  17.456  13.792  1.00 17.79  ? 130 ASP A CB  1 
ATOM   1073 C  CG  . ASP A 1 129 ? -7.318  17.944  13.979  1.00 15.95  ? 130 ASP A CG  1 
ATOM   1074 O  OD1 . ASP A 1 129 ? -6.661  17.623  14.984  1.00 27.46  ? 130 ASP A OD1 1 
ATOM   1075 O  OD2 . ASP A 1 129 ? -6.866  18.642  13.078  1.00 24.40  ? 130 ASP A OD2 1 
ATOM   1076 N  N   . PHE A 1 130 ? -8.429  14.695  14.689  1.00 13.85  ? 131 PHE A N   1 
ATOM   1077 C  CA  . PHE A 1 130 ? -7.768  13.432  15.075  1.00 12.73  ? 131 PHE A CA  1 
ATOM   1078 C  C   . PHE A 1 130 ? -6.298  13.606  15.482  1.00 12.36  ? 131 PHE A C   1 
ATOM   1079 O  O   . PHE A 1 130 ? -5.829  13.026  16.460  1.00 12.23  ? 131 PHE A O   1 
ATOM   1080 C  CB  . PHE A 1 130 ? -7.903  12.435  13.933  1.00 13.55  ? 131 PHE A CB  1 
ATOM   1081 C  CG  . PHE A 1 130 ? -7.257  11.104  14.215  1.00 11.36  ? 131 PHE A CG  1 
ATOM   1082 C  CD1 . PHE A 1 130 ? -7.953  10.143  14.883  1.00 11.79  ? 131 PHE A CD1 1 
ATOM   1083 C  CD2 . PHE A 1 130 ? -5.999  10.805  13.826  1.00 14.41  ? 131 PHE A CD2 1 
ATOM   1084 C  CE1 . PHE A 1 130 ? -7.425  8.940   15.174  1.00 12.70  ? 131 PHE A CE1 1 
ATOM   1085 C  CE2 . PHE A 1 130 ? -5.431  9.575   14.102  1.00 14.47  ? 131 PHE A CE2 1 
ATOM   1086 C  CZ  . PHE A 1 130 ? -6.200  8.635   14.792  1.00 13.91  ? 131 PHE A CZ  1 
ATOM   1087 N  N   . GLY A 1 131 ? -5.508  14.400  14.696  1.00 14.25  ? 132 GLY A N   1 
ATOM   1088 C  CA  . GLY A 1 131 ? -4.082  14.526  14.977  1.00 16.10  ? 132 GLY A CA  1 
ATOM   1089 C  C   . GLY A 1 131 ? -3.815  15.163  16.342  1.00 14.66  ? 132 GLY A C   1 
ATOM   1090 O  O   . GLY A 1 131 ? -2.808  14.841  17.010  1.00 16.79  ? 132 GLY A O   1 
ATOM   1091 N  N   . LYS A 1 132 ? -4.663  16.081  16.735  1.00 13.78  ? 133 LYS A N   1 
ATOM   1092 C  CA  . LYS A 1 132 ? -4.497  16.654  18.081  1.00 13.44  ? 133 LYS A CA  1 
ATOM   1093 C  C   . LYS A 1 132 ? -5.033  15.671  19.123  1.00 12.48  ? 133 LYS A C   1 
ATOM   1094 O  O   . LYS A 1 132 ? -4.475  15.570  20.218  1.00 13.00  ? 133 LYS A O   1 
ATOM   1095 C  CB  . LYS A 1 132 ? -5.316  17.969  18.185  1.00 14.56  ? 133 LYS A CB  1 
ATOM   1096 C  CG  . LYS A 1 132 ? -4.675  19.123  17.439  1.00 20.68  ? 133 LYS A CG  1 
ATOM   1097 C  CD  . LYS A 1 132 ? -3.343  19.485  18.063  1.00 29.31  ? 133 LYS A CD  1 
ATOM   1098 C  CE  . LYS A 1 132 ? -3.284  20.909  18.614  1.00 44.87  ? 133 LYS A CE  1 
ATOM   1099 N  NZ  . LYS A 1 132 ? -1.914  21.281  19.004  1.00 37.73  ? 133 LYS A NZ  1 
ATOM   1100 N  N   . ALA A 1 133 ? -6.112  14.957  18.820  1.00 12.27  ? 134 ALA A N   1 
ATOM   1101 C  CA  . ALA A 1 133 ? -6.655  14.015  19.797  1.00 11.46  ? 134 ALA A CA  1 
ATOM   1102 C  C   . ALA A 1 133 ? -5.663  12.928  20.176  1.00 10.69  ? 134 ALA A C   1 
ATOM   1103 O  O   . ALA A 1 133 ? -5.659  12.562  21.345  1.00 11.43  ? 134 ALA A O   1 
ATOM   1104 C  CB  . ALA A 1 133 ? -7.962  13.415  19.250  1.00 11.71  ? 134 ALA A CB  1 
ATOM   1105 N  N   . VAL A 1 134 ? -4.877  12.427  19.251  1.00 11.55  ? 135 VAL A N   1 
ATOM   1106 C  CA  . VAL A 1 134 ? -3.966  11.302  19.612  1.00 11.91  ? 135 VAL A CA  1 
ATOM   1107 C  C   . VAL A 1 134 ? -2.861  11.749  20.558  1.00 11.39  ? 135 VAL A C   1 
ATOM   1108 O  O   . VAL A 1 134 ? -2.155  10.876  21.115  1.00 12.50  ? 135 VAL A O   1 
ATOM   1109 C  CB  . VAL A 1 134 ? -3.331  10.604  18.405  1.00 13.58  ? 135 VAL A CB  1 
ATOM   1110 C  CG1 . VAL A 1 134 ? -4.427  9.961   17.550  1.00 14.29  ? 135 VAL A CG1 1 
ATOM   1111 C  CG2 . VAL A 1 134 ? -2.484  11.555  17.561  1.00 13.60  ? 135 VAL A CG2 1 
ATOM   1112 N  N   . GLN A 1 135 ? -2.712  13.071  20.746  1.00 11.75  ? 136 GLN A N   1 
ATOM   1113 C  CA  . GLN A 1 135 ? -1.769  13.591  21.726  1.00 13.11  ? 136 GLN A CA  1 
ATOM   1114 C  C   . GLN A 1 135 ? -2.307  13.713  23.090  1.00 12.18  ? 136 GLN A C   1 
ATOM   1115 O  O   . GLN A 1 135 ? -1.630  14.279  23.998  1.00 15.00  ? 136 GLN A O   1 
ATOM   1116 C  CB  . GLN A 1 135 ? -1.197  14.957  21.215  1.00 14.81  ? 136 GLN A CB  1 
ATOM   1117 C  CG  . GLN A 1 135 ? -0.594  14.815  19.867  1.00 18.35  ? 136 GLN A CG  1 
ATOM   1118 C  CD  . GLN A 1 135 ? -0.118  16.167  19.380  1.00 22.52  ? 136 GLN A CD  1 
ATOM   1119 O  OE1 . GLN A 1 135 ? 0.729   16.842  20.067  1.00 29.13  ? 136 GLN A OE1 1 
ATOM   1120 N  NE2 . GLN A 1 135 ? -0.662  16.643  18.243  1.00 24.68  ? 136 GLN A NE2 1 
ATOM   1121 N  N   . GLN A 1 136 ? -3.532  13.230  23.321  1.00 11.25  ? 137 GLN A N   1 
ATOM   1122 C  CA  . GLN A 1 136 ? -4.164  13.424  24.624  1.00 11.02  ? 137 GLN A CA  1 
ATOM   1123 C  C   . GLN A 1 136 ? -4.529  12.111  25.242  1.00 11.03  ? 137 GLN A C   1 
ATOM   1124 O  O   . GLN A 1 136 ? -4.934  11.188  24.544  1.00 11.02  ? 137 GLN A O   1 
ATOM   1125 C  CB  . GLN A 1 136 ? -5.451  14.266  24.500  1.00 12.17  ? 137 GLN A CB  1 
ATOM   1126 C  CG  . GLN A 1 136 ? -5.396  15.489  23.603  1.00 15.81  ? 137 GLN A CG  1 
ATOM   1127 C  CD  . GLN A 1 136 ? -4.413  16.411  24.059  1.00 18.48  ? 137 GLN A CD  1 
ATOM   1128 O  OE1 . GLN A 1 136 ? -4.138  16.530  25.274  1.00 18.74  ? 137 GLN A OE1 1 
ATOM   1129 N  NE2 . GLN A 1 136 ? -3.778  17.124  23.077  1.00 29.14  ? 137 GLN A NE2 1 
ATOM   1130 N  N   A PRO A 1 137 ? -4.600  12.034  26.579  0.50 10.56  ? 138 PRO A N   1 
ATOM   1131 N  N   B PRO A 1 137 ? -4.501  12.020  26.596  0.50 12.02  ? 138 PRO A N   1 
ATOM   1132 C  CA  A PRO A 1 137 ? -4.854  10.716  27.233  0.50 11.83  ? 138 PRO A CA  1 
ATOM   1133 C  CA  B PRO A 1 137 ? -4.801  10.705  27.212  0.50 13.01  ? 138 PRO A CA  1 
ATOM   1134 C  C   A PRO A 1 137 ? -6.263  10.222  27.058  0.50 11.91  ? 138 PRO A C   1 
ATOM   1135 C  C   B PRO A 1 137 ? -6.219  10.231  27.032  0.50 11.58  ? 138 PRO A C   1 
ATOM   1136 O  O   A PRO A 1 137 ? -6.536  9.029   27.170  0.50 15.00  ? 138 PRO A O   1 
ATOM   1137 O  O   B PRO A 1 137 ? -6.449  9.033   27.152  0.50 15.58  ? 138 PRO A O   1 
ATOM   1138 C  CB  A PRO A 1 137 ? -4.508  10.968  28.701  0.50 15.58  ? 138 PRO A CB  1 
ATOM   1139 C  CB  B PRO A 1 137 ? -4.488  10.910  28.698  0.50 16.05  ? 138 PRO A CB  1 
ATOM   1140 C  CG  A PRO A 1 137 ? -4.550  12.433  28.854  0.50 13.65  ? 138 PRO A CG  1 
ATOM   1141 C  CG  B PRO A 1 137 ? -3.496  11.994  28.738  0.50 17.46  ? 138 PRO A CG  1 
ATOM   1142 C  CD  A PRO A 1 137 ? -4.144  13.046  27.564  0.50 13.99  ? 138 PRO A CD  1 
ATOM   1143 C  CD  B PRO A 1 137 ? -3.836  12.912  27.583  0.50 16.15  ? 138 PRO A CD  1 
ATOM   1144 N  N   . ASP A 1 138 ? -7.178  11.160  26.786  1.00 10.69  ? 139 ASP A N   1 
ATOM   1145 C  CA  . ASP A 1 138 ? -8.576  10.825  26.520  1.00 11.39  ? 139 ASP A CA  1 
ATOM   1146 C  C   . ASP A 1 138 ? -8.943  11.226  25.100  1.00 9.80   ? 139 ASP A C   1 
ATOM   1147 O  O   . ASP A 1 138 ? -10.080 11.670  24.820  1.00 10.76  ? 139 ASP A O   1 
ATOM   1148 C  CB  . ASP A 1 138 ? -9.555  11.425  27.528  1.00 13.75  ? 139 ASP A CB  1 
ATOM   1149 C  CG  . ASP A 1 138 ? -9.426  12.930  27.582  1.00 13.41  ? 139 ASP A CG  1 
ATOM   1150 O  OD1 . ASP A 1 138 ? -8.497  13.524  26.980  1.00 13.56  ? 139 ASP A OD1 1 
ATOM   1151 O  OD2 . ASP A 1 138 ? -10.299 13.535  28.243  1.00 16.87  ? 139 ASP A OD2 1 
ATOM   1152 N  N   . GLY A 1 139 ? -7.987  11.160  24.164  1.00 9.45   ? 140 GLY A N   1 
ATOM   1153 C  CA  . GLY A 1 139 ? -8.210  11.592  22.809  1.00 9.84   ? 140 GLY A CA  1 
ATOM   1154 C  C   . GLY A 1 139 ? -9.095  10.696  21.964  1.00 8.64   ? 140 GLY A C   1 
ATOM   1155 O  O   . GLY A 1 139 ? -9.776  11.186  21.085  1.00 9.40   ? 140 GLY A O   1 
ATOM   1156 N  N   . LEU A 1 140 ? -8.982  9.367   22.152  1.00 8.81   ? 141 LEU A N   1 
ATOM   1157 C  CA  . LEU A 1 140 ? -9.659  8.414   21.275  1.00 8.70   ? 141 LEU A CA  1 
ATOM   1158 C  C   . LEU A 1 140 ? -10.457 7.473   22.052  1.00 8.16   ? 141 LEU A C   1 
ATOM   1159 O  O   . LEU A 1 140 ? -10.202 7.177   23.194  1.00 8.83   ? 141 LEU A O   1 
ATOM   1160 C  CB  . LEU A 1 140 ? -8.634  7.587   20.466  1.00 9.09   ? 141 LEU A CB  1 
ATOM   1161 C  CG  . LEU A 1 140 ? -7.719  8.198   19.395  1.00 11.74  ? 141 LEU A CG  1 
ATOM   1162 C  CD1 . LEU A 1 140 ? -7.125  7.121   18.496  1.00 11.40  ? 141 LEU A CD1 1 
ATOM   1163 C  CD2 . LEU A 1 140 ? -8.378  9.318   18.595  1.00 16.27  ? 141 LEU A CD2 1 
ATOM   1164 N  N   . ALA A 1 141 ? -11.519 6.973   21.400  1.00 8.56   ? 142 ALA A N   1 
ATOM   1165 C  CA  . ALA A 1 141 ? -12.313 5.828   21.912  1.00 9.05   ? 142 ALA A CA  1 
ATOM   1166 C  C   . ALA A 1 141 ? -12.352 4.862   20.794  1.00 8.71   ? 142 ALA A C   1 
ATOM   1167 O  O   . ALA A 1 141 ? -12.771 5.190   19.669  1.00 9.09   ? 142 ALA A O   1 
ATOM   1168 C  CB  . ALA A 1 141 ? -13.726 6.282   22.322  1.00 10.13  ? 142 ALA A CB  1 
ATOM   1169 N  N   . VAL A 1 142 ? -11.825 3.647   21.032  1.00 8.18   ? 143 VAL A N   1 
ATOM   1170 C  CA  . VAL A 1 142 ? -11.869 2.563   20.038  1.00 8.74   ? 143 VAL A CA  1 
ATOM   1171 C  C   . VAL A 1 142 ? -12.827 1.502   20.518  1.00 7.97   ? 143 VAL A C   1 
ATOM   1172 O  O   . VAL A 1 142 ? -12.707 1.004   21.639  1.00 8.43   ? 143 VAL A O   1 
ATOM   1173 C  CB  . VAL A 1 142 ? -10.472 2.026   19.661  1.00 8.60   ? 143 VAL A CB  1 
ATOM   1174 C  CG1 . VAL A 1 142 ? -10.634 0.988   18.551  1.00 9.46   ? 143 VAL A CG1 1 
ATOM   1175 C  CG2 . VAL A 1 142 ? -9.552  3.141   19.221  1.00 9.60   ? 143 VAL A CG2 1 
ATOM   1176 N  N   . LEU A 1 143 ? -13.835 1.244   19.668  1.00 8.44   ? 144 LEU A N   1 
ATOM   1177 C  CA  . LEU A 1 143 ? -14.779 0.205   19.913  1.00 8.08   ? 144 LEU A CA  1 
ATOM   1178 C  C   . LEU A 1 143 ? -14.280 -1.050  19.223  1.00 8.56   ? 144 LEU A C   1 
ATOM   1179 O  O   . LEU A 1 143 ? -14.120 -1.092  18.009  1.00 9.05   ? 144 LEU A O   1 
ATOM   1180 C  CB  . LEU A 1 143 ? -16.131 0.646   19.368  1.00 10.06  ? 144 LEU A CB  1 
ATOM   1181 C  CG  . LEU A 1 143 ? -17.301 -0.334  19.519  1.00 10.54  ? 144 LEU A CG  1 
ATOM   1182 C  CD1 . LEU A 1 143 ? -17.545 -0.689  20.959  1.00 12.68  ? 144 LEU A CD1 1 
ATOM   1183 C  CD2 . LEU A 1 143 ? -18.538 0.263   18.873  1.00 13.34  ? 144 LEU A CD2 1 
ATOM   1184 N  N   . GLY A 1 144 ? -13.986 -2.066  20.032  1.00 8.37   ? 145 GLY A N   1 
ATOM   1185 C  CA  . GLY A 1 144 ? -13.449 -3.346  19.553  1.00 8.47   ? 145 GLY A CA  1 
ATOM   1186 C  C   . GLY A 1 144 ? -14.507 -4.422  19.582  1.00 7.53   ? 145 GLY A C   1 
ATOM   1187 O  O   . GLY A 1 144 ? -15.233 -4.541  20.558  1.00 8.81   ? 145 GLY A O   1 
ATOM   1188 N  N   . ILE A 1 145 ? -14.570 -5.167  18.461  1.00 8.14   ? 146 ILE A N   1 
ATOM   1189 C  CA  . ILE A 1 145 ? -15.596 -6.195  18.293  1.00 8.05   ? 146 ILE A CA  1 
ATOM   1190 C  C   . ILE A 1 145 ? -14.856 -7.419  17.787  1.00 7.86   ? 146 ILE A C   1 
ATOM   1191 O  O   . ILE A 1 145 ? -14.191 -7.394  16.762  1.00 8.44   ? 146 ILE A O   1 
ATOM   1192 C  CB  . ILE A 1 145 ? -16.703 -5.723  17.325  1.00 8.89   ? 146 ILE A CB  1 
ATOM   1193 C  CG1 . ILE A 1 145 ? -17.283 -4.412  17.810  1.00 10.75  ? 146 ILE A CG1 1 
ATOM   1194 C  CG2 . ILE A 1 145 ? -17.696 -6.822  17.081  1.00 11.52  ? 146 ILE A CG2 1 
ATOM   1195 C  CD1 . ILE A 1 145 ? -18.380 -3.820  16.928  1.00 11.05  ? 146 ILE A CD1 1 
ATOM   1196 N  N   . PHE A 1 146 ? -15.062 -8.544  18.452  1.00 8.36   ? 147 PHE A N   1 
ATOM   1197 C  CA  . PHE A 1 146 ? -14.436 -9.799  18.029  1.00 8.71   ? 147 PHE A CA  1 
ATOM   1198 C  C   . PHE A 1 146 ? -15.214 -10.411 16.873  1.00 8.69   ? 147 PHE A C   1 
ATOM   1199 O  O   . PHE A 1 146 ? -16.438 -10.302 16.805  1.00 9.68   ? 147 PHE A O   1 
ATOM   1200 C  CB  . PHE A 1 146 ? -14.473 -10.771 19.207  1.00 9.19   ? 147 PHE A CB  1 
ATOM   1201 C  CG  . PHE A 1 146 ? -13.594 -10.302 20.359  1.00 7.89   ? 147 PHE A CG  1 
ATOM   1202 C  CD1 . PHE A 1 146 ? -12.232 -10.125 20.168  1.00 8.55   ? 147 PHE A CD1 1 
ATOM   1203 C  CD2 . PHE A 1 146 ? -14.123 -10.073 21.604  1.00 9.22   ? 147 PHE A CD2 1 
ATOM   1204 C  CE1 . PHE A 1 146 ? -11.422 -9.719  21.255  1.00 8.71   ? 147 PHE A CE1 1 
ATOM   1205 C  CE2 . PHE A 1 146 ? -13.355 -9.678  22.688  1.00 9.40   ? 147 PHE A CE2 1 
ATOM   1206 C  CZ  . PHE A 1 146 ? -11.992 -9.528  22.485  1.00 8.82   ? 147 PHE A CZ  1 
ATOM   1207 N  N   . LEU A 1 147 ? -14.492 -11.145 16.050  1.00 8.95   ? 148 LEU A N   1 
ATOM   1208 C  CA  . LEU A 1 147 ? -15.068 -11.917 14.943  1.00 9.32   ? 148 LEU A CA  1 
ATOM   1209 C  C   . LEU A 1 147 ? -14.755 -13.395 15.174  1.00 9.10   ? 148 LEU A C   1 
ATOM   1210 O  O   . LEU A 1 147 ? -13.565 -13.746 15.376  1.00 9.99   ? 148 LEU A O   1 
ATOM   1211 C  CB  . LEU A 1 147 ? -14.452 -11.552 13.595  1.00 10.15  ? 148 LEU A CB  1 
ATOM   1212 C  CG  . LEU A 1 147 ? -15.042 -10.277 12.906  1.00 10.35  ? 148 LEU A CG  1 
ATOM   1213 C  CD1 . LEU A 1 147 ? -14.791 -9.006  13.775  1.00 11.38  ? 148 LEU A CD1 1 
ATOM   1214 C  CD2 . LEU A 1 147 ? -14.420 -10.088 11.558  1.00 11.59  ? 148 LEU A CD2 1 
ATOM   1215 N  N   . LYS A 1 148 ? -15.769 -14.231 15.093  1.00 9.82   ? 149 LYS A N   1 
ATOM   1216 C  CA  . LYS A 1 148 ? -15.612 -15.681 15.059  1.00 10.71  ? 149 LYS A CA  1 
ATOM   1217 C  C   . LYS A 1 148 ? -16.097 -16.184 13.681  1.00 11.56  ? 149 LYS A C   1 
ATOM   1218 O  O   . LYS A 1 148 ? -16.935 -15.530 13.057  1.00 12.11  ? 149 LYS A O   1 
ATOM   1219 C  CB  . LYS A 1 148 ? -16.334 -16.357 16.200  1.00 11.89  ? 149 LYS A CB  1 
ATOM   1220 C  CG  . LYS A 1 148 ? -17.832 -16.233 16.134  1.00 13.25  ? 149 LYS A CG  1 
ATOM   1221 C  CD  . LYS A 1 148 ? -18.415 -16.917 17.378  1.00 19.72  ? 149 LYS A CD  1 
ATOM   1222 C  CE  . LYS A 1 148 ? -19.871 -17.062 17.213  1.00 28.70  ? 149 LYS A CE  1 
ATOM   1223 N  NZ  . LYS A 1 148 ? -20.411 -17.900 18.299  1.00 46.20  ? 149 LYS A NZ  1 
ATOM   1224 N  N   . VAL A 1 149 ? -15.556 -17.313 13.270  1.00 11.87  ? 150 VAL A N   1 
ATOM   1225 C  CA  . VAL A 1 149 ? -15.989 -17.898 12.006  1.00 12.14  ? 150 VAL A CA  1 
ATOM   1226 C  C   . VAL A 1 149 ? -17.202 -18.806 12.180  1.00 12.81  ? 150 VAL A C   1 
ATOM   1227 O  O   . VAL A 1 149 ? -17.142 -19.784 12.966  1.00 14.12  ? 150 VAL A O   1 
ATOM   1228 C  CB  . VAL A 1 149 ? -14.796 -18.640 11.407  1.00 12.15  ? 150 VAL A CB  1 
ATOM   1229 C  CG1 . VAL A 1 149 ? -15.174 -19.406 10.150  1.00 14.93  ? 150 VAL A CG1 1 
ATOM   1230 C  CG2 . VAL A 1 149 ? -13.699 -17.648 11.077  1.00 14.42  ? 150 VAL A CG2 1 
ATOM   1231 N  N   . GLY A 1 150 ? -18.236 -18.549 11.434  1.00 12.60  ? 151 GLY A N   1 
ATOM   1232 C  CA  . GLY A 1 150 ? -19.480 -19.365 11.467  1.00 14.36  ? 151 GLY A CA  1 
ATOM   1233 C  C   . GLY A 1 150 ? -20.332 -18.890 10.357  1.00 12.80  ? 151 GLY A C   1 
ATOM   1234 O  O   . GLY A 1 150 ? -19.956 -18.959 9.166   1.00 14.46  ? 151 GLY A O   1 
ATOM   1235 N  N   A SER A 1 151 ? -21.544 -18.409 10.653  0.50 14.48  ? 152 SER A N   1 
ATOM   1236 N  N   B SER A 1 151 ? -21.514 -18.383 10.712  0.50 14.57  ? 152 SER A N   1 
ATOM   1237 C  CA  A SER A 1 151 ? -22.431 -17.874 9.597   0.50 14.78  ? 152 SER A CA  1 
ATOM   1238 C  CA  B SER A 1 151 ? -22.399 -17.735 9.739   0.50 14.14  ? 152 SER A CA  1 
ATOM   1239 C  C   A SER A 1 151 ? -21.892 -16.532 9.145   0.50 13.67  ? 152 SER A C   1 
ATOM   1240 C  C   B SER A 1 151 ? -21.706 -16.543 9.079   0.50 12.99  ? 152 SER A C   1 
ATOM   1241 O  O   A SER A 1 151 ? -21.279 -15.782 9.947   0.50 12.20  ? 152 SER A O   1 
ATOM   1242 O  O   B SER A 1 151 ? -20.811 -15.897 9.644   0.50 12.00  ? 152 SER A O   1 
ATOM   1243 C  CB  A SER A 1 151 ? -23.846 -17.687 10.109  0.50 19.58  ? 152 SER A CB  1 
ATOM   1244 C  CB  B SER A 1 151 ? -23.720 -17.343 10.387  0.50 17.12  ? 152 SER A CB  1 
ATOM   1245 O  OG  A SER A 1 151 ? -23.817 -16.663 11.091  0.50 22.51  ? 152 SER A OG  1 
ATOM   1246 O  OG  B SER A 1 151 ? -24.346 -18.505 10.906  0.50 21.11  ? 152 SER A OG  1 
ATOM   1247 N  N   . ALA A 1 152 ? -22.097 -16.228 7.848   1.00 14.34  ? 153 ALA A N   1 
ATOM   1248 C  CA  . ALA A 1 152 ? -21.704 -14.995 7.256   1.00 14.29  ? 153 ALA A CA  1 
ATOM   1249 C  C   . ALA A 1 152 ? -22.335 -13.776 7.943   1.00 14.65  ? 153 ALA A C   1 
ATOM   1250 O  O   . ALA A 1 152 ? -23.419 -13.830 8.479   1.00 15.80  ? 153 ALA A O   1 
ATOM   1251 C  CB  . ALA A 1 152 ? -22.062 -14.955 5.766   1.00 16.08  ? 153 ALA A CB  1 
ATOM   1252 N  N   . LYS A 1 153 ? -21.582 -12.664 7.866   1.00 13.95  ? 154 LYS A N   1 
ATOM   1253 C  CA  . LYS A 1 153 ? -22.144 -11.341 8.317   1.00 14.92  ? 154 LYS A CA  1 
ATOM   1254 C  C   . LYS A 1 153 ? -22.540 -10.564 7.078   1.00 13.59  ? 154 LYS A C   1 
ATOM   1255 O  O   . LYS A 1 153 ? -21.707 -10.134 6.273   1.00 14.07  ? 154 LYS A O   1 
ATOM   1256 C  CB  . LYS A 1 153 ? -21.091 -10.604 9.121   1.00 14.62  ? 154 LYS A CB  1 
ATOM   1257 C  CG  . LYS A 1 153 ? -21.506 -9.413  9.853   1.00 17.55  ? 154 LYS A CG  1 
ATOM   1258 C  CD  . LYS A 1 153 ? -22.411 -9.717  11.006  1.00 16.79  ? 154 LYS A CD  1 
ATOM   1259 C  CE  . LYS A 1 153 ? -22.463 -8.498  11.881  1.00 16.57  ? 154 LYS A CE  1 
ATOM   1260 N  NZ  . LYS A 1 153 ? -23.432 -8.886  12.866  1.00 16.73  ? 154 LYS A NZ  1 
ATOM   1261 N  N   . PRO A 1 154 ? -23.853 -10.493 6.822   1.00 15.34  ? 155 PRO A N   1 
ATOM   1262 C  CA  . PRO A 1 154 ? -24.256 -9.909  5.536   1.00 16.11  ? 155 PRO A CA  1 
ATOM   1263 C  C   . PRO A 1 154 ? -23.780 -8.443  5.366   1.00 17.07  ? 155 PRO A C   1 
ATOM   1264 O  O   . PRO A 1 154 ? -23.350 -8.066  4.249   1.00 17.78  ? 155 PRO A O   1 
ATOM   1265 C  CB  . PRO A 1 154 ? -25.803 -10.010 5.573   1.00 19.12  ? 155 PRO A CB  1 
ATOM   1266 C  CG  . PRO A 1 154 ? -26.018 -11.187 6.496   1.00 21.07  ? 155 PRO A CG  1 
ATOM   1267 C  CD  . PRO A 1 154 ? -24.998 -11.063 7.581   1.00 18.07  ? 155 PRO A CD  1 
ATOM   1268 N  N   . GLY A 1 155 ? -23.705 -7.725  6.473   1.00 15.79  ? 156 GLY A N   1 
ATOM   1269 C  CA  . GLY A 1 155 ? -23.318 -6.360  6.454   1.00 17.89  ? 156 GLY A CA  1 
ATOM   1270 C  C   . GLY A 1 155 ? -21.865 -6.161  6.229   1.00 16.04  ? 156 GLY A C   1 
ATOM   1271 O  O   . GLY A 1 155 ? -21.401 -5.044  6.023   1.00 19.93  ? 156 GLY A O   1 
ATOM   1272 N  N   . LEU A 1 156 ? -21.077 -7.220  6.229   1.00 15.58  ? 157 LEU A N   1 
ATOM   1273 C  CA  . LEU A 1 156 ? -19.644 -7.221  5.887   1.00 14.91  ? 157 LEU A CA  1 
ATOM   1274 C  C   . LEU A 1 156 ? -19.379 -7.399  4.423   1.00 14.52  ? 157 LEU A C   1 
ATOM   1275 O  O   . LEU A 1 156 ? -18.273 -7.103  3.944   1.00 14.78  ? 157 LEU A O   1 
ATOM   1276 C  CB  . LEU A 1 156 ? -18.881 -8.253  6.716   1.00 15.06  ? 157 LEU A CB  1 
ATOM   1277 C  CG  . LEU A 1 156 ? -17.370 -8.339  6.573   1.00 13.95  ? 157 LEU A CG  1 
ATOM   1278 C  CD1 . LEU A 1 156 ? -16.609 -7.094  6.943   1.00 16.31  ? 157 LEU A CD1 1 
ATOM   1279 C  CD2 . LEU A 1 156 ? -16.795 -9.491  7.382   1.00 14.52  ? 157 LEU A CD2 1 
ATOM   1280 N  N   . GLN A 1 157 ? -20.348 -7.987  3.676   1.00 15.16  ? 158 GLN A N   1 
ATOM   1281 C  CA  . GLN A 1 157 ? -19.989 -8.459  2.341   1.00 16.34  ? 158 GLN A CA  1 
ATOM   1282 C  C   . GLN A 1 157 ? -19.593 -7.317  1.442   1.00 14.89  ? 158 GLN A C   1 
ATOM   1283 O  O   . GLN A 1 157 ? -18.715 -7.520  0.591   1.00 15.85  ? 158 GLN A O   1 
ATOM   1284 C  CB  . GLN A 1 157 ? -21.126 -9.293  1.744   1.00 16.85  ? 158 GLN A CB  1 
ATOM   1285 C  CG  . GLN A 1 157 ? -20.695 -9.991  0.432   1.00 17.92  ? 158 GLN A CG  1 
ATOM   1286 C  CD  . GLN A 1 157 ? -19.576 -11.016 0.661   1.00 16.56  ? 158 GLN A CD  1 
ATOM   1287 O  OE1 . GLN A 1 157 ? -19.446 -11.577 1.805   1.00 17.04  ? 158 GLN A OE1 1 
ATOM   1288 N  NE2 . GLN A 1 157 ? -18.763 -11.294 -0.384  1.00 19.64  ? 158 GLN A NE2 1 
ATOM   1289 N  N   . LYS A 1 158 ? -20.172 -6.101  1.575   1.00 17.14  ? 159 LYS A N   1 
ATOM   1290 C  CA  . LYS A 1 158 ? -19.766 -4.987  0.698   1.00 16.38  ? 159 LYS A CA  1 
ATOM   1291 C  C   . LYS A 1 158 ? -18.251 -4.665  0.866   1.00 15.92  ? 159 LYS A C   1 
ATOM   1292 O  O   . LYS A 1 158 ? -17.598 -4.326  -0.069  1.00 17.03  ? 159 LYS A O   1 
ATOM   1293 C  CB  . LYS A 1 158 ? -20.623 -3.762  0.932   1.00 18.54  ? 159 LYS A CB  1 
ATOM   1294 C  CG  . LYS A 1 158 ? -21.982 -3.840  0.255   1.00 28.60  ? 159 LYS A CG  1 
ATOM   1295 N  N   . VAL A 1 159 ? -17.729 -4.834  2.078   1.00 15.68  ? 160 VAL A N   1 
ATOM   1296 C  CA  . VAL A 1 159 ? -16.287 -4.615  2.335   1.00 13.64  ? 160 VAL A CA  1 
ATOM   1297 C  C   . VAL A 1 159 ? -15.493 -5.721  1.646   1.00 14.81  ? 160 VAL A C   1 
ATOM   1298 O  O   . VAL A 1 159 ? -14.564 -5.495  0.912   1.00 15.71  ? 160 VAL A O   1 
ATOM   1299 C  CB  . VAL A 1 159 ? -16.009 -4.619  3.848   1.00 14.14  ? 160 VAL A CB  1 
ATOM   1300 C  CG1 . VAL A 1 159 ? -14.519 -4.675  4.139   1.00 16.89  ? 160 VAL A CG1 1 
ATOM   1301 C  CG2 . VAL A 1 159 ? -16.713 -3.452  4.504   1.00 16.87  ? 160 VAL A CG2 1 
ATOM   1302 N  N   . VAL A 1 160 ? -15.871 -6.961  1.892   1.00 14.42  ? 161 VAL A N   1 
ATOM   1303 C  CA  . VAL A 1 160 ? -15.195 -8.098  1.300   1.00 15.29  ? 161 VAL A CA  1 
ATOM   1304 C  C   . VAL A 1 160 ? -15.091 -8.021  -0.207  1.00 14.95  ? 161 VAL A C   1 
ATOM   1305 O  O   . VAL A 1 160 ? -14.069 -8.342  -0.786  1.00 18.77  ? 161 VAL A O   1 
ATOM   1306 C  CB  . VAL A 1 160 ? -15.898 -9.415  1.681   1.00 20.13  ? 161 VAL A CB  1 
ATOM   1307 C  CG1 . VAL A 1 160 ? -15.345 -10.569 0.860   1.00 20.69  ? 161 VAL A CG1 1 
ATOM   1308 C  CG2 . VAL A 1 160 ? -15.744 -9.684  3.170   1.00 17.83  ? 161 VAL A CG2 1 
ATOM   1309 N  N   . ASP A 1 161 ? -16.198 -7.594  -0.832  1.00 17.97  ? 162 ASP A N   1 
ATOM   1310 C  CA  . ASP A 1 161 ? -16.188 -7.618  -2.266  1.00 20.14  ? 162 ASP A CA  1 
ATOM   1311 C  C   . ASP A 1 161 ? -15.327 -6.549  -2.938  1.00 21.57  ? 162 ASP A C   1 
ATOM   1312 O  O   . ASP A 1 161 ? -14.929 -6.699  -4.117  1.00 25.58  ? 162 ASP A O   1 
ATOM   1313 C  CB  . ASP A 1 161 ? -17.609 -7.549  -2.716  1.00 24.42  ? 162 ASP A CB  1 
ATOM   1314 C  CG  . ASP A 1 161 ? -18.280 -8.924  -2.691  1.00 21.93  ? 162 ASP A CG  1 
ATOM   1315 O  OD1 . ASP A 1 161 ? -17.567 -10.001 -2.728  1.00 26.81  ? 162 ASP A OD1 1 
ATOM   1316 O  OD2 . ASP A 1 161 ? -19.504 -8.915  -2.562  1.00 28.11  ? 162 ASP A OD2 1 
ATOM   1317 N  N   . VAL A 1 162 ? -14.955 -5.500  -2.195  1.00 18.69  ? 163 VAL A N   1 
ATOM   1318 C  CA  . VAL A 1 162 ? -14.206 -4.407  -2.760  1.00 20.49  ? 163 VAL A CA  1 
ATOM   1319 C  C   . VAL A 1 162 ? -12.698 -4.706  -2.596  1.00 16.88  ? 163 VAL A C   1 
ATOM   1320 O  O   . VAL A 1 162 ? -11.814 -4.070  -3.137  1.00 19.13  ? 163 VAL A O   1 
ATOM   1321 C  CB  . VAL A 1 162 ? -14.600 -3.036  -2.179  1.00 21.51  ? 163 VAL A CB  1 
ATOM   1322 C  CG1 . VAL A 1 162 ? -13.939 -2.800  -0.877  1.00 21.48  ? 163 VAL A CG1 1 
ATOM   1323 C  CG2 . VAL A 1 162 ? -14.314 -1.837  -3.089  1.00 20.77  ? 163 VAL A CG2 1 
ATOM   1324 N  N   . LEU A 1 163 ? -12.401 -5.707  -1.755  1.00 18.63  ? 164 LEU A N   1 
ATOM   1325 C  CA  . LEU A 1 163 ? -11.000 -5.986  -1.460  1.00 16.27  ? 164 LEU A CA  1 
ATOM   1326 C  C   . LEU A 1 163 ? -10.116 -6.315  -2.639  1.00 16.94  ? 164 LEU A C   1 
ATOM   1327 O  O   . LEU A 1 163 ? -8.904  -6.040  -2.654  1.00 17.31  ? 164 LEU A O   1 
ATOM   1328 C  CB  . LEU A 1 163 ? -10.747 -7.007  -0.344  1.00 15.67  ? 164 LEU A CB  1 
ATOM   1329 C  CG  . LEU A 1 163 ? -11.382 -6.704  1.009   1.00 15.48  ? 164 LEU A CG  1 
ATOM   1330 C  CD1 . LEU A 1 163 ? -11.204 -7.840  2.012   1.00 16.92  ? 164 LEU A CD1 1 
ATOM   1331 C  CD2 . LEU A 1 163 ? -10.872 -5.387  1.569   1.00 15.89  ? 164 LEU A CD2 1 
ATOM   1332 N  N   . ASP A 1 164 ? -10.669 -7.008  -3.628  1.00 20.56  ? 165 ASP A N   1 
ATOM   1333 C  CA  . ASP A 1 164 ? -9.843  -7.337  -4.805  1.00 28.42  ? 165 ASP A CA  1 
ATOM   1334 C  C   . ASP A 1 164 ? -9.355  -6.042  -5.505  1.00 25.21  ? 165 ASP A C   1 
ATOM   1335 O  O   . ASP A 1 164 ? -8.334  -6.122  -6.238  1.00 28.67  ? 165 ASP A O   1 
ATOM   1336 C  CB  . ASP A 1 164 ? -10.621 -8.201  -5.837  1.00 41.10  ? 165 ASP A CB  1 
ATOM   1337 C  CG  . ASP A 1 164 ? -11.493 -7.360  -6.746  1.00 64.92  ? 165 ASP A CG  1 
ATOM   1338 O  OD1 . ASP A 1 164 ? -12.357 -6.587  -6.267  1.00 90.29  ? 165 ASP A OD1 1 
ATOM   1339 O  OD2 . ASP A 1 164 ? -11.364 -7.526  -8.003  1.00 113.05 ? 165 ASP A OD2 1 
ATOM   1340 N  N   . SER A 1 165 ? -10.041 -4.889  -5.284  1.00 20.97  ? 166 SER A N   1 
ATOM   1341 C  CA  . SER A 1 165 ? -9.627  -3.638  -5.954  1.00 22.98  ? 166 SER A CA  1 
ATOM   1342 C  C   . SER A 1 165 ? -8.566  -2.906  -5.159  1.00 20.47  ? 166 SER A C   1 
ATOM   1343 O  O   . SER A 1 165 ? -8.010  -1.914  -5.625  1.00 20.07  ? 166 SER A O   1 
ATOM   1344 C  CB  . SER A 1 165 ? -10.838 -2.778  -6.261  1.00 29.33  ? 166 SER A CB  1 
ATOM   1345 O  OG  . SER A 1 165 ? -11.290 -2.225  -5.062  1.00 23.48  ? 166 SER A OG  1 
ATOM   1346 N  N   . ILE A 1 166 ? -8.304  -3.365  -3.923  1.00 16.40  ? 167 ILE A N   1 
ATOM   1347 C  CA  . ILE A 1 166 ? -7.262  -2.719  -3.080  1.00 15.30  ? 167 ILE A CA  1 
ATOM   1348 C  C   . ILE A 1 166 ? -6.239  -3.735  -2.579  1.00 14.80  ? 167 ILE A C   1 
ATOM   1349 O  O   . ILE A 1 166 ? -5.840  -3.761  -1.418  1.00 15.03  ? 167 ILE A O   1 
ATOM   1350 C  CB  . ILE A 1 166 ? -7.844  -1.842  -1.897  1.00 16.90  ? 167 ILE A CB  1 
ATOM   1351 C  CG1 . ILE A 1 166 ? -8.741  -2.724  -1.024  1.00 15.38  ? 167 ILE A CG1 1 
ATOM   1352 C  CG2 . ILE A 1 166 ? -8.570  -0.660  -2.517  1.00 16.94  ? 167 ILE A CG2 1 
ATOM   1353 C  CD1 . ILE A 1 166 ? -8.749  -2.202  0.381   1.00 15.52  ? 167 ILE A CD1 1 
ATOM   1354 N  N   . LYS A 1 167 ? -5.858  -4.649  -3.486  1.00 15.51  ? 168 LYS A N   1 
ATOM   1355 C  CA  . LYS A 1 167 ? -5.072  -5.774  -3.058  1.00 15.84  ? 168 LYS A CA  1 
ATOM   1356 C  C   . LYS A 1 167 ? -3.768  -5.428  -2.403  1.00 16.14  ? 168 LYS A C   1 
ATOM   1357 O  O   . LYS A 1 167 ? -3.304  -6.074  -1.429  1.00 14.49  ? 168 LYS A O   1 
ATOM   1358 C  CB  . LYS A 1 167 ? -4.812  -6.723  -4.239  1.00 17.67  ? 168 LYS A CB  1 
ATOM   1359 C  CG  . LYS A 1 167 ? -4.082  -7.974  -3.825  1.00 18.20  ? 168 LYS A CG  1 
ATOM   1360 C  CD  . LYS A 1 167 ? -3.935  -8.846  -5.067  1.00 23.93  ? 168 LYS A CD  1 
ATOM   1361 C  CE  . LYS A 1 167 ? -2.623  -9.526  -5.016  1.00 38.59  ? 168 LYS A CE  1 
ATOM   1362 N  NZ  . LYS A 1 167 ? -2.832  -10.734 -4.210  1.00 61.88  ? 168 LYS A NZ  1 
ATOM   1363 N  N   . THR A 1 168 ? -3.167  -4.366  -2.896  1.00 15.26  ? 169 THR A N   1 
ATOM   1364 C  CA  . THR A 1 168 ? -1.808  -4.065  -2.501  1.00 15.38  ? 169 THR A CA  1 
ATOM   1365 C  C   . THR A 1 168 ? -1.675  -2.599  -1.839  1.00 13.95  ? 169 THR A C   1 
ATOM   1366 O  O   . THR A 1 168 ? -2.611  -1.772  -1.914  1.00 16.17  ? 169 THR A O   1 
ATOM   1367 C  CB  . THR A 1 168 ? -0.840  -4.076  -3.708  1.00 16.75  ? 169 THR A CB  1 
ATOM   1368 O  OG1 . THR A 1 168 ? -1.420  -3.321  -4.752  1.00 17.45  ? 169 THR A OG1 1 
ATOM   1369 C  CG2 . THR A 1 168 ? -0.626  -5.579  -4.168  1.00 18.63  ? 169 THR A CG2 1 
ATOM   1370 N  N   A LYS A 1 169 ? -0.593  -2.517  -1.072  0.50 17.80  ? 170 LYS A N   1 
ATOM   1371 N  N   B LYS A 1 169 ? -0.632  -2.510  -1.084  0.50 17.61  ? 170 LYS A N   1 
ATOM   1372 C  CA  A LYS A 1 169 ? -0.247  -1.292  -0.287  0.50 17.74  ? 170 LYS A CA  1 
ATOM   1373 C  CA  B LYS A 1 169 ? -0.429  -1.312  -0.298  0.50 14.18  ? 170 LYS A CA  1 
ATOM   1374 C  C   A LYS A 1 169 ? -0.451  -0.047  -1.123  0.50 14.93  ? 170 LYS A C   1 
ATOM   1375 C  C   B LYS A 1 169 ? -0.370  -0.039  -1.062  0.50 15.77  ? 170 LYS A C   1 
ATOM   1376 O  O   A LYS A 1 169 ? -0.023  -0.007  -2.283  0.50 15.52  ? 170 LYS A O   1 
ATOM   1377 O  O   B LYS A 1 169 ? 0.413   0.047   -2.059  0.50 21.60  ? 170 LYS A O   1 
ATOM   1378 C  CB  A LYS A 1 169 ? 1.186   -1.412  0.265   0.50 18.60  ? 170 LYS A CB  1 
ATOM   1379 C  CB  B LYS A 1 169 ? 0.880   -1.524  0.316   0.50 12.68  ? 170 LYS A CB  1 
ATOM   1380 C  CG  A LYS A 1 169 ? 1.606   -0.247  1.203   0.50 19.10  ? 170 LYS A CG  1 
ATOM   1381 C  CG  B LYS A 1 169 ? 1.423   -0.210  0.876   0.50 17.52  ? 170 LYS A CG  1 
ATOM   1382 C  CD  A LYS A 1 169 ? 3.006   -0.396  1.811   0.50 22.64  ? 170 LYS A CD  1 
ATOM   1383 C  CD  B LYS A 1 169 ? 2.641   -0.471  1.704   0.50 14.89  ? 170 LYS A CD  1 
ATOM   1384 C  CE  A LYS A 1 169 ? 3.426   0.783   2.715   0.50 29.57  ? 170 LYS A CE  1 
ATOM   1385 C  CE  B LYS A 1 169 ? 3.783   -0.947  0.816   0.50 19.97  ? 170 LYS A CE  1 
ATOM   1386 N  NZ  A LYS A 1 169 ? 4.861   0.662   3.102   0.50 33.37  ? 170 LYS A NZ  1 
ATOM   1387 N  NZ  B LYS A 1 169 ? 5.099   -1.139  1.483   0.50 27.68  ? 170 LYS A NZ  1 
ATOM   1388 N  N   . GLY A 1 170 ? -1.209  0.900   -0.596  1.00 17.27  ? 171 GLY A N   1 
ATOM   1389 C  CA  . GLY A 1 170 ? -1.373  2.185   -1.306  1.00 17.70  ? 171 GLY A CA  1 
ATOM   1390 C  C   . GLY A 1 170 ? -2.566  2.278   -2.249  1.00 17.15  ? 171 GLY A C   1 
ATOM   1391 O  O   . GLY A 1 170 ? -2.829  3.396   -2.711  1.00 20.47  ? 171 GLY A O   1 
ATOM   1392 N  N   . LYS A 1 171 ? -3.229  1.158   -2.574  1.00 15.82  ? 172 LYS A N   1 
ATOM   1393 C  CA  . LYS A 1 171 ? -4.448  1.234   -3.305  1.00 18.42  ? 172 LYS A CA  1 
ATOM   1394 C  C   . LYS A 1 171 ? -5.624  1.692   -2.475  1.00 15.24  ? 172 LYS A C   1 
ATOM   1395 O  O   . LYS A 1 171 ? -5.786  1.267   -1.342  1.00 15.57  ? 172 LYS A O   1 
ATOM   1396 C  CB  . LYS A 1 171 ? -4.690  -0.117  -3.962  1.00 17.23  ? 172 LYS A CB  1 
ATOM   1397 C  CG  . LYS A 1 171 ? -3.673  -0.502  -4.966  1.00 20.88  ? 172 LYS A CG  1 
ATOM   1398 C  CD  . LYS A 1 171 ? -4.089  -1.555  -6.064  1.00 27.13  ? 172 LYS A CD  1 
ATOM   1399 C  CE  . LYS A 1 171 ? -5.251  -1.175  -7.008  1.00 37.67  ? 172 LYS A CE  1 
ATOM   1400 N  NZ  . LYS A 1 171 ? -5.615  -2.292  -7.986  1.00 35.59  ? 172 LYS A NZ  1 
ATOM   1401 N  N   . SER A 1 172 ? -6.473  2.517   -3.021  1.00 18.66  ? 173 SER A N   1 
ATOM   1402 C  CA  . SER A 1 172 ? -7.709  2.936   -2.443  1.00 19.54  ? 173 SER A CA  1 
ATOM   1403 C  C   . SER A 1 172 ? -8.834  2.824   -3.425  1.00 15.73  ? 173 SER A C   1 
ATOM   1404 O  O   . SER A 1 172 ? -8.590  2.743   -4.713  1.00 20.10  ? 173 SER A O   1 
ATOM   1405 C  CB  . SER A 1 172 ? -7.608  4.345   -1.932  1.00 19.25  ? 173 SER A CB  1 
ATOM   1406 O  OG  . SER A 1 172 ? -7.284  5.246   -2.959  1.00 25.73  ? 173 SER A OG  1 
ATOM   1407 N  N   . ALA A 1 173 ? -10.105 2.765   -2.979  1.00 17.60  ? 174 ALA A N   1 
ATOM   1408 C  CA  . ALA A 1 173 ? -11.255 2.724   -3.855  1.00 21.16  ? 174 ALA A CA  1 
ATOM   1409 C  C   . ALA A 1 173 ? -12.408 3.538   -3.195  1.00 16.25  ? 174 ALA A C   1 
ATOM   1410 O  O   . ALA A 1 173 ? -12.497 3.594   -1.949  1.00 16.13  ? 174 ALA A O   1 
ATOM   1411 C  CB  . ALA A 1 173 ? -11.653 1.279   -4.084  1.00 22.93  ? 174 ALA A CB  1 
ATOM   1412 N  N   . ASP A 1 174 ? -13.202 4.232   -3.988  1.00 19.43  ? 175 ASP A N   1 
ATOM   1413 C  CA  . ASP A 1 174 ? -14.428 4.900   -3.440  1.00 19.02  ? 175 ASP A CA  1 
ATOM   1414 C  C   . ASP A 1 174 ? -15.236 3.870   -2.743  1.00 19.78  ? 175 ASP A C   1 
ATOM   1415 O  O   . ASP A 1 174 ? -15.302 2.672   -3.171  1.00 21.57  ? 175 ASP A O   1 
ATOM   1416 C  CB  . ASP A 1 174 ? -15.277 5.434   -4.626  1.00 21.68  ? 175 ASP A CB  1 
ATOM   1417 C  CG  . ASP A 1 174 ? -14.558 6.533   -5.385  1.00 34.43  ? 175 ASP A CG  1 
ATOM   1418 O  OD1 . ASP A 1 174 ? -13.939 7.398   -4.746  1.00 82.19  ? 175 ASP A OD1 1 
ATOM   1419 O  OD2 . ASP A 1 174 ? -14.653 6.604   -6.655  1.00 28.58  ? 175 ASP A OD2 1 
ATOM   1420 N  N   . PHE A 1 175 ? -15.771 4.281   -1.578  1.00 18.76  ? 176 PHE A N   1 
ATOM   1421 C  CA  . PHE A 1 175 ? -16.553 3.371   -0.733  1.00 17.47  ? 176 PHE A CA  1 
ATOM   1422 C  C   . PHE A 1 175 ? -17.539 4.184   -0.015  1.00 17.62  ? 176 PHE A C   1 
ATOM   1423 O  O   . PHE A 1 175 ? -17.369 4.419   1.156   1.00 19.68  ? 176 PHE A O   1 
ATOM   1424 C  CB  . PHE A 1 175 ? -15.602 2.597   0.143   1.00 18.00  ? 176 PHE A CB  1 
ATOM   1425 C  CG  . PHE A 1 175 ? -16.172 1.318   0.649   1.00 16.51  ? 176 PHE A CG  1 
ATOM   1426 C  CD1 . PHE A 1 175 ? -16.472 0.267   -0.208  1.00 21.43  ? 176 PHE A CD1 1 
ATOM   1427 C  CD2 . PHE A 1 175 ? -16.480 1.182   2.004   1.00 17.61  ? 176 PHE A CD2 1 
ATOM   1428 C  CE1 . PHE A 1 175 ? -17.011 -0.879  0.298   1.00 22.00  ? 176 PHE A CE1 1 
ATOM   1429 C  CE2 . PHE A 1 175 ? -16.977 0.001   2.515   1.00 19.53  ? 176 PHE A CE2 1 
ATOM   1430 C  CZ  . PHE A 1 175 ? -17.307 -1.002  1.653   1.00 18.76  ? 176 PHE A CZ  1 
ATOM   1431 N  N   . THR A 1 176 ? -18.542 4.635   -0.729  1.00 18.53  ? 177 THR A N   1 
ATOM   1432 C  CA  . THR A 1 176 ? -19.612 5.426   -0.125  1.00 17.92  ? 177 THR A CA  1 
ATOM   1433 C  C   . THR A 1 176 ? -20.803 4.633   0.306   1.00 14.99  ? 177 THR A C   1 
ATOM   1434 O  O   . THR A 1 176 ? -20.960 3.465   -0.181  1.00 16.95  ? 177 THR A O   1 
ATOM   1435 C  CB  . THR A 1 176 ? -20.085 6.457   -1.176  1.00 17.56  ? 177 THR A CB  1 
ATOM   1436 O  OG1 . THR A 1 176 ? -20.405 5.842   -2.421  1.00 23.59  ? 177 THR A OG1 1 
ATOM   1437 C  CG2 . THR A 1 176 ? -18.950 7.471   -1.433  1.00 26.08  ? 177 THR A CG2 1 
ATOM   1438 N  N   . ASN A 1 177 ? -21.625 5.153   1.204   1.00 16.29  ? 178 ASN A N   1 
ATOM   1439 C  CA  . ASN A 1 177 ? -22.883 4.600   1.586   1.00 17.26  ? 178 ASN A CA  1 
ATOM   1440 C  C   . ASN A 1 177 ? -22.736 3.295   2.347   1.00 15.91  ? 178 ASN A C   1 
ATOM   1441 O  O   . ASN A 1 177 ? -23.644 2.519   2.322   1.00 23.12  ? 178 ASN A O   1 
ATOM   1442 C  CB  . ASN A 1 177 ? -23.786 4.492   0.385   1.00 19.55  ? 178 ASN A CB  1 
ATOM   1443 C  CG  . ASN A 1 177 ? -24.010 5.886   -0.195  1.00 19.09  ? 178 ASN A CG  1 
ATOM   1444 O  OD1 . ASN A 1 177 ? -24.674 6.730   0.400   1.00 19.96  ? 178 ASN A OD1 1 
ATOM   1445 N  ND2 . ASN A 1 177 ? -23.368 6.142   -1.342  1.00 17.26  ? 178 ASN A ND2 1 
ATOM   1446 N  N   . PHE A 1 178 ? -21.527 3.045   2.918   1.00 16.28  ? 179 PHE A N   1 
ATOM   1447 C  CA  . PHE A 1 178 ? -21.350 1.840   3.713   1.00 15.35  ? 179 PHE A CA  1 
ATOM   1448 C  C   . PHE A 1 178 ? -21.885 2.102   5.101   1.00 14.93  ? 179 PHE A C   1 
ATOM   1449 O  O   . PHE A 1 178 ? -21.435 3.082   5.725   1.00 16.97  ? 179 PHE A O   1 
ATOM   1450 C  CB  . PHE A 1 178 ? -19.941 1.384   3.800   1.00 15.40  ? 179 PHE A CB  1 
ATOM   1451 C  CG  . PHE A 1 178 ? -19.821 0.137   4.641   1.00 15.51  ? 179 PHE A CG  1 
ATOM   1452 C  CD1 . PHE A 1 178 ? -20.192 -1.111  4.084   1.00 17.06  ? 179 PHE A CD1 1 
ATOM   1453 C  CD2 . PHE A 1 178 ? -19.458 0.226   5.969   1.00 14.67  ? 179 PHE A CD2 1 
ATOM   1454 C  CE1 . PHE A 1 178 ? -20.132 -2.245  4.811   1.00 17.88  ? 179 PHE A CE1 1 
ATOM   1455 C  CE2 . PHE A 1 178 ? -19.458 -0.978  6.734   1.00 14.49  ? 179 PHE A CE2 1 
ATOM   1456 C  CZ  . PHE A 1 178 ? -19.777 -2.188  6.163   1.00 15.54  ? 179 PHE A CZ  1 
ATOM   1457 N  N   . ASP A 1 179 ? -22.787 1.276   5.635   1.00 15.37  ? 180 ASP A N   1 
ATOM   1458 C  CA  . ASP A 1 179 ? -23.381 1.482   6.922   1.00 16.04  ? 180 ASP A CA  1 
ATOM   1459 C  C   . ASP A 1 179 ? -22.704 0.632   7.970   1.00 14.00  ? 180 ASP A C   1 
ATOM   1460 O  O   . ASP A 1 179 ? -22.870 -0.595  7.993   1.00 15.18  ? 180 ASP A O   1 
ATOM   1461 C  CB  . ASP A 1 179 ? -24.873 1.081   6.823   1.00 18.27  ? 180 ASP A CB  1 
ATOM   1462 C  CG  . ASP A 1 179 ? -25.631 1.440   8.079   1.00 20.33  ? 180 ASP A CG  1 
ATOM   1463 O  OD1 . ASP A 1 179 ? -25.029 1.759   9.136   1.00 17.42  ? 180 ASP A OD1 1 
ATOM   1464 O  OD2 . ASP A 1 179 ? -26.866 1.498   7.990   1.00 25.74  ? 180 ASP A OD2 1 
ATOM   1465 N  N   . PRO A 1 180 ? -21.891 1.230   8.867   1.00 13.16  ? 181 PRO A N   1 
ATOM   1466 C  CA  . PRO A 1 180 ? -21.149 0.376   9.842   1.00 13.59  ? 181 PRO A CA  1 
ATOM   1467 C  C   . PRO A 1 180 ? -22.073 -0.225  10.909  1.00 13.93  ? 181 PRO A C   1 
ATOM   1468 O  O   . PRO A 1 180 ? -21.605 -1.110  11.629  1.00 13.57  ? 181 PRO A O   1 
ATOM   1469 C  CB  . PRO A 1 180 ? -20.170 1.375   10.446  1.00 14.66  ? 181 PRO A CB  1 
ATOM   1470 C  CG  . PRO A 1 180 ? -20.856 2.724   10.314  1.00 15.62  ? 181 PRO A CG  1 
ATOM   1471 C  CD  . PRO A 1 180 ? -21.592 2.661   8.993   1.00 14.45  ? 181 PRO A CD  1 
ATOM   1472 N  N   . ARG A 1 181 ? -23.339 0.169   10.937  1.00 13.77  ? 182 ARG A N   1 
ATOM   1473 C  CA  . ARG A 1 181 ? -24.274 -0.499  11.897  1.00 14.35  ? 182 ARG A CA  1 
ATOM   1474 C  C   . ARG A 1 181 ? -24.357 -1.978  11.538  1.00 14.26  ? 182 ARG A C   1 
ATOM   1475 O  O   . ARG A 1 181 ? -24.736 -2.772  12.400  1.00 15.58  ? 182 ARG A O   1 
ATOM   1476 C  CB  . ARG A 1 181 ? -25.636 0.132   11.852  1.00 14.28  ? 182 ARG A CB  1 
ATOM   1477 C  CG  . ARG A 1 181 ? -25.560 1.565   12.389  1.00 15.89  ? 182 ARG A CG  1 
ATOM   1478 C  CD  . ARG A 1 181 ? -26.883 2.308   12.376  1.00 19.32  ? 182 ARG A CD  1 
ATOM   1479 N  NE  . ARG A 1 181 ? -27.318 2.474   11.004  1.00 18.34  ? 182 ARG A NE  1 
ATOM   1480 C  CZ  . ARG A 1 181 ? -28.448 3.125   10.703  1.00 18.83  ? 182 ARG A CZ  1 
ATOM   1481 N  NH1 . ARG A 1 181 ? -29.218 3.619   11.663  1.00 23.08  ? 182 ARG A NH1 1 
ATOM   1482 N  NH2 . ARG A 1 181 ? -28.805 3.232   9.425   1.00 24.95  ? 182 ARG A NH2 1 
ATOM   1483 N  N   . GLY A 1 182 ? -24.124 -2.344  10.288  1.00 14.29  ? 183 GLY A N   1 
ATOM   1484 C  CA  . GLY A 1 182 ? -24.245 -3.738  9.905   1.00 14.85  ? 183 GLY A CA  1 
ATOM   1485 C  C   . GLY A 1 182 ? -23.095 -4.608  10.423  1.00 15.30  ? 183 GLY A C   1 
ATOM   1486 O  O   . GLY A 1 182 ? -23.074 -5.782  10.136  1.00 17.98  ? 183 GLY A O   1 
ATOM   1487 N  N   . LEU A 1 183 ? -22.116 -4.046  11.163  1.00 14.03  ? 184 LEU A N   1 
ATOM   1488 C  CA  . LEU A 1 183 ? -20.990 -4.772  11.689  1.00 13.43  ? 184 LEU A CA  1 
ATOM   1489 C  C   . LEU A 1 183 ? -21.124 -4.998  13.175  1.00 13.22  ? 184 LEU A C   1 
ATOM   1490 O  O   . LEU A 1 183 ? -20.212 -5.582  13.808  1.00 14.61  ? 184 LEU A O   1 
ATOM   1491 C  CB  . LEU A 1 183 ? -19.687 -4.034  11.425  1.00 13.87  ? 184 LEU A CB  1 
ATOM   1492 C  CG  . LEU A 1 183 ? -19.405 -3.907  9.910   1.00 15.70  ? 184 LEU A CG  1 
ATOM   1493 C  CD1 . LEU A 1 183 ? -18.138 -3.091  9.791   1.00 18.72  ? 184 LEU A CD1 1 
ATOM   1494 C  CD2 . LEU A 1 183 ? -19.291 -5.217  9.191   1.00 18.54  ? 184 LEU A CD2 1 
ATOM   1495 N  N   . LEU A 1 184 ? -22.201 -4.530  13.804  1.00 13.65  ? 185 LEU A N   1 
ATOM   1496 C  CA  . LEU A 1 184 ? -22.380 -4.607  15.249  1.00 12.59  ? 185 LEU A CA  1 
ATOM   1497 C  C   . LEU A 1 184 ? -23.094 -5.915  15.633  1.00 14.81  ? 185 LEU A C   1 
ATOM   1498 O  O   . LEU A 1 184 ? -23.893 -6.432  14.853  1.00 19.69  ? 185 LEU A O   1 
ATOM   1499 C  CB  . LEU A 1 184 ? -23.212 -3.394  15.792  1.00 13.31  ? 185 LEU A CB  1 
ATOM   1500 C  CG  . LEU A 1 184 ? -22.644 -2.042  15.397  1.00 13.03  ? 185 LEU A CG  1 
ATOM   1501 C  CD1 . LEU A 1 184 ? -23.541 -0.913  15.874  1.00 15.33  ? 185 LEU A CD1 1 
ATOM   1502 C  CD2 . LEU A 1 184 ? -21.227 -1.882  15.910  1.00 16.84  ? 185 LEU A CD2 1 
ATOM   1503 N  N   . PRO A 1 185 ? -22.811 -6.450  16.852  1.00 12.88  ? 186 PRO A N   1 
ATOM   1504 C  CA  . PRO A 1 185 ? -23.574 -7.567  17.399  1.00 13.15  ? 186 PRO A CA  1 
ATOM   1505 C  C   . PRO A 1 185 ? -24.851 -7.022  17.981  1.00 13.28  ? 186 PRO A C   1 
ATOM   1506 O  O   . PRO A 1 185 ? -25.076 -5.823  17.991  1.00 16.93  ? 186 PRO A O   1 
ATOM   1507 C  CB  . PRO A 1 185 ? -22.646 -8.112  18.465  1.00 12.85  ? 186 PRO A CB  1 
ATOM   1508 C  CG  . PRO A 1 185 ? -21.950 -6.927  18.959  1.00 12.28  ? 186 PRO A CG  1 
ATOM   1509 C  CD  . PRO A 1 185 ? -21.704 -6.030  17.727  1.00 11.69  ? 186 PRO A CD  1 
ATOM   1510 N  N   A GLU A 1 186 ? -25.663 -7.923  18.507  0.50 15.26  ? 187 GLU A N   1 
ATOM   1511 N  N   B GLU A 1 186 ? -25.703 -7.915  18.506  0.50 15.06  ? 187 GLU A N   1 
ATOM   1512 C  CA  A GLU A 1 186 ? -26.956 -7.518  19.033  0.50 15.60  ? 187 GLU A CA  1 
ATOM   1513 C  CA  B GLU A 1 186 ? -26.996 -7.483  19.117  0.50 14.16  ? 187 GLU A CA  1 
ATOM   1514 C  C   A GLU A 1 186 ? -26.771 -6.766  20.377  0.50 13.85  ? 187 GLU A C   1 
ATOM   1515 C  C   B GLU A 1 186 ? -26.742 -6.707  20.397  0.50 14.16  ? 187 GLU A C   1 
ATOM   1516 O  O   A GLU A 1 186 ? -27.440 -5.742  20.607  0.50 19.69  ? 187 GLU A O   1 
ATOM   1517 O  O   B GLU A 1 186 ? -27.345 -5.637  20.629  0.50 17.82  ? 187 GLU A O   1 
ATOM   1518 C  CB  A GLU A 1 186 ? -27.713 -8.788  19.201  0.50 18.83  ? 187 GLU A CB  1 
ATOM   1519 C  CB  B GLU A 1 186 ? -27.746 -8.700  19.501  0.50 20.16  ? 187 GLU A CB  1 
ATOM   1520 C  CG  A GLU A 1 186 ? -28.792 -8.688  20.226  0.50 22.13  ? 187 GLU A CG  1 
ATOM   1521 C  CG  B GLU A 1 186 ? -28.442 -9.332  18.324  0.50 22.66  ? 187 GLU A CG  1 
ATOM   1522 C  CD  A GLU A 1 186 ? -29.457 -10.006 20.551  0.50 24.63  ? 187 GLU A CD  1 
ATOM   1523 C  CD  B GLU A 1 186 ? -29.286 -10.506 18.719  0.50 23.41  ? 187 GLU A CD  1 
ATOM   1524 O  OE1 A GLU A 1 186 ? -29.305 -10.976 19.741  0.50 24.04  ? 187 GLU A OE1 1 
ATOM   1525 O  OE1 B GLU A 1 186 ? -29.516 -10.734 19.939  0.50 24.81  ? 187 GLU A OE1 1 
ATOM   1526 O  OE2 A GLU A 1 186 ? -30.076 -10.032 21.635  0.50 26.08  ? 187 GLU A OE2 1 
ATOM   1527 O  OE2 B GLU A 1 186 ? -29.795 -11.232 17.802  0.50 27.35  ? 187 GLU A OE2 1 
ATOM   1528 N  N   . SER A 1 187 ? -25.869 -7.240  21.260  1.00 13.72  ? 188 SER A N   1 
ATOM   1529 C  CA  . SER A 1 187 ? -25.697 -6.608  22.551  1.00 14.38  ? 188 SER A CA  1 
ATOM   1530 C  C   . SER A 1 187 ? -24.563 -5.622  22.557  1.00 14.09  ? 188 SER A C   1 
ATOM   1531 O  O   . SER A 1 187 ? -23.521 -5.887  21.927  1.00 14.90  ? 188 SER A O   1 
ATOM   1532 C  CB  . SER A 1 187 ? -25.266 -7.690  23.533  1.00 16.31  ? 188 SER A CB  1 
ATOM   1533 O  OG  . SER A 1 187 ? -25.039 -7.149  24.852  1.00 16.28  ? 188 SER A OG  1 
ATOM   1534 N  N   . LEU A 1 188 ? -24.710 -4.552  23.279  1.00 12.83  ? 189 LEU A N   1 
ATOM   1535 C  CA  . LEU A 1 188 ? -23.633 -3.583  23.508  1.00 13.10  ? 189 LEU A CA  1 
ATOM   1536 C  C   . LEU A 1 188 ? -23.034 -3.703  24.880  1.00 12.92  ? 189 LEU A C   1 
ATOM   1537 O  O   . LEU A 1 188 ? -22.329 -2.797  25.331  1.00 14.43  ? 189 LEU A O   1 
ATOM   1538 C  CB  . LEU A 1 188 ? -24.119 -2.146  23.233  1.00 15.96  ? 189 LEU A CB  1 
ATOM   1539 C  CG  . LEU A 1 188 ? -24.596 -1.841  21.838  1.00 17.25  ? 189 LEU A CG  1 
ATOM   1540 C  CD1 . LEU A 1 188 ? -25.130 -0.389  21.708  1.00 18.26  ? 189 LEU A CD1 1 
ATOM   1541 C  CD2 . LEU A 1 188 ? -23.511 -2.161  20.826  1.00 19.86  ? 189 LEU A CD2 1 
ATOM   1542 N  N   . ASP A 1 189 ? -23.148 -4.869  25.565  1.00 12.38  ? 190 ASP A N   1 
ATOM   1543 C  CA  . ASP A 1 189 ? -22.401 -5.061  26.794  1.00 14.16  ? 190 ASP A CA  1 
ATOM   1544 C  C   . ASP A 1 189 ? -20.885 -5.050  26.507  1.00 11.34  ? 190 ASP A C   1 
ATOM   1545 O  O   . ASP A 1 189 ? -20.453 -5.535  25.460  1.00 11.21  ? 190 ASP A O   1 
ATOM   1546 C  CB  . ASP A 1 189 ? -22.725 -6.422  27.422  1.00 16.08  ? 190 ASP A CB  1 
ATOM   1547 C  CG  . ASP A 1 189 ? -24.107 -6.529  28.060  1.00 19.57  ? 190 ASP A CG  1 
ATOM   1548 O  OD1 . ASP A 1 189 ? -24.767 -5.483  28.232  1.00 26.67  ? 190 ASP A OD1 1 
