data_6YH4
# 
_entry.id   6YH4 
# 
_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   6YH4         pdb_00006yh4 10.2210/pdb6yh4/pdb 
WWPDB D_1292106575 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2021-04-07 
2 'Structure model' 1 1 2021-06-02 
3 'Structure model' 1 2 2024-01-24 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation                      
2 2 'Structure model' citation_author               
3 3 'Structure model' chem_comp_atom                
4 3 'Structure model' chem_comp_bond                
5 3 'Structure model' database_2                    
6 3 'Structure model' pdbx_initial_refinement_model 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                   
2  2 'Structure model' '_citation.journal_abbrev'            
3  2 'Structure model' '_citation.journal_id_CSD'            
4  2 'Structure model' '_citation.journal_id_ISSN'           
5  2 'Structure model' '_citation.journal_volume'            
6  2 'Structure model' '_citation.page_first'                
7  2 'Structure model' '_citation.page_last'                 
8  2 'Structure model' '_citation.pdbx_database_id_DOI'      
9  2 'Structure model' '_citation.pdbx_database_id_PubMed'   
10 2 'Structure model' '_citation.title'                     
11 2 'Structure model' '_citation.year'                      
12 3 'Structure model' '_database_2.pdbx_DOI'                
13 3 'Structure model' '_database_2.pdbx_database_accession' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6YH4 
_pdbx_database_status.recvd_initial_deposition_date   2020-03-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 0000-0001-5080-9367 
'Manakova, E.' 2 0000-0002-6027-2265 
'Grazulis, S.' 3 0000-0002-7928-5218 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemistryopen 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2191-1363 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                567 
_citation.page_last                 580 
_citation.title                     'Switching the Inhibitor-Enzyme Recognition Profile via Chimeric Carbonic Anhydrase XII.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/open.202100042 
_citation.pdbx_database_id_PubMed   33945229 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnoviene, J.'   1  0000-0001-5503-4775 
primary 'Smirnov, A.'       2  ?                   
primary 'Zaksauskas, A.'    3  ?                   
primary 'Zubriene, A.'      4  0000-0001-5996-1883 
primary 'Petrauskas, V.'    5  0000-0001-7983-4128 
primary 'Mickeviciute, A.'  6  ?                   
primary 'Michailoviene, V.' 7  ?                   
primary 'Capkauskaite, E.'  8  ?                   
primary 'Manakova, E.'      9  0000-0002-6027-2265 
primary 'Grazulis, S.'      10 0000-0002-7928-5218 
primary 'Baranauskiene, L.' 11 0000-0002-9924-9177 
primary 'Chen, W.Y.'        12 ?                   
primary 'Ladbury, J.E.'     13 0000-0002-6328-7200 
primary 'Matulis, D.'       14 0000-0002-6178-6276 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                               29220.879 1   4.2.1.1 
'A65S, N67K, I91T, F130A, V134S, L203N' ? ? 
2 non-polymer syn 'ZINC ION'                                                           65.409    1   ?       ? ? ? 
3 non-polymer syn '2,3,5,6-tetrafluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 337.268   1   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                 78.133    1   ?       ? ? ? 
5 water       nat water                                                                18.015    231 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                           ZN  
3 '2,3,5,6-tetrafluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' V13 
4 'DIMETHYL SULFOXIDE'                                                 DMS 
5 water                                                                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  SER n 
1 66  PHE n 
1 67  LYS n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  THR n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 ALA n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 SER n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 ASN n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                              ? 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                                                             ? 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                           ? 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                      ? 'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                                                             ? 'C3 H7 N O2 S'     121.158 
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 
V13 non-polymer         . '2,3,5,6-tetrafluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 'C8 H7 F4 N O5 S2' 337.268 
VAL 'L-peptide linking' y VALINE                                                               ? 'C5 H11 N O2'      117.146 
ZN  non-polymer         . 'ZINC ION'                                                           ? 'Zn 2'             65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 ALA 130 131 131 ALA ALA A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 SER 134 135 135 SER SER A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 ASN 203 204 204 ASN ASN A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 V13 1   302 301 V13 V13 A . 
D 4 DMS 1   303 1   DMS DMS A . 
E 5 HOH 1   401 25  HOH HOH A . 
E 5 HOH 2   402 58  HOH HOH A . 
E 5 HOH 3   403 90  HOH HOH A . 
E 5 HOH 4   404 39  HOH HOH A . 
E 5 HOH 5   405 134 HOH HOH A . 
E 5 HOH 6   406 99  HOH HOH A . 
E 5 HOH 7   407 207 HOH HOH A . 
E 5 HOH 8   408 150 HOH HOH A . 
E 5 HOH 9   409 101 HOH HOH A . 
E 5 HOH 10  410 115 HOH HOH A . 
E 5 HOH 11  411 76  HOH HOH A . 
E 5 HOH 12  412 145 HOH HOH A . 
E 5 HOH 13  413 89  HOH HOH A . 
E 5 HOH 14  414 178 HOH HOH A . 
E 5 HOH 15  415 142 HOH HOH A . 
E 5 HOH 16  416 108 HOH HOH A . 
E 5 HOH 17  417 75  HOH HOH A . 
E 5 HOH 18  418 120 HOH HOH A . 
E 5 HOH 19  419 153 HOH HOH A . 
E 5 HOH 20  420 34  HOH HOH A . 
E 5 HOH 21  421 5   HOH HOH A . 
E 5 HOH 22  422 27  HOH HOH A . 
E 5 HOH 23  423 93  HOH HOH A . 
E 5 HOH 24  424 54  HOH HOH A . 
E 5 HOH 25  425 59  HOH HOH A . 
E 5 HOH 26  426 194 HOH HOH A . 
E 5 HOH 27  427 109 HOH HOH A . 
E 5 HOH 28  428 225 HOH HOH A . 
E 5 HOH 29  429 60  HOH HOH A . 
E 5 HOH 30  430 45  HOH HOH A . 
E 5 HOH 31  431 68  HOH HOH A . 
E 5 HOH 32  432 139 HOH HOH A . 
E 5 HOH 33  433 8   HOH HOH A . 
E 5 HOH 34  434 9   HOH HOH A . 
E 5 HOH 35  435 169 HOH HOH A . 
E 5 HOH 36  436 40  HOH HOH A . 
E 5 HOH 37  437 131 HOH HOH A . 
E 5 HOH 38  438 10  HOH HOH A . 
E 5 HOH 39  439 44  HOH HOH A . 
E 5 HOH 40  440 46  HOH HOH A . 
E 5 HOH 41  441 151 HOH HOH A . 
E 5 HOH 42  442 136 HOH HOH A . 
E 5 HOH 43  443 176 HOH HOH A . 
E 5 HOH 44  444 147 HOH HOH A . 
E 5 HOH 45  445 2   HOH HOH A . 
E 5 HOH 46  446 36  HOH HOH A . 
E 5 HOH 47  447 92  HOH HOH A . 
E 5 HOH 48  448 164 HOH HOH A . 
E 5 HOH 49  449 168 HOH HOH A . 
E 5 HOH 50  450 124 HOH HOH A . 
E 5 HOH 51  451 138 HOH HOH A . 
E 5 HOH 52  452 7   HOH HOH A . 
E 5 HOH 53  453 77  HOH HOH A . 
E 5 HOH 54  454 128 HOH HOH A . 
E 5 HOH 55  455 74  HOH HOH A . 
E 5 HOH 56  456 55  HOH HOH A . 
E 5 HOH 57  457 42  HOH HOH A . 
E 5 HOH 58  458 214 HOH HOH A . 
E 5 HOH 59  459 220 HOH HOH A . 
E 5 HOH 60  460 121 HOH HOH A . 
E 5 HOH 61  461 32  HOH HOH A . 
E 5 HOH 62  462 61  HOH HOH A . 
E 5 HOH 63  463 184 HOH HOH A . 
E 5 HOH 64  464 125 HOH HOH A . 
E 5 HOH 65  465 70  HOH HOH A . 
E 5 HOH 66  466 18  HOH HOH A . 
E 5 HOH 67  467 29  HOH HOH A . 
E 5 HOH 68  468 57  HOH HOH A . 
E 5 HOH 69  469 98  HOH HOH A . 
E 5 HOH 70  470 17  HOH HOH A . 
E 5 HOH 71  471 13  HOH HOH A . 
E 5 HOH 72  472 47  HOH HOH A . 
E 5 HOH 73  473 88  HOH HOH A . 
E 5 HOH 74  474 3   HOH HOH A . 
E 5 HOH 75  475 135 HOH HOH A . 
E 5 HOH 76  476 193 HOH HOH A . 
E 5 HOH 77  477 38  HOH HOH A . 
E 5 HOH 78  478 173 HOH HOH A . 
E 5 HOH 79  479 83  HOH HOH A . 
E 5 HOH 80  480 112 HOH HOH A . 
E 5 HOH 81  481 123 HOH HOH A . 
E 5 HOH 82  482 37  HOH HOH A . 
E 5 HOH 83  483 14  HOH HOH A . 
E 5 HOH 84  484 1   HOH HOH A . 
E 5 HOH 85  485 231 HOH HOH A . 
E 5 HOH 86  486 52  HOH HOH A . 
E 5 HOH 87  487 165 HOH HOH A . 
E 5 HOH 88  488 105 HOH HOH A . 
E 5 HOH 89  489 219 HOH HOH A . 
E 5 HOH 90  490 11  HOH HOH A . 
E 5 HOH 91  491 209 HOH HOH A . 
E 5 HOH 92  492 156 HOH HOH A . 
E 5 HOH 93  493 20  HOH HOH A . 
E 5 HOH 94  494 78  HOH HOH A . 
E 5 HOH 95  495 127 HOH HOH A . 
E 5 HOH 96  496 63  HOH HOH A . 
E 5 HOH 97  497 104 HOH HOH A . 
E 5 HOH 98  498 12  HOH HOH A . 
E 5 HOH 99  499 80  HOH HOH A . 
E 5 HOH 100 500 4   HOH HOH A . 
E 5 HOH 101 501 43  HOH HOH A . 
E 5 HOH 102 502 195 HOH HOH A . 
E 5 HOH 103 503 226 HOH HOH A . 
E 5 HOH 104 504 19  HOH HOH A . 
E 5 HOH 105 505 28  HOH HOH A . 
E 5 HOH 106 506 84  HOH HOH A . 
E 5 HOH 107 507 129 HOH HOH A . 
E 5 HOH 108 508 23  HOH HOH A . 
E 5 HOH 109 509 15  HOH HOH A . 
E 5 HOH 110 510 206 HOH HOH A . 
E 5 HOH 111 511 31  HOH HOH A . 
E 5 HOH 112 512 24  HOH HOH A . 
E 5 HOH 113 513 163 HOH HOH A . 
E 5 HOH 114 514 16  HOH HOH A . 
E 5 HOH 115 515 96  HOH HOH A . 
E 5 HOH 116 516 182 HOH HOH A . 
E 5 HOH 117 517 216 HOH HOH A . 
E 5 HOH 118 518 230 HOH HOH A . 
E 5 HOH 119 519 130 HOH HOH A . 
E 5 HOH 120 520 190 HOH HOH A . 
E 5 HOH 121 521 100 HOH HOH A . 
E 5 HOH 122 522 171 HOH HOH A . 
E 5 HOH 123 523 33  HOH HOH A . 
E 5 HOH 124 524 198 HOH HOH A . 
E 5 HOH 125 525 200 HOH HOH A . 
E 5 HOH 126 526 114 HOH HOH A . 
E 5 HOH 127 527 81  HOH HOH A . 
E 5 HOH 128 528 160 HOH HOH A . 
E 5 HOH 129 529 177 HOH HOH A . 
E 5 HOH 130 530 51  HOH HOH A . 
E 5 HOH 131 531 141 HOH HOH A . 
E 5 HOH 132 532 126 HOH HOH A . 
E 5 HOH 133 533 133 HOH HOH A . 
E 5 HOH 134 534 140 HOH HOH A . 
E 5 HOH 135 535 22  HOH HOH A . 
E 5 HOH 136 536 26  HOH HOH A . 
E 5 HOH 137 537 86  HOH HOH A . 
E 5 HOH 138 538 73  HOH HOH A . 
E 5 HOH 139 539 187 HOH HOH A . 
E 5 HOH 140 540 62  HOH HOH A . 
E 5 HOH 141 541 122 HOH HOH A . 
E 5 HOH 142 542 152 HOH HOH A . 
E 5 HOH 143 543 227 HOH HOH A . 
E 5 HOH 144 544 197 HOH HOH A . 
E 5 HOH 145 545 35  HOH HOH A . 
E 5 HOH 146 546 229 HOH HOH A . 
E 5 HOH 147 547 185 HOH HOH A . 
E 5 HOH 148 548 94  HOH HOH A . 
E 5 HOH 149 549 144 HOH HOH A . 
E 5 HOH 150 550 56  HOH HOH A . 
E 5 HOH 151 551 208 HOH HOH A . 
E 5 HOH 152 552 91  HOH HOH A . 
E 5 HOH 153 553 66  HOH HOH A . 
E 5 HOH 154 554 72  HOH HOH A . 
E 5 HOH 155 555 107 HOH HOH A . 
E 5 HOH 156 556 102 HOH HOH A . 
E 5 HOH 157 557 137 HOH HOH A . 
E 5 HOH 158 558 179 HOH HOH A . 
E 5 HOH 159 559 217 HOH HOH A . 
E 5 HOH 160 560 48  HOH HOH A . 
E 5 HOH 161 561 50  HOH HOH A . 
E 5 HOH 162 562 95  HOH HOH A . 
E 5 HOH 163 563 30  HOH HOH A . 
E 5 HOH 164 564 6   HOH HOH A . 
E 5 HOH 165 565 21  HOH HOH A . 
E 5 HOH 166 566 103 HOH HOH A . 
E 5 HOH 167 567 41  HOH HOH A . 
E 5 HOH 168 568 157 HOH HOH A . 
E 5 HOH 169 569 170 HOH HOH A . 
E 5 HOH 170 570 143 HOH HOH A . 
E 5 HOH 171 571 202 HOH HOH A . 
E 5 HOH 172 572 175 HOH HOH A . 
E 5 HOH 173 573 199 HOH HOH A . 
E 5 HOH 174 574 113 HOH HOH A . 
E 5 HOH 175 575 174 HOH HOH A . 
E 5 HOH 176 576 158 HOH HOH A . 
E 5 HOH 177 577 203 HOH HOH A . 
E 5 HOH 178 578 79  HOH HOH A . 
E 5 HOH 179 579 189 HOH HOH A . 
E 5 HOH 180 580 212 HOH HOH A . 
E 5 HOH 181 581 183 HOH HOH A . 
E 5 HOH 182 582 146 HOH HOH A . 
E 5 HOH 183 583 119 HOH HOH A . 
E 5 HOH 184 584 186 HOH HOH A . 
E 5 HOH 185 585 49  HOH HOH A . 
E 5 HOH 186 586 82  HOH HOH A . 
E 5 HOH 187 587 155 HOH HOH A . 
E 5 HOH 188 588 181 HOH HOH A . 
E 5 HOH 189 589 223 HOH HOH A . 
E 5 HOH 190 590 64  HOH HOH A . 
E 5 HOH 191 591 188 HOH HOH A . 
E 5 HOH 192 592 204 HOH HOH A . 
E 5 HOH 193 593 180 HOH HOH A . 
E 5 HOH 194 594 161 HOH HOH A . 
E 5 HOH 195 595 166 HOH HOH A . 
E 5 HOH 196 596 228 HOH HOH A . 
E 5 HOH 197 597 210 HOH HOH A . 
E 5 HOH 198 598 97  HOH HOH A . 
E 5 HOH 199 599 205 HOH HOH A . 
E 5 HOH 200 600 159 HOH HOH A . 
E 5 HOH 201 601 154 HOH HOH A . 
E 5 HOH 202 602 221 HOH HOH A . 
E 5 HOH 203 603 222 HOH HOH A . 
E 5 HOH 204 604 67  HOH HOH A . 
E 5 HOH 205 605 71  HOH HOH A . 
E 5 HOH 206 606 85  HOH HOH A . 
E 5 HOH 207 607 87  HOH HOH A . 
E 5 HOH 208 608 211 HOH HOH A . 
E 5 HOH 209 609 201 HOH HOH A . 
E 5 HOH 210 610 192 HOH HOH A . 
E 5 HOH 211 611 162 HOH HOH A . 
E 5 HOH 212 612 149 HOH HOH A . 
E 5 HOH 213 613 191 HOH HOH A . 
E 5 HOH 214 614 118 HOH HOH A . 
E 5 HOH 215 615 172 HOH HOH A . 
E 5 HOH 216 616 65  HOH HOH A . 
E 5 HOH 217 617 132 HOH HOH A . 
E 5 HOH 218 618 213 HOH HOH A . 
E 5 HOH 219 619 196 HOH HOH A . 
E 5 HOH 220 620 224 HOH HOH A . 
E 5 HOH 221 621 215 HOH HOH A . 
E 5 HOH 222 622 111 HOH HOH A . 
E 5 HOH 223 623 148 HOH HOH A . 
E 5 HOH 224 624 53  HOH HOH A . 
E 5 HOH 225 625 106 HOH HOH A . 
E 5 HOH 226 626 110 HOH HOH A . 
E 5 HOH 227 627 167 HOH HOH A . 
E 5 HOH 228 628 69  HOH HOH A . 
E 5 HOH 229 629 117 HOH HOH A . 
E 5 HOH 230 630 218 HOH HOH A . 
E 5 HOH 231 631 116 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
3  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
4  1 Y 1 A LYS 45  ? CD  ? A LYS 45  CD  
5  1 Y 1 A LYS 45  ? CE  ? A LYS 45  CE  
6  1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
7  1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
8  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
9  1 Y 1 A LYS 133 ? NZ  ? A LYS 132 NZ  
10 1 Y 1 A LYS 168 ? NZ  ? A LYS 167 NZ  
11 1 Y 1 A LYS 172 ? CE  ? A LYS 171 CE  
12 1 Y 1 A LYS 172 ? NZ  ? A LYS 171 NZ  
13 1 Y 1 A LYS 213 ? CE  ? A LYS 212 CE  
14 1 Y 1 A LYS 213 ? NZ  ? A LYS 212 NZ  
15 1 Y 1 A LEU 224 ? CD1 ? A LEU 223 CD1 
16 1 Y 1 A LYS 225 ? CD  ? A LYS 224 CD  
17 1 Y 1 A LYS 225 ? CE  ? A LYS 224 CE  
18 1 Y 1 A LYS 225 ? NZ  ? A LYS 224 NZ  
19 1 Y 1 A LYS 228 ? NZ  ? A LYS 227 NZ  
20 1 Y 1 A GLN 255 ? CD  ? A GLN 254 CD  
21 1 Y 1 A GLN 255 ? OE1 ? A GLN 254 OE1 
22 1 Y 1 A GLN 255 ? NE2 ? A GLN 254 NE2 
23 1 Y 1 A LYS 257 ? CD  ? A LYS 256 CD  
24 1 Y 1 A LYS 257 ? CE  ? A LYS 256 CE  
25 1 Y 1 A LYS 257 ? NZ  ? A LYS 256 NZ  
26 1 Y 1 A LYS 261 ? CG  ? A LYS 260 CG  
27 1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
28 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
29 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.22   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.020 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6YH4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.980 
_cell.length_a_esd                 ? 
_cell.length_b                     40.995 
_cell.length_b_esd                 ? 
_cell.length_c                     71.374 
_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                         6YH4 
_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                   6YH4 
_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            2.04 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.68 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-23 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.976300 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976300 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6YH4 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.300 
_reflns.d_resolution_low                 40.995 
_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                       57383 
_reflns.number_obs                       57383 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             98.700 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.700 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.049 
_reflns.pdbx_netI_over_av_sigmaI         7.800 
_reflns.pdbx_netI_over_sigmaI            16.500 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.058 
_reflns.pdbx_Rpim_I_all                  0.022 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         385099 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
1.300 1.370  ? 1.800  54121 ? ? ? 8156 96.800 ? ? ? ? 0.406 ? ? ? ? ? ? ? ? 6.600 0.406 ? ? 4.300  0.477 0.182 ? 1  1 ? ? ? 
1.370 1.450  ? 2.600  51862 ? ? ? 7838 98.100 ? ? ? ? 0.280 ? ? ? ? ? ? ? ? 6.600 0.280 ? ? 5.800  0.330 0.126 ? 2  1 ? ? ? 
1.450 1.550  ? 4.100  48399 ? ? ? 7443 98.800 ? ? ? ? 0.174 ? ? ? ? ? ? ? ? 6.500 0.174 ? ? 8.100  0.207 0.080 ? 3  1 ? ? ? 
1.550 1.680  ? 5.800  46737 ? ? ? 6889 98.500 ? ? ? ? 0.122 ? ? ? ? ? ? ? ? 6.800 0.122 ? ? 11.200 0.145 0.055 ? 4  1 ? ? ? 
1.680 1.840  ? 8.200  44118 ? ? ? 6420 99.600 ? ? ? ? 0.082 ? ? ? ? ? ? ? ? 6.900 0.082 ? ? 15.600 0.098 0.037 ? 5  1 ? ? ? 
1.840 2.060  ? 11.300 39534 ? ? ? 5788 99.300 ? ? ? ? 0.059 ? ? ? ? ? ? ? ? 6.800 0.059 ? ? 21.700 0.070 0.027 ? 6  1 ? ? ? 
2.060 2.370  ? 13.500 34958 ? ? ? 5147 99.500 ? ? ? ? 0.048 ? ? ? ? ? ? ? ? 6.800 0.048 ? ? 27.700 0.057 0.022 ? 7  1 ? ? ? 
2.370 2.910  ? 15.100 30164 ? ? ? 4376 99.800 ? ? ? ? 0.041 ? ? ? ? ? ? ? ? 6.900 0.041 ? ? 32.700 0.050 0.019 ? 8  1 ? ? ? 
2.910 4.110  ? 17.200 22030 ? ? ? 3414 99.800 ? ? ? ? 0.035 ? ? ? ? ? ? ? ? 6.500 0.035 ? ? 39.200 0.041 0.016 ? 9  1 ? ? ? 
4.110 40.995 ? 16.300 13176 ? ? ? 1912 99.300 ? ? ? ? 0.032 ? ? ? ? ? ? ? ? 6.900 0.032 ? ? 42.500 0.038 0.014 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            0.2500 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            -0.1900 
_refine.aniso_B[2][2]                            -0.7800 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            0.5600 
_refine.B_iso_max                                88.130 
_refine.B_iso_mean                               19.7360 
_refine.B_iso_min                                6.180 
_refine.correlation_coeff_Fo_to_Fc               0.9790 
_refine.correlation_coeff_Fo_to_Fc_free          0.9720 
_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                                 6YH4 
_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                            1.3000 
_refine.ls_d_res_low                             39.5400 
_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                     51473 
_refine.ls_number_reflns_R_free                  5895 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.6400 
_refine.ls_percent_reflns_R_free                 10.3000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1354 
_refine.ls_R_factor_R_free                       0.1658 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1318 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4Q09 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0500 
_refine.pdbx_overall_ESU_R_Free                  0.0480 
_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             0.0505 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.3000 
_refine_hist.d_res_low                        39.5400 
_refine_hist.number_atoms_solvent             231 
_refine_hist.number_atoms_total               2287 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       257 
_refine_hist.pdbx_B_iso_mean_ligand           22.69 
_refine_hist.pdbx_B_iso_mean_solvent          33.12 
_refine_hist.pdbx_number_atoms_protein        2014 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.023  0.012  2237 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.173  1.660  3071 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.018  5.000  283  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 37.102 23.889 108  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.368 15.000 351  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 18.802 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.140  0.200  275  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.020  1777 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 6.268  3.000  2237 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 27.631 5.000  150  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 16.603 5.000  2244 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.3000 
_refine_ls_shell.d_res_low                        1.3340 
_refine_ls_shell.number_reflns_all                4136 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             460 
_refine_ls_shell.number_reflns_R_work             3676 
_refine_ls_shell.percent_reflns_obs               96.6100 
_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                  0.2440 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1870 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     6YH4 
_struct.title                        
'Crystal structure of chimeric carbonic anhydrase XII with 2,3,5,6-Tetrafluoro-4-(propylthio)benzenesulfonamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6YH4 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_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              6YH4 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 6YH4 SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6YH4 LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6YH4 THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 6YH4 ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 4 
1 6YH4 SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 5 
1 6YH4 ASN A 203 ? UNP P00918 LEU 203 'engineered mutation' 204 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 230   ? 
1 MORE         2     ? 
1 'SSA (A^2)'  11160 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? SER A 134 ? ASP A 130 SER A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? ASP A 161 ? LEU A 157 ASP A 162 1 ? 6 
HELX_P HELX_P7 AA7 VAL A 162 ? LYS A 167 ? VAL A 163 LYS A 168 5 ? 6 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.970 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V13 . N10 A ? A ZN  301 A V13 302 1_555 ? ? ? ? ? ? ? 1.962 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V13 . N10 B ? A ZN  301 A V13 302 1_555 ? ? ? ? ? ? ? 1.969 ? ? 
metalc6 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V13 . S7  B ? A ZN  301 A V13 302 1_555 ? ? ? ? ? ? ? 2.974 ? ? 
# 
_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_555 103.9 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 112.0 ? 
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_555 100.1 ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C V13 .   ? A V13 302 ? 1_555 110.2 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C V13 .   ? A V13 302 ? 1_555 113.4 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C V13 .   ? A V13 302 ? 1_555 116.2 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V13 .   ? A V13 302 ? 1_555 116.7 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V13 .   ? A V13 302 ? 1_555 110.8 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V13 .   ? A V13 302 ? 1_555 111.7 ? 
10 N10 A C V13 .   ? A V13 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V13 .   ? A V13 302 ? 1_555 6.5   ? 
11 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B C V13 .   ? A V13 302 ? 1_555 98.2  ? 
12 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B C V13 .   ? A V13 302 ? 1_555 141.9 ? 
13 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B C V13 .   ? A V13 302 ? 1_555 99.7  ? 
14 N10 A C V13 .   ? A V13 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B C V13 .   ? A V13 302 ? 1_555 28.7  ? 
15 N10 B C V13 .   ? A V13 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B C V13 .   ? A V13 302 ? 1_555 31.2  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -3.78 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 13.05 
# 
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 VAL A 121 ? O VAL A 121 N THR A 91  ? N THR A 91  
AA2 7 8  O THR A 91  ? O THR A 91  N PHE A 70  ? N PHE A 70  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 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 THR A 91  ? N THR A 91  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A V13 302 ? 17 'binding site for residue V13 A 302' 
AC3 Software A DMS 303 ? 4  'binding site for residue DMS A 303' 
# 
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  V13 C .   ? V13 A 302 . ? 1_555 ? 
5  AC2 17 HIS A 64  ? HIS A 64  . ? 1_555 ? 
6  AC2 17 LYS A 67  ? LYS A 67  . ? 1_555 ? 
7  AC2 17 GLN A 92  ? GLN A 92  . ? 1_555 ? 
8  AC2 17 HIS A 94  ? HIS A 94  . ? 1_555 ? 
9  AC2 17 HIS A 96  ? HIS A 96  . ? 1_555 ? 
10 AC2 17 HIS A 119 ? HIS A 119 . ? 1_555 ? 
11 AC2 17 VAL A 121 ? VAL A 121 . ? 1_555 ? 
12 AC2 17 ALA A 130 ? ALA A 131 . ? 1_555 ? 
13 AC2 17 LEU A 197 ? LEU A 198 . ? 1_555 ? 
14 AC2 17 THR A 198 ? THR A 199 . ? 1_555 ? 
15 AC2 17 THR A 199 ? THR A 200 . ? 1_555 ? 
16 AC2 17 PRO A 200 ? PRO A 201 . ? 1_555 ? 
17 AC2 17 PRO A 201 ? PRO A 202 . ? 1_555 ? 
18 AC2 17 TRP A 208 ? TRP A 209 . ? 1_555 ? 
19 AC2 17 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
20 AC2 17 HOH E .   ? HOH A 463 . ? 1_555 ? 
21 AC2 17 HOH E .   ? HOH A 560 . ? 1_555 ? 
22 AC3 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
23 AC3 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
24 AC3 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
25 AC3 4  HOH E .   ? HOH A 543 . ? 1_555 ? 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A HIS 36  ? ? CD2 A HIS 36  ? ? 1.419 1.354 0.065 0.009 N 
2 1 CG A ASP 175 ? B OD2 A ASP 175 ? ? 1.487 1.249 0.238 0.023 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              175 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              175 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              175 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                123.08 
_pdbx_validate_rmsd_angle.angle_target_value         110.40 
_pdbx_validate_rmsd_angle.angle_deviation            12.68 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.00 
_pdbx_validate_rmsd_angle.linker_flag                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 ASN A 11  ? ? -140.19 17.10   
2  1 ARG A 27  ? ? -142.68 53.11   
3  1 ASP A 75  ? B -67.83  86.82   
4  1 LYS A 76  ? ? -96.33  -104.74 
5  1 LYS A 76  ? ? -118.00 -104.74 
6  1 GLU A 106 ? ? -90.54  -61.29  
7  1 LYS A 111 ? ? 74.80   -1.86   
8  1 PHE A 176 ? ? -154.53 78.34   
9  1 PHE A 176 ? ? -160.81 78.34   
10 1 ASN A 244 ? ? -94.93  48.97   
11 1 LYS A 252 ? ? 56.14   -135.15 
12 1 ASN A 253 ? ? -92.80  49.21   
# 
_pdbx_entry_details.entry_id                 6YH4 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
THR N    N  N N 314 
THR CA   C  N S 315 
THR C    C  N N 316 
THR O    O  N N 317 
THR CB   C  N R 318 
THR OG1  O  N N 319 
THR CG2  C  N N 320 
THR OXT  O  N N 321 
THR H    H  N N 322 
THR H2   H  N N 323 
THR HA   H  N N 324 
THR HB   H  N N 325 
THR HG1  H  N N 326 
THR HG21 H  N N 327 
THR HG22 H  N N 328 
THR HG23 H  N N 329 
THR HXT  H  N N 330 
TRP N    N  N N 331 
TRP CA   C  N S 332 
TRP C    C  N N 333 
TRP O    O  N N 334 
TRP CB   C  N N 335 
TRP CG   C  Y N 336 
TRP CD1  C  Y N 337 
TRP CD2  C  Y N 338 
TRP NE1  N  Y N 339 
TRP CE2  C  Y N 340 
TRP CE3  C  Y N 341 
TRP CZ2  C  Y N 342 
TRP CZ3  C  Y N 343 
TRP CH2  C  Y N 344 
TRP OXT  O  N N 345 
TRP H    H  N N 346 
TRP H2   H  N N 347 
TRP HA   H  N N 348 
TRP HB2  H  N N 349 
TRP HB3  H  N N 350 
TRP HD1  H  N N 351 
TRP HE1  H  N N 352 
TRP HE3  H  N N 353 
TRP HZ2  H  N N 354 
TRP HZ3  H  N N 355 
TRP HH2  H  N N 356 
TRP HXT  H  N N 357 
TYR N    N  N N 358 
TYR CA   C  N S 359 
TYR C    C  N N 360 
TYR O    O  N N 361 
TYR CB   C  N N 362 
TYR CG   C  Y N 363 
TYR CD1  C  Y N 364 
TYR CD2  C  Y N 365 
TYR CE1  C  Y N 366 
TYR CE2  C  Y N 367 
TYR CZ   C  Y N 368 
TYR OH   O  N N 369 
TYR OXT  O  N N 370 
TYR H    H  N N 371 
TYR H2   H  N N 372 
TYR HA   H  N N 373 
TYR HB2  H  N N 374 
TYR HB3  H  N N 375 
TYR HD1  H  N N 376 
TYR HD2  H  N N 377 
TYR HE1  H  N N 378 
TYR HE2  H  N N 379 
TYR HH   H  N N 380 
TYR HXT  H  N N 381 
V13 O20  O  N N 382 
V13 S15  S  N N 383 
V13 O19  O  N N 384 
V13 C16  C  N N 385 
V13 C17  C  N N 386 
V13 O18  O  N N 387 
V13 C1   C  Y N 388 
V13 C6   C  Y N 389 
V13 F11  F  N N 390 
V13 C5   C  Y N 391 
V13 F12  F  N N 392 
V13 C4   C  Y N 393 
V13 S7   S  N N 394 
V13 O9   O  N N 395 
V13 N10  N  N N 396 
V13 O8   O  N N 397 
V13 C3   C  Y N 398 
V13 F13  F  N N 399 
V13 C2   C  Y N 400 
V13 F14  F  N N 401 
V13 H1   H  N N 402 
V13 H2   H  N N 403 
V13 H3   H  N N 404 
V13 H4   H  N N 405 
V13 H5   H  N N 406 
V13 H6   H  N N 407 
V13 H7   H  N N 408 
VAL N    N  N N 409 
VAL CA   C  N S 410 
VAL C    C  N N 411 
VAL O    O  N N 412 
VAL CB   C  N N 413 
VAL CG1  C  N N 414 
VAL CG2  C  N N 415 
VAL OXT  O  N N 416 
VAL H    H  N N 417 
VAL H2   H  N N 418 
VAL HA   H  N N 419 
VAL HB   H  N N 420 
VAL HG11 H  N N 421 
VAL HG12 H  N N 422 
VAL HG13 H  N N 423 
VAL HG21 H  N N 424 
VAL HG22 H  N N 425 
VAL HG23 H  N N 426 
VAL HXT  H  N N 427 
ZN  ZN   ZN N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
V13 C17 C16  sing N N 367 
V13 C17 O18  sing N N 368 
V13 F11 C6   sing N N 369 
V13 O20 S15  doub N N 370 
V13 C16 S15  sing N N 371 
V13 S15 C1   sing N N 372 
V13 S15 O19  doub N N 373 
V13 F12 C5   sing N N 374 
V13 C6  C5   doub Y N 375 
V13 C6  C1   sing Y N 376 
V13 C5  C4   sing Y N 377 
V13 C1  C2   doub Y N 378 
V13 C2  F14  sing N N 379 
V13 C2  C3   sing Y N 380 
V13 C4  C3   doub Y N 381 
V13 C4  S7   sing N N 382 
V13 O8  S7   doub N N 383 
V13 O9  S7   doub N N 384 
V13 C3  F13  sing N N 385 
V13 S7  N10  sing N N 386 
V13 C16 H1   sing N N 387 
V13 C16 H2   sing N N 388 
V13 C17 H3   sing N N 389 
V13 C17 H4   sing N N 390 
V13 O18 H5   sing N N 391 
V13 N10 H6   sing N N 392 
V13 N10 H7   sing N N 393 
VAL N   CA   sing N N 394 
VAL N   H    sing N N 395 
VAL N   H2   sing N N 396 
VAL CA  C    sing N N 397 
VAL CA  CB   sing N N 398 
VAL CA  HA   sing N N 399 
VAL C   O    doub N N 400 
VAL C   OXT  sing N N 401 
VAL CB  CG1  sing N N 402 
VAL CB  CG2  sing N N 403 
VAL CB  HB   sing N N 404 
VAL CG1 HG11 sing N N 405 
VAL CG1 HG12 sing N N 406 
VAL CG1 HG13 sing N N 407 
VAL CG2 HG21 sing N N 408 
VAL CG2 HG22 sing N N 409 
VAL CG2 HG23 sing N N 410 
VAL OXT HXT  sing N N 411 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        V13 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   V13 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4Q09 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6YH4 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.023821 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005948 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024393 
_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]   0.014441 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 11.054  -0.343  7.612   1.00 47.52 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.069  0.241   8.482   1.00 48.85 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.538   -0.870  9.390   1.00 33.06 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.945   -2.021  9.315   1.00 34.76 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 9.056   0.994   7.628   1.00 43.28 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 8.599   2.186   8.389   1.00 57.56 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 9.252   2.635   9.521   1.00 61.95 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 7.561   3.027   8.192   1.00 78.32 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 8.635   3.701   9.989   1.00 76.39 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 7.593   3.962   9.190   1.00 85.21 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.581   -0.520  10.221  1.00 23.28 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.953   -1.466  11.146  1.00 20.59 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.947   -2.330  10.388  1.00 19.86 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.410   -1.940  9.364   1.00 20.68 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.288   -0.784  12.356  1.00 20.10 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 6.090   0.006   11.972  1.00 16.94 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 6.057   1.319   11.624  1.00 20.07 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.747   -0.483  11.877  1.00 15.94 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.773   1.728   11.390  1.00 18.38 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.947   0.631   11.525  1.00 17.66 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 4.141   -1.721  12.185  1.00 15.52 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.566   0.513   11.402  1.00 18.42 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.757   -1.821  12.058  1.00 16.71 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.999   -0.720  11.673  1.00 16.84 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.701   -3.522  10.922  1.00 17.98 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.714   -4.420  10.344  1.00 19.58 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.416   -5.529  11.334  1.00 17.77 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.404   -5.301  12.532  1.00 16.09 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 5.127   -6.726  10.805  1.00 18.93 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.680   -7.848  11.617  1.00 18.46 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.610   -9.064  11.492  1.00 22.46 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.304   -10.125 12.085  1.00 26.92 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.204   -8.179  11.345  1.00 17.11 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.290   -7.082  11.835  1.00 14.33 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.941   -7.059  13.200  1.00 13.85 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.835   -6.062  11.001  1.00 15.18 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 1.052   -6.085  13.674  1.00 13.08 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.954   -5.080  11.444  1.00 14.23 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.591   -5.105  12.807  1.00 12.62 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.248  -4.144  13.271  1.00 13.66 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.739   -8.890  10.777  1.00 22.74 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.700   -9.968  10.533  1.00 25.51 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.676   -10.238 11.685  1.00 28.27 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.798   -9.507  12.676  1.00 26.55 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.506   -11.262 11.467  1.00 26.46 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.537  -11.694 12.398  1.00 31.08 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.479  -10.532 12.696  1.00 23.02 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.924  -10.385 13.848  1.00 23.35 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.285  -12.885 11.800  1.00 34.90 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.388  -13.433 12.680  1.00 36.07 ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? 11.835  -9.748  11.656  1.00 26.22 ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? 12.866  -8.753  11.877  1.00 26.13 ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? 12.300  -7.371  12.069  1.00 24.01 ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? 13.108  -6.518  12.453  1.00 23.91 ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? 13.929  -8.702  10.792  1.00 22.41 ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? 14.588  -10.031 10.623  1.00 24.27 ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? 15.584  -10.549 11.462  1.00 25.45 ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? 14.239  -10.992 9.772   1.00 24.81 ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? 15.835  -11.790 11.087  1.00 24.43 ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? 15.032  -12.064 9.995   1.00 25.77 ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? 10.962  -7.158  11.928  1.00 22.94 ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? 10.449  -5.806  12.187  1.00 18.54 ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? 9.122   -5.797  12.926  1.00 18.28 ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? 8.471   -4.752  12.964  1.00 17.49 ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? 10.255  -5.036  10.883  1.00 19.39 ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? 9.248   -5.673  9.937   1.00 20.27 ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? 8.596   -6.670  10.271  1.00 24.44 ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? 8.991   -5.051  8.800   1.00 26.72 ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? 8.783   -6.944  13.545  1.00 18.55 ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? 7.476   -7.091  14.185  1.00 17.07 ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? 7.487   -6.559  15.595  1.00 14.91 ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? 8.375   -5.800  16.009  1.00 16.57 ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? 6.372   -6.852  16.306  1.00 14.55 ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? 6.132   -6.299  17.632  1.00 14.18 ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? 7.284   -6.270  18.603  1.00 14.89 ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? 7.380   -5.294  19.358  1.00 16.99 ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? 4.938   -7.089  18.150  1.00 15.97 ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? 4.183   -7.382  16.882  1.00 14.97 ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? 5.204   -7.556  15.768  1.00 15.40 ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? 8.137   -7.301  18.587  1.00 15.19 ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? 9.237   -7.338  19.537  1.00 17.67 ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? 10.349  -6.332  19.198  1.00 15.29 ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? 11.231  -6.138  20.031  1.00 17.99 ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? 9.809   -8.766  19.611  1.00 22.36 ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? 8.788   -9.809  20.026  1.00 28.80 ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? 7.930   -9.495  21.248  1.00 40.27 ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? 8.507   -9.383  22.343  1.00 53.53 ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? 6.663   -9.380  21.110  1.00 43.04 ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? 10.312  -5.756  17.994  1.00 15.36 ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? 11.308  -4.775  17.573  1.00 15.86 ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? 10.803  -3.335  17.717  1.00 15.49 ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? 11.634  -2.413  17.676  1.00 16.23 ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? 11.586  -4.965  16.068  1.00 17.79 ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? 12.332  -6.212  15.798  1.00 18.45 ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? 13.748  -6.277  15.887  1.00 21.04 ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? 11.881  -7.471  15.530  1.00 22.49 ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? 14.111  -7.516  15.639  1.00 26.13 ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? 13.013  -8.254  15.382  1.00 23.93 ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? 9.483   -3.136  17.901  1.00 14.74 ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? 8.954   -1.798  17.760  1.00 14.07 ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? 9.515   -0.822  18.794  1.00 13.46 ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? 9.625   0.371   18.522  1.00 15.00 ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? 7.428   -1.841  17.918  1.00 13.60 ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? 6.775   -2.523  16.772  1.00 12.33 ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? 7.304   -2.946  15.599  1.00 14.54 ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? 5.353   -2.855  16.716  1.00 11.40 ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? 6.347   -3.541  14.834  1.00 13.08 ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? 5.130   -3.497  15.485  1.00 12.60 ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? 4.295   -2.723  17.624  1.00 11.91 ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? 3.846   -3.945  15.108  1.00 12.85 ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? 3.056   -3.176  17.235  1.00 12.37 ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? 2.825   -3.773  16.026  1.00 12.76 ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? 9.886   -1.323  19.983  1.00 14.66 ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? 10.385  -0.459  21.041  1.00 16.18 ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? 11.633  0.314   20.579  1.00 16.75 ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? 11.894  1.353   21.171  1.00 18.32 ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? 10.651  -1.253  22.335  1.00 16.13 ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? 11.888  -2.094  22.231  1.00 18.09 ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? 13.116  -1.658  22.739  1.00 19.96 ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? 12.110  -3.259  21.578  1.00 17.50 ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? 13.996  -2.598  22.478  1.00 20.81 ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? 13.435  -3.580  21.771  1.00 18.67 ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? 12.408  -0.195  19.597  1.00 17.05 ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? 13.593  0.542   19.251  1.00 19.07 ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? 13.277  1.885   18.606  1.00 21.04 ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? 13.967  2.857   18.868  1.00 26.96 ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? 14.488  -0.306  18.351  1.00 19.64 ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? 15.064  -1.522  19.058  1.00 22.16 ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? 15.774  -2.460  18.145  1.00 20.42 ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? 14.842  -3.453  17.515  1.00 20.50 ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? 15.507  -4.219  16.442  1.00 19.51 ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 19  ? 12.285  1.950   17.750  1.00 19.54 ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 19  ? 11.862  3.234   17.200  1.00 20.48 ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 19  ? 10.827  3.934   18.056  1.00 20.40 ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 19  ? 10.677  5.130   17.938  1.00 22.43 ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 19  ? 11.351  3.106   15.780  1.00 23.48 ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 19  ? 12.415  3.039   14.748  1.00 29.85 ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 19  ? 13.469  3.688   14.947  1.00 30.97 ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 19  ? 12.195  2.283   13.817  1.00 51.70 ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 20  ? 10.104  3.180   18.875  1.00 16.84 ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 20  ? 8.964   3.735   19.583  1.00 17.39 ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 20  ? 9.057   3.243   21.018  1.00 16.98 ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 20  ? 8.412   2.242   21.403  1.00 15.90 ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 20  ? 7.614   3.297   18.952  1.00 18.39 ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 20  ? 7.547   3.652   17.477  1.00 18.14 ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 20  ? 7.234   4.934   17.075  1.00 21.58 ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 20  ? 7.923   2.745   16.486  1.00 18.89 ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 20  ? 7.207   5.261   15.715  1.00 19.86 ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 20  ? 7.969   3.073   15.133  1.00 20.34 ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 20  ? 7.610   4.348   14.762  1.00 21.46 ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 21  ? 9.900   3.877   21.839  1.00 17.33 ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 21  ? 10.172  3.362   23.195  1.00 18.32 ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 21  ? 8.938   3.249   24.103  1.00 17.70 ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 21  ? 8.999   2.461   25.059  1.00 18.74 ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 21  ? 11.202  4.308   23.822  1.00 24.66 ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 21  ? 11.525  5.323   22.765  1.00 30.62 ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 21  ? 10.819  4.975   21.470  1.00 23.33 ? 21  PRO A CD  1 
ATOM   158  N  N   A ILE A 1 22  ? 7.853   3.987   23.797  0.50 16.90 ? 22  ILE A N   1 
ATOM   159  N  N   B ILE A 1 22  ? 7.848   3.991   23.808  0.50 17.43 ? 22  ILE A N   1 
ATOM   160  C  CA  A ILE A 1 22  ? 6.611   3.854   24.544  0.50 16.88 ? 22  ILE A CA  1 
ATOM   161  C  CA  B ILE A 1 22  ? 6.610   3.848   24.565  0.50 17.68 ? 22  ILE A CA  1 
ATOM   162  C  C   A ILE A 1 22  ? 6.041   2.434   24.421  0.50 14.54 ? 22  ILE A C   1 
ATOM   163  C  C   B ILE A 1 22  ? 6.044   2.428   24.427  0.50 15.08 ? 22  ILE A C   1 
ATOM   164  O  O   A ILE A 1 22  ? 5.138   2.111   25.172  0.50 15.26 ? 22  ILE A O   1 
ATOM   165  O  O   B ILE A 1 22  ? 5.145   2.096   25.177  0.50 15.94 ? 22  ILE A O   1 
ATOM   166  C  CB  A ILE A 1 22  ? 5.604   4.927   24.097  0.50 16.26 ? 22  ILE A CB  1 
ATOM   167  C  CB  B ILE A 1 22  ? 5.584   4.931   24.173  0.50 15.93 ? 22  ILE A CB  1 
ATOM   168  C  CG1 A ILE A 1 22  ? 4.591   5.278   25.184  0.50 16.12 ? 22  ILE A CG1 1 
ATOM   169  C  CG1 B ILE A 1 22  ? 4.523   5.180   25.249  0.50 19.46 ? 22  ILE A CG1 1 
ATOM   170  C  CG2 A ILE A 1 22  ? 4.963   4.511   22.767  0.50 16.22 ? 22  ILE A CG2 1 
ATOM   171  C  CG2 B ILE A 1 22  ? 4.987   4.611   22.801  0.50 17.64 ? 22  ILE A CG2 1 
ATOM   172  C  CD1 A ILE A 1 22  ? 3.621   6.346   24.767  0.50 17.78 ? 22  ILE A CD1 1 
ATOM   173  C  CD1 B ILE A 1 22  ? 5.034   5.800   26.551  0.50 21.44 ? 22  ILE A CD1 1 
ATOM   174  N  N   . ALA A 1 23  ? 6.567   1.603   23.497  1.00 13.71 ? 23  ALA A N   1 
ATOM   175  C  CA  . ALA A 1 23  ? 6.162   0.213   23.401  1.00 13.53 ? 23  ALA A CA  1 
ATOM   176  C  C   . ALA A 1 23  ? 6.260   -0.498  24.738  1.00 13.74 ? 23  ALA A C   1 
ATOM   177  O  O   . ALA A 1 23  ? 5.557   -1.502  24.938  1.00 15.06 ? 23  ALA A O   1 
ATOM   178  C  CB  . ALA A 1 23  ? 6.970   -0.526  22.345  1.00 13.87 ? 23  ALA A CB  1 
ATOM   179  N  N   . LYS A 1 24  ? 7.169   -0.026  25.622  1.00 15.89 ? 24  LYS A N   1 
ATOM   180  C  CA  . LYS A 1 24  ? 7.360   -0.643  26.926  1.00 15.86 ? 24  LYS A CA  1 
ATOM   181  C  C   . LYS A 1 24  ? 6.744   0.214   28.023  1.00 17.25 ? 24  LYS A C   1 
ATOM   182  O  O   . LYS A 1 24  ? 7.100   0.157   29.210  1.00 20.47 ? 24  LYS A O   1 
ATOM   183  C  CB  . LYS A 1 24  ? 8.841   -0.887  27.221  1.00 18.92 ? 24  LYS A CB  1 
ATOM   184  C  CG  . LYS A 1 24  ? 9.500   -1.863  26.253  1.00 20.08 ? 24  LYS A CG  1 
ATOM   185  C  CD  . LYS A 1 24  ? 10.928  -2.144  26.689  1.00 27.00 ? 24  LYS A CD  1 
ATOM   186  C  CE  . LYS A 1 24  ? 11.601  -3.021  25.675  1.00 24.78 ? 24  LYS A CE  1 
ATOM   187  N  NZ  . LYS A 1 24  ? 11.157  -4.419  25.907  1.00 31.64 ? 24  LYS A NZ  1 
ATOM   188  N  N   . GLY A 1 25  ? 5.729   0.983   27.642  1.00 17.26 ? 25  GLY A N   1 
ATOM   189  C  CA  . GLY A 1 25  ? 5.108   1.943   28.536  1.00 19.75 ? 25  GLY A CA  1 
ATOM   190  C  C   . GLY A 1 25  ? 4.150   1.295   29.521  1.00 16.62 ? 25  GLY A C   1 
ATOM   191  O  O   . GLY A 1 25  ? 3.973   0.063   29.589  1.00 17.82 ? 25  GLY A O   1 
ATOM   192  N  N   . GLU A 1 26  ? 3.484   2.165   30.278  1.00 18.68 ? 26  GLU A N   1 
ATOM   193  C  CA  . GLU A 1 26  ? 2.626   1.766   31.374  1.00 18.73 ? 26  GLU A CA  1 
ATOM   194  C  C   . GLU A 1 26  ? 1.171   1.570   30.963  1.00 16.94 ? 26  GLU A C   1 
ATOM   195  O  O   . GLU A 1 26  ? 0.388   1.026   31.743  1.00 17.84 ? 26  GLU A O   1 
ATOM   196  C  CB  . GLU A 1 26  ? 2.647   2.820   32.522  1.00 23.69 ? 26  GLU A CB  1 
ATOM   197  C  CG  . GLU A 1 26  ? 4.029   3.074   33.100  1.00 32.06 ? 26  GLU A CG  1 
ATOM   198  C  CD  . GLU A 1 26  ? 4.713   1.802   33.611  1.00 37.11 ? 26  GLU A CD  1 
ATOM   199  O  OE1 . GLU A 1 26  ? 4.084   1.065   34.429  1.00 40.29 ? 26  GLU A OE1 1 
ATOM   200  O  OE2 . GLU A 1 26  ? 5.905   1.540   33.203  1.00 50.66 ? 26  GLU A OE2 1 
ATOM   201  N  N   . ARG A 1 27  ? 0.818   1.892   29.716  1.00 12.35 ? 27  ARG A N   1 
ATOM   202  C  CA  . ARG A 1 27  ? -0.585  1.701   29.326  1.00 11.59 ? 27  ARG A CA  1 
ATOM   203  C  C   . ARG A 1 27  ? -0.679  1.213   27.880  1.00 11.60 ? 27  ARG A C   1 
ATOM   204  O  O   . ARG A 1 27  ? -1.384  1.786   27.046  1.00 11.76 ? 27  ARG A O   1 
ATOM   205  C  CB  . ARG A 1 27  ? -1.489  2.903   29.655  1.00 13.69 ? 27  ARG A CB  1 
ATOM   206  C  CG  . ARG A 1 27  ? -1.077  4.212   29.012  1.00 17.20 ? 27  ARG A CG  1 
ATOM   207  C  CD  . ARG A 1 27  ? -2.065  5.397   29.168  1.00 22.86 ? 27  ARG A CD  1 
ATOM   208  N  NE  . ARG A 1 27  ? -3.248  5.355   28.293  1.00 18.87 ? 27  ARG A NE  1 
ATOM   209  C  CZ  . ARG A 1 27  ? -4.182  6.295   28.168  1.00 17.04 ? 27  ARG A CZ  1 
ATOM   210  N  NH1 . ARG A 1 27  ? -4.101  7.408   28.876  1.00 15.76 ? 27  ARG A NH1 1 
ATOM   211  N  NH2 . ARG A 1 27  ? -5.193  6.116   27.337  1.00 18.17 ? 27  ARG A NH2 1 
ATOM   212  N  N   . GLN A 1 28  ? 0.051   0.127   27.597  1.00 11.11 ? 28  GLN A N   1 
ATOM   213  C  CA  . GLN A 1 28  ? 0.057   -0.378  26.204  1.00 10.19 ? 28  GLN A CA  1 
ATOM   214  C  C   . GLN A 1 28  ? -1.091  -1.338  25.968  1.00 9.76  ? 28  GLN A C   1 
ATOM   215  O  O   . GLN A 1 28  ? -1.589  -2.018  26.863  1.00 10.57 ? 28  GLN A O   1 
ATOM   216  C  CB  . GLN A 1 28  ? 1.428   -1.054  26.005  1.00 11.10 ? 28  GLN A CB  1 
ATOM   217  C  CG  . GLN A 1 28  ? 2.544   -0.005  25.907  1.00 11.96 ? 28  GLN A CG  1 
ATOM   218  C  CD  . GLN A 1 28  ? 2.419   0.789   24.617  1.00 11.39 ? 28  GLN A CD  1 
ATOM   219  O  OE1 . GLN A 1 28  ? 2.596   0.250   23.538  1.00 11.44 ? 28  GLN A OE1 1 
ATOM   220  N  NE2 . GLN A 1 28  ? 2.064   2.091   24.690  1.00 12.06 ? 28  GLN A NE2 1 
ATOM   221  N  N   . SER A 1 29  ? -1.467  -1.400  24.688  1.00 9.22  ? 29  SER A N   1 
ATOM   222  C  CA  . SER A 1 29  ? -2.544  -2.279  24.232  1.00 8.99  ? 29  SER A CA  1 
ATOM   223  C  C   . SER A 1 29  ? -2.029  -3.150  23.115  1.00 8.64  ? 29  SER A C   1 
ATOM   224  O  O   . SER A 1 29  ? -1.075  -2.805  22.421  1.00 9.64  ? 29  SER A O   1 
ATOM   225  C  CB  . SER A 1 29  ? -3.661  -1.429  23.682  1.00 9.21  ? 29  SER A CB  1 
ATOM   226  O  OG  . SER A 1 29  ? -4.286  -0.712  24.743  1.00 8.90  ? 29  SER A OG  1 
ATOM   227  N  N   . PRO A 1 30  ? -2.670  -4.292  22.819  1.00 8.52  ? 30  PRO A N   1 
ATOM   228  C  CA  . PRO A 1 30  ? -3.841  -4.858  23.552  1.00 8.91  ? 30  PRO A CA  1 
ATOM   229  C  C   . PRO A 1 30  ? -3.421  -5.501  24.860  1.00 8.20  ? 30  PRO A C   1 
ATOM   230  O  O   . PRO A 1 30  ? -2.226  -5.534  25.188  1.00 9.77  ? 30  PRO A O   1 
ATOM   231  C  CB  . PRO A 1 30  ? -4.365  -5.837  22.512  1.00 9.26  ? 30  PRO A CB  1 
ATOM   232  C  CG  . PRO A 1 30  ? -3.084  -6.426  21.956  1.00 9.27  ? 30  PRO A CG  1 
ATOM   233  C  CD  . PRO A 1 30  ? -2.171  -5.204  21.740  1.00 9.08  ? 30  PRO A CD  1 
ATOM   234  N  N   . VAL A 1 31  ? -4.426  -6.042  25.531  1.00 8.98  ? 31  VAL A N   1 
ATOM   235  C  CA  . VAL A 1 31  ? -4.232  -6.789  26.771  1.00 9.63  ? 31  VAL A CA  1 
ATOM   236  C  C   . VAL A 1 31  ? -5.101  -8.023  26.720  1.00 9.14  ? 31  VAL A C   1 
ATOM   237  O  O   . VAL A 1 31  ? -6.064  -8.051  25.948  1.00 9.78  ? 31  VAL A O   1 
ATOM   238  C  CB  . VAL A 1 31  ? -4.558  -5.962  28.037  1.00 10.20 ? 31  VAL A CB  1 
ATOM   239  C  CG1 . VAL A 1 31  ? -3.632  -4.733  28.111  1.00 12.11 ? 31  VAL A CG1 1 
ATOM   240  C  CG2 . VAL A 1 31  ? -6.042  -5.501  28.038  1.00 11.50 ? 31  VAL A CG2 1 
ATOM   241  N  N   . ASP A 1 32  ? -4.774  -8.997  27.574  1.00 9.76  ? 32  ASP A N   1 
ATOM   242  C  CA  . ASP A 1 32  ? -5.722  -10.067 27.864  1.00 10.47 ? 32  ASP A CA  1 
ATOM   243  C  C   . ASP A 1 32  ? -6.778  -9.522  28.814  1.00 10.42 ? 32  ASP A C   1 
ATOM   244  O  O   . ASP A 1 32  ? -6.459  -8.904  29.844  1.00 13.69 ? 32  ASP A O   1 
ATOM   245  C  CB  . ASP A 1 32  ? -4.986  -11.250 28.475  1.00 11.99 ? 32  ASP A CB  1 
ATOM   246  C  CG  . ASP A 1 32  ? -5.927  -12.400 28.777  1.00 12.51 ? 32  ASP A CG  1 
ATOM   247  O  OD1 . ASP A 1 32  ? -6.642  -12.831 27.817  1.00 12.42 ? 32  ASP A OD1 1 
ATOM   248  O  OD2 . ASP A 1 32  ? -5.954  -12.847 29.955  1.00 16.06 ? 32  ASP A OD2 1 
ATOM   249  N  N   . ILE A 1 33  ? -8.029  -9.824  28.493  1.00 10.21 ? 33  ILE A N   1 
ATOM   250  C  CA  . ILE A 1 33  ? -9.144  -9.434  29.355  1.00 12.09 ? 33  ILE A CA  1 
ATOM   251  C  C   . ILE A 1 33  ? -9.423  -10.674 30.196  1.00 12.20 ? 33  ILE A C   1 
ATOM   252  O  O   . ILE A 1 33  ? -10.002 -11.657 29.727  1.00 13.81 ? 33  ILE A O   1 
ATOM   253  C  CB  . ILE A 1 33  ? -10.340 -8.988  28.533  1.00 12.01 ? 33  ILE A CB  1 
ATOM   254  C  CG1 . ILE A 1 33  ? -9.957  -7.781  27.679  1.00 11.98 ? 33  ILE A CG1 1 
ATOM   255  C  CG2 . ILE A 1 33  ? -11.554 -8.734  29.472  1.00 14.40 ? 33  ILE A CG2 1 
ATOM   256  C  CD1 . ILE A 1 33  ? -10.976 -7.476  26.577  1.00 14.09 ? 33  ILE A CD1 1 
ATOM   257  N  N   A ASP A 1 34  ? -9.065  -10.589 31.484  0.50 14.46 ? 34  ASP A N   1 
ATOM   258  N  N   B ASP A 1 34  ? -9.057  -10.583 31.490  0.50 13.56 ? 34  ASP A N   1 
ATOM   259  C  CA  A ASP A 1 34  ? -9.378  -11.695 32.373  0.50 14.86 ? 34  ASP A CA  1 
ATOM   260  C  CA  B ASP A 1 34  ? -9.383  -11.616 32.465  0.50 14.04 ? 34  ASP A CA  1 
ATOM   261  C  C   A ASP A 1 34  ? -10.757 -11.413 32.975  0.50 14.96 ? 34  ASP A C   1 
ATOM   262  C  C   B ASP A 1 34  ? -10.810 -11.322 32.926  0.50 13.36 ? 34  ASP A C   1 
ATOM   263  O  O   A ASP A 1 34  ? -10.915 -10.520 33.826  0.50 16.83 ? 34  ASP A O   1 
ATOM   264  O  O   B ASP A 1 34  ? -11.059 -10.326 33.622  0.50 15.56 ? 34  ASP A O   1 
ATOM   265  C  CB  A ASP A 1 34  ? -8.266  -11.917 33.391  0.50 19.11 ? 34  ASP A CB  1 
ATOM   266  C  CB  B ASP A 1 34  ? -8.396  -11.577 33.634  0.50 15.41 ? 34  ASP A CB  1 
ATOM   267  C  CG  A ASP A 1 34  ? -8.588  -13.143 34.220  0.50 25.96 ? 34  ASP A CG  1 
ATOM   268  C  CG  B ASP A 1 34  ? -8.664  -12.644 34.684  0.50 15.55 ? 34  ASP A CG  1 
ATOM   269  O  OD1 A ASP A 1 34  ? -8.235  -14.292 33.760  0.50 34.16 ? 34  ASP A OD1 1 
ATOM   270  O  OD1 B ASP A 1 34  ? -9.829  -13.119 34.789  0.50 17.00 ? 34  ASP A OD1 1 
ATOM   271  O  OD2 A ASP A 1 34  ? -9.223  -12.951 35.296  0.50 22.16 ? 34  ASP A OD2 1 
ATOM   272  O  OD2 B ASP A 1 34  ? -7.686  -13.018 35.396  0.50 21.30 ? 34  ASP A OD2 1 
ATOM   273  N  N   . THR A 1 35  ? -11.761 -12.143 32.468  1.00 15.17 ? 35  THR A N   1 
ATOM   274  C  CA  . THR A 1 35  ? -13.163 -11.798 32.696  1.00 16.85 ? 35  THR A CA  1 
ATOM   275  C  C   . THR A 1 35  ? -13.519 -11.935 34.155  1.00 17.61 ? 35  THR A C   1 
ATOM   276  O  O   . THR A 1 35  ? -14.463 -11.311 34.621  1.00 20.62 ? 35  THR A O   1 
ATOM   277  C  CB  . THR A 1 35  ? -14.079 -12.691 31.873  1.00 19.14 ? 35  THR A CB  1 
ATOM   278  O  OG1 . THR A 1 35  ? -13.938 -14.035 32.313  1.00 19.43 ? 35  THR A OG1 1 
ATOM   279  C  CG2 . THR A 1 35  ? -13.842 -12.532 30.391  1.00 18.65 ? 35  THR A CG2 1 
ATOM   280  N  N   . HIS A 1 36  ? -12.783 -12.752 34.871  1.00 20.53 ? 36  HIS A N   1 
ATOM   281  C  CA  . HIS A 1 36  ? -13.096 -13.050 36.242  1.00 22.70 ? 36  HIS A CA  1 
ATOM   282  C  C   . HIS A 1 36  ? -12.660 -11.908 37.126  1.00 27.21 ? 36  HIS A C   1 
ATOM   283  O  O   . HIS A 1 36  ? -13.373 -11.636 38.099  1.00 31.74 ? 36  HIS A O   1 
ATOM   284  C  CB  . HIS A 1 36  ? -12.546 -14.419 36.643  1.00 24.65 ? 36  HIS A CB  1 
ATOM   285  C  CG  . HIS A 1 36  ? -13.313 -15.456 35.901  1.00 30.90 ? 36  HIS A CG  1 
ATOM   286  N  ND1 . HIS A 1 36  ? -14.673 -15.616 36.147  1.00 39.34 ? 36  HIS A ND1 1 
ATOM   287  C  CD2 . HIS A 1 36  ? -12.942 -16.295 34.818  1.00 38.20 ? 36  HIS A CD2 1 
ATOM   288  C  CE1 . HIS A 1 36  ? -15.098 -16.585 35.280  1.00 43.82 ? 36  HIS A CE1 1 
ATOM   289  N  NE2 . HIS A 1 36  ? -14.068 -17.002 34.513  1.00 52.83 ? 36  HIS A NE2 1 
ATOM   290  N  N   . THR A 1 37  ? -11.593 -11.233 36.712  1.00 21.17 ? 37  THR A N   1 
ATOM   291  C  CA  . THR A 1 37  ? -10.906 -10.144 37.406  1.00 23.55 ? 37  THR A CA  1 
ATOM   292  C  C   . THR A 1 37  ? -11.454 -8.768  37.017  1.00 21.35 ? 37  THR A C   1 
ATOM   293  O  O   . THR A 1 37  ? -11.297 -7.787  37.737  1.00 26.44 ? 37  THR A O   1 
ATOM   294  C  CB  . THR A 1 37  ? -9.401  -10.270 37.105  1.00 32.83 ? 37  THR A CB  1 
ATOM   295  O  OG1 . THR A 1 37  ? -8.976  -11.366 37.895  1.00 38.40 ? 37  THR A OG1 1 
ATOM   296  C  CG2 . THR A 1 37  ? -8.632  -9.068  37.601  1.00 33.72 ? 37  THR A CG2 1 
ATOM   297  N  N   . ALA A 1 38  ? -12.111 -8.664  35.885  1.00 19.08 ? 38  ALA A N   1 
ATOM   298  C  CA  . ALA A 1 38  ? -12.669 -7.367  35.493  1.00 18.72 ? 38  ALA A CA  1 
ATOM   299  C  C   . ALA A 1 38  ? -13.726 -6.949  36.504  1.00 21.48 ? 38  ALA A C   1 
ATOM   300  O  O   . ALA A 1 38  ? -14.409 -7.783  37.062  1.00 24.11 ? 38  ALA A O   1 
ATOM   301  C  CB  . ALA A 1 38  ? -13.246 -7.487  34.113  1.00 17.59 ? 38  ALA A CB  1 
ATOM   302  N  N   . LYS A 1 39  ? -13.806 -5.664  36.843  1.00 20.89 ? 39  LYS A N   1 
ATOM   303  C  CA  . LYS A 1 39  ? -14.743 -5.187  37.859  1.00 23.15 ? 39  LYS A CA  1 
ATOM   304  C  C   . LYS A 1 39  ? -16.013 -4.674  37.179  1.00 18.67 ? 39  LYS A C   1 
ATOM   305  O  O   . LYS A 1 39  ? -15.970 -3.735  36.401  1.00 17.62 ? 39  LYS A O   1 
ATOM   306  C  CB  . LYS A 1 39  ? -14.050 -4.028  38.589  1.00 26.97 ? 39  LYS A CB  1 
ATOM   307  C  CG  . LYS A 1 39  ? -14.764 -3.248  39.679  1.00 26.10 ? 39  LYS A CG  1 
ATOM   308  C  CD  . LYS A 1 39  ? -15.226 -4.041  40.907  1.00 27.76 ? 39  LYS A CD  1 
ATOM   309  C  CE  . LYS A 1 39  ? -15.791 -3.075  41.925  1.00 30.43 ? 39  LYS A CE  1 
ATOM   310  N  NZ  . LYS A 1 39  ? -16.254 -3.773  43.145  1.00 34.03 ? 39  LYS A NZ  1 
ATOM   311  N  N   . TYR A 1 40  ? -17.164 -5.228  37.558  1.00 19.61 ? 40  TYR A N   1 
ATOM   312  C  CA  . TYR A 1 40  ? -18.438 -4.705  37.110  1.00 20.34 ? 40  TYR A CA  1 
ATOM   313  C  C   . TYR A 1 40  ? -18.594 -3.320  37.718  1.00 21.05 ? 40  TYR A C   1 
ATOM   314  O  O   . TYR A 1 40  ? -18.441 -3.100  38.933  1.00 21.27 ? 40  TYR A O   1 
ATOM   315  C  CB  . TYR A 1 40  ? -19.630 -5.607  37.457  1.00 25.92 ? 40  TYR A CB  1 
ATOM   316  C  CG  . TYR A 1 40  ? -20.961 -4.910  37.331  1.00 26.46 ? 40  TYR A CG  1 
ATOM   317  C  CD1 . TYR A 1 40  ? -21.429 -4.457  36.109  1.00 24.22 ? 40  TYR A CD1 1 
ATOM   318  C  CD2 . TYR A 1 40  ? -21.741 -4.691  38.450  1.00 36.43 ? 40  TYR A CD2 1 
ATOM   319  C  CE1 . TYR A 1 40  ? -22.659 -3.850  35.956  1.00 34.54 ? 40  TYR A CE1 1 
ATOM   320  C  CE2 . TYR A 1 40  ? -22.986 -4.080  38.314  1.00 41.36 ? 40  TYR A CE2 1 
ATOM   321  C  CZ  . TYR A 1 40  ? -23.438 -3.646  37.079  1.00 43.09 ? 40  TYR A CZ  1 
ATOM   322  O  OH  . TYR A 1 40  ? -24.619 -2.994  36.932  1.00 48.51 ? 40  TYR A OH  1 
ATOM   323  N  N   . ASP A 1 41  ? -18.848 -2.352  36.855  1.00 20.99 ? 41  ASP A N   1 
ATOM   324  C  CA  . ASP A 1 41  ? -18.942 -0.997  37.360  1.00 22.38 ? 41  ASP A CA  1 
ATOM   325  C  C   . ASP A 1 41  ? -20.353 -0.475  37.084  1.00 28.57 ? 41  ASP A C   1 
ATOM   326  O  O   . ASP A 1 41  ? -20.668 -0.103  35.956  1.00 24.48 ? 41  ASP A O   1 
ATOM   327  C  CB  . ASP A 1 41  ? -17.866 -0.068  36.791  1.00 27.40 ? 41  ASP A CB  1 
ATOM   328  C  CG  . ASP A 1 41  ? -17.990 1.336   37.375  1.00 34.03 ? 41  ASP A CG  1 
ATOM   329  O  OD1 . ASP A 1 41  ? -19.049 1.615   38.032  1.00 35.87 ? 41  ASP A OD1 1 
ATOM   330  O  OD2 . ASP A 1 41  ? -17.062 2.154   37.172  1.00 35.73 ? 41  ASP A OD2 1 
ATOM   331  N  N   . PRO A 1 42  ? -21.254 -0.474  38.095  1.00 35.62 ? 42  PRO A N   1 
ATOM   332  C  CA  . PRO A 1 42  ? -22.654 -0.100  37.850  1.00 37.04 ? 42  PRO A CA  1 
ATOM   333  C  C   . PRO A 1 42  ? -22.800 1.381   37.506  1.00 42.90 ? 42  PRO A C   1 
ATOM   334  O  O   . PRO A 1 42  ? -23.860 1.821   37.015  1.00 49.16 ? 42  PRO A O   1 
ATOM   335  C  CB  . PRO A 1 42  ? -23.299 -0.456  39.199  1.00 47.55 ? 42  PRO A CB  1 
ATOM   336  C  CG  . PRO A 1 42  ? -22.166 -0.255  40.192  1.00 47.15 ? 42  PRO A CG  1 
ATOM   337  C  CD  . PRO A 1 42  ? -20.967 -0.878  39.486  1.00 36.06 ? 42  PRO A CD  1 
ATOM   338  N  N   . SER A 1 43  ? -21.711 2.154   37.699  1.00 31.05 ? 43  SER A N   1 
ATOM   339  C  CA  . SER A 1 43  ? -21.813 3.565   37.323  1.00 32.15 ? 43  SER A CA  1 
ATOM   340  C  C   . SER A 1 43  ? -21.524 3.782   35.814  1.00 33.91 ? 43  SER A C   1 
ATOM   341  O  O   . SER A 1 43  ? -21.812 4.874   35.294  1.00 39.60 ? 43  SER A O   1 
ATOM   342  C  CB  . SER A 1 43  ? -20.934 4.412   38.193  1.00 43.91 ? 43  SER A CB  1 
ATOM   343  O  OG  . SER A 1 43  ? -19.578 4.219   37.844  1.00 37.88 ? 43  SER A OG  1 
ATOM   344  N  N   . LEU A 1 44  ? -21.027 2.761   35.081  1.00 31.73 ? 44  LEU A N   1 
ATOM   345  C  CA  . LEU A 1 44  ? -20.796 2.957   33.645  1.00 27.57 ? 44  LEU A CA  1 
ATOM   346  C  C   . LEU A 1 44  ? -22.131 3.147   32.925  1.00 30.09 ? 44  LEU A C   1 
ATOM   347  O  O   . LEU A 1 44  ? -23.106 2.498   33.280  1.00 39.24 ? 44  LEU A O   1 
ATOM   348  C  CB  . LEU A 1 44  ? -20.056 1.768   33.039  1.00 29.89 ? 44  LEU A CB  1 
ATOM   349  C  CG  . LEU A 1 44  ? -18.565 1.649   33.332  1.00 22.42 ? 44  LEU A CG  1 
ATOM   350  C  CD1 . LEU A 1 44  ? -18.053 0.270   32.907  1.00 23.17 ? 44  LEU A CD1 1 
ATOM   351  C  CD2 . LEU A 1 44  ? -17.844 2.712   32.533  1.00 22.34 ? 44  LEU A CD2 1 
ATOM   352  N  N   . LYS A 1 45  ? -22.130 3.973   31.876  1.00 32.21 ? 45  LYS A N   1 
ATOM   353  C  CA  . LYS A 1 45  ? -23.330 4.223   31.086  1.00 32.37 ? 45  LYS A CA  1 
ATOM   354  C  C   . LYS A 1 45  ? -23.399 3.223   29.945  1.00 25.48 ? 45  LYS A C   1 
ATOM   355  O  O   . LYS A 1 45  ? -22.375 2.582   29.577  1.00 26.91 ? 45  LYS A O   1 
ATOM   356  C  CB  . LYS A 1 45  ? -23.415 5.673   30.627  1.00 31.41 ? 45  LYS A CB  1 
ATOM   357  C  CG  . LYS A 1 45  ? -23.205 6.765   31.683  1.00 31.88 ? 45  LYS A CG  1 
ATOM   358  N  N   . PRO A 1 46  ? -24.614 2.975   29.383  1.00 23.34 ? 46  PRO A N   1 
ATOM   359  C  CA  . PRO A 1 46  ? -24.654 2.187   28.156  1.00 28.67 ? 46  PRO A CA  1 
ATOM   360  C  C   . PRO A 1 46  ? -23.862 3.032   27.204  1.00 21.91 ? 46  PRO A C   1 
ATOM   361  O  O   . PRO A 1 46  ? -23.822 4.250   27.324  1.00 24.73 ? 46  PRO A O   1 
ATOM   362  C  CB  . PRO A 1 46  ? -26.110 2.266   27.674  1.00 28.84 ? 46  PRO A CB  1 
ATOM   363  C  CG  . PRO A 1 46  ? -26.864 2.584   28.923  1.00 31.76 ? 46  PRO A CG  1 
ATOM   364  C  CD  . PRO A 1 46  ? -25.935 3.460   29.756  1.00 31.66 ? 46  PRO A CD  1 
ATOM   365  N  N   A LEU A 1 47  ? -23.244 2.359   26.237  0.50 25.07 ? 47  LEU A N   1 
ATOM   366  N  N   B LEU A 1 47  ? -23.245 2.322   26.253  0.50 24.32 ? 47  LEU A N   1 
ATOM   367  C  CA  A LEU A 1 47  ? -22.518 3.059   25.217  0.50 24.22 ? 47  LEU A CA  1 
ATOM   368  C  CA  B LEU A 1 47  ? -22.628 2.975   25.135  0.50 19.75 ? 47  LEU A CA  1 
ATOM   369  C  C   A LEU A 1 47  ? -23.564 3.573   24.223  0.50 23.89 ? 47  LEU A C   1 
ATOM   370  C  C   B LEU A 1 47  ? -23.709 3.630   24.299  0.50 23.97 ? 47  LEU A C   1 
ATOM   371  O  O   A LEU A 1 47  ? -24.565 2.895   23.976  0.50 26.62 ? 47  LEU A O   1 
ATOM   372  O  O   B LEU A 1 47  ? -24.772 3.034   24.128  0.50 25.38 ? 47  LEU A O   1 
ATOM   373  C  CB  A LEU A 1 47  ? -21.594 1.997   24.614  0.50 28.84 ? 47  LEU A CB  1 
ATOM   374  C  CB  B LEU A 1 47  ? -22.004 1.910   24.222  0.50 25.17 ? 47  LEU A CB  1 
ATOM   375  C  CG  A LEU A 1 47  ? -20.649 2.471   23.516  0.50 28.77 ? 47  LEU A CG  1 
ATOM   376  C  CG  B LEU A 1 47  ? -20.546 1.561   24.396  0.50 22.01 ? 47  LEU A CG  1 
ATOM   377  C  CD1 A LEU A 1 47  ? -19.530 3.295   24.171  0.50 27.91 ? 47  LEU A CD1 1 
ATOM   378  C  CD1 B LEU A 1 47  ? -20.132 0.873   23.101  0.50 22.55 ? 47  LEU A CD1 1 
ATOM   379  C  CD2 A LEU A 1 47  ? -20.099 1.266   22.747  0.50 37.09 ? 47  LEU A CD2 1 
ATOM   380  C  CD2 B LEU A 1 47  ? -19.718 2.851   24.660  0.50 27.08 ? 47  LEU A CD2 1 
ATOM   381  N  N   . SER A 1 48  ? -23.425 4.831   23.808  1.00 17.14 ? 48  SER A N   1 
ATOM   382  C  CA  . SER A 1 48  ? -24.252 5.403   22.765  1.00 18.03 ? 48  SER A CA  1 
ATOM   383  C  C   . SER A 1 48  ? -23.447 5.340   21.461  1.00 17.31 ? 48  SER A C   1 
ATOM   384  O  O   . SER A 1 48  ? -22.453 6.039   21.305  1.00 18.16 ? 48  SER A O   1 
ATOM   385  C  CB  . SER A 1 48  ? -24.603 6.843   23.140  1.00 20.58 ? 48  SER A CB  1 
ATOM   386  O  OG  . SER A 1 48  ? -25.237 7.483   22.036  1.00 24.93 ? 48  SER A OG  1 
ATOM   387  N  N   . VAL A 1 49  ? -23.865 4.499   20.532  1.00 19.78 ? 49  VAL A N   1 
ATOM   388  C  CA  . VAL A 1 49  ? -23.259 4.409   19.222  1.00 22.02 ? 49  VAL A CA  1 
ATOM   389  C  C   . VAL A 1 49  ? -24.261 5.001   18.243  1.00 22.42 ? 49  VAL A C   1 
ATOM   390  O  O   . VAL A 1 49  ? -25.335 4.427   18.041  1.00 28.08 ? 49  VAL A O   1 
ATOM   391  C  CB  . VAL A 1 49  ? -22.984 2.946   18.843  1.00 23.49 ? 49  VAL A CB  1 
ATOM   392  C  CG1 . VAL A 1 49  ? -22.261 2.877   17.482  1.00 29.16 ? 49  VAL A CG1 1 
ATOM   393  C  CG2 . VAL A 1 49  ? -22.212 2.240   19.949  1.00 25.30 ? 49  VAL A CG2 1 
ATOM   394  N  N   . SER A 1 50  ? -23.918 6.164   17.664  1.00 21.20 ? 50  SER A N   1 
ATOM   395  C  CA  . SER A 1 50  ? -24.855 6.904   16.819  1.00 21.44 ? 50  SER A CA  1 
ATOM   396  C  C   . SER A 1 50  ? -24.318 7.034   15.410  1.00 20.11 ? 50  SER A C   1 
ATOM   397  O  O   . SER A 1 50  ? -23.655 8.029   15.115  1.00 22.73 ? 50  SER A O   1 
ATOM   398  C  CB  . SER A 1 50  ? -25.238 8.259   17.345  1.00 27.87 ? 50  SER A CB  1 
ATOM   399  O  OG  . SER A 1 50  ? -25.795 8.166   18.633  1.00 33.14 ? 50  SER A OG  1 
ATOM   400  N  N   . TYR A 1 51  ? -24.499 5.985   14.606  1.00 20.14 ? 51  TYR A N   1 
ATOM   401  C  CA  . TYR A 1 51  ? -23.914 5.867   13.283  1.00 20.45 ? 51  TYR A CA  1 
ATOM   402  C  C   . TYR A 1 51  ? -24.855 6.170   12.114  1.00 19.33 ? 51  TYR A C   1 
ATOM   403  O  O   . TYR A 1 51  ? -24.446 5.990   10.972  1.00 21.85 ? 51  TYR A O   1 
ATOM   404  C  CB  . TYR A 1 51  ? -23.265 4.494   13.124  1.00 18.14 ? 51  TYR A CB  1 
ATOM   405  C  CG  . TYR A 1 51  ? -22.002 4.209   13.901  1.00 15.32 ? 51  TYR A CG  1 
ATOM   406  C  CD1 . TYR A 1 51  ? -21.313 5.178   14.620  1.00 15.55 ? 51  TYR A CD1 1 
ATOM   407  C  CD2 . TYR A 1 51  ? -21.506 2.908   13.897  1.00 16.22 ? 51  TYR A CD2 1 
ATOM   408  C  CE1 . TYR A 1 51  ? -20.120 4.865   15.264  1.00 14.20 ? 51  TYR A CE1 1 
ATOM   409  C  CE2 . TYR A 1 51  ? -20.317 2.589   14.527  1.00 16.03 ? 51  TYR A CE2 1 
ATOM   410  C  CZ  . TYR A 1 51  ? -19.659 3.564   15.267  1.00 13.49 ? 51  TYR A CZ  1 
ATOM   411  O  OH  . TYR A 1 51  ? -18.502 3.207   15.874  1.00 14.35 ? 51  TYR A OH  1 
ATOM   412  N  N   . ASP A 1 52  ? -26.098 6.634   12.399  1.00 22.37 ? 52  ASP A N   1 
ATOM   413  C  CA  . ASP A 1 52  ? -27.096 6.899   11.363  1.00 24.71 ? 52  ASP A CA  1 
ATOM   414  C  C   . ASP A 1 52  ? -26.624 7.759   10.183  1.00 30.32 ? 52  ASP A C   1 
ATOM   415  O  O   . ASP A 1 52  ? -27.048 7.521   9.031   1.00 30.66 ? 52  ASP A O   1 
ATOM   416  C  CB  . ASP A 1 52  ? -28.382 7.442   11.973  1.00 32.73 ? 52  ASP A CB  1 
ATOM   417  C  CG  . ASP A 1 52  ? -28.255 8.386   13.169  1.00 43.41 ? 52  ASP A CG  1 
ATOM   418  O  OD1 . ASP A 1 52  ? -27.538 8.030   14.185  1.00 50.77 ? 52  ASP A OD1 1 
ATOM   419  O  OD2 . ASP A 1 52  ? -28.909 9.460   13.119  1.00 55.76 ? 52  ASP A OD2 1 
ATOM   420  N  N   . GLN A 1 53  ? -25.769 8.760   10.431  1.00 28.05 ? 53  GLN A N   1 
ATOM   421  C  CA  . GLN A 1 53  ? -25.401 9.659   9.327   1.00 25.64 ? 53  GLN A CA  1 
ATOM   422  C  C   . GLN A 1 53  ? -23.947 9.457   8.914   1.00 20.70 ? 53  GLN A C   1 
ATOM   423  O  O   . GLN A 1 53  ? -23.363 10.323  8.295   1.00 22.50 ? 53  GLN A O   1 
ATOM   424  C  CB  . GLN A 1 53  ? -25.579 11.143  9.686   1.00 26.82 ? 53  GLN A CB  1 
ATOM   425  C  CG  . GLN A 1 53  ? -27.043 11.551  9.902   1.00 33.64 ? 53  GLN A CG  1 
ATOM   426  C  CD  . GLN A 1 53  ? -27.870 11.313  8.668   1.00 48.95 ? 53  GLN A CD  1 
ATOM   427  O  OE1 . GLN A 1 53  ? -28.873 10.599  8.737   1.00 47.43 ? 53  GLN A OE1 1 
ATOM   428  N  NE2 . GLN A 1 53  ? -27.435 11.878  7.537   1.00 38.39 ? 53  GLN A NE2 1 
ATOM   429  N  N   . ALA A 1 54  ? -23.376 8.287   9.170   1.00 20.68 ? 54  ALA A N   1 
ATOM   430  C  CA  . ALA A 1 54  ? -21.992 8.053   8.781   1.00 17.84 ? 54  ALA A CA  1 
ATOM   431  C  C   . ALA A 1 54  ? -21.824 8.197   7.268   1.00 19.45 ? 54  ALA A C   1 
ATOM   432  O  O   . ALA A 1 54  ? -22.701 7.751   6.471   1.00 22.38 ? 54  ALA A O   1 
ATOM   433  C  CB  . ALA A 1 54  ? -21.535 6.681   9.217   1.00 19.94 ? 54  ALA A CB  1 
ATOM   434  N  N   . THR A 1 55  ? -20.689 8.807   6.867   1.00 18.51 ? 55  THR A N   1 
ATOM   435  C  CA  . THR A 1 55  ? -20.357 8.985   5.447   1.00 17.57 ? 55  THR A CA  1 
ATOM   436  C  C   . THR A 1 55  ? -18.991 8.346   5.197   1.00 16.26 ? 55  THR A C   1 
ATOM   437  O  O   . THR A 1 55  ? -17.989 8.979   5.467   1.00 18.17 ? 55  THR A O   1 
ATOM   438  C  CB  . THR A 1 55  ? -20.208 10.473  5.106   1.00 22.24 ? 55  THR A CB  1 
ATOM   439  O  OG1 . THR A 1 55  ? -21.493 11.061  5.268   1.00 26.32 ? 55  THR A OG1 1 
ATOM   440  C  CG2 . THR A 1 55  ? -19.750 10.679  3.659   1.00 23.04 ? 55  THR A CG2 1 
ATOM   441  N  N   . SER A 1 56  ? -18.956 7.119   4.670   1.00 16.39 ? 56  SER A N   1 
ATOM   442  C  CA  . SER A 1 56  ? -17.682 6.537   4.309   1.00 18.02 ? 56  SER A CA  1 
ATOM   443  C  C   . SER A 1 56  ? -17.176 7.242   3.049   1.00 15.46 ? 56  SER A C   1 
ATOM   444  O  O   . SER A 1 56  ? -18.006 7.681   2.188   1.00 18.73 ? 56  SER A O   1 
ATOM   445  C  CB  . SER A 1 56  ? -17.769 5.044   4.097   1.00 17.19 ? 56  SER A CB  1 
ATOM   446  O  OG  . SER A 1 56  ? -18.647 4.716   3.006   1.00 18.31 ? 56  SER A OG  1 
ATOM   447  N  N   . LEU A 1 57  ? -15.856 7.330   2.873   1.00 16.97 ? 57  LEU A N   1 
ATOM   448  C  CA  . LEU A 1 57  ? -15.263 7.936   1.689   1.00 17.43 ? 57  LEU A CA  1 
ATOM   449  C  C   . LEU A 1 57  ? -14.427 6.987   0.837   1.00 19.07 ? 57  LEU A C   1 
ATOM   450  O  O   . LEU A 1 57  ? -14.602 6.955   -0.390  1.00 20.92 ? 57  LEU A O   1 
ATOM   451  C  CB  . LEU A 1 57  ? -14.404 9.139   2.075   1.00 19.37 ? 57  LEU A CB  1 
ATOM   452  C  CG  . LEU A 1 57  ? -15.166 10.298  2.690   1.00 21.22 ? 57  LEU A CG  1 
ATOM   453  C  CD1 . LEU A 1 57  ? -14.158 11.289  3.268   1.00 23.28 ? 57  LEU A CD1 1 
ATOM   454  C  CD2 . LEU A 1 57  ? -16.099 10.978  1.644   1.00 28.39 ? 57  LEU A CD2 1 
ATOM   455  N  N   . ARG A 1 58  ? -13.493 6.275   1.473   1.00 19.24 ? 58  ARG A N   1 
ATOM   456  C  CA  . ARG A 1 58  ? -12.429 5.615   0.697   1.00 18.13 ? 58  ARG A CA  1 
ATOM   457  C  C   . ARG A 1 58  ? -12.020 4.376   1.506   1.00 17.64 ? 58  ARG A C   1 
ATOM   458  O  O   . ARG A 1 58  ? -12.244 4.332   2.740   1.00 19.50 ? 58  ARG A O   1 
ATOM   459  C  CB  . ARG A 1 58  ? -11.162 6.475   0.411   1.00 20.19 ? 58  ARG A CB  1 
ATOM   460  C  CG  . ARG A 1 58  ? -11.310 7.683   -0.539  1.00 23.89 ? 58  ARG A CG  1 
ATOM   461  C  CD  . ARG A 1 58  ? -10.038 8.403   -0.973  1.00 25.49 ? 58  ARG A CD  1 
ATOM   462  N  NE  . ARG A 1 58  ? -9.304  7.548   -1.883  1.00 31.11 ? 58  ARG A NE  1 
ATOM   463  C  CZ  . ARG A 1 58  ? -9.609  7.282   -3.164  1.00 27.84 ? 58  ARG A CZ  1 
ATOM   464  N  NH1 . ARG A 1 58  ? -10.680 7.825   -3.732  1.00 39.43 ? 58  ARG A NH1 1 
ATOM   465  N  NH2 . ARG A 1 58  ? -8.825  6.468   -3.846  1.00 30.58 ? 58  ARG A NH2 1 
ATOM   466  N  N   . ILE A 1 59  ? -11.473 3.404   0.798   1.00 19.29 ? 59  ILE A N   1 
ATOM   467  C  CA  . ILE A 1 59  ? -10.868 2.257   1.456   1.00 19.17 ? 59  ILE A CA  1 
ATOM   468  C  C   . ILE A 1 59  ? -9.426  2.149   0.947   1.00 19.05 ? 59  ILE A C   1 
ATOM   469  O  O   . ILE A 1 59  ? -9.185  2.367   -0.232  1.00 19.45 ? 59  ILE A O   1 
ATOM   470  C  CB  . ILE A 1 59  ? -11.728 0.998   1.201   1.00 18.78 ? 59  ILE A CB  1 
ATOM   471  C  CG1 . ILE A 1 59  ? -11.266 -0.194  2.060   1.00 17.74 ? 59  ILE A CG1 1 
ATOM   472  C  CG2 . ILE A 1 59  ? -11.731 0.613   -0.324  1.00 17.43 ? 59  ILE A CG2 1 
ATOM   473  C  CD1 . ILE A 1 59  ? -12.172 -1.424  2.020   1.00 19.24 ? 59  ILE A CD1 1 
ATOM   474  N  N   A LEU A 1 60  ? -8.443  1.923   1.823   0.50 17.26 ? 60  LEU A N   1 
ATOM   475  N  N   B LEU A 1 60  ? -8.513  1.717   1.811   0.50 19.73 ? 60  LEU A N   1 
ATOM   476  C  CA  A LEU A 1 60  ? -7.077  1.807   1.330   0.50 19.60 ? 60  LEU A CA  1 
ATOM   477  C  CA  B LEU A 1 60  ? -7.104  1.872   1.515   0.50 21.76 ? 60  LEU A CA  1 
ATOM   478  C  C   A LEU A 1 60  ? -6.395  0.648   2.038   0.50 14.11 ? 60  LEU A C   1 
ATOM   479  C  C   B LEU A 1 60  ? -6.334  0.690   2.114   0.50 18.89 ? 60  LEU A C   1 
ATOM   480  O  O   A LEU A 1 60  ? -6.755  0.285   3.181   0.50 17.49 ? 60  LEU A O   1 
ATOM   481  O  O   B LEU A 1 60  ? -6.638  0.266   3.245   0.50 19.60 ? 60  LEU A O   1 
ATOM   482  C  CB  A LEU A 1 60  ? -6.251  3.068   1.609   0.50 19.33 ? 60  LEU A CB  1 
ATOM   483  C  CB  B LEU A 1 60  ? -6.702  3.186   2.198   0.50 25.44 ? 60  LEU A CB  1 
ATOM   484  C  CG  A LEU A 1 60  ? -6.134  3.455   3.083   0.50 23.22 ? 60  LEU A CG  1 
ATOM   485  C  CG  B LEU A 1 60  ? -5.200  3.420   2.265   0.50 27.71 ? 60  LEU A CG  1 
ATOM   486  C  CD1 A LEU A 1 60  ? -5.310  4.728   3.237   0.50 23.11 ? 60  LEU A CD1 1 
ATOM   487  C  CD1 B LEU A 1 60  ? -4.697  3.693   0.860   0.50 24.51 ? 60  LEU A CD1 1 
ATOM   488  C  CD2 A LEU A 1 60  ? -7.516  3.704   3.641   0.50 31.90 ? 60  LEU A CD2 1 
ATOM   489  C  CD2 B LEU A 1 60  ? -4.877  4.591   3.187   0.50 33.19 ? 60  LEU A CD2 1 
ATOM   490  N  N   . ASN A 1 61  ? -5.377  0.124   1.367   1.00 16.84 ? 61  ASN A N   1 
ATOM   491  C  CA  . ASN A 1 61  ? -4.414  -0.822  1.934   1.00 16.81 ? 61  ASN A CA  1 
ATOM   492  C  C   . ASN A 1 61  ? -3.153  -0.028  2.245   1.00 21.39 ? 61  ASN A C   1 
ATOM   493  O  O   . ASN A 1 61  ? -2.558  0.541   1.341   1.00 22.02 ? 61  ASN A O   1 
ATOM   494  C  CB  . ASN A 1 61  ? -4.085  -1.890  0.889   1.00 17.10 ? 61  ASN A CB  1 
ATOM   495  C  CG  . ASN A 1 61  ? -3.055  -2.874  1.333   1.00 17.69 ? 61  ASN A CG  1 
ATOM   496  O  OD1 . ASN A 1 61  ? -2.254  -2.544  2.178   1.00 18.69 ? 61  ASN A OD1 1 
ATOM   497  N  ND2 . ASN A 1 61  ? -3.075  -4.060  0.747   1.00 16.96 ? 61  ASN A ND2 1 
ATOM   498  N  N   . ASN A 1 62  ? -2.832  0.100   3.531   1.00 19.21 ? 62  ASN A N   1 
ATOM   499  C  CA  . ASN A 1 62  ? -1.701  0.916   3.984   1.00 20.16 ? 62  ASN A CA  1 
ATOM   500  C  C   . ASN A 1 62  ? -0.477  0.062   4.296   1.00 22.99 ? 62  ASN A C   1 
ATOM   501  O  O   . ASN A 1 62  ? 0.527   0.557   4.832   1.00 26.25 ? 62  ASN A O   1 
ATOM   502  C  CB  . ASN A 1 62  ? -2.047  1.789   5.201   1.00 23.63 ? 62  ASN A CB  1 
ATOM   503  C  CG  . ASN A 1 62  ? -2.524  0.950   6.383   1.00 21.79 ? 62  ASN A CG  1 
ATOM   504  O  OD1 . ASN A 1 62  ? -2.269  -0.238  6.419   1.00 19.08 ? 62  ASN A OD1 1 
ATOM   505  N  ND2 . ASN A 1 62  ? -3.078  1.585   7.391   1.00 30.86 ? 62  ASN A ND2 1 
ATOM   506  N  N   . GLY A 1 63  ? -0.511  -1.211  3.886   1.00 18.02 ? 63  GLY A N   1 
ATOM   507  C  CA  . GLY A 1 63  ? 0.642   -2.068  4.059   1.00 21.11 ? 63  GLY A CA  1 
ATOM   508  C  C   . GLY A 1 63  ? 0.655   -2.715  5.431   1.00 17.02 ? 63  GLY A C   1 
ATOM   509  O  O   . GLY A 1 63  ? 1.481   -3.608  5.661   1.00 20.51 ? 63  GLY A O   1 
ATOM   510  N  N   A HIS A 1 64  ? -0.308  -2.297  6.277   0.50 15.14 ? 64  HIS A N   1 
ATOM   511  N  N   B HIS A 1 64  ? -0.320  -2.361  6.312   0.50 16.67 ? 64  HIS A N   1 
ATOM   512  C  CA  A HIS A 1 64  ? -0.428  -2.924  7.589   0.50 15.46 ? 64  HIS A CA  1 
ATOM   513  C  CA  B HIS A 1 64  ? -0.432  -3.082  7.591   0.50 16.77 ? 64  HIS A CA  1 
ATOM   514  C  C   A HIS A 1 64  ? -1.778  -3.626  7.748   0.50 16.27 ? 64  HIS A C   1 
ATOM   515  C  C   B HIS A 1 64  ? -1.854  -3.512  7.965   0.50 13.88 ? 64  HIS A C   1 
ATOM   516  O  O   A HIS A 1 64  ? -1.845  -4.749  8.254   0.50 18.05 ? 64  HIS A O   1 
ATOM   517  O  O   B HIS A 1 64  ? -2.065  -4.304  8.891   0.50 14.35 ? 64  HIS A O   1 
ATOM   518  C  CB  A HIS A 1 64  ? -0.162  -1.895  8.684   0.50 16.19 ? 64  HIS A CB  1 
ATOM   519  C  CB  B HIS A 1 64  ? 0.147   -2.323  8.790   0.50 21.90 ? 64  HIS A CB  1 
ATOM   520  C  CG  A HIS A 1 64  ? 1.152   -1.200  8.480   0.50 15.84 ? 64  HIS A CG  1 
ATOM   521  C  CG  B HIS A 1 64  ? -0.236  -0.881  8.929   0.50 25.45 ? 64  HIS A CG  1 
ATOM   522  N  ND1 A HIS A 1 64  ? 2.393   -1.847  8.611   0.50 18.22 ? 64  HIS A ND1 1 
ATOM   523  N  ND1 B HIS A 1 64  ? -1.213  -0.445  9.818   0.50 25.53 ? 64  HIS A ND1 1 
ATOM   524  C  CD2 A HIS A 1 64  ? 1.450   0.097   8.223   0.50 16.72 ? 64  HIS A CD2 1 
ATOM   525  C  CD2 B HIS A 1 64  ? 0.268   0.241   8.369   0.50 20.02 ? 64  HIS A CD2 1 
ATOM   526  C  CE1 A HIS A 1 64  ? 3.375   -0.995  8.390   0.50 19.98 ? 64  HIS A CE1 1 
ATOM   527  C  CE1 B HIS A 1 64  ? -1.296  0.874   9.805   0.50 25.58 ? 64  HIS A CE1 1 
ATOM   528  N  NE2 A HIS A 1 64  ? 2.814   0.218   8.156   0.50 19.41 ? 64  HIS A NE2 1 
ATOM   529  N  NE2 B HIS A 1 64  ? -0.407  1.311   8.904   0.50 26.39 ? 64  HIS A NE2 1 
ATOM   530  N  N   . SER A 1 65  ? -2.841  -2.967  7.260   1.00 13.98 ? 65  SER A N   1 
ATOM   531  C  CA  . SER A 1 65  ? -4.231  -3.366  7.372   1.00 13.01 ? 65  SER A CA  1 
ATOM   532  C  C   . SER A 1 65  ? -4.905  -2.820  6.120   1.00 14.51 ? 65  SER A C   1 
ATOM   533  O  O   . SER A 1 65  ? -4.246  -2.256  5.235   1.00 15.21 ? 65  SER A O   1 
ATOM   534  C  CB  . SER A 1 65  ? -4.870  -2.800  8.691   1.00 17.22 ? 65  SER A CB  1 
ATOM   535  O  OG  . SER A 1 65  ? -6.156  -3.345  8.819   1.00 19.57 ? 65  SER A OG  1 
ATOM   536  N  N   . PHE A 1 66  ? -6.232  -2.931  6.100   1.00 14.36 ? 66  PHE A N   1 
ATOM   537  C  CA  . PHE A 1 66  ? -6.985  -2.062  5.240   1.00 15.23 ? 66  PHE A CA  1 
ATOM   538  C  C   . PHE A 1 66  ? -7.918  -1.236  6.117   1.00 14.65 ? 66  PHE A C   1 
ATOM   539  O  O   . PHE A 1 66  ? -8.372  -1.671  7.193   1.00 14.62 ? 66  PHE A O   1 
ATOM   540  C  CB  . PHE A 1 66  ? -7.750  -2.867  4.165   1.00 17.26 ? 66  PHE A CB  1 
ATOM   541  C  CG  . PHE A 1 66  ? -8.911  -3.692  4.685   1.00 15.55 ? 66  PHE A CG  1 
ATOM   542  C  CD1 . PHE A 1 66  ? -10.157 -3.093  4.860   1.00 15.85 ? 66  PHE A CD1 1 
ATOM   543  C  CD2 . PHE A 1 66  ? -8.751  -5.010  5.113   1.00 15.83 ? 66  PHE A CD2 1 
ATOM   544  C  CE1 . PHE A 1 66  ? -11.235 -3.845  5.318   1.00 16.69 ? 66  PHE A CE1 1 
ATOM   545  C  CE2 . PHE A 1 66  ? -9.847  -5.749  5.569   1.00 15.58 ? 66  PHE A CE2 1 
ATOM   546  C  CZ  . PHE A 1 66  ? -11.102 -5.167  5.696   1.00 15.00 ? 66  PHE A CZ  1 
ATOM   547  N  N   . LYS A 1 67  ? -8.225  -0.038  5.642   1.00 16.52 ? 67  LYS A N   1 
ATOM   548  C  CA  . LYS A 1 67  ? -8.928  0.923   6.429   1.00 16.17 ? 67  LYS A CA  1 
ATOM   549  C  C   . LYS A 1 67  ? -10.017 1.559   5.596   1.00 16.67 ? 67  LYS A C   1 
ATOM   550  O  O   . LYS A 1 67  ? -9.772  1.937   4.444   1.00 19.85 ? 67  LYS A O   1 
ATOM   551  C  CB  . LYS A 1 67  ? -7.873  1.932   6.861   1.00 21.88 ? 67  LYS A CB  1 
ATOM   552  C  CG  . LYS A 1 67  ? -8.424  3.093   7.610   1.00 21.72 ? 67  LYS A CG  1 
ATOM   553  C  CD  . LYS A 1 67  ? -7.381  4.266   7.817   1.00 25.37 ? 67  LYS A CD  1 
ATOM   554  C  CE  . LYS A 1 67  ? -5.977  3.872   8.195   1.00 33.83 ? 67  LYS A CE  1 
ATOM   555  N  NZ  . LYS A 1 67  ? -5.190  5.081   8.559   1.00 38.10 ? 67  LYS A NZ  1 
ATOM   556  N  N   . VAL A 1 68  ? -11.188 1.727   6.187   1.00 16.19 ? 68  VAL A N   1 
ATOM   557  C  CA  . VAL A 1 68  ? -12.253 2.523   5.590   1.00 17.66 ? 68  VAL A CA  1 
ATOM   558  C  C   . VAL A 1 68  ? -12.241 3.860   6.322   1.00 16.10 ? 68  VAL A C   1 
ATOM   559  O  O   . VAL A 1 68  ? -12.420 3.884   7.556   1.00 16.89 ? 68  VAL A O   1 
ATOM   560  C  CB  . VAL A 1 68  ? -13.596 1.808   5.748   1.00 16.17 ? 68  VAL A CB  1 
ATOM   561  C  CG1 . VAL A 1 68  ? -14.775 2.713   5.299   1.00 18.24 ? 68  VAL A CG1 1 
ATOM   562  C  CG2 . VAL A 1 68  ? -13.663 0.478   4.946   1.00 18.95 ? 68  VAL A CG2 1 
ATOM   563  N  N   . GLU A 1 69  ? -12.101 4.922   5.538   1.00 17.92 ? 69  GLU A N   1 
ATOM   564  C  CA  . GLU A 1 69  ? -12.051 6.240   6.109   1.00 16.75 ? 69  GLU A CA  1 
ATOM   565  C  C   . GLU A 1 69  ? -13.394 6.910   5.914   1.00 16.50 ? 69  GLU A C   1 
ATOM   566  O  O   . GLU A 1 69  ? -13.999 6.772   4.825   1.00 20.52 ? 69  GLU A O   1 
ATOM   567  C  CB  . GLU A 1 69  ? -10.888 7.023   5.468   1.00 22.18 ? 69  GLU A CB  1 
ATOM   568  C  CG  . GLU A 1 69  ? -9.536  6.404   5.912   1.00 30.87 ? 69  GLU A CG  1 
ATOM   569  C  CD  . GLU A 1 69  ? -8.259  7.238   5.672   1.00 31.35 ? 69  GLU A CD  1 
ATOM   570  O  OE1 . GLU A 1 69  ? -7.774  7.256   4.524   1.00 39.64 ? 69  GLU A OE1 1 
ATOM   571  O  OE2 . GLU A 1 69  ? -7.769  7.857   6.637   1.00 45.62 ? 69  GLU A OE2 1 
ATOM   572  N  N   . PHE A 1 70  ? -13.788 7.732   6.919   1.00 15.70 ? 70  PHE A N   1 
ATOM   573  C  CA  . PHE A 1 70  ? -15.060 8.445   6.968   1.00 14.87 ? 70  PHE A CA  1 
ATOM   574  C  C   . PHE A 1 70  ? -14.906 9.969   6.870   1.00 14.05 ? 70  PHE A C   1 
ATOM   575  O  O   . PHE A 1 70  ? -13.876 10.500  7.260   1.00 17.70 ? 70  PHE A O   1 
ATOM   576  C  CB  . PHE A 1 70  ? -15.841 8.152   8.256   1.00 15.13 ? 70  PHE A CB  1 
ATOM   577  C  CG  . PHE A 1 70  ? -16.402 6.760   8.260   1.00 16.26 ? 70  PHE A CG  1 
ATOM   578  C  CD1 . PHE A 1 70  ? -15.570 5.676   8.527   1.00 16.68 ? 70  PHE A CD1 1 
ATOM   579  C  CD2 . PHE A 1 70  ? -17.718 6.505   7.936   1.00 15.27 ? 70  PHE A CD2 1 
ATOM   580  C  CE1 . PHE A 1 70  ? -16.052 4.375   8.432   1.00 19.09 ? 70  PHE A CE1 1 
ATOM   581  C  CE2 . PHE A 1 70  ? -18.194 5.193   7.823   1.00 16.90 ? 70  PHE A CE2 1 
ATOM   582  C  CZ  . PHE A 1 70  ? -17.360 4.136   8.101   1.00 18.30 ? 70  PHE A CZ  1 
ATOM   583  N  N   A ASP A 1 71  ? -15.935 10.701  6.390   0.50 17.93 ? 71  ASP A N   1 
ATOM   584  N  N   B ASP A 1 71  ? -15.988 10.635  6.412   0.50 17.40 ? 71  ASP A N   1 
ATOM   585  C  CA  A ASP A 1 71  ? -15.870 12.167  6.442   0.50 15.67 ? 71  ASP A CA  1 
ATOM   586  C  CA  B ASP A 1 71  ? -16.103 12.077  6.585   0.50 16.48 ? 71  ASP A CA  1 
ATOM   587  C  C   A ASP A 1 71  ? -16.262 12.599  7.858   0.50 16.98 ? 71  ASP A C   1 
ATOM   588  C  C   B ASP A 1 71  ? -16.267 12.353  8.075   0.50 14.86 ? 71  ASP A C   1 
ATOM   589  O  O   A ASP A 1 71  ? -17.446 12.590  8.197   0.50 19.54 ? 71  ASP A O   1 
ATOM   590  O  O   B ASP A 1 71  ? -17.295 12.042  8.672   0.50 19.22 ? 71  ASP A O   1 
ATOM   591  C  CB  A ASP A 1 71  ? -16.698 12.779  5.299   0.50 16.66 ? 71  ASP A CB  1 
ATOM   592  C  CB  B ASP A 1 71  ? -17.303 12.628  5.819   0.50 16.32 ? 71  ASP A CB  1 
ATOM   593  C  CG  A ASP A 1 71  ? -16.931 14.272  5.415   0.50 18.39 ? 71  ASP A CG  1 
ATOM   594  C  CG  B ASP A 1 71  ? -17.352 14.129  5.929   0.50 22.03 ? 71  ASP A CG  1 
ATOM   595  O  OD1 A ASP A 1 71  ? -16.679 14.819  6.561   0.50 17.45 ? 71  ASP A OD1 1 
ATOM   596  O  OD1 B ASP A 1 71  ? -16.268 14.752  6.242   0.50 18.65 ? 71  ASP A OD1 1 
ATOM   597  O  OD2 A ASP A 1 71  ? -17.440 14.875  4.426   0.50 19.61 ? 71  ASP A OD2 1 
ATOM   598  O  OD2 B ASP A 1 71  ? -18.449 14.655  5.732   0.50 21.51 ? 71  ASP A OD2 1 
ATOM   599  N  N   . ASP A 1 72  ? -15.264 12.971  8.664   1.00 15.84 ? 72  ASP A N   1 
ATOM   600  C  CA  . ASP A 1 72  ? -15.425 13.335  10.071  1.00 15.31 ? 72  ASP A CA  1 
ATOM   601  C  C   . ASP A 1 72  ? -15.340 14.836  10.253  1.00 17.09 ? 72  ASP A C   1 
ATOM   602  O  O   . ASP A 1 72  ? -14.863 15.302  11.299  1.00 20.01 ? 72  ASP A O   1 
ATOM   603  C  CB  . ASP A 1 72  ? -14.362 12.609  10.908  1.00 16.48 ? 72  ASP A CB  1 
ATOM   604  C  CG  . ASP A 1 72  ? -12.943 12.949  10.540  1.00 16.87 ? 72  ASP A CG  1 
ATOM   605  O  OD1 . ASP A 1 72  ? -12.735 13.640  9.503   1.00 20.64 ? 72  ASP A OD1 1 
ATOM   606  O  OD2 . ASP A 1 72  ? -12.020 12.486  11.269  1.00 18.05 ? 72  ASP A OD2 1 
ATOM   607  N  N   . SER A 1 73  ? -15.713 15.584  9.238   1.00 17.58 ? 73  SER A N   1 
ATOM   608  C  CA  . SER A 1 73  ? -15.665 17.048  9.272   1.00 18.69 ? 73  SER A CA  1 
ATOM   609  C  C   . SER A 1 73  ? -16.935 17.662  9.876   1.00 21.90 ? 73  SER A C   1 
ATOM   610  O  O   . SER A 1 73  ? -16.998 18.861  10.041  1.00 21.50 ? 73  SER A O   1 
ATOM   611  C  CB  . SER A 1 73  ? -15.397 17.565  7.861   1.00 21.61 ? 73  SER A CB  1 
ATOM   612  O  OG  . SER A 1 73  ? -16.602 17.438  7.110   1.00 21.00 ? 73  SER A OG  1 
ATOM   613  N  N   . GLN A 1 74  ? -17.946 16.866  10.240  1.00 20.42 ? 74  GLN A N   1 
ATOM   614  C  CA  . GLN A 1 74  ? -19.158 17.320  10.902  1.00 25.74 ? 74  GLN A CA  1 
ATOM   615  C  C   . GLN A 1 74  ? -19.509 16.273  11.942  1.00 22.08 ? 74  GLN A C   1 
ATOM   616  O  O   . GLN A 1 74  ? -19.021 15.157  11.849  1.00 20.62 ? 74  GLN A O   1 
ATOM   617  C  CB  . GLN A 1 74  ? -20.344 17.368  9.908   1.00 31.16 ? 74  GLN A CB  1 
ATOM   618  C  CG  . GLN A 1 74  ? -20.221 18.433  8.830   1.00 40.32 ? 74  GLN A CG  1 
ATOM   619  C  CD  . GLN A 1 74  ? -20.702 17.994  7.460   1.00 49.56 ? 74  GLN A CD  1 
ATOM   620  O  OE1 . GLN A 1 74  ? -21.886 17.804  7.248   1.00 36.62 ? 74  GLN A OE1 1 
ATOM   621  N  NE2 . GLN A 1 74  ? -19.782 17.895  6.490   1.00 47.77 ? 74  GLN A NE2 1 
ATOM   622  N  N   A ASP A 1 75  ? -20.344 16.598  12.953  0.50 27.04 ? 75  ASP A N   1 
ATOM   623  N  N   B ASP A 1 75  ? -20.493 16.689  12.721  0.50 22.73 ? 75  ASP A N   1 
ATOM   624  C  CA  A ASP A 1 75  ? -20.712 15.622  13.985  0.50 29.20 ? 75  ASP A CA  1 
ATOM   625  C  CA  B ASP A 1 75  ? -21.145 15.933  13.754  0.50 22.91 ? 75  ASP A CA  1 
ATOM   626  C  C   A ASP A 1 75  ? -21.790 14.675  13.452  0.50 27.97 ? 75  ASP A C   1 
ATOM   627  C  C   B ASP A 1 75  ? -21.918 14.823  13.036  0.50 24.76 ? 75  ASP A C   1 
ATOM   628  O  O   A ASP A 1 75  ? -22.995 14.817  13.702  0.50 33.07 ? 75  ASP A O   1 
ATOM   629  O  O   B ASP A 1 75  ? -23.077 15.029  12.728  0.50 28.54 ? 75  ASP A O   1 
ATOM   630  C  CB  A ASP A 1 75  ? -21.096 16.222  15.345  0.50 27.68 ? 75  ASP A CB  1 
ATOM   631  C  CB  B ASP A 1 75  ? -21.922 16.954  14.601  0.50 19.68 ? 75  ASP A CB  1 
ATOM   632  C  CG  A ASP A 1 75  ? -20.031 16.219  16.439  0.50 30.43 ? 75  ASP A CG  1 
ATOM   633  C  CG  B ASP A 1 75  ? -22.479 16.373  15.882  0.50 21.63 ? 75  ASP A CG  1 
ATOM   634  O  OD1 A ASP A 1 75  ? -19.439 15.117  16.743  0.50 21.16 ? 75  ASP A OD1 1 
ATOM   635  O  OD1 B ASP A 1 75  ? -22.178 15.218  16.141  0.50 24.48 ? 75  ASP A OD1 1 
ATOM   636  O  OD2 A ASP A 1 75  ? -19.849 17.303  17.052  0.50 40.93 ? 75  ASP A OD2 1 
ATOM   637  O  OD2 B ASP A 1 75  ? -23.226 17.072  16.584  0.50 27.91 ? 75  ASP A OD2 1 
ATOM   638  N  N   . LYS A 1 76  ? -21.298 13.665  12.745  1.00 23.89 ? 76  LYS A N   1 
ATOM   639  C  CA  . LYS A 1 76  ? -22.076 12.608  12.128  1.00 28.75 ? 76  LYS A CA  1 
ATOM   640  C  C   . LYS A 1 76  ? -22.108 11.383  13.045  1.00 39.59 ? 76  LYS A C   1 
ATOM   641  O  O   . LYS A 1 76  ? -22.809 11.378  14.047  1.00 56.00 ? 76  LYS A O   1 
ATOM   642  C  CB  . LYS A 1 76  ? -21.624 12.371  10.677  1.00 28.27 ? 76  LYS A CB  1 
ATOM   643  C  CG  . LYS A 1 76  ? -22.120 13.404  9.666   1.00 34.76 ? 76  LYS A CG  1 
ATOM   644  C  CD  . LYS A 1 76  ? -21.393 13.315  8.338   1.00 36.81 ? 76  LYS A CD  1 
ATOM   645  C  CE  . LYS A 1 76  ? -22.059 14.164  7.269   1.00 37.29 ? 76  LYS A CE  1 
ATOM   646  N  NZ  . LYS A 1 76  ? -21.395 14.018  5.960   1.00 35.51 ? 76  LYS A NZ  1 
ATOM   647  N  N   . ALA A 1 77  ? -21.344 10.371  12.687  1.00 30.07 ? 77  ALA A N   1 
ATOM   648  C  CA  . ALA A 1 77  ? -21.150 9.092   13.359  1.00 21.28 ? 77  ALA A CA  1 
ATOM   649  C  C   . ALA A 1 77  ? -20.370 9.317   14.640  1.00 22.52 ? 77  ALA A C   1 
ATOM   650  O  O   . ALA A 1 77  ? -19.180 9.560   14.592  1.00 24.91 ? 77  ALA A O   1 
ATOM   651  C  CB  . ALA A 1 77  ? -20.360 8.284   12.383  1.00 24.63 ? 77  ALA A CB  1 
ATOM   652  N  N   . VAL A 1 78  ? -21.019 9.195   15.790  1.00 19.17 ? 78  VAL A N   1 
ATOM   653  C  CA  . VAL A 1 78  ? -20.378 9.507   17.045  1.00 21.15 ? 78  VAL A CA  1 
ATOM   654  C  C   . VAL A 1 78  ? -20.613 8.465   18.113  1.00 17.44 ? 78  VAL A C   1 
ATOM   655  O  O   . VAL A 1 78  ? -21.633 7.778   18.123  1.00 20.43 ? 78  VAL A O   1 
ATOM   656  C  CB  . VAL A 1 78  ? -20.759 10.878  17.587  1.00 24.61 ? 78  VAL A CB  1 
ATOM   657  C  CG1 . VAL A 1 78  ? -20.539 12.052  16.645  1.00 27.17 ? 78  VAL A CG1 1 
ATOM   658  C  CG2 . VAL A 1 78  ? -22.155 10.849  18.082  1.00 26.60 ? 78  VAL A CG2 1 
ATOM   659  N  N   . LEU A 1 79  ? -19.627 8.323   18.991  1.00 15.52 ? 79  LEU A N   1 
ATOM   660  C  CA  . LEU A 1 79  ? -19.652 7.462   20.142  1.00 14.91 ? 79  LEU A CA  1 
ATOM   661  C  C   . LEU A 1 79  ? -19.654 8.355   21.370  1.00 14.99 ? 79  LEU A C   1 
ATOM   662  O  O   . LEU A 1 79  ? -18.800 9.247   21.479  1.00 17.27 ? 79  LEU A O   1 
ATOM   663  C  CB  . LEU A 1 79  ? -18.386 6.607   20.075  1.00 15.94 ? 79  LEU A CB  1 
ATOM   664  C  CG  . LEU A 1 79  ? -18.219 5.537   21.125  1.00 17.03 ? 79  LEU A CG  1 
ATOM   665  C  CD1 . LEU A 1 79  ? -19.238 4.444   20.902  1.00 22.25 ? 79  LEU A CD1 1 
ATOM   666  C  CD2 . LEU A 1 79  ? -16.825 4.963   20.999  1.00 17.78 ? 79  LEU A CD2 1 
ATOM   667  N  N   . LYS A 1 80  ? -20.545 8.049   22.303  1.00 16.94 ? 80  LYS A N   1 
ATOM   668  C  CA  . LYS A 1 80  ? -20.520 8.733   23.585  1.00 18.48 ? 80  LYS A CA  1 
ATOM   669  C  C   . LYS A 1 80  ? -21.033 7.816   24.680  1.00 17.79 ? 80  LYS A C   1 
ATOM   670  O  O   . LYS A 1 80  ? -21.347 6.668   24.380  1.00 19.22 ? 80  LYS A O   1 
ATOM   671  C  CB  . LYS A 1 80  ? -21.186 10.099  23.579  1.00 23.13 ? 80  LYS A CB  1 
ATOM   672  C  CG  . LYS A 1 80  ? -22.690 10.017  23.560  1.00 26.62 ? 80  LYS A CG  1 
ATOM   673  C  CD  . LYS A 1 80  ? -23.269 11.434  23.473  1.00 30.21 ? 80  LYS A CD  1 
ATOM   674  N  N   . GLY A 1 81  ? -21.070 8.332   25.902  1.00 20.56 ? 81  GLY A N   1 
ATOM   675  C  CA  . GLY A 1 81  ? -21.536 7.579   27.059  1.00 21.22 ? 81  GLY A CA  1 
ATOM   676  C  C   . GLY A 1 81  ? -20.500 6.485   27.369  1.00 20.07 ? 81  GLY A C   1 
ATOM   677  O  O   . GLY A 1 81  ? -19.298 6.639   27.107  1.00 20.19 ? 81  GLY A O   1 
ATOM   678  N  N   . GLY A 1 82  ? -20.971 5.369   27.919  1.00 25.51 ? 82  GLY A N   1 
ATOM   679  C  CA  . GLY A 1 82  ? -20.010 4.397   28.401  1.00 28.22 ? 82  GLY A CA  1 
ATOM   680  C  C   . GLY A 1 82  ? -19.076 5.043   29.422  1.00 25.72 ? 82  GLY A C   1 
ATOM   681  O  O   . GLY A 1 82  ? -19.490 5.829   30.277  1.00 29.47 ? 82  GLY A O   1 
ATOM   682  N  N   . PRO A 1 83  ? -17.757 4.814   29.282  1.00 21.64 ? 83  PRO A N   1 
ATOM   683  C  CA  . PRO A 1 83  ? -16.786 5.429   30.166  1.00 22.23 ? 83  PRO A CA  1 
ATOM   684  C  C   . PRO A 1 83  ? -16.370 6.814   29.687  1.00 21.17 ? 83  PRO A C   1 
ATOM   685  O  O   . PRO A 1 83  ? -15.516 7.424   30.318  1.00 25.72 ? 83  PRO A O   1 
ATOM   686  C  CB  . PRO A 1 83  ? -15.577 4.494   29.975  1.00 20.84 ? 83  PRO A CB  1 
ATOM   687  C  CG  . PRO A 1 83  ? -15.696 4.078   28.516  1.00 18.97 ? 83  PRO A CG  1 
ATOM   688  C  CD  . PRO A 1 83  ? -17.168 3.916   28.257  1.00 20.96 ? 83  PRO A CD  1 
ATOM   689  N  N   . LEU A 1 84  ? -16.954 7.298   28.572  1.00 18.46 ? 84  LEU A N   1 
ATOM   690  C  CA  . LEU A 1 84  ? -16.405 8.471   27.891  1.00 16.95 ? 84  LEU A CA  1 
ATOM   691  C  C   . LEU A 1 84  ? -17.013 9.736   28.481  1.00 19.00 ? 84  LEU A C   1 
ATOM   692  O  O   . LEU A 1 84  ? -18.181 9.766   28.807  1.00 22.10 ? 84  LEU A O   1 
ATOM   693  C  CB  . LEU A 1 84  ? -16.743 8.391   26.410  1.00 15.73 ? 84  LEU A CB  1 
ATOM   694  C  CG  . LEU A 1 84  ? -16.151 7.159   25.745  1.00 14.39 ? 84  LEU A CG  1 
ATOM   695  C  CD1 . LEU A 1 84  ? -16.588 7.072   24.303  1.00 17.02 ? 84  LEU A CD1 1 
ATOM   696  C  CD2 . LEU A 1 84  ? -14.628 7.150   25.840  1.00 14.52 ? 84  LEU A CD2 1 
ATOM   697  N  N   . ASP A 1 85  ? -16.203 10.783  28.555  1.00 22.67 ? 85  ASP A N   1 
ATOM   698  C  CA  . ASP A 1 85  ? -16.715 12.106  28.871  1.00 22.49 ? 85  ASP A CA  1 
ATOM   699  C  C   . ASP A 1 85  ? -16.687 12.830  27.548  1.00 23.41 ? 85  ASP A C   1 
ATOM   700  O  O   . ASP A 1 85  ? -15.701 12.777  26.823  1.00 29.68 ? 85  ASP A O   1 
ATOM   701  C  CB  . ASP A 1 85  ? -15.799 12.799  29.892  1.00 25.49 ? 85  ASP A CB  1 
ATOM   702  C  CG  . ASP A 1 85  ? -15.953 12.296  31.337  1.00 38.49 ? 85  ASP A CG  1 
ATOM   703  O  OD1 . ASP A 1 85  ? -17.057 11.787  31.731  1.00 48.80 ? 85  ASP A OD1 1 
ATOM   704  O  OD2 . ASP A 1 85  ? -14.950 12.392  32.091  1.00 43.63 ? 85  ASP A OD2 1 
ATOM   705  N  N   . GLY A 1 86  ? -17.766 13.451  27.177  1.00 26.51 ? 86  GLY A N   1 
ATOM   706  C  CA  . GLY A 1 86  ? -17.846 14.140  25.889  1.00 21.05 ? 86  GLY A CA  1 
ATOM   707  C  C   . GLY A 1 86  ? -18.182 13.261  24.661  1.00 23.75 ? 86  GLY A C   1 
ATOM   708  O  O   . GLY A 1 86  ? -18.768 12.191  24.766  1.00 31.81 ? 86  GLY A O   1 
ATOM   709  N  N   . THR A 1 87  ? -17.801 13.724  23.452  1.00 20.66 ? 87  THR A N   1 
ATOM   710  C  CA  . THR A 1 87  ? -18.312 13.223  22.162  1.00 20.08 ? 87  THR A CA  1 
ATOM   711  C  C   . THR A 1 87  ? -17.094 12.777  21.355  1.00 17.25 ? 87  THR A C   1 
ATOM   712  O  O   . THR A 1 87  ? -16.138 13.516  21.198  1.00 17.93 ? 87  THR A O   1 
ATOM   713  C  CB  . THR A 1 87  ? -19.083 14.332  21.414  1.00 27.85 ? 87  THR A CB  1 
ATOM   714  O  OG1 . THR A 1 87  ? -20.313 14.518  22.127  1.00 36.94 ? 87  THR A OG1 1 
ATOM   715  C  CG2 . THR A 1 87  ? -19.429 13.874  19.999  1.00 27.89 ? 87  THR A CG2 1 
ATOM   716  N  N   . TYR A 1 88  ? -17.135 11.563  20.838  1.00 14.96 ? 88  TYR A N   1 
ATOM   717  C  CA  . TYR A 1 88  ? -16.043 11.083  20.014  1.00 14.56 ? 88  TYR A CA  1 
ATOM   718  C  C   . TYR A 1 88  ? -16.560 10.778  18.623  1.00 15.24 ? 88  TYR A C   1 
ATOM   719  O  O   . TYR A 1 88  ? -17.580 10.136  18.479  1.00 20.09 ? 88  TYR A O   1 
ATOM   720  C  CB  . TYR A 1 88  ? -15.413 9.832   20.626  1.00 13.34 ? 88  TYR A CB  1 
ATOM   721  C  CG  . TYR A 1 88  ? -14.597 10.065  21.871  1.00 12.24 ? 88  TYR A CG  1 
ATOM   722  C  CD1 . TYR A 1 88  ? -15.202 10.493  23.038  1.00 13.01 ? 88  TYR A CD1 1 
ATOM   723  C  CD2 . TYR A 1 88  ? -13.219 9.822   21.837  1.00 10.73 ? 88  TYR A CD2 1 
ATOM   724  C  CE1 . TYR A 1 88  ? -14.460 10.615  24.198  1.00 14.59 ? 88  TYR A CE1 1 
ATOM   725  C  CE2 . TYR A 1 88  ? -12.472 9.984   22.977  1.00 12.40 ? 88  TYR A CE2 1 
ATOM   726  C  CZ  . TYR A 1 88  ? -13.085 10.365  24.155  1.00 12.80 ? 88  TYR A CZ  1 
ATOM   727  O  OH  . TYR A 1 88  ? -12.355 10.485  25.307  1.00 13.78 ? 88  TYR A OH  1 
ATOM   728  N  N   . ARG A 1 89  ? -15.856 11.250  17.605  1.00 13.14 ? 89  ARG A N   1 
ATOM   729  C  CA  . ARG A 1 89  ? -16.354 11.127  16.251  1.00 13.84 ? 89  ARG A CA  1 
ATOM   730  C  C   . ARG A 1 89  ? -15.639 10.027  15.465  1.00 11.70 ? 89  ARG A C   1 
ATOM   731  O  O   . ARG A 1 89  ? -14.403 9.914   15.511  1.00 10.71 ? 89  ARG A O   1 
ATOM   732  C  CB  . ARG A 1 89  ? -16.048 12.452  15.586  1.00 18.77 ? 89  ARG A CB  1 
ATOM   733  C  CG  . ARG A 1 89  ? -16.796 12.611  14.291  1.00 22.27 ? 89  ARG A CG  1 
ATOM   734  C  CD  . ARG A 1 89  ? -16.540 14.071  13.854  1.00 20.56 ? 89  ARG A CD  1 
ATOM   735  N  NE  . ARG A 1 89  ? -17.266 15.075  14.644  1.00 21.86 ? 89  ARG A NE  1 
ATOM   736  C  CZ  . ARG A 1 89  ? -17.115 16.375  14.464  1.00 17.67 ? 89  ARG A CZ  1 
ATOM   737  N  NH1 . ARG A 1 89  ? -16.314 16.836  13.508  1.00 19.85 ? 89  ARG A NH1 1 
ATOM   738  N  NH2 . ARG A 1 89  ? -17.823 17.220  15.213  1.00 23.46 ? 89  ARG A NH2 1 
ATOM   739  N  N   . LEU A 1 90  ? -16.393 9.191   14.728  1.00 12.64 ? 90  LEU A N   1 
ATOM   740  C  CA  . LEU A 1 90  ? -15.824 8.075   14.012  1.00 12.56 ? 90  LEU A CA  1 
ATOM   741  C  C   . LEU A 1 90  ? -15.007 8.648   12.855  1.00 11.42 ? 90  LEU A C   1 
ATOM   742  O  O   . LEU A 1 90  ? -15.482 9.473   12.044  1.00 15.72 ? 90  LEU A O   1 
ATOM   743  C  CB  . LEU A 1 90  ? -16.947 7.199   13.421  1.00 13.22 ? 90  LEU A CB  1 
ATOM   744  C  CG  . LEU A 1 90  ? -16.463 6.070   12.473  1.00 13.33 ? 90  LEU A CG  1 
ATOM   745  C  CD1 . LEU A 1 90  ? -15.705 4.965   13.244  1.00 14.46 ? 90  LEU A CD1 1 
ATOM   746  C  CD2 . LEU A 1 90  ? -17.700 5.440   11.838  1.00 16.20 ? 90  LEU A CD2 1 
ATOM   747  N  N   . THR A 1 91  ? -13.748 8.193   12.711  1.00 12.66 ? 91  THR A N   1 
ATOM   748  C  CA  . THR A 1 91  ? -12.875 8.616   11.625  1.00 12.24 ? 91  THR A CA  1 
ATOM   749  C  C   . THR A 1 91  ? -12.547 7.462   10.677  1.00 12.01 ? 91  THR A C   1 
ATOM   750  O  O   . THR A 1 91  ? -12.434 7.674   9.469   1.00 12.79 ? 91  THR A O   1 
ATOM   751  C  CB  . THR A 1 91  ? -11.656 9.355   12.166  1.00 14.37 ? 91  THR A CB  1 
ATOM   752  O  OG1 . THR A 1 91  ? -10.952 9.921   11.069  1.00 18.32 ? 91  THR A OG1 1 
ATOM   753  C  CG2 . THR A 1 91  ? -10.713 8.459   12.945  1.00 13.99 ? 91  THR A CG2 1 
ATOM   754  N  N   . GLN A 1 92  ? -12.414 6.204   11.188  1.00 11.91 ? 92  GLN A N   1 
ATOM   755  C  CA  . GLN A 1 92  ? -12.057 5.106   10.298  1.00 12.39 ? 92  GLN A CA  1 
ATOM   756  C  C   . GLN A 1 92  ? -12.310 3.810   11.022  1.00 11.27 ? 92  GLN A C   1 
ATOM   757  O  O   . GLN A 1 92  ? -12.424 3.801   12.250  1.00 11.29 ? 92  GLN A O   1 
ATOM   758  C  CB  . GLN A 1 92  ? -10.571 5.156   9.893   1.00 13.70 ? 92  GLN A CB  1 
ATOM   759  C  CG  . GLN A 1 92  ? -9.600  5.257   11.066  1.00 14.05 ? 92  GLN A CG  1 
ATOM   760  C  CD  . GLN A 1 92  ? -8.811  3.999   11.282  1.00 14.68 ? 92  GLN A CD  1 
ATOM   761  O  OE1 . GLN A 1 92  ? -9.310  2.887   11.163  1.00 14.36 ? 92  GLN A OE1 1 
ATOM   762  N  NE2 . GLN A 1 92  ? -7.550  4.155   11.638  1.00 17.87 ? 92  GLN A NE2 1 
ATOM   763  N  N   . PHE A 1 93  ? -12.373 2.707   10.244  1.00 11.67 ? 93  PHE A N   1 
ATOM   764  C  CA  . PHE A 1 93  ? -12.250 1.403   10.894  1.00 11.29 ? 93  PHE A CA  1 
ATOM   765  C  C   . PHE A 1 93  ? -11.270 0.568   10.113  1.00 12.33 ? 93  PHE A C   1 
ATOM   766  O  O   . PHE A 1 93  ? -11.010 0.795   8.904   1.00 12.43 ? 93  PHE A O   1 
ATOM   767  C  CB  . PHE A 1 93  ? -13.615 0.714   11.108  1.00 12.32 ? 93  PHE A CB  1 
ATOM   768  C  CG  . PHE A 1 93  ? -14.321 0.272   9.844   1.00 12.07 ? 93  PHE A CG  1 
ATOM   769  C  CD1 . PHE A 1 93  ? -13.913 -0.850  9.121   1.00 13.99 ? 93  PHE A CD1 1 
ATOM   770  C  CD2 . PHE A 1 93  ? -15.464 0.941   9.437   1.00 13.79 ? 93  PHE A CD2 1 
ATOM   771  C  CE1 . PHE A 1 93  ? -14.583 -1.255  7.972   1.00 14.48 ? 93  PHE A CE1 1 
ATOM   772  C  CE2 . PHE A 1 93  ? -16.155 0.530   8.301   1.00 13.60 ? 93  PHE A CE2 1 
ATOM   773  C  CZ  . PHE A 1 93  ? -15.716 -0.559  7.576   1.00 14.91 ? 93  PHE A CZ  1 
ATOM   774  N  N   . HIS A 1 94  ? -10.732 -0.449  10.764  1.00 11.10 ? 94  HIS A N   1 
ATOM   775  C  CA  . HIS A 1 94  ? -9.823  -1.375  10.116  1.00 10.59 ? 94  HIS A CA  1 
ATOM   776  C  C   . HIS A 1 94  ? -9.894  -2.644  10.926  1.00 9.56  ? 94  HIS A C   1 
ATOM   777  O  O   . HIS A 1 94  ? -10.579 -2.756  11.956  1.00 9.65  ? 94  HIS A O   1 
ATOM   778  C  CB  . HIS A 1 94  ? -8.383  -0.811  10.112  1.00 10.80 ? 94  HIS A CB  1 
ATOM   779  C  CG  . HIS A 1 94  ? -7.898  -0.551  11.495  1.00 10.23 ? 94  HIS A CG  1 
ATOM   780  N  ND1 . HIS A 1 94  ? -8.146  0.607   12.214  1.00 10.69 ? 94  HIS A ND1 1 
ATOM   781  C  CD2 . HIS A 1 94  ? -7.258  -1.369  12.370  1.00 9.36  ? 94  HIS A CD2 1 
ATOM   782  C  CE1 . HIS A 1 94  ? -7.633  0.474   13.451  1.00 10.00 ? 94  HIS A CE1 1 
ATOM   783  N  NE2 . HIS A 1 94  ? -7.104  -0.789  13.581  1.00 9.36  ? 94  HIS A NE2 1 
ATOM   784  N  N   . PHE A 1 95  ? -9.146  -3.657  10.480  1.00 10.08 ? 95  PHE A N   1 
ATOM   785  C  CA  . PHE A 1 95  ? -9.197  -4.961  11.119  1.00 9.10  ? 95  PHE A CA  1 
ATOM   786  C  C   . PHE A 1 95  ? -7.777  -5.483  11.342  1.00 9.65  ? 95  PHE A C   1 
ATOM   787  O  O   . PHE A 1 95  ? -6.818  -5.049  10.714  1.00 10.25 ? 95  PHE A O   1 
ATOM   788  C  CB  . PHE A 1 95  ? -9.880  -6.020  10.228  1.00 9.93  ? 95  PHE A CB  1 
ATOM   789  C  CG  . PHE A 1 95  ? -11.334 -5.732  9.954   1.00 9.33  ? 95  PHE A CG  1 
ATOM   790  C  CD1 . PHE A 1 95  ? -11.684 -4.830  8.954   1.00 11.58 ? 95  PHE A CD1 1 
ATOM   791  C  CD2 . PHE A 1 95  ? -12.317 -6.413  10.637  1.00 11.13 ? 95  PHE A CD2 1 
ATOM   792  C  CE1 . PHE A 1 95  ? -13.039 -4.628  8.661   1.00 12.51 ? 95  PHE A CE1 1 
ATOM   793  C  CE2 . PHE A 1 95  ? -13.653 -6.255  10.318  1.00 12.14 ? 95  PHE A CE2 1 
ATOM   794  C  CZ  . PHE A 1 95  ? -14.015 -5.338  9.322   1.00 12.97 ? 95  PHE A CZ  1 
ATOM   795  N  N   . HIS A 1 96  ? -7.658  -6.432  12.241  1.00 8.91  ? 96  HIS A N   1 
ATOM   796  C  CA  . HIS A 1 96  ? -6.473  -7.248  12.443  1.00 8.40  ? 96  HIS A CA  1 
ATOM   797  C  C   . HIS A 1 96  ? -6.923  -8.696  12.317  1.00 8.46  ? 96  HIS A C   1 
ATOM   798  O  O   . HIS A 1 96  ? -8.027  -9.032  12.792  1.00 9.29  ? 96  HIS A O   1 
ATOM   799  C  CB  . HIS A 1 96  ? -5.844  -7.023  13.848  1.00 9.20  ? 96  HIS A CB  1 
ATOM   800  C  CG  . HIS A 1 96  ? -5.546  -5.581  14.097  1.00 8.36  ? 96  HIS A CG  1 
ATOM   801  N  ND1 . HIS A 1 96  ? -4.313  -5.018  13.868  1.00 9.49  ? 96  HIS A ND1 1 
ATOM   802  C  CD2 . HIS A 1 96  ? -6.346  -4.552  14.471  1.00 8.96  ? 96  HIS A CD2 1 
ATOM   803  C  CE1 . HIS A 1 96  ? -4.389  -3.707  14.174  1.00 9.22  ? 96  HIS A CE1 1 
ATOM   804  N  NE2 . HIS A 1 96  ? -5.613  -3.392  14.519  1.00 9.10  ? 96  HIS A NE2 1 
ATOM   805  N  N   . TRP A 1 97  ? -6.128  -9.570  11.674  1.00 9.09  ? 97  TRP A N   1 
ATOM   806  C  CA  . TRP A 1 97  ? -6.574  -10.930 11.515  1.00 9.17  ? 97  TRP A CA  1 
ATOM   807  C  C   . TRP A 1 97  ? -5.395  -11.876 11.386  1.00 9.65  ? 97  TRP A C   1 
ATOM   808  O  O   . TRP A 1 97  ? -4.209  -11.455 11.326  1.00 10.19 ? 97  TRP A O   1 
ATOM   809  C  CB  . TRP A 1 97  ? -7.484  -11.076 10.285  1.00 10.76 ? 97  TRP A CB  1 
ATOM   810  C  CG  . TRP A 1 97  ? -6.800  -10.699 8.993   1.00 9.88  ? 97  TRP A CG  1 
ATOM   811  C  CD1 . TRP A 1 97  ? -6.122  -11.545 8.150   1.00 10.95 ? 97  TRP A CD1 1 
ATOM   812  C  CD2 . TRP A 1 97  ? -6.722  -9.406  8.406   1.00 10.39 ? 97  TRP A CD2 1 
ATOM   813  N  NE1 . TRP A 1 97  ? -5.630  -10.867 7.059   1.00 12.50 ? 97  TRP A NE1 1 
ATOM   814  C  CE2 . TRP A 1 97  ? -5.979  -9.548  7.212   1.00 10.17 ? 97  TRP A CE2 1 
ATOM   815  C  CE3 . TRP A 1 97  ? -7.181  -8.128  8.777   1.00 10.32 ? 97  TRP A CE3 1 
ATOM   816  C  CZ2 . TRP A 1 97  ? -5.704  -8.476  6.372   1.00 12.31 ? 97  TRP A CZ2 1 
ATOM   817  C  CZ3 . TRP A 1 97  ? -6.944  -7.054  7.947   1.00 11.69 ? 97  TRP A CZ3 1 
ATOM   818  C  CH2 . TRP A 1 97  ? -6.203  -7.235  6.757   1.00 12.08 ? 97  TRP A CH2 1 
ATOM   819  N  N   . GLY A 1 98  ? -5.701  -13.174 11.381  1.00 9.96  ? 98  GLY A N   1 
ATOM   820  C  CA  . GLY A 1 98  ? -4.678  -14.197 11.458  1.00 10.52 ? 98  GLY A CA  1 
ATOM   821  C  C   . GLY A 1 98  ? -4.468  -14.931 10.142  1.00 10.85 ? 98  GLY A C   1 
ATOM   822  O  O   . GLY A 1 98  ? -5.188  -14.742 9.187   1.00 12.20 ? 98  GLY A O   1 
ATOM   823  N  N   . SER A 1 99  ? -3.481  -15.825 10.170  1.00 11.46 ? 99  SER A N   1 
ATOM   824  C  CA  . SER A 1 99  ? -3.243  -16.757 9.092   1.00 13.31 ? 99  SER A CA  1 
ATOM   825  C  C   . SER A 1 99  ? -4.138  -17.989 9.246   1.00 13.24 ? 99  SER A C   1 
ATOM   826  O  O   . SER A 1 99  ? -4.274  -18.734 8.280   1.00 18.35 ? 99  SER A O   1 
ATOM   827  C  CB  . SER A 1 99  ? -1.808  -17.144 9.041   1.00 16.34 ? 99  SER A CB  1 
ATOM   828  O  OG  . SER A 1 99  ? -1.386  -17.628 10.324  1.00 14.72 ? 99  SER A OG  1 
ATOM   829  N  N   . LEU A 1 100 ? -4.708  -18.215 10.420  1.00 13.26 ? 100 LEU A N   1 
ATOM   830  C  CA  . LEU A 1 100 ? -5.541  -19.350 10.768  1.00 15.76 ? 100 LEU A CA  1 
ATOM   831  C  C   . LEU A 1 100 ? -6.668  -18.820 11.625  1.00 14.59 ? 100 LEU A C   1 
ATOM   832  O  O   . LEU A 1 100 ? -6.480  -17.827 12.307  1.00 14.99 ? 100 LEU A O   1 
ATOM   833  C  CB  . LEU A 1 100 ? -4.737  -20.306 11.668  1.00 22.33 ? 100 LEU A CB  1 
ATOM   834  C  CG  . LEU A 1 100 ? -3.465  -20.811 11.043  1.00 22.11 ? 100 LEU A CG  1 
ATOM   835  C  CD1 . LEU A 1 100 ? -2.473  -21.340 12.080  1.00 28.41 ? 100 LEU A CD1 1 
ATOM   836  C  CD2 . LEU A 1 100 ? -3.841  -21.898 10.029  1.00 28.05 ? 100 LEU A CD2 1 
ATOM   837  N  N   . ASP A 1 101 ? -7.766  -19.568 11.722  1.00 14.98 ? 101 ASP A N   1 
ATOM   838  C  CA  . ASP A 1 101 ? -8.955  -19.064 12.391  1.00 14.45 ? 101 ASP A CA  1 
ATOM   839  C  C   . ASP A 1 101 ? -8.701  -18.993 13.911  1.00 14.53 ? 101 ASP A C   1 
ATOM   840  O  O   . ASP A 1 101 ? -9.397  -18.230 14.580  1.00 16.77 ? 101 ASP A O   1 
ATOM   841  C  CB  . ASP A 1 101 ? -10.178 -19.924 12.094  1.00 15.73 ? 101 ASP A CB  1 
ATOM   842  C  CG  . ASP A 1 101 ? -10.657 -19.950 10.659  1.00 17.72 ? 101 ASP A CG  1 
ATOM   843  O  OD1 . ASP A 1 101 ? -10.230 -19.139 9.805   1.00 17.83 ? 101 ASP A OD1 1 
ATOM   844  O  OD2 . ASP A 1 101 ? -11.480 -20.814 10.388  1.00 22.12 ? 101 ASP A OD2 1 
ATOM   845  N  N   . GLY A 1 102 ? -7.719  -19.753 14.439  1.00 16.24 ? 102 GLY A N   1 
ATOM   846  C  CA  . GLY A 1 102 ? -7.391  -19.733 15.850  1.00 16.26 ? 102 GLY A CA  1 
ATOM   847  C  C   . GLY A 1 102 ? -6.538  -18.578 16.330  1.00 13.89 ? 102 GLY A C   1 
ATOM   848  O  O   . GLY A 1 102 ? -6.157  -18.528 17.504  1.00 15.36 ? 102 GLY A O   1 
ATOM   849  N  N   . GLN A 1 103 ? -6.271  -17.564 15.493  1.00 13.39 ? 103 GLN A N   1 
ATOM   850  C  CA  . GLN A 1 103 ? -5.520  -16.393 15.961  1.00 11.25 ? 103 GLN A CA  1 
ATOM   851  C  C   . GLN A 1 103 ? -5.883  -15.225 15.061  1.00 10.19 ? 103 GLN A C   1 
ATOM   852  O  O   . GLN A 1 103 ? -6.430  -15.441 13.971  1.00 11.34 ? 103 GLN A O   1 
ATOM   853  C  CB  . GLN A 1 103 ? -4.024  -16.687 15.937  1.00 11.24 ? 103 GLN A CB  1 
ATOM   854  C  CG  . GLN A 1 103 ? -3.469  -16.915 14.533  1.00 12.48 ? 103 GLN A CG  1 
ATOM   855  C  CD  . GLN A 1 103 ? -2.073  -17.472 14.581  1.00 17.80 ? 103 GLN A CD  1 
ATOM   856  O  OE1 . GLN A 1 103 ? -1.157  -17.054 13.864  1.00 18.45 ? 103 GLN A OE1 1 
ATOM   857  N  NE2 . GLN A 1 103 ? -1.901  -18.461 15.397  1.00 22.33 ? 103 GLN A NE2 1 
ATOM   858  N  N   . GLY A 1 104 ? -5.533  -14.018 15.526  1.00 9.44  ? 104 GLY A N   1 
ATOM   859  C  CA  . GLY A 1 104 ? -5.832  -12.873 14.691  1.00 9.23  ? 104 GLY A CA  1 
ATOM   860  C  C   . GLY A 1 104 ? -6.279  -11.679 15.492  1.00 8.94  ? 104 GLY A C   1 
ATOM   861  O  O   . GLY A 1 104 ? -5.997  -10.539 15.114  1.00 10.19 ? 104 GLY A O   1 
ATOM   862  N  N   . SER A 1 105 ? -6.980  -11.917 16.624  1.00 8.47  ? 105 SER A N   1 
ATOM   863  C  CA  . SER A 1 105 ? -7.359  -10.785 17.458  1.00 8.67  ? 105 SER A CA  1 
ATOM   864  C  C   . SER A 1 105 ? -6.149  -10.231 18.212  1.00 8.25  ? 105 SER A C   1 
ATOM   865  O  O   . SER A 1 105 ? -5.128  -10.909 18.412  1.00 9.79  ? 105 SER A O   1 
ATOM   866  C  CB  . SER A 1 105 ? -8.498  -11.128 18.379  1.00 8.45  ? 105 SER A CB  1 
ATOM   867  O  OG  . SER A 1 105 ? -8.131  -12.090 19.370  1.00 8.88  ? 105 SER A OG  1 
ATOM   868  N  N   . GLU A 1 106 ? -6.279  -8.978  18.614  1.00 8.31  ? 106 GLU A N   1 
ATOM   869  C  CA  . GLU A 1 106 ? -5.276  -8.285  19.419  1.00 8.54  ? 106 GLU A CA  1 
ATOM   870  C  C   . GLU A 1 106 ? -5.608  -8.501  20.881  1.00 8.22  ? 106 GLU A C   1 
ATOM   871  O  O   . GLU A 1 106 ? -4.839  -9.076  21.666  1.00 8.93  ? 106 GLU A O   1 
ATOM   872  C  CB  . GLU A 1 106 ? -5.212  -6.808  19.018  1.00 8.80  ? 106 GLU A CB  1 
ATOM   873  C  CG  . GLU A 1 106 ? -4.858  -6.664  17.532  1.00 10.00 ? 106 GLU A CG  1 
ATOM   874  C  CD  . GLU A 1 106 ? -4.104  -5.426  17.274  1.00 9.12  ? 106 GLU A CD  1 
ATOM   875  O  OE1 . GLU A 1 106 ? -4.674  -4.343  17.484  1.00 9.89  ? 106 GLU A OE1 1 
ATOM   876  O  OE2 . GLU A 1 106 ? -2.912  -5.512  16.863  1.00 10.93 ? 106 GLU A OE2 1 
ATOM   877  N  N   . HIS A 1 107 ? -6.788  -8.032  21.289  1.00 8.31  ? 107 HIS A N   1 
ATOM   878  C  CA  . HIS A 1 107 ? -7.246  -8.393  22.619  1.00 8.23  ? 107 HIS A CA  1 
ATOM   879  C  C   . HIS A 1 107 ? -7.548  -9.893  22.662  1.00 8.32  ? 107 HIS A C   1 
ATOM   880  O  O   . HIS A 1 107 ? -7.878  -10.499 21.633  1.00 8.92  ? 107 HIS A O   1 
ATOM   881  C  CB  . HIS A 1 107 ? -8.492  -7.612  23.017  1.00 8.29  ? 107 HIS A CB  1 
ATOM   882  C  CG  . HIS A 1 107 ? -8.140  -6.169  23.173  1.00 7.74  ? 107 HIS A CG  1 
ATOM   883  N  ND1 . HIS A 1 107 ? -8.196  -5.278  22.105  1.00 8.55  ? 107 HIS A ND1 1 
ATOM   884  C  CD2 . HIS A 1 107 ? -7.727  -5.455  24.254  1.00 8.13  ? 107 HIS A CD2 1 
ATOM   885  C  CE1 . HIS A 1 107 ? -7.768  -4.073  22.545  1.00 9.19  ? 107 HIS A CE1 1 
ATOM   886  N  NE2 . HIS A 1 107 ? -7.461  -4.161  23.857  1.00 8.24  ? 107 HIS A NE2 1 
ATOM   887  N  N   . THR A 1 108 ? -7.446  -10.456 23.873  1.00 9.42  ? 108 THR A N   1 
ATOM   888  C  CA  . THR A 1 108 ? -7.828  -11.838 24.096  1.00 9.49  ? 108 THR A CA  1 
ATOM   889  C  C   . THR A 1 108 ? -8.782  -11.821 25.288  1.00 8.79  ? 108 THR A C   1 
ATOM   890  O  O   . THR A 1 108 ? -8.785  -10.868 26.069  1.00 9.97  ? 108 THR A O   1 
ATOM   891  C  CB  . THR A 1 108 ? -6.616  -12.755 24.299  1.00 9.88  ? 108 THR A CB  1 
ATOM   892  O  OG1 . THR A 1 108 ? -5.794  -12.265 25.367  1.00 10.99 ? 108 THR A OG1 1 
ATOM   893  C  CG2 . THR A 1 108 ? -5.741  -12.794 23.048  1.00 12.00 ? 108 THR A CG2 1 
ATOM   894  N  N   . VAL A 1 109 ? -9.561  -12.904 25.438  1.00 10.22 ? 109 VAL A N   1 
ATOM   895  C  CA  . VAL A 1 109 ? -10.517 -12.983 26.545  1.00 11.19 ? 109 VAL A CA  1 
ATOM   896  C  C   . VAL A 1 109 ? -10.206 -14.280 27.268  1.00 10.62 ? 109 VAL A C   1 
ATOM   897  O  O   . VAL A 1 109 ? -10.406 -15.356 26.695  1.00 11.96 ? 109 VAL A O   1 
ATOM   898  C  CB  . VAL A 1 109 ? -11.966 -12.990 25.975  1.00 12.29 ? 109 VAL A CB  1 
ATOM   899  C  CG1 . VAL A 1 109 ? -12.977 -13.138 27.102  1.00 13.98 ? 109 VAL A CG1 1 
ATOM   900  C  CG2 . VAL A 1 109 ? -12.247 -11.757 25.123  1.00 14.28 ? 109 VAL A CG2 1 