ATOM   1549 O  OD2 . ASP A 1 189 ? -24.558 -7.665  28.306  1.00 29.17  ? 190 ASP A OD2 1 
ATOM   1550 N  N   . TYR A 1 190 ? -20.120 -4.457  27.403  1.00 11.03  ? 191 TYR A N   1 
ATOM   1551 C  CA  . TYR A 1 190 ? -18.715 -4.226  27.088  1.00 11.33  ? 191 TYR A CA  1 
ATOM   1552 C  C   . TYR A 1 190 ? -17.833 -4.269  28.323  1.00 9.03   ? 191 TYR A C   1 
ATOM   1553 O  O   . TYR A 1 190 ? -18.240 -4.145  29.463  1.00 10.71  ? 191 TYR A O   1 
ATOM   1554 C  CB  . TYR A 1 190 ? -18.560 -2.813  26.434  1.00 11.14  ? 191 TYR A CB  1 
ATOM   1555 C  CG  . TYR A 1 190 ? -18.961 -1.657  27.274  1.00 10.41  ? 191 TYR A CG  1 
ATOM   1556 C  CD1 . TYR A 1 190 ? -18.024 -1.056  28.162  1.00 11.21  ? 191 TYR A CD1 1 
ATOM   1557 C  CD2 . TYR A 1 190 ? -20.248 -1.145  27.267  1.00 12.01  ? 191 TYR A CD2 1 
ATOM   1558 C  CE1 . TYR A 1 190 ? -18.413 0.002   28.983  1.00 12.30  ? 191 TYR A CE1 1 
ATOM   1559 C  CE2 . TYR A 1 190 ? -20.632 -0.069  28.054  1.00 12.48  ? 191 TYR A CE2 1 
ATOM   1560 C  CZ  . TYR A 1 190 ? -19.738 0.476   28.933  1.00 12.13  ? 191 TYR A CZ  1 
ATOM   1561 O  OH  . TYR A 1 190 ? -20.075 1.488   29.769  1.00 13.20  ? 191 TYR A OH  1 
ATOM   1562 N  N   . TRP A 1 191 ? -16.543 -4.406  28.035  1.00 9.24   ? 192 TRP A N   1 
ATOM   1563 C  CA  . TRP A 1 191 ? -15.460 -4.144  28.974  1.00 8.89   ? 192 TRP A CA  1 
ATOM   1564 C  C   . TRP A 1 191 ? -14.780 -2.865  28.562  1.00 8.78   ? 192 TRP A C   1 
ATOM   1565 O  O   . TRP A 1 191 ? -14.713 -2.536  27.382  1.00 10.01  ? 192 TRP A O   1 
ATOM   1566 C  CB  . TRP A 1 191 ? -14.396 -5.267  28.966  1.00 9.60   ? 192 TRP A CB  1 
ATOM   1567 C  CG  . TRP A 1 191 ? -14.911 -6.613  29.392  1.00 9.82   ? 192 TRP A CG  1 
ATOM   1568 C  CD1 . TRP A 1 191 ? -15.159 -7.024  30.669  1.00 11.40  ? 192 TRP A CD1 1 
ATOM   1569 C  CD2 . TRP A 1 191 ? -15.187 -7.720  28.529  1.00 9.62   ? 192 TRP A CD2 1 
ATOM   1570 N  NE1 . TRP A 1 191 ? -15.539 -8.364  30.636  1.00 12.02  ? 192 TRP A NE1 1 
ATOM   1571 C  CE2 . TRP A 1 191 ? -15.569 -8.788  29.365  1.00 11.74  ? 192 TRP A CE2 1 
ATOM   1572 C  CE3 . TRP A 1 191 ? -15.092 -7.913  27.158  1.00 10.47  ? 192 TRP A CE3 1 
ATOM   1573 C  CZ2 . TRP A 1 191 ? -15.893 -10.066 28.837  1.00 12.28  ? 192 TRP A CZ2 1 
ATOM   1574 C  CZ3 . TRP A 1 191 ? -15.390 -9.164  26.659  1.00 11.62  ? 192 TRP A CZ3 1 
ATOM   1575 C  CH2 . TRP A 1 191 ? -15.767 -10.209 27.497  1.00 12.36  ? 192 TRP A CH2 1 
ATOM   1576 N  N   . THR A 1 192 ? -14.132 -2.164  29.509  1.00 8.87   ? 193 THR A N   1 
ATOM   1577 C  CA  . THR A 1 192 ? -13.416 -0.918  29.179  1.00 9.06   ? 193 THR A CA  1 
ATOM   1578 C  C   . THR A 1 192 ? -12.170 -0.784  30.029  1.00 8.47   ? 193 THR A C   1 
ATOM   1579 O  O   . THR A 1 192 ? -12.166 -1.158  31.218  1.00 9.68   ? 193 THR A O   1 
ATOM   1580 C  CB  . THR A 1 192 ? -14.379 0.276   29.297  1.00 8.97   ? 193 THR A CB  1 
ATOM   1581 O  OG1 . THR A 1 192 ? -13.672 1.462   28.886  1.00 9.52   ? 193 THR A OG1 1 
ATOM   1582 C  CG2 . THR A 1 192 ? -14.906 0.478   30.699  1.00 10.31  ? 193 THR A CG2 1 
ATOM   1583 N  N   . TYR A 1 193 ? -11.142 -0.159  29.469  1.00 8.57   ? 194 TYR A N   1 
ATOM   1584 C  CA  . TYR A 1 193 ? -9.936  0.104   30.179  1.00 8.89   ? 194 TYR A CA  1 
ATOM   1585 C  C   . TYR A 1 193 ? -9.167  1.174   29.416  1.00 8.53   ? 194 TYR A C   1 
ATOM   1586 O  O   . TYR A 1 193 ? -9.363  1.341   28.226  1.00 9.06   ? 194 TYR A O   1 
ATOM   1587 C  CB  . TYR A 1 193 ? -9.079  -1.177  30.391  1.00 9.94   ? 194 TYR A CB  1 
ATOM   1588 C  CG  . TYR A 1 193 ? -8.380  -1.666  29.124  1.00 9.06   ? 194 TYR A CG  1 
ATOM   1589 C  CD1 . TYR A 1 193 ? -9.057  -2.410  28.145  1.00 8.51   ? 194 TYR A CD1 1 
ATOM   1590 C  CD2 . TYR A 1 193 ? -7.045  -1.308  28.906  1.00 8.85   ? 194 TYR A CD2 1 
ATOM   1591 C  CE1 . TYR A 1 193 ? -8.444  -2.711  26.954  1.00 8.60   ? 194 TYR A CE1 1 
ATOM   1592 C  CE2 . TYR A 1 193 ? -6.419  -1.631  27.738  1.00 8.96   ? 194 TYR A CE2 1 
ATOM   1593 C  CZ  . TYR A 1 193 ? -7.117  -2.363  26.742  1.00 8.44   ? 194 TYR A CZ  1 
ATOM   1594 O  OH  . TYR A 1 193 ? -6.455  -2.623  25.583  1.00 8.66   ? 194 TYR A OH  1 
ATOM   1595 N  N   . PRO A 1 194 ? -8.177  1.826   30.086  1.00 8.68   ? 195 PRO A N   1 
ATOM   1596 C  CA  . PRO A 1 194 ? -7.365  2.846   29.398  1.00 9.40   ? 195 PRO A CA  1 
ATOM   1597 C  C   . PRO A 1 194 ? -6.192  2.201   28.714  1.00 7.98   ? 195 PRO A C   1 
ATOM   1598 O  O   . PRO A 1 194 ? -5.430  1.403   29.383  1.00 9.80   ? 195 PRO A O   1 
ATOM   1599 C  CB  . PRO A 1 194 ? -6.897  3.760   30.547  1.00 10.81  ? 195 PRO A CB  1 
ATOM   1600 C  CG  . PRO A 1 194 ? -6.854  2.789   31.760  1.00 11.65  ? 195 PRO A CG  1 
ATOM   1601 C  CD  . PRO A 1 194 ? -7.977  1.824   31.539  1.00 10.64  ? 195 PRO A CD  1 
ATOM   1602 N  N   . GLY A 1 195 ? -5.948  2.502   27.458  1.00 8.43   ? 196 GLY A N   1 
ATOM   1603 C  CA  . GLY A 1 195 ? -4.809  1.896   26.715  1.00 8.90   ? 196 GLY A CA  1 
ATOM   1604 C  C   . GLY A 1 195 ? -4.310  2.731   25.649  1.00 7.73   ? 196 GLY A C   1 
ATOM   1605 O  O   . GLY A 1 195 ? -4.185  3.988   25.776  1.00 8.49   ? 196 GLY A O   1 
ATOM   1606 N  N   . SER A 1 196 ? -3.861  2.108   24.600  1.00 8.20   ? 197 SER A N   1 
ATOM   1607 C  CA  . SER A 1 196 ? -3.043  2.736   23.565  1.00 8.23   ? 197 SER A CA  1 
ATOM   1608 C  C   . SER A 1 196 ? -3.504  2.328   22.166  1.00 7.75   ? 197 SER A C   1 
ATOM   1609 O  O   . SER A 1 196 ? -4.258  1.365   21.995  1.00 8.57   ? 197 SER A O   1 
ATOM   1610 C  CB  . SER A 1 196 ? -1.561  2.340   23.712  1.00 9.03   ? 197 SER A CB  1 
ATOM   1611 O  OG  . SER A 1 196 ? -1.323  0.999   23.276  1.00 8.74   ? 197 SER A OG  1 
ATOM   1612 N  N   . LEU A 1 197 ? -2.950  2.996   21.170  1.00 8.45   ? 198 LEU A N   1 
ATOM   1613 C  CA  . LEU A 1 197 ? -2.974  2.463   19.809  1.00 8.38   ? 198 LEU A CA  1 
ATOM   1614 C  C   . LEU A 1 197 ? -2.236  1.164   19.834  1.00 8.80   ? 198 LEU A C   1 
ATOM   1615 O  O   . LEU A 1 197 ? -1.207  1.005   20.522  1.00 9.05   ? 198 LEU A O   1 
ATOM   1616 C  CB  . LEU A 1 197 ? -2.233  3.425   18.867  1.00 9.64   ? 198 LEU A CB  1 
ATOM   1617 C  CG  . LEU A 1 197 ? -2.772  4.859   18.796  1.00 9.50   ? 198 LEU A CG  1 
ATOM   1618 C  CD1 . LEU A 1 197 ? -1.906  5.665   17.802  1.00 12.08  ? 198 LEU A CD1 1 
ATOM   1619 C  CD2 . LEU A 1 197 ? -4.196  4.915   18.416  1.00 11.42  ? 198 LEU A CD2 1 
ATOM   1620 N  N   . THR A 1 198 ? -2.674  0.189   19.018  1.00 8.42   ? 199 THR A N   1 
ATOM   1621 C  CA  . THR A 1 198 ? -2.008  -1.096  18.923  1.00 8.94   ? 199 THR A CA  1 
ATOM   1622 C  C   . THR A 1 198 ? -1.033  -1.203  17.778  1.00 8.82   ? 199 THR A C   1 
ATOM   1623 O  O   . THR A 1 198 ? -0.410  -2.266  17.610  1.00 9.61   ? 199 THR A O   1 
ATOM   1624 C  CB  . THR A 1 198 ? -3.033  -2.249  18.849  1.00 8.45   ? 199 THR A CB  1 
ATOM   1625 O  OG1 . THR A 1 198 ? -3.604  -2.207  17.565  1.00 8.38   ? 199 THR A OG1 1 
ATOM   1626 C  CG2 . THR A 1 198 ? -4.019  -2.228  19.992  1.00 9.14   ? 199 THR A CG2 1 
ATOM   1627 N  N   . THR A 1 199 ? -0.830  -0.120  17.002  1.00 9.73   ? 200 THR A N   1 
ATOM   1628 C  CA  . THR A 1 199 ? 0.184   -0.036  16.017  1.00 10.12  ? 200 THR A CA  1 
ATOM   1629 C  C   . THR A 1 199 ? 1.046   1.194   16.335  1.00 10.29  ? 200 THR A C   1 
ATOM   1630 O  O   . THR A 1 199 ? 0.548   2.143   16.937  1.00 10.50  ? 200 THR A O   1 
ATOM   1631 C  CB  . THR A 1 199 ? -0.288  0.056   14.561  1.00 10.57  ? 200 THR A CB  1 
ATOM   1632 O  OG1 . THR A 1 199 ? -1.110  1.183   14.401  1.00 15.72  ? 200 THR A OG1 1 
ATOM   1633 C  CG2 . THR A 1 199 ? -1.112  -1.129  14.205  1.00 14.14  ? 200 THR A CG2 1 
ATOM   1634 N  N   . PRO A 1 200 ? 2.312   1.228   15.864  1.00 10.56  ? 201 PRO A N   1 
ATOM   1635 C  CA  . PRO A 1 200 ? 3.057   2.436   15.968  1.00 10.79  ? 201 PRO A CA  1 
ATOM   1636 C  C   . PRO A 1 200 ? 2.215   3.596   15.447  1.00 11.72  ? 201 PRO A C   1 
ATOM   1637 O  O   . PRO A 1 200 ? 1.550   3.465   14.421  1.00 13.48  ? 201 PRO A O   1 
ATOM   1638 C  CB  . PRO A 1 200 ? 4.286   2.112   15.074  1.00 12.57  ? 201 PRO A CB  1 
ATOM   1639 C  CG  . PRO A 1 200 ? 4.490   0.661   15.315  1.00 12.57  ? 201 PRO A CG  1 
ATOM   1640 C  CD  . PRO A 1 200 ? 3.102   0.099   15.282  1.00 12.39  ? 201 PRO A CD  1 
ATOM   1641 N  N   . PRO A 1 201 ? 2.257   4.748   16.085  1.00 11.43  ? 202 PRO A N   1 
ATOM   1642 C  CA  . PRO A 1 201 ? 3.189   5.139   17.182  1.00 11.21  ? 202 PRO A CA  1 
ATOM   1643 C  C   . PRO A 1 201 ? 2.802   4.729   18.606  1.00 10.65  ? 202 PRO A C   1 
ATOM   1644 O  O   . PRO A 1 201 ? 3.473   5.151   19.542  1.00 11.63  ? 202 PRO A O   1 
ATOM   1645 C  CB  . PRO A 1 201 ? 3.196   6.677   17.024  1.00 13.56  ? 202 PRO A CB  1 
ATOM   1646 C  CG  . PRO A 1 201 ? 1.748   7.031   16.547  1.00 14.46  ? 202 PRO A CG  1 
ATOM   1647 C  CD  . PRO A 1 201 ? 1.475   5.903   15.547  1.00 12.98  ? 202 PRO A CD  1 
ATOM   1648 N  N   . LEU A 1 202 ? 1.788   3.872   18.762  1.00 9.77   ? 203 LEU A N   1 
ATOM   1649 C  CA  . LEU A 1 202 ? 1.566   3.235   20.058  1.00 9.72   ? 203 LEU A CA  1 
ATOM   1650 C  C   . LEU A 1 202 ? 1.220   4.238   21.161  1.00 9.93   ? 203 LEU A C   1 
ATOM   1651 O  O   . LEU A 1 202 ? 1.332   3.996   22.354  1.00 9.36   ? 203 LEU A O   1 
ATOM   1652 C  CB  . LEU A 1 202 ? 2.730   2.361   20.516  1.00 9.90   ? 203 LEU A CB  1 
ATOM   1653 C  CG  . LEU A 1 202 ? 3.064   1.192   19.557  1.00 10.64  ? 203 LEU A CG  1 
ATOM   1654 C  CD1 . LEU A 1 202 ? 4.365   0.550   20.038  1.00 12.44  ? 203 LEU A CD1 1 
ATOM   1655 C  CD2 . LEU A 1 202 ? 1.950   0.157   19.478  1.00 11.15  ? 203 LEU A CD2 1 
ATOM   1656 N  N   . LEU A 1 203 ? 0.567   5.361   20.757  1.00 9.87   ? 204 LEU A N   1 
ATOM   1657 C  CA  . LEU A 1 203 ? 0.308   6.491   21.660  1.00 10.53  ? 204 LEU A CA  1 
ATOM   1658 C  C   . LEU A 1 203 ? -0.761  6.069   22.668  1.00 9.96   ? 204 LEU A C   1 
ATOM   1659 O  O   . LEU A 1 203 ? -1.730  5.335   22.378  1.00 9.70   ? 204 LEU A O   1 
ATOM   1660 C  CB  . LEU A 1 203 ? -0.178  7.710   20.880  1.00 12.08  ? 204 LEU A CB  1 
ATOM   1661 C  CG  . LEU A 1 203 ? 0.902   8.264   19.963  1.00 13.38  ? 204 LEU A CG  1 
ATOM   1662 C  CD1 . LEU A 1 203 ? 0.253   9.303   19.020  1.00 15.16  ? 204 LEU A CD1 1 
ATOM   1663 C  CD2 . LEU A 1 203 ? 2.046   8.907   20.800  1.00 18.42  ? 204 LEU A CD2 1 
ATOM   1664 N  N   . GLU A 1 204 ? -0.587  6.506   23.923  1.00 10.11  ? 205 GLU A N   1 
ATOM   1665 C  CA  . GLU A 1 204 ? -1.379  6.165   25.046  1.00 10.19  ? 205 GLU A CA  1 
ATOM   1666 C  C   . GLU A 1 204 ? -2.564  7.130   25.165  1.00 9.92   ? 205 GLU A C   1 
ATOM   1667 O  O   . GLU A 1 204 ? -2.671  7.905   26.110  1.00 12.69  ? 205 GLU A O   1 
ATOM   1668 C  CB  . GLU A 1 204 ? -0.546  6.016   26.311  1.00 11.63  ? 205 GLU A CB  1 
ATOM   1669 C  CG  . GLU A 1 204 ? 0.365   4.804   26.166  1.00 11.60  ? 205 GLU A CG  1 
ATOM   1670 C  CD  . GLU A 1 204 ? 1.287   4.514   27.324  1.00 12.23  ? 205 GLU A CD  1 
ATOM   1671 O  OE1 . GLU A 1 204 ? 1.630   5.439   28.087  1.00 14.73  ? 205 GLU A OE1 1 
ATOM   1672 O  OE2 . GLU A 1 204 ? 1.707   3.319   27.498  1.00 12.19  ? 205 GLU A OE2 1 
ATOM   1673 N  N   . CYS A 1 205 ? -3.475  7.021   24.228  1.00 9.27   ? 206 CYS A N   1 
ATOM   1674 C  CA  . CYS A 1 205 ? -4.521  8.026   23.999  1.00 9.56   ? 206 CYS A CA  1 
ATOM   1675 C  C   . CYS A 1 205 ? -5.853  7.402   23.888  1.00 8.99   ? 206 CYS A C   1 
ATOM   1676 O  O   . CYS A 1 205 ? -6.827  8.097   23.537  1.00 10.49  ? 206 CYS A O   1 
ATOM   1677 C  CB  . CYS A 1 205 ? -4.221  8.866   22.757  1.00 9.91   ? 206 CYS A CB  1 
ATOM   1678 S  SG  . CYS A 1 205 ? -4.196  7.839   21.229  1.00 11.12  ? 206 CYS A SG  1 
ATOM   1679 N  N   . VAL A 1 206 ? -6.029  6.112   24.203  1.00 8.84   ? 207 VAL A N   1 
ATOM   1680 C  CA  . VAL A 1 206 ? -7.283  5.400   23.866  1.00 8.29   ? 207 VAL A CA  1 
ATOM   1681 C  C   . VAL A 1 206 ? -8.056  4.942   25.098  1.00 8.24   ? 207 VAL A C   1 
ATOM   1682 O  O   . VAL A 1 206 ? -7.477  4.291   25.975  1.00 10.01  ? 207 VAL A O   1 
ATOM   1683 C  CB  . VAL A 1 206 ? -6.987  4.135   23.013  1.00 8.50   ? 207 VAL A CB  1 
ATOM   1684 C  CG1 . VAL A 1 206 ? -8.269  3.408   22.663  1.00 8.90   ? 207 VAL A CG1 1 
ATOM   1685 C  CG2 . VAL A 1 206 ? -6.243  4.480   21.748  1.00 10.02  ? 207 VAL A CG2 1 
ATOM   1686 N  N   . THR A 1 207 ? -9.352  5.269   25.157  1.00 8.30   ? 208 THR A N   1 
ATOM   1687 C  CA  . THR A 1 207 ? -10.284 4.531   25.982  1.00 8.96   ? 208 THR A CA  1 
ATOM   1688 C  C   . THR A 1 207 ? -10.814 3.341   25.161  1.00 8.33   ? 208 THR A C   1 
ATOM   1689 O  O   . THR A 1 207 ? -11.491 3.558   24.137  1.00 8.50   ? 208 THR A O   1 
ATOM   1690 C  CB  . THR A 1 207 ? -11.476 5.388   26.446  1.00 8.96   ? 208 THR A CB  1 
ATOM   1691 O  OG1 . THR A 1 207 ? -10.938 6.531   27.174  1.00 10.35  ? 208 THR A OG1 1 
ATOM   1692 C  CG2 . THR A 1 207 ? -12.379 4.601   27.334  1.00 10.40  ? 208 THR A CG2 1 
ATOM   1693 N  N   . TRP A 1 208 ? -10.420 2.148   25.564  1.00 7.80   ? 209 TRP A N   1 
ATOM   1694 C  CA  . TRP A 1 208 ? -10.878 0.938   24.877  1.00 7.75   ? 209 TRP A CA  1 
ATOM   1695 C  C   . TRP A 1 208 ? -12.242 0.530   25.394  1.00 7.11   ? 209 TRP A C   1 
ATOM   1696 O  O   . TRP A 1 208 ? -12.476 0.486   26.596  1.00 8.14   ? 209 TRP A O   1 
ATOM   1697 C  CB  . TRP A 1 208 ? -9.842  -0.203  25.092  1.00 7.97   ? 209 TRP A CB  1 
ATOM   1698 C  CG  . TRP A 1 208 ? -8.766  -0.113  24.107  1.00 7.49   ? 209 TRP A CG  1 
ATOM   1699 C  CD1 . TRP A 1 208 ? -7.491  0.480   24.277  1.00 7.89   ? 209 TRP A CD1 1 
ATOM   1700 C  CD2 . TRP A 1 208 ? -8.829  -0.478  22.746  1.00 7.61   ? 209 TRP A CD2 1 
ATOM   1701 N  NE1 . TRP A 1 208 ? -6.814  0.484   23.123  1.00 7.96   ? 209 TRP A NE1 1 
ATOM   1702 C  CE2 . TRP A 1 208 ? -7.568  -0.123  22.126  1.00 8.10   ? 209 TRP A CE2 1 
ATOM   1703 C  CE3 . TRP A 1 208 ? -9.801  -1.138  21.968  1.00 7.65   ? 209 TRP A CE3 1 
ATOM   1704 C  CZ2 . TRP A 1 208 ? -7.282  -0.330  20.794  1.00 8.31   ? 209 TRP A CZ2 1 
ATOM   1705 C  CZ3 . TRP A 1 208 ? -9.507  -1.382  20.659  1.00 9.09   ? 209 TRP A CZ3 1 
ATOM   1706 C  CH2 . TRP A 1 208 ? -8.278  -0.998  20.073  1.00 8.96   ? 209 TRP A CH2 1 
ATOM   1707 N  N   . ILE A 1 209 ? -13.120 0.178   24.454  1.00 7.92   ? 210 ILE A N   1 
ATOM   1708 C  CA  . ILE A 1 209 ? -14.455 -0.343  24.777  1.00 8.15   ? 210 ILE A CA  1 
ATOM   1709 C  C   . ILE A 1 209 ? -14.582 -1.599  23.927  1.00 7.57   ? 210 ILE A C   1 
ATOM   1710 O  O   . ILE A 1 209 ? -14.612 -1.531  22.698  1.00 9.21   ? 210 ILE A O   1 
ATOM   1711 C  CB  . ILE A 1 209 ? -15.535 0.667   24.414  1.00 8.91   ? 210 ILE A CB  1 
ATOM   1712 C  CG1 . ILE A 1 209 ? -15.314 1.965   25.235  1.00 10.57  ? 210 ILE A CG1 1 
ATOM   1713 C  CG2 . ILE A 1 209 ? -16.921 0.079   24.630  1.00 10.26  ? 210 ILE A CG2 1 
ATOM   1714 C  CD1 . ILE A 1 209 ? -16.162 3.110   24.734  1.00 12.21  ? 210 ILE A CD1 1 
ATOM   1715 N  N   . VAL A 1 210 ? -14.522 -2.766  24.565  1.00 8.07   ? 211 VAL A N   1 
ATOM   1716 C  CA  . VAL A 1 210 ? -14.471 -4.076  23.865  1.00 8.05   ? 211 VAL A CA  1 
ATOM   1717 C  C   . VAL A 1 210 ? -15.796 -4.758  24.112  1.00 7.71   ? 211 VAL A C   1 
ATOM   1718 O  O   . VAL A 1 210 ? -16.164 -5.020  25.264  1.00 8.97   ? 211 VAL A O   1 
ATOM   1719 C  CB  . VAL A 1 210 ? -13.288 -4.894  24.310  1.00 8.79   ? 211 VAL A CB  1 
ATOM   1720 C  CG1 . VAL A 1 210 ? -13.282 -6.259  23.575  1.00 10.15  ? 211 VAL A CG1 1 
ATOM   1721 C  CG2 . VAL A 1 210 ? -11.979 -4.133  24.044  1.00 9.74   ? 211 VAL A CG2 1 
ATOM   1722 N  N   . LEU A 1 211 ? -16.568 -5.015  23.059  1.00 8.91   ? 212 LEU A N   1 
ATOM   1723 C  CA  . LEU A 1 211 ? -17.869 -5.683  23.228  1.00 9.44   ? 212 LEU A CA  1 
ATOM   1724 C  C   . LEU A 1 211 ? -17.697 -7.150  23.597  1.00 9.60   ? 212 LEU A C   1 
ATOM   1725 O  O   . LEU A 1 211 ? -16.824 -7.857  23.082  1.00 9.84   ? 212 LEU A O   1 
ATOM   1726 C  CB  . LEU A 1 211 ? -18.662 -5.584  21.937  1.00 10.69  ? 212 LEU A CB  1 
ATOM   1727 C  CG  . LEU A 1 211 ? -19.057 -4.161  21.538  1.00 10.77  ? 212 LEU A CG  1 
ATOM   1728 C  CD1 . LEU A 1 211 ? -20.033 -4.242  20.333  1.00 12.94  ? 212 LEU A CD1 1 
ATOM   1729 C  CD2 . LEU A 1 211 ? -19.574 -3.316  22.647  1.00 12.28  ? 212 LEU A CD2 1 
ATOM   1730 N  N   . LYS A 1 212 ? -18.540 -7.596  24.505  1.00 10.49  ? 213 LYS A N   1 
ATOM   1731 C  CA  . LYS A 1 212 ? -18.479 -9.029  24.888  1.00 10.77  ? 213 LYS A CA  1 
ATOM   1732 C  C   . LYS A 1 212 ? -18.977 -9.969  23.794  1.00 9.76   ? 213 LYS A C   1 
ATOM   1733 O  O   . LYS A 1 212 ? -18.435 -11.055 23.665  1.00 12.48  ? 213 LYS A O   1 
ATOM   1734 C  CB  . LYS A 1 212 ? -19.262 -9.195  26.141  1.00 13.61  ? 213 LYS A CB  1 
ATOM   1735 C  CG  . LYS A 1 212 ? -19.389 -10.682 26.596  1.00 18.78  ? 213 LYS A CG  1 
ATOM   1736 C  CD  . LYS A 1 212 ? -20.235 -10.853 27.864  1.00 26.18  ? 213 LYS A CD  1 
ATOM   1737 C  CE  . LYS A 1 212 ? -20.424 -12.280 28.307  1.00 35.13  ? 213 LYS A CE  1 
ATOM   1738 N  NZ  . LYS A 1 212 ? -21.520 -12.435 29.347  1.00 41.29  ? 213 LYS A NZ  1 
ATOM   1739 N  N   . GLU A 1 213 ? -19.987 -9.567  23.050  1.00 9.47   ? 214 GLU A N   1 
ATOM   1740 C  CA  . GLU A 1 213 ? -20.582 -10.478 22.060  1.00 10.59  ? 214 GLU A CA  1 
ATOM   1741 C  C   . GLU A 1 213 ? -19.838 -10.360 20.738  1.00 9.82   ? 214 GLU A C   1 
ATOM   1742 O  O   . GLU A 1 213 ? -19.748 -9.265  20.161  1.00 10.48  ? 214 GLU A O   1 
ATOM   1743 C  CB  . GLU A 1 213 ? -22.040 -10.104 21.842  1.00 11.75  ? 214 GLU A CB  1 
ATOM   1744 C  CG  . GLU A 1 213 ? -22.687 -11.010 20.868  1.00 15.09  ? 214 GLU A CG  1 
ATOM   1745 C  CD  . GLU A 1 213 ? -24.139 -10.914 20.709  1.00 18.18  ? 214 GLU A CD  1 
ATOM   1746 O  OE1 . GLU A 1 213 ? -24.781 -9.973  21.203  1.00 17.22  ? 214 GLU A OE1 1 
ATOM   1747 O  OE2 . GLU A 1 213 ? -24.673 -11.945 20.113  1.00 26.00  ? 214 GLU A OE2 1 
ATOM   1748 N  N   A PRO A 1 214 ? -19.244 -11.452 20.257  0.50 9.60   ? 215 PRO A N   1 
ATOM   1749 N  N   B PRO A 1 214 ? -19.145 -11.444 20.260  0.50 9.87   ? 215 PRO A N   1 
ATOM   1750 C  CA  A PRO A 1 214 ? -18.634 -11.407 18.961  0.50 9.93   ? 215 PRO A CA  1 
ATOM   1751 C  CA  B PRO A 1 214 ? -18.536 -11.407 18.957  0.50 10.17  ? 215 PRO A CA  1 
ATOM   1752 C  C   A PRO A 1 214 ? -19.633 -11.362 17.836  0.50 10.69  ? 215 PRO A C   1 
ATOM   1753 C  C   B PRO A 1 214 ? -19.545 -11.367 17.837  0.50 10.85  ? 215 PRO A C   1 
ATOM   1754 O  O   A PRO A 1 214 ? -20.805 -11.787 18.027  0.50 12.63  ? 215 PRO A O   1 
ATOM   1755 O  O   B PRO A 1 214 ? -20.704 -11.788 18.028  0.50 12.90  ? 215 PRO A O   1 
ATOM   1756 C  CB  A PRO A 1 214 ? -17.866 -12.719 18.877  0.50 10.71  ? 215 PRO A CB  1 
ATOM   1757 C  CB  B PRO A 1 214 ? -17.766 -12.719 18.880  0.50 11.03  ? 215 PRO A CB  1 
ATOM   1758 C  CG  A PRO A 1 214 ? -18.670 -13.685 19.707  0.50 13.96  ? 215 PRO A CG  1 
ATOM   1759 C  CG  B PRO A 1 214 ? -17.484 -13.053 20.338  0.50 17.15  ? 215 PRO A CG  1 
ATOM   1760 C  CD  A PRO A 1 214 ? -19.282 -12.844 20.819  0.50 9.77   ? 215 PRO A CD  1 
ATOM   1761 C  CD  B PRO A 1 214 ? -18.682 -12.596 21.089  0.50 15.39  ? 215 PRO A CD  1 
ATOM   1762 N  N   . ILE A 1 215 ? -19.212 -10.927 16.664  1.00 10.14  ? 216 ILE A N   1 
ATOM   1763 C  CA  . ILE A 1 215 ? -19.990 -11.166 15.464  1.00 11.36  ? 216 ILE A CA  1 
ATOM   1764 C  C   . ILE A 1 215 ? -19.456 -12.402 14.772  1.00 10.01  ? 216 ILE A C   1 
ATOM   1765 O  O   . ILE A 1 215 ? -18.306 -12.773 14.926  1.00 11.70  ? 216 ILE A O   1 
ATOM   1766 C  CB  . ILE A 1 215 ? -19.994 -9.950  14.512  1.00 11.58  ? 216 ILE A CB  1 
ATOM   1767 C  CG1 . ILE A 1 215 ? -18.579 -9.612  14.046  1.00 12.23  ? 216 ILE A CG1 1 
ATOM   1768 C  CG2 . ILE A 1 215 ? -20.673 -8.736  15.190  1.00 13.80  ? 216 ILE A CG2 1 
ATOM   1769 C  CD1 . ILE A 1 215 ? -18.583 -8.615  12.847  1.00 14.57  ? 216 ILE A CD1 1 
ATOM   1770 N  N   . SER A 1 216 ? -20.336 -13.037 14.014  1.00 11.66  ? 217 SER A N   1 
ATOM   1771 C  CA  . SER A 1 216 ? -19.945 -14.185 13.176  1.00 12.00  ? 217 SER A CA  1 
ATOM   1772 C  C   . SER A 1 216 ? -19.738 -13.755 11.773  1.00 10.86  ? 217 SER A C   1 
ATOM   1773 O  O   . SER A 1 216 ? -20.612 -12.991 11.221  1.00 13.12  ? 217 SER A O   1 
ATOM   1774 C  CB  . SER A 1 216 ? -21.108 -15.238 13.190  1.00 16.23  ? 217 SER A CB  1 
ATOM   1775 O  OG  . SER A 1 216 ? -21.120 -15.880 14.394  1.00 20.81  ? 217 SER A OG  1 
ATOM   1776 N  N   . VAL A 1 217 ? -18.651 -14.199 11.157  1.00 11.17  ? 218 VAL A N   1 
ATOM   1777 C  CA  . VAL A 1 217 ? -18.388 -14.000 9.753   1.00 11.73  ? 218 VAL A CA  1 
ATOM   1778 C  C   . VAL A 1 217 ? -18.165 -15.366 9.136   1.00 11.85  ? 218 VAL A C   1 
ATOM   1779 O  O   . VAL A 1 217 ? -17.765 -16.314 9.860   1.00 12.56  ? 218 VAL A O   1 
ATOM   1780 C  CB  . VAL A 1 217 ? -17.157 -13.075 9.525   1.00 12.49  ? 218 VAL A CB  1 
ATOM   1781 C  CG1 . VAL A 1 217 ? -17.379 -11.758 10.219  1.00 12.98  ? 218 VAL A CG1 1 
ATOM   1782 C  CG2 . VAL A 1 217 ? -15.898 -13.716 10.070  1.00 14.35  ? 218 VAL A CG2 1 
ATOM   1783 N  N   . SER A 1 218 ? -18.271 -15.489 7.836   1.00 12.01  ? 219 SER A N   1 
ATOM   1784 C  CA  . SER A 1 218 ? -18.052 -16.837 7.297   1.00 12.24  ? 219 SER A CA  1 
ATOM   1785 C  C   . SER A 1 218 ? -16.587 -17.086 7.006   1.00 12.28  ? 219 SER A C   1 
ATOM   1786 O  O   . SER A 1 218 ? -15.785 -16.175 6.865   1.00 12.76  ? 219 SER A O   1 
ATOM   1787 C  CB  . SER A 1 218 ? -18.859 -17.011 6.025   1.00 13.51  ? 219 SER A CB  1 
ATOM   1788 O  OG  . SER A 1 218 ? -18.391 -16.139 5.006   1.00 14.96  ? 219 SER A OG  1 
ATOM   1789 N  N   A SER A 1 219 ? -16.273 -18.363 6.837   0.50 12.61  ? 220 SER A N   1 
ATOM   1790 N  N   B SER A 1 219 ? -16.241 -18.346 6.827   0.50 12.94  ? 220 SER A N   1 
ATOM   1791 C  CA  A SER A 1 219 ? -14.931 -18.771 6.476   0.50 13.80  ? 220 SER A CA  1 
ATOM   1792 C  CA  B SER A 1 219 ? -14.876 -18.693 6.488   0.50 14.19  ? 220 SER A CA  1 
ATOM   1793 C  C   A SER A 1 219 ? -14.542 -18.058 5.189   0.50 14.46  ? 220 SER A C   1 
ATOM   1794 C  C   B SER A 1 219 ? -14.505 -18.065 5.144   0.50 14.73  ? 220 SER A C   1 
ATOM   1795 O  O   A SER A 1 219 ? -13.436 -17.560 5.062   0.50 15.48  ? 220 SER A O   1 
ATOM   1796 O  O   B SER A 1 219 ? -13.375 -17.631 4.919   0.50 16.35  ? 220 SER A O   1 
ATOM   1797 C  CB  A SER A 1 219 ? -14.846 -20.305 6.380   0.50 17.72  ? 220 SER A CB  1 
ATOM   1798 C  CB  B SER A 1 219 ? -14.773 -20.201 6.482   0.50 16.76  ? 220 SER A CB  1 
ATOM   1799 O  OG  A SER A 1 219 ? -15.789 -20.837 5.471   0.50 15.34  ? 220 SER A OG  1 
ATOM   1800 O  OG  B SER A 1 219 ? -13.473 -20.629 6.177   0.50 19.16  ? 220 SER A OG  1 
ATOM   1801 N  N   . GLU A 1 220 ? -15.475 -17.939 4.239   1.00 14.09  ? 221 GLU A N   1 
ATOM   1802 C  CA  . GLU A 1 220 ? -15.169 -17.313 2.947   1.00 15.49  ? 221 GLU A CA  1 
ATOM   1803 C  C   . GLU A 1 220 ? -14.875 -15.809 3.075   1.00 15.06  ? 221 GLU A C   1 
ATOM   1804 O  O   . GLU A 1 220 ? -14.008 -15.279 2.391   1.00 15.32  ? 221 GLU A O   1 
ATOM   1805 C  CB  . GLU A 1 220 ? -16.345 -17.480 1.979   1.00 17.57  ? 221 GLU A CB  1 
ATOM   1806 C  CG  . GLU A 1 220 ? -16.454 -18.938 1.546   1.00 23.05  ? 221 GLU A CG  1 
ATOM   1807 C  CD  . GLU A 1 220 ? -17.441 -19.708 2.416   1.00 24.33  ? 221 GLU A CD  1 
ATOM   1808 O  OE1 . GLU A 1 220 ? -17.917 -19.270 3.489   1.00 21.68  ? 221 GLU A OE1 1 
ATOM   1809 O  OE2 . GLU A 1 220 ? -17.757 -20.806 2.027   1.00 66.74  ? 221 GLU A OE2 1 
ATOM   1810 N  N   . GLN A 1 221 ? -15.577 -15.160 4.004   1.00 13.50  ? 222 GLN A N   1 
ATOM   1811 C  CA  . GLN A 1 221 ? -15.314 -13.726 4.239   1.00 13.55  ? 222 GLN A CA  1 
ATOM   1812 C  C   . GLN A 1 221 ? -13.910 -13.537 4.802   1.00 12.30  ? 222 GLN A C   1 
ATOM   1813 O  O   . GLN A 1 221 ? -13.159 -12.688 4.292   1.00 13.25  ? 222 GLN A O   1 
ATOM   1814 C  CB  . GLN A 1 221 ? -16.385 -13.177 5.166   1.00 13.28  ? 222 GLN A CB  1 
ATOM   1815 C  CG  . GLN A 1 221 ? -17.719 -13.034 4.486   1.00 13.13  ? 222 GLN A CG  1 
ATOM   1816 C  CD  . GLN A 1 221 ? -18.834 -12.530 5.330   1.00 12.42  ? 222 GLN A CD  1 
ATOM   1817 O  OE1 . GLN A 1 221 ? -18.984 -12.869 6.509   1.00 12.24  ? 222 GLN A OE1 1 
ATOM   1818 N  NE2 . GLN A 1 221 ? -19.639 -11.635 4.752   1.00 13.35  ? 222 GLN A NE2 1 
ATOM   1819 N  N   . VAL A 1 222 ? -13.483 -14.307 5.812   1.00 12.77  ? 223 VAL A N   1 
ATOM   1820 C  CA  . VAL A 1 222 ? -12.137 -14.123 6.348   1.00 13.22  ? 223 VAL A CA  1 
ATOM   1821 C  C   . VAL A 1 222 ? -11.064 -14.563 5.340   1.00 13.46  ? 223 VAL A C   1 
ATOM   1822 O  O   . VAL A 1 222 ? -10.002 -13.971 5.297   1.00 14.61  ? 223 VAL A O   1 
ATOM   1823 C  CB  . VAL A 1 222 ? -11.967 -14.715 7.756   1.00 15.17  ? 223 VAL A CB  1 
ATOM   1824 C  CG1 . VAL A 1 222 ? -12.052 -16.174 7.749   1.00 16.59  ? 223 VAL A CG1 1 
ATOM   1825 C  CG2 . VAL A 1 222 ? -10.757 -14.180 8.460   1.00 17.23  ? 223 VAL A CG2 1 
ATOM   1826 N  N   . LEU A 1 223 ? -11.362 -15.572 4.549   1.00 13.94  ? 224 LEU A N   1 
ATOM   1827 C  CA  . LEU A 1 223 ? -10.444 -15.981 3.516   1.00 16.26  ? 224 LEU A CA  1 
ATOM   1828 C  C   . LEU A 1 223 ? -10.120 -14.827 2.595   1.00 15.89  ? 224 LEU A C   1 
ATOM   1829 O  O   . LEU A 1 223 ? -9.003  -14.698 2.163   1.00 16.42  ? 224 LEU A O   1 
ATOM   1830 C  CB  . LEU A 1 223 ? -10.996 -17.190 2.801   1.00 19.88  ? 224 LEU A CB  1 
ATOM   1831 C  CG  . LEU A 1 223 ? -10.689 -18.477 3.603   1.00 25.69  ? 224 LEU A CG  1 
ATOM   1832 C  CD1 . LEU A 1 223 ? -11.656 -19.587 3.104   1.00 29.82  ? 224 LEU A CD1 1 
ATOM   1833 C  CD2 . LEU A 1 223 ? -9.195  -18.904 3.563   1.00 29.03  ? 224 LEU A CD2 1 
ATOM   1834 N  N   . LYS A 1 224 ? -11.134 -14.019 2.270   1.00 14.24  ? 225 LYS A N   1 
ATOM   1835 C  CA  . LYS A 1 224 ? -10.846 -12.869 1.398   1.00 15.39  ? 225 LYS A CA  1 
ATOM   1836 C  C   . LYS A 1 224 ? -9.981  -11.810 2.080   1.00 13.23  ? 225 LYS A C   1 
ATOM   1837 O  O   . LYS A 1 224 ? -9.201  -11.198 1.430   1.00 14.44  ? 225 LYS A O   1 
ATOM   1838 C  CB  . LYS A 1 224 ? -12.141 -12.344 0.827   1.00 17.57  ? 225 LYS A CB  1 
ATOM   1839 C  CG  . LYS A 1 224 ? -12.709 -13.427 -0.178  1.00 24.01  ? 225 LYS A CG  1 
ATOM   1840 C  CD  . LYS A 1 224 ? -14.007 -13.141 -0.875  1.00 26.65  ? 225 LYS A CD  1 
ATOM   1841 C  CE  . LYS A 1 224 ? -14.392 -14.302 -1.765  1.00 37.68  ? 225 LYS A CE  1 
ATOM   1842 N  NZ  . LYS A 1 224 ? -15.740 -14.069 -2.406  1.00 37.67  ? 225 LYS A NZ  1 
ATOM   1843 N  N   . PHE A 1 225 ? -10.073 -11.632 3.405   1.00 13.00  ? 226 PHE A N   1 
ATOM   1844 C  CA  . PHE A 1 225 ? -9.156  -10.732 4.079   1.00 12.23  ? 226 PHE A CA  1 
ATOM   1845 C  C   . PHE A 1 225 ? -7.688  -11.233 3.847   1.00 12.43  ? 226 PHE A C   1 
ATOM   1846 O  O   . PHE A 1 225 ? -6.755  -10.463 3.644   1.00 13.78  ? 226 PHE A O   1 
ATOM   1847 C  CB  . PHE A 1 225 ? -9.324  -10.723 5.587   1.00 13.08  ? 226 PHE A CB  1 
ATOM   1848 C  CG  . PHE A 1 225 ? -10.539 -9.980  6.132   1.00 12.91  ? 226 PHE A CG  1 
ATOM   1849 C  CD1 . PHE A 1 225 ? -11.596 -9.520  5.339   1.00 16.47  ? 226 PHE A CD1 1 
ATOM   1850 C  CD2 . PHE A 1 225 ? -10.623 -9.759  7.501   1.00 15.55  ? 226 PHE A CD2 1 
ATOM   1851 C  CE1 . PHE A 1 225 ? -12.673 -8.863  5.921   1.00 18.14  ? 226 PHE A CE1 1 
ATOM   1852 C  CE2 . PHE A 1 225 ? -11.696 -9.101  8.084   1.00 16.89  ? 226 PHE A CE2 1 
ATOM   1853 C  CZ  . PHE A 1 225 ? -12.730 -8.654  7.290   1.00 15.87  ? 226 PHE A CZ  1 
ATOM   1854 N  N   . ARG A 1 226 ? -7.522  -12.574 3.895   1.00 12.48  ? 227 ARG A N   1 
ATOM   1855 C  CA  . ARG A 1 226 ? -6.226  -13.157 3.877   1.00 12.69  ? 227 ARG A CA  1 
ATOM   1856 C  C   . ARG A 1 226 ? -5.627  -13.161 2.452   1.00 14.46  ? 227 ARG A C   1 
ATOM   1857 O  O   . ARG A 1 226 ? -4.464  -13.569 2.308   1.00 15.67  ? 227 ARG A O   1 
ATOM   1858 C  CB  . ARG A 1 226 ? -6.258  -14.621 4.408   1.00 13.27  ? 227 ARG A CB  1 
ATOM   1859 C  CG  . ARG A 1 226 ? -6.750  -14.729 5.828   1.00 12.66  ? 227 ARG A CG  1 
ATOM   1860 C  CD  . ARG A 1 226 ? -6.736  -16.168 6.293   1.00 14.52  ? 227 ARG A CD  1 
ATOM   1861 N  NE  . ARG A 1 226 ? -7.225  -16.328 7.609   1.00 13.20  ? 227 ARG A NE  1 
ATOM   1862 C  CZ  . ARG A 1 226 ? -8.137  -17.190 7.980   1.00 13.82  ? 227 ARG A CZ  1 
ATOM   1863 N  NH1 . ARG A 1 226 ? -8.589  -18.127 7.115   1.00 18.87  ? 227 ARG A NH1 1 
ATOM   1864 N  NH2 . ARG A 1 226 ? -8.617  -17.176 9.182   1.00 14.94  ? 227 ARG A NH2 1 
ATOM   1865 N  N   . LYS A 1 227 ? -6.379  -12.724 1.434   1.00 12.99  ? 228 LYS A N   1 
ATOM   1866 C  CA  . LYS A 1 227 ? -5.828  -12.611 0.064   1.00 14.82  ? 228 LYS A CA  1 
ATOM   1867 C  C   . LYS A 1 227 ? -5.212  -11.225 -0.183  1.00 13.57  ? 228 LYS A C   1 
ATOM   1868 O  O   . LYS A 1 227 ? -4.606  -11.001 -1.208  1.00 16.34  ? 228 LYS A O   1 
ATOM   1869 C  CB  . LYS A 1 227 ? -6.939  -12.828 -0.993  1.00 17.23  ? 228 LYS A CB  1 
ATOM   1870 C  CG  . LYS A 1 227 ? -7.472  -14.221 -1.002  1.00 20.09  ? 228 LYS A CG  1 
ATOM   1871 C  CD  . LYS A 1 227 ? -8.523  -14.259 -2.120  1.00 28.80  ? 228 LYS A CD  1 
ATOM   1872 N  N   . LEU A 1 228 ? -5.426  -10.271 0.752   1.00 14.18  ? 229 LEU A N   1 
ATOM   1873 C  CA  . LEU A 1 228 ? -4.815  -8.957  0.657   1.00 14.12  ? 229 LEU A CA  1 
ATOM   1874 C  C   . LEU A 1 228 ? -3.355  -9.128  0.777   1.00 14.26  ? 229 LEU A C   1 
ATOM   1875 O  O   . LEU A 1 228 ? -2.769  -10.180 1.207   1.00 13.91  ? 229 LEU A O   1 
ATOM   1876 C  CB  . LEU A 1 228 ? -5.368  -8.033  1.741   1.00 13.50  ? 229 LEU A CB  1 
ATOM   1877 C  CG  . LEU A 1 228 ? -6.803  -7.551  1.524   1.00 14.65  ? 229 LEU A CG  1 
ATOM   1878 C  CD1 . LEU A 1 228 ? -7.273  -6.957  2.807   1.00 15.14  ? 229 LEU A CD1 1 
ATOM   1879 C  CD2 . LEU A 1 228 ? -6.817  -6.542  0.377   1.00 16.62  ? 229 LEU A CD2 1 
ATOM   1880 N  N   . ASN A 1 229 ? -2.664  -8.069  0.427   1.00 14.84  ? 230 ASN A N   1 
ATOM   1881 C  CA  . ASN A 1 229 ? -1.232  -8.127  0.440   1.00 14.00  ? 230 ASN A CA  1 
ATOM   1882 C  C   . ASN A 1 229 ? -0.676  -6.920  1.265   1.00 14.63  ? 230 ASN A C   1 
ATOM   1883 O  O   . ASN A 1 229 ? -1.125  -5.812  1.232   1.00 15.59  ? 230 ASN A O   1 
ATOM   1884 C  CB  . ASN A 1 229 ? -0.565  -7.894  -0.975  1.00 15.87  ? 230 ASN A CB  1 
ATOM   1885 C  CG  . ASN A 1 229 ? -0.581  -9.086  -1.904  1.00 16.77  ? 230 ASN A CG  1 
ATOM   1886 O  OD1 . ASN A 1 229 ? -0.068  -8.956  -3.018  1.00 20.30  ? 230 ASN A OD1 1 
ATOM   1887 N  ND2 . ASN A 1 229 ? -1.239  -10.200 -1.540  1.00 16.60  ? 230 ASN A ND2 1 
ATOM   1888 N  N   . PHE A 1 230 ? 0.395   -7.243  2.005   1.00 14.33  ? 231 PHE A N   1 
ATOM   1889 C  CA  . PHE A 1 230 ? 1.139   -6.164  2.709   1.00 14.17  ? 231 PHE A CA  1 
ATOM   1890 C  C   . PHE A 1 230 ? 2.050   -5.381  1.750   1.00 15.59  ? 231 PHE A C   1 
ATOM   1891 O  O   . PHE A 1 230 ? 2.306   -4.200  2.019   1.00 17.67  ? 231 PHE A O   1 
ATOM   1892 C  CB  . PHE A 1 230 ? 2.145   -6.789  3.681   1.00 14.34  ? 231 PHE A CB  1 
ATOM   1893 C  CG  . PHE A 1 230 ? 1.578   -7.363  4.994   1.00 14.72  ? 231 PHE A CG  1 
ATOM   1894 C  CD1 . PHE A 1 230 ? 0.795   -6.609  5.895   1.00 14.38  ? 231 PHE A CD1 1 
ATOM   1895 C  CD2 . PHE A 1 230 ? 1.964   -8.657  5.375   1.00 13.75  ? 231 PHE A CD2 1 
ATOM   1896 C  CE1 . PHE A 1 230 ? 0.360   -7.117  7.097   1.00 15.06  ? 231 PHE A CE1 1 
ATOM   1897 C  CE2 . PHE A 1 230 ? 1.509   -9.171  6.590   1.00 14.69  ? 231 PHE A CE2 1 
ATOM   1898 C  CZ  . PHE A 1 230 ? 0.733   -8.421  7.447   1.00 13.88  ? 231 PHE A CZ  1 
ATOM   1899 N  N   . ASN A 1 231 ? 2.533   -6.017  0.704   1.00 15.57  ? 232 ASN A N   1 
ATOM   1900 C  CA  . ASN A 1 231 ? 3.396   -5.370  -0.310  1.00 17.20  ? 232 ASN A CA  1 
ATOM   1901 C  C   . ASN A 1 231 ? 2.586   -4.490  -1.218  1.00 15.12  ? 232 ASN A C   1 
ATOM   1902 O  O   . ASN A 1 231 ? 1.386   -4.570  -1.397  1.00 17.47  ? 232 ASN A O   1 
ATOM   1903 C  CB  . ASN A 1 231 ? 4.082   -6.472  -1.113  1.00 17.60  ? 232 ASN A CB  1 
ATOM   1904 C  CG  . ASN A 1 231 ? 3.073   -7.393  -1.698  1.00 17.04  ? 232 ASN A CG  1 
ATOM   1905 O  OD1 . ASN A 1 231 ? 2.533   -8.272  -1.009  1.00 19.96  ? 232 ASN A OD1 1 
ATOM   1906 N  ND2 . ASN A 1 231 ? 2.817   -7.237  -2.980  1.00 21.54  ? 232 ASN A ND2 1 
ATOM   1907 N  N   . GLY A 1 232 ? 3.375   -3.578  -1.900  1.00 17.98  ? 233 GLY A N   1 
ATOM   1908 C  CA  . GLY A 1 232 ? 2.807   -2.772  -2.991  1.00 18.83  ? 233 GLY A CA  1 
ATOM   1909 C  C   . GLY A 1 232 ? 2.806   -3.558  -4.280  1.00 16.08  ? 233 GLY A C   1 
ATOM   1910 O  O   . GLY A 1 232 ? 3.544   -4.557  -4.350  1.00 19.88  ? 233 GLY A O   1 
ATOM   1911 N  N   . GLU A 1 233 ? 2.048   -3.065  -5.268  1.00 18.33  ? 234 GLU A N   1 
ATOM   1912 C  CA  . GLU A 1 233 ? 1.993   -3.623  -6.605  1.00 17.14  ? 234 GLU A CA  1 
ATOM   1913 C  C   . GLU A 1 233 ? 3.434   -3.754  -7.157  1.00 19.47  ? 234 GLU A C   1 
ATOM   1914 O  O   . GLU A 1 233 ? 4.258   -2.881  -7.005  1.00 23.10  ? 234 GLU A O   1 
ATOM   1915 C  CB  . GLU A 1 233 ? 1.110   -2.823  -7.488  1.00 18.24  ? 234 GLU A CB  1 
ATOM   1916 C  CG  . GLU A 1 233 ? 0.855   -3.368  -8.864  1.00 21.75  ? 234 GLU A CG  1 
ATOM   1917 C  CD  . GLU A 1 233 ? 0.025   -2.440  -9.730  1.00 30.73  ? 234 GLU A CD  1 
ATOM   1918 O  OE1 . GLU A 1 233 ? -0.317  -1.335  -9.262  1.00 26.41  ? 234 GLU A OE1 1 
ATOM   1919 O  OE2 . GLU A 1 233 ? -0.288  -2.822  -10.880 1.00 30.13  ? 234 GLU A OE2 1 
ATOM   1920 N  N   . GLY A 1 234 ? 3.677   -4.906  -7.802  1.00 23.62  ? 235 GLY A N   1 
ATOM   1921 C  CA  . GLY A 1 234 ? 4.952   -5.175  -8.432  1.00 26.31  ? 235 GLY A CA  1 
ATOM   1922 C  C   . GLY A 1 234 ? 6.089   -5.540  -7.481  1.00 25.30  ? 235 GLY A C   1 
ATOM   1923 O  O   . GLY A 1 234 ? 7.288   -5.622  -7.858  1.00 33.71  ? 235 GLY A O   1 
ATOM   1924 N  N   . GLU A 1 235 ? 5.699   -5.804  -6.221  1.00 23.46  ? 236 GLU A N   1 
ATOM   1925 C  CA  . GLU A 1 235 ? 6.692   -6.334  -5.322  1.00 21.63  ? 236 GLU A CA  1 
ATOM   1926 C  C   . GLU A 1 235 ? 6.325   -7.764  -4.951  1.00 27.64  ? 236 GLU A C   1 
ATOM   1927 O  O   . GLU A 1 235 ? 5.188   -8.206  -5.188  1.00 27.26  ? 236 GLU A O   1 
ATOM   1928 C  CB  . GLU A 1 235 ? 6.656   -5.559  -3.971  1.00 23.87  ? 236 GLU A CB  1 
ATOM   1929 C  CG  . GLU A 1 235 ? 7.035   -4.085  -4.140  1.00 27.96  ? 236 GLU A CG  1 
ATOM   1930 C  CD  . GLU A 1 235 ? 6.960   -3.289  -2.860  1.00 36.59  ? 236 GLU A CD  1 
ATOM   1931 O  OE1 . GLU A 1 235 ? 6.160   -3.692  -1.951  1.00 32.98  ? 236 GLU A OE1 1 
ATOM   1932 O  OE2 . GLU A 1 235 ? 7.695   -2.266  -2.778  1.00 52.32  ? 236 GLU A OE2 1 
ATOM   1933 N  N   . PRO A 1 236 ? 7.267   -8.496  -4.319  1.00 26.70  ? 237 PRO A N   1 
ATOM   1934 C  CA  . PRO A 1 236 ? 7.052   -9.910  -4.010  1.00 30.93  ? 237 PRO A CA  1 
ATOM   1935 C  C   . PRO A 1 236 ? 5.838   -10.038 -3.089  1.00 23.38  ? 237 PRO A C   1 
ATOM   1936 O  O   . PRO A 1 236 ? 5.688   -9.285  -2.156  1.00 22.98  ? 237 PRO A O   1 
ATOM   1937 C  CB  . PRO A 1 236 ? 8.350   -10.317 -3.288  1.00 36.68  ? 237 PRO A CB  1 
ATOM   1938 C  CG  . PRO A 1 236 ? 9.392   -9.331  -3.784  1.00 31.87  ? 237 PRO A CG  1 
ATOM   1939 C  CD  . PRO A 1 236 ? 8.663   -8.049  -4.008  1.00 30.06  ? 237 PRO A CD  1 
ATOM   1940 N  N   . GLU A 1 237 ? 4.983   -11.030 -3.319  1.00 24.82  ? 238 GLU A N   1 
ATOM   1941 C  CA  . GLU A 1 237 ? 3.738   -11.114 -2.610  1.00 22.10  ? 238 GLU A CA  1 
ATOM   1942 C  C   . GLU A 1 237 ? 3.913   -11.557 -1.167  1.00 20.49  ? 238 GLU A C   1 
ATOM   1943 O  O   . GLU A 1 237 ? 4.500   -12.590 -0.926  1.00 18.08  ? 238 GLU A O   1 
ATOM   1944 C  CB  . GLU A 1 237 ? 2.802   -12.140 -3.270  1.00 25.29  ? 238 GLU A CB  1 
ATOM   1945 C  CG  . GLU A 1 237 ? 1.452   -12.164 -2.559  1.00 26.45  ? 238 GLU A CG  1 
ATOM   1946 C  CD  . GLU A 1 237 ? 0.344   -12.928 -3.273  1.00 23.07  ? 238 GLU A CD  1 
ATOM   1947 O  OE1 . GLU A 1 237 ? 0.671   -14.006 -3.873  1.00 40.17  ? 238 GLU A OE1 1 
ATOM   1948 O  OE2 . GLU A 1 237 ? -0.846  -12.448 -3.307  1.00 22.33  ? 238 GLU A OE2 1 
ATOM   1949 N  N   . GLU A 1 238 ? 3.372   -10.814 -0.213  1.00 16.91  ? 239 GLU A N   1 
ATOM   1950 C  CA  . GLU A 1 238 ? 3.363   -11.138 1.206   1.00 16.60  ? 239 GLU A CA  1 
ATOM   1951 C  C   . GLU A 1 238 ? 1.953   -10.993 1.648   1.00 13.99  ? 239 GLU A C   1 
ATOM   1952 O  O   . GLU A 1 238 ? 1.438   -9.915  1.697   1.00 18.46  ? 239 GLU A O   1 
ATOM   1953 C  CB  . GLU A 1 238 ? 4.283   -10.237 1.946   1.00 21.96  ? 239 GLU A CB  1 
ATOM   1954 C  CG  . GLU A 1 238 ? 4.503   -10.643 3.403   1.00 44.10  ? 239 GLU A CG  1 
ATOM   1955 N  N   . LEU A 1 239 ? 1.315   -12.174 1.919   1.00 14.93  ? 240 LEU A N   1 
ATOM   1956 C  CA  . LEU A 1 239 ? -0.072  -12.110 2.259   1.00 13.01  ? 240 LEU A CA  1 
ATOM   1957 C  C   . LEU A 1 239 ? -0.268  -11.305 3.552   1.00 12.91  ? 240 LEU A C   1 
ATOM   1958 O  O   . LEU A 1 239 ? 0.483   -11.446 4.510   1.00 14.20  ? 240 LEU A O   1 
ATOM   1959 C  CB  . LEU A 1 239 ? -0.622  -13.526 2.482   1.00 14.50  ? 240 LEU A CB  1 
ATOM   1960 C  CG  . LEU A 1 239 ? -0.683  -14.411 1.233   1.00 15.45  ? 240 LEU A CG  1 
ATOM   1961 C  CD1 . LEU A 1 239 ? -1.262  -15.739 1.726   1.00 19.97  ? 240 LEU A CD1 1 
ATOM   1962 C  CD2 . LEU A 1 239 ? -1.475  -13.747 0.138   1.00 15.88  ? 240 LEU A CD2 1 
ATOM   1963 N  N   . MET A 1 240 ? -1.288  -10.483 3.547   1.00 13.30  ? 241 MET A N   1 
ATOM   1964 C  CA  . MET A 1 240 ? -1.669  -9.687  4.725   1.00 14.08  ? 241 MET A CA  1 
ATOM   1965 C  C   . MET A 1 240 ? -2.478  -10.618 5.656   1.00 12.03  ? 241 MET A C   1 
ATOM   1966 O  O   . MET A 1 240 ? -3.642  -10.786 5.567   1.00 12.51  ? 241 MET A O   1 
ATOM   1967 C  CB  . MET A 1 240 ? -2.557  -8.529  4.269   1.00 13.96  ? 241 MET A CB  1 
ATOM   1968 C  CG  . MET A 1 240 ? -2.848  -7.501  5.459   1.00 14.59  ? 241 MET A CG  1 
ATOM   1969 S  SD  . MET A 1 240 ? -3.844  -6.136  4.932   1.00 14.52  ? 241 MET A SD  1 
ATOM   1970 C  CE  . MET A 1 240 ? -2.527  -5.079  4.296   1.00 16.24  ? 241 MET A CE  1 
ATOM   1971 N  N   . VAL A 1 241 ? -1.675  -11.210 6.572   1.00 12.00  ? 242 VAL A N   1 
ATOM   1972 C  CA  . VAL A 1 241 ? -2.200  -12.118 7.624   1.00 11.00  ? 242 VAL A CA  1 
ATOM   1973 C  C   . VAL A 1 241 ? -1.421  -11.898 8.903   1.00 10.90  ? 242 VAL A C   1 
ATOM   1974 O  O   . VAL A 1 241 ? -0.257  -11.451 8.863   1.00 11.31  ? 242 VAL A O   1 
ATOM   1975 C  CB  . VAL A 1 241 ? -2.121  -13.627 7.232   1.00 11.81  ? 242 VAL A CB  1 
ATOM   1976 C  CG1 . VAL A 1 241 ? -3.040  -13.937 6.052   1.00 14.45  ? 242 VAL A CG1 1 
ATOM   1977 C  CG2 . VAL A 1 241 ? -0.718  -14.089 6.984   1.00 13.57  ? 242 VAL A CG2 1 
ATOM   1978 N  N   . ASP A 1 242 ? -2.028  -12.201 10.054  1.00 10.41  ? 243 ASP A N   1 
ATOM   1979 C  CA  . ASP A 1 242 ? -1.359  -12.070 11.332  1.00 10.48  ? 243 ASP A CA  1 
ATOM   1980 C  C   . ASP A 1 242 ? -0.876  -10.621 11.578  1.00 9.99   ? 243 ASP A C   1 
ATOM   1981 O  O   . ASP A 1 242 ? 0.224   -10.368 12.044  1.00 11.90  ? 243 ASP A O   1 
ATOM   1982 C  CB  . ASP A 1 242 ? -0.240  -13.113 11.557  1.00 11.67  ? 243 ASP A CB  1 
ATOM   1983 C  CG  . ASP A 1 242 ? -0.844  -14.527 11.656  1.00 11.33  ? 243 ASP A CG  1 
ATOM   1984 O  OD1 . ASP A 1 242 ? -1.887  -14.679 12.298  1.00 11.02  ? 243 ASP A OD1 1 
ATOM   1985 O  OD2 . ASP A 1 242 ? -0.221  -15.430 11.031  1.00 13.20  ? 243 ASP A OD2 1 
ATOM   1986 N  N   . ASN A 1 243 ? -1.781  -9.688  11.287  1.00 9.85   ? 244 ASN A N   1 
ATOM   1987 C  CA  . ASN A 1 243 ? -1.512  -8.223  11.518  1.00 10.09  ? 244 ASN A CA  1 
ATOM   1988 C  C   . ASN A 1 243 ? -2.049  -7.832  12.861  1.00 9.32   ? 244 ASN A C   1 
ATOM   1989 O  O   . ASN A 1 243 ? -2.716  -6.782  12.966  1.00 10.91  ? 244 ASN A O   1 
ATOM   1990 C  CB  . ASN A 1 243 ? -2.040  -7.409  10.328  1.00 10.98  ? 244 ASN A CB  1 
ATOM   1991 C  CG  . ASN A 1 243 ? -3.486  -7.582  10.125  1.00 10.93  ? 244 ASN A CG  1 
ATOM   1992 O  OD1 . ASN A 1 243 ? -4.171  -8.447  10.702  1.00 11.53  ? 244 ASN A OD1 1 
ATOM   1993 N  ND2 . ASN A 1 243 ? -4.021  -6.790  9.207   1.00 15.12  ? 244 ASN A ND2 1 
ATOM   1994 N  N   . TRP A 1 244 ? -1.778  -8.582  13.925  1.00 9.23   ? 245 TRP A N   1 
ATOM   1995 C  CA  . TRP A 1 244 ? -2.193  -8.340  15.290  1.00 8.74   ? 245 TRP A CA  1 
ATOM   1996 C  C   . TRP A 1 244 ? -0.973  -8.245  16.175  1.00 9.26   ? 245 TRP A C   1 
ATOM   1997 O  O   . TRP A 1 244 ? 0.022   -8.954  16.038  1.00 10.41  ? 245 TRP A O   1 
ATOM   1998 C  CB  . TRP A 1 244 ? -3.158  -9.452  15.786  1.00 9.57   ? 245 TRP A CB  1 
ATOM   1999 C  CG  . TRP A 1 244 ? -2.681  -10.854 15.609  1.00 9.46   ? 245 TRP A CG  1 
ATOM   2000 C  CD1 . TRP A 1 244 ? -2.794  -11.618 14.455  1.00 9.27   ? 245 TRP A CD1 1 
ATOM   2001 C  CD2 . TRP A 1 244 ? -2.084  -11.695 16.577  1.00 8.96   ? 245 TRP A CD2 1 
ATOM   2002 N  NE1 . TRP A 1 244 ? -2.267  -12.866 14.651  1.00 9.69   ? 245 TRP A NE1 1 
ATOM   2003 C  CE2 . TRP A 1 244 ? -1.855  -12.970 15.926  1.00 10.26  ? 245 TRP A CE2 1 
ATOM   2004 C  CE3 . TRP A 1 244 ? -1.820  -11.563 17.928  1.00 10.18  ? 245 TRP A CE3 1 
ATOM   2005 C  CZ2 . TRP A 1 244 ? -1.255  -14.037 16.610  1.00 11.38  ? 245 TRP A CZ2 1 
ATOM   2006 C  CZ3 . TRP A 1 244 ? -1.230  -12.645 18.598  1.00 12.09  ? 245 TRP A CZ3 1 
ATOM   2007 C  CH2 . TRP A 1 244 ? -0.973  -13.879 17.938  1.00 12.35  ? 245 TRP A CH2 1 
ATOM   2008 N  N   . ARG A 1 245 ? -1.091  -7.354  17.163  1.00 9.20   ? 246 ARG A N   1 
ATOM   2009 C  CA  . ARG A 1 245 ? -0.158  -7.269  18.282  1.00 9.42   ? 246 ARG A CA  1 
ATOM   2010 C  C   . ARG A 1 245 ? -0.615  -8.182  19.392  1.00 9.27   ? 246 ARG A C   1 
ATOM   2011 O  O   . ARG A 1 245 ? -1.810  -8.144  19.736  1.00 9.92   ? 246 ARG A O   1 
ATOM   2012 C  CB  . ARG A 1 245 ? -0.079  -5.793  18.753  1.00 9.54   ? 246 ARG A CB  1 
ATOM   2013 C  CG  . ARG A 1 245 ? 1.016   -5.573  19.749  1.00 9.68   ? 246 ARG A CG  1 
ATOM   2014 C  CD  . ARG A 1 245 ? 0.954   -4.193  20.398  1.00 9.72   ? 246 ARG A CD  1 
ATOM   2015 N  NE  . ARG A 1 245 ? 2.180   -3.883  21.102  1.00 10.45  ? 246 ARG A NE  1 
ATOM   2016 C  CZ  . ARG A 1 245 ? 2.383   -2.847  21.937  1.00 9.90   ? 246 ARG A CZ  1 
ATOM   2017 N  NH1 . ARG A 1 245 ? 1.380   -2.086  22.298  1.00 10.67  ? 246 ARG A NH1 1 
ATOM   2018 N  NH2 . ARG A 1 245 ? 3.631   -2.611  22.380  1.00 11.96  ? 246 ARG A NH2 1 
ATOM   2019 N  N   A PRO A 1 246 ? 0.288   -8.953  20.008  0.50 9.49   ? 247 PRO A N   1 
ATOM   2020 N  N   B PRO A 1 246 ? 0.292   -8.925  20.031  0.50 9.85   ? 247 PRO A N   1 
ATOM   2021 C  CA  A PRO A 1 246 ? -0.107  -9.758  21.146  0.50 10.24  ? 247 PRO A CA  1 
ATOM   2022 C  CA  B PRO A 1 246 ? -0.151  -9.764  21.134  0.50 10.97  ? 247 PRO A CA  1 
ATOM   2023 C  C   A PRO A 1 246 ? -0.496  -8.949  22.394  0.50 9.37   ? 247 PRO A C   1 
ATOM   2024 C  C   B PRO A 1 246 ? -0.487  -8.960  22.388  0.50 9.64   ? 247 PRO A C   1 
ATOM   2025 O  O   A PRO A 1 246 ? -0.175  -7.753  22.527  0.50 9.96   ? 247 PRO A O   1 
ATOM   2026 O  O   B PRO A 1 246 ? -0.124  -7.774  22.510  0.50 10.51  ? 247 PRO A O   1 
ATOM   2027 C  CB  A PRO A 1 246 ? 1.121   -10.634 21.415  0.50 12.34  ? 247 PRO A CB  1 
ATOM   2028 C  CB  B PRO A 1 246 ? 1.029   -10.688 21.384  0.50 13.46  ? 247 PRO A CB  1 
ATOM   2029 C  CG  A PRO A 1 246 ? 1.894   -10.640 20.128  0.50 10.68  ? 247 PRO A CG  1 
ATOM   2030 C  CG  B PRO A 1 246 ? 2.186   -9.899  20.940  0.50 15.30  ? 247 PRO A CG  1 
ATOM   2031 C  CD  A PRO A 1 246 ? 1.642   -9.297  19.519  0.50 9.37   ? 247 PRO A CD  1 
ATOM   2032 C  CD  B PRO A 1 246 ? 1.757   -8.936  19.867  0.50 12.16  ? 247 PRO A CD  1 
ATOM   2033 N  N   . ALA A 1 247 ? -1.139  -9.614  23.342  1.00 10.56  ? 248 ALA A N   1 
ATOM   2034 C  CA  . ALA A 1 247 ? -1.493  -8.987  24.610  1.00 10.10  ? 248 ALA A CA  1 
ATOM   2035 C  C   . ALA A 1 247 ? -0.257  -8.471  25.318  1.00 10.03  ? 248 ALA A C   1 
ATOM   2036 O  O   . ALA A 1 247 ? 0.791   -9.120  25.374  1.00 11.61  ? 248 ALA A O   1 
ATOM   2037 C  CB  . ALA A 1 247 ? -2.240  -9.982  25.483  1.00 12.95  ? 248 ALA A CB  1 
ATOM   2038 N  N   . GLN A 1 248 ? -0.401  -7.255  25.932  1.00 9.89   ? 249 GLN A N   1 
ATOM   2039 C  CA  . GLN A 1 248 ? 0.668   -6.539  26.655  1.00 10.02  ? 249 GLN A CA  1 
ATOM   2040 C  C   . GLN A 1 248 ? 0.366   -6.568  28.099  1.00 10.14  ? 249 GLN A C   1 
ATOM   2041 O  O   . GLN A 1 248 ? -0.764  -6.768  28.560  1.00 11.33  ? 249 GLN A O   1 
ATOM   2042 C  CB  . GLN A 1 248 ? 0.677   -5.105  26.121  1.00 10.91  ? 249 GLN A CB  1 
ATOM   2043 C  CG  . GLN A 1 248 ? 0.993   -5.042  24.636  1.00 10.82  ? 249 GLN A CG  1 
ATOM   2044 C  CD  . GLN A 1 248 ? 2.336   -5.700  24.281  1.00 12.85  ? 249 GLN A CD  1 
ATOM   2045 O  OE1 . GLN A 1 248 ? 3.355   -5.334  24.858  1.00 15.15  ? 249 GLN A OE1 1 
ATOM   2046 N  NE2 . GLN A 1 248 ? 2.344   -6.628  23.305  1.00 13.05  ? 249 GLN A NE2 1 
ATOM   2047 N  N   . PRO A 1 249 ? 1.390   -6.270  28.951  1.00 12.87  ? 250 PRO A N   1 
ATOM   2048 C  CA  . PRO A 1 249 ? 1.172   -6.304  30.413  1.00 14.31  ? 250 PRO A CA  1 
ATOM   2049 C  C   . PRO A 1 249 ? 0.098   -5.312  30.838  1.00 12.28  ? 250 PRO A C   1 
ATOM   2050 O  O   . PRO A 1 249 ? 0.092   -4.133  30.509  1.00 12.15  ? 250 PRO A O   1 
ATOM   2051 C  CB  . PRO A 1 249 ? 2.591   -5.879  30.932  1.00 17.17  ? 250 PRO A CB  1 
ATOM   2052 C  CG  . PRO A 1 249 ? 3.524   -6.328  29.896  1.00 18.95  ? 250 PRO A CG  1 
ATOM   2053 C  CD  . PRO A 1 249 ? 2.789   -6.029  28.608  1.00 15.87  ? 250 PRO A CD  1 
ATOM   2054 N  N   . LEU A 1 250 ? -0.782  -5.798  31.742  1.00 12.99  ? 251 LEU A N   1 
ATOM   2055 C  CA  . LEU A 1 250 ? -1.820  -4.927  32.240  1.00 11.93  ? 251 LEU A CA  1 
ATOM   2056 C  C   . LEU A 1 250 ? -1.298  -3.843  33.168  1.00 11.53  ? 251 LEU A C   1 
ATOM   2057 O  O   . LEU A 1 250 ? -1.889  -2.755  33.226  1.00 12.30  ? 251 LEU A O   1 
ATOM   2058 C  CB  . LEU A 1 250 ? -2.878  -5.815  32.961  1.00 14.41  ? 251 LEU A CB  1 
ATOM   2059 C  CG  . LEU A 1 250 ? -4.130  -5.088  33.378  1.00 13.90  ? 251 LEU A CG  1 
ATOM   2060 C  CD1 . LEU A 1 250 ? -4.908  -4.529  32.169  1.00 15.11  ? 251 LEU A CD1 1 
ATOM   2061 C  CD2 . LEU A 1 250 ? -5.059  -6.061  34.143  1.00 17.52  ? 251 LEU A CD2 1 
ATOM   2062 N  N   . LYS A 1 251 ? -0.222  -4.113  33.894  1.00 13.85  ? 252 LYS A N   1 
ATOM   2063 C  CA  . LYS A 1 251 ? 0.430   -3.081  34.792  1.00 14.24  ? 252 LYS A CA  1 
ATOM   2064 C  C   . LYS A 1 251 ? -0.642  -2.521  35.727  1.00 15.36  ? 252 LYS A C   1 
ATOM   2065 O  O   . LYS A 1 251 ? -1.438  -3.343  36.268  1.00 17.42  ? 252 LYS A O   1 
ATOM   2066 C  CB  . LYS A 1 251 ? 1.184   -2.063  33.992  1.00 17.65  ? 252 LYS A CB  1 
ATOM   2067 C  CG  . LYS A 1 251 ? 2.295   -2.785  33.235  1.00 20.53  ? 252 LYS A CG  1 
ATOM   2068 C  CD  . LYS A 1 251 ? 3.228   -1.817  32.635  1.00 23.58  ? 252 LYS A CD  1 
ATOM   2069 C  CE  . LYS A 1 251 ? 4.529   -2.459  32.364  1.00 27.87  ? 252 LYS A CE  1 
ATOM   2070 N  NZ  . LYS A 1 251 ? 5.286   -1.616  31.372  1.00 32.41  ? 252 LYS A NZ  1 
ATOM   2071 N  N   . ASN A 1 252 ? -0.670  -1.249  35.977  1.00 15.04  ? 253 ASN A N   1 
ATOM   2072 C  CA  . ASN A 1 252 ? -1.507  -0.773  36.959  1.00 23.03  ? 253 ASN A CA  1 
ATOM   2073 C  C   . ASN A 1 252 ? -2.818  -0.370  36.392  1.00 24.15  ? 253 ASN A C   1 
ATOM   2074 O  O   . ASN A 1 252 ? -3.104  0.821   36.340  1.00 23.59  ? 253 ASN A O   1 
ATOM   2075 C  CB  . ASN A 1 252 ? -0.769  0.463   37.594  1.00 28.28  ? 253 ASN A CB  1 
ATOM   2076 C  CG  . ASN A 1 252 ? -1.437  0.971   38.848  1.00 31.49  ? 253 ASN A CG  1 
ATOM   2077 O  OD1 . ASN A 1 252 ? -1.631  0.234   39.805  1.00 55.86  ? 253 ASN A OD1 1 
ATOM   2078 N  ND2 . ASN A 1 252 ? -1.778  2.249   38.852  1.00 48.88  ? 253 ASN A ND2 1 
ATOM   2079 N  N   . ARG A 1 253 ? -3.648  -1.397  35.822  1.00 16.64  ? 254 ARG A N   1 
ATOM   2080 C  CA  . ARG A 1 253 ? -4.903  -1.034  35.254  1.00 12.05  ? 254 ARG A CA  1 
ATOM   2081 C  C   . ARG A 1 253 ? -6.007  -1.973  35.738  1.00 13.64  ? 254 ARG A C   1 
ATOM   2082 O  O   . ARG A 1 253 ? -5.791  -3.131  35.926  1.00 20.98  ? 254 ARG A O   1 
ATOM   2083 C  CB  . ARG A 1 253 ? -4.855  -1.003  33.772  1.00 11.58  ? 254 ARG A CB  1 
ATOM   2084 C  CG  . ARG A 1 253 ? -3.944  0.136   33.280  1.00 11.49  ? 254 ARG A CG  1 
ATOM   2085 C  CD  . ARG A 1 253 ? -3.827  0.162   31.767  1.00 10.99  ? 254 ARG A CD  1 
ATOM   2086 N  NE  . ARG A 1 253 ? -3.020  -1.012  31.333  1.00 9.71   ? 254 ARG A NE  1 
ATOM   2087 C  CZ  . ARG A 1 253 ? -2.753  -1.274  30.062  1.00 9.00   ? 254 ARG A CZ  1 
ATOM   2088 N  NH1 . ARG A 1 253 ? -3.365  -0.603  29.059  1.00 9.39   ? 254 ARG A NH1 1 
ATOM   2089 N  NH2 . ARG A 1 253 ? -1.922  -2.257  29.710  1.00 9.88   ? 254 ARG A NH2 1 
ATOM   2090 N  N   . GLN A 1 254 ? -7.199  -1.436  35.779  1.00 12.91  ? 255 GLN A N   1 
ATOM   2091 C  CA  . GLN A 1 254 ? -8.406  -2.210  36.063  1.00 14.59  ? 255 GLN A CA  1 
ATOM   2092 C  C   . GLN A 1 254 ? -9.264  -2.224  34.836  1.00 13.78  ? 255 GLN A C   1 
ATOM   2093 O  O   . GLN A 1 254 ? -9.526  -1.175  34.175  1.00 17.96  ? 255 GLN A O   1 
ATOM   2094 C  CB  . GLN A 1 254 ? -9.146  -1.614  37.241  1.00 19.69  ? 255 GLN A CB  1 
ATOM   2095 C  CG  . GLN A 1 254 ? -8.525  -2.015  38.543  1.00 27.77  ? 255 GLN A CG  1 
ATOM   2096 N  N   . ILE A 1 255 ? -9.759  -3.407  34.462  1.00 12.35  ? 256 ILE A N   1 
ATOM   2097 C  CA  . ILE A 1 255 ? -10.718 -3.557  33.387  1.00 11.62  ? 256 ILE A CA  1 
ATOM   2098 C  C   . ILE A 1 255 ? -12.093 -3.595  34.062  1.00 11.81  ? 256 ILE A C   1 
ATOM   2099 O  O   . ILE A 1 255 ? -12.294 -4.307  35.043  1.00 13.29  ? 256 ILE A O   1 
ATOM   2100 C  CB  . ILE A 1 255 ? -10.490 -4.826  32.595  1.00 11.97  ? 256 ILE A CB  1 
ATOM   2101 C  CG1 . ILE A 1 255 ? -9.043  -4.801  32.013  1.00 12.18  ? 256 ILE A CG1 1 
ATOM   2102 C  CG2 . ILE A 1 255 ? -11.536 -4.951  31.489  1.00 13.38  ? 256 ILE A CG2 1 
ATOM   2103 C  CD1 . ILE A 1 255 ? -8.709  -5.955  31.156  1.00 13.84  ? 256 ILE A CD1 1 
ATOM   2104 N  N   . LYS A 1 256 ? -13.031 -2.756  33.584  1.00 10.86  ? 257 LYS A N   1 
ATOM   2105 C  CA  . LYS A 1 256 ? -14.347 -2.664  34.136  1.00 11.47  ? 257 LYS A CA  1 
ATOM   2106 C  C   . LYS A 1 256 ? -15.360 -3.270  33.172  1.00 10.57  ? 257 LYS A C   1 
ATOM   2107 O  O   . LYS A 1 256 ? -15.153 -3.157  31.972  1.00 12.69  ? 257 LYS A O   1 
ATOM   2108 C  CB  . LYS A 1 256 ? -14.702 -1.202  34.409  1.00 12.44  ? 257 LYS A CB  1 
ATOM   2109 C  CG  . LYS A 1 256 ? -13.774 -0.621  35.467  1.00 17.77  ? 257 LYS A CG  1 
ATOM   2110 N  N   . ALA A 1 257 ? -16.407 -3.896  33.690  1.00 11.75  ? 258 ALA A N   1 
ATOM   2111 C  CA  . ALA A 1 257 ? -17.467 -4.494  32.912  1.00 12.08  ? 258 ALA A CA  1 
ATOM   2112 C  C   . ALA A 1 257 ? -18.738 -3.701  33.085  1.00 11.29  ? 258 ALA A C   1 
ATOM   2113 O  O   . ALA A 1 257 ? -19.080 -3.297  34.214  1.00 12.71  ? 258 ALA A O   1 
ATOM   2114 C  CB  . ALA A 1 257 ? -17.713 -5.944  33.324  1.00 14.30  ? 258 ALA A CB  1 
ATOM   2115 N  N   . SER A 1 258 ? -19.498 -3.542  31.984  1.00 11.94  ? 259 SER A N   1 
ATOM   2116 C  CA  . SER A 1 258 ? -20.758 -2.836  32.021  1.00 13.29  ? 259 SER A CA  1 
ATOM   2117 C  C   . SER A 1 258 ? -21.889 -3.770  32.449  1.00 13.99  ? 259 SER A C   1 
ATOM   2118 O  O   . SER A 1 258 ? -22.993 -3.253  32.547  1.00 18.34  ? 259 SER A O   1 
ATOM   2119 C  CB  . SER A 1 258 ? -21.085 -2.295  30.642  1.00 14.75  ? 259 SER A CB  1 
ATOM   2120 O  OG  . SER A 1 258 ? -21.474 -3.320  29.745  1.00 13.33  ? 259 SER A OG  1 
ATOM   2121 N  N   . PHE A 1 259 ? -21.614 -5.030  32.661  1.00 14.55  ? 260 PHE A N   1 
ATOM   2122 C  CA  . PHE A 1 259 ? -22.627 -6.060  32.812  1.00 17.21  ? 260 PHE A CA  1 
ATOM   2123 C  C   . PHE A 1 259 ? -22.203 -6.955  33.947  1.00 20.82  ? 260 PHE A C   1 
ATOM   2124 O  O   . PHE A 1 259 ? -21.012 -7.111  34.279  1.00 21.37  ? 260 PHE A O   1 
ATOM   2125 C  CB  . PHE A 1 259 ? -22.826 -6.821  31.512  1.00 18.39  ? 260 PHE A CB  1 
ATOM   2126 C  CG  . PHE A 1 259 ? -21.584 -7.576  31.116  1.00 17.32  ? 260 PHE A CG  1 
ATOM   2127 C  CD1 . PHE A 1 259 ? -20.587 -6.886  30.388  1.00 14.64  ? 260 PHE A CD1 1 
ATOM   2128 C  CD2 . PHE A 1 259 ? -21.303 -8.870  31.562  1.00 19.84  ? 260 PHE A CD2 1 
ATOM   2129 C  CE1 . PHE A 1 259 ? -19.339 -7.493  30.108  1.00 15.96  ? 260 PHE A CE1 1 
ATOM   2130 C  CE2 . PHE A 1 259 ? -20.065 -9.466  31.213  1.00 22.24  ? 260 PHE A CE2 1 
ATOM   2131 C  CZ  . PHE A 1 259 ? -19.098 -8.794  30.479  1.00 19.98  ? 260 PHE A CZ  1 
ATOM   2132 N  N   . LYS A 1 260 ? -23.246 -7.576  34.478  1.00 31.01  ? 261 LYS A N   1 
ATOM   2133 C  CA  . LYS A 1 260 ? -23.292 -8.765  35.385  1.00 40.82  ? 261 LYS A CA  1 
ATOM   2134 C  C   . LYS A 1 260 ? -22.439 -8.702  36.615  1.00 39.25  ? 261 LYS A C   1 
ATOM   2135 O  O   . LYS A 1 260 ? -21.211 -8.815  36.635  0.01 36.20  ? 261 LYS A O   1 
ATOM   2136 C  CB  . LYS A 1 260 ? -23.069 -10.085 34.641  1.00 47.20  ? 261 LYS A CB  1 
ATOM   2137 C  CG  . LYS A 1 260 ? -24.045 -10.390 33.507  1.00 46.59  ? 261 LYS A CG  1 
ATOM   2138 C  CD  . LYS A 1 260 ? -23.718 -11.775 32.917  1.00 55.45  ? 261 LYS A CD  1 
ATOM   2139 C  CE  . LYS A 1 260 ? -22.197 -11.982 32.748  1.00 54.36  ? 261 LYS A CE  1 
ATOM   2140 N  NZ  . LYS A 1 260 ? -21.684 -13.247 32.122  1.00 54.37  ? 261 LYS A NZ  1 
ATOM   2141 O  OXT . LYS A 1 260 ? -23.077 -8.521  37.635  1.00 71.64  ? 261 LYS A OXT 1 
HETATM 2142 ZN ZN  . ZN  B 2 .   ? -6.686  -1.725  15.290  1.00 8.15   ? 301 ZN  A ZN  1 
HETATM 2143 O  O4  . VD9 C 3 .   ? -5.375  0.902   18.109  1.00 8.82   ? 302 VD9 A O4  1 
HETATM 2144 S  S2  . VD9 C 3 .   ? -5.924  0.787   16.800  1.00 8.48   ? 302 VD9 A S2  1 
HETATM 2145 O  O1  . VD9 C 3 .   ? -7.364  0.843   16.684  1.00 8.66   ? 302 VD9 A O1  1 
HETATM 2146 N  N3  . VD9 C 3 .   ? -5.401  -0.583  16.081  1.00 8.38   ? 302 VD9 A N3  1 
HETATM 2147 C  C5  . VD9 C 3 .   ? -5.361  2.198   15.902  1.00 9.58   ? 302 VD9 A C5  1 
HETATM 2148 C  C10 . VD9 C 3 .   ? -4.021  2.233   15.534  1.00 10.76  ? 302 VD9 A C10 1 
HETATM 2149 C  C9  . VD9 C 3 .   ? -3.561  3.385   14.848  1.00 12.96  ? 302 VD9 A C9  1 
HETATM 2150 C  C8  . VD9 C 3 .   ? -4.445  4.422   14.521  1.00 11.73  ? 302 VD9 A C8  1 
HETATM 2151 C  C7  . VD9 C 3 .   ? -5.795  4.370   14.872  1.00 11.76  ? 302 VD9 A C7  1 
HETATM 2152 C  C6  . VD9 C 3 .   ? -6.263  3.249   15.594  1.00 10.40  ? 302 VD9 A C6  1 
HETATM 2153 S  S11 . VD9 C 3 .   ? -3.942  5.860   13.622  1.00 19.81  ? 302 VD9 A S11 1 
HETATM 2154 C  C12 . VD9 C 3 .   ? -2.064  5.833   13.655  1.00 18.90  ? 302 VD9 A C12 1 
HETATM 2155 C  C13 . VD9 C 3 .   ? -1.538  7.217   13.297  1.00 29.91  ? 302 VD9 A C13 1 
HETATM 2156 C  C14 . VD9 C 3 .   ? -1.654  7.930   14.645  1.00 25.25  ? 302 VD9 A C14 1 
HETATM 2157 O  O4  . VD9 D 3 .   ? 9.946   0.416   13.579  1.00 24.44  ? 303 VD9 A O4  1 
HETATM 2158 S  S2  . VD9 D 3 .   ? 10.546  -0.881  13.925  1.00 21.02  ? 303 VD9 A S2  1 
HETATM 2159 O  O1  . VD9 D 3 .   ? 9.764   -2.106  14.199  1.00 24.96  ? 303 VD9 A O1  1 
HETATM 2160 N  N3  . VD9 D 3 .   ? 11.372  -0.572  15.474  1.00 21.32  ? 303 VD9 A N3  1 
HETATM 2161 C  C5  . VD9 D 3 .   ? 11.661  -1.368  12.682  1.00 19.53  ? 303 VD9 A C5  1 
HETATM 2162 C  C10 . VD9 D 3 .   ? 11.977  -2.750  12.662  1.00 28.31  ? 303 VD9 A C10 1 
HETATM 2163 C  C9  . VD9 D 3 .   ? 12.855  -3.183  11.686  1.00 23.45  ? 303 VD9 A C9  1 
HETATM 2164 C  C8  . VD9 D 3 .   ? 13.472  -2.202  10.808  1.00 24.97  ? 303 VD9 A C8  1 
HETATM 2165 C  C7  . VD9 D 3 .   ? 13.114  -0.830  10.877  1.00 37.87  ? 303 VD9 A C7  1 
HETATM 2166 C  C6  . VD9 D 3 .   ? 12.242  -0.397  11.845  1.00 24.18  ? 303 VD9 A C6  1 
HETATM 2167 S  S11 . VD9 D 3 .   ? 14.593  -2.723  9.524   1.00 31.00  ? 303 VD9 A S11 1 
HETATM 2168 C  C12 . VD9 D 3 .   ? 14.512  -1.247  8.390   1.00 44.50  ? 303 VD9 A C12 1 
HETATM 2169 C  C13 . VD9 D 3 .   ? 13.379  -1.311  7.342   1.00 41.63  ? 303 VD9 A C13 1 
HETATM 2170 C  C14 . VD9 D 3 .   ? 13.296  -0.112  6.397   1.00 37.16  ? 303 VD9 A C14 1 
HETATM 2171 S  S   . DMS E 4 .   ? 1.324   -11.753 14.941  1.00 21.43  ? 304 DMS A S   1 
HETATM 2172 O  O   . DMS E 4 .   ? 1.894   -13.096 14.482  1.00 30.34  ? 304 DMS A O   1 
HETATM 2173 C  C1  . DMS E 4 .   ? 1.579   -11.651 16.585  1.00 19.08  ? 304 DMS A C1  1 
HETATM 2174 C  C2  . DMS E 4 .   ? 2.419   -10.515 14.518  1.00 23.20  ? 304 DMS A C2  1 
HETATM 2175 N  N1  . BCN F 5 .   ? -20.662 -14.750 23.438  1.00 35.54  ? 305 BCN A N1  1 
HETATM 2176 C  C1  . BCN F 5 .   ? -19.695 -14.112 24.410  1.00 29.83  ? 305 BCN A C1  1 
HETATM 2177 C  C2  . BCN F 5 .   ? -19.936 -15.060 25.600  1.00 31.32  ? 305 BCN A C2  1 
HETATM 2178 O  O21 . BCN F 5 .   ? -20.827 -16.011 25.513  1.00 46.68  ? 305 BCN A O21 1 
HETATM 2179 O  O22 . BCN F 5 .   ? -19.316 -14.926 26.676  1.00 38.13  ? 305 BCN A O22 1 
HETATM 2180 C  C3  . BCN F 5 .   ? -21.731 -13.840 22.990  1.00 26.27  ? 305 BCN A C3  1 
HETATM 2181 C  C4  . BCN F 5 .   ? -22.838 -13.515 24.012  1.00 48.54  ? 305 BCN A C4  1 
HETATM 2182 O  O4  . BCN F 5 .   ? -22.517 -12.378 24.862  1.00 32.41  ? 305 BCN A O4  1 
HETATM 2183 C  C5  . BCN F 5 .   ? -20.110 -15.629 22.375  1.00 19.23  ? 305 BCN A C5  1 
HETATM 2184 C  C6  . BCN F 5 .   ? -21.129 -16.540 21.642  1.00 57.04  ? 305 BCN A C6  1 
HETATM 2185 O  O6  . BCN F 5 .   ? -21.129 -16.251 20.231  1.00 48.06  ? 305 BCN A O6  1 
HETATM 2186 S  S   . DMS G 4 .   ? -5.747  7.629   11.162  1.00 36.48  ? 306 DMS A S   1 
HETATM 2187 O  O   . DMS G 4 .   ? -6.446  6.469   10.630  1.00 29.31  ? 306 DMS A O   1 
HETATM 2188 C  C1  . DMS G 4 .   ? -4.513  8.297   10.160  1.00 58.16  ? 306 DMS A C1  1 
HETATM 2189 C  C2  . DMS G 4 .   ? -6.787  8.919   10.728  1.00 34.70  ? 306 DMS A C2  1 
HETATM 2190 O  O   . HOH H 6 .   ? -25.171 9.656   12.995  1.00 31.79  ? 401 HOH A O   1 
HETATM 2191 O  O   . HOH H 6 .   ? -3.465  17.967  21.441  1.00 29.59  ? 402 HOH A O   1 
HETATM 2192 O  O   . HOH H 6 .   ? 1.737   -15.340 -5.008  1.00 43.45  ? 403 HOH A O   1 
HETATM 2193 O  O   . HOH H 6 .   ? -1.599  1.868   11.672  1.00 33.49  ? 404 HOH A O   1 
HETATM 2194 O  O   . HOH H 6 .   ? -22.988 15.144  18.871  1.00 35.08  ? 405 HOH A O   1 
HETATM 2195 O  O   . HOH H 6 .   ? -6.321  -11.614 36.336  1.00 36.96  ? 406 HOH A O   1 
HETATM 2196 O  O   . HOH H 6 .   ? -10.510 -5.816  38.271  1.00 29.33  ? 407 HOH A O   1 
HETATM 2197 O  O   . HOH H 6 .   ? -20.742 -6.869  -2.188  1.00 42.85  ? 408 HOH A O   1 
HETATM 2198 O  O   . HOH H 6 .   ? -17.781 -22.101 6.025   1.00 18.50  ? 409 HOH A O   1 
HETATM 2199 O  O   . HOH H 6 .   ? -0.494  2.908   12.802  1.00 27.78  ? 410 HOH A O   1 
HETATM 2200 O  O   . HOH H 6 .   ? -19.461 17.256  6.001   1.00 31.65  ? 411 HOH A O   1 
HETATM 2201 O  O   . HOH H 6 .   ? -11.131 -15.166 34.123  1.00 28.72  ? 412 HOH A O   1 
HETATM 2202 O  O   . HOH H 6 .   ? -7.730  -4.894  39.976  1.00 31.14  ? 413 HOH A O   1 
HETATM 2203 O  O   . HOH H 6 .   ? -15.600 -10.353 37.455  1.00 35.70  ? 414 HOH A O   1 
HETATM 2204 O  O   . HOH H 6 .   ? -15.117 2.442   38.652  1.00 28.80  ? 415 HOH A O   1 
HETATM 2205 O  O   . HOH H 6 .   ? -2.912  -19.338 6.301   1.00 31.14  ? 416 HOH A O   1 
HETATM 2206 O  O   . HOH H 6 .   ? -6.280  -4.630  -6.421  1.00 25.08  ? 417 HOH A O   1 
HETATM 2207 O  O   . HOH H 6 .   ? 4.619   -1.026  -5.271  1.00 33.96  ? 418 HOH A O   1 
HETATM 2208 O  O   . HOH H 6 .   ? 9.237   7.311   18.158  1.00 36.70  ? 419 HOH A O   1 
HETATM 2209 O  O   . HOH H 6 .   ? -16.471 14.379  33.185  1.00 27.97  ? 420 HOH A O   1 
HETATM 2210 O  O   . HOH H 6 .   ? -21.117 7.787   1.888   1.00 21.07  ? 421 HOH A O   1 
HETATM 2211 O  O   . HOH H 6 .   ? 15.134  -6.796  11.849  1.00 32.84  ? 422 HOH A O   1 
HETATM 2212 O  O   . HOH H 6 .   ? -15.955 3.504   35.253  1.00 32.37  ? 423 HOH A O   1 
HETATM 2213 O  O   . HOH H 6 .   ? 1.542   4.918   12.247  1.00 35.61  ? 424 HOH A O   1 
HETATM 2214 O  O   . HOH H 6 .   ? -5.070  0.479   9.900   1.00 23.52  ? 425 HOH A O   1 
HETATM 2215 O  O   . HOH H 6 .   ? -12.396 12.322  29.256  1.00 26.04  ? 426 HOH A O   1 
HETATM 2216 O  O   . HOH H 6 .   ? 11.362  -7.131  22.269  1.00 30.38  ? 427 HOH A O   1 
HETATM 2217 O  O   . HOH H 6 .   ? -22.812 -14.756 16.065  1.00 33.32  ? 428 HOH A O   1 
HETATM 2218 O  O   . HOH H 6 .   ? -12.159 10.664  5.770   1.00 29.56  ? 429 HOH A O   1 
HETATM 2219 O  O   . HOH H 6 .   ? -27.278 -5.405  27.423  1.00 33.02  ? 430 HOH A O   1 
HETATM 2220 O  O   . HOH H 6 .   ? -20.654 8.206   30.037  1.00 31.36  ? 431 HOH A O   1 
HETATM 2221 O  O   . HOH H 6 .   ? -8.718  -3.913  7.892   1.00 11.18  ? 432 HOH A O   1 
HETATM 2222 O  O   . HOH H 6 .   ? -25.603 -1.193  35.120  1.00 36.01  ? 433 HOH A O   1 
HETATM 2223 O  O   . HOH H 6 .   ? -1.292  -4.185  15.731  1.00 10.88  ? 434 HOH A O   1 
HETATM 2224 O  O   . HOH H 6 .   ? -10.660 8.628   25.586  1.00 10.91  ? 435 HOH A O   1 
HETATM 2225 O  O   . HOH H 6 .   ? 0.058   -1.072  -4.705  1.00 18.74  ? 436 HOH A O   1 
HETATM 2226 O  O   . HOH H 6 .   ? 3.587   4.941   29.799  1.00 18.45  ? 437 HOH A O   1 
HETATM 2227 O  O   . HOH H 6 .   ? 4.438   -2.593  29.061  1.00 25.76  ? 438 HOH A O   1 
HETATM 2228 O  O   . HOH H 6 .   ? -19.283 -20.801 5.166   1.00 27.72  ? 439 HOH A O   1 
HETATM 2229 O  O   . HOH H 6 .   ? -23.989 -2.738  29.138  1.00 36.99  ? 440 HOH A O   1 
HETATM 2230 O  O   . HOH H 6 .   ? -24.154 8.558   20.160  1.00 20.96  ? 441 HOH A O   1 
HETATM 2231 O  O   . HOH H 6 .   ? -7.029  5.872   6.381   1.00 21.49  ? 442 HOH A O   1 
HETATM 2232 O  O   . HOH H 6 .   ? -25.945 6.056   27.060  1.00 25.80  ? 443 HOH A O   1 
HETATM 2233 O  O   . HOH H 6 .   ? -16.847 -13.976 26.410  1.00 20.67  ? 444 HOH A O   1 
HETATM 2234 O  O   . HOH H 6 .   ? 4.233   -3.457  26.525  1.00 20.77  ? 445 HOH A O   1 
HETATM 2235 O  O   . HOH H 6 .   ? -14.391 -16.632 29.043  1.00 22.48  ? 446 HOH A O   1 
HETATM 2236 O  O   . HOH H 6 .   ? -16.453 -15.421 32.810  1.00 37.38  ? 447 HOH A O   1 
HETATM 2237 O  O   . HOH H 6 .   ? -10.453 13.354  8.739   1.00 31.27  ? 448 HOH A O   1 
HETATM 2238 O  O   . HOH H 6 .   ? -16.436 5.162   -8.017  1.00 29.84  ? 449 HOH A O   1 
HETATM 2239 O  O   . HOH H 6 .   ? -4.779  -12.005 32.101  1.00 20.59  ? 450 HOH A O   1 
HETATM 2240 O  O   . HOH H 6 .   ? 1.860   8.093   27.922  1.00 36.15  ? 451 HOH A O   1 
HETATM 2241 O  O   . HOH H 6 .   ? -9.167  5.830   29.057  1.00 18.99  ? 452 HOH A O   1 
HETATM 2242 O  O   . HOH H 6 .   ? 1.000   14.704  24.307  1.00 32.03  ? 453 HOH A O   1 
HETATM 2243 O  O   . HOH H 6 .   ? -2.557  -3.588  11.433  1.00 22.06  ? 454 HOH A O   1 
HETATM 2244 O  O   . HOH H 6 .   ? -17.419 -16.226 22.039  1.00 23.26  ? 455 HOH A O   1 
HETATM 2245 O  O   . HOH H 6 .   ? -10.441 -18.327 17.077  1.00 13.51  ? 456 HOH A O   1 
HETATM 2246 O  O   . HOH H 6 .   ? -12.398 16.131  8.325   1.00 40.97  ? 457 HOH A O   1 
HETATM 2247 O  O   . HOH H 6 .   ? -8.005  -15.487 11.369  1.00 11.99  ? 458 HOH A O   1 
HETATM 2248 O  O   . HOH H 6 .   ? -0.486  13.836  16.080  1.00 24.95  ? 459 HOH A O   1 
HETATM 2249 O  O   . HOH H 6 .   ? -14.098 14.209  27.203  1.00 22.96  ? 460 HOH A O   1 
HETATM 2250 O  O   . HOH H 6 .   ? -22.785 -5.875  2.778   1.00 22.83  ? 461 HOH A O   1 
HETATM 2251 O  O   . HOH H 6 .   ? -25.416 11.009  19.649  1.00 31.11  ? 462 HOH A O   1 
HETATM 2252 O  O   . HOH H 6 .   ? -27.395 -7.675  26.062  1.00 34.81  ? 463 HOH A O   1 
HETATM 2253 O  O   . HOH H 6 .   ? -11.991 9.346   3.193   1.00 22.53  ? 464 HOH A O   1 
HETATM 2254 O  O   . HOH H 6 .   ? -15.425 -21.867 13.088  1.00 16.75  ? 465 HOH A O   1 
HETATM 2255 O  O   . HOH H 6 .   ? -12.801 13.112  31.862  1.00 31.88  ? 466 HOH A O   1 
HETATM 2256 O  O   . HOH H 6 .   ? -17.968 10.605  11.272  1.00 16.83  ? 467 HOH A O   1 
HETATM 2257 O  O   . HOH H 6 .   ? -6.966  -14.938 31.624  1.00 25.92  ? 468 HOH A O   1 
HETATM 2258 O  O   . HOH H 6 .   ? 1.845   -15.710 9.293   1.00 23.48  ? 469 HOH A O   1 
HETATM 2259 O  O   . HOH H 6 .   ? -21.964 -14.163 18.709  1.00 33.27  ? 470 HOH A O   1 
HETATM 2260 O  O   . HOH H 6 .   ? 3.633   2.642   8.297   1.00 39.70  ? 471 HOH A O   1 
HETATM 2261 O  O   . HOH H 6 .   ? 9.357   2.309   11.720  1.00 30.18  ? 472 HOH A O   1 
HETATM 2262 O  O   . HOH H 6 .   ? 7.430   -7.792  -0.699  1.00 34.79  ? 473 HOH A O   1 
HETATM 2263 O  O   . HOH H 6 .   ? -1.950  -4.726  -7.020  1.00 30.74  ? 474 HOH A O   1 
HETATM 2264 O  O   . HOH H 6 .   ? 15.407  0.660   15.275  1.00 39.94  ? 475 HOH A O   1 
HETATM 2265 O  O   . HOH H 6 .   ? -1.246  9.065   28.121  1.00 30.54  ? 476 HOH A O   1 
HETATM 2266 O  O   . HOH H 6 .   ? -4.581  -13.573 18.071  1.00 10.51  ? 477 HOH A O   1 
HETATM 2267 O  O   . HOH H 6 .   ? -20.353 10.666  26.736  1.00 20.63  ? 478 HOH A O   1 
HETATM 2268 O  O   . HOH H 6 .   ? -18.705 -21.142 14.753  1.00 24.34  ? 479 HOH A O   1 
HETATM 2269 O  O   . HOH H 6 .   ? -18.508 -12.421 -3.588  1.00 25.85  ? 480 HOH A O   1 
HETATM 2270 O  O   . HOH H 6 .   ? -0.173  1.050   34.519  1.00 27.78  ? 481 HOH A O   1 
HETATM 2271 O  O   . HOH H 6 .   ? -10.696 8.449   7.738   1.00 23.26  ? 482 HOH A O   1 
HETATM 2272 O  O   . HOH H 6 .   ? 8.546   -3.875  20.960  1.00 14.79  ? 483 HOH A O   1 
HETATM 2273 O  O   . HOH H 6 .   ? 15.468  -2.363  14.528  1.00 24.66  ? 484 HOH A O   1 
HETATM 2274 O  O   . HOH H 6 .   ? 5.787   -2.972  6.895   1.00 34.13  ? 485 HOH A O   1 
HETATM 2275 O  O   . HOH H 6 .   ? -3.533  -11.216 20.899  1.00 10.86  ? 486 HOH A O   1 
HETATM 2276 O  O   . HOH H 6 .   ? 6.088   -11.097 15.343  1.00 35.42  ? 487 HOH A O   1 
HETATM 2277 O  O   . HOH H 6 .   ? -17.054 -8.458  20.412  1.00 10.26  ? 488 HOH A O   1 
HETATM 2278 O  O   . HOH H 6 .   ? 2.573   -4.399  7.784   1.00 19.44  ? 489 HOH A O   1 
HETATM 2279 O  O   . HOH H 6 .   ? -1.436  -1.429  -12.953 1.00 49.06  ? 490 HOH A O   1 
HETATM 2280 O  O   . HOH H 6 .   ? -3.624  -12.988 -2.834  1.00 28.13  ? 491 HOH A O   1 
HETATM 2281 O  O   . HOH H 6 .   ? -8.583  0.621   -6.530  1.00 31.10  ? 492 HOH A O   1 
HETATM 2282 O  O   . HOH H 6 .   ? 13.360  0.198   24.376  1.00 20.03  ? 493 HOH A O   1 
HETATM 2283 O  O   . HOH H 6 .   ? -25.642 -3.323  31.800  1.00 39.55  ? 494 HOH A O   1 
HETATM 2284 O  O   . HOH H 6 .   ? -2.540  -8.798  29.117  1.00 12.10  ? 495 HOH A O   1 
HETATM 2285 O  O   . HOH H 6 .   ? -8.503  -15.436 36.718  1.00 30.06  ? 496 HOH A O   1 
HETATM 2286 O  O   . HOH H 6 .   ? -14.993 19.987  17.692  1.00 19.12  ? 497 HOH A O   1 
HETATM 2287 O  O   . HOH H 6 .   ? -16.127 -12.346 24.438  1.00 15.72  ? 498 HOH A O   1 
HETATM 2288 O  O   . HOH H 6 .   ? -15.590 8.932   -2.152  1.00 25.81  ? 499 HOH A O   1 
HETATM 2289 O  O   . HOH H 6 .   ? -19.845 -4.341  41.351  1.00 33.28  ? 500 HOH A O   1 
HETATM 2290 O  O   . HOH H 6 .   ? -25.621 -8.925  11.191  1.00 24.50  ? 501 HOH A O   1 
HETATM 2291 O  O   . HOH H 6 .   ? -16.237 15.801  23.723  1.00 17.92  ? 502 HOH A O   1 
HETATM 2292 O  O   . HOH H 6 .   ? -10.663 21.633  20.061  1.00 18.89  ? 503 HOH A O   1 
HETATM 2293 O  O   . HOH H 6 .   ? -4.262  -8.539  31.160  1.00 18.99  ? 504 HOH A O   1 
HETATM 2294 O  O   . HOH H 6 .   ? 7.768   -5.183  -0.268  1.00 50.46  ? 505 HOH A O   1 
HETATM 2295 O  O   . HOH H 6 .   ? -2.640  -19.239 21.647  1.00 34.88  ? 506 HOH A O   1 
HETATM 2296 O  O   . HOH H 6 .   ? -12.542 18.299  29.024  1.00 38.50  ? 507 HOH A O   1 
HETATM 2297 O  O   . HOH H 6 .   ? -11.091 0.990   33.462  1.00 24.39  ? 508 HOH A O   1 
HETATM 2298 O  O   . HOH H 6 .   ? -17.984 20.653  8.001   1.00 15.50  ? 509 HOH A O   1 
HETATM 2299 O  O   . HOH H 6 .   ? 1.256   -11.831 25.072  1.00 24.17  ? 510 HOH A O   1 
HETATM 2300 O  O   . HOH H 6 .   ? 5.502   -12.823 11.489  1.00 37.30  ? 511 HOH A O   1 
HETATM 2301 O  O   . HOH H 6 .   ? -6.825  20.862  19.548  1.00 14.97  ? 512 HOH A O   1 
HETATM 2302 O  O   . HOH H 6 .   ? -0.502  10.738  23.332  1.00 17.19  ? 513 HOH A O   1 
HETATM 2303 O  O   . HOH H 6 .   ? -24.940 4.685   8.468   1.00 34.68  ? 514 HOH A O   1 
HETATM 2304 O  O   . HOH H 6 .   ? -13.928 10.281  27.944  1.00 18.37  ? 515 HOH A O   1 
HETATM 2305 O  O   . HOH H 6 .   ? 0.269   -19.627 10.862  1.00 32.66  ? 516 HOH A O   1 
HETATM 2306 O  O   . HOH H 6 .   ? -1.419  4.391   -4.881  1.00 35.67  ? 517 HOH A O   1 
HETATM 2307 O  O   . HOH H 6 .   ? -26.486 -7.723  30.301  1.00 64.50  ? 518 HOH A O   1 
HETATM 2308 O  O   . HOH H 6 .   ? -3.842  -15.943 24.350  1.00 13.99  ? 519 HOH A O   1 
HETATM 2309 O  O   . HOH H 6 .   ? -3.421  -13.318 25.177  1.00 12.54  ? 520 HOH A O   1 
HETATM 2310 O  O   . HOH H 6 .   ? 5.384   7.048   20.222  1.00 18.54  ? 521 HOH A O   1 
HETATM 2311 O  O   . HOH H 6 .   ? 12.948  6.249   15.748  1.00 36.27  ? 522 HOH A O   1 
HETATM 2312 O  O   . HOH H 6 .   ? -14.733 -18.590 18.736  1.00 16.08  ? 523 HOH A O   1 
HETATM 2313 O  O   . HOH H 6 .   ? 8.234   -5.956  -10.450 1.00 30.05  ? 524 HOH A O   1 
HETATM 2314 O  O   . HOH H 6 .   ? -13.493 -0.913  -6.141  1.00 39.08  ? 525 HOH A O   1 
HETATM 2315 O  O   . HOH H 6 .   ? -12.930 -8.898  -3.263  1.00 35.01  ? 526 HOH A O   1 
HETATM 2316 O  O   . HOH H 6 .   ? -23.378 -13.307 11.299  1.00 23.99  ? 527 HOH A O   1 
HETATM 2317 O  O   . HOH H 6 .   ? -21.644 -7.215  23.584  1.00 13.21  ? 528 HOH A O   1 
HETATM 2318 O  O   . HOH H 6 .   ? -23.251 -3.019  6.674   1.00 21.07  ? 529 HOH A O   1 
HETATM 2319 O  O   . HOH H 6 .   ? -6.694  -5.335  37.375  1.00 19.00  ? 530 HOH A O   1 
HETATM 2320 O  O   . HOH H 6 .   ? 10.832  4.323   8.338   1.00 42.36  ? 531 HOH A O   1 
HETATM 2321 O  O   . HOH H 6 .   ? -26.434 2.790   20.750  1.00 30.95  ? 532 HOH A O   1 
HETATM 2322 O  O   . HOH H 6 .   ? -4.463  -4.759  11.142  1.00 27.66  ? 533 HOH A O   1 
HETATM 2323 O  O   . HOH H 6 .   ? -22.108 -18.353 13.561  1.00 23.18  ? 534 HOH A O   1 
HETATM 2324 O  O   . HOH H 6 .   ? -7.023  -8.405  -7.167  1.00 43.50  ? 535 HOH A O   1 
HETATM 2325 O  O   . HOH H 6 .   ? -18.439 -3.737  -2.675  1.00 30.98  ? 536 HOH A O   1 
HETATM 2326 O  O   . HOH H 6 .   ? -13.431 -18.575 14.601  1.00 16.06  ? 537 HOH A O   1 
HETATM 2327 O  O   . HOH H 6 .   ? 8.297   2.987   27.706  1.00 32.17  ? 538 HOH A O   1 
HETATM 2328 O  O   . HOH H 6 .   ? -9.679  6.259   -4.018  1.00 43.59  ? 539 HOH A O   1 
HETATM 2329 O  O   . HOH H 6 .   ? -13.792 19.884  15.149  1.00 18.59  ? 540 HOH A O   1 
HETATM 2330 O  O   . HOH H 6 .   ? -21.854 5.674   4.728   1.00 19.20  ? 541 HOH A O   1 
HETATM 2331 O  O   . HOH H 6 .   ? -22.228 3.774   -2.962  1.00 33.57  ? 542 HOH A O   1 
HETATM 2332 O  O   . HOH H 6 .   ? -24.758 -7.769  9.078   1.00 19.19  ? 543 HOH A O   1 
HETATM 2333 O  O   . HOH H 6 .   ? -11.086 -19.437 7.066   1.00 27.47  ? 544 HOH A O   1 
HETATM 2334 O  O   . HOH H 6 .   ? -7.872  -19.010 30.630  1.00 26.37  ? 545 HOH A O   1 
HETATM 2335 O  O   . HOH H 6 .   ? -20.019 16.848  23.279  1.00 34.94  ? 546 HOH A O   1 
HETATM 2336 O  O   . HOH H 6 .   ? -25.577 -10.689 17.764  1.00 23.59  ? 547 HOH A O   1 
HETATM 2337 O  O   . HOH H 6 .   ? -26.169 3.493   15.402  1.00 23.47  ? 548 HOH A O   1 
HETATM 2338 O  O   . HOH H 6 .   ? -11.725 -3.387  42.066  1.00 31.91  ? 549 HOH A O   1 
HETATM 2339 O  O   . HOH H 6 .   ? -18.861 2.194   40.823  1.00 44.34  ? 550 HOH A O   1 
HETATM 2340 O  O   . HOH H 6 .   ? -13.058 -16.916 26.711  1.00 16.32  ? 551 HOH A O   1 
HETATM 2341 O  O   . HOH H 6 .   ? 2.480   -13.290 5.267   1.00 21.91  ? 552 HOH A O   1 
HETATM 2342 O  O   . HOH H 6 .   ? -19.297 9.964   8.864   1.00 14.94  ? 553 HOH A O   1 
HETATM 2343 O  O   . HOH H 6 .   ? -5.267  -13.616 34.356  1.00 46.52  ? 554 HOH A O   1 
HETATM 2344 O  O   . HOH H 6 .   ? -7.242  -16.818 1.538   1.00 22.02  ? 555 HOH A O   1 
HETATM 2345 O  O   . HOH H 6 .   ? -23.255 -0.409  34.551  1.00 28.71  ? 556 HOH A O   1 
HETATM 2346 O  O   . HOH H 6 .   ? -17.239 -7.522  39.614  1.00 37.67  ? 557 HOH A O   1 
HETATM 2347 O  O   . HOH H 6 .   ? 1.500   -6.300  34.397  1.00 25.83  ? 558 HOH A O   1 
HETATM 2348 O  O   . HOH H 6 .   ? -9.393  -10.105 -1.173  1.00 25.91  ? 559 HOH A O   1 
HETATM 2349 O  O   . HOH H 6 .   ? -4.683  -15.909 0.725   1.00 28.59  ? 560 HOH A O   1 
HETATM 2350 O  O   . HOH H 6 .   ? -23.395 -11.166 17.050  1.00 27.46  ? 561 HOH A O   1 
HETATM 2351 O  O   . HOH H 6 .   ? -24.125 -0.068  1.260   1.00 35.65  ? 562 HOH A O   1 
HETATM 2352 O  O   . HOH H 6 .   ? -8.095  -22.199 10.447  1.00 22.45  ? 563 HOH A O   1 
HETATM 2353 O  O   . HOH H 6 .   ? 4.215   -6.629  7.751   1.00 24.36  ? 564 HOH A O   1 
HETATM 2354 O  O   . HOH H 6 .   ? -12.061 2.676   30.895  1.00 18.17  ? 565 HOH A O   1 
HETATM 2355 O  O   . HOH H 6 .   ? 6.400   -5.824  6.704   1.00 30.96  ? 566 HOH A O   1 
HETATM 2356 O  O   . HOH H 6 .   ? -26.940 -4.077  24.989  1.00 21.34  ? 567 HOH A O   1 
HETATM 2357 O  O   . HOH H 6 .   ? -2.915  5.976   -1.501  1.00 31.30  ? 568 HOH A O   1 
HETATM 2358 O  O   . HOH H 6 .   ? -15.047 6.011   32.827  1.00 36.14  ? 569 HOH A O   1 
HETATM 2359 O  O   . HOH H 6 .   ? -16.377 -9.953  32.943  1.00 18.87  ? 570 HOH A O   1 
HETATM 2360 O  O   . HOH H 6 .   ? 4.863   -4.905  20.939  1.00 14.62  ? 571 HOH A O   1 
HETATM 2361 O  O   . HOH H 6 .   ? 3.580   4.314   10.558  1.00 42.40  ? 572 HOH A O   1 
HETATM 2362 O  O   . HOH H 6 .   ? -7.441  -8.724  32.651  1.00 17.23  ? 573 HOH A O   1 
HETATM 2363 O  O   . HOH H 6 .   ? -23.583 -18.018 6.183   1.00 30.66  ? 574 HOH A O   1 
HETATM 2364 O  O   . HOH H 6 .   ? 4.960   -7.325  22.365  1.00 29.87  ? 575 HOH A O   1 
HETATM 2365 O  O   . HOH H 6 .   ? -23.855 -0.787  3.956   1.00 23.68  ? 576 HOH A O   1 
HETATM 2366 O  O   . HOH H 6 .   ? 1.212   8.707   24.335  1.00 18.19  ? 577 HOH A O   1 
HETATM 2367 O  O   . HOH H 6 .   ? -24.022 -0.769  26.459  1.00 18.00  ? 578 HOH A O   1 
HETATM 2368 O  O   . HOH H 6 .   ? 2.551   -11.420 9.472   1.00 22.56  ? 579 HOH A O   1 
HETATM 2369 O  O   . HOH H 6 .   ? 11.195  1.293   25.917  1.00 23.64  ? 580 HOH A O   1 
HETATM 2370 O  O   . HOH H 6 .   ? -18.453 3.655   -3.448  1.00 70.89  ? 581 HOH A O   1 
HETATM 2371 O  O   . HOH H 6 .   ? -10.139 14.732  12.185  1.00 20.77  ? 582 HOH A O   1 
HETATM 2372 O  O   . HOH H 6 .   ? 1.227   -1.612  29.422  1.00 14.01  ? 583 HOH A O   1 
HETATM 2373 O  O   . HOH H 6 .   ? -22.791 -9.543  25.390  1.00 24.63  ? 584 HOH A O   1 
HETATM 2374 O  O   . HOH H 6 .   ? -8.577  -19.863 26.645  1.00 22.49  ? 585 HOH A O   1 
HETATM 2375 O  O   . HOH H 6 .   ? -0.587  -8.593  32.536  1.00 22.83  ? 586 HOH A O   1 
HETATM 2376 O  O   . HOH H 6 .   ? -12.852 7.853   28.937  1.00 24.67  ? 587 HOH A O   1 
HETATM 2377 O  O   . HOH H 6 .   ? 3.145   1.068   -1.914  1.00 42.10  ? 588 HOH A O   1 
HETATM 2378 O  O   . HOH H 6 .   ? 13.004  -5.863  24.321  1.00 24.03  ? 589 HOH A O   1 
HETATM 2379 O  O   . HOH H 6 .   ? -21.217 -19.659 6.621   1.00 23.42  ? 590 HOH A O   1 
HETATM 2380 O  O   . HOH H 6 .   ? -6.284  -19.805 23.825  1.00 23.60  ? 591 HOH A O   1 
HETATM 2381 O  O   . HOH H 6 .   ? 5.735   0.847   8.310   1.00 28.91  ? 592 HOH A O   1 
HETATM 2382 O  O   . HOH H 6 .   ? -21.515 15.836  3.603   1.00 33.40  ? 593 HOH A O   1 
HETATM 2383 O  O   . HOH H 6 .   ? -9.103  -5.877  35.919  1.00 18.45  ? 594 HOH A O   1 
HETATM 2384 O  O   . HOH H 6 .   ? -25.951 7.791   6.303   1.00 33.28  ? 595 HOH A O   1 
HETATM 2385 O  O   . HOH H 6 .   ? -5.908  15.257  11.908  1.00 34.31  ? 596 HOH A O   1 
HETATM 2386 O  O   . HOH H 6 .   ? -2.115  -12.350 22.853  1.00 11.27  ? 597 HOH A O   1 
HETATM 2387 O  O   . HOH H 6 .   ? 0.037   -14.380 31.219  1.00 37.84  ? 598 HOH A O   1 
HETATM 2388 O  O   . HOH H 6 .   ? -24.777 12.009  6.251   1.00 29.96  ? 599 HOH A O   1 
HETATM 2389 O  O   . HOH H 6 .   ? -12.781 3.629   -6.860  1.00 27.04  ? 600 HOH A O   1 
HETATM 2390 O  O   . HOH H 6 .   ? 1.230   2.346   35.802  1.00 48.43  ? 601 HOH A O   1 
HETATM 2391 O  O   . HOH H 6 .   ? -22.954 -11.634 14.037  1.00 19.97  ? 602 HOH A O   1 
HETATM 2392 O  O   . HOH H 6 .   ? -7.056  1.468   35.159  1.00 26.90  ? 603 HOH A O   1 
HETATM 2393 O  O   . HOH H 6 .   ? -11.243 17.514  12.263  1.00 22.75  ? 604 HOH A O   1 
HETATM 2394 O  O   . HOH H 6 .   ? -9.603  -8.006  34.152  1.00 21.63  ? 605 HOH A O   1 
HETATM 2395 O  O   . HOH H 6 .   ? -12.613 -18.431 32.372  1.00 32.49  ? 606 HOH A O   1 
HETATM 2396 O  O   . HOH H 6 .   ? -8.243  -19.419 21.724  1.00 14.74  ? 607 HOH A O   1 
HETATM 2397 O  O   . HOH H 6 .   ? -3.124  4.563   7.212   1.00 39.83  ? 608 HOH A O   1 
HETATM 2398 O  O   . HOH H 6 .   ? 7.554   6.061   21.634  1.00 16.74  ? 609 HOH A O   1 
HETATM 2399 O  O   . HOH H 6 .   ? -1.072  -17.558 18.008  1.00 37.73  ? 610 HOH A O   1 
HETATM 2400 O  O   . HOH H 6 .   ? -25.550 4.169   4.021   1.00 38.57  ? 611 HOH A O   1 
HETATM 2401 O  O   . HOH H 6 .   ? -3.959  0.065   13.478  1.00 16.73  ? 612 HOH A O   1 
HETATM 2402 O  O   . HOH H 6 .   ? 10.107  -8.827  8.264   1.00 29.99  ? 613 HOH A O   1 
HETATM 2403 O  O   . HOH H 6 .   ? -5.376  2.130   12.042  1.00 16.54  ? 614 HOH A O   1 
HETATM 2404 O  O   . HOH H 6 .   ? -7.461  -8.722  -2.434  1.00 31.71  ? 615 HOH A O   1 
HETATM 2405 O  O   . HOH H 6 .   ? -5.467  3.278   -5.808  1.00 56.45  ? 616 HOH A O   1 
HETATM 2406 O  O   . HOH H 6 .   ? -8.235  7.388   8.318   1.00 28.93  ? 617 HOH A O   1 
HETATM 2407 O  O   . HOH H 6 .   ? -24.708 -9.572  1.940   1.00 25.69  ? 618 HOH A O   1 
HETATM 2408 O  O   . HOH H 6 .   ? -0.274  -14.301 22.309  1.00 25.70  ? 619 HOH A O   1 
HETATM 2409 O  O   . HOH H 6 .   ? 0.099   3.537   10.356  1.00 36.50  ? 620 HOH A O   1 
HETATM 2410 O  O   . HOH H 6 .   ? -1.623  11.170  25.870  1.00 27.85  ? 621 HOH A O   1 
HETATM 2411 O  O   . HOH H 6 .   ? 4.914   -13.035 -5.687  1.00 30.92  ? 622 HOH A O   1 
HETATM 2412 O  O   . HOH H 6 .   ? -23.882 -0.370  31.755  1.00 38.57  ? 623 HOH A O   1 
HETATM 2413 O  O   . HOH H 6 .   ? 13.863  5.704   19.180  1.00 33.63  ? 624 HOH A O   1 
HETATM 2414 O  O   . HOH H 6 .   ? 1.619   -15.688 -1.390  1.00 54.49  ? 625 HOH A O   1 
HETATM 2415 O  O   . HOH H 6 .   ? -21.856 19.506  12.158  1.00 30.40  ? 626 HOH A O   1 
HETATM 2416 O  O   . HOH H 6 .   ? -26.972 10.273  4.861   1.00 33.85  ? 627 HOH A O   1 
HETATM 2417 O  O   . HOH H 6 .   ? -18.471 -8.993  34.617  1.00 33.05  ? 628 HOH A O   1 
HETATM 2418 O  O   . HOH H 6 .   ? -0.213  -21.048 14.967  1.00 94.06  ? 629 HOH A O   1 
HETATM 2419 O  O   . HOH H 6 .   ? -2.813  -14.932 32.836  1.00 32.11  ? 630 HOH A O   1 
HETATM 2420 O  O   . HOH H 6 .   ? -16.915 -14.174 37.457  1.00 32.35  ? 631 HOH A O   1 
HETATM 2421 O  O   . HOH H 6 .   ? 0.436   0.585   -6.749  1.00 31.65  ? 632 HOH A O   1 
HETATM 2422 O  O   . HOH H 6 .   ? -12.920 -17.257 16.914  1.00 13.64  ? 633 HOH A O   1 
HETATM 2423 O  O   . HOH H 6 .   ? -4.133  3.694   10.245  1.00 34.73  ? 634 HOH A O   1 
HETATM 2424 O  O   . HOH H 6 .   ? -1.690  17.887  15.378  1.00 34.58  ? 635 HOH A O   1 
HETATM 2425 O  O   . HOH H 6 .   ? 16.481  -5.098  13.348  1.00 22.56  ? 636 HOH A O   1 
HETATM 2426 O  O   . HOH H 6 .   ? 10.263  6.638   14.849  1.00 46.20  ? 637 HOH A O   1 
HETATM 2427 O  O   . HOH H 6 .   ? 8.550   -4.626  23.603  1.00 23.17  ? 638 HOH A O   1 
HETATM 2428 O  O   . HOH H 6 .   ? -0.057  -15.286 27.029  1.00 46.27  ? 639 HOH A O   1 
HETATM 2429 O  O   . HOH H 6 .   ? -16.620 -14.750 28.893  1.00 37.01  ? 640 HOH A O   1 
HETATM 2430 O  O   . HOH H 6 .   ? -15.404 -16.296 25.550  1.00 37.35  ? 641 HOH A O   1 
HETATM 2431 O  O   . HOH H 6 .   ? -8.383  -17.626 34.786  1.00 26.79  ? 642 HOH A O   1 
HETATM 2432 O  O   . HOH H 6 .   ? 14.221  2.349   23.234  1.00 38.70  ? 643 HOH A O   1 
HETATM 2433 O  O   . HOH H 6 .   ? 5.285   -10.784 18.776  1.00 34.75  ? 644 HOH A O   1 
HETATM 2434 O  O   . HOH H 6 .   ? -3.855  -1.324  11.298  1.00 27.30  ? 645 HOH A O   1 
HETATM 2435 O  O   . HOH H 6 .   ? -23.841 -3.453  3.915   1.00 37.87  ? 646 HOH A O   1 
HETATM 2436 O  O   . HOH H 6 .   ? -17.779 19.844  17.467  1.00 23.89  ? 647 HOH A O   1 
HETATM 2437 O  O   . HOH H 6 .   ? -25.103 8.591   26.119  1.00 33.43  ? 648 HOH A O   1 
HETATM 2438 O  O   . HOH H 6 .   ? -13.182 18.775  11.809  1.00 36.08  ? 649 HOH A O   1 
HETATM 2439 O  O   . HOH H 6 .   ? -10.144 -12.561 39.984  1.00 31.13  ? 650 HOH A O   1 
HETATM 2440 O  O   . HOH H 6 .   ? -1.459  -13.124 27.123  1.00 26.67  ? 651 HOH A O   1 
HETATM 2441 O  O   . HOH H 6 .   ? 2.833   -13.477 8.109   1.00 29.38  ? 652 HOH A O   1 
HETATM 2442 O  O   . HOH H 6 .   ? -4.935  20.353  21.460  1.00 24.33  ? 653 HOH A O   1 
HETATM 2443 O  O   . HOH H 6 .   ? 11.735  -6.578  7.743   1.00 41.56  ? 654 HOH A O   1 
HETATM 2444 O  O   . HOH H 6 .   ? 10.416  5.131   12.550  1.00 42.43  ? 655 HOH A O   1 
HETATM 2445 O  O   . HOH H 6 .   ? -21.807 19.393  17.361  1.00 41.30  ? 656 HOH A O   1 
HETATM 2446 O  O   . HOH H 6 .   ? 6.370   -5.393  27.255  1.00 37.82  ? 657 HOH A O   1 
HETATM 2447 O  O   . HOH H 6 .   ? -17.011 -17.940 20.162  1.00 24.46  ? 658 HOH A O   1 
HETATM 2448 O  O   . HOH H 6 .   ? 5.740   -9.630  21.015  1.00 34.14  ? 659 HOH A O   1 
HETATM 2449 O  O   . HOH H 6 .   ? 3.299   2.818   0.155   1.00 41.57  ? 660 HOH A O   1 
HETATM 2450 O  O   . HOH H 6 .   ? -10.629 4.863   30.916  1.00 24.54  ? 661 HOH A O   1 
HETATM 2451 O  O   . HOH H 6 .   ? -2.012  -17.584 25.590  1.00 28.20  ? 662 HOH A O   1 
HETATM 2452 O  O   . HOH H 6 .   ? 1.012   3.207   1.834   1.00 35.15  ? 663 HOH A O   1 
HETATM 2453 O  O   . HOH H 6 .   ? -17.848 -12.128 31.741  1.00 32.35  ? 664 HOH A O   1 
HETATM 2454 O  O   . HOH H 6 .   ? 1.715   12.434  22.583  1.00 26.35  ? 665 HOH A O   1 
HETATM 2455 O  O   . HOH H 6 .   ? 1.745   -9.770  31.033  1.00 44.31  ? 666 HOH A O   1 
HETATM 2456 O  O   . HOH H 6 .   ? -4.952  -9.654  33.538  1.00 31.90  ? 667 HOH A O   1 
HETATM 2457 O  O   . HOH H 6 .   ? -24.128 -7.138  0.331   1.00 33.88  ? 668 HOH A O   1 
HETATM 2458 O  O   . HOH H 6 .   ? -11.112 -11.011 -2.780  1.00 35.66  ? 669 HOH A O   1 
HETATM 2459 O  O   . HOH H 6 .   ? -11.530 0.896   -7.804  1.00 37.45  ? 670 HOH A O   1 
HETATM 2460 O  O   . HOH H 6 .   ? -16.214 16.802  26.347  1.00 33.83  ? 671 HOH A O   1 
HETATM 2461 O  O   . HOH H 6 .   ? -2.136  -11.933 31.597  1.00 31.76  ? 672 HOH A O   1 
HETATM 2462 O  O   . HOH H 6 .   ? -6.045  -20.901 26.289  1.00 30.09  ? 673 HOH A O   1 
HETATM 2463 O  O   . HOH H 6 .   ? -1.111  -13.227 33.097  1.00 28.09  ? 674 HOH A O   1 
HETATM 2464 O  O   . HOH H 6 .   ? 1.460   -17.641 7.232   1.00 30.55  ? 675 HOH A O   1 
HETATM 2465 O  O   . HOH H 6 .   ? 5.712   -14.107 8.637   1.00 38.57  ? 676 HOH A O   1 
HETATM 2466 O  O   . HOH H 6 .   ? -7.250  -10.221 -4.557  1.00 32.85  ? 677 HOH A O   1 
HETATM 2467 O  O   . HOH H 6 .   ? 1.553   3.145   -4.899  1.00 39.54  ? 678 HOH A O   1 
HETATM 2468 O  O   . HOH H 6 .   ? -10.619 -20.410 24.959  1.00 21.02  ? 679 HOH A O   1 
HETATM 2469 O  O   . HOH H 6 .   ? 1.981   -14.191 20.491  1.00 33.99  ? 680 HOH A O   1 
HETATM 2470 O  O   . HOH H 6 .   ? -21.288 -20.649 14.520  1.00 31.72  ? 681 HOH A O   1 
HETATM 2471 O  O   . HOH H 6 .   ? -12.303 13.462  4.886   1.00 36.61  ? 682 HOH A O   1 
HETATM 2472 O  O   . HOH H 6 .   ? -11.674 10.741  0.734   1.00 27.77  ? 683 HOH A O   1 
HETATM 2473 O  O   . HOH H 6 .   ? -12.882 18.889  8.487   1.00 28.90  ? 684 HOH A O   1 
HETATM 2474 O  O   . HOH H 6 .   ? -1.260  -11.201 29.006  1.00 19.24  ? 685 HOH A O   1 
HETATM 2475 O  O   . HOH H 6 .   ? -0.291  -7.033  -7.397  1.00 47.12  ? 686 HOH A O   1 
HETATM 2476 O  O   . HOH H 6 .   ? 6.356   -5.677  3.419   1.00 38.20  ? 687 HOH A O   1 
HETATM 2477 O  O   . HOH H 6 .   ? -4.043  -15.564 -2.352  1.00 32.80  ? 688 HOH A O   1 
HETATM 2478 O  O   . HOH H 6 .   ? 12.361  3.906   27.326  1.00 35.78  ? 689 HOH A O   1 
HETATM 2479 O  O   . HOH H 6 .   ? 6.302   5.351   29.006  1.00 39.28  ? 690 HOH A O   1 
HETATM 2480 O  O   . HOH H 6 .   ? -26.866 -1.319  25.918  1.00 22.80  ? 691 HOH A O   1 
HETATM 2481 O  O   . HOH H 6 .   ? 6.563   8.357   18.021  1.00 31.19  ? 692 HOH A O   1 
HETATM 2482 O  O   . HOH H 6 .   ? 4.046   -11.873 23.229  1.00 44.62  ? 693 HOH A O   1 
HETATM 2483 O  O   . HOH H 6 .   ? -12.970 -19.594 26.114  1.00 24.75  ? 694 HOH A O   1 
HETATM 2484 O  O   . HOH H 6 .   ? -14.051 3.537   33.193  1.00 27.12  ? 695 HOH A O   1 
HETATM 2485 O  O   . HOH H 6 .   ? -2.499  -9.189  34.668  1.00 44.08  ? 696 HOH A O   1 
HETATM 2486 O  O   . HOH H 6 .   ? 14.931  -6.712  7.840   1.00 37.00  ? 697 HOH A O   1 
HETATM 2487 O  O   . HOH H 6 .   ? -0.555  11.901  13.894  1.00 36.04  ? 698 HOH A O   1 
HETATM 2488 O  O   . HOH H 6 .   ? -3.506  -19.980 27.251  1.00 48.25  ? 699 HOH A O   1 
HETATM 2489 O  O   . HOH H 6 .   ? 5.369   9.063   21.889  1.00 31.56  ? 700 HOH A O   1 
HETATM 2490 O  O   . HOH H 6 .   ? 14.118  -1.517  28.435  1.00 30.24  ? 701 HOH A O   1 
HETATM 2491 O  O   . HOH H 6 .   ? -7.144  -24.408 10.598  1.00 33.74  ? 702 HOH A O   1 
HETATM 2492 O  O   . HOH H 6 .   ? -6.426  12.253  10.232  1.00 40.40  ? 703 HOH A O   1 
HETATM 2493 O  O   . HOH H 6 .   ? 3.762   9.750   23.820  1.00 32.11  ? 704 HOH A O   1 
HETATM 2494 O  O   . HOH H 6 .   ? 14.119  4.813   25.013  1.00 43.82  ? 705 HOH A O   1 
HETATM 2495 O  O   . HOH H 6 .   ? -11.989 13.670  1.990   1.00 38.57  ? 706 HOH A 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 4   ? 0.2469 0.5170 0.4684 0.0438  0.0900  0.1683  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.2911 0.3158 0.4526 -0.0403 0.1536  0.1066  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.3151 0.2630 0.2694 -0.0564 0.1045  0.0209  4   HIS A C   