ATOM   901  N  N   . ASP A 1 110 ? -9.772  -14.187 28.514  1.00 11.80 ? 110 ASP A N   1 
ATOM   902  C  CA  . ASP A 1 110 ? -9.310  -15.401 29.188  1.00 14.01 ? 110 ASP A CA  1 
ATOM   903  C  C   . ASP A 1 110 ? -8.324  -16.194 28.332  1.00 12.92 ? 110 ASP A C   1 
ATOM   904  O  O   . ASP A 1 110 ? -8.388  -17.427 28.296  1.00 15.05 ? 110 ASP A O   1 
ATOM   905  C  CB  . ASP A 1 110 ? -10.497 -16.209 29.698  1.00 16.92 ? 110 ASP A CB  1 
ATOM   906  C  CG  . ASP A 1 110 ? -11.347 -15.432 30.708  1.00 16.57 ? 110 ASP A CG  1 
ATOM   907  O  OD1 . ASP A 1 110 ? -10.798 -14.586 31.405  1.00 17.98 ? 110 ASP A OD1 1 
ATOM   908  O  OD2 . ASP A 1 110 ? -12.567 -15.673 30.741  1.00 22.63 ? 110 ASP A OD2 1 
ATOM   909  N  N   . LYS A 1 111 ? -7.435  -15.480 27.629  1.00 12.33 ? 111 LYS A N   1 
ATOM   910  C  CA  . LYS A 1 111 ? -6.371  -16.001 26.773  1.00 12.57 ? 111 LYS A CA  1 
ATOM   911  C  C   . LYS A 1 111 ? -6.931  -16.536 25.456  1.00 12.27 ? 111 LYS A C   1 
ATOM   912  O  O   . LYS A 1 111 ? -6.162  -16.844 24.556  1.00 14.65 ? 111 LYS A O   1 
ATOM   913  C  CB  . LYS A 1 111 ? -5.530  -17.098 27.458  1.00 15.86 ? 111 LYS A CB  1 
ATOM   914  C  CG  . LYS A 1 111 ? -4.913  -16.615 28.756  1.00 20.76 ? 111 LYS A CG  1 
ATOM   915  C  CD  . LYS A 1 111 ? -3.945  -15.467 28.459  1.00 23.72 ? 111 LYS A CD  1 
ATOM   916  C  CE  . LYS A 1 111 ? -3.165  -14.977 29.672  1.00 30.35 ? 111 LYS A CE  1 
ATOM   917  N  NZ  . LYS A 1 111 ? -1.761  -15.382 29.497  1.00 32.71 ? 111 LYS A NZ  1 
ATOM   918  N  N   . LYS A 1 112 ? -8.247  -16.515 25.244  1.00 12.20 ? 112 LYS A N   1 
ATOM   919  C  CA  . LYS A 1 112 ? -8.790  -16.929 23.959  1.00 11.56 ? 112 LYS A CA  1 
ATOM   920  C  C   . LYS A 1 112 ? -8.507  -15.865 22.873  1.00 11.01 ? 112 LYS A C   1 
ATOM   921  O  O   . LYS A 1 112 ? -8.763  -14.692 23.083  1.00 11.31 ? 112 LYS A O   1 
ATOM   922  C  CB  . LYS A 1 112 ? -10.318 -17.049 24.021  1.00 14.64 ? 112 LYS A CB  1 
ATOM   923  C  CG  . LYS A 1 112 ? -11.019 -17.400 22.700  1.00 17.41 ? 112 LYS A CG  1 
ATOM   924  C  CD  . LYS A 1 112 ? -12.533 -17.539 22.764  1.00 21.02 ? 112 LYS A CD  1 
ATOM   925  C  CE  . LYS A 1 112 ? -13.091 -17.759 21.380  1.00 24.24 ? 112 LYS A CE  1 
ATOM   926  N  NZ  . LYS A 1 112 ? -12.496 -18.917 20.700  1.00 31.89 ? 112 LYS A NZ  1 
ATOM   927  N  N   A LYS A 1 113 ? -7.975  -16.324 21.739  0.50 10.96 ? 113 LYS A N   1 
ATOM   928  N  N   B LYS A 1 113 ? -7.975  -16.324 21.738  0.50 11.33 ? 113 LYS A N   1 
ATOM   929  C  CA  A LYS A 1 113 ? -7.781  -15.497 20.569  0.50 10.83 ? 113 LYS A CA  1 
ATOM   930  C  CA  B LYS A 1 113 ? -7.776  -15.501 20.565  0.50 11.47 ? 113 LYS A CA  1 
ATOM   931  C  C   A LYS A 1 113 ? -8.916  -15.741 19.583  0.50 10.31 ? 113 LYS A C   1 
ATOM   932  C  C   B LYS A 1 113 ? -8.912  -15.740 19.579  0.50 10.52 ? 113 LYS A C   1 
ATOM   933  O  O   A LYS A 1 113 ? -9.308  -16.881 19.356  0.50 12.72 ? 113 LYS A O   1 
ATOM   934  O  O   B LYS A 1 113 ? -9.295  -16.881 19.342  0.50 15.45 ? 113 LYS A O   1 
ATOM   935  C  CB  A LYS A 1 113 ? -6.496  -15.885 19.849  0.50 11.31 ? 113 LYS A CB  1 
ATOM   936  C  CB  B LYS A 1 113 ? -6.482  -15.884 19.855  0.50 11.70 ? 113 LYS A CB  1 
ATOM   937  C  CG  A LYS A 1 113 ? -5.238  -15.634 20.662  0.50 11.25 ? 113 LYS A CG  1 
ATOM   938  C  CG  B LYS A 1 113 ? -5.235  -15.605 20.677  0.50 12.86 ? 113 LYS A CG  1 
ATOM   939  C  CD  A LYS A 1 113 ? -4.028  -16.219 19.992  0.50 12.65 ? 113 LYS A CD  1 
ATOM   940  C  CD  B LYS A 1 113 ? -3.963  -16.161 20.089  0.50 14.41 ? 113 LYS A CD  1 
ATOM   941  C  CE  A LYS A 1 113 ? -2.731  -15.763 20.632  0.50 14.20 ? 113 LYS A CE  1 
ATOM   942  C  CE  B LYS A 1 113 ? -2.760  -15.530 20.774  0.50 15.00 ? 113 LYS A CE  1 
ATOM   943  N  NZ  A LYS A 1 113 ? -2.459  -16.517 21.871  0.50 15.20 ? 113 LYS A NZ  1 
ATOM   944  N  NZ  B LYS A 1 113 ? -1.518  -16.326 20.636  0.50 18.14 ? 113 LYS A NZ  1 
ATOM   945  N  N   . TYR A 1 114 ? -9.462  -14.652 19.060  1.00 9.68  ? 114 TYR A N   1 
ATOM   946  C  CA  . TYR A 1 114 ? -10.489 -14.757 18.003  1.00 9.47  ? 114 TYR A CA  1 
ATOM   947  C  C   . TYR A 1 114 ? -9.784  -14.694 16.637  1.00 9.06  ? 114 TYR A C   1 
ATOM   948  O  O   . TYR A 1 114 ? -8.590  -14.406 16.524  1.00 10.60 ? 114 TYR A O   1 
ATOM   949  C  CB  . TYR A 1 114 ? -11.460 -13.604 18.127  1.00 9.45  ? 114 TYR A CB  1 
ATOM   950  C  CG  . TYR A 1 114 ? -12.392 -13.858 19.293  1.00 9.55  ? 114 TYR A CG  1 
ATOM   951  C  CD1 . TYR A 1 114 ? -12.114 -13.400 20.572  1.00 12.10 ? 114 TYR A CD1 1 
ATOM   952  C  CD2 . TYR A 1 114 ? -13.611 -14.490 19.098  1.00 11.05 ? 114 TYR A CD2 1 
ATOM   953  C  CE1 . TYR A 1 114 ? -12.995 -13.606 21.626  1.00 13.79 ? 114 TYR A CE1 1 
ATOM   954  C  CE2 . TYR A 1 114 ? -14.501 -14.703 20.140  1.00 14.65 ? 114 TYR A CE2 1 
ATOM   955  C  CZ  . TYR A 1 114 ? -14.197 -14.260 21.415  1.00 14.79 ? 114 TYR A CZ  1 
ATOM   956  O  OH  . TYR A 1 114 ? -15.084 -14.468 22.442  1.00 22.22 ? 114 TYR A OH  1 
ATOM   957  N  N   . ALA A 1 115 ? -10.550 -14.955 15.581  1.00 9.71  ? 115 ALA A N   1 
ATOM   958  C  CA  . ALA A 1 115 ? -10.026 -14.994 14.224  1.00 9.33  ? 115 ALA A CA  1 
ATOM   959  C  C   . ALA A 1 115 ? -9.614  -13.606 13.770  1.00 9.95  ? 115 ALA A C   1 
ATOM   960  O  O   . ALA A 1 115 ? -8.760  -13.474 12.861  1.00 10.51 ? 115 ALA A O   1 
ATOM   961  C  CB  . ALA A 1 115 ? -11.010 -15.599 13.256  1.00 11.21 ? 115 ALA A CB  1 
ATOM   962  N  N   . ALA A 1 116 ? -10.265 -12.559 14.272  1.00 8.99  ? 116 ALA A N   1 
ATOM   963  C  CA  . ALA A 1 116 ? -9.976  -11.196 13.802  1.00 8.32  ? 116 ALA A CA  1 
ATOM   964  C  C   . ALA A 1 116 ? -10.555 -10.245 14.826  1.00 8.37  ? 116 ALA A C   1 
ATOM   965  O  O   . ALA A 1 116 ? -11.299 -10.648 15.740  1.00 8.95  ? 116 ALA A O   1 
ATOM   966  C  CB  . ALA A 1 116 ? -10.471 -10.937 12.370  1.00 9.97  ? 116 ALA A CB  1 
ATOM   967  N  N   . GLU A 1 117 ? -10.205 -8.953  14.666  1.00 8.53  ? 117 GLU A N   1 
ATOM   968  C  CA  . GLU A 1 117 ? -10.740 -7.912  15.539  1.00 8.14  ? 117 GLU A CA  1 
ATOM   969  C  C   . GLU A 1 117 ? -10.922 -6.684  14.673  1.00 8.83  ? 117 GLU A C   1 
ATOM   970  O  O   . GLU A 1 117 ? -10.005 -6.298  13.930  1.00 9.95  ? 117 GLU A O   1 
ATOM   971  C  CB  . GLU A 1 117 ? -9.759  -7.699  16.687  1.00 8.82  ? 117 GLU A CB  1 
ATOM   972  C  CG  . GLU A 1 117 ? -10.271 -6.744  17.767  1.00 8.80  ? 117 GLU A CG  1 
ATOM   973  C  CD  . GLU A 1 117 ? -9.368  -6.710  18.987  1.00 9.71  ? 117 GLU A CD  1 
ATOM   974  O  OE1 . GLU A 1 117 ? -8.717  -7.731  19.277  1.00 9.47  ? 117 GLU A OE1 1 
ATOM   975  O  OE2 . GLU A 1 117 ? -9.313  -5.606  19.633  1.00 11.04 ? 117 GLU A OE2 1 
ATOM   976  N  N   . LEU A 1 118 ? -12.089 -6.109  14.799  1.00 8.47  ? 118 LEU A N   1 
ATOM   977  C  CA  . LEU A 1 118 ? -12.494 -4.857  14.147  1.00 8.32  ? 118 LEU A CA  1 
ATOM   978  C  C   . LEU A 1 118 ? -12.259 -3.712  15.129  1.00 8.24  ? 118 LEU A C   1 
ATOM   979  O  O   . LEU A 1 118 ? -12.658 -3.805  16.276  1.00 8.55  ? 118 LEU A O   1 
ATOM   980  C  CB  . LEU A 1 118 ? -13.982 -4.981  13.799  1.00 9.75  ? 118 LEU A CB  1 
ATOM   981  C  CG  . LEU A 1 118 ? -14.706 -3.651  13.473  1.00 10.19 ? 118 LEU A CG  1 
ATOM   982  C  CD1 . LEU A 1 118 ? -14.136 -2.984  12.225  1.00 12.04 ? 118 LEU A CD1 1 
ATOM   983  C  CD2 . LEU A 1 118 ? -16.167 -3.976  13.210  1.00 12.98 ? 118 LEU A CD2 1 
ATOM   984  N  N   . HIS A 1 119 ? -11.630 -2.636  14.650  1.00 8.13  ? 119 HIS A N   1 
ATOM   985  C  CA  . HIS A 1 119 ? -11.393 -1.436  15.441  1.00 8.46  ? 119 HIS A CA  1 
ATOM   986  C  C   . HIS A 1 119 ? -12.077 -0.271  14.756  1.00 8.09  ? 119 HIS A C   1 
ATOM   987  O  O   . HIS A 1 119 ? -11.708 0.097   13.622  1.00 9.63  ? 119 HIS A O   1 
ATOM   988  C  CB  . HIS A 1 119 ? -9.864  -1.146  15.520  1.00 8.63  ? 119 HIS A CB  1 
ATOM   989  C  CG  . HIS A 1 119 ? -9.226  -2.153  16.427  1.00 7.75  ? 119 HIS A CG  1 
ATOM   990  N  ND1 . HIS A 1 119 ? -7.859  -2.359  16.417  1.00 8.39  ? 119 HIS A ND1 1 
ATOM   991  C  CD2 . HIS A 1 119 ? -9.751  -2.956  17.359  1.00 8.60  ? 119 HIS A CD2 1 
ATOM   992  C  CE1 . HIS A 1 119 ? -7.559  -3.276  17.328  1.00 8.80  ? 119 HIS A CE1 1 
ATOM   993  N  NE2 . HIS A 1 119 ? -8.702  -3.669  17.902  1.00 8.53  ? 119 HIS A NE2 1 
ATOM   994  N  N   . LEU A 1 120 ? -13.078 0.294   15.435  1.00 8.01  ? 120 LEU A N   1 
ATOM   995  C  CA  . LEU A 1 120 ? -13.751 1.518   15.003  1.00 8.81  ? 120 LEU A CA  1 
ATOM   996  C  C   . LEU A 1 120 ? -13.155 2.668   15.815  1.00 7.95  ? 120 LEU A C   1 
ATOM   997  O  O   . LEU A 1 120 ? -13.247 2.674   17.020  1.00 8.46  ? 120 LEU A O   1 
ATOM   998  C  CB  . LEU A 1 120 ? -15.260 1.361   15.241  1.00 9.39  ? 120 LEU A CB  1 
ATOM   999  C  CG  . LEU A 1 120 ? -15.967 0.339   14.347  1.00 10.44 ? 120 LEU A CG  1 
ATOM   1000 C  CD1 . LEU A 1 120 ? -16.872 -0.560  15.152  1.00 14.66 ? 120 LEU A CD1 1 
ATOM   1001 C  CD2 . LEU A 1 120 ? -16.697 1.038   13.217  1.00 13.21 ? 120 LEU A CD2 1 
ATOM   1002 N  N   . VAL A 1 121 ? -12.480 3.569   15.111  1.00 9.27  ? 121 VAL A N   1 
ATOM   1003 C  CA  . VAL A 1 121 ? -11.580 4.564   15.729  1.00 9.40  ? 121 VAL A CA  1 
ATOM   1004 C  C   . VAL A 1 121 ? -12.301 5.900   15.763  1.00 10.20 ? 121 VAL A C   1 
ATOM   1005 O  O   . VAL A 1 121 ? -12.758 6.383   14.712  1.00 11.41 ? 121 VAL A O   1 
ATOM   1006 C  CB  . VAL A 1 121 ? -10.237 4.662   14.942  1.00 9.29  ? 121 VAL A CB  1 
ATOM   1007 C  CG1 . VAL A 1 121 ? -9.306  5.659   15.627  1.00 10.95 ? 121 VAL A CG1 1 
ATOM   1008 C  CG2 . VAL A 1 121 ? -9.621  3.286   14.748  1.00 11.39 ? 121 VAL A CG2 1 
ATOM   1009 N  N   . HIS A 1 122 ? -12.371 6.495   16.949  1.00 9.22  ? 122 HIS A N   1 
ATOM   1010 C  CA  . HIS A 1 122 ? -13.083 7.754   17.138  1.00 9.57  ? 122 HIS A CA  1 
ATOM   1011 C  C   . HIS A 1 122 ? -12.162 8.742   17.850  1.00 9.34  ? 122 HIS A C   1 
ATOM   1012 O  O   . HIS A 1 122 ? -11.363 8.341   18.707  1.00 10.59 ? 122 HIS A O   1 
ATOM   1013 C  CB  . HIS A 1 122 ? -14.313 7.549   18.017  1.00 9.68  ? 122 HIS A CB  1 
ATOM   1014 C  CG  . HIS A 1 122 ? -15.179 6.428   17.598  1.00 10.11 ? 122 HIS A CG  1 
ATOM   1015 N  ND1 . HIS A 1 122 ? -14.824 5.100   17.830  1.00 10.56 ? 122 HIS A ND1 1 
ATOM   1016 C  CD2 . HIS A 1 122 ? -16.410 6.388   17.024  1.00 11.58 ? 122 HIS A CD2 1 
ATOM   1017 C  CE1 . HIS A 1 122 ? -15.819 4.322   17.417  1.00 11.21 ? 122 HIS A CE1 1 
ATOM   1018 N  NE2 . HIS A 1 122 ? -16.819 5.078   16.917  1.00 11.11 ? 122 HIS A NE2 1 
ATOM   1019 N  N   . TRP A 1 123 ? -12.309 10.034  17.581  1.00 9.61  ? 123 TRP A N   1 
ATOM   1020 C  CA  . TRP A 1 123 ? -11.488 11.042  18.264  1.00 9.77  ? 123 TRP A CA  1 
ATOM   1021 C  C   . TRP A 1 123 ? -12.358 11.994  19.059  1.00 10.22 ? 123 TRP A C   1 
ATOM   1022 O  O   . TRP A 1 123 ? -13.482 12.333  18.648  1.00 12.35 ? 123 TRP A O   1 
ATOM   1023 C  CB  . TRP A 1 123 ? -10.564 11.792  17.290  1.00 11.75 ? 123 TRP A CB  1 
ATOM   1024 C  CG  . TRP A 1 123 ? -11.259 12.432  16.125  1.00 12.11 ? 123 TRP A CG  1 
ATOM   1025 C  CD1 . TRP A 1 123 ? -11.572 11.771  14.962  1.00 14.39 ? 123 TRP A CD1 1 
ATOM   1026 C  CD2 . TRP A 1 123 ? -11.761 13.767  15.970  1.00 14.29 ? 123 TRP A CD2 1 
ATOM   1027 N  NE1 . TRP A 1 123 ? -12.164 12.609  14.070  1.00 16.66 ? 123 TRP A NE1 1 
ATOM   1028 C  CE2 . TRP A 1 123 ? -12.350 13.844  14.677  1.00 15.82 ? 123 TRP A CE2 1 
ATOM   1029 C  CE3 . TRP A 1 123 ? -11.791 14.888  16.794  1.00 14.18 ? 123 TRP A CE3 1 
ATOM   1030 C  CZ2 . TRP A 1 123 ? -12.906 15.035  14.193  1.00 18.24 ? 123 TRP A CZ2 1 
ATOM   1031 C  CZ3 . TRP A 1 123 ? -12.331 16.061  16.320  1.00 17.77 ? 123 TRP A CZ3 1 
ATOM   1032 C  CH2 . TRP A 1 123 ? -12.852 16.147  15.011  1.00 18.08 ? 123 TRP A CH2 1 
ATOM   1033 N  N   . ASN A 1 124 ? -11.799 12.441  20.194  1.00 10.56 ? 124 ASN A N   1 
ATOM   1034 C  CA  . ASN A 1 124 ? -12.510 13.324  21.102  1.00 12.60 ? 124 ASN A CA  1 
ATOM   1035 C  C   . ASN A 1 124 ? -12.662 14.688  20.448  1.00 11.41 ? 124 ASN A C   1 
ATOM   1036 O  O   . ASN A 1 124 ? -11.663 15.355  20.150  1.00 11.63 ? 124 ASN A O   1 
ATOM   1037 C  CB  . ASN A 1 124 ? -11.703 13.358  22.396  1.00 12.77 ? 124 ASN A CB  1 
ATOM   1038 C  CG  . ASN A 1 124 ? -12.424 14.026  23.527  1.00 13.98 ? 124 ASN A CG  1 
ATOM   1039 O  OD1 . ASN A 1 124 ? -13.240 14.938  23.258  1.00 15.63 ? 124 ASN A OD1 1 
ATOM   1040 N  ND2 . ASN A 1 124 ? -12.095 13.563  24.748  1.00 15.08 ? 124 ASN A ND2 1 
ATOM   1041 N  N   . THR A 1 125 ? -13.915 15.138  20.244  1.00 13.55 ? 125 THR A N   1 
ATOM   1042 C  CA  . THR A 1 125 ? -14.151 16.412  19.538  1.00 13.41 ? 125 THR A CA  1 
ATOM   1043 C  C   . THR A 1 125 ? -13.499 17.612  20.272  1.00 13.93 ? 125 THR A C   1 
ATOM   1044 O  O   . THR A 1 125 ? -13.357 18.651  19.613  1.00 15.69 ? 125 THR A O   1 
ATOM   1045 C  CB  . THR A 1 125 ? -15.629 16.620  19.192  1.00 18.08 ? 125 THR A CB  1 
ATOM   1046 O  OG1 . THR A 1 125 ? -16.351 16.643  20.439  1.00 21.29 ? 125 THR A OG1 1 
ATOM   1047 C  CG2 . THR A 1 125 ? -16.119 15.507  18.293  1.00 21.55 ? 125 THR A CG2 1 
ATOM   1048 N  N   . LYS A 1 126 ? -13.294 17.498  21.586  1.00 13.68 ? 127 LYS A N   1 
ATOM   1049 C  CA  . LYS A 1 126 ? -12.680 18.658  22.270  1.00 17.41 ? 127 LYS A CA  1 
ATOM   1050 C  C   . LYS A 1 126 ? -11.294 18.995  21.706  1.00 14.90 ? 127 LYS A C   1 
ATOM   1051 O  O   . LYS A 1 126 ? -10.796 20.074  21.941  1.00 17.70 ? 127 LYS A O   1 
ATOM   1052 C  CB  . LYS A 1 126 ? -12.730 18.410  23.777  1.00 19.31 ? 127 LYS A CB  1 
ATOM   1053 C  CG  . LYS A 1 126 ? -11.677 17.519  24.385  1.00 20.12 ? 127 LYS A CG  1 
ATOM   1054 C  CD  . LYS A 1 126 ? -11.946 17.112  25.873  1.00 27.31 ? 127 LYS A CD  1 
ATOM   1055 C  CE  . LYS A 1 126 ? -10.683 17.249  26.700  1.00 39.76 ? 127 LYS A CE  1 
ATOM   1056 N  NZ  . LYS A 1 126 ? -10.866 17.190  28.175  1.00 37.67 ? 127 LYS A NZ  1 
ATOM   1057 N  N   . TYR A 1 127 ? -10.664 18.090  20.946  1.00 10.94 ? 128 TYR A N   1 
ATOM   1058 C  CA  . TYR A 1 127 ? -9.345  18.306  20.398  1.00 10.68 ? 128 TYR A CA  1 
ATOM   1059 C  C   . TYR A 1 127 ? -9.359  18.654  18.919  1.00 11.39 ? 128 TYR A C   1 
ATOM   1060 O  O   . TYR A 1 127 ? -8.283  18.908  18.349  1.00 13.62 ? 128 TYR A O   1 
ATOM   1061 C  CB  . TYR A 1 127 ? -8.405  17.130  20.676  1.00 12.00 ? 128 TYR A CB  1 
ATOM   1062 C  CG  . TYR A 1 127 ? -8.291  16.842  22.141  1.00 11.61 ? 128 TYR A CG  1 
ATOM   1063 C  CD1 . TYR A 1 127 ? -7.814  17.808  23.016  1.00 15.23 ? 128 TYR A CD1 1 
ATOM   1064 C  CD2 . TYR A 1 127 ? -8.577  15.585  22.645  1.00 12.40 ? 128 TYR A CD2 1 
ATOM   1065 C  CE1 . TYR A 1 127 ? -7.744  17.550  24.363  1.00 16.04 ? 128 TYR A CE1 1 
ATOM   1066 C  CE2 . TYR A 1 127 ? -8.490  15.306  24.012  1.00 13.49 ? 128 TYR A CE2 1 
ATOM   1067 C  CZ  . TYR A 1 127 ? -8.063  16.322  24.887  1.00 13.70 ? 128 TYR A CZ  1 
ATOM   1068 O  OH  . TYR A 1 127 ? -7.943  16.123  26.217  1.00 16.91 ? 128 TYR A OH  1 
ATOM   1069 N  N   . GLY A 1 128 ? -10.557 18.787  18.320  1.00 11.88 ? 129 GLY A N   1 
ATOM   1070 C  CA  . GLY A 1 128 ? -10.645 19.467  17.046  1.00 13.00 ? 129 GLY A CA  1 
ATOM   1071 C  C   . GLY A 1 128 ? -10.343 18.613  15.817  1.00 14.07 ? 129 GLY A C   1 
ATOM   1072 O  O   . GLY A 1 128 ? -10.983 18.772  14.789  1.00 17.48 ? 129 GLY A O   1 
ATOM   1073 N  N   . ASP A 1 129 ? -9.340  17.731  15.905  1.00 15.78 ? 130 ASP A N   1 
ATOM   1074 C  CA  . ASP A 1 129 ? -8.992  16.848  14.821  1.00 16.50 ? 130 ASP A CA  1 
ATOM   1075 C  C   . ASP A 1 129 ? -8.302  15.609  15.383  1.00 17.43 ? 130 ASP A C   1 
ATOM   1076 O  O   . ASP A 1 129 ? -7.821  15.601  16.505  1.00 16.45 ? 130 ASP A O   1 
ATOM   1077 C  CB  . ASP A 1 129 ? -8.088  17.526  13.765  1.00 23.48 ? 130 ASP A CB  1 
ATOM   1078 C  CG  . ASP A 1 129 ? -6.654  17.847  14.177  1.00 27.21 ? 130 ASP A CG  1 
ATOM   1079 O  OD1 . ASP A 1 129 ? -5.827  16.946  14.256  1.00 28.24 ? 130 ASP A OD1 1 
ATOM   1080 O  OD2 . ASP A 1 129 ? -6.279  19.037  14.283  1.00 35.79 ? 130 ASP A OD2 1 
ATOM   1081 N  N   . ALA A 1 130 ? -8.340  14.544  14.561  1.00 18.97 ? 131 ALA A N   1 
ATOM   1082 C  CA  . ALA A 1 130 ? -7.839  13.249  14.994  1.00 17.73 ? 131 ALA A CA  1 
ATOM   1083 C  C   . ALA A 1 130 ? -6.343  13.328  15.350  1.00 17.08 ? 131 ALA A C   1 
ATOM   1084 O  O   . ALA A 1 130 ? -5.859  12.604  16.231  1.00 14.95 ? 131 ALA A O   1 
ATOM   1085 C  CB  . ALA A 1 130 ? -8.116  12.161  13.975  1.00 21.54 ? 131 ALA A CB  1 
ATOM   1086 N  N   . GLY A 1 131 ? -5.576  14.121  14.576  1.00 19.05 ? 132 GLY A N   1 
ATOM   1087 C  CA  . GLY A 1 131 ? -4.131  14.178  14.787  1.00 20.61 ? 132 GLY A CA  1 
ATOM   1088 C  C   . GLY A 1 131 ? -3.797  14.764  16.157  1.00 16.42 ? 132 GLY A C   1 
ATOM   1089 O  O   . GLY A 1 131 ? -3.019  14.202  16.944  1.00 20.66 ? 132 GLY A O   1 
ATOM   1090 N  N   A LYS A 1 132 ? -4.425  15.897  16.478  0.25 16.96 ? 133 LYS A N   1 
ATOM   1091 N  N   B LYS A 1 132 ? -4.491  15.870  16.453  0.25 15.66 ? 133 LYS A N   1 
ATOM   1092 N  N   C LYS A 1 132 ? -4.436  15.903  16.476  0.50 16.08 ? 133 LYS A N   1 
ATOM   1093 C  CA  A LYS A 1 132 ? -4.211  16.456  17.800  0.25 15.93 ? 133 LYS A CA  1 
ATOM   1094 C  CA  B LYS A 1 132 ? -4.347  16.572  17.717  0.25 13.18 ? 133 LYS A CA  1 
ATOM   1095 C  CA  C LYS A 1 132 ? -4.207  16.491  17.787  0.50 17.17 ? 133 LYS A CA  1 
ATOM   1096 C  C   A LYS A 1 132 ? -4.708  15.476  18.850  0.25 12.69 ? 133 LYS A C   1 
ATOM   1097 C  C   B LYS A 1 132 ? -4.847  15.714  18.877  0.25 13.59 ? 133 LYS A C   1 
ATOM   1098 C  C   C LYS A 1 132 ? -4.758  15.576  18.882  0.50 13.87 ? 133 LYS A C   1 
ATOM   1099 O  O   A LYS A 1 132 ? -4.025  15.228  19.843  0.25 13.21 ? 133 LYS A O   1 
ATOM   1100 O  O   B LYS A 1 132 ? -4.294  15.774  19.975  0.25 13.69 ? 133 LYS A O   1 
ATOM   1101 O  O   C LYS A 1 132 ? -4.161  15.454  19.953  0.50 13.89 ? 133 LYS A O   1 
ATOM   1102 C  CB  A LYS A 1 132 ? -5.008  17.742  17.980  0.25 15.51 ? 133 LYS A CB  1 
ATOM   1103 C  CB  B LYS A 1 132 ? -5.072  17.918  17.670  0.25 11.33 ? 133 LYS A CB  1 
ATOM   1104 C  CB  C LYS A 1 132 ? -4.771  17.912  17.914  0.50 15.91 ? 133 LYS A CB  1 
ATOM   1105 C  CG  A LYS A 1 132 ? -4.873  18.685  16.812  0.25 16.30 ? 133 LYS A CG  1 
ATOM   1106 C  CG  B LYS A 1 132 ? -4.266  19.070  17.098  0.25 13.45 ? 133 LYS A CG  1 
ATOM   1107 C  CG  C LYS A 1 132 ? -4.903  18.420  19.359  0.50 17.80 ? 133 LYS A CG  1 
ATOM   1108 C  CD  A LYS A 1 132 ? -3.482  19.133  16.543  0.25 13.90 ? 133 LYS A CD  1 
ATOM   1109 C  CD  B LYS A 1 132 ? -2.977  19.372  17.857  0.25 14.35 ? 133 LYS A CD  1 
ATOM   1110 C  CD  C LYS A 1 132 ? -3.883  19.517  19.741  0.50 26.80 ? 133 LYS A CD  1 
ATOM   1111 C  CE  A LYS A 1 132 ? -3.636  20.355  15.687  0.25 10.61 ? 133 LYS A CE  1 
ATOM   1112 C  CE  C LYS A 1 132 ? -4.186  20.204  21.060  0.50 22.87 ? 133 LYS A CE  1 
ATOM   1113 N  N   . ALA A 1 133 ? -5.915  14.940  18.628  1.00 12.14 ? 134 ALA A N   1 
ATOM   1114 C  CA  . ALA A 1 133 ? -6.456  14.033  19.635  1.00 11.19 ? 134 ALA A CA  1 
ATOM   1115 C  C   . ALA A 1 133 ? -5.476  12.909  19.990  1.00 11.89 ? 134 ALA A C   1 
ATOM   1116 O  O   . ALA A 1 133 ? -5.409  12.482  21.147  1.00 12.33 ? 134 ALA A O   1 
ATOM   1117 C  CB  . ALA A 1 133 ? -7.757  13.429  19.121  1.00 11.81 ? 134 ALA A CB  1 
ATOM   1118 N  N   . SER A 1 134 ? -4.728  12.415  19.008  1.00 12.97 ? 135 SER A N   1 
ATOM   1119 C  CA  . SER A 1 134 ? -3.823  11.273  19.261  1.00 13.80 ? 135 SER A CA  1 
ATOM   1120 C  C   . SER A 1 134 ? -2.641  11.667  20.153  1.00 13.31 ? 135 SER A C   1 
ATOM   1121 O  O   . SER A 1 134 ? -1.956  10.781  20.636  1.00 17.07 ? 135 SER A O   1 
ATOM   1122 C  CB  . SER A 1 134 ? -3.332  10.755  17.931  1.00 18.74 ? 135 SER A CB  1 
ATOM   1123 O  OG  . SER A 1 134 ? -2.304  11.572  17.383  1.00 21.14 ? 135 SER A OG  1 
ATOM   1124 N  N   . GLN A 1 135 ? -2.495  12.962  20.484  1.00 13.65 ? 136 GLN A N   1 
ATOM   1125 C  CA  . GLN A 1 135 ? -1.465  13.458  21.381  1.00 16.88 ? 136 GLN A CA  1 
ATOM   1126 C  C   . GLN A 1 135 ? -1.990  13.620  22.808  1.00 15.36 ? 136 GLN A C   1 
ATOM   1127 O  O   . GLN A 1 135 ? -1.283  14.097  23.711  1.00 19.77 ? 136 GLN A O   1 
ATOM   1128 C  CB  . GLN A 1 135 ? -0.872  14.795  20.857  1.00 21.63 ? 136 GLN A CB  1 
ATOM   1129 C  CG  . GLN A 1 135 ? -0.494  14.739  19.399  1.00 23.42 ? 136 GLN A CG  1 
ATOM   1130 C  CD  . GLN A 1 135 ? 0.560   13.692  19.124  1.00 35.53 ? 136 GLN A CD  1 
ATOM   1131 O  OE1 . GLN A 1 135 ? 1.616   13.666  19.752  1.00 48.06 ? 136 GLN A OE1 1 
ATOM   1132 N  NE2 . GLN A 1 135 ? 0.236   12.758  18.247  1.00 41.57 ? 136 GLN A NE2 1 
ATOM   1133 N  N   . GLN A 1 136 ? -3.240  13.201  23.050  1.00 13.27 ? 137 GLN A N   1 
ATOM   1134 C  CA  . GLN A 1 136 ? -3.836  13.456  24.360  1.00 12.91 ? 137 GLN A CA  1 
ATOM   1135 C  C   . GLN A 1 136 ? -4.173  12.149  25.031  1.00 12.91 ? 137 GLN A C   1 
ATOM   1136 O  O   . GLN A 1 136 ? -4.576  11.199  24.363  1.00 12.68 ? 137 GLN A O   1 
ATOM   1137 C  CB  . GLN A 1 136 ? -5.129  14.272  24.224  1.00 14.49 ? 137 GLN A CB  1 
ATOM   1138 C  CG  . GLN A 1 136 ? -4.931  15.517  23.332  1.00 17.50 ? 137 GLN A CG  1 
ATOM   1139 C  CD  . GLN A 1 136 ? -3.912  16.428  23.931  1.00 20.16 ? 137 GLN A CD  1 
ATOM   1140 O  OE1 . GLN A 1 136 ? -3.786  16.542  25.155  1.00 21.10 ? 137 GLN A OE1 1 
ATOM   1141 N  NE2 . GLN A 1 136 ? -3.226  17.186  23.066  1.00 29.54 ? 137 GLN A NE2 1 
ATOM   1142 N  N   . PRO A 1 137 ? -4.113  12.090  26.383  1.00 13.09 ? 138 PRO A N   1 
ATOM   1143 C  CA  . PRO A 1 137 ? -4.352  10.823  27.045  1.00 13.63 ? 138 PRO A CA  1 
ATOM   1144 C  C   . PRO A 1 137 ? -5.768  10.280  26.928  1.00 14.49 ? 138 PRO A C   1 
ATOM   1145 O  O   . PRO A 1 137 ? -5.946  9.085   27.060  1.00 17.48 ? 138 PRO A O   1 
ATOM   1146 C  CB  . PRO A 1 137 ? -3.999  11.093  28.492  1.00 18.96 ? 138 PRO A CB  1 
ATOM   1147 C  CG  . PRO A 1 137 ? -3.979  12.573  28.589  1.00 23.26 ? 138 PRO A CG  1 
ATOM   1148 C  CD  . PRO A 1 137 ? -3.639  13.176  27.272  1.00 17.50 ? 138 PRO A CD  1 
ATOM   1149 N  N   . ASP A 1 138 ? -6.738  11.177  26.645  1.00 12.58 ? 139 ASP A N   1 
ATOM   1150 C  CA  . ASP A 1 138 ? -8.161  10.839  26.425  1.00 14.24 ? 139 ASP A CA  1 
ATOM   1151 C  C   . ASP A 1 138 ? -8.547  11.233  25.004  1.00 12.55 ? 139 ASP A C   1 
ATOM   1152 O  O   . ASP A 1 138 ? -9.653  11.666  24.741  1.00 13.28 ? 139 ASP A O   1 
ATOM   1153 C  CB  . ASP A 1 138 ? -9.055  11.538  27.458  1.00 16.63 ? 139 ASP A CB  1 
ATOM   1154 C  CG  . ASP A 1 138 ? -8.964  13.045  27.411  1.00 18.73 ? 139 ASP A CG  1 
ATOM   1155 O  OD1 . ASP A 1 138 ? -7.999  13.596  26.795  1.00 17.65 ? 139 ASP A OD1 1 
ATOM   1156 O  OD2 . ASP A 1 138 ? -9.820  13.690  28.074  1.00 22.63 ? 139 ASP A OD2 1 
ATOM   1157 N  N   . GLY A 1 139 ? -7.618  11.131  24.051  1.00 10.13 ? 140 GLY A N   1 
ATOM   1158 C  CA  . GLY A 1 139 ? -7.880  11.637  22.714  1.00 10.09 ? 140 GLY A CA  1 
ATOM   1159 C  C   . GLY A 1 139 ? -8.728  10.724  21.846  1.00 8.97  ? 140 GLY A C   1 
ATOM   1160 O  O   . GLY A 1 139 ? -9.463  11.232  21.008  1.00 9.75  ? 140 GLY A O   1 
ATOM   1161 N  N   . LEU A 1 140 ? -8.526  9.419   21.972  1.00 9.53  ? 141 LEU A N   1 
ATOM   1162 C  CA  . LEU A 1 140 ? -9.206  8.495   21.077  1.00 8.36  ? 141 LEU A CA  1 
ATOM   1163 C  C   . LEU A 1 140 ? -10.030 7.524   21.889  1.00 8.03  ? 141 LEU A C   1 
ATOM   1164 O  O   . LEU A 1 140 ? -9.712  7.208   23.023  1.00 9.08  ? 141 LEU A O   1 
ATOM   1165 C  CB  . LEU A 1 140 ? -8.212  7.692   20.221  1.00 9.84  ? 141 LEU A CB  1 
ATOM   1166 C  CG  . LEU A 1 140 ? -7.296  8.499   19.316  1.00 12.40 ? 141 LEU A CG  1 
ATOM   1167 C  CD1 . LEU A 1 140 ? -6.444  7.596   18.480  1.00 13.65 ? 141 LEU A CD1 1 
ATOM   1168 C  CD2 . LEU A 1 140 ? -7.982  9.495   18.430  1.00 13.93 ? 141 LEU A CD2 1 
ATOM   1169 N  N   . ALA A 1 141 ? -11.088 7.010   21.238  1.00 8.49  ? 142 ALA A N   1 
ATOM   1170 C  CA  . ALA A 1 141 ? -11.844 5.896   21.783  1.00 9.27  ? 142 ALA A CA  1 
ATOM   1171 C  C   . ALA A 1 141 ? -11.956 4.887   20.668  1.00 8.42  ? 142 ALA A C   1 
ATOM   1172 O  O   . ALA A 1 141 ? -12.380 5.216   19.573  1.00 9.40  ? 142 ALA A O   1 
ATOM   1173 C  CB  . ALA A 1 141 ? -13.229 6.294   22.243  1.00 10.64 ? 142 ALA A CB  1 
ATOM   1174 N  N   . VAL A 1 142 ? -11.466 3.666   20.918  1.00 8.75  ? 143 VAL A N   1 
ATOM   1175 C  CA  . VAL A 1 142 ? -11.537 2.616   19.902  1.00 8.70  ? 143 VAL A CA  1 
ATOM   1176 C  C   . VAL A 1 142 ? -12.530 1.576   20.421  1.00 7.77  ? 143 VAL A C   1 
ATOM   1177 O  O   . VAL A 1 142 ? -12.377 1.056   21.515  1.00 8.30  ? 143 VAL A O   1 
ATOM   1178 C  CB  . VAL A 1 142 ? -10.171 1.995   19.568  1.00 8.56  ? 143 VAL A CB  1 
ATOM   1179 C  CG1 . VAL A 1 142 ? -10.379 0.986   18.424  1.00 9.66  ? 143 VAL A CG1 1 
ATOM   1180 C  CG2 . VAL A 1 142 ? -9.213  3.072   19.096  1.00 9.82  ? 143 VAL A CG2 1 
ATOM   1181 N  N   . LEU A 1 143 ? -13.529 1.325   19.576  1.00 8.63  ? 144 LEU A N   1 
ATOM   1182 C  CA  . LEU A 1 143 ? -14.500 0.267   19.815  1.00 8.76  ? 144 LEU A CA  1 
ATOM   1183 C  C   . LEU A 1 143 ? -13.977 -0.986  19.153  1.00 7.64  ? 144 LEU A C   1 
ATOM   1184 O  O   . LEU A 1 143 ? -13.820 -0.994  17.942  1.00 9.44  ? 144 LEU A O   1 
ATOM   1185 C  CB  . LEU A 1 143 ? -15.846 0.736   19.258  1.00 11.09 ? 144 LEU A CB  1 
ATOM   1186 C  CG  . LEU A 1 143 ? -17.018 -0.217  19.449  1.00 11.57 ? 144 LEU A CG  1 
ATOM   1187 C  CD1 . LEU A 1 143 ? -17.284 -0.451  20.960  1.00 15.17 ? 144 LEU A CD1 1 
ATOM   1188 C  CD2 . LEU A 1 143 ? -18.270 0.359   18.758  1.00 15.36 ? 144 LEU A CD2 1 
ATOM   1189 N  N   . GLY A 1 144 ? -13.663 -1.998  19.969  1.00 8.23  ? 145 GLY A N   1 
ATOM   1190 C  CA  . GLY A 1 144 ? -13.138 -3.241  19.436  1.00 8.06  ? 145 GLY A CA  1 
ATOM   1191 C  C   . GLY A 1 144 ? -14.205 -4.313  19.450  1.00 8.11  ? 145 GLY A C   1 
ATOM   1192 O  O   . GLY A 1 144 ? -14.904 -4.484  20.421  1.00 9.19  ? 145 GLY A O   1 
ATOM   1193 N  N   . ILE A 1 145 ? -14.263 -5.055  18.350  1.00 8.04  ? 146 ILE A N   1 
ATOM   1194 C  CA  . ILE A 1 145 ? -15.272 -6.081  18.185  1.00 8.29  ? 146 ILE A CA  1 
ATOM   1195 C  C   . ILE A 1 145 ? -14.569 -7.313  17.665  1.00 8.25  ? 146 ILE A C   1 
ATOM   1196 O  O   . ILE A 1 145 ? -13.847 -7.298  16.661  1.00 8.82  ? 146 ILE A O   1 
ATOM   1197 C  CB  . ILE A 1 145 ? -16.353 -5.610  17.189  1.00 9.33  ? 146 ILE A CB  1 
ATOM   1198 C  CG1 . ILE A 1 145 ? -17.006 -4.334  17.727  1.00 10.89 ? 146 ILE A CG1 1 
ATOM   1199 C  CG2 . ILE A 1 145 ? -17.387 -6.738  16.967  1.00 11.55 ? 146 ILE A CG2 1 
ATOM   1200 C  CD1 . ILE A 1 145 ? -18.089 -3.714  16.785  1.00 12.18 ? 146 ILE A CD1 1 
ATOM   1201 N  N   . PHE A 1 146 ? -14.765 -8.430  18.359  1.00 8.43  ? 147 PHE A N   1 
ATOM   1202 C  CA  . PHE A 1 146 ? -14.123 -9.687  17.929  1.00 8.54  ? 147 PHE A CA  1 
ATOM   1203 C  C   . PHE A 1 146 ? -14.893 -10.310 16.782  1.00 8.86  ? 147 PHE A C   1 
ATOM   1204 O  O   . PHE A 1 146 ? -16.125 -10.209 16.734  1.00 10.15 ? 147 PHE A O   1 
ATOM   1205 C  CB  . PHE A 1 146 ? -14.149 -10.673 19.109  1.00 8.96  ? 147 PHE A CB  1 
ATOM   1206 C  CG  . PHE A 1 146 ? -13.328 -10.200 20.264  1.00 8.06  ? 147 PHE A CG  1 
ATOM   1207 C  CD1 . PHE A 1 146 ? -11.942 -10.047 20.082  1.00 8.82  ? 147 PHE A CD1 1 
ATOM   1208 C  CD2 . PHE A 1 146 ? -13.867 -9.955  21.521  1.00 8.64  ? 147 PHE A CD2 1 
ATOM   1209 C  CE1 . PHE A 1 146 ? -11.149 -9.657  21.149  1.00 8.90  ? 147 PHE A CE1 1 
ATOM   1210 C  CE2 . PHE A 1 146 ? -13.057 -9.552  22.580  1.00 9.69  ? 147 PHE A CE2 1 
ATOM   1211 C  CZ  . PHE A 1 146 ? -11.711 -9.437  22.395  1.00 8.69  ? 147 PHE A CZ  1 
ATOM   1212 N  N   . LEU A 1 147 ? -14.173 -11.022 15.920  1.00 9.07  ? 148 LEU A N   1 
ATOM   1213 C  CA  . LEU A 1 147 ? -14.779 -11.816 14.843  1.00 8.91  ? 148 LEU A CA  1 
ATOM   1214 C  C   . LEU A 1 147 ? -14.424 -13.273 15.047  1.00 8.69  ? 148 LEU A C   1 
ATOM   1215 O  O   . LEU A 1 147 ? -13.273 -13.621 15.268  1.00 10.42 ? 148 LEU A O   1 
ATOM   1216 C  CB  . LEU A 1 147 ? -14.155 -11.389 13.492  1.00 10.70 ? 148 LEU A CB  1 
ATOM   1217 C  CG  . LEU A 1 147 ? -14.751 -10.164 12.844  1.00 11.02 ? 148 LEU A CG  1 
ATOM   1218 C  CD1 . LEU A 1 147 ? -14.522 -8.888  13.705  1.00 12.86 ? 148 LEU A CD1 1 
ATOM   1219 C  CD2 . LEU A 1 147 ? -14.131 -9.950  11.450  1.00 12.63 ? 148 LEU A CD2 1 
ATOM   1220 N  N   . LYS A 1 148 ? -15.469 -14.123 15.011  1.00 9.98  ? 149 LYS A N   1 
ATOM   1221 C  CA  . LYS A 1 148 ? -15.267 -15.558 14.981  1.00 10.35 ? 149 LYS A CA  1 
ATOM   1222 C  C   . LYS A 1 148 ? -15.792 -16.068 13.652  1.00 10.52 ? 149 LYS A C   1 
ATOM   1223 O  O   . LYS A 1 148 ? -16.603 -15.426 12.989  1.00 12.79 ? 149 LYS A O   1 
ATOM   1224 C  CB  . LYS A 1 148 ? -16.034 -16.225 16.136  1.00 13.54 ? 149 LYS A CB  1 
ATOM   1225 C  CG  . LYS A 1 148 ? -17.557 -16.090 16.082  1.00 14.64 ? 149 LYS A CG  1 
ATOM   1226 C  CD  . LYS A 1 148 ? -18.223 -16.824 17.262  1.00 20.77 ? 149 LYS A CD  1 
ATOM   1227 C  CE  . LYS A 1 148 ? -19.731 -16.740 17.177  1.00 29.14 ? 149 LYS A CE  1 
ATOM   1228 N  NZ  . LYS A 1 148 ? -20.415 -17.453 18.278  1.00 39.78 ? 149 LYS A NZ  1 
ATOM   1229 N  N   . VAL A 1 149 ? -15.293 -17.234 13.276  1.00 12.51 ? 150 VAL A N   1 
ATOM   1230 C  CA  . VAL A 1 149 ? -15.682 -17.781 11.979  1.00 12.07 ? 150 VAL A CA  1 
ATOM   1231 C  C   . VAL A 1 149 ? -16.893 -18.696 12.168  1.00 13.81 ? 150 VAL A C   1 
ATOM   1232 O  O   . VAL A 1 149 ? -16.873 -19.651 12.946  1.00 14.34 ? 150 VAL A O   1 
ATOM   1233 C  CB  . VAL A 1 149 ? -14.494 -18.502 11.334  1.00 13.06 ? 150 VAL A CB  1 
ATOM   1234 C  CG1 . VAL A 1 149 ? -14.878 -19.284 10.080  1.00 14.81 ? 150 VAL A CG1 1 
ATOM   1235 C  CG2 . VAL A 1 149 ? -13.400 -17.526 11.044  1.00 16.14 ? 150 VAL A CG2 1 
ATOM   1236 N  N   . GLY A 1 150 ? -17.950 -18.456 11.391  1.00 13.28 ? 151 GLY A N   1 
ATOM   1237 C  CA  . GLY A 1 150 ? -19.148 -19.289 11.435  1.00 15.21 ? 151 GLY A CA  1 
ATOM   1238 C  C   . GLY A 1 150 ? -20.050 -18.829 10.305  1.00 13.09 ? 151 GLY A C   1 
ATOM   1239 O  O   . GLY A 1 150 ? -19.653 -18.901 9.142   1.00 14.06 ? 151 GLY A O   1 
ATOM   1240 N  N   A SER A 1 151 ? -21.234 -18.319 10.640  0.50 16.04 ? 152 SER A N   1 
ATOM   1241 N  N   B SER A 1 151 ? -21.201 -18.270 10.687  0.50 15.76 ? 152 SER A N   1 
ATOM   1242 C  CA  A SER A 1 151 ? -22.108 -17.784 9.595   0.50 16.58 ? 152 SER A CA  1 
ATOM   1243 C  CA  B SER A 1 151 ? -22.111 -17.666 9.717   0.50 16.13 ? 152 SER A CA  1 
ATOM   1244 C  C   A SER A 1 151 ? -21.569 -16.442 9.113   0.50 13.11 ? 152 SER A C   1 
ATOM   1245 C  C   B SER A 1 151 ? -21.446 -16.452 9.071   0.50 13.76 ? 152 SER A C   1 
ATOM   1246 O  O   A SER A 1 151 ? -20.946 -15.710 9.889   0.50 12.54 ? 152 SER A O   1 
ATOM   1247 O  O   B SER A 1 151 ? -20.554 -15.841 9.657   0.50 13.39 ? 152 SER A O   1 
ATOM   1248 C  CB  A SER A 1 151 ? -23.485 -17.610 10.136  0.50 20.77 ? 152 SER A CB  1 
ATOM   1249 C  CB  B SER A 1 151 ? -23.425 -17.324 10.387  0.50 19.35 ? 152 SER A CB  1 
ATOM   1250 O  OG  A SER A 1 151 ? -23.451 -16.655 11.181  0.50 19.97 ? 152 SER A OG  1 
ATOM   1251 O  OG  B SER A 1 151 ? -24.069 -18.512 10.849  0.50 19.85 ? 152 SER A OG  1 
ATOM   1252 N  N   . ALA A 1 152 ? -21.863 -16.102 7.848   1.00 14.05 ? 153 ALA A N   1 
ATOM   1253 C  CA  . ALA A 1 152 ? -21.435 -14.835 7.261   1.00 14.90 ? 153 ALA A CA  1 
ATOM   1254 C  C   . ALA A 1 152 ? -22.087 -13.654 7.966   1.00 13.75 ? 153 ALA A C   1 
ATOM   1255 O  O   . ALA A 1 152 ? -23.189 -13.712 8.497   1.00 16.31 ? 153 ALA A O   1 
ATOM   1256 C  CB  . ALA A 1 152 ? -21.801 -14.826 5.769   1.00 18.01 ? 153 ALA A CB  1 
ATOM   1257 N  N   . LYS A 1 153 ? -21.375 -12.535 7.900   1.00 13.97 ? 154 LYS A N   1 
ATOM   1258 C  CA  . LYS A 1 153 ? -21.915 -11.251 8.339   1.00 13.73 ? 154 LYS A CA  1 
ATOM   1259 C  C   . LYS A 1 153 ? -22.324 -10.484 7.084   1.00 14.33 ? 154 LYS A C   1 
ATOM   1260 O  O   . LYS A 1 153 ? -21.477 -10.025 6.303   1.00 14.64 ? 154 LYS A O   1 
ATOM   1261 C  CB  . LYS A 1 153 ? -20.820 -10.497 9.120   1.00 14.65 ? 154 LYS A CB  1 
ATOM   1262 C  CG  . LYS A 1 153 ? -21.341 -9.263  9.835   1.00 16.29 ? 154 LYS A CG  1 
ATOM   1263 C  CD  . LYS A 1 153 ? -22.261 -9.621  10.963  1.00 18.09 ? 154 LYS A CD  1 
ATOM   1264 C  CE  . LYS A 1 153 ? -22.449 -8.475  11.936  1.00 21.72 ? 154 LYS A CE  1 
ATOM   1265 N  NZ  . LYS A 1 153 ? -23.532 -8.844  12.874  1.00 28.67 ? 154 LYS A NZ  1 
ATOM   1266 N  N   . PRO A 1 154 ? -23.648 -10.370 6.791   1.00 14.97 ? 155 PRO A N   1 
ATOM   1267 C  CA  . PRO A 1 154 ? -24.055 -9.770  5.506   1.00 15.99 ? 155 PRO A CA  1 
ATOM   1268 C  C   . PRO A 1 154 ? -23.528 -8.342  5.340   1.00 16.25 ? 155 PRO A C   1 
ATOM   1269 O  O   . PRO A 1 154 ? -23.085 -7.976  4.250   1.00 18.21 ? 155 PRO A O   1 
ATOM   1270 C  CB  . PRO A 1 154 ? -25.587 -9.823  5.615   1.00 18.06 ? 155 PRO A CB  1 
ATOM   1271 C  CG  . PRO A 1 154 ? -25.881 -10.980 6.574   1.00 23.86 ? 155 PRO A CG  1 
ATOM   1272 C  CD  . PRO A 1 154 ? -24.755 -10.954 7.583   1.00 16.40 ? 155 PRO A CD  1 
ATOM   1273 N  N   . GLY A 1 155 ? -23.443 -7.609  6.471   1.00 15.59 ? 156 GLY A N   1 
ATOM   1274 C  CA  . GLY A 1 155 ? -22.990 -6.214  6.458   1.00 17.68 ? 156 GLY A CA  1 
ATOM   1275 C  C   . GLY A 1 155 ? -21.518 -6.055  6.151   1.00 16.21 ? 156 GLY A C   1 
ATOM   1276 O  O   . GLY A 1 155 ? -21.046 -4.951  5.945   1.00 19.90 ? 156 GLY A O   1 
ATOM   1277 N  N   . LEU A 1 156 ? -20.754 -7.126  6.207   1.00 15.47 ? 157 LEU A N   1 
ATOM   1278 C  CA  . LEU A 1 156 ? -19.341 -7.080  5.866   1.00 15.96 ? 157 LEU A CA  1 
ATOM   1279 C  C   . LEU A 1 156 ? -19.089 -7.327  4.375   1.00 14.77 ? 157 LEU A C   1 
ATOM   1280 O  O   . LEU A 1 156 ? -18.017 -7.052  3.871   1.00 14.56 ? 157 LEU A O   1 
ATOM   1281 C  CB  . LEU A 1 156 ? -18.609 -8.120  6.705   1.00 14.95 ? 157 LEU A CB  1 
ATOM   1282 C  CG  . LEU A 1 156 ? -17.089 -8.229  6.532   1.00 14.06 ? 157 LEU A CG  1 
ATOM   1283 C  CD1 . LEU A 1 156 ? -16.325 -6.935  6.859   1.00 16.01 ? 157 LEU A CD1 1 
ATOM   1284 C  CD2 . LEU A 1 156 ? -16.507 -9.366  7.354   1.00 16.68 ? 157 LEU A CD2 1 
ATOM   1285 N  N   . GLN A 1 157 ? -20.090 -7.874  3.660   1.00 15.15 ? 158 GLN A N   1 
ATOM   1286 C  CA  . GLN A 1 157 ? -19.797 -8.334  2.308   1.00 15.64 ? 158 GLN A CA  1 
ATOM   1287 C  C   . GLN A 1 157 ? -19.344 -7.215  1.362   1.00 15.13 ? 158 GLN A C   1 
ATOM   1288 O  O   . GLN A 1 157 ? -18.456 -7.430  0.532   1.00 16.44 ? 158 GLN A O   1 
ATOM   1289 C  CB  . GLN A 1 157 ? -20.976 -9.126  1.769   1.00 16.09 ? 158 GLN A CB  1 
ATOM   1290 C  CG  . GLN A 1 157 ? -20.602 -9.854  0.479   1.00 19.17 ? 158 GLN A CG  1 
ATOM   1291 C  CD  . GLN A 1 157 ? -19.536 -10.900 0.759   1.00 18.38 ? 158 GLN A CD  1 
ATOM   1292 O  OE1 . GLN A 1 157 ? -19.401 -11.476 1.872   1.00 20.43 ? 158 GLN A OE1 1 
ATOM   1293 N  NE2 . GLN A 1 157 ? -18.775 -11.207 -0.267  1.00 21.80 ? 158 GLN A NE2 1 
ATOM   1294 N  N   . LYS A 1 158 ? -19.919 -6.004  1.516   1.00 17.38 ? 159 LYS A N   1 
ATOM   1295 C  CA  . LYS A 1 158 ? -19.529 -4.905  0.656   1.00 16.14 ? 159 LYS A CA  1 
ATOM   1296 C  C   . LYS A 1 158 ? -18.036 -4.627  0.787   1.00 16.53 ? 159 LYS A C   1 
ATOM   1297 O  O   . LYS A 1 158 ? -17.393 -4.238  -0.185  1.00 17.55 ? 159 LYS A O   1 
ATOM   1298 C  CB  . LYS A 1 158 ? -20.360 -3.635  0.877   1.00 20.36 ? 159 LYS A CB  1 
ATOM   1299 C  CG  . LYS A 1 158 ? -20.024 -2.437  -0.023  1.00 26.10 ? 159 LYS A CG  1 
ATOM   1300 C  CD  . LYS A 1 158 ? -20.944 -1.204  0.284   1.00 30.25 ? 159 LYS A CD  1 
ATOM   1301 C  CE  . LYS A 1 158 ? -20.446 0.124   -0.272  1.00 30.79 ? 159 LYS A CE  1 
ATOM   1302 N  NZ  . LYS A 1 158 ? -20.865 0.290   -1.690  1.00 31.65 ? 159 LYS A NZ  1 
ATOM   1303 N  N   . VAL A 1 159 ? -17.515 -4.762  2.012   1.00 15.35 ? 160 VAL A N   1 
ATOM   1304 C  CA  . VAL A 1 159 ? -16.092 -4.547  2.252   1.00 15.08 ? 160 VAL A CA  1 
ATOM   1305 C  C   . VAL A 1 159 ? -15.319 -5.665  1.557   1.00 14.66 ? 160 VAL A C   1 
ATOM   1306 O  O   . VAL A 1 159 ? -14.357 -5.422  0.847   1.00 15.78 ? 160 VAL A O   1 
ATOM   1307 C  CB  . VAL A 1 159 ? -15.764 -4.532  3.739   1.00 15.31 ? 160 VAL A CB  1 
ATOM   1308 C  CG1 . VAL A 1 159 ? -14.237 -4.593  3.967   1.00 17.96 ? 160 VAL A CG1 1 
ATOM   1309 C  CG2 . VAL A 1 159 ? -16.357 -3.292  4.384   1.00 19.40 ? 160 VAL A CG2 1 
ATOM   1310 N  N   . VAL A 1 160 ? -15.671 -6.916  1.849   1.00 14.77 ? 161 VAL A N   1 
ATOM   1311 C  CA  . VAL A 1 160 ? -14.943 -8.069  1.312   1.00 15.97 ? 161 VAL A CA  1 
ATOM   1312 C  C   . VAL A 1 160 ? -14.862 -7.992  -0.200  1.00 16.97 ? 161 VAL A C   1 
ATOM   1313 O  O   . VAL A 1 160 ? -13.835 -8.290  -0.774  1.00 17.45 ? 161 VAL A O   1 
ATOM   1314 C  CB  . VAL A 1 160 ? -15.641 -9.409  1.774   1.00 17.88 ? 161 VAL A CB  1 
ATOM   1315 C  CG1 . VAL A 1 160 ? -15.317 -10.613 0.877   1.00 18.61 ? 161 VAL A CG1 1 
ATOM   1316 C  CG2 . VAL A 1 160 ? -15.433 -9.563  3.254   1.00 18.97 ? 161 VAL A CG2 1 
ATOM   1317 N  N   . ASP A 1 161 ? -15.937 -7.583  -0.836  1.00 16.83 ? 162 ASP A N   1 
ATOM   1318 C  CA  . ASP A 1 161 ? -15.969 -7.640  -2.287  1.00 19.23 ? 162 ASP A CA  1 
ATOM   1319 C  C   . ASP A 1 161 ? -15.094 -6.606  -3.003  1.00 19.55 ? 162 ASP A C   1 
ATOM   1320 O  O   . ASP A 1 161 ? -14.843 -6.756  -4.193  1.00 24.18 ? 162 ASP A O   1 
ATOM   1321 C  CB  . ASP A 1 161 ? -17.425 -7.510  -2.708  1.00 23.89 ? 162 ASP A CB  1 
ATOM   1322 C  CG  . ASP A 1 161 ? -18.134 -8.872  -2.674  1.00 21.44 ? 162 ASP A CG  1 
ATOM   1323 O  OD1 . ASP A 1 161 ? -17.422 -9.936  -2.793  1.00 28.27 ? 162 ASP A OD1 1 
ATOM   1324 O  OD2 . ASP A 1 161 ? -19.369 -8.873  -2.503  1.00 25.28 ? 162 ASP A OD2 1 
ATOM   1325 N  N   . VAL A 1 162 ? -14.636 -5.563  -2.318  1.00 20.44 ? 163 VAL A N   1 
ATOM   1326 C  CA  . VAL A 1 162 ? -13.821 -4.519  -2.923  1.00 21.86 ? 163 VAL A CA  1 
ATOM   1327 C  C   . VAL A 1 162 ? -12.336 -4.832  -2.643  1.00 20.23 ? 163 VAL A C   1 
ATOM   1328 O  O   . VAL A 1 162 ? -11.453 -4.158  -3.173  1.00 20.88 ? 163 VAL A O   1 
ATOM   1329 C  CB  . VAL A 1 162 ? -14.271 -3.130  -2.392  1.00 24.17 ? 163 VAL A CB  1 
ATOM   1330 C  CG1 . VAL A 1 162 ? -13.741 -2.822  -1.008  1.00 24.23 ? 163 VAL A CG1 1 
ATOM   1331 C  CG2 . VAL A 1 162 ? -13.964 -1.937  -3.254  1.00 31.47 ? 163 VAL A CG2 1 
ATOM   1332 N  N   . LEU A 1 163 ? -12.025 -5.811  -1.761  1.00 18.92 ? 164 LEU A N   1 
ATOM   1333 C  CA  . LEU A 1 163 ? -10.625 -5.989  -1.386  1.00 17.79 ? 164 LEU A CA  1 
ATOM   1334 C  C   . LEU A 1 163 ? -9.725  -6.346  -2.580  1.00 17.76 ? 164 LEU A C   1 
ATOM   1335 O  O   . LEU A 1 163 ? -8.528  -6.003  -2.571  1.00 19.69 ? 164 LEU A O   1 
ATOM   1336 C  CB  . LEU A 1 163 ? -10.516 -7.006  -0.260  1.00 15.75 ? 164 LEU A CB  1 
ATOM   1337 C  CG  . LEU A 1 163 ? -11.140 -6.622  1.086   1.00 15.48 ? 164 LEU A CG  1 
ATOM   1338 C  CD1 . LEU A 1 163 ? -10.879 -7.753  2.078   1.00 17.36 ? 164 LEU A CD1 1 
ATOM   1339 C  CD2 . LEU A 1 163 ? -10.584 -5.322  1.577   1.00 16.41 ? 164 LEU A CD2 1 
ATOM   1340 N  N   . ASP A 1 164 ? -10.262 -7.022  -3.584  1.00 21.70 ? 165 ASP A N   1 
ATOM   1341 C  CA  . ASP A 1 164 ? -9.430  -7.385  -4.744  1.00 24.75 ? 165 ASP A CA  1 
ATOM   1342 C  C   . ASP A 1 164 ? -8.921  -6.126  -5.470  1.00 25.90 ? 165 ASP A C   1 
ATOM   1343 O  O   . ASP A 1 164 ? -7.913  -6.178  -6.193  1.00 30.87 ? 165 ASP A O   1 
ATOM   1344 C  CB  . ASP A 1 164 ? -10.153 -8.325  -5.704  1.00 31.55 ? 165 ASP A CB  1 
ATOM   1345 C  CG  . ASP A 1 164 ? -11.142 -7.515  -6.523  1.00 37.00 ? 165 ASP A CG  1 
ATOM   1346 O  OD1 . ASP A 1 164 ? -12.128 -7.022  -5.892  1.00 39.97 ? 165 ASP A OD1 1 
ATOM   1347 O  OD2 . ASP A 1 164 ? -10.868 -7.298  -7.765  1.00 48.59 ? 165 ASP A OD2 1 
ATOM   1348 N  N   . SER A 1 165 ? -9.576  -4.984  -5.247  1.00 23.12 ? 166 SER A N   1 
ATOM   1349 C  CA  . SER A 1 165 ? -9.166  -3.741  -5.891  1.00 22.87 ? 166 SER A CA  1 
ATOM   1350 C  C   . SER A 1 165 ? -8.108  -2.954  -5.102  1.00 21.97 ? 166 SER A C   1 
ATOM   1351 O  O   . SER A 1 165 ? -7.535  -1.974  -5.598  1.00 24.23 ? 166 SER A O   1 
ATOM   1352 C  CB  . SER A 1 165 ? -10.385 -2.932  -6.175  1.00 30.72 ? 166 SER A CB  1 
ATOM   1353 O  OG  . SER A 1 165 ? -10.813 -2.269  -4.998  1.00 28.16 ? 166 SER A OG  1 
ATOM   1354 N  N   . ILE A 1 166 ? -7.839  -3.383  -3.873  1.00 18.84 ? 167 ILE A N   1 
ATOM   1355 C  CA  . ILE A 1 166 ? -6.839  -2.760  -3.011  1.00 19.27 ? 167 ILE A CA  1 
ATOM   1356 C  C   . ILE A 1 166 ? -5.831  -3.813  -2.538  1.00 19.07 ? 167 ILE A C   1 
ATOM   1357 O  O   . ILE A 1 166 ? -5.432  -3.849  -1.376  1.00 20.04 ? 167 ILE A O   1 
ATOM   1358 C  CB  . ILE A 1 166 ? -7.444  -1.910  -1.872  1.00 20.01 ? 167 ILE A CB  1 
ATOM   1359 C  CG1 . ILE A 1 166 ? -8.397  -2.735  -1.011  1.00 18.46 ? 167 ILE A CG1 1 
ATOM   1360 C  CG2 . ILE A 1 166 ? -8.179  -0.715  -2.480  1.00 22.22 ? 167 ILE A CG2 1 
ATOM   1361 C  CD1 . ILE A 1 166 ? -8.498  -2.153  0.382   1.00 18.36 ? 167 ILE A CD1 1 
ATOM   1362 N  N   . LYS A 1 167 ? -5.459  -4.733  -3.428  1.00 19.14 ? 168 LYS A N   1 
ATOM   1363 C  CA  . LYS A 1 167 ? -4.683  -5.894  -3.001  1.00 17.41 ? 168 LYS A CA  1 
ATOM   1364 C  C   . LYS A 1 167 ? -3.348  -5.513  -2.348  1.00 19.10 ? 168 LYS A C   1 
ATOM   1365 O  O   . LYS A 1 167 ? -2.920  -6.198  -1.410  1.00 17.63 ? 168 LYS A O   1 
ATOM   1366 C  CB  . LYS A 1 167 ? -4.435  -6.833  -4.188  1.00 22.38 ? 168 LYS A CB  1 
ATOM   1367 C  CG  . LYS A 1 167 ? -3.612  -8.075  -3.849  1.00 22.58 ? 168 LYS A CG  1 
ATOM   1368 C  CD  . LYS A 1 167 ? -3.442  -8.969  -5.067  1.00 30.09 ? 168 LYS A CD  1 
ATOM   1369 C  CE  . LYS A 1 167 ? -2.638  -10.188 -4.682  1.00 37.63 ? 168 LYS A CE  1 
ATOM   1370 N  N   . THR A 1 168 ? -2.663  -4.458  -2.851  1.00 19.67 ? 169 THR A N   1 
ATOM   1371 C  CA  . THR A 1 168 ? -1.287  -4.215  -2.431  1.00 23.03 ? 169 THR A CA  1 
ATOM   1372 C  C   . THR A 1 168 ? -1.187  -2.878  -1.694  1.00 20.46 ? 169 THR A C   1 
ATOM   1373 O  O   . THR A 1 168 ? -2.034  -2.005  -1.877  1.00 21.19 ? 169 THR A O   1 
ATOM   1374 C  CB  . THR A 1 168 ? -0.308  -4.267  -3.634  1.00 24.88 ? 169 THR A CB  1 
ATOM   1375 O  OG1 . THR A 1 168 ? -0.891  -3.541  -4.707  1.00 25.94 ? 169 THR A OG1 1 
ATOM   1376 C  CG2 . THR A 1 168 ? -0.162  -5.691  -4.141  1.00 25.14 ? 169 THR A CG2 1 
ATOM   1377 N  N   . LYS A 1 169 ? -0.095  -2.735  -0.930  1.00 20.52 ? 170 LYS A N   1 
ATOM   1378 C  CA  . LYS A 1 169 ? 0.267   -1.518  -0.232  1.00 19.57 ? 170 LYS A CA  1 
ATOM   1379 C  C   . LYS A 1 169 ? 0.157   -0.326  -1.146  1.00 22.83 ? 170 LYS A C   1 
ATOM   1380 O  O   . LYS A 1 169 ? 0.816   -0.288  -2.176  1.00 28.75 ? 170 LYS A O   1 
ATOM   1381 C  CB  . LYS A 1 169 ? 1.663   -1.602  0.401   1.00 24.26 ? 170 LYS A CB  1 
ATOM   1382 C  CG  . LYS A 1 169 ? 2.087   -0.409  1.248   1.00 21.43 ? 170 LYS A CG  1 
ATOM   1383 C  CD  . LYS A 1 169 ? 3.512   -0.535  1.691   1.00 30.29 ? 170 LYS A CD  1 
ATOM   1384 C  CE  . LYS A 1 169 ? 3.923   0.615   2.597   1.00 37.33 ? 170 LYS A CE  1 
ATOM   1385 N  NZ  . LYS A 1 169 ? 5.381   0.892   2.504   1.00 46.21 ? 170 LYS A NZ  1 
ATOM   1386 N  N   . GLY A 1 170 ? -0.561  0.687   -0.678  1.00 20.74 ? 171 GLY A N   1 
ATOM   1387 C  CA  . GLY A 1 170 ? -0.614  1.941   -1.399  1.00 25.60 ? 171 GLY A CA  1 
ATOM   1388 C  C   . GLY A 1 170 ? -1.866  2.069   -2.249  1.00 24.33 ? 171 GLY A C   1 
ATOM   1389 O  O   . GLY A 1 170 ? -2.153  3.167   -2.758  1.00 35.29 ? 171 GLY A O   1 
ATOM   1390 N  N   . LYS A 1 171 ? -2.575  0.954   -2.472  1.00 22.24 ? 172 LYS A N   1 
ATOM   1391 C  CA  . LYS A 1 171 ? -3.759  1.048   -3.298  1.00 19.92 ? 172 LYS A CA  1 
ATOM   1392 C  C   . LYS A 1 171 ? -4.944  1.571   -2.515  1.00 19.54 ? 172 LYS A C   1 
ATOM   1393 O  O   . LYS A 1 171 ? -5.240  1.229   -1.358  1.00 22.85 ? 172 LYS A O   1 
ATOM   1394 C  CB  . LYS A 1 171 ? -4.131  -0.244  -4.017  1.00 23.47 ? 172 LYS A CB  1 
ATOM   1395 C  CG  . LYS A 1 171 ? -3.078  -0.692  -5.014  1.00 27.00 ? 172 LYS A CG  1 
ATOM   1396 C  CD  . LYS A 1 171 ? -3.535  -1.751  -5.975  1.00 34.28 ? 172 LYS A CD  1 
ATOM   1397 N  N   . SER A 1 172 ? -5.734  2.367   -3.204  1.00 24.15 ? 173 SER A N   1 
ATOM   1398 C  CA  . SER A 1 172 ? -6.952  2.863   -2.574  1.00 22.16 ? 173 SER A CA  1 
ATOM   1399 C  C   . SER A 1 172 ? -8.130  2.866   -3.561  1.00 26.30 ? 173 SER A C   1 
ATOM   1400 O  O   . SER A 1 172 ? -7.951  2.854   -4.782  1.00 27.03 ? 173 SER A O   1 
ATOM   1401 C  CB  . SER A 1 172 ? -6.779  4.214   -1.898  1.00 23.83 ? 173 SER A CB  1 
ATOM   1402 O  OG  . SER A 1 172 ? -6.475  5.244   -2.812  1.00 27.88 ? 173 SER A OG  1 
ATOM   1403 N  N   . ALA A 1 173 ? -9.349  2.963   -3.030  1.00 21.07 ? 174 ALA A N   1 
ATOM   1404 C  CA  . ALA A 1 173 ? -10.524 3.082   -3.903  1.00 23.84 ? 174 ALA A CA  1 
ATOM   1405 C  C   . ALA A 1 173 ? -11.602 3.943   -3.260  1.00 23.36 ? 174 ALA A C   1 
ATOM   1406 O  O   . ALA A 1 173 ? -11.704 3.949   -2.027  1.00 24.85 ? 174 ALA A O   1 
ATOM   1407 C  CB  . ALA A 1 173 ? -11.042 1.698   -4.216  1.00 22.63 ? 174 ALA A CB  1 
ATOM   1408 N  N   A ASP A 1 174 ? -12.498 4.527   -4.089  0.50 28.18 ? 175 ASP A N   1 
ATOM   1409 N  N   B ASP A 1 174 ? -12.416 4.648   -4.044  0.50 25.97 ? 175 ASP A N   1 
ATOM   1410 C  CA  A ASP A 1 174 ? -13.712 5.150   -3.553  0.50 32.25 ? 175 ASP A CA  1 
ATOM   1411 C  CA  B ASP A 1 174 ? -13.509 5.286   -3.323  0.50 26.24 ? 175 ASP A CA  1 
ATOM   1412 C  C   A ASP A 1 174 ? -14.561 4.083   -2.826  0.50 30.81 ? 175 ASP A C   1 
ATOM   1413 C  C   B ASP A 1 174 ? -14.420 4.173   -2.766  0.50 23.78 ? 175 ASP A C   1 
ATOM   1414 O  O   A ASP A 1 174 ? -14.577 2.826   -3.150  0.50 37.41 ? 175 ASP A O   1 
ATOM   1415 O  O   B ASP A 1 174 ? -14.300 2.953   -3.128  0.50 27.31 ? 175 ASP A O   1 
ATOM   1416 C  CB  A ASP A 1 174 ? -14.450 6.095   -4.523  0.50 33.69 ? 175 ASP A CB  1 
ATOM   1417 C  CB  B ASP A 1 174 ? -14.050 6.532   -4.039  0.50 35.25 ? 175 ASP A CB  1 
ATOM   1418 C  CG  A ASP A 1 174 ? -13.550 7.120   -5.198  0.50 36.00 ? 175 ASP A CG  1 
ATOM   1419 C  CG  B ASP A 1 174 ? -14.218 6.234   -5.509  0.50 41.33 ? 175 ASP A CG  1 
ATOM   1420 O  OD1 A ASP A 1 174 ? -13.219 8.114   -4.580  0.50 35.84 ? 175 ASP A OD1 1 
ATOM   1421 O  OD1 B ASP A 1 174 ? -15.199 5.395   -5.768  0.50 38.99 ? 175 ASP A OD1 1 
ATOM   1422 O  OD2 . ASP A 1 174 ? -13.204 6.900   -6.369  1.00 39.34 ? 175 ASP A OD2 1 
ATOM   1423 N  N   . PHE A 1 175 ? -15.174 4.525   -1.706  1.00 23.74 ? 176 PHE A N   1 
ATOM   1424 C  CA  . PHE A 1 175 ? -15.930 3.532   -0.971  1.00 21.14 ? 176 PHE A CA  1 
ATOM   1425 C  C   . PHE A 1 175 ? -17.009 4.263   -0.186  1.00 20.17 ? 176 PHE A C   1 
ATOM   1426 O  O   . PHE A 1 175 ? -16.821 4.560   1.000   1.00 21.62 ? 176 PHE A O   1 
ATOM   1427 C  CB  . PHE A 1 175 ? -15.035 2.715   -0.028  1.00 21.12 ? 176 PHE A CB  1 
ATOM   1428 C  CG  . PHE A 1 175 ? -15.705 1.470   0.508   1.00 19.70 ? 176 PHE A CG  1 
ATOM   1429 C  CD1 . PHE A 1 175 ? -16.012 0.389   -0.319  1.00 20.61 ? 176 PHE A CD1 1 
ATOM   1430 C  CD2 . PHE A 1 175 ? -16.001 1.325   1.855   1.00 20.76 ? 176 PHE A CD2 1 
ATOM   1431 C  CE1 . PHE A 1 175 ? -16.597 -0.762  0.197   1.00 19.51 ? 176 PHE A CE1 1 
ATOM   1432 C  CE2 . PHE A 1 175 ? -16.573 0.164   2.366   1.00 19.48 ? 176 PHE A CE2 1 
ATOM   1433 C  CZ  . PHE A 1 175 ? -16.856 -0.884  1.538   1.00 20.27 ? 176 PHE A CZ  1 
ATOM   1434 N  N   . THR A 1 176 ? -18.077 4.642   -0.878  1.00 20.33 ? 177 THR A N   1 
ATOM   1435 C  CA  . THR A 1 176 ? -19.123 5.450   -0.299  1.00 20.58 ? 177 THR A CA  1 
ATOM   1436 C  C   . THR A 1 176 ? -20.316 4.607   0.111   1.00 20.14 ? 177 THR A C   1 
ATOM   1437 O  O   . THR A 1 176 ? -20.480 3.479   -0.332  1.00 19.94 ? 177 THR A O   1 
ATOM   1438 C  CB  . THR A 1 176 ? -19.576 6.551   -1.278  1.00 22.57 ? 177 THR A CB  1 
ATOM   1439 O  OG1 . THR A 1 176 ? -20.019 5.931   -2.483  1.00 24.88 ? 177 THR A OG1 1 
ATOM   1440 C  CG2 . THR A 1 176 ? -18.458 7.547   -1.513  1.00 29.41 ? 177 THR A CG2 1 
ATOM   1441 N  N   . ASN A 1 177 ? -21.108 5.177   0.996   1.00 20.12 ? 178 ASN A N   1 
ATOM   1442 C  CA  . ASN A 1 177 ? -22.377 4.663   1.421   1.00 18.73 ? 178 ASN A CA  1 
ATOM   1443 C  C   . ASN A 1 177 ? -22.257 3.333   2.165   1.00 20.21 ? 178 ASN A C   1 
ATOM   1444 O  O   . ASN A 1 177 ? -23.169 2.532   2.118   1.00 24.62 ? 178 ASN A O   1 
ATOM   1445 C  CB  . ASN A 1 177 ? -23.363 4.504   0.262   1.00 21.00 ? 178 ASN A CB  1 
ATOM   1446 C  CG  . ASN A 1 177 ? -23.697 5.871   -0.306  1.00 20.75 ? 178 ASN A CG  1 
ATOM   1447 O  OD1 . ASN A 1 177 ? -24.413 6.644   0.320   1.00 24.29 ? 178 ASN A OD1 1 
ATOM   1448 N  ND2 . ASN A 1 177 ? -23.145 6.177   -1.468  1.00 20.04 ? 178 ASN A ND2 1 
ATOM   1449 N  N   . PHE A 1 178 ? -21.157 3.119   2.888   1.00 19.18 ? 179 PHE A N   1 
ATOM   1450 C  CA  . PHE A 1 178 ? -21.000 1.925   3.674   1.00 15.78 ? 179 PHE A CA  1 
ATOM   1451 C  C   . PHE A 1 178 ? -21.520 2.209   5.067   1.00 16.93 ? 179 PHE A C   1 
ATOM   1452 O  O   . PHE A 1 178 ? -21.093 3.185   5.669   1.00 17.65 ? 179 PHE A O   1 
ATOM   1453 C  CB  . PHE A 1 178 ? -19.566 1.448   3.767   1.00 17.94 ? 179 PHE A CB  1 
ATOM   1454 C  CG  . PHE A 1 178 ? -19.518 0.218   4.617   1.00 18.88 ? 179 PHE A CG  1 
ATOM   1455 C  CD1 . PHE A 1 178 ? -19.873 -1.016  4.081   1.00 19.56 ? 179 PHE A CD1 1 
ATOM   1456 C  CD2 . PHE A 1 178 ? -19.120 0.296   5.963   1.00 16.80 ? 179 PHE A CD2 1 
ATOM   1457 C  CE1 . PHE A 1 178 ? -19.866 -2.162  4.871   1.00 20.97 ? 179 PHE A CE1 1 
ATOM   1458 C  CE2 . PHE A 1 178 ? -19.143 -0.861  6.734   1.00 16.56 ? 179 PHE A CE2 1 
ATOM   1459 C  CZ  . PHE A 1 178 ? -19.455 -2.075  6.180   1.00 17.37 ? 179 PHE A CZ  1 
ATOM   1460 N  N   . ASP A 1 179 ? -22.418 1.339   5.547   1.00 17.94 ? 180 ASP A N   1 
ATOM   1461 C  CA  . ASP A 1 179 ? -23.055 1.544   6.836   1.00 17.30 ? 180 ASP A CA  1 
ATOM   1462 C  C   . ASP A 1 179 ? -22.392 0.709   7.917   1.00 16.09 ? 180 ASP A C   1 
ATOM   1463 O  O   . ASP A 1 179 ? -22.559 -0.503  7.988   1.00 16.38 ? 180 ASP A O   1 
ATOM   1464 C  CB  . ASP A 1 179 ? -24.529 1.189   6.748   1.00 20.53 ? 180 ASP A CB  1 
ATOM   1465 C  CG  . ASP A 1 179 ? -25.350 1.607   7.944   1.00 23.50 ? 180 ASP A CG  1 
ATOM   1466 O  OD1 . ASP A 1 179 ? -24.772 1.860   9.012   1.00 19.90 ? 180 ASP A OD1 1 
ATOM   1467 O  OD2 . ASP A 1 179 ? -26.539 1.711   7.780   1.00 31.71 ? 180 ASP A OD2 1 
ATOM   1468 N  N   . PRO A 1 180 ? -21.616 1.322   8.830   1.00 14.57 ? 181 PRO A N   1 
ATOM   1469 C  CA  . PRO A 1 180 ? -20.918 0.493   9.830   1.00 14.25 ? 181 PRO A CA  1 
ATOM   1470 C  C   . PRO A 1 180 ? -21.834 -0.117  10.872  1.00 13.19 ? 181 PRO A C   1 
ATOM   1471 O  O   . PRO A 1 180 ? -21.399 -1.021  11.613  1.00 14.69 ? 181 PRO A O   1 
ATOM   1472 C  CB  . PRO A 1 180 ? -19.908 1.502   10.428  1.00 15.58 ? 181 PRO A CB  1 
ATOM   1473 C  CG  . PRO A 1 180 ? -20.608 2.862   10.250  1.00 17.22 ? 181 PRO A CG  1 
ATOM   1474 C  CD  . PRO A 1 180 ? -21.234 2.745   8.847   1.00 15.84 ? 181 PRO A CD  1 
ATOM   1475 N  N   . ARG A 1 181 ? -23.105 0.304   10.912  1.00 14.71 ? 182 ARG A N   1 
ATOM   1476 C  CA  . ARG A 1 181 ? -24.012 -0.407  11.821  1.00 14.23 ? 182 ARG A CA  1 
ATOM   1477 C  C   . ARG A 1 181 ? -24.093 -1.895  11.462  1.00 15.22 ? 182 ARG A C   1 
ATOM   1478 O  O   . ARG A 1 181 ? -24.453 -2.695  12.333  1.00 17.48 ? 182 ARG A O   1 
ATOM   1479 C  CB  . ARG A 1 181 ? -25.396 0.259   11.770  1.00 17.39 ? 182 ARG A CB  1 
ATOM   1480 C  CG  . ARG A 1 181 ? -25.382 1.676   12.351  1.00 19.48 ? 182 ARG A CG  1 
ATOM   1481 C  CD  . ARG A 1 181 ? -26.742 2.298   12.261  1.00 21.64 ? 182 ARG A CD  1 
ATOM   1482 N  NE  . ARG A 1 181 ? -27.054 2.589   10.867  1.00 21.38 ? 182 ARG A NE  1 
ATOM   1483 C  CZ  . ARG A 1 181 ? -28.084 3.352   10.530  1.00 23.08 ? 182 ARG A CZ  1 
ATOM   1484 N  NH1 . ARG A 1 181 ? -28.891 3.835   11.466  1.00 31.75 ? 182 ARG A NH1 1 
ATOM   1485 N  NH2 . ARG A 1 181 ? -28.297 3.666   9.273   1.00 27.88 ? 182 ARG A NH2 1 
ATOM   1486 N  N   . GLY A 1 182 ? -23.832 -2.251  10.194  1.00 16.73 ? 183 GLY A N   1 
ATOM   1487 C  CA  . GLY A 1 182 ? -23.939 -3.661  9.801   1.00 18.16 ? 183 GLY A CA  1 
ATOM   1488 C  C   . GLY A 1 182 ? -22.760 -4.498  10.300  1.00 17.53 ? 183 GLY A C   1 
ATOM   1489 O  O   . GLY A 1 182 ? -22.754 -5.695  10.017  1.00 19.24 ? 183 GLY A O   1 
ATOM   1490 N  N   . LEU A 1 183 ? -21.840 -3.921  11.102  1.00 16.22 ? 184 LEU A N   1 
ATOM   1491 C  CA  . LEU A 1 183 ? -20.713 -4.677  11.644  1.00 13.90 ? 184 LEU A CA  1 
ATOM   1492 C  C   . LEU A 1 183 ? -20.882 -4.885  13.150  1.00 13.02 ? 184 LEU A C   1 
ATOM   1493 O  O   . LEU A 1 183 ? -20.017 -5.480  13.770  1.00 15.82 ? 184 LEU A O   1 
ATOM   1494 C  CB  . LEU A 1 183 ? -19.428 -3.892  11.380  1.00 15.73 ? 184 LEU A CB  1 
ATOM   1495 C  CG  . LEU A 1 183 ? -19.072 -3.740  9.894   1.00 16.19 ? 184 LEU A CG  1 
ATOM   1496 C  CD1 . LEU A 1 183 ? -17.830 -2.920  9.751   1.00 19.13 ? 184 LEU A CD1 1 
ATOM   1497 C  CD2 . LEU A 1 183 ? -18.946 -5.062  9.162   1.00 17.54 ? 184 LEU A CD2 1 
ATOM   1498 N  N   . LEU A 1 184 ? -21.977 -4.404  13.752  1.00 14.60 ? 185 LEU A N   1 
ATOM   1499 C  CA  . LEU A 1 184 ? -22.114 -4.479  15.196  1.00 12.94 ? 185 LEU A CA  1 
ATOM   1500 C  C   . LEU A 1 184 ? -22.880 -5.724  15.625  1.00 16.82 ? 185 LEU A C   1 
ATOM   1501 O  O   . LEU A 1 184 ? -23.812 -6.156  14.959  1.00 24.48 ? 185 LEU A O   1 
ATOM   1502 C  CB  . LEU A 1 184 ? -22.900 -3.252  15.700  1.00 14.08 ? 185 LEU A CB  1 
ATOM   1503 C  CG  . LEU A 1 184 ? -22.313 -1.911  15.267  1.00 13.03 ? 185 LEU A CG  1 
ATOM   1504 C  CD1 . LEU A 1 184 ? -23.129 -0.765  15.785  1.00 15.14 ? 185 LEU A CD1 1 
ATOM   1505 C  CD2 . LEU A 1 184 ? -20.929 -1.803  15.837  1.00 15.73 ? 185 LEU A CD2 1 
ATOM   1506 N  N   . PRO A 1 185 ? -22.520 -6.302  16.794  1.00 14.06 ? 186 PRO A N   1 
ATOM   1507 C  CA  . PRO A 1 185 ? -23.307 -7.410  17.350  1.00 15.10 ? 186 PRO A CA  1 
ATOM   1508 C  C   . PRO A 1 185 ? -24.576 -6.884  18.003  1.00 14.92 ? 186 PRO A C   1 
ATOM   1509 O  O   . PRO A 1 185 ? -24.766 -5.675  18.049  1.00 17.82 ? 186 PRO A O   1 
ATOM   1510 C  CB  . PRO A 1 185 ? -22.339 -8.012  18.355  1.00 13.96 ? 186 PRO A CB  1 
ATOM   1511 C  CG  . PRO A 1 185 ? -21.567 -6.787  18.845  1.00 12.41 ? 186 PRO A CG  1 
ATOM   1512 C  CD  . PRO A 1 185 ? -21.380 -5.898  17.615  1.00 11.87 ? 186 PRO A CD  1 
ATOM   1513 N  N   . GLU A 1 186 ? -25.408 -7.794  18.533  1.00 16.46 ? 187 GLU A N   1 
ATOM   1514 C  CA  . GLU A 1 186 ? -26.660 -7.378  19.135  1.00 18.56 ? 187 GLU A CA  1 
ATOM   1515 C  C   . GLU A 1 186 ? -26.396 -6.575  20.383  1.00 16.58 ? 187 GLU A C   1 
ATOM   1516 O  O   . GLU A 1 186 ? -27.011 -5.511  20.584  1.00 21.06 ? 187 GLU A O   1 
ATOM   1517 C  CB  . GLU A 1 186 ? -27.461 -8.582  19.640  1.00 24.58 ? 187 GLU A CB  1 
ATOM   1518 C  CG  . GLU A 1 186 ? -28.267 -9.246  18.573  1.00 25.68 ? 187 GLU A CG  1 
ATOM   1519 C  CD  . GLU A 1 186 ? -28.963 -10.538 19.017  1.00 24.59 ? 187 GLU A CD  1 
ATOM   1520 O  OE1 . GLU A 1 186 ? -28.989 -10.803 20.217  1.00 28.47 ? 187 GLU A OE1 1 
ATOM   1521 O  OE2 . GLU A 1 186 ? -29.502 -11.232 18.156  1.00 35.76 ? 187 GLU A OE2 1 
ATOM   1522 N  N   . SER A 1 187 ? -25.520 -7.123  21.248  1.00 17.46 ? 188 SER A N   1 
ATOM   1523 C  CA  . SER A 1 187 ? -25.326 -6.516  22.550  1.00 17.69 ? 188 SER A CA  1 