4    O  O   . HIS A 4   ? 0.2752 0.2745 0.3241 0.0063  0.0951  0.0082  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.3058 0.5460 0.7070 0.0472  0.1613  0.2642  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.4799 0.4811 0.7124 -0.1268 0.2399  0.0012  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.3240 1.1346 1.1700 0.1884  -0.1658 -0.1395 4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.4631 0.9128 0.6589 -0.2624 -0.0395 0.1925  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 1.1533 0.9412 1.2411 0.1703  -0.2657 -0.0186 4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 1.2589 0.9588 1.0311 -0.0130 -0.0491 0.5213  4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.1606 0.2590 0.2518 -0.0320 0.0333  0.0093  5   TRP A N   
12   C  CA  . TRP A 5   ? 0.1600 0.2277 0.1895 -0.0388 0.0454  -0.0019 5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1844 0.2056 0.1985 -0.0137 0.0357  -0.0174 5   TRP A C   
14   O  O   . TRP A 5   ? 0.1923 0.2345 0.2530 -0.0342 0.0386  0.0156  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1691 0.1938 0.2056 -0.0205 0.0187  -0.0041 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1667 0.1682 0.1781 -0.0294 0.0147  0.0020  5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.2054 0.1806 0.1972 -0.0146 0.0281  0.0164  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1492 0.1923 0.1577 -0.0146 0.0285  -0.0153 5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.2228 0.1970 0.1876 -0.0077 0.0282  0.0232  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1548 0.2196 0.1776 0.0082  0.0109  0.0060  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1695 0.1967 0.1664 -0.0579 0.0412  -0.0359 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.1806 0.2415 0.1582 0.0104  -0.0043 -0.0097 5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1747 0.2125 0.1609 -0.0285 0.0379  -0.0394 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1991 0.2363 0.1747 -0.0130 0.0166  -0.0551 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1686 0.1895 0.1970 -0.0142 0.0478  -0.0296 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1920 0.1796 0.2028 -0.0350 0.0421  -0.0252 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1648 0.1904 0.1977 -0.0052 0.0619  0.0057  6   GLY A C   
28   O  O   . GLY A 6   ? 0.1580 0.1886 0.1946 -0.0142 0.0329  0.0010  6   GLY A O   
29   N  N   . TYR A 7   ? 0.1948 0.2029 0.2308 -0.0370 0.0661  -0.0181 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.1916 0.1746 0.3187 -0.0109 0.0860  0.0030  7   TYR A CA  
31   C  C   . TYR A 7   ? 0.2080 0.1912 0.5741 -0.0377 0.1422  -0.0527 7   TYR A C   
32   O  O   . TYR A 7   ? 0.3572 0.2116 0.9659 -0.0126 0.2150  -0.0098 7   TYR A O   
33   C  CB  . TYR A 7   ? 0.1532 0.2053 0.2712 -0.0151 0.0750  -0.0196 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1422 0.1657 0.1837 -0.0335 0.0244  -0.0126 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.1315 0.1684 0.1755 -0.0318 0.0220  -0.0204 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.1668 0.1591 0.2018 -0.0450 0.0188  -0.0076 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.1252 0.1485 0.1686 -0.0392 0.0109  -0.0093 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.1528 0.1886 0.1483 -0.0392 0.0288  -0.0241 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.1289 0.1618 0.1509 -0.0439 0.0195  -0.0265 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.1519 0.1715 0.1641 -0.0124 0.0104  -0.0152 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.2442 0.1875 0.4731 -0.0487 0.1474  -0.0821 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.2641 0.2124 0.6312 -0.0657 0.1348  -0.0948 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.2770 0.2537 0.3881 0.0555  0.1254  -0.0597 8   GLY A C   
44   O  O   . GLY A 8   ? 0.2605 0.3191 0.5030 -0.0137 0.2084  -0.0068 8   GLY A O   
45   N  N   . LYS A 9   ? 0.2774 0.1419 0.9775 0.0306  0.1675  -0.0057 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.4466 0.2301 0.7286 -0.0052 0.0644  -0.0544 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.3065 0.5270 0.4983 -0.1598 0.0498  0.1035  9   LYS A C   
48   O  O   . LYS A 9   ? 0.2615 0.2814 0.6740 0.0522  0.0361  -0.1286 9   LYS A O   
49   C  CB  . LYS A 9   ? 0.4857 0.4203 1.0335 0.1554  0.0427  0.1172  9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.4670 0.3205 0.7404 0.0930  0.0208  -0.0114 9   LYS A CG  
51   N  NZ  . LYS A 9   ? 1.3811 0.4857 0.8223 -0.1013 -0.4230 0.2268  9   LYS A NZ  
52   N  N   . HIS A 10  ? 0.1623 0.2207 0.3858 0.0260  0.0807  0.0054  10  HIS A N   
53   C  CA  . HIS A 10  ? 0.1555 0.3014 0.2791 0.0164  0.0331  -0.0662 10  HIS A CA  
54   C  C   . HIS A 10  ? 0.1803 0.2652 0.2824 0.0436  0.0588  0.0297  10  HIS A C   
55   O  O   . HIS A 10  ? 0.1476 0.3525 0.3798 0.0379  0.0487  -0.0913 10  HIS A O   
56   C  CB  . HIS A 10  ? 0.2013 0.2832 0.3033 0.0405  0.0996  -0.0463 10  HIS A CB  
57   C  CG  . HIS A 10  ? 0.1693 0.3094 0.2469 -0.0438 0.0177  -0.0450 10  HIS A CG  
58   N  ND1 . HIS A 10  ? 0.2354 0.3125 0.2961 0.0653  0.0175  -0.0063 10  HIS A ND1 
59   C  CD2 . HIS A 10  ? 0.2727 0.3238 0.3111 0.0091  0.0076  -0.1044 10  HIS A CD2 
60   C  CE1 . HIS A 10  ? 0.1912 0.2169 0.2889 0.0194  0.0427  -0.0303 10  HIS A CE1 
61   N  NE2 . HIS A 10  ? 0.3209 0.3531 0.3600 0.0566  0.0071  -0.1615 10  HIS A NE2 
62   N  N   . ASN A 11  ? 0.1814 0.2386 0.2839 0.0264  0.1036  -0.0031 11  ASN A N   
63   C  CA  . ASN A 11  ? 0.1589 0.2435 0.2361 0.0348  0.0794  -0.0076 11  ASN A CA  
64   C  C   . ASN A 11  ? 0.1440 0.2158 0.1995 0.0229  0.0351  -0.0088 11  ASN A C   
65   O  O   . ASN A 11  ? 0.1580 0.2054 0.2302 0.0142  0.0683  -0.0054 11  ASN A O   
66   C  CB  . ASN A 11  ? 0.1685 0.2331 0.2231 0.0166  0.0697  0.0076  11  ASN A CB  
67   C  CG  . ASN A 11  ? 0.2029 0.2299 0.2345 0.0000  0.0493  -0.0436 11  ASN A CG  
68   O  OD1 . ASN A 11  ? 0.2019 0.2304 0.2626 -0.0195 0.0454  -0.0046 11  ASN A OD1 
69   N  ND2 . ASN A 11  ? 0.2476 0.2540 0.2949 0.0003  0.0500  0.0283  11  ASN A ND2 
70   N  N   . GLY A 12  ? 0.1571 0.2248 0.2223 -0.0074 0.0705  0.0034  12  GLY A N   
71   C  CA  . GLY A 12  ? 0.1492 0.2212 0.1961 0.0294  0.0553  -0.0103 12  GLY A CA  
72   C  C   . GLY A 12  ? 0.1440 0.1525 0.2126 0.0087  0.0412  0.0284  12  GLY A C   
73   O  O   . GLY A 12  ? 0.1169 0.1665 0.2458 0.0253  0.0131  0.0082  12  GLY A O   
74   N  N   . PRO A 13  ? 0.1289 0.1582 0.1781 0.0031  0.0306  0.0020  13  PRO A N   
75   C  CA  . PRO A 13  ? 0.1263 0.1764 0.2063 -0.0082 0.0258  -0.0175 13  PRO A CA  
76   C  C   . PRO A 13  ? 0.1567 0.1510 0.1717 -0.0109 0.0271  0.0065  13  PRO A C   
77   O  O   . PRO A 13  ? 0.1163 0.1889 0.2146 -0.0107 0.0184  -0.0178 13  PRO A O   
78   C  CB  . PRO A 13  ? 0.1667 0.1873 0.1914 -0.0507 0.0494  -0.0197 13  PRO A CB  
79   C  CG  . PRO A 13  ? 0.1367 0.1623 0.2020 -0.0192 0.0403  -0.0255 13  PRO A CG  
80   C  CD  . PRO A 13  ? 0.1374 0.1902 0.2013 -0.0043 0.0423  0.0000  13  PRO A CD  
81   N  N   . GLU A 14  ? 0.1588 0.1603 0.2119 0.0063  0.0170  0.0129  14  GLU A N   
82   C  CA  . GLU A 14  ? 0.2207 0.1588 0.2302 0.0109  0.0211  0.0227  14  GLU A CA  
83   C  C   . GLU A 14  ? 0.1136 0.2087 0.2372 0.0553  -0.0249 0.0098  14  GLU A C   
84   O  O   . GLU A 14  ? 0.1846 0.1882 0.2478 0.0386  -0.0043 0.0285  14  GLU A O   
85   C  CB  . GLU A 14  ? 0.3614 0.1821 0.3230 0.0383  -0.0432 0.0252  14  GLU A CB  
86   C  CG  . GLU A 14  ? 0.3123 0.3636 0.3488 -0.0590 -0.0131 0.0175  14  GLU A CG  
87   C  CD  . GLU A 14  ? 0.2533 0.5350 0.3783 0.1221  -0.0590 -0.0186 14  GLU A CD  
88   O  OE1 . GLU A 14  ? 0.2501 0.2867 0.3955 0.1171  -0.0847 -0.1216 14  GLU A OE1 
89   O  OE2 . GLU A 14  ? 0.4763 0.1885 0.3977 0.0141  0.0199  -0.0175 14  GLU A OE2 
90   N  N   . HIS A 15  ? 0.1431 0.1499 0.2264 0.0208  0.0274  0.0048  15  HIS A N   
91   C  CA  . HIS A 15  ? 0.1045 0.1571 0.2456 0.0254  -0.0015 0.0086  15  HIS A CA  
92   C  C   . HIS A 15  ? 0.0926 0.1643 0.2205 0.0162  0.0181  -0.0006 15  HIS A C   
93   O  O   . HIS A 15  ? 0.0996 0.1679 0.2587 0.0156  0.0121  0.0182  15  HIS A O   
94   C  CB  . HIS A 15  ? 0.1237 0.1905 0.2620 0.0566  0.0177  0.0137  15  HIS A CB  
95   C  CG  . HIS A 15  ? 0.1727 0.1993 0.2785 0.0303  0.0439  -0.0027 15  HIS A CG  
96   N  ND1 . HIS A 15  ? 0.1650 0.2713 0.3417 0.0753  0.0250  -0.0164 15  HIS A ND1 
97   C  CD2 . HIS A 15  ? 0.2161 0.1794 0.2960 0.0705  0.0104  -0.0102 15  HIS A CD2 
98   C  CE1 . HIS A 15  ? 0.3284 0.3140 0.4028 0.1449  -0.0304 -0.1289 15  HIS A CE1 
99   N  NE2 . HIS A 15  ? 0.2820 0.2299 0.3923 0.1063  0.0434  -0.0799 15  HIS A NE2 
100  N  N   . TRP A 16  ? 0.0894 0.1481 0.2417 0.0221  0.0023  0.0098  16  TRP A N   
101  C  CA  . TRP A 16  ? 0.0709 0.1345 0.2354 0.0120  -0.0049 -0.0146 16  TRP A CA  
102  C  C   . TRP A 16  ? 0.1031 0.1607 0.2038 0.0120  0.0031  -0.0023 16  TRP A C   
103  O  O   . TRP A 16  ? 0.1124 0.1455 0.2353 0.0035  -0.0124 0.0068  16  TRP A O   
104  C  CB  . TRP A 16  ? 0.0746 0.1632 0.1914 0.0175  -0.0006 -0.0120 16  TRP A CB  
105  C  CG  . TRP A 16  ? 0.0974 0.1314 0.1754 -0.0186 0.0020  -0.0115 16  TRP A CG  
106  C  CD1 . TRP A 16  ? 0.1255 0.1740 0.1471 0.0037  0.0131  0.0162  16  TRP A CD1 
107  C  CD2 . TRP A 16  ? 0.0953 0.1455 0.1880 -0.0026 0.0137  -0.0091 16  TRP A CD2 
108  N  NE1 . TRP A 16  ? 0.1275 0.1641 0.1803 -0.0121 0.0296  -0.0170 16  TRP A NE1 
109  C  CE2 . TRP A 16  ? 0.1169 0.1474 0.1699 0.0068  0.0082  0.0164  16  TRP A CE2 
110  C  CE3 . TRP A 16  ? 0.1023 0.1280 0.1932 0.0003  0.0185  0.0052  16  TRP A CE3 
111  C  CZ2 . TRP A 16  ? 0.1115 0.1339 0.1700 -0.0109 0.0153  0.0000  16  TRP A CZ2 
112  C  CZ3 . TRP A 16  ? 0.0965 0.1413 0.1673 -0.0013 0.0162  -0.0027 16  TRP A CZ3 
113  C  CH2 . TRP A 16  ? 0.1430 0.1192 0.1801 0.0099  0.0253  0.0000  16  TRP A CH2 
114  N  N   . HIS A 17  ? 0.0864 0.1587 0.1991 -0.0085 -0.0194 -0.0088 17  HIS A N   
115  C  CA  . HIS A 17  ? 0.0886 0.1761 0.2031 -0.0175 -0.0199 0.0077  17  HIS A CA  
116  C  C   . HIS A 17  ? 0.0948 0.1882 0.2222 -0.0121 -0.0225 0.0074  17  HIS A C   
117  O  O   . HIS A 17  ? 0.1001 0.1785 0.2548 -0.0060 -0.0239 0.0035  17  HIS A O   
118  C  CB  . HIS A 17  ? 0.0900 0.2113 0.2065 0.0227  -0.0309 0.0041  17  HIS A CB  
119  C  CG  . HIS A 17  ? 0.0966 0.2011 0.2465 -0.0027 -0.0288 0.0333  17  HIS A CG  
120  N  ND1 . HIS A 17  ? 0.1262 0.2035 0.2807 0.0057  -0.0410 0.0377  17  HIS A ND1 
121  C  CD2 . HIS A 17  ? 0.1279 0.1833 0.2770 0.0434  0.0007  0.0507  17  HIS A CD2 
122  C  CE1 . HIS A 17  ? 0.1506 0.2316 0.2656 0.0601  -0.0114 0.0395  17  HIS A CE1 
123  N  NE2 . HIS A 17  ? 0.1374 0.2225 0.2827 0.0428  -0.0015 0.0493  17  HIS A NE2 
124  N  N   . LYS A 18  ? 0.0917 0.1888 0.2518 -0.0086 -0.0037 0.0076  18  LYS A N   
125  C  CA  . LYS A 18  ? 0.0996 0.1972 0.2875 -0.0151 -0.0048 0.0221  18  LYS A CA  
126  C  C   . LYS A 18  ? 0.1361 0.1895 0.2526 -0.0129 -0.0175 0.0270  18  LYS A C   
127  O  O   . LYS A 18  ? 0.1582 0.2153 0.3959 -0.0460 -0.0898 0.0570  18  LYS A O   
128  C  CB  . LYS A 18  ? 0.1053 0.2256 0.2767 -0.0027 -0.0015 0.0383  18  LYS A CB  
129  C  CG  . LYS A 18  ? 0.1254 0.2277 0.3215 0.0723  0.0318  0.0392  18  LYS A CG  
130  C  CD  . LYS A 18  ? 0.1307 0.2361 0.2736 0.0337  -0.0041 0.0469  18  LYS A CD  
131  C  CE  . LYS A 18  ? 0.1589 0.2149 0.2723 0.0252  -0.0270 0.0450  18  LYS A CE  
132  N  NZ  . LYS A 18  ? 0.1140 0.2702 0.3065 0.0772  0.0026  0.0307  18  LYS A NZ  
133  N  N   . ASP A 19  ? 0.1172 0.1831 0.2406 0.0174  -0.0052 0.0071  19  ASP A N   
134  C  CA  . ASP A 19  ? 0.1257 0.1641 0.2584 -0.0026 -0.0041 -0.0013 19  ASP A CA  
135  C  C   . ASP A 19  ? 0.1194 0.1613 0.2626 0.0175  -0.0031 0.0019  19  ASP A C   
136  O  O   . ASP A 19  ? 0.1618 0.1476 0.3241 -0.0065 0.0346  0.0275  19  ASP A O   
137  C  CB  . ASP A 19  ? 0.1510 0.2433 0.2189 0.0368  -0.0148 0.0296  19  ASP A CB  
138  C  CG  . ASP A 19  ? 0.2939 0.2311 0.3140 0.0020  0.1071  -0.0074 19  ASP A CG  
139  O  OD1 . ASP A 19  ? 0.2108 0.2605 0.3445 0.0298  0.0096  0.0333  19  ASP A OD1 
140  O  OD2 . ASP A 19  ? 0.2781 0.3112 0.4067 0.1168  0.0419  -0.0151 19  ASP A OD2 
141  N  N   . PHE A 20  ? 0.0878 0.1867 0.2505 -0.0043 -0.0161 0.0241  20  PHE A N   
142  C  CA  . PHE A 20  ? 0.1000 0.1823 0.2494 -0.0070 -0.0137 0.0000  20  PHE A CA  
143  C  C   . PHE A 20  ? 0.0785 0.1787 0.2468 0.0000  -0.0031 -0.0063 20  PHE A C   
144  O  O   . PHE A 20  ? 0.1054 0.1639 0.2345 -0.0114 -0.0098 0.0012  20  PHE A O   
145  C  CB  . PHE A 20  ? 0.1221 0.1641 0.2286 -0.0153 0.0041  0.0082  20  PHE A CB  
146  C  CG  . PHE A 20  ? 0.1142 0.1722 0.2275 -0.0439 0.0068  0.0219  20  PHE A CG  
147  C  CD1 . PHE A 20  ? 0.1368 0.2010 0.2630 -0.0381 0.0129  0.0531  20  PHE A CD1 
148  C  CD2 . PHE A 20  ? 0.1093 0.2316 0.2566 -0.0216 0.0155  0.0065  20  PHE A CD2 
149  C  CE1 . PHE A 20  ? 0.1275 0.2620 0.2580 -0.0386 0.0097  0.0540  20  PHE A CE1 
150  C  CE2 . PHE A 20  ? 0.1261 0.2465 0.2518 0.0093  0.0065  0.0233  20  PHE A CE2 
151  C  CZ  . PHE A 20  ? 0.1155 0.2666 0.2791 -0.0219 0.0098  0.0502  20  PHE A CZ  
152  N  N   . PRO A 21  ? 0.1273 0.1934 0.2342 -0.0277 -0.0104 -0.0017 21  PRO A N   
153  C  CA  . PRO A 21  ? 0.1077 0.2249 0.2108 -0.0372 -0.0156 0.0054  21  PRO A CA  
154  C  C   . PRO A 21  ? 0.1045 0.1840 0.2379 -0.0258 -0.0306 -0.0096 21  PRO A C   
155  O  O   . PRO A 21  ? 0.1041 0.1958 0.2250 -0.0104 -0.0399 -0.0007 21  PRO A O   
156  C  CB  . PRO A 21  ? 0.1212 0.3029 0.3090 -0.0988 -0.0709 0.0346  21  PRO A CB  
157  C  CG  . PRO A 21  ? 0.2713 0.3108 0.3402 -0.1118 -0.1172 0.0263  21  PRO A CG  
158  C  CD  . PRO A 21  ? 0.1419 0.1973 0.3057 -0.0480 -0.0296 0.0377  21  PRO A CD  
159  N  N   A ILE A 22  ? 0.0913 0.1564 0.2415 -0.0143 -0.0333 -0.0317 22  ILE A N   
160  N  N   B ILE A 22  ? 0.0895 0.1571 0.2458 -0.0142 -0.0322 -0.0328 22  ILE A N   
161  C  CA  A ILE A 22  ? 0.0908 0.1815 0.2257 -0.0129 -0.0274 -0.0142 22  ILE A CA  
162  C  CA  B ILE A 22  ? 0.0900 0.1800 0.2268 -0.0124 -0.0261 -0.0148 22  ILE A CA  
163  C  C   A ILE A 22  ? 0.1004 0.1625 0.1819 -0.0146 -0.0237 -0.0175 22  ILE A C   
164  C  C   B ILE A 22  ? 0.1004 0.1611 0.1810 -0.0136 -0.0251 -0.0166 22  ILE A C   
165  O  O   A ILE A 22  ? 0.0966 0.1485 0.2222 -0.0046 -0.0093 -0.0077 22  ILE A O   
166  O  O   B ILE A 22  ? 0.0956 0.1512 0.2284 -0.0049 -0.0082 -0.0076 22  ILE A O   
167  C  CB  A ILE A 22  ? 0.1097 0.1553 0.2061 -0.0113 -0.0282 -0.0192 22  ILE A CB  
168  C  CB  B ILE A 22  ? 0.1169 0.1684 0.2142 0.0017  -0.0307 -0.0210 22  ILE A CB  
169  C  CG1 A ILE A 22  ? 0.1307 0.1810 0.2435 0.0000  -0.0241 -0.0715 22  ILE A CG1 
170  C  CG1 B ILE A 22  ? 0.1187 0.2040 0.2853 -0.0093 -0.0109 -0.0573 22  ILE A CG1 
171  C  CG2 A ILE A 22  ? 0.1115 0.1782 0.2192 -0.0288 -0.0485 -0.0087 22  ILE A CG2 
172  C  CG2 B ILE A 22  ? 0.1181 0.1650 0.2155 -0.0006 -0.0513 0.0000  22  ILE A CG2 
173  C  CD1 A ILE A 22  ? 0.1088 0.1735 0.2379 -0.0040 -0.0043 -0.0370 22  ILE A CD1 
174  C  CD1 B ILE A 22  ? 0.2228 0.2627 0.2446 0.0390  -0.0390 -0.0346 22  ILE A CD1 
175  N  N   . ALA A 23  ? 0.0996 0.1615 0.2028 -0.0217 -0.0194 -0.0192 23  ALA A N   
176  C  CA  . ALA A 23  ? 0.1000 0.1467 0.2078 -0.0238 0.0013  -0.0071 23  ALA A CA  
177  C  C   . ALA A 23  ? 0.0920 0.1620 0.2148 -0.0015 -0.0163 -0.0238 23  ALA A C   
178  O  O   . ALA A 23  ? 0.1146 0.1518 0.1878 -0.0087 -0.0006 -0.0096 23  ALA A O   
179  C  CB  . ALA A 23  ? 0.0921 0.1600 0.2282 0.0099  -0.0208 -0.0218 23  ALA A CB  
180  N  N   . LYS A 24  ? 0.1368 0.1825 0.1895 0.0006  -0.0263 0.0027  24  LYS A N   
181  C  CA  . LYS A 24  ? 0.1027 0.2247 0.1853 -0.0063 -0.0324 -0.0057 24  LYS A CA  
182  C  C   . LYS A 24  ? 0.1412 0.2407 0.1977 -0.0260 -0.0388 -0.0244 24  LYS A C   
183  O  O   . LYS A 24  ? 0.1706 0.2526 0.2155 0.0038  -0.0395 0.0000  24  LYS A O   
184  C  CB  . LYS A 24  ? 0.1122 0.2204 0.2476 0.0181  -0.0386 0.0104  24  LYS A CB  
185  C  CG  . LYS A 24  ? 0.1639 0.2548 0.2283 0.0643  -0.0205 0.0283  24  LYS A CG  
186  C  CD  . LYS A 24  ? 0.1736 0.3043 0.3334 0.0754  -0.0087 0.0362  24  LYS A CD  
187  C  CE  . LYS A 24  ? 0.2397 0.3651 0.3611 0.0834  0.0597  0.0559  24  LYS A CE  
188  N  NZ  . LYS A 24  ? 0.4386 0.3725 0.6836 0.1185  0.1722  0.0768  24  LYS A NZ  
189  N  N   . GLY A 25  ? 0.1251 0.1981 0.2031 -0.0020 -0.0241 -0.0241 25  GLY A N   
190  C  CA  . GLY A 25  ? 0.1385 0.2268 0.2350 -0.0304 -0.0113 -0.0307 25  GLY A CA  
191  C  C   . GLY A 25  ? 0.1406 0.2122 0.1519 -0.0015 -0.0328 -0.0287 25  GLY A C   
192  O  O   . GLY A 25  ? 0.1485 0.2128 0.1834 -0.0006 -0.0303 -0.0285 25  GLY A O   
193  N  N   . GLU A 26  ? 0.1343 0.2342 0.1661 0.0003  -0.0540 -0.0434 26  GLU A N   
194  C  CA  . GLU A 26  ? 0.1600 0.2566 0.1485 0.0142  -0.0507 -0.0186 26  GLU A CA  
195  C  C   . GLU A 26  ? 0.1500 0.2099 0.1494 0.0109  -0.0331 -0.0181 26  GLU A C   
196  O  O   . GLU A 26  ? 0.1835 0.2377 0.1385 -0.0107 -0.0533 -0.0024 26  GLU A O   
197  C  CB  . GLU A 26  ? 0.2230 0.3553 0.1747 -0.0375 -0.0854 -0.0978 26  GLU A CB  
198  C  CG  . GLU A 26  ? 0.2261 0.3345 0.2257 -0.0161 -0.0520 -0.0361 26  GLU A CG  
199  C  CD  . GLU A 26  ? 0.2957 0.4717 0.3079 0.0185  -0.1387 -0.0357 26  GLU A CD  
200  O  OE1 . GLU A 26  ? 0.4340 0.4017 0.3945 0.0020  -0.1278 0.0197  26  GLU A OE1 
201  O  OE2 . GLU A 26  ? 0.2748 0.7023 0.5486 0.1422  -0.1808 -0.0390 26  GLU A OE2 
202  N  N   . ARG A 27  ? 0.1259 0.1512 0.1573 0.0041  -0.0494 -0.0241 27  ARG A N   
203  C  CA  . ARG A 27  ? 0.1004 0.1615 0.1312 0.0171  -0.0272 -0.0098 27  ARG A CA  
204  C  C   . ARG A 27  ? 0.1118 0.1291 0.1278 -0.0057 -0.0178 -0.0170 27  ARG A C   
205  O  O   . ARG A 27  ? 0.1005 0.1476 0.1300 0.0114  -0.0324 -0.0124 27  ARG A O   
206  C  CB  . ARG A 27  ? 0.1864 0.1553 0.1589 0.0003  -0.0252 -0.0326 27  ARG A CB  
207  C  CG  . ARG A 27  ? 0.2171 0.2307 0.1600 -0.0057 -0.0182 -0.0277 27  ARG A CG  
208  C  CD  . ARG A 27  ? 0.2874 0.2967 0.1938 0.0934  -0.0662 -0.0337 27  ARG A CD  
209  N  NE  . ARG A 27  ? 0.2020 0.2079 0.1702 -0.0043 0.0131  -0.0030 27  ARG A NE  
210  C  CZ  . ARG A 27  ? 0.1817 0.2126 0.1422 0.0273  -0.0099 -0.0060 27  ARG A CZ  
211  N  NH1 . ARG A 27  ? 0.1895 0.2742 0.2029 0.0308  -0.0208 -0.1181 27  ARG A NH1 
212  N  NH2 . ARG A 27  ? 0.1909 0.1977 0.1928 -0.0166 -0.0206 -0.0283 27  ARG A NH2 
213  N  N   . GLN A 28  ? 0.0975 0.1327 0.1215 0.0068  -0.0252 -0.0164 28  GLN A N   
214  C  CA  . GLN A 28  ? 0.0926 0.1348 0.1181 0.0003  -0.0164 -0.0208 28  GLN A CA  
215  C  C   . GLN A 28  ? 0.1005 0.1178 0.1167 0.0006  0.0017  0.0019  28  GLN A C   
216  O  O   . GLN A 28  ? 0.1201 0.1440 0.1049 -0.0087 -0.0184 -0.0031 28  GLN A O   
217  C  CB  . GLN A 28  ? 0.1004 0.1381 0.1400 0.0003  -0.0115 -0.0153 28  GLN A CB  
218  C  CG  . GLN A 28  ? 0.1032 0.1539 0.1413 0.0015  -0.0171 -0.0110 28  GLN A CG  
219  C  CD  . GLN A 28  ? 0.1027 0.1560 0.1370 0.0005  -0.0320 -0.0253 28  GLN A CD  
220  O  OE1 . GLN A 28  ? 0.0978 0.1342 0.1492 -0.0177 -0.0087 -0.0165 28  GLN A OE1 
221  N  NE2 . GLN A 28  ? 0.0899 0.1278 0.1571 -0.0051 -0.0159 -0.0109 28  GLN A NE2 
222  N  N   . SER A 29  ? 0.0913 0.1146 0.1084 0.0087  -0.0153 -0.0098 29  SER A N   
223  C  CA  . SER A 29  ? 0.0881 0.1027 0.1221 0.0051  -0.0109 -0.0228 29  SER A CA  
224  C  C   . SER A 29  ? 0.0865 0.1133 0.1137 0.0017  -0.0071 0.0203  29  SER A C   
225  O  O   . SER A 29  ? 0.0995 0.1115 0.1251 -0.0010 0.0005  -0.0013 29  SER A O   
226  C  CB  . SER A 29  ? 0.0856 0.1300 0.1169 0.0080  -0.0110 -0.0186 29  SER A CB  
227  O  OG  . SER A 29  ? 0.0926 0.1093 0.1239 -0.0054 0.0000  -0.0087 29  SER A OG  
228  N  N   . PRO A 30  ? 0.0872 0.1149 0.1086 -0.0003 -0.0059 -0.0057 30  PRO A N   
229  C  CA  . PRO A 30  ? 0.0832 0.1014 0.1246 -0.0054 -0.0093 0.0091  30  PRO A CA  
230  C  C   . PRO A 30  ? 0.0869 0.1099 0.1088 0.0035  -0.0103 0.0017  30  PRO A C   
231  O  O   . PRO A 30  ? 0.0908 0.1221 0.1203 0.0087  -0.0118 -0.0038 30  PRO A O   
232  C  CB  . PRO A 30  ? 0.0881 0.1081 0.1216 0.0024  -0.0142 -0.0197 30  PRO A CB  
233  C  CG  . PRO A 30  ? 0.0983 0.1196 0.1242 -0.0041 -0.0137 -0.0091 30  PRO A CG  
234  C  CD  . PRO A 30  ? 0.0925 0.1342 0.1169 -0.0020 0.0135  -0.0187 30  PRO A CD  
235  N  N   . VAL A 31  ? 0.1090 0.1178 0.1045 0.0082  0.0005  0.0085  31  VAL A N   
236  C  CA  . VAL A 31  ? 0.1027 0.1375 0.0885 0.0000  -0.0049 0.0120  31  VAL A CA  
237  C  C   . VAL A 31  ? 0.1049 0.1351 0.1154 0.0318  -0.0108 0.0121  31  VAL A C   
238  O  O   . VAL A 31  ? 0.1075 0.1239 0.1361 0.0070  -0.0197 0.0142  31  VAL A O   
239  C  CB  . VAL A 31  ? 0.1271 0.1356 0.1185 0.0098  -0.0219 -0.0146 31  VAL A CB  
240  C  CG1 . VAL A 31  ? 0.1440 0.1257 0.1388 -0.0228 0.0030  -0.0126 31  VAL A CG1 
241  C  CG2 . VAL A 31  ? 0.1140 0.1361 0.1519 0.0103  0.0152  -0.0092 31  VAL A CG2 
242  N  N   . ASP A 32  ? 0.1248 0.1124 0.1246 0.0110  -0.0196 0.0120  32  ASP A N   
243  C  CA  . ASP A 32  ? 0.1272 0.1158 0.1309 0.0141  0.0006  -0.0124 32  ASP A CA  
244  C  C   . ASP A 32  ? 0.1413 0.1360 0.1097 0.0015  -0.0252 -0.0013 32  ASP A C   
245  O  O   . ASP A 32  ? 0.1336 0.1650 0.1363 0.0052  -0.0164 -0.0109 32  ASP A O   
246  C  CB  . ASP A 32  ? 0.1561 0.1228 0.1395 0.0230  -0.0027 0.0164  32  ASP A CB  
247  C  CG  . ASP A 32  ? 0.1421 0.1524 0.1242 0.0208  -0.0119 -0.0010 32  ASP A CG  
248  O  OD1 . ASP A 32  ? 0.1474 0.1304 0.1410 0.0118  -0.0238 0.0142  32  ASP A OD1 
249  O  OD2 . ASP A 32  ? 0.2365 0.1679 0.1286 -0.0239 -0.0174 0.0230  32  ASP A OD2 
250  N  N   . ILE A 33  ? 0.1224 0.1154 0.1192 0.0043  -0.0017 0.0098  33  ILE A N   
251  C  CA  . ILE A 33  ? 0.1217 0.1456 0.1303 0.0153  0.0051  0.0163  33  ILE A CA  
252  C  C   . ILE A 33  ? 0.1706 0.1284 0.1176 0.0093  0.0264  0.0186  33  ILE A C   
253  O  O   . ILE A 33  ? 0.1697 0.1358 0.1539 0.0082  0.0148  0.0152  33  ILE A O   
254  C  CB  . ILE A 33  ? 0.1174 0.1185 0.1665 0.0093  0.0131  0.0115  33  ILE A CB  
255  C  CG1 . ILE A 33  ? 0.1332 0.1284 0.1560 0.0225  -0.0054 0.0230  33  ILE A CG1 
256  C  CG2 . ILE A 33  ? 0.1709 0.1749 0.1691 0.0274  0.0252  0.0031  33  ILE A CG2 
257  C  CD1 . ILE A 33  ? 0.1377 0.1880 0.1762 0.0166  -0.0176 0.0284  33  ILE A CD1 
258  N  N   A ASP A 34  ? 0.1898 0.1855 0.1242 0.0211  0.0118  0.0340  34  ASP A N   
259  N  N   B ASP A 34  ? 0.1712 0.1641 0.1111 0.0436  0.0261  0.0346  34  ASP A N   
260  C  CA  A ASP A 34  ? 0.2293 0.1510 0.1243 0.0397  0.0177  0.0204  34  ASP A CA  
261  C  CA  B ASP A 34  ? 0.2087 0.1479 0.1221 0.0412  0.0208  0.0355  34  ASP A CA  
262  C  C   A ASP A 34  ? 0.2169 0.1706 0.1571 0.0414  0.0361  0.0432  34  ASP A C   
263  C  C   B ASP A 34  ? 0.2020 0.1500 0.1239 0.0478  0.0450  0.0353  34  ASP A C   
264  O  O   A ASP A 34  ? 0.2192 0.2474 0.1842 0.0891  0.0130  0.0006  34  ASP A O   
265  O  O   B ASP A 34  ? 0.2544 0.1652 0.0838 0.0538  0.0557  0.0272  34  ASP A O   
266  C  CB  A ASP A 34  ? 0.2308 0.1448 0.1458 0.0872  0.0119  0.0017  34  ASP A CB  
267  C  CB  B ASP A 34  ? 0.2777 0.1887 0.1339 0.0086  -0.0186 0.0381  34  ASP A CB  
268  C  CG  A ASP A 34  ? 0.3197 0.1880 0.1731 0.0377  0.0337  0.0148  34  ASP A CG  
269  C  CG  B ASP A 34  ? 0.2037 0.2446 0.1627 0.0463  0.0151  0.0675  34  ASP A CG  
270  O  OD1 A ASP A 34  ? 0.3334 0.2378 0.2325 0.0710  0.0623  -0.0240 34  ASP A OD1 
271  O  OD1 B ASP A 34  ? 0.2255 0.1787 0.1333 0.0241  0.0049  0.0675  34  ASP A OD1 
272  O  OD2 A ASP A 34  ? 0.3895 0.2631 0.2000 0.1515  0.0297  0.0425  34  ASP A OD2 
273  O  OD2 B ASP A 34  ? 0.2572 0.3136 0.2083 0.0412  -0.0505 0.1102  34  ASP A OD2 
274  N  N   . THR A 35  ? 0.2158 0.1864 0.1657 0.0315  0.0432  0.0619  35  THR A N   
275  C  CA  . THR A 35  ? 0.2046 0.1943 0.1492 0.0491  0.0187  0.0359  35  THR A CA  
276  C  C   . THR A 35  ? 0.2245 0.1632 0.1527 0.0531  0.0353  0.0165  35  THR A C   
277  O  O   . THR A 35  ? 0.2810 0.2144 0.1972 0.0754  0.0513  0.0386  35  THR A O   
278  C  CB  . THR A 35  ? 0.2137 0.1993 0.2171 0.0296  0.0373  0.0340  35  THR A CB  
279  O  OG1 . THR A 35  ? 0.2694 0.2143 0.1964 0.0258  0.0631  0.0307  35  THR A OG1 
280  C  CG2 . THR A 35  ? 0.2115 0.2681 0.2069 0.0706  0.0318  0.0553  35  THR A CG2 
281  N  N   . HIS A 36  ? 0.2946 0.1880 0.1562 0.0649  0.0590  0.0653  36  HIS A N   
282  C  CA  . HIS A 36  ? 0.3054 0.2040 0.1454 0.0379  0.0377  0.0593  36  HIS A CA  
283  C  C   . HIS A 36  ? 0.3281 0.2576 0.1324 0.0357  0.0423  0.0093  36  HIS A C   
284  O  O   . HIS A 36  ? 0.2982 0.3151 0.1650 0.0798  -0.0019 0.0348  36  HIS A O   
285  C  CB  . HIS A 36  ? 0.4028 0.2515 0.1546 0.0326  0.0043  0.0865  36  HIS A CB  
286  C  CG  . HIS A 36  ? 0.3266 0.1952 0.1808 0.0573  -0.0296 0.0344  36  HIS A CG  
287  N  ND1 . HIS A 36  ? 0.3787 0.2433 0.2392 0.0162  -0.1120 0.0636  36  HIS A ND1 
288  C  CD2 . HIS A 36  ? 0.3417 0.2128 0.2381 0.0176  -0.0241 0.0326  36  HIS A CD2 
289  C  CE1 . HIS A 36  ? 0.4179 0.2286 0.3765 0.0346  -0.0684 0.0837  36  HIS A CE1 
290  N  NE2 . HIS A 36  ? 0.5404 0.4178 0.4099 -0.0819 -0.1203 -0.0573 36  HIS A NE2 
291  N  N   . THR A 37  ? 0.3240 0.1791 0.2184 0.0763  0.0603  0.0221  37  THR A N   
292  C  CA  . THR A 37  ? 0.3072 0.2064 0.1835 0.0966  0.0516  0.0573  37  THR A CA  
293  C  C   . THR A 37  ? 0.2627 0.2106 0.1607 0.0560  0.0436  0.0080  37  THR A C   
294  O  O   . THR A 37  ? 0.3470 0.2548 0.1871 0.0710  -0.0103 -0.0057 37  THR A O   
295  C  CB  . THR A 37  ? 0.3518 0.3054 0.2467 0.1413  0.0098  0.0728  37  THR A CB  
296  O  OG1 . THR A 37  ? 0.4875 0.2864 0.3000 0.1332  0.0208  0.0509  37  THR A OG1 
297  C  CG2 . THR A 37  ? 0.3568 0.2311 0.4146 0.1289  -0.0597 0.0285  37  THR A CG2 
298  N  N   . ALA A 38  ? 0.2888 0.2148 0.1379 0.0636  0.0379  0.0496  38  ALA A N   
299  C  CA  . ALA A 38  ? 0.2833 0.1790 0.1309 0.0653  0.0428  0.0081  38  ALA A CA  
300  C  C   . ALA A 38  ? 0.2695 0.2038 0.2272 0.0373  0.0754  0.0577  38  ALA A C   
301  O  O   . ALA A 38  ? 0.3837 0.2308 0.3669 0.0570  0.1677  0.0397  38  ALA A O   
302  C  CB  . ALA A 38  ? 0.2196 0.1955 0.1586 0.0463  0.0020  0.0020  38  ALA A CB  
303  N  N   A LYS A 39  ? 0.3033 0.2185 0.1782 0.1155  0.0206  0.0164  39  LYS A N   
304  N  N   B LYS A 39  ? 0.3061 0.2316 0.2046 0.1045  0.0373  0.0379  39  LYS A N   
305  C  CA  A LYS A 39  ? 0.2433 0.2663 0.1158 0.0566  -0.0221 -0.0076 39  LYS A CA  
306  C  CA  B LYS A 39  ? 0.2795 0.3244 0.1959 0.1503  0.0073  -0.0031 39  LYS A CA  
307  C  C   A LYS A 39  ? 0.2395 0.2392 0.1668 0.1076  0.0384  0.0281  39  LYS A C   
308  C  C   B LYS A 39  ? 0.2372 0.2343 0.1203 0.0878  0.0331  0.0093  39  LYS A C   
309  O  O   A LYS A 39  ? 0.2069 0.2541 0.1208 0.0266  0.0000  -0.0015 39  LYS A O   
310  O  O   B LYS A 39  ? 0.1733 0.2439 0.1404 0.0615  0.0109  0.0049  39  LYS A O   
311  C  CB  A LYS A 39  ? 0.2551 0.2404 0.1120 0.0241  0.0098  0.0375  39  LYS A CB  
312  C  CB  B LYS A 39  ? 0.1920 0.4293 0.1084 0.1599  -0.0310 0.0063  39  LYS A CB  
313  C  CG  A LYS A 39  ? 0.2150 0.3026 0.2238 0.1080  0.0060  0.0254  39  LYS A CG  
314  C  CG  B LYS A 39  ? 0.2110 0.3859 0.1142 0.1392  -0.0307 -0.0366 39  LYS A CG  
315  C  CD  A LYS A 39  ? 0.2458 0.2673 0.1896 -0.0206 -0.0309 -0.0692 39  LYS A CD  
316  C  CD  B LYS A 39  ? 0.2753 0.5302 0.0696 0.1668  -0.0812 -0.1172 39  LYS A CD  
317  C  CE  A LYS A 39  ? 0.2713 0.3941 0.1853 0.0052  0.1142  -0.0252 39  LYS A CE  
318  C  CE  B LYS A 39  ? 0.2748 0.6517 0.2450 0.1234  0.0649  -0.0296 39  LYS A CE  
319  N  NZ  A LYS A 39  ? 0.1773 0.4375 0.3988 0.0900  0.0076  0.2310  39  LYS A NZ  
320  N  NZ  B LYS A 39  ? 0.3614 0.9789 0.3105 0.1555  0.0551  0.2099  39  LYS A NZ  
321  N  N   . TYR A 40  ? 0.2766 0.2583 0.1588 0.0571  0.0671  0.0370  40  TYR A N   
322  C  CA  . TYR A 40  ? 0.2196 0.2318 0.1884 0.0236  0.0627  -0.0006 40  TYR A CA  
323  C  C   . TYR A 40  ? 0.2252 0.2602 0.1365 0.0115  0.0295  0.0159  40  TYR A C   
324  O  O   . TYR A 40  ? 0.2350 0.2918 0.1325 0.0546  0.0263  0.0012  40  TYR A O   
325  C  CB  . TYR A 40  ? 0.3036 0.3057 0.2071 -0.0560 0.0649  0.0309  40  TYR A CB  
326  C  CG  . TYR A 40  ? 0.2748 0.3751 0.2125 -0.0785 0.0891  0.0087  40  TYR A CG  
327  C  CD1 . TYR A 40  ? 0.2752 0.2803 0.2067 -0.0662 0.0340  -0.0065 40  TYR A CD1 
328  C  CD2 . TYR A 40  ? 0.3859 0.5651 0.2489 0.0198  0.1370  0.0186  40  TYR A CD2 
329  C  CE1 . TYR A 40  ? 0.3223 0.3985 0.2144 -0.0277 0.0430  -0.0406 40  TYR A CE1 
330  C  CE2 . TYR A 40  ? 0.2986 0.6007 0.2749 -0.0006 0.1102  -0.0081 40  TYR A CE2 
331  C  CZ  . TYR A 40  ? 0.1713 0.6226 0.2706 -0.0377 0.0351  -0.0086 40  TYR A CZ  
332  O  OH  . TYR A 40  ? 0.2480 0.5845 0.3306 0.0441  0.0432  -0.0507 40  TYR A OH  
333  N  N   . ASP A 41  ? 0.1712 0.2052 0.1864 0.0344  0.0333  0.0195  41  ASP A N   
334  C  CA  . ASP A 41  ? 0.1756 0.2222 0.1914 0.0098  -0.0020 0.0082  41  ASP A CA  
335  C  C   . ASP A 41  ? 0.1941 0.2968 0.1665 0.0307  0.0006  -0.0110 41  ASP A C   
336  O  O   . ASP A 41  ? 0.2155 0.2720 0.1877 0.0331  -0.0041 0.0000  41  ASP A O   
337  C  CB  . ASP A 41  ? 0.2320 0.2159 0.2899 -0.0099 -0.0175 0.0132  41  ASP A CB  
338  C  CG  . ASP A 41  ? 0.2886 0.2788 0.2311 -0.0625 0.0293  -0.0130 41  ASP A CG  
339  O  OD1 . ASP A 41  ? 0.3136 0.2964 0.2422 0.0071  -0.0103 -0.0606 41  ASP A OD1 
340  O  OD2 . ASP A 41  ? 0.2773 0.3531 0.3054 -0.0575 -0.0320 -0.0031 41  ASP A OD2 
341  N  N   . PRO A 42  ? 0.2089 0.3650 0.1961 0.0557  0.0562  0.0015  42  PRO A N   
342  C  CA  . PRO A 42  ? 0.2371 0.3557 0.2508 0.0719  0.0614  0.0274  42  PRO A CA  
343  C  C   . PRO A 42  ? 0.2831 0.3209 0.2738 0.1057  0.0900  0.0020  42  PRO A C   
344  O  O   . PRO A 42  ? 0.3460 0.5285 0.3240 0.1976  0.0944  0.0631  42  PRO A O   
345  C  CB  . PRO A 42  ? 0.3137 0.7307 0.3161 0.1049  0.1124  0.0900  42  PRO A CB  
346  C  CG  . PRO A 42  ? 0.3542 0.7605 0.2788 0.1429  0.0974  -0.0205 42  PRO A CG  
347  C  CD  . PRO A 42  ? 0.3324 0.3920 0.1889 0.1106  0.0859  0.0130  42  PRO A CD  
348  N  N   . SER A 43  ? 0.2799 0.3636 0.2090 0.1036  0.0449  -0.0243 43  SER A N   
349  C  CA  . SER A 43  ? 0.4013 0.3179 0.2874 0.0979  -0.0807 -0.0546 43  SER A CA  
350  C  C   . SER A 43  ? 0.2447 0.2949 0.2590 0.0671  -0.0593 -0.0557 43  SER A C   
351  O  O   . SER A 43  ? 0.5073 0.2946 0.3452 0.1932  -0.0555 -0.0124 43  SER A O   
352  C  CB  . SER A 43  ? 0.2809 0.2773 0.3183 0.0395  0.0006  -0.0667 43  SER A CB  
353  O  OG  . SER A 43  ? 0.3549 0.3323 0.3690 0.0549  -0.1036 -0.0864 43  SER A OG  
354  N  N   . LEU A 44  ? 0.3007 0.3335 0.2034 0.0832  -0.0130 -0.0571 44  LEU A N   
355  C  CA  . LEU A 44  ? 0.2335 0.2900 0.2187 0.0588  -0.0172 0.0135  44  LEU A CA  
356  C  C   . LEU A 44  ? 0.2108 0.2633 0.2681 0.0328  -0.0184 -0.0303 44  LEU A C   
357  O  O   . LEU A 44  ? 0.2389 0.4610 0.3511 0.0082  0.0027  0.1456  44  LEU A O   
358  C  CB  . LEU A 44  ? 0.2044 0.2763 0.1923 0.0121  -0.0020 -0.0177 44  LEU A CB  
359  C  CG  . LEU A 44  ? 0.1844 0.2540 0.1773 -0.0088 -0.0031 0.0137  44  LEU A CG  
360  C  CD1 . LEU A 44  ? 0.1959 0.2613 0.2171 0.0447  0.0258  0.0140  44  LEU A CD1 
361  C  CD2 . LEU A 44  ? 0.2565 0.2372 0.1916 -0.0318 0.0070  -0.0060 44  LEU A CD2 
362  N  N   . LYS A 45  ? 0.2407 0.2494 0.2784 0.0328  -0.0555 0.0030  45  LYS A N   
363  C  CA  . LYS A 45  ? 0.2266 0.2415 0.2964 0.0516  -0.0366 -0.0280 45  LYS A CA  
364  C  C   . LYS A 45  ? 0.2106 0.2591 0.2471 0.0652  0.0118  -0.0263 45  LYS A C   
365  O  O   . LYS A 45  ? 0.1981 0.2090 0.2741 0.0439  -0.0109 -0.0153 45  LYS A O   
366  C  CB  . LYS A 45  ? 0.2680 0.2548 0.2354 0.0979  0.0171  0.0148  45  LYS A CB  
367  C  CG  . LYS A 45  ? 0.2537 0.4473 0.3026 0.0199  -0.0423 -0.0335 45  LYS A CG  
368  C  CD  . LYS A 45  ? 0.7544 0.4293 0.6394 0.1316  -0.1825 0.1339  45  LYS A CD  
369  N  N   . PRO A 46  ? 0.1582 0.2851 0.2699 -0.0065 0.0225  0.0074  46  PRO A N   
370  C  CA  . PRO A 46  ? 0.1747 0.3079 0.2318 -0.0043 0.0159  0.0076  46  PRO A CA  
371  C  C   . PRO A 46  ? 0.1383 0.2096 0.1988 -0.0017 0.0154  -0.0077 46  PRO A C   
372  O  O   . PRO A 46  ? 0.1467 0.2225 0.2421 -0.0137 -0.0135 0.0052  46  PRO A O   
373  C  CB  . PRO A 46  ? 0.1694 0.2936 0.2408 -0.0208 0.0076  0.0148  46  PRO A CB  
374  C  CG  . PRO A 46  ? 0.1691 0.4832 0.2839 0.0000  0.0082  -0.0706 46  PRO A CG  
375  C  CD  . PRO A 46  ? 0.1817 0.3391 0.2651 0.0807  -0.0120 -0.0630 46  PRO A CD  
376  N  N   . LEU A 47  ? 0.1368 0.2842 0.2293 0.0120  0.0023  -0.0031 47  LEU A N   
377  C  CA  . LEU A 47  ? 0.1165 0.2146 0.2196 -0.0126 0.0035  0.0120  47  LEU A CA  
378  C  C   . LEU A 47  ? 0.1239 0.2164 0.2773 -0.0165 -0.0203 0.0174  47  LEU A C   
379  O  O   . LEU A 47  ? 0.1440 0.2871 0.3837 -0.0599 -0.0723 0.0842  47  LEU A O   
380  C  CB  . LEU A 47  ? 0.1674 0.2605 0.2947 0.0612  0.0296  0.0109  47  LEU A CB  
381  C  CG  . LEU A 47  ? 0.1643 0.3054 0.2731 -0.0304 0.0137  -0.0785 47  LEU A CG  
382  C  CD1 . LEU A 47  ? 0.1415 0.3137 0.4605 -0.0450 -0.0186 -0.0692 47  LEU A CD1 
383  C  CD2 . LEU A 47  ? 0.1788 0.2511 0.3614 0.0151  0.0340  -0.0344 47  LEU A CD2 
384  N  N   . SER A 48  ? 0.1203 0.2110 0.2192 -0.0063 -0.0119 0.0285  48  SER A N   
385  C  CA  . SER A 48  ? 0.1235 0.2029 0.2031 -0.0043 -0.0020 0.0222  48  SER A CA  
386  C  C   . SER A 48  ? 0.1442 0.1902 0.2194 -0.0165 -0.0093 0.0115  48  SER A C   
387  O  O   . SER A 48  ? 0.1589 0.2094 0.2210 -0.0494 0.0087  -0.0108 48  SER A O   
388  C  CB  . SER A 48  ? 0.1835 0.2000 0.2559 -0.0137 -0.0209 0.0222  48  SER A CB  
389  O  OG  . SER A 48  ? 0.2216 0.2799 0.2882 0.0749  0.0207  0.0700  48  SER A OG  
390  N  N   . VAL A 49  ? 0.1817 0.2089 0.2000 -0.0502 -0.0335 0.0154  49  VAL A N   
391  C  CA  . VAL A 49  ? 0.1932 0.1966 0.2353 -0.0724 -0.0359 0.0176  49  VAL A CA  
392  C  C   . VAL A 49  ? 0.2049 0.2150 0.2298 -0.0551 -0.0516 -0.0143 49  VAL A C   
393  O  O   . VAL A 49  ? 0.2282 0.3238 0.2609 -0.1186 -0.0643 0.0121  49  VAL A O   
394  C  CB  . VAL A 49  ? 0.2299 0.2169 0.2358 -0.0509 0.0035  -0.0364 49  VAL A CB  
395  C  CG1 . VAL A 49  ? 0.4189 0.2317 0.2533 -0.0882 0.0447  -0.0306 49  VAL A CG1 
396  C  CG2 . VAL A 49  ? 0.2164 0.2408 0.3046 -0.0562 0.0142  0.0141  49  VAL A CG2 
397  N  N   . SER A 50  ? 0.1570 0.2425 0.2232 -0.0452 -0.0263 -0.0065 50  SER A N   
398  C  CA  . SER A 50  ? 0.1242 0.2745 0.2781 -0.0015 -0.0307 -0.0013 50  SER A CA  
399  C  C   . SER A 50  ? 0.1465 0.2489 0.2698 0.0195  -0.0581 0.0063  50  SER A C   
400  O  O   . SER A 50  ? 0.1952 0.2318 0.2494 -0.0148 -0.0449 0.0167  50  SER A O   
401  C  CB  . SER A 50  ? 0.2286 0.3212 0.3129 0.0196  0.0153  -0.0108 50  SER A CB  
402  O  OG  . SER A 50  ? 0.2791 0.4168 0.3439 -0.0082 -0.0137 -0.0469 50  SER A OG  
403  N  N   . TYR A 51  ? 0.1844 0.1993 0.2257 -0.0261 -0.0472 0.0015  51  TYR A N   
404  C  CA  . TYR A 51  ? 0.1453 0.2257 0.2177 -0.0027 -0.0597 0.0255  51  TYR A CA  
405  C  C   . TYR A 51  ? 0.1780 0.2540 0.2522 0.0302  -0.0416 0.0291  51  TYR A C   
406  O  O   . TYR A 51  ? 0.1897 0.2293 0.2343 0.0137  -0.0454 0.0329  51  TYR A O   
407  C  CB  . TYR A 51  ? 0.1447 0.2342 0.2301 -0.0065 -0.0619 -0.0015 51  TYR A CB  
408  C  CG  . TYR A 51  ? 0.1465 0.1975 0.2028 0.0030  -0.0489 -0.0003 51  TYR A CG  
409  C  CD1 . TYR A 51  ? 0.1492 0.1591 0.2541 -0.0097 -0.0772 0.0162  51  TYR A CD1 
410  C  CD2 . TYR A 51  ? 0.1555 0.1828 0.1843 -0.0068 -0.0449 -0.0052 51  TYR A CD2 
411  C  CE1 . TYR A 51  ? 0.1578 0.1536 0.1695 -0.0035 -0.0375 0.0172  51  TYR A CE1 
412  C  CE2 . TYR A 51  ? 0.1577 0.1455 0.1925 -0.0322 -0.0582 0.0093  51  TYR A CE2 
413  C  CZ  . TYR A 51  ? 0.1336 0.1616 0.1772 -0.0248 -0.0392 0.0049  51  TYR A CZ  
414  O  OH  . TYR A 51  ? 0.1316 0.1665 0.1985 -0.0081 -0.0430 0.0057  51  TYR A OH  
415  N  N   A ASP A 52  ? 0.1194 0.3047 0.2982 -0.0148 -0.0697 0.0762  52  ASP A N   
416  N  N   B ASP A 52  ? 0.1190 0.3054 0.3003 -0.0153 -0.0688 0.0740  52  ASP A N   
417  C  CA  A ASP A 52  ? 0.1977 0.3280 0.2702 0.0322  -0.0627 0.0771  52  ASP A CA  
418  C  CA  B ASP A 52  ? 0.1986 0.3281 0.2753 0.0331  -0.0631 0.0781  52  ASP A CA  
419  C  C   A ASP A 52  ? 0.2674 0.2516 0.3148 0.0516  -0.1162 0.0649  52  ASP A C   
420  C  C   B ASP A 52  ? 0.2673 0.2500 0.3165 0.0509  -0.1120 0.0640  52  ASP A C   
421  O  O   A ASP A 52  ? 0.2766 0.3108 0.3205 -0.0093 -0.1492 0.0979  52  ASP A O   
422  O  O   B ASP A 52  ? 0.2802 0.3194 0.3273 -0.0131 -0.1423 0.0894  52  ASP A O   
423  C  CB  A ASP A 52  ? 0.1773 0.3183 0.3513 0.0480  -0.0793 0.1062  52  ASP A CB  
424  C  CB  B ASP A 52  ? 0.2238 0.3324 0.3920 0.0366  -0.0277 0.1102  52  ASP A CB  
425  C  CG  A ASP A 52  ? 0.3633 0.4720 0.4796 0.2153  0.0732  -0.1322 52  ASP A CG  
426  C  CG  B ASP A 52  ? 0.3197 0.5022 0.4423 0.2097  -0.0766 0.0441  52  ASP A CG  
427  O  OD1 A ASP A 52  ? 0.4599 0.4009 0.4857 -0.1045 0.0781  0.1092  52  ASP A OD1 
428  O  OD1 B ASP A 52  ? 0.4426 0.5515 0.4225 0.0076  -0.0307 0.1252  52  ASP A OD1 
429  O  OD2 A ASP A 52  ? 0.4994 0.6394 0.7407 0.3100  -0.1106 0.2878  52  ASP A OD2 
430  O  OD2 B ASP A 52  ? 0.6876 0.5971 0.6973 0.3075  0.1849  0.2363  52  ASP A OD2 
431  N  N   . GLN A 53  ? 0.1817 0.2569 0.3960 0.0263  -0.0851 0.0731  53  GLN A N   
432  C  CA  . GLN A 53  ? 0.2745 0.2626 0.3858 0.0298  -0.0540 0.1027  53  GLN A CA  
433  C  C   . GLN A 53  ? 0.2616 0.2213 0.2177 -0.0065 -0.0483 0.0093  53  GLN A C   
434  O  O   . GLN A 53  ? 0.2350 0.2257 0.3065 -0.0020 -0.0553 0.0372  53  GLN A O   
435  C  CB  . GLN A 53  ? 0.2605 0.2850 0.4611 0.0483  -0.0003 0.1005  53  GLN A CB  
436  C  CG  . GLN A 53  ? 0.2659 0.6521 0.3963 0.0566  0.0019  0.0899  53  GLN A CG  
437  C  CD  . GLN A 53  ? 0.6546 1.0842 0.7214 0.0601  -0.2804 0.0868  53  GLN A CD  
438  O  OE1 . GLN A 53  ? 0.5493 0.8992 1.2539 0.0259  0.0219  0.1612  53  GLN A OE1 
439  N  NE2 . GLN A 53  ? 0.8069 1.0515 1.4902 -0.0759 0.2642  0.2824  53  GLN A NE2 
440  N  N   . ALA A 54  ? 0.2638 0.1807 0.2763 -0.0088 -0.0719 0.0057  54  ALA A N   
441  C  CA  . ALA A 54  ? 0.2372 0.1710 0.2108 0.0132  -0.0555 -0.0221 54  ALA A CA  
442  C  C   . ALA A 54  ? 0.2623 0.1973 0.1925 -0.0080 -0.0469 -0.0359 54  ALA A C   
443  O  O   . ALA A 54  ? 0.3269 0.3331 0.2435 -0.0766 -0.0882 -0.0592 54  ALA A O   
444  C  CB  . ALA A 54  ? 0.2117 0.1817 0.3172 0.0093  -0.0324 -0.0241 54  ALA A CB  
445  N  N   . THR A 55  ? 0.2358 0.1673 0.1923 0.0264  -0.0619 -0.0024 55  THR A N   
446  C  CA  . THR A 55  ? 0.2247 0.1912 0.2081 0.0478  -0.0465 0.0142  55  THR A CA  
447  C  C   . THR A 55  ? 0.2295 0.1465 0.1518 0.0065  -0.0571 0.0286  55  THR A C   
448  O  O   . THR A 55  ? 0.2295 0.1586 0.1697 0.0164  -0.0417 0.0266  55  THR A O   
449  C  CB  . THR A 55  ? 0.3179 0.2363 0.2486 0.0570  -0.0390 0.0627  55  THR A CB  
450  O  OG1 . THR A 55  ? 0.4103 0.2254 0.4649 0.0617  -0.1263 0.0159  55  THR A OG1 
451  C  CG2 . THR A 55  ? 0.4451 0.2601 0.2286 0.1655  -0.0119 0.0533  55  THR A CG2 
452  N  N   . SER A 56  ? 0.2691 0.1402 0.1758 0.0285  -0.0969 0.0153  56  SER A N   
453  C  CA  . SER A 56  ? 0.3319 0.1422 0.1546 0.0353  -0.0740 0.0062  56  SER A CA  
454  C  C   . SER A 56  ? 0.3021 0.1867 0.1837 0.0571  -0.0529 0.0006  56  SER A C   
455  O  O   . SER A 56  ? 0.3244 0.1797 0.1972 0.0658  -0.0847 0.0320  56  SER A O   
456  C  CB  . SER A 56  ? 0.3273 0.1500 0.1562 0.0261  -0.0908 -0.0015 56  SER A CB  
457  O  OG  . SER A 56  ? 0.3312 0.1625 0.1861 0.0038  -0.1190 0.0130  56  SER A OG  
458  N  N   . LEU A 57  ? 0.2766 0.1472 0.1206 0.0342  -0.0239 0.0187  57  LEU A N   
459  C  CA  . LEU A 57  ? 0.2254 0.1932 0.1970 0.0167  -0.0097 0.0370  57  LEU A CA  
460  C  C   . LEU A 57  ? 0.2745 0.1494 0.1287 0.0184  -0.0163 0.0142  57  LEU A C   
461  O  O   . LEU A 57  ? 0.3510 0.1761 0.1235 0.0355  -0.0353 0.0335  57  LEU A O   
462  C  CB  . LEU A 57  ? 0.3291 0.2250 0.2098 -0.0450 0.0195  0.0582  57  LEU A CB  
463  C  CG  . LEU A 57  ? 0.3507 0.1609 0.2875 -0.0003 -0.0346 0.0273  57  LEU A CG  
464  C  CD1 . LEU A 57  ? 0.3039 0.3894 0.3651 -0.1111 -0.0617 0.1084  57  LEU A CD1 
465  C  CD2 . LEU A 57  ? 0.4480 0.2397 0.2860 0.1014  -0.0518 0.0772  57  LEU A CD2 
466  N  N   . ARG A 58  ? 0.2930 0.1761 0.1512 0.0520  -0.0386 0.0287  58  ARG A N   
467  C  CA  . ARG A 58  ? 0.2529 0.1747 0.1664 0.0186  -0.0463 0.0375  58  ARG A CA  
468  C  C   . ARG A 58  ? 0.2414 0.1582 0.1376 0.0003  -0.0458 0.0209  58  ARG A C   
469  O  O   . ARG A 58  ? 0.2705 0.1740 0.1221 0.0205  -0.0199 0.0263  58  ARG A O   
470  C  CB  . ARG A 58  ? 0.2108 0.2889 0.1476 -0.0017 -0.0109 0.0205  58  ARG A CB  
471  C  CG  . ARG A 58  ? 0.1630 0.2171 0.3009 -0.0251 -0.0052 0.1049  58  ARG A CG  
472  C  CD  . ARG A 58  ? 0.2864 0.2777 0.2433 -0.0881 -0.0781 0.0684  58  ARG A CD  
473  N  NE  . ARG A 58  ? 0.1932 0.2669 0.2318 -0.0041 -0.0142 0.0208  58  ARG A NE  
474  C  CZ  . ARG A 58  ? 0.1932 0.3032 0.1893 -0.0162 0.0019  0.0740  58  ARG A CZ  
475  N  NH1 . ARG A 58  ? 0.3100 0.2753 0.2017 -0.0997 0.0137  0.0414  58  ARG A NH1 
476  N  NH2 . ARG A 58  ? 0.2512 0.2085 0.2097 -0.0263 0.0082  0.0366  58  ARG A NH2 
477  N  N   . ILE A 59  ? 0.2523 0.1625 0.1295 0.0088  -0.0259 0.0120  59  ILE A N   
478  C  CA  . ILE A 59  ? 0.2928 0.1693 0.1479 -0.0370 -0.0236 0.0447  59  ILE A CA  
479  C  C   . ILE A 59  ? 0.2619 0.1185 0.1234 -0.0076 -0.0432 0.0197  59  ILE A C   
480  O  O   . ILE A 59  ? 0.2864 0.2046 0.1088 0.0281  -0.0194 0.0307  59  ILE A O   
481  C  CB  . ILE A 59  ? 0.2505 0.1534 0.1137 0.0037  -0.0263 0.0236  59  ILE A CB  
482  C  CG1 . ILE A 59  ? 0.3093 0.1368 0.1286 0.0020  -0.0390 0.0209  59  ILE A CG1 
483  C  CG2 . ILE A 59  ? 0.3291 0.1659 0.1296 0.0147  -0.0617 0.0031  59  ILE A CG2 
484  C  CD1 . ILE A 59  ? 0.2971 0.1421 0.1553 0.0070  -0.0454 0.0086  59  ILE A CD1 
485  N  N   . LEU A 60  ? 0.2213 0.1503 0.1825 -0.0182 -0.0379 -0.0013 60  LEU A N   
486  C  CA  . LEU A 60  ? 0.2526 0.1433 0.1309 0.0038  -0.0553 0.0204  60  LEU A CA  
487  C  C   . LEU A 60  ? 0.2322 0.1542 0.1133 -0.0175 -0.0305 -0.0003 60  LEU A C   
488  O  O   . LEU A 60  ? 0.2037 0.1753 0.1031 -0.0259 -0.0076 0.0164  60  LEU A O   
489  C  CB  . LEU A 60  ? 0.2247 0.1422 0.1870 -0.0182 -0.0295 0.0020  60  LEU A CB  
490  C  CG  . LEU A 60  ? 0.2529 0.1536 0.1798 -0.0038 -0.0408 0.0285  60  LEU A CG  
491  C  CD1 . LEU A 60  ? 0.2489 0.1885 0.2011 -0.0197 0.0048  0.0324  60  LEU A CD1 
492  C  CD2 . LEU A 60  ? 0.2713 0.1661 0.2257 -0.0551 -0.0193 -0.0027 60  LEU A CD2 
493  N  N   . ASN A 61  ? 0.2116 0.1282 0.1409 -0.0109 -0.0052 0.0227  61  ASN A N   
494  C  CA  . ASN A 61  ? 0.2389 0.1515 0.1433 -0.0299 0.0114  -0.0137 61  ASN A CA  
495  C  C   . ASN A 61  ? 0.2320 0.1798 0.1077 -0.0274 0.0024  0.0074  61  ASN A C   
496  O  O   . ASN A 61  ? 0.2702 0.1586 0.1500 -0.0335 0.0186  0.0219  61  ASN A O   
497  C  CB  . ASN A 61  ? 0.2560 0.1453 0.1480 -0.0109 0.0130  -0.0031 61  ASN A CB  
498  C  CG  . ASN A 61  ? 0.2310 0.1525 0.1444 -0.0339 0.0043  -0.0181 61  ASN A CG  
499  O  OD1 . ASN A 61  ? 0.2638 0.1686 0.1394 -0.0456 0.0118  0.0063  61  ASN A OD1 
500  N  ND2 . ASN A 61  ? 0.2809 0.1438 0.1397 -0.0377 0.0412  -0.0076 61  ASN A ND2 
501  N  N   . ASN A 62  ? 0.2745 0.1395 0.1172 -0.0566 0.0013  0.0070  62  ASN A N   
502  C  CA  . ASN A 62  ? 0.2451 0.1638 0.1498 -0.0287 -0.0010 0.0082  62  ASN A CA  
503  C  C   . ASN A 62  ? 0.2040 0.1764 0.1676 -0.0907 0.0181  0.0031  62  ASN A C   
504  O  O   . ASN A 62  ? 0.2551 0.2175 0.2175 -0.0882 0.0103  -0.0015 62  ASN A O   
505  C  CB  . ASN A 62  ? 0.2832 0.1703 0.1600 -0.0414 -0.0147 -0.0063 62  ASN A CB  
506  C  CG  . ASN A 62  ? 0.3244 0.1903 0.1289 -0.0601 -0.0155 -0.0322 62  ASN A CG  
507  O  OD1 . ASN A 62  ? 0.2652 0.1632 0.1527 -0.0562 0.0026  0.0007  62  ASN A OD1 
508  N  ND2 . ASN A 62  ? 0.5138 0.1878 0.2004 -0.0482 0.0891  -0.0041 62  ASN A ND2 
509  N  N   . GLY A 63  ? 0.2451 0.1729 0.1550 -0.0452 0.0126  0.0200  63  GLY A N   
510  C  CA  . GLY A 63  ? 0.2055 0.1986 0.1586 -0.0750 0.0015  0.0200  63  GLY A CA  
511  C  C   . GLY A 63  ? 0.2046 0.1650 0.1700 -0.0502 0.0043  -0.0031 63  GLY A C   
512  O  O   . GLY A 63  ? 0.2162 0.2027 0.1864 -0.0241 0.0091  -0.0085 63  GLY A O   
513  N  N   A HIS A 64  ? 0.1941 0.1560 0.1289 -0.0427 -0.0023 0.0031  64  HIS A N   
514  N  N   B HIS A 64  ? 0.1934 0.1952 0.1630 -0.0746 0.0342  0.0274  64  HIS A N   
515  C  CA  A HIS A 64  ? 0.1548 0.1949 0.1351 -0.0320 0.0006  0.0043  64  HIS A CA  
516  C  CA  B HIS A 64  ? 0.1900 0.2522 0.1557 -0.0465 0.0171  0.0317  64  HIS A CA  
517  C  C   A HIS A 64  ? 0.1607 0.1518 0.1914 -0.0406 0.0077  -0.0076 64  HIS A C   
518  C  C   B HIS A 64  ? 0.1770 0.1677 0.1217 -0.0274 0.0252  0.0140  64  HIS A C   
519  O  O   A HIS A 64  ? 0.1693 0.1738 0.1440 -0.0285 0.0186  0.0287  64  HIS A O   
520  O  O   B HIS A 64  ? 0.1961 0.1670 0.1291 -0.0073 0.0403  0.0241  64  HIS A O   
521  C  CB  A HIS A 64  ? 0.1356 0.1600 0.1174 -0.0096 -0.0030 -0.0027 64  HIS A CB  
522  C  CB  B HIS A 64  ? 0.2399 0.2261 0.1636 -0.0240 -0.0388 0.0308  64  HIS A CB  
523  C  CG  A HIS A 64  ? 0.1688 0.1871 0.1343 -0.0350 0.0146  0.0126  64  HIS A CG  
524  C  CG  B HIS A 64  ? 0.3628 0.2645 0.1420 -0.0254 -0.0529 -0.0463 64  HIS A CG  
525  N  ND1 A HIS A 64  ? 0.1837 0.2395 0.1260 -0.0458 -0.0010 -0.0231 64  HIS A ND1 
526  N  ND1 B HIS A 64  ? 0.2612 0.2763 0.2666 -0.0049 -0.0175 -0.0798 64  HIS A ND1 
527  C  CD2 A HIS A 64  ? 0.2008 0.1834 0.1142 -0.0617 0.0161  -0.0250 64  HIS A CD2 
528  C  CD2 B HIS A 64  ? 0.4552 0.2284 0.0904 -0.0320 -0.1045 -0.0476 64  HIS A CD2 
529  C  CE1 A HIS A 64  ? 0.1394 0.2634 0.1878 -0.0619 -0.0074 -0.0461 64  HIS A CE1 
530  C  CE1 B HIS A 64  ? 0.2774 0.2386 0.2572 -0.0701 -0.0566 -0.0996 64  HIS A CE1 
531  N  NE2 A HIS A 64  ? 0.1949 0.2426 0.1810 -0.0504 0.0527  -0.0110 64  HIS A NE2 
532  N  NE2 B HIS A 64  ? 0.3697 0.2756 0.3424 -0.1027 0.0102  -0.0491 64  HIS A NE2 
533  N  N   . ALA A 65  ? 0.1720 0.1616 0.1527 -0.0406 -0.0065 0.0151  65  ALA A N   
534  C  CA  . ALA A 65  ? 0.1914 0.1379 0.1424 -0.0439 -0.0035 0.0093  65  ALA A CA  
535  C  C   . ALA A 65  ? 0.2026 0.1458 0.0938 -0.0114 -0.0046 -0.0057 65  ALA A C   
536  O  O   . ALA A 65  ? 0.2338 0.1668 0.1436 -0.0540 0.0163  0.0177  65  ALA A O   
537  C  CB  . ALA A 65  ? 0.2356 0.1870 0.1377 -0.0274 -0.0093 0.0070  65  ALA A CB  
538  N  N   . PHE A 66  ? 0.1896 0.1386 0.1122 -0.0167 -0.0068 0.0017  66  PHE A N   
539  C  CA  . PHE A 66  ? 0.2261 0.1368 0.1163 -0.0054 -0.0109 0.0350  66  PHE A CA  
540  C  C   . PHE A 66  ? 0.2152 0.1406 0.1108 -0.0024 -0.0098 0.0019  66  PHE A C   
541  O  O   . PHE A 66  ? 0.2243 0.1370 0.1142 -0.0120 -0.0065 0.0070  66  PHE A O   
542  C  CB  . PHE A 66  ? 0.2022 0.1787 0.1203 -0.0167 -0.0221 0.0164  66  PHE A CB  
543  C  CG  . PHE A 66  ? 0.2634 0.1708 0.0891 -0.0253 -0.0386 -0.0026 66  PHE A CG  
544  C  CD1 . PHE A 66  ? 0.2361 0.2081 0.1054 -0.0318 -0.0395 -0.0221 66  PHE A CD1 
545  C  CD2 . PHE A 66  ? 0.2349 0.1675 0.1081 -0.0093 -0.0110 -0.0153 66  PHE A CD2 
546  C  CE1 . PHE A 66  ? 0.2061 0.1764 0.1246 0.0006  -0.0570 0.0000  66  PHE A CE1 
547  C  CE2 . PHE A 66  ? 0.2474 0.1649 0.1268 -0.0348 -0.0487 -0.0082 66  PHE A CE2 
548  C  CZ  . PHE A 66  ? 0.2478 0.1747 0.1289 -0.0285 -0.0427 -0.0113 66  PHE A CZ  
549  N  N   . ASN A 67  ? 0.2309 0.1491 0.1178 -0.0057 -0.0241 0.0226  67  ASN A N   
550  C  CA  . ASN A 67  ? 0.1928 0.1321 0.1327 -0.0188 -0.0236 0.0000  67  ASN A CA  
551  C  C   . ASN A 67  ? 0.2178 0.1212 0.0939 -0.0027 -0.0216 0.0068  67  ASN A C   
552  O  O   . ASN A 67  ? 0.2428 0.1688 0.1145 -0.0093 -0.0166 0.0241  67  ASN A O   
553  C  CB  . ASN A 67  ? 0.2483 0.1882 0.1151 -0.0606 -0.0153 0.0155  67  ASN A CB  
554  C  CG  . ASN A 67  ? 0.2223 0.1543 0.1846 -0.0505 -0.0205 -0.0068 67  ASN A CG  
555  O  OD1 . ASN A 67  ? 0.2694 0.2189 0.1600 -0.0930 -0.0337 0.0333  67  ASN A OD1 
556  N  ND2 . ASN A 67  ? 0.2736 0.2125 0.2645 -0.0772 -0.0625 -0.0233 67  ASN A ND2 
557  N  N   . VAL A 68  ? 0.1985 0.1336 0.1212 0.0059  -0.0108 0.0091  68  VAL A N   
558  C  CA  . VAL A 68  ? 0.2213 0.1212 0.1210 0.0527  -0.0350 0.0082  68  VAL A CA  
559  C  C   . VAL A 68  ? 0.2580 0.1295 0.1431 0.0471  -0.0277 0.0096  68  VAL A C   
560  O  O   . VAL A 68  ? 0.2325 0.1262 0.1210 0.0211  -0.0259 0.0142  68  VAL A O   
561  C  CB  . VAL A 68  ? 0.2182 0.1206 0.1756 0.0038  -0.0535 0.0131  68  VAL A CB  
562  C  CG1 . VAL A 68  ? 0.2340 0.1724 0.1577 0.0384  -0.0758 0.0052  68  VAL A CG1 
563  C  CG2 . VAL A 68  ? 0.2295 0.1858 0.1616 0.0175  -0.0348 -0.0236 68  VAL A CG2 
564  N  N   . GLU A 69  ? 0.2921 0.1376 0.1322 0.0370  -0.0082 0.0142  69  GLU A N   
565  C  CA  . GLU A 69  ? 0.2360 0.1600 0.1439 0.0266  0.0006  0.0080  69  GLU A CA  
566  C  C   . GLU A 69  ? 0.2327 0.1374 0.1577 0.0405  -0.0467 0.0049  69  GLU A C   
567  O  O   . GLU A 69  ? 0.2680 0.1427 0.1686 0.0178  -0.0542 0.0228  69  GLU A O   
568  C  CB  . GLU A 69  ? 0.1661 0.1921 0.2205 0.0087  -0.0120 0.0120  69  GLU A CB  
569  C  CG  . GLU A 69  ? 0.1621 0.2257 0.1846 -0.0370 -0.0063 0.0408  69  GLU A CG  
570  C  CD  . GLU A 69  ? 0.2536 0.2056 0.2493 0.0115  0.0173  0.0652  69  GLU A CD  
571  O  OE1 . GLU A 69  ? 0.2483 0.2061 0.2397 0.0019  0.0052  0.0771  69  GLU A OE1 
572  O  OE2 . GLU A 69  ? 0.2802 0.2168 0.2619 -0.0216 0.0099  0.0566  69  GLU A OE2 
573  N  N   . PHE A 70  ? 0.2523 0.1447 0.1312 0.0274  -0.0260 0.0088  70  PHE A N   
574  C  CA  . PHE A 70  ? 0.2071 0.1106 0.1639 0.0093  -0.0500 -0.0027 70  PHE A CA  
575  C  C   . PHE A 70  ? 0.2169 0.1465 0.1685 0.0177  -0.0285 0.0181  70  PHE A C   
576  O  O   . PHE A 70  ? 0.2284 0.1315 0.2113 0.0109  -0.0447 0.0291  70  PHE A O   
577  C  CB  . PHE A 70  ? 0.2265 0.1376 0.1270 0.0000  -0.0421 0.0071  70  PHE A CB  
578  C  CG  . PHE A 70  ? 0.2236 0.1289 0.1632 0.0226  -0.0590 0.0174  70  PHE A CG  
579  C  CD1 . PHE A 70  ? 0.2415 0.1212 0.1485 0.0273  -0.0266 0.0296  70  PHE A CD1 
580  C  CD2 . PHE A 70  ? 0.2310 0.1448 0.1448 0.0109  -0.0551 0.0148  70  PHE A CD2 
581  C  CE1 . PHE A 70  ? 0.2214 0.1465 0.1785 0.0077  -0.0230 0.0361  70  PHE A CE1 
582  C  CE2 . PHE A 70  ? 0.2587 0.1433 0.1629 0.0148  -0.0392 0.0335  70  PHE A CE2 
583  C  CZ  . PHE A 70  ? 0.2432 0.1436 0.1589 0.0049  -0.0236 0.0082  70  PHE A CZ  
584  N  N   . ASP A 71  ? 0.2763 0.1251 0.2210 0.0399  -0.0909 0.0132  71  ASP A N   
585  C  CA  . ASP A 71  ? 0.2630 0.1124 0.2631 0.0551  -0.0299 0.0439  71  ASP A CA  
586  C  C   . ASP A 71  ? 0.2293 0.1005 0.2885 0.0175  -0.0184 -0.0027 71  ASP A C   
587  O  O   . ASP A 71  ? 0.2370 0.1905 0.4139 -0.0164 -0.0063 -0.0259 71  ASP A O   
588  C  CB  . ASP A 71  ? 0.3179 0.1464 0.3701 0.0263  -0.1576 0.0476  71  ASP A CB  
589  C  CG  . ASP A 71  ? 0.3980 0.1568 0.4943 0.0333  -0.2172 0.0428  71  ASP A CG  
590  O  OD1 . ASP A 71  ? 0.3341 0.1454 0.4332 0.0337  -0.0930 0.0472  71  ASP A OD1 
591  O  OD2 . ASP A 71  ? 0.4611 0.1913 0.6969 0.0261  -0.2716 0.0368  71  ASP A OD2 
592  N  N   . ASP A 72  ? 0.2090 0.1036 0.2544 0.0030  -0.0099 0.0185  72  ASP A N   
593  C  CA  . ASP A 72  ? 0.2515 0.1049 0.2630 -0.0080 0.0286  -0.0065 72  ASP A CA  
594  C  C   . ASP A 72  ? 0.2817 0.1298 0.3452 0.0003  0.0167  0.0320  72  ASP A C   
595  O  O   . ASP A 72  ? 0.3981 0.1208 0.3276 -0.0231 0.0439  0.0074  72  ASP A O   
596  C  CB  . ASP A 72  ? 0.2250 0.1641 0.2451 0.0119  0.0421  0.0306  72  ASP A CB  
597  C  CG  . ASP A 72  ? 0.2615 0.2158 0.1600 0.0228  -0.0054 0.0137  72  ASP A CG  
598  O  OD1 . ASP A 72  ? 0.2541 0.2652 0.2047 -0.0164 -0.0216 0.0520  72  ASP A OD1 
599  O  OD2 . ASP A 72  ? 0.2547 0.2485 0.1706 -0.0310 -0.0252 0.0208  72  ASP A OD2 
600  N  N   . SER A 73  ? 0.2698 0.1194 0.3047 -0.0137 0.0063  0.0076  73  SER A N   
601  C  CA  . SER A 73  ? 0.2930 0.1270 0.3837 0.0093  0.0038  0.0126  73  SER A CA  
602  C  C   . SER A 73  ? 0.2795 0.1506 0.4010 -0.0436 0.0597  -0.0511 73  SER A C   
603  O  O   . SER A 73  ? 0.3424 0.1307 0.3148 -0.0099 0.0160  -0.0031 73  SER A O   
604  C  CB  . SER A 73  ? 0.3452 0.1932 0.4275 -0.0403 0.0115  0.0564  73  SER A CB  
605  O  OG  . SER A 73  ? 0.3388 0.1604 0.3535 0.0284  0.0617  0.0511  73  SER A OG  
606  N  N   . GLN A 74  ? 0.2857 0.1433 0.4577 0.0068  0.0863  0.0173  74  GLN A N   
607  C  CA  . GLN A 74  ? 0.3101 0.2518 0.4878 -0.0414 0.1076  -0.0436 74  GLN A CA  
608  C  C   . GLN A 74  ? 0.3033 0.2295 0.3277 -0.0068 0.0428  -0.0535 74  GLN A C   
609  O  O   . GLN A 74  ? 0.2241 0.1995 0.2821 -0.0423 -0.0538 0.0062  74  GLN A O   
610  C  CB  . GLN A 74  ? 0.3162 0.1614 0.6388 0.0241  0.0860  0.0904  74  GLN A CB  
611  C  CG  . GLN A 74  ? 0.3840 0.2634 0.7056 0.0653  0.1606  0.1190  74  GLN A CG  
612  C  CD  . GLN A 74  ? 0.4074 0.4890 0.7185 0.0265  0.0776  0.2151  74  GLN A CD  
613  O  OE1 . GLN A 74  ? 0.7559 0.6575 1.1762 0.0483  0.4063  0.2745  74  GLN A OE1 
614  N  NE2 . GLN A 74  ? 0.4853 0.3040 0.7565 0.0403  -0.2020 -0.1052 74  GLN A NE2 
615  N  N   . ASP A 75  ? 0.3956 0.3894 0.2778 -0.1432 0.0895  -0.0811 75  ASP A N   
616  C  CA  . ASP A 75  ? 0.2612 0.2964 0.2595 -0.0531 0.0046  -0.0375 75  ASP A CA  
617  C  C   . ASP A 75  ? 0.2363 0.3334 0.3230 -0.0217 -0.0557 -0.0452 75  ASP A C   
618  O  O   . ASP A 75  ? 0.2681 0.3525 0.4376 -0.0538 -0.0324 -0.0328 75  ASP A O   
619  C  CB  . ASP A 75  ? 0.3794 0.4447 0.2982 -0.0851 0.0375  -0.0275 75  ASP A CB  
620  C  CG  . ASP A 75  ? 0.3713 0.3930 0.3902 0.0337  0.0210  0.0740  75  ASP A CG  
621  O  OD1 . ASP A 75  ? 0.3488 0.4670 0.4721 -0.0182 -0.0065 -0.0046 75  ASP A OD1 
622  O  OD2 . ASP A 75  ? 0.3143 0.3669 0.5544 -0.0264 0.0649  0.0313  75  ASP A OD2 
623  N  N   . LYS A 76  ? 0.2637 0.2487 0.2512 -0.0241 -0.0714 0.0559  76  LYS A N   
624  C  CA  . LYS A 76  ? 0.2577 0.1673 0.3550 0.0175  -0.0666 0.0410  76  LYS A CA  
625  C  C   . LYS A 76  ? 0.2942 0.2681 0.5518 -0.0156 -0.1129 0.0763  76  LYS A C   
626  O  O   . LYS A 76  ? 0.2652 0.5501 0.6496 -0.0934 -0.0524 0.1052  76  LYS A O   
627  C  CB  . LYS A 76  ? 0.3039 0.1986 0.3143 -0.0540 -0.1430 0.0284  76  LYS A CB  
628  C  CG  . LYS A 76  ? 0.6312 0.2128 0.3273 -0.0623 -0.1773 0.0485  76  LYS A CG  
629  C  CD  . LYS A 76  ? 0.8036 0.2325 0.2809 -0.1084 -0.1879 -0.0013 76  LYS A CD  
630  C  CE  . LYS A 76  ? 0.5536 0.3779 0.3844 0.0052  -0.0383 0.0644  76  LYS A CE  
631  N  NZ  . LYS A 76  ? 0.3725 0.4046 0.5109 0.0419  0.0394  0.0037  76  LYS A NZ  
632  N  N   . ALA A 77  ? 0.3176 0.2947 0.3258 0.0749  -0.1254 0.0197  77  ALA A N   
633  C  CA  . ALA A 77  ? 0.1864 0.2171 0.2304 0.0038  -0.0740 0.0093  77  ALA A CA  
634  C  C   . ALA A 77  ? 0.1638 0.1995 0.2397 -0.0184 -0.0732 -0.0146 77  ALA A C   
635  O  O   . ALA A 77  ? 0.1483 0.3812 0.3161 -0.0232 -0.0636 -0.1076 77  ALA A O   
636  C  CB  . ALA A 77  ? 0.2414 0.2221 0.1657 0.0120  -0.0533 -0.0024 77  ALA A CB  
637  N  N   . VAL A 78  ? 0.1686 0.1497 0.2105 -0.0126 -0.0631 -0.0003 78  VAL A N   
638  C  CA  . VAL A 78  ? 0.2169 0.1570 0.2081 -0.0087 -0.0658 0.0266  78  VAL A CA  
639  C  C   . VAL A 78  ? 0.1518 0.1758 0.2220 -0.0132 -0.0463 0.0258  78  VAL A C   
640  O  O   . VAL A 78  ? 0.1783 0.1557 0.2777 -0.0277 -0.0723 0.0353  78  VAL A O   
641  C  CB  . VAL A 78  ? 0.3082 0.1968 0.2442 0.0498  -0.0700 -0.0043 78  VAL A CB  
642  C  CG1 . VAL A 78  ? 0.3503 0.1841 0.3319 0.0386  -0.0689 0.0346  78  VAL A CG1 
643  C  CG2 . VAL A 78  ? 0.2856 0.2415 0.3323 0.0318  0.0465  0.0024  78  VAL A CG2 
644  N  N   . LEU A 79  ? 0.1517 0.1624 0.1968 0.0108  -0.0291 0.0126  79  LEU A N   
645  C  CA  . LEU A 79  ? 0.1691 0.1986 0.1814 0.0097  -0.0320 0.0081  79  LEU A CA  
646  C  C   . LEU A 79  ? 0.1510 0.1625 0.1676 -0.0098 -0.0177 0.0115  79  LEU A C   
647  O  O   . LEU A 79  ? 0.1622 0.1774 0.1956 -0.0329 0.0007  -0.0155 79  LEU A O   
648  C  CB  . LEU A 79  ? 0.1404 0.1940 0.2231 -0.0059 -0.0252 0.0306  79  LEU A CB  
649  C  CG  . LEU A 79  ? 0.1498 0.1832 0.2092 0.0110  -0.0131 -0.0015 79  LEU A CG  
650  C  CD1 . LEU A 79  ? 0.1796 0.1650 0.4448 -0.0337 -0.0147 0.0595  79  LEU A CD1 
651  C  CD2 . LEU A 79  ? 0.1394 0.1979 0.1937 0.0214  -0.0031 -0.0063 79  LEU A CD2 
652  N  N   . LYS A 80  ? 0.1675 0.2034 0.1752 -0.0131 0.0059  0.0104  80  LYS A N   
653  C  CA  . LYS A 80  ? 0.1510 0.2002 0.2286 0.0030  0.0048  0.0118  80  LYS A CA  
654  C  C   . LYS A 80  ? 0.1327 0.2134 0.2161 0.0192  0.0308  -0.0024 80  LYS A C   
655  O  O   . LYS A 80  ? 0.1528 0.1801 0.2124 -0.0120 -0.0175 0.0119  80  LYS A O   
656  C  CB  . LYS A 80  ? 0.2311 0.2264 0.2723 0.0548  0.0000  0.0000  80  LYS A CB  
657  C  CG  . LYS A 80  ? 0.2404 0.1986 0.3165 0.0185  0.0240  0.0171  80  LYS A CG  
658  C  CD  . LYS A 80  ? 0.1880 0.2997 0.5472 0.0640  -0.0348 0.0099  80  LYS A CD  
659  C  CE  . LYS A 80  ? 0.5921 0.5598 0.4620 -0.2388 0.0273  -0.0983 80  LYS A CE  
660  N  NZ  . LYS A 80  ? 0.6930 1.1030 0.7131 0.0098  0.0274  0.0205  80  LYS A NZ  
661  N  N   . GLY A 81  ? 0.1524 0.2311 0.2022 0.0193  0.0220  0.0006  81  GLY A N   
662  C  CA  . GLY A 81  ? 0.1500 0.2289 0.2182 0.0200  0.0500  0.0463  81  GLY A CA  
663  C  C   . GLY A 81  ? 0.1481 0.1895 0.2460 0.0219  0.0328  0.0296  81  GLY A C   
664  O  O   . GLY A 81  ? 0.1647 0.1879 0.2160 -0.0146 0.0155  -0.0054 81  GLY A O   
665  N  N   . GLY A 82  ? 0.1611 0.2223 0.3355 -0.0054 0.0379  0.0286  82  GLY A N   
666  C  CA  . GLY A 82  ? 0.1909 0.2108 0.3561 0.0000  0.0239  0.0551  82  GLY A CA  
667  C  C   . GLY A 82  ? 0.1670 0.2142 0.3029 0.0372  0.0401  0.0151  82  GLY A C   
668  O  O   . GLY A 82  ? 0.2175 0.3801 0.2789 0.1067  0.0542  0.0399  82  GLY A O   
669  N  N   . PRO A 83  ? 0.1679 0.2144 0.2508 0.0342  0.0217  0.0186  83  PRO A N   
670  C  CA  . PRO A 83  ? 0.2010 0.1844 0.2151 0.0529  0.0189  0.0125  83  PRO A CA  
671  C  C   . PRO A 83  ? 0.1967 0.2338 0.1976 0.0399  -0.0020 -0.0296 83  PRO A C   
672  O  O   . PRO A 83  ? 0.2232 0.2651 0.2264 0.0286  -0.0357 0.0077  83  PRO A O   
673  C  CB  . PRO A 83  ? 0.1758 0.2263 0.2192 0.0575  -0.0346 -0.0027 83  PRO A CB  
674  C  CG  . PRO A 83  ? 0.1607 0.2117 0.2035 0.0597  0.0184  0.0189  83  PRO A CG  
675  C  CD  . PRO A 83  ? 0.1526 0.1688 0.2325 0.0198  0.0230  0.0020  83  PRO A CD  
676  N  N   . LEU A 84  ? 0.1743 0.1871 0.1668 0.0373  0.0093  0.0121  84  LEU A N   
677  C  CA  . LEU A 84  ? 0.1875 0.1553 0.1789 0.0344  -0.0027 -0.0196 84  LEU A CA  
678  C  C   . LEU A 84  ? 0.1720 0.1711 0.2256 0.0456  -0.0020 -0.0351 84  LEU A C   
679  O  O   . LEU A 84  ? 0.2081 0.1956 0.2809 0.0505  0.0434  -0.0529 84  LEU A O   
680  C  CB  . LEU A 84  ? 0.1467 0.1325 0.1823 0.0340  0.0038  0.0038  84  LEU A CB  
681  C  CG  . LEU A 84  ? 0.1342 0.1325 0.1905 0.0087  0.0113  -0.0142 84  LEU A CG  
682  C  CD1 . LEU A 84  ? 0.1620 0.1503 0.1898 0.0381  -0.0076 -0.0085 84  LEU A CD1 
683  C  CD2 . LEU A 84  ? 0.1419 0.1429 0.1946 0.0153  0.0148  -0.0165 84  LEU A CD2 
684  N  N   . ASP A 85  ? 0.2011 0.2043 0.2439 0.0178  -0.0104 -0.0793 85  ASP A N   
685  C  CA  . ASP A 85  ? 0.3180 0.1597 0.2820 -0.0054 0.0194  -0.0841 85  ASP A CA  
686  C  C   . ASP A 85  ? 0.2169 0.1691 0.3826 0.0309  0.0197  0.0099  85  ASP A C   
687  O  O   . ASP A 85  ? 0.3112 0.2997 0.3925 0.0284  0.0439  -0.0615 85  ASP A O   
688  C  CB  . ASP A 85  ? 0.4541 0.2440 0.3075 0.0249  0.0148  -0.1279 85  ASP A CB  
689  C  CG  . ASP A 85  ? 0.3981 0.3190 0.4304 0.0719  0.0640  -0.0860 85  ASP A CG  
690  O  OD1 . ASP A 85  ? 0.4703 0.8216 0.4174 -0.1282 0.0645  -0.1344 85  ASP A OD1 
691  O  OD2 . ASP A 85  ? 0.5655 0.6804 0.5845 -0.0825 -0.1342 -0.1956 85  ASP A OD2 
692  N  N   . GLY A 86  ? 0.3057 0.3108 0.3747 -0.0410 -0.0824 0.0366  86  GLY A N   
693  C  CA  . GLY A 86  ? 0.3554 0.3255 0.2874 -0.1120 0.0228  0.0091  86  GLY A CA  
694  C  C   . GLY A 86  ? 0.3082 0.2868 0.2796 -0.0834 -0.0167 0.0048  86  GLY A C   
695  O  O   . GLY A 86  ? 0.3866 0.3381 0.3288 -0.1814 -0.0082 -0.0153 86  GLY A O   
696  N  N   A THR A 87  ? 0.2013 0.1719 0.2345 0.0449  0.0109  -0.0252 87  THR A N   
697  N  N   B THR A 87  ? 0.1817 0.1568 0.2180 0.0110  -0.0040 -0.0231 87  THR A N   
698  C  CA  A THR A 87  ? 0.1983 0.2356 0.2601 0.0296  0.0027  -0.0253 87  THR A CA  
699  C  CA  B THR A 87  ? 0.1655 0.1643 0.2061 0.0467  0.0414  -0.0465 87  THR A CA  
700  C  C   A THR A 87  ? 0.1817 0.1442 0.2449 -0.0051 -0.0215 -0.0450 87  THR A C   
701  C  C   B THR A 87  ? 0.1391 0.1406 0.2020 0.0087  0.0109  -0.0214 87  THR A C   
702  O  O   A THR A 87  ? 0.1577 0.1300 0.2752 0.0216  -0.0275 -0.0280 87  THR A O   
703  O  O   B THR A 87  ? 0.1577 0.1183 0.2356 0.0000  0.0320  -0.0087 87  THR A O   
704  C  CB  A THR A 87  ? 0.1720 0.2090 0.3057 0.0386  -0.0331 -0.0416 87  THR A CB  
705  C  CB  B THR A 87  ? 0.1377 0.1624 0.2583 0.0166  0.0221  -0.0344 87  THR A CB  
706  O  OG1 A THR A 87  ? 0.2500 0.3008 0.2943 0.0754  0.0040  -0.0430 87  THR A OG1 
707  O  OG1 B THR A 87  ? 0.1797 0.1755 0.2146 0.0200  0.0163  0.0205  87  THR A OG1 
708  C  CG2 A THR A 87  ? 0.1952 0.2720 0.2824 0.0467  -0.0057 -0.0205 87  THR A CG2 
709  C  CG2 B THR A 87  ? 0.1440 0.2308 0.2627 0.0781  0.0173  0.0065  87  THR A CG2 
710  N  N   . TYR A 88  ? 0.1325 0.1282 0.2013 0.0096  -0.0041 -0.0151 88  TYR A N   
711  C  CA  . TYR A 88  ? 0.1342 0.1442 0.1614 0.0154  -0.0153 -0.0126 88  TYR A CA  
712  C  C   . TYR A 88  ? 0.1199 0.1388 0.1729 0.0211  -0.0263 0.0000  88  TYR A C   
713  O  O   . TYR A 88  ? 0.1613 0.1964 0.2318 -0.0463 -0.0588 0.0198  88  TYR A O   
714  C  CB  . TYR A 88  ? 0.1093 0.1287 0.1912 0.0252  -0.0183 -0.0131 88  TYR A CB  
715  C  CG  . TYR A 88  ? 0.1194 0.1133 0.1607 0.0130  -0.0102 -0.0027 88  TYR A CG  
716  C  CD1 . TYR A 88  ? 0.1546 0.1342 0.1616 -0.0046 -0.0104 -0.0115 88  TYR A CD1 
717  C  CD2 . TYR A 88  ? 0.1224 0.1004 0.1613 0.0175  -0.0176 0.0027  88  TYR A CD2 
718  C  CE1 . TYR A 88  ? 0.1316 0.1418 0.1624 0.0218  0.0051  -0.0027 88  TYR A CE1 
719  C  CE2 . TYR A 88  ? 0.1343 0.1079 0.1375 -0.0121 -0.0035 0.0109  88  TYR A CE2 
720  C  CZ  . TYR A 88  ? 0.1309 0.1262 0.1532 0.0006  -0.0176 -0.0142 88  TYR A CZ  
721  O  OH  . TYR A 88  ? 0.1395 0.1298 0.1517 0.0065  0.0015  -0.0137 88  TYR A OH  
722  N  N   . ARG A 89  ? 0.1314 0.1070 0.1685 0.0250  -0.0131 -0.0076 89  ARG A N   
723  C  CA  . ARG A 89  ? 0.1794 0.1093 0.1606 0.0175  -0.0326 0.0043  89  ARG A CA  
724  C  C   . ARG A 89  ? 0.1225 0.1146 0.1351 -0.0013 -0.0182 0.0070  89  ARG A C   
725  O  O   . ARG A 89  ? 0.1216 0.1122 0.1439 0.0052  -0.0147 0.0049  89  ARG A O   
726  C  CB  . ARG A 89  ? 0.2274 0.1005 0.2255 0.0177  -0.0636 0.0239  89  ARG A CB  
727  C  CG  . ARG A 89  ? 0.2674 0.1618 0.2143 -0.0131 -0.0586 0.0417  89  ARG A CG  
728  C  CD  . ARG A 89  ? 0.2888 0.1586 0.2457 0.0377  -0.0119 0.0284  89  ARG A CD  
729  N  NE  . ARG A 89  ? 0.3040 0.2098 0.2446 0.0357  -0.0093 0.0542  89  ARG A NE  
730  C  CZ  . ARG A 89  ? 0.2325 0.1755 0.2161 -0.0115 -0.0175 0.0006  89  ARG A CZ  
731  N  NH1 . ARG A 89  ? 0.3445 0.1923 0.2756 0.0480  0.0599  0.0644  89  ARG A NH1 
732  N  NH2 . ARG A 89  ? 0.2763 0.2194 0.2465 0.0430  0.0233  0.0342  89  ARG A NH2 
733  N  N   . LEU A 90  ? 0.1360 0.1120 0.1483 0.0031  -0.0249 0.0065  90  LEU A N   
734  C  CA  . LEU A 90  ? 0.1368 0.1190 0.1322 -0.0031 -0.0229 0.0187  90  LEU A CA  
735  C  C   . LEU A 90  ? 0.1510 0.1345 0.1194 0.0027  -0.0414 0.0165  90  LEU A C   
736  O  O   . LEU A 90  ? 0.1719 0.1458 0.1553 0.0126  -0.0315 0.0395  90  LEU A O   
737  C  CB  . LEU A 90  ? 0.1499 0.1248 0.1639 -0.0038 -0.0243 0.0142  90  LEU A CB  
738  C  CG  . LEU A 90  ? 0.1542 0.1433 0.1512 -0.0114 -0.0302 0.0091  90  LEU A CG  
739  C  CD1 . LEU A 90  ? 0.1747 0.1264 0.1550 0.0046  -0.0329 -0.0088 90  LEU A CD1 
740  C  CD2 . LEU A 90  ? 0.1790 0.1656 0.1905 -0.0126 -0.0634 -0.0093 90  LEU A CD2 
741  N  N   . ILE A 91  ? 0.1525 0.1058 0.1230 -0.0013 -0.0142 0.0038  91  ILE A N   
742  C  CA  . ILE A 91  ? 0.1530 0.1118 0.1333 0.0020  -0.0052 -0.0007 91  ILE A CA  
743  C  C   . ILE A 91  ? 0.1400 0.0979 0.1167 0.0035  -0.0156 -0.0006 91  ILE A C   
744  O  O   . ILE A 91  ? 0.1767 0.1115 0.1124 -0.0098 -0.0229 0.0046  91  ILE A O   
745  C  CB  . ILE A 91  ? 0.1879 0.1212 0.1279 -0.0161 -0.0172 -0.0027 91  ILE A CB  
746  C  CG1 . ILE A 91  ? 0.2266 0.1561 0.1615 -0.0724 -0.0005 -0.0035 91  ILE A CG1 
747  C  CG2 . ILE A 91  ? 0.1852 0.1275 0.1474 -0.0189 -0.0275 0.0040  91  ILE A CG2 
748  C  CD1 . ILE A 91  ? 0.2322 0.2008 0.1852 -0.0775 0.0097  -0.0177 91  ILE A CD1 
749  N  N   . GLN A 92  ? 0.1536 0.0987 0.1361 0.0099  -0.0258 0.0005  92  GLN A N   
750  C  CA  . GLN A 92  ? 0.1738 0.1097 0.1190 0.0062  -0.0015 0.0200  92  GLN A CA  
751  C  C   . GLN A 92  ? 0.1415 0.1058 0.1004 -0.0125 -0.0063 0.0115  92  GLN A C   
752  O  O   . GLN A 92  ? 0.1536 0.1010 0.1036 -0.0107 -0.0173 -0.0015 92  GLN A O   
753  C  CB  . GLN A 92  ? 0.1879 0.1324 0.1273 -0.0024 -0.0262 0.0151  92  GLN A CB  
754  C  CG  . GLN A 92  ? 0.1810 0.1280 0.1771 0.0020  -0.0232 0.0196  92  GLN A CG  
755  C  CD  . GLN A 92  ? 0.1984 0.1357 0.1111 -0.0155 -0.0164 0.0175  92  GLN A CD  
756  O  OE1 . GLN A 92  ? 0.1902 0.1133 0.1410 -0.0038 -0.0274 0.0178  92  GLN A OE1 
757  N  NE2 . GLN A 92  ? 0.1879 0.1580 0.1772 -0.0110 -0.0172 0.0038  92  GLN A NE2 
758  N  N   . PHE A 93  ? 0.1615 0.0944 0.1106 0.0006  -0.0269 -0.0005 93  PHE A N   
759  C  CA  . PHE A 93  ? 0.1591 0.0903 0.1230 0.0046  -0.0215 0.0065  93  PHE A CA  
760  C  C   . PHE A 93  ? 0.1386 0.1058 0.1163 -0.0006 -0.0208 0.0015  93  PHE A C   
761  O  O   . PHE A 93  ? 0.2054 0.1102 0.1142 0.0076  -0.0285 0.0038  93  PHE A O   
762  C  CB  . PHE A 93  ? 0.1552 0.1131 0.1086 -0.0125 -0.0460 0.0076  93  PHE A CB  
763  C  CG  . PHE A 93  ? 0.1688 0.1066 0.1252 -0.0003 -0.0366 0.0062  93  PHE A CG  
764  C  CD1 . PHE A 93  ? 0.2061 0.1164 0.1263 0.0081  -0.0377 -0.0020 93  PHE A CD1 
765  C  CD2 . PHE A 93  ? 0.1940 0.1228 0.1424 0.0109  -0.0680 0.0129  93  PHE A CD2 
766  C  CE1 . PHE A 93  ? 0.1967 0.1233 0.1411 0.0131  -0.0553 0.0062  93  PHE A CE1 
767  C  CE2 . PHE A 93  ? 0.2029 0.1316 0.1577 0.0333  -0.0762 -0.0172 93  PHE A CE2 
768  C  CZ  . PHE A 93  ? 0.2074 0.1248 0.1573 0.0160  -0.0666 0.0082  93  PHE A CZ  
769  N  N   . HIS A 94  ? 0.1573 0.0957 0.1149 0.0035  -0.0280 0.0010  94  HIS A N   
770  C  CA  . HIS A 94  ? 0.1567 0.0886 0.1027 -0.0060 -0.0221 0.0120  94  HIS A CA  
771  C  C   . HIS A 94  ? 0.1217 0.1044 0.0979 -0.0043 -0.0229 0.0104  94  HIS A C   
772  O  O   . HIS A 94  ? 0.1397 0.0957 0.0943 -0.0003 -0.0080 0.0093  94  HIS A O   
773  C  CB  . HIS A 94  ? 0.1456 0.1108 0.1018 -0.0120 -0.0161 0.0113  94  HIS A CB  
774  C  CG  . HIS A 94  ? 0.1472 0.0921 0.1088 -0.0126 -0.0087 0.0057  94  HIS A CG  
775  N  ND1 . HIS A 94  ? 0.1395 0.1070 0.1124 -0.0186 -0.0214 0.0086  94  HIS A ND1 
776  C  CD2 . HIS A 94  ? 0.1557 0.1244 0.0812 -0.0165 -0.0131 0.0082  94  HIS A CD2 
777  C  CE1 . HIS A 94  ? 0.1255 0.0838 0.1243 -0.0077 -0.0220 0.0120  94  HIS A CE1 
778  N  NE2 . HIS A 94  ? 0.1263 0.1088 0.1036 -0.0049 -0.0214 0.0031  94  HIS A NE2 
779  N  N   . PHE A 95  ? 0.1395 0.1097 0.1097 0.0015  -0.0059 0.0063  95  PHE A N   
780  C  CA  . PHE A 95  ? 0.1323 0.0890 0.1199 -0.0104 -0.0137 0.0108  95  PHE A CA  
781  C  C   . PHE A 95  ? 0.1318 0.1090 0.0948 -0.0037 -0.0175 -0.0017 95  PHE A C   
782  O  O   . PHE A 95  ? 0.1383 0.1158 0.1185 -0.0020 0.0031  0.0186  95  PHE A O   
783  C  CB  . PHE A 95  ? 0.1455 0.1145 0.1124 -0.0007 -0.0306 -0.0049 95  PHE A CB  
784  C  CG  . PHE A 95  ? 0.1476 0.0995 0.1140 0.0013  -0.0313 -0.0027 95  PHE A CG  
785  C  CD1 . PHE A 95  ? 0.1688 0.1199 0.1270 0.0031  -0.0329 -0.0074 95  PHE A CD1 
786  C  CD2 . PHE A 95  ? 0.1365 0.1239 0.1201 -0.0173 -0.0318 -0.0171 95  PHE A CD2 
787  C  CE1 . PHE A 95  ? 0.1867 0.1271 0.1334 -0.0081 -0.0425 -0.0102 95  PHE A CE1 
788  C  CE2 . PHE A 95  ? 0.1571 0.1325 0.1331 0.0082  -0.0346 -0.0274 95  PHE A CE2 
789  C  CZ  . PHE A 95  ? 0.1674 0.1352 0.1437 0.0020  -0.0425 -0.0326 95  PHE A CZ  
790  N  N   . HIS A 96  ? 0.1437 0.0922 0.0886 -0.0003 -0.0142 0.0005  96  HIS A N   
791  C  CA  . HIS A 96  ? 0.1254 0.1075 0.1149 -0.0120 -0.0210 0.0093  96  HIS A CA  
792  C  C   . HIS A 96  ? 0.1036 0.1178 0.1039 -0.0087 -0.0087 0.0135  96  HIS A C   
793  O  O   . HIS A 96  ? 0.1277 0.0983 0.1206 -0.0015 0.0027  0.0024  96  HIS A O   
794  C  CB  . HIS A 96  ? 0.1185 0.0907 0.1176 -0.0097 -0.0230 -0.0115 96  HIS A CB  
795  C  CG  . HIS A 96  ? 0.1164 0.1093 0.1023 -0.0068 -0.0153 -0.0007 96  HIS A CG  
796  N  ND1 . HIS A 96  ? 0.1054 0.1030 0.1576 -0.0003 -0.0099 -0.0081 96  HIS A ND1 
797  C  CD2 . HIS A 96  ? 0.1163 0.0960 0.1090 -0.0131 -0.0076 -0.0054 96  HIS A CD2 
798  C  CE1 . HIS A 96  ? 0.1262 0.1036 0.1607 0.0054  -0.0143 -0.0151 96  HIS A CE1 
799  N  NE2 . HIS A 96  ? 0.1351 0.0750 0.1142 -0.0126 0.0031  -0.0037 96  HIS A NE2 
800  N  N   . TRP A 97  ? 0.1054 0.0992 0.1124 -0.0070 -0.0013 0.0020  97  TRP A N   
801  C  CA  . TRP A 97  ? 0.1255 0.0961 0.1254 -0.0114 -0.0063 -0.0068 97  TRP A CA  
802  C  C   . TRP A 97  ? 0.1210 0.1066 0.1176 -0.0097 -0.0142 0.0003  97  TRP A C   
803  O  O   . TRP A 97  ? 0.1370 0.1009 0.1289 -0.0098 0.0038  -0.0037 97  TRP A O   
804  C  CB  . TRP A 97  ? 0.1363 0.1203 0.1146 -0.0096 -0.0120 -0.0103 97  TRP A CB  
805  C  CG  . TRP A 97  ? 0.1454 0.1062 0.1151 -0.0104 -0.0115 -0.0207 97  TRP A CG  
806  C  CD1 . TRP A 97  ? 0.1464 0.1413 0.1149 -0.0260 0.0093  -0.0216 97  TRP A CD1 
807  C  CD2 . TRP A 97  ? 0.1606 0.1108 0.1106 -0.0237 -0.0040 -0.0120 97  TRP A CD2 
808  N  NE1 . TRP A 97  ? 0.1896 0.1273 0.1208 -0.0220 0.0175  -0.0148 97  TRP A NE1 
809  C  CE2 . TRP A 97  ? 0.1877 0.1234 0.1018 -0.0252 0.0052  -0.0143 97  TRP A CE2 
810  C  CE3 . TRP A 97  ? 0.1594 0.1097 0.1067 -0.0057 -0.0240 -0.0031 97  TRP A CE3 
811  C  CZ2 . TRP A 97  ? 0.1861 0.1330 0.1187 -0.0291 -0.0037 0.0046  97  TRP A CZ2 
812  C  CZ3 . TRP A 97  ? 0.1846 0.1327 0.1031 -0.0274 -0.0080 0.0043  97  TRP A CZ3 
813  C  CH2 . TRP A 97  ? 0.2092 0.1206 0.0974 -0.0302 -0.0017 -0.0143 97  TRP A CH2 
814  N  N   . GLY A 98  ? 0.1524 0.0942 0.1172 -0.0080 -0.0013 -0.0057 98  GLY A N   
815  C  CA  . GLY A 98  ? 0.1527 0.1254 0.1156 0.0120  0.0023  -0.0038 98  GLY A CA  
816  C  C   . GLY A 98  ? 0.1431 0.1093 0.1313 -0.0049 0.0065  -0.0049 98  GLY A C   
817  O  O   . GLY A 98  ? 0.1648 0.1199 0.1528 -0.0143 -0.0155 -0.0143 98  GLY A O   
818  N  N   . SER A 99  ? 0.1632 0.1131 0.1404 0.0026  0.0175  -0.0219 99  SER A N   
819  C  CA  . SER A 99  ? 0.1817 0.1523 0.1499 -0.0171 0.0432  -0.0509 99  SER A CA  
820  C  C   . SER A 99  ? 0.2056 0.1316 0.1729 0.0080  0.0000  -0.0551 99  SER A C   
821  O  O   . SER A 99  ? 0.2540 0.1745 0.1789 -0.0113 0.0048  -0.0384 99  SER A O   
822  C  CB  . SER A 99  ? 0.2126 0.1555 0.1864 0.0114  0.0296  -0.0445 99  SER A CB  
823  O  OG  . SER A 99  ? 0.1762 0.1349 0.2328 0.0051  0.0162  -0.0291 99  SER A OG  
824  N  N   . LEU A 100 ? 0.1567 0.1239 0.2040 -0.0126 0.0162  -0.0355 100 LEU A N   
825  C  CA  . LEU A 100 ? 0.1956 0.0891 0.2541 0.0006  0.0294  -0.0337 100 LEU A CA  
826  C  C   . LEU A 100 ? 0.1781 0.1120 0.2025 -0.0277 0.0052  -0.0285 100 LEU A C   
827  O  O   . LEU A 100 ? 0.1650 0.1160 0.1914 0.0027  0.0043  -0.0175 100 LEU A O   
828  C  CB  . LEU A 100 ? 0.2670 0.1985 0.2989 0.0546  0.0619  0.0419  100 LEU A CB  
829  C  CG  . LEU A 100 ? 0.2533 0.2670 0.3075 0.0527  0.0273  0.0115  100 LEU A CG  
830  C  CD1 . LEU A 100 ? 0.4049 0.3784 0.3970 0.2451  -0.0485 -0.0491 100 LEU A CD1 
831  C  CD2 . LEU A 100 ? 0.4332 0.2735 0.4541 -0.0118 0.2003  -0.1377 100 LEU A CD2 
832  N  N   . ASP A 101 ? 0.1740 0.1174 0.2144 -0.0063 -0.0006 -0.0148 101 ASP A N   
833  C  CA  . ASP A 101 ? 0.1774 0.1120 0.1914 -0.0276 0.0135  0.0171  101 ASP A CA  
834  C  C   . ASP A 101 ? 0.1638 0.1058 0.2168 0.0054  0.0215  0.0174  101 ASP A C   
835  O  O   . ASP A 101 ? 0.2225 0.1366 0.2117 0.0098  0.0265  0.0146  101 ASP A O   
836  C  CB  . ASP A 101 ? 0.1835 0.1325 0.2124 -0.0165 -0.0162 0.0287  101 ASP A CB  
837  C  CG  . ASP A 101 ? 0.1826 0.1729 0.2630 -0.0318 -0.0166 0.0041  101 ASP A CG  
838  O  OD1 . ASP A 101 ? 0.2186 0.1758 0.2055 -0.0277 -0.0041 -0.0110 101 ASP A OD1 
839  O  OD2 . ASP A 101 ? 0.2835 0.2171 0.2749 -0.0952 -0.0384 0.0074  101 ASP A OD2 
840  N  N   . GLY A 102 ? 0.1738 0.1260 0.2137 -0.0313 -0.0126 0.0253  102 GLY A N   
841  C  CA  . GLY A 102 ? 0.2358 0.1167 0.2176 -0.0328 0.0041  0.0377  102 GLY A CA  
842  C  C   . GLY A 102 ? 0.1790 0.1508 0.1712 0.0104  0.0082  0.0186  102 GLY A C   
843  O  O   . GLY A 102 ? 0.2019 0.1333 0.1893 0.0038  0.0196  0.0273  102 GLY A O   
844  N  N   . GLN A 103 ? 0.1507 0.1063 0.1774 -0.0126 0.0034  0.0152  103 GLN A N   
845  C  CA  . GLN A 103 ? 0.1480 0.1331 0.1340 0.0098  -0.0012 -0.0019 103 GLN A CA  
846  C  C   . GLN A 103 ? 0.1342 0.1106 0.1412 0.0104  0.0070  0.0054  103 GLN A C   
847  O  O   . GLN A 103 ? 0.1591 0.1079 0.1488 -0.0060 0.0015  -0.0013 103 GLN A O   
848  C  CB  . GLN A 103 ? 0.1612 0.1360 0.1550 0.0326  0.0081  0.0126  103 GLN A CB  
849  C  CG  . GLN A 103 ? 0.1688 0.1388 0.1709 0.0274  0.0340  0.0120  103 GLN A CG  
850  C  CD  . GLN A 103 ? 0.1967 0.1800 0.2249 0.0571  0.0568  0.0610  103 GLN A CD  
851  O  OE1 . GLN A 103 ? 0.3230 0.3054 0.3729 0.1817  0.1670  0.1667  103 GLN A OE1 
852  N  NE2 . GLN A 103 ? 0.1792 0.1905 0.2338 0.0511  0.0392  0.0305  103 GLN A NE2 
853  N  N   . GLY A 104 ? 0.1203 0.1215 0.1208 0.0043  0.0080  -0.0010 104 GLY A N   
854  C  CA  . GLY A 104 ? 0.1411 0.1058 0.1217 0.0137  0.0030  -0.0027 104 GLY A CA  
855  C  C   . GLY A 104 ? 0.1072 0.1045 0.1263 -0.0031 -0.0081 -0.0074 104 GLY A C   
856  O  O   . GLY A 104 ? 0.1314 0.1128 0.1336 -0.0208 -0.0030 0.0046  104 GLY A O   
857  N  N   . SER A 105 ? 0.1036 0.1203 0.1072 0.0023  0.0109  -0.0113 105 SER A N   
858  C  CA  . SER A 105 ? 0.1032 0.1151 0.1120 -0.0035 -0.0038 -0.0118 105 SER A CA  
859  C  C   . SER A 105 ? 0.0891 0.0878 0.1070 0.0015  0.0017  0.0125  105 SER A C   
860  O  O   . SER A 105 ? 0.1192 0.1054 0.1282 0.0110  -0.0163 -0.0038 105 SER A O   
861  C  CB  . SER A 105 ? 0.0942 0.1172 0.1262 0.0043  0.0024  0.0093  105 SER A CB  
862  O  OG  . SER A 105 ? 0.1262 0.0991 0.1381 0.0034  0.0054  -0.0015 105 SER A OG  
863  N  N   . GLU A 106 ? 0.0996 0.0917 0.1129 0.0020  -0.0040 0.0015  106 GLU A N   
864  C  CA  . GLU A 106 ? 0.1086 0.0935 0.0986 -0.0070 -0.0118 -0.0031 106 GLU A CA  
865  C  C   . GLU A 106 ? 0.1036 0.0788 0.1102 -0.0073 -0.0163 -0.0108 106 GLU A C   
866  O  O   . GLU A 106 ? 0.0996 0.1086 0.1263 0.0046  -0.0059 0.0027  106 GLU A O   
867  C  CB  . GLU A 106 ? 0.1115 0.0952 0.0939 -0.0091 0.0023  0.0007  106 GLU A CB  
868  C  CG  . GLU A 106 ? 0.1316 0.0979 0.1333 -0.0088 0.0093  0.0043  106 GLU A CG  
869  C  CD  . GLU A 106 ? 0.1167 0.1158 0.1111 0.0068  0.0003  -0.0104 106 GLU A CD  
870  O  OE1 . GLU A 106 ? 0.0851 0.1068 0.1304 -0.0109 0.0005  -0.0086 106 GLU A OE1 
871  O  OE2 . GLU A 106 ? 0.1129 0.1360 0.1518 0.0024  0.0077  -0.0132 106 GLU A OE2 
872  N  N   . HIS A 107 ? 0.1041 0.0939 0.1061 0.0098  -0.0082 0.0000  107 HIS A N   
873  C  CA  . HIS A 107 ? 0.1000 0.0997 0.1010 0.0087  -0.0027 -0.0010 107 HIS A CA  
874  C  C   . HIS A 107 ? 0.0931 0.1137 0.0877 0.0148  -0.0046 -0.0013 107 HIS A C   
875  O  O   . HIS A 107 ? 0.1149 0.1001 0.1133 0.0003  -0.0030 0.0043  107 HIS A O   
876  C  CB  . HIS A 107 ? 0.1208 0.0970 0.1061 0.0020  -0.0043 -0.0087 107 HIS A CB  
877  C  CG  . HIS A 107 ? 0.0904 0.1066 0.1084 0.0054  -0.0038 0.0049  107 HIS A CG  
878  N  ND1 . HIS A 107 ? 0.1062 0.1053 0.1129 0.0017  -0.0126 0.0046  107 HIS A ND1 
879  C  CD2 . HIS A 107 ? 0.0876 0.0944 0.1255 0.0156  -0.0131 -0.0124 107 HIS A CD2 
880  C  CE1 . HIS A 107 ? 0.1061 0.0899 0.1282 0.0000  -0.0062 -0.0038 107 HIS A CE1 
881  N  NE2 . HIS A 107 ? 0.0916 0.0988 0.1145 0.0103  -0.0113 -0.0136 107 HIS A NE2 
882  N  N   . THR A 108 ? 0.1079 0.1155 0.1154 -0.0071 0.0015  0.0130  108 THR A N   
883  C  CA  . THR A 108 ? 0.1099 0.0925 0.1224 0.0063  -0.0031 0.0027  108 THR A CA  
884  C  C   . THR A 108 ? 0.1160 0.0966 0.1048 0.0096  -0.0074 0.0020  108 THR A C   
885  O  O   . THR A 108 ? 0.1196 0.1068 0.1331 0.0052  -0.0048 0.0065  108 THR A O   
886  C  CB  . THR A 108 ? 0.1084 0.1212 0.1316 0.0153  -0.0098 0.0031  108 THR A CB  
887  O  OG1 . THR A 108 ? 0.1379 0.1156 0.1375 0.0176  -0.0197 0.0024  108 THR A OG1 
888  C  CG2 . THR A 108 ? 0.1489 0.1194 0.1251 0.0148  0.0071  -0.0006 108 THR A CG2 
889  N  N   . VAL A 109 ? 0.1298 0.1009 0.1251 -0.0010 0.0000  0.0059  109 VAL A N   
890  C  CA  . VAL A 109 ? 0.1278 0.1151 0.1316 0.0017  0.0109  0.0172  109 VAL A CA  
891  C  C   . VAL A 109 ? 0.1528 0.1049 0.1386 -0.0131 0.0012  0.0207  109 VAL A C   
892  O  O   . VAL A 109 ? 0.1424 0.1137 0.1571 -0.0068 0.0060  0.0195  109 VAL A O   
893  C  CB  . VAL A 109 ? 0.1322 0.1291 0.1494 0.0063  -0.0038 0.0205  109 VAL A CB  
894  C  CG1 . VAL A 109 ? 0.1266 0.1668 0.1659 0.0040  0.0205  0.0370  109 VAL A CG1 
895  C  CG2 . VAL A 109 ? 0.1552 0.1485 0.1713 0.0082  -0.0137 0.0306  109 VAL A CG2 
896  N  N   . ASP A 110 ? 0.1643 0.1323 0.1291 0.0197  0.0062  0.0208  110 ASP A N   
897  C  CA  . ASP A 110 ? 0.1909 0.1352 0.1341 0.0214  0.0285  0.0390  110 ASP A CA  
898  C  C   . ASP A 110 ? 0.1835 0.1181 0.1532 0.0126  0.0046  0.0151  110 ASP A C   
899  O  O   . ASP A 110 ? 0.1979 0.1246 0.1494 0.0233  0.0019  0.0230  110 ASP A O   
900  C  CB  . ASP A 110 ? 0.2008 0.1621 0.1880 0.0186  0.0527  0.0443  110 ASP A CB  
901  C  CG  . ASP A 110 ? 0.2044 0.1762 0.1832 0.0109  0.0244  0.0527  110 ASP A CG  
902  O  OD1 . ASP A 110 ? 0.2313 0.1745 0.2016 0.0236  0.0533  0.0346  110 ASP A OD1 
903  O  OD2 . ASP A 110 ? 0.2180 0.2483 0.2204 0.0381  0.0458  0.0397  110 ASP A OD2 
904  N  N   . LYS A 111 ? 0.1422 0.1388 0.1359 0.0130  -0.0054 0.0185  111 LYS A N   
905  C  CA  . LYS A 111 ? 0.1627 0.1288 0.1454 0.0337  -0.0207 0.0065  111 LYS A CA  
906  C  C   . LYS A 111 ? 0.1747 0.1066 0.1391 0.0102  -0.0006 0.0175  111 LYS A C   
907  O  O   . LYS A 111 ? 0.1562 0.1615 0.1564 0.0098  0.0035  0.0000  111 LYS A O   
908  C  CB  . LYS A 111 ? 0.1867 0.1591 0.1620 0.0450  -0.0151 0.0291  111 LYS A CB  
909  C  CG  . LYS A 111 ? 0.2845 0.2189 0.1823 0.1010  -0.0619 0.0302  111 LYS A CG  
910  C  CD  . LYS A 111 ? 0.2317 0.2892 0.2601 0.0494  -0.1014 -0.0688 111 LYS A CD  
911  C  CE  . LYS A 111 ? 0.2875 0.3467 0.2605 0.0755  -0.0890 -0.0397 111 LYS A CE  
912  N  NZ  . LYS A 111 ? 0.2087 0.3636 0.4143 -0.0040 -0.1171 0.0493  111 LYS A NZ  
913  N  N   . LYS A 112 ? 0.1656 0.1041 0.1312 0.0142  -0.0099 0.0175  112 LYS A N   
914  C  CA  . LYS A 112 ? 0.1458 0.1595 0.1368 0.0071  0.0126  0.0135  112 LYS A CA  
915  C  C   . LYS A 112 ? 0.1254 0.1309 0.1246 0.0024  -0.0049 0.0077  112 LYS A C   
916  O  O   . LYS A 112 ? 0.1585 0.1160 0.1282 0.0054  -0.0068 -0.0034 112 LYS A O   
917  C  CB  . LYS A 112 ? 0.1471 0.1634 0.1577 -0.0263 -0.0031 0.0010  112 LYS A CB  
918  C  CG  . LYS A 112 ? 0.1606 0.1959 0.1783 -0.0148 -0.0085 -0.0294 112 LYS A CG  
919  C  CD  . LYS A 112 ? 0.1436 0.2512 0.2354 0.0065  -0.0423 0.0130  112 LYS A CD  
920  C  CE  . LYS A 112 ? 0.2675 0.1648 0.2573 -0.0313 -0.0582 0.0135  112 LYS A CE  
921  N  NZ  . LYS A 112 ? 0.2431 0.1780 0.2424 -0.0153 -0.0439 0.0220  112 LYS A NZ  
922  N  N   A LYS A 113 ? 0.1354 0.1230 0.1235 0.0276  -0.0038 0.0119  113 LYS A N   
923  N  N   B LYS A 113 ? 0.1438 0.1264 0.1244 0.0147  -0.0073 0.0027  113 LYS A N   
924  C  CA  A LYS A 113 ? 0.1368 0.1429 0.1133 0.0131  0.0060  0.0115  113 LYS A CA  
925  C  CA  B LYS A 113 ? 0.1528 0.1305 0.1239 0.0153  -0.0013 0.0034  113 LYS A CA  
926  C  C   A LYS A 113 ? 0.1297 0.1133 0.1217 -0.0176 0.0209  0.0430  113 LYS A C   
927  C  C   B LYS A 113 ? 0.1476 0.1031 0.1474 0.0274  -0.0020 -0.0076 113 LYS A C   
928  O  O   A LYS A 113 ? 0.1401 0.0930 0.1510 -0.0104 0.0285  0.0228  113 LYS A O   
929  O  O   B LYS A 113 ? 0.1284 0.0992 0.1172 0.0060  0.0000  0.0031  113 LYS A O   
930  C  CB  A LYS A 113 ? 0.1485 0.1102 0.1289 -0.0062 0.0076  -0.0068 113 LYS A CB  
931  C  CB  B LYS A 113 ? 0.1541 0.1324 0.1476 0.0091  -0.0082 0.0062  113 LYS A CB  
932  C  CG  A LYS A 113 ? 0.1303 0.1401 0.1145 0.0048  0.0109  0.0226  113 LYS A CG  
933  C  CG  B LYS A 113 ? 0.1438 0.1738 0.1532 0.0269  -0.0172 -0.0318 113 LYS A CG  
934  C  CD  A LYS A 113 ? 0.1129 0.1684 0.1837 0.0080  0.0041  -0.0355 113 LYS A CD  
935  C  CD  B LYS A 113 ? 0.1391 0.1844 0.1524 0.0340  0.0087  0.0017  113 LYS A CD  
936  C  CE  A LYS A 113 ? 0.1305 0.1639 0.1958 0.0339  -0.0065 -0.0286 113 LYS A CE  
937  C  CE  B LYS A 113 ? 0.1783 0.2440 0.1776 0.0208  -0.0346 0.0012  113 LYS A CE  
938  N  NZ  A LYS A 113 ? 0.1449 0.2529 0.2019 0.0306  -0.0284 -0.0087 113 LYS A NZ  
939  N  NZ  B LYS A 113 ? 0.1697 0.2232 0.2442 0.0086  -0.0104 -0.0137 113 LYS A NZ  
940  N  N   . TYR A 114 ? 0.1079 0.1049 0.1406 0.0082  -0.0076 0.0041  114 TYR A N   
941  C  CA  . TYR A 114 ? 0.1113 0.1133 0.1345 0.0020  -0.0176 0.0214  114 TYR A CA  
942  C  C   . TYR A 114 ? 0.1312 0.0943 0.1248 -0.0006 -0.0195 0.0148  114 TYR A C   
943  O  O   . TYR A 114 ? 0.1261 0.1163 0.1386 -0.0043 0.0035  -0.0046 114 TYR A O   
944  C  CB  . TYR A 114 ? 0.1316 0.0982 0.1386 0.0041  0.0024  0.0068  114 TYR A CB  
945  C  CG  . TYR A 114 ? 0.1237 0.1093 0.1347 0.0121  -0.0222 0.0164  114 TYR A CG  
946  C  CD1 . TYR A 114 ? 0.1649 0.1076 0.1485 0.0210  0.0027  0.0151  114 TYR A CD1 
947  C  CD2 . TYR A 114 ? 0.1246 0.1040 0.1958 -0.0107 -0.0010 0.0140  114 TYR A CD2 
948  C  CE1 . TYR A 114 ? 0.1870 0.1614 0.1494 0.0284  0.0140  0.0239  114 TYR A CE1 
949  C  CE2 . TYR A 114 ? 0.1582 0.1460 0.2034 -0.0006 0.0283  0.0003  114 TYR A CE2 
950  C  CZ  . TYR A 114 ? 0.1659 0.1634 0.1999 0.0140  0.0458  0.0208  114 TYR A CZ  
951  O  OH  . TYR A 114 ? 0.2383 0.2560 0.2325 0.0219  0.0825  0.0219  114 TYR A OH  
952  N  N   . ALA A 115 ? 0.1372 0.0935 0.1333 -0.0148 -0.0252 0.0006  115 ALA A N   
953  C  CA  . ALA A 115 ? 0.1339 0.0842 0.1314 -0.0205 -0.0063 -0.0054 115 ALA A CA  
954  C  C   . ALA A 115 ? 0.1342 0.0988 0.1252 -0.0087 -0.0034 0.0027  115 ALA A C   
955  O  O   . ALA A 115 ? 0.1345 0.0986 0.1460 -0.0126 0.0063  -0.0068 115 ALA A O   
956  C  CB  . ALA A 115 ? 0.1703 0.1013 0.1523 -0.0274 -0.0249 -0.0121 115 ALA A CB  
957  N  N   . ALA A 116 ? 0.1316 0.0930 0.1370 -0.0068 -0.0110 -0.0103 116 ALA A N   
958  C  CA  . ALA A 116 ? 0.1273 0.1070 0.1199 -0.0068 -0.0087 -0.0119 116 ALA A CA  
959  C  C   . ALA A 116 ? 0.1041 0.1088 0.1010 -0.0003 -0.0103 0.0057  116 ALA A C   
960  O  O   . ALA A 116 ? 0.1165 0.1014 0.1079 0.0000  -0.0006 0.0048  116 ALA A O   
961  C  CB  . ALA A 116 ? 0.1386 0.1158 0.1264 -0.0054 -0.0024 0.0027  116 ALA A CB  
962  N  N   . GLU A 117 ? 0.1309 0.0869 0.1111 0.0000  -0.0110 0.0007  117 GLU A N   
963  C  CA  . GLU A 117 ? 0.1246 0.1062 0.1032 0.0087  -0.0165 -0.0019 117 GLU A CA  
964  C  C   . GLU A 117 ? 0.1199 0.1000 0.0900 0.0068  0.0007  0.0068  117 GLU A C   
965  O  O   . GLU A 117 ? 0.1194 0.1169 0.1253 0.0175  0.0006  0.0210  117 GLU A O   
966  C  CB  . GLU A 117 ? 0.1254 0.1048 0.1093 -0.0063 -0.0013 -0.0115 117 GLU A CB  
967  C  CG  . GLU A 117 ? 0.1208 0.1176 0.1154 -0.0043 -0.0188 -0.0013 117 GLU A CG  
968  C  CD  . GLU A 117 ? 0.1001 0.1018 0.1118 0.0060  0.0065  0.0023  117 GLU A CD  
969  O  OE1 . GLU A 117 ? 0.1146 0.1230 0.1215 0.0093  -0.0148 0.0027  117 GLU A OE1 
970  O  OE2 . GLU A 117 ? 0.1368 0.1124 0.1217 -0.0076 -0.0209 0.0020  117 GLU A OE2 
971  N  N   . LEU A 118 ? 0.1088 0.0900 0.1088 -0.0017 -0.0197 0.0060  118 LEU A N   
972  C  CA  . LEU A 118 ? 0.1264 0.0741 0.1086 -0.0003 -0.0296 0.0010  118 LEU A CA  
973  C  C   . LEU A 118 ? 0.1040 0.0832 0.1032 -0.0054 -0.0080 0.0026  118 LEU A C   
974  O  O   . LEU A 118 ? 0.1054 0.0900 0.1009 -0.0086 -0.0091 -0.0043 118 LEU A O   
975  C  CB  . LEU A 118 ? 0.1167 0.1049 0.1298 0.0093  -0.0463 -0.0049 118 LEU A CB  
976  C  CG  . LEU A 118 ? 0.1142 0.1163 0.1253 0.0125  -0.0410 0.0174  118 LEU A CG  
977  C  CD1 . LEU A 118 ? 0.1436 0.1252 0.1437 -0.0048 -0.0373 0.0207  118 LEU A CD1 
978  C  CD2 . LEU A 118 ? 0.1106 0.1537 0.1588 0.0000  -0.0478 0.0068  118 LEU A CD2 
979  N  N   . HIS A 119 ? 0.1140 0.0816 0.1008 -0.0076 -0.0208 0.0076  119 HIS A N   
980  C  CA  . HIS A 119 ? 0.1000 0.0864 0.1088 -0.0087 -0.0233 0.0041  119 HIS A CA  
981  C  C   . HIS A 119 ? 0.0983 0.0957 0.1088 -0.0115 -0.0174 -0.0019 119 HIS A C   
982  O  O   . HIS A 119 ? 0.1303 0.0961 0.1070 -0.0054 -0.0148 0.0023  119 HIS A O   
983  C  CB  . HIS A 119 ? 0.1005 0.0930 0.1145 0.0087  -0.0244 0.0049  119 HIS A CB  
984  C  CG  . HIS A 119 ? 0.0837 0.1036 0.0970 0.0020  -0.0093 -0.0035 119 HIS A CG  
985  N  ND1 . HIS A 119 ? 0.0973 0.1004 0.0960 -0.0062 0.0038  0.0052  119 HIS A ND1 
986  C  CD2 . HIS A 119 ? 0.1005 0.0943 0.1030 -0.0020 -0.0209 0.0024  119 HIS A CD2 
987  C  CE1 . HIS A 119 ? 0.1136 0.1149 0.0991 -0.0062 -0.0135 0.0015  119 HIS A CE1 
988  N  NE2 . HIS A 119 ? 0.0995 0.1088 0.1128 -0.0006 -0.0208 0.0038  119 HIS A NE2 
989  N  N   . LEU A 120 ? 0.1149 0.0908 0.1079 0.0052  -0.0207 -0.0017 120 LEU A N   
990  C  CA  . LEU A 120 ? 0.1268 0.0859 0.1199 0.0074  -0.0282 0.0046  120 LEU A CA  
991  C  C   . LEU A 120 ? 0.0842 0.0843 0.0961 0.0104  -0.0153 0.0085  120 LEU A C   
992  O  O   . LEU A 120 ? 0.1142 0.0935 0.1019 -0.0093 -0.0175 0.0077  120 LEU A O   
993  C  CB  . LEU A 120 ? 0.1142 0.1040 0.1343 -0.0113 -0.0230 -0.0070 120 LEU A CB  
994  C  CG  . LEU A 120 ? 0.1384 0.1212 0.1366 -0.0132 -0.0428 0.0049  120 LEU A CG  
995  C  CD1 . LEU A 120 ? 0.2019 0.1533 0.1785 -0.0767 -0.0282 0.0049  120 LEU A CD1 
996  C  CD2 . LEU A 120 ? 0.1668 0.1659 0.1533 0.0010  -0.0661 -0.0088 120 LEU A CD2 
997  N  N   . VAL A 121 ? 0.1097 0.1075 0.1131 -0.0060 -0.0097 0.0186  121 VAL A N   
998  C  CA  . VAL A 121 ? 0.1219 0.0837 0.1190 -0.0065 -0.0167 0.0038  121 VAL A CA  
999  C  C   . VAL A 121 ? 0.1226 0.1053 0.1040 -0.0103 -0.0153 0.0076  121 VAL A C   