ATOM   1524 C  C   . SER A 1 187 ? -24.204 -5.475  22.506  1.00 15.08 ? 188 SER A C   1 
ATOM   1525 O  O   . SER A 1 187 ? -23.175 -5.656  21.853  1.00 17.24 ? 188 SER A O   1 
ATOM   1526 C  CB  . SER A 1 187 ? -24.916 -7.565  23.549  1.00 17.49 ? 188 SER A CB  1 
ATOM   1527 O  OG  . SER A 1 187 ? -24.681 -7.036  24.852  1.00 19.12 ? 188 SER A OG  1 
ATOM   1528 N  N   . LEU A 1 188 ? -24.372 -4.385  23.259  1.00 15.83 ? 189 LEU A N   1 
ATOM   1529 C  CA  . LEU A 1 188 ? -23.312 -3.418  23.470  1.00 15.72 ? 189 LEU A CA  1 
ATOM   1530 C  C   . LEU A 1 188 ? -22.689 -3.565  24.862  1.00 14.49 ? 189 LEU A C   1 
ATOM   1531 O  O   . LEU A 1 188 ? -21.995 -2.673  25.321  1.00 17.86 ? 189 LEU A O   1 
ATOM   1532 C  CB  . LEU A 1 188 ? -23.815 -1.981  23.235  1.00 18.63 ? 189 LEU A CB  1 
ATOM   1533 C  CG  . LEU A 1 188 ? -24.202 -1.635  21.802  1.00 20.22 ? 189 LEU A CG  1 
ATOM   1534 C  CD1 . LEU A 1 188 ? -24.708 -0.190  21.736  1.00 23.61 ? 189 LEU A CD1 1 
ATOM   1535 C  CD2 . LEU A 1 188 ? -23.018 -1.823  20.856  1.00 23.21 ? 189 LEU A CD2 1 
ATOM   1536 N  N   . ASP A 1 189 ? -22.819 -4.730  25.500  1.00 15.99 ? 190 ASP A N   1 
ATOM   1537 C  CA  . ASP A 1 189 ? -22.062 -4.985  26.726  1.00 14.50 ? 190 ASP A CA  1 
ATOM   1538 C  C   . ASP A 1 189 ? -20.551 -4.988  26.445  1.00 11.90 ? 190 ASP A C   1 
ATOM   1539 O  O   . ASP A 1 189 ? -20.107 -5.431  25.366  1.00 13.02 ? 190 ASP A O   1 
ATOM   1540 C  CB  . ASP A 1 189 ? -22.328 -6.379  27.265  1.00 18.55 ? 190 ASP A CB  1 
ATOM   1541 C  CG  . ASP A 1 189 ? -23.681 -6.461  27.940  1.00 26.72 ? 190 ASP A CG  1 
ATOM   1542 O  OD1 . ASP A 1 189 ? -24.250 -5.408  28.116  1.00 35.60 ? 190 ASP A OD1 1 
ATOM   1543 O  OD2 . ASP A 1 189 ? -24.122 -7.574  28.254  1.00 32.91 ? 190 ASP A OD2 1 
ATOM   1544 N  N   . TYR A 1 190 ? -19.764 -4.375  27.356  1.00 12.73 ? 191 TYR A N   1 
ATOM   1545 C  CA  . TYR A 1 190 ? -18.369 -4.126  27.011  1.00 11.40 ? 191 TYR A CA  1 
ATOM   1546 C  C   . TYR A 1 190 ? -17.472 -4.209  28.217  1.00 11.28 ? 191 TYR A C   1 
ATOM   1547 O  O   . TYR A 1 190 ? -17.889 -4.055  29.364  1.00 12.31 ? 191 TYR A O   1 
ATOM   1548 C  CB  . TYR A 1 190 ? -18.247 -2.744  26.343  1.00 11.93 ? 191 TYR A CB  1 
ATOM   1549 C  CG  . TYR A 1 190 ? -18.599 -1.552  27.205  1.00 11.49 ? 191 TYR A CG  1 
ATOM   1550 C  CD1 . TYR A 1 190 ? -17.663 -0.906  28.022  1.00 12.55 ? 191 TYR A CD1 1 
ATOM   1551 C  CD2 . TYR A 1 190 ? -19.896 -1.053  27.193  1.00 13.36 ? 191 TYR A CD2 1 
ATOM   1552 C  CE1 . TYR A 1 190 ? -18.039 0.156   28.871  1.00 12.72 ? 191 TYR A CE1 1 
ATOM   1553 C  CE2 . TYR A 1 190 ? -20.235 0.048   27.936  1.00 14.41 ? 191 TYR A CE2 1 
ATOM   1554 C  CZ  . TYR A 1 190 ? -19.354 0.601   28.839  1.00 13.86 ? 191 TYR A CZ  1 
ATOM   1555 O  OH  . TYR A 1 190 ? -19.714 1.619   29.668  1.00 16.41 ? 191 TYR A OH  1 
ATOM   1556 N  N   . TRP A 1 191 ? -16.172 -4.329  27.933  1.00 10.76 ? 192 TRP A N   1 
ATOM   1557 C  CA  . TRP A 1 191 ? -15.109 -4.048  28.882  1.00 10.39 ? 192 TRP A CA  1 
ATOM   1558 C  C   . TRP A 1 191 ? -14.411 -2.764  28.447  1.00 9.95  ? 192 TRP A C   1 
ATOM   1559 O  O   . TRP A 1 191 ? -14.389 -2.425  27.257  1.00 11.77 ? 192 TRP A O   1 
ATOM   1560 C  CB  . TRP A 1 191 ? -14.094 -5.177  28.867  1.00 12.12 ? 192 TRP A CB  1 
ATOM   1561 C  CG  . TRP A 1 191 ? -14.634 -6.518  29.234  1.00 11.19 ? 192 TRP A CG  1 
ATOM   1562 C  CD1 . TRP A 1 191 ? -14.900 -6.926  30.517  1.00 13.11 ? 192 TRP A CD1 1 
ATOM   1563 C  CD2 . TRP A 1 191 ? -14.906 -7.636  28.391  1.00 11.23 ? 192 TRP A CD2 1 
ATOM   1564 N  NE1 . TRP A 1 191 ? -15.327 -8.229  30.512  1.00 13.62 ? 192 TRP A NE1 1 
ATOM   1565 C  CE2 . TRP A 1 191 ? -15.319 -8.692  29.219  1.00 12.10 ? 192 TRP A CE2 1 
ATOM   1566 C  CE3 . TRP A 1 191 ? -14.822 -7.833  27.003  1.00 12.23 ? 192 TRP A CE3 1 
ATOM   1567 C  CZ2 . TRP A 1 191 ? -15.660 -9.940  28.701  1.00 14.29 ? 192 TRP A CZ2 1 
ATOM   1568 C  CZ3 . TRP A 1 191 ? -15.097 -9.089  26.500  1.00 12.56 ? 192 TRP A CZ3 1 
ATOM   1569 C  CH2 . TRP A 1 191 ? -15.511 -10.121 27.347  1.00 13.10 ? 192 TRP A CH2 1 
ATOM   1570 N  N   . THR A 1 192 ? -13.835 -2.053  29.418  1.00 10.29 ? 193 THR A N   1 
ATOM   1571 C  CA  . THR A 1 192 ? -13.118 -0.824  29.061  1.00 10.49 ? 193 THR A CA  1 
ATOM   1572 C  C   . THR A 1 192 ? -11.858 -0.675  29.936  1.00 10.39 ? 193 THR A C   1 
ATOM   1573 O  O   . THR A 1 192 ? -11.859 -1.075  31.096  1.00 11.16 ? 193 THR A O   1 
ATOM   1574 C  CB  . THR A 1 192 ? -14.025 0.392   29.167  1.00 10.89 ? 193 THR A CB  1 
ATOM   1575 O  OG1 . THR A 1 192 ? -13.344 1.572   28.734  1.00 10.94 ? 193 THR A OG1 1 
ATOM   1576 C  CG2 . THR A 1 192 ? -14.582 0.622   30.562  1.00 12.49 ? 193 THR A CG2 1 
ATOM   1577 N  N   . TYR A 1 193 ? -10.820 -0.094  29.335  1.00 9.65  ? 194 TYR A N   1 
ATOM   1578 C  CA  . TYR A 1 193 ? -9.599  0.172   30.088  1.00 10.52 ? 194 TYR A CA  1 
ATOM   1579 C  C   . TYR A 1 193 ? -8.831  1.230   29.329  1.00 9.55  ? 194 TYR A C   1 
ATOM   1580 O  O   . TYR A 1 193 ? -9.030  1.406   28.128  1.00 10.11 ? 194 TYR A O   1 
ATOM   1581 C  CB  . TYR A 1 193 ? -8.776  -1.124  30.303  1.00 11.09 ? 194 TYR A CB  1 
ATOM   1582 C  CG  . TYR A 1 193 ? -8.097  -1.589  29.054  1.00 9.09  ? 194 TYR A CG  1 
ATOM   1583 C  CD1 . TYR A 1 193 ? -8.757  -2.337  28.074  1.00 9.31  ? 194 TYR A CD1 1 
ATOM   1584 C  CD2 . TYR A 1 193 ? -6.771  -1.261  28.820  1.00 9.71  ? 194 TYR A CD2 1 
ATOM   1585 C  CE1 . TYR A 1 193 ? -8.139  -2.666  26.873  1.00 8.89  ? 194 TYR A CE1 1 
ATOM   1586 C  CE2 . TYR A 1 193 ? -6.119  -1.603  27.629  1.00 10.31 ? 194 TYR A CE2 1 
ATOM   1587 C  CZ  . TYR A 1 193 ? -6.810  -2.293  26.665  1.00 8.25  ? 194 TYR A CZ  1 
ATOM   1588 O  OH  . TYR A 1 193 ? -6.162  -2.598  25.504  1.00 8.83  ? 194 TYR A OH  1 
ATOM   1589 N  N   . PRO A 1 194 ? -7.892  1.926   29.991  1.00 10.04 ? 195 PRO A N   1 
ATOM   1590 C  CA  . PRO A 1 194 ? -7.031  2.925   29.333  1.00 10.63 ? 195 PRO A CA  1 
ATOM   1591 C  C   . PRO A 1 194 ? -5.846  2.256   28.672  1.00 9.03  ? 195 PRO A C   1 
ATOM   1592 O  O   . PRO A 1 194 ? -5.117  1.470   29.316  1.00 11.32 ? 195 PRO A O   1 
ATOM   1593 C  CB  . PRO A 1 194 ? -6.580  3.828   30.488  1.00 13.02 ? 195 PRO A CB  1 
ATOM   1594 C  CG  . PRO A 1 194 ? -6.580  2.911   31.665  1.00 13.97 ? 195 PRO A CG  1 
ATOM   1595 C  CD  . PRO A 1 194 ? -7.722  1.931   31.471  1.00 13.34 ? 195 PRO A CD  1 
ATOM   1596 N  N   . GLY A 1 195 ? -5.619  2.567   27.399  1.00 9.02  ? 196 GLY A N   1 
ATOM   1597 C  CA  . GLY A 1 195 ? -4.497  1.936   26.700  1.00 9.62  ? 196 GLY A CA  1 
ATOM   1598 C  C   . GLY A 1 195 ? -3.941  2.804   25.586  1.00 9.27  ? 196 GLY A C   1 
ATOM   1599 O  O   . GLY A 1 195 ? -3.821  4.040   25.705  1.00 9.87  ? 196 GLY A O   1 
ATOM   1600 N  N   . SER A 1 196 ? -3.530  2.114   24.513  1.00 8.82  ? 197 SER A N   1 
ATOM   1601 C  CA  . SER A 1 196 ? -2.680  2.745   23.527  1.00 9.19  ? 197 SER A CA  1 
ATOM   1602 C  C   . SER A 1 196 ? -3.154  2.371   22.129  1.00 9.04  ? 197 SER A C   1 
ATOM   1603 O  O   . SER A 1 196 ? -3.904  1.409   21.942  1.00 8.68  ? 197 SER A O   1 
ATOM   1604 C  CB  . SER A 1 196 ? -1.221  2.362   23.619  1.00 11.02 ? 197 SER A CB  1 
ATOM   1605 O  OG  . SER A 1 196 ? -0.993  1.004   23.231  1.00 9.37  ? 197 SER A OG  1 
ATOM   1606 N  N   . LEU A 1 197 ? -2.580  3.034   21.128  1.00 8.53  ? 198 LEU A N   1 
ATOM   1607 C  CA  . LEU A 1 197 ? -2.585  2.486   19.778  1.00 9.15  ? 198 LEU A CA  1 
ATOM   1608 C  C   . LEU A 1 197 ? -1.899  1.146   19.812  1.00 9.04  ? 198 LEU A C   1 
ATOM   1609 O  O   . LEU A 1 197 ? -0.882  0.992   20.501  1.00 9.73  ? 198 LEU A O   1 
ATOM   1610 C  CB  . LEU A 1 197 ? -1.820  3.437   18.854  1.00 11.04 ? 198 LEU A CB  1 
ATOM   1611 C  CG  . LEU A 1 197 ? -2.342  4.877   18.828  1.00 11.98 ? 198 LEU A CG  1 
ATOM   1612 C  CD1 . LEU A 1 197 ? -1.424  5.658   17.894  1.00 15.42 ? 198 LEU A CD1 1 
ATOM   1613 C  CD2 . LEU A 1 197 ? -3.773  4.938   18.356  1.00 14.07 ? 198 LEU A CD2 1 
ATOM   1614 N  N   . THR A 1 198 ? -2.341  0.192   18.974  1.00 9.27  ? 199 THR A N   1 
ATOM   1615 C  CA  . THR A 1 198 ? -1.700  -1.121  18.950  1.00 9.18  ? 199 THR A CA  1 
ATOM   1616 C  C   . THR A 1 198 ? -0.647  -1.231  17.836  1.00 9.86  ? 199 THR A C   1 
ATOM   1617 O  O   . THR A 1 198 ? -0.057  -2.299  17.672  1.00 10.68 ? 199 THR A O   1 
ATOM   1618 C  CB  . THR A 1 198 ? -2.701  -2.240  18.810  1.00 8.54  ? 199 THR A CB  1 
ATOM   1619 O  OG1 . THR A 1 198 ? -3.271  -2.146  17.499  1.00 9.06  ? 199 THR A OG1 1 
ATOM   1620 C  CG2 . THR A 1 198 ? -3.758  -2.264  19.898  1.00 9.80  ? 199 THR A CG2 1 
ATOM   1621 N  N   . THR A 1 199 ? -0.471  -0.183  17.048  1.00 11.85 ? 200 THR A N   1 
ATOM   1622 C  CA  . THR A 1 199 ? 0.619   -0.136  16.088  1.00 11.57 ? 200 THR A CA  1 
ATOM   1623 C  C   . THR A 1 199 ? 1.426   1.108   16.380  1.00 12.31 ? 200 THR A C   1 
ATOM   1624 O  O   . THR A 1 199 ? 0.930   2.044   16.987  1.00 12.84 ? 200 THR A O   1 
ATOM   1625 C  CB  . THR A 1 199 ? 0.151   -0.033  14.634  1.00 14.18 ? 200 THR A CB  1 
ATOM   1626 O  OG1 . THR A 1 199 ? -0.393  1.239   14.347  1.00 21.29 ? 200 THR A OG1 1 
ATOM   1627 C  CG2 . THR A 1 199 ? -0.889  -1.053  14.265  1.00 14.01 ? 200 THR A CG2 1 
ATOM   1628 N  N   . PRO A 1 200 ? 2.694   1.166   15.899  1.00 12.61 ? 201 PRO A N   1 
ATOM   1629 C  CA  . PRO A 1 200 ? 3.465   2.402   15.959  1.00 14.21 ? 201 PRO A CA  1 
ATOM   1630 C  C   . PRO A 1 200 ? 2.583   3.540   15.430  1.00 13.85 ? 201 PRO A C   1 
ATOM   1631 O  O   . PRO A 1 200 ? 1.851   3.368   14.431  1.00 14.86 ? 201 PRO A O   1 
ATOM   1632 C  CB  . PRO A 1 200 ? 4.634   2.092   14.990  1.00 14.99 ? 201 PRO A CB  1 
ATOM   1633 C  CG  . PRO A 1 200 ? 4.883   0.586   15.248  1.00 15.03 ? 201 PRO A CG  1 
ATOM   1634 C  CD  . PRO A 1 200 ? 3.437   0.054   15.262  1.00 14.80 ? 201 PRO A CD  1 
ATOM   1635 N  N   . PRO A 1 201 ? 2.577   4.729   16.059  1.00 12.73 ? 202 PRO A N   1 
ATOM   1636 C  CA  . PRO A 1 201 ? 3.577   5.111   17.075  1.00 13.66 ? 202 PRO A CA  1 
ATOM   1637 C  C   . PRO A 1 201 ? 3.241   4.720   18.512  1.00 12.59 ? 202 PRO A C   1 
ATOM   1638 O  O   . PRO A 1 201 ? 3.948   5.107   19.450  1.00 14.50 ? 202 PRO A O   1 
ATOM   1639 C  CB  . PRO A 1 201 ? 3.586   6.629   16.923  1.00 14.10 ? 202 PRO A CB  1 
ATOM   1640 C  CG  . PRO A 1 201 ? 2.134   6.970   16.504  1.00 17.27 ? 202 PRO A CG  1 
ATOM   1641 C  CD  . PRO A 1 201 ? 1.760   5.860   15.526  1.00 15.77 ? 202 PRO A CD  1 
ATOM   1642 N  N   . LEU A 1 202 ? 2.177   3.926   18.721  1.00 11.82 ? 203 LEU A N   1 
ATOM   1643 C  CA  . LEU A 1 202 ? 1.894   3.299   20.018  1.00 11.21 ? 203 LEU A CA  1 
ATOM   1644 C  C   . LEU A 1 202 ? 1.504   4.317   21.082  1.00 11.35 ? 203 LEU A C   1 
ATOM   1645 O  O   . LEU A 1 202 ? 1.551   4.012   22.295  1.00 11.45 ? 203 LEU A O   1 
ATOM   1646 C  CB  . LEU A 1 202 ? 3.027   2.401   20.525  1.00 11.87 ? 203 LEU A CB  1 
ATOM   1647 C  CG  . LEU A 1 202 ? 3.395   1.247   19.584  1.00 12.08 ? 203 LEU A CG  1 
ATOM   1648 C  CD1 . LEU A 1 202 ? 4.698   0.612   20.023  1.00 13.84 ? 203 LEU A CD1 1 
ATOM   1649 C  CD2 . LEU A 1 202 ? 2.318   0.188   19.536  1.00 11.88 ? 203 LEU A CD2 1 
ATOM   1650 N  N   . ASN A 1 203 ? 1.036   5.489   20.632  1.00 12.13 ? 204 ASN A N   1 
ATOM   1651 C  CA  . ASN A 1 203 ? 0.655   6.539   21.566  1.00 11.83 ? 204 ASN A CA  1 
ATOM   1652 C  C   . ASN A 1 203 ? -0.321  6.046   22.629  1.00 10.67 ? 204 ASN A C   1 
ATOM   1653 O  O   . ASN A 1 203 ? -1.275  5.341   22.303  1.00 10.80 ? 204 ASN A O   1 
ATOM   1654 C  CB  . ASN A 1 203 ? -0.027  7.725   20.851  1.00 14.64 ? 204 ASN A CB  1 
ATOM   1655 C  CG  . ASN A 1 203 ? 0.863   8.423   19.866  1.00 15.88 ? 204 ASN A CG  1 
ATOM   1656 O  OD1 . ASN A 1 203 ? 1.975   7.963   19.581  1.00 21.29 ? 204 ASN A OD1 1 
ATOM   1657 N  ND2 . ASN A 1 203 ? 0.404   9.549   19.347  1.00 19.83 ? 204 ASN A ND2 1 
ATOM   1658 N  N   . GLU A 1 204 ? -0.148  6.487   23.882  1.00 12.58 ? 205 GLU A N   1 
ATOM   1659 C  CA  . GLU A 1 204 ? -1.018  6.124   24.984  1.00 11.69 ? 205 GLU A CA  1 
ATOM   1660 C  C   . GLU A 1 204 ? -2.189  7.096   25.043  1.00 12.30 ? 205 GLU A C   1 
ATOM   1661 O  O   . GLU A 1 204 ? -2.333  7.854   25.986  1.00 14.89 ? 205 GLU A O   1 
ATOM   1662 C  CB  . GLU A 1 204 ? -0.187  6.023   26.245  1.00 14.52 ? 205 GLU A CB  1 
ATOM   1663 C  CG  . GLU A 1 204 ? 0.692   4.786   26.165  1.00 14.58 ? 205 GLU A CG  1 
ATOM   1664 C  CD  . GLU A 1 204 ? 1.583   4.511   27.365  1.00 14.11 ? 205 GLU A CD  1 
ATOM   1665 O  OE1 . GLU A 1 204 ? 1.881   5.449   28.145  1.00 18.82 ? 205 GLU A OE1 1 
ATOM   1666 O  OE2 . GLU A 1 204 ? 1.983   3.332   27.517  1.00 15.31 ? 205 GLU A OE2 1 
ATOM   1667 N  N   . CYS A 1 205 ? -3.064  7.023   24.056  1.00 10.27 ? 206 CYS A N   1 
ATOM   1668 C  CA  . CYS A 1 205 ? -4.093  8.031   23.861  1.00 9.88  ? 206 CYS A CA  1 
ATOM   1669 C  C   . CYS A 1 205 ? -5.484  7.424   23.760  1.00 9.81  ? 206 CYS A C   1 
ATOM   1670 O  O   . CYS A 1 205 ? -6.437  8.129   23.364  1.00 11.67 ? 206 CYS A O   1 
ATOM   1671 C  CB  . CYS A 1 205 ? -3.755  8.844   22.617  1.00 12.05 ? 206 CYS A CB  1 
ATOM   1672 S  SG  . CYS A 1 205 ? -3.750  7.868   21.093  1.00 12.36 ? 206 CYS A SG  1 
ATOM   1673 N  N   . VAL A 1 206 ? -5.642  6.124   24.055  1.00 9.61  ? 207 VAL A N   1 
ATOM   1674 C  CA  . VAL A 1 206 ? -6.886  5.413   23.709  1.00 8.42  ? 207 VAL A CA  1 
ATOM   1675 C  C   . VAL A 1 206 ? -7.637  4.999   24.978  1.00 8.50  ? 207 VAL A C   1 
ATOM   1676 O  O   . VAL A 1 206 ? -7.111  4.302   25.831  1.00 10.23 ? 207 VAL A O   1 
ATOM   1677 C  CB  . VAL A 1 206 ? -6.589  4.150   22.866  1.00 8.93  ? 207 VAL A CB  1 
ATOM   1678 C  CG1 . VAL A 1 206 ? -7.950  3.488   22.519  1.00 9.86  ? 207 VAL A CG1 1 
ATOM   1679 C  CG2 . VAL A 1 206 ? -5.864  4.528   21.556  1.00 10.38 ? 207 VAL A CG2 1 
ATOM   1680 N  N   . THR A 1 207 ? -8.941  5.301   25.014  1.00 8.94  ? 208 THR A N   1 
ATOM   1681 C  CA  . THR A 1 207 ? -9.878  4.575   25.857  1.00 9.60  ? 208 THR A CA  1 
ATOM   1682 C  C   . THR A 1 207 ? -10.429 3.400   25.051  1.00 8.04  ? 208 THR A C   1 
ATOM   1683 O  O   . THR A 1 207 ? -11.066 3.611   24.024  1.00 9.39  ? 208 THR A O   1 
ATOM   1684 C  CB  . THR A 1 207 ? -11.041 5.461   26.320  1.00 10.28 ? 208 THR A CB  1 
ATOM   1685 O  OG1 . THR A 1 207 ? -10.536 6.586   27.047  1.00 12.15 ? 208 THR A OG1 1 
ATOM   1686 C  CG2 . THR A 1 207 ? -12.003 4.685   27.209  1.00 11.64 ? 208 THR A CG2 1 
ATOM   1687 N  N   . TRP A 1 208 ? -10.067 2.208   25.487  1.00 8.34  ? 209 TRP A N   1 
ATOM   1688 C  CA  . TRP A 1 208 ? -10.527 1.016   24.773  1.00 8.09  ? 209 TRP A CA  1 
ATOM   1689 C  C   . TRP A 1 208 ? -11.923 0.596   25.269  1.00 8.36  ? 209 TRP A C   1 
ATOM   1690 O  O   . TRP A 1 208 ? -12.140 0.548   26.491  1.00 9.50  ? 209 TRP A O   1 
ATOM   1691 C  CB  . TRP A 1 208 ? -9.555  -0.154  24.945  1.00 7.94  ? 209 TRP A CB  1 
ATOM   1692 C  CG  . TRP A 1 208 ? -8.414  -0.041  24.013  1.00 7.91  ? 209 TRP A CG  1 
ATOM   1693 C  CD1 . TRP A 1 208 ? -7.178  0.551   24.212  1.00 8.50  ? 209 TRP A CD1 1 
ATOM   1694 C  CD2 . TRP A 1 208 ? -8.465  -0.431  22.644  1.00 7.47  ? 209 TRP A CD2 1 
ATOM   1695 N  NE1 . TRP A 1 208 ? -6.476  0.534   23.051  1.00 9.43  ? 209 TRP A NE1 1 
ATOM   1696 C  CE2 . TRP A 1 208 ? -7.222  -0.069  22.067  1.00 8.29  ? 209 TRP A CE2 1 
ATOM   1697 C  CE3 . TRP A 1 208 ? -9.418  -1.063  21.867  1.00 7.89  ? 209 TRP A CE3 1 
ATOM   1698 C  CZ2 . TRP A 1 208 ? -6.969  -0.301  20.727  1.00 9.20  ? 209 TRP A CZ2 1 
ATOM   1699 C  CZ3 . TRP A 1 208 ? -9.143  -1.317  20.556  1.00 9.53  ? 209 TRP A CZ3 1 
ATOM   1700 C  CH2 . TRP A 1 208 ? -7.927  -0.951  19.976  1.00 8.75  ? 209 TRP A CH2 1 
ATOM   1701 N  N   . ILE A 1 209 ? -12.795 0.267   24.332  1.00 8.20  ? 210 ILE A N   1 
ATOM   1702 C  CA  . ILE A 1 209 ? -14.135 -0.234  24.668  1.00 8.98  ? 210 ILE A CA  1 
ATOM   1703 C  C   . ILE A 1 209 ? -14.239 -1.510  23.823  1.00 8.44  ? 210 ILE A C   1 
ATOM   1704 O  O   . ILE A 1 209 ? -14.322 -1.427  22.598  1.00 9.38  ? 210 ILE A O   1 
ATOM   1705 C  CB  . ILE A 1 209 ? -15.204 0.790   24.295  1.00 9.77  ? 210 ILE A CB  1 
ATOM   1706 C  CG1 . ILE A 1 209 ? -14.970 2.070   25.112  1.00 11.87 ? 210 ILE A CG1 1 
ATOM   1707 C  CG2 . ILE A 1 209 ? -16.587 0.200   24.594  1.00 10.96 ? 210 ILE A CG2 1 
ATOM   1708 C  CD1 . ILE A 1 209 ? -15.796 3.228   24.671  1.00 15.87 ? 210 ILE A CD1 1 
ATOM   1709 N  N   . VAL A 1 210 ? -14.199 -2.682  24.475  1.00 8.74  ? 211 VAL A N   1 
ATOM   1710 C  CA  . VAL A 1 210 ? -14.144 -3.944  23.748  1.00 8.50  ? 211 VAL A CA  1 
ATOM   1711 C  C   . VAL A 1 210 ? -15.478 -4.638  24.020  1.00 8.71  ? 211 VAL A C   1 
ATOM   1712 O  O   . VAL A 1 210 ? -15.822 -4.918  25.147  1.00 9.80  ? 211 VAL A O   1 
ATOM   1713 C  CB  . VAL A 1 210 ? -12.962 -4.793  24.224  1.00 8.39  ? 211 VAL A CB  1 
ATOM   1714 C  CG1 . VAL A 1 210 ? -12.980 -6.163  23.484  1.00 10.10 ? 211 VAL A CG1 1 
ATOM   1715 C  CG2 . VAL A 1 210 ? -11.667 -4.073  23.903  1.00 10.19 ? 211 VAL A CG2 1 
ATOM   1716 N  N   . LEU A 1 211 ? -16.221 -4.925  22.950  1.00 9.35  ? 212 LEU A N   1 
ATOM   1717 C  CA  . LEU A 1 211 ? -17.513 -5.565  23.137  1.00 9.51  ? 212 LEU A CA  1 
ATOM   1718 C  C   . LEU A 1 211 ? -17.364 -7.037  23.521  1.00 10.13 ? 212 LEU A C   1 
ATOM   1719 O  O   . LEU A 1 211 ? -16.511 -7.756  23.004  1.00 10.55 ? 212 LEU A O   1 
ATOM   1720 C  CB  . LEU A 1 211 ? -18.311 -5.444  21.831  1.00 10.42 ? 212 LEU A CB  1 
ATOM   1721 C  CG  . LEU A 1 211 ? -18.684 -4.022  21.399  1.00 11.15 ? 212 LEU A CG  1 
ATOM   1722 C  CD1 . LEU A 1 211 ? -19.751 -4.088  20.274  1.00 13.72 ? 212 LEU A CD1 1 
ATOM   1723 C  CD2 . LEU A 1 211 ? -19.229 -3.218  22.587  1.00 13.26 ? 212 LEU A CD2 1 
ATOM   1724 N  N   . LYS A 1 212 ? -18.232 -7.470  24.421  1.00 10.13 ? 213 LYS A N   1 
ATOM   1725 C  CA  . LYS A 1 212 ? -18.183 -8.861  24.814  1.00 12.15 ? 213 LYS A CA  1 
ATOM   1726 C  C   . LYS A 1 212 ? -18.645 -9.804  23.723  1.00 11.45 ? 213 LYS A C   1 
ATOM   1727 O  O   . LYS A 1 212 ? -18.171 -10.918 23.624  1.00 13.17 ? 213 LYS A O   1 
ATOM   1728 C  CB  . LYS A 1 212 ? -19.047 -9.049  26.067  1.00 14.81 ? 213 LYS A CB  1 
ATOM   1729 C  CG  . LYS A 1 212 ? -19.243 -10.493 26.486  1.00 22.04 ? 213 LYS A CG  1 
ATOM   1730 C  CD  . LYS A 1 212 ? -20.103 -10.641 27.688  1.00 33.63 ? 213 LYS A CD  1 
ATOM   1731 N  N   . GLU A 1 213 ? -19.669 -9.417  22.994  1.00 10.93 ? 214 GLU A N   1 
ATOM   1732 C  CA  . GLU A 1 213 ? -20.272 -10.316 21.995  1.00 11.00 ? 214 GLU A CA  1 
ATOM   1733 C  C   . GLU A 1 213 ? -19.489 -10.235 20.682  1.00 10.71 ? 214 GLU A C   1 
ATOM   1734 O  O   . GLU A 1 213 ? -19.421 -9.158  20.087  1.00 10.79 ? 214 GLU A O   1 
ATOM   1735 C  CB  . GLU A 1 213 ? -21.719 -9.925  21.720  1.00 13.21 ? 214 GLU A CB  1 
ATOM   1736 C  CG  . GLU A 1 213 ? -22.411 -10.912 20.841  1.00 16.10 ? 214 GLU A CG  1 
ATOM   1737 C  CD  . GLU A 1 213 ? -23.871 -10.619 20.548  1.00 22.54 ? 214 GLU A CD  1 
ATOM   1738 O  OE1 . GLU A 1 213 ? -24.488 -9.837  21.278  1.00 21.13 ? 214 GLU A OE1 1 
ATOM   1739 O  OE2 . GLU A 1 213 ? -24.407 -11.269 19.624  1.00 44.28 ? 214 GLU A OE2 1 
ATOM   1740 N  N   . PRO A 1 214 ? -18.906 -11.334 20.185  1.00 10.11 ? 215 PRO A N   1 
ATOM   1741 C  CA  . PRO A 1 214 ? -18.274 -11.313 18.872  1.00 10.44 ? 215 PRO A CA  1 
ATOM   1742 C  C   . PRO A 1 214 ? -19.309 -11.263 17.764  1.00 11.40 ? 215 PRO A C   1 
ATOM   1743 O  O   . PRO A 1 214 ? -20.493 -11.639 17.970  1.00 14.43 ? 215 PRO A O   1 
ATOM   1744 C  CB  . PRO A 1 214 ? -17.538 -12.644 18.802  1.00 12.30 ? 215 PRO A CB  1 
ATOM   1745 C  CG  . PRO A 1 214 ? -18.268 -13.539 19.721  1.00 19.77 ? 215 PRO A CG  1 
ATOM   1746 C  CD  . PRO A 1 214 ? -18.841 -12.661 20.823  1.00 13.08 ? 215 PRO A CD  1 
ATOM   1747 N  N   . ILE A 1 215 ? -18.876 -10.840 16.591  1.00 10.48 ? 216 ILE A N   1 
ATOM   1748 C  CA  . ILE A 1 215 ? -19.704 -11.036 15.391  1.00 11.79 ? 216 ILE A CA  1 
ATOM   1749 C  C   . ILE A 1 215 ? -19.170 -12.282 14.716  1.00 11.80 ? 216 ILE A C   1 
ATOM   1750 O  O   . ILE A 1 215 ? -18.008 -12.665 14.862  1.00 12.01 ? 216 ILE A O   1 
ATOM   1751 C  CB  . ILE A 1 215 ? -19.694 -9.837  14.407  1.00 12.35 ? 216 ILE A CB  1 
ATOM   1752 C  CG1 . ILE A 1 215 ? -18.256 -9.498  13.941  1.00 11.96 ? 216 ILE A CG1 1 
ATOM   1753 C  CG2 . ILE A 1 215 ? -20.397 -8.636  15.048  1.00 13.84 ? 216 ILE A CG2 1 
ATOM   1754 C  CD1 . ILE A 1 215 ? -18.256 -8.534  12.742  1.00 15.10 ? 216 ILE A CD1 1 
ATOM   1755 N  N   . SER A 1 216 ? -20.042 -12.951 13.968  1.00 12.75 ? 217 SER A N   1 
ATOM   1756 C  CA  A SER A 1 216 ? -19.634 -14.105 13.178  0.50 13.78 ? 217 SER A CA  1 
ATOM   1757 C  CA  B SER A 1 216 ? -19.724 -14.115 13.166  0.50 12.52 ? 217 SER A CA  1 
ATOM   1758 C  C   . SER A 1 216 ? -19.432 -13.651 11.745  1.00 11.33 ? 217 SER A C   1 
ATOM   1759 O  O   . SER A 1 216 ? -20.264 -12.931 11.178  1.00 13.48 ? 217 SER A O   1 
ATOM   1760 C  CB  A SER A 1 216 ? -20.610 -15.268 13.186  0.50 15.47 ? 217 SER A CB  1 
ATOM   1761 C  CB  B SER A 1 216 ? -20.864 -15.106 13.182  0.50 17.09 ? 217 SER A CB  1 
ATOM   1762 O  OG  A SER A 1 216 ? -20.827 -15.774 14.482  0.50 16.01 ? 217 SER A OG  1 
ATOM   1763 O  OG  B SER A 1 216 ? -20.425 -16.282 12.550  0.50 19.54 ? 217 SER A OG  1 
ATOM   1764 N  N   . VAL A 1 217 ? -18.330 -14.147 11.144  1.00 11.53 ? 218 VAL A N   1 
ATOM   1765 C  CA  . VAL A 1 217 ? -18.090 -13.922 9.729   1.00 11.50 ? 218 VAL A CA  1 
ATOM   1766 C  C   . VAL A 1 217 ? -17.866 -15.287 9.116   1.00 10.84 ? 218 VAL A C   1 
ATOM   1767 O  O   . VAL A 1 217 ? -17.476 -16.225 9.794   1.00 12.44 ? 218 VAL A O   1 
ATOM   1768 C  CB  . VAL A 1 217 ? -16.906 -12.987 9.482   1.00 12.84 ? 218 VAL A CB  1 
ATOM   1769 C  CG1 . VAL A 1 217 ? -17.151 -11.609 10.155  1.00 13.40 ? 218 VAL A CG1 1 
ATOM   1770 C  CG2 . VAL A 1 217 ? -15.608 -13.625 10.008  1.00 14.37 ? 218 VAL A CG2 1 
ATOM   1771 N  N   . SER A 1 218 ? -18.043 -15.414 7.809   1.00 12.26 ? 219 SER A N   1 
ATOM   1772 C  CA  . SER A 1 218 ? -17.823 -16.743 7.251   1.00 12.25 ? 219 SER A CA  1 
ATOM   1773 C  C   . SER A 1 218 ? -16.351 -16.991 6.951   1.00 10.82 ? 219 SER A C   1 
ATOM   1774 O  O   . SER A 1 218 ? -15.541 -16.082 6.783   1.00 11.78 ? 219 SER A O   1 
ATOM   1775 C  CB  . SER A 1 218 ? -18.643 -16.940 5.977   1.00 14.27 ? 219 SER A CB  1 
ATOM   1776 O  OG  . SER A 1 218 ? -18.210 -16.026 4.995   1.00 14.50 ? 219 SER A OG  1 
ATOM   1777 N  N   . SER A 1 219 ? -16.032 -18.265 6.759   1.00 12.35 ? 220 SER A N   1 
ATOM   1778 C  CA  . SER A 1 219 ? -14.680 -18.619 6.346   1.00 13.62 ? 220 SER A CA  1 
ATOM   1779 C  C   . SER A 1 219 ? -14.367 -17.937 5.017   1.00 14.56 ? 220 SER A C   1 
ATOM   1780 O  O   . SER A 1 219 ? -13.255 -17.481 4.845   1.00 15.06 ? 220 SER A O   1 
ATOM   1781 C  CB  . SER A 1 219 ? -14.538 -20.139 6.265   1.00 16.77 ? 220 SER A CB  1 
ATOM   1782 O  OG  . SER A 1 219 ? -15.499 -20.714 5.367   1.00 19.51 ? 220 SER A OG  1 
ATOM   1783 N  N   . GLU A 1 220 ? -15.349 -17.823 4.077   1.00 13.76 ? 221 GLU A N   1 
ATOM   1784 C  CA  . GLU A 1 220 ? -15.011 -17.161 2.822   1.00 15.70 ? 221 GLU A CA  1 
ATOM   1785 C  C   . GLU A 1 220 ? -14.677 -15.685 3.041   1.00 13.69 ? 221 GLU A C   1 
ATOM   1786 O  O   . GLU A 1 220 ? -13.840 -15.136 2.302   1.00 15.62 ? 221 GLU A O   1 
ATOM   1787 C  CB  . GLU A 1 220 ? -16.167 -17.301 1.827   1.00 16.96 ? 221 GLU A CB  1 
ATOM   1788 C  CG  . GLU A 1 220 ? -16.403 -18.751 1.387   1.00 23.49 ? 221 GLU A CG  1 
ATOM   1789 C  CD  . GLU A 1 220 ? -17.401 -19.534 2.236   1.00 25.97 ? 221 GLU A CD  1 
ATOM   1790 O  OE1 . GLU A 1 220 ? -17.844 -19.052 3.321   1.00 22.05 ? 221 GLU A OE1 1 
ATOM   1791 O  OE2 . GLU A 1 220 ? -17.858 -20.572 1.761   1.00 37.53 ? 221 GLU A OE2 1 
ATOM   1792 N  N   . GLN A 1 221 ? -15.372 -15.012 3.980   1.00 12.76 ? 222 GLN A N   1 
ATOM   1793 C  CA  . GLN A 1 221 ? -15.108 -13.601 4.165   1.00 12.36 ? 222 GLN A CA  1 
ATOM   1794 C  C   . GLN A 1 221 ? -13.682 -13.436 4.701   1.00 12.14 ? 222 GLN A C   1 
ATOM   1795 O  O   . GLN A 1 221 ? -12.941 -12.572 4.255   1.00 13.24 ? 222 GLN A O   1 
ATOM   1796 C  CB  . GLN A 1 221 ? -16.130 -13.062 5.147   1.00 12.45 ? 222 GLN A CB  1 
ATOM   1797 C  CG  . GLN A 1 221 ? -17.509 -12.923 4.435   1.00 14.21 ? 222 GLN A CG  1 
ATOM   1798 C  CD  . GLN A 1 221 ? -18.597 -12.383 5.336   1.00 12.00 ? 222 GLN A CD  1 
ATOM   1799 O  OE1 . GLN A 1 221 ? -18.724 -12.759 6.521   1.00 12.79 ? 222 GLN A OE1 1 
ATOM   1800 N  NE2 . GLN A 1 221 ? -19.405 -11.511 4.749   1.00 13.60 ? 222 GLN A NE2 1 
ATOM   1801 N  N   . VAL A 1 222 ? -13.295 -14.225 5.697   1.00 12.58 ? 223 VAL A N   1 
ATOM   1802 C  CA  . VAL A 1 222 ? -11.962 -14.025 6.252   1.00 12.30 ? 223 VAL A CA  1 
ATOM   1803 C  C   . VAL A 1 222 ? -10.884 -14.476 5.264   1.00 13.40 ? 223 VAL A C   1 
ATOM   1804 O  O   . VAL A 1 222 ? -9.802  -13.890 5.199   1.00 13.51 ? 223 VAL A O   1 
ATOM   1805 C  CB  . VAL A 1 222 ? -11.859 -14.635 7.668   1.00 16.28 ? 223 VAL A CB  1 
ATOM   1806 C  CG1 . VAL A 1 222 ? -11.808 -16.135 7.646   1.00 20.14 ? 223 VAL A CG1 1 
ATOM   1807 C  CG2 . VAL A 1 222 ? -10.642 -14.073 8.412   1.00 18.81 ? 223 VAL A CG2 1 
ATOM   1808 N  N   A LEU A 1 223 ? -11.163 -15.513 4.457   0.50 14.58 ? 224 LEU A N   1 
ATOM   1809 N  N   B LEU A 1 223 ? -11.174 -15.486 4.441   0.50 14.14 ? 224 LEU A N   1 
ATOM   1810 C  CA  A LEU A 1 223 ? -10.234 -15.898 3.401   0.50 16.96 ? 224 LEU A CA  1 
ATOM   1811 C  CA  B LEU A 1 223 ? -10.214 -15.864 3.417   0.50 15.80 ? 224 LEU A CA  1 
ATOM   1812 C  C   A LEU A 1 223 ? -9.920  -14.687 2.526   0.50 15.60 ? 224 LEU A C   1 
ATOM   1813 C  C   B LEU A 1 223 ? -9.934  -14.711 2.464   0.50 15.01 ? 224 LEU A C   1 
ATOM   1814 O  O   A LEU A 1 223 ? -8.754  -14.506 2.161   0.50 15.70 ? 224 LEU A O   1 
ATOM   1815 O  O   B LEU A 1 223 ? -8.807  -14.611 1.972   0.50 16.76 ? 224 LEU A O   1 
ATOM   1816 C  CB  A LEU A 1 223 ? -10.851 -17.055 2.593   0.50 21.79 ? 224 LEU A CB  1 
ATOM   1817 C  CB  B LEU A 1 223 ? -10.759 -17.093 2.682   0.50 18.58 ? 224 LEU A CB  1 
ATOM   1818 C  CG  A LEU A 1 223 ? -9.906  -18.092 1.978   0.50 33.34 ? 224 LEU A CG  1 
ATOM   1819 C  CG  B LEU A 1 223 ? -10.517 -18.383 3.448   0.50 20.45 ? 224 LEU A CG  1 
ATOM   1820 C  CD2 . LEU A 1 223 ? -9.158  -18.928 3.039   1.00 33.99 ? 224 LEU A CD2 1 
ATOM   1821 N  N   . LYS A 1 224 ? -10.920 -13.834 2.226   1.00 14.75 ? 225 LYS A N   1 
ATOM   1822 C  CA  . LYS A 1 224 ? -10.656 -12.681 1.396   1.00 15.32 ? 225 LYS A CA  1 
ATOM   1823 C  C   . LYS A 1 224 ? -9.717  -11.677 2.074   1.00 14.48 ? 225 LYS A C   1 
ATOM   1824 O  O   . LYS A 1 224 ? -8.855  -11.067 1.437   1.00 14.87 ? 225 LYS A O   1 
ATOM   1825 C  CB  . LYS A 1 224 ? -11.936 -12.090 0.819   1.00 19.21 ? 225 LYS A CB  1 
ATOM   1826 C  CG  . LYS A 1 224 ? -12.650 -13.025 -0.175  1.00 24.11 ? 225 LYS A CG  1 
ATOM   1827 N  N   . PHE A 1 225 ? -9.854  -11.482 3.399   1.00 13.24 ? 226 PHE A N   1 
ATOM   1828 C  CA  . PHE A 1 225 ? -8.862  -10.665 4.088   1.00 12.35 ? 226 PHE A CA  1 
ATOM   1829 C  C   . PHE A 1 225 ? -7.450  -11.206 3.859   1.00 14.05 ? 226 PHE A C   1 
ATOM   1830 O  O   . PHE A 1 225 ? -6.502  -10.434 3.669   1.00 14.63 ? 226 PHE A O   1 
ATOM   1831 C  CB  . PHE A 1 225 ? -9.052  -10.695 5.612   1.00 12.71 ? 226 PHE A CB  1 
ATOM   1832 C  CG  . PHE A 1 225 ? -10.247 -9.958  6.198   1.00 12.49 ? 226 PHE A CG  1 
ATOM   1833 C  CD1 . PHE A 1 225 ? -11.294 -9.438  5.453   1.00 15.62 ? 226 PHE A CD1 1 
ATOM   1834 C  CD2 . PHE A 1 225 ? -10.289 -9.785  7.575   1.00 14.69 ? 226 PHE A CD2 1 
ATOM   1835 C  CE1 . PHE A 1 225 ? -12.342 -8.775  6.087   1.00 17.04 ? 226 PHE A CE1 1 
ATOM   1836 C  CE2 . PHE A 1 225 ? -11.332 -9.124  8.204   1.00 16.78 ? 226 PHE A CE2 1 
ATOM   1837 C  CZ  . PHE A 1 225 ? -12.366 -8.614  7.461   1.00 18.30 ? 226 PHE A CZ  1 
ATOM   1838 N  N   . ARG A 1 226 ? -7.295  -12.533 3.905   1.00 13.00 ? 227 ARG A N   1 
ATOM   1839 C  CA  . ARG A 1 226 ? -5.958  -13.140 3.841   1.00 14.07 ? 227 ARG A CA  1 
ATOM   1840 C  C   . ARG A 1 226 ? -5.369  -13.112 2.457   1.00 13.76 ? 227 ARG A C   1 
ATOM   1841 O  O   . ARG A 1 226 ? -4.210  -13.550 2.297   1.00 17.03 ? 227 ARG A O   1 
ATOM   1842 C  CB  . ARG A 1 226 ? -6.049  -14.591 4.351   1.00 14.00 ? 227 ARG A CB  1 
ATOM   1843 C  CG  . ARG A 1 226 ? -6.478  -14.702 5.820   1.00 12.71 ? 227 ARG A CG  1 
ATOM   1844 C  CD  . ARG A 1 226 ? -6.451  -16.148 6.249   1.00 15.41 ? 227 ARG A CD  1 
ATOM   1845 N  NE  . ARG A 1 226 ? -6.987  -16.296 7.589   1.00 13.92 ? 227 ARG A NE  1 
ATOM   1846 C  CZ  . ARG A 1 226 ? -7.858  -17.209 7.960   1.00 14.10 ? 227 ARG A CZ  1 
ATOM   1847 N  NH1 . ARG A 1 226 ? -8.314  -18.085 7.081   1.00 20.92 ? 227 ARG A NH1 1 
ATOM   1848 N  NH2 . ARG A 1 226 ? -8.279  -17.252 9.211   1.00 15.96 ? 227 ARG A NH2 1 
ATOM   1849 N  N   . LYS A 1 227 ? -6.129  -12.630 1.455   1.00 14.04 ? 228 LYS A N   1 
ATOM   1850 C  CA  . LYS A 1 227 ? -5.611  -12.541 0.116   1.00 16.27 ? 228 LYS A CA  1 
ATOM   1851 C  C   . LYS A 1 227 ? -4.933  -11.186 -0.097  1.00 14.84 ? 228 LYS A C   1 
ATOM   1852 O  O   . LYS A 1 227 ? -4.313  -10.949 -1.136  1.00 17.94 ? 228 LYS A O   1 
ATOM   1853 C  CB  . LYS A 1 227 ? -6.714  -12.758 -0.946  1.00 18.39 ? 228 LYS A CB  1 
ATOM   1854 C  CG  . LYS A 1 227 ? -7.137  -14.210 -1.124  1.00 22.61 ? 228 LYS A CG  1 
ATOM   1855 C  CD  . LYS A 1 227 ? -8.212  -14.405 -2.210  1.00 33.10 ? 228 LYS A CD  1 
ATOM   1856 C  CE  . LYS A 1 227 ? -7.671  -14.625 -3.614  1.00 44.30 ? 228 LYS A CE  1 
ATOM   1857 N  N   . LEU A 1 228 ? -5.120  -10.211 0.799   1.00 15.39 ? 229 LEU A N   1 
ATOM   1858 C  CA  . LEU A 1 228 ? -4.414  -8.956  0.743   1.00 15.20 ? 229 LEU A CA  1 
ATOM   1859 C  C   . LEU A 1 228 ? -2.902  -9.196  0.897   1.00 17.31 ? 229 LEU A C   1 
ATOM   1860 O  O   . LEU A 1 228 ? -2.468  -10.235 1.320   1.00 15.64 ? 229 LEU A O   1 
ATOM   1861 C  CB  . LEU A 1 228 ? -4.955  -8.034  1.832   1.00 14.69 ? 229 LEU A CB  1 
ATOM   1862 C  CG  . LEU A 1 228 ? -6.407  -7.584  1.650   1.00 15.20 ? 229 LEU A CG  1 
ATOM   1863 C  CD1 . LEU A 1 228 ? -6.861  -6.945  2.936   1.00 16.25 ? 229 LEU A CD1 1 
ATOM   1864 C  CD2 . LEU A 1 228 ? -6.448  -6.545  0.506   1.00 19.44 ? 229 LEU A CD2 1 
ATOM   1865 N  N   . ASN A 1 229 ? -2.104  -8.204  0.488   1.00 17.31 ? 230 ASN A N   1 
ATOM   1866 C  CA  . ASN A 1 229 ? -0.651  -8.247  0.540   1.00 18.23 ? 230 ASN A CA  1 
ATOM   1867 C  C   . ASN A 1 229 ? -0.134  -7.092  1.383   1.00 18.90 ? 230 ASN A C   1 
ATOM   1868 O  O   . ASN A 1 229 ? -0.661  -5.954  1.293   1.00 20.48 ? 230 ASN A O   1 
ATOM   1869 C  CB  . ASN A 1 229 ? -0.104  -8.007  -0.877  1.00 19.70 ? 230 ASN A CB  1 
ATOM   1870 C  CG  . ASN A 1 229 ? -0.193  -9.165  -1.854  1.00 20.66 ? 230 ASN A CG  1 
ATOM   1871 O  OD1 . ASN A 1 229 ? 0.369   -9.085  -2.948  1.00 27.54 ? 230 ASN A OD1 1 
ATOM   1872 N  ND2 . ASN A 1 229 ? -0.898  -10.224 -1.516  1.00 21.63 ? 230 ASN A ND2 1 
ATOM   1873 N  N   . PHE A 1 230 ? 0.927   -7.415  2.145   1.00 17.48 ? 231 PHE A N   1 
ATOM   1874 C  CA  . PHE A 1 230 ? 1.729   -6.401  2.821   1.00 17.51 ? 231 PHE A CA  1 
ATOM   1875 C  C   . PHE A 1 230 ? 2.567   -5.549  1.866   1.00 18.99 ? 231 PHE A C   1 
ATOM   1876 O  O   . PHE A 1 230 ? 2.746   -4.357  2.096   1.00 22.05 ? 231 PHE A O   1 
ATOM   1877 C  CB  . PHE A 1 230 ? 2.714   -7.042  3.815   1.00 20.88 ? 231 PHE A CB  1 
ATOM   1878 C  CG  . PHE A 1 230 ? 2.118   -7.609  5.091   1.00 18.01 ? 231 PHE A CG  1 
ATOM   1879 C  CD1 . PHE A 1 230 ? 1.409   -6.783  5.947   1.00 19.10 ? 231 PHE A CD1 1 
ATOM   1880 C  CD2 . PHE A 1 230 ? 2.417   -8.917  5.505   1.00 18.82 ? 231 PHE A CD2 1 
ATOM   1881 C  CE1 . PHE A 1 230 ? 0.987   -7.276  7.181   1.00 18.84 ? 231 PHE A CE1 1 
ATOM   1882 C  CE2 . PHE A 1 230 ? 1.954   -9.430  6.705   1.00 17.47 ? 231 PHE A CE2 1 
ATOM   1883 C  CZ  . PHE A 1 230 ? 1.232   -8.600  7.541   1.00 18.71 ? 231 PHE A CZ  1 
ATOM   1884 N  N   . ASN A 1 231 ? 3.054   -6.189  0.803   1.00 20.83 ? 232 ASN A N   1 
ATOM   1885 C  CA  . ASN A 1 231 ? 4.046   -5.633  -0.090  1.00 20.25 ? 232 ASN A CA  1 
ATOM   1886 C  C   . ASN A 1 231 ? 3.320   -4.698  -1.042  1.00 23.61 ? 232 ASN A C   1 
ATOM   1887 O  O   . ASN A 1 231 ? 2.094   -4.836  -1.245  1.00 20.42 ? 232 ASN A O   1 
ATOM   1888 C  CB  . ASN A 1 231 ? 4.719   -6.750  -0.901  1.00 21.37 ? 232 ASN A CB  1 
ATOM   1889 C  CG  . ASN A 1 231 ? 3.710   -7.681  -1.528  1.00 23.36 ? 232 ASN A CG  1 
ATOM   1890 O  OD1 . ASN A 1 231 ? 3.176   -8.578  -0.825  1.00 22.08 ? 232 ASN A OD1 1 
ATOM   1891 N  ND2 . ASN A 1 231 ? 3.433   -7.494  -2.813  1.00 28.25 ? 232 ASN A ND2 1 
ATOM   1892 N  N   . GLY A 1 232 ? 4.072   -3.792  -1.670  1.00 22.33 ? 233 GLY A N   1 
ATOM   1893 C  CA  . GLY A 1 232 ? 3.509   -3.095  -2.815  1.00 26.93 ? 233 GLY A CA  1 
ATOM   1894 C  C   . GLY A 1 232 ? 3.529   -3.966  -4.083  1.00 23.24 ? 233 GLY A C   1 
ATOM   1895 O  O   . GLY A 1 232 ? 4.286   -4.957  -4.145  1.00 27.68 ? 233 GLY A O   1 
ATOM   1896 N  N   . GLU A 1 233 ? 2.745   -3.535  -5.107  1.00 30.41 ? 234 GLU A N   1 
ATOM   1897 C  CA  . GLU A 1 233 ? 2.688   -4.104  -6.468  1.00 35.64 ? 234 GLU A CA  1 
ATOM   1898 C  C   . GLU A 1 233 ? 4.073   -4.043  -7.108  1.00 37.60 ? 234 GLU A C   1 
ATOM   1899 O  O   . GLU A 1 233 ? 4.725   -2.997  -7.063  1.00 40.77 ? 234 GLU A O   1 
ATOM   1900 C  CB  . GLU A 1 233 ? 1.658   -3.345  -7.316  1.00 38.94 ? 234 GLU A CB  1 
ATOM   1901 C  CG  . GLU A 1 233 ? 1.533   -3.840  -8.753  1.00 61.01 ? 234 GLU A CG  1 
ATOM   1902 C  CD  . GLU A 1 233 ? 0.524   -3.114  -9.637  1.00 86.98 ? 234 GLU A CD  1 
ATOM   1903 O  OE1 . GLU A 1 233 ? -0.106  -2.156  -9.148  1.00 65.40 ? 234 GLU A OE1 1 
ATOM   1904 O  OE2 . GLU A 1 233 ? 0.374   -3.511  -10.810 1.00 56.88 ? 234 GLU A OE2 1 
ATOM   1905 N  N   . GLY A 1 234 ? 4.581   -5.208  -7.528  1.00 42.77 ? 235 GLY A N   1 
ATOM   1906 C  CA  . GLY A 1 234 ? 5.938   -5.338  -8.043  1.00 39.36 ? 235 GLY A CA  1 
ATOM   1907 C  C   . GLY A 1 234 ? 6.926   -5.998  -7.075  1.00 47.04 ? 235 GLY A C   1 
ATOM   1908 O  O   . GLY A 1 234 ? 7.961   -6.445  -7.553  1.00 52.69 ? 235 GLY A O   1 
ATOM   1909 N  N   . GLU A 1 235 ? 6.627   -6.051  -5.748  1.00 40.87 ? 236 GLU A N   1 
ATOM   1910 C  CA  . GLU A 1 235 ? 7.598   -6.571  -4.776  1.00 40.19 ? 236 GLU A CA  1 
ATOM   1911 C  C   . GLU A 1 235 ? 7.268   -8.022  -4.433  1.00 32.89 ? 236 GLU A C   1 
ATOM   1912 O  O   . GLU A 1 235 ? 6.133   -8.461  -4.682  1.00 41.64 ? 236 GLU A O   1 
ATOM   1913 C  CB  . GLU A 1 235 ? 7.590   -5.777  -3.464  1.00 32.72 ? 236 GLU A CB  1 
ATOM   1914 C  CG  . GLU A 1 235 ? 7.657   -4.260  -3.667  1.00 38.58 ? 236 GLU A CG  1 
ATOM   1915 C  CD  . GLU A 1 235 ? 7.290   -3.340  -2.495  1.00 51.15 ? 236 GLU A CD  1 
ATOM   1916 O  OE1 . GLU A 1 235 ? 6.675   -3.811  -1.464  1.00 52.10 ? 236 GLU A OE1 1 
ATOM   1917 O  OE2 . GLU A 1 235 ? 7.616   -2.122  -2.606  1.00 63.98 ? 236 GLU A OE2 1 
ATOM   1918 N  N   . PRO A 1 236 ? 8.226   -8.833  -3.895  1.00 32.83 ? 237 PRO A N   1 
ATOM   1919 C  CA  . PRO A 1 236 ? 7.912   -10.233 -3.594  1.00 29.62 ? 237 PRO A CA  1 
ATOM   1920 C  C   . PRO A 1 236 ? 6.610   -10.228 -2.772  1.00 26.60 ? 237 PRO A C   1 
ATOM   1921 O  O   . PRO A 1 236 ? 6.366   -9.369  -1.883  1.00 28.07 ? 237 PRO A O   1 
ATOM   1922 C  CB  . PRO A 1 236 ? 9.188   -10.764 -2.888  1.00 32.22 ? 237 PRO A CB  1 
ATOM   1923 C  CG  . PRO A 1 236 ? 10.293  -9.787  -3.323  1.00 32.14 ? 237 PRO A CG  1 
ATOM   1924 C  CD  . PRO A 1 236 ? 9.602   -8.462  -3.539  1.00 32.51 ? 237 PRO A CD  1 
ATOM   1925 N  N   . GLU A 1 237 ? 5.697   -11.147 -3.094  1.00 28.53 ? 238 GLU A N   1 
ATOM   1926 C  CA  . GLU A 1 237 ? 4.390   -11.255 -2.418  1.00 26.54 ? 238 GLU A CA  1 
ATOM   1927 C  C   . GLU A 1 237 ? 4.542   -11.799 -0.995  1.00 19.14 ? 238 GLU A C   1 
ATOM   1928 O  O   . GLU A 1 237 ? 5.151   -12.874 -0.825  1.00 23.46 ? 238 GLU A O   1 
ATOM   1929 C  CB  . GLU A 1 237 ? 3.451   -12.212 -3.191  1.00 29.80 ? 238 GLU A CB  1 
ATOM   1930 C  CG  . GLU A 1 237 ? 2.000   -12.221 -2.675  1.00 34.30 ? 238 GLU A CG  1 
ATOM   1931 C  CD  . GLU A 1 237 ? 0.853   -12.909 -3.418  1.00 42.10 ? 238 GLU A CD  1 
ATOM   1932 O  OE1 . GLU A 1 237 ? 1.129   -13.857 -4.180  1.00 44.05 ? 238 GLU A OE1 1 
ATOM   1933 O  OE2 . GLU A 1 237 ? -0.307  -12.491 -3.229  1.00 32.57 ? 238 GLU A OE2 1 
ATOM   1934 N  N   . GLU A 1 238 ? 3.991   -11.058 -0.015  1.00 20.73 ? 239 GLU A N   1 
ATOM   1935 C  CA  . GLU A 1 238 ? 3.896   -11.478 1.354   1.00 21.09 ? 239 GLU A CA  1 
ATOM   1936 C  C   . GLU A 1 238 ? 2.436   -11.231 1.745   1.00 18.03 ? 239 GLU A C   1 
ATOM   1937 O  O   . GLU A 1 238 ? 1.985   -10.091 1.803   1.00 19.22 ? 239 GLU A O   1 
ATOM   1938 C  CB  . GLU A 1 238 ? 4.864   -10.686 2.235   1.00 25.98 ? 239 GLU A CB  1 
ATOM   1939 C  CG  . GLU A 1 238 ? 6.348   -11.090 2.087   1.00 27.16 ? 239 GLU A CG  1 
ATOM   1940 C  CD  . GLU A 1 238 ? 7.287   -10.386 3.065   1.00 34.14 ? 239 GLU A CD  1 
ATOM   1941 O  OE1 . GLU A 1 238 ? 7.222   -10.692 4.282   1.00 35.81 ? 239 GLU A OE1 1 
ATOM   1942 O  OE2 . GLU A 1 238 ? 8.107   -9.516  2.614   1.00 34.32 ? 239 GLU A OE2 1 
ATOM   1943 N  N   . LEU A 1 239 ? 1.661   -12.299 1.959   1.00 15.95 ? 240 LEU A N   1 
ATOM   1944 C  CA  . LEU A 1 239 ? 0.264   -12.118 2.299   1.00 15.50 ? 240 LEU A CA  1 
ATOM   1945 C  C   . LEU A 1 239 ? 0.104   -11.339 3.605   1.00 14.06 ? 240 LEU A C   1 
ATOM   1946 O  O   . LEU A 1 239 ? 0.833   -11.581 4.586   1.00 16.10 ? 240 LEU A O   1 
ATOM   1947 C  CB  . LEU A 1 239 ? -0.394  -13.477 2.497   1.00 17.52 ? 240 LEU A CB  1 
ATOM   1948 C  CG  . LEU A 1 239 ? -0.462  -14.350 1.248   1.00 17.58 ? 240 LEU A CG  1 
ATOM   1949 C  CD1 . LEU A 1 239 ? -1.188  -15.628 1.572   1.00 23.78 ? 240 LEU A CD1 1 
ATOM   1950 C  CD2 . LEU A 1 239 ? -1.118  -13.587 0.130   1.00 21.79 ? 240 LEU A CD2 1 
ATOM   1951 N  N   . MET A 1 240 ? -0.938  -10.504 3.597   1.00 13.86 ? 241 MET A N   1 
ATOM   1952 C  CA  . MET A 1 240 ? -1.232  -9.738  4.797   1.00 15.06 ? 241 MET A CA  1 
ATOM   1953 C  C   . MET A 1 240 ? -2.060  -10.630 5.724   1.00 12.57 ? 241 MET A C   1 
ATOM   1954 O  O   . MET A 1 240 ? -3.296  -10.782 5.598   1.00 13.16 ? 241 MET A O   1 
ATOM   1955 C  CB  . MET A 1 240 ? -2.034  -8.513  4.389   1.00 16.49 ? 241 MET A CB  1 
ATOM   1956 C  CG  . MET A 1 240 ? -2.373  -7.587  5.592   1.00 15.30 ? 241 MET A CG  1 
ATOM   1957 S  SD  . MET A 1 240 ? -3.287  -6.127  5.133   1.00 17.55 ? 241 MET A SD  1 
ATOM   1958 C  CE  . MET A 1 240 ? -1.993  -5.080  4.434   1.00 18.02 ? 241 MET A CE  1 
ATOM   1959 N  N   . VAL A 1 241 ? -1.333  -11.252 6.665   1.00 12.42 ? 242 VAL A N   1 
ATOM   1960 C  CA  . VAL A 1 241 ? -1.945  -12.126 7.669   1.00 11.94 ? 242 VAL A CA  1 
ATOM   1961 C  C   . VAL A 1 241 ? -1.118  -11.931 8.932   1.00 11.38 ? 242 VAL A C   1 
ATOM   1962 O  O   . VAL A 1 241 ? 0.034   -11.513 8.862   1.00 12.53 ? 242 VAL A O   1 
ATOM   1963 C  CB  . VAL A 1 241 ? -1.896  -13.624 7.259   1.00 12.32 ? 242 VAL A CB  1 
ATOM   1964 C  CG1 . VAL A 1 241 ? -2.786  -13.933 6.079   1.00 15.20 ? 242 VAL A CG1 1 
ATOM   1965 C  CG2 . VAL A 1 241 ? -0.458  -14.107 7.049   1.00 13.82 ? 242 VAL A CG2 1 
ATOM   1966 N  N   . ASP A 1 242 ? -1.724  -12.181 10.092  1.00 10.58 ? 243 ASP A N   1 
ATOM   1967 C  CA  . ASP A 1 242 ? -1.050  -12.059 11.394  1.00 11.61 ? 243 ASP A CA  1 
ATOM   1968 C  C   . ASP A 1 242 ? -0.547  -10.633 11.584  1.00 11.04 ? 243 ASP A C   1 
ATOM   1969 O  O   . ASP A 1 242 ? 0.558   -10.401 12.110  1.00 12.21 ? 243 ASP A O   1 
ATOM   1970 C  CB  . ASP A 1 242 ? 0.030   -13.122 11.579  1.00 12.07 ? 243 ASP A CB  1 
ATOM   1971 C  CG  . ASP A 1 242 ? -0.555  -14.501 11.678  1.00 11.70 ? 243 ASP A CG  1 
ATOM   1972 O  OD1 . ASP A 1 242 ? -1.636  -14.676 12.294  1.00 11.76 ? 243 ASP A OD1 1 
ATOM   1973 O  OD2 . ASP A 1 242 ? 0.016   -15.415 11.052  1.00 14.95 ? 243 ASP A OD2 1 
ATOM   1974 N  N   . ASN A 1 243 ? -1.444  -9.675  11.296  1.00 10.02 ? 244 ASN A N   1 
ATOM   1975 C  CA  . ASN A 1 243 ? -1.174  -8.254  11.534  1.00 9.99  ? 244 ASN A CA  1 
ATOM   1976 C  C   . ASN A 1 243 ? -1.724  -7.805  12.883  1.00 9.90  ? 244 ASN A C   1 
ATOM   1977 O  O   . ASN A 1 243 ? -2.420  -6.793  12.953  1.00 11.51 ? 244 ASN A O   1 
ATOM   1978 C  CB  . ASN A 1 243 ? -1.681  -7.370  10.393  1.00 11.85 ? 244 ASN A CB  1 
ATOM   1979 C  CG  . ASN A 1 243 ? -3.155  -7.572  10.108  1.00 11.35 ? 244 ASN A CG  1 
ATOM   1980 O  OD1 . ASN A 1 243 ? -3.815  -8.465  10.626  1.00 12.10 ? 244 ASN A OD1 1 
ATOM   1981 N  ND2 . ASN A 1 243 ? -3.736  -6.623  9.361   1.00 14.26 ? 244 ASN A ND2 1 
ATOM   1982 N  N   . TRP A 1 244 ? -1.423  -8.564  13.927  1.00 10.21 ? 245 TRP A N   1 
ATOM   1983 C  CA  . TRP A 1 244 ? -1.896  -8.311  15.282  1.00 9.26  ? 245 TRP A CA  1 
ATOM   1984 C  C   . TRP A 1 244 ? -0.691  -8.214  16.201  1.00 10.07 ? 245 TRP A C   1 
ATOM   1985 O  O   . TRP A 1 244 ? 0.311   -8.916  16.054  1.00 10.93 ? 245 TRP A O   1 
ATOM   1986 C  CB  . TRP A 1 244 ? -2.863  -9.391  15.760  1.00 8.89  ? 245 TRP A CB  1 
ATOM   1987 C  CG  . TRP A 1 244 ? -2.392  -10.795 15.576  1.00 9.62  ? 245 TRP A CG  1 
ATOM   1988 C  CD1 . TRP A 1 244 ? -2.504  -11.529 14.409  1.00 9.77  ? 245 TRP A CD1 1 
ATOM   1989 C  CD2 . TRP A 1 244 ? -1.825  -11.668 16.565  1.00 9.59  ? 245 TRP A CD2 1 
ATOM   1990 N  NE1 . TRP A 1 244 ? -2.014  -12.810 14.602  1.00 10.50 ? 245 TRP A NE1 1 
ATOM   1991 C  CE2 . TRP A 1 244 ? -1.580  -12.912 15.915  1.00 10.07 ? 245 TRP A CE2 1 
ATOM   1992 C  CE3 . TRP A 1 244 ? -1.511  -11.530 17.918  1.00 10.98 ? 245 TRP A CE3 1 
ATOM   1993 C  CZ2 . TRP A 1 244 ? -1.054  -14.009 16.604  1.00 11.18 ? 245 TRP A CZ2 1 
ATOM   1994 C  CZ3 . TRP A 1 244 ? -0.989  -12.622 18.584  1.00 11.81 ? 245 TRP A CZ3 1 
ATOM   1995 C  CH2 . TRP A 1 244 ? -0.747  -13.834 17.927  1.00 12.41 ? 245 TRP A CH2 1 
ATOM   1996 N  N   . ARG A 1 245 ? -0.798  -7.317  17.172  1.00 9.83  ? 246 ARG A N   1 
ATOM   1997 C  CA  . ARG A 1 245 ? 0.168   -7.207  18.269  1.00 9.79  ? 246 ARG A CA  1 
ATOM   1998 C  C   . ARG A 1 245 ? -0.318  -8.115  19.372  1.00 9.49  ? 246 ARG A C   1 
ATOM   1999 O  O   . ARG A 1 245 ? -1.506  -8.134  19.694  1.00 11.19 ? 246 ARG A O   1 
ATOM   2000 C  CB  . ARG A 1 245 ? 0.218   -5.758  18.777  1.00 9.29  ? 246 ARG A CB  1 
ATOM   2001 C  CG  . ARG A 1 245 ? 1.358   -5.539  19.772  1.00 10.05 ? 246 ARG A CG  1 
ATOM   2002 C  CD  . ARG A 1 245 ? 1.246   -4.190  20.405  1.00 10.41 ? 246 ARG A CD  1 
ATOM   2003 N  NE  . ARG A 1 245 ? 2.514   -3.842  21.100  1.00 10.54 ? 246 ARG A NE  1 
ATOM   2004 C  CZ  . ARG A 1 245 ? 2.672   -2.819  21.904  1.00 10.38 ? 246 ARG A CZ  1 
ATOM   2005 N  NH1 . ARG A 1 245 ? 1.659   -2.006  22.148  1.00 11.49 ? 246 ARG A NH1 1 
ATOM   2006 N  NH2 . ARG A 1 245 ? 3.844   -2.599  22.472  1.00 13.21 ? 246 ARG A NH2 1 
ATOM   2007 N  N   . PRO A 1 246 ? 0.568   -8.894  20.006  1.00 10.46 ? 247 PRO A N   1 
ATOM   2008 C  CA  . PRO A 1 246 ? 0.137   -9.729  21.117  1.00 10.98 ? 247 PRO A CA  1 
ATOM   2009 C  C   . PRO A 1 246 ? -0.201  -8.911  22.346  1.00 10.22 ? 247 PRO A C   1 
ATOM   2010 O  O   . PRO A 1 246 ? 0.139   -7.735  22.466  1.00 10.80 ? 247 PRO A O   1 
ATOM   2011 C  CB  . PRO A 1 246 ? 1.395   -10.554 21.439  1.00 15.20 ? 247 PRO A CB  1 
ATOM   2012 C  CG  . PRO A 1 246 ? 2.274   -10.494 20.242  1.00 18.70 ? 247 PRO A CG  1 
ATOM   2013 C  CD  . PRO A 1 246 ? 1.976   -9.132  19.629  1.00 12.77 ? 247 PRO A CD  1 
ATOM   2014 N  N   . ALA A 1 247 ? -0.864  -9.585  23.304  1.00 10.67 ? 248 ALA A N   1 
ATOM   2015 C  CA  . ALA A 1 247 ? -1.196  -8.937  24.566  1.00 11.13 ? 248 ALA A CA  1 
ATOM   2016 C  C   . ALA A 1 247 ? 0.036   -8.397  25.269  1.00 12.05 ? 248 ALA A C   1 
ATOM   2017 O  O   . ALA A 1 247 ? 1.048   -9.066  25.342  1.00 13.54 ? 248 ALA A O   1 
ATOM   2018 C  CB  . ALA A 1 247 ? -1.974  -9.962  25.429  1.00 14.16 ? 248 ALA A CB  1 
ATOM   2019 N  N   . GLN A 1 248 ? -0.110  -7.217  25.874  1.00 10.80 ? 249 GLN A N   1 
ATOM   2020 C  CA  . GLN A 1 248 ? 0.931   -6.512  26.581  1.00 10.90 ? 249 GLN A CA  1 
ATOM   2021 C  C   . GLN A 1 248 ? 0.613   -6.543  28.064  1.00 11.06 ? 249 GLN A C   1 
ATOM   2022 O  O   . GLN A 1 248 ? -0.541  -6.707  28.489  1.00 13.10 ? 249 GLN A O   1 
ATOM   2023 C  CB  . GLN A 1 248 ? 0.964   -5.096  26.070  1.00 12.66 ? 249 GLN A CB  1 
ATOM   2024 C  CG  . GLN A 1 248 ? 1.279   -5.016  24.564  1.00 12.22 ? 249 GLN A CG  1 
ATOM   2025 C  CD  . GLN A 1 248 ? 2.596   -5.700  24.267  1.00 12.89 ? 249 GLN A CD  1 
ATOM   2026 O  OE1 . GLN A 1 248 ? 3.642   -5.365  24.839  1.00 16.76 ? 249 GLN A OE1 1 
ATOM   2027 N  NE2 . GLN A 1 248 ? 2.587   -6.607  23.301  1.00 14.42 ? 249 GLN A NE2 1 
ATOM   2028 N  N   . PRO A 1 249 ? 1.599   -6.224  28.921  1.00 14.12 ? 250 PRO A N   1 
ATOM   2029 C  CA  . PRO A 1 249 ? 1.403   -6.234  30.353  1.00 15.42 ? 250 PRO A CA  1 
ATOM   2030 C  C   . PRO A 1 249 ? 0.335   -5.249  30.799  1.00 15.05 ? 250 PRO A C   1 
ATOM   2031 O  O   . PRO A 1 249 ? 0.373   -4.069  30.456  1.00 14.63 ? 250 PRO A O   1 
ATOM   2032 C  CB  . PRO A 1 249 ? 2.795   -5.879  30.916  1.00 19.65 ? 250 PRO A CB  1 
ATOM   2033 C  CG  . PRO A 1 249 ? 3.766   -6.300  29.824  1.00 22.57 ? 250 PRO A CG  1 
ATOM   2034 C  CD  . PRO A 1 249 ? 2.995   -5.941  28.571  1.00 16.78 ? 250 PRO A CD  1 
ATOM   2035 N  N   . LEU A 1 250 ? -0.562  -5.738  31.651  1.00 15.18 ? 251 LEU A N   1 
ATOM   2036 C  CA  . LEU A 1 250 ? -1.612  -4.868  32.168  1.00 13.96 ? 251 LEU A CA  1 
ATOM   2037 C  C   . LEU A 1 250 ? -1.041  -3.809  33.112  1.00 15.06 ? 251 LEU A C   1 
ATOM   2038 O  O   . LEU A 1 250 ? -1.585  -2.705  33.231  1.00 14.61 ? 251 LEU A O   1 
ATOM   2039 C  CB  . LEU A 1 250 ? -2.627  -5.731  32.922  1.00 18.36 ? 251 LEU A CB  1 
ATOM   2040 C  CG  . LEU A 1 250 ? -3.923  -5.038  33.318  1.00 16.95 ? 251 LEU A CG  1 
ATOM   2041 C  CD1 . LEU A 1 250 ? -4.683  -4.492  32.094  1.00 17.06 ? 251 LEU A CD1 1 
ATOM   2042 C  CD2 . LEU A 1 250 ? -4.835  -6.021  34.044  1.00 22.31 ? 251 LEU A CD2 1 
ATOM   2043 N  N   . LYS A 1 251 ? 0.049   -4.125  33.834  1.00 16.54 ? 252 LYS A N   1 
ATOM   2044 C  CA  . LYS A 1 251 ? 0.696   -3.139  34.717  1.00 18.70 ? 252 LYS A CA  1 
ATOM   2045 C  C   . LYS A 1 251 ? -0.324  -2.593  35.722  1.00 19.64 ? 252 LYS A C   1 
ATOM   2046 O  O   . LYS A 1 251 ? -1.072  -3.357  36.287  1.00 23.77 ? 252 LYS A O   1 
ATOM   2047 C  CB  . LYS A 1 251 ? 1.510   -2.090  33.950  1.00 19.96 ? 252 LYS A CB  1 
ATOM   2048 C  CG  . LYS A 1 251 ? 2.645   -2.737  33.170  1.00 22.26 ? 252 LYS A CG  1 
ATOM   2049 C  CD  . LYS A 1 251 ? 3.543   -1.828  32.456  1.00 25.87 ? 252 LYS A CD  1 
ATOM   2050 C  CE  . LYS A 1 251 ? 4.794   -2.543  32.015  1.00 29.35 ? 252 LYS A CE  1 
ATOM   2051 N  NZ  . LYS A 1 251 ? 5.620   -1.643  31.167  1.00 37.04 ? 252 LYS A NZ  1 
ATOM   2052 N  N   . ASN A 1 252 ? -0.364  -1.297  35.946  1.00 19.04 ? 253 ASN A N   1 
ATOM   2053 C  CA  . ASN A 1 252 ? -1.217  -0.863  37.047  1.00 29.29 ? 253 ASN A CA  1 
ATOM   2054 C  C   . ASN A 1 252 ? -2.630  -0.509  36.547  1.00 30.16 ? 253 ASN A C   1 
ATOM   2055 O  O   . ASN A 1 252 ? -3.063  0.626   36.806  1.00 46.02 ? 253 ASN A O   1 
ATOM   2056 C  CB  . ASN A 1 252 ? -0.498  0.240   37.837  1.00 35.17 ? 253 ASN A CB  1 
ATOM   2057 C  CG  . ASN A 1 252 ? -1.230  0.901   38.987  1.00 40.02 ? 253 ASN A CG  1 
ATOM   2058 O  OD1 . ASN A 1 252 ? -1.674  0.236   39.933  1.00 62.63 ? 253 ASN A OD1 1 
ATOM   2059 N  ND2 . ASN A 1 252 ? -1.259  2.224   38.955  1.00 47.33 ? 253 ASN A ND2 1 
ATOM   2060 N  N   . ARG A 1 253 ? -3.309  -1.381  35.732  1.00 17.25 ? 254 ARG A N   1 
ATOM   2061 C  CA  . ARG A 1 253 ? -4.620  -1.041  35.238  1.00 14.26 ? 254 ARG A CA  1 
ATOM   2062 C  C   . ARG A 1 253 ? -5.663  -2.032  35.715  1.00 15.84 ? 254 ARG A C   1 
ATOM   2063 O  O   . ARG A 1 253 ? -5.400  -3.210  35.844  1.00 23.33 ? 254 ARG A O   1 
ATOM   2064 C  CB  . ARG A 1 253 ? -4.557  -0.974  33.709  1.00 13.77 ? 254 ARG A CB  1 
ATOM   2065 C  CG  . ARG A 1 253 ? -3.675  0.171   33.202  1.00 14.03 ? 254 ARG A CG  1 
ATOM   2066 C  CD  . ARG A 1 253 ? -3.552  0.186   31.696  1.00 13.48 ? 254 ARG A CD  1 
ATOM   2067 N  NE  . ARG A 1 253 ? -2.742  -0.947  31.295  1.00 12.27 ? 254 ARG A NE  1 
ATOM   2068 C  CZ  . ARG A 1 253 ? -2.505  -1.221  30.011  1.00 10.64 ? 254 ARG A CZ  1 
ATOM   2069 N  NH1 . ARG A 1 253 ? -3.103  -0.549  29.034  1.00 10.46 ? 254 ARG A NH1 1 
ATOM   2070 N  NH2 . ARG A 1 253 ? -1.687  -2.201  29.677  1.00 10.46 ? 254 ARG A NH2 1 
ATOM   2071 N  N   . GLN A 1 254 ? -6.889  -1.531  35.825  1.00 17.21 ? 255 GLN A N   1 
ATOM   2072 C  CA  . GLN A 1 254 ? -8.113  -2.301  36.045  1.00 18.68 ? 255 GLN A CA  1 
ATOM   2073 C  C   . GLN A 1 254 ? -8.940  -2.236  34.766  1.00 17.02 ? 255 GLN A C   1 
ATOM   2074 O  O   . GLN A 1 254 ? -9.075  -1.191  34.136  1.00 22.59 ? 255 GLN A O   1 
ATOM   2075 C  CB  . GLN A 1 254 ? -8.936  -1.701  37.182  1.00 24.88 ? 255 GLN A CB  1 
ATOM   2076 C  CG  . GLN A 1 254 ? -8.273  -1.953  38.519  1.00 30.03 ? 255 GLN A CG  1 
ATOM   2077 N  N   . ILE A 1 255 ? -9.448  -3.379  34.394  1.00 14.63 ? 256 ILE A N   1 
ATOM   2078 C  CA  . ILE A 1 255 ? -10.409 -3.448  33.330  1.00 12.81 ? 256 ILE A CA  1 
ATOM   2079 C  C   . ILE A 1 255 ? -11.784 -3.478  33.994  1.00 13.50 ? 256 ILE A C   1 
ATOM   2080 O  O   . ILE A 1 255 ? -12.007 -4.184  34.982  1.00 14.42 ? 256 ILE A O   1 
ATOM   2081 C  CB  . ILE A 1 255 ? -10.185 -4.702  32.490  1.00 12.92 ? 256 ILE A CB  1 
ATOM   2082 C  CG1 . ILE A 1 255 ? -8.757  -4.727  31.926  1.00 14.43 ? 256 ILE A CG1 1 
ATOM   2083 C  CG2 . ILE A 1 255 ? -11.269 -4.767  31.386  1.00 14.67 ? 256 ILE A CG2 1 
ATOM   2084 C  CD1 . ILE A 1 255 ? -8.512  -5.980  31.109  1.00 17.79 ? 256 ILE A CD1 1 
ATOM   2085 N  N   . LYS A 1 256 ? -12.695 -2.627  33.493  1.00 13.41 ? 257 LYS A N   1 
ATOM   2086 C  CA  . LYS A 1 256 ? -14.025 -2.482  34.045  1.00 13.97 ? 257 LYS A CA  1 
ATOM   2087 C  C   . LYS A 1 256 ? -15.007 -3.100  33.076  1.00 14.76 ? 257 LYS A C   1 
ATOM   2088 O  O   . LYS A 1 256 ? -14.782 -3.085  31.872  1.00 15.91 ? 257 LYS A O   1 
ATOM   2089 C  CB  . LYS A 1 256 ? -14.349 -1.002  34.236  1.00 16.47 ? 257 LYS A CB  1 
ATOM   2090 C  CG  . LYS A 1 256 ? -13.529 -0.285  35.317  1.00 23.43 ? 257 LYS A CG  1 
ATOM   2091 N  N   . ALA A 1 257 ? -16.063 -3.720  33.578  1.00 15.19 ? 258 ALA A N   1 
ATOM   2092 C  CA  . ALA A 1 257 ? -17.116 -4.350  32.798  1.00 15.44 ? 258 ALA A CA  1 
ATOM   2093 C  C   . ALA A 1 257 ? -18.392 -3.535  32.948  1.00 15.54 ? 258 ALA A C   1 
ATOM   2094 O  O   . ALA A 1 257 ? -18.742 -3.100  34.039  1.00 17.08 ? 258 ALA A O   1 
ATOM   2095 C  CB  . ALA A 1 257 ? -17.347 -5.774  33.231  1.00 16.79 ? 258 ALA A CB  1 
ATOM   2096 N  N   . SER A 1 258 ? -19.176 -3.435  31.870  1.00 15.09 ? 259 SER A N   1 
ATOM   2097 C  CA  . SER A 1 258 ? -20.453 -2.714  31.906  1.00 15.99 ? 259 SER A CA  1 
ATOM   2098 C  C   . SER A 1 258 ? -21.580 -3.644  32.326  1.00 17.74 ? 259 SER A C   1 
ATOM   2099 O  O   . SER A 1 258 ? -22.716 -3.170  32.409  1.00 22.01 ? 259 SER A O   1 
ATOM   2100 C  CB  . SER A 1 258 ? -20.719 -2.178  30.542  1.00 17.34 ? 259 SER A CB  1 
ATOM   2101 O  OG  . SER A 1 258 ? -21.142 -3.184  29.656  1.00 16.20 ? 259 SER A OG  1 
ATOM   2102 N  N   . PHE A 1 259 ? -21.269 -4.912  32.620  1.00 17.78 ? 260 PHE A N   1 
ATOM   2103 C  CA  . PHE A 1 259 ? -22.293 -5.939  32.752  1.00 19.60 ? 260 PHE A CA  1 
ATOM   2104 C  C   . PHE A 1 259 ? -21.821 -6.946  33.816  1.00 24.78 ? 260 PHE A C   1 
ATOM   2105 O  O   . PHE A 1 259 ? -20.590 -7.070  34.089  1.00 22.78 ? 260 PHE A O   1 
ATOM   2106 C  CB  . PHE A 1 259 ? -22.547 -6.615  31.390  1.00 21.31 ? 260 PHE A CB  1 
ATOM   2107 C  CG  . PHE A 1 259 ? -21.309 -7.367  30.932  1.00 19.00 ? 260 PHE A CG  1 
ATOM   2108 C  CD1 . PHE A 1 259 ? -20.252 -6.716  30.291  1.00 18.42 ? 260 PHE A CD1 1 
ATOM   2109 C  CD2 . PHE A 1 259 ? -21.098 -8.694  31.319  1.00 24.82 ? 260 PHE A CD2 1 
ATOM   2110 C  CE1 . PHE A 1 259 ? -19.075 -7.387  29.950  1.00 21.75 ? 260 PHE A CE1 1 
ATOM   2111 C  CE2 . PHE A 1 259 ? -19.915 -9.353  30.999  1.00 23.31 ? 260 PHE A CE2 1 
ATOM   2112 C  CZ  . PHE A 1 259 ? -18.908 -8.702  30.335  1.00 21.70 ? 260 PHE A CZ  1 
ATOM   2113 N  N   . LYS A 1 260 ? -22.860 -7.625  34.333  1.00 36.80 ? 261 LYS A N   1 
ATOM   2114 C  CA  . LYS A 1 260 ? -22.978 -8.835  35.130  1.00 54.27 ? 261 LYS A CA  1 
ATOM   2115 C  C   . LYS A 1 260 ? -22.778 -8.501  36.609  1.00 68.71 ? 261 LYS A C   1 
ATOM   2116 O  O   . LYS A 1 260 ? -23.454 -7.579  37.099  1.00 68.37 ? 261 LYS A O   1 
ATOM   2117 C  CB  . LYS A 1 260 ? -22.269 -10.059 34.517  1.00 70.95 ? 261 LYS A CB  1 
ATOM   2118 O  OXT . LYS A 1 260 ? -21.978 -9.126  37.307  1.00 88.13 ? 261 LYS A OXT 1 
HETATM 2119 ZN ZN  . ZN  B 2 .   ? -6.379  -1.650  15.198  1.00 9.04  ? 301 ZN  A ZN  1 
HETATM 2120 O  O20 A V13 C 3 .   ? -1.521  5.901   14.049  0.50 22.87 ? 302 V13 A O20 1 
HETATM 2121 O  O20 B V13 C 3 .   ? -3.525  4.912   11.308  0.50 77.23 ? 302 V13 A O20 1 
HETATM 2122 S  S15 A V13 C 3 .   ? -2.960  6.011   13.954  0.50 22.78 ? 302 V13 A S15 1 
HETATM 2123 S  S15 B V13 C 3 .   ? -3.982  5.529   12.639  0.50 41.95 ? 302 V13 A S15 1 
HETATM 2124 O  O19 A V13 C 3 .   ? -3.386  7.175   14.862  0.50 26.02 ? 302 V13 A O19 1 
HETATM 2125 O  O19 B V13 C 3 .   ? -2.623  6.117   13.089  0.50 51.82 ? 302 V13 A O19 1 
HETATM 2126 C  C16 A V13 C 3 .   ? -3.357  6.308   12.217  0.50 27.81 ? 302 V13 A C16 1 
HETATM 2127 C  C16 B V13 C 3 .   ? -4.903  7.067   12.272  0.05 40.11 ? 302 V13 A C16 1 
HETATM 2128 C  C17 A V13 C 3 .   ? -4.229  5.144   11.659  0.50 38.09 ? 302 V13 A C17 1 
HETATM 2129 C  C17 B V13 C 3 .   ? -4.917  8.012   13.760  0.05 35.08 ? 302 V13 A C17 1 
HETATM 2130 O  O18 A V13 C 3 .   ? -3.632  4.226   10.727  0.50 40.74 ? 302 V13 A O18 1 
HETATM 2131 O  O18 B V13 C 3 .   ? -6.788  8.919   13.049  0.05 30.02 ? 302 V13 A O18 1 
HETATM 2132 C  C1  A V13 C 3 .   ? -3.632  4.555   14.716  0.50 15.35 ? 302 V13 A C1  1 
HETATM 2133 C  C1  B V13 C 3 .   ? -4.405  4.129   13.696  0.50 31.55 ? 302 V13 A C1  1 
HETATM 2134 C  C6  A V13 C 3 .   ? -5.008  4.482   14.929  0.50 16.16 ? 302 V13 A C6  1 
HETATM 2135 C  C6  B V13 C 3 .   ? -5.215  4.401   14.799  0.50 28.32 ? 302 V13 A C6  1 
HETATM 2136 F  F11 A V13 C 3 .   ? -5.865  5.450   14.603  0.50 18.64 ? 302 V13 A F11 1 
HETATM 2137 F  F11 B V13 C 3 .   ? -5.640  5.675   15.035  0.50 36.95 ? 302 V13 A F11 1 
HETATM 2138 C  C5  A V13 C 3 .   ? -5.633  3.394   15.553  0.50 11.77 ? 302 V13 A C5  1 
HETATM 2139 C  C5  B V13 C 3 .   ? -5.597  3.373   15.684  0.50 18.65 ? 302 V13 A C5  1 
HETATM 2140 F  F12 A V13 C 3 .   ? -6.989  3.409   15.717  0.50 16.40 ? 302 V13 A F12 1 
HETATM 2141 F  F12 B V13 C 3 .   ? -6.382  3.605   16.753  0.50 22.08 ? 302 V13 A F12 1 
HETATM 2142 C  C4  A V13 C 3 .   ? -4.864  2.300   15.938  0.50 8.08  ? 302 V13 A C4  1 
HETATM 2143 C  C4  B V13 C 3 .   ? -5.163  2.068   15.493  0.50 18.39 ? 302 V13 A C4  1 
HETATM 2144 S  S7  A V13 C 3 .   ? -5.571  0.850   16.758  0.50 7.06  ? 302 V13 A S7  1 
HETATM 2145 S  S7  B V13 C 3 .   ? -5.634  0.811   16.692  0.50 15.26 ? 302 V13 A S7  1 
HETATM 2146 O  O9  A V13 C 3 .   ? -6.998  0.989   16.574  0.50 6.32  ? 302 V13 A O9  1 
HETATM 2147 O  O9  B V13 C 3 .   ? -7.096  0.932   16.636  0.50 17.20 ? 302 V13 A O9  1 
HETATM 2148 N  N10 A V13 C 3 .   ? -5.043  -0.489  16.044  0.50 6.18  ? 302 V13 A N10 1 
HETATM 2149 N  N10 B V13 C 3 .   ? -5.026  -0.638  16.209  0.50 18.27 ? 302 V13 A N10 1 
HETATM 2150 O  O8  A V13 C 3 .   ? -5.018  0.984   18.081  0.50 7.89  ? 302 V13 A O8  1 
HETATM 2151 O  O8  B V13 C 3 .   ? -5.001  1.149   17.972  0.50 14.36 ? 302 V13 A O8  1 
HETATM 2152 C  C3  A V13 C 3 .   ? -3.487  2.394   15.707  0.50 8.61  ? 302 V13 A C3  1 
HETATM 2153 C  C3  B V13 C 3 .   ? -4.377  1.792   14.361  0.50 19.48 ? 302 V13 A C3  1 
HETATM 2154 F  F13 A V13 C 3 .   ? -2.700  1.378   16.131  0.50 9.20  ? 302 V13 A F13 1 
HETATM 2155 F  F13 B V13 C 3 .   ? -3.951  0.524   14.052  0.50 23.45 ? 302 V13 A F13 1 
HETATM 2156 C  C2  A V13 C 3 .   ? -2.875  3.476   15.108  0.50 11.76 ? 302 V13 A C2  1 
HETATM 2157 C  C2  B V13 C 3 .   ? -3.992  2.790   13.465  0.50 23.99 ? 302 V13 A C2  1 
HETATM 2158 F  F14 A V13 C 3 .   ? -1.537  3.475   14.992  0.50 13.59 ? 302 V13 A F14 1 
HETATM 2159 F  F14 B V13 C 3 .   ? -3.198  2.342   12.440  0.50 34.83 ? 302 V13 A F14 1 
HETATM 2160 S  S   . DMS D 4 .   ? 1.569   -11.748 14.977  1.00 25.09 ? 303 DMS A S   1 
HETATM 2161 O  O   . DMS D 4 .   ? 2.159   -13.137 14.524  1.00 33.87 ? 303 DMS A O   1 
HETATM 2162 C  C1  . DMS D 4 .   ? 2.793   -10.581 14.552  1.00 29.16 ? 303 DMS A C1  1 
HETATM 2163 C  C2  . DMS D 4 .   ? 1.856   -11.656 16.716  1.00 21.52 ? 303 DMS A C2  1 
HETATM 2164 O  O   . HOH E 5 .   ? -17.651 19.098  5.964   1.00 16.00 ? 401 HOH A O   1 
HETATM 2165 O  O   . HOH E 5 .   ? -4.670  2.181   37.402  1.00 33.67 ? 402 HOH A O   1 
HETATM 2166 O  O   . HOH E 5 .   ? -15.254 -10.202 37.336  1.00 26.00 ? 403 HOH A O   1 
HETATM 2167 O  O   . HOH E 5 .   ? -23.942 8.722   20.303  1.00 27.39 ? 404 HOH A O   1 
HETATM 2168 O  O   . HOH E 5 .   ? -14.181 -16.371 28.960  1.00 31.60 ? 405 HOH A O   1 
HETATM 2169 O  O   . HOH E 5 .   ? -17.606 5.728   38.232  1.00 52.30 ? 406 HOH A O   1 
HETATM 2170 O  O   . HOH E 5 .   ? 11.590  -7.097  22.329  1.00 35.95 ? 407 HOH A O   1 
HETATM 2171 O  O   . HOH E 5 .   ? 2.116   7.949   27.967  1.00 28.75 ? 408 HOH A O   1 
HETATM 2172 O  O   . HOH E 5 .   ? -13.690 -8.896  -5.263  1.00 29.93 ? 409 HOH A O   1 
HETATM 2173 O  O   . HOH E 5 .   ? -8.881  6.164   28.931  1.00 49.69 ? 410 HOH A O   1 
HETATM 2174 O  O   . HOH E 5 .   ? -10.480 13.258  8.382   1.00 33.64 ? 411 HOH A O   1 
HETATM 2175 O  O   . HOH E 5 .   ? 4.706   -2.564  28.969  1.00 30.51 ? 412 HOH A O   1 
HETATM 2176 O  O   . HOH E 5 .   ? 15.965  3.601   15.477  1.00 32.01 ? 413 HOH A O   1 
HETATM 2177 O  O   . HOH E 5 .   ? -19.956 8.515   30.163  1.00 34.16 ? 414 HOH A O   1 
HETATM 2178 O  O   . HOH E 5 .   ? -12.950 -22.297 11.873  1.00 34.83 ? 415 HOH A O   1 
HETATM 2179 O  O   . HOH E 5 .   ? -24.545 4.779   8.715   1.00 51.69 ? 416 HOH A O   1 
HETATM 2180 O  O   . HOH E 5 .   ? -12.477 13.056  31.743  1.00 34.69 ? 417 HOH A O   1 
HETATM 2181 O  O   . HOH E 5 .   ? -0.975  -4.146  15.756  1.00 11.91 ? 418 HOH A O   1 
HETATM 2182 O  O   . HOH E 5 .   ? 10.914  -9.265  9.282   1.00 38.70 ? 419 HOH A O   1 
HETATM 2183 O  O   . HOH E 5 .   ? -19.131 -20.617 4.956   1.00 26.36 ? 420 HOH A O   1 
HETATM 2184 O  O   . HOH E 5 .   ? -18.959 10.041  8.822   1.00 19.04 ? 421 HOH A O   1 
HETATM 2185 O  O   . HOH E 5 .   ? -10.209 -18.202 17.064  1.00 20.78 ? 422 HOH A O   1 
HETATM 2186 O  O   . HOH E 5 .   ? 1.681   10.940  17.048  1.00 42.30 ? 423 HOH A O   1 
HETATM 2187 O  O   . HOH E 5 .   ? -19.872 -16.609 3.052   1.00 28.16 ? 424 HOH A O   1 
HETATM 2188 O  O   . HOH E 5 .   ? -3.347  5.503   -2.648  1.00 35.64 ? 425 HOH A O   1 
HETATM 2189 O  O   . HOH E 5 .   ? -13.879 -5.221  -6.658  1.00 34.05 ? 426 HOH A O   1 
HETATM 2190 O  O   . HOH E 5 .   ? -12.008 12.586  29.026  1.00 30.49 ? 427 HOH A O   1 
HETATM 2191 O  O   . HOH E 5 .   ? -23.794 -3.085  29.278  1.00 37.86 ? 428 HOH A O   1 
HETATM 2192 O  O   . HOH E 5 .   ? -16.356 -14.917 32.893  1.00 39.73 ? 429 HOH A O   1 
HETATM 2193 O  O   . HOH E 5 .   ? -25.620 -6.107  13.025  1.00 34.70 ? 430 HOH A O   1 
HETATM 2194 O  O   . HOH E 5 .   ? -5.803  -4.584  -6.337  1.00 36.13 ? 431 HOH A O   1 
HETATM 2195 O  O   . HOH E 5 .   ? 4.542   -3.472  26.460  1.00 25.50 ? 432 HOH A O   1 
HETATM 2196 O  O   . HOH E 5 .   ? -10.165 8.652   25.429  1.00 14.58 ? 433 HOH A O   1 
HETATM 2197 O  O   . HOH E 5 .   ? 3.833   4.944   29.878  1.00 25.65 ? 434 HOH A O   1 
HETATM 2198 O  O   . HOH E 5 .   ? -12.472 -22.108 8.286   1.00 31.90 ? 435 HOH A O   1 
HETATM 2199 O  O   . HOH E 5 .   ? 13.580  0.335   24.446  1.00 26.07 ? 436 HOH A O   1 
HETATM 2200 O  O   . HOH E 5 .   ? -4.573  -11.909 32.033  1.00 24.48 ? 437 HOH A O   1 
HETATM 2201 O  O   . HOH E 5 .   ? 0.701   -1.338  -4.625  1.00 30.66 ? 438 HOH A O   1 
HETATM 2202 O  O   . HOH E 5 .   ? -19.923 10.850  26.768  1.00 24.78 ? 439 HOH A O   1 
HETATM 2203 O  O   . HOH E 5 .   ? -22.681 -5.870  2.647   1.00 24.72 ? 440 HOH A O   1 
HETATM 2204 O  O   . HOH E 5 .   ? -6.724  -14.897 31.496  1.00 26.66 ? 441 HOH A O   1 
HETATM 2205 O  O   . HOH E 5 .   ? -13.486 14.232  27.244  1.00 30.04 ? 442 HOH A O   1 
HETATM 2206 O  O   . HOH E 5 .   ? 12.044  -0.392  15.958  1.00 32.53 ? 443 HOH A O   1 
HETATM 2207 O  O   . HOH E 5 .   ? -8.300  -15.413 36.442  1.00 32.82 ? 444 HOH A O   1 
HETATM 2208 O  O   . HOH E 5 .   ? -4.331  -13.443 18.000  1.00 10.75 ? 445 HOH A O   1 
HETATM 2209 O  O   . HOH E 5 .   ? -21.859 -18.324 13.561  1.00 26.87 ? 446 HOH A O   1 
HETATM 2210 O  O   . HOH E 5 .   ? -18.422 -20.977 14.705  1.00 30.79 ? 447 HOH A O   1 
HETATM 2211 O  O   . HOH E 5 .   ? -21.660 -13.988 18.580  1.00 38.61 ? 448 HOH A O   1 
HETATM 2212 O  O   . HOH E 5 .   ? 10.633  -10.801 16.182  1.00 31.16 ? 449 HOH A O   1 
HETATM 2213 O  O   . HOH E 5 .   ? -3.284  -11.129 20.841  1.00 12.82 ? 450 HOH A O   1 
HETATM 2214 O  O   . HOH E 5 .   ? 2.150   -15.611 9.402   1.00 24.76 ? 451 HOH A O   1 
HETATM 2215 O  O   . HOH E 5 .   ? -7.765  -15.477 11.340  1.00 12.63 ? 452 HOH A O   1 
HETATM 2216 O  O   . HOH E 5 .   ? -14.213 -21.183 3.034   1.00 37.96 ? 453 HOH A O   1 
HETATM 2217 O  O   . HOH E 5 .   ? 8.814   -3.791  21.093  1.00 17.51 ? 454 HOH A O   1 
HETATM 2218 O  O   . HOH E 5 .   ? 5.479   7.128   20.398  1.00 25.43 ? 455 HOH A O   1 
HETATM 2219 O  O   . HOH E 5 .   ? 0.218   1.032   34.454  1.00 31.62 ? 456 HOH A O   1 
HETATM 2220 O  O   . HOH E 5 .   ? -15.121 -21.725 13.124  1.00 22.29 ? 457 HOH A O   1 
HETATM 2221 O  O   . HOH E 5 .   ? 4.050   -3.500  4.766   1.00 41.06 ? 458 HOH A O   1 
HETATM 2222 O  O   . HOH E 5 .   ? -1.815  -4.804  -6.935  1.00 49.60 ? 459 HOH A O   1 
HETATM 2223 O  O   . HOH E 5 .   ? -2.303  -8.700  29.088  1.00 14.49 ? 460 HOH A O   1 
HETATM 2224 O  O   . HOH E 5 .   ? -13.401 10.442  27.825  1.00 20.40 ? 461 HOH A O   1 
HETATM 2225 O  O   . HOH E 5 .   ? -26.234 3.207   20.953  1.00 35.90 ? 462 HOH A O   1 
HETATM 2226 O  O   . HOH E 5 .   ? -5.306  2.306   11.716  1.00 31.86 ? 463 HOH A O   1 
HETATM 2227 O  O   . HOH E 5 .   ? -3.618  -15.859 24.379  1.00 15.91 ? 464 HOH A O   1 
HETATM 2228 O  O   . HOH E 5 .   ? -23.057 -11.216 17.114  1.00 29.46 ? 465 HOH A O   1 
HETATM 2229 O  O   . HOH E 5 .   ? -17.848 10.667  11.327  1.00 19.49 ? 466 HOH A O   1 
HETATM 2230 O  O   . HOH E 5 .   ? -13.494 19.861  15.017  1.00 24.37 ? 467 HOH A O   1 
HETATM 2231 O  O   . HOH E 5 .   ? -25.617 6.289   26.918  1.00 29.45 ? 468 HOH A O   1 
HETATM 2232 O  O   . HOH E 5 .   ? -18.438 -3.943  -2.709  1.00 31.13 ? 469 HOH A O   1 
HETATM 2233 O  O   . HOH E 5 .   ? -6.468  20.696  19.382  1.00 17.83 ? 470 HOH A O   1 
HETATM 2234 O  O   . HOH E 5 .   ? -2.208  -3.404  11.485  1.00 19.22 ? 471 HOH A O   1 
HETATM 2235 O  O   . HOH E 5 .   ? -20.889 -6.583  -2.382  1.00 50.06 ? 472 HOH A O   1 
HETATM 2236 O  O   . HOH E 5 .   ? -7.122  -16.696 1.335   1.00 26.88 ? 473 HOH A O   1 
HETATM 2237 O  O   . HOH E 5 .   ? -21.315 -6.994  23.445  1.00 15.75 ? 474 HOH A O   1 
HETATM 2238 O  O   . HOH E 5 .   ? 1.489   -11.768 25.030  1.00 24.35 ? 475 HOH A O   1 
HETATM 2239 O  O   . HOH E 5 .   ? -18.856 -12.211 -3.409  1.00 29.57 ? 476 HOH A O   1 
HETATM 2240 O  O   . HOH E 5 .   ? -0.837  9.219   27.864  1.00 30.86 ? 477 HOH A O   1 
HETATM 2241 O  O   . HOH E 5 .   ? -4.069  -8.650  31.205  1.00 23.86 ? 478 HOH A O   1 
HETATM 2242 O  O   . HOH E 5 .   ? -5.515  17.328  27.163  1.00 38.52 ? 479 HOH A O   1 
HETATM 2243 O  O   . HOH E 5 .   ? -25.456 -15.169 7.879   1.00 39.64 ? 480 HOH A O   1 
HETATM 2244 O  O   . HOH E 5 .   ? -3.209  -13.230 25.185  1.00 13.88 ? 481 HOH A O   1 
HETATM 2245 O  O   . HOH E 5 .   ? -15.771 15.952  23.731  1.00 23.87 ? 482 HOH A O   1 
HETATM 2246 O  O   . HOH E 5 .   ? -17.682 -20.402 7.909   1.00 15.43 ? 483 HOH A O   1 
HETATM 2247 O  O   . HOH E 5 .   ? -16.743 -8.331  20.306  1.00 10.03 ? 484 HOH A O   1 
HETATM 2248 O  O   . HOH E 5 .   ? -3.771  -4.647  37.562  1.00 34.47 ? 485 HOH A O   1 
HETATM 2249 O  O   . HOH E 5 .   ? -17.203 -16.181 21.946  1.00 29.92 ? 486 HOH A O   1 
HETATM 2250 O  O   . HOH E 5 .   ? 1.583   -6.382  34.326  1.00 36.82 ? 487 HOH A O   1 
HETATM 2251 O  O   . HOH E 5 .   ? -3.543  -12.872 -2.980  1.00 30.62 ? 488 HOH A O   1 
HETATM 2252 O  O   . HOH E 5 .   ? -19.731 -16.488 20.791  1.00 63.58 ? 489 HOH A O   1 
HETATM 2253 O  O   . HOH E 5 .   ? -20.746 7.868   1.770   1.00 19.98 ? 490 HOH A O   1 
HETATM 2254 O  O   . HOH E 5 .   ? 9.560   7.563   18.681  1.00 52.34 ? 491 HOH A O   1 
HETATM 2255 O  O   . HOH E 5 .   ? 2.996   -4.469  7.917   1.00 25.63 ? 492 HOH A O   1 
HETATM 2256 O  O   . HOH E 5 .   ? -15.879 -12.320 24.333  1.00 19.28 ? 493 HOH A O   1 
HETATM 2257 O  O   . HOH E 5 .   ? -14.374 -18.515 18.688  1.00 25.28 ? 494 HOH A O   1 
HETATM 2258 O  O   . HOH E 5 .   ? 5.148   -4.883  20.980  1.00 17.60 ? 495 HOH A O   1 
HETATM 2259 O  O   . HOH E 5 .   ? -14.623 20.012  17.516  1.00 29.00 ? 496 HOH A O   1 
HETATM 2260 O  O   . HOH E 5 .   ? -19.532 -4.331  41.202  1.00 36.23 ? 497 HOH A O   1 
HETATM 2261 O  O   . HOH E 5 .   ? -22.945 -2.864  6.526   1.00 23.18 ? 498 HOH A O   1 
HETATM 2262 O  O   . HOH E 5 .   ? -23.678 -0.737  26.454  1.00 23.42 ? 499 HOH A O   1 
HETATM 2263 O  O   . HOH E 5 .   ? -21.474 5.772   4.652   1.00 20.33 ? 500 HOH A O   1 
HETATM 2264 O  O   . HOH E 5 .   ? 11.441  1.502   26.064  1.00 27.52 ? 501 HOH A O   1 
HETATM 2265 O  O   . HOH E 5 .   ? -6.617  -8.511  -7.086  1.00 42.08 ? 502 HOH A O   1 
HETATM 2266 O  O   . HOH E 5 .   ? -26.045 -7.213  30.277  1.00 42.96 ? 503 HOH A O   1 
HETATM 2267 O  O   . HOH E 5 .   ? -11.672 2.948   30.536  1.00 22.93 ? 504 HOH A O   1 
HETATM 2268 O  O   . HOH E 5 .   ? -12.837 -16.771 26.530  1.00 20.26 ? 505 HOH A O   1 
HETATM 2269 O  O   . HOH E 5 .   ? -12.602 -8.981  -3.213  1.00 27.02 ? 506 HOH A O   1 
HETATM 2270 O  O   . HOH E 5 .   ? -7.187  -8.696  32.562  1.00 21.12 ? 507 HOH A O   1 
HETATM 2271 O  O   . HOH E 5 .   ? -24.987 9.783   13.210  1.00 35.03 ? 508 HOH A O   1 
HETATM 2272 O  O   . HOH E 5 .   ? -24.627 -7.589  9.039   1.00 21.51 ? 509 HOH A O   1 
HETATM 2273 O  O   . HOH E 5 .   ? 5.440   -7.179  22.410  1.00 39.53 ? 510 HOH A O   1 
HETATM 2274 O  O   . HOH E 5 .   ? -13.142 -18.462 14.657  1.00 21.37 ? 511 HOH A O   1 
HETATM 2275 O  O   . HOH E 5 .   ? -23.081 -13.237 11.295  1.00 24.84 ? 512 HOH A O   1 
HETATM 2276 O  O   . HOH E 5 .   ? -7.596  6.878   0.281   1.00 32.98 ? 513 HOH A O   1 
HETATM 2277 O  O   . HOH E 5 .   ? -16.136 -9.834  32.869  1.00 21.17 ? 514 HOH A O   1 
HETATM 2278 O  O   . HOH E 5 .   ? -8.393  0.617   -6.471  1.00 40.58 ? 515 HOH A O   1 
HETATM 2279 O  O   . HOH E 5 .   ? -3.529  -0.980  11.373  1.00 40.14 ? 516 HOH A O   1 
HETATM 2280 O  O   . HOH E 5 .   ? -1.166  -17.716 18.040  1.00 35.08 ? 517 HOH A O   1 
HETATM 2281 O  O   . HOH E 5 .   ? 1.951   2.243   35.896  1.00 35.95 ? 518 HOH A O   1 
HETATM 2282 O  O   . HOH E 5 .   ? 8.362   -9.311  16.579  1.00 25.63 ? 519 HOH A O   1 
HETATM 2283 O  O   . HOH E 5 .   ? -6.415  14.466  29.005  1.00 35.09 ? 520 HOH A O   1 
HETATM 2284 O  O   . HOH E 5 .   ? -15.442 9.004   -2.192  1.00 31.05 ? 521 HOH A O   1 
HETATM 2285 O  O   . HOH E 5 .   ? 8.218   -8.239  -0.022  1.00 34.25 ? 522 HOH A O   1 
HETATM 2286 O  O   . HOH E 5 .   ? -11.179 10.084  8.123   1.00 24.67 ? 523 HOH A O   1 
HETATM 2287 O  O   . HOH E 5 .   ? 3.594   9.969   18.336  1.00 42.86 ? 524 HOH A O   1 
HETATM 2288 O  O   . HOH E 5 .   ? -10.611 1.153   33.536  1.00 43.24 ? 525 HOH A O   1 
HETATM 2289 O  O   . HOH E 5 .   ? -8.912  10.463  6.980   1.00 54.26 ? 526 HOH A O   1 
HETATM 2290 O  O   . HOH E 5 .   ? -19.981 13.735  28.988  1.00 40.91 ? 527 HOH A O   1 
HETATM 2291 O  O   . HOH E 5 .   ? -13.028 -0.680  -5.916  1.00 35.12 ? 528 HOH A O   1 
HETATM 2292 O  O   . HOH E 5 .   ? -24.483 11.939  6.195   1.00 28.71 ? 529 HOH A O   1 
HETATM 2293 O  O   . HOH E 5 .   ? -4.449  -15.975 0.767   1.00 31.65 ? 530 HOH A O   1 
HETATM 2294 O  O   . HOH E 5 .   ? 4.677   -6.819  7.960   1.00 31.20 ? 531 HOH A O   1 
HETATM 2295 O  O   . HOH E 5 .   ? 1.495   -1.597  29.405  1.00 16.79 ? 532 HOH A O   1 
HETATM 2296 O  O   . HOH E 5 .   ? 2.842   -11.526 9.530   1.00 28.80 ? 533 HOH A O   1 
HETATM 2297 O  O   . HOH E 5 .   ? -0.365  -8.470  32.584  1.00 28.39 ? 534 HOH A O   1 
HETATM 2298 O  O   . HOH E 5 .   ? -23.454 -0.786  3.877   1.00 28.15 ? 535 HOH A O   1 
HETATM 2299 O  O   . HOH E 5 .   ? -26.467 -3.853  25.186  1.00 25.31 ? 536 HOH A O   1 
HETATM 2300 O  O   . HOH E 5 .   ? -26.382 -2.284  14.458  1.00 24.04 ? 537 HOH A O   1 
HETATM 2301 O  O   . HOH E 5 .   ? 1.832   8.600   24.081  1.00 29.61 ? 538 HOH A O   1 
HETATM 2302 O  O   . HOH E 5 .   ? -16.793 -7.153  39.714  1.00 34.29 ? 539 HOH A O   1 
HETATM 2303 O  O   . HOH E 5 .   ? -16.886 -14.056 37.233  1.00 32.91 ? 540 HOH A O   1 
HETATM 2304 O  O   . HOH E 5 .   ? -1.848  -12.301 22.824  1.00 11.98 ? 541 HOH A O   1 
HETATM 2305 O  O   . HOH E 5 .   ? -22.921 -0.719  34.177  1.00 38.64 ? 542 HOH A O   1 
HETATM 2306 O  O   . HOH E 5 .   ? 3.772   -12.748 12.097  1.00 48.05 ? 543 HOH A O   1 
HETATM 2307 O  O   . HOH E 5 .   ? -13.445 -16.077 -0.460  1.00 44.73 ? 544 HOH A O   1 
HETATM 2308 O  O   . HOH E 5 .   ? -22.695 -11.667 13.967  1.00 24.23 ? 545 HOH A O   1 
HETATM 2309 O  O   . HOH E 5 .   ? -5.933  -19.691 23.828  1.00 31.62 ? 546 HOH A O   1 
HETATM 2310 O  O   . HOH E 5 .   ? 4.356   4.594   10.822  1.00 40.29 ? 547 HOH A O   1 
HETATM 2311 O  O   . HOH E 5 .   ? -11.028 -19.166 6.656   1.00 46.98 ? 548 HOH A O   1 
HETATM 2312 O  O   . HOH E 5 .   ? -4.708  3.167   -5.854  1.00 33.45 ? 549 HOH A O   1 
HETATM 2313 O  O   . HOH E 5 .   ? -8.899  -5.864  35.897  1.00 24.64 ? 550 HOH A O   1 
HETATM 2314 O  O   . HOH E 5 .   ? 14.094  5.796   19.182  1.00 43.18 ? 551 HOH A O   1 
HETATM 2315 O  O   . HOH E 5 .   ? -18.367 -9.002  34.506  1.00 33.42 ? 552 HOH A O   1 
HETATM 2316 O  O   . HOH E 5 .   ? -12.473 7.908   28.878  1.00 27.03 ? 553 HOH A O   1 
HETATM 2317 O  O   . HOH E 5 .   ? -27.562 2.331   23.366  1.00 49.23 ? 554 HOH A O   1 
HETATM 2318 O  O   . HOH E 5 .   ? 8.464   3.348   27.853  1.00 41.81 ? 555 HOH A O   1 
HETATM 2319 O  O   . HOH E 5 .   ? -0.422  10.495  23.193  1.00 27.21 ? 556 HOH A O   1 
HETATM 2320 O  O   . HOH E 5 .   ? 0.006   -14.286 22.216  1.00 27.63 ? 557 HOH A O   1 
HETATM 2321 O  O   . HOH E 5 .   ? -20.966 -19.489 6.513   1.00 27.02 ? 558 HOH A O   1 
HETATM 2322 O  O   . HOH E 5 .   ? -19.592 -13.454 24.355  1.00 41.15 ? 559 HOH A O   1 
HETATM 2323 O  O   . HOH E 5 .   ? -6.573  6.872   10.832  1.00 36.08 ? 560 HOH A O   1 
HETATM 2324 O  O   . HOH E 5 .   ? -16.543 18.865  22.453  1.00 47.93 ? 561 HOH A O   1 
HETATM 2325 O  O   . HOH E 5 .   ? -7.316  -8.748  -2.387  1.00 30.99 ? 562 HOH A O   1 
HETATM 2326 O  O   . HOH E 5 .   ? -9.309  -7.901  34.017  1.00 28.86 ? 563 HOH A O   1 
HETATM 2327 O  O   . HOH E 5 .   ? -7.847  -19.335 21.601  1.00 22.78 ? 564 HOH A O   1 
HETATM 2328 O  O   . HOH E 5 .   ? -8.998  -9.996  -1.383  1.00 31.22 ? 565 HOH A O   1 
HETATM 2329 O  O   . HOH E 5 .   ? 7.530   3.389   34.959  1.00 50.15 ? 566 HOH A O   1 
HETATM 2330 O  O   . HOH E 5 .   ? 7.757   6.173   21.707  1.00 20.57 ? 567 HOH A O   1 
HETATM 2331 O  O   . HOH E 5 .   ? -5.027  6.798   5.840   1.00 48.74 ? 568 HOH A O   1 
HETATM 2332 O  O   . HOH E 5 .   ? 10.375  -2.494  13.834  1.00 28.56 ? 569 HOH A O   1 
HETATM 2333 O  O   . HOH E 5 .   ? -17.797 4.356   -3.959  1.00 37.83 ? 570 HOH A O   1 
HETATM 2334 O  O   . HOH E 5 .   ? -6.767  1.559   35.626  1.00 41.20 ? 571 HOH A O   1 
HETATM 2335 O  O   . HOH E 5 .   ? 15.085  -10.440 14.643  1.00 44.80 ? 572 HOH A O   1 
HETATM 2336 O  O   . HOH E 5 .   ? 8.472   -5.892  -0.018  1.00 47.72 ? 573 HOH A O   1 
HETATM 2337 O  O   . HOH E 5 .   ? -23.833 -17.917 6.267   1.00 41.04 ? 574 HOH A O   1 
HETATM 2338 O  O   . HOH E 5 .   ? 6.624   -10.907 14.792  1.00 43.89 ? 575 HOH A O   1 
HETATM 2339 O  O   . HOH E 5 .   ? 8.865   -4.650  23.737  1.00 31.78 ? 576 HOH A O   1 
HETATM 2340 O  O   . HOH E 5 .   ? 11.218  -6.622  7.181   1.00 49.92 ? 577 HOH A O   1 
HETATM 2341 O  O   . HOH E 5 .   ? -0.279  -21.196 15.226  1.00 73.87 ? 578 HOH A O   1 
HETATM 2342 O  O   . HOH E 5 .   ? -11.863 12.744  6.143   1.00 43.73 ? 579 HOH A O   1 
HETATM 2343 O  O   . HOH E 5 .   ? -2.051  -14.509 32.584  1.00 46.35 ? 580 HOH A O   1 
HETATM 2344 O  O   . HOH E 5 .   ? -4.735  0.733   10.019  1.00 36.59 ? 581 HOH A O   1 
HETATM 2345 O  O   . HOH E 5 .   ? -1.283  -13.198 27.173  1.00 28.94 ? 582 HOH A O   1 
HETATM 2346 O  O   . HOH E 5 .   ? -1.162  11.197  25.430  1.00 38.41 ? 583 HOH A O   1 
HETATM 2347 O  O   . HOH E 5 .   ? 13.138  -3.467  13.508  1.00 28.69 ? 584 HOH A O   1 
HETATM 2348 O  O   . HOH E 5 .   ? -12.612 -17.145 16.768  1.00 19.62 ? 585 HOH A O   1 
HETATM 2349 O  O   . HOH E 5 .   ? -17.235 -23.114 4.034   1.00 36.82 ? 586 HOH A O   1 
HETATM 2350 O  O   . HOH E 5 .   ? -25.010 11.148  19.808  1.00 40.61 ? 587 HOH A O   1 
HETATM 2351 O  O   . HOH E 5 .   ? -22.587 -9.576  25.710  1.00 45.50 ? 588 HOH A O   1 
HETATM 2352 O  O   . HOH E 5 .   ? 0.620   -2.486  39.181  1.00 50.79 ? 589 HOH A O   1 
HETATM 2353 O  O   . HOH E 5 .   ? -17.545 19.894  17.489  1.00 28.10 ? 590 HOH A O   1 
HETATM 2354 O  O   . HOH E 5 .   ? -27.594 4.900   25.012  1.00 30.16 ? 591 HOH A O   1 
HETATM 2355 O  O   . HOH E 5 .   ? 4.902   -10.347 8.133   1.00 45.64 ? 592 HOH A O   1 
HETATM 2356 O  O   . HOH E 5 .   ? -26.417 -6.104  5.012   1.00 44.11 ? 593 HOH A O   1 
HETATM 2357 O  O   . HOH E 5 .   ? 0.531   0.523   -6.741  1.00 37.38 ? 594 HOH A O   1 
HETATM 2358 O  O   . HOH E 5 .   ? 4.216   8.705   22.384  1.00 36.57 ? 595 HOH A O   1 
HETATM 2359 O  O   . HOH E 5 .   ? 5.281   -10.824 17.932  1.00 53.92 ? 596 HOH A O   1 
HETATM 2360 O  O   . HOH E 5 .   ? 10.579  5.526   12.823  1.00 53.11 ? 597 HOH A O   1 
HETATM 2361 O  O   . HOH E 5 .   ? -24.828 8.688   26.125  1.00 41.94 ? 598 HOH A O   1 
HETATM 2362 O  O   . HOH E 5 .   ? 3.127   -13.521 8.003   1.00 36.54 ? 599 HOH A O   1 
HETATM 2363 O  O   . HOH E 5 .   ? -1.930  -12.085 31.390  1.00 36.37 ? 600 HOH A O   1 
HETATM 2364 O  O   . HOH E 5 .   ? -1.737  -17.470 25.499  1.00 35.00 ? 601 HOH A O   1 
HETATM 2365 O  O   . HOH E 5 .   ? -2.485  -17.487 5.143   1.00 37.88 ? 602 HOH A O   1 
HETATM 2366 O  O   . HOH E 5 .   ? 6.675   -5.662  27.207  1.00 36.79 ? 603 HOH A O   1 
HETATM 2367 O  O   . HOH E 5 .   ? -15.178 20.696  22.657  1.00 38.19 ? 604 HOH A O   1 
HETATM 2368 O  O   . HOH E 5 .   ? -27.046 -6.711  7.865   1.00 36.64 ? 605 HOH A O   1 
HETATM 2369 O  O   . HOH E 5 .   ? -16.682 -14.003 26.218  1.00 30.26 ? 606 HOH A O   1 
HETATM 2370 O  O   . HOH E 5 .   ? -28.648 -5.798  24.489  1.00 30.05 ? 607 HOH A O   1 
HETATM 2371 O  O   . HOH E 5 .   ? -4.891  -9.637  33.699  1.00 39.16 ? 608 HOH A O   1 
HETATM 2372 O  O   . HOH E 5 .   ? -8.959  2.979   34.824  1.00 37.01 ? 609 HOH A O   1 
HETATM 2373 O  O   . HOH E 5 .   ? -20.923 -20.462 14.300  1.00 75.26 ? 610 HOH A O   1 
HETATM 2374 O  O   . HOH E 5 .   ? 4.208   -11.873 23.499  1.00 43.32 ? 611 HOH A O   1 
HETATM 2375 O  O   . HOH E 5 .   ? 2.190   -14.207 20.686  1.00 35.65 ? 612 HOH A O   1 
HETATM 2376 O  O   . HOH E 5 .   ? -16.638 -17.916 20.347  1.00 37.13 ? 613 HOH A O   1 
HETATM 2377 O  O   . HOH E 5 .   ? -10.696 15.144  32.005  1.00 30.83 ? 614 HOH A O   1 
HETATM 2378 O  O   . HOH E 5 .   ? -17.658 -12.066 31.463  1.00 38.93 ? 615 HOH A O   1 
HETATM 2379 O  O   . HOH E 5 .   ? -10.994 -11.211 -2.961  1.00 40.29 ? 616 HOH A O   1 
HETATM 2380 O  O   . HOH E 5 .   ? -1.004  -11.161 29.020  1.00 23.88 ? 617 HOH A O   1 
HETATM 2381 O  O   . HOH E 5 .   ? -16.295 -14.731 28.592  1.00 41.91 ? 618 HOH A O   1 
HETATM 2382 O  O   . HOH E 5 .   ? -7.471  -10.362 -4.288  1.00 51.91 ? 619 HOH A O   1 
HETATM 2383 O  O   . HOH E 5 .   ? -24.241 13.465  20.404  1.00 41.03 ? 620 HOH A O   1 
HETATM 2384 O  O   . HOH E 5 .   ? -15.898 17.335  26.048  1.00 43.82 ? 621 HOH A O   1 
HETATM 2385 O  O   . HOH E 5 .   ? -26.508 -1.256  25.909  1.00 25.65 ? 622 HOH A O   1 
HETATM 2386 O  O   . HOH E 5 .   ? -3.586  -15.597 -2.216  1.00 37.15 ? 623 HOH A O   1 
HETATM 2387 O  O   . HOH E 5 .   ? -12.687 -19.428 26.107  1.00 30.10 ? 624 HOH A O   1 
HETATM 2388 O  O   . HOH E 5 .   ? -27.215 0.033   15.041  1.00 42.44 ? 625 HOH A O   1 
HETATM 2389 O  O   . HOH E 5 .   ? -2.891  7.265   -5.198  1.00 24.43 ? 626 HOH A O   1 
HETATM 2390 O  O   . HOH E 5 .   ? -2.677  -9.252  34.329  1.00 40.04 ? 627 HOH A O   1 
HETATM 2391 O  O   . HOH E 5 .   ? -9.546  1.413   38.808  1.00 39.97 ? 628 HOH A O   1 
HETATM 2392 O  O   . HOH E 5 .   ? -18.051 13.458  -0.373  1.00 35.66 ? 629 HOH A O   1 
HETATM 2393 O  O   . HOH E 5 .   ? -20.375 -15.693 23.183  1.00 80.84 ? 630 HOH A O   1 
HETATM 2394 O  O   . HOH E 5 .   ? -17.295 11.180  -2.071  1.00 28.61 ? 631 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   ? 0.4767 0.3876 0.9413 -0.0534 0.1897  0.1694  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.6123 0.5413 0.7026 -0.0409 0.1506  0.1018  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.2938 0.5279 0.4344 0.0754  0.1557  0.0757  4   HIS A C   
4    O  O   . HIS A 4   ? 0.3030 0.5052 0.5126 -0.0622 0.0923  0.0353  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.4118 0.5122 0.7205 -0.0647 0.2718  0.1701  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.9060 0.5677 0.7134 -0.0517 0.2990  0.3943  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.5290 0.8903 0.9347 -0.0121 -0.1070 0.3563  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.8580 1.2133 0.9046 0.0044  0.0103  0.3256  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 0.8470 1.0058 1.0496 -0.1231 0.2214  0.1266  4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 1.0124 1.1002 1.1249 -0.0914 0.2203  0.3095  4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.1504 0.4004 0.3336 -0.0565 0.0955  0.0472  5   TRP A N   
12   C  CA  . TRP A 5   ? 0.1981 0.2494 0.3347 -0.0316 0.1170  -0.0009 5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1864 0.2524 0.3157 -0.0006 0.1002  0.0142  5   TRP A C   
14   O  O   . TRP A 5   ? 0.2067 0.2841 0.2951 -0.0352 0.0710  0.0089  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1333 0.2617 0.3686 0.0139  0.0797  -0.0168 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1663 0.2276 0.2496 -0.0305 0.0469  0.0482  5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.2123 0.2261 0.3240 0.0231  0.0388  0.0643  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1390 0.2286 0.2381 -0.0005 0.0574  -0.0380 5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.2071 0.2414 0.2496 0.0108  0.0292  0.0313  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1864 0.2599 0.2245 -0.0049 0.0648  0.0055  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1516 0.2521 0.1857 -0.0335 0.0433  -0.0154 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.1946 0.3076 0.1975 -0.0064 0.0096  0.0167  5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1703 0.2983 0.1661 0.0064  0.0466  -0.0545 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1834 0.2998 0.1566 0.0069  0.0439  -0.0457 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1814 0.1983 0.3033 -0.0111 0.0919  -0.0305 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1852 0.2582 0.3005 -0.0265 0.1062  -0.0306 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1534 0.2651 0.2568 -0.0133 0.0952  -0.0256 6   GLY A C   
28   O  O   . GLY A 6   ? 0.1090 0.2464 0.2560 0.0109  0.0730  -0.0291 6   GLY A O   
29   N  N   . TYR A 7   ? 0.1673 0.2542 0.2979 -0.0305 0.1040  -0.0486 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.1256 0.2203 0.3555 -0.0131 0.1087  -0.0319 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.1637 0.2455 0.4440 0.0254  0.1361  -0.0040 7   TYR A C   
32   O  O   . TYR A 7   ? 0.1956 0.2875 0.5398 0.0008  0.1081  0.0421  7   TYR A O   
33   C  CB  . TYR A 7   ? 0.1343 0.2111 0.3045 -0.0031 0.0935  -0.0420 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1155 0.2132 0.2157 -0.0165 0.0665  -0.0573 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.1153 0.2201 0.1907 -0.0044 0.0491  -0.0298 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.1378 0.2406 0.1983 -0.0294 0.0372  -0.0699 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.0996 0.1557 0.2417 -0.0433 0.0347  -0.0283 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.1279 0.2299 0.1828 -0.0413 0.0670  -0.0324 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.1268 0.1864 0.1662 -0.0340 0.0411  -0.0364 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.1537 0.1794 0.1857 -0.0108 0.0263  -0.0164 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.1541 0.2820 0.4278 0.0153  0.1247  -0.0684 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.1817 0.2743 0.5131 0.0287  0.1696  -0.0499 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.2854 0.2500 0.5386 0.0658  0.1152  0.0308  8   GLY A C   
44   O  O   . GLY A 8   ? 0.1279 0.3671 0.5136 -0.0134 0.1209  -0.0105 8   GLY A O   
45   N  N   . LYS A 9   ? 0.1918 0.2410 0.5725 0.0055  0.1056  -0.0275 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.2259 0.3194 0.6354 0.0332  0.0679  0.0311  9   LYS A CA  
47   C  C   . LYS A 9   ? 0.1691 0.3330 0.3727 0.0692  0.0599  0.0113  9   LYS A C   
48   O  O   . LYS A 9   ? 0.1676 0.2837 0.4358 -0.0484 0.0458  0.0301  9   LYS A O   
49   C  CB  . LYS A 9   ? 0.2710 0.3749 0.6802 0.0666  0.0442  0.0048  9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.2338 0.3967 0.7400 0.0328  0.0576  0.0815  9   LYS A CG  
51   N  N   . HIS A 10  ? 0.2225 0.2264 0.5472 0.0506  0.1601  0.0310  10  HIS A N   
52   C  CA  . HIS A 10  ? 0.2528 0.2202 0.5197 0.0272  0.2166  0.0132  10  HIS A CA  
53   C  C   . HIS A 10  ? 0.1728 0.2407 0.4988 0.0424  0.1894  -0.0252 10  HIS A C   
54   O  O   . HIS A 10  ? 0.1498 0.2680 0.4908 0.0543  0.1247  0.0395  10  HIS A O   
55   C  CB  . HIS A 10  ? 0.2524 0.2449 0.3541 0.0495  0.1439  0.0006  10  HIS A CB  
56   C  CG  . HIS A 10  ? 0.2431 0.2550 0.4240 0.0411  0.1013  0.0710  10  HIS A CG  
57   N  ND1 . HIS A 10  ? 0.3068 0.2924 0.3679 0.0850  0.0512  -0.0516 10  HIS A ND1 
58   C  CD2 . HIS A 10  ? 0.2925 0.2920 0.3580 0.0193  0.1785  0.0182  10  HIS A CD2 
59   C  CE1 . HIS A 10  ? 0.2698 0.2632 0.3950 0.1149  0.0425  -0.0023 10  HIS A CE1 
60   N  NE2 . HIS A 10  ? 0.2000 0.3662 0.4129 0.0588  0.0866  -0.0186 10  HIS A NE2 
61   N  N   . ASN A 11  ? 0.1789 0.2209 0.4718 0.0257  0.1919  0.0002  11  ASN A N   
62   C  CA  . ASN A 11  ? 0.1825 0.2180 0.3039 0.0302  0.1623  -0.0030 11  ASN A CA  
63   C  C   . ASN A 11  ? 0.1638 0.1932 0.3373 0.0082  0.1531  -0.0248 11  ASN A C   
64   O  O   . ASN A 11  ? 0.1123 0.2381 0.3141 0.0284  0.1018  0.0244  11  ASN A O   
65   C  CB  . ASN A 11  ? 0.1857 0.2876 0.2634 0.0119  0.1301  -0.0122 11  ASN A CB  
66   C  CG  . ASN A 11  ? 0.2014 0.3040 0.2647 -0.0081 0.1424  -0.0532 11  ASN A CG  
67   O  OD1 . ASN A 11  ? 0.2370 0.2922 0.3993 -0.0187 0.1220  -0.0087 11  ASN A OD1 
68   N  ND2 . ASN A 11  ? 0.3280 0.3630 0.3244 -0.0345 0.1626  0.0008  11  ASN A ND2 
69   N  N   . GLY A 12  ? 0.1127 0.2355 0.3567 -0.0063 0.1124  0.0178  12  GLY A N   
70   C  CA  . GLY A 12  ? 0.1297 0.2646 0.2541 0.0243  0.1147  -0.0031 12  GLY A CA  
71   C  C   . GLY A 12  ? 0.0969 0.1932 0.2763 0.0229  0.0785  0.0133  12  GLY A C   
72   O  O   . GLY A 12  ? 0.1146 0.1938 0.3210 0.0144  0.0763  0.0254  12  GLY A O   
73   N  N   . PRO A 13  ? 0.1051 0.2019 0.2458 0.0106  0.0767  -0.0013 13  PRO A N   
74   C  CA  . PRO A 13  ? 0.1100 0.1820 0.2466 -0.0136 0.0573  -0.0093 13  PRO A CA  
75   C  C   . PRO A 13  ? 0.1139 0.1882 0.2635 0.0086  0.0587  0.0104  13  PRO A C   
76   O  O   . PRO A 13  ? 0.0891 0.2233 0.3332 -0.0010 0.0559  -0.0392 13  PRO A O   
77   C  CB  . PRO A 13  ? 0.1430 0.1990 0.2645 -0.0444 0.0812  -0.0206 13  PRO A CB  
78   C  CG  . PRO A 13  ? 0.1363 0.1889 0.2434 0.0012  0.0807  -0.0306 13  PRO A CG  
79   C  CD  . PRO A 13  ? 0.1116 0.2256 0.2480 -0.0012 0.0702  -0.0165 13  PRO A CD  
80   N  N   . GLU A 14  ? 0.1092 0.1859 0.2820 0.0209  0.0615  0.0337  14  GLU A N   
81   C  CA  . GLU A 14  ? 0.1392 0.1893 0.3426 0.0062  0.0231  0.0664  14  GLU A CA  
82   C  C   . GLU A 14  ? 0.1072 0.1918 0.2820 0.0226  0.0570  0.0234  14  GLU A C   
83   O  O   . GLU A 14  ? 0.1155 0.2446 0.3234 0.0212  0.0308  0.0268  14  GLU A O   
84   C  CB  . GLU A 14  ? 0.1917 0.1961 0.4617 0.0243  -0.0280 0.1141  14  GLU A CB  
85   C  CG  . GLU A 14  ? 0.3359 0.2533 0.5052 -0.0577 0.0188  0.0840  14  GLU A CG  
86   C  CD  . GLU A 14  ? 0.5497 0.5519 0.4285 0.0295  0.0067  0.0957  14  GLU A CD  
87   O  OE1 . GLU A 14  ? 0.5928 0.8110 0.6302 -0.0390 -0.2235 0.1097  14  GLU A OE1 
88   O  OE2 . GLU A 14  ? 0.6373 0.4156 0.5826 0.1766  0.1026  -0.0117 14  GLU A OE2 
89   N  N   . HIS A 15  ? 0.1029 0.1861 0.2946 0.0085  0.0403  0.0331  15  HIS A N   
90   C  CA  . HIS A 15  ? 0.0898 0.1742 0.3384 0.0120  0.0627  0.0059  15  HIS A CA  
91   C  C   . HIS A 15  ? 0.0584 0.1748 0.3554 0.0152  0.0334  0.0381  15  HIS A C   
92   O  O   . HIS A 15  ? 0.0435 0.1982 0.3749 0.0043  0.0361  0.0436  15  HIS A O   
93   C  CB  . HIS A 15  ? 0.0947 0.2223 0.3588 0.0340  0.0876  0.0414  15  HIS A CB  
94   C  CG  . HIS A 15  ? 0.1268 0.2209 0.3534 0.0538  0.0803  0.0416  15  HIS A CG  
95   N  ND1 . HIS A 15  ? 0.1347 0.2365 0.4282 0.0623  0.0787  0.0323  15  HIS A ND1 
96   C  CD2 . HIS A 15  ? 0.2126 0.2412 0.4005 0.0846  0.1111  0.0103  15  HIS A CD2 
97   C  CE1 . HIS A 15  ? 0.2366 0.2967 0.4594 0.1615  0.0031  0.0042  15  HIS A CE1 
98   N  NE2 . HIS A 15  ? 0.2202 0.2859 0.4032 0.1227  0.0366  0.0095  15  HIS A NE2 
99   N  N   . TRP A 16  ? 0.0624 0.1737 0.3240 0.0256  0.0421  0.0421  16  TRP A N   
100  C  CA  . TRP A 16  ? 0.0252 0.1731 0.3362 0.0153  0.0178  0.0060  16  TRP A CA  
101  C  C   . TRP A 16  ? 0.0371 0.1800 0.2945 0.0057  0.0243  0.0088  16  TRP A C   
102  O  O   . TRP A 16  ? 0.0713 0.1655 0.3333 -0.0027 0.0071  0.0073  16  TRP A O   
103  C  CB  . TRP A 16  ? 0.0283 0.1970 0.2913 -0.0022 0.0294  -0.0032 16  TRP A CB  
104  C  CG  . TRP A 16  ? 0.0573 0.1641 0.2471 0.0020  0.0347  0.0176  16  TRP A CG  
105  C  CD1 . TRP A 16  ? 0.1112 0.1774 0.2637 0.0002  0.0476  -0.0055 16  TRP A CD1 
106  C  CD2 . TRP A 16  ? 0.0571 0.1390 0.2370 0.0003  0.0447  0.0000  16  TRP A CD2 
107  N  NE1 . TRP A 16  ? 0.0875 0.1953 0.2142 0.0269  0.0526  -0.0318 16  TRP A NE1 
108  C  CE2 . TRP A 16  ? 0.0823 0.1780 0.2183 0.0136  0.0528  0.0017  16  TRP A CE2 
109  C  CE3 . TRP A 16  ? 0.0502 0.1483 0.2540 0.0093  0.0450  0.0034  16  TRP A CE3 
110  C  CZ2 . TRP A 16  ? 0.1012 0.1759 0.2112 -0.0111 0.0544  0.0085  16  TRP A CZ2 
111  C  CZ3 . TRP A 16  ? 0.0641 0.1893 0.2165 0.0128  0.0315  -0.0273 16  TRP A CZ3 
112  C  CH2 . TRP A 16  ? 0.1256 0.1710 0.1881 -0.0033 0.0557  -0.0227 16  TRP A CH2 
113  N  N   . HIS A 17  ? 0.0627 0.1971 0.2972 -0.0065 0.0109  0.0223  17  HIS A N   
114  C  CA  . HIS A 17  ? 0.0729 0.2298 0.3119 -0.0278 0.0110  0.0274  17  HIS A CA  
115  C  C   . HIS A 17  ? 0.0751 0.2284 0.3330 -0.0147 0.0288  0.0352  17  HIS A C   
116  O  O   . HIS A 17  ? 0.0877 0.2182 0.3903 -0.0027 -0.0122 0.0069  17  HIS A O   
117  C  CB  . HIS A 17  ? 0.0947 0.2057 0.3123 0.0196  0.0036  0.0325  17  HIS A CB  
118  C  CG  . HIS A 17  ? 0.0945 0.1812 0.4118 0.0044  -0.0225 0.0354  17  HIS A CG  
119  N  ND1 . HIS A 17  ? 0.0814 0.2634 0.4133 0.0146  -0.0124 0.0486  17  HIS A ND1 
120  C  CD2 . HIS A 17  ? 0.0866 0.2451 0.3331 0.0267  0.0060  0.0170  17  HIS A CD2 
121  C  CE1 . HIS A 17  ? 0.1200 0.2685 0.4020 0.0280  -0.0074 0.0147  17  HIS A CE1 
122  N  NE2 . HIS A 17  ? 0.0927 0.2658 0.3507 0.0226  -0.0042 0.0691  17  HIS A NE2 
123  N  N   . LYS A 18  ? 0.0384 0.2337 0.3756 -0.0132 0.0317  0.0653  18  LYS A N   
124  C  CA  . LYS A 18  ? 0.0551 0.2569 0.4126 -0.0203 0.0660  0.0803  18  LYS A CA  
125  C  C   . LYS A 18  ? 0.1045 0.2632 0.4318 -0.0501 -0.0308 0.0853  18  LYS A C   
126  O  O   . LYS A 18  ? 0.0674 0.2955 0.6613 -0.1159 -0.0605 0.1379  18  LYS A O   
127  C  CB  . LYS A 18  ? 0.0568 0.2508 0.4385 0.0255  0.0159  0.0639  18  LYS A CB  
128  C  CG  . LYS A 18  ? 0.0871 0.2773 0.4776 0.0870  0.0623  0.0847  18  LYS A CG  
129  C  CD  . LYS A 18  ? 0.0945 0.2611 0.4203 0.0713  0.0190  0.0837  18  LYS A CD  
130  C  CE  . LYS A 18  ? 0.1467 0.2488 0.3834 0.0220  0.0734  0.0710  18  LYS A CE  
131  N  NZ  . LYS A 18  ? 0.1042 0.2682 0.3689 0.0381  0.0596  0.1229  18  LYS A NZ  
132  N  N   . ASP A 19  ? 0.0696 0.2748 0.3979 -0.0095 -0.0010 0.0810  19  ASP A N   
133  C  CA  . ASP A 19  ? 0.1173 0.2508 0.4101 -0.0087 0.0100  0.0595  19  ASP A CA  
134  C  C   . ASP A 19  ? 0.1057 0.1936 0.4758 -0.0384 0.0204  0.0414  19  ASP A C   
135  O  O   . ASP A 19  ? 0.1254 0.1985 0.5282 -0.0199 0.0453  0.0788  19  ASP A O   
136  C  CB  . ASP A 19  ? 0.1213 0.3674 0.4034 -0.0044 0.0099  0.0627  19  ASP A CB  
137  C  CG  . ASP A 19  ? 0.2040 0.4113 0.5189 -0.0528 0.1024  -0.0561 19  ASP A CG  
138  O  OD1 . ASP A 19  ? 0.1902 0.3859 0.6006 -0.0391 0.0552  0.0343  19  ASP A OD1 
139  O  OD2 . ASP A 19  ? 0.6173 0.7217 0.6254 -0.1366 0.2222  -0.2710 19  ASP A OD2 
140  N  N   . PHE A 20  ? 0.0575 0.1921 0.3900 -0.0116 -0.0048 0.0489  20  PHE A N   
141  C  CA  . PHE A 20  ? 0.0645 0.2308 0.3656 -0.0149 -0.0020 0.0140  20  PHE A CA  
142  C  C   . PHE A 20  ? 0.0796 0.1990 0.3665 -0.0160 -0.0113 0.0226  20  PHE A C   
143  O  O   . PHE A 20  ? 0.0929 0.1796 0.3314 0.0055  0.0089  0.0308  20  PHE A O   
144  C  CB  . PHE A 20  ? 0.0560 0.3003 0.3425 -0.0435 -0.0077 0.0635  20  PHE A CB  
145  C  CG  . PHE A 20  ? 0.0234 0.3195 0.3461 -0.0374 0.0118  0.0677  20  PHE A CG  
146  C  CD1 . PHE A 20  ? 0.0970 0.3278 0.3950 -0.0292 -0.0153 0.1030  20  PHE A CD1 
147  C  CD2 . PHE A 20  ? 0.0907 0.3398 0.2870 -0.0663 0.0114  0.0741  20  PHE A CD2 
148  C  CE1 . PHE A 20  ? 0.0845 0.3583 0.3116 -0.0281 -0.0196 0.0258  20  PHE A CE1 
149  C  CE2 . PHE A 20  ? 0.1060 0.3471 0.3199 -0.0240 0.0464  0.0904  20  PHE A CE2 
150  C  CZ  . PHE A 20  ? 0.1172 0.3459 0.3524 -0.0370 0.0324  0.1015  20  PHE A CZ  
151  N  N   . PRO A 21  ? 0.1044 0.2094 0.3446 -0.0239 -0.0124 0.0110  21  PRO A N   
152  C  CA  . PRO A 21  ? 0.1045 0.2554 0.3361 -0.0259 -0.0250 0.0270  21  PRO A CA  
153  C  C   . PRO A 21  ? 0.0584 0.2158 0.3984 -0.0179 -0.0411 -0.0171 21  PRO A C   
154  O  O   . PRO A 21  ? 0.0924 0.2299 0.3897 -0.0110 -0.0700 0.0016  21  PRO A O   
155  C  CB  . PRO A 21  ? 0.1454 0.3271 0.4646 -0.0778 -0.0508 0.0208  21  PRO A CB  
156  C  CG  . PRO A 21  ? 0.3133 0.3394 0.5105 -0.1925 -0.1115 0.0372  21  PRO A CG  
157  C  CD  . PRO A 21  ? 0.1169 0.3018 0.4678 -0.0983 -0.0438 0.0510  21  PRO A CD  
158  N  N   A ILE A 22  ? 0.1008 0.1731 0.3680 0.0037  -0.0482 -0.0402 22  ILE A N   
159  N  N   B ILE A 22  ? 0.0965 0.1893 0.3762 0.0085  -0.0421 -0.0359 22  ILE A N   
160  C  CA  A ILE A 22  ? 0.1196 0.1774 0.3441 0.0107  -0.0388 -0.0425 22  ILE A CA  
161  C  CA  B ILE A 22  ? 0.1141 0.1943 0.3632 -0.0087 -0.0356 -0.0434 22  ILE A CA  
162  C  C   A ILE A 22  ? 0.0442 0.2075 0.3006 0.0043  -0.0337 -0.0410 22  ILE A C   
163  C  C   B ILE A 22  ? 0.0611 0.2130 0.2988 -0.0023 -0.0333 -0.0486 22  ILE A C   
164  O  O   A ILE A 22  ? 0.0793 0.1960 0.3046 0.0275  -0.0006 -0.0167 22  ILE A O   
165  O  O   B ILE A 22  ? 0.0938 0.1949 0.3169 0.0052  0.0018  -0.0348 22  ILE A O   
166  C  CB  A ILE A 22  ? 0.1342 0.1781 0.3054 0.0302  -0.0326 -0.0661 22  ILE A CB  
167  C  CB  B ILE A 22  ? 0.1303 0.1724 0.3025 0.0031  -0.0103 -0.0627 22  ILE A CB  
168  C  CG1 A ILE A 22  ? 0.1392 0.1555 0.3177 -0.0225 -0.0130 -0.0291 22  ILE A CG1 
169  C  CG1 B ILE A 22  ? 0.1802 0.2819 0.2773 -0.0120 -0.0030 -0.0588 22  ILE A CG1 
170  C  CG2 A ILE A 22  ? 0.1216 0.2001 0.2944 0.0270  -0.0372 -0.0287 22  ILE A CG2 
171  C  CG2 B ILE A 22  ? 0.1291 0.1929 0.3482 -0.0679 -0.0617 -0.0073 22  ILE A CG2 
172  C  CD1 A ILE A 22  ? 0.1792 0.1782 0.3179 0.0300  -0.0250 -0.0656 22  ILE A CD1 
173  C  CD1 B ILE A 22  ? 0.2419 0.2809 0.2920 -0.0450 -0.0280 -0.0525 22  ILE A CD1 
174  N  N   . ALA A 23  ? 0.0974 0.1699 0.2536 -0.0031 -0.0406 -0.0252 23  ALA A N   
175  C  CA  . ALA A 23  ? 0.0771 0.1758 0.2613 -0.0070 0.0097  -0.0044 23  ALA A CA  
176  C  C   . ALA A 23  ? 0.0961 0.1957 0.2301 -0.0179 0.0057  -0.0128 23  ALA A C   
177  O  O   . ALA A 23  ? 0.1221 0.1764 0.2736 -0.0003 0.0084  0.0004  23  ALA A O   
178  C  CB  . ALA A 23  ? 0.0776 0.1985 0.2507 0.0095  -0.0008 -0.0234 23  ALA A CB  
179  N  N   . LYS A 24  ? 0.1207 0.2139 0.2692 0.0017  -0.0318 -0.0177 24  LYS A N   
180  C  CA  . LYS A 24  ? 0.1010 0.2645 0.2372 0.0009  -0.0128 -0.0325 24  LYS A CA  
181  C  C   . LYS A 24  ? 0.1091 0.2714 0.2749 0.0122  -0.0319 -0.0595 24  LYS A C   
182  O  O   . LYS A 24  ? 0.1611 0.3228 0.2938 -0.0037 -0.0709 -0.0227 24  LYS A O   
183  C  CB  . LYS A 24  ? 0.1200 0.3328 0.2658 0.0538  -0.0363 -0.0066 24  LYS A CB  
184  C  CG  . LYS A 24  ? 0.1333 0.3337 0.2957 0.0347  0.0312  0.0047  24  LYS A CG  
185  C  CD  . LYS A 24  ? 0.1889 0.3847 0.4521 0.1213  -0.0293 -0.0251 24  LYS A CD  
186  C  CE  . LYS A 24  ? 0.2047 0.3614 0.3755 0.0162  0.0465  0.0372  24  LYS A CE  
187  N  NZ  . LYS A 24  ? 0.2762 0.3523 0.5738 -0.0195 0.1518  0.0192  24  LYS A NZ  
188  N  N   . GLY A 25  ? 0.1188 0.2205 0.3166 0.0110  -0.0167 -0.0425 25  GLY A N   
189  C  CA  . GLY A 25  ? 0.1647 0.2721 0.3134 -0.0047 -0.0287 -0.0898 25  GLY A CA  
190  C  C   . GLY A 25  ? 0.1124 0.2798 0.2391 0.0588  -0.0366 -0.0763 25  GLY A C   
191  O  O   . GLY A 25  ? 0.1530 0.2906 0.2336 0.0399  -0.0442 -0.0390 25  GLY A O   
192  N  N   . GLU A 26  ? 0.1457 0.3303 0.2336 0.0713  -0.0668 -0.1187 26  GLU A N   
193  C  CA  . GLU A 26  ? 0.1738 0.3601 0.1776 0.0737  -0.0660 -0.1110 26  GLU A CA  
194  C  C   . GLU A 26  ? 0.1681 0.3066 0.1688 0.0565  -0.0582 -0.0612 26  GLU A C   
195  O  O   . GLU A 26  ? 0.2137 0.2925 0.1713 0.0475  -0.0705 -0.0422 26  GLU A O   
196  C  CB  . GLU A 26  ? 0.2327 0.4175 0.2500 0.0204  -0.0722 -0.1861 26  GLU A CB  
197  C  CG  . GLU A 26  ? 0.2484 0.5519 0.4177 -0.0145 -0.1181 -0.1143 26  GLU A CG  
198  C  CD  . GLU A 26  ? 0.3730 0.6253 0.4118 -0.0041 -0.2169 0.0022  26  GLU A CD  
199  O  OE1 . GLU A 26  ? 0.3791 0.6801 0.4718 -0.1773 -0.1706 -0.0721 26  GLU A OE1 
200  O  OE2 . GLU A 26  ? 0.5843 0.7770 0.5634 0.2458  -0.1073 -0.2179 26  GLU A OE2 
201  N  N   . ARG A 27  ? 0.1261 0.1893 0.1539 0.0087  -0.0231 -0.0385 27  ARG A N   
202  C  CA  . ARG A 27  ? 0.1241 0.1709 0.1451 -0.0071 -0.0234 -0.0259 27  ARG A CA  
203  C  C   . ARG A 27  ? 0.1286 0.1552 0.1568 -0.0049 -0.0330 -0.0380 27  ARG A C   
204  O  O   . ARG A 27  ? 0.1232 0.1785 0.1450 0.0168  -0.0083 -0.0129 27  ARG A O   
205  C  CB  . ARG A 27  ? 0.1741 0.1947 0.1515 0.0162  0.0003  -0.0507 27  ARG A CB  
206  C  CG  . ARG A 27  ? 0.1667 0.2980 0.1889 -0.0223 0.0156  -0.0052 27  ARG A CG  
207  C  CD  . ARG A 27  ? 0.2137 0.3211 0.3339 0.0095  0.0118  0.0062  27  ARG A CD  
208  N  NE  . ARG A 27  ? 0.2536 0.2496 0.2139 0.0190  0.0386  0.0031  27  ARG A NE  
209  C  CZ  . ARG A 27  ? 0.2525 0.2166 0.1784 0.0435  0.0329  -0.0463 27  ARG A CZ  
210  N  NH1 . ARG A 27  ? 0.1562 0.2547 0.1878 0.0212  0.0032  -0.1224 27  ARG A NH1 
211  N  NH2 . ARG A 27  ? 0.2004 0.2379 0.2518 -0.0374 0.0460  -0.0759 27  ARG A NH2 
212  N  N   . GLN A 28  ? 0.1080 0.1645 0.1497 0.0019  -0.0175 -0.0384 28  GLN A N   
213  C  CA  . GLN A 28  ? 0.0724 0.1688 0.1455 -0.0012 0.0013  -0.0345 28  GLN A CA  
214  C  C   . GLN A 28  ? 0.0938 0.1386 0.1383 0.0000  -0.0018 -0.0215 28  GLN A C   
215  O  O   . GLN A 28  ? 0.1065 0.1670 0.1279 -0.0092 -0.0104 -0.0152 28  GLN A O   
216  C  CB  . GLN A 28  ? 0.0768 0.1684 0.1767 0.0131  -0.0089 -0.0366 28  GLN A CB  
217  C  CG  . GLN A 28  ? 0.0810 0.1746 0.1986 -0.0032 -0.0272 -0.0122 28  GLN A CG  
218  C  CD  . GLN A 28  ? 0.0796 0.1796 0.1735 -0.0054 -0.0322 -0.0441 28  GLN A CD  
219  O  OE1 . GLN A 28  ? 0.0954 0.1586 0.1805 -0.0113 0.0072  -0.0330 28  GLN A OE1 
220  N  NE2 . GLN A 28  ? 0.0593 0.1685 0.2302 -0.0072 -0.0128 -0.0193 28  GLN A NE2 
221  N  N   . SER A 29  ? 0.0672 0.1475 0.1356 0.0099  -0.0044 -0.0245 29  SER A N   
222  C  CA  . SER A 29  ? 0.0895 0.1202 0.1320 0.0167  -0.0188 -0.0267 29  SER A CA  
223  C  C   . SER A 29  ? 0.0886 0.1084 0.1311 0.0185  0.0163  0.0030  29  SER A C   
224  O  O   . SER A 29  ? 0.0769 0.1552 0.1342 0.0074  0.0181  -0.0122 29  SER A O   
225  C  CB  . SER A 29  ? 0.0834 0.1150 0.1515 0.0333  0.0019  -0.0251 29  SER A CB  
226  O  OG  . SER A 29  ? 0.0787 0.1261 0.1332 0.0175  0.0064  -0.0238 29  SER A OG  
227  N  N   . PRO A 30  ? 0.0717 0.1282 0.1236 0.0096  0.0086  -0.0060 30  PRO A N   
228  C  CA  . PRO A 30  ? 0.0988 0.1437 0.0961 -0.0200 0.0074  -0.0034 30  PRO A CA  
229  C  C   . PRO A 30  ? 0.0780 0.1447 0.0889 -0.0118 -0.0046 -0.0190 30  PRO A C   
230  O  O   . PRO A 30  ? 0.0789 0.1661 0.1261 -0.0054 -0.0111 -0.0137 30  PRO A O   
231  C  CB  . PRO A 30  ? 0.0744 0.1401 0.1371 0.0132  -0.0063 -0.0270 30  PRO A CB  
232  C  CG  . PRO A 30  ? 0.0568 0.1509 0.1444 -0.0120 0.0219  -0.0113 30  PRO A CG  
233  C  CD  . PRO A 30  ? 0.0773 0.1264 0.1412 0.0072  0.0152  -0.0210 30  PRO A CD  
234  N  N   . VAL A 31  ? 0.0814 0.1293 0.1303 0.0139  0.0207  0.0157  31  VAL A N   
235  C  CA  . VAL A 31  ? 0.1239 0.1318 0.1101 -0.0006 0.0074  0.0121  31  VAL A CA  
236  C  C   . VAL A 31  ? 0.1011 0.1410 0.1053 0.0146  0.0248  0.0135  31  VAL A C   
237  O  O   . VAL A 31  ? 0.0972 0.1534 0.1209 0.0069  0.0097  0.0172  31  VAL A O   
238  C  CB  . VAL A 31  ? 0.0943 0.1651 0.1282 -0.0031 0.0234  -0.0065 31  VAL A CB  
239  C  CG1 . VAL A 31  ? 0.1407 0.1624 0.1570 -0.0104 -0.0012 -0.0067 31  VAL A CG1 
240  C  CG2 . VAL A 31  ? 0.1049 0.1893 0.1424 0.0211  0.0232  -0.0062 31  VAL A CG2 
241  N  N   . ASP A 32  ? 0.1229 0.1473 0.1008 0.0176  0.0040  0.0190  32  ASP A N   
242  C  CA  . ASP A 32  ? 0.1189 0.1460 0.1329 0.0208  0.0296  0.0295  32  ASP A CA  
243  C  C   . ASP A 32  ? 0.1401 0.1645 0.0913 0.0146  0.0134  0.0201  32  ASP A C   
244  O  O   . ASP A 32  ? 0.1728 0.2259 0.1213 0.0152  -0.0015 -0.0140 32  ASP A O   
245  C  CB  . ASP A 32  ? 0.1645 0.1552 0.1356 0.0396  -0.0015 0.0129  32  ASP A CB  
246  C  CG  . ASP A 32  ? 0.1602 0.1713 0.1435 0.0524  -0.0009 0.0259  32  ASP A CG  
247  O  OD1 . ASP A 32  ? 0.1731 0.1605 0.1383 0.0094  0.0046  0.0239  32  ASP A OD1 
248  O  OD2 . ASP A 32  ? 0.2856 0.1817 0.1430 0.0048  -0.0063 0.0268  32  ASP A OD2 
249  N  N   . ILE A 33  ? 0.1200 0.1566 0.1114 0.0249  0.0292  0.0242  33  ILE A N   
250  C  CA  . ILE A 33  ? 0.1451 0.1834 0.1309 0.0507  0.0489  0.0425  33  ILE A CA  
251  C  C   . ILE A 33  ? 0.1577 0.1625 0.1432 0.0286  0.0355  0.0312  33  ILE A C   
252  O  O   . ILE A 33  ? 0.1863 0.1794 0.1591 0.0122  0.0427  0.0280  33  ILE A O   
253  C  CB  . ILE A 33  ? 0.1485 0.1659 0.1417 0.0359  0.0474  0.0357  33  ILE A CB  
254  C  CG1 . ILE A 33  ? 0.1516 0.1518 0.1515 0.0223  0.0215  0.0370  33  ILE A CG1 
255  C  CG2 . ILE A 33  ? 0.1372 0.2421 0.1679 0.0248  0.0524  0.0109  33  ILE A CG2 
256  C  CD1 . ILE A 33  ? 0.1361 0.2072 0.1918 0.0424  0.0011  0.0400  33  ILE A CD1 
257  N  N   A ASP A 34  ? 0.2215 0.1889 0.1389 0.0519  0.0271  0.0544  34  ASP A N   
258  N  N   B ASP A 34  ? 0.2058 0.1748 0.1347 0.0502  0.0352  0.0516  34  ASP A N   
259  C  CA  A ASP A 34  ? 0.2029 0.2078 0.1539 0.0399  0.0486  0.0670  34  ASP A CA  
260  C  CA  B ASP A 34  ? 0.1809 0.1889 0.1637 0.0245  0.0482  0.0641  34  ASP A CA  
261  C  C   A ASP A 34  ? 0.2119 0.2083 0.1483 0.0317  0.0547  0.0460  34  ASP A C   
262  C  C   B ASP A 34  ? 0.2083 0.1800 0.1193 0.0296  0.0723  0.0612  34  ASP A C   
263  O  O   A ASP A 34  ? 0.2449 0.2283 0.1663 0.0255  0.0464  0.0223  34  ASP A O   
264  O  O   B ASP A 34  ? 0.2588 0.2137 0.1187 0.0842  0.0973  0.0499  34  ASP A O   
265  C  CB  A ASP A 34  ? 0.3037 0.2277 0.1946 0.1076  0.0020  0.0850  34  ASP A CB  
266  C  CB  B ASP A 34  ? 0.2264 0.1802 0.1789 0.0791  0.0302  0.0450  34  ASP A CB  
267  C  CG  A ASP A 34  ? 0.3967 0.3886 0.2010 0.0620  0.0844  0.1656  34  ASP A CG  
268  C  CG  B ASP A 34  ? 0.2320 0.2161 0.1428 0.0387  -0.0009 0.0365  34  ASP A CG  
269  O  OD1 A ASP A 34  ? 0.4958 0.4271 0.3752 0.1296  0.0806  0.2103  34  ASP A OD1 
270  O  OD1 B ASP A 34  ? 0.2194 0.2403 0.1863 0.0546  -0.0032 0.0875  34  ASP A OD1 
271  O  OD2 A ASP A 34  ? 0.2781 0.3164 0.2474 0.0584  0.0569  0.0368  34  ASP A OD2 
272  O  OD2 B ASP A 34  ? 0.2543 0.3701 0.1848 0.0309  -0.0179 0.1240  34  ASP A OD2 
273  N  N   . THR A 35  ? 0.1882 0.2119 0.1763 0.0356  0.0502  0.0757  35  THR A N   
274  C  CA  . THR A 35  ? 0.2173 0.2234 0.1996 0.0681  0.1035  0.0634  35  THR A CA  
275  C  C   . THR A 35  ? 0.2559 0.2132 0.2001 0.0610  0.1169  0.0735  35  THR A C   
276  O  O   . THR A 35  ? 0.2696 0.2667 0.2470 0.0607  0.1441  0.0226  35  THR A O   
277  C  CB  . THR A 35  ? 0.2525 0.2507 0.2241 0.0653  0.0972  0.0891  35  THR A CB  
278  O  OG1 . THR A 35  ? 0.2586 0.2428 0.2367 0.0511  0.0841  0.0781  35  THR A OG1 
279  C  CG2 . THR A 35  ? 0.2237 0.2869 0.1981 0.0834  0.0617  0.0974  35  THR A CG2 
280  N  N   . HIS A 36  ? 0.3674 0.2442 0.1683 0.1052  0.1202  0.0753  36  HIS A N   
281  C  CA  . HIS A 36  ? 0.4488 0.2487 0.1649 0.1010  0.1127  0.0968  36  HIS A CA  
282  C  C   . HIS A 36  ? 0.5190 0.3540 0.1609 0.0158  0.1500  0.0263  36  HIS A C   
283  O  O   . HIS A 36  ? 0.6458 0.4191 0.1408 0.0406  0.1732  0.0061  36  HIS A O   
284  C  CB  . HIS A 36  ? 0.5865 0.2055 0.1447 0.0820  0.1247  0.0707  36  HIS A CB  
285  C  CG  . HIS A 36  ? 0.6915 0.2514 0.2311 0.0763  0.0084  0.0159  36  HIS A CG  
286  N  ND1 . HIS A 36  ? 0.7468 0.4065 0.3414 -0.0336 -0.0779 -0.0218 36  HIS A ND1 
287  C  CD2 . HIS A 36  ? 0.9777 0.4053 0.0686 0.0956  -0.2036 -0.0501 36  HIS A CD2 
288  C  CE1 . HIS A 36  ? 0.9892 0.5059 0.1697 0.0886  -0.2949 0.0319  36  HIS A CE1 
289  N  NE2 . HIS A 36  ? 0.9307 0.4161 0.6604 0.0684  0.0265  0.1016  36  HIS A NE2 
290  N  N   . THR A 37  ? 0.3619 0.2469 0.1954 0.1144  0.0982  0.0306  37  THR A N   
291  C  CA  . THR A 37  ? 0.4077 0.2884 0.1986 0.1002  0.1086  0.0493  37  THR A CA  
292  C  C   . THR A 37  ? 0.3614 0.3055 0.1444 0.1148  0.0990  0.0396  37  THR A C   
293  O  O   . THR A 37  ? 0.4801 0.3246 0.1999 0.1228  0.0188  0.0468  37  THR A O   
294  C  CB  . THR A 37  ? 0.3569 0.3713 0.5192 0.1667  -0.0374 0.0380  37  THR A CB  
295  O  OG1 . THR A 37  ? 0.6158 0.3577 0.4857 0.1301  0.1453  0.0634  37  THR A OG1 
296  C  CG2 . THR A 37  ? 0.3240 0.5002 0.4570 0.0738  -0.0763 0.2169  37  THR A CG2 
297  N  N   . ALA A 38  ? 0.3091 0.2545 0.1612 0.1175  0.1159  0.0625  38  ALA A N   
298  C  CA  . ALA A 38  ? 0.3353 0.2542 0.1218 0.1288  0.1005  0.0656  38  ALA A CA  
299  C  C   . ALA A 38  ? 0.3577 0.2602 0.1983 0.0819  0.1713  0.0813  38  ALA A C   
300  O  O   . ALA A 38  ? 0.3254 0.2854 0.3054 0.0671  0.1835  0.0811  38  ALA A O   
301  C  CB  . ALA A 38  ? 0.2503 0.2263 0.1918 0.0753  0.0498  0.0299  38  ALA A CB  
302  N  N   . LYS A 39  ? 0.2739 0.2697 0.2500 0.1458  0.0767  0.0347  39  LYS A N   
303  C  CA  . LYS A 39  ? 0.3233 0.3380 0.2182 0.1865  0.0385  -0.0238 39  LYS A CA  
304  C  C   . LYS A 39  ? 0.2567 0.2887 0.1641 0.0704  0.0820  0.0389  39  LYS A C   
305  O  O   . LYS A 39  ? 0.2344 0.3015 0.1335 0.0583  0.0629  0.0330  39  LYS A O   
306  C  CB  . LYS A 39  ? 0.3361 0.3616 0.3270 0.2107  -0.0494 -0.0505 39  LYS A CB  
307  C  CG  . LYS A 39  ? 0.2896 0.4291 0.2730 0.0995  0.0098  -0.0197 39  LYS A CG  
308  C  CD  . LYS A 39  ? 0.2881 0.4703 0.2964 0.1832  0.0312  0.0525  39  LYS A CD  
309  C  CE  . LYS A 39  ? 0.2854 0.4804 0.3905 0.1459  0.0506  0.0142  39  LYS A CE  
310  N  NZ  . LYS A 39  ? 0.2025 0.6291 0.4615 -0.0173 -0.0042 0.0898  39  LYS A NZ  
311  N  N   . TYR A 40  ? 0.2273 0.3059 0.2119 0.0425  0.0566  0.0234  40  TYR A N   
312  C  CA  . TYR A 40  ? 0.2220 0.3589 0.1921 0.0040  0.0702  -0.0079 40  TYR A CA  
313  C  C   . TYR A 40  ? 0.3023 0.3259 0.1716 0.0230  0.0746  0.0029  40  TYR A C   
314  O  O   . TYR A 40  ? 0.2904 0.3395 0.1782 0.0750  0.0710  -0.0152 40  TYR A O   
315  C  CB  . TYR A 40  ? 0.1825 0.4758 0.3263 -0.0334 0.1414  0.0238  40  TYR A CB  
316  C  CG  . TYR A 40  ? 0.2904 0.4861 0.2286 0.0046  0.0996  0.0501  40  TYR A CG  
317  C  CD1 . TYR A 40  ? 0.2563 0.4362 0.2276 -0.0761 0.0602  0.0066  40  TYR A CD1 
318  C  CD2 . TYR A 40  ? 0.4363 0.7110 0.2367 0.0648  0.1423  0.0279  40  TYR A CD2 
319  C  CE1 . TYR A 40  ? 0.3300 0.7234 0.2590 0.0132  0.0131  0.0598  40  TYR A CE1 
320  C  CE2 . TYR A 40  ? 0.4284 0.8183 0.3247 0.1720  0.1887  -0.0221 40  TYR A CE2 
321  C  CZ  . TYR A 40  ? 0.4934 0.8677 0.2763 -0.0134 0.0348  -0.0816 40  TYR A CZ  
322  O  OH  . TYR A 40  ? 0.3994 0.9429 0.5006 -0.0247 -0.0008 -0.0998 40  TYR A OH  
323  N  N   . ASP A 41  ? 0.2516 0.3292 0.2166 0.0980  0.0977  0.0229  41  ASP A N   
324  C  CA  . ASP A 41  ? 0.3495 0.3298 0.1709 0.0567  0.0093  0.0115  41  ASP A CA  
325  C  C   . ASP A 41  ? 0.3899 0.4536 0.2421 0.1728  0.0491  0.0003  41  ASP A C   
326  O  O   . ASP A 41  ? 0.2660 0.3986 0.2656 0.1034  0.0312  0.0055  41  ASP A O   
327  C  CB  . ASP A 41  ? 0.3512 0.3289 0.3610 0.0285  0.0410  -0.0398 41  ASP A CB  
328  C  CG  . ASP A 41  ? 0.5129 0.2903 0.4898 -0.0326 -0.0269 -0.0549 41  ASP A CG  
329  O  OD1 . ASP A 41  ? 0.4905 0.4510 0.4212 0.1018  -0.1752 -0.1547 41  ASP A OD1 
330  O  OD2 . ASP A 41  ? 0.4960 0.3446 0.5168 -0.0752 -0.0656 0.0648  41  ASP A OD2 
331  N  N   . PRO A 42  ? 0.4381 0.6373 0.2780 0.2390  0.0903  0.0378  42  PRO A N   
332  C  CA  . PRO A 42  ? 0.4212 0.6829 0.3032 0.1913  0.0946  0.1423  42  PRO A CA  
333  C  C   . PRO A 42  ? 0.5687 0.6098 0.4514 0.0216  0.0991  0.1018  42  PRO A C   
334  O  O   . PRO A 42  ? 0.4846 0.8158 0.5676 0.1077  0.0250  0.1527  42  PRO A O   
335  C  CB  . PRO A 42  ? 0.5547 0.8373 0.4148 0.2035  0.2509  0.1243  42  PRO A CB  
336  C  CG  . PRO A 42  ? 0.4997 0.9947 0.2969 0.4441  0.2555  -0.0114 42  PRO A CG  
337  C  CD  . PRO A 42  ? 0.4158 0.7052 0.2489 0.3359  0.2297  0.0932  42  PRO A CD  
338  N  N   . SER A 43  ? 0.4150 0.4137 0.3511 0.2161  0.1011  0.0222  43  SER A N   
339  C  CA  . SER A 43  ? 0.6044 0.3608 0.2563 0.2145  0.0017  -0.0527 43  SER A CA  
340  C  C   . SER A 43  ? 0.5988 0.4155 0.2743 0.2114  0.0244  -0.0046 43  SER A C   
341  O  O   . SER A 43  ? 0.5413 0.3409 0.6225 0.1511  -0.0970 -0.0080 43  SER A O   
342  C  CB  . SER A 43  ? 0.6118 0.5747 0.4818 0.2152  -0.0705 -0.1015 43  SER A CB  
343  O  OG  . SER A 43  ? 0.5608 0.5186 0.3600 0.0761  -0.0623 -0.2024 43  SER A OG  
344  N  N   . LEU A 44  ? 0.5034 0.4264 0.2758 0.1742  0.0423  0.0184  44  LEU A N   
345  C  CA  . LEU A 44  ? 0.2909 0.4997 0.2569 0.1286  -0.0054 0.0359  44  LEU A CA  
346  C  C   . LEU A 44  ? 0.1652 0.5646 0.4133 0.0643  0.0804  0.1505  44  LEU A C   
347  O  O   . LEU A 44  ? 0.2522 0.8112 0.4273 -0.0700 0.0652  0.2946  44  LEU A O   
348  C  CB  . LEU A 44  ? 0.2336 0.5614 0.3407 0.1282  0.1118  0.0722  44  LEU A CB  
349  C  CG  . LEU A 44  ? 0.2402 0.3526 0.2588 0.0775  0.0687  0.0595  44  LEU A CG  
350  C  CD1 . LEU A 44  ? 0.3173 0.3847 0.1782 0.0423  0.0674  -0.0010 44  LEU A CD1 
351  C  CD2 . LEU A 44  ? 0.2105 0.3233 0.3152 0.0315  0.0603  0.0150  44  LEU A CD2 
352  N  N   . LYS A 45  ? 0.3143 0.3867 0.5228 0.0048  -0.0456 0.1603  45  LYS A N   
353  C  CA  . LYS A 45  ? 0.4261 0.5269 0.2769 0.0767  -0.0823 -0.0525 45  LYS A CA  
354  C  C   . LYS A 45  ? 0.2175 0.4315 0.3193 0.1164  0.0160  -0.0035 45  LYS A C   
355  O  O   . LYS A 45  ? 0.1823 0.4995 0.3405 0.0286  0.0938  -0.0818 45  LYS A O   
356  C  CB  . LYS A 45  ? 0.3824 0.5018 0.3091 0.2231  0.0250  -0.1212 45  LYS A CB  
357  C  CG  . LYS A 45  ? 0.4208 0.6049 0.1856 0.0693  0.0048  -0.0980 45  LYS A CG  
358  N  N   . PRO A 46  ? 0.1746 0.3928 0.3193 -0.0346 0.0595  0.0544  46  PRO A N   
359  C  CA  . PRO A 46  ? 0.2355 0.4682 0.3856 -0.1120 0.0323  0.0403  46  PRO A CA  
360  C  C   . PRO A 46  ? 0.0997 0.3790 0.3536 0.0384  0.0532  0.0625  46  PRO A C   
361  O  O   . PRO A 46  ? 0.1002 0.4525 0.3868 -0.0100 0.0570  0.0312  46  PRO A O   
362  C  CB  . PRO A 46  ? 0.2001 0.4804 0.4150 -0.0133 0.0716  -0.0784 46  PRO A CB  
363  C  CG  . PRO A 46  ? 0.2019 0.5800 0.4249 0.0879  0.0996  -0.1053 46  PRO A CG  
364  C  CD  . PRO A 46  ? 0.3296 0.4666 0.4065 0.0883  0.1238  -0.1337 46  PRO A CD  
365  N  N   A LEU A 47  ? 0.2263 0.3565 0.3698 0.0700  0.0043  0.0766  47  LEU A N   
366  N  N   B LEU A 47  ? 0.1745 0.3662 0.3832 0.0783  0.0515  0.1068  47  LEU A N   
367  C  CA  A LEU A 47  ? 0.2239 0.3185 0.3778 -0.0563 -0.0289 0.0568  47  LEU A CA  
368  C  CA  B LEU A 47  ? 0.0692 0.2804 0.4007 -0.0150 0.1033  0.0238  47  LEU A CA  
369  C  C   A LEU A 47  ? 0.1856 0.2737 0.4484 -0.0499 0.0018  0.1172  47  LEU A C   
370  C  C   B LEU A 47  ? 0.1781 0.2754 0.4571 -0.0736 0.0292  0.1161  47  LEU A C   
371  O  O   A LEU A 47  ? 0.1965 0.3322 0.4825 -0.0380 -0.0845 0.0916  47  LEU A O   
372  O  O   B LEU A 47  ? 0.1778 0.2784 0.5079 -0.0722 -0.0326 0.1507  47  LEU A O   
373  C  CB  A LEU A 47  ? 0.2427 0.3351 0.5181 -0.0347 -0.0168 0.0580  47  LEU A CB  
374  C  CB  B LEU A 47  ? 0.2031 0.3184 0.4348 0.0974  0.1379  0.0555  47  LEU A CB  
375  C  CG  A LEU A 47  ? 0.3198 0.2979 0.4754 -0.0864 -0.0089 -0.0086 47  LEU A CG  
376  C  CG  B LEU A 47  ? 0.1896 0.2984 0.3483 0.0312  0.0796  0.0328  47  LEU A CG  
377  C  CD1 A LEU A 47  ? 0.1623 0.2222 0.6761 -0.0886 0.0436  0.0816  47  LEU A CD1 
378  C  CD1 B LEU A 47  ? 0.0996 0.3318 0.4255 0.0189  -0.0143 -0.0825 47  LEU A CD1 
379  C  CD2 A LEU A 47  ? 0.3477 0.3782 0.6831 0.0182  0.0130  -0.0378 47  LEU A CD2 
380  C  CD2 B LEU A 47  ? 0.1683 0.3519 0.5089 -0.0333 0.0229  0.0303  47  LEU A CD2 
381  N  N   . SER A 48  ? 0.0954 0.2407 0.3153 -0.0151 0.0080  0.0825  48  SER A N   
382  C  CA  . SER A 48  ? 0.0859 0.2823 0.3167 0.0538  0.0525  0.0658  48  SER A CA  