1000 O  O   . VAL A 121 ? 0.1343 0.1032 0.1185 0.0013  -0.0252 0.0013  121 VAL A O   
1001 C  CB  . VAL A 121 ? 0.1263 0.0938 0.1252 -0.0076 -0.0097 0.0107  121 VAL A CB  
1002 C  CG1 . VAL A 121 ? 0.1512 0.1208 0.1255 -0.0320 -0.0031 0.0097  121 VAL A CG1 
1003 C  CG2 . VAL A 121 ? 0.1254 0.1005 0.1298 0.0091  -0.0074 0.0012  121 VAL A CG2 
1004 N  N   . HIS A 122 ? 0.1115 0.1052 0.1172 0.0091  -0.0153 0.0049  122 HIS A N   
1005 C  CA  . HIS A 122 ? 0.1185 0.0886 0.1352 0.0006  -0.0167 0.0130  122 HIS A CA  
1006 C  C   . HIS A 122 ? 0.1185 0.1140 0.1215 -0.0034 -0.0135 0.0046  122 HIS A C   
1007 O  O   . HIS A 122 ? 0.1372 0.1000 0.1341 -0.0120 -0.0241 0.0062  122 HIS A O   
1008 C  CB  . HIS A 122 ? 0.1146 0.0966 0.1465 0.0049  -0.0093 0.0063  122 HIS A CB  
1009 C  CG  . HIS A 122 ? 0.1359 0.0988 0.1225 -0.0020 -0.0034 0.0003  122 HIS A CG  
1010 N  ND1 . HIS A 122 ? 0.1325 0.0860 0.1419 -0.0005 -0.0082 0.0076  122 HIS A ND1 
1011 C  CD2 . HIS A 122 ? 0.1288 0.1342 0.1395 -0.0236 -0.0211 0.0019  122 HIS A CD2 
1012 C  CE1 . HIS A 122 ? 0.0930 0.1181 0.1500 0.0024  -0.0091 -0.0041 122 HIS A CE1 
1013 N  NE2 . HIS A 122 ? 0.1072 0.1248 0.1429 -0.0109 -0.0065 -0.0005 122 HIS A NE2 
1014 N  N   . TRP A 123 ? 0.1156 0.1018 0.1291 -0.0074 -0.0156 0.0010  123 TRP A N   
1015 C  CA  . TRP A 123 ? 0.1388 0.0819 0.1406 -0.0049 -0.0057 -0.0126 123 TRP A CA  
1016 C  C   . TRP A 123 ? 0.1129 0.0881 0.1409 0.0024  -0.0126 0.0043  123 TRP A C   
1017 O  O   . TRP A 123 ? 0.1212 0.1014 0.1613 0.0093  -0.0219 -0.0054 123 TRP A O   
1018 C  CB  . TRP A 123 ? 0.1361 0.1598 0.1379 -0.0252 -0.0215 -0.0046 123 TRP A CB  
1019 C  CG  . TRP A 123 ? 0.1652 0.1140 0.1516 -0.0297 -0.0010 0.0104  123 TRP A CG  
1020 C  CD1 . TRP A 123 ? 0.1878 0.1324 0.1370 -0.0148 -0.0142 0.0147  123 TRP A CD1 
1021 C  CD2 . TRP A 123 ? 0.2107 0.0978 0.1679 -0.0302 -0.0131 0.0000  123 TRP A CD2 
1022 N  NE1 . TRP A 123 ? 0.2169 0.0886 0.1765 -0.0244 -0.0196 0.0091  123 TRP A NE1 
1023 C  CE2 . TRP A 123 ? 0.2483 0.0943 0.1808 -0.0384 -0.0252 0.0155  123 TRP A CE2 
1024 C  CE3 . TRP A 123 ? 0.2885 0.0820 0.1873 -0.0627 0.0027  0.0098  123 TRP A CE3 
1025 C  CZ2 . TRP A 123 ? 0.3054 0.0939 0.1993 -0.0126 0.0109  0.0054  123 TRP A CZ2 
1026 C  CZ3 . TRP A 123 ? 0.3176 0.0996 0.1794 -0.0494 -0.0037 0.0108  123 TRP A CZ3 
1027 C  CH2 . TRP A 123 ? 0.3361 0.1169 0.1871 -0.0218 0.0017  0.0200  123 TRP A CH2 
1028 N  N   . ASN A 124 ? 0.1242 0.0995 0.1413 0.0065  -0.0159 -0.0175 124 ASN A N   
1029 C  CA  . ASN A 124 ? 0.1489 0.0882 0.1490 0.0060  -0.0160 -0.0178 124 ASN A CA  
1030 C  C   . ASN A 124 ? 0.1448 0.0961 0.1589 0.0152  -0.0173 -0.0273 124 ASN A C   
1031 O  O   . ASN A 124 ? 0.1352 0.1164 0.1462 -0.0031 -0.0074 -0.0046 124 ASN A O   
1032 C  CB  . ASN A 124 ? 0.1580 0.1330 0.1336 0.0012  0.0051  -0.0126 124 ASN A CB  
1033 C  CG  . ASN A 124 ? 0.1397 0.1297 0.1377 -0.0154 0.0013  -0.0151 124 ASN A CG  
1034 O  OD1 . ASN A 124 ? 0.1745 0.1174 0.1810 0.0244  -0.0034 -0.0207 124 ASN A OD1 
1035 N  ND2 . ASN A 124 ? 0.2134 0.1381 0.1471 -0.0043 -0.0003 -0.0252 124 ASN A ND2 
1036 N  N   . THR A 125 ? 0.1386 0.1070 0.1788 0.0373  -0.0193 -0.0120 125 THR A N   
1037 C  CA  . THR A 125 ? 0.1835 0.1075 0.1938 0.0266  -0.0259 0.0049  125 THR A CA  
1038 C  C   . THR A 125 ? 0.2013 0.1072 0.1934 0.0284  0.0104  -0.0098 125 THR A C   
1039 O  O   . THR A 125 ? 0.2072 0.1272 0.2207 0.0209  -0.0258 0.0020  125 THR A O   
1040 C  CB  . THR A 125 ? 0.1683 0.1606 0.2363 0.0175  -0.0542 0.0166  125 THR A CB  
1041 O  OG1 . THR A 125 ? 0.2365 0.1959 0.3302 0.0953  0.0020  0.0167  125 THR A OG1 
1042 C  CG2 . THR A 125 ? 0.1999 0.1571 0.2900 0.0063  -0.1085 -0.0115 125 THR A CG2 
1043 N  N   . LYS A 126 ? 0.1961 0.0944 0.1808 0.0155  0.0062  -0.0219 127 LYS A N   
1044 C  CA  . LYS A 126 ? 0.2182 0.1264 0.1747 -0.0065 0.0093  -0.0423 127 LYS A CA  
1045 C  C   . LYS A 126 ? 0.1791 0.1167 0.1720 -0.0120 -0.0131 -0.0049 127 LYS A C   
1046 O  O   . LYS A 126 ? 0.2250 0.1235 0.2381 -0.0218 -0.0005 -0.0348 127 LYS A O   
1047 C  CB  . LYS A 126 ? 0.2486 0.1343 0.1826 -0.0197 -0.0192 -0.0340 127 LYS A CB  
1048 C  CG  . LYS A 126 ? 0.2257 0.2022 0.1767 -0.0155 -0.0274 -0.0057 127 LYS A CG  
1049 C  CD  . LYS A 126 ? 0.3021 0.2559 0.2055 -0.0469 -0.0328 -0.0183 127 LYS A CD  
1050 C  CE  . LYS A 126 ? 0.2274 0.2832 0.2921 -0.0012 -0.0099 -0.0335 127 LYS A CE  
1051 N  NZ  . LYS A 126 ? 0.5411 0.3787 0.2169 0.1783  0.0241  0.0241  127 LYS A NZ  
1052 N  N   . TYR A 127 ? 0.1771 0.1212 0.1517 0.0043  -0.0073 -0.0031 128 TYR A N   
1053 C  CA  . TYR A 127 ? 0.1878 0.1133 0.1588 -0.0027 -0.0315 0.0005  128 TYR A CA  
1054 C  C   . TYR A 127 ? 0.1703 0.1115 0.1749 -0.0259 -0.0041 -0.0227 128 TYR A C   
1055 O  O   . TYR A 127 ? 0.1853 0.1246 0.1746 -0.0142 -0.0031 -0.0024 128 TYR A O   
1056 C  CB  . TYR A 127 ? 0.1729 0.1172 0.1861 -0.0027 0.0020  -0.0104 128 TYR A CB  
1057 C  CG  . TYR A 127 ? 0.1740 0.1217 0.1560 0.0041  -0.0207 -0.0131 128 TYR A CG  
1058 C  CD1 . TYR A 127 ? 0.1738 0.1228 0.1807 -0.0070 0.0046  -0.0120 128 TYR A CD1 
1059 C  CD2 . TYR A 127 ? 0.1659 0.1131 0.1597 -0.0024 -0.0059 -0.0126 128 TYR A CD2 
1060 C  CE1 . TYR A 127 ? 0.1995 0.1312 0.1594 0.0136  -0.0060 -0.0228 128 TYR A CE1 
1061 C  CE2 . TYR A 127 ? 0.1754 0.1377 0.1488 0.0129  -0.0073 -0.0226 128 TYR A CE2 
1062 C  CZ  . TYR A 127 ? 0.1824 0.1412 0.1449 0.0171  -0.0166 -0.0285 128 TYR A CZ  
1063 O  OH  . TYR A 127 ? 0.2465 0.1463 0.1621 0.0109  -0.0208 -0.0337 128 TYR A OH  
1064 N  N   . GLY A 128 ? 0.1798 0.1176 0.1446 -0.0140 -0.0199 0.0054  129 GLY A N   
1065 C  CA  . GLY A 128 ? 0.2115 0.1252 0.1634 -0.0092 0.0131  0.0104  129 GLY A CA  
1066 C  C   . GLY A 128 ? 0.2122 0.1293 0.1342 -0.0015 -0.0164 0.0197  129 GLY A C   
1067 O  O   . GLY A 128 ? 0.2813 0.1111 0.1783 0.0003  -0.0205 0.0174  129 GLY A O   
1068 N  N   . ASP A 129 ? 0.2239 0.1287 0.1597 0.0151  -0.0230 -0.0073 130 ASP A N   
1069 C  CA  . ASP A 129 ? 0.3057 0.1187 0.1492 0.0088  0.0121  0.0035  130 ASP A CA  
1070 C  C   . ASP A 129 ? 0.2748 0.1343 0.1360 0.0000  -0.0155 -0.0010 130 ASP A C   
1071 O  O   . ASP A 129 ? 0.3000 0.1280 0.1474 0.0326  -0.0254 -0.0024 130 ASP A O   
1072 C  CB  . ASP A 129 ? 0.2835 0.1709 0.2213 0.0348  0.0555  0.0238  130 ASP A CB  
1073 C  CG  . ASP A 129 ? 0.2773 0.1412 0.1875 0.0221  0.0549  0.0351  130 ASP A CG  
1074 O  OD1 . ASP A 129 ? 0.5195 0.2487 0.2752 -0.1482 -0.1376 0.0447  130 ASP A OD1 
1075 O  OD2 . ASP A 129 ? 0.3378 0.2353 0.3539 -0.0082 0.1456  0.0463  130 ASP A OD2 
1076 N  N   . PHE A 130 ? 0.2681 0.1176 0.1404 0.0048  -0.0086 0.0051  131 PHE A N   
1077 C  CA  . PHE A 130 ? 0.2186 0.1363 0.1288 0.0015  -0.0164 -0.0060 131 PHE A CA  
1078 C  C   . PHE A 130 ? 0.1993 0.1206 0.1498 0.0000  0.0203  0.0027  131 PHE A C   
1079 O  O   . PHE A 130 ? 0.1997 0.1298 0.1351 -0.0230 0.0000  0.0006  131 PHE A O   
1080 C  CB  . PHE A 130 ? 0.2045 0.1525 0.1577 0.0282  -0.0178 -0.0219 131 PHE A CB  
1081 C  CG  . PHE A 130 ? 0.1473 0.1264 0.1577 0.0215  -0.0192 -0.0205 131 PHE A CG  
1082 C  CD1 . PHE A 130 ? 0.1679 0.1314 0.1485 -0.0247 -0.0074 -0.0107 131 PHE A CD1 
1083 C  CD2 . PHE A 130 ? 0.2178 0.1347 0.1950 0.0052  0.0447  -0.0006 131 PHE A CD2 
1084 C  CE1 . PHE A 130 ? 0.1886 0.1385 0.1555 -0.0136 -0.0068 -0.0372 131 PHE A CE1 
1085 C  CE2 . PHE A 130 ? 0.1902 0.1589 0.2006 0.0346  0.0037  0.0115  131 PHE A CE2 
1086 C  CZ  . PHE A 130 ? 0.2171 0.1327 0.1783 0.0093  0.0035  0.0026  131 PHE A CZ  
1087 N  N   . GLY A 131 ? 0.2462 0.1376 0.1576 -0.0230 0.0397  0.0054  132 GLY A N   
1088 C  CA  . GLY A 131 ? 0.2587 0.1889 0.1639 -0.0390 0.0715  0.0104  132 GLY A CA  
1089 C  C   . GLY A 131 ? 0.2146 0.1632 0.1791 -0.0337 0.0693  0.0048  132 GLY A C   
1090 O  O   . GLY A 131 ? 0.2293 0.1650 0.2435 -0.0263 0.0478  -0.0305 132 GLY A O   
1091 N  N   . LYS A 132 ? 0.1934 0.1262 0.2038 -0.0397 0.0231  0.0013  133 LYS A N   
1092 C  CA  . LYS A 132 ? 0.2196 0.1113 0.1794 -0.0181 0.0230  0.0093  133 LYS A CA  
1093 C  C   . LYS A 132 ? 0.1665 0.1358 0.1720 -0.0285 -0.0015 -0.0120 133 LYS A C   
1094 O  O   . LYS A 132 ? 0.1837 0.1419 0.1684 -0.0505 -0.0098 -0.0205 133 LYS A O   
1095 C  CB  . LYS A 132 ? 0.1715 0.1424 0.2390 -0.0181 0.0024  0.0065  133 LYS A CB  
1096 C  CG  . LYS A 132 ? 0.2361 0.1879 0.3615 -0.0680 0.0057  0.0390  133 LYS A CG  
1097 C  CD  . LYS A 132 ? 0.2489 0.1746 0.6898 -0.0355 -0.0185 0.1861  133 LYS A CD  
1098 C  CE  . LYS A 132 ? 0.5055 0.3848 0.8144 -0.1084 -0.3086 -0.0904 133 LYS A CE  
1099 N  NZ  . LYS A 132 ? 0.5260 0.3500 0.5576 -0.0337 -0.2398 0.0031  133 LYS A NZ  
1100 N  N   . ALA A 133 ? 0.1737 0.1306 0.1620 -0.0461 0.0082  -0.0048 134 ALA A N   
1101 C  CA  . ALA A 133 ? 0.1469 0.1386 0.1500 -0.0227 -0.0140 -0.0052 134 ALA A CA  
1102 C  C   . ALA A 133 ? 0.1386 0.1419 0.1254 -0.0403 0.0143  -0.0171 134 ALA A C   
1103 O  O   . ALA A 133 ? 0.1449 0.1553 0.1339 -0.0259 -0.0007 -0.0113 134 ALA A O   
1104 C  CB  . ALA A 133 ? 0.1606 0.1445 0.1400 -0.0361 -0.0031 -0.0026 134 ALA A CB  
1105 N  N   . VAL A 134 ? 0.1636 0.1239 0.1510 -0.0353 0.0143  -0.0070 135 VAL A N   
1106 C  CA  . VAL A 134 ? 0.1528 0.1634 0.1361 -0.0098 0.0020  0.0063  135 VAL A CA  
1107 C  C   . VAL A 134 ? 0.1571 0.1383 0.1374 -0.0238 0.0238  -0.0060 135 VAL A C   
1108 O  O   . VAL A 134 ? 0.1591 0.1458 0.1699 -0.0054 0.0206  0.0097  135 VAL A O   
1109 C  CB  . VAL A 134 ? 0.1835 0.1553 0.1770 -0.0474 0.0184  -0.0071 135 VAL A CB  
1110 C  CG1 . VAL A 134 ? 0.1948 0.1641 0.1842 -0.0315 -0.0063 -0.0077 135 VAL A CG1 
1111 C  CG2 . VAL A 134 ? 0.1808 0.1508 0.1851 -0.0282 0.0241  -0.0154 135 VAL A CG2 
1112 N  N   . GLN A 135 ? 0.1562 0.1330 0.1571 -0.0308 0.0155  -0.0141 136 GLN A N   
1113 C  CA  . GLN A 135 ? 0.1580 0.1594 0.1808 -0.0253 0.0000  -0.0154 136 GLN A CA  
1114 C  C   . GLN A 135 ? 0.1670 0.1342 0.1614 -0.0307 -0.0164 -0.0041 136 GLN A C   
1115 O  O   . GLN A 135 ? 0.1737 0.2099 0.1862 -0.0421 -0.0119 -0.0357 136 GLN A O   
1116 C  CB  . GLN A 135 ? 0.1780 0.1950 0.1897 -0.0658 0.0142  -0.0024 136 GLN A CB  
1117 C  CG  . GLN A 135 ? 0.2476 0.2389 0.2105 -0.0872 0.0494  0.0228  136 GLN A CG  
1118 C  CD  . GLN A 135 ? 0.2860 0.2911 0.2784 -0.0886 0.0219  -0.0163 136 GLN A CD  
1119 O  OE1 . GLN A 135 ? 0.3004 0.4247 0.3815 -0.1075 -0.0406 -0.0130 136 GLN A OE1 
1120 N  NE2 . GLN A 135 ? 0.2318 0.3151 0.3906 -0.0671 0.0142  0.0502  136 GLN A NE2 
1121 N  N   . GLN A 136 ? 0.1325 0.1483 0.1464 -0.0104 0.0091  -0.0143 137 GLN A N   
1122 C  CA  . GLN A 136 ? 0.1421 0.1482 0.1282 -0.0148 -0.0188 -0.0183 137 GLN A CA  
1123 C  C   . GLN A 136 ? 0.1318 0.1485 0.1386 -0.0068 -0.0087 -0.0176 137 GLN A C   
1124 O  O   . GLN A 136 ? 0.1606 0.1288 0.1291 -0.0098 -0.0068 -0.0108 137 GLN A O   
1125 C  CB  . GLN A 136 ? 0.1444 0.1325 0.1853 -0.0020 -0.0176 -0.0038 137 GLN A CB  
1126 C  CG  . GLN A 136 ? 0.2404 0.1641 0.1959 -0.0034 0.0259  -0.0012 137 GLN A CG  
1127 C  CD  . GLN A 136 ? 0.1648 0.2293 0.3079 0.0513  0.0230  0.0337  137 GLN A CD  
1128 O  OE1 . GLN A 136 ? 0.2417 0.1713 0.2986 -0.0131 -0.0171 -0.0662 137 GLN A OE1 
1129 N  NE2 . GLN A 136 ? 0.3980 0.3258 0.3833 0.0006  0.0957  0.0894  137 GLN A NE2 
1130 N  N   A PRO A 137 ? 0.1066 0.1655 0.1291 -0.0198 -0.0167 -0.0153 138 PRO A N   
1131 N  N   B PRO A 137 ? 0.1360 0.1816 0.1391 0.0093  -0.0126 -0.0193 138 PRO A N   
1132 C  CA  A PRO A 137 ? 0.1518 0.1840 0.1138 0.0155  0.0006  0.0041  138 PRO A CA  
1133 C  CA  B PRO A 137 ? 0.1706 0.2053 0.1185 0.0219  -0.0155 0.0137  138 PRO A CA  
1134 C  C   A PRO A 137 ? 0.1485 0.1810 0.1230 0.0060  -0.0024 -0.0023 138 PRO A C   
1135 C  C   B PRO A 137 ? 0.1571 0.1844 0.0983 0.0162  0.0071  -0.0041 138 PRO A C   
1136 O  O   A PRO A 137 ? 0.1825 0.1656 0.2219 0.0214  -0.0238 0.0346  138 PRO A O   
1137 O  O   B PRO A 137 ? 0.2157 0.1676 0.2087 0.0178  0.0119  0.0198  138 PRO A O   
1138 C  CB  A PRO A 137 ? 0.2140 0.2590 0.1190 0.0346  -0.0270 0.0092  138 PRO A CB  
1139 C  CB  B PRO A 137 ? 0.2379 0.2569 0.1149 0.0195  -0.0046 0.0012  138 PRO A CB  
1140 C  CG  A PRO A 137 ? 0.1614 0.2734 0.0837 0.0103  -0.0348 -0.0377 138 PRO A CG  
1141 C  CG  B PRO A 137 ? 0.1826 0.3528 0.1280 -0.0292 -0.0219 -0.0438 138 PRO A CG  
1142 C  CD  A PRO A 137 ? 0.1379 0.2773 0.1163 -0.0723 -0.0359 -0.0390 138 PRO A CD  
1143 C  CD  B PRO A 137 ? 0.2076 0.2849 0.1210 -0.0137 -0.0173 -0.0577 138 PRO A CD  
1144 N  N   . ASP A 138 ? 0.1336 0.1596 0.1129 0.0035  -0.0071 -0.0107 139 ASP A N   
1145 C  CA  . ASP A 138 ? 0.1632 0.1562 0.1131 -0.0141 0.0088  -0.0104 139 ASP A CA  
1146 C  C   . ASP A 138 ? 0.1402 0.1154 0.1167 -0.0131 0.0019  -0.0005 139 ASP A C   
1147 O  O   . ASP A 138 ? 0.1321 0.1397 0.1370 0.0057  -0.0082 -0.0010 139 ASP A O   
1148 C  CB  . ASP A 138 ? 0.2083 0.1833 0.1307 -0.0041 0.0251  -0.0037 139 ASP A CB  
1149 C  CG  . ASP A 138 ? 0.1624 0.1995 0.1476 0.0142  0.0119  -0.0098 139 ASP A CG  
1150 O  OD1 . ASP A 138 ? 0.1907 0.1656 0.1589 0.0219  -0.0091 -0.0303 139 ASP A OD1 
1151 O  OD2 . ASP A 138 ? 0.2046 0.2275 0.2087 0.0175  0.0152  -0.0531 139 ASP A OD2 
1152 N  N   . GLY A 139 ? 0.1383 0.1129 0.1077 -0.0175 -0.0062 -0.0126 140 GLY A N   
1153 C  CA  . GLY A 139 ? 0.1512 0.1252 0.0974 -0.0262 -0.0104 -0.0153 140 GLY A CA  
1154 C  C   . GLY A 139 ? 0.0970 0.1122 0.1187 -0.0023 -0.0020 0.0035  140 GLY A C   
1155 O  O   . GLY A 139 ? 0.1287 0.1045 0.1237 -0.0043 -0.0102 -0.0019 140 GLY A O   
1156 N  N   . LEU A 140 ? 0.1019 0.0966 0.1361 -0.0154 -0.0080 0.0013  141 LEU A N   
1157 C  CA  . LEU A 140 ? 0.0961 0.1054 0.1289 0.0005  -0.0013 -0.0015 141 LEU A CA  
1158 C  C   . LEU A 140 ? 0.0983 0.1009 0.1108 -0.0024 -0.0151 -0.0017 141 LEU A C   
1159 O  O   . LEU A 140 ? 0.1185 0.1001 0.1167 0.0010  -0.0107 -0.0031 141 LEU A O   
1160 C  CB  . LEU A 140 ? 0.1099 0.1221 0.1133 0.0003  0.0024  0.0000  141 LEU A CB  
1161 C  CG  . LEU A 140 ? 0.1357 0.1491 0.1613 0.0456  0.0248  0.0136  141 LEU A CG  
1162 C  CD1 . LEU A 140 ? 0.1194 0.1658 0.1476 0.0265  0.0049  0.0000  141 LEU A CD1 
1163 C  CD2 . LEU A 140 ? 0.2670 0.1333 0.2177 0.0498  0.0790  0.0262  141 LEU A CD2 
1164 N  N   . ALA A 141 ? 0.1061 0.1001 0.1187 0.0020  -0.0019 -0.0023 142 ALA A N   
1165 C  CA  . ALA A 141 ? 0.1063 0.0979 0.1395 -0.0114 -0.0230 -0.0051 142 ALA A CA  
1166 C  C   . ALA A 141 ? 0.1066 0.1133 0.1111 0.0054  -0.0187 0.0065  142 ALA A C   
1167 O  O   . ALA A 141 ? 0.1206 0.1023 0.1221 -0.0015 -0.0252 0.0070  142 ALA A O   
1168 C  CB  . ALA A 141 ? 0.1070 0.1239 0.1537 -0.0048 -0.0041 0.0000  142 ALA A CB  
1169 N  N   . VAL A 142 ? 0.0944 0.1054 0.1108 -0.0104 -0.0040 -0.0024 143 VAL A N   
1170 C  CA  . VAL A 142 ? 0.1040 0.1106 0.1172 0.0060  -0.0103 -0.0054 143 VAL A CA  
1171 C  C   . VAL A 142 ? 0.0979 0.1093 0.0957 -0.0087 0.0013  -0.0037 143 VAL A C   
1172 O  O   . VAL A 142 ? 0.1172 0.1086 0.0944 -0.0077 -0.0077 0.0030  143 VAL A O   
1173 C  CB  . VAL A 142 ? 0.0909 0.1172 0.1183 0.0043  -0.0104 -0.0096 143 VAL A CB  
1174 C  CG1 . VAL A 142 ? 0.1221 0.1263 0.1111 0.0120  -0.0098 -0.0071 143 VAL A CG1 
1175 C  CG2 . VAL A 142 ? 0.1176 0.1351 0.1118 -0.0194 -0.0153 0.0013  143 VAL A CG2 
1176 N  N   . LEU A 143 ? 0.1090 0.0864 0.1252 -0.0038 -0.0164 -0.0015 144 LEU A N   
1177 C  CA  . LEU A 143 ? 0.1014 0.0821 0.1233 -0.0065 -0.0187 -0.0027 144 LEU A CA  
1178 C  C   . LEU A 143 ? 0.1163 0.1018 0.1070 -0.0071 -0.0024 0.0010  144 LEU A C   
1179 O  O   . LEU A 143 ? 0.1318 0.1045 0.1072 0.0024  -0.0013 0.0000  144 LEU A O   
1180 C  CB  . LEU A 143 ? 0.1254 0.1358 0.1210 0.0019  -0.0203 0.0068  144 LEU A CB  
1181 C  CG  . LEU A 143 ? 0.1067 0.1312 0.1625 -0.0006 -0.0148 -0.0060 144 LEU A CG  
1182 C  CD1 . LEU A 143 ? 0.1279 0.1828 0.1711 -0.0107 -0.0019 0.0252  144 LEU A CD1 
1183 C  CD2 . LEU A 143 ? 0.1280 0.1853 0.1932 0.0071  -0.0427 0.0043  144 LEU A CD2 
1184 N  N   . GLY A 144 ? 0.1045 0.0913 0.1221 0.0006  -0.0135 0.0051  145 GLY A N   
1185 C  CA  . GLY A 144 ? 0.1053 0.0882 0.1282 -0.0041 -0.0006 0.0003  145 GLY A CA  
1186 C  C   . GLY A 144 ? 0.0842 0.1026 0.0991 0.0000  -0.0165 0.0052  145 GLY A C   
1187 O  O   . GLY A 144 ? 0.1063 0.1115 0.1167 0.0000  0.0049  -0.0051 145 GLY A O   
1188 N  N   . ILE A 145 ? 0.1058 0.0988 0.1044 -0.0005 -0.0130 -0.0040 146 ILE A N   
1189 C  CA  . ILE A 145 ? 0.0917 0.0860 0.1279 -0.0052 -0.0211 0.0013  146 ILE A CA  
1190 C  C   . ILE A 145 ? 0.0843 0.0964 0.1176 -0.0115 -0.0175 0.0027  146 ILE A C   
1191 O  O   . ILE A 145 ? 0.1040 0.0983 0.1181 -0.0026 -0.0076 0.0006  146 ILE A O   
1192 C  CB  . ILE A 145 ? 0.1039 0.0944 0.1394 0.0098  -0.0220 0.0097  146 ILE A CB  
1193 C  CG1 . ILE A 145 ? 0.1137 0.1185 0.1762 0.0164  -0.0340 0.0041  146 ILE A CG1 
1194 C  CG2 . ILE A 145 ? 0.1111 0.1286 0.1979 -0.0131 -0.0487 -0.0063 146 ILE A CG2 
1195 C  CD1 . ILE A 145 ? 0.1235 0.1185 0.1776 0.0137  -0.0351 0.0115  146 ILE A CD1 
1196 N  N   . PHE A 146 ? 0.0969 0.1023 0.1183 0.0000  -0.0166 0.0102  147 PHE A N   
1197 C  CA  . PHE A 146 ? 0.1208 0.0948 0.1154 0.0148  -0.0239 0.0054  147 PHE A CA  
1198 C  C   . PHE A 146 ? 0.0860 0.1081 0.1360 -0.0087 -0.0209 0.0046  147 PHE A C   
1199 O  O   . PHE A 146 ? 0.1041 0.1127 0.1509 -0.0015 -0.0254 -0.0043 147 PHE A O   
1200 C  CB  . PHE A 146 ? 0.1142 0.1172 0.1178 -0.0076 -0.0241 0.0129  147 PHE A CB  
1201 C  CG  . PHE A 146 ? 0.0961 0.0935 0.1097 -0.0082 -0.0181 0.0076  147 PHE A CG  
1202 C  CD1 . PHE A 146 ? 0.0834 0.1061 0.1354 0.0114  -0.0259 0.0103  147 PHE A CD1 
1203 C  CD2 . PHE A 146 ? 0.1248 0.0944 0.1307 -0.0031 -0.0140 0.0217  147 PHE A CD2 
1204 C  CE1 . PHE A 146 ? 0.1031 0.1106 0.1169 -0.0020 -0.0153 0.0164  147 PHE A CE1 
1205 C  CE2 . PHE A 146 ? 0.1090 0.1120 0.1361 -0.0065 -0.0082 0.0038  147 PHE A CE2 
1206 C  CZ  . PHE A 146 ? 0.1133 0.1040 0.1176 -0.0163 -0.0197 0.0243  147 PHE A CZ  
1207 N  N   . LEU A 147 ? 0.1053 0.1023 0.1324 -0.0027 -0.0065 -0.0013 148 LEU A N   
1208 C  CA  . LEU A 147 ? 0.1386 0.0952 0.1201 -0.0068 -0.0241 0.0005  148 LEU A CA  
1209 C  C   . LEU A 147 ? 0.1212 0.1133 0.1111 0.0027  -0.0093 -0.0020 148 LEU A C   
1210 O  O   . LEU A 147 ? 0.1221 0.1048 0.1525 0.0046  -0.0115 0.0080  148 LEU A O   
1211 C  CB  . LEU A 147 ? 0.1448 0.0939 0.1467 -0.0038 -0.0244 -0.0057 148 LEU A CB  
1212 C  CG  . LEU A 147 ? 0.1611 0.0992 0.1331 -0.0062 -0.0297 -0.0148 148 LEU A CG  
1213 C  CD1 . LEU A 147 ? 0.1709 0.1099 0.1515 -0.0194 -0.0307 -0.0052 148 LEU A CD1 
1214 C  CD2 . LEU A 147 ? 0.1634 0.1297 0.1473 -0.0098 -0.0370 -0.0013 148 LEU A CD2 
1215 N  N   . LYS A 148 ? 0.1352 0.0903 0.1474 -0.0132 -0.0217 -0.0126 149 LYS A N   
1216 C  CA  . LYS A 148 ? 0.1360 0.0988 0.1720 -0.0086 -0.0187 -0.0035 149 LYS A CA  
1217 C  C   . LYS A 148 ? 0.1555 0.1268 0.1570 0.0200  -0.0310 0.0013  149 LYS A C   
1218 O  O   . LYS A 148 ? 0.1634 0.1341 0.1624 0.0164  -0.0340 -0.0104 149 LYS A O   
1219 C  CB  . LYS A 148 ? 0.1462 0.1386 0.1668 -0.0252 -0.0159 0.0124  149 LYS A CB  
1220 C  CG  . LYS A 148 ? 0.1553 0.1586 0.1896 -0.0231 -0.0017 0.0237  149 LYS A CG  
1221 C  CD  . LYS A 148 ? 0.2354 0.2410 0.2727 -0.0432 0.0185  0.0573  149 LYS A CD  
1222 C  CE  . LYS A 148 ? 0.2533 0.4332 0.4038 -0.0798 0.0856  0.1045  149 LYS A CE  
1223 N  NZ  . LYS A 148 ? 0.6150 0.6668 0.4735 -0.2910 0.1039  0.1437  149 LYS A NZ  
1224 N  N   . VAL A 149 ? 0.1648 0.1079 0.1782 0.0076  -0.0247 -0.0137 150 VAL A N   
1225 C  CA  . VAL A 149 ? 0.1552 0.1215 0.1844 -0.0012 -0.0260 -0.0181 150 VAL A CA  
1226 C  C   . VAL A 149 ? 0.1647 0.1348 0.1873 -0.0093 -0.0209 -0.0093 150 VAL A C   
1227 O  O   . VAL A 149 ? 0.1941 0.1411 0.2011 -0.0153 -0.0381 0.0110  150 VAL A O   
1228 C  CB  . VAL A 149 ? 0.1677 0.1242 0.1695 0.0115  -0.0199 -0.0030 150 VAL A CB  
1229 C  CG1 . VAL A 149 ? 0.2081 0.1923 0.1666 -0.0015 -0.0346 -0.0282 150 VAL A CG1 
1230 C  CG2 . VAL A 149 ? 0.1718 0.1713 0.2047 -0.0233 -0.0071 -0.0164 150 VAL A CG2 
1231 N  N   . GLY A 150 ? 0.1706 0.1339 0.1743 -0.0166 -0.0487 -0.0119 151 GLY A N   
1232 C  CA  . GLY A 150 ? 0.1598 0.1688 0.2169 -0.0423 -0.0520 0.0074  151 GLY A CA  
1233 C  C   . GLY A 150 ? 0.1710 0.1322 0.1832 -0.0502 -0.0425 0.0019  151 GLY A C   
1234 O  O   . GLY A 150 ? 0.2034 0.1499 0.1961 -0.0370 -0.0232 -0.0186 151 GLY A O   
1235 N  N   A SER A 151 ? 0.1528 0.1679 0.2291 -0.0275 -0.0483 -0.0081 152 SER A N   
1236 N  N   B SER A 151 ? 0.1582 0.1576 0.2377 -0.0386 -0.0467 -0.0344 152 SER A N   
1237 C  CA  A SER A 151 ? 0.1907 0.1519 0.2187 -0.0082 -0.0476 0.0038  152 SER A CA  
1238 C  CA  B SER A 151 ? 0.1589 0.1629 0.2152 -0.0265 -0.0425 -0.0283 152 SER A CA  
1239 C  C   A SER A 151 ? 0.2046 0.1377 0.1772 -0.0308 -0.0088 -0.0359 152 SER A C   
1240 C  C   B SER A 151 ? 0.1921 0.1106 0.1907 -0.0092 -0.0617 -0.0383 152 SER A C   
1241 O  O   A SER A 151 ? 0.1406 0.1309 0.1920 -0.0098 0.0020  -0.0379 152 SER A O   
1242 O  O   B SER A 151 ? 0.1577 0.1546 0.1437 -0.0240 -0.0172 -0.0397 152 SER A O   
1243 C  CB  A SER A 151 ? 0.2178 0.2308 0.2953 -0.0329 0.0195  -0.0006 152 SER A CB  
1244 C  CB  B SER A 151 ? 0.1606 0.2013 0.2882 -0.0307 -0.0003 -0.0207 152 SER A CB  
1245 O  OG  A SER A 151 ? 0.2320 0.3586 0.2645 -0.0412 -0.0375 -0.0214 152 SER A OG  
1246 O  OG  B SER A 151 ? 0.1717 0.2870 0.3434 -0.0283 0.0038  0.1217  152 SER A OG  
1247 N  N   . ALA A 152 ? 0.2123 0.1467 0.1858 -0.0296 -0.0649 -0.0240 153 ALA A N   
1248 C  CA  . ALA A 152 ? 0.1949 0.1562 0.1916 0.0020  -0.0348 -0.0384 153 ALA A CA  
1249 C  C   . ALA A 152 ? 0.2074 0.1765 0.1727 -0.0060 -0.0384 -0.0313 153 ALA A C   
1250 O  O   . ALA A 152 ? 0.2004 0.1442 0.2554 0.0013  -0.0291 -0.0184 153 ALA A O   
1251 C  CB  . ALA A 152 ? 0.2512 0.1812 0.1783 0.0098  -0.0688 -0.0307 153 ALA A CB  
1252 N  N   . LYS A 153 ? 0.2028 0.1296 0.1976 0.0082  -0.0579 -0.0177 154 LYS A N   
1253 C  CA  . LYS A 153 ? 0.2275 0.1277 0.2116 0.0211  -0.0625 -0.0017 154 LYS A CA  
1254 C  C   . LYS A 153 ? 0.1782 0.1431 0.1950 0.0265  -0.0559 -0.0219 154 LYS A C   
1255 O  O   . LYS A 153 ? 0.1940 0.1580 0.1824 0.0151  -0.0612 -0.0197 154 LYS A O   
1256 C  CB  . LYS A 153 ? 0.2140 0.1410 0.2004 0.0043  -0.0666 0.0020  154 LYS A CB  
1257 C  CG  . LYS A 153 ? 0.3040 0.1798 0.1828 0.0401  -0.0794 -0.0119 154 LYS A CG  
1258 C  CD  . LYS A 153 ? 0.2442 0.1578 0.2360 0.0229  -0.0815 -0.0359 154 LYS A CD  
1259 C  CE  . LYS A 153 ? 0.2562 0.1884 0.1846 0.0181  -0.0161 -0.0178 154 LYS A CE  
1260 N  NZ  . LYS A 153 ? 0.2035 0.1844 0.2476 -0.0199 -0.0328 -0.0344 154 LYS A NZ  
1261 N  N   . PRO A 154 ? 0.2060 0.1670 0.2099 0.0140  -0.0807 -0.0269 155 PRO A N   
1262 C  CA  . PRO A 154 ? 0.2065 0.1613 0.2442 -0.0126 -0.0838 -0.0177 155 PRO A CA  
1263 C  C   . PRO A 154 ? 0.2126 0.2284 0.2073 0.0104  -0.0838 -0.0031 155 PRO A C   
1264 O  O   . PRO A 154 ? 0.2518 0.2135 0.2099 0.0114  -0.0974 0.0071  155 PRO A O   
1265 C  CB  . PRO A 154 ? 0.2061 0.2328 0.2875 -0.0140 -0.0944 0.0177  155 PRO A CB  
1266 C  CG  . PRO A 154 ? 0.2104 0.2860 0.3040 0.0087  -0.0258 0.0405  155 PRO A CG  
1267 C  CD  . PRO A 154 ? 0.2343 0.2113 0.2408 0.0359  -0.0516 0.0142  155 PRO A CD  
1268 N  N   . GLY A 155 ? 0.2223 0.1501 0.2275 0.0255  -0.0873 -0.0041 156 GLY A N   
1269 C  CA  . GLY A 155 ? 0.2451 0.1578 0.2766 0.0031  -0.0803 -0.0248 156 GLY A CA  
1270 C  C   . GLY A 155 ? 0.2559 0.1456 0.2078 -0.0063 -0.0662 0.0195  156 GLY A C   
1271 O  O   . GLY A 155 ? 0.2870 0.1431 0.3270 0.0068  -0.0772 0.0353  156 GLY A O   
1272 N  N   . LEU A 156 ? 0.2417 0.1509 0.1993 -0.0003 -0.0701 -0.0027 157 LEU A N   
1273 C  CA  . LEU A 156 ? 0.2551 0.1246 0.1869 0.0015  -0.0934 -0.0148 157 LEU A CA  
1274 C  C   . LEU A 156 ? 0.2335 0.1435 0.1747 0.0210  -0.0798 -0.0098 157 LEU A C   
1275 O  O   . LEU A 156 ? 0.2451 0.1473 0.1688 -0.0121 -0.0829 -0.0104 157 LEU A O   
1276 C  CB  . LEU A 156 ? 0.2137 0.1648 0.1938 -0.0063 -0.0860 -0.0196 157 LEU A CB  
1277 C  CG  . LEU A 156 ? 0.1937 0.1715 0.1645 -0.0181 -0.0553 -0.0049 157 LEU A CG  
1278 C  CD1 . LEU A 156 ? 0.2583 0.1679 0.1932 -0.0472 -0.0710 -0.0197 157 LEU A CD1 
1279 C  CD2 . LEU A 156 ? 0.2137 0.1808 0.1571 -0.0098 -0.0430 0.0019  157 LEU A CD2 
1280 N  N   . GLN A 157 ? 0.2336 0.1650 0.1773 -0.0217 -0.0843 0.0000  158 GLN A N   
1281 C  CA  . GLN A 157 ? 0.2705 0.1907 0.1597 -0.0401 -0.0706 -0.0307 158 GLN A CA  
1282 C  C   . GLN A 157 ? 0.2073 0.1808 0.1774 -0.0205 -0.0811 -0.0142 158 GLN A C   
1283 O  O   . GLN A 157 ? 0.2349 0.1767 0.1904 -0.0161 -0.0758 -0.0121 158 GLN A O   
1284 C  CB  . GLN A 157 ? 0.2547 0.1703 0.2152 -0.0297 -0.0785 -0.0164 158 GLN A CB  
1285 C  CG  . GLN A 157 ? 0.2752 0.1932 0.2124 -0.0107 -0.0807 -0.0366 158 GLN A CG  
1286 C  CD  . GLN A 157 ? 0.2738 0.1595 0.1958 -0.0199 -0.0894 -0.0024 158 GLN A CD  
1287 O  OE1 . GLN A 157 ? 0.2964 0.1634 0.1876 -0.0249 -0.0623 -0.0162 158 GLN A OE1 
1288 N  NE2 . GLN A 157 ? 0.3046 0.2249 0.2167 -0.0443 -0.0606 -0.0351 158 GLN A NE2 
1289 N  N   . LYS A 158 ? 0.2791 0.1743 0.1977 -0.0227 -0.1089 -0.0126 159 LYS A N   
1290 C  CA  . LYS A 158 ? 0.2522 0.1841 0.1860 -0.0249 -0.0961 0.0054  159 LYS A CA  
1291 C  C   . LYS A 158 ? 0.2785 0.1658 0.1603 -0.0251 -0.0582 -0.0005 159 LYS A C   
1292 O  O   . LYS A 158 ? 0.2684 0.1913 0.1871 -0.0270 -0.0802 -0.0057 159 LYS A O   
1293 C  CB  . LYS A 158 ? 0.2997 0.1977 0.2069 -0.0087 -0.0732 0.0631  159 LYS A CB  
1294 C  CG  . LYS A 158 ? 0.3919 0.3762 0.3183 0.0675  -0.1272 0.0733  159 LYS A CG  
1295 N  N   . VAL A 159 ? 0.2727 0.1580 0.1650 -0.0043 -0.0922 -0.0226 160 VAL A N   
1296 C  CA  . VAL A 159 ? 0.2426 0.1404 0.1351 -0.0120 -0.0450 -0.0153 160 VAL A CA  
1297 C  C   . VAL A 159 ? 0.2474 0.1395 0.1758 0.0000  -0.0562 -0.0136 160 VAL A C   
1298 O  O   . VAL A 159 ? 0.2595 0.1510 0.1862 -0.0017 -0.0635 -0.0230 160 VAL A O   
1299 C  CB  . VAL A 159 ? 0.2489 0.1427 0.1456 -0.0141 -0.0631 -0.0171 160 VAL A CB  
1300 C  CG1 . VAL A 159 ? 0.2350 0.2022 0.2043 -0.0483 -0.0714 0.0131  160 VAL A CG1 
1301 C  CG2 . VAL A 159 ? 0.2824 0.1990 0.1595 0.0005  -0.0588 -0.0370 160 VAL A CG2 
1302 N  N   . VAL A 160 ? 0.2583 0.1509 0.1386 -0.0178 -0.0399 -0.0161 161 VAL A N   
1303 C  CA  . VAL A 160 ? 0.2666 0.1448 0.1695 0.0012  -0.0351 -0.0041 161 VAL A CA  
1304 C  C   . VAL A 160 ? 0.2675 0.1176 0.1826 -0.0329 -0.0410 -0.0228 161 VAL A C   
1305 O  O   . VAL A 160 ? 0.3388 0.1667 0.2076 -0.0368 -0.0070 -0.0244 161 VAL A O   
1306 C  CB  . VAL A 160 ? 0.4175 0.1508 0.1964 -0.0153 0.0355  -0.0162 161 VAL A CB  
1307 C  CG1 . VAL A 160 ? 0.3281 0.2198 0.2381 -0.0579 -0.0522 -0.0414 161 VAL A CG1 
1308 C  CG2 . VAL A 160 ? 0.2950 0.1715 0.2108 0.0131  -0.0445 -0.0219 161 VAL A CG2 
1309 N  N   . ASP A 161 ? 0.3424 0.1900 0.1500 -0.0439 -0.0790 -0.0110 162 ASP A N   
1310 C  CA  . ASP A 161 ? 0.3787 0.2248 0.1615 -0.0829 -0.0627 -0.0087 162 ASP A CA  
1311 C  C   . ASP A 161 ? 0.3985 0.2871 0.1339 -0.0825 -0.0838 -0.0166 162 ASP A C   
1312 O  O   . ASP A 161 ? 0.4789 0.2982 0.1948 -0.1221 -0.0074 -0.0348 162 ASP A O   
1313 C  CB  . ASP A 161 ? 0.4502 0.3036 0.1737 -0.0997 -0.0820 -0.0434 162 ASP A CB  
1314 C  CG  . ASP A 161 ? 0.4361 0.2347 0.1624 -0.0027 -0.0310 -0.0269 162 ASP A CG  
1315 O  OD1 . ASP A 161 ? 0.4301 0.2849 0.3036 -0.0603 -0.1083 -0.0304 162 ASP A OD1 
1316 O  OD2 . ASP A 161 ? 0.4609 0.3665 0.2406 -0.0432 -0.0878 -0.0263 162 ASP A OD2 
1317 N  N   . VAL A 162 ? 0.3567 0.1968 0.1564 -0.0274 -0.1053 -0.0071 163 VAL A N   
1318 C  CA  . VAL A 162 ? 0.3639 0.2028 0.2117 -0.0595 -0.1019 0.0296  163 VAL A CA  
1319 C  C   . VAL A 162 ? 0.3349 0.1686 0.1377 -0.0472 -0.0307 0.0337  163 VAL A C   
1320 O  O   . VAL A 162 ? 0.3888 0.1952 0.1424 -0.0351 -0.0189 0.0108  163 VAL A O   
1321 C  CB  . VAL A 162 ? 0.3633 0.2230 0.2308 -0.0285 -0.0487 0.0162  163 VAL A CB  
1322 C  CG1 . VAL A 162 ? 0.4027 0.1683 0.2450 -0.0165 -0.0975 0.0049  163 VAL A CG1 
1323 C  CG2 . VAL A 162 ? 0.2918 0.2345 0.2627 0.0366  0.0017  0.0758  163 VAL A CG2 
1324 N  N   . LEU A 163 ? 0.3097 0.1940 0.2038 -0.0533 -0.0781 0.0153  164 LEU A N   
1325 C  CA  . LEU A 163 ? 0.3334 0.1543 0.1304 -0.0154 0.0092  0.0006  164 LEU A CA  
1326 C  C   . LEU A 163 ? 0.3000 0.1670 0.1765 0.0092  0.0115  -0.0164 164 LEU A C   
1327 O  O   . LEU A 163 ? 0.3151 0.2090 0.1333 0.0110  0.0153  0.0013  164 LEU A O   
1328 C  CB  . LEU A 163 ? 0.2838 0.1430 0.1686 -0.0243 -0.0263 0.0140  164 LEU A CB  
1329 C  CG  . LEU A 163 ? 0.3033 0.1539 0.1307 -0.0239 -0.0221 0.0048  164 LEU A CG  
1330 C  CD1 . LEU A 163 ? 0.2939 0.1587 0.1902 -0.0102 -0.0456 0.0331  164 LEU A CD1 
1331 C  CD2 . LEU A 163 ? 0.2613 0.1782 0.1640 0.0077  -0.0430 -0.0143 164 LEU A CD2 
1332 N  N   . ASP A 164 ? 0.4495 0.1893 0.1422 -0.0636 0.0052  -0.0461 165 ASP A N   
1333 C  CA  . ASP A 164 ? 0.6068 0.2662 0.2065 -0.0939 0.0750  -0.0610 165 ASP A CA  
1334 C  C   . ASP A 164 ? 0.4933 0.3255 0.1388 -0.0198 0.0516  -0.0063 165 ASP A C   
1335 O  O   . ASP A 164 ? 0.5968 0.2713 0.2212 0.0251  0.0909  -0.0046 165 ASP A O   
1336 C  CB  . ASP A 164 ? 0.6887 0.4659 0.4067 -0.1155 -0.0226 -0.0397 165 ASP A CB  
1337 C  CG  . ASP A 164 ? 0.9817 0.4440 1.0411 -0.0847 -0.1976 -0.0754 165 ASP A CG  
1338 O  OD1 . ASP A 164 ? 1.3868 1.6963 0.3474 -0.0147 -0.0222 -0.1735 165 ASP A OD1 
1339 O  OD2 . ASP A 164 ? 1.2222 1.8974 1.1757 -0.2784 0.0643  -1.1375 165 ASP A OD2 
1340 N  N   . SER A 165 ? 0.3837 0.2806 0.1323 -0.0573 -0.0331 0.0059  166 SER A N   
1341 C  CA  . SER A 165 ? 0.4610 0.2511 0.1611 -0.0502 -0.0219 -0.0172 166 SER A CA  
1342 C  C   . SER A 165 ? 0.4268 0.2469 0.1040 -0.0597 -0.0038 0.0288  166 SER A C   
1343 O  O   . SER A 165 ? 0.3888 0.2189 0.1546 -0.0197 -0.0219 0.0373  166 SER A O   
1344 C  CB  . SER A 165 ? 0.5914 0.3122 0.2107 -0.0472 0.0847  0.0306  166 SER A CB  
1345 O  OG  . SER A 165 ? 0.4444 0.2308 0.2169 0.0087  -0.0115 0.0388  166 SER A OG  
1346 N  N   . ILE A 166 ? 0.2817 0.2072 0.1342 0.0187  -0.0274 0.0096  167 ILE A N   
1347 C  CA  . ILE A 166 ? 0.2261 0.1941 0.1611 -0.0093 -0.0102 0.0406  167 ILE A CA  
1348 C  C   . ILE A 166 ? 0.2602 0.1949 0.1072 -0.0208 -0.0130 -0.0162 167 ILE A C   
1349 O  O   . ILE A 166 ? 0.2730 0.1704 0.1275 -0.0231 -0.0062 0.0006  167 ILE A O   
1350 C  CB  . ILE A 166 ? 0.3428 0.1743 0.1248 -0.0270 0.0024  -0.0038 167 ILE A CB  
1351 C  CG1 . ILE A 166 ? 0.2720 0.1911 0.1210 -0.0146 -0.0186 -0.0024 167 ILE A CG1 
1352 C  CG2 . ILE A 166 ? 0.2986 0.1923 0.1526 0.0071  -0.0329 0.0013  167 ILE A CG2 
1353 C  CD1 . ILE A 166 ? 0.2741 0.1882 0.1271 -0.0176 0.0185  -0.0104 167 ILE A CD1 
1354 N  N   . LYS A 167 ? 0.2684 0.1787 0.1422 0.0059  0.0068  -0.0013 168 LYS A N   
1355 C  CA  . LYS A 167 ? 0.2219 0.2274 0.1527 -0.0118 0.0261  -0.0421 168 LYS A CA  
1356 C  C   . LYS A 167 ? 0.2738 0.2073 0.1318 -0.0230 0.0293  0.0305  168 LYS A C   
1357 O  O   . LYS A 167 ? 0.2526 0.1560 0.1418 -0.0357 -0.0059 -0.0054 168 LYS A O   
1358 C  CB  . LYS A 167 ? 0.3079 0.1982 0.1652 -0.0057 -0.0162 -0.0375 168 LYS A CB  
1359 C  CG  . LYS A 167 ? 0.2978 0.2128 0.1808 0.0062  0.0074  -0.0329 168 LYS A CG  
1360 C  CD  . LYS A 167 ? 0.3963 0.2738 0.2388 0.0197  -0.0304 -0.0894 168 LYS A CD  
1361 C  CE  . LYS A 167 ? 0.5705 0.3967 0.4990 0.1356  -0.0992 -0.2052 168 LYS A CE  
1362 N  NZ  . LYS A 167 ? 0.8539 0.5957 0.9013 0.0366  -0.0099 0.1010  168 LYS A NZ  
1363 N  N   . THR A 168 ? 0.2476 0.1787 0.1535 -0.0251 -0.0131 0.0175  169 THR A N   
1364 C  CA  . THR A 168 ? 0.2469 0.2070 0.1305 0.0091  0.0373  0.0359  169 THR A CA  
1365 C  C   . THR A 168 ? 0.2126 0.2002 0.1169 -0.0031 0.0326  0.0060  169 THR A C   
1366 O  O   . THR A 168 ? 0.2572 0.1862 0.1709 -0.0419 0.0152  -0.0015 169 THR A O   
1367 C  CB  . THR A 168 ? 0.2731 0.2064 0.1567 -0.0043 0.0142  0.0147  169 THR A CB  
1368 O  OG1 . THR A 168 ? 0.2985 0.2363 0.1282 -0.0375 0.0225  0.0114  169 THR A OG1 
1369 C  CG2 . THR A 168 ? 0.3185 0.2119 0.1771 -0.0165 0.0474  -0.0141 169 THR A CG2 
1370 N  N   A LYS A 169 ? 0.3287 0.2038 0.1439 -0.0931 0.0458  0.0174  170 LYS A N   
1371 N  N   B LYS A 169 ? 0.3198 0.2008 0.1483 -0.0904 0.0394  0.0182  170 LYS A N   
1372 C  CA  A LYS A 169 ? 0.2993 0.1889 0.1858 -0.0467 0.0295  0.0046  170 LYS A CA  
1373 C  CA  B LYS A 169 ? 0.1749 0.1686 0.1949 -0.0230 -0.0199 0.0222  170 LYS A CA  
1374 C  C   A LYS A 169 ? 0.2105 0.2211 0.1354 -0.0445 0.0386  0.0315  170 LYS A C   
1375 C  C   B LYS A 169 ? 0.2283 0.2117 0.1591 -0.0487 0.0126  0.0522  170 LYS A C   
1376 O  O   A LYS A 169 ? 0.2578 0.2310 0.1009 -0.0071 0.0057  0.0326  170 LYS A O   
1377 O  O   B LYS A 169 ? 0.3944 0.2684 0.1579 -0.1439 0.0427  -0.0186 170 LYS A O   
1378 C  CB  A LYS A 169 ? 0.2870 0.1988 0.2207 -0.0702 0.0847  -0.0034 170 LYS A CB  
1379 C  CB  B LYS A 169 ? 0.1562 0.1649 0.1607 0.0412  0.0216  0.0335  170 LYS A CB  
1380 C  CG  A LYS A 169 ? 0.3377 0.2396 0.1485 -0.1058 -0.0219 0.0741  170 LYS A CG  
1381 C  CG  B LYS A 169 ? 0.2020 0.2158 0.2478 0.0109  -0.0294 -0.0031 170 LYS A CG  
1382 C  CD  A LYS A 169 ? 0.2824 0.3227 0.2551 -0.0526 0.0732  -0.0476 170 LYS A CD  
1383 C  CD  B LYS A 169 ? 0.1884 0.1674 0.2098 0.0013  0.0097  0.0357  170 LYS A CD  
1384 C  CE  A LYS A 169 ? 0.3650 0.3554 0.4031 -0.1110 -0.1376 -0.0310 170 LYS A CE  
1385 C  CE  B LYS A 169 ? 0.2569 0.2558 0.2460 -0.0038 0.0197  0.0241  170 LYS A CE  
1386 N  NZ  A LYS A 169 ? 0.3417 0.4265 0.4994 0.1194  -0.0368 -0.1171 170 LYS A NZ  
1387 N  NZ  B LYS A 169 ? 0.3313 0.4490 0.2713 -0.0939 -0.0472 0.0164  170 LYS A NZ  
1388 N  N   . GLY A 170 ? 0.2882 0.1794 0.1882 -0.0634 0.0185  0.0172  171 GLY A N   
1389 C  CA  . GLY A 170 ? 0.2749 0.1571 0.2401 -0.0294 -0.0175 0.0544  171 GLY A CA  
1390 C  C   . GLY A 170 ? 0.2778 0.1758 0.1977 0.0038  -0.0160 0.0269  171 GLY A C   
1391 O  O   . GLY A 170 ? 0.3449 0.1824 0.2504 -0.0305 0.0126  0.0714  171 GLY A O   
1392 N  N   . LYS A 171 ? 0.2332 0.1553 0.2125 -0.0219 0.0164  0.0573  172 LYS A N   
1393 C  CA  . LYS A 171 ? 0.2651 0.1982 0.2365 -0.0054 0.0080  0.0335  172 LYS A CA  
1394 C  C   . LYS A 171 ? 0.2633 0.1855 0.1300 0.0087  0.0087  0.0098  172 LYS A C   
1395 O  O   . LYS A 171 ? 0.2627 0.1965 0.1324 -0.0065 0.0081  0.0322  172 LYS A O   
1396 C  CB  . LYS A 171 ? 0.3075 0.2016 0.1454 -0.0282 0.0071  0.0126  172 LYS A CB  
1397 C  CG  . LYS A 171 ? 0.2870 0.2516 0.2547 -0.0469 0.0007  -0.0260 172 LYS A CG  
1398 C  CD  . LYS A 171 ? 0.4215 0.1931 0.4160 0.0076  -0.0903 -0.0269 172 LYS A CD  
1399 C  CE  . LYS A 171 ? 0.6161 0.4531 0.3618 0.0162  -0.1631 -0.0104 172 LYS A CE  
1400 N  NZ  . LYS A 171 ? 0.7419 0.3068 0.3033 -0.0285 0.1118  0.0120  172 LYS A NZ  
1401 N  N   . SER A 172 ? 0.3222 0.2106 0.1763 -0.0120 -0.0188 0.0957  173 SER A N   
1402 C  CA  . SER A 172 ? 0.2961 0.2328 0.2135 0.0132  -0.0104 0.0135  173 SER A CA  
1403 C  C   . SER A 172 ? 0.2694 0.1913 0.1368 0.0081  0.0037  0.0513  173 SER A C   
1404 O  O   . SER A 172 ? 0.3791 0.2669 0.1176 0.0447  0.0024  0.0412  173 SER A O   
1405 C  CB  . SER A 172 ? 0.3105 0.2273 0.1934 -0.0086 0.0103  0.0546  173 SER A CB  
1406 O  OG  . SER A 172 ? 0.5393 0.2081 0.2300 0.0093  0.0230  0.0771  173 SER A OG  
1407 N  N   . ALA A 173 ? 0.2572 0.2569 0.1546 0.0625  -0.0130 0.0164  174 ALA A N   
1408 C  CA  . ALA A 173 ? 0.3122 0.3524 0.1395 0.0564  -0.0403 0.0987  174 ALA A CA  
1409 C  C   . ALA A 173 ? 0.2395 0.2302 0.1476 -0.0081 -0.0359 0.0342  174 ALA A C   
1410 O  O   . ALA A 173 ? 0.2669 0.2236 0.1224 0.0248  -0.0295 0.0262  174 ALA A O   
1411 C  CB  . ALA A 173 ? 0.4289 0.2675 0.1747 0.0644  -0.0472 0.0142  174 ALA A CB  
1412 N  N   . ASP A 174 ? 0.2997 0.3069 0.1313 0.0403  -0.0252 0.0684  175 ASP A N   
1413 C  CA  . ASP A 174 ? 0.2996 0.2878 0.1352 0.0303  -0.0132 0.0443  175 ASP A CA  
1414 C  C   . ASP A 174 ? 0.3675 0.2196 0.1643 -0.0109 -0.0891 0.0634  175 ASP A C   
1415 O  O   . ASP A 174 ? 0.3726 0.2544 0.1923 0.0403  -0.0219 -0.0076 175 ASP A O   
1416 C  CB  . ASP A 174 ? 0.2169 0.2990 0.3075 0.0065  -0.0811 0.0983  175 ASP A CB  
1417 C  CG  . ASP A 174 ? 0.5690 0.4196 0.3194 -0.0665 -0.0838 0.1783  175 ASP A CG  
1418 O  OD1 . ASP A 174 ? 1.2022 1.0844 0.8363 -0.1745 -0.7210 0.0549  175 ASP A OD1 
1419 O  OD2 . ASP A 174 ? 0.4020 0.3784 0.3054 0.0198  0.0135  0.1164  175 ASP A OD2 
1420 N  N   . PHE A 175 ? 0.3298 0.2307 0.1523 0.0102  -0.0310 0.0035  176 PHE A N   
1421 C  CA  . PHE A 175 ? 0.2835 0.1981 0.1821 0.0214  -0.0460 0.0421  176 PHE A CA  
1422 C  C   . PHE A 175 ? 0.3097 0.1641 0.1957 -0.0126 -0.0790 0.0051  176 PHE A C   
1423 O  O   . PHE A 175 ? 0.3496 0.2331 0.1648 0.0478  -0.0975 -0.0219 176 PHE A O   
1424 C  CB  . PHE A 175 ? 0.3324 0.1670 0.1844 0.0054  -0.0575 0.0137  176 PHE A CB  
1425 C  CG  . PHE A 175 ? 0.3076 0.1429 0.1767 0.0388  -0.0406 0.0060  176 PHE A CG  
1426 C  CD1 . PHE A 175 ? 0.4477 0.1700 0.1965 0.0160  -0.0137 -0.0227 176 PHE A CD1 
1427 C  CD2 . PHE A 175 ? 0.3298 0.1826 0.1567 0.0031  -0.0842 0.0038  176 PHE A CD2 
1428 C  CE1 . PHE A 175 ? 0.4567 0.1562 0.2228 0.0252  -0.0076 0.0152  176 PHE A CE1 
1429 C  CE2 . PHE A 175 ? 0.3657 0.1828 0.1934 0.0432  -0.0777 0.0331  176 PHE A CE2 
1430 C  CZ  . PHE A 175 ? 0.3379 0.1641 0.2107 0.0337  -0.0767 -0.0038 176 PHE A CZ  
1431 N  N   . THR A 176 ? 0.3492 0.2159 0.1388 0.0041  -0.0873 0.0307  177 THR A N   
1432 C  CA  . THR A 176 ? 0.2925 0.2223 0.1659 0.0516  -0.0454 0.0507  177 THR A CA  
1433 C  C   . THR A 176 ? 0.2408 0.1686 0.1600 -0.0098 -0.0680 0.0487  177 THR A C   
1434 O  O   . THR A 176 ? 0.3172 0.1616 0.1650 -0.0110 -0.0771 0.0285  177 THR A O   
1435 C  CB  . THR A 176 ? 0.3118 0.1958 0.1597 0.0164  -0.0674 0.0603  177 THR A CB  
1436 O  OG1 . THR A 176 ? 0.5066 0.2299 0.1597 0.0750  -0.0966 0.0592  177 THR A OG1 
1437 C  CG2 . THR A 176 ? 0.2996 0.3586 0.3324 0.0344  -0.0482 0.1720  177 THR A CG2 
1438 N  N   . ASN A 177 ? 0.2842 0.1893 0.1453 0.0211  -0.0781 0.0196  178 ASN A N   
1439 C  CA  . ASN A 177 ? 0.2526 0.1977 0.2053 -0.0142 -0.0952 0.0544  178 ASN A CA  
1440 C  C   . ASN A 177 ? 0.2605 0.1864 0.1573 0.0006  -0.0811 0.0346  178 ASN A C   
1441 O  O   . ASN A 177 ? 0.3632 0.2089 0.3064 -0.0174 -0.1136 0.0922  178 ASN A O   
1442 C  CB  . ASN A 177 ? 0.3269 0.1943 0.2216 0.0241  -0.1184 0.0445  178 ASN A CB  
1443 C  CG  . ASN A 177 ? 0.3179 0.2313 0.1758 0.0626  -0.0878 0.0200  178 ASN A CG  
1444 O  OD1 . ASN A 177 ? 0.3082 0.1990 0.2512 0.0549  -0.0263 0.0500  178 ASN A OD1 
1445 N  ND2 . ASN A 177 ? 0.2716 0.2001 0.1840 -0.0126 -0.1001 0.0436  178 ASN A ND2 
1446 N  N   . PHE A 178 ? 0.2950 0.1694 0.1541 0.0048  -0.0854 0.0261  179 PHE A N   
1447 C  CA  . PHE A 178 ? 0.2875 0.1342 0.1613 0.0026  -0.0593 0.0318  179 PHE A CA  
1448 C  C   . PHE A 178 ? 0.2630 0.1570 0.1471 -0.0052 -0.0834 0.0110  179 PHE A C   
1449 O  O   . PHE A 178 ? 0.3360 0.1557 0.1527 -0.0087 -0.0812 0.0108  179 PHE A O   
1450 C  CB  . PHE A 178 ? 0.2838 0.1526 0.1488 0.0232  -0.0276 0.0318  179 PHE A CB  
1451 C  CG  . PHE A 178 ? 0.2788 0.1379 0.1726 0.0076  -0.0627 0.0305  179 PHE A CG  
1452 C  CD1 . PHE A 178 ? 0.3219 0.1582 0.1679 0.0225  -0.0535 0.0208  179 PHE A CD1 
1453 C  CD2 . PHE A 178 ? 0.2559 0.1453 0.1561 0.0214  -0.0421 0.0280  179 PHE A CD2 
1454 C  CE1 . PHE A 178 ? 0.3331 0.1891 0.1571 0.0071  -0.0549 0.0370  179 PHE A CE1 
1455 C  CE2 . PHE A 178 ? 0.2178 0.1451 0.1875 -0.0054 -0.0588 0.0195  179 PHE A CE2 
1456 C  CZ  . PHE A 178 ? 0.2759 0.1528 0.1615 -0.0024 -0.0221 0.0205  179 PHE A CZ  
1457 N  N   . ASP A 179 ? 0.2449 0.1801 0.1589 0.0281  -0.0838 0.0241  180 ASP A N   
1458 C  CA  . ASP A 179 ? 0.2727 0.1972 0.1395 0.0357  -0.1040 0.0041  180 ASP A CA  
1459 C  C   . ASP A 179 ? 0.2213 0.1564 0.1541 0.0076  -0.0564 0.0176  180 ASP A C   
1460 O  O   . ASP A 179 ? 0.2641 0.1632 0.1492 0.0024  -0.0636 0.0063  180 ASP A O   
1461 C  CB  . ASP A 179 ? 0.2453 0.2201 0.2286 0.0230  -0.0964 0.0292  180 ASP A CB  
1462 C  CG  . ASP A 179 ? 0.2577 0.2435 0.2710 0.0443  -0.1159 0.0366  180 ASP A CG  
1463 O  OD1 . ASP A 179 ? 0.2440 0.1879 0.2301 0.0299  -0.0851 0.0392  180 ASP A OD1 
1464 O  OD2 . ASP A 179 ? 0.2587 0.4161 0.3029 0.0135  -0.0860 -0.0239 180 ASP A OD2 
1465 N  N   . PRO A 180 ? 0.2101 0.1424 0.1473 0.0115  -0.0524 0.0093  181 PRO A N   
1466 C  CA  . PRO A 180 ? 0.1846 0.1557 0.1758 0.0124  -0.0697 0.0335  181 PRO A CA  
1467 C  C   . PRO A 180 ? 0.2013 0.1521 0.1756 0.0242  -0.0812 0.0143  181 PRO A C   
1468 O  O   . PRO A 180 ? 0.1880 0.1562 0.1712 0.0141  -0.0636 0.0077  181 PRO A O   
1469 C  CB  . PRO A 180 ? 0.1946 0.1743 0.1882 -0.0104 -0.0340 0.0184  181 PRO A CB  
1470 C  CG  . PRO A 180 ? 0.2318 0.1864 0.1749 0.0031  -0.0693 0.0147  181 PRO A CG  
1471 C  CD  . PRO A 180 ? 0.2240 0.1600 0.1650 -0.0070 -0.0781 0.0091  181 PRO A CD  
1472 N  N   . ARG A 181 ? 0.2034 0.1570 0.1629 0.0141  -0.0581 0.0208  182 ARG A N   
1473 C  CA  . ARG A 181 ? 0.1968 0.1384 0.2098 0.0299  -0.0568 0.0049  182 ARG A CA  
1474 C  C   . ARG A 181 ? 0.1923 0.1729 0.1764 0.0219  -0.0741 0.0293  182 ARG A C   
1475 O  O   . ARG A 181 ? 0.2220 0.1679 0.2020 0.0103  -0.0593 0.0186  182 ARG A O   
1476 C  CB  . ARG A 181 ? 0.1762 0.1808 0.1853 0.0076  -0.0355 0.0109  182 ARG A CB  
1477 C  CG  . ARG A 181 ? 0.2119 0.1639 0.2277 0.0131  -0.0412 -0.0085 182 ARG A CG  
1478 C  CD  . ARG A 181 ? 0.2187 0.2273 0.2878 0.0310  -0.0241 0.0200  182 ARG A CD  
1479 N  NE  . ARG A 181 ? 0.2044 0.2044 0.2881 -0.0023 -0.0381 0.0421  182 ARG A NE  
1480 C  CZ  . ARG A 181 ? 0.1972 0.2435 0.2748 0.0136  0.0000  0.0559  182 ARG A CZ  
1481 N  NH1 . ARG A 181 ? 0.1891 0.3488 0.3388 0.0439  0.0445  0.0995  182 ARG A NH1 
1482 N  NH2 . ARG A 181 ? 0.2273 0.3949 0.3255 0.0557  -0.0119 0.0935  182 ARG A NH2 
1483 N  N   . GLY A 182 ? 0.2055 0.1573 0.1799 0.0286  -0.0781 0.0043  183 GLY A N   
1484 C  CA  . GLY A 182 ? 0.2094 0.1403 0.2143 0.0074  -0.0745 0.0282  183 GLY A CA  
1485 C  C   . GLY A 182 ? 0.2160 0.1483 0.2171 0.0175  -0.0922 0.0120  183 GLY A C   
1486 O  O   . GLY A 182 ? 0.2699 0.1489 0.2641 0.0087  -0.1224 0.0073  183 GLY A O   
1487 N  N   . LEU A 183 ? 0.2002 0.1607 0.1719 0.0182  -0.0816 0.0006  184 LEU A N   
1488 C  CA  . LEU A 183 ? 0.2101 0.1377 0.1621 0.0273  -0.0758 -0.0088 184 LEU A CA  
1489 C  C   . LEU A 183 ? 0.2004 0.1305 0.1712 0.0060  -0.0635 -0.0204 184 LEU A C   
1490 O  O   . LEU A 183 ? 0.1968 0.1624 0.1957 0.0054  -0.0544 0.0294  184 LEU A O   
1491 C  CB  . LEU A 183 ? 0.1782 0.1589 0.1898 0.0107  -0.0658 -0.0013 184 LEU A CB  
1492 C  CG  . LEU A 183 ? 0.2345 0.1964 0.1657 0.0502  -0.0798 -0.0007 184 LEU A CG  
1493 C  CD1 . LEU A 183 ? 0.2587 0.2706 0.1816 0.0434  -0.0656 0.0491  184 LEU A CD1 
1494 C  CD2 . LEU A 183 ? 0.3105 0.1914 0.2022 0.0559  -0.0362 -0.0003 184 LEU A CD2 
1495 N  N   . LEU A 184 ? 0.2079 0.1421 0.1686 0.0027  -0.0483 0.0087  185 LEU A N   
1496 C  CA  . LEU A 184 ? 0.1458 0.1458 0.1864 -0.0274 -0.0399 0.0255  185 LEU A CA  
1497 C  C   . LEU A 184 ? 0.1807 0.1580 0.2241 -0.0313 -0.0992 0.0344  185 LEU A C   
1498 O  O   . LEU A 184 ? 0.2415 0.2036 0.3029 -0.0688 -0.1532 0.0710  185 LEU A O   
1499 C  CB  . LEU A 184 ? 0.1612 0.1570 0.1875 -0.0266 -0.0255 0.0160  185 LEU A CB  
1500 C  CG  . LEU A 184 ? 0.1333 0.1668 0.1949 -0.0015 -0.0344 0.0031  185 LEU A CG  
1501 C  CD1 . LEU A 184 ? 0.1659 0.2261 0.1903 0.0296  -0.0206 0.0147  185 LEU A CD1 
1502 C  CD2 . LEU A 184 ? 0.1614 0.1815 0.2968 -0.0108 -0.0860 0.0222  185 LEU A CD2 
1503 N  N   . PRO A 185 ? 0.1307 0.1490 0.2096 -0.0211 -0.0540 0.0143  186 PRO A N   
1504 C  CA  . PRO A 185 ? 0.1124 0.1598 0.2275 -0.0006 -0.0405 0.0236  186 PRO A CA  
1505 C  C   . PRO A 185 ? 0.1318 0.1316 0.2410 -0.0035 -0.0579 0.0151  186 PRO A C   
1506 O  O   . PRO A 185 ? 0.1124 0.1518 0.3790 0.0000  -0.0680 0.0410  186 PRO A O   
1507 C  CB  . PRO A 185 ? 0.1049 0.1862 0.1970 0.0214  -0.0281 0.0187  186 PRO A CB  
1508 C  CG  . PRO A 185 ? 0.1343 0.1724 0.1597 0.0121  -0.0225 0.0076  186 PRO A CG  
1509 C  CD  . PRO A 185 ? 0.1420 0.1609 0.1412 0.0115  -0.0304 -0.0007 186 PRO A CD  
1510 N  N   A GLU A 186 ? 0.1367 0.1720 0.2712 -0.0401 -0.0627 0.0194  187 GLU A N   
1511 N  N   B GLU A 186 ? 0.1421 0.1591 0.2710 -0.0346 -0.0584 0.0142  187 GLU A N   
1512 C  CA  A GLU A 186 ? 0.1271 0.1886 0.2770 -0.0397 -0.0505 -0.0024 187 GLU A CA  
1513 C  CA  B GLU A 186 ? 0.0995 0.1542 0.2845 -0.0412 -0.0562 0.0046  187 GLU A CA  
1514 C  C   A GLU A 186 ? 0.0951 0.1685 0.2626 -0.0006 -0.0188 0.0143  187 GLU A C   
1515 C  C   B GLU A 186 ? 0.0997 0.1670 0.2712 -0.0115 -0.0322 0.0098  187 GLU A C   
1516 O  O   A GLU A 186 ? 0.1275 0.2268 0.3934 0.0549  -0.0303 0.0175  187 GLU A O   
1517 O  O   B GLU A 186 ? 0.0834 0.2011 0.3925 -0.0054 -0.0236 0.0035  187 GLU A O   
1518 C  CB  A GLU A 186 ? 0.1955 0.2189 0.3009 -0.0623 -0.0562 0.0175  187 GLU A CB  
1519 C  CB  B GLU A 186 ? 0.1861 0.1961 0.3837 -0.0930 -0.0447 0.0143  187 GLU A CB  
1520 C  CG  A GLU A 186 ? 0.2356 0.2182 0.3869 0.0790  -0.0207 0.0793  187 GLU A CG  
1521 C  CG  B GLU A 186 ? 0.2637 0.1853 0.4118 -0.0737 -0.1111 0.0361  187 GLU A CG  
1522 C  CD  A GLU A 186 ? 0.1918 0.3532 0.3905 -0.0522 0.0648  0.0120  187 GLU A CD  
1523 C  CD  B GLU A 186 ? 0.1203 0.3245 0.4444 -0.0886 -0.0881 0.0249  187 GLU A CD  
1524 O  OE1 A GLU A 186 ? 0.2220 0.2342 0.4570 0.0639  -0.0377 0.0309  187 GLU A OE1 
1525 O  OE1 B GLU A 186 ? 0.1947 0.2896 0.4584 -0.1230 -0.0529 0.0559  187 GLU A OE1 
1526 O  OE2 A GLU A 186 ? 0.2523 0.3180 0.4203 -0.0252 0.0834  0.1151  187 GLU A OE2 
1527 O  OE2 B GLU A 186 ? 0.1386 0.3151 0.5852 -0.0487 -0.0540 -0.0935 187 GLU A OE2 
1528 N  N   . SER A 187 ? 0.0921 0.1708 0.2584 -0.0132 -0.0262 -0.0063 188 SER A N   
1529 C  CA  . SER A 187 ? 0.1199 0.1735 0.2529 -0.0164 -0.0071 0.0226  188 SER A CA  
1530 C  C   . SER A 187 ? 0.0986 0.1907 0.2460 -0.0027 0.0052  0.0121  188 SER A C   
1531 O  O   . SER A 187 ? 0.1206 0.2180 0.2274 -0.0225 -0.0065 -0.0296 188 SER A O   
1532 C  CB  . SER A 187 ? 0.1835 0.2126 0.2234 -0.0333 -0.0266 0.0335  188 SER A CB  
1533 O  OG  . SER A 187 ? 0.1518 0.2213 0.2453 -0.0326 -0.0006 0.0265  188 SER A OG  
1534 N  N   . LEU A 188 ? 0.1027 0.1548 0.2295 -0.0096 -0.0126 -0.0017 189 LEU A N   
1535 C  CA  . LEU A 188 ? 0.1102 0.1611 0.2263 0.0006  -0.0041 -0.0186 189 LEU A CA  
1536 C  C   . LEU A 188 ? 0.1300 0.1697 0.1911 -0.0181 -0.0010 -0.0322 189 LEU A C   
1537 O  O   . LEU A 188 ? 0.1293 0.1905 0.2282 -0.0126 -0.0219 -0.0135 189 LEU A O   
1538 C  CB  . LEU A 188 ? 0.1388 0.2153 0.2519 -0.0184 -0.0221 0.0041  189 LEU A CB  
1539 C  CG  . LEU A 188 ? 0.1676 0.2062 0.2815 -0.0082 -0.0126 0.0401  189 LEU A CG  
1540 C  CD1 . LEU A 188 ? 0.1918 0.1976 0.3043 -0.0230 -0.0557 0.0474  189 LEU A CD1 
1541 C  CD2 . LEU A 188 ? 0.1632 0.3395 0.2516 0.0052  -0.0527 0.0270  189 LEU A CD2 
1542 N  N   . ASP A 189 ? 0.1045 0.1685 0.1975 0.0131  0.0076  -0.0182 190 ASP A N   
1543 C  CA  . ASP A 189 ? 0.1415 0.2212 0.1753 -0.0443 0.0282  -0.0183 190 ASP A CA  
1544 C  C   . ASP A 189 ? 0.1199 0.1448 0.1661 -0.0342 0.0087  -0.0027 190 ASP A C   
1545 O  O   . ASP A 189 ? 0.1062 0.1562 0.1632 -0.0098 0.0010  -0.0093 190 ASP A O   
1546 C  CB  . ASP A 189 ? 0.1588 0.2274 0.2249 -0.0930 0.0216  0.0131  190 ASP A CB  
1547 C  CG  . ASP A 189 ? 0.2020 0.3503 0.1911 -0.0912 -0.0166 0.0160  190 ASP A CG  
1548 O  OD1 . ASP A 189 ? 0.2228 0.4505 0.3399 -0.0702 0.0837  -0.0436 190 ASP A OD1 
1549 O  OD2 . ASP A 189 ? 0.2381 0.5325 0.3374 -0.1744 0.0154  0.0619  190 ASP A OD2 
1550 N  N   . TYR A 190 ? 0.1216 0.1442 0.1532 -0.0142 0.0120  0.0054  191 TYR A N   
1551 C  CA  . TYR A 190 ? 0.1129 0.1701 0.1474 -0.0240 -0.0120 0.0140  191 TYR A CA  
1552 C  C   . TYR A 190 ? 0.0988 0.1262 0.1181 -0.0147 0.0104  0.0152  191 TYR A C   
1553 O  O   . TYR A 190 ? 0.1158 0.1600 0.1309 -0.0081 0.0148  0.0046  191 TYR A O   
1554 C  CB  . TYR A 190 ? 0.1361 0.1431 0.1438 -0.0109 0.0037  0.0114  191 TYR A CB  
1555 C  CG  . TYR A 190 ? 0.1133 0.1305 0.1518 -0.0070 0.0005  0.0214  191 TYR A CG  
1556 C  CD1 . TYR A 190 ? 0.0917 0.1543 0.1798 -0.0065 0.0060  0.0059  191 TYR A CD1 
1557 C  CD2 . TYR A 190 ? 0.1406 0.1578 0.1579 0.0153  0.0173  0.0211  191 TYR A CD2 
1558 C  CE1 . TYR A 190 ? 0.1230 0.1555 0.1886 -0.0093 -0.0015 0.0152  191 TYR A CE1 
1559 C  CE2 . TYR A 190 ? 0.1244 0.1594 0.1905 0.0054  -0.0120 0.0096  191 TYR A CE2 
1560 C  CZ  . TYR A 190 ? 0.1455 0.1726 0.1428 0.0146  0.0087  0.0052  191 TYR A CZ  
1561 O  OH  . TYR A 190 ? 0.1471 0.1711 0.1832 0.0353  -0.0137 -0.0020 191 TYR A OH  
1562 N  N   . TRP A 191 ? 0.0995 0.1300 0.1215 -0.0142 -0.0017 -0.0019 192 TRP A N   
1563 C  CA  . TRP A 191 ? 0.0926 0.1194 0.1255 0.0000  0.0087  0.0140  192 TRP A CA  
1564 C  C   . TRP A 191 ? 0.1036 0.1259 0.1040 0.0065  0.0041  -0.0126 192 TRP A C   
1565 O  O   . TRP A 191 ? 0.1277 0.1336 0.1187 -0.0214 -0.0038 0.0049  192 TRP A O   
1566 C  CB  . TRP A 191 ? 0.1084 0.1149 0.1413 -0.0065 0.0000  0.0006  192 TRP A CB  
1567 C  CG  . TRP A 191 ? 0.1120 0.1307 0.1300 0.0048  -0.0046 -0.0019 192 TRP A CG  
1568 C  CD1 . TRP A 191 ? 0.1509 0.1424 0.1395 0.0126  0.0126  0.0062  192 TRP A CD1 
1569 C  CD2 . TRP A 191 ? 0.0983 0.1306 0.1366 0.0142  -0.0120 0.0136  192 TRP A CD2 
1570 N  NE1 . TRP A 191 ? 0.1758 0.1342 0.1465 0.0000  0.0065  0.0140  192 TRP A NE1 
1571 C  CE2 . TRP A 191 ? 0.1746 0.1395 0.1318 0.0073  0.0076  0.0043  192 TRP A CE2 
1572 C  CE3 . TRP A 191 ? 0.1178 0.1321 0.1476 0.0114  -0.0020 0.0073  192 TRP A CE3 
1573 C  CZ2 . TRP A 191 ? 0.1597 0.1199 0.1870 0.0010  -0.0076 0.0148  192 TRP A CZ2 
1574 C  CZ3 . TRP A 191 ? 0.0992 0.1740 0.1682 -0.0024 -0.0129 -0.0027 192 TRP A CZ3 
1575 C  CH2 . TRP A 191 ? 0.1472 0.1257 0.1966 0.0012  -0.0196 -0.0063 192 TRP A CH2 
1576 N  N   . THR A 192 ? 0.0983 0.1226 0.1163 -0.0037 -0.0076 0.0031  193 THR A N   
1577 C  CA  . THR A 192 ? 0.0856 0.1324 0.1261 -0.0052 0.0038  0.0059  193 THR A CA  
1578 C  C   . THR A 192 ? 0.0965 0.1255 0.0996 0.0121  -0.0013 0.0114  193 THR A C   
1579 O  O   . THR A 192 ? 0.1124 0.1481 0.1070 -0.0068 0.0068  0.0017  193 THR A O   
1580 C  CB  . THR A 192 ? 0.1070 0.1133 0.1203 0.0037  0.0065  0.0062  193 THR A CB  
1581 O  OG1 . THR A 192 ? 0.1088 0.1282 0.1244 0.0000  0.0000  -0.0010 193 THR A OG1 
1582 C  CG2 . THR A 192 ? 0.1273 0.1379 0.1263 0.0068  0.0164  0.0003  193 THR A CG2 
1583 N  N   . TYR A 193 ? 0.0856 0.1190 0.1208 0.0020  -0.0007 0.0043  194 TYR A N   
1584 C  CA  . TYR A 193 ? 0.0948 0.1300 0.1128 -0.0076 -0.0074 0.0037  194 TYR A CA  
1585 C  C   . TYR A 193 ? 0.1014 0.1124 0.1099 -0.0010 -0.0115 -0.0054 194 TYR A C   
1586 O  O   . TYR A 193 ? 0.1063 0.1315 0.1062 0.0054  -0.0103 0.0015  194 TYR A O   
1587 C  CB  . TYR A 193 ? 0.1260 0.1439 0.1079 0.0087  -0.0020 -0.0052 194 TYR A CB  
1588 C  CG  . TYR A 193 ? 0.1142 0.1102 0.1194 0.0023  -0.0170 0.0120  194 TYR A CG  
1589 C  CD1 . TYR A 193 ? 0.1106 0.1106 0.1019 -0.0026 -0.0060 0.0071  194 TYR A CD1 
1590 C  CD2 . TYR A 193 ? 0.1072 0.1163 0.1127 0.0080  -0.0131 -0.0087 194 TYR A CD2 
1591 C  CE1 . TYR A 193 ? 0.0890 0.1167 0.1208 -0.0005 -0.0093 0.0088  194 TYR A CE1 
1592 C  CE2 . TYR A 193 ? 0.1081 0.1133 0.1187 0.0110  -0.0161 0.0038  194 TYR A CE2 
1593 C  CZ  . TYR A 193 ? 0.1106 0.1063 0.1036 0.0068  -0.0065 0.0051  194 TYR A CZ  
1594 O  OH  . TYR A 193 ? 0.1088 0.1090 0.1111 0.0012  -0.0102 0.0003  194 TYR A OH  
1595 N  N   . PRO A 194 ? 0.0983 0.1230 0.1084 -0.0007 -0.0043 -0.0093 195 PRO A N   
1596 C  CA  . PRO A 194 ? 0.0960 0.1386 0.1225 0.0051  -0.0027 -0.0175 195 PRO A CA  
1597 C  C   . PRO A 194 ? 0.0850 0.1057 0.1124 -0.0102 -0.0132 -0.0147 195 PRO A C   
1598 O  O   . PRO A 194 ? 0.1203 0.1377 0.1142 0.0208  -0.0063 -0.0027 195 PRO A O   
1599 C  CB  . PRO A 194 ? 0.1194 0.1720 0.1190 -0.0167 -0.0003 -0.0148 195 PRO A CB  
1600 C  CG  . PRO A 194 ? 0.1606 0.1562 0.1259 -0.0230 -0.0087 -0.0154 195 PRO A CG  
1601 C  CD  . PRO A 194 ? 0.1469 0.1641 0.0930 -0.0307 -0.0068 -0.0041 195 PRO A CD  
1602 N  N   . GLY A 195 ? 0.0935 0.1120 0.1147 -0.0020 -0.0027 -0.0148 196 GLY A N   
1603 C  CA  . GLY A 195 ? 0.1104 0.1176 0.1099 -0.0005 -0.0065 -0.0051 196 GLY A CA  
1604 C  C   . GLY A 195 ? 0.0790 0.1138 0.1008 -0.0115 -0.0007 -0.0020 196 GLY A C   
1605 O  O   . GLY A 195 ? 0.1010 0.1079 0.1133 -0.0024 -0.0043 -0.0074 196 GLY A O   
1606 N  N   . SER A 196 ? 0.0934 0.1255 0.0926 -0.0027 -0.0135 -0.0071 197 SER A N   
1607 C  CA  . SER A 196 ? 0.0816 0.1272 0.1040 0.0131  0.0017  -0.0057 197 SER A CA  
1608 C  C   . SER A 196 ? 0.0740 0.1040 0.1163 0.0076  -0.0132 -0.0076 197 SER A C   
1609 O  O   . SER A 196 ? 0.0970 0.1084 0.1203 -0.0093 -0.0103 -0.0019 197 SER A O   
1610 C  CB  . SER A 196 ? 0.0964 0.1185 0.1280 0.0073  -0.0099 -0.0041 197 SER A CB  
1611 O  OG  . SER A 196 ? 0.0904 0.1102 0.1314 0.0085  -0.0126 -0.0035 197 SER A OG  
1612 N  N   . LEU A 197 ? 0.0872 0.1187 0.1149 0.0082  0.0034  -0.0054 198 LEU A N   
1613 C  CA  . LEU A 197 ? 0.0926 0.1262 0.0996 -0.0005 0.0076  -0.0031 198 LEU A CA  
1614 C  C   . LEU A 197 ? 0.0979 0.1237 0.1127 -0.0160 -0.0006 -0.0038 198 LEU A C   
1615 O  O   . LEU A 197 ? 0.0974 0.1181 0.1284 -0.0060 -0.0096 -0.0176 198 LEU A O   
1616 C  CB  . LEU A 197 ? 0.1093 0.1237 0.1330 -0.0071 -0.0017 -0.0076 198 LEU A CB  
1617 C  CG  . LEU A 197 ? 0.1093 0.1336 0.1178 -0.0057 0.0000  -0.0019 198 LEU A CG  
1618 C  CD1 . LEU A 197 ? 0.1336 0.1747 0.1506 -0.0252 0.0142  0.0041  198 LEU A CD1 
1619 C  CD2 . LEU A 197 ? 0.1058 0.1609 0.1670 0.0015  0.0082  0.0241  198 LEU A CD2 
1620 N  N   . THR A 198 ? 0.0908 0.1088 0.1201 0.0046  -0.0062 -0.0081 199 THR A N   
1621 C  CA  . THR A 198 ? 0.0904 0.1124 0.1367 -0.0076 0.0024  -0.0086 199 THR A CA  
1622 C  C   . THR A 198 ? 0.0803 0.1142 0.1404 -0.0054 -0.0003 -0.0114 199 THR A C   
1623 O  O   . THR A 198 ? 0.0900 0.1277 0.1473 0.0000  0.0024  -0.0068 199 THR A O   
1624 C  CB  . THR A 198 ? 0.1155 0.1010 0.1045 -0.0043 -0.0137 -0.0097 199 THR A CB  
1625 O  OG1 . THR A 198 ? 0.1111 0.1049 0.1022 -0.0070 -0.0049 -0.0013 199 THR A OG1 
1626 C  CG2 . THR A 198 ? 0.1058 0.1154 0.1257 -0.0077 0.0065  -0.0043 199 THR A CG2 
1627 N  N   . THR A 199 ? 0.1115 0.1203 0.1377 -0.0135 0.0218  -0.0125 200 THR A N   
1628 C  CA  . THR A 199 ? 0.1129 0.1196 0.1518 -0.0137 0.0198  -0.0137 200 THR A CA  
1629 C  C   . THR A 199 ? 0.0930 0.1298 0.1683 -0.0140 0.0113  -0.0019 200 THR A C   
1630 O  O   . THR A 199 ? 0.1068 0.1287 0.1632 -0.0148 0.0137  -0.0208 200 THR A O   
1631 C  CB  . THR A 199 ? 0.1212 0.1286 0.1517 -0.0043 0.0017  -0.0071 200 THR A CB  
1632 O  OG1 . THR A 199 ? 0.2397 0.2119 0.1453 0.0864  0.0194  0.0003  200 THR A OG1 
1633 C  CG2 . THR A 199 ? 0.1722 0.2055 0.1594 -0.0797 -0.0175 -0.0012 200 THR A CG2 
1634 N  N   . PRO A 200 ? 0.1048 0.1498 0.1465 -0.0211 0.0252  -0.0102 201 PRO A N   
1635 C  CA  . PRO A 200 ? 0.1093 0.1465 0.1541 -0.0441 0.0214  -0.0030 201 PRO A CA  
1636 C  C   . PRO A 200 ? 0.1263 0.1631 0.1557 -0.0285 0.0048  -0.0027 201 PRO A C   
1637 O  O   . PRO A 200 ? 0.1607 0.1731 0.1782 -0.0126 -0.0074 -0.0023 201 PRO A O   
1638 C  CB  . PRO A 200 ? 0.1284 0.1703 0.1788 -0.0177 0.0098  -0.0140 201 PRO A CB  
1639 C  CG  . PRO A 200 ? 0.1097 0.1862 0.1816 -0.0088 0.0162  -0.0242 201 PRO A CG  
1640 C  CD  . PRO A 200 ? 0.1226 0.1770 0.1712 -0.0040 0.0177  -0.0449 201 PRO A CD  
1641 N  N   . PRO A 201 ? 0.1178 0.1483 0.1677 -0.0263 0.0068  0.0010  202 PRO A N   
1642 C  CA  . PRO A 201 ? 0.1215 0.1448 0.1597 -0.0206 0.0010  -0.0082 202 PRO A CA  
1643 C  C   . PRO A 201 ? 0.1018 0.1411 0.1616 -0.0041 0.0005  -0.0096 202 PRO A C   
1644 O  O   . PRO A 201 ? 0.1190 0.1500 0.1728 -0.0287 -0.0027 -0.0059 202 PRO A O   
1645 C  CB  . PRO A 201 ? 0.1597 0.1418 0.2135 -0.0254 0.0237  0.0110  202 PRO A CB  
1646 C  CG  . PRO A 201 ? 0.1532 0.1724 0.2237 -0.0211 -0.0074 -0.0096 202 PRO A CG  
1647 C  CD  . PRO A 201 ? 0.1668 0.1503 0.1761 0.0023  0.0019  0.0093  202 PRO A CD  
1648 N  N   . LEU A 202 ? 0.0948 0.1368 0.1395 -0.0153 0.0088  0.0003  203 LEU A N   
1649 C  CA  . LEU A 202 ? 0.0878 0.1413 0.1400 0.0037  -0.0041 -0.0219 203 LEU A CA  
1650 C  C   . LEU A 202 ? 0.1084 0.1372 0.1315 -0.0241 0.0000  -0.0035 203 LEU A C   
1651 O  O   . LEU A 202 ? 0.1001 0.1254 0.1298 -0.0065 -0.0020 -0.0137 203 LEU A O   
1652 C  CB  . LEU A 202 ? 0.0903 0.1289 0.1571 0.0031  -0.0017 -0.0020 203 LEU A CB  
1653 C  CG  . LEU A 202 ? 0.1022 0.1422 0.1597 -0.0040 0.0159  -0.0219 203 LEU A CG  
1654 C  CD1 . LEU A 202 ? 0.0992 0.1736 0.1997 0.0120  -0.0030 -0.0331 203 LEU A CD1 
1655 C  CD2 . LEU A 202 ? 0.1058 0.1395 0.1783 -0.0046 -0.0043 -0.0142 203 LEU A CD2 
1656 N  N   . LEU A 203 ? 0.0913 0.1160 0.1676 0.0005  -0.0051 -0.0132 204 LEU A N   
1657 C  CA  . LEU A 203 ? 0.1053 0.1300 0.1647 -0.0063 0.0093  -0.0173 204 LEU A CA  
1658 C  C   . LEU A 203 ? 0.1040 0.1079 0.1665 0.0020  0.0065  -0.0137 204 LEU A C   
1659 O  O   . LEU A 203 ? 0.1058 0.1239 0.1388 -0.0177 -0.0104 -0.0098 204 LEU A O   
1660 C  CB  . LEU A 203 ? 0.1374 0.1225 0.1988 -0.0087 0.0065  0.0019  204 LEU A CB  
1661 C  CG  . LEU A 203 ? 0.1553 0.1510 0.2020 -0.0031 0.0318  0.0107  204 LEU A CG  
1662 C  CD1 . LEU A 203 ? 0.1815 0.1494 0.2450 0.0196  0.0485  0.0166  204 LEU A CD1 
1663 C  CD2 . LEU A 203 ? 0.1611 0.1761 0.3625 -0.0856 0.0188  0.0037  204 LEU A CD2 
1664 N  N   . GLU A 204 ? 0.1041 0.1315 0.1485 -0.0052 -0.0115 -0.0143 205 GLU A N   
1665 C  CA  . GLU A 204 ? 0.1206 0.1321 0.1343 -0.0019 -0.0153 -0.0176 205 GLU A CA  
1666 C  C   . GLU A 204 ? 0.1058 0.1463 0.1248 -0.0071 -0.0324 -0.0184 205 GLU A C   
1667 O  O   . GLU A 204 ? 0.1465 0.1833 0.1521 0.0230  -0.0344 -0.0471 205 GLU A O   
1668 C  CB  . GLU A 204 ? 0.1497 0.1444 0.1476 0.0130  -0.0351 -0.0282 205 GLU A CB  
1669 C  CG  . GLU A 204 ? 0.1155 0.1521 0.1731 0.0153  -0.0419 -0.0178 205 GLU A CG  
1670 C  CD  . GLU A 204 ? 0.1571 0.1682 0.1394 -0.0031 -0.0364 -0.0269 205 GLU A CD  
1671 O  OE1 . GLU A 204 ? 0.1508 0.1833 0.2255 0.0164  -0.0820 -0.0527 205 GLU A OE1 
1672 O  OE2 . GLU A 204 ? 0.1253 0.1589 0.1789 -0.0043 -0.0397 -0.0147 205 GLU A OE2 
1673 N  N   . CYS A 205 ? 0.0987 0.1167 0.1368 -0.0093 -0.0152 -0.0104 206 CYS A N   
1674 C  CA  . CYS A 205 ? 0.1040 0.1361 0.1230 -0.0024 -0.0208 -0.0137 206 CYS A CA  
1675 C  C   . CYS A 205 ? 0.1061 0.0996 0.1357 -0.0017 -0.0207 -0.0140 206 CYS A C   
1676 O  O   . CYS A 205 ? 0.1146 0.1124 0.1713 0.0076  -0.0307 -0.0013 206 CYS A O   
1677 C  CB  . CYS A 205 ? 0.1049 0.1500 0.1217 -0.0104 0.0038  -0.0054 206 CYS A CB  
1678 S  SG  . CYS A 205 ? 0.1464 0.1332 0.1428 -0.0020 -0.0062 -0.0059 206 CYS A SG  
1679 N  N   . VAL A 206 ? 0.1030 0.1036 0.1291 -0.0092 -0.0074 -0.0080 207 VAL A N   
1680 C  CA  . VAL A 206 ? 0.0930 0.0944 0.1273 0.0015  -0.0051 -0.0046 207 VAL A CA  
1681 C  C   . VAL A 206 ? 0.1032 0.0956 0.1142 0.0137  -0.0208 -0.0087 207 VAL A C   
1682 O  O   . VAL A 206 ? 0.1156 0.1286 0.1360 0.0088  -0.0185 0.0082  207 VAL A O   
1683 C  CB  . VAL A 206 ? 0.0904 0.1072 0.1252 0.0065  0.0074  0.0003  207 VAL A CB  
1684 C  CG1 . VAL A 206 ? 0.0970 0.1151 0.1259 -0.0013 -0.0175 -0.0031 207 VAL A CG1 
1685 C  CG2 . VAL A 206 ? 0.1045 0.1406 0.1354 0.0167  0.0124  -0.0126 207 VAL A CG2 
1686 N  N   . THR A 207 ? 0.0952 0.1014 0.1185 0.0010  -0.0082 0.0035  208 THR A N   
1687 C  CA  . THR A 207 ? 0.0942 0.1266 0.1196 -0.0034 -0.0104 -0.0003 208 THR A CA  
1688 C  C   . THR A 207 ? 0.1036 0.0974 0.1154 -0.0120 -0.0148 0.0052  208 THR A C   
1689 O  O   . THR A 207 ? 0.0964 0.1079 0.1185 0.0000  -0.0186 -0.0006 208 THR A O   
1690 C  CB  . THR A 207 ? 0.0913 0.1149 0.1342 -0.0059 0.0020  -0.0065 208 THR A CB  
1691 O  OG1 . THR A 207 ? 0.1264 0.1261 0.1406 -0.0003 -0.0006 -0.0154 208 THR A OG1 
1692 C  CG2 . THR A 207 ? 0.1049 0.1263 0.1638 0.0003  0.0054  0.0063  208 THR A CG2 
1693 N  N   . TRP A 208 ? 0.0939 0.0957 0.1066 -0.0035 -0.0027 0.0065  209 TRP A N   
1694 C  CA  . TRP A 208 ? 0.0772 0.0939 0.1235 -0.0037 -0.0087 -0.0043 209 TRP A CA  
1695 C  C   . TRP A 208 ? 0.0890 0.0891 0.0921 0.0099  0.0003  -0.0003 209 TRP A C   
1696 O  O   . TRP A 208 ? 0.0947 0.1118 0.1027 0.0037  0.0065  -0.0017 209 TRP A O   
1697 C  CB  . TRP A 208 ? 0.0876 0.1026 0.1127 -0.0006 -0.0068 0.0081  209 TRP A CB  
1698 C  CG  . TRP A 208 ? 0.0850 0.1004 0.0991 0.0222  -0.0038 0.0017  209 TRP A CG  
1699 C  CD1 . TRP A 208 ? 0.0975 0.0935 0.1084 0.0065  -0.0049 -0.0041 209 TRP A CD1 
1700 C  CD2 . TRP A 208 ? 0.0759 0.0891 0.1242 0.0104  -0.0065 -0.0020 209 TRP A CD2 
1701 N  NE1 . TRP A 208 ? 0.0873 0.1086 0.1066 -0.0034 -0.0038 -0.0003 209 TRP A NE1 
1702 C  CE2 . TRP A 208 ? 0.0966 0.0900 0.1210 0.0043  -0.0107 0.0137  209 TRP A CE2 
1703 C  CE3 . TRP A 208 ? 0.0900 0.0973 0.1035 0.0003  -0.0109 0.0074  209 TRP A CE3 
1704 C  CZ2 . TRP A 208 ? 0.1044 0.1018 0.1097 0.0199  0.0013  -0.0048 209 TRP A CZ2 
1705 C  CZ3 . TRP A 208 ? 0.1230 0.1031 0.1190 0.0162  -0.0027 0.0230  209 TRP A CZ3 
1706 C  CH2 . TRP A 208 ? 0.1212 0.1000 0.1192 0.0175  0.0114  0.0017  209 TRP A CH2 
1707 N  N   . ILE A 209 ? 0.0863 0.1010 0.1133 -0.0027 -0.0115 -0.0031 210 ILE A N   
1708 C  CA  . ILE A 209 ? 0.0855 0.0964 0.1279 -0.0107 -0.0059 0.0010  210 ILE A CA  
1709 C  C   . ILE A 209 ? 0.0847 0.0997 0.1032 -0.0148 -0.0027 -0.0037 210 ILE A C   
1710 O  O   . ILE A 209 ? 0.1309 0.1084 0.1106 0.0043  -0.0062 -0.0012 210 ILE A O   
1711 C  CB  . ILE A 209 ? 0.0850 0.1108 0.1427 0.0000  -0.0071 0.0007  210 ILE A CB  
1712 C  CG1 . ILE A 209 ? 0.0930 0.1104 0.1983 0.0115  -0.0258 -0.0187 210 ILE A CG1 
1713 C  CG2 . ILE A 209 ? 0.0921 0.1406 0.1570 0.0020  -0.0162 0.0006  210 ILE A CG2 
1714 C  CD1 . ILE A 209 ? 0.1111 0.1280 0.2249 0.0296  -0.0107 0.0041  210 ILE A CD1 
1715 N  N   . VAL A 210 ? 0.1018 0.0885 0.1164 -0.0073 -0.0020 0.0020  211 VAL A N   
1716 C  CA  . VAL A 210 ? 0.0920 0.1018 0.1120 -0.0087 -0.0003 0.0017  211 VAL A CA  
1717 C  C   . VAL A 210 ? 0.0975 0.0863 0.1090 0.0103  0.0005  -0.0024 211 VAL A C   
1718 O  O   . VAL A 210 ? 0.1099 0.1149 0.1158 -0.0093 -0.0015 0.0000  211 VAL A O   
1719 C  CB  . VAL A 210 ? 0.0920 0.1057 0.1361 0.0051  -0.0052 0.0057  211 VAL A CB  
1720 C  CG1 . VAL A 210 ? 0.1224 0.1054 0.1576 -0.0007 -0.0120 0.0000  211 VAL A CG1 
1721 C  CG2 . VAL A 210 ? 0.1019 0.1279 0.1403 -0.0031 -0.0005 0.0109  211 VAL A CG2 
1722 N  N   . LEU A 211 ? 0.0856 0.1228 0.1298 -0.0114 -0.0126 -0.0006 212 LEU A N   
1723 C  CA  . LEU A 211 ? 0.0832 0.1293 0.1460 -0.0062 -0.0148 0.0023  212 LEU A CA  
1724 C  C   . LEU A 211 ? 0.1068 0.1255 0.1324 -0.0093 -0.0057 0.0043  212 LEU A C   
1725 O  O   . LEU A 211 ? 0.1131 0.1287 0.1318 -0.0097 -0.0024 -0.0007 212 LEU A O   
1726 C  CB  . LEU A 211 ? 0.1331 0.1304 0.1424 -0.0073 -0.0238 0.0065  212 LEU A CB  
1727 C  CG  . LEU A 211 ? 0.1040 0.1510 0.1541 -0.0074 -0.0175 0.0126  212 LEU A CG  
1728 C  CD1 . LEU A 211 ? 0.1181 0.1961 0.1773 -0.0142 -0.0366 0.0165  212 LEU A CD1 
1729 C  CD2 . LEU A 211 ? 0.1303 0.1613 0.1747 -0.0137 0.0031  -0.0006 212 LEU A CD2 
1730 N  N   . LYS A 212 ? 0.1172 0.1415 0.1397 -0.0193 -0.0076 0.0031  213 LYS A N   
1731 C  CA  . LYS A 212 ? 0.1366 0.1394 0.1333 -0.0225 0.0041  0.0226  213 LYS A CA  
1732 C  C   . LYS A 212 ? 0.0864 0.1424 0.1420 -0.0135 -0.0136 0.0141  213 LYS A C   
1733 O  O   . LYS A 212 ? 0.1279 0.1404 0.2056 -0.0031 -0.0346 0.0217  213 LYS A O   
1734 C  CB  . LYS A 212 ? 0.1914 0.1724 0.1534 -0.0675 0.0197  -0.0005 213 LYS A CB  
1735 C  CG  . LYS A 212 ? 0.2559 0.2240 0.2336 -0.0098 0.0030  0.0436  213 LYS A CG  
1736 C  CD  . LYS A 212 ? 0.4677 0.3090 0.2178 -0.1567 0.0131  0.0208  213 LYS A CD  
1737 C  CE  . LYS A 212 ? 0.5504 0.4253 0.3589 -0.1576 -0.0037 0.1955  213 LYS A CE  
1738 N  NZ  . LYS A 212 ? 0.6118 0.5486 0.4083 -0.2017 0.0461  0.1080  213 LYS A NZ  
1739 N  N   . GLU A 213 ? 0.0860 0.1307 0.1429 -0.0088 -0.0119 0.0109  214 GLU A N   
1740 C  CA  . GLU A 213 ? 0.1164 0.1199 0.1661 -0.0161 -0.0292 0.0093  214 GLU A CA  
1741 C  C   . GLU A 213 ? 0.0979 0.1386 0.1363 -0.0096 -0.0225 0.0104  214 GLU A C   
1742 O  O   . GLU A 213 ? 0.1088 0.1330 0.1562 -0.0031 -0.0126 0.0208  214 GLU A O   
1743 C  CB  . GLU A 213 ? 0.1062 0.1471 0.1932 -0.0178 -0.0368 0.0129  214 GLU A CB  
1744 C  CG  . GLU A 213 ? 0.1453 0.2020 0.2257 -0.0472 -0.0640 -0.0063 214 GLU A CG  
1745 C  CD  . GLU A 213 ? 0.1756 0.2478 0.2670 -0.0562 -0.0428 0.0019  214 GLU A CD  
1746 O  OE1 . GLU A 213 ? 0.1528 0.1934 0.3079 -0.0172 -0.0610 0.0115  214 GLU A OE1 
1747 O  OE2 . GLU A 213 ? 0.2529 0.2702 0.4648 -0.0702 -0.1052 -0.0355 214 GLU A OE2 
1748 N  N   A PRO A 214 ? 0.1088 0.1136 0.1421 -0.0003 -0.0119 0.0166  215 PRO A N   
1749 N  N   B PRO A 214 ? 0.1133 0.1164 0.1453 -0.0027 -0.0102 0.0148  215 PRO A N   
1750 C  CA  A PRO A 214 ? 0.1185 0.1280 0.1307 0.0175  -0.0121 0.0114  215 PRO A CA  
1751 C  CA  B PRO A 214 ? 0.1226 0.1316 0.1324 0.0164  -0.0119 0.0102  215 PRO A CA  
1752 C  C   A PRO A 214 ? 0.1138 0.1309 0.1614 -0.0185 -0.0216 -0.0118 215 PRO A C   
1753 C  C   B PRO A 214 ? 0.1176 0.1322 0.1624 -0.0186 -0.0208 -0.0126 215 PRO A C   
1754 O  O   A PRO A 214 ? 0.1428 0.1668 0.1703 -0.0436 -0.0359 0.0175  215 PRO A O   
1755 O  O   B PRO A 214 ? 0.1474 0.1701 0.1724 -0.0417 -0.0353 0.0181  215 PRO A O   
1756 C  CB  A PRO A 214 ? 0.1192 0.1120 0.1756 0.0049  -0.0142 0.0031  215 PRO A CB  
1757 C  CB  B PRO A 214 ? 0.1264 0.1120 0.1803 0.0020  -0.0131 0.0046  215 PRO A CB  
1758 C  CG  A PRO A 214 ? 0.1898 0.1471 0.1932 -0.0208 0.0199  0.0015  215 PRO A CG  
1759 C  CG  B PRO A 214 ? 0.2311 0.2002 0.2202 0.0019  0.0109  -0.0114 215 PRO A CG  
1760 C  CD  A PRO A 214 ? 0.1023 0.0913 0.1776 -0.0211 0.0098  0.0148  215 PRO A CD  
1761 C  CD  B PRO A 214 ? 0.2085 0.1544 0.2214 0.0228  0.0167  0.0292  215 PRO A CD  
1762 N  N   . ILE A 215 ? 0.1321 0.1183 0.1345 0.0068  -0.0306 -0.0017 216 ILE A N   
1763 C  CA  . ILE A 215 ? 0.1464 0.1316 0.1536 0.0136  -0.0348 -0.0228 216 ILE A CA  
1764 C  C   . ILE A 215 ? 0.1169 0.1167 0.1467 -0.0003 -0.0186 -0.0152 216 ILE A C   
1765 O  O   . ILE A 215 ? 0.1259 0.1264 0.1920 -0.0038 -0.0285 -0.0233 216 ILE A O   
1766 C  CB  . ILE A 215 ? 0.1598 0.1259 0.1542 0.0258  -0.0320 -0.0148 216 ILE A CB  
1767 C  CG1 . ILE A 215 ? 0.1668 0.1474 0.1503 0.0181  -0.0307 0.0048  216 ILE A CG1 
1768 C  CG2 . ILE A 215 ? 0.1582 0.1550 0.2108 0.0258  -0.0208 -0.0219 216 ILE A CG2 
1769 C  CD1 . ILE A 215 ? 0.2107 0.1629 0.1799 0.0087  -0.0251 0.0038  216 ILE A CD1 
1770 N  N   . SER A 216 ? 0.1273 0.1298 0.1855 -0.0043 -0.0373 -0.0207 217 SER A N   
1771 C  CA  . SER A 216 ? 0.1532 0.1420 0.1607 -0.0071 -0.0164 -0.0269 217 SER A CA  
1772 C  C   . SER A 216 ? 0.1336 0.1313 0.1476 -0.0185 -0.0337 -0.0227 217 SER A C   
1773 O  O   . SER A 216 ? 0.1571 0.1571 0.1842 0.0148  -0.0472 -0.0098 217 SER A O   
1774 C  CB  . SER A 216 ? 0.2985 0.1316 0.1862 -0.0480 0.0270  -0.0189 217 SER A CB  
1775 O  OG  . SER A 216 ? 0.3054 0.2486 0.2365 -0.0513 -0.0247 -0.0148 217 SER A OG  
1776 N  N   . VAL A 217 ? 0.1516 0.1226 0.1501 -0.0274 -0.0197 -0.0307 218 VAL A N   
1777 C  CA  . VAL A 217 ? 0.1826 0.1048 0.1580 -0.0099 -0.0215 -0.0229 218 VAL A CA  
1778 C  C   . VAL A 217 ? 0.1647 0.1261 0.1596 -0.0153 -0.0333 -0.0153 218 VAL A C   
1779 O  O   . VAL A 217 ? 0.1914 0.1158 0.1701 -0.0192 -0.0472 -0.0099 218 VAL A O   
1780 C  CB  . VAL A 217 ? 0.1544 0.1005 0.2195 -0.0285 -0.0441 -0.0093 218 VAL A CB  
1781 C  CG1 . VAL A 217 ? 0.2004 0.1023 0.1902 -0.0243 -0.0366 -0.0129 218 VAL A CG1 
1782 C  CG2 . VAL A 217 ? 0.1489 0.1393 0.2569 -0.0137 -0.0434 -0.0148 218 VAL A CG2 
1783 N  N   . SER A 218 ? 0.1925 0.1111 0.1526 -0.0109 -0.0299 -0.0211 219 SER A N   
1784 C  CA  . SER A 218 ? 0.1843 0.1079 0.1729 -0.0160 -0.0231 -0.0271 219 SER A CA  
1785 C  C   . SER A 218 ? 0.1842 0.1151 0.1670 -0.0137 -0.0176 -0.0109 219 SER A C   
1786 O  O   . SER A 218 ? 0.1923 0.1165 0.1758 -0.0208 -0.0421 -0.0035 219 SER A O   
1787 C  CB  . SER A 218 ? 0.2119 0.1406 0.1607 -0.0057 -0.0155 -0.0099 219 SER A CB  
1788 O  OG  . SER A 218 ? 0.2245 0.1629 0.1810 -0.0159 -0.0315 -0.0137 219 SER A OG  
1789 N  N   A SER A 219 ? 0.1879 0.1108 0.1801 -0.0070 -0.0263 -0.0109 220 SER A N   
1790 N  N   B SER A 219 ? 0.1957 0.1070 0.1887 -0.0130 -0.0259 -0.0098 220 SER A N   
1791 C  CA  A SER A 219 ? 0.1975 0.1163 0.2105 0.0115  -0.0335 -0.0071 220 SER A CA  
1792 C  CA  B SER A 219 ? 0.2079 0.1111 0.2198 -0.0052 -0.0296 -0.0013 220 SER A CA  
1793 C  C   A SER A 219 ? 0.2211 0.1323 0.1959 -0.0073 -0.0280 -0.0242 220 SER A C   
1794 C  C   B SER A 219 ? 0.2151 0.1365 0.2081 0.0086  -0.0272 -0.0140 220 SER A C   
1795 O  O   A SER A 219 ? 0.2301 0.1324 0.2257 0.0160  -0.0137 0.0132  220 SER A O   
1796 O  O   B SER A 219 ? 0.2478 0.1053 0.2681 -0.0020 -0.0288 -0.0035 220 SER A O   
1797 C  CB  A SER A 219 ? 0.2777 0.1336 0.2619 0.0244  -0.0513 -0.0277 220 SER A CB  
1798 C  CB  B SER A 219 ? 0.2802 0.1215 0.2352 -0.0362 -0.0759 0.0115  220 SER A CB  
1799 O  OG  A SER A 219 ? 0.2392 0.1129 0.2308 0.0307  -0.0197 -0.0331 220 SER A OG  
1800 O  OG  B SER A 219 ? 0.3158 0.2013 0.2108 -0.0120 -0.0463 0.0308  220 SER A OG  
1801 N  N   . GLU A 220 ? 0.2207 0.1309 0.1835 0.0046  -0.0115 -0.0027 221 GLU A N   
1802 C  CA  . GLU A 220 ? 0.2444 0.1472 0.1968 -0.0175 -0.0288 -0.0074 221 GLU A CA  
1803 C  C   . GLU A 220 ? 0.2343 0.1488 0.1889 -0.0049 -0.0148 0.0093  221 GLU A C   
1804 O  O   . GLU A 220 ? 0.2302 0.1670 0.1846 0.0115  0.0131  -0.0104 221 GLU A O   
1805 C  CB  . GLU A 220 ? 0.2889 0.1783 0.2002 -0.0027 -0.0549 -0.0538 221 GLU A CB  
1806 C  CG  . GLU A 220 ? 0.3794 0.1968 0.2993 -0.0513 -0.0829 -0.0533 221 GLU A CG  
1807 C  CD  . GLU A 220 ? 0.3999 0.1807 0.3438 -0.0876 -0.0392 -0.0951 221 GLU A CD  
1808 O  OE1 . GLU A 220 ? 0.3234 0.1862 0.3137 -0.0768 -0.0155 -0.0562 221 GLU A OE1 
1809 O  OE2 . GLU A 220 ? 1.2287 0.3865 0.9207 -0.5342 0.3231  -0.3964 221 GLU A OE2 
1810 N  N   . GLN A 221 ? 0.2110 0.1206 0.1814 -0.0175 -0.0337 -0.0043 222 GLN A N   
1811 C  CA  . GLN A 221 ? 0.2105 0.1122 0.1920 -0.0406 -0.0200 -0.0041 222 GLN A CA  
1812 C  C   . GLN A 221 ? 0.1859 0.1282 0.1533 -0.0142 -0.0155 0.0082  222 GLN A C   
1813 O  O   . GLN A 221 ? 0.1925 0.1467 0.1641 -0.0163 -0.0102 0.0148  222 GLN A O   
1814 C  CB  . GLN A 221 ? 0.2178 0.1449 0.1415 -0.0225 -0.0469 -0.0109 222 GLN A CB  
1815 C  CG  . GLN A 221 ? 0.1918 0.1445 0.1624 -0.0324 -0.0474 -0.0073 222 GLN A CG  
1816 C  CD  . GLN A 221 ? 0.1800 0.1333 0.1585 -0.0381 -0.0443 -0.0060 222 GLN A CD  
1817 O  OE1 . GLN A 221 ? 0.1686 0.1277 0.1686 -0.0098 -0.0412 -0.0160 222 GLN A OE1 
1818 N  NE2 . GLN A 221 ? 0.1842 0.1336 0.1891 -0.0148 -0.0544 -0.0007 222 GLN A NE2 
1819 N  N   . VAL A 222 ? 0.1949 0.1254 0.1650 -0.0076 -0.0362 0.0060  223 VAL A N   
1820 C  CA  . VAL A 222 ? 0.1983 0.1553 0.1488 -0.0294 -0.0220 0.0082  223 VAL A CA  
1821 C  C   . VAL A 222 ? 0.2061 0.1336 0.1717 -0.0092 -0.0082 0.0104  223 VAL A C   
1822 O  O   . VAL A 222 ? 0.2031 0.1624 0.1894 -0.0372 -0.0215 0.0259  223 VAL A O   
1823 C  CB  . VAL A 222 ? 0.1997 0.2004 0.1762 -0.0082 -0.0240 0.0351  223 VAL A CB  
1824 C  CG1 . VAL A 222 ? 0.1819 0.2020 0.2462 -0.0361 -0.0344 0.0441  223 VAL A CG1 
1825 C  CG2 . VAL A 222 ? 0.2221 0.2250 0.2074 -0.0386 -0.0719 0.0205  223 VAL A CG2 
1826 N  N   . LEU A 223 ? 0.2046 0.1318 0.1931 -0.0137 -0.0012 0.0031  224 LEU A N   
1827 C  CA  . LEU A 223 ? 0.2523 0.1454 0.2198 -0.0392 0.0208  -0.0228 224 LEU A CA  
1828 C  C   . LEU A 223 ? 0.2338 0.1870 0.1826 -0.0153 0.0120  -0.0280 224 LEU A C   
1829 O  O   . LEU A 223 ? 0.2284 0.1817 0.2135 -0.0194 0.0142  -0.0175 224 LEU A O   
1830 C  CB  . LEU A 223 ? 0.3215 0.1645 0.2692 -0.0555 0.0142  -0.0353 224 LEU A CB  
1831 C  CG  . LEU A 223 ? 0.4204 0.2238 0.3319 -0.0020 0.0239  -0.0176 224 LEU A CG  
1832 C  CD1 . LEU A 223 ? 0.3862 0.2551 0.4915 -0.0362 0.0674  -0.0425 224 LEU A CD1 
1833 C  CD2 . LEU A 223 ? 0.3913 0.2917 0.4199 -0.0170 -0.0873 -0.0882 224 LEU A CD2 
1834 N  N   . LYS A 224 ? 0.2074 0.1649 0.1686 -0.0132 -0.0109 -0.0093 225 LYS A N   
1835 C  CA  . LYS A 224 ? 0.2049 0.1745 0.2052 -0.0159 -0.0114 0.0020  225 LYS A CA  
1836 C  C   . LYS A 224 ? 0.2006 0.1580 0.1438 -0.0115 0.0003  0.0366  225 LYS A C   
1837 O  O   . LYS A 224 ? 0.2413 0.1652 0.1421 -0.0137 0.0065  0.0000  225 LYS A O   
1838 C  CB  . LYS A 224 ? 0.2159 0.2583 0.1932 -0.0098 -0.0410 0.0399  225 LYS A CB  
1839 C  CG  . LYS A 224 ? 0.2896 0.3924 0.2302 -0.0768 -0.0819 -0.0129 225 LYS A CG  
1840 C  CD  . LYS A 224 ? 0.4473 0.2049 0.3603 0.0037  -0.0719 -0.0658 225 LYS A CD  
1841 C  CE  . LYS A 224 ? 0.4832 0.4771 0.4710 -0.1439 -0.0688 -0.1995 225 LYS A CE  
1842 N  NZ  . LYS A 224 ? 0.5037 0.3750 0.5526 -0.0432 0.0666  -0.1439 225 LYS A NZ  
1843 N  N   . PHE A 225 ? 0.2046 0.1503 0.1391 -0.0120 -0.0059 0.0073  226 PHE A N   
1844 C  CA  . PHE A 225 ? 0.1850 0.1377 0.1421 -0.0211 0.0104  0.0010  226 PHE A CA  
1845 C  C   . PHE A 225 ? 0.1889 0.1534 0.1298 -0.0155 0.0115  0.0043  226 PHE A C   
1846 O  O   . PHE A 225 ? 0.2283 0.1464 0.1490 -0.0331 0.0237  -0.0093 226 PHE A O   
1847 C  CB  . PHE A 225 ? 0.2110 0.1351 0.1508 -0.0198 0.0176  -0.0070 226 PHE A CB  
1848 C  CG  . PHE A 225 ? 0.1914 0.1571 0.1421 -0.0491 0.0010  -0.0115 226 PHE A CG  
1849 C  CD1 . PHE A 225 ? 0.2544 0.1952 0.1761 0.0124  0.0024  0.0082  226 PHE A CD1 
1850 C  CD2 . PHE A 225 ? 0.2026 0.2212 0.1670 -0.0270 0.0167  -0.0384 226 PHE A CD2 
1851 C  CE1 . PHE A 225 ? 0.2809 0.2169 0.1912 0.0264  0.0377  0.0280  226 PHE A CE1 
1852 C  CE2 . PHE A 225 ? 0.2144 0.2291 0.1983 -0.0225 0.0007  -0.0679 226 PHE A CE2 
1853 C  CZ  . PHE A 225 ? 0.2222 0.1720 0.2085 -0.0405 -0.0164 -0.0362 226 PHE A CZ  
1854 N  N   . ARG A 226 ? 0.1941 0.1370 0.1429 0.0038  -0.0006 -0.0020 227 ARG A N   
1855 C  CA  . ARG A 226 ? 0.1993 0.1559 0.1271 -0.0154 0.0030  -0.0126 227 ARG A CA  
1856 C  C   . ARG A 226 ? 0.2249 0.1397 0.1846 -0.0281 0.0092  -0.0005 227 ARG A C   
1857 O  O   . ARG A 226 ? 0.2345 0.1694 0.1914 0.0000  0.0110  -0.0104 227 ARG A O   
1858 C  CB  . ARG A 226 ? 0.2316 0.1333 0.1392 -0.0200 0.0015  0.0040  227 ARG A CB  
1859 C  CG  . ARG A 226 ? 0.1887 0.1542 0.1379 -0.0118 -0.0043 -0.0051 227 ARG A CG  
1860 C  CD  . ARG A 226 ? 0.2465 0.1372 0.1677 -0.0153 0.0000  0.0155  227 ARG A CD  
1861 N  NE  . ARG A 226 ? 0.2056 0.1333 0.1624 -0.0384 -0.0120 -0.0073 227 ARG A NE  
1862 C  CZ  . ARG A 226 ? 0.2245 0.1424 0.1580 -0.0491 -0.0104 -0.0238 227 ARG A CZ  
1863 N  NH1 . ARG A 226 ? 0.2583 0.1720 0.2867 -0.0667 -0.0432 -0.0634 227 ARG A NH1 
1864 N  NH2 . ARG A 226 ? 0.2623 0.1518 0.1534 -0.0601 0.0175  -0.0003 227 ARG A NH2 
1865 N  N   . LYS A 227 ? 0.2201 0.1532 0.1203 -0.0315 0.0015  -0.0184 228 LYS A N   
1866 C  CA  . LYS A 227 ? 0.2425 0.1824 0.1381 -0.0381 0.0231  -0.0302 228 LYS A CA  
1867 C  C   . LYS A 227 ? 0.2124 0.1688 0.1342 -0.0214 0.0165  -0.0205 228 LYS A C   
1868 O  O   . LYS A 227 ? 0.2885 0.1902 0.1421 -0.0542 0.0318  -0.0239 228 LYS A O   
1869 C  CB  . LYS A 227 ? 0.2662 0.2425 0.1460 -0.0689 -0.0135 -0.0276 228 LYS A CB  
1870 C  CG  . LYS A 227 ? 0.3104 0.2613 0.1916 -0.0943 0.0204  -0.0375 228 LYS A CG  
1871 C  CD  . LYS A 227 ? 0.4056 0.4340 0.2547 -0.1679 -0.0287 -0.0357 228 LYS A CD  
1872 N  N   . LEU A 228 ? 0.2266 0.1667 0.1451 -0.0348 0.0059  -0.0236 229 LEU A N   
1873 C  CA  . LEU A 228 ? 0.2153 0.1789 0.1421 -0.0386 0.0043  -0.0163 229 LEU A CA  
1874 C  C   . LEU A 228 ? 0.2784 0.1614 0.1019 -0.0175 0.0229  -0.0296 229 LEU A C   
1875 O  O   . LEU A 228 ? 0.2240 0.1701 0.1343 -0.0129 0.0271  -0.0057 229 LEU A O   
1876 C  CB  . LEU A 228 ? 0.2372 0.1695 0.1062 -0.0386 0.0170  -0.0185 229 LEU A CB  
1877 C  CG  . LEU A 228 ? 0.2238 0.2108 0.1221 -0.0262 0.0143  -0.0086 229 LEU A CG  
1878 C  CD1 . LEU A 228 ? 0.2609 0.1828 0.1313 -0.0346 0.0142  -0.0231 229 LEU A CD1 
1879 C  CD2 . LEU A 228 ? 0.3051 0.1826 0.1437 0.0003  0.0362  0.0230  229 LEU A CD2 
1880 N  N   . ASN A 229 ? 0.2383 0.1885 0.1368 -0.0581 0.0148  -0.0195 230 ASN A N   
1881 C  CA  . ASN A 229 ? 0.2526 0.1627 0.1164 -0.0252 0.0043  -0.0102 230 ASN A CA  
1882 C  C   . ASN A 229 ? 0.2404 0.1961 0.1192 -0.0043 0.0188  0.0104  230 ASN A C   
1883 O  O   . ASN A 229 ? 0.2565 0.1800 0.1560 -0.0320 0.0175  -0.0071 230 ASN A O   
1884 C  CB  . ASN A 229 ? 0.2641 0.2098 0.1289 -0.0351 0.0318  -0.0182 230 ASN A CB  
1885 C  CG  . ASN A 229 ? 0.3072 0.2092 0.1206 -0.0377 0.0233  -0.0231 230 ASN A CG  
1886 O  OD1 . ASN A 229 ? 0.3844 0.2368 0.1500 -0.0241 0.0515  -0.0423 230 ASN A OD1 
1887 N  ND2 . ASN A 229 ? 0.2784 0.1903 0.1621 -0.0370 0.0306  -0.0406 230 ASN A ND2 
1888 N  N   . PHE A 230 ? 0.2085 0.1798 0.1560 -0.0595 0.0478  -0.0165 231 PHE A N   
1889 C  CA  . PHE A 230 ? 0.2264 0.1473 0.1648 -0.0452 -0.0038 0.0197  231 PHE A CA  
1890 C  C   . PHE A 230 ? 0.2284 0.1920 0.1720 -0.0428 0.0340  0.0060  231 PHE A C   
1891 O  O   . PHE A 230 ? 0.2889 0.2065 0.1756 -0.0983 0.0285  0.0031  231 PHE A O   
1892 C  CB  . PHE A 230 ? 0.2124 0.1650 0.1676 -0.0414 0.0447  -0.0120 231 PHE A CB  
1893 C  CG  . PHE A 230 ? 0.2264 0.1699 0.1629 -0.0373 0.0098  -0.0142 231 PHE A CG  
1894 C  CD1 . PHE A 230 ? 0.2184 0.1976 0.1305 -0.0438 0.0151  -0.0362 231 PHE A CD1 
1895 C  CD2 . PHE A 230 ? 0.1984 0.1952 0.1288 0.0161  0.0074  -0.0142 231 PHE A CD2 
1896 C  CE1 . PHE A 230 ? 0.2325 0.1738 0.1659 -0.0461 0.0189  -0.0219 231 PHE A CE1 
1897 C  CE2 . PHE A 230 ? 0.2134 0.1916 0.1532 -0.0259 0.0125  -0.0142 231 PHE A CE2 
1898 C  CZ  . PHE A 230 ? 0.1875 0.2019 0.1377 -0.0361 0.0074  -0.0027 231 PHE A CZ  
1899 N  N   . ASN A 231 ? 0.2058 0.2309 0.1546 -0.0500 0.0405  -0.0164 232 ASN A N   
1900 C  CA  . ASN A 231 ? 0.2169 0.2144 0.2220 -0.0284 0.0428  0.0153  232 ASN A CA  
1901 C  C   . ASN A 231 ? 0.1821 0.2655 0.1269 0.0353  0.0135  -0.0091 232 ASN A C   
1902 O  O   . ASN A 231 ? 0.2562 0.2422 0.1650 -0.0274 0.0340  0.0000  232 ASN A O   
1903 C  CB  . ASN A 231 ? 0.1948 0.2512 0.2225 -0.0140 0.0581  0.0107  232 ASN A CB  
1904 C  CG  . ASN A 231 ? 0.2374 0.2336 0.1764 -0.0109 0.0346  0.0074  232 ASN A CG  
1905 O  OD1 . ASN A 231 ? 0.3342 0.2349 0.1889 -0.0373 0.0854  -0.0230 232 ASN A OD1 
1906 N  ND2 . ASN A 231 ? 0.3672 0.2985 0.1526 0.0174  0.0680  -0.0026 232 ASN A ND2 
1907 N  N   . GLY A 232 ? 0.2562 0.2389 0.1880 -0.0104 0.0384  0.0307  233 GLY A N   
1908 C  CA  . GLY A 232 ? 0.2630 0.2864 0.1659 0.0454  0.0584  0.0238  233 GLY A CA  
1909 C  C   . GLY A 232 ? 0.1844 0.2090 0.2171 0.0390  -0.0233 0.0124  233 GLY A C   
1910 O  O   . GLY A 232 ? 0.2648 0.2953 0.1950 0.0542  0.0878  0.0584  233 GLY A O   
1911 N  N   . GLU A 233 ? 0.2249 0.2899 0.1817 -0.0041 0.0197  0.0187  234 GLU A N   
1912 C  CA  . GLU A 233 ? 0.1940 0.2469 0.2101 0.0285  0.0030  -0.0147 234 GLU A CA  
1913 C  C   . GLU A 233 ? 0.2474 0.2912 0.2010 0.0074  0.0264  0.0046  234 GLU A C   
1914 O  O   . GLU A 233 ? 0.3539 0.3511 0.1726 -0.0463 0.0364  0.0228  234 GLU A O   
1915 C  CB  . GLU A 233 ? 0.2605 0.2336 0.1986 0.0137  -0.0225 0.0331  234 GLU A CB  
1916 C  CG  . GLU A 233 ? 0.3155 0.3105 0.2002 -0.0935 0.0373  0.0229  234 GLU A CG  
1917 C  CD  . GLU A 233 ? 0.4386 0.4749 0.2541 0.1137  0.0745  -0.0366 234 GLU A CD  
1918 O  OE1 . GLU A 233 ? 0.3457 0.3625 0.2950 -0.0329 0.0702  0.0535  234 GLU A OE1 
1919 O  OE2 . GLU A 233 ? 0.4462 0.4300 0.2684 0.0204  0.0093  -0.0131 234 GLU A OE2 
1920 N  N   . GLY A 234 ? 0.3679 0.3476 0.1817 0.0348  0.0763  -0.0329 235 GLY A N   
1921 C  CA  . GLY A 234 ? 0.3616 0.4031 0.2347 0.0979  0.0175  -0.0291 235 GLY A CA  
1922 C  C   . GLY A 234 ? 0.3248 0.4559 0.1806 0.0634  0.0538  0.0228  235 GLY A C   
1923 O  O   . GLY A 234 ? 0.4117 0.6474 0.2219 0.0982  0.1211  0.0834  235 GLY A O   
1924 N  N   . GLU A 235 ? 0.3122 0.3392 0.2397 0.0434  0.0758  0.0172  236 GLU A N   
1925 C  CA  . GLU A 235 ? 0.3180 0.2687 0.2349 0.1008  0.0493  0.0675  236 GLU A CA  
1926 C  C   . GLU A 235 ? 0.4057 0.4386 0.2058 0.0197  0.1215  0.0886  236 GLU A C   
1927 O  O   . GLU A 235 ? 0.3791 0.3956 0.2609 0.0511  0.1483  0.0272  236 GLU A O   
1928 C  CB  . GLU A 235 ? 0.3198 0.3550 0.2320 0.0337  0.0909  0.0631  236 GLU A CB  
1929 C  CG  . GLU A 235 ? 0.4315 0.3826 0.2480 -0.0586 0.1427  0.0164  236 GLU A CG  
1930 C  CD  . GLU A 235 ? 0.4616 0.6549 0.2735 -0.1661 0.1675  -0.0982 236 GLU A CD  
1931 O  OE1 . GLU A 235 ? 0.3855 0.4879 0.3794 -0.0838 0.1843  -0.0197 236 GLU A OE1 
1932 O  OE2 . GLU A 235 ? 0.6424 0.6171 0.7286 -0.2135 0.2145  0.1893  236 GLU A OE2 
1933 N  N   . PRO A 236 ? 0.3245 0.4156 0.2742 0.0780  0.1377  0.1307  237 PRO A N   
1934 C  CA  . PRO A 236 ? 0.3791 0.4885 0.3072 0.0269  0.1492  0.1208  237 PRO A CA  
1935 C  C   . PRO A 236 ? 0.3374 0.3823 0.1683 -0.0392 0.0768  0.0454  237 PRO A C   
1936 O  O   . PRO A 236 ? 0.3118 0.3503 0.2108 -0.0171 0.0943  0.0093  237 PRO A O   
1937 C  CB  . PRO A 236 ? 0.3661 0.6376 0.3901 0.0452  0.2017  0.1314  237 PRO A CB  
1938 C  CG  . PRO A 236 ? 0.2888 0.4642 0.4580 0.1279  0.0865  0.2319  237 PRO A CG  
1939 C  CD  . PRO A 236 ? 0.2835 0.4860 0.3725 0.1176  0.0904  0.1105  237 PRO A CD  
1940 N  N   . GLU A 237 ? 0.3776 0.3460 0.2194 -0.0031 0.1151  -0.0649 238 GLU A N   
1941 C  CA  . GLU A 237 ? 0.3388 0.3241 0.1767 -0.0493 0.0732  -0.0450 238 GLU A CA  
1942 C  C   . GLU A 237 ? 0.2928 0.2554 0.2302 -0.0430 0.0601  -0.0346 238 GLU A C   
1943 O  O   . GLU A 237 ? 0.2259 0.2669 0.1940 -0.0052 0.0294  -0.0397 238 GLU A O   
1944 C  CB  . GLU A 237 ? 0.3549 0.3585 0.2475 0.0307  -0.0310 -0.0895 238 GLU A CB  
1945 C  CG  . GLU A 237 ? 0.3949 0.2763 0.3337 -0.0588 -0.0163 -0.0855 238 GLU A CG  
1946 C  CD  . GLU A 237 ? 0.3363 0.2752 0.2648 0.0115  -0.0185 -0.1045 238 GLU A CD  
1947 O  OE1 . GLU A 237 ? 0.5271 0.4666 0.5325 0.0992  -0.1133 -0.3059 238 GLU A OE1 
1948 O  OE2 . GLU A 237 ? 0.3507 0.2613 0.2363 0.0262  -0.0120 -0.0869 238 GLU A OE2 
1949 N  N   . GLU A 238 ? 0.2342 0.2476 0.1606 -0.0700 0.0515  -0.0399 239 GLU A N   
1950 C  CA  . GLU A 238 ? 0.2006 0.2791 0.1509 -0.0640 0.0461  -0.0181 239 GLU A CA  
1951 C  C   . GLU A 238 ? 0.1752 0.2137 0.1424 -0.0317 0.0372  -0.0142 239 GLU A C   
1952 O  O   . GLU A 238 ? 0.2867 0.2002 0.2143 -0.0386 0.0557  -0.0322 239 GLU A O   
1953 C  CB  . GLU A 238 ? 0.2583 0.3173 0.2584 -0.1277 0.0421  -0.0687 239 GLU A CB  
1954 C  CG  . GLU A 238 ? 0.5558 0.6973 0.4225 0.0807  -0.1014 0.0068  239 GLU A CG  
1955 N  N   . LEU A 239 ? 0.2169 0.2140 0.1363 -0.0230 0.0287  -0.0302 240 LEU A N   
1956 C  CA  . LEU A 239 ? 0.1598 0.1871 0.1471 -0.0292 0.0348  -0.0275 240 LEU A CA  
1957 C  C   . LEU A 239 ? 0.1993 0.1603 0.1307 -0.0476 0.0225  0.0031  240 LEU A C   
1958 O  O   . LEU A 239 ? 0.2002 0.1889 0.1501 -0.0211 0.0412  -0.0286 240 LEU A O   
1959 C  CB  . LEU A 239 ? 0.2020 0.1749 0.1738 -0.0164 0.0164  -0.0104 240 LEU A CB  
1960 C  CG  . LEU A 239 ? 0.1920 0.1702 0.2248 -0.0164 -0.0219 -0.0414 240 LEU A CG  
1961 C  CD1 . LEU A 239 ? 0.2929 0.1455 0.3201 0.0093  -0.0232 -0.0427 240 LEU A CD1 
1962 C  CD2 . LEU A 239 ? 0.2128 0.2049 0.1853 0.0295  -0.0164 -0.0348 240 LEU A CD2 
1963 N  N   . MET A 240 ? 0.2010 0.1652 0.1388 -0.0193 0.0412  -0.0143 241 MET A N   
1964 C  CA  . MET A 240 ? 0.2223 0.1749 0.1375 -0.0088 0.0513  -0.0159 241 MET A CA  
1965 C  C   . MET A 240 ? 0.1703 0.1640 0.1226 -0.0331 0.0098  -0.0346 241 MET A C   
1966 O  O   . MET A 240 ? 0.1815 0.1694 0.1246 -0.0295 0.0183  -0.0155 241 MET A O   
1967 C  CB  . MET A 240 ? 0.2088 0.1573 0.1641 0.0063  0.0198  -0.0131 241 MET A CB  
1968 C  CG  . MET A 240 ? 0.2207 0.2097 0.1237 -0.0272 0.0482  -0.0237 241 MET A CG  
1969 S  SD  . MET A 240 ? 0.2442 0.1492 0.1580 -0.0251 0.0287  -0.0043 241 MET A SD  
1970 C  CE  . MET A 240 ? 0.2863 0.1455 0.1853 -0.0461 0.0595  0.0120  241 MET A CE  
1971 N  N   . VAL A 241 ? 0.1877 0.1481 0.1201 -0.0155 0.0217  -0.0214 242 VAL A N   
1972 C  CA  . VAL A 241 ? 0.1636 0.1316 0.1226 -0.0087 0.0226  -0.0046 242 VAL A CA  
1973 C  C   . VAL A 241 ? 0.1588 0.1303 0.1251 -0.0031 0.0119  -0.0165 242 VAL A C   
1974 O  O   . VAL A 241 ? 0.1469 0.1499 0.1330 -0.0194 0.0280  -0.0186 242 VAL A O   
1975 C  CB  . VAL A 241 ? 0.1620 0.1307 0.1560 -0.0146 0.0172  -0.0255 242 VAL A CB  
1976 C  CG1 . VAL A 241 ? 0.2207 0.1659 0.1624 -0.0377 0.0126  -0.0372 242 VAL A CG1 
1977 C  CG2 . VAL A 241 ? 0.2035 0.1638 0.1483 -0.0040 0.0333  -0.0326 242 VAL A CG2 
1978 N  N   . ASP A 242 ? 0.1670 0.1196 0.1086 -0.0071 0.0165  -0.0120 243 ASP A N   
1979 C  CA  . ASP A 242 ? 0.1467 0.1316 0.1196 -0.0034 0.0146  -0.0264 243 ASP A CA  
1980 C  C   . ASP A 242 ? 0.1352 0.1341 0.1099 -0.0228 0.0148  -0.0104 243 ASP A C   
1981 O  O   . ASP A 242 ? 0.1510 0.1354 0.1655 -0.0153 0.0086  -0.0216 243 ASP A O   
1982 C  CB  . ASP A 242 ? 0.1634 0.1360 0.1439 -0.0210 0.0099  0.0000  243 ASP A CB  
1983 C  CG  . ASP A 242 ? 0.1397 0.1360 0.1546 -0.0074 0.0172  -0.0226 243 ASP A CG  
1984 O  OD1 . ASP A 242 ? 0.1370 0.1225 0.1589 0.0065  0.0154  -0.0093 243 ASP A OD1 
1985 O  OD2 . ASP A 242 ? 0.1615 0.1562 0.1835 0.0043  0.0217  -0.0271 243 ASP A OD2 
1986 N  N   . ASN A 243 ? 0.1316 0.1127 0.1297 -0.0093 0.0173  -0.0183 244 ASN A N   
1987 C  CA  . ASN A 243 ? 0.1503 0.1049 0.1278 -0.0126 0.0141  -0.0163 244 ASN A CA  
1988 C  C   . ASN A 243 ? 0.1352 0.1181 0.1005 -0.0232 0.0046  -0.0063 244 ASN A C   
1989 O  O   . ASN A 243 ? 0.1560 0.1313 0.1273 0.0077  0.0121  -0.0087 244 ASN A O   
1990 C  CB  . ASN A 243 ? 0.1604 0.1403 0.1163 -0.0322 0.0076  0.0043  244 ASN A CB  
1991 C  CG  . ASN A 243 ? 0.1570 0.1324 0.1260 -0.0452 0.0136  -0.0104 244 ASN A CG  
1992 O  OD1 . ASN A 243 ? 0.1471 0.1273 0.1634 -0.0185 0.0126  0.0057  244 ASN A OD1 
1993 N  ND2 . ASN A 243 ? 0.1916 0.1885 0.1941 -0.0527 -0.0253 0.0542  244 ASN A ND2 
1994 N  N   . TRP A 244 ? 0.1133 0.1176 0.1196 -0.0065 -0.0043 -0.0109 245 TRP A N   
1995 C  CA  . TRP A 244 ? 0.0935 0.1263 0.1122 -0.0054 0.0020  -0.0153 245 TRP A CA  
1996 C  C   . TRP A 244 ? 0.1058 0.1303 0.1158 -0.0041 0.0049  0.0000  245 TRP A C   