383  C  C   . SER A 48  ? 0.1072 0.2408 0.3096 -0.0311 0.0464  0.0348  48  SER A C   
384  O  O   . SER A 48  ? 0.1329 0.2100 0.3470 -0.0528 0.0362  -0.0100 48  SER A O   
385  C  CB  . SER A 48  ? 0.1583 0.2600 0.3635 0.0010  0.0134  0.0310  48  SER A CB  
386  O  OG  . SER A 48  ? 0.2141 0.3309 0.4022 0.0427  -0.0011 0.0284  48  SER A OG  
387  N  N   . VAL A 49  ? 0.1353 0.2663 0.3498 -0.0377 0.0111  0.0049  49  VAL A N   
388  C  CA  . VAL A 49  ? 0.1999 0.2613 0.3754 -0.0800 0.0378  -0.0047 49  VAL A CA  
389  C  C   . VAL A 49  ? 0.1292 0.3328 0.3899 -0.0713 0.0124  -0.0367 49  VAL A C   
390  O  O   . VAL A 49  ? 0.2345 0.3617 0.4708 -0.1903 -0.0299 -0.0159 49  VAL A O   
391  C  CB  . VAL A 49  ? 0.2277 0.2782 0.3863 -0.0893 0.0588  -0.0223 49  VAL A CB  
392  C  CG1 . VAL A 49  ? 0.3870 0.3393 0.3817 -0.1146 0.1118  -0.0151 49  VAL A CG1 
393  C  CG2 . VAL A 49  ? 0.2689 0.2942 0.3982 -0.0677 0.0713  0.0355  49  VAL A CG2 
394  N  N   . SER A 50  ? 0.1598 0.3083 0.3374 -0.0684 -0.0074 -0.0236 50  SER A N   
395  C  CA  . SER A 50  ? 0.1310 0.2524 0.4312 -0.0387 -0.0424 -0.0232 50  SER A CA  
396  C  C   . SER A 50  ? 0.1497 0.2663 0.3481 -0.0278 -0.0986 -0.0179 50  SER A C   
397  O  O   . SER A 50  ? 0.2148 0.2597 0.3890 -0.0465 -0.0897 0.0138  50  SER A O   
398  C  CB  . SER A 50  ? 0.2938 0.2901 0.4750 0.0000  0.0652  -0.0647 50  SER A CB  
399  O  OG  . SER A 50  ? 0.2812 0.4230 0.5550 -0.0905 0.0533  -0.0708 50  SER A OG  
400  N  N   . TYR A 51  ? 0.1511 0.2151 0.3990 -0.0285 -0.0688 -0.0078 51  TYR A N   
401  C  CA  . TYR A 51  ? 0.2046 0.2358 0.3367 -0.0125 -0.1046 0.0347  51  TYR A CA  
402  C  C   . TYR A 51  ? 0.1688 0.2391 0.3264 -0.0038 -0.0655 0.0411  51  TYR A C   
403  O  O   . TYR A 51  ? 0.2216 0.2797 0.3289 -0.0212 -0.1001 0.0364  51  TYR A O   
404  C  CB  . TYR A 51  ? 0.1381 0.2451 0.3061 -0.0111 -0.0825 0.0158  51  TYR A CB  
405  C  CG  . TYR A 51  ? 0.1324 0.2042 0.2456 -0.0337 -0.0502 0.0301  51  TYR A CG  
406  C  CD1 . TYR A 51  ? 0.1139 0.2310 0.2460 -0.0376 -0.0385 0.0133  51  TYR A CD1 
407  C  CD2 . TYR A 51  ? 0.1396 0.2018 0.2750 -0.0200 -0.0243 0.0160  51  TYR A CD2 
408  C  CE1 . TYR A 51  ? 0.1439 0.1766 0.2191 -0.0359 -0.0438 0.0163  51  TYR A CE1 
409  C  CE2 . TYR A 51  ? 0.1630 0.1742 0.2718 -0.0529 -0.0497 0.0350  51  TYR A CE2 
410  C  CZ  . TYR A 51  ? 0.1157 0.1688 0.2281 -0.0428 -0.0363 0.0356  51  TYR A CZ  
411  O  OH  . TYR A 51  ? 0.1306 0.1917 0.2230 -0.0207 -0.0365 0.0061  51  TYR A OH  
412  N  N   . ASP A 52  ? 0.1347 0.2852 0.4299 -0.0076 -0.0774 0.0533  52  ASP A N   
413  C  CA  . ASP A 52  ? 0.1947 0.3098 0.4342 -0.0127 -0.0806 0.0876  52  ASP A CA  
414  C  C   . ASP A 52  ? 0.3271 0.3752 0.4498 -0.0190 -0.1303 0.1021  52  ASP A C   
415  O  O   . ASP A 52  ? 0.3727 0.4029 0.3890 -0.0166 -0.0878 0.1258  52  ASP A O   
416  C  CB  . ASP A 52  ? 0.1540 0.4453 0.6444 0.0294  -0.0660 0.1196  52  ASP A CB  
417  C  CG  . ASP A 52  ? 0.3001 0.4925 0.8567 0.0631  -0.0854 -0.0031 52  ASP A CG  
418  O  OD1 . ASP A 52  ? 0.4825 0.6080 0.8386 -0.0257 -0.0937 0.0961  52  ASP A OD1 
419  O  OD2 . ASP A 52  ? 0.5281 0.5312 1.0594 0.1627  -0.0035 0.2471  52  ASP A OD2 
420  N  N   . GLN A 53  ? 0.2233 0.2819 0.5604 -0.0010 -0.0004 0.1522  53  GLN A N   
421  C  CA  . GLN A 53  ? 0.2635 0.2979 0.4129 0.0165  0.0033  0.0949  53  GLN A CA  
422  C  C   . GLN A 53  ? 0.2509 0.2293 0.3061 0.0283  -0.0396 0.0264  53  GLN A C   
423  O  O   . GLN A 53  ? 0.2683 0.2137 0.3730 0.0190  -0.1037 0.0564  53  GLN A O   
424  C  CB  . GLN A 53  ? 0.3073 0.3328 0.3789 0.0527  -0.0446 0.0797  53  GLN A CB  
425  C  CG  . GLN A 53  ? 0.2624 0.4258 0.5900 -0.0214 -0.0842 0.1483  53  GLN A CG  
426  C  CD  . GLN A 53  ? 0.5197 0.6618 0.6782 0.0054  -0.1562 0.0505  53  GLN A CD  
427  O  OE1 . GLN A 53  ? 0.5427 0.5338 0.7258 0.0930  0.0669  0.2048  53  GLN A OE1 
428  N  NE2 . GLN A 53  ? 0.2493 0.4747 0.7347 0.0703  -0.1165 0.0538  53  GLN A NE2 
429  N  N   . ALA A 54  ? 0.2304 0.1864 0.3689 -0.0290 -0.0783 0.0439  54  ALA A N   
430  C  CA  . ALA A 54  ? 0.2468 0.1846 0.2464 0.0177  -0.0738 0.0279  54  ALA A CA  
431  C  C   . ALA A 54  ? 0.2926 0.2139 0.2327 -0.0075 -0.0890 -0.0267 54  ALA A C   
432  O  O   . ALA A 54  ? 0.2883 0.2604 0.3016 -0.0386 -0.1167 -0.0257 54  ALA A O   
433  C  CB  . ALA A 54  ? 0.2195 0.1652 0.3728 0.0302  -0.0387 0.0237  54  ALA A CB  
434  N  N   . THR A 55  ? 0.3021 0.1687 0.2324 0.0167  -0.0806 0.0190  55  THR A N   
435  C  CA  . THR A 55  ? 0.2815 0.1703 0.2158 0.0071  -0.0920 0.0212  55  THR A CA  
436  C  C   . THR A 55  ? 0.2839 0.1594 0.1745 -0.0100 -0.0903 0.0727  55  THR A C   
437  O  O   . THR A 55  ? 0.3180 0.1597 0.2126 -0.0178 -0.0935 0.0352  55  THR A O   
438  C  CB  . THR A 55  ? 0.4120 0.1885 0.2446 0.0264  -0.1093 0.0549  55  THR A CB  
439  O  OG1 . THR A 55  ? 0.4539 0.2152 0.3307 -0.0286 -0.0869 0.0131  55  THR A OG1 
440  C  CG2 . THR A 55  ? 0.4220 0.2194 0.2338 0.0632  -0.1262 0.0018  55  THR A CG2 
441  N  N   . SER A 56  ? 0.2997 0.1533 0.1698 -0.0067 -0.0788 0.0432  56  SER A N   
442  C  CA  . SER A 56  ? 0.3427 0.1437 0.1983 -0.0242 -0.0741 0.0205  56  SER A CA  
443  C  C   . SER A 56  ? 0.2962 0.1318 0.1595 -0.0195 -0.0844 0.0295  56  SER A C   
444  O  O   . SER A 56  ? 0.3546 0.1864 0.1706 0.0047  -0.1171 0.0212  56  SER A O   
445  C  CB  . SER A 56  ? 0.3282 0.1393 0.1857 -0.0104 -0.1071 0.0024  56  SER A CB  
446  O  OG  . SER A 56  ? 0.3711 0.1432 0.1814 -0.0188 -0.1202 0.0091  56  SER A OG  
447  N  N   . LEU A 57  ? 0.3131 0.1785 0.1529 0.0082  -0.0289 0.0199  57  LEU A N   
448  C  CA  . LEU A 57  ? 0.3961 0.1482 0.1181 0.0033  -0.0550 0.0105  57  LEU A CA  
449  C  C   . LEU A 57  ? 0.3856 0.1670 0.1719 0.0364  -0.1092 -0.0447 57  LEU A C   
450  O  O   . LEU A 57  ? 0.4604 0.1843 0.1498 0.0109  -0.0888 0.0182  57  LEU A O   
451  C  CB  . LEU A 57  ? 0.3609 0.1498 0.2251 0.0262  -0.0594 -0.0086 57  LEU A CB  
452  C  CG  . LEU A 57  ? 0.3752 0.2028 0.2281 0.0416  -0.0606 -0.0348 57  LEU A CG  
453  C  CD1 . LEU A 57  ? 0.4113 0.1782 0.2949 -0.0318 0.0483  -0.0643 57  LEU A CD1 
454  C  CD2 . LEU A 57  ? 0.5088 0.2622 0.3076 0.0745  -0.1202 0.0310  57  LEU A CD2 
455  N  N   . ARG A 58  ? 0.3855 0.1861 0.1591 0.0469  -0.0608 0.0342  58  ARG A N   
456  C  CA  . ARG A 58  ? 0.3134 0.2063 0.1690 0.0132  -0.0317 0.0515  58  ARG A CA  
457  C  C   . ARG A 58  ? 0.3257 0.2119 0.1327 0.0527  -0.0080 0.0397  58  ARG A C   
458  O  O   . ARG A 58  ? 0.4367 0.1835 0.1207 0.0142  -0.0135 0.0263  58  ARG A O   
459  C  CB  . ARG A 58  ? 0.2841 0.2151 0.2678 -0.0146 -0.0100 0.0925  58  ARG A CB  
460  C  CG  . ARG A 58  ? 0.3352 0.2403 0.3321 -0.0392 0.0613  0.1271  58  ARG A CG  
461  C  CD  . ARG A 58  ? 0.3039 0.2901 0.3746 -0.0594 0.0758  0.0314  58  ARG A CD  
462  N  NE  . ARG A 58  ? 0.4672 0.3335 0.3814 -0.1577 0.1698  0.0108  58  ARG A NE  
463  C  CZ  . ARG A 58  ? 0.3919 0.2996 0.3664 0.0105  0.1506  0.0650  58  ARG A CZ  
464  N  NH1 . ARG A 58  ? 0.5314 0.5321 0.4345 0.0455  -0.0078 0.2182  58  ARG A NH1 
465  N  NH2 . ARG A 58  ? 0.5630 0.2568 0.3420 0.0610  0.1887  0.0760  58  ARG A NH2 
466  N  N   . ILE A 59  ? 0.4015 0.1810 0.1500 0.0419  -0.0296 0.0201  59  ILE A N   
467  C  CA  . ILE A 59  ? 0.4257 0.1534 0.1493 0.0272  -0.0600 0.0089  59  ILE A CA  
468  C  C   . ILE A 59  ? 0.4321 0.1785 0.1133 -0.0088 -0.0737 0.0407  59  ILE A C   
469  O  O   . ILE A 59  ? 0.4086 0.2191 0.1114 -0.0105 -0.0514 0.0449  59  ILE A O   
470  C  CB  . ILE A 59  ? 0.4100 0.1814 0.1223 -0.0200 -0.0565 0.0410  59  ILE A CB  
471  C  CG1 . ILE A 59  ? 0.3432 0.1961 0.1346 0.0006  -0.0680 0.0354  59  ILE A CG1 
472  C  CG2 . ILE A 59  ? 0.3482 0.2004 0.1135 0.0052  -0.0468 0.0279  59  ILE A CG2 
473  C  CD1 . ILE A 59  ? 0.3913 0.1819 0.1580 0.0103  -0.0691 -0.0234 59  ILE A CD1 
474  N  N   A LEU A 60  ? 0.3818 0.1925 0.0814 0.0173  -0.0328 0.0187  60  LEU A N   
475  N  N   B LEU A 60  ? 0.4236 0.2274 0.0985 0.0109  -0.0553 0.0428  60  LEU A N   
476  C  CA  A LEU A 60  ? 0.3540 0.1809 0.2099 -0.0186 -0.0392 0.0396  60  LEU A CA  
477  C  CA  B LEU A 60  ? 0.4364 0.2388 0.1515 -0.0142 -0.0627 0.0471  60  LEU A CA  
478  C  C   A LEU A 60  ? 0.2552 0.1684 0.1126 -0.0797 -0.0204 0.0454  60  LEU A C   
479  C  C   B LEU A 60  ? 0.3702 0.2050 0.1425 -0.0237 0.0142  0.0560  60  LEU A C   
480  O  O   A LEU A 60  ? 0.2854 0.2539 0.1254 -0.0908 0.0107  0.0576  60  LEU A O   
481  O  O   B LEU A 60  ? 0.4215 0.2245 0.0986 0.0219  -0.0201 0.0510  60  LEU A O   
482  C  CB  A LEU A 60  ? 0.3086 0.1886 0.2372 -0.0310 0.0537  0.0323  60  LEU A CB  
483  C  CB  B LEU A 60  ? 0.5511 0.2361 0.1795 -0.0761 -0.0631 0.0714  60  LEU A CB  
484  C  CG  A LEU A 60  ? 0.4563 0.1480 0.2778 -0.0463 0.0660  -0.0551 60  LEU A CG  
485  C  CG  B LEU A 60  ? 0.5637 0.1706 0.3183 -0.0640 -0.0509 0.0148  60  LEU A CG  
486  C  CD1 A LEU A 60  ? 0.2980 0.2006 0.3792 -0.0302 0.1128  -0.0271 60  LEU A CD1 
487  C  CD1 B LEU A 60  ? 0.4347 0.1573 0.3389 -0.1011 -0.0528 0.0468  60  LEU A CD1 
488  C  CD2 A LEU A 60  ? 0.4242 0.3665 0.4215 0.0165  0.0075  0.0596  60  LEU A CD2 
489  C  CD2 B LEU A 60  ? 0.6797 0.2621 0.3191 -0.0847 -0.0803 -0.0308 60  LEU A CD2 
490  N  N   . ASN A 61  ? 0.2953 0.2153 0.1291 -0.0629 -0.0058 0.0149  61  ASN A N   
491  C  CA  . ASN A 61  ? 0.3097 0.1954 0.1335 -0.0647 0.0020  0.0078  61  ASN A CA  
492  C  C   . ASN A 61  ? 0.4037 0.2405 0.1685 -0.1235 -0.0088 -0.0078 61  ASN A C   
493  O  O   . ASN A 61  ? 0.4176 0.2475 0.1716 -0.1236 -0.0370 0.0501  61  ASN A O   
494  C  CB  . ASN A 61  ? 0.3321 0.1715 0.1461 -0.0564 0.0115  0.0071  61  ASN A CB  
495  C  CG  . ASN A 61  ? 0.3088 0.1927 0.1708 -0.0899 0.0336  0.0553  61  ASN A CG  
496  O  OD1 . ASN A 61  ? 0.2936 0.2675 0.1491 -0.0982 0.0425  0.0150  61  ASN A OD1 
497  N  ND2 . ASN A 61  ? 0.2802 0.2117 0.1523 -0.0603 0.0484  0.0155  61  ASN A ND2 
498  N  N   . ASN A 62  ? 0.3157 0.2524 0.1616 -0.1217 -0.0165 0.0336  62  ASN A N   
499  C  CA  . ASN A 62  ? 0.3585 0.2264 0.1810 -0.1361 -0.0114 0.0255  62  ASN A CA  
500  C  C   . ASN A 62  ? 0.3653 0.2810 0.2270 -0.1458 0.0391  0.0673  62  ASN A C   
501  O  O   . ASN A 62  ? 0.4194 0.3283 0.2495 -0.1898 0.0307  0.0153  62  ASN A O   
502  C  CB  . ASN A 62  ? 0.4755 0.2297 0.1925 -0.1400 -0.0208 0.0036  62  ASN A CB  
503  C  CG  . ASN A 62  ? 0.4635 0.2010 0.1634 -0.0924 -0.0267 -0.0093 62  ASN A CG  
504  O  OD1 . ASN A 62  ? 0.3288 0.2147 0.1816 -0.0888 0.0164  -0.0221 62  ASN A OD1 
505  N  ND2 . ASN A 62  ? 0.6012 0.2653 0.3061 0.0030  0.0550  -0.0250 62  ASN A ND2 
506  N  N   . GLY A 63  ? 0.2892 0.2617 0.1336 -0.1116 0.0444  0.0390  63  GLY A N   
507  C  CA  . GLY A 63  ? 0.2818 0.2943 0.2259 -0.1128 0.0373  0.0548  63  GLY A CA  
508  C  C   . GLY A 63  ? 0.1498 0.3085 0.1882 -0.1018 0.0502  0.0305  63  GLY A C   
509  O  O   . GLY A 63  ? 0.2396 0.3114 0.2284 -0.0547 0.0268  -0.0464 63  GLY A O   
510  N  N   A HIS A 64  ? 0.2013 0.2360 0.1379 -0.0929 0.0357  0.0199  64  HIS A N   
511  N  N   B HIS A 64  ? 0.1846 0.2924 0.1565 -0.1099 0.0572  0.0422  64  HIS A N   
512  C  CA  A HIS A 64  ? 0.2205 0.2291 0.1376 -0.0525 0.0357  0.0282  64  HIS A CA  
513  C  CA  B HIS A 64  ? 0.2310 0.2842 0.1218 -0.0544 0.0333  0.0259  64  HIS A CA  
514  C  C   A HIS A 64  ? 0.2344 0.1922 0.1914 -0.0580 0.0159  0.0242  64  HIS A C   
515  C  C   B HIS A 64  ? 0.2270 0.1709 0.1293 -0.0335 0.0456  -0.0197 64  HIS A C   
516  O  O   A HIS A 64  ? 0.2342 0.2355 0.2162 -0.0574 -0.0067 0.0670  64  HIS A O   
517  O  O   B HIS A 64  ? 0.2103 0.1806 0.1543 -0.0372 0.0027  0.0000  64  HIS A O   
518  C  CB  A HIS A 64  ? 0.1734 0.2471 0.1943 -0.0178 0.0446  -0.0236 64  HIS A CB  
519  C  CB  B HIS A 64  ? 0.2957 0.2931 0.2431 -0.1197 -0.0372 0.0006  64  HIS A CB  
520  C  CG  A HIS A 64  ? 0.2204 0.2287 0.1527 -0.0697 0.0000  -0.0113 64  HIS A CG  
521  C  CG  B HIS A 64  ? 0.4149 0.3237 0.2283 -0.0489 -0.0299 0.0351  64  HIS A CG  
522  N  ND1 A HIS A 64  ? 0.2372 0.2769 0.1782 -0.0557 -0.0079 -0.0460 64  HIS A ND1 
523  N  ND1 B HIS A 64  ? 0.3423 0.3685 0.2591 -0.0801 -0.0528 0.0664  64  HIS A ND1 
524  C  CD2 A HIS A 64  ? 0.2144 0.2218 0.1988 -0.0536 0.0157  -0.0298 64  HIS A CD2 
525  C  CD2 B HIS A 64  ? 0.2744 0.3520 0.1342 -0.0467 -0.0763 0.0314  64  HIS A CD2 
526  C  CE1 A HIS A 64  ? 0.2349 0.2879 0.2363 -0.0602 0.0398  -0.0593 64  HIS A CE1 
527  C  CE1 B HIS A 64  ? 0.4527 0.3484 0.1709 -0.0915 -0.0631 0.0416  64  HIS A CE1 
528  N  NE2 A HIS A 64  ? 0.2160 0.2619 0.2595 -0.0858 0.1020  -0.0333 64  HIS A NE2 
529  N  NE2 B HIS A 64  ? 0.3790 0.3623 0.2614 -0.0502 -0.0117 -0.0254 64  HIS A NE2 
530  N  N   . SER A 65  ? 0.1974 0.1922 0.1412 -0.0416 0.0630  0.0160  65  SER A N   
531  C  CA  . SER A 65  ? 0.1713 0.1602 0.1627 -0.0140 0.0248  0.0223  65  SER A CA  
532  C  C   . SER A 65  ? 0.2405 0.1731 0.1375 -0.0225 0.0174  0.0075  65  SER A C   
533  O  O   . SER A 65  ? 0.2256 0.2094 0.1429 -0.0377 0.0187  0.0156  65  SER A O   
534  C  CB  . SER A 65  ? 0.2179 0.3300 0.1065 -0.0594 0.0126  0.0075  65  SER A CB  
535  O  OG  . SER A 65  ? 0.2759 0.2971 0.1705 -0.0254 -0.0143 0.0638  65  SER A OG  
536  N  N   . PHE A 66  ? 0.2315 0.1832 0.1311 -0.0096 -0.0143 0.0065  66  PHE A N   
537  C  CA  . PHE A 66  ? 0.2029 0.2527 0.1227 0.0000  -0.0119 0.0172  66  PHE A CA  
538  C  C   . PHE A 66  ? 0.2736 0.1631 0.1200 0.0201  -0.0146 0.0264  66  PHE A C   
539  O  O   . PHE A 66  ? 0.2653 0.1766 0.1135 0.0020  -0.0136 0.0129  66  PHE A O   
540  C  CB  . PHE A 66  ? 0.3084 0.2154 0.1320 -0.0264 -0.0084 0.0057  66  PHE A CB  
541  C  CG  . PHE A 66  ? 0.2608 0.2011 0.1289 -0.0091 -0.0253 -0.0347 66  PHE A CG  
542  C  CD1 . PHE A 66  ? 0.2355 0.2667 0.0999 -0.0238 0.0096  -0.0203 66  PHE A CD1 
543  C  CD2 . PHE A 66  ? 0.2349 0.2051 0.1613 0.0134  -0.0172 -0.0242 66  PHE A CD2 
544  C  CE1 . PHE A 66  ? 0.2291 0.2426 0.1623 -0.0127 -0.0151 -0.0076 66  PHE A CE1 
545  C  CE2 . PHE A 66  ? 0.2340 0.2058 0.1521 0.0100  -0.0070 -0.0550 66  PHE A CE2 
546  C  CZ  . PHE A 66  ? 0.2305 0.2108 0.1286 0.0100  0.0009  -0.0447 66  PHE A CZ  
547  N  N   . LYS A 67  ? 0.3235 0.1794 0.1249 0.0383  -0.0496 0.0200  67  LYS A N   
548  C  CA  . LYS A 67  ? 0.3125 0.1769 0.1249 0.0137  -0.0560 0.0035  67  LYS A CA  
549  C  C   . LYS A 67  ? 0.3426 0.1749 0.1157 0.0146  -0.0483 0.0154  67  LYS A C   
550  O  O   . LYS A 67  ? 0.3728 0.2707 0.1105 0.0659  -0.0200 0.0359  67  LYS A O   
551  C  CB  . LYS A 67  ? 0.3492 0.2049 0.2773 0.0013  -0.1137 -0.0201 67  LYS A CB  
552  C  CG  . LYS A 67  ? 0.3171 0.2697 0.2385 -0.0184 -0.0553 -0.0343 67  LYS A CG  
553  C  CD  . LYS A 67  ? 0.3908 0.2699 0.3033 -0.0756 -0.0824 -0.0452 67  LYS A CD  
554  C  CE  . LYS A 67  ? 0.3260 0.4190 0.5404 -0.0597 0.0287  -0.0401 67  LYS A CE  
555  N  NZ  . LYS A 67  ? 0.4661 0.5862 0.3951 -0.1311 0.0077  -0.1353 67  LYS A NZ  
556  N  N   . VAL A 68  ? 0.3097 0.1566 0.1487 0.0164  -0.0696 0.0259  68  VAL A N   
557  C  CA  . VAL A 68  ? 0.3265 0.1983 0.1461 0.0553  -0.0812 -0.0073 68  VAL A CA  
558  C  C   . VAL A 68  ? 0.3324 0.1852 0.0939 0.0456  -0.0097 0.0190  68  VAL A C   
559  O  O   . VAL A 68  ? 0.3953 0.1537 0.0929 0.0407  -0.0254 0.0135  68  VAL A O   
560  C  CB  . VAL A 68  ? 0.2972 0.1810 0.1360 0.0619  -0.0506 -0.0078 68  VAL A CB  
561  C  CG1 . VAL A 68  ? 0.3388 0.2245 0.1297 0.0935  -0.0825 -0.0094 68  VAL A CG1 
562  C  CG2 . VAL A 68  ? 0.3985 0.1838 0.1379 0.0455  -0.0588 -0.0064 68  VAL A CG2 
563  N  N   . GLU A 69  ? 0.3878 0.1733 0.1195 0.0403  -0.0502 0.0176  69  GLU A N   
564  C  CA  . GLU A 69  ? 0.2948 0.1760 0.1655 -0.0002 -0.0749 -0.0105 69  GLU A CA  
565  C  C   . GLU A 69  ? 0.2895 0.1444 0.1932 -0.0089 -0.0847 0.0018  69  GLU A C   
566  O  O   . GLU A 69  ? 0.3985 0.1789 0.2022 0.0846  -0.1399 -0.0098 69  GLU A O   
567  C  CB  . GLU A 69  ? 0.4243 0.2251 0.1932 -0.0315 0.0210  0.0596  69  GLU A CB  
568  C  CG  . GLU A 69  ? 0.4496 0.3524 0.3710 -0.0254 0.0690  0.1516  69  GLU A CG  
569  C  CD  . GLU A 69  ? 0.4577 0.3698 0.3635 -0.0144 -0.0556 0.1949  69  GLU A CD  
570  O  OE1 . GLU A 69  ? 0.6979 0.4823 0.3261 0.0648  -0.0181 0.1249  69  GLU A OE1 
571  O  OE2 . GLU A 69  ? 0.3054 0.7677 0.6602 -0.0217 -0.0905 -0.0820 69  GLU A OE2 
572  N  N   . PHE A 70  ? 0.3042 0.1268 0.1655 0.0144  -0.0769 0.0299  70  PHE A N   
573  C  CA  . PHE A 70  ? 0.2734 0.1397 0.1518 -0.0129 -0.0671 0.0145  70  PHE A CA  
574  C  C   . PHE A 70  ? 0.2518 0.1421 0.1397 -0.0197 -0.0367 0.0184  70  PHE A C   
575  O  O   . PHE A 70  ? 0.2860 0.1575 0.2292 -0.0259 -0.0928 0.0193  70  PHE A O   
576  C  CB  . PHE A 70  ? 0.2579 0.1620 0.1548 -0.0294 -0.0691 0.0237  70  PHE A CB  
577  C  CG  . PHE A 70  ? 0.2943 0.1410 0.1824 -0.0100 -0.1227 0.0190  70  PHE A CG  
578  C  CD1 . PHE A 70  ? 0.3096 0.1480 0.1763 0.0234  -0.0485 0.0319  70  PHE A CD1 
579  C  CD2 . PHE A 70  ? 0.2810 0.1519 0.1473 -0.0182 -0.0882 0.0275  70  PHE A CD2 
580  C  CE1 . PHE A 70  ? 0.3792 0.1823 0.1638 -0.0244 -0.0450 0.0281  70  PHE A CE1 
581  C  CE2 . PHE A 70  ? 0.3116 0.1433 0.1870 0.0002  -0.1021 0.0218  70  PHE A CE2 
582  C  CZ  . PHE A 70  ? 0.3628 0.1680 0.1645 0.0348  -0.0557 0.0345  70  PHE A CZ  
583  N  N   A ASP A 71  ? 0.3294 0.1339 0.2180 0.0120  -0.0873 0.0154  71  ASP A N   
584  N  N   B ASP A 71  ? 0.3507 0.1257 0.1846 0.0128  -0.0968 0.0343  71  ASP A N   
585  C  CA  A ASP A 71  ? 0.2351 0.1421 0.2183 -0.0512 -0.0727 0.0455  71  ASP A CA  
586  C  CA  B ASP A 71  ? 0.3236 0.1385 0.1641 0.0199  -0.0796 0.0197  71  ASP A CA  
587  C  C   A ASP A 71  ? 0.2876 0.1148 0.2425 -0.0722 -0.0638 0.0231  71  ASP A C   
588  C  C   B ASP A 71  ? 0.3274 0.0821 0.1550 -0.0290 -0.0872 0.0409  71  ASP A C   
589  O  O   A ASP A 71  ? 0.2694 0.2223 0.2508 -0.0674 -0.0717 0.0605  71  ASP A O   
590  O  O   B ASP A 71  ? 0.3182 0.1212 0.2909 -0.0845 -0.0749 0.0427  71  ASP A O   
591  C  CB  A ASP A 71  ? 0.1918 0.1706 0.2707 0.0049  -0.0868 0.0293  71  ASP A CB  
592  C  CB  B ASP A 71  ? 0.2843 0.1523 0.1832 0.0030  -0.0719 0.0312  71  ASP A CB  
593  C  CG  A ASP A 71  ? 0.2764 0.1527 0.2694 -0.0548 -0.1053 0.0411  71  ASP A CG  
594  C  CG  B ASP A 71  ? 0.2945 0.1634 0.3792 0.0181  -0.1244 0.0275  71  ASP A CG  
595  O  OD1 A ASP A 71  ? 0.2706 0.1598 0.2324 -0.0043 -0.0829 0.0359  71  ASP A OD1 
596  O  OD1 B ASP A 71  ? 0.2288 0.1860 0.2936 0.0427  -0.0512 0.0003  71  ASP A OD1 
597  O  OD2 A ASP A 71  ? 0.2663 0.2065 0.2722 0.0565  -0.0668 0.0279  71  ASP A OD2 
598  O  OD2 B ASP A 71  ? 0.2094 0.2075 0.4005 0.0023  -0.0379 0.0234  71  ASP A OD2 
599  N  N   . ASP A 72  ? 0.3042 0.1114 0.1861 -0.0264 -0.0722 0.0044  72  ASP A N   
600  C  CA  . ASP A 72  ? 0.2778 0.1078 0.1963 -0.0243 -0.0661 0.0000  72  ASP A CA  
601  C  C   . ASP A 72  ? 0.3238 0.1017 0.2238 -0.0037 -0.0513 0.0134  72  ASP A C   
602  O  O   . ASP A 72  ? 0.3699 0.1483 0.2419 -0.0237 -0.0974 0.0057  72  ASP A O   
603  C  CB  . ASP A 72  ? 0.3036 0.1141 0.2085 -0.0069 -0.0576 0.0156  72  ASP A CB  
604  C  CG  . ASP A 72  ? 0.3181 0.1285 0.1945 -0.0326 -0.0869 0.0320  72  ASP A CG  
605  O  OD1 . ASP A 72  ? 0.3438 0.2216 0.2189 -0.0387 -0.1034 0.0858  72  ASP A OD1 
606  O  OD2 . ASP A 72  ? 0.2926 0.2232 0.1701 -0.0195 -0.0736 0.0566  72  ASP A OD2 
607  N  N   . SER A 73  ? 0.2992 0.1164 0.2524 -0.0290 -0.0653 0.0461  73  SER A N   
608  C  CA  . SER A 73  ? 0.3231 0.1194 0.2676 -0.0472 -0.0917 0.0036  73  SER A CA  
609  C  C   . SER A 73  ? 0.4004 0.1168 0.3148 -0.0458 -0.0261 0.0003  73  SER A C   
610  O  O   . SER A 73  ? 0.3960 0.1221 0.2987 -0.0194 -0.0842 0.0017  73  SER A O   
611  C  CB  . SER A 73  ? 0.3371 0.1669 0.3169 -0.0547 -0.0391 0.0483  73  SER A CB  
612  O  OG  . SER A 73  ? 0.3546 0.1645 0.2788 -0.0024 -0.0550 0.0603  73  SER A OG  
613  N  N   . GLN A 74  ? 0.2843 0.1462 0.3452 0.0195  0.0052  0.0325  74  GLN A N   
614  C  CA  . GLN A 74  ? 0.3628 0.2360 0.3792 0.0110  0.0416  -0.0381 74  GLN A CA  
615  C  C   . GLN A 74  ? 0.2593 0.2469 0.3326 -0.0312 -0.0313 -0.0731 74  GLN A C   
616  O  O   . GLN A 74  ? 0.2582 0.2209 0.3042 -0.0508 -0.0898 0.0316  74  GLN A O   
617  C  CB  . GLN A 74  ? 0.3270 0.3301 0.5268 0.0800  -0.0052 0.1599  74  GLN A CB  
618  C  CG  . GLN A 74  ? 0.6144 0.2602 0.6572 -0.0560 0.0384  0.1596  74  GLN A CG  
619  C  CD  . GLN A 74  ? 0.4452 0.5679 0.8701 -0.1488 -0.0945 0.1033  74  GLN A CD  
620  O  OE1 . GLN A 74  ? 0.3364 0.5200 0.5351 0.0146  -0.1004 0.2000  74  GLN A OE1 
621  N  NE2 . GLN A 74  ? 0.4473 0.8159 0.5517 -0.2486 -0.2404 0.3483  74  GLN A NE2 
622  N  N   A ASP A 75  ? 0.3734 0.3547 0.2991 -0.0370 0.0048  -0.0127 75  ASP A N   
623  N  N   B ASP A 75  ? 0.3235 0.3220 0.2180 -0.0776 -0.0341 -0.1118 75  ASP A N   
624  C  CA  A ASP A 75  ? 0.2958 0.4206 0.3931 -0.1176 -0.0155 0.0263  75  ASP A CA  
625  C  CA  B ASP A 75  ? 0.1886 0.2682 0.4137 -0.0617 -0.0359 -0.0279 75  ASP A CA  
626  C  C   A ASP A 75  ? 0.1893 0.4036 0.4699 0.0038  -0.0796 -0.0096 75  ASP A C   
627  C  C   B ASP A 75  ? 0.2025 0.3079 0.4305 -0.0312 -0.0973 -0.0540 75  ASP A C   
628  O  O   A ASP A 75  ? 0.1831 0.6644 0.4090 -0.0876 -0.0488 0.0418  75  ASP A O   
629  O  O   B ASP A 75  ? 0.3133 0.2006 0.5705 0.0250  -0.2735 0.0144  75  ASP A O   
630  C  CB  A ASP A 75  ? 0.2848 0.4201 0.3467 -0.0192 -0.0860 0.0710  75  ASP A CB  
631  C  CB  B ASP A 75  ? 0.1606 0.2227 0.3642 -0.0321 -0.0950 0.0287  75  ASP A CB  
632  C  CG  A ASP A 75  ? 0.4283 0.3023 0.4257 0.0579  -0.2079 0.0855  75  ASP A CG  
633  C  CG  B ASP A 75  ? 0.2036 0.2466 0.3714 0.0069  -0.0366 0.0096  75  ASP A CG  
634  O  OD1 A ASP A 75  ? 0.1307 0.3289 0.3443 0.0346  -0.0217 0.1183  75  ASP A OD1 
635  O  OD1 B ASP A 75  ? 0.1645 0.2515 0.5141 0.0016  -0.0829 0.0491  75  ASP A OD1 
636  O  OD2 A ASP A 75  ? 0.6365 0.2975 0.6211 0.1231  -0.0196 0.0499  75  ASP A OD2 
637  O  OD2 B ASP A 75  ? 0.3154 0.2971 0.4481 -0.0037 0.0870  0.0154  75  ASP A OD2 
638  N  N   . LYS A 76  ? 0.2861 0.2760 0.3455 -0.0054 -0.1054 0.0739  76  LYS A N   
639  C  CA  . LYS A 76  ? 0.3957 0.1832 0.5134 0.0133  -0.1087 0.0439  76  LYS A CA  
640  C  C   . LYS A 76  ? 0.6488 0.3230 0.5326 0.0849  -0.0930 0.1401  76  LYS A C   
641  O  O   . LYS A 76  ? 0.6059 0.7656 0.7561 -0.0366 -0.0625 0.1846  76  LYS A O   
642  C  CB  . LYS A 76  ? 0.4428 0.2155 0.4158 -0.0902 -0.2085 0.0585  76  LYS A CB  
643  C  CG  . LYS A 76  ? 0.5638 0.2990 0.4578 -0.0328 -0.1492 0.1180  76  LYS A CG  
644  C  CD  . LYS A 76  ? 0.7164 0.2534 0.4288 -0.1060 -0.1077 0.0419  76  LYS A CD  
645  C  CE  . LYS A 76  ? 0.7615 0.2782 0.3770 -0.0886 0.0002  0.0817  76  LYS A CE  
646  N  NZ  . LYS A 76  ? 0.6792 0.3017 0.3683 0.1077  -0.0026 0.0595  76  LYS A NZ  
647  N  N   . ALA A 77  ? 0.2620 0.3276 0.5529 0.0517  -0.2332 0.1356  77  ALA A N   
648  C  CA  . ALA A 77  ? 0.2317 0.2469 0.3301 -0.0215 -0.1254 0.0418  77  ALA A CA  
649  C  C   . ALA A 77  ? 0.1740 0.2739 0.4078 -0.0225 -0.1524 0.0277  77  ALA A C   
650  O  O   . ALA A 77  ? 0.1566 0.3280 0.4616 0.0057  -0.1040 -0.0608 77  ALA A O   
651  C  CB  . ALA A 77  ? 0.3093 0.2620 0.3644 0.0326  -0.0908 0.0631  77  ALA A CB  
652  N  N   . VAL A 78  ? 0.2026 0.1755 0.3502 -0.0179 -0.0998 0.0532  78  VAL A N   
653  C  CA  . VAL A 78  ? 0.2609 0.1990 0.3436 -0.0411 -0.1236 0.0861  78  VAL A CA  
654  C  C   . VAL A 78  ? 0.1386 0.2053 0.3188 -0.0509 -0.0687 0.0534  78  VAL A C   
655  O  O   . VAL A 78  ? 0.1414 0.2244 0.4105 -0.0524 -0.0967 0.0553  78  VAL A O   
656  C  CB  . VAL A 78  ? 0.3039 0.3173 0.3140 0.0370  0.0062  0.0456  78  VAL A CB  
657  C  CG1 . VAL A 78  ? 0.3864 0.1986 0.4472 -0.0229 -0.1117 0.0584  78  VAL A CG1 
658  C  CG2 . VAL A 78  ? 0.3167 0.2979 0.3961 0.0937  0.0697  -0.0317 78  VAL A CG2 
659  N  N   . LEU A 79  ? 0.1272 0.1648 0.2978 -0.0131 -0.0383 0.0377  79  LEU A N   
660  C  CA  . LEU A 79  ? 0.1275 0.1694 0.2694 -0.0025 -0.0060 0.0128  79  LEU A CA  
661  C  C   . LEU A 79  ? 0.1273 0.1339 0.3085 -0.0079 0.0017  0.0027  79  LEU A C   
662  O  O   . LEU A 79  ? 0.1570 0.1731 0.3261 -0.0396 0.0351  -0.0277 79  LEU A O   
663  C  CB  . LEU A 79  ? 0.1022 0.2148 0.2887 -0.0109 -0.0077 0.0525  79  LEU A CB  
664  C  CG  . LEU A 79  ? 0.1424 0.1947 0.3098 0.0114  0.0030  0.0287  79  LEU A CG  
665  C  CD1 . LEU A 79  ? 0.1661 0.1950 0.4841 -0.0297 0.0253  0.0904  79  LEU A CD1 
666  C  CD2 . LEU A 79  ? 0.1782 0.2329 0.2644 0.0651  0.0847  0.0561  79  LEU A CD2 
667  N  N   . LYS A 80  ? 0.1584 0.2154 0.2697 -0.0211 0.0064  0.0097  80  LYS A N   
668  C  CA  . LYS A 80  ? 0.1960 0.2112 0.2949 -0.0004 0.0367  -0.0032 80  LYS A CA  
669  C  C   . LYS A 80  ? 0.1360 0.2072 0.3326 -0.0067 0.1028  -0.0241 80  LYS A C   
670  O  O   . LYS A 80  ? 0.1494 0.2060 0.3748 -0.0351 0.0345  0.0166  80  LYS A O   
671  C  CB  . LYS A 80  ? 0.2653 0.2478 0.3657 0.0578  0.0277  0.0323  80  LYS A CB  
672  C  CG  . LYS A 80  ? 0.2724 0.2952 0.4440 0.0316  0.0697  0.1007  80  LYS A CG  
673  C  CD  . LYS A 80  ? 0.2381 0.2861 0.6233 0.0422  -0.0207 0.0713  80  LYS A CD  
674  N  N   . GLY A 81  ? 0.2410 0.2291 0.3109 0.0144  0.1267  -0.0048 81  GLY A N   
675  C  CA  . GLY A 81  ? 0.1974 0.2312 0.3776 0.0648  0.1526  0.0383  81  GLY A CA  
676  C  C   . GLY A 81  ? 0.2121 0.1839 0.3664 0.0537  0.1287  0.0159  81  GLY A C   
677  O  O   . GLY A 81  ? 0.1981 0.2358 0.3333 0.0128  0.1030  -0.0209 81  GLY A O   
678  N  N   . GLY A 82  ? 0.2415 0.2270 0.5006 0.0131  0.0796  0.1181  82  GLY A N   
679  C  CA  . GLY A 82  ? 0.2670 0.1705 0.6347 0.0412  0.1155  0.0914  82  GLY A CA  
680  C  C   . GLY A 82  ? 0.2405 0.2649 0.4719 0.1527  0.1225  0.0666  82  GLY A C   
681  O  O   . GLY A 82  ? 0.3034 0.3825 0.4338 0.1550  0.1972  0.0811  82  GLY A O   
682  N  N   . PRO A 83  ? 0.2142 0.2050 0.4029 0.0862  0.1229  0.0532  83  PRO A N   
683  C  CA  . PRO A 83  ? 0.3236 0.2212 0.2998 0.0983  0.0902  0.0398  83  PRO A CA  
684  C  C   . PRO A 83  ? 0.2327 0.2313 0.3403 0.0774  0.0768  0.0037  83  PRO A C   
685  O  O   . PRO A 83  ? 0.3121 0.3328 0.3324 0.0607  -0.0044 -0.0024 83  PRO A O   
686  C  CB  . PRO A 83  ? 0.3309 0.2669 0.1940 0.1157  0.0995  0.0743  83  PRO A CB  
687  C  CG  . PRO A 83  ? 0.2281 0.2679 0.2249 0.0819  0.0592  0.0240  83  PRO A CG  
688  C  CD  . PRO A 83  ? 0.1954 0.2039 0.3971 0.0856  0.1054  0.0261  83  PRO A CD  
689  N  N   . LEU A 84  ? 0.2047 0.1904 0.3062 0.0514  0.0946  0.0108  84  LEU A N   
690  C  CA  . LEU A 84  ? 0.2394 0.1462 0.2583 0.0143  0.0705  -0.0498 84  LEU A CA  
691  C  C   . LEU A 84  ? 0.2117 0.2062 0.3039 0.0609  0.0816  -0.0597 84  LEU A C   
692  O  O   . LEU A 84  ? 0.2261 0.2361 0.3776 0.0529  0.1230  -0.0744 84  LEU A O   
693  C  CB  . LEU A 84  ? 0.1762 0.1583 0.2632 0.0368  0.0710  -0.0333 84  LEU A CB  
694  C  CG  . LEU A 84  ? 0.1155 0.1529 0.2784 0.0350  0.0444  -0.0252 84  LEU A CG  
695  C  CD1 . LEU A 84  ? 0.1370 0.2470 0.2628 0.0318  0.0168  -0.0318 84  LEU A CD1 
696  C  CD2 . LEU A 84  ? 0.1151 0.1882 0.2482 0.0104  0.0504  -0.0245 84  LEU A CD2 
697  N  N   . ASP A 85  ? 0.2605 0.2033 0.3977 0.0229  0.1024  -0.0790 85  ASP A N   
698  C  CA  . ASP A 85  ? 0.2891 0.1956 0.3698 0.0351  0.0913  -0.0497 85  ASP A CA  
699  C  C   . ASP A 85  ? 0.2520 0.2129 0.4244 0.0497  0.0449  0.0223  85  ASP A C   
700  O  O   . ASP A 85  ? 0.3374 0.3947 0.3955 0.0619  0.0888  -0.0861 85  ASP A O   
701  C  CB  . ASP A 85  ? 0.3724 0.2229 0.3731 0.0397  0.1060  -0.0728 85  ASP A CB  
702  C  CG  . ASP A 85  ? 0.5877 0.4033 0.4715 0.1042  0.0256  0.0118  85  ASP A CG  
703  O  OD1 . ASP A 85  ? 0.7045 0.8482 0.3013 0.0337  0.0901  0.1470  85  ASP A OD1 
704  O  OD2 . ASP A 85  ? 0.5962 0.5994 0.4621 0.0412  -0.0055 -0.0035 85  ASP A OD2 
705  N  N   . GLY A 86  ? 0.2302 0.3089 0.4681 0.0072  0.0344  0.1307  86  GLY A N   
706  C  CA  . GLY A 86  ? 0.2667 0.2169 0.3161 -0.0055 0.0476  0.0154  86  GLY A CA  
707  C  C   . GLY A 86  ? 0.3115 0.2024 0.3885 -0.0367 -0.0362 0.0162  86  GLY A C   
708  O  O   . GLY A 86  ? 0.3775 0.2974 0.5339 -0.1315 -0.0480 0.0977  86  GLY A O   
709  N  N   . THR A 87  ? 0.1694 0.2615 0.3540 0.0697  0.0130  0.0173  87  THR A N   
710  C  CA  . THR A 87  ? 0.1457 0.2390 0.3782 0.0061  0.0480  -0.0053 87  THR A CA  
711  C  C   . THR A 87  ? 0.1184 0.1451 0.3918 -0.0009 0.0210  0.0023  87  THR A C   
712  O  O   . THR A 87  ? 0.1397 0.1300 0.4115 -0.0079 0.0491  -0.0069 87  THR A O   
713  C  CB  . THR A 87  ? 0.1753 0.5529 0.3300 0.1984  -0.0155 -0.0308 87  THR A CB  
714  O  OG1 . THR A 87  ? 0.1758 0.5115 0.7164 0.1939  0.0332  -0.2034 87  THR A OG1 
715  C  CG2 . THR A 87  ? 0.2313 0.3982 0.4300 0.0591  -0.0204 -0.0194 87  THR A CG2 
716  N  N   . TYR A 88  ? 0.1014 0.1444 0.3225 0.0212  0.0178  0.0054  88  TYR A N   
717  C  CA  . TYR A 88  ? 0.0870 0.1576 0.3087 -0.0035 0.0016  0.0027  88  TYR A CA  
718  C  C   . TYR A 88  ? 0.1033 0.1778 0.2980 -0.0016 -0.0008 0.0015  88  TYR A C   
719  O  O   . TYR A 88  ? 0.1807 0.2453 0.3371 -0.0803 -0.0743 0.0571  88  TYR A O   
720  C  CB  . TYR A 88  ? 0.1261 0.1428 0.2378 0.0211  0.0029  -0.0301 88  TYR A CB  
721  C  CG  . TYR A 88  ? 0.1146 0.1173 0.2331 0.0037  0.0210  -0.0281 88  TYR A CG  
722  C  CD1 . TYR A 88  ? 0.1186 0.1467 0.2291 0.0206  0.0240  -0.0225 88  TYR A CD1 
723  C  CD2 . TYR A 88  ? 0.1040 0.0983 0.2051 0.0000  0.0205  0.0084  88  TYR A CD2 
724  C  CE1 . TYR A 88  ? 0.1430 0.1868 0.2245 0.0027  0.0412  -0.0299 88  TYR A CE1 
725  C  CE2 . TYR A 88  ? 0.1584 0.1155 0.1972 0.0009  0.0074  -0.0141 88  TYR A CE2 
726  C  CZ  . TYR A 88  ? 0.1424 0.1157 0.2284 0.0163  -0.0005 -0.0388 88  TYR A CZ  
727  O  OH  . TYR A 88  ? 0.1354 0.1827 0.2055 -0.0070 0.0268  -0.0318 88  TYR A OH  
728  N  N   . ARG A 89  ? 0.1188 0.1340 0.2463 0.0227  -0.0152 -0.0346 89  ARG A N   
729  C  CA  . ARG A 89  ? 0.1565 0.1329 0.2363 0.0153  -0.0486 0.0269  89  ARG A CA  
730  C  C   . ARG A 89  ? 0.1195 0.1257 0.1993 -0.0216 -0.0547 0.0307  89  ARG A C   
731  O  O   . ARG A 89  ? 0.1137 0.1238 0.1692 0.0012  -0.0332 0.0118  89  ARG A O   
732  C  CB  . ARG A 89  ? 0.2344 0.1382 0.3407 0.0043  -0.1234 0.0490  89  ARG A CB  
733  C  CG  . ARG A 89  ? 0.3925 0.2269 0.2269 0.0388  -0.0769 0.0947  89  ARG A CG  
734  C  CD  . ARG A 89  ? 0.2940 0.1821 0.3046 0.0902  -0.0330 0.0480  89  ARG A CD  
735  N  NE  . ARG A 89  ? 0.3558 0.2039 0.2707 0.0638  -0.0828 0.0345  89  ARG A NE  
736  C  CZ  . ARG A 89  ? 0.3344 0.1870 0.1500 0.0284  -0.0232 0.0044  89  ARG A CZ  
737  N  NH1 . ARG A 89  ? 0.3173 0.2241 0.2129 0.0966  -0.0036 0.0196  89  ARG A NH1 
738  N  NH2 . ARG A 89  ? 0.3465 0.2361 0.3089 0.0729  -0.0111 -0.0604 89  ARG A NH2 
739  N  N   . LEU A 90  ? 0.1489 0.1257 0.2057 -0.0185 -0.0598 0.0195  90  LEU A N   
740  C  CA  . LEU A 90  ? 0.1376 0.1551 0.1845 -0.0340 -0.0310 0.0156  90  LEU A CA  
741  C  C   . LEU A 90  ? 0.1738 0.1049 0.1551 -0.0081 -0.0325 0.0194  90  LEU A C   
742  O  O   . LEU A 90  ? 0.1631 0.1879 0.2460 -0.0039 -0.0469 0.0823  90  LEU A O   
743  C  CB  . LEU A 90  ? 0.1643 0.1376 0.2001 -0.0272 -0.0644 0.0144  90  LEU A CB  
744  C  CG  . LEU A 90  ? 0.1943 0.1302 0.1819 -0.0398 -0.0565 0.0253  90  LEU A CG  
745  C  CD1 . LEU A 90  ? 0.2072 0.1401 0.2019 -0.0134 -0.0442 0.0155  90  LEU A CD1 
746  C  CD2 . LEU A 90  ? 0.2011 0.1821 0.2323 -0.0321 -0.0996 0.0220  90  LEU A CD2 
747  N  N   . THR A 91  ? 0.1835 0.1291 0.1684 -0.0099 -0.0220 0.0076  91  THR A N   
748  C  CA  . THR A 91  ? 0.1606 0.1342 0.1699 -0.0118 -0.0340 0.0210  91  THR A CA  
749  C  C   . THR A 91  ? 0.1904 0.1354 0.1304 -0.0006 -0.0347 0.0399  91  THR A C   
750  O  O   . THR A 91  ? 0.2320 0.1343 0.1196 -0.0187 -0.0554 0.0332  91  THR A O   
751  C  CB  . THR A 91  ? 0.2061 0.1525 0.1873 -0.0546 -0.0502 0.0479  91  THR A CB  
752  O  OG1 . THR A 91  ? 0.2679 0.2395 0.1885 -0.1079 -0.0368 0.0653  91  THR A OG1 
753  C  CG2 . THR A 91  ? 0.2092 0.1368 0.1857 -0.0400 -0.0586 0.0058  91  THR A CG2 
754  N  N   . GLN A 92  ? 0.2024 0.1067 0.1436 -0.0083 -0.0384 0.0149  92  GLN A N   
755  C  CA  . GLN A 92  ? 0.1990 0.1256 0.1460 -0.0124 -0.0296 0.0214  92  GLN A CA  
756  C  C   . GLN A 92  ? 0.1902 0.1200 0.1178 -0.0015 -0.0190 0.0147  92  GLN A C   
757  O  O   . GLN A 92  ? 0.1814 0.1205 0.1268 -0.0165 -0.0299 0.0258  92  GLN A O   
758  C  CB  . GLN A 92  ? 0.2193 0.1523 0.1490 -0.0335 -0.0104 0.0178  92  GLN A CB  
759  C  CG  . GLN A 92  ? 0.2007 0.1315 0.2015 -0.0413 -0.0446 0.0488  92  GLN A CG  
760  C  CD  . GLN A 92  ? 0.2165 0.1631 0.1780 -0.0318 -0.0304 0.0559  92  GLN A CD  
761  O  OE1 . GLN A 92  ? 0.2288 0.1534 0.1631 -0.0084 -0.0277 0.0293  92  GLN A OE1 
762  N  NE2 . GLN A 92  ? 0.1911 0.2502 0.2374 -0.0214 -0.0154 0.0841  92  GLN A NE2 
763  N  N   . PHE A 93  ? 0.2079 0.1139 0.1216 0.0013  -0.0491 0.0234  93  PHE A N   
764  C  CA  . PHE A 93  ? 0.1831 0.1017 0.1443 -0.0124 -0.0321 0.0251  93  PHE A CA  
765  C  C   . PHE A 93  ? 0.2367 0.1137 0.1181 -0.0089 -0.0184 0.0081  93  PHE A C   
766  O  O   . PHE A 93  ? 0.2266 0.1412 0.1045 -0.0093 -0.0229 0.0158  93  PHE A O   
767  C  CB  . PHE A 93  ? 0.1873 0.1546 0.1263 -0.0359 -0.0641 0.0222  93  PHE A CB  
768  C  CG  . PHE A 93  ? 0.1983 0.1231 0.1372 0.0027  -0.0728 0.0122  93  PHE A CG  
769  C  CD1 . PHE A 93  ? 0.2403 0.1279 0.1633 -0.0154 -0.0541 -0.0059 93  PHE A CD1 
770  C  CD2 . PHE A 93  ? 0.1976 0.1785 0.1478 -0.0038 -0.0928 0.0477  93  PHE A CD2 
771  C  CE1 . PHE A 93  ? 0.2500 0.1259 0.1744 0.0067  -0.0914 0.0153  93  PHE A CE1 
772  C  CE2 . PHE A 93  ? 0.2254 0.1397 0.1515 0.0033  -0.0869 0.0251  93  PHE A CE2 
773  C  CZ  . PHE A 93  ? 0.2503 0.1229 0.1935 0.0183  -0.0836 0.0071  93  PHE A CZ  
774  N  N   . HIS A 94  ? 0.1843 0.1182 0.1189 -0.0088 -0.0306 0.0020  94  HIS A N   
775  C  CA  . HIS A 94  ? 0.1839 0.1195 0.0988 -0.0190 -0.0057 0.0207  94  HIS A CA  
776  C  C   . HIS A 94  ? 0.1591 0.1234 0.0807 0.0002  -0.0173 0.0154  94  HIS A C   
777  O  O   . HIS A 94  ? 0.1557 0.1272 0.0838 0.0054  -0.0110 0.0111  94  HIS A O   
778  C  CB  . HIS A 94  ? 0.1781 0.1644 0.0678 -0.0345 -0.0078 0.0118  94  HIS A CB  
779  C  CG  . HIS A 94  ? 0.1787 0.1353 0.0746 -0.0373 -0.0100 0.0161  94  HIS A CG  
780  N  ND1 . HIS A 94  ? 0.1509 0.1511 0.1040 -0.0189 -0.0004 0.0020  94  HIS A ND1 
781  C  CD2 . HIS A 94  ? 0.1317 0.1526 0.0712 -0.0357 0.0003  0.0146  94  HIS A CD2 
782  C  CE1 . HIS A 94  ? 0.1379 0.1214 0.1206 -0.0214 -0.0034 0.0165  94  HIS A CE1 
783  N  NE2 . HIS A 94  ? 0.1408 0.1392 0.0757 -0.0152 -0.0052 0.0119  94  HIS A NE2 
784  N  N   . PHE A 95  ? 0.1410 0.1115 0.1304 0.0030  -0.0137 0.0131  95  PHE A N   
785  C  CA  . PHE A 95  ? 0.1605 0.0956 0.0897 0.0030  -0.0223 0.0025  95  PHE A CA  
786  C  C   . PHE A 95  ? 0.1299 0.1295 0.1071 -0.0156 0.0068  0.0095  95  PHE A C   
787  O  O   . PHE A 95  ? 0.1404 0.1289 0.1200 -0.0127 0.0208  0.0187  95  PHE A O   
788  C  CB  . PHE A 95  ? 0.1248 0.1415 0.1109 -0.0136 -0.0022 -0.0223 95  PHE A CB  
789  C  CG  . PHE A 95  ? 0.1347 0.1193 0.1006 -0.0055 -0.0077 -0.0081 95  PHE A CG  
790  C  CD1 . PHE A 95  ? 0.1703 0.1455 0.1239 0.0075  -0.0272 -0.0074 95  PHE A CD1 
791  C  CD2 . PHE A 95  ? 0.1327 0.1498 0.1401 -0.0163 0.0068  -0.0184 95  PHE A CD2 
792  C  CE1 . PHE A 95  ? 0.1735 0.1512 0.1507 0.0013  -0.0366 -0.0247 95  PHE A CE1 
793  C  CE2 . PHE A 95  ? 0.1461 0.1511 0.1641 0.0200  -0.0168 -0.0375 95  PHE A CE2 
794  C  CZ  . PHE A 95  ? 0.1565 0.1749 0.1615 -0.0065 -0.0299 -0.0364 95  PHE A CZ  
795  N  N   . HIS A 96  ? 0.1273 0.1177 0.0936 0.0019  -0.0010 -0.0001 96  HIS A N   
796  C  CA  . HIS A 96  ? 0.1178 0.1202 0.0810 -0.0050 0.0126  0.0030  96  HIS A CA  
797  C  C   . HIS A 96  ? 0.1062 0.1225 0.0927 -0.0127 0.0200  -0.0037 96  HIS A C   
798  O  O   . HIS A 96  ? 0.1084 0.1353 0.1092 -0.0022 0.0201  0.0042  96  HIS A O   
799  C  CB  . HIS A 96  ? 0.1444 0.1231 0.0818 -0.0243 -0.0037 -0.0121 96  HIS A CB  
800  C  CG  . HIS A 96  ? 0.0987 0.1180 0.1011 -0.0097 0.0064  -0.0044 96  HIS A CG  
801  N  ND1 . HIS A 96  ? 0.1150 0.1259 0.1195 -0.0348 0.0228  -0.0063 96  HIS A ND1 
802  C  CD2 . HIS A 96  ? 0.1252 0.1157 0.0996 0.0034  0.0080  -0.0039 96  HIS A CD2 
803  C  CE1 . HIS A 96  ? 0.1171 0.1299 0.1033 -0.0060 0.0315  -0.0038 96  HIS A CE1 
804  N  NE2 . HIS A 96  ? 0.1112 0.1134 0.1211 0.0013  0.0148  -0.0063 96  HIS A NE2 
805  N  N   . TRP A 97  ? 0.1415 0.1229 0.0810 0.0041  0.0063  -0.0082 97  TRP A N   
806  C  CA  . TRP A 97  ? 0.1340 0.1134 0.1008 0.0098  0.0008  -0.0062 97  TRP A CA  
807  C  C   . TRP A 97  ? 0.1230 0.1322 0.1115 0.0011  0.0048  -0.0057 97  TRP A C   
808  O  O   . TRP A 97  ? 0.1209 0.1437 0.1224 -0.0025 0.0223  -0.0047 97  TRP A O   
809  C  CB  . TRP A 97  ? 0.1604 0.1611 0.0875 -0.0140 0.0031  -0.0106 97  TRP A CB  
810  C  CG  . TRP A 97  ? 0.1519 0.1234 0.0999 -0.0289 0.0122  -0.0164 97  TRP A CG  
811  C  CD1 . TRP A 97  ? 0.1713 0.1582 0.0863 -0.0062 0.0030  -0.0121 97  TRP A CD1 
812  C  CD2 . TRP A 97  ? 0.1543 0.1444 0.0961 -0.0185 0.0183  -0.0097 97  TRP A CD2 
813  N  NE1 . TRP A 97  ? 0.2270 0.1469 0.1008 -0.0055 0.0102  0.0022  97  TRP A NE1 
814  C  CE2 . TRP A 97  ? 0.1624 0.1379 0.0859 -0.0161 0.0209  -0.0012 97  TRP A CE2 
815  C  CE3 . TRP A 97  ? 0.1521 0.1345 0.1056 -0.0064 -0.0149 -0.0060 97  TRP A CE3 
816  C  CZ2 . TRP A 97  ? 0.2182 0.1342 0.1155 -0.0397 -0.0060 0.0084  97  TRP A CZ2 
817  C  CZ3 . TRP A 97  ? 0.1893 0.1606 0.0939 -0.0003 -0.0012 0.0064  97  TRP A CZ3 
818  C  CH2 . TRP A 97  ? 0.2037 0.1453 0.1099 -0.0205 0.0221  0.0020  97  TRP A CH2 
819  N  N   . GLY A 98  ? 0.1697 0.1172 0.0917 0.0068  0.0196  -0.0083 98  GLY A N   
820  C  CA  . GLY A 98  ? 0.1419 0.1296 0.1282 0.0182  0.0187  -0.0062 98  GLY A CA  
821  C  C   . GLY A 98  ? 0.1566 0.1236 0.1318 -0.0006 0.0229  -0.0048 98  GLY A C   
822  O  O   . GLY A 98  ? 0.1792 0.1590 0.1253 0.0054  0.0234  -0.0239 98  GLY A O   
823  N  N   . SER A 99  ? 0.1807 0.1112 0.1436 0.0044  0.0292  -0.0359 99  SER A N   
824  C  CA  . SER A 99  ? 0.1688 0.1501 0.1867 0.0027  0.0443  -0.0732 99  SER A CA  
825  C  C   . SER A 99  ? 0.1911 0.1544 0.1573 -0.0091 0.0121  -0.0302 99  SER A C   
826  O  O   . SER A 99  ? 0.2679 0.2056 0.2236 -0.0305 0.0019  -0.0863 99  SER A O   
827  C  CB  . SER A 99  ? 0.1850 0.2394 0.1964 0.0326  0.0339  -0.0545 99  SER A CB  
828  O  OG  . SER A 99  ? 0.1525 0.1917 0.2152 0.0179  0.0553  -0.0388 99  SER A OG  
829  N  N   . LEU A 100 ? 0.1282 0.1584 0.2172 -0.0186 0.0254  -0.0225 100 LEU A N   
830  C  CA  . LEU A 100 ? 0.1684 0.1114 0.3189 -0.0070 0.0452  -0.0182 100 LEU A CA  
831  C  C   . LEU A 100 ? 0.1952 0.1756 0.1834 -0.0243 0.0335  -0.0295 100 LEU A C   
832  O  O   . LEU A 100 ? 0.1903 0.1550 0.2241 0.0051  0.0089  -0.0348 100 LEU A O   
833  C  CB  . LEU A 100 ? 0.2658 0.2238 0.3588 0.0605  0.0819  0.0443  100 LEU A CB  
834  C  CG  . LEU A 100 ? 0.2630 0.2673 0.3098 0.0649  0.0610  0.0550  100 LEU A CG  
835  C  CD1 . LEU A 100 ? 0.1838 0.4546 0.4408 0.0907  -0.0013 -0.0091 100 LEU A CD1 
836  C  CD2 . LEU A 100 ? 0.3811 0.3437 0.3409 0.0976  0.1141  -0.0959 100 LEU A CD2 
837  N  N   . ASP A 101 ? 0.1623 0.1412 0.2655 0.0100  0.0599  -0.0185 101 ASP A N   
838  C  CA  . ASP A 101 ? 0.1479 0.1766 0.2244 0.0109  0.0473  0.0054  101 ASP A CA  
839  C  C   . ASP A 101 ? 0.2039 0.1245 0.2237 -0.0035 0.0129  0.0002  101 ASP A C   
840  O  O   . ASP A 101 ? 0.2216 0.1583 0.2573 0.0150  0.0342  0.0084  101 ASP A O   
841  C  CB  . ASP A 101 ? 0.1932 0.1613 0.2431 -0.0303 0.0136  0.0395  101 ASP A CB  
842  C  CG  . ASP A 101 ? 0.1806 0.2172 0.2754 0.0024  0.0188  0.0277  101 ASP A CG  
843  O  OD1 . ASP A 101 ? 0.2252 0.2026 0.2495 -0.0384 0.0068  0.0215  101 ASP A OD1 
844  O  OD2 . ASP A 101 ? 0.2673 0.2295 0.3434 -0.0725 -0.0018 0.0097  101 ASP A OD2 
845  N  N   . GLY A 102 ? 0.2380 0.1225 0.2564 -0.0048 -0.0107 0.0149  102 GLY A N   
846  C  CA  . GLY A 102 ? 0.1710 0.1724 0.2744 -0.0329 -0.0243 0.0381  102 GLY A CA  
847  C  C   . GLY A 102 ? 0.1651 0.1327 0.2298 -0.0005 0.0036  0.0313  102 GLY A C   
848  O  O   . GLY A 102 ? 0.1796 0.1972 0.2068 -0.0229 0.0088  0.0385  102 GLY A O   
849  N  N   . GLN A 103 ? 0.1487 0.1491 0.2107 -0.0195 0.0276  0.0203  103 GLN A N   
850  C  CA  . GLN A 103 ? 0.1407 0.1368 0.1500 0.0002  0.0265  -0.0027 103 GLN A CA  
851  C  C   . GLN A 103 ? 0.1261 0.1401 0.1209 -0.0069 0.0440  -0.0107 103 GLN A C   
852  O  O   . GLN A 103 ? 0.1426 0.1365 0.1516 -0.0103 0.0269  -0.0196 103 GLN A O   
853  C  CB  . GLN A 103 ? 0.1401 0.1433 0.1437 0.0122  0.0329  -0.0124 103 GLN A CB  
854  C  CG  . GLN A 103 ? 0.1533 0.1667 0.1540 0.0378  0.0502  -0.0103 103 GLN A CG  
855  C  CD  . GLN A 103 ? 0.1934 0.2441 0.2390 0.0842  0.0606  0.0493  103 GLN A CD  
856  O  OE1 . GLN A 103 ? 0.1927 0.2692 0.2391 0.0366  0.0727  0.0299  103 GLN A OE1 
857  N  NE2 . GLN A 103 ? 0.2124 0.3087 0.3274 0.1837  0.1388  0.1307  103 GLN A NE2 
858  N  N   . GLY A 104 ? 0.0914 0.1254 0.1419 0.0189  0.0291  -0.0052 104 GLY A N   
859  C  CA  . GLY A 104 ? 0.1032 0.1317 0.1157 0.0138  0.0120  -0.0094 104 GLY A CA  
860  C  C   . GLY A 104 ? 0.1076 0.1231 0.1090 -0.0111 0.0086  -0.0188 104 GLY A C   
861  O  O   . GLY A 104 ? 0.1223 0.1314 0.1335 -0.0087 0.0046  0.0062  104 GLY A O   
862  N  N   . SER A 105 ? 0.0880 0.1458 0.0880 0.0172  0.0042  -0.0163 105 SER A N   
863  C  CA  . SER A 105 ? 0.0814 0.1200 0.1282 -0.0192 0.0313  -0.0162 105 SER A CA  
864  C  C   . SER A 105 ? 0.0875 0.1123 0.1137 -0.0120 0.0254  0.0004  105 SER A C   
865  O  O   . SER A 105 ? 0.1084 0.1231 0.1406 0.0098  0.0077  -0.0102 105 SER A O   
866  C  CB  . SER A 105 ? 0.0688 0.1342 0.1178 0.0001  0.0172  0.0178  105 SER A CB  
867  O  OG  . SER A 105 ? 0.1024 0.1089 0.1261 -0.0083 0.0229  0.0114  105 SER A OG  
868  N  N   . GLU A 106 ? 0.1008 0.1118 0.1032 -0.0068 0.0189  -0.0119 106 GLU A N   
869  C  CA  . GLU A 106 ? 0.0976 0.1169 0.1101 -0.0184 0.0144  -0.0082 106 GLU A CA  
870  C  C   . GLU A 106 ? 0.0812 0.1143 0.1169 -0.0031 0.0162  0.0137  106 GLU A C   
871  O  O   . GLU A 106 ? 0.0733 0.1451 0.1209 0.0129  0.0051  -0.0034 106 GLU A O   
872  C  CB  . GLU A 106 ? 0.1195 0.1247 0.0900 -0.0136 0.0127  0.0077  106 GLU A CB  
873  C  CG  . GLU A 106 ? 0.1647 0.1125 0.1027 -0.0151 0.0417  0.0039  106 GLU A CG  
874  C  CD  . GLU A 106 ? 0.1040 0.1336 0.1089 -0.0105 0.0355  0.0059  106 GLU A CD  
875  O  OE1 . GLU A 106 ? 0.0900 0.1435 0.1421 0.0004  0.0187  0.0027  106 GLU A OE1 
876  O  OE2 . GLU A 106 ? 0.0996 0.1697 0.1460 -0.0065 0.0370  -0.0026 106 GLU A OE2 
877  N  N   . HIS A 107 ? 0.0927 0.1159 0.1073 0.0046  0.0194  -0.0044 107 HIS A N   
878  C  CA  . HIS A 107 ? 0.0969 0.1200 0.0956 0.0152  0.0221  -0.0013 107 HIS A CA  
879  C  C   . HIS A 107 ? 0.0895 0.1206 0.1058 0.0117  0.0311  -0.0032 107 HIS A C   
880  O  O   . HIS A 107 ? 0.0999 0.1243 0.1146 0.0003  0.0225  0.0002  107 HIS A O   
881  C  CB  . HIS A 107 ? 0.0888 0.1139 0.1121 0.0050  0.0204  0.0017  107 HIS A CB  
882  C  CG  . HIS A 107 ? 0.0762 0.1155 0.1022 0.0122  0.0162  -0.0033 107 HIS A CG  
883  N  ND1 . HIS A 107 ? 0.0866 0.1267 0.1117 0.0173  0.0073  0.0106  107 HIS A ND1 
884  C  CD2 . HIS A 107 ? 0.0832 0.1152 0.1105 0.0140  0.0212  -0.0165 107 HIS A CD2 
885  C  CE1 . HIS A 107 ? 0.0930 0.1454 0.1107 0.0095  -0.0026 -0.0116 107 HIS A CE1 
886  N  NE2 . HIS A 107 ? 0.0868 0.1184 0.1076 0.0156  0.0095  0.0000  107 HIS A NE2 
887  N  N   . THR A 108 ? 0.1087 0.1230 0.1264 0.0035  0.0099  0.0225  108 THR A N   
888  C  CA  . THR A 108 ? 0.1031 0.1205 0.1370 0.0139  0.0362  0.0095  108 THR A CA  
889  C  C   . THR A 108 ? 0.0941 0.1264 0.1136 0.0052  0.0183  0.0066  108 THR A C   
890  O  O   . THR A 108 ? 0.1112 0.1332 0.1343 0.0131  0.0197  0.0031  108 THR A O   
891  C  CB  . THR A 108 ? 0.1225 0.1526 0.1002 0.0368  0.0055  -0.0041 108 THR A CB  
892  O  OG1 . THR A 108 ? 0.1339 0.1623 0.1212 0.0304  -0.0002 -0.0041 108 THR A OG1 
893  C  CG2 . THR A 108 ? 0.1430 0.2071 0.1058 0.0339  0.0279  -0.0089 108 THR A CG2 
894  N  N   . VAL A 109 ? 0.1227 0.1379 0.1278 -0.0018 0.0230  0.0331  109 VAL A N   
895  C  CA  . VAL A 109 ? 0.1257 0.1648 0.1343 0.0198  0.0300  0.0578  109 VAL A CA  
896  C  C   . VAL A 109 ? 0.1432 0.1392 0.1211 0.0052  0.0368  0.0340  109 VAL A C   
897  O  O   . VAL A 109 ? 0.1243 0.1367 0.1935 -0.0035 0.0408  0.0215  109 VAL A O   
898  C  CB  . VAL A 109 ? 0.1182 0.1687 0.1798 0.0153  0.0319  0.0431  109 VAL A CB  
899  C  CG1 . VAL A 109 ? 0.1375 0.2025 0.1911 0.0186  0.0512  0.0296  109 VAL A CG1 
900  C  CG2 . VAL A 109 ? 0.1688 0.1706 0.2032 0.0238  0.0060  0.0425  109 VAL A CG2 
901  N  N   . ASP A 110 ? 0.1867 0.1580 0.1037 0.0334  0.0512  0.0330  110 ASP A N   
902  C  CA  . ASP A 110 ? 0.1843 0.1910 0.1570 0.0702  0.0724  0.0763  110 ASP A CA  
903  C  C   . ASP A 110 ? 0.1791 0.1478 0.1638 0.0453  0.0541  0.0485  110 ASP A C   
904  O  O   . ASP A 110 ? 0.2373 0.1429 0.1918 0.0288  0.0512  0.0595  110 ASP A O   
905  C  CB  . ASP A 110 ? 0.2874 0.1787 0.1767 0.0038  0.1104  0.0519  110 ASP A CB  
906  C  CG  . ASP A 110 ? 0.3060 0.1699 0.1537 0.0289  0.0860  0.0488  110 ASP A CG  
907  O  OD1 . ASP A 110 ? 0.2951 0.1992 0.1889 0.0530  0.0989  0.0340  110 ASP A OD1 
908  O  OD2 . ASP A 110 ? 0.3195 0.2980 0.2421 0.0199  0.0754  0.0589  110 ASP A OD2 
909  N  N   . LYS A 111 ? 0.1613 0.1645 0.1424 0.0347  0.0414  0.0401  111 LYS A N   
910  C  CA  . LYS A 111 ? 0.1426 0.1738 0.1613 0.0533  0.0133  0.0038  111 LYS A CA  
911  C  C   . LYS A 111 ? 0.1771 0.1439 0.1451 0.0263  0.0023  0.0083  111 LYS A C   
912  O  O   . LYS A 111 ? 0.1695 0.1681 0.2187 0.0262  0.0476  0.0074  111 LYS A O   
913  C  CB  . LYS A 111 ? 0.1798 0.2128 0.2099 0.0811  -0.0040 0.0244  111 LYS A CB  
914  C  CG  . LYS A 111 ? 0.2676 0.3147 0.2062 0.0770  -0.0341 0.0137  111 LYS A CG  
915  C  CD  . LYS A 111 ? 0.2764 0.3607 0.2642 0.0430  -0.0771 -0.0381 111 LYS A CD  
916  C  CE  . LYS A 111 ? 0.4000 0.4939 0.2591 0.1285  -0.0992 -0.1335 111 LYS A CE  
917  N  NZ  . LYS A 111 ? 0.3283 0.5177 0.3968 -0.0594 0.0136  0.1280  111 LYS A NZ  
918  N  N   . LYS A 112 ? 0.1812 0.1121 0.1703 0.0226  -0.0009 0.0150  112 LYS A N   
919  C  CA  . LYS A 112 ? 0.1399 0.1376 0.1616 -0.0097 0.0372  0.0097  112 LYS A CA  
920  C  C   . LYS A 112 ? 0.1085 0.1637 0.1461 0.0488  0.0127  0.0279  112 LYS A C   
921  O  O   . LYS A 112 ? 0.1304 0.1418 0.1573 0.0193  0.0240  0.0094  112 LYS A O   
922  C  CB  . LYS A 112 ? 0.1361 0.2130 0.2068 -0.0267 0.0055  0.0016  112 LYS A CB  
923  C  CG  . LYS A 112 ? 0.1741 0.2694 0.2179 -0.0656 0.0356  -0.0632 112 LYS A CG  
924  C  CD  . LYS A 112 ? 0.1734 0.3152 0.3102 -0.0340 -0.0279 -0.0198 112 LYS A CD  
925  C  CE  . LYS A 112 ? 0.2136 0.4334 0.2741 0.0588  -0.0250 0.0660  112 LYS A CE  
926  N  NZ  . LYS A 112 ? 0.4209 0.3512 0.4395 0.1125  -0.1267 0.0739  112 LYS A NZ  
927  N  N   A LYS A 113 ? 0.1202 0.1597 0.1364 0.0225  0.0239  0.0242  113 LYS A N   
928  N  N   B LYS A 113 ? 0.1278 0.1643 0.1383 0.0241  0.0293  0.0253  113 LYS A N   
929  C  CA  A LYS A 113 ? 0.1275 0.1551 0.1289 0.0163  0.0035  0.0167  113 LYS A CA  
930  C  CA  B LYS A 113 ? 0.1389 0.1615 0.1353 0.0218  0.0084  0.0229  113 LYS A CA  
931  C  C   A LYS A 113 ? 0.1144 0.1093 0.1681 -0.0077 0.0016  0.0206  113 LYS A C   
932  C  C   B LYS A 113 ? 0.1268 0.1162 0.1568 0.0105  0.0115  0.0160  113 LYS A C   
933  O  O   A LYS A 113 ? 0.1552 0.1263 0.2015 -0.0139 -0.0222 0.0088  113 LYS A O   
934  O  O   B LYS A 113 ? 0.2216 0.1253 0.2399 0.0102  -0.0300 0.0117  113 LYS A O   
935  C  CB  A LYS A 113 ? 0.1177 0.1720 0.1401 0.0265  0.0032  0.0033  113 LYS A CB  
936  C  CB  B LYS A 113 ? 0.1467 0.1534 0.1443 0.0461  0.0121  0.0038  113 LYS A CB  
937  C  CG  A LYS A 113 ? 0.1198 0.1676 0.1399 0.0193  0.0096  -0.0113 113 LYS A CG  
938  C  CG  B LYS A 113 ? 0.1720 0.2078 0.1087 0.0300  0.0130  0.0060  113 LYS A CG  
939  C  CD  A LYS A 113 ? 0.1184 0.2258 0.1364 0.0245  0.0114  -0.0229 113 LYS A CD  
940  C  CD  B LYS A 113 ? 0.1491 0.1881 0.2103 0.0323  -0.0038 -0.0089 113 LYS A CD  
941  C  CE  A LYS A 113 ? 0.1182 0.2428 0.1782 0.0003  -0.0038 0.0282  113 LYS A CE  
942  C  CE  B LYS A 113 ? 0.1509 0.2451 0.1740 0.0098  0.0023  0.0051  113 LYS A CE  
943  N  NZ  A LYS A 113 ? 0.1169 0.2884 0.1723 0.0158  -0.0147 0.0319  113 LYS A NZ  
944  N  NZ  B LYS A 113 ? 0.1568 0.2309 0.3016 0.0104  0.0337  -0.0155 113 LYS A NZ  
945  N  N   . TYR A 114 ? 0.1139 0.1155 0.1383 0.0080  -0.0061 0.0106  114 TYR A N   
946  C  CA  . TYR A 114 ? 0.1177 0.1232 0.1189 0.0108  0.0061  -0.0085 114 TYR A CA  
947  C  C   . TYR A 114 ? 0.1199 0.1075 0.1169 -0.0159 0.0099  -0.0105 114 TYR A C   
948  O  O   . TYR A 114 ? 0.1227 0.1253 0.1546 -0.0175 0.0016  -0.0063 114 TYR A O   
949  C  CB  . TYR A 114 ? 0.1006 0.1097 0.1485 0.0046  0.0260  0.0103  114 TYR A CB  
950  C  CG  . TYR A 114 ? 0.1200 0.1078 0.1351 -0.0145 0.0190  0.0143  114 TYR A CG  
951  C  CD1 . TYR A 114 ? 0.1694 0.1566 0.1336 0.0175  0.0362  0.0055  114 TYR A CD1 
952  C  CD2 . TYR A 114 ? 0.1087 0.1132 0.1981 -0.0106 0.0564  -0.0021 114 TYR A CD2 
953  C  CE1 . TYR A 114 ? 0.1913 0.1884 0.1443 0.0196  0.0406  0.0309  114 TYR A CE1 
954  C  CE2 . TYR A 114 ? 0.1746 0.1947 0.1874 0.0129  0.0796  0.0392  114 TYR A CE2 
955  C  CZ  . TYR A 114 ? 0.1842 0.2071 0.1705 0.0103  0.0823  0.0316  114 TYR A CZ  
956  O  OH  . TYR A 114 ? 0.2720 0.3525 0.2196 0.0263  0.1266  0.0631  114 TYR A OH  
957  N  N   . ALA A 115 ? 0.1213 0.1164 0.1310 0.0035  -0.0087 -0.0051 115 ALA A N   
958  C  CA  . ALA A 115 ? 0.1390 0.0908 0.1247 -0.0055 -0.0024 -0.0188 115 ALA A CA  
959  C  C   . ALA A 115 ? 0.1496 0.0974 0.1311 0.0179  0.0081  0.0055  115 ALA A C   
960  O  O   . ALA A 115 ? 0.1356 0.1282 0.1354 0.0026  0.0201  -0.0054 115 ALA A O   
961  C  CB  . ALA A 115 ? 0.1112 0.1408 0.1737 0.0009  -0.0229 -0.0217 115 ALA A CB  
962  N  N   . ALA A 116 ? 0.1168 0.0873 0.1375 0.0001  0.0087  -0.0006 116 ALA A N   
963  C  CA  . ALA A 116 ? 0.1074 0.0992 0.1094 -0.0019 0.0157  0.0058  116 ALA A CA  
964  C  C   . ALA A 116 ? 0.0884 0.1128 0.1170 0.0104  0.0122  0.0074  116 ALA A C   
965  O  O   . ALA A 116 ? 0.1051 0.1232 0.1115 -0.0127 0.0133  0.0088  116 ALA A O   
966  C  CB  . ALA A 116 ? 0.1157 0.1457 0.1173 -0.0055 0.0055  0.0012  116 ALA A CB  
967  N  N   . GLU A 117 ? 0.1087 0.1011 0.1143 0.0078  0.0086  0.0044  117 GLU A N   
968  C  CA  . GLU A 117 ? 0.1073 0.0944 0.1076 0.0049  -0.0044 0.0025  117 GLU A CA  
969  C  C   . GLU A 117 ? 0.1125 0.1132 0.1099 0.0009  0.0163  0.0175  117 GLU A C   
970  O  O   . GLU A 117 ? 0.1213 0.1295 0.1273 -0.0018 0.0309  0.0194  117 GLU A O   
971  C  CB  . GLU A 117 ? 0.1098 0.1426 0.0825 -0.0039 0.0070  0.0017  117 GLU A CB  
972  C  CG  . GLU A 117 ? 0.0999 0.1324 0.1017 0.0052  0.0119  0.0078  117 GLU A CG  
973  C  CD  . GLU A 117 ? 0.1094 0.1363 0.1231 0.0078  0.0027  0.0144  117 GLU A CD  
974  O  OE1 . GLU A 117 ? 0.0933 0.1461 0.1203 0.0099  0.0034  0.0118  117 GLU A OE1 
975  O  OE2 . GLU A 117 ? 0.1641 0.1483 0.1071 0.0001  -0.0136 0.0091  117 GLU A OE2 
976  N  N   . LEU A 118 ? 0.1121 0.0936 0.1159 0.0061  -0.0041 0.0050  118 LEU A N   
977  C  CA  . LEU A 118 ? 0.0990 0.0934 0.1238 -0.0063 -0.0044 0.0024  118 LEU A CA  
978  C  C   . LEU A 118 ? 0.1175 0.1014 0.0941 0.0073  -0.0087 0.0143  118 LEU A C   
979  O  O   . LEU A 118 ? 0.1163 0.1110 0.0977 0.0005  0.0027  0.0121  118 LEU A O   
980  C  CB  . LEU A 118 ? 0.0956 0.1163 0.1587 -0.0050 -0.0205 0.0188  118 LEU A CB  
981  C  CG  . LEU A 118 ? 0.1302 0.1185 0.1386 0.0091  -0.0271 0.0206  118 LEU A CG  
982  C  CD1 . LEU A 118 ? 0.1788 0.1404 0.1383 -0.0179 -0.0365 0.0293  118 LEU A CD1 
983  C  CD2 . LEU A 118 ? 0.1439 0.1898 0.1595 -0.0089 -0.0557 0.0034  118 LEU A CD2 
984  N  N   . HIS A 119 ? 0.1085 0.0923 0.1080 -0.0043 -0.0142 0.0097  119 HIS A N   
985  C  CA  . HIS A 119 ? 0.1033 0.1017 0.1164 -0.0137 -0.0076 0.0093  119 HIS A CA  
986  C  C   . HIS A 119 ? 0.0812 0.1120 0.1142 -0.0074 -0.0165 -0.0003 119 HIS A C   
987  O  O   . HIS A 119 ? 0.1307 0.1199 0.1152 0.0084  -0.0115 0.0135  119 HIS A O   
988  C  CB  . HIS A 119 ? 0.0825 0.1408 0.1045 0.0066  0.0053  0.0201  119 HIS A CB  
989  C  CG  . HIS A 119 ? 0.0834 0.1307 0.0805 0.0036  0.0073  -0.0040 119 HIS A CG  
990  N  ND1 . HIS A 119 ? 0.0798 0.1412 0.0976 -0.0044 0.0162  0.0057  119 HIS A ND1 
991  C  CD2 . HIS A 119 ? 0.1221 0.1310 0.0737 0.0211  0.0019  0.0119  119 HIS A CD2 
992  C  CE1 . HIS A 119 ? 0.1186 0.1361 0.0796 -0.0220 -0.0047 -0.0018 119 HIS A CE1 
993  N  NE2 . HIS A 119 ? 0.0952 0.1279 0.1008 0.0108  0.0020  0.0021  119 HIS A NE2 
994  N  N   . LEU A 120 ? 0.0895 0.1051 0.1098 -0.0013 -0.0209 0.0030  120 LEU A N   
995  C  CA  . LEU A 120 ? 0.1042 0.0996 0.1310 -0.0041 -0.0100 0.0099  120 LEU A CA  
996  C  C   . LEU A 120 ? 0.1051 0.0845 0.1123 0.0225  -0.0098 0.0088  120 LEU A C   
997  O  O   . LEU A 120 ? 0.0993 0.1103 0.1117 0.0000  -0.0107 0.0149  120 LEU A O   
998  C  CB  . LEU A 120 ? 0.1112 0.1153 0.1304 -0.0091 -0.0036 0.0010  120 LEU A CB  
999  C  CG  . LEU A 120 ? 0.1209 0.1371 0.1383 -0.0089 -0.0347 0.0047  120 LEU A CG  
1000 C  CD1 . LEU A 120 ? 0.1832 0.1469 0.2270 -0.0628 -0.0166 0.0145  120 LEU A CD1 
1001 C  CD2 . LEU A 120 ? 0.1554 0.1838 0.1626 -0.0005 -0.0707 0.0042  120 LEU A CD2 
1002 N  N   . VAL A 121 ? 0.1250 0.1085 0.1186 -0.0143 -0.0155 0.0197  121 VAL A N   
1003 C  CA  . VAL A 121 ? 0.1107 0.1033 0.1430 -0.0175 0.0150  0.0026  121 VAL A CA  
1004 C  C   . VAL A 121 ? 0.1512 0.1013 0.1351 -0.0062 -0.0206 0.0088  121 VAL A C   
1005 O  O   . VAL A 121 ? 0.1803 0.1286 0.1245 -0.0109 -0.0234 0.0195  121 VAL A O   
1006 C  CB  . VAL A 121 ? 0.0943 0.1268 0.1318 0.0039  0.0067  0.0054  121 VAL A CB  
1007 C  CG1 . VAL A 121 ? 0.0968 0.1485 0.1706 -0.0245 0.0113  0.0160  121 VAL A CG1 
1008 C  CG2 . VAL A 121 ? 0.1681 0.1260 0.1383 0.0154  0.0340  0.0140  121 VAL A CG2 
1009 N  N   . HIS A 122 ? 0.0986 0.0988 0.1527 -0.0143 -0.0164 -0.0022 122 HIS A N   
1010 C  CA  . HIS A 122 ? 0.1088 0.0959 0.1590 -0.0155 0.0026  0.0015  122 HIS A CA  
1011 C  C   . HIS A 122 ? 0.1164 0.0978 0.1404 -0.0160 -0.0133 0.0105  122 HIS A C   
1012 O  O   . HIS A 122 ? 0.1282 0.1101 0.1641 -0.0067 -0.0294 0.0231  122 HIS A O   
1013 C  CB  . HIS A 122 ? 0.1026 0.1073 0.1580 -0.0100 0.0048  0.0086  122 HIS A CB  
1014 C  CG  . HIS A 122 ? 0.1176 0.1021 0.1643 -0.0146 0.0009  0.0131  122 HIS A CG  
1015 N  ND1 . HIS A 122 ? 0.1188 0.1023 0.1802 0.0003  -0.0062 0.0097  122 HIS A ND1 
1016 C  CD2 . HIS A 122 ? 0.1297 0.1353 0.1746 -0.0287 -0.0181 0.0088  122 HIS A CD2 
1017 C  CE1 . HIS A 122 ? 0.1018 0.1300 0.1939 0.0136  -0.0179 -0.0076 122 HIS A CE1 
1018 N  NE2 . HIS A 122 ? 0.1008 0.1368 0.1842 -0.0085 -0.0308 0.0002  122 HIS A NE2 
1019 N  N   . TRP A 123 ? 0.1296 0.0918 0.1436 -0.0131 -0.0147 0.0000  123 TRP A N   
1020 C  CA  . TRP A 123 ? 0.1214 0.0846 0.1652 -0.0222 -0.0032 -0.0077 123 TRP A CA  
1021 C  C   . TRP A 123 ? 0.1032 0.1264 0.1587 -0.0063 -0.0118 -0.0094 123 TRP A C   
1022 O  O   . TRP A 123 ? 0.1114 0.1284 0.2295 -0.0021 -0.0336 0.0075  123 TRP A O   
1023 C  CB  . TRP A 123 ? 0.1392 0.1534 0.1537 -0.0403 -0.0168 0.0262  123 TRP A CB  
1024 C  CG  . TRP A 123 ? 0.1728 0.1333 0.1540 -0.0167 -0.0210 0.0004  123 TRP A CG  
1025 C  CD1 . TRP A 123 ? 0.2651 0.1482 0.1333 -0.0259 -0.0381 0.0153  123 TRP A CD1 
1026 C  CD2 . TRP A 123 ? 0.2797 0.1150 0.1482 -0.0431 -0.0479 0.0237  123 TRP A CD2 