1997 O  O   . TRP A 244 ? 0.1199 0.1298 0.1456 0.0109  -0.0043 -0.0209 245 TRP A O   
1998 C  CB  . TRP A 244 ? 0.1142 0.1120 0.1372 -0.0052 0.0120  -0.0020 245 TRP A CB  
1999 C  CG  . TRP A 244 ? 0.1005 0.1259 0.1330 0.0060  0.0093  -0.0019 245 TRP A CG  
2000 C  CD1 . TRP A 244 ? 0.1053 0.1246 0.1221 -0.0060 0.0241  -0.0060 245 TRP A CD1 
2001 C  CD2 . TRP A 244 ? 0.1001 0.1224 0.1181 -0.0049 0.0124  -0.0080 245 TRP A CD2 
2002 N  NE1 . TRP A 244 ? 0.1203 0.1124 0.1351 -0.0031 0.0031  0.0019  245 TRP A NE1 
2003 C  CE2 . TRP A 244 ? 0.1361 0.1131 0.1404 -0.0020 0.0080  0.0000  245 TRP A CE2 
2004 C  CE3 . TRP A 244 ? 0.1172 0.1498 0.1196 0.0034  -0.0015 0.0000  245 TRP A CE3 
2005 C  CZ2 . TRP A 244 ? 0.1582 0.1263 0.1476 0.0236  0.0063  -0.0049 245 TRP A CZ2 
2006 C  CZ3 . TRP A 244 ? 0.1436 0.1481 0.1677 0.0244  -0.0057 0.0024  245 TRP A CZ3 
2007 C  CH2 . TRP A 244 ? 0.1491 0.1509 0.1691 0.0164  0.0216  0.0082  245 TRP A CH2 
2008 N  N   . ARG A 245 ? 0.1086 0.1270 0.1138 0.0065  0.0027  -0.0175 246 ARG A N   
2009 C  CA  . ARG A 245 ? 0.1070 0.1363 0.1145 -0.0088 0.0026  -0.0046 246 ARG A CA  
2010 C  C   . ARG A 245 ? 0.0833 0.1467 0.1219 0.0108  -0.0065 -0.0261 246 ARG A C   
2011 O  O   . ARG A 245 ? 0.1102 0.1273 0.1394 -0.0020 0.0017  -0.0120 246 ARG A O   
2012 C  CB  . ARG A 245 ? 0.0917 0.1388 0.1318 -0.0107 -0.0017 -0.0241 246 ARG A CB  
2013 C  CG  . ARG A 245 ? 0.1113 0.1269 0.1296 -0.0027 -0.0027 -0.0071 246 ARG A CG  
2014 C  CD  . ARG A 245 ? 0.0843 0.1327 0.1521 -0.0080 -0.0070 -0.0238 246 ARG A CD  
2015 N  NE  . ARG A 245 ? 0.0865 0.1539 0.1562 -0.0109 -0.0041 -0.0228 246 ARG A NE  
2016 C  CZ  . ARG A 245 ? 0.0992 0.1367 0.1401 -0.0233 -0.0068 -0.0196 246 ARG A CZ  
2017 N  NH1 . ARG A 245 ? 0.1049 0.1453 0.1551 -0.0103 0.0013  -0.0206 246 ARG A NH1 
2018 N  NH2 . ARG A 245 ? 0.1104 0.1587 0.1853 -0.0183 -0.0092 -0.0142 246 ARG A NH2 
2019 N  N   A PRO A 246 ? 0.1023 0.1268 0.1312 0.0093  -0.0013 -0.0082 247 PRO A N   
2020 N  N   B PRO A 246 ? 0.1102 0.1282 0.1359 0.0131  -0.0040 -0.0086 247 PRO A N   
2021 C  CA  A PRO A 246 ? 0.1176 0.1544 0.1167 0.0085  -0.0082 0.0081  247 PRO A CA  
2022 C  CA  B PRO A 246 ? 0.1330 0.1647 0.1190 0.0104  -0.0077 0.0098  247 PRO A CA  
2023 C  C   A PRO A 246 ? 0.1129 0.1289 0.1142 0.0071  -0.0136 -0.0007 247 PRO A C   
2024 C  C   B PRO A 246 ? 0.1158 0.1336 0.1167 0.0074  -0.0142 0.0024  247 PRO A C   
2025 O  O   A PRO A 246 ? 0.1203 0.1219 0.1361 -0.0007 -0.0126 -0.0076 247 PRO A O   
2026 O  O   B PRO A 246 ? 0.1298 0.1289 0.1404 -0.0041 -0.0164 -0.0046 247 PRO A O   
2027 C  CB  A PRO A 246 ? 0.1722 0.1375 0.1589 0.0478  0.0104  0.0049  247 PRO A CB  
2028 C  CB  B PRO A 246 ? 0.1782 0.1586 0.1746 0.0373  0.0038  0.0024  247 PRO A CB  
2029 C  CG  A PRO A 246 ? 0.1368 0.1172 0.1518 0.0172  -0.0046 0.0131  247 PRO A CG  
2030 C  CG  B PRO A 246 ? 0.1974 0.1497 0.2343 0.0161  -0.0186 0.0154  247 PRO A CG  
2031 C  CD  A PRO A 246 ? 0.0992 0.0966 0.1603 0.0204  -0.0104 -0.0098 247 PRO A CD  
2032 C  CD  B PRO A 246 ? 0.1145 0.1974 0.1501 0.0472  -0.0020 -0.0097 247 PRO A CD  
2033 N  N   . ALA A 247 ? 0.1270 0.1542 0.1199 0.0142  -0.0024 0.0038  248 ALA A N   
2034 C  CA  . ALA A 247 ? 0.0908 0.1615 0.1314 0.0086  -0.0098 0.0054  248 ALA A CA  
2035 C  C   . ALA A 247 ? 0.1137 0.1412 0.1263 0.0195  -0.0057 0.0273  248 ALA A C   
2036 O  O   . ALA A 247 ? 0.1212 0.1625 0.1571 0.0410  -0.0232 0.0049  248 ALA A O   
2037 C  CB  . ALA A 247 ? 0.1710 0.1905 0.1305 0.0006  0.0209  0.0086  248 ALA A CB  
2038 N  N   . GLN A 248 ? 0.1264 0.1269 0.1221 0.0099  -0.0174 0.0048  249 GLN A N   
2039 C  CA  . GLN A 248 ? 0.1142 0.1392 0.1271 0.0109  -0.0254 0.0015  249 GLN A CA  
2040 C  C   . GLN A 248 ? 0.1137 0.1242 0.1474 0.0208  -0.0219 0.0132  249 GLN A C   
2041 O  O   . GLN A 248 ? 0.1385 0.1541 0.1377 0.0030  -0.0038 0.0115  249 GLN A O   
2042 C  CB  . GLN A 248 ? 0.1244 0.1315 0.1586 0.0046  -0.0350 -0.0031 249 GLN A CB  
2043 C  CG  . GLN A 248 ? 0.1359 0.1361 0.1392 -0.0098 -0.0170 0.0006  249 GLN A CG  
2044 C  CD  . GLN A 248 ? 0.1237 0.1968 0.1674 -0.0293 -0.0163 -0.0043 249 GLN A CD  
2045 O  OE1 . GLN A 248 ? 0.1469 0.2397 0.1889 -0.0533 -0.0015 -0.0286 249 GLN A OE1 
2046 N  NE2 . GLN A 248 ? 0.1616 0.1966 0.1377 0.0003  -0.0027 -0.0104 249 GLN A NE2 
2047 N  N   . PRO A 249 ? 0.1360 0.1864 0.1665 0.0417  -0.0357 -0.0121 250 PRO A N   
2048 C  CA  . PRO A 249 ? 0.1807 0.2144 0.1483 0.0737  -0.0416 -0.0093 250 PRO A CA  
2049 C  C   . PRO A 249 ? 0.1699 0.1536 0.1430 0.0447  -0.0313 0.0031  250 PRO A C   
2050 O  O   . PRO A 249 ? 0.1386 0.1699 0.1532 0.0405  -0.0288 0.0074  250 PRO A O   
2051 C  CB  . PRO A 249 ? 0.1555 0.2857 0.2108 0.0529  -0.0395 -0.0408 250 PRO A CB  
2052 C  CG  . PRO A 249 ? 0.1846 0.3629 0.1722 0.0161  -0.0595 -0.0395 250 PRO A CG  
2053 C  CD  . PRO A 249 ? 0.1014 0.2885 0.2128 0.0505  -0.0750 -0.0035 250 PRO A CD  
2054 N  N   . LEU A 250 ? 0.1656 0.1867 0.1413 0.0555  -0.0274 0.0175  251 LEU A N   
2055 C  CA  . LEU A 250 ? 0.1631 0.1518 0.1383 0.0137  -0.0153 0.0087  251 LEU A CA  
2056 C  C   . LEU A 250 ? 0.1347 0.1542 0.1492 0.0208  -0.0252 0.0259  251 LEU A C   
2057 O  O   . LEU A 250 ? 0.1445 0.1553 0.1673 0.0203  -0.0452 0.0006  251 LEU A O   
2058 C  CB  . LEU A 250 ? 0.1893 0.1704 0.1878 0.0186  0.0200  0.0126  251 LEU A CB  
2059 C  CG  . LEU A 250 ? 0.2022 0.1837 0.1419 -0.0206 0.0208  0.0000  251 LEU A CG  
2060 C  CD1 . LEU A 250 ? 0.1913 0.1923 0.1903 0.0057  -0.0366 -0.0154 251 LEU A CD1 
2061 C  CD2 . LEU A 250 ? 0.2555 0.2011 0.2090 -0.0399 0.0251  -0.0275 251 LEU A CD2 
2062 N  N   . LYS A 251 ? 0.1758 0.1939 0.1562 0.0368  -0.0625 0.0057  252 LYS A N   
2063 C  CA  . LYS A 251 ? 0.1647 0.2221 0.1542 0.0333  -0.0511 -0.0230 252 LYS A CA  
2064 C  C   . LYS A 251 ? 0.1641 0.1869 0.2325 0.0148  -0.0573 0.0143  252 LYS A C   
2065 O  O   . LYS A 251 ? 0.2035 0.2623 0.1961 -0.0153 -0.0024 -0.0187 252 LYS A O   
2066 C  CB  . LYS A 251 ? 0.2222 0.2363 0.2122 -0.0057 -0.0538 -0.0247 252 LYS A CB  
2067 C  CG  . LYS A 251 ? 0.2651 0.2870 0.2281 -0.0046 0.0318  -0.0384 252 LYS A CG  
2068 C  CD  . LYS A 251 ? 0.2921 0.2698 0.3341 0.0063  0.0381  -0.0394 252 LYS A CD  
2069 C  CE  . LYS A 251 ? 0.2842 0.3888 0.3859 0.0253  0.0675  -0.1045 252 LYS A CE  
2070 N  NZ  . LYS A 251 ? 0.2868 0.4458 0.4986 0.0755  0.0070  0.1133  252 LYS A NZ  
2071 N  N   . ASN A 252 ? 0.2352 0.1914 0.1446 0.0291  -0.0368 -0.0207 253 ASN A N   
2072 C  CA  . ASN A 252 ? 0.2284 0.4685 0.1781 0.0194  -0.0557 -0.0619 253 ASN A CA  
2073 C  C   . ASN A 252 ? 0.2659 0.3335 0.3179 0.0794  -0.0661 -0.0544 253 ASN A C   
2074 O  O   . ASN A 252 ? 0.2720 0.3410 0.2831 0.0505  0.0000  -0.0174 253 ASN A O   
2075 C  CB  . ASN A 252 ? 0.3316 0.4555 0.2875 -0.0163 -0.1106 -0.0816 253 ASN A CB  
2076 C  CG  . ASN A 252 ? 0.4585 0.4128 0.3248 0.0284  -0.1181 -0.0436 253 ASN A CG  
2077 O  OD1 . ASN A 252 ? 0.9473 0.7069 0.4682 -0.2569 0.0983  0.1523  253 ASN A OD1 
2078 N  ND2 . ASN A 252 ? 0.6409 0.3511 0.8651 -0.0333 0.0965  -0.1967 253 ASN A ND2 
2079 N  N   . ARG A 253 ? 0.1712 0.3111 0.1500 0.0443  -0.0037 0.0414  254 ARG A N   
2080 C  CA  . ARG A 253 ? 0.1469 0.1867 0.1242 0.0296  -0.0109 0.0010  254 ARG A CA  
2081 C  C   . ARG A 253 ? 0.2222 0.1536 0.1424 0.0430  0.0109  -0.0027 254 ARG A C   
2082 O  O   . ARG A 253 ? 0.2716 0.2010 0.3244 0.0693  0.1199  0.0744  254 ARG A O   
2083 C  CB  . ARG A 253 ? 0.1494 0.1728 0.1176 0.0219  0.0000  -0.0017 254 ARG A CB  
2084 C  CG  . ARG A 253 ? 0.1699 0.1463 0.1201 0.0166  0.0048  -0.0020 254 ARG A CG  
2085 C  CD  . ARG A 253 ? 0.1607 0.1397 0.1167 0.0153  0.0082  -0.0082 254 ARG A CD  
2086 N  NE  . ARG A 253 ? 0.1032 0.1476 0.1178 0.0071  -0.0143 -0.0043 254 ARG A NE  
2087 C  CZ  . ARG A 253 ? 0.1058 0.1303 0.1058 -0.0054 -0.0076 0.0013  254 ARG A CZ  
2088 N  NH1 . ARG A 253 ? 0.0978 0.1307 0.1280 0.0015  -0.0210 0.0000  254 ARG A NH1 
2089 N  NH2 . ARG A 253 ? 0.1151 0.1360 0.1243 0.0166  -0.0206 -0.0020 254 ARG A NH2 
2090 N  N   . GLN A 254 ? 0.1623 0.1921 0.1361 0.0175  -0.0093 -0.0410 255 GLN A N   
2091 C  CA  . GLN A 254 ? 0.1943 0.2072 0.1526 0.0294  -0.0104 -0.0328 255 GLN A CA  
2092 C  C   . GLN A 254 ? 0.1670 0.1825 0.1738 0.0098  -0.0340 -0.0109 255 GLN A C   
2093 O  O   . GLN A 254 ? 0.2615 0.1713 0.2494 0.0035  -0.0815 -0.0035 255 GLN A O   
2094 C  CB  . GLN A 254 ? 0.2257 0.3664 0.1557 -0.0502 0.0103  -0.0821 255 GLN A CB  
2095 C  CG  . GLN A 254 ? 0.4246 0.4250 0.2056 0.0326  0.0566  -0.0109 255 GLN A CG  
2096 N  N   . ILE A 255 ? 0.1577 0.1692 0.1424 0.0005  -0.0109 -0.0013 256 ILE A N   
2097 C  CA  . ILE A 255 ? 0.1492 0.1643 0.1277 0.0088  -0.0035 0.0035  256 ILE A CA  
2098 C  C   . ILE A 255 ? 0.1585 0.1664 0.1239 0.0082  0.0249  0.0249  256 ILE A C   
2099 O  O   . ILE A 255 ? 0.1719 0.1738 0.1589 0.0287  0.0200  0.0379  256 ILE A O   
2100 C  CB  . ILE A 255 ? 0.1717 0.1462 0.1368 0.0115  0.0057  0.0041  256 ILE A CB  
2101 C  CG1 . ILE A 255 ? 0.1528 0.1508 0.1591 0.0131  0.0164  -0.0163 256 ILE A CG1 
2102 C  CG2 . ILE A 255 ? 0.1494 0.2052 0.1537 0.0024  -0.0073 0.0051  256 ILE A CG2 
2103 C  CD1 . ILE A 255 ? 0.1746 0.1840 0.1670 -0.0046 0.0186  -0.0236 256 ILE A CD1 
2104 N  N   . LYS A 256 ? 0.1279 0.1659 0.1185 0.0035  -0.0035 0.0148  257 LYS A N   
2105 C  CA  . LYS A 256 ? 0.1348 0.1764 0.1246 -0.0098 0.0093  0.0270  257 LYS A CA  
2106 C  C   . LYS A 256 ? 0.1404 0.1539 0.1072 0.0082  0.0000  0.0231  257 LYS A C   
2107 O  O   . LYS A 256 ? 0.1645 0.2090 0.1084 -0.0428 0.0109  0.0176  257 LYS A O   
2108 C  CB  . LYS A 256 ? 0.1395 0.1658 0.1674 0.0068  0.0076  -0.0130 257 LYS A CB  
2109 C  CG  . LYS A 256 ? 0.2368 0.2125 0.2257 -0.0103 0.0494  -0.0524 257 LYS A CG  
2110 N  N   . ALA A 257 ? 0.1404 0.1789 0.1272 0.0000  0.0288  0.0173  258 ALA A N   
2111 C  CA  . ALA A 257 ? 0.1503 0.1567 0.1519 0.0035  0.0082  0.0151  258 ALA A CA  
2112 C  C   . ALA A 257 ? 0.1291 0.1736 0.1260 -0.0170 0.0265  0.0080  258 ALA A C   
2113 O  O   . ALA A 257 ? 0.1451 0.1986 0.1391 -0.0035 0.0274  -0.0110 258 ALA A O   
2114 C  CB  . ALA A 257 ? 0.1586 0.1923 0.1923 -0.0109 0.0155  0.0082  258 ALA A CB  
2115 N  N   . SER A 258 ? 0.1413 0.1736 0.1386 -0.0052 0.0049  -0.0052 259 SER A N   
2116 C  CA  . SER A 258 ? 0.1406 0.1826 0.1817 0.0082  0.0164  -0.0120 259 SER A CA  
2117 C  C   . SER A 258 ? 0.1516 0.1979 0.1819 -0.0109 0.0285  -0.0019 259 SER A C   
2118 O  O   . SER A 258 ? 0.1703 0.2864 0.2401 0.0086  0.0428  -0.0043 259 SER A O   
2119 C  CB  . SER A 258 ? 0.1898 0.1835 0.1870 -0.0182 -0.0197 0.0087  259 SER A CB  
2120 O  OG  . SER A 258 ? 0.1359 0.2078 0.1625 -0.0063 0.0185  -0.0057 259 SER A OG  
2121 N  N   . PHE A 259 ? 0.1424 0.2203 0.1902 -0.0310 0.0408  0.0000  260 PHE A N   
2122 C  CA  . PHE A 259 ? 0.2110 0.2340 0.2087 -0.0697 0.0483  0.0276  260 PHE A CA  
2123 C  C   . PHE A 259 ? 0.2781 0.2968 0.2160 -0.0838 0.0487  0.0185  260 PHE A C   
2124 O  O   . PHE A 259 ? 0.3212 0.2508 0.2397 -0.0631 0.0043  0.0631  260 PHE A O   
2125 C  CB  . PHE A 259 ? 0.2090 0.2598 0.2298 -0.0579 0.0399  -0.0243 260 PHE A CB  
2126 C  CG  . PHE A 259 ? 0.1761 0.2125 0.2694 -0.0516 0.0031  0.0266  260 PHE A CG  
2127 C  CD1 . PHE A 259 ? 0.1623 0.2070 0.1870 -0.0460 -0.0076 -0.0076 260 PHE A CD1 
2128 C  CD2 . PHE A 259 ? 0.3125 0.2040 0.2372 -0.0229 0.0520  0.0175  260 PHE A CD2 
2129 C  CE1 . PHE A 259 ? 0.1458 0.2090 0.2512 -0.0340 -0.0097 0.0013  260 PHE A CE1 
2130 C  CE2 . PHE A 259 ? 0.2803 0.2558 0.3087 -0.0406 0.0164  0.0125  260 PHE A CE2 
2131 C  CZ  . PHE A 259 ? 0.2644 0.1950 0.2997 -0.0143 0.0242  -0.0231 260 PHE A CZ  
2132 N  N   . LYS A 260 ? 0.4886 0.4193 0.2702 -0.2381 0.0991  0.0516  261 LYS A N   
2133 C  CA  . LYS A 260 ? 0.7246 0.5224 0.3036 -0.1167 -0.0228 0.0961  261 LYS A CA  
2134 C  C   . LYS A 260 ? 0.6068 0.4523 0.4319 -0.0961 -0.0973 0.0851  261 LYS A C   
2135 O  O   . LYS A 260 ? 0.5835 0.4462 0.3457 -0.1142 -0.0080 0.0619  261 LYS A O   
2136 C  CB  . LYS A 260 ? 0.8176 0.4502 0.5253 -0.2413 0.0953  0.0054  261 LYS A CB  
2137 C  CG  . LYS A 260 ? 0.7357 0.4591 0.5755 -0.3122 0.2122  -0.1067 261 LYS A CG  
2138 C  CD  . LYS A 260 ? 0.8474 0.5974 0.6621 -0.1032 0.0487  -0.1254 261 LYS A CD  
2139 C  CE  . LYS A 260 ? 0.8313 0.6172 0.6169 -0.0196 0.2469  -0.0068 261 LYS A CE  
2140 N  NZ  . LYS A 260 ? 0.8615 0.7221 0.4821 0.0359  0.3025  0.0812  261 LYS A NZ  
2141 O  OXT . LYS A 260 ? 1.0693 1.0492 0.6032 -0.4616 0.2881  0.0982  261 LYS A OXT 
2142 ZN ZN  . ZN  B .   ? 0.1075 0.0988 0.1035 -0.0082 -0.0073 -0.0003 301 ZN  A ZN  
2143 O  O4  . VD9 C .   ? 0.1104 0.1115 0.1131 0.0012  -0.0136 -0.0043 302 VD9 A O4  
2144 S  S2  . VD9 C .   ? 0.1045 0.0992 0.1183 -0.0091 -0.0142 -0.0071 302 VD9 A S2  
2145 O  O1  . VD9 C .   ? 0.1081 0.1072 0.1133 0.0038  -0.0147 -0.0087 302 VD9 A O1  
2146 N  N3  . VD9 C .   ? 0.1113 0.0952 0.1118 -0.0063 0.0031  0.0006  302 VD9 A N3  
2147 C  C5  . VD9 C .   ? 0.1169 0.1127 0.1342 -0.0195 0.0027  -0.0114 302 VD9 A C5  
2148 C  C10 . VD9 C .   ? 0.1370 0.1194 0.1523 -0.0178 0.0187  0.0057  302 VD9 A C10 
2149 C  C9  . VD9 C .   ? 0.1673 0.1444 0.1808 -0.0154 0.0142  0.0211  302 VD9 A C9  
2150 C  C8  . VD9 C .   ? 0.1798 0.0983 0.1674 -0.0071 0.0340  0.0130  302 VD9 A C8  
2151 C  C7  . VD9 C .   ? 0.1343 0.1140 0.1985 -0.0114 -0.0167 0.0126  302 VD9 A C7  
2152 C  C6  . VD9 C .   ? 0.1156 0.1156 0.1641 -0.0010 -0.0151 -0.0135 302 VD9 A C6  
2153 S  S11 . VD9 C .   ? 0.2832 0.1562 0.3130 0.0126  0.0939  0.0658  302 VD9 A S11 
2154 C  C12 . VD9 C .   ? 0.2587 0.2029 0.2566 0.0073  0.1128  0.0854  302 VD9 A C12 
2155 C  C13 . VD9 C .   ? 0.3621 0.3173 0.4569 -0.1005 0.1370  0.0671  302 VD9 A C13 
2156 C  C14 . VD9 C .   ? 0.2390 0.3651 0.3550 0.0582  0.0307  0.0579  302 VD9 A C14 
2157 O  O4  . VD9 D .   ? 0.2064 0.2983 0.4239 0.0803  -0.0153 0.0384  303 VD9 A O4  
2158 S  S2  . VD9 D .   ? 0.2128 0.2889 0.2967 0.0003  -0.0093 0.0154  303 VD9 A S2  
2159 O  O1  . VD9 D .   ? 0.2256 0.3647 0.3578 -0.1375 0.0037  0.0653  303 VD9 A O1  
2160 N  N3  . VD9 D .   ? 0.1713 0.2644 0.3743 0.0344  0.0463  -0.0076 303 VD9 A N3  
2161 C  C5  . VD9 D .   ? 0.1806 0.2833 0.2778 -0.0302 -0.0219 0.0182  303 VD9 A C5  
2162 C  C10 . VD9 D .   ? 0.3269 0.2824 0.4660 0.0597  0.0346  -0.1203 303 VD9 A C10 
2163 C  C9  . VD9 D .   ? 0.2756 0.3126 0.3025 -0.0206 -0.0527 -0.0291 303 VD9 A C9  
2164 C  C8  . VD9 D .   ? 0.1940 0.4355 0.3191 -0.0588 -0.0171 0.0153  303 VD9 A C8  
2165 C  C7  . VD9 D .   ? 0.4825 0.5188 0.4375 0.1620  0.1339  0.0364  303 VD9 A C7  
2166 C  C6  . VD9 D .   ? 0.2591 0.4035 0.2559 -0.0410 0.0688  0.0816  303 VD9 A C6  
2167 S  S11 . VD9 D .   ? 0.2731 0.4805 0.4239 0.0322  0.0372  -0.0298 303 VD9 A S11 
2168 C  C12 . VD9 D .   ? 0.6923 0.4304 0.5680 -0.3224 -0.0198 0.1202  303 VD9 A C12 
2169 C  C13 . VD9 D .   ? 0.4728 0.5192 0.5895 -0.0485 0.0903  0.1535  303 VD9 A C13 
2170 C  C14 . VD9 D .   ? 0.6114 0.3244 0.4760 0.0291  -0.0754 -0.0017 303 VD9 A C14 
2171 S  S   . DMS E .   ? 0.2562 0.2741 0.2838 -0.0198 0.0315  -0.0294 304 DMS A S   
2172 O  O   . DMS E .   ? 0.4372 0.3485 0.3671 0.0886  0.0768  -0.0917 304 DMS A O   
2173 C  C1  . DMS E .   ? 0.2295 0.2766 0.2186 0.0544  0.0204  -0.0658 304 DMS A C1  
2174 C  C2  . DMS E .   ? 0.1907 0.2162 0.4745 -0.0031 -0.0027 -0.0143 304 DMS A C2  
2175 N  N1  . BCN F .   ? 0.4947 0.4753 0.3801 -0.0619 0.0653  -0.0951 305 BCN A N1  
2176 C  C1  . BCN F .   ? 0.3097 0.4696 0.3537 -0.1444 0.0038  0.0342  305 BCN A C1  
2177 C  C2  . BCN F .   ? 0.3238 0.4200 0.4459 -0.1500 0.0511  0.0377  305 BCN A C2  
2178 O  O21 . BCN F .   ? 0.6656 0.4362 0.6718 -0.2777 -0.1367 0.1216  305 BCN A O21 
2179 O  O22 . BCN F .   ? 0.4448 0.5115 0.4922 -0.0232 -0.0377 0.1233  305 BCN A O22 
2180 C  C3  . BCN F .   ? 0.3481 0.2505 0.3995 -0.0825 0.0564  -0.0054 305 BCN A C3  
2181 C  C4  . BCN F .   ? 0.7458 0.5098 0.5885 0.0498  0.1800  -0.2066 305 BCN A C4  
2182 O  O4  . BCN F .   ? 0.4426 0.2601 0.5289 -0.0361 0.1106  -0.0186 305 BCN A O4  
2183 C  C5  . BCN F .   ? 0.2257 0.2336 0.2710 -0.0109 0.0222  0.0485  305 BCN A C5  
2184 C  C6  . BCN F .   ? 0.8615 0.8033 0.5023 -0.2266 -0.2538 -0.1840 305 BCN A C6  
2185 O  O6  . BCN F .   ? 0.7332 0.4933 0.5995 -0.3592 0.0527  0.0178  305 BCN A O6  
2186 S  S   . DMS G .   ? 0.6171 0.3499 0.4189 0.0031  -0.1000 -0.0303 306 DMS A S   
2187 O  O   . DMS G .   ? 0.3991 0.2378 0.4768 -0.1324 0.0076  -0.0093 306 DMS A O   
2188 C  C1  . DMS G .   ? 0.6315 0.5091 1.0693 -0.3702 -0.0383 0.1532  306 DMS A C1  
2189 C  C2  . DMS G .   ? 0.5055 0.2820 0.5309 0.0957  -0.0623 -0.1014 306 DMS A C2  
2190 O  O   . HOH H .   ? 0.3998 0.3004 0.5077 0.0362  -0.2148 0.0287  401 HOH A O   
2191 O  O   . HOH H .   ? 0.3894 0.3173 0.4174 -0.0088 -0.0271 -0.0005 402 HOH A O   
2192 O  O   . HOH H .   ? 0.5436 0.3072 0.8001 0.1305  -0.1316 -0.1888 403 HOH A O   
2193 O  O   . HOH H .   ? 0.3901 0.4199 0.4624 -0.0942 -0.1361 0.0379  404 HOH A O   
2194 O  O   . HOH H .   ? 0.4322 0.4584 0.4419 0.0255  0.0335  -0.0098 405 HOH A O   
2195 O  O   . HOH H .   ? 0.6172 0.4544 0.3327 0.0027  -0.0098 0.0344  406 HOH A O   
2196 O  O   . HOH H .   ? 0.3496 0.5389 0.2257 -0.0248 -0.0263 0.0344  407 HOH A O   
2197 O  O   . HOH H .   ? 0.5450 0.4344 0.6485 0.0907  -0.1875 -0.0812 408 HOH A O   
2198 O  O   . HOH H .   ? 0.2637 0.1577 0.2814 -0.0082 -0.0329 -0.0049 409 HOH A O   
2199 O  O   . HOH H .   ? 0.3345 0.3125 0.4085 -0.0351 -0.0392 0.0571  410 HOH A O   
2200 O  O   . HOH H .   ? 0.3938 0.3870 0.4214 -0.0035 -0.0255 -0.0003 411 HOH A O   
2201 O  O   . HOH H .   ? 0.4221 0.2983 0.3707 0.0494  0.0491  0.0710  412 HOH A O   
2202 O  O   . HOH H .   ? 0.5644 0.3241 0.2943 0.0737  0.1106  0.0873  413 HOH A O   
2203 O  O   . HOH H .   ? 0.6205 0.2336 0.5023 0.0847  0.0930  0.1324  414 HOH A O   
2204 O  O   . HOH H .   ? 0.2731 0.4706 0.3503 -0.0588 0.0204  -0.0997 415 HOH A O   
2205 O  O   . HOH H .   ? 0.4275 0.4397 0.3161 0.0096  -0.0185 -0.0408 416 HOH A O   
2206 O  O   . HOH H .   ? 0.4617 0.3331 0.1579 -0.0355 -0.0251 0.0164  417 HOH A O   
2207 O  O   . HOH H .   ? 0.4865 0.4211 0.3823 -0.1615 0.0562  -0.0086 418 HOH A O   
2208 O  O   . HOH H .   ? 0.4329 0.4089 0.5526 -0.0417 0.0107  0.0410  419 HOH A O   
2209 O  O   . HOH H .   ? 0.5231 0.2832 0.2562 -0.0544 -0.0375 -0.0728 420 HOH A O   
2210 O  O   . HOH H .   ? 0.4142 0.1625 0.2236 0.0317  -0.1387 0.0096  421 HOH A O   
2211 O  O   . HOH H .   ? 0.2056 0.4516 0.5903 -0.0043 -0.0559 -0.2312 422 HOH A O   
2212 O  O   . HOH H .   ? 0.4559 0.4082 0.3654 -0.0529 0.0043  -0.0197 423 HOH A O   
2213 O  O   . HOH H .   ? 0.6144 0.3889 0.3496 0.1879  0.0337  0.0522  424 HOH A O   
2214 O  O   . HOH H .   ? 0.3604 0.3161 0.2169 0.0074  -0.0403 -0.0640 425 HOH A O   
2215 O  O   . HOH H .   ? 0.2936 0.3726 0.3230 -0.0983 0.0939  -0.1344 426 HOH A O   
2216 O  O   . HOH H .   ? 0.5059 0.3432 0.3050 0.0031  -0.0913 0.0615  427 HOH A O   
2217 O  O   . HOH H .   ? 0.4581 0.4162 0.3916 -0.0335 -0.0171 -0.0272 428 HOH A O   
2218 O  O   . HOH H .   ? 0.4035 0.3388 0.3805 -0.0680 0.1430  -0.0715 429 HOH A O   
2219 O  O   . HOH H .   ? 0.4049 0.4179 0.4315 0.0221  -0.0230 0.0115  430 HOH A O   
2220 O  O   . HOH H .   ? 0.3607 0.4383 0.3925 0.1571  0.1520  0.0220  431 HOH A O   
2221 O  O   . HOH H .   ? 0.1914 0.1280 0.1053 -0.0238 -0.0176 0.0006  432 HOH A O   
2222 O  O   . HOH H .   ? 0.2070 0.6110 0.5504 -0.0373 0.0758  -0.0527 433 HOH A O   
2223 O  O   . HOH H .   ? 0.1280 0.1358 0.1494 -0.0076 0.0074  -0.0114 434 HOH A O   
2224 O  O   . HOH H .   ? 0.1479 0.1291 0.1376 -0.0104 0.0063  -0.0093 435 HOH A O   
2225 O  O   . HOH H .   ? 0.3356 0.2192 0.1571 -0.0310 0.0379  0.0148  436 HOH A O   
2226 O  O   . HOH H .   ? 0.2037 0.2083 0.2889 0.0210  -0.1172 -0.0399 437 HOH A O   
2227 O  O   . HOH H .   ? 0.3543 0.2723 0.3518 -0.0357 0.0842  -0.0988 438 HOH A O   
2228 O  O   . HOH H .   ? 0.4476 0.2126 0.3927 -0.0494 0.0176  -0.0217 439 HOH A O   
2229 O  O   . HOH H .   ? 0.2161 0.7278 0.4616 0.1230  -0.0392 -0.2721 440 HOH A O   
2230 O  O   . HOH H .   ? 0.2627 0.2551 0.2785 0.0259  0.0005  -0.0102 441 HOH A O   
2231 O  O   . HOH H .   ? 0.2846 0.2004 0.3312 -0.0419 -0.0489 0.0384  442 HOH A O   
2232 O  O   . HOH H .   ? 0.1855 0.3361 0.4585 0.0656  -0.0071 0.0214  443 HOH A O   
2233 O  O   . HOH H .   ? 0.2698 0.2166 0.2990 0.0266  0.0068  0.0452  444 HOH A O   
2234 O  O   . HOH H .   ? 0.3119 0.2293 0.2476 -0.0772 -0.0529 -0.0163 445 HOH A O   
2235 O  O   . HOH H .   ? 0.2706 0.3118 0.2716 -0.0575 0.0746  -0.0037 446 HOH A O   
2236 O  O   . HOH H .   ? 0.3115 0.6866 0.4222 -0.0812 0.0277  0.2445  447 HOH A O   
2237 O  O   . HOH H .   ? 0.2967 0.4695 0.4218 0.0406  0.0434  0.1507  448 HOH A O   
2238 O  O   . HOH H .   ? 0.2964 0.3665 0.4706 0.0899  -0.1190 -0.0177 449 HOH A O   
2239 O  O   . HOH H .   ? 0.3264 0.2817 0.1738 -0.0167 -0.0346 0.0219  450 HOH A O   
2240 O  O   . HOH H .   ? 0.5813 0.2580 0.5339 -0.0895 -0.1146 -0.0966 451 HOH A O   
2241 O  O   . HOH H .   ? 0.2275 0.2518 0.2422 0.0263  -0.0564 -0.0003 452 HOH A O   
2242 O  O   . HOH H .   ? 0.3718 0.5105 0.3345 -0.0522 0.0395  -0.0864 453 HOH A O   
2243 O  O   . HOH H .   ? 0.2580 0.3898 0.1904 0.0372  -0.0096 -0.0549 454 HOH A O   
2244 O  O   . HOH H .   ? 0.2641 0.2462 0.3731 -0.0013 0.0768  0.0571  455 HOH A O   
2245 O  O   . HOH H .   ? 0.1868 0.1282 0.1983 -0.0137 -0.0092 0.0071  456 HOH A O   
2246 O  O   . HOH H .   ? 0.6366 0.2316 0.6883 -0.0368 0.0876  0.0733  457 HOH A O   
2247 O  O   . HOH H .   ? 0.1544 0.1419 0.1589 0.0059  -0.0024 -0.0164 458 HOH A O   
2248 O  O   . HOH H .   ? 0.3378 0.2749 0.3349 -0.0143 0.1404  0.0388  459 HOH A O   
2249 O  O   . HOH H .   ? 0.3783 0.2791 0.2150 -0.0934 0.0979  -0.0758 460 HOH A O   
2250 O  O   . HOH H .   ? 0.3126 0.2440 0.3108 0.0337  -0.0658 0.0608  461 HOH A O   
2251 O  O   . HOH H .   ? 0.4908 0.3549 0.3363 0.0087  0.0288  -0.0041 462 HOH A O   
2252 O  O   . HOH H .   ? 0.3560 0.4592 0.5073 -0.1501 0.1499  -0.0788 463 HOH A O   
2253 O  O   . HOH H .   ? 0.2939 0.2284 0.3337 0.0318  -0.0414 0.0395  464 HOH A O   
2254 O  O   . HOH H .   ? 0.2383 0.1616 0.2363 -0.0013 -0.0296 0.0146  465 HOH A O   
2255 O  O   . HOH H .   ? 0.4947 0.3889 0.3273 -0.1818 0.1581  -0.1467 466 HOH A O   
2256 O  O   . HOH H .   ? 0.2076 0.2277 0.2040 0.0057  -0.0489 0.0221  467 HOH A O   
2257 O  O   . HOH H .   ? 0.5000 0.2601 0.2246 -0.0658 -0.0020 0.0617  468 HOH A O   
2258 O  O   . HOH H .   ? 0.2748 0.3560 0.2615 0.0244  0.0537  -0.0161 469 HOH A O   
2259 O  O   . HOH H .   ? 0.4358 0.2569 0.5712 -0.1247 0.0012  0.0436  470 HOH A O   
2260 O  O   . HOH H .   ? 0.7016 0.4171 0.3895 -0.1563 -0.0366 0.0935  471 HOH A O   
2261 O  O   . HOH H .   ? 0.3740 0.4167 0.3560 0.0627  0.0148  -0.0362 472 HOH A O   
2262 O  O   . HOH H .   ? 0.3018 0.4857 0.5342 0.1067  -0.0159 0.1527  473 HOH A O   
2263 O  O   . HOH H .   ? 0.5580 0.3779 0.2320 -0.1559 -0.0361 0.0062  474 HOH A O   
2264 O  O   . HOH H .   ? 0.6639 0.4860 0.3675 0.3289  0.1145  0.1799  475 HOH A O   
2265 O  O   . HOH H .   ? 0.3252 0.3582 0.4768 0.0527  -0.1732 -0.2325 476 HOH A O   
2266 O  O   . HOH H .   ? 0.1388 0.1304 0.1298 0.0098  -0.0063 -0.0024 477 HOH A O   
2267 O  O   . HOH H .   ? 0.2237 0.2248 0.3355 0.0110  0.0317  0.0073  478 HOH A O   
2268 O  O   . HOH H .   ? 0.3615 0.2548 0.3082 -0.0062 -0.0024 0.0785  479 HOH A O   
2269 O  O   . HOH H .   ? 0.3985 0.3108 0.2724 -0.1010 -0.0966 -0.0421 480 HOH A O   
2270 O  O   . HOH H .   ? 0.5788 0.3198 0.1568 -0.0482 -0.0006 -0.0071 481 HOH A O   
2271 O  O   . HOH H .   ? 0.2949 0.3147 0.2742 -0.0798 0.0041  -0.0388 482 HOH A O   
2272 O  O   . HOH H .   ? 0.1422 0.1724 0.2471 -0.0184 0.0023  0.0140  483 HOH A O   
2273 O  O   . HOH H .   ? 0.2953 0.3632 0.2785 0.1298  0.0465  0.0983  484 HOH A O   
2274 O  O   . HOH H .   ? 0.5547 0.3718 0.3701 0.0996  0.0104  -0.0309 485 HOH A O   
2275 O  O   . HOH H .   ? 0.1212 0.1536 0.1377 0.0233  -0.0166 -0.0019 486 HOH A O   
2276 O  O   . HOH H .   ? 0.3040 0.3651 0.6764 0.0200  -0.1456 -0.1057 487 HOH A O   
2277 O  O   . HOH H .   ? 0.1158 0.1361 0.1379 -0.0031 0.0131  0.0034  488 HOH A O   
2278 O  O   . HOH H .   ? 0.2204 0.2401 0.2781 -0.0384 -0.0081 -0.0175 489 HOH A O   
2279 O  O   . HOH H .   ? 0.7518 0.6804 0.4315 -0.0996 -0.2592 0.0241  490 HOH A O   
2280 O  O   . HOH H .   ? 0.5238 0.3094 0.2356 -0.0381 0.0974  -0.0886 491 HOH A O   
2281 O  O   . HOH H .   ? 0.6761 0.2810 0.2241 0.0215  0.0060  0.0529  492 HOH A O   
2282 O  O   . HOH H .   ? 0.1541 0.2645 0.3421 -0.0339 -0.0465 0.0207  493 HOH A O   
2283 O  O   . HOH H .   ? 0.3388 0.5774 0.5866 0.0020  -0.0337 -0.1763 494 HOH A O   
2284 O  O   . HOH H .   ? 0.1331 0.1700 0.1567 0.0027  -0.0285 0.0148  495 HOH A O   
2285 O  O   . HOH H .   ? 0.3143 0.3334 0.4944 0.0575  0.0648  0.2063  496 HOH A O   
2286 O  O   . HOH H .   ? 0.2516 0.2390 0.2354 -0.0281 -0.0785 0.0020  497 HOH A O   
2287 O  O   . HOH H .   ? 0.1704 0.2029 0.2238 0.0270  -0.0186 0.0119  498 HOH A O   
2288 O  O   . HOH H .   ? 0.4444 0.2612 0.2752 -0.0344 -0.0776 0.1395  499 HOH A O   
2289 O  O   . HOH H .   ? 0.4972 0.5468 0.2203 -0.0987 0.0155  0.0608  500 HOH A O   
2290 O  O   . HOH H .   ? 0.2304 0.3273 0.3729 0.0196  -0.1066 0.0023  501 HOH A O   
2291 O  O   . HOH H .   ? 0.2126 0.1782 0.2900 0.0271  -0.0182 -0.0370 502 HOH A O   
2292 O  O   . HOH H .   ? 0.2929 0.1568 0.2680 -0.0423 -0.0054 0.0020  503 HOH A O   
2293 O  O   . HOH H .   ? 0.2283 0.3087 0.1844 -0.0181 -0.0010 -0.0612 504 HOH A O   
2294 O  O   . HOH H .   ? 0.7346 0.5659 0.6165 -0.1431 -0.1916 -0.0723 505 HOH A O   
2295 O  O   . HOH H .   ? 0.4304 0.2569 0.6377 0.0092  -0.1965 -0.0057 506 HOH A O   
2296 O  O   . HOH H .   ? 0.5665 0.4731 0.4232 -0.0939 -0.1239 0.2107  507 HOH A O   
2297 O  O   . HOH H .   ? 0.3391 0.3101 0.2774 0.0041  0.0577  -0.0057 508 HOH A O   
2298 O  O   . HOH H .   ? 0.2311 0.1510 0.2065 -0.0399 -0.0103 -0.0248 509 HOH A O   
2299 O  O   . HOH H .   ? 0.3690 0.2153 0.3337 0.0995  -0.0719 -0.0057 510 HOH A O   
2300 O  O   . HOH H .   ? 0.3700 0.4617 0.5853 0.0564  0.0917  0.0816  511 HOH A O   
2301 O  O   . HOH H .   ? 0.2169 0.1629 0.1889 -0.0236 -0.0020 0.0175  512 HOH A O   
2302 O  O   . HOH H .   ? 0.2040 0.1958 0.2533 0.0054  -0.0342 -0.0230 513 HOH A O   
2303 O  O   . HOH H .   ? 0.5410 0.2634 0.5131 0.0063  -0.1482 -0.0819 514 HOH A O   
2304 O  O   . HOH H .   ? 0.2395 0.2536 0.2047 0.0070  0.0454  -0.0298 515 HOH A O   
2305 O  O   . HOH H .   ? 0.4045 0.3137 0.5228 0.1611  -0.1324 -0.0564 516 HOH A O   
2306 O  O   . HOH H .   ? 0.5235 0.5378 0.2936 -0.2013 -0.0109 0.1463  517 HOH A O   
2307 O  O   . HOH H .   ? 0.5076 0.9294 1.0138 -0.1336 0.3609  -0.1280 518 HOH A O   
2308 O  O   . HOH H .   ? 0.1753 0.1603 0.1958 0.0370  0.0065  0.0010  519 HOH A O   
2309 O  O   . HOH H .   ? 0.1386 0.1544 0.1831 0.0229  -0.0294 0.0174  520 HOH A O   
2310 O  O   . HOH H .   ? 0.1862 0.1771 0.3410 -0.0395 -0.0724 0.0181  521 HOH A O   
2311 O  O   . HOH H .   ? 0.4706 0.4365 0.4710 0.0221  0.0131  0.0258  522 HOH A O   
2312 O  O   . HOH H .   ? 0.2122 0.2029 0.1958 -0.0131 -0.0163 0.0098  523 HOH A O   
2313 O  O   . HOH H .   ? 0.4329 0.4167 0.2921 -0.0126 0.0938  -0.0322 524 HOH A O   
2314 O  O   . HOH H .   ? 0.6905 0.3819 0.4125 0.1439  0.0697  -0.0754 525 HOH A O   
2315 O  O   . HOH H .   ? 0.6840 0.3822 0.2641 -0.1207 0.0291  -0.1321 526 HOH A O   
2316 O  O   . HOH H .   ? 0.2612 0.4114 0.2389 -0.0942 -0.0939 0.0227  527 HOH A O   
2317 O  O   . HOH H .   ? 0.1095 0.1536 0.2386 -0.0065 -0.0170 -0.0362 528 HOH A O   
2318 O  O   . HOH H .   ? 0.3410 0.1895 0.2699 -0.0087 -0.0582 -0.0154 529 HOH A O   
2319 O  O   . HOH H .   ? 0.2444 0.2878 0.1894 0.0401  -0.0003 0.0152  530 HOH A O   
2320 O  O   . HOH H .   ? 0.2856 0.6326 0.6912 -0.0582 0.0151  0.1221  531 HOH A O   
2321 O  O   . HOH H .   ? 0.2810 0.4401 0.4548 -0.2312 -0.0701 0.0737  532 HOH A O   
2322 O  O   . HOH H .   ? 0.2911 0.3241 0.4354 -0.0529 0.0432  -0.0120 533 HOH A O   
2323 O  O   . HOH H .   ? 0.3452 0.2395 0.2961 -0.0542 -0.0098 -0.0324 534 HOH A O   
2324 O  O   . HOH H .   ? 0.8277 0.4013 0.4235 -0.1172 -0.0013 -0.1543 535 HOH A O   
2325 O  O   . HOH H .   ? 0.4218 0.5023 0.2529 -0.0405 -0.1667 0.1260  536 HOH A O   
2326 O  O   . HOH H .   ? 0.2504 0.1555 0.2040 0.0408  -0.0124 0.0140  537 HOH A O   
2327 O  O   . HOH H .   ? 0.3524 0.4674 0.4024 -0.0568 -0.0131 0.0161  538 HOH A O   
2328 O  O   . HOH H .   ? 0.9463 0.3855 0.3244 0.2590  0.1296  0.0776  539 HOH A O   
2329 O  O   . HOH H .   ? 0.3061 0.1352 0.2651 0.0063  -0.0860 0.0114  540 HOH A O   
2330 O  O   . HOH H .   ? 0.3266 0.1828 0.2201 -0.0054 -0.0996 -0.0024 541 HOH A O   
2331 O  O   . HOH H .   ? 0.3967 0.5763 0.3025 0.1454  -0.0403 -0.0886 542 HOH A O   
2332 O  O   . HOH H .   ? 0.2896 0.1995 0.2399 0.0238  -0.0952 -0.0185 543 HOH A O   
2333 O  O   . HOH H .   ? 0.3029 0.3646 0.3762 -0.1111 0.0419  -0.1067 544 HOH A O   
2334 O  O   . HOH H .   ? 0.5181 0.2827 0.2010 0.0740  0.0006  0.0410  545 HOH A O   
2335 O  O   . HOH H .   ? 0.4265 0.4415 0.4592 0.0434  0.0219  -0.0405 546 HOH A O   
2336 O  O   . HOH H .   ? 0.2921 0.2161 0.3880 -0.0197 -0.0970 -0.0135 547 HOH A O   
2337 O  O   . HOH H .   ? 0.2523 0.3319 0.3075 -0.0935 -0.0505 0.0070  548 HOH A O   
2338 O  O   . HOH H .   ? 0.3992 0.4835 0.3295 0.1023  -0.0568 0.0303  549 HOH A O   
2339 O  O   . HOH H .   ? 0.6553 0.7260 0.3032 0.0266  -0.0943 -0.1507 550 HOH A O   
2340 O  O   . HOH H .   ? 0.1808 0.1810 0.2580 -0.0097 0.0414  -0.0099 551 HOH A O   
2341 O  O   . HOH H .   ? 0.3356 0.2583 0.2383 0.0357  0.0230  -0.0203 552 HOH A O   
2342 O  O   . HOH H .   ? 0.2013 0.1765 0.1897 0.0000  -0.0599 0.0131  553 HOH A O   
2343 O  O   . HOH H .   ? 0.6237 0.6449 0.4986 0.1054  -0.0258 0.0320  554 HOH A O   
2344 O  O   . HOH H .   ? 0.2565 0.2500 0.3302 0.0054  -0.0254 -0.0662 555 HOH A O   
2345 O  O   . HOH H .   ? 0.3039 0.5097 0.2771 -0.0185 -0.0388 0.1238  556 HOH A O   
2346 O  O   . HOH H .   ? 0.6941 0.3815 0.3557 0.1905  0.1386  0.1650  557 HOH A O   
2347 O  O   . HOH H .   ? 0.3773 0.3471 0.2566 0.1908  -0.0516 0.0355  558 HOH A O   
2348 O  O   . HOH H .   ? 0.5109 0.2349 0.2386 0.0759  0.0241  0.0186  559 HOH A O   
2349 O  O   . HOH H .   ? 0.3044 0.2518 0.5299 -0.0348 0.0096  -0.0493 560 HOH A O   
2350 O  O   . HOH H .   ? 0.2731 0.4411 0.3288 -0.1032 -0.1096 0.0749  561 HOH A O   
2351 O  O   . HOH H .   ? 0.5320 0.4095 0.4128 0.0120  -0.1395 0.1253  562 HOH A O   
2352 O  O   . HOH H .   ? 0.4308 0.1844 0.2374 -0.0540 -0.0498 -0.0467 563 HOH A O   
2353 O  O   . HOH H .   ? 0.3176 0.3384 0.2695 0.0274  0.0538  -0.0308 564 HOH A O   
2354 O  O   . HOH H .   ? 0.2060 0.2180 0.2662 -0.0198 -0.0269 -0.0544 565 HOH A O   
2355 O  O   . HOH H .   ? 0.4764 0.4027 0.2972 0.0203  0.0560  -0.0206 566 HOH A O   
2356 O  O   . HOH H .   ? 0.1776 0.2724 0.3604 0.0798  0.0392  0.0023  567 HOH A O   
2357 O  O   . HOH H .   ? 0.2363 0.2029 0.7498 -0.0010 0.1252  0.0891  568 HOH A O   
2358 O  O   . HOH H .   ? 0.6061 0.3596 0.4071 0.0881  -0.0129 -0.0375 569 HOH A O   
2359 O  O   . HOH H .   ? 0.2583 0.2155 0.2431 0.0491  0.0454  0.0842  570 HOH A O   
2360 O  O   . HOH H .   ? 0.1049 0.2186 0.2320 0.0038  0.0071  -0.0274 571 HOH A O   
2361 O  O   . HOH H .   ? 0.7342 0.4065 0.4702 0.1579  0.1208  0.0794  572 HOH A O   
2362 O  O   . HOH H .   ? 0.2645 0.2126 0.1774 0.0097  -0.0060 -0.0296 573 HOH A O   
2363 O  O   . HOH H .   ? 0.4059 0.3755 0.3833 -0.0957 -0.0702 -0.0432 574 HOH A O   
2364 O  O   . HOH H .   ? 0.3467 0.4200 0.3682 0.1159  0.0903  0.0719  575 HOH A O   
2365 O  O   . HOH H .   ? 0.4369 0.2128 0.2496 -0.0570 -0.1254 -0.0049 576 HOH A O   
2366 O  O   . HOH H .   ? 0.2232 0.1977 0.2699 -0.0904 -0.0185 -0.0419 577 HOH A O   
2367 O  O   . HOH H .   ? 0.1888 0.2386 0.2565 0.0052  -0.0164 -0.0200 578 HOH A O   
2368 O  O   . HOH H .   ? 0.2205 0.3331 0.3032 0.0478  0.0151  0.0019  579 HOH A O   
2369 O  O   . HOH H .   ? 0.1334 0.3482 0.4164 0.0210  -0.0233 0.1133  580 HOH A O   
2370 O  O   . HOH H .   ? 1.1991 1.1806 0.3137 0.6796  -0.2500 -0.4208 581 HOH A O   
2371 O  O   . HOH H .   ? 0.3481 0.2241 0.2169 0.0610  -0.0412 0.0126  582 HOH A O   
2372 O  O   . HOH H .   ? 0.1339 0.2371 0.1614 -0.0035 -0.0383 0.0384  583 HOH A O   
2373 O  O   . HOH H .   ? 0.2626 0.3079 0.3651 -0.0379 -0.0658 -0.0019 584 HOH A O   
2374 O  O   . HOH H .   ? 0.3378 0.2088 0.3079 0.0093  -0.0535 -0.0303 585 HOH A O   
2375 O  O   . HOH H .   ? 0.3406 0.2058 0.3208 0.0626  -0.0115 0.0513  586 HOH A O   
2376 O  O   . HOH H .   ? 0.2467 0.2465 0.4440 0.0599  0.0197  0.0715  587 HOH A O   
2377 O  O   . HOH H .   ? 0.6053 0.5414 0.4530 -0.0750 0.2355  -0.0348 588 HOH A O   
2378 O  O   . HOH H .   ? 0.1846 0.3525 0.3758 0.0141  0.0148  0.0286  589 HOH A O   
2379 O  O   . HOH H .   ? 0.3220 0.2949 0.2727 -0.0005 -0.0419 -0.0073 590 HOH A O   
2380 O  O   . HOH H .   ? 0.4053 0.1888 0.3025 0.0538  -0.0131 -0.0286 591 HOH A O   
2381 O  O   . HOH H .   ? 0.3945 0.3672 0.3366 -0.0241 0.0013  -0.0037 592 HOH A O   
2382 O  O   . HOH H .   ? 0.4020 0.4617 0.4052 0.0060  -0.1045 0.0060  593 HOH A O   
2383 O  O   . HOH H .   ? 0.2433 0.2414 0.2162 0.0454  -0.0253 0.0307  594 HOH A O   
2384 O  O   . HOH H .   ? 0.4354 0.4239 0.4052 0.0076  -0.0399 0.0164  595 HOH A O   
2385 O  O   . HOH H .   ? 0.5777 0.5163 0.2094 0.0013  0.0772  0.1093  596 HOH A O   
2386 O  O   . HOH H .   ? 0.1304 0.1246 0.1729 0.0074  -0.0093 -0.0054 597 HOH A O   
2387 O  O   . HOH H .   ? 0.4584 0.4526 0.5267 0.1272  -0.1580 -0.0275 598 HOH A O   
2388 O  O   . HOH H .   ? 0.4052 0.3495 0.3837 -0.0439 -0.0736 0.1066  599 HOH A O   
2389 O  O   . HOH H .   ? 0.4085 0.4322 0.1864 0.0900  -0.0292 0.0228  600 HOH A O   
2390 O  O   . HOH H .   ? 0.7171 0.7896 0.3334 -0.2386 0.1463  -0.1507 601 HOH A O   
2391 O  O   . HOH H .   ? 0.1852 0.2292 0.3442 0.0542  -0.0873 -0.0342 602 HOH A O   
2392 O  O   . HOH H .   ? 0.3822 0.2529 0.3870 0.0847  0.0952  0.0640  603 HOH A O   
2393 O  O   . HOH H .   ? 0.3212 0.2204 0.3226 -0.0109 -0.0595 0.0098  604 HOH A O   
2394 O  O   . HOH H .   ? 0.3169 0.2259 0.2788 0.0790  0.0692  0.0315  605 HOH A O   
2395 O  O   . HOH H .   ? 0.3730 0.2540 0.6075 -0.0146 -0.0173 0.1344  606 HOH A O   
2396 O  O   . HOH H .   ? 0.2055 0.1361 0.2185 0.0135  -0.0142 -0.0097 607 HOH A O   
2397 O  O   . HOH H .   ? 0.7261 0.2347 0.5526 -0.0986 0.1344  -0.0361 608 HOH A O   
2398 O  O   . HOH H .   ? 0.1494 0.2036 0.2831 -0.0154 -0.0164 0.0081  609 HOH A O   
2399 O  O   . HOH H .   ? 0.6990 0.2982 0.4365 0.1488  -0.1370 -0.0625 610 HOH A O   
2400 O  O   . HOH H .   ? 0.5824 0.5465 0.3363 0.1401  -0.0957 0.0483  611 HOH A O   
2401 O  O   . HOH H .   ? 0.2444 0.1950 0.1959 0.0003  0.0551  0.0054  612 HOH A O   
2402 O  O   . HOH H .   ? 0.3094 0.4933 0.3366 0.0684  -0.0172 -0.0834 613 HOH A O   
2403 O  O   . HOH H .   ? 0.2099 0.2029 0.2155 0.0093  -0.0152 0.0003  614 HOH A O   
2404 O  O   . HOH H .   ? 0.4871 0.4459 0.2716 -0.0944 0.0108  0.0688  615 HOH A O   
2405 O  O   . HOH H .   ? 0.8295 1.2056 0.1095 0.0443  0.0251  0.1931  616 HOH A O   
2406 O  O   . HOH H .   ? 0.2975 0.4760 0.3255 0.0119  0.0287  0.0282  617 HOH A O   
2407 O  O   . HOH H .   ? 0.3697 0.3597 0.2465 -0.0917 -0.0768 -0.0115 618 HOH A O   
2408 O  O   . HOH H .   ? 0.2383 0.2910 0.4469 0.1281  0.0188  0.0379  619 HOH A O   
2409 O  O   . HOH H .   ? 0.4832 0.4487 0.4549 -0.0197 -0.0136 0.0054  620 HOH A O   
2410 O  O   . HOH H .   ? 0.2868 0.5000 0.2712 0.0934  0.0342  0.0063  621 HOH A O   
2411 O  O   . HOH H .   ? 0.3925 0.4153 0.3668 0.0952  0.0557  -0.0322 622 HOH A O   
2412 O  O   . HOH H .   ? 0.4803 0.4056 0.5795 0.0582  0.2732  -0.0485 623 HOH A O   
2413 O  O   . HOH H .   ? 0.3082 0.2763 0.6934 -0.1075 0.0559  0.0746  624 HOH A O   
2414 O  O   . HOH H .   ? 0.5579 1.0334 0.4792 0.3761  0.1676  0.2985  625 HOH A O   
2415 O  O   . HOH H .   ? 0.4180 0.3273 0.4096 -0.0068 -0.0006 0.0436  626 HOH A O   
2416 O  O   . HOH H .   ? 0.4473 0.4067 0.4319 0.0068  0.0024  0.0449  627 HOH A O   
2417 O  O   . HOH H .   ? 0.5109 0.2425 0.5023 0.0812  0.2330  0.0970  628 HOH A O   
2418 O  O   . HOH H .   ? 1.1763 0.6212 1.7762 0.2653  0.3095  -0.0551 629 HOH A O   
2419 O  O   . HOH H .   ? 0.4972 0.4412 0.2814 0.0692  -0.0108 0.0304  630 HOH A O   
2420 O  O   . HOH H .   ? 0.4164 0.5192 0.2932 -0.0423 -0.0248 0.1164  631 HOH A O   
2421 O  O   . HOH H .   ? 0.6261 0.2929 0.2835 -0.0555 0.1234  0.1032  632 HOH A O   
2422 O  O   . HOH H .   ? 0.1747 0.1467 0.1966 -0.0093 -0.0288 -0.0124 633 HOH A O   
2423 O  O   . HOH H .   ? 0.4735 0.5414 0.3046 -0.2980 -0.0417 0.0443  634 HOH A O   
2424 O  O   . HOH H .   ? 0.4405 0.4307 0.4423 0.0020  -0.0049 0.0335  635 HOH A O   
2425 O  O   . HOH H .   ? 0.2052 0.2918 0.3600 -0.0024 -0.0513 -0.0170 636 HOH A O   
2426 O  O   . HOH H .   ? 0.3245 0.3876 1.0433 -0.1376 -0.0755 0.1045  637 HOH A O   
2427 O  O   . HOH H .   ? 0.2967 0.3377 0.2458 -0.0153 -0.0329 -0.0020 638 HOH A O   
2428 O  O   . HOH H .   ? 0.3689 0.6926 0.6966 0.2372  -0.1441 -0.2089 639 HOH A O   
2429 O  O   . HOH H .   ? 0.3658 0.6021 0.4383 0.0230  0.0645  0.2520  640 HOH A O   
2430 O  O   . HOH H .   ? 0.3616 0.3773 0.6801 0.1062  -0.2167 -0.0799 641 HOH A O   
2431 O  O   . HOH H .   ? 0.3528 0.4142 0.2508 -0.0678 0.0263  0.0566  642 HOH A O   
2432 O  O   . HOH H .   ? 0.3711 0.4477 0.6517 0.1828  0.2461  0.2788  643 HOH A O   
2433 O  O   . HOH H .   ? 0.4416 0.4275 0.4512 0.0148  0.0348  -0.0348 644 HOH A O   
2434 O  O   . HOH H .   ? 0.4441 0.3962 0.1968 0.0952  -0.0395 -0.0802 645 HOH A O   
2435 O  O   . HOH H .   ? 0.5443 0.2168 0.6776 0.0631  -0.2219 0.0104  646 HOH A O   
2436 O  O   . HOH H .   ? 0.2730 0.3185 0.3162 -0.0017 0.0115  0.0293  647 HOH A O   
2437 O  O   . HOH H .   ? 0.3212 0.4099 0.5389 -0.0065 -0.0454 0.0074  648 HOH A O   
2438 O  O   . HOH H .   ? 0.4732 0.2408 0.6564 -0.0644 0.1837  -0.0034 649 HOH A O   
2439 O  O   . HOH H .   ? 0.4156 0.3776 0.3895 0.0082  0.0292  0.0115  650 HOH A O   
2440 O  O   . HOH H .   ? 0.3220 0.2569 0.4340 0.0511  -0.2381 -0.0109 651 HOH A O   
2441 O  O   . HOH H .   ? 0.4146 0.3773 0.3241 -0.1493 -0.0098 0.0595  652 HOH A O   
2442 O  O   . HOH H .   ? 0.3201 0.2515 0.3528 0.0414  -0.0784 0.0006  653 HOH A O   
2443 O  O   . HOH H .   ? 0.5090 0.6434 0.4268 0.0535  0.2347  -0.1242 654 HOH A O   
2444 O  O   . HOH H .   ? 0.4074 0.5633 0.6413 -0.2135 -0.0593 0.1655  655 HOH A O   
2445 O  O   . HOH H .   ? 0.4465 0.4800 0.6427 0.1114  0.0601  0.0900  656 HOH A O   
2446 O  O   . HOH H .   ? 0.3165 0.7584 0.3621 0.0750  0.0010  0.1018  657 HOH A O   
2447 O  O   . HOH H .   ? 0.3061 0.3248 0.2982 -0.0196 0.0258  -0.0355 658 HOH A O   
2448 O  O   . HOH H .   ? 0.4516 0.4189 0.4265 -0.0005 0.0013  -0.0299 659 HOH A O   
2449 O  O   . HOH H .   ? 0.4362 0.4113 0.7318 0.0188  0.0401  0.1826  660 HOH A O   
2450 O  O   . HOH H .   ? 0.2968 0.3064 0.3291 -0.1080 -0.0467 -0.0236 661 HOH A O   
2451 O  O   . HOH H .   ? 0.3111 0.3701 0.3902 0.1783  -0.0887 -0.0500 662 HOH A O   
2452 O  O   . HOH H .   ? 0.6291 0.2878 0.4182 0.0030  0.1045  0.0483  663 HOH A O   
2453 O  O   . HOH H .   ? 0.2982 0.3090 0.6219 -0.0252 -0.0340 0.0015  664 HOH A O   
2454 O  O   . HOH H .   ? 0.2467 0.3191 0.4354 -0.0662 -0.0024 -0.0305 665 HOH A O   
2455 O  O   . HOH H .   ? 0.4620 0.2379 0.9834 0.0886  -0.0518 -0.0258 666 HOH A O   
2456 O  O   . HOH H .   ? 0.4760 0.3309 0.4049 -0.0351 0.0181  -0.0509 667 HOH A O   
2457 O  O   . HOH H .   ? 0.5102 0.4189 0.3582 -0.0878 -0.2166 0.0763  668 HOH A O   
2458 O  O   . HOH H .   ? 0.5486 0.4078 0.3985 -0.0059 -0.0296 0.0210  669 HOH A O   
2459 O  O   . HOH H .   ? 0.5612 0.5565 0.3051 -0.0174 -0.0741 0.0929  670 HOH A O   
2460 O  O   . HOH H .   ? 0.3082 0.6082 0.3690 0.1067  -0.0876 -0.2356 671 HOH A O   
2461 O  O   . HOH H .   ? 0.3561 0.5468 0.3039 0.0746  0.0027  0.0649  672 HOH A O   
2462 O  O   . HOH H .   ? 0.4799 0.2062 0.4573 0.0041  -0.0956 0.0068  673 HOH A O   
2463 O  O   . HOH H .   ? 0.5188 0.3180 0.2302 -0.1361 -0.0188 0.0054  674 HOH A O   
2464 O  O   . HOH H .   ? 0.4785 0.4010 0.2810 0.0193  0.0850  -0.1023 675 HOH A O   
2465 O  O   . HOH H .   ? 0.4595 0.4957 0.5102 0.0065  -0.0156 -0.0392 676 HOH A O   
2466 O  O   . HOH H .   ? 0.4355 0.3826 0.4297 0.0218  -0.0225 -0.0142 677 HOH A O   
2467 O  O   . HOH H .   ? 0.7728 0.2985 0.4311 -0.1040 -0.0176 0.0538  678 HOH A O   
2468 O  O   . HOH H .   ? 0.3579 0.1855 0.2551 0.0027  -0.0573 -0.0164 679 HOH A O   
2469 O  O   . HOH H .   ? 0.3251 0.3787 0.5874 0.1263  -0.0381 0.0178  680 HOH A O   
2470 O  O   . HOH H .   ? 0.4611 0.2379 0.5059 0.0689  0.1105  0.0494  681 HOH A O   
2471 O  O   . HOH H .   ? 0.5224 0.4221 0.4466 -0.0115 0.0942  -0.0339 682 HOH A O   
2472 O  O   . HOH H .   ? 0.3834 0.2921 0.3794 -0.0428 -0.1145 0.0953  683 HOH A O   
2473 O  O   . HOH H .   ? 0.4933 0.2512 0.3535 -0.0592 -0.1265 0.0397  684 HOH A O   
2474 O  O   . HOH H .   ? 0.2756 0.2143 0.2411 0.0318  -0.0575 0.0390  685 HOH A O   
2475 O  O   . HOH H .   ? 0.8507 0.4717 0.4678 -0.0697 0.2406  -0.1745 686 HOH A O   
2476 O  O   . HOH H .   ? 0.4192 0.3816 0.6503 0.0441  -0.1155 0.0526  687 HOH A O   
2477 O  O   . HOH H .   ? 0.4246 0.3819 0.4397 -0.0491 0.0227  -0.0333 688 HOH A O   
2478 O  O   . HOH H .   ? 0.2508 0.6057 0.5026 -0.0983 -0.0584 0.0627  689 HOH A O   
2479 O  O   . HOH H .   ? 0.3068 0.3554 0.8302 -0.0825 -0.2202 -0.0005 690 HOH A O   
2480 O  O   . HOH H .   ? 0.2663 0.2946 0.3051 0.0171  -0.0342 0.0261  691 HOH A O   
2481 O  O   . HOH H .   ? 0.3887 0.3476 0.4487 -0.0643 0.0142  0.0653  692 HOH A O   
2482 O  O   . HOH H .   ? 0.4875 0.6115 0.5963 0.3109  0.0076  0.0579  693 HOH A O   
2483 O  O   . HOH H .   ? 0.3417 0.1831 0.4153 -0.0416 0.1456  -0.0337 694 HOH A O   
2484 O  O   . HOH H .   ? 0.4509 0.3240 0.2554 0.0244  -0.0104 -0.0082 695 HOH A O   
2485 O  O   . HOH H .   ? 0.7192 0.4893 0.4663 0.1773  0.1404  0.1115  696 HOH A O   
2486 O  O   . HOH H .   ? 0.3841 0.4726 0.5490 0.1342  0.0504  0.0644  697 HOH A O   
2487 O  O   . HOH H .   ? 0.4889 0.3546 0.5256 0.0571  0.0935  0.0549  698 HOH A O   
2488 O  O   . HOH H .   ? 0.6607 0.4275 0.7450 0.2230  -0.2926 0.0005  699 HOH A O   
2489 O  O   . HOH H .   ? 0.2971 0.4077 0.4944 -0.0320 -0.0285 -0.1324 700 HOH A O   
2490 O  O   . HOH H .   ? 0.2857 0.3877 0.4753 -0.0728 0.0599  0.0000  701 HOH A O   
2491 O  O   . HOH H .   ? 0.5041 0.4738 0.3040 0.0364  0.0675  0.0564  702 HOH A O   
2492 O  O   . HOH H .   ? 0.5044 0.6700 0.3603 -0.2861 -0.0608 0.1318  703 HOH A O   
2493 O  O   . HOH H .   ? 0.2946 0.4383 0.4872 -0.1667 -0.0125 -0.1018 704 HOH A O   
2494 O  O   . HOH H .   ? 0.2979 0.4526 0.9143 -0.0297 -0.1554 0.2280  705 HOH A O   
2495 O  O   . HOH H .   ? 0.5090 0.3765 0.5799 0.0841  -0.0043 0.0271  706 HOH A O   
# 