1027 N  NE1 . TRP A 123 ? 0.3033 0.1296 0.2001 -0.0604 -0.0734 0.0307  123 TRP A NE1 
1028 C  CE2 . TRP A 123 ? 0.3095 0.1221 0.1694 -0.0347 -0.0573 0.0362  123 TRP A CE2 
1029 C  CE3 . TRP A 123 ? 0.2511 0.1078 0.1796 -0.0420 -0.0406 0.0185  123 TRP A CE3 
1030 C  CZ2 . TRP A 123 ? 0.3732 0.1345 0.1852 -0.0253 -0.0952 0.0304  123 TRP A CZ2 
1031 C  CZ3 . TRP A 123 ? 0.3409 0.1267 0.2074 -0.0418 -0.0639 0.0363  123 TRP A CZ3 
1032 C  CH2 . TRP A 123 ? 0.3782 0.1408 0.1677 -0.0627 -0.0439 0.0177  123 TRP A CH2 
1033 N  N   . ASN A 124 ? 0.1234 0.1146 0.1631 -0.0079 -0.0089 -0.0283 124 ASN A N   
1034 C  CA  . ASN A 124 ? 0.1758 0.1006 0.2024 0.0146  -0.0042 -0.0312 124 ASN A CA  
1035 C  C   . ASN A 124 ? 0.1486 0.1117 0.1731 -0.0044 -0.0030 -0.0297 124 ASN A C   
1036 O  O   . ASN A 124 ? 0.1273 0.1311 0.1834 -0.0013 0.0069  -0.0258 124 ASN A O   
1037 C  CB  . ASN A 124 ? 0.1633 0.1661 0.1557 -0.0135 0.0436  -0.0231 124 ASN A CB  
1038 C  CG  . ASN A 124 ? 0.1879 0.1458 0.1972 0.0058  0.0632  -0.0108 124 ASN A CG  
1039 O  OD1 . ASN A 124 ? 0.1773 0.1551 0.2614 0.0113  0.0678  -0.0257 124 ASN A OD1 
1040 N  ND2 . ASN A 124 ? 0.2216 0.1651 0.1860 0.0023  0.0366  -0.0034 124 ASN A ND2 
1041 N  N   . THR A 125 ? 0.1410 0.1194 0.2543 0.0107  -0.0037 -0.0072 125 THR A N   
1042 C  CA  . THR A 125 ? 0.1353 0.1096 0.2648 0.0130  -0.0190 -0.0164 125 THR A CA  
1043 C  C   . THR A 125 ? 0.1329 0.1263 0.2700 0.0174  0.0215  -0.0266 125 THR A C   
1044 O  O   . THR A 125 ? 0.1523 0.1487 0.2951 0.0280  0.0055  0.0047  125 THR A O   
1045 C  CB  . THR A 125 ? 0.1450 0.1584 0.3834 0.0098  -0.0573 -0.0300 125 THR A CB  
1046 O  OG1 . THR A 125 ? 0.1454 0.1988 0.4646 0.0325  0.0154  -0.0272 125 THR A OG1 
1047 C  CG2 . THR A 125 ? 0.2310 0.1662 0.4216 -0.0034 -0.1360 -0.0008 125 THR A CG2 
1048 N  N   . LYS A 126 ? 0.1457 0.1429 0.2312 0.0110  0.0502  -0.0350 127 LYS A N   
1049 C  CA  . LYS A 126 ? 0.2295 0.1842 0.2478 -0.0303 0.0652  -0.0713 127 LYS A CA  
1050 C  C   . LYS A 126 ? 0.1904 0.1343 0.2414 0.0012  0.0324  -0.0488 127 LYS A C   
1051 O  O   . LYS A 126 ? 0.1992 0.1426 0.3307 -0.0212 0.0478  -0.0570 127 LYS A O   
1052 C  CB  . LYS A 126 ? 0.2972 0.1791 0.2575 -0.0410 0.0420  -0.0571 127 LYS A CB  
1053 C  CG  . LYS A 126 ? 0.2660 0.2680 0.2306 -0.0200 0.0306  -0.0789 127 LYS A CG  
1054 C  CD  . LYS A 126 ? 0.4884 0.3255 0.2234 -0.0950 0.0638  -0.0789 127 LYS A CD  
1055 C  CE  . LYS A 126 ? 0.4961 0.6676 0.3470 0.0210  0.0651  0.0171  127 LYS A CE  
1056 N  NZ  . LYS A 126 ? 0.6918 0.4027 0.3366 -0.0925 -0.0785 0.0190  127 LYS A NZ  
1057 N  N   . TYR A 127 ? 0.1322 0.1223 0.1609 0.0088  0.0113  -0.0165 128 TYR A N   
1058 C  CA  . TYR A 127 ? 0.1221 0.1272 0.1565 -0.0103 -0.0077 -0.0105 128 TYR A CA  
1059 C  C   . TYR A 127 ? 0.1566 0.1120 0.1641 -0.0160 -0.0065 -0.0174 128 TYR A C   
1060 O  O   . TYR A 127 ? 0.1518 0.1514 0.2142 -0.0179 0.0044  0.0054  128 TYR A O   
1061 C  CB  . TYR A 127 ? 0.1582 0.1400 0.1577 0.0116  -0.0052 -0.0117 128 TYR A CB  
1062 C  CG  . TYR A 127 ? 0.1692 0.1304 0.1414 0.0133  -0.0145 -0.0225 128 TYR A CG  
1063 C  CD1 . TYR A 127 ? 0.2035 0.1512 0.2238 -0.0058 -0.0372 -0.0467 128 TYR A CD1 
1064 C  CD2 . TYR A 127 ? 0.1612 0.1401 0.1697 0.0085  0.0163  -0.0100 128 TYR A CD2 
1065 C  CE1 . TYR A 127 ? 0.2608 0.1396 0.2092 0.0203  -0.0167 -0.0411 128 TYR A CE1 
1066 C  CE2 . TYR A 127 ? 0.1997 0.1648 0.1480 0.0272  0.0296  -0.0510 128 TYR A CE2 
1067 C  CZ  . TYR A 127 ? 0.2205 0.1579 0.1421 0.0234  0.0250  -0.0445 128 TYR A CZ  
1068 O  OH  . TYR A 127 ? 0.3093 0.1838 0.1494 0.0332  0.0002  -0.0419 128 TYR A OH  
1069 N  N   . GLY A 128 ? 0.1630 0.1137 0.1744 0.0111  -0.0027 0.0086  129 GLY A N   
1070 C  CA  . GLY A 128 ? 0.1963 0.1313 0.1662 0.0037  0.0108  0.0245  129 GLY A CA  
1071 C  C   . GLY A 128 ? 0.2124 0.1234 0.1989 -0.0089 -0.0018 0.0134  129 GLY A C   
1072 O  O   . GLY A 128 ? 0.3110 0.1733 0.1800 0.0013  -0.0326 0.0275  129 GLY A O   
1073 N  N   . ASP A 129 ? 0.2864 0.1514 0.1618 0.0432  -0.0013 0.0000  130 ASP A N   
1074 C  CA  . ASP A 129 ? 0.3486 0.1430 0.1353 0.0296  0.0405  0.0081  130 ASP A CA  
1075 C  C   . ASP A 129 ? 0.3033 0.2013 0.1577 0.0294  -0.0165 0.0050  130 ASP A C   
1076 O  O   . ASP A 129 ? 0.2737 0.2011 0.1501 0.0722  0.0093  0.0183  130 ASP A O   
1077 C  CB  . ASP A 129 ? 0.4877 0.2028 0.2014 0.0831  0.1317  0.0477  130 ASP A CB  
1078 C  CG  . ASP A 129 ? 0.4222 0.2460 0.3653 0.1564  0.2075  -0.0113 130 ASP A CG  
1079 O  OD1 . ASP A 129 ? 0.4402 0.2888 0.3440 0.1247  0.1367  0.1125  130 ASP A OD1 
1080 O  OD2 . ASP A 129 ? 0.3972 0.3128 0.6498 0.1113  0.0977  0.1681  130 ASP A OD2 
1081 N  N   . ALA A 130 ? 0.4300 0.1622 0.1286 0.0314  0.0724  0.0234  131 ALA A N   
1082 C  CA  . ALA A 130 ? 0.3251 0.1976 0.1509 0.0429  0.0444  0.0194  131 ALA A CA  
1083 C  C   . ALA A 130 ? 0.2916 0.2053 0.1518 0.0089  0.0565  0.0242  131 ALA A C   
1084 O  O   . ALA A 130 ? 0.2599 0.1778 0.1300 0.0153  0.0469  0.0153  131 ALA A O   
1085 C  CB  . ALA A 130 ? 0.3926 0.2128 0.2129 -0.0258 0.0859  -0.0326 131 ALA A CB  
1086 N  N   . GLY A 131 ? 0.3482 0.2086 0.1670 0.0186  0.1039  0.0170  132 GLY A N   
1087 C  CA  . GLY A 131 ? 0.3371 0.2205 0.2252 0.0113  0.0988  0.0054  132 GLY A CA  
1088 C  C   . GLY A 131 ? 0.2154 0.1555 0.2530 -0.0238 0.0769  0.0207  132 GLY A C   
1089 O  O   . GLY A 131 ? 0.2302 0.2584 0.2961 0.0057  0.0895  0.0438  132 GLY A O   
1090 N  N   A LYS A 132 ? 0.2306 0.1728 0.2410 -0.0138 0.0877  0.0133  133 LYS A N   
1091 N  N   B LYS A 132 ? 0.1759 0.1534 0.2657 -0.0361 0.0871  0.0254  133 LYS A N   
1092 N  N   C LYS A 132 ? 0.1746 0.1749 0.2614 -0.0324 0.1310  0.0291  133 LYS A N   
1093 C  CA  A LYS A 132 ? 0.2157 0.1655 0.2239 -0.0091 0.0446  0.0265  133 LYS A CA  
1094 C  CA  B LYS A 132 ? 0.1199 0.1221 0.2588 -0.0178 0.0290  0.0322  133 LYS A CA  
1095 C  CA  C LYS A 132 ? 0.2155 0.1835 0.2532 -0.0110 0.0494  0.0255  133 LYS A CA  
1096 C  C   A LYS A 132 ? 0.1404 0.1500 0.1918 -0.0005 0.0131  0.0116  133 LYS A C   
1097 C  C   B LYS A 132 ? 0.1284 0.1680 0.2201 -0.0150 0.0403  0.0156  133 LYS A C   
1098 C  C   C LYS A 132 ? 0.1328 0.1746 0.2196 -0.0040 0.0166  0.0085  133 LYS A C   
1099 O  O   A LYS A 132 ? 0.1473 0.1421 0.2126 -0.0265 -0.0205 -0.0018 133 LYS A O   
1100 O  O   B LYS A 132 ? 0.0995 0.2082 0.2123 0.0015  0.0586  -0.0103 133 LYS A O   
1101 O  O   C LYS A 132 ? 0.1647 0.1401 0.2231 0.0000  -0.0001 0.0022  133 LYS A O   
1102 C  CB  A LYS A 132 ? 0.2190 0.1676 0.2025 -0.0078 0.0396  0.0070  133 LYS A CB  
1103 C  CB  B LYS A 132 ? 0.0706 0.1066 0.2532 -0.0419 0.0181  0.0573  133 LYS A CB  
1104 C  CB  C LYS A 132 ? 0.1040 0.2328 0.2678 0.0252  0.0304  -0.0223 133 LYS A CB  
1105 C  CG  A LYS A 132 ? 0.2164 0.2198 0.1828 0.0253  0.0292  0.0218  133 LYS A CG  
1106 C  CG  B LYS A 132 ? 0.0617 0.1620 0.2874 -0.0282 0.0717  0.1012  133 LYS A CG  
1107 C  CG  C LYS A 132 ? 0.1963 0.2520 0.2281 -0.0003 0.0017  0.0233  133 LYS A CG  
1108 C  CD  A LYS A 132 ? 0.2374 0.1947 0.0960 0.0361  0.0499  0.0269  133 LYS A CD  
1109 C  CD  B LYS A 132 ? 0.0939 0.1527 0.2987 0.0080  0.0170  0.1507  133 LYS A CD  
1110 C  CD  C LYS A 132 ? 0.3251 0.4356 0.2575 -0.0778 -0.1434 -0.0308 133 LYS A CD  
1111 C  CE  A LYS A 132 ? 0.1653 0.2209 0.0170 0.0412  0.0406  0.0177  133 LYS A CE  
1112 C  CE  C LYS A 132 ? 0.3243 0.2435 0.3012 -0.1033 -0.1514 -0.0219 133 LYS A CE  
1113 N  N   . ALA A 133 ? 0.1448 0.1465 0.1699 -0.0155 0.0462  0.0073  134 ALA A N   
1114 C  CA  . ALA A 133 ? 0.1238 0.1436 0.1579 -0.0078 0.0267  0.0102  134 ALA A CA  
1115 C  C   . ALA A 133 ? 0.1186 0.1568 0.1764 0.0002  0.0153  -0.0008 134 ALA A C   
1116 O  O   . ALA A 133 ? 0.1214 0.1812 0.1659 -0.0181 0.0186  0.0006  134 ALA A O   
1117 C  CB  . ALA A 133 ? 0.1451 0.1435 0.1600 -0.0290 -0.0004 0.0217  134 ALA A CB  
1118 N  N   . SER A 134 ? 0.1810 0.1443 0.1674 0.0211  0.0413  0.0050  135 SER A N   
1119 C  CA  . SER A 134 ? 0.1706 0.1946 0.1591 0.0480  0.0330  0.0074  135 SER A CA  
1120 C  C   . SER A 134 ? 0.1151 0.1871 0.2035 0.0030  0.0633  0.0248  135 SER A C   
1121 O  O   . SER A 134 ? 0.1543 0.2258 0.2685 0.0154  0.0625  0.0696  135 SER A O   
1122 C  CB  . SER A 134 ? 0.3064 0.2263 0.1792 0.0613  0.1391  0.0381  135 SER A CB  
1123 O  OG  . SER A 134 ? 0.2667 0.2909 0.2456 0.0637  0.0996  0.0366  135 SER A OG  
1124 N  N   . GLN A 135 ? 0.1440 0.1859 0.1886 -0.0205 0.0567  0.0071  136 GLN A N   
1125 C  CA  . GLN A 135 ? 0.1681 0.2044 0.2687 -0.0200 0.0077  0.0211  136 GLN A CA  
1126 C  C   . GLN A 135 ? 0.1447 0.1916 0.2473 -0.0055 -0.0325 0.0221  136 GLN A C   
1127 O  O   . GLN A 135 ? 0.1753 0.2943 0.2813 -0.0336 -0.0489 0.0097  136 GLN A O   
1128 C  CB  . GLN A 135 ? 0.1857 0.2885 0.3477 -0.1055 0.0413  0.0274  136 GLN A CB  
1129 C  CG  . GLN A 135 ? 0.2008 0.3297 0.3594 -0.0506 0.0732  0.0337  136 GLN A CG  
1130 C  CD  . GLN A 135 ? 0.2117 0.6022 0.5360 0.0243  0.1465  -0.0595 136 GLN A CD  
1131 O  OE1 . GLN A 135 ? 0.3392 0.7661 0.7207 0.0163  -0.0036 0.0000  136 GLN A OE1 
1132 N  NE2 . GLN A 135 ? 0.4285 0.5564 0.5946 -0.0496 0.0912  0.0081  136 GLN A NE2 
1133 N  N   . GLN A 136 ? 0.1529 0.1767 0.1746 0.0000  0.0262  -0.0029 137 GLN A N   
1134 C  CA  . GLN A 136 ? 0.1751 0.1787 0.1367 -0.0019 -0.0256 -0.0306 137 GLN A CA  
1135 C  C   . GLN A 136 ? 0.1590 0.1985 0.1329 0.0023  0.0192  -0.0334 137 GLN A C   
1136 O  O   . GLN A 136 ? 0.1609 0.1778 0.1428 0.0222  0.0026  -0.0326 137 GLN A O   
1137 C  CB  . GLN A 136 ? 0.1723 0.1810 0.1971 0.0099  0.0091  -0.0050 137 GLN A CB  
1138 C  CG  . GLN A 136 ? 0.2385 0.2069 0.2197 0.0036  0.0127  0.0147  137 GLN A CG  
1139 C  CD  . GLN A 136 ? 0.2450 0.2008 0.3201 0.0025  -0.0122 0.0527  137 GLN A CD  
1140 O  OE1 . GLN A 136 ? 0.3274 0.1900 0.2840 -0.0359 0.0194  -0.0430 137 GLN A OE1 
1141 N  NE2 . GLN A 136 ? 0.2935 0.3468 0.4819 -0.0312 0.0747  0.1192  137 GLN A NE2 
1142 N  N   . PRO A 137 ? 0.1521 0.2063 0.1390 0.0245  -0.0210 -0.0336 138 PRO A N   
1143 C  CA  . PRO A 137 ? 0.2063 0.1999 0.1116 0.0545  -0.0207 -0.0171 138 PRO A CA  
1144 C  C   . PRO A 137 ? 0.2205 0.2046 0.1254 0.0328  0.0195  0.0006  138 PRO A C   
1145 O  O   . PRO A 137 ? 0.2529 0.1881 0.2230 0.0269  0.0263  0.0252  138 PRO A O   
1146 C  CB  . PRO A 137 ? 0.3303 0.3133 0.0769 0.0567  0.0013  -0.0011 138 PRO A CB  
1147 C  CG  . PRO A 137 ? 0.3969 0.3525 0.1342 -0.0315 -0.0847 -0.0752 138 PRO A CG  
1148 C  CD  . PRO A 137 ? 0.2241 0.3023 0.1383 0.0119  -0.0525 -0.0844 138 PRO A CD  
1149 N  N   . ASP A 138 ? 0.1681 0.1850 0.1245 0.0110  0.0044  -0.0011 139 ASP A N   
1150 C  CA  . ASP A 138 ? 0.1623 0.2506 0.1281 0.0095  0.0266  0.0126  139 ASP A CA  
1151 C  C   . ASP A 138 ? 0.1503 0.1978 0.1289 -0.0010 0.0200  -0.0130 139 ASP A C   
1152 O  O   . ASP A 138 ? 0.1544 0.1979 0.1522 0.0013  0.0034  0.0040  139 ASP A O   
1153 C  CB  . ASP A 138 ? 0.2639 0.2566 0.1114 0.0390  0.0192  -0.0287 139 ASP A CB  
1154 C  CG  . ASP A 138 ? 0.2471 0.2917 0.1726 0.0797  0.0100  -0.0425 139 ASP A CG  
1155 O  OD1 . ASP A 138 ? 0.2630 0.2261 0.1814 0.0508  -0.0204 -0.0553 139 ASP A OD1 
1156 O  OD2 . ASP A 138 ? 0.2757 0.3400 0.2442 0.0822  0.0533  -0.0878 139 ASP A OD2 
1157 N  N   . GLY A 139 ? 0.1394 0.1451 0.1003 -0.0175 0.0099  -0.0099 140 GLY A N   
1158 C  CA  . GLY A 139 ? 0.1425 0.1383 0.1024 -0.0091 -0.0055 -0.0048 140 GLY A CA  
1159 C  C   . GLY A 139 ? 0.1093 0.1250 0.1065 0.0021  0.0096  0.0046  140 GLY A C   
1160 O  O   . GLY A 139 ? 0.1234 0.1153 0.1318 0.0137  0.0006  0.0025  140 GLY A O   
1161 N  N   . LEU A 140 ? 0.1069 0.1078 0.1473 -0.0078 -0.0001 -0.0041 141 LEU A N   
1162 C  CA  . LEU A 140 ? 0.0884 0.0988 0.1302 -0.0044 0.0062  0.0012  141 LEU A CA  
1163 C  C   . LEU A 140 ? 0.0909 0.0979 0.1162 0.0015  0.0000  0.0000  141 LEU A C   
1164 O  O   . LEU A 140 ? 0.1056 0.1234 0.1159 -0.0089 -0.0011 0.0121  141 LEU A O   
1165 C  CB  . LEU A 140 ? 0.1148 0.1324 0.1264 0.0144  0.0132  0.0068  141 LEU A CB  
1166 C  CG  . LEU A 140 ? 0.1449 0.1541 0.1720 0.0355  0.0622  0.0260  141 LEU A CG  
1167 C  CD1 . LEU A 140 ? 0.1516 0.1606 0.2065 0.0511  0.0574  0.0041  141 LEU A CD1 
1168 C  CD2 . LEU A 140 ? 0.2215 0.1460 0.1615 0.0138  0.0337  0.0272  141 LEU A CD2 
1169 N  N   . ALA A 141 ? 0.0902 0.1029 0.1295 -0.0046 -0.0098 -0.0120 142 ALA A N   
1170 C  CA  . ALA A 141 ? 0.0974 0.1069 0.1478 -0.0089 0.0070  -0.0100 142 ALA A CA  
1171 C  C   . ALA A 141 ? 0.0838 0.1182 0.1179 -0.0168 -0.0046 0.0124  142 ALA A C   
1172 O  O   . ALA A 141 ? 0.1171 0.1170 0.1230 -0.0029 -0.0226 0.0130  142 ALA A O   
1173 C  CB  . ALA A 141 ? 0.1006 0.1329 0.1706 -0.0001 0.0174  0.0039  142 ALA A CB  
1174 N  N   . VAL A 142 ? 0.0848 0.1111 0.1367 -0.0026 0.0132  -0.0010 143 VAL A N   
1175 C  CA  . VAL A 142 ? 0.0830 0.1252 0.1221 -0.0038 0.0275  -0.0043 143 VAL A CA  
1176 C  C   . VAL A 142 ? 0.0848 0.1080 0.1024 -0.0024 -0.0010 0.0223  143 VAL A C   
1177 O  O   . VAL A 142 ? 0.0956 0.1267 0.0929 -0.0062 0.0063  0.0078  143 VAL A O   
1178 C  CB  . VAL A 142 ? 0.0749 0.1368 0.1135 -0.0075 0.0129  -0.0093 143 VAL A CB  
1179 C  CG1 . VAL A 142 ? 0.1142 0.1437 0.1093 0.0218  -0.0035 -0.0173 143 VAL A CG1 
1180 C  CG2 . VAL A 142 ? 0.0850 0.1703 0.1177 -0.0150 0.0256  0.0117  143 VAL A CG2 
1181 N  N   . LEU A 143 ? 0.0981 0.1008 0.1289 -0.0121 -0.0156 -0.0017 144 LEU A N   
1182 C  CA  . LEU A 143 ? 0.0967 0.1012 0.1350 -0.0070 -0.0126 0.0054  144 LEU A CA  
1183 C  C   . LEU A 143 ? 0.0829 0.1018 0.1054 -0.0248 0.0035  0.0131  144 LEU A C   
1184 O  O   . LEU A 143 ? 0.1257 0.1238 0.1090 -0.0199 0.0072  0.0171  144 LEU A O   
1185 C  CB  . LEU A 143 ? 0.0939 0.1404 0.1867 -0.0128 -0.0223 0.0248  144 LEU A CB  
1186 C  CG  . LEU A 143 ? 0.1004 0.1475 0.1918 -0.0182 -0.0179 0.0057  144 LEU A CG  
1187 C  CD1 . LEU A 143 ? 0.1300 0.2297 0.2166 0.0013  0.0214  0.0551  144 LEU A CD1 
1188 C  CD2 . LEU A 143 ? 0.0911 0.2351 0.2572 -0.0011 -0.0362 0.0214  144 LEU A CD2 
1189 N  N   . GLY A 144 ? 0.0771 0.0985 0.1371 0.0001  -0.0044 0.0138  145 GLY A N   
1190 C  CA  . GLY A 144 ? 0.0807 0.1064 0.1189 -0.0018 0.0097  -0.0010 145 GLY A CA  
1191 C  C   . GLY A 144 ? 0.1078 0.0996 0.1006 -0.0052 0.0145  0.0079  145 GLY A C   
1192 O  O   . GLY A 144 ? 0.1039 0.1224 0.1230 -0.0147 0.0197  0.0100  145 GLY A O   
1193 N  N   . ILE A 145 ? 0.0857 0.0945 0.1252 -0.0091 -0.0125 -0.0064 146 ILE A N   
1194 C  CA  . ILE A 145 ? 0.0581 0.1029 0.1541 -0.0042 -0.0205 -0.0026 146 ILE A CA  
1195 C  C   . ILE A 145 ? 0.0848 0.1133 0.1153 -0.0027 0.0027  -0.0001 146 ILE A C   
1196 O  O   . ILE A 145 ? 0.0889 0.1150 0.1311 -0.0031 0.0113  0.0027  146 ILE A O   
1197 C  CB  . ILE A 145 ? 0.0807 0.1144 0.1593 0.0029  -0.0241 0.0061  146 ILE A CB  
1198 C  CG1 . ILE A 145 ? 0.0974 0.1211 0.1950 0.0263  -0.0178 0.0068  146 ILE A CG1 
1199 C  CG2 . ILE A 145 ? 0.0960 0.1554 0.1873 -0.0173 -0.0442 -0.0079 146 ILE A CG2 
1200 C  CD1 . ILE A 145 ? 0.0970 0.1435 0.2222 0.0108  -0.0388 0.0322  146 ILE A CD1 
1201 N  N   . PHE A 146 ? 0.0958 0.1027 0.1216 0.0068  0.0079  -0.0044 147 PHE A N   
1202 C  CA  . PHE A 146 ? 0.1073 0.1058 0.1114 0.0179  -0.0072 0.0000  147 PHE A CA  
1203 C  C   . PHE A 146 ? 0.0891 0.1081 0.1393 -0.0058 -0.0069 -0.0006 147 PHE A C   
1204 O  O   . PHE A 146 ? 0.0841 0.1526 0.1487 -0.0050 0.0044  -0.0037 147 PHE A O   
1205 C  CB  . PHE A 146 ? 0.0902 0.1256 0.1243 -0.0066 -0.0087 0.0257  147 PHE A CB  
1206 C  CG  . PHE A 146 ? 0.0817 0.0994 0.1250 -0.0009 0.0053  0.0031  147 PHE A CG  
1207 C  CD1 . PHE A 146 ? 0.0835 0.1137 0.1378 0.0064  -0.0059 -0.0020 147 PHE A CD1 
1208 C  CD2 . PHE A 146 ? 0.1015 0.1015 0.1250 -0.0020 -0.0010 0.0136  147 PHE A CD2 
1209 C  CE1 . PHE A 146 ? 0.1062 0.1370 0.0951 0.0089  -0.0038 0.0083  147 PHE A CE1 
1210 C  CE2 . PHE A 146 ? 0.0936 0.1289 0.1457 -0.0237 -0.0079 0.0193  147 PHE A CE2 
1211 C  CZ  . PHE A 146 ? 0.0981 0.1273 0.1045 -0.0233 0.0080  0.0165  147 PHE A CZ  
1212 N  N   . LEU A 147 ? 0.1194 0.1006 0.1247 -0.0048 0.0006  -0.0100 148 LEU A N   
1213 C  CA  . LEU A 147 ? 0.1013 0.1008 0.1363 -0.0055 -0.0147 0.0058  148 LEU A CA  
1214 C  C   . LEU A 147 ? 0.1022 0.1130 0.1146 -0.0047 -0.0008 -0.0060 148 LEU A C   
1215 O  O   . LEU A 147 ? 0.1094 0.1234 0.1633 -0.0015 0.0000  0.0062  148 LEU A O   
1216 C  CB  . LEU A 147 ? 0.1597 0.1207 0.1257 0.0079  0.0064  0.0138  148 LEU A CB  
1217 C  CG  . LEU A 147 ? 0.1648 0.1121 0.1415 -0.0163 -0.0217 0.0119  148 LEU A CG  
1218 C  CD1 . LEU A 147 ? 0.2004 0.1133 0.1748 -0.0250 -0.0462 -0.0022 148 LEU A CD1 
1219 C  CD2 . LEU A 147 ? 0.1582 0.1710 0.1507 -0.0176 -0.0080 0.0364  148 LEU A CD2 
1220 N  N   . LYS A 148 ? 0.1109 0.1121 0.1561 -0.0158 0.0021  -0.0166 149 LYS A N   
1221 C  CA  . LYS A 148 ? 0.1404 0.1160 0.1368 -0.0003 -0.0075 -0.0058 149 LYS A CA  
1222 C  C   . LYS A 148 ? 0.1385 0.1184 0.1428 -0.0072 -0.0296 0.0059  149 LYS A C   
1223 O  O   . LYS A 148 ? 0.1708 0.1636 0.1516 0.0410  -0.0425 -0.0113 149 LYS A O   
1224 C  CB  . LYS A 148 ? 0.1536 0.1929 0.1680 -0.0359 -0.0107 0.0364  149 LYS A CB  
1225 C  CG  . LYS A 148 ? 0.1616 0.1979 0.1967 -0.0361 -0.0027 0.0285  149 LYS A CG  
1226 C  CD  . LYS A 148 ? 0.2301 0.3152 0.2440 -0.0064 0.0380  0.0873  149 LYS A CD  
1227 C  CE  . LYS A 148 ? 0.2480 0.4905 0.3684 -0.0441 0.0418  0.1309  149 LYS A CE  
1228 N  NZ  . LYS A 148 ? 0.3814 0.5996 0.5304 -0.1989 0.1740  0.0813  149 LYS A NZ  
1229 N  N   . VAL A 149 ? 0.1845 0.0963 0.1943 -0.0017 -0.0532 -0.0108 150 VAL A N   
1230 C  CA  . VAL A 149 ? 0.1625 0.1227 0.1734 0.0049  -0.0245 0.0012  150 VAL A CA  
1231 C  C   . VAL A 149 ? 0.1868 0.1155 0.2223 -0.0229 -0.0559 0.0000  150 VAL A C   
1232 O  O   . VAL A 149 ? 0.2004 0.1523 0.1921 -0.0162 -0.0322 0.0055  150 VAL A O   
1233 C  CB  . VAL A 149 ? 0.1679 0.1491 0.1794 -0.0031 -0.0093 -0.0245 150 VAL A CB  
1234 C  CG1 . VAL A 149 ? 0.2090 0.1848 0.1690 0.0065  -0.0556 -0.0100 150 VAL A CG1 
1235 C  CG2 . VAL A 149 ? 0.1771 0.2013 0.2345 -0.0242 -0.0078 -0.0146 150 VAL A CG2 
1236 N  N   . GLY A 150 ? 0.1587 0.1421 0.2035 -0.0085 -0.0353 -0.0031 151 GLY A N   
1237 C  CA  . GLY A 150 ? 0.1643 0.1868 0.2266 -0.0270 -0.0562 0.0181  151 GLY A CA  
1238 C  C   . GLY A 150 ? 0.1444 0.1629 0.1900 -0.0486 -0.0324 0.0027  151 GLY A C   
1239 O  O   . GLY A 150 ? 0.1949 0.1460 0.1932 -0.0412 -0.0283 -0.0100 151 GLY A O   
1240 N  N   A SER A 151 ? 0.1717 0.1758 0.2618 -0.0100 -0.0416 0.0204  152 SER A N   
1241 N  N   B SER A 151 ? 0.1731 0.1594 0.2664 -0.0139 -0.0452 0.0067  152 SER A N   
1242 C  CA  A SER A 151 ? 0.1777 0.1773 0.2748 -0.0230 -0.0541 0.0348  152 SER A CA  
1243 C  CA  B SER A 151 ? 0.1873 0.1580 0.2676 -0.0168 -0.0389 0.0358  152 SER A CA  
1244 C  C   A SER A 151 ? 0.1722 0.1500 0.1760 -0.0233 -0.0505 -0.0229 152 SER A C   
1245 C  C   B SER A 151 ? 0.1897 0.1555 0.1776 -0.0226 -0.0379 0.0030  152 SER A C   
1246 O  O   A SER A 151 ? 0.0936 0.1609 0.2221 0.0010  -0.0568 -0.0475 152 SER A O   
1247 O  O   B SER A 151 ? 0.1626 0.1755 0.1706 -0.0275 -0.0247 -0.0005 152 SER A O   
1248 C  CB  A SER A 151 ? 0.1866 0.2732 0.3294 -0.0696 -0.0289 -0.0223 152 SER A CB  
1249 C  CB  B SER A 151 ? 0.2093 0.2550 0.2708 -0.0639 -0.0163 -0.0580 152 SER A CB  
1250 O  OG  A SER A 151 ? 0.0970 0.3520 0.3098 -0.0145 -0.0173 -0.0623 152 SER A OG  
1251 O  OG  B SER A 151 ? 0.1135 0.3252 0.3154 -0.0157 0.0513  0.0339  152 SER A OG  
1252 N  N   . ALA A 152 ? 0.1871 0.1767 0.1699 -0.0055 -0.0512 -0.0107 153 ALA A N   
1253 C  CA  . ALA A 152 ? 0.2335 0.1379 0.1945 0.0167  -0.0826 -0.0108 153 ALA A CA  
1254 C  C   . ALA A 152 ? 0.1529 0.1557 0.2139 -0.0093 -0.0761 -0.0172 153 ALA A C   
1255 O  O   . ALA A 152 ? 0.1845 0.1552 0.2801 -0.0109 -0.0274 -0.0029 153 ALA A O   
1256 C  CB  . ALA A 152 ? 0.2770 0.2083 0.1990 -0.0026 -0.1064 -0.0107 153 ALA A CB  
1257 N  N   . LYS A 153 ? 0.2029 0.1105 0.2172 -0.0076 -0.1034 -0.0023 154 LYS A N   
1258 C  CA  . LYS A 153 ? 0.1685 0.1399 0.2132 0.0119  -0.0662 0.0048  154 LYS A CA  
1259 C  C   . LYS A 153 ? 0.1846 0.1333 0.2263 0.0075  -0.0784 -0.0020 154 LYS A C   
1260 O  O   . LYS A 153 ? 0.1947 0.1588 0.2025 0.0024  -0.0811 -0.0115 154 LYS A O   
1261 C  CB  . LYS A 153 ? 0.2214 0.1200 0.2153 -0.0105 -0.0832 -0.0137 154 LYS A CB  
1262 C  CG  . LYS A 153 ? 0.2645 0.1428 0.2116 -0.0055 -0.0952 -0.0238 154 LYS A CG  
1263 C  CD  . LYS A 153 ? 0.3285 0.1770 0.1820 0.0494  -0.0663 -0.0272 154 LYS A CD  
1264 C  CE  . LYS A 153 ? 0.4017 0.1846 0.2388 0.0901  -0.1206 -0.0534 154 LYS A CE  
1265 N  NZ  . LYS A 153 ? 0.4949 0.3375 0.2567 0.0929  -0.0141 -0.0478 154 LYS A NZ  
1266 N  N   . PRO A 154 ? 0.1853 0.1595 0.2239 -0.0006 -0.0794 0.0002  155 PRO A N   
1267 C  CA  . PRO A 154 ? 0.1685 0.2137 0.2251 0.0162  -0.0738 0.0220  155 PRO A CA  
1268 C  C   . PRO A 154 ? 0.1929 0.1961 0.2284 0.0381  -0.0687 -0.0079 155 PRO A C   
1269 O  O   . PRO A 154 ? 0.2324 0.2318 0.2277 0.0013  -0.0999 -0.0076 155 PRO A O   
1270 C  CB  . PRO A 154 ? 0.1595 0.2385 0.2882 0.0447  -0.0908 0.0010  155 PRO A CB  
1271 C  CG  . PRO A 154 ? 0.2144 0.3184 0.3735 -0.0108 -0.1289 0.0686  155 PRO A CG  
1272 C  CD  . PRO A 154 ? 0.1986 0.1619 0.2625 0.0081  -0.0664 0.0306  155 PRO A CD  
1273 N  N   . GLY A 155 ? 0.1922 0.1448 0.2552 0.0145  -0.0773 -0.0184 156 GLY A N   
1274 C  CA  . GLY A 155 ? 0.2178 0.1640 0.2899 -0.0111 -0.0792 0.0103  156 GLY A CA  
1275 C  C   . GLY A 155 ? 0.2326 0.1399 0.2434 -0.0174 -0.0588 0.0094  156 GLY A C   
1276 O  O   . GLY A 155 ? 0.2628 0.1351 0.3582 -0.0148 -0.0685 0.0294  156 GLY A O   
1277 N  N   . LEU A 156 ? 0.2494 0.1461 0.1921 0.0098  -0.0678 0.0078  157 LEU A N   
1278 C  CA  . LEU A 156 ? 0.2612 0.1493 0.1960 -0.0165 -0.0934 0.0002  157 LEU A CA  
1279 C  C   . LEU A 156 ? 0.2214 0.1444 0.1954 -0.0099 -0.0564 -0.0181 157 LEU A C   
1280 O  O   . LEU A 156 ? 0.2257 0.1519 0.1753 -0.0170 -0.0882 0.0062  157 LEU A O   
1281 C  CB  . LEU A 156 ? 0.2128 0.1612 0.1940 -0.0140 -0.0941 0.0092  157 LEU A CB  
1282 C  CG  . LEU A 156 ? 0.2035 0.1733 0.1573 -0.0104 -0.0696 -0.0002 157 LEU A CG  
1283 C  CD1 . LEU A 156 ? 0.2247 0.1889 0.1946 -0.0444 -0.0658 -0.0032 157 LEU A CD1 
1284 C  CD2 . LEU A 156 ? 0.2538 0.1570 0.2227 -0.0176 -0.1048 0.0088  157 LEU A CD2 
1285 N  N   . GLN A 157 ? 0.2673 0.1419 0.1666 -0.0132 -0.0897 -0.0088 158 GLN A N   
1286 C  CA  . GLN A 157 ? 0.2394 0.1705 0.1843 -0.0522 -0.0515 -0.0309 158 GLN A CA  
1287 C  C   . GLN A 157 ? 0.2008 0.1839 0.1900 -0.0078 -0.0620 -0.0117 158 GLN A C   
1288 O  O   . GLN A 157 ? 0.2671 0.1780 0.1796 0.0042  -0.0757 -0.0186 158 GLN A O   
1289 C  CB  . GLN A 157 ? 0.2209 0.1952 0.1953 -0.0366 -0.0694 -0.0200 158 GLN A CB  
1290 C  CG  . GLN A 157 ? 0.3606 0.1945 0.1734 -0.0365 -0.0604 -0.0223 158 GLN A CG  
1291 C  CD  . GLN A 157 ? 0.3668 0.1699 0.1613 -0.0432 -0.0911 -0.0269 158 GLN A CD  
1292 O  OE1 . GLN A 157 ? 0.4060 0.1749 0.1954 -0.0302 -0.1161 0.0015  158 GLN A OE1 
1293 N  NE2 . GLN A 157 ? 0.4133 0.2196 0.1954 -0.0438 -0.0795 -0.0624 158 GLN A NE2 
1294 N  N   . LYS A 158 ? 0.2764 0.1649 0.2190 0.0031  -0.1388 0.0091  159 LYS A N   
1295 C  CA  . LYS A 158 ? 0.2743 0.1864 0.1527 -0.0091 -0.0885 -0.0117 159 LYS A CA  
1296 C  C   . LYS A 158 ? 0.3131 0.1505 0.1645 -0.0433 -0.1004 0.0163  159 LYS A C   
1297 O  O   . LYS A 158 ? 0.3122 0.1986 0.1561 -0.0394 -0.0825 0.0281  159 LYS A O   
1298 C  CB  . LYS A 158 ? 0.3606 0.1737 0.2394 0.0181  -0.1168 0.0220  159 LYS A CB  
1299 C  CG  . LYS A 158 ? 0.5116 0.2204 0.2597 0.0763  -0.0547 0.0509  159 LYS A CG  
1300 C  CD  . LYS A 158 ? 0.5038 0.2439 0.4014 0.1069  -0.0822 0.0586  159 LYS A CD  
1301 C  CE  . LYS A 158 ? 0.4614 0.3334 0.3750 -0.0532 -0.1529 0.0961  159 LYS A CE  
1302 N  NZ  . LYS A 158 ? 0.4560 0.3818 0.3647 -0.0612 -0.1694 0.1064  159 LYS A NZ  
1303 N  N   . VAL A 159 ? 0.2535 0.1683 0.1613 0.0086  -0.0963 0.0000  160 VAL A N   
1304 C  CA  . VAL A 159 ? 0.2628 0.1606 0.1493 -0.0275 -0.0751 -0.0021 160 VAL A CA  
1305 C  C   . VAL A 159 ? 0.2318 0.1407 0.1843 -0.0139 -0.0776 0.0021  160 VAL A C   
1306 O  O   . VAL A 159 ? 0.2516 0.1501 0.1979 -0.0144 -0.0703 0.0134  160 VAL A O   
1307 C  CB  . VAL A 159 ? 0.2570 0.1860 0.1386 0.0238  -0.0615 -0.0030 160 VAL A CB  
1308 C  CG1 . VAL A 159 ? 0.2525 0.2602 0.1695 -0.0414 -0.1209 0.0232  160 VAL A CG1 
1309 C  CG2 . VAL A 159 ? 0.3696 0.2124 0.1552 0.0659  -0.0824 -0.0243 160 VAL A CG2 
1310 N  N   . VAL A 160 ? 0.2491 0.1318 0.1801 -0.0054 -0.0703 0.0012  161 VAL A N   
1311 C  CA  . VAL A 160 ? 0.2791 0.1351 0.1922 0.0002  -0.0285 0.0126  161 VAL A CA  
1312 C  C   . VAL A 160 ? 0.2922 0.1544 0.1979 0.0027  -0.0439 -0.0002 161 VAL A C   
1313 O  O   . VAL A 160 ? 0.3153 0.1773 0.1702 -0.0237 -0.0316 -0.0194 161 VAL A O   
1314 C  CB  . VAL A 160 ? 0.3477 0.1501 0.1813 0.0027  -0.0055 -0.0122 161 VAL A CB  
1315 C  CG1 . VAL A 160 ? 0.3154 0.1903 0.2015 -0.0347 -0.0262 -0.0285 161 VAL A CG1 
1316 C  CG2 . VAL A 160 ? 0.3141 0.2007 0.2061 0.0029  -0.0158 0.0095  161 VAL A CG2 
1317 N  N   . ASP A 161 ? 0.3136 0.1814 0.1443 -0.0020 -0.0691 0.0044  162 ASP A N   
1318 C  CA  . ASP A 161 ? 0.3490 0.2366 0.1451 -0.0052 -0.0487 -0.0089 162 ASP A CA  
1319 C  C   . ASP A 161 ? 0.3565 0.2559 0.1304 -0.0196 -0.0646 0.0050  162 ASP A C   
1320 O  O   . ASP A 161 ? 0.3868 0.3547 0.1773 -0.0672 -0.0146 -0.0485 162 ASP A O   
1321 C  CB  . ASP A 161 ? 0.3638 0.3334 0.2105 -0.0436 -0.0710 -0.0430 162 ASP A CB  
1322 C  CG  . ASP A 161 ? 0.2822 0.3096 0.2227 -0.0119 -0.0439 -0.0586 162 ASP A CG  
1323 O  OD1 . ASP A 161 ? 0.3749 0.3338 0.3652 0.0119  -0.0682 -0.0599 162 ASP A OD1 
1324 O  OD2 . ASP A 161 ? 0.3061 0.3943 0.2600 -0.0439 -0.0649 -0.0153 162 ASP A OD2 
1325 N  N   . VAL A 162 ? 0.3441 0.2737 0.1588 -0.0499 -0.0826 0.0114  163 VAL A N   
1326 C  CA  . VAL A 162 ? 0.4126 0.2513 0.1665 -0.0286 -0.0922 0.0243  163 VAL A CA  
1327 C  C   . VAL A 162 ? 0.3780 0.2488 0.1419 -0.0445 -0.0253 0.0127  163 VAL A C   
1328 O  O   . VAL A 162 ? 0.4230 0.2319 0.1385 -0.0601 -0.0480 0.0270  163 VAL A O   
1329 C  CB  . VAL A 162 ? 0.3928 0.2139 0.3116 0.0273  -0.1127 0.0638  163 VAL A CB  
1330 C  CG1 . VAL A 162 ? 0.3914 0.1875 0.3416 -0.0447 -0.1267 0.0405  163 VAL A CG1 
1331 C  CG2 . VAL A 162 ? 0.4819 0.3210 0.3926 -0.0328 -0.0236 0.1035  163 VAL A CG2 
1332 N  N   . LEU A 163 ? 0.3562 0.2284 0.1342 -0.0401 -0.0350 -0.0003 164 LEU A N   
1333 C  CA  . LEU A 163 ? 0.3734 0.2186 0.0837 -0.0567 -0.0047 0.0135  164 LEU A CA  
1334 C  C   . LEU A 163 ? 0.3437 0.2329 0.0981 -0.0408 -0.0138 -0.0274 164 LEU A C   
1335 O  O   . LEU A 163 ? 0.3511 0.2119 0.1850 -0.0286 -0.0098 0.0097  164 LEU A O   
1336 C  CB  . LEU A 163 ? 0.3103 0.1889 0.0993 -0.0242 -0.0089 0.0055  164 LEU A CB  
1337 C  CG  . LEU A 163 ? 0.3274 0.1760 0.0845 -0.0466 0.0064  0.0201  164 LEU A CG  
1338 C  CD1 . LEU A 163 ? 0.2772 0.2098 0.1724 -0.0089 0.0201  0.0675  164 LEU A CD1 
1339 C  CD2 . LEU A 163 ? 0.2806 0.1974 0.1455 -0.0212 -0.0370 -0.0055 164 LEU A CD2 
1340 N  N   . ASP A 164 ? 0.5094 0.2106 0.1046 -0.0894 -0.0093 -0.0207 165 ASP A N   
1341 C  CA  . ASP A 164 ? 0.5382 0.2623 0.1399 -0.0662 0.0083  -0.0451 165 ASP A CA  
1342 C  C   . ASP A 164 ? 0.4567 0.3405 0.1868 -0.0697 0.0008  0.0092  165 ASP A C   
1343 O  O   . ASP A 164 ? 0.5247 0.4424 0.2056 -0.0812 0.0627  -0.0270 165 ASP A O   
1344 C  CB  . ASP A 164 ? 0.6006 0.4000 0.1979 -0.1318 -0.0179 -0.0958 165 ASP A CB  
1345 C  CG  . ASP A 164 ? 0.6554 0.4746 0.2758 -0.0790 0.0026  -0.1181 165 ASP A CG  
1346 O  OD1 . ASP A 164 ? 0.5565 0.6667 0.2954 -0.1542 0.0037  -0.1187 165 ASP A OD1 
1347 O  OD2 . ASP A 164 ? 0.5971 0.8853 0.3639 -0.1630 0.2002  -0.1420 165 ASP A OD2 
1348 N  N   . SER A 165 ? 0.4740 0.2875 0.1168 -0.0873 -0.0302 0.0248  166 SER A N   
1349 C  CA  . SER A 165 ? 0.4632 0.2962 0.1094 -0.1083 -0.0249 0.0232  166 SER A CA  
1350 C  C   . SER A 165 ? 0.4685 0.2687 0.0974 -0.1130 -0.0052 0.0164  166 SER A C   
1351 O  O   . SER A 165 ? 0.4876 0.2612 0.1719 -0.1050 -0.0030 0.0630  166 SER A O   
1352 C  CB  . SER A 165 ? 0.6034 0.3343 0.2295 -0.0135 -0.0102 0.0869  166 SER A CB  
1353 O  OG  . SER A 165 ? 0.5801 0.2727 0.2171 -0.0357 -0.0694 0.0728  166 SER A OG  
1354 N  N   . ILE A 166 ? 0.3534 0.2528 0.1098 -0.0802 -0.0070 0.0388  167 ILE A N   
1355 C  CA  . ILE A 166 ? 0.3166 0.2532 0.1623 -0.0542 -0.0060 0.0156  167 ILE A CA  
1356 C  C   . ILE A 166 ? 0.3752 0.1706 0.1787 -0.0285 0.0008  -0.0204 167 ILE A C   
1357 O  O   . ILE A 166 ? 0.3814 0.2361 0.1437 -0.0798 0.0262  0.0110  167 ILE A O   
1358 C  CB  . ILE A 166 ? 0.4244 0.1917 0.1442 -0.0763 0.0048  0.0120  167 ILE A CB  
1359 C  CG1 . ILE A 166 ? 0.3882 0.2037 0.1094 -0.0493 0.0158  0.0263  167 ILE A CG1 
1360 C  CG2 . ILE A 166 ? 0.4269 0.2008 0.2164 -0.0722 -0.0026 0.0295  167 ILE A CG2 
1361 C  CD1 . ILE A 166 ? 0.3316 0.2125 0.1536 -0.0314 -0.0510 -0.0277 167 ILE A CD1 
1362 N  N   . LYS A 167 ? 0.3804 0.1846 0.1624 -0.0595 0.0347  -0.0030 168 LYS A N   
1363 C  CA  . LYS A 167 ? 0.2639 0.2258 0.1719 -0.0504 0.0602  -0.0442 168 LYS A CA  
1364 C  C   . LYS A 167 ? 0.3675 0.2248 0.1336 -0.1203 -0.0059 0.0004  168 LYS A C   
1365 O  O   . LYS A 167 ? 0.2687 0.2717 0.1293 -0.0734 0.0498  0.0171  168 LYS A O   
1366 C  CB  . LYS A 167 ? 0.4571 0.2201 0.1730 -0.0078 0.0348  -0.0589 168 LYS A CB  
1367 C  CG  . LYS A 167 ? 0.4108 0.1997 0.2475 -0.0400 0.0632  -0.0269 168 LYS A CG  
1368 C  CD  . LYS A 167 ? 0.5700 0.3190 0.2542 -0.0016 -0.0820 -0.1118 168 LYS A CD  
1369 C  CE  . LYS A 167 ? 0.7108 0.3051 0.4139 0.0124  0.0080  0.0100  168 LYS A CE  
1370 N  N   . THR A 168 ? 0.3604 0.2360 0.1509 -0.1191 0.0684  -0.0046 169 THR A N   
1371 C  CA  . THR A 168 ? 0.3642 0.2991 0.2117 -0.1801 0.0672  -0.0091 169 THR A CA  
1372 C  C   . THR A 168 ? 0.3731 0.2728 0.1315 -0.1103 0.0547  0.0567  169 THR A C   
1373 O  O   . THR A 168 ? 0.4121 0.2561 0.1367 -0.1138 0.0468  0.0343  169 THR A O   
1374 C  CB  . THR A 168 ? 0.4602 0.3157 0.1694 -0.1337 0.0897  0.0313  169 THR A CB  
1375 O  OG1 . THR A 168 ? 0.4714 0.3592 0.1548 -0.1518 0.0610  0.0230  169 THR A OG1 
1376 C  CG2 . THR A 168 ? 0.4860 0.3208 0.1485 -0.0827 0.0951  0.0197  169 THR A CG2 
1377 N  N   . LYS A 169 ? 0.3419 0.2803 0.1573 -0.0944 0.0439  -0.0214 170 LYS A N   
1378 C  CA  . LYS A 169 ? 0.3459 0.2342 0.1631 -0.0942 0.0809  0.0065  170 LYS A CA  
1379 C  C   . LYS A 169 ? 0.3129 0.2822 0.2725 -0.1698 0.0234  0.0359  170 LYS A C   
1380 O  O   . LYS A 169 ? 0.4847 0.3688 0.2389 -0.2157 0.0570  0.0732  170 LYS A O   
1381 C  CB  . LYS A 169 ? 0.3768 0.3195 0.2255 -0.1495 0.0181  -0.0072 170 LYS A CB  
1382 C  CG  . LYS A 169 ? 0.2975 0.3353 0.1813 -0.1285 0.0981  -0.0441 170 LYS A CG  
1383 C  CD  . LYS A 169 ? 0.3252 0.4180 0.4077 -0.1785 -0.0536 -0.0010 170 LYS A CD  
1384 C  CE  . LYS A 169 ? 0.4751 0.4886 0.4545 -0.2469 -0.0545 -0.0322 170 LYS A CE  
1385 N  NZ  . LYS A 169 ? 0.4021 0.6222 0.7314 -0.0627 -0.1239 0.0024  170 LYS A NZ  
1386 N  N   . GLY A 170 ? 0.3538 0.2518 0.1821 -0.1123 0.0094  0.0431  171 GLY A N   
1387 C  CA  . GLY A 170 ? 0.4141 0.3105 0.2478 -0.1725 -0.0392 0.1083  171 GLY A CA  
1388 C  C   . GLY A 170 ? 0.3623 0.2721 0.2902 -0.1513 -0.0091 0.1161  171 GLY A C   
1389 O  O   . GLY A 170 ? 0.6608 0.3019 0.3782 -0.1532 -0.1084 0.1239  171 GLY A O   
1390 N  N   . LYS A 171 ? 0.4440 0.2398 0.1612 -0.1263 -0.0364 0.0798  172 LYS A N   
1391 C  CA  . LYS A 171 ? 0.3552 0.2374 0.1643 -0.0551 0.0496  0.0832  172 LYS A CA  
1392 C  C   . LYS A 171 ? 0.2852 0.2703 0.1868 -0.0860 0.0582  0.0611  172 LYS A C   
1393 O  O   . LYS A 171 ? 0.4561 0.2549 0.1570 -0.0725 0.0609  0.0504  172 LYS A O   
1394 C  CB  . LYS A 171 ? 0.3820 0.2591 0.2507 -0.0847 0.0067  0.0402  172 LYS A CB  
1395 C  CG  . LYS A 171 ? 0.4604 0.3364 0.2288 -0.0833 0.0394  0.0091  172 LYS A CG  
1396 C  CD  . LYS A 171 ? 0.6513 0.2452 0.4058 -0.0377 0.0555  -0.0753 172 LYS A CD  
1397 N  N   . SER A 172 ? 0.4658 0.2514 0.2004 -0.0594 -0.0584 -0.0079 173 SER A N   
1398 C  CA  . SER A 172 ? 0.4945 0.2125 0.1351 -0.0789 0.0107  0.0751  173 SER A CA  
1399 C  C   . SER A 172 ? 0.5483 0.2848 0.1662 -0.0164 -0.0135 0.0322  173 SER A C   
1400 O  O   . SER A 172 ? 0.5848 0.3060 0.1363 0.0190  0.0160  0.0559  173 SER A O   
1401 C  CB  . SER A 172 ? 0.5191 0.2200 0.1662 -0.0955 0.0066  0.0548  173 SER A CB  
1402 O  OG  . SER A 172 ? 0.5202 0.2713 0.2678 -0.0488 0.0677  0.1218  173 SER A OG  
1403 N  N   . ALA A 173 ? 0.4488 0.2466 0.1049 0.0096  -0.0345 0.0368  174 ALA A N   
1404 C  CA  . ALA A 173 ? 0.4235 0.3239 0.1584 0.0313  -0.0425 -0.0372 174 ALA A CA  
1405 C  C   . ALA A 173 ? 0.4491 0.3276 0.1108 0.0928  0.0091  0.0700  174 ALA A C   
1406 O  O   . ALA A 173 ? 0.5979 0.2450 0.1013 0.0979  -0.0050 0.0365  174 ALA A O   
1407 C  CB  . ALA A 173 ? 0.3279 0.3462 0.1856 -0.0168 -0.0793 -0.0225 174 ALA A CB  
1408 N  N   A ASP A 174 ? 0.6269 0.2748 0.1691 0.0968  -0.0954 0.0996  175 ASP A N   
1409 N  N   B ASP A 174 ? 0.5330 0.2840 0.1699 0.0538  -0.0978 0.0688  175 ASP A N   
1410 C  CA  A ASP A 174 ? 0.6172 0.4201 0.1879 0.0640  -0.0790 0.0006  175 ASP A CA  
1411 C  CA  B ASP A 174 ? 0.3950 0.4005 0.2013 0.0530  -0.1331 0.1062  175 ASP A CA  
1412 C  C   A ASP A 174 ? 0.6327 0.4137 0.1241 0.0228  -0.1367 -0.0292 175 ASP A C   
1413 C  C   B ASP A 174 ? 0.3981 0.3531 0.1522 0.0049  -0.1557 -0.0134 175 ASP A C   
1414 O  O   A ASP A 174 ? 0.7182 0.2196 0.4837 -0.0039 -0.0652 0.0164  175 ASP A O   
1415 O  O   B ASP A 174 ? 0.4881 0.2894 0.2601 0.1202  -0.1344 -0.0171 175 ASP A O   
1416 C  CB  A ASP A 174 ? 0.6801 0.5005 0.0995 0.1210  -0.1056 0.0212  175 ASP A CB  
1417 C  CB  B ASP A 174 ? 0.5681 0.3206 0.4505 0.1021  -0.0074 0.1018  175 ASP A CB  
1418 C  CG  A ASP A 174 ? 0.5075 0.5896 0.2709 0.0572  -0.2150 -0.0065 175 ASP A CG  
1419 C  CG  B ASP A 174 ? 0.4974 0.5623 0.5105 -0.0429 0.0273  0.0389  175 ASP A CG  
1420 O  OD1 A ASP A 174 ? 0.6074 0.5172 0.2370 0.0906  0.0018  0.0559  175 ASP A OD1 
1421 O  OD1 B ASP A 174 ? 0.6079 0.3233 0.5502 0.0460  -0.0707 0.0464  175 ASP A OD1 
1422 O  OD2 . ASP A 174 ? 0.4765 0.5303 0.4877 0.0559  0.0285  0.0075  175 ASP A OD2 
1423 N  N   . PHE A 175 ? 0.5077 0.2275 0.1669 0.0156  -0.0554 0.0765  176 PHE A N   
1424 C  CA  . PHE A 175 ? 0.4264 0.1873 0.1897 -0.0003 -0.1224 0.0206  176 PHE A CA  
1425 C  C   . PHE A 175 ? 0.3993 0.2083 0.1586 0.0343  -0.0913 0.0449  176 PHE A C   
1426 O  O   . PHE A 175 ? 0.4315 0.2083 0.1816 0.0434  -0.1116 0.0290  176 PHE A O   
1427 C  CB  . PHE A 175 ? 0.4127 0.1557 0.2342 0.0163  -0.1362 0.0142  176 PHE A CB  
1428 C  CG  . PHE A 175 ? 0.3677 0.1904 0.1906 0.0207  -0.0906 0.0096  176 PHE A CG  
1429 C  CD1 . PHE A 175 ? 0.4080 0.1810 0.1940 0.0083  -0.0608 0.0006  176 PHE A CD1 
1430 C  CD2 . PHE A 175 ? 0.4315 0.1561 0.2010 0.0333  -0.0845 0.0091  176 PHE A CD2 
1431 C  CE1 . PHE A 175 ? 0.3741 0.1859 0.1813 0.0026  -0.0801 -0.0150 176 PHE A CE1 
1432 C  CE2 . PHE A 175 ? 0.3902 0.1661 0.1838 0.0174  -0.0633 -0.0048 176 PHE A CE2 
1433 C  CZ  . PHE A 175 ? 0.3763 0.1907 0.2029 0.0405  -0.0829 -0.0179 176 PHE A CZ  
1434 N  N   . THR A 176 ? 0.3651 0.1809 0.2266 -0.0054 -0.1196 0.0135  177 THR A N   
1435 C  CA  . THR A 176 ? 0.3805 0.2137 0.1879 -0.0108 -0.0820 0.0795  177 THR A CA  
1436 C  C   . THR A 176 ? 0.4096 0.2036 0.1518 -0.0620 -0.1289 0.0225  177 THR A C   
1437 O  O   . THR A 176 ? 0.3834 0.1970 0.1773 -0.0384 -0.1427 0.0400  177 THR A O   
1438 C  CB  . THR A 176 ? 0.4381 0.1877 0.2316 -0.0582 -0.1619 0.0812  177 THR A CB  
1439 O  OG1 . THR A 176 ? 0.4854 0.2514 0.2087 0.0050  -0.1336 0.0706  177 THR A OG1 
1440 C  CG2 . THR A 176 ? 0.4798 0.2710 0.3665 -0.0529 -0.1555 0.1702  177 THR A CG2 
1441 N  N   . ASN A 177 ? 0.3430 0.1940 0.2275 -0.0082 -0.1477 0.0521  178 ASN A N   
1442 C  CA  . ASN A 177 ? 0.3061 0.2322 0.1733 0.0211  -0.1008 0.0502  178 ASN A CA  
1443 C  C   . ASN A 177 ? 0.3532 0.1720 0.2426 -0.0204 -0.1639 0.0157  178 ASN A C   
1444 O  O   . ASN A 177 ? 0.3662 0.2477 0.3216 -0.0658 -0.1703 0.1302  178 ASN A O   
1445 C  CB  . ASN A 177 ? 0.2891 0.2143 0.2945 -0.0166 -0.1694 0.0944  178 ASN A CB  
1446 C  CG  . ASN A 177 ? 0.3221 0.2153 0.2509 0.0059  -0.1229 0.0737  178 ASN A CG  
1447 O  OD1 . ASN A 177 ? 0.3987 0.2413 0.2828 -0.0021 -0.0727 0.0500  178 ASN A OD1 
1448 N  ND2 . ASN A 177 ? 0.3375 0.2063 0.2177 -0.0318 -0.1421 0.0769  178 ASN A ND2 
1449 N  N   . PHE A 178 ? 0.3864 0.1412 0.2010 -0.0277 -0.1735 0.0588  179 PHE A N   
1450 C  CA  . PHE A 178 ? 0.3026 0.1480 0.1490 -0.0299 -0.0923 0.0510  179 PHE A CA  
1451 C  C   . PHE A 178 ? 0.3567 0.1408 0.1457 -0.0036 -0.0926 0.0369  179 PHE A C   
1452 O  O   . PHE A 178 ? 0.3253 0.1512 0.1942 -0.0209 -0.0947 0.0105  179 PHE A O   
1453 C  CB  . PHE A 178 ? 0.3213 0.1834 0.1767 0.0363  -0.0804 0.0547  179 PHE A CB  
1454 C  CG  . PHE A 178 ? 0.3703 0.1771 0.1697 -0.0082 -0.0915 0.0547  179 PHE A CG  
1455 C  CD1 . PHE A 178 ? 0.4089 0.1770 0.1573 -0.0165 -0.0243 0.0298  179 PHE A CD1 
1456 C  CD2 . PHE A 178 ? 0.2687 0.1947 0.1749 -0.0281 -0.1027 0.0494  179 PHE A CD2 
1457 C  CE1 . PHE A 178 ? 0.4105 0.1983 0.1879 0.0008  -0.0870 0.0501  179 PHE A CE1 
1458 C  CE2 . PHE A 178 ? 0.2674 0.1831 0.1787 0.0116  -0.0736 0.0464  179 PHE A CE2 
1459 C  CZ  . PHE A 178 ? 0.2581 0.2094 0.1924 -0.0121 -0.0841 0.0434  179 PHE A CZ  
1460 N  N   . ASP A 179 ? 0.2741 0.2151 0.1924 -0.0027 -0.1087 0.0571  180 ASP A N   
1461 C  CA  . ASP A 179 ? 0.2270 0.1861 0.2442 0.0130  -0.0980 0.0424  180 ASP A CA  
1462 C  C   . ASP A 179 ? 0.2412 0.1526 0.2173 -0.0035 -0.0928 0.0217  180 ASP A C   
1463 O  O   . ASP A 179 ? 0.2451 0.1483 0.2291 -0.0249 -0.0634 0.0064  180 ASP A O   
1464 C  CB  . ASP A 179 ? 0.2470 0.1925 0.3405 -0.0447 -0.1264 0.0486  180 ASP A CB  
1465 C  CG  . ASP A 179 ? 0.2460 0.3419 0.3048 -0.0120 -0.1409 0.0695  180 ASP A CG  
1466 O  OD1 . ASP A 179 ? 0.2680 0.2115 0.2764 0.0326  -0.0926 0.0385  180 ASP A OD1 
1467 O  OD2 . ASP A 179 ? 0.2473 0.5869 0.3705 -0.0110 -0.0951 0.0036  180 ASP A OD2 
1468 N  N   . PRO A 180 ? 0.2306 0.1236 0.1992 -0.0001 -0.0837 0.0018  181 PRO A N   
1469 C  CA  . PRO A 180 ? 0.1595 0.1931 0.1889 -0.0300 -0.0589 0.0391  181 PRO A CA  
1470 C  C   . PRO A 180 ? 0.1746 0.1654 0.1613 0.0155  -0.0250 0.0172  181 PRO A C   
1471 O  O   . PRO A 180 ? 0.2148 0.1518 0.1916 0.0052  -0.0723 0.0225  181 PRO A O   
1472 C  CB  . PRO A 180 ? 0.2137 0.1654 0.2128 -0.0136 -0.0707 -0.0006 181 PRO A CB  
1473 C  CG  . PRO A 180 ? 0.2573 0.1548 0.2420 -0.0308 -0.0963 -0.0051 181 PRO A CG  
1474 C  CD  . PRO A 180 ? 0.2356 0.1458 0.2205 -0.0196 -0.0873 0.0065  181 PRO A CD  
1475 N  N   . ARG A 181 ? 0.1637 0.1873 0.2078 0.0173  -0.0348 0.0111  182 ARG A N   
1476 C  CA  . ARG A 181 ? 0.1735 0.1688 0.1982 0.0129  -0.0392 -0.0050 182 ARG A CA  
1477 C  C   . ARG A 181 ? 0.1669 0.1638 0.2474 0.0207  -0.0526 0.0238  182 ARG A C   
1478 O  O   . ARG A 181 ? 0.2029 0.1995 0.2618 -0.0273 -0.0970 0.0491  182 ARG A O   
1479 C  CB  . ARG A 181 ? 0.1476 0.1788 0.3341 -0.0018 -0.0520 -0.0048 182 ARG A CB  
1480 C  CG  . ARG A 181 ? 0.2155 0.1681 0.3567 0.0322  -0.0431 -0.0002 182 ARG A CG  
1481 C  CD  . ARG A 181 ? 0.2119 0.2118 0.3986 0.0355  0.0104  0.0765  182 ARG A CD  
1482 N  NE  . ARG A 181 ? 0.2257 0.1756 0.4108 0.0188  -0.0364 0.0927  182 ARG A NE  
1483 C  CZ  . ARG A 181 ? 0.2252 0.2266 0.4250 0.0201  -0.0193 0.1152  182 ARG A CZ  
1484 N  NH1 . ARG A 181 ? 0.2789 0.3685 0.5589 0.0458  0.0855  0.1202  182 ARG A NH1 
1485 N  NH2 . ARG A 181 ? 0.2925 0.3450 0.4220 0.0284  -0.0433 0.1654  182 ARG A NH2 
1486 N  N   . GLY A 182 ? 0.2318 0.1426 0.2610 0.0019  -0.1093 0.0002  183 GLY A N   
1487 C  CA  . GLY A 182 ? 0.2582 0.1354 0.2965 0.0199  -0.1254 0.0036  183 GLY A CA  
1488 C  C   . GLY A 182 ? 0.2313 0.1505 0.2841 -0.0017 -0.1214 0.0242  183 GLY A C   
1489 O  O   . GLY A 182 ? 0.3098 0.1500 0.2711 -0.0068 -0.1418 -0.0126 183 GLY A O   
1490 N  N   . LEU A 183 ? 0.2191 0.1652 0.2318 0.0096  -0.1079 0.0156  184 LEU A N   
1491 C  CA  . LEU A 183 ? 0.2124 0.1569 0.1590 0.0356  -0.0378 0.0182  184 LEU A CA  
1492 C  C   . LEU A 183 ? 0.1697 0.1638 0.1609 0.0231  -0.0343 0.0275  184 LEU A C   
1493 O  O   . LEU A 183 ? 0.1916 0.1976 0.2119 0.0376  -0.0523 0.0392  184 LEU A O   
1494 C  CB  . LEU A 183 ? 0.2196 0.1861 0.1917 0.0303  -0.0443 0.0500  184 LEU A CB  
1495 C  CG  . LEU A 183 ? 0.2601 0.1845 0.1705 0.0566  -0.0596 0.0215  184 LEU A CG  
1496 C  CD1 . LEU A 183 ? 0.2789 0.2169 0.2308 0.0178  -0.0817 0.0379  184 LEU A CD1 
1497 C  CD2 . LEU A 183 ? 0.2833 0.1903 0.1927 0.0697  -0.0018 0.0131  184 LEU A CD2 
1498 N  N   . LEU A 184 ? 0.1649 0.1821 0.2076 0.0041  -0.0260 0.0129  185 LEU A N   
1499 C  CA  . LEU A 184 ? 0.1462 0.1408 0.2044 -0.0197 -0.0387 0.0153  185 LEU A CA  
1500 C  C   . LEU A 184 ? 0.2358 0.1595 0.2438 -0.0674 -0.1264 0.0496  185 LEU A C   
1501 O  O   . LEU A 184 ? 0.3371 0.2295 0.3633 -0.1167 -0.2424 0.0900  185 LEU A O   
1502 C  CB  . LEU A 184 ? 0.1491 0.1491 0.2367 -0.0068 -0.0184 0.0057  185 LEU A CB  
1503 C  CG  . LEU A 184 ? 0.0846 0.1606 0.2496 -0.0057 -0.0081 0.0074  185 LEU A CG  
1504 C  CD1 . LEU A 184 ? 0.1699 0.1503 0.2549 0.0084  -0.0152 0.0027  185 LEU A CD1 
1505 C  CD2 . LEU A 184 ? 0.0827 0.2223 0.2925 0.0122  -0.0230 0.0369  185 LEU A CD2 
1506 N  N   . PRO A 185 ? 0.1478 0.1755 0.2108 -0.0126 -0.0604 0.0432  186 PRO A N   
1507 C  CA  . PRO A 185 ? 0.1253 0.1947 0.2537 -0.0139 -0.0329 0.0613  186 PRO A CA  
1508 C  C   . PRO A 185 ? 0.1151 0.1508 0.3009 -0.0190 -0.0288 0.0516  186 PRO A C   
1509 O  O   . PRO A 185 ? 0.0644 0.1741 0.4387 -0.0003 -0.0228 0.0753  186 PRO A O   
1510 C  CB  . PRO A 185 ? 0.1170 0.2037 0.2097 -0.0170 -0.0275 0.0414  186 PRO A CB  
1511 C  CG  . PRO A 185 ? 0.0844 0.1920 0.1949 0.0079  -0.0200 0.0298  186 PRO A CG  
1512 C  CD  . PRO A 185 ? 0.1164 0.1625 0.1720 -0.0060 -0.0333 0.0155  186 PRO A CD  
1513 N  N   . GLU A 186 ? 0.1243 0.1683 0.3327 -0.0318 -0.0245 0.0571  187 GLU A N   
1514 C  CA  . GLU A 186 ? 0.1372 0.2078 0.3602 -0.0207 -0.0047 0.0411  187 GLU A CA  
1515 C  C   . GLU A 186 ? 0.0735 0.2176 0.3387 -0.0116 0.0120  0.0531  187 GLU A C   
1516 O  O   . GLU A 186 ? 0.1224 0.2304 0.4474 0.0313  -0.0108 0.0260  187 GLU A O   
1517 C  CB  . GLU A 186 ? 0.2288 0.2361 0.4688 -0.0782 -0.0610 0.0635  187 GLU A CB  
1518 C  CG  . GLU A 186 ? 0.2737 0.2720 0.4302 -0.0577 -0.0923 0.1179  187 GLU A CG  
1519 C  CD  . GLU A 186 ? 0.1861 0.2684 0.4796 -0.0212 -0.0353 0.1109  187 GLU A CD  
1520 O  OE1 . GLU A 186 ? 0.2602 0.3440 0.4775 -0.1054 -0.0965 0.1322  187 GLU A OE1 
1521 O  OE2 . GLU A 186 ? 0.2506 0.3957 0.7126 -0.0758 -0.0458 0.0054  187 GLU A OE2 
1522 N  N   . SER A 187 ? 0.0713 0.2489 0.3432 -0.0168 0.0081  0.0724  188 SER A N   
1523 C  CA  . SER A 187 ? 0.1142 0.2244 0.3336 -0.0290 -0.0031 0.0674  188 SER A CA  
1524 C  C   . SER A 187 ? 0.0994 0.2086 0.2651 -0.0175 0.0538  0.0365  188 SER A C   
1525 O  O   . SER A 187 ? 0.0917 0.2430 0.3203 -0.0036 0.0535  0.0075  188 SER A O   
1526 C  CB  . SER A 187 ? 0.1121 0.2401 0.3123 -0.0203 0.0664  0.0810  188 SER A CB  
1527 O  OG  . SER A 187 ? 0.1412 0.2254 0.3597 -0.0144 0.0334  0.0317  188 SER A OG  
1528 N  N   . LEU A 188 ? 0.0934 0.1929 0.3152 -0.0159 0.0194  0.0039  189 LEU A N   
1529 C  CA  . LEU A 188 ? 0.1157 0.1819 0.2997 -0.0269 -0.0052 0.0057  189 LEU A CA  
1530 C  C   . LEU A 188 ? 0.1076 0.1746 0.2681 0.0199  0.0351  -0.0011 189 LEU A C   
1531 O  O   . LEU A 188 ? 0.1340 0.2499 0.2947 -0.0237 0.0291  -0.0411 189 LEU A O   
1532 C  CB  . LEU A 188 ? 0.1791 0.1774 0.3512 -0.0339 -0.0089 -0.0121 189 LEU A CB  
1533 C  CG  . LEU A 188 ? 0.1199 0.2349 0.4134 0.0005  0.0076  0.0548  189 LEU A CG  
1534 C  CD1 . LEU A 188 ? 0.1597 0.2207 0.5166 0.0152  0.0227  0.0510  189 LEU A CD1 
1535 C  CD2 . LEU A 188 ? 0.1112 0.3799 0.3904 -0.0117 0.0182  0.0840  189 LEU A CD2 
1536 N  N   . ASP A 189 ? 0.1062 0.2117 0.2895 0.0314  0.0366  0.0237  190 ASP A N   
1537 C  CA  . ASP A 189 ? 0.0798 0.2348 0.2361 -0.0046 0.0614  0.0000  190 ASP A CA  
1538 C  C   . ASP A 189 ? 0.0848 0.1676 0.1996 0.0025  0.0603  0.0117  190 ASP A C   
1539 O  O   . ASP A 189 ? 0.1029 0.2001 0.1918 0.0102  0.0580  -0.0044 190 ASP A O   
1540 C  CB  . ASP A 189 ? 0.2137 0.2866 0.2044 -0.0675 0.1147  0.0332  190 ASP A CB  
1541 C  CG  . ASP A 189 ? 0.1877 0.4773 0.3502 -0.0767 0.1408  0.0353  190 ASP A CG  
1542 O  OD1 . ASP A 189 ? 0.3961 0.4349 0.5216 -0.0512 -0.0279 -0.0892 190 ASP A OD1 
1543 O  OD2 . ASP A 189 ? 0.3545 0.5152 0.3809 -0.0881 -0.0013 0.0468  190 ASP A OD2 
1544 N  N   . TYR A 190 ? 0.0873 0.1886 0.2079 -0.0027 0.0725  0.0126  191 TYR A N   
1545 C  CA  . TYR A 190 ? 0.0746 0.1787 0.1800 -0.0094 0.0389  0.0240  191 TYR A CA  
1546 C  C   . TYR A 190 ? 0.1117 0.1728 0.1439 0.0253  0.0530  -0.0023 191 TYR A C   
1547 O  O   . TYR A 190 ? 0.1336 0.1943 0.1399 0.0129  0.0713  -0.0082 191 TYR A O   
1548 C  CB  . TYR A 190 ? 0.1313 0.1516 0.1702 -0.0023 0.0411  0.0102  191 TYR A CB  
1549 C  CG  . TYR A 190 ? 0.1092 0.1449 0.1823 -0.0214 0.0668  0.0185  191 TYR A CG  
1550 C  CD1 . TYR A 190 ? 0.1439 0.1687 0.1641 -0.0332 0.0605  -0.0105 191 TYR A CD1 
1551 C  CD2 . TYR A 190 ? 0.1336 0.1825 0.1914 0.0270  0.0660  0.0077  191 TYR A CD2 
1552 C  CE1 . TYR A 190 ? 0.1497 0.1762 0.1573 0.0160  0.0422  -0.0049 191 TYR A CE1 
1553 C  CE2 . TYR A 190 ? 0.1527 0.1917 0.2032 0.0023  0.0724  -0.0154 191 TYR A CE2 
1554 C  CZ  . TYR A 190 ? 0.1770 0.1624 0.1873 0.0228  0.0455  0.0025  191 TYR A CZ  
1555 O  OH  . TYR A 190 ? 0.2266 0.1740 0.2229 0.0186  0.0683  -0.0177 191 TYR A OH  
1556 N  N   . TRP A 191 ? 0.0926 0.1523 0.1638 0.0002  0.0411  0.0164  192 TRP A N   
1557 C  CA  . TRP A 191 ? 0.1225 0.1419 0.1303 0.0057  0.0328  0.0077  192 TRP A CA  
1558 C  C   . TRP A 191 ? 0.1198 0.1478 0.1105 0.0036  0.0424  -0.0024 192 TRP A C   
1559 O  O   . TRP A 191 ? 0.1537 0.1676 0.1257 -0.0032 0.0365  0.0107  192 TRP A O   
1560 C  CB  . TRP A 191 ? 0.1350 0.1559 0.1695 0.0186  0.0453  0.0111  192 TRP A CB  
1561 C  CG  . TRP A 191 ? 0.0952 0.1730 0.1570 0.0181  0.0474  0.0134  192 TRP A CG  
1562 C  CD1 . TRP A 191 ? 0.1663 0.1605 0.1713 0.0234  0.0643  0.0383  192 TRP A CD1 
1563 C  CD2 . TRP A 191 ? 0.1166 0.1419 0.1681 0.0179  0.0304  0.0188  192 TRP A CD2 
1564 N  NE1 . TRP A 191 ? 0.1557 0.1820 0.1796 0.0111  0.0717  0.0362  192 TRP A NE1 
1565 C  CE2 . TRP A 191 ? 0.1300 0.1497 0.1802 0.0435  0.0535  0.0178  192 TRP A CE2 
1566 C  CE3 . TRP A 191 ? 0.1023 0.1897 0.1728 0.0155  0.0248  -0.0077 192 TRP A CE3 
1567 C  CZ2 . TRP A 191 ? 0.1615 0.1615 0.2200 0.0064  0.0409  0.0147  192 TRP A CZ2 
1568 C  CZ3 . TRP A 191 ? 0.1102 0.1877 0.1791 -0.0035 0.0374  -0.0032 192 TRP A CZ3 
1569 C  CH2 . TRP A 191 ? 0.1033 0.1742 0.2202 0.0109  0.0358  0.0065  192 TRP A CH2 
1570 N  N   . THR A 192 ? 0.1311 0.1435 0.1163 0.0111  0.0158  0.0088  193 THR A N   
1571 C  CA  . THR A 192 ? 0.1085 0.1594 0.1304 0.0100  0.0240  0.0063  193 THR A CA  
1572 C  C   . THR A 192 ? 0.1236 0.1802 0.0909 0.0291  0.0344  0.0087  193 THR A C   
1573 O  O   . THR A 192 ? 0.1372 0.2021 0.0848 0.0167  0.0211  0.0147  193 THR A O   
1574 C  CB  . THR A 192 ? 0.1461 0.1504 0.1171 0.0217  0.0403  -0.0033 193 THR A CB  
1575 O  OG1 . THR A 192 ? 0.1306 0.1349 0.1500 0.0207  0.0249  -0.0069 193 THR A OG1 
1576 C  CG2 . THR A 192 ? 0.1687 0.2056 0.1001 0.0414  0.0275  0.0027  193 THR A CG2 
1577 N  N   . TYR A 193 ? 0.1012 0.1579 0.1075 0.0220  0.0272  -0.0176 194 TYR A N   
1578 C  CA  . TYR A 193 ? 0.1123 0.1620 0.1253 0.0283  0.0069  -0.0051 194 TYR A CA  
1579 C  C   . TYR A 193 ? 0.1189 0.1278 0.1162 0.0314  0.0039  -0.0286 194 TYR A C   
1580 O  O   . TYR A 193 ? 0.1179 0.1600 0.1063 0.0139  0.0009  -0.0137 194 TYR A O   
1581 C  CB  . TYR A 193 ? 0.1282 0.1762 0.1169 0.0557  0.0127  -0.0275 194 TYR A CB  
1582 C  CG  . TYR A 193 ? 0.1141 0.1318 0.0996 0.0263  0.0057  -0.0057 194 TYR A CG  
1583 C  CD1 . TYR A 193 ? 0.1358 0.1343 0.0834 0.0201  -0.0059 0.0040  194 TYR A CD1 
1584 C  CD2 . TYR A 193 ? 0.1013 0.1421 0.1254 0.0238  -0.0159 -0.0184 194 TYR A CD2 
1585 C  CE1 . TYR A 193 ? 0.0974 0.1336 0.1067 0.0179  0.0194  0.0201  194 TYR A CE1 
1586 C  CE2 . TYR A 193 ? 0.1182 0.1433 0.1303 0.0259  -0.0099 -0.0367 194 TYR A CE2 
1587 C  CZ  . TYR A 193 ? 0.0945 0.1148 0.1040 0.0232  0.0021  -0.0160 194 TYR A CZ  
1588 O  OH  . TYR A 193 ? 0.0990 0.1293 0.1072 0.0063  0.0070  -0.0075 194 TYR A OH  
1589 N  N   . PRO A 194 ? 0.1096 0.1643 0.1076 0.0156  -0.0003 -0.0250 195 PRO A N   
1590 C  CA  . PRO A 194 ? 0.1112 0.1465 0.1458 0.0173  0.0154  -0.0409 195 PRO A CA  
1591 C  C   . PRO A 194 ? 0.1021 0.1242 0.1166 0.0194  0.0013  -0.0263 195 PRO A C   
1592 O  O   . PRO A 194 ? 0.1390 0.1583 0.1327 0.0461  -0.0165 -0.0242 195 PRO A O   
1593 C  CB  . PRO A 194 ? 0.1688 0.1964 0.1293 0.0263  -0.0078 -0.0431 195 PRO A CB  
1594 C  CG  . PRO A 194 ? 0.1746 0.1972 0.1590 -0.0027 0.0024  -0.0228 195 PRO A CG  
1595 C  CD  . PRO A 194 ? 0.1615 0.2493 0.0958 -0.0126 0.0216  -0.0484 195 PRO A CD  
1596 N  N   . GLY A 195 ? 0.0916 0.1530 0.0979 0.0076  -0.0059 -0.0341 196 GLY A N   
1597 C  CA  . GLY A 195 ? 0.0692 0.1555 0.1407 0.0137  0.0079  0.0053  196 GLY A CA  
1598 C  C   . GLY A 195 ? 0.0873 0.1328 0.1321 -0.0027 -0.0075 -0.0148 196 GLY A C   
1599 O  O   . GLY A 195 ? 0.1072 0.1300 0.1376 0.0153  -0.0022 -0.0147 196 GLY A O   
1600 N  N   . SER A 196 ? 0.0798 0.1268 0.1282 0.0049  -0.0026 -0.0105 197 SER A N   
1601 C  CA  . SER A 196 ? 0.0619 0.1493 0.1378 0.0072  0.0061  -0.0092 197 SER A CA  
1602 C  C   . SER A 196 ? 0.0821 0.1189 0.1425 0.0044  0.0136  -0.0145 197 SER A C   
1603 O  O   . SER A 196 ? 0.0651 0.1324 0.1324 -0.0027 0.0050  -0.0044 197 SER A O   
1604 C  CB  . SER A 196 ? 0.0659 0.1358 0.2169 0.0115  -0.0034 -0.0286 197 SER A CB  
1605 O  OG  . SER A 196 ? 0.0699 0.1383 0.1476 0.0023  0.0081  -0.0175 197 SER A OG  
1606 N  N   . LEU A 197 ? 0.0549 0.1324 0.1365 -0.0004 0.0087  -0.0063 198 LEU A N   
1607 C  CA  . LEU A 197 ? 0.0879 0.1289 0.1310 -0.0279 0.0111  -0.0018 198 LEU A CA  
1608 C  C   . LEU A 197 ? 0.0591 0.1429 0.1412 -0.0089 -0.0030 -0.0104 198 LEU A C   
1609 O  O   . LEU A 197 ? 0.0688 0.1494 0.1512 -0.0027 -0.0066 -0.0277 198 LEU A O   
1610 C  CB  . LEU A 197 ? 0.0970 0.1465 0.1759 -0.0039 0.0542  0.0127  198 LEU A CB  
1611 C  CG  . LEU A 197 ? 0.0936 0.1516 0.2096 -0.0129 0.0410  0.0125  198 LEU A CG  
1612 C  CD1 . LEU A 197 ? 0.1530 0.1942 0.2385 -0.0398 0.0495  0.0520  198 LEU A CD1 
1613 C  CD2 . LEU A 197 ? 0.0965 0.1846 0.2535 0.0085  0.0260  0.0217  198 LEU A CD2 
1614 N  N   . THR A 198 ? 0.0763 0.1253 0.1505 -0.0098 0.0086  -0.0125 199 THR A N   
1615 C  CA  . THR A 198 ? 0.0656 0.1365 0.1465 -0.0077 0.0287  0.0003  199 THR A CA  
1616 C  C   . THR A 198 ? 0.0566 0.1703 0.1478 0.0034  0.0206  -0.0033 199 THR A C   
1617 O  O   . THR A 198 ? 0.0627 0.1669 0.1763 0.0044  0.0141  -0.0222 199 THR A O   
1618 C  CB  . THR A 198 ? 0.0686 0.1370 0.1189 -0.0069 0.0093  -0.0037 199 THR A CB  
1619 O  OG1 . THR A 198 ? 0.0842 0.1428 0.1171 -0.0084 0.0113  0.0148  199 THR A OG1 
1620 C  CG2 . THR A 198 ? 0.1073 0.1347 0.1302 0.0100  0.0423  -0.0212 199 THR A CG2 
1621 N  N   . THR A 199 ? 0.1008 0.1809 0.1683 -0.0172 0.0485  -0.0006 200 THR A N   
1622 C  CA  . THR A 199 ? 0.1189 0.1676 0.1532 -0.0309 0.0536  -0.0183 200 THR A CA  
1623 C  C   . THR A 199 ? 0.0866 0.1821 0.1986 -0.0187 0.0451  -0.0100 200 THR A C   
1624 O  O   . THR A 199 ? 0.0839 0.1756 0.2281 -0.0176 0.0491  -0.0245 200 THR A O   
1625 C  CB  . THR A 199 ? 0.1530 0.2202 0.1656 -0.0497 0.0381  -0.0247 200 THR A CB  
1626 O  OG1 . THR A 199 ? 0.3610 0.2067 0.2413 -0.0209 -0.0400 -0.0008 200 THR A OG1 
1627 C  CG2 . THR A 199 ? 0.1487 0.2104 0.1733 -0.0598 0.0313  -0.0176 200 THR A CG2 
1628 N  N   . PRO A 200 ? 0.0920 0.1852 0.2018 -0.0310 0.0599  -0.0149 201 PRO A N   
1629 C  CA  . PRO A 200 ? 0.0748 0.1911 0.2740 -0.0328 0.0566  0.0294  201 PRO A CA  
1630 C  C   . PRO A 200 ? 0.0942 0.1999 0.2323 -0.0157 0.0265  -0.0106 201 PRO A C   
1631 O  O   . PRO A 200 ? 0.1130 0.2112 0.2405 -0.0068 0.0138  0.0070  201 PRO A O   
1632 C  CB  . PRO A 200 ? 0.0785 0.2334 0.2575 -0.0058 0.0450  0.0132  201 PRO A CB  
1633 C  CG  . PRO A 200 ? 0.1155 0.2390 0.2164 -0.0236 0.0203  0.0103  201 PRO A CG  
1634 C  CD  . PRO A 200 ? 0.1005 0.2291 0.2327 -0.0006 0.0626  -0.0220 201 PRO A CD  
1635 N  N   . PRO A 201 ? 0.0880 0.1950 0.2004 -0.0158 0.0299  0.0070  202 PRO A N   
1636 C  CA  . PRO A 201 ? 0.1279 0.1781 0.2130 -0.0118 0.0208  0.0151  202 PRO A CA  
1637 C  C   . PRO A 201 ? 0.0987 0.1719 0.2076 -0.0209 0.0309  0.0052  202 PRO A C   
1638 O  O   . PRO A 201 ? 0.0945 0.1842 0.2721 -0.0125 0.0215  -0.0391 202 PRO A O   
1639 C  CB  . PRO A 201 ? 0.1103 0.1719 0.2533 -0.0032 0.0464  0.0161  202 PRO A CB  
1640 C  CG  . PRO A 201 ? 0.1379 0.2227 0.2956 0.0058  -0.0048 -0.0127 202 PRO A CG  
1641 C  CD  . PRO A 201 ? 0.1771 0.2141 0.2078 0.0055  0.0174  0.0290  202 PRO A CD  
1642 N  N   . LEU A 202 ? 0.0785 0.1544 0.2160 -0.0018 0.0442  -0.0033 203 LEU A N   
1643 C  CA  . LEU A 202 ? 0.0769 0.1681 0.1807 0.0049  0.0170  -0.0142 203 LEU A CA  
1644 C  C   . LEU A 202 ? 0.0674 0.1577 0.2060 -0.0129 0.0104  -0.0223 203 LEU A C   
1645 O  O   . LEU A 202 ? 0.0729 0.1584 0.2035 0.0012  0.0021  -0.0234 203 LEU A O   
1646 C  CB  . LEU A 202 ? 0.0645 0.1731 0.2133 0.0081  -0.0046 -0.0366 203 LEU A CB  
1647 C  CG  . LEU A 202 ? 0.0688 0.1643 0.2259 -0.0010 -0.0039 -0.0412 203 LEU A CG  
1648 C  CD1 . LEU A 202 ? 0.0550 0.2029 0.2680 0.0079  0.0121  -0.0197 203 LEU A CD1 
1649 C  CD2 . LEU A 202 ? 0.0821 0.1591 0.2103 -0.0066 0.0201  -0.0118 203 LEU A CD2 
1650 N  N   . ASN A 203 ? 0.0956 0.1550 0.2103 -0.0006 0.0201  -0.0223 204 ASN A N   
1651 C  CA  . ASN A 203 ? 0.0930 0.1473 0.2088 -0.0199 0.0291  -0.0242 204 ASN A CA  
1652 C  C   . ASN A 203 ? 0.0961 0.1324 0.1767 -0.0018 0.0307  -0.0346 204 ASN A C   
1653 O  O   . ASN A 203 ? 0.0884 0.1532 0.1687 -0.0025 -0.0029 -0.0268 204 ASN A O   
1654 C  CB  . ASN A 203 ? 0.1436 0.1468 0.2657 -0.0085 0.0156  0.0182  204 ASN A CB  
1655 C  CG  . ASN A 203 ? 0.1429 0.1685 0.2920 -0.0073 0.0535  -0.0066 204 ASN A CG  
1656 O  OD1 . ASN A 203 ? 0.1688 0.1981 0.4417 0.0006  0.1060  0.0401  204 ASN A OD1 
1657 N  ND2 . ASN A 203 ? 0.2415 0.1837 0.3283 0.0367  0.0924  0.0316  204 ASN A ND2 
1658 N  N   . GLU A 204 ? 0.1185 0.1561 0.2035 -0.0141 0.0104  -0.0638 205 GLU A N   
1659 C  CA  . GLU A 204 ? 0.1020 0.1681 0.1741 0.0267  -0.0189 -0.0562 205 GLU A CA  
1660 C  C   . GLU A 204 ? 0.1345 0.1418 0.1909 0.0292  -0.0308 -0.0425 205 GLU A C   
1661 O  O   . GLU A 204 ? 0.1458 0.2182 0.2015 0.0444  -0.0532 -0.0688 205 GLU A O   
1662 C  CB  . GLU A 204 ? 0.1498 0.1703 0.2313 0.0306  -0.0738 -0.0790 205 GLU A CB  
1663 C  CG  . GLU A 204 ? 0.1406 0.1940 0.2194 0.0397  -0.0570 -0.0463 205 GLU A CG  
1664 C  CD  . GLU A 204 ? 0.1584 0.1924 0.1852 -0.0227 -0.0558 -0.0287 205 GLU A CD  
1665 O  OE1 . GLU A 204 ? 0.1780 0.2369 0.3001 0.0013  -0.1153 -0.0879 205 GLU A OE1 
1666 O  OE2 . GLU A 204 ? 0.1461 0.2008 0.2347 -0.0026 -0.0595 -0.0192 205 GLU A OE2 
1667 N  N   . CYS A 205 ? 0.0976 0.1289 0.1638 0.0089  -0.0147 -0.0085 206 CYS A N   
1668 C  CA  . CYS A 205 ? 0.0875 0.1361 0.1516 0.0027  -0.0130 -0.0100 206 CYS A CA  
1669 C  C   . CYS A 205 ? 0.0900 0.1205 0.1622 0.0026  -0.0219 -0.0157 206 CYS A C   
1670 O  O   . CYS A 205 ? 0.1069 0.1328 0.2035 0.0034  -0.0394 0.0120  206 CYS A O   
1671 C  CB  . CYS A 205 ? 0.1432 0.1817 0.1329 0.0099  -0.0002 0.0018  206 CYS A CB  
1672 S  SG  . CYS A 205 ? 0.1396 0.1618 0.1684 0.0068  -0.0100 -0.0217 206 CYS A SG  
1673 N  N   . VAL A 206 ? 0.1087 0.1198 0.1365 -0.0190 -0.0182 -0.0104 207 VAL A N   
1674 C  CA  . VAL A 206 ? 0.0803 0.1163 0.1231 0.0006  0.0052  -0.0137 207 VAL A CA  
1675 C  C   . VAL A 206 ? 0.0913 0.1199 0.1118 0.0113  0.0005  -0.0074 207 VAL A C   
1676 O  O   . VAL A 206 ? 0.1056 0.1503 0.1328 0.0116  0.0072  0.0140  207 VAL A O   
1677 C  CB  . VAL A 206 ? 0.0802 0.1285 0.1306 -0.0082 0.0121  -0.0335 207 VAL A CB  
1678 C  CG1 . VAL A 206 ? 0.0819 0.1439 0.1487 0.0061  -0.0269 -0.0474 207 VAL A CG1 
1679 C  CG2 . VAL A 206 ? 0.1075 0.1559 0.1311 0.0113  0.0303  -0.0157 207 VAL A CG2 
1680 N  N   . THR A 207 ? 0.0898 0.1085 0.1412 0.0017  0.0017  -0.0082 208 THR A N   
1681 C  CA  . THR A 207 ? 0.1189 0.1188 0.1271 0.0057  0.0179  -0.0190 208 THR A CA  
1682 C  C   . THR A 207 ? 0.0992 0.1044 0.1017 0.0027  0.0171  0.0074  208 THR A C   
1683 O  O   . THR A 207 ? 0.1200 0.1318 0.1049 0.0069  0.0015  0.0120  208 THR A O   
1684 C  CB  . THR A 207 ? 0.1368 0.1162 0.1376 0.0153  0.0155  -0.0226 208 THR A CB  
1685 O  OG1 . THR A 207 ? 0.1392 0.1329 0.1897 0.0002  0.0237  -0.0530 208 THR A OG1 
1686 C  CG2 . THR A 207 ? 0.1209 0.1530 0.1680 -0.0124 0.0176  -0.0104 208 THR A CG2 
1687 N  N   . TRP A 208 ? 0.1004 0.0961 0.1203 0.0116  0.0210  0.0038  209 TRP A N   
1688 C  CA  . TRP A 208 ? 0.0681 0.1047 0.1343 0.0087  0.0206  -0.0082 209 TRP A CA  
1689 C  C   . TRP A 208 ? 0.0671 0.1349 0.1157 -0.0009 0.0100  -0.0042 209 TRP A C   
1690 O  O   . TRP A 208 ? 0.1085 0.1393 0.1130 0.0079  0.0130  0.0037  209 TRP A O   
1691 C  CB  . TRP A 208 ? 0.0909 0.1213 0.0891 0.0283  0.0223  0.0084  209 TRP A CB  
1692 C  CG  . TRP A 208 ? 0.0685 0.1299 0.1022 0.0088  0.0138  -0.0099 209 TRP A CG  
1693 C  CD1 . TRP A 208 ? 0.0760 0.1214 0.1254 0.0030  0.0070  -0.0061 209 TRP A CD1 
1694 C  CD2 . TRP A 208 ? 0.0771 0.0938 0.1128 0.0032  -0.0043 -0.0058 209 TRP A CD2 
1695 N  NE1 . TRP A 208 ? 0.0956 0.1349 0.1277 0.0157  0.0037  -0.0132 209 TRP A NE1 
1696 C  CE2 . TRP A 208 ? 0.0753 0.1297 0.1097 0.0088  -0.0005 0.0120  209 TRP A CE2 
1697 C  CE3 . TRP A 208 ? 0.1040 0.0970 0.0988 0.0128  -0.0155 -0.0129 209 TRP A CE3 
1698 C  CZ2 . TRP A 208 ? 0.0900 0.1422 0.1173 0.0294  0.0065  0.0091  209 TRP A CZ2 
1699 C  CZ3 . TRP A 208 ? 0.1049 0.1494 0.1078 0.0204  0.0141  -0.0139 209 TRP A CZ3 
1700 C  CH2 . TRP A 208 ? 0.1032 0.1130 0.1161 0.0229  0.0223  -0.0113 209 TRP A CH2 
1701 N  N   . ILE A 209 ? 0.0690 0.1238 0.1189 0.0049  0.0069  -0.0065 210 ILE A N   
1702 C  CA  . ILE A 209 ? 0.0719 0.1213 0.1479 0.0026  0.0113  -0.0035 210 ILE A CA  
1703 C  C   . ILE A 209 ? 0.0828 0.1252 0.1128 0.0057  0.0114  0.0043  210 ILE A C   
1704 O  O   . ILE A 209 ? 0.1136 0.1331 0.1097 0.0100  0.0037  0.0086  210 ILE A O   
1705 C  CB  . ILE A 209 ? 0.0732 0.1203 0.1774 0.0063  0.0211  0.0081  210 ILE A CB  
1706 C  CG1 . ILE A 209 ? 0.1117 0.1142 0.2250 0.0320  0.0209  -0.0160 210 ILE A CG1 
1707 C  CG2 . ILE A 209 ? 0.0728 0.1577 0.1857 -0.0107 0.0200  -0.0013 210 ILE A CG2 
1708 C  CD1 . ILE A 209 ? 0.1417 0.1550 0.3063 0.0594  0.0212  0.0048  210 ILE A CD1 
1709 N  N   . VAL A 210 ? 0.0730 0.1185 0.1407 0.0174  0.0192  0.0006  211 VAL A N   
1710 C  CA  . VAL A 210 ? 0.0877 0.1146 0.1205 0.0089  0.0233  0.0030  211 VAL A CA  
1711 C  C   . VAL A 210 ? 0.0985 0.1048 0.1275 0.0062  0.0322  0.0207  211 VAL A C   
1712 O  O   . VAL A 210 ? 0.1038 0.1412 0.1275 -0.0026 0.0369  0.0179  211 VAL A O   
1713 C  CB  . VAL A 210 ? 0.0611 0.1340 0.1236 0.0049  0.0221  -0.0032 211 VAL A CB  
1714 C  CG1 . VAL A 210 ? 0.0933 0.1082 0.1821 0.0099  0.0128  -0.0034 211 VAL A CG1 
1715 C  CG2 . VAL A 210 ? 0.0627 0.1455 0.1789 0.0042  0.0230  0.0117  211 VAL A CG2 
1716 N  N   . LEU A 211 ? 0.0742 0.1304 0.1505 0.0010  0.0259  0.0109  212 LEU A N   
1717 C  CA  . LEU A 211 ? 0.0842 0.1302 0.1469 -0.0153 0.0195  0.0137  212 LEU A CA  
1718 C  C   . LEU A 211 ? 0.1040 0.1335 0.1475 -0.0153 0.0414  0.0200  212 LEU A C   
1719 O  O   . LEU A 211 ? 0.0792 0.1550 0.1666 -0.0087 0.0131  0.0037  212 LEU A O   
1720 C  CB  . LEU A 211 ? 0.1040 0.1468 0.1450 -0.0122 0.0111  0.0188  212 LEU A CB  
1721 C  CG  . LEU A 211 ? 0.1032 0.1519 0.1684 0.0010  -0.0009 0.0234  212 LEU A CG  
1722 C  CD1 . LEU A 211 ? 0.1065 0.2173 0.1975 -0.0176 -0.0219 0.0270  212 LEU A CD1 
1723 C  CD2 . LEU A 211 ? 0.1230 0.1782 0.2026 0.0015  0.0498  0.0134  212 LEU A CD2 
1724 N  N   . LYS A 212 ? 0.0875 0.1659 0.1311 -0.0244 0.0255  0.0355  213 LYS A N   
1725 C  CA  . LYS A 212 ? 0.1828 0.1577 0.1211 -0.0111 0.0388  0.0159  213 LYS A CA  
1726 C  C   . LYS A 212 ? 0.1253 0.1454 0.1645 -0.0139 0.0179  0.0200  213 LYS A C   
1727 O  O   . LYS A 212 ? 0.1247 0.1519 0.2237 -0.0069 -0.0075 0.0201  213 LYS A O   
1728 C  CB  . LYS A 212 ? 0.2496 0.2010 0.1123 -0.0561 0.0504  -0.0039 213 LYS A CB  
1729 C  CG  . LYS A 212 ? 0.3581 0.2241 0.2552 -0.0436 0.0241  0.0539  213 LYS A CG  
1730 C  CD  . LYS A 212 ? 0.6728 0.3323 0.2728 -0.2044 0.1205  0.0104  213 LYS A CD  
1731 N  N   . GLU A 213 ? 0.0810 0.1652 0.1690 -0.0152 0.0181  0.0081  214 GLU A N   
1732 C  CA  . GLU A 213 ? 0.0911 0.1588 0.1677 -0.0174 0.0152  0.0063  214 GLU A CA  
1733 C  C   . GLU A 213 ? 0.0951 0.1379 0.1738 0.0034  0.0061  0.0218  214 GLU A C   
1734 O  O   . GLU A 213 ? 0.0768 0.1450 0.1881 -0.0087 0.0051  0.0286  214 GLU A O   
1735 C  CB  . GLU A 213 ? 0.0868 0.1819 0.2333 -0.0109 0.0013  0.0145  214 GLU A CB  
1736 C  CG  . GLU A 213 ? 0.1214 0.2160 0.2744 -0.0413 -0.0339 -0.0027 214 GLU A CG  
1737 C  CD  . GLU A 213 ? 0.1126 0.3195 0.4242 -0.0586 -0.0259 -0.0190 214 GLU A CD  
1738 O  OE1 . GLU A 213 ? 0.0839 0.2420 0.4769 -0.0344 0.0122  0.0350  214 GLU A OE1 
1739 O  OE2 . GLU A 213 ? 0.4787 0.7929 0.4110 -0.0807 -0.0108 -0.2184 214 GLU A OE2 
1740 N  N   . PRO A 214 ? 0.0884 0.1286 0.1670 -0.0190 0.0013  0.0128  215 PRO A N   
1741 C  CA  . PRO A 214 ? 0.1072 0.1363 0.1532 0.0034  -0.0073 -0.0127 215 PRO A CA  
1742 C  C   . PRO A 214 ? 0.1107 0.1397 0.1827 -0.0245 -0.0214 0.0190  215 PRO A C   
1743 O  O   . PRO A 214 ? 0.1071 0.1906 0.2505 -0.0431 -0.0319 0.0356  215 PRO A O   
1744 C  CB  . PRO A 214 ? 0.1401 0.1093 0.2180 -0.0149 0.0127  -0.0094 215 PRO A CB  
1745 C  CG  . PRO A 214 ? 0.2753 0.1899 0.2861 0.0487  0.1277  0.0346  215 PRO A CG  
1746 C  CD  . PRO A 214 ? 0.1514 0.1390 0.2065 0.0030  0.0554  0.0295  215 PRO A CD  
1747 N  N   . ILE A 215 ? 0.1171 0.1364 0.1448 0.0047  -0.0343 0.0124  216 ILE A N   
1748 C  CA  . ILE A 215 ? 0.1410 0.1526 0.1543 0.0164  -0.0480 -0.0097 216 ILE A CA  
1749 C  C   . ILE A 215 ? 0.1224 0.1543 0.1716 0.0107  -0.0207 -0.0020 216 ILE A C   
1750 O  O   . ILE A 215 ? 0.1139 0.1516 0.1907 0.0146  -0.0103 -0.0174 216 ILE A O   
1751 C  CB  . ILE A 215 ? 0.1368 0.1415 0.1907 0.0147  -0.0343 -0.0102 216 ILE A CB  
1752 C  CG1 . ILE A 215 ? 0.1627 0.1342 0.1573 -0.0022 -0.0355 0.0065  216 ILE A CG1 
1753 C  CG2 . ILE A 215 ? 0.1509 0.1559 0.2189 0.0032  -0.0170 -0.0425 216 ILE A CG2 
1754 C  CD1 . ILE A 215 ? 0.2033 0.1478 0.2227 0.0106  -0.0520 0.0462  216 ILE A CD1 
1755 N  N   . SER A 216 ? 0.1656 0.1277 0.1911 -0.0163 -0.0374 -0.0070 217 SER A N   
1756 C  CA  A SER A 216 ? 0.1881 0.1533 0.1821 -0.0150 -0.0031 -0.0160 217 SER A CA  
1757 C  CA  B SER A 216 ? 0.1331 0.1616 0.1809 0.0055  -0.0129 -0.0078 217 SER A CA  
1758 C  C   . SER A 216 ? 0.1534 0.0933 0.1838 -0.0153 -0.0187 -0.0051 217 SER A C   
1759 O  O   . SER A 216 ? 0.1540 0.1702 0.1878 0.0165  -0.0234 0.0041  217 SER A O   
1760 C  CB  A SER A 216 ? 0.2834 0.1126 0.1918 -0.0329 -0.0006 -0.0505 217 SER A CB  
1761 C  CB  B SER A 216 ? 0.3231 0.0927 0.2336 -0.0710 0.0078  0.0649  217 SER A CB  
1762 O  OG  A SER A 216 ? 0.1949 0.1975 0.2160 -0.0348 -0.0043 -0.0130 217 SER A OG  
1763 O  OG  B SER A 216 ? 0.3210 0.1848 0.2365 -0.0309 -0.0151 0.0176  217 SER A OG  
1764 N  N   . VAL A 217 ? 0.1451 0.1368 0.1559 -0.0120 -0.0208 -0.0121 218 VAL A N   
1765 C  CA  . VAL A 217 ? 0.1498 0.1241 0.1627 -0.0168 -0.0175 -0.0107 218 VAL A CA  
1766 C  C   . VAL A 217 ? 0.1296 0.1078 0.1742 -0.0114 -0.0343 0.0034  218 VAL A C   
1767 O  O   . VAL A 217 ? 0.1698 0.1315 0.1712 -0.0126 -0.0592 0.0051  218 VAL A O   
1768 C  CB  . VAL A 217 ? 0.1577 0.1231 0.2071 -0.0234 -0.0597 -0.0044 218 VAL A CB  
1769 C  CG1 . VAL A 217 ? 0.2099 0.1188 0.1806 0.0064  -0.0267 0.0012  218 VAL A CG1 
1770 C  CG2 . VAL A 217 ? 0.1756 0.1272 0.2430 -0.0092 -0.0806 -0.0069 218 VAL A CG2 
1771 N  N   . SER A 218 ? 0.1820 0.1168 0.1670 -0.0071 -0.0567 -0.0053 219 SER A N   
1772 C  CA  . SER A 218 ? 0.1486 0.1202 0.1967 -0.0027 -0.0263 -0.0160 219 SER A CA  
1773 C  C   . SER A 218 ? 0.1491 0.1080 0.1537 -0.0127 -0.0326 0.0003  219 SER A C   
1774 O  O   . SER A 218 ? 0.1713 0.1163 0.1597 -0.0201 -0.0340 0.0095  219 SER A O   
1775 C  CB  . SER A 218 ? 0.1843 0.1666 0.1913 -0.0227 -0.0317 -0.0044 219 SER A CB  
1776 O  OG  . SER A 218 ? 0.1806 0.1674 0.2028 -0.0280 -0.0370 -0.0158 219 SER A OG  
1777 N  N   . SER A 219 ? 0.1950 0.1132 0.1611 0.0167  -0.0277 -0.0080 220 SER A N   
1778 C  CA  . SER A 219 ? 0.2074 0.1177 0.1925 0.0077  -0.0043 -0.0019 220 SER A CA  
1779 C  C   . SER A 219 ? 0.2137 0.1209 0.2185 -0.0409 -0.0500 0.0044  220 SER A C   
1780 O  O   . SER A 219 ? 0.1988 0.1303 0.2430 -0.0294 -0.0214 0.0062  220 SER A O   
1781 C  CB  . SER A 219 ? 0.2723 0.1098 0.2549 -0.0355 -0.0251 -0.0025 220 SER A CB  
1782 O  OG  . SER A 219 ? 0.2766 0.1540 0.3107 -0.0234 -0.0250 -0.0212 220 SER A OG  
1783 N  N   . GLU A 220 ? 0.2006 0.1644 0.1579 -0.0138 -0.0141 -0.0129 221 GLU A N   
1784 C  CA  . GLU A 220 ? 0.2444 0.1615 0.1904 -0.0185 -0.0417 0.0006  221 GLU A CA  
1785 C  C   . GLU A 220 ? 0.2155 0.1551 0.1494 0.0000  -0.0266 -0.0027 221 GLU A C   
1786 O  O   . GLU A 220 ? 0.2670 0.1640 0.1623 0.0036  0.0181  -0.0162 221 GLU A O   
1787 C  CB  . GLU A 220 ? 0.2524 0.1976 0.1943 -0.0548 -0.0509 -0.0471 221 GLU A CB  
1788 C  CG  . GLU A 220 ? 0.3813 0.1960 0.3153 -0.0282 -0.0458 -0.0692 221 GLU A CG  
1789 C  CD  . GLU A 220 ? 0.4230 0.1886 0.3752 -0.0595 -0.0348 -0.0639 221 GLU A CD  
1790 O  OE1 . GLU A 220 ? 0.2755 0.2407 0.3216 -0.0828 -0.0495 -0.0421 221 GLU A OE1 
1791 O  OE2 . GLU A 220 ? 0.6770 0.2972 0.4516 -0.2384 0.0963  -0.1434 221 GLU A OE2 
1792 N  N   . GLN A 221 ? 0.1810 0.1346 0.1691 0.0005  -0.0390 -0.0011 222 GLN A N   
1793 C  CA  . GLN A 221 ? 0.1827 0.1371 0.1500 0.0114  -0.0507 -0.0192 222 GLN A CA  
1794 C  C   . GLN A 221 ? 0.1789 0.1324 0.1498 -0.0096 -0.0368 0.0145  222 GLN A C   
1795 O  O   . GLN A 221 ? 0.2010 0.1536 0.1483 -0.0280 -0.0133 0.0204  222 GLN A O   
1796 C  CB  . GLN A 221 ? 0.1728 0.1570 0.1430 0.0046  -0.0289 -0.0099 222 GLN A CB  
1797 C  CG  . GLN A 221 ? 0.2033 0.1588 0.1777 -0.0087 -0.0609 -0.0236 222 GLN A CG  
1798 C  CD  . GLN A 221 ? 0.1892 0.1082 0.1584 -0.0253 -0.0615 0.0104  222 GLN A CD  
1799 O  OE1 . GLN A 221 ? 0.1785 0.1487 0.1587 0.0035  -0.0498 0.0130  222 GLN A OE1 
1800 N  NE2 . GLN A 221 ? 0.2006 0.1216 0.1943 0.0012  -0.0595 0.0125  222 GLN A NE2 
1801 N  N   . VAL A 222 ? 0.1703 0.1430 0.1643 -0.0122 -0.0496 0.0218  223 VAL A N   
1802 C  CA  . VAL A 222 ? 0.1318 0.1652 0.1702 -0.0025 -0.0171 0.0231  223 VAL A CA  
1803 C  C   . VAL A 222 ? 0.1810 0.1544 0.1734 -0.0296 0.0243  0.0220  223 VAL A C   
1804 O  O   . VAL A 222 ? 0.1886 0.1860 0.1385 -0.0269 0.0063  0.0242  223 VAL A O   
1805 C  CB  . VAL A 222 ? 0.2026 0.2327 0.1832 -0.0008 -0.0743 0.0378  223 VAL A CB  
1806 C  CG1 . VAL A 222 ? 0.2707 0.2426 0.2520 -0.0208 -0.0280 0.0240  223 VAL A CG1 
1807 C  CG2 . VAL A 222 ? 0.2310 0.2302 0.2535 -0.0513 -0.0807 0.0151  223 VAL A CG2 
1808 N  N   A LEU A 223 ? 0.2144 0.1618 0.1777 0.0006  0.0146  0.0060  224 LEU A N   
1809 N  N   B LEU A 223 ? 0.2022 0.1620 0.1728 -0.0013 0.0278  0.0038  224 LEU A N   
1810 C  CA  A LEU A 223 ? 0.2219 0.2101 0.2123 -0.0231 0.0345  -0.0117 224 LEU A CA  
1811 C  CA  B LEU A 223 ? 0.2202 0.1776 0.2025 -0.0248 0.0447  -0.0253 224 LEU A CA  
1812 C  C   A LEU A 223 ? 0.1753 0.2126 0.2046 -0.0100 0.0027  -0.0094 224 LEU A C   
1813 C  C   B LEU A 223 ? 0.1878 0.1986 0.1841 -0.0092 0.0100  -0.0172 224 LEU A C   
1814 O  O   A LEU A 223 ? 0.1730 0.1992 0.2241 -0.0020 0.0177  -0.0127 224 LEU A O   
1815 O  O   B LEU A 223 ? 0.2026 0.2496 0.1846 -0.0175 0.0365  -0.0283 224 LEU A O   
1816 C  CB  A LEU A 223 ? 0.2561 0.2123 0.3597 -0.0523 -0.0333 -0.0205 224 LEU A CB  
1817 C  CB  B LEU A 223 ? 0.2737 0.1429 0.2894 0.0201  0.0389  -0.0665 224 LEU A CB  
1818 C  CG  A LEU A 223 ? 0.3380 0.4730 0.4557 0.0683  0.0416  -0.0480 224 LEU A CG  
1819 C  CG  B LEU A 223 ? 0.3611 0.1512 0.2646 -0.0340 0.0737  -0.0388 224 LEU A CG  
1820 C  CD2 . LEU A 223 ? 0.4485 0.2852 0.5578 0.0851  0.1033  0.0058  224 LEU A CD2 
1821 N  N   . LYS A 224 ? 0.2179 0.1801 0.1623 -0.0114 -0.0183 0.0024  225 LYS A N   
1822 C  CA  . LYS A 224 ? 0.2187 0.2057 0.1577 -0.0176 0.0249  0.0020  225 LYS A CA  
1823 C  C   . LYS A 224 ? 0.2326 0.1940 0.1236 -0.0098 0.0231  0.0070  225 LYS A C   
1824 O  O   . LYS A 224 ? 0.1999 0.2259 0.1390 -0.0204 0.0219  0.0035  225 LYS A O   
1825 C  CB  . LYS A 224 ? 0.2961 0.2345 0.1993 0.0367  -0.0249 0.0284  225 LYS A CB  
1826 C  CG  . LYS A 224 ? 0.2464 0.3555 0.3142 -0.0138 -0.0355 0.0041  225 LYS A CG  
1827 N  N   . PHE A 225 ? 0.2347 0.1600 0.1084 -0.0053 0.0037  0.0079  226 PHE A N   
1828 C  CA  . PHE A 225 ? 0.2126 0.1426 0.1139 0.0039  0.0087  -0.0063 226 PHE A CA  
1829 C  C   . PHE A 225 ? 0.2284 0.1753 0.1297 -0.0117 0.0232  0.0158  226 PHE A C   
1830 O  O   . PHE A 225 ? 0.2177 0.1940 0.1442 -0.0170 0.0211  -0.0104 226 PHE A O   
1831 C  CB  . PHE A 225 ? 0.1821 0.1813 0.1193 -0.0023 0.0332  -0.0049 226 PHE A CB  
1832 C  CG  . PHE A 225 ? 0.1767 0.1548 0.1429 -0.0030 0.0233  -0.0031 226 PHE A CG  
1833 C  CD1 . PHE A 225 ? 0.2162 0.1976 0.1798 0.0030  -0.0039 -0.0002 226 PHE A CD1 
1834 C  CD2 . PHE A 225 ? 0.1619 0.2473 0.1489 -0.0117 0.0408  -0.0135 226 PHE A CD2 
1835 C  CE1 . PHE A 225 ? 0.2341 0.2119 0.2015 0.0297  -0.0126 0.0064  226 PHE A CE1 
1836 C  CE2 . PHE A 225 ? 0.1340 0.2545 0.2489 0.0138  0.0150  -0.0409 226 PHE A CE2 
1837 C  CZ  . PHE A 225 ? 0.2105 0.2568 0.2280 -0.0002 -0.0414 -0.0782 226 PHE A CZ  
1838 N  N   . ARG A 226 ? 0.1927 0.1708 0.1306 0.0088  0.0290  -0.0020 227 ARG A N   
1839 C  CA  . ARG A 226 ? 0.2037 0.2007 0.1302 0.0126  0.0683  0.0117  227 ARG A CA  
1840 C  C   . ARG A 226 ? 0.2075 0.2063 0.1091 -0.0037 0.0424  0.0190  227 ARG A C   
1841 O  O   . ARG A 226 ? 0.1820 0.2717 0.1932 -0.0205 0.0341  -0.0025 227 ARG A O   
1842 C  CB  . ARG A 226 ? 0.2385 0.1724 0.1209 0.0021  0.0218  0.0134  227 ARG A CB  
1843 C  CG  . ARG A 226 ? 0.1976 0.1530 0.1322 -0.0245 0.0401  0.0071  227 ARG A CG  
1844 C  CD  . ARG A 226 ? 0.2834 0.1539 0.1483 0.0075  0.0633  0.0030  227 ARG A CD  
1845 N  NE  . ARG A 226 ? 0.2459 0.1651 0.1178 -0.0186 0.0070  0.0064  227 ARG A NE  
1846 C  CZ  . ARG A 226 ? 0.2094 0.1496 0.1767 -0.0233 0.0038  -0.0261 227 ARG A CZ  
1847 N  NH1 . ARG A 226 ? 0.3133 0.2304 0.2509 -0.0712 0.0030  -0.1010 227 ARG A NH1 
1848 N  NH2 . ARG A 226 ? 0.2291 0.1778 0.1993 -0.0366 0.0160  -0.0139 227 ARG A NH2 
1849 N  N   . LYS A 227 ? 0.2039 0.2306 0.0987 -0.0215 0.0161  -0.0237 228 LYS A N   
1850 C  CA  . LYS A 227 ? 0.2731 0.2455 0.0996 -0.0681 0.0343  -0.0083 228 LYS A CA  
1851 C  C   . LYS A 227 ? 0.2611 0.2121 0.0907 -0.0400 0.0149  -0.0307 228 LYS A C   
1852 O  O   . LYS A 227 ? 0.2938 0.2615 0.1263 -0.0207 0.0712  -0.0354 228 LYS A O   
1853 C  CB  . LYS A 227 ? 0.3004 0.2736 0.1248 -0.0347 0.0000  -0.0096 228 LYS A CB  
1854 C  CG  . LYS A 227 ? 0.3533 0.3719 0.1340 -0.1278 0.0104  -0.0450 228 LYS A CG  
1855 C  CD  . LYS A 227 ? 0.4596 0.5253 0.2728 0.0012  -0.1159 -0.1317 228 LYS A CD  
1856 C  CE  . LYS A 227 ? 0.6884 0.7210 0.2736 -0.1251 -0.0374 -0.0460 228 LYS A CE  
1857 N  N   . LEU A 228 ? 0.2767 0.1961 0.1118 -0.0497 0.0216  -0.0257 229 LEU A N   
1858 C  CA  . LEU A 228 ? 0.2680 0.1903 0.1191 -0.0365 0.0251  -0.0179 229 LEU A CA  
1859 C  C   . LEU A 228 ? 0.2807 0.2151 0.1619 -0.0166 0.0666  -0.0291 229 LEU A C   
1860 O  O   . LEU A 228 ? 0.2435 0.2128 0.1381 -0.0337 0.0447  -0.0174 229 LEU A O   
1861 C  CB  . LEU A 228 ? 0.2093 0.2146 0.1340 -0.0414 0.0468  -0.0287 229 LEU A CB  
1862 C  CG  . LEU A 228 ? 0.2606 0.1954 0.1213 0.0053  0.0138  0.0034  229 LEU A CG  
1863 C  CD1 . LEU A 228 ? 0.2771 0.2001 0.1403 -0.0238 0.0188  -0.0330 229 LEU A CD1 
1864 C  CD2 . LEU A 228 ? 0.3686 0.2166 0.1536 -0.0274 -0.0143 0.0255  229 LEU A CD2 
1865 N  N   . ASN A 229 ? 0.3030 0.2421 0.1126 -0.0477 0.0416  -0.0083 230 ASN A N   
1866 C  CA  . ASN A 229 ? 0.2680 0.3182 0.1063 -0.1126 0.0660  -0.0353 230 ASN A CA  
1867 C  C   . ASN A 229 ? 0.2694 0.3043 0.1444 -0.1059 0.0688  -0.0173 230 ASN A C   
1868 O  O   . ASN A 229 ? 0.3712 0.2780 0.1289 -0.0916 0.1037  -0.0172 230 ASN A O   
1869 C  CB  . ASN A 229 ? 0.3365 0.2989 0.1130 -0.0604 0.0775  -0.0068 230 ASN A CB  
1870 C  CG  . ASN A 229 ? 0.3260 0.3229 0.1361 -0.0969 0.0593  -0.0352 230 ASN A CG  
1871 O  OD1 . ASN A 229 ? 0.4936 0.4054 0.1473 -0.0690 0.0986  -0.0642 230 ASN A OD1 
1872 N  ND2 . ASN A 229 ? 0.3219 0.3179 0.1819 -0.0782 0.0924  -0.0612 230 ASN A ND2 
1873 N  N   . PHE A 230 ? 0.2505 0.2873 0.1264 -0.1064 0.0591  -0.0282 231 PHE A N   
1874 C  CA  . PHE A 230 ? 0.2847 0.2503 0.1304 -0.1206 0.0609  -0.0185 231 PHE A CA  
1875 C  C   . PHE A 230 ? 0.2879 0.2897 0.1440 -0.1225 0.0769  -0.0348 231 PHE A C   
1876 O  O   . PHE A 230 ? 0.3708 0.3045 0.1625 -0.1646 0.0730  -0.0312 231 PHE A O   
1877 C  CB  . PHE A 230 ? 0.3306 0.3343 0.1282 -0.0913 0.0279  0.0158  231 PHE A CB  
1878 C  CG  . PHE A 230 ? 0.2827 0.2773 0.1242 -0.1223 0.0381  -0.0439 231 PHE A CG  
1879 C  CD1 . PHE A 230 ? 0.2706 0.3423 0.1128 -0.1303 0.0592  -0.0635 231 PHE A CD1 
1880 C  CD2 . PHE A 230 ? 0.2518 0.2850 0.1782 -0.1261 0.0550  -0.0229 231 PHE A CD2 
1881 C  CE1 . PHE A 230 ? 0.2884 0.2918 0.1354 -0.1439 0.0436  -0.0444 231 PHE A CE1 
1882 C  CE2 . PHE A 230 ? 0.2746 0.2504 0.1386 -0.1009 0.0330  -0.0375 231 PHE A CE2 
1883 C  CZ  . PHE A 230 ? 0.2284 0.2706 0.2119 -0.1240 0.0462  -0.0774 231 PHE A CZ  
1884 N  N   . ASN A 231 ? 0.3375 0.3228 0.1310 -0.1225 0.0986  -0.0450 232 ASN A N   
1885 C  CA  . ASN A 231 ? 0.2561 0.3130 0.2004 -0.0780 0.0986  -0.0013 232 ASN A CA  
1886 C  C   . ASN A 231 ? 0.2954 0.3219 0.2799 -0.0986 0.0681  0.0073  232 ASN A C   
1887 O  O   . ASN A 231 ? 0.3048 0.3048 0.1663 -0.0916 0.0683  -0.0208 232 ASN A O   
1888 C  CB  . ASN A 231 ? 0.3059 0.3434 0.1627 -0.0944 0.0639  -0.0538 232 ASN A CB  
1889 C  CG  . ASN A 231 ? 0.2768 0.4506 0.1601 -0.1534 0.0787  -0.0417 232 ASN A CG  
1890 O  OD1 . ASN A 231 ? 0.2903 0.3558 0.1929 -0.1085 0.1070  -0.0607 232 ASN A OD1 
1891 N  ND2 . ASN A 231 ? 0.4570 0.4496 0.1667 -0.1190 0.0994  -0.0594 232 ASN A ND2 
1892 N  N   . GLY A 232 ? 0.2503 0.3531 0.2449 -0.1045 0.0649  -0.0228 233 GLY A N   
1893 C  CA  . GLY A 232 ? 0.4923 0.2852 0.2457 -0.0952 0.0556  -0.0691 233 GLY A CA  
1894 C  C   . GLY A 232 ? 0.4203 0.3077 0.1551 -0.0703 0.1944  -0.0118 233 GLY A C   
1895 O  O   . GLY A 232 ? 0.4959 0.3393 0.2166 -0.0879 0.1112  0.0292  233 GLY A O   
1896 N  N   . GLU A 233 ? 0.4277 0.4481 0.2796 -0.1865 0.0794  -0.0494 234 GLU A N   
1897 C  CA  . GLU A 233 ? 0.5406 0.4811 0.3323 -0.1102 0.1322  -0.1474 234 GLU A CA  
1898 C  C   . GLU A 233 ? 0.5243 0.4870 0.4172 -0.1329 0.0838  -0.1830 234 GLU A C   
1899 O  O   . GLU A 233 ? 0.6520 0.5801 0.3171 -0.2780 0.1314  -0.0643 234 GLU A O   
1900 C  CB  . GLU A 233 ? 0.3395 0.4455 0.6946 -0.1549 0.1497  0.0611  234 GLU A CB  
1901 C  CG  . GLU A 233 ? 1.2227 0.6945 0.4008 -0.3908 -0.0133 -0.4667 234 GLU A CG  
1902 C  CD  . GLU A 233 ? 1.2227 1.1375 0.9448 -0.0006 -0.3042 -0.3828 234 GLU A CD  
1903 O  OE1 . GLU A 233 ? 0.7930 1.2112 0.4805 -0.1018 0.0159  -0.1101 234 GLU A OE1 
1904 O  OE2 . GLU A 233 ? 0.4704 0.8742 0.8165 -0.2332 0.0281  -0.1214 234 GLU A OE2 
1905 N  N   . GLY A 234 ? 0.9164 0.5428 0.1659 -0.0976 0.3604  -0.1329 235 GLY A N   
1906 C  CA  . GLY A 234 ? 0.6373 0.4488 0.4093 -0.0456 0.0332  -0.0435 235 GLY A CA  
1907 C  C   . GLY A 234 ? 0.7252 0.5827 0.4795 0.1069  0.1993  -0.0754 235 GLY A C   
1908 O  O   . GLY A 234 ? 0.5965 1.0542 0.3511 -0.0899 0.3071  -0.1303 235 GLY A O   
1909 N  N   . GLU A 235 ? 0.5906 0.5162 0.4460 -0.1869 0.2091  -0.1272 236 GLU A N   
1910 C  CA  . GLU A 235 ? 0.6707 0.3889 0.4673 -0.0622 0.1681  -0.1777 236 GLU A CA  
1911 C  C   . GLU A 235 ? 0.4830 0.3960 0.3705 0.1139  0.1641  -0.0127 236 GLU A C   
1912 O  O   . GLU A 235 ? 0.6483 0.6956 0.2384 -0.1138 0.2728  -0.0410 236 GLU A O   
1913 C  CB  . GLU A 235 ? 0.4798 0.3960 0.3674 -0.1845 0.2383  -0.0845 236 GLU A CB  
1914 C  CG  . GLU A 235 ? 0.5578 0.3943 0.5134 -0.2273 0.2523  -0.1114 236 GLU A CG  
1915 C  CD  . GLU A 235 ? 0.7368 0.6544 0.5522 -0.2525 0.3687  -0.1768 236 GLU A CD  
1916 O  OE1 . GLU A 235 ? 0.6474 0.6250 0.7072 -0.3289 0.3862  -0.0547 236 GLU A OE1 
1917 O  OE2 . GLU A 235 ? 0.8732 0.5128 1.0451 0.0892  0.2724  0.0811  236 GLU A OE2 
1918 N  N   . PRO A 236 ? 0.4792 0.4536 0.3146 -0.0320 0.1595  0.0217  237 PRO A N   
1919 C  CA  . PRO A 236 ? 0.3545 0.4126 0.3585 0.0234  0.1820  0.0184  237 PRO A CA  
1920 C  C   . PRO A 236 ? 0.3172 0.4786 0.2147 -0.0816 0.1043  -0.0986 237 PRO A C   
1921 O  O   . PRO A 236 ? 0.3919 0.4258 0.2487 -0.1298 0.1742  -0.1111 237 PRO A O   
1922 C  CB  . PRO A 236 ? 0.2918 0.4036 0.5288 -0.0027 0.2330  -0.0240 237 PRO A CB  
1923 C  CG  . PRO A 236 ? 0.2410 0.4615 0.5184 0.0020  0.1517  0.0694  237 PRO A CG  
1924 C  CD  . PRO A 236 ? 0.4431 0.3163 0.4759 0.0035  0.2258  -0.0666 237 PRO A CD  
1925 N  N   . GLU A 237 ? 0.4184 0.4364 0.2291 -0.1506 0.0954  -0.0576 238 GLU A N   
1926 C  CA  . GLU A 237 ? 0.4383 0.3954 0.1746 -0.1640 0.1285  -0.0228 238 GLU A CA  
1927 C  C   . GLU A 237 ? 0.2026 0.3480 0.1764 -0.0164 0.0796  -0.0684 238 GLU A C   
1928 O  O   . GLU A 237 ? 0.2861 0.4014 0.2035 -0.0055 0.0472  -0.0934 238 GLU A O   
1929 C  CB  . GLU A 237 ? 0.5611 0.3762 0.1950 -0.0644 -0.0987 0.0107  238 GLU A CB  
1930 C  CG  . GLU A 237 ? 0.5802 0.3203 0.4028 -0.1925 0.0339  -0.0067 238 GLU A CG  
1931 C  CD  . GLU A 237 ? 0.4812 0.6596 0.4588 -0.0372 0.0294  -0.2149 238 GLU A CD  
1932 O  OE1 . GLU A 237 ? 0.6766 0.5199 0.4773 0.0240  -0.1225 -0.1667 238 GLU A OE1 
1933 O  OE2 . GLU A 237 ? 0.5164 0.3713 0.3498 -0.0925 0.1391  -0.1204 238 GLU A OE2 
1934 N  N   . GLU A 238 ? 0.2935 0.3441 0.1498 -0.1023 0.1205  -0.0860 239 GLU A N   
1935 C  CA  . GLU A 238 ? 0.2148 0.4122 0.1744 -0.1376 0.0828  -0.0436 239 GLU A CA  
1936 C  C   . GLU A 238 ? 0.2013 0.3010 0.1825 -0.0872 0.0408  -0.0849 239 GLU A C   
1937 O  O   . GLU A 238 ? 0.2387 0.2929 0.1985 -0.0670 0.0638  -0.0197 239 GLU A O   
1938 C  CB  . GLU A 238 ? 0.1541 0.4438 0.3892 -0.1289 0.0240  -0.0669 239 GLU A CB  
1939 C  CG  . GLU A 238 ? 0.1835 0.5362 0.3123 -0.0533 0.0305  -0.0838 239 GLU A CG  
1940 C  CD  . GLU A 238 ? 0.4300 0.5291 0.3379 -0.2550 0.0039  -0.0305 239 GLU A CD  
1941 O  OE1 . GLU A 238 ? 0.4208 0.5938 0.3459 -0.0406 0.0122  -0.0119 239 GLU A OE1 
1942 O  OE2 . GLU A 238 ? 0.4488 0.5542 0.3009 -0.2141 0.0741  -0.0012 239 GLU A OE2 
1943 N  N   . LEU A 239 ? 0.1900 0.2715 0.1443 -0.0356 0.0496  -0.0282 240 LEU A N   
1944 C  CA  . LEU A 239 ? 0.1800 0.2381 0.1706 0.0037  0.0516  -0.0500 240 LEU A CA  
1945 C  C   . LEU A 239 ? 0.1615 0.2381 0.1345 -0.0171 0.0469  -0.0149 240 LEU A C   
1946 O  O   . LEU A 239 ? 0.1807 0.2778 0.1533 -0.0179 0.0588  0.0089  240 LEU A O   
1947 C  CB  . LEU A 239 ? 0.1651 0.2384 0.2620 0.0134  0.0294  -0.0587 240 LEU A CB  
1948 C  CG  . LEU A 239 ? 0.1358 0.2934 0.2387 -0.0004 0.0379  -0.0573 240 LEU A CG  
1949 C  CD1 . LEU A 239 ? 0.1681 0.2491 0.4862 0.0116  0.0010  -0.0343 240 LEU A CD1 
1950 C  CD2 . LEU A 239 ? 0.3054 0.2716 0.2509 0.0704  -0.0285 -0.0939 240 LEU A CD2 
1951 N  N   . MET A 240 ? 0.1852 0.2237 0.1175 -0.0032 0.0784  -0.0115 241 MET A N   
1952 C  CA  . MET A 240 ? 0.2288 0.2359 0.1075 -0.0234 0.0972  -0.0109 241 MET A CA  
1953 C  C   . MET A 240 ? 0.1587 0.1896 0.1292 -0.0157 0.0630  -0.0145 241 MET A C   
1954 O  O   . MET A 240 ? 0.1713 0.2197 0.1092 0.0078  0.0334  -0.0245 241 MET A O   
1955 C  CB  . MET A 240 ? 0.2420 0.2336 0.1511 0.0061  0.0996  -0.0266 241 MET A CB  
1956 C  CG  . MET A 240 ? 0.2640 0.1562 0.1609 -0.0569 0.0899  -0.0188 241 MET A CG  
1957 S  SD  . MET A 240 ? 0.2896 0.2088 0.1683 -0.0435 0.0803  -0.0053 241 MET A SD  
1958 C  CE  . MET A 240 ? 0.3147 0.2275 0.1426 -0.0613 0.0915  0.0035  241 MET A CE  
1959 N  N   . VAL A 241 ? 0.1970 0.1767 0.0979 -0.0193 0.0318  -0.0132 242 VAL A N   
1960 C  CA  . VAL A 241 ? 0.1825 0.1659 0.1049 -0.0107 0.0414  -0.0102 242 VAL A CA  
1961 C  C   . VAL A 241 ? 0.1428 0.1633 0.1261 -0.0190 0.0414  -0.0113 242 VAL A C   
1962 O  O   . VAL A 241 ? 0.1426 0.1898 0.1435 -0.0315 0.0451  -0.0340 242 VAL A O   
1963 C  CB  . VAL A 241 ? 0.1440 0.1749 0.1489 -0.0303 0.0501  -0.0231 242 VAL A CB  
1964 C  CG1 . VAL A 241 ? 0.1927 0.2057 0.1791 -0.0226 0.0107  -0.0506 242 VAL A CG1 
1965 C  CG2 . VAL A 241 ? 0.1735 0.1674 0.1841 -0.0042 0.0719  -0.0214 242 VAL A CG2 
1966 N  N   . ASP A 242 ? 0.1613 0.1430 0.0977 0.0078  0.0434  -0.0128 243 ASP A N   
1967 C  CA  . ASP A 242 ? 0.1527 0.1785 0.1098 0.0121  0.0553  -0.0267 243 ASP A CA  
1968 C  C   . ASP A 242 ? 0.1279 0.1784 0.1132 -0.0071 0.0340  -0.0279 243 ASP A C   
1969 O  O   . ASP A 242 ? 0.1195 0.1841 0.1602 -0.0074 0.0189  -0.0152 243 ASP A O   
1970 C  CB  . ASP A 242 ? 0.1336 0.1740 0.1509 -0.0031 0.0302  -0.0271 243 ASP A CB  
1971 C  CG  . ASP A 242 ? 0.1372 0.1638 0.1433 -0.0060 0.0484  -0.0334 243 ASP A CG  
1972 O  OD1 . ASP A 242 ? 0.1361 0.1505 0.1602 0.0033  0.0438  -0.0220 243 ASP A OD1 
1973 O  OD2 . ASP A 242 ? 0.1832 0.1756 0.2090 0.0129  0.0579  -0.0477 243 ASP A OD2 
1974 N  N   . ASN A 243 ? 0.1112 0.1393 0.1300 -0.0151 0.0561  -0.0250 244 ASN A N   
1975 C  CA  . ASN A 243 ? 0.1224 0.1518 0.1055 -0.0270 0.0442  -0.0122 244 ASN A CA  
1976 C  C   . ASN A 243 ? 0.1057 0.1458 0.1245 -0.0144 0.0454  -0.0240 244 ASN A C   
1977 O  O   . ASN A 243 ? 0.1623 0.1421 0.1328 0.0050  0.0374  0.0044  244 ASN A O   
1978 C  CB  . ASN A 243 ? 0.1082 0.1964 0.1455 -0.0186 0.0442  0.0093  244 ASN A CB  
1979 C  CG  . ASN A 243 ? 0.1178 0.1791 0.1342 -0.0309 0.0411  0.0065  244 ASN A CG  
1980 O  OD1 . ASN A 243 ? 0.1297 0.1694 0.1605 -0.0234 0.0275  0.0222  244 ASN A OD1 
1981 N  ND2 . ASN A 243 ? 0.1730 0.1830 0.1857 -0.0230 -0.0006 0.0340  244 ASN A ND2 
1982 N  N   . TRP A 244 ? 0.1225 0.1494 0.1159 -0.0205 0.0528  -0.0095 245 TRP A N   
1983 C  CA  . TRP A 244 ? 0.1006 0.1464 0.1048 -0.0118 0.0359  -0.0081 245 TRP A CA  
1984 C  C   . TRP A 244 ? 0.1083 0.1329 0.1412 -0.0015 0.0311  -0.0040 245 TRP A C   
1985 O  O   . TRP A 244 ? 0.1014 0.1636 0.1504 0.0187  0.0179  -0.0227 245 TRP A O   
1986 C  CB  . TRP A 244 ? 0.1231 0.1212 0.0934 -0.0078 0.0337  0.0077  245 TRP A CB  
1987 C  CG  . TRP A 244 ? 0.0947 0.1444 0.1264 0.0055  0.0140  -0.0058 245 TRP A CG  
1988 C  CD1 . TRP A 244 ? 0.1194 0.1238 0.1281 -0.0099 0.0219  -0.0119 245 TRP A CD1 
1989 C  CD2 . TRP A 244 ? 0.1029 0.1297 0.1317 -0.0114 0.0125  -0.0030 245 TRP A CD2 
1990 N  NE1 . TRP A 244 ? 0.1229 0.1455 0.1303 0.0078  0.0241  -0.0182 245 TRP A NE1 
1991 C  CE2 . TRP A 244 ? 0.1062 0.1393 0.1372 0.0100  0.0220  -0.0100 245 TRP A CE2 
1992 C  CE3 . TRP A 244 ? 0.1130 0.1782 0.1260 0.0011  0.0337  0.0046  245 TRP A CE3 
1993 C  CZ2 . TRP A 244 ? 0.1274 0.1367 0.1606 0.0111  0.0019  -0.0089 245 TRP A CZ2 
1994 C  CZ3 . TRP A 244 ? 0.1342 0.1633 0.1512 0.0206  0.0383  0.0073  245 TRP A CZ3 
1995 C  CH2 . TRP A 244 ? 0.1350 0.1634 0.1733 0.0376  0.0067  -0.0025 245 TRP A CH2 
1996 N  N   . ARG A 245 ? 0.0923 0.1447 0.1364 -0.0146 0.0200  -0.0207 246 ARG A N   
1997 C  CA  . ARG A 245 ? 0.0893 0.1426 0.1400 -0.0222 0.0115  -0.0196 246 ARG A CA  
1998 C  C   . ARG A 245 ? 0.0914 0.1580 0.1112 0.0118  0.0099  -0.0237 246 ARG A C   
1999 O  O   . ARG A 245 ? 0.1053 0.1728 0.1469 -0.0124 0.0342  -0.0196 246 ARG A O   
2000 C  CB  . ARG A 245 ? 0.0967 0.1584 0.0978 0.0002  0.0247  -0.0351 246 ARG A CB  
2001 C  CG  . ARG A 245 ? 0.0856 0.1457 0.1507 -0.0193 0.0036  -0.0309 246 ARG A CG  
2002 C  CD  . ARG A 245 ? 0.0778 0.1737 0.1439 -0.0185 0.0179  -0.0422 246 ARG A CD  
2003 N  NE  . ARG A 245 ? 0.0749 0.1694 0.1562 -0.0222 0.0141  -0.0416 246 ARG A NE  
2004 C  CZ  . ARG A 245 ? 0.0927 0.1426 0.1590 -0.0042 0.0051  -0.0319 246 ARG A CZ  
2005 N  NH1 . ARG A 245 ? 0.0924 0.1601 0.1842 -0.0003 0.0431  -0.0130 246 ARG A NH1 
2006 N  NH2 . ARG A 245 ? 0.0932 0.2286 0.1800 -0.0363 0.0005  -0.0110 246 ARG A NH2 
2007 N  N   . PRO A 246 ? 0.1093 0.1713 0.1166 0.0133  0.0167  -0.0080 247 PRO A N   
2008 C  CA  . PRO A 246 ? 0.1394 0.1566 0.1209 0.0208  0.0208  -0.0017 247 PRO A CA  
2009 C  C   . PRO A 246 ? 0.1067 0.1469 0.1345 0.0115  0.0326  -0.0030 247 PRO A C   
2010 O  O   . PRO A 246 ? 0.1137 0.1504 0.1460 0.0029  0.0038  -0.0152 247 PRO A O   
2011 C  CB  . PRO A 246 ? 0.1868 0.1974 0.1932 0.0813  0.0239  0.0244  247 PRO A CB  
2012 C  CG  . PRO A 246 ? 0.1866 0.2714 0.2526 0.0622  0.0383  0.0894  247 PRO A CG  
2013 C  CD  . PRO A 246 ? 0.1106 0.1960 0.1785 0.0491  0.0228  0.0184  247 PRO A CD  
2014 N  N   . ALA A 247 ? 0.1241 0.1512 0.1300 0.0066  0.0274  0.0057  248 ALA A N   
2015 C  CA  . ALA A 247 ? 0.1428 0.1485 0.1315 0.0062  0.0137  -0.0126 248 ALA A CA  
2016 C  C   . ALA A 247 ? 0.1410 0.1634 0.1533 0.0331  -0.0110 0.0194  248 ALA A C   
2017 O  O   . ALA A 247 ? 0.1640 0.1867 0.1637 0.0596  -0.0133 0.0083  248 ALA A O   
2018 C  CB  . ALA A 247 ? 0.2107 0.1728 0.1544 0.0069  0.0527  0.0149  248 ALA A CB  
2019 N  N   . GLN A 248 ? 0.0838 0.1742 0.1525 0.0000  -0.0017 0.0005  249 GLN A N   
2020 C  CA  . GLN A 248 ? 0.0877 0.1893 0.1371 0.0150  -0.0088 0.0051  249 GLN A CA  
2021 C  C   . GLN A 248 ? 0.1329 0.1544 0.1329 0.0331  -0.0040 -0.0163 249 GLN A C   
2022 O  O   . GLN A 248 ? 0.1483 0.2010 0.1483 0.0401  0.0060  0.0076  249 GLN A O   
2023 C  CB  . GLN A 248 ? 0.1257 0.1710 0.1841 0.0026  0.0068  0.0069  249 GLN A CB  
2024 C  CG  . GLN A 248 ? 0.1234 0.1769 0.1638 0.0062  0.0006  0.0126  249 GLN A CG  
2025 C  CD  . GLN A 248 ? 0.1112 0.2054 0.1730 -0.0034 -0.0204 0.0017  249 GLN A CD  
2026 O  OE1 . GLN A 248 ? 0.1382 0.2746 0.2239 -0.0339 -0.0200 -0.0432 249 GLN A OE1 
2027 N  NE2 . GLN A 248 ? 0.1394 0.2327 0.1758 0.0086  -0.0006 -0.0240 249 GLN A NE2 
2028 N  N   . PRO A 249 ? 0.1347 0.2552 0.1462 0.0544  -0.0240 -0.0277 250 PRO A N   
2029 C  CA  . PRO A 249 ? 0.1896 0.2622 0.1340 0.0954  -0.0499 -0.0328 250 PRO A CA  
2030 C  C   . PRO A 249 ? 0.1866 0.1979 0.1873 0.0687  -0.0412 -0.0221 250 PRO A C   
2031 O  O   . PRO A 249 ? 0.1476 0.2275 0.1809 0.0375  -0.0122 -0.0027 250 PRO A O   
2032 C  CB  . PRO A 249 ? 0.2056 0.3608 0.1802 0.0921  -0.0890 -0.0379 250 PRO A CB  
2033 C  CG  . PRO A 249 ? 0.2606 0.4441 0.1526 0.0198  -0.0516 -0.0560 250 PRO A CG  
2034 C  CD  . PRO A 249 ? 0.1055 0.2837 0.2485 0.0516  -0.0447 -0.0218 250 PRO A CD  
2035 N  N   . LEU A 250 ? 0.2083 0.2193 0.1490 0.0489  -0.0297 -0.0279 251 LEU A N   
2036 C  CA  . LEU A 250 ? 0.1946 0.2282 0.1078 0.0309  -0.0107 -0.0212 251 LEU A CA  
2037 C  C   . LEU A 250 ? 0.2597 0.2021 0.1103 0.0669  -0.0406 -0.0192 251 LEU A C   
2038 O  O   . LEU A 250 ? 0.1857 0.1983 0.1712 0.0571  -0.0438 -0.0171 251 LEU A O   
2039 C  CB  . LEU A 250 ? 0.2842 0.2305 0.1828 0.0386  0.0479  0.0290  251 LEU A CB  
2040 C  CG  . LEU A 250 ? 0.2416 0.2661 0.1363 0.0054  0.0179  -0.0081 251 LEU A CG  
2041 C  CD1 . LEU A 250 ? 0.1832 0.2975 0.1674 -0.0027 -0.0095 -0.0039 251 LEU A CD1 
2042 C  CD2 . LEU A 250 ? 0.3686 0.2453 0.2337 -0.0614 0.0296  0.0099  251 LEU A CD2 
2043 N  N   . LYS A 251 ? 0.2166 0.2585 0.1530 0.0462  -0.0549 -0.0164 252 LYS A N   
2044 C  CA  . LYS A 251 ? 0.2882 0.3057 0.1168 0.0572  -0.0533 -0.0312 252 LYS A CA  
2045 C  C   . LYS A 251 ? 0.2778 0.2832 0.1850 0.0627  -0.0308 -0.0454 252 LYS A C   
2046 O  O   . LYS A 251 ? 0.2997 0.4111 0.1925 0.0217  0.0199  -0.0013 252 LYS A O   
2047 C  CB  . LYS A 251 ? 0.2108 0.2954 0.2522 0.0412  -0.0428 -0.0358 252 LYS A CB  
2048 C  CG  . LYS A 251 ? 0.2848 0.2763 0.2845 0.0247  0.0006  -0.0738 252 LYS A CG  
2049 C  CD  . LYS A 251 ? 0.2349 0.4249 0.3230 -0.0147 0.0134  -0.1059 252 LYS A CD  
2050 C  CE  . LYS A 251 ? 0.2840 0.4257 0.4054 0.0729  -0.0734 -0.1550 252 LYS A CE  
2051 N  NZ  . LYS A 251 ? 0.3640 0.5181 0.5253 0.0961  -0.1108 0.0209  252 LYS A NZ  
2052 N  N   . ASN A 252 ? 0.2111 0.3120 0.2001 0.0594  -0.0684 -0.0600 253 ASN A N   
2053 C  CA  . ASN A 252 ? 0.2507 0.5867 0.2754 0.0886  -0.0465 -0.1274 253 ASN A CA  
2054 C  C   . ASN A 252 ? 0.2861 0.5690 0.2907 0.1659  -0.1109 -0.2145 253 ASN A C   
2055 O  O   . ASN A 252 ? 0.4870 0.6530 0.6084 0.2424  -0.2522 -0.3677 253 ASN A O   
2056 C  CB  . ASN A 252 ? 0.4890 0.5598 0.2875 0.1138  -0.1468 -0.1772 253 ASN A CB  
2057 C  CG  . ASN A 252 ? 0.7494 0.5790 0.1920 0.1694  -0.0391 -0.0245 253 ASN A CG  
2058 O  OD1 . ASN A 252 ? 1.0591 0.8898 0.4307 0.0803  0.0185  0.2026  253 ASN A OD1 
2059 N  ND2 . ASN A 252 ? 0.6438 0.5478 0.6066 -0.1439 0.1358  0.0433  253 ASN A ND2 
2060 N  N   . ARG A 253 ? 0.1961 0.3565 0.1027 0.0584  -0.0078 -0.0092 254 ARG A N   
2061 C  CA  . ARG A 253 ? 0.1925 0.2423 0.1069 0.0526  0.0065  -0.0353 254 ARG A CA  
2062 C  C   . ARG A 253 ? 0.2481 0.2281 0.1256 0.0316  0.0233  -0.0538 254 ARG A C   
2063 O  O   . ARG A 253 ? 0.3504 0.2398 0.2960 0.0475  0.0937  0.0318  254 ARG A O   
2064 C  CB  . ARG A 253 ? 0.1985 0.2180 0.1066 0.0252  -0.0021 -0.0041 254 ARG A CB  
2065 C  CG  . ARG A 253 ? 0.2193 0.2063 0.1075 0.0037  -0.0024 -0.0132 254 ARG A CG  
2066 C  CD  . ARG A 253 ? 0.2007 0.2015 0.1100 0.0666  -0.0016 -0.0160 254 ARG A CD  
2067 N  NE  . ARG A 253 ? 0.1390 0.1785 0.1485 0.0332  -0.0031 -0.0314 254 ARG A NE  
2068 C  CZ  . ARG A 253 ? 0.1328 0.1365 0.1347 0.0179  -0.0232 -0.0148 254 ARG A CZ  
2069 N  NH1 . ARG A 253 ? 0.1238 0.1537 0.1199 0.0144  -0.0205 -0.0013 254 ARG A NH1 
2070 N  NH2 . ARG A 253 ? 0.1227 0.1539 0.1209 0.0253  0.0020  -0.0088 254 ARG A NH2 
2071 N  N   . GLN A 254 ? 0.2222 0.2485 0.1832 0.0354  0.0029  -0.0734 255 GLN A N   
2072 C  CA  . GLN A 254 ? 0.2706 0.2967 0.1426 -0.0129 -0.0048 -0.0501 255 GLN A CA  
2073 C  C   . GLN A 254 ? 0.2397 0.2524 0.1544 -0.0206 0.0002  0.0027  255 GLN A C   
2074 O  O   . GLN A 254 ? 0.3820 0.2351 0.2413 -0.0060 -0.0974 -0.0111 255 GLN A O   
2075 C  CB  . GLN A 254 ? 0.3735 0.4072 0.1645 -0.0458 0.0298  -0.1152 255 GLN A CB  
2076 C  CG  . GLN A 254 ? 0.3951 0.5163 0.2295 -0.0024 0.0074  -0.0788 255 GLN A CG  
2077 N  N   . ILE A 255 ? 0.2125 0.2204 0.1230 0.0044  0.0130  0.0038  256 ILE A N   
2078 C  CA  . ILE A 255 ? 0.1561 0.2100 0.1207 0.0454  0.0276  -0.0203 256 ILE A CA  
2079 C  C   . ILE A 255 ? 0.1648 0.2194 0.1286 0.0314  0.0469  0.0277  256 ILE A C   
2080 O  O   . ILE A 255 ? 0.1806 0.2277 0.1394 0.0502  0.0409  0.0337  256 ILE A O   
2081 C  CB  . ILE A 255 ? 0.1444 0.1861 0.1602 0.0261  0.0157  -0.0151 256 ILE A CB  
2082 C  CG1 . ILE A 255 ? 0.1583 0.2245 0.1656 0.0782  0.0412  -0.0270 256 ILE A CG1 
2083 C  CG2 . ILE A 255 ? 0.1903 0.2277 0.1393 0.0326  0.0168  -0.0225 256 ILE A CG2 
2084 C  CD1 . ILE A 255 ? 0.2310 0.2560 0.1889 0.0118  0.0464  -0.0666 256 ILE A CD1 
2085 N  N   . LYS A 256 ? 0.1472 0.2068 0.1555 0.0214  0.0313  0.0251  257 LYS A N   
2086 C  CA  . LYS A 256 ? 0.1641 0.2195 0.1471 0.0384  0.0558  0.0288  257 LYS A CA  
2087 C  C   . LYS A 256 ? 0.1866 0.2413 0.1329 0.0290  0.0389  0.0214  257 LYS A C   
2088 O  O   . LYS A 256 ? 0.2144 0.2595 0.1304 -0.0186 0.0582  0.0266  257 LYS A O   
2089 C  CB  . LYS A 256 ? 0.2155 0.2256 0.1846 0.0334  0.0317  0.0050  257 LYS A CB  
2090 C  CG  . LYS A 256 ? 0.3270 0.3511 0.2119 -0.0036 0.0243  -0.0512 257 LYS A CG  
2091 N  N   . ALA A 257 ? 0.1940 0.2226 0.1602 0.0330  0.0612  0.0306  258 ALA A N   
2092 C  CA  . ALA A 257 ? 0.1806 0.2426 0.1634 0.0435  0.0544  0.0284  258 ALA A CA  
2093 C  C   . ALA A 257 ? 0.1670 0.2604 0.1630 0.0295  0.0784  0.0044  258 ALA A C   
2094 O  O   . ALA A 257 ? 0.2130 0.2938 0.1419 0.0688  0.0850  0.0179  258 ALA A O   
2095 C  CB  . ALA A 257 ? 0.1864 0.2414 0.2100 0.0354  0.1082  0.0490  258 ALA A CB  
2096 N  N   . SER A 258 ? 0.1791 0.2230 0.1713 0.0469  0.0619  0.0134  259 SER A N   
2097 C  CA  . SER A 258 ? 0.1835 0.2234 0.2004 0.0555  0.0901  0.0330  259 SER A CA  
2098 C  C   . SER A 258 ? 0.1491 0.2735 0.2514 0.0504  0.1011  0.0283  259 SER A C   
2099 O  O   . SER A 258 ? 0.1649 0.3784 0.2929 0.0876  0.1097  0.0372  259 SER A O   
2100 C  CB  . SER A 258 ? 0.2288 0.2221 0.2080 0.0504  0.0366  0.0135  259 SER A CB  
2101 O  OG  . SER A 258 ? 0.1649 0.2441 0.2064 0.0220  0.0961  0.0142  259 SER A OG  
2102 N  N   . PHE A 259 ? 0.1207 0.2971 0.2578 0.0102  0.1064  0.0434  260 PHE A N   
2103 C  CA  . PHE A 259 ? 0.1497 0.3357 0.2592 -0.0249 0.0807  0.0509  260 PHE A CA  
2104 C  C   . PHE A 259 ? 0.2722 0.3871 0.2821 -0.0143 0.0947  0.0545  260 PHE A C   
2105 O  O   . PHE A 259 ? 0.3111 0.3028 0.2515 -0.0395 0.0773  0.0868  260 PHE A O   
2106 C  CB  . PHE A 259 ? 0.1720 0.3055 0.3319 0.0047  0.1032  -0.0494 260 PHE A CB  
2107 C  CG  . PHE A 259 ? 0.1602 0.2671 0.2945 0.0125  0.0719  0.0266  260 PHE A CG  
2108 C  CD1 . PHE A 259 ? 0.1609 0.3031 0.2356 0.0106  0.0721  0.0283  260 PHE A CD1 
2109 C  CD2 . PHE A 259 ? 0.2270 0.2703 0.4456 0.0211  0.0410  0.0270  260 PHE A CD2 
2110 C  CE1 . PHE A 259 ? 0.2144 0.2610 0.3511 0.0391  0.0818  0.0294  260 PHE A CE1 
2111 C  CE2 . PHE A 259 ? 0.1863 0.3143 0.3849 -0.0043 0.0425  0.0465  260 PHE A CE2 
2112 C  CZ  . PHE A 259 ? 0.1810 0.2464 0.3970 0.0330  0.0738  0.0102  260 PHE A CZ  
2113 N  N   . LYS A 260 ? 0.3605 0.5203 0.5174 -0.1746 0.1921  -0.0976 261 LYS A N   
2114 C  CA  . LYS A 260 ? 0.8258 0.5350 0.7012 0.0473  0.1357  -0.1460 261 LYS A CA  
2115 C  C   . LYS A 260 ? 0.9504 0.7878 0.8725 0.0449  -0.1483 -0.3423 261 LYS A C   
2116 O  O   . LYS A 260 ? 0.9750 0.4890 1.1339 0.1868  -0.0025 0.1454  261 LYS A O   
2117 C  CB  . LYS A 260 ? 0.8702 1.0203 0.8051 -0.0071 0.1998  0.4370  261 LYS A CB  
2118 O  OXT . LYS A 260 ? 1.1601 0.7228 1.4656 0.0175  -0.0554 0.1972  261 LYS A OXT 
2119 ZN ZN  . ZN  B .   ? 0.1006 0.1347 0.1080 -0.0054 0.0051  -0.0031 301 ZN  A ZN  
2120 O  O20 A V13 C .   ? 0.2428 0.3461 0.2798 -0.0532 0.0728  0.1497  302 V13 A O20 
2121 O  O20 B V13 C .   ? 1.2992 1.1769 0.4584 -0.1043 0.1307  0.0281  302 V13 A O20 
2122 S  S15 A V13 C .   ? 0.2740 0.2551 0.3366 -0.0754 0.0000  0.0987  302 V13 A S15 
2123 S  S15 B V13 C .   ? 0.5651 0.6521 0.3768 -0.1265 -0.0261 0.1368  302 V13 A S15 
2124 O  O19 A V13 C .   ? 0.3245 0.2324 0.4318 -0.1141 -0.0761 0.0490  302 V13 A O19 
2125 O  O19 B V13 C .   ? 0.6595 0.8375 0.4719 -0.2256 -0.0309 0.0289  302 V13 A O19 
2126 C  C16 A V13 C .   ? 0.3439 0.3136 0.3991 0.0116  -0.1209 0.1622  302 V13 A C16 
2127 C  C16 B V13 C .   ? 0.6057 0.6330 0.2854 -0.1109 -0.0526 0.0857  302 V13 A C16 
2128 C  C17 A V13 C .   ? 0.4247 0.4574 0.5650 -0.2471 0.0574  0.1641  302 V13 A C17 
2129 C  C17 B V13 C .   ? 0.5970 0.5304 0.2054 -0.0854 -0.1078 0.1439  302 V13 A C17 
2130 O  O18 A V13 C .   ? 0.5416 0.3145 0.6919 -0.1577 -0.0576 0.1320  302 V13 A O18 
2131 O  O18 B V13 C .   ? 0.5991 0.5138 0.0276 -0.1247 -0.1115 0.0350  302 V13 A O18 
2132 C  C1  A V13 C .   ? 0.1868 0.1861 0.2103 -0.0205 -0.0054 0.0572  302 V13 A C1  
2133 C  C1  B V13 C .   ? 0.5033 0.3903 0.3050 -0.0263 -0.0313 0.0161  302 V13 A C1  
2134 C  C6  A V13 C .   ? 0.1637 0.1720 0.2784 -0.0032 -0.0700 0.0760  302 V13 A C6  
2135 C  C6  B V13 C .   ? 0.3899 0.3657 0.3203 0.0144  -0.0767 0.0839  302 V13 A C6  
2136 F  F11 A V13 C .   ? 0.1698 0.1536 0.3847 -0.0203 -0.0804 0.0944  302 V13 A F11 
2137 F  F11 B V13 C .   ? 0.5042 0.3933 0.5065 -0.0081 -0.0212 0.0082  302 V13 A F11 
2138 C  C5  A V13 C .   ? 0.1109 0.1379 0.1982 0.0175  -0.0377 0.0298  302 V13 A C5  
2139 C  C5  B V13 C .   ? 0.1803 0.2372 0.2909 -0.0347 -0.0150 -0.0414 302 V13 A C5  
2140 F  F12 A V13 C .   ? 0.1141 0.1367 0.3724 0.0057  -0.0611 0.0591  302 V13 A F12 
2141 F  F12 B V13 C .   ? 0.2718 0.2254 0.3419 -0.0436 0.0485  -0.0544 302 V13 A F12 
2142 C  C4  A V13 C .   ? 0.0726 0.1072 0.1272 0.0098  -0.0009 -0.0042 302 V13 A C4  
2143 C  C4  B V13 C .   ? 0.2106 0.2389 0.2492 0.0089  0.0040  0.0217  302 V13 A C4  
2144 S  S7  A V13 C .   ? 0.0577 0.1029 0.1074 0.0128  0.0034  -0.0061 302 V13 A S7  
2145 S  S7  B V13 C .   ? 0.1734 0.2065 0.2000 -0.0193 -0.0089 -0.0232 302 V13 A S7  
2146 O  O9  A V13 C .   ? 0.0583 0.0987 0.0832 0.0060  0.0011  -0.0145 302 V13 A O9  
2147 O  O9  B V13 C .   ? 0.1892 0.2408 0.2236 0.0118  -0.0245 -0.0296 302 V13 A O9  
2148 N  N10 A V13 C .   ? 0.0308 0.0839 0.1202 -0.0221 -0.0041 -0.0168 302 V13 A N10 
2149 N  N10 B V13 C .   ? 0.2782 0.2086 0.2072 -0.0294 0.0402  -0.1157 302 V13 A N10 
2150 O  O8  A V13 C .   ? 0.0560 0.1195 0.1239 0.0137  -0.0058 -0.0286 302 V13 A O8  
2151 O  O8  B V13 C .   ? 0.1731 0.1996 0.1730 0.0405  -0.0193 -0.0086 302 V13 A O8  
2152 C  C3  A V13 C .   ? 0.0794 0.1284 0.1195 -0.0076 0.0190  -0.0132 302 V13 A C3  
2153 C  C3  B V13 C .   ? 0.2195 0.2714 0.2492 -0.0068 0.0274  0.0540  302 V13 A C3  
2154 F  F13 A V13 C .   ? 0.0435 0.1584 0.1475 0.0079  0.0392  0.0140  302 V13 A F13 
2155 F  F13 B V13 C .   ? 0.1609 0.2606 0.4695 -0.0232 0.0630  0.0568  302 V13 A F13 
2156 C  C2  A V13 C .   ? 0.1307 0.1569 0.1591 -0.0208 0.0308  0.0107  302 V13 A C2  
2157 C  C2  B V13 C .   ? 0.3227 0.3110 0.2778 -0.0836 -0.0600 0.0914  302 V13 A C2  
2158 F  F14 A V13 C .   ? 0.1451 0.1631 0.2081 0.0131  0.0494  0.0134  302 V13 A F14 
2159 F  F14 B V13 C .   ? 0.6312 0.4292 0.2628 -0.2119 0.0212  -0.0064 302 V13 A F14 
2160 S  S   . DMS D .   ? 0.2349 0.3771 0.3411 -0.0127 0.0289  -0.0519 303 DMS A S   
2161 O  O   . DMS D .   ? 0.4197 0.4860 0.3813 0.1273  0.1084  -0.1148 303 DMS A O   
2162 C  C1  . DMS D .   ? 0.2743 0.2847 0.5490 -0.0234 0.0458  0.0012  303 DMS A C1  
2163 C  C2  . DMS D .   ? 0.2508 0.3224 0.2444 0.0302  0.0822  -0.0464 303 DMS A C2  
2164 O  O   . HOH E .   ? 0.2584 0.1379 0.2116 -0.0195 -0.0623 0.0013  401 HOH A O   
2165 O  O   . HOH E .   ? 0.2999 0.3991 0.5802 0.0842  -0.0320 -0.1709 402 HOH A O   
2166 O  O   . HOH E .   ? 0.3906 0.2991 0.2980 -0.0065 -0.0013 0.0627  403 HOH A O   
2167 O  O   . HOH E .   ? 0.2094 0.3386 0.4927 0.0234  0.0138  -0.0083 404 HOH A O   
2168 O  O   . HOH E .   ? 0.3378 0.5273 0.3356 -0.1058 0.1076  -0.0195 405 HOH A O   
2169 O  O   . HOH E .   ? 0.7713 0.6496 0.5663 -0.2515 -0.2215 0.1727  406 HOH A O   
2170 O  O   . HOH E .   ? 0.3982 0.4087 0.5591 0.0270  -0.0096 0.0928  407 HOH A O   
2171 O  O   . HOH E .   ? 0.3892 0.3175 0.3856 0.0015  -0.1085 -0.0391 408 HOH A O   
2172 O  O   . HOH E .   ? 0.5743 0.3273 0.2356 -0.0886 -0.0066 -0.0757 409 HOH A O   
2173 O  O   . HOH E .   ? 0.7440 0.4258 0.7180 0.3899  -0.5061 -0.4004 410 HOH A O   
2174 O  O   . HOH E .   ? 0.1832 0.7466 0.3483 0.0842  0.0022  0.1610  411 HOH A O   
2175 O  O   . HOH E .   ? 0.4520 0.2726 0.4345 -0.0753 0.1171  -0.1354 412 HOH A O   
2176 O  O   . HOH E .   ? 0.2547 0.5523 0.4093 -0.1298 -0.0192 -0.0436 413 HOH A O   
2177 O  O   . HOH E .   ? 0.4618 0.4161 0.4200 0.0858  0.2259  -0.0198 414 HOH A O   
2178 O  O   . HOH E .   ? 0.4646 0.2498 0.6088 -0.0872 0.1685  0.0289  415 HOH A O   
2179 O  O   . HOH E .   ? 0.4711 0.4690 1.0237 0.0036  -0.1702 -0.1086 416 HOH A O   
2180 O  O   . HOH E .   ? 0.4949 0.5118 0.3111 -0.2174 0.1377  -0.1505 417 HOH A O   
2181 O  O   . HOH E .   ? 0.1310 0.1505 0.1710 -0.0071 0.0412  -0.0047 418 HOH A O   
2182 O  O   . HOH E .   ? 0.2383 0.5735 0.6585 0.0052  0.0922  -0.1430 419 HOH A O   
2183 O  O   . HOH E .   ? 0.2879 0.2693 0.4445 -0.0469 0.0143  -0.0540 420 HOH A O   
2184 O  O   . HOH E .   ? 0.2688 0.2122 0.2425 -0.0419 -0.1078 0.0359  421 HOH A O   
2185 O  O   . HOH E .   ? 0.3087 0.1846 0.2964 -0.0306 0.0139  0.0274  422 HOH A O   
2186 O  O   . HOH E .   ? 0.6558 0.5218 0.4297 0.0075  0.0912  0.0640  423 HOH A O   
2187 O  O   . HOH E .   ? 0.3495 0.4945 0.2259 -0.1261 -0.1375 0.0254  424 HOH A O   
2188 O  O   . HOH E .   ? 0.2524 0.3057 0.7962 0.0145  0.1884  0.1449  425 HOH A O   
2189 O  O   . HOH E .   ? 0.3714 0.5924 0.3297 -0.0467 -0.0365 0.0927  426 HOH A O   
2190 O  O   . HOH E .   ? 0.3400 0.5066 0.3120 -0.0113 0.0769  -0.2093 427 HOH A O   
2191 O  O   . HOH E .   ? 0.2392 0.7217 0.4776 -0.0187 0.0530  -0.1835 428 HOH A O   
2192 O  O   . HOH E .   ? 0.3696 0.5385 0.6014 0.0076  0.1300  0.2291  429 HOH A O   
2193 O  O   . HOH E .   ? 0.3899 0.6298 0.2986 0.2342  0.0318  -0.0077 430 HOH A O   
2194 O  O   . HOH E .   ? 0.8150 0.4747 0.0832 -0.0370 0.0133  0.0231  431 HOH A O   
2195 O  O   . HOH E .   ? 0.3576 0.2672 0.3441 -0.0641 -0.0791 0.0044  432 HOH A O   
2196 O  O   . HOH E .   ? 0.2080 0.1680 0.1778 -0.0107 0.0315  -0.0016 433 HOH A O   
2197 O  O   . HOH E .   ? 0.2694 0.2929 0.4122 0.0380  -0.2027 -0.0895 434 HOH A O   
2198 O  O   . HOH E .   ? 0.4500 0.4178 0.3441 -0.0132 -0.0908 0.0055  435 HOH A O   
2199 O  O   . HOH E .   ? 0.1401 0.3495 0.5009 -0.0350 -0.0264 0.0669  436 HOH A O   
2200 O  O   . HOH E .   ? 0.3401 0.3862 0.2037 0.0039  -0.0413 0.0267  437 HOH A O   
2201 O  O   . HOH E .   ? 0.5845 0.3984 0.1821 -0.2159 0.0719  0.0697  438 HOH A O   
2202 O  O   . HOH E .   ? 0.2596 0.2506 0.4314 0.0181  0.0833  -0.0465 439 HOH A O   
2203 O  O   . HOH E .   ? 0.3455 0.2911 0.3027 0.0480  -0.0469 0.0823  440 HOH A O   
2204 O  O   . HOH E .   ? 0.4879 0.2884 0.2365 -0.0419 0.0639  0.0741  441 HOH A O   
2205 O  O   . HOH E .   ? 0.5105 0.3580 0.2728 -0.0866 0.2108  -0.0785 442 HOH A O   
2206 O  O   . HOH E .   ? 0.3862 0.2882 0.5615 -0.0752 0.0768  -0.1271 443 HOH A O   
2207 O  O   . HOH E .   ? 0.3513 0.3994 0.4963 -0.0779 -0.0708 0.2035  444 HOH A O   
2208 O  O   . HOH E .   ? 0.1066 0.1634 0.1382 0.0136  0.0052  -0.0163 445 HOH A O   
2209 O  O   . HOH E .   ? 0.3725 0.2832 0.3651 -0.0842 0.0089  -0.0427 446 HOH A O   
2210 O  O   . HOH E .   ? 0.4336 0.2934 0.4428 0.0061  0.0833  0.1248  447 HOH A O   
2211 O  O   . HOH E .   ? 0.4876 0.4032 0.5759 -0.2411 -0.1068 0.1052  448 HOH A O   
2212 O  O   . HOH E .   ? 0.3614 0.2585 0.5642 0.0020  0.0282  -0.0294 449 HOH A O   
2213 O  O   . HOH E .   ? 0.1281 0.2114 0.1476 0.0478  0.0133  0.0115  450 HOH A O   
2214 O  O   . HOH E .   ? 0.2212 0.3536 0.3660 -0.0063 0.1122  -0.0263 451 HOH A O   
2215 O  O   . HOH E .   ? 0.1594 0.1625 0.1577 -0.0199 0.0291  -0.0367 452 HOH A O   
2216 O  O   . HOH E .   ? 0.4780 0.5087 0.4557 0.0627  0.1770  -0.0026 453 HOH A O   
2217 O  O   . HOH E .   ? 0.1135 0.2176 0.3341 -0.0144 0.0119  0.0306  454 HOH A O   
2218 O  O   . HOH E .   ? 0.2108 0.2026 0.5528 -0.0465 -0.1001 0.0292  455 HOH A O   
2219 O  O   . HOH E .   ? 0.6355 0.3534 0.2125 -0.0389 -0.0488 -0.0402 456 HOH A O   
2220 O  O   . HOH E .   ? 0.3059 0.2128 0.3283 -0.0205 -0.0508 0.0635  457 HOH A O   
2221 O  O   . HOH E .   ? 0.2869 0.6166 0.6565 -0.0690 0.0640  -0.2794 458 HOH A O   
2222 O  O   . HOH E .   ? 0.9069 0.7056 0.2721 -0.3385 -0.1183 -0.0076 459 HOH A O   
2223 O  O   . HOH E .   ? 0.1483 0.2262 0.1758 0.0434  -0.0239 0.0171  460 HOH A O   
2224 O  O   . HOH E .   ? 0.2318 0.2974 0.2458 0.0414  0.0768  -0.0502 461 HOH A O   
2225 O  O   . HOH E .   ? 0.3351 0.5125 0.5164 -0.3277 0.0632  -0.0154 462 HOH A O   
2226 O  O   . HOH E .   ? 0.2395 0.3943 0.5766 0.0266  0.0942  0.1785  463 HOH A O   
2227 O  O   . HOH E .   ? 0.1753 0.1879 0.2412 0.0269  0.0219  0.0186  464 HOH A O   
2228 O  O   . HOH E .   ? 0.2617 0.4101 0.4474 -0.0250 -0.0829 -0.0268 465 HOH A O   
2229 O  O   . HOH E .   ? 0.2438 0.2575 0.2392 -0.0160 -0.0973 0.0419  466 HOH A O   
2230 O  O   . HOH E .   ? 0.3495 0.1995 0.3770 0.0167  -0.1179 0.0037  467 HOH A O   
2231 O  O   . HOH E .   ? 0.2705 0.3820 0.4661 0.0642  -0.0212 -0.0251 468 HOH A O   
2232 O  O   . HOH E .   ? 0.4073 0.5595 0.2158 -0.0002 -0.1130 0.0811  469 HOH A O   
2233 O  O   . HOH E .   ? 0.2153 0.2234 0.2389 0.0194  -0.0126 0.0012  470 HOH A O   
2234 O  O   . HOH E .   ? 0.1734 0.3488 0.2082 0.0046  0.0430  -0.0004 471 HOH A O   
2235 O  O   . HOH E .   ? 0.7218 0.5362 0.6440 -0.0464 -0.1285 -0.1844 472 HOH A O   
2236 O  O   . HOH E .   ? 0.3186 0.3347 0.3680 0.0458  0.0120  -0.0464 473 HOH A O   
2237 O  O   . HOH E .   ? 0.0926 0.2022 0.3037 0.0188  0.0266  -0.0285 474 HOH A O   
2238 O  O   . HOH E .   ? 0.3203 0.2660 0.3388 0.0789  -0.0502 -0.0142 475 HOH A O   
2239 O  O   . HOH E .   ? 0.4848 0.3752 0.2635 -0.0389 -0.1606 -0.0223 476 HOH A O   
2240 O  O   . HOH E .   ? 0.3157 0.4341 0.4229 0.0893  -0.1205 -0.1962 477 HOH A O   
2241 O  O   . HOH E .   ? 0.2446 0.4521 0.2098 0.0097  0.0330  -0.0518 478 HOH A O   
2242 O  O   . HOH E .   ? 0.3885 0.6600 0.4149 0.0818  -0.1344 -0.0826 479 HOH A O   
2243 O  O   . HOH E .   ? 0.3210 0.5186 0.6664 -0.1577 -0.1418 0.0920  480 HOH A O   
2244 O  O   . HOH E .   ? 0.1282 0.2073 0.1918 0.0136  0.0067  0.0243  481 HOH A O   
2245 O  O   . HOH E .   ? 0.2879 0.1907 0.4282 -0.0017 0.1151  -0.0424 482 HOH A O   
2246 O  O   . HOH E .   ? 0.2164 0.1455 0.2241 -0.0232 -0.0186 -0.0152 483 HOH A O   
2247 O  O   . HOH E .   ? 0.0830 0.1473 0.1509 -0.0110 0.0355  0.0179  484 HOH A O   
2248 O  O   . HOH E .   ? 0.4448 0.4796 0.3852 0.0713  0.0163  0.0337  485 HOH A O   
2249 O  O   . HOH E .   ? 0.3154 0.3516 0.4697 -0.0476 0.0533  0.1750  486 HOH A O   
2250 O  O   . HOH E .   ? 0.6397 0.4841 0.2751 0.2745  -0.0574 -0.0955 487 HOH A O   
2251 O  O   . HOH E .   ? 0.4330 0.4654 0.2651 0.0229  0.1206  -0.1250 488 HOH A O   
2252 O  O   . HOH E .   ? 0.8212 0.4517 1.1428 -0.0891 0.0219  0.0434  489 HOH A O   
2253 O  O   . HOH E .   ? 0.3499 0.1795 0.2298 0.0118  -0.1192 0.0085  490 HOH A O   
2254 O  O   . HOH E .   ? 0.4676 0.2705 1.2503 0.0385  -0.0450 0.0409  491 HOH A O   
2255 O  O   . HOH E .   ? 0.3018 0.3247 0.3472 -0.0831 0.0297  -0.0995 492 HOH A O   
2256 O  O   . HOH E .   ? 0.2046 0.2986 0.2292 0.0616  -0.0024 0.0053  493 HOH A O   
2257 O  O   . HOH E .   ? 0.3237 0.2955 0.3412 -0.0524 -0.0675 0.0989  494 HOH A O   
2258 O  O   . HOH E .   ? 0.0949 0.2606 0.3131 0.0325  0.0020  -0.0308 495 HOH A O   
2259 O  O   . HOH E .   ? 0.2706 0.5111 0.3201 -0.0523 -0.0130 -0.0304 496 HOH A O   
2260 O  O   . HOH E .   ? 0.5833 0.5202 0.2731 -0.0879 0.0324  0.1124  497 HOH A O   
2261 O  O   . HOH E .   ? 0.3088 0.1947 0.3773 -0.0292 -0.0545 -0.0227 498 HOH A O   
2262 O  O   . HOH E .   ? 0.1694 0.3573 0.3632 0.0070  0.0648  -0.0119 499 HOH A O   
2263 O  O   . HOH E .   ? 0.3515 0.1841 0.2367 -0.0364 -0.1259 0.0300  500 HOH A O   
2264 O  O   . HOH E .   ? 0.1566 0.3841 0.5048 0.0002  -0.0550 0.0524  501 HOH A O   
2265 O  O   . HOH E .   ? 0.7207 0.3834 0.4948 0.0400  -0.1274 -0.0205 502 HOH A O   
2266 O  O   . HOH E .   ? 0.3903 0.7207 0.5213 0.0083  0.0403  0.1069  503 HOH A O   
2267 O  O   . HOH E .   ? 0.3321 0.2464 0.2927 0.0183  -0.0508 -0.0455 504 HOH A O   
2268 O  O   . HOH E .   ? 0.2011 0.2252 0.3433 -0.0211 0.0950  -0.0137 505 HOH A O   
2269 O  O   . HOH E .   ? 0.4295 0.3365 0.2606 -0.0475 0.0340  -0.0765 506 HOH A O   
2270 O  O   . HOH E .   ? 0.2842 0.3216 0.1967 0.0086  0.0261  -0.0027 507 HOH A O   
2271 O  O   . HOH E .   ? 0.2848 0.3641 0.6821 0.0091  -0.1143 0.1958  508 HOH A O   
2272 O  O   . HOH E .   ? 0.2971 0.2031 0.3170 0.0356  -0.1293 -0.0199 509 HOH A O   
2273 O  O   . HOH E .   ? 0.4804 0.5401 0.4816 0.2597  0.1285  0.1414  510 HOH A O   
2274 O  O   . HOH E .   ? 0.2725 0.2820 0.2576 0.0668  -0.0442 0.0150  511 HOH A O   
2275 O  O   . HOH E .   ? 0.2599 0.4039 0.2800 -0.0485 -0.0719 0.0187  512 HOH A O   
2276 O  O   . HOH E .   ? 0.2419 0.6091 0.4020 0.0346  -0.0626 -0.0771 513 HOH A O   
2277 O  O   . HOH E .   ? 0.2744 0.2463 0.2836 0.0086  0.0893  0.1082  514 HOH A O   
2278 O  O   . HOH E .   ? 0.9407 0.3553 0.2459 -0.0774 -0.0206 0.1523  515 HOH A O   
2279 O  O   . HOH E .   ? 0.5036 0.5710 0.4506 0.2275  -0.1870 -0.1657 516 HOH A O   
2280 O  O   . HOH E .   ? 0.4997 0.4512 0.3818 0.2112  -0.1160 -0.0697 517 HOH A O   
2281 O  O   . HOH E .   ? 0.4839 0.5035 0.3784 0.0062  -0.0234 -0.0284 518 HOH A O   
2282 O  O   . HOH E .   ? 0.3118 0.2821 0.3800 0.0959  -0.0233 -0.0592 519 HOH A O   
2283 O  O   . HOH E .   ? 0.4072 0.6019 0.3240 0.1128  -0.0655 0.0780  520 HOH A O   
2284 O  O   . HOH E .   ? 0.6063 0.3380 0.2353 0.0113  -0.1371 0.1360  521 HOH A O   
2285 O  O   . HOH E .   ? 0.4329 0.5557 0.3125 -0.2008 0.0942  -0.1427 522 HOH A O   
2286 O  O   . HOH E .   ? 0.2773 0.3685 0.2916 -0.0898 -0.0631 0.1086  523 HOH A O   
2287 O  O   . HOH E .   ? 0.4093 0.3213 0.8975 -0.0579 0.2517  0.0247  524 HOH A O   
2288 O  O   . HOH E .   ? 0.6237 0.3255 0.6937 0.0171  0.3486  0.0372  525 HOH A O   
2289 O  O   . HOH E .   ? 0.6124 0.9681 0.4810 0.0240  0.0268  0.1876  526 HOH A O   
2290 O  O   . HOH E .   ? 0.4328 0.6279 0.4936 0.1638  0.2013  -0.0133 527 HOH A O   
2291 O  O   . HOH E .   ? 0.6369 0.2988 0.3986 0.0365  0.0802  -0.0034 528 HOH A O   
2292 O  O   . HOH E .   ? 0.5003 0.3457 0.2449 0.0571  -0.0280 0.0315  529 HOH A O   
2293 O  O   . HOH E .   ? 0.3096 0.3291 0.5639 0.0026  0.0098  -0.1507 530 HOH A O   
2294 O  O   . HOH E .   ? 0.4061 0.5014 0.2778 0.0069  0.0575  -0.0948 531 HOH A O   
2295 O  O   . HOH E .   ? 0.1559 0.2676 0.2144 0.0151  -0.0465 0.0263  532 HOH A O   
2296 O  O   . HOH E .   ? 0.1861 0.5139 0.3943 0.0086  0.0515  -0.0252 533 HOH A O   
2297 O  O   . HOH E .   ? 0.4654 0.2879 0.3253 0.0774  -0.0483 0.0496  534 HOH A O   
2298 O  O   . HOH E .   ? 0.4841 0.2530 0.3323 -0.0592 -0.1902 -0.0115 535 HOH A O   
2299 O  O   . HOH E .   ? 0.1681 0.3734 0.4203 0.0842  0.1042  0.0253  536 HOH A O   
2300 O  O   . HOH E .   ? 0.2108 0.3263 0.3762 0.0196  -0.0299 0.1289  537 HOH A O   
2301 O  O   . HOH E .   ? 0.2742 0.3203 0.5305 -0.1315 0.1082  -0.1946 538 HOH A O   
2302 O  O   . HOH E .   ? 0.3756 0.4560 0.4711 0.0465  0.0735  0.2052  539 HOH A O   
2303 O  O   . HOH E .   ? 0.5404 0.4236 0.2866 -0.0844 0.0147  0.1069  540 HOH A O   
2304 O  O   . HOH E .   ? 0.1252 0.1593 0.1706 0.0002  -0.0024 -0.0038 541 HOH A O   
2305 O  O   . HOH E .   ? 0.3091 0.7672 0.3920 -0.1176 -0.0835 0.1162  542 HOH A O   
2306 O  O   . HOH E .   ? 0.3576 0.9804 0.4876 0.0729  0.0315  -0.3410 543 HOH A O   
2307 O  O   . HOH E .   ? 0.5351 0.8245 0.3398 -0.0027 0.1883  -0.3337 544 HOH A O   
2308 O  O   . HOH E .   ? 0.1746 0.4099 0.3361 0.0897  -0.0785 -0.0212 545 HOH A O   
2309 O  O   . HOH E .   ? 0.4884 0.3061 0.4071 0.0525  -0.0539 -0.0440 546 HOH A O   
2310 O  O   . HOH E .   ? 0.6941 0.3703 0.4665 0.1452  0.0889  0.1122  547 HOH A O   
2311 O  O   . HOH E .   ? 0.4230 0.3277 1.0341 -0.0345 0.0592  -0.1211 548 HOH A O   
2312 O  O   . HOH E .   ? 0.5476 0.4546 0.2687 -0.0792 0.0881  0.1692  549 HOH A O   
2313 O  O   . HOH E .   ? 0.3747 0.3113 0.2502 0.0550  0.0301  0.0991  550 HOH A O   
2314 O  O   . HOH E .   ? 0.3015 0.3596 0.9796 -0.0233 0.1701  0.0598  551 HOH A O   
2315 O  O   . HOH E .   ? 0.5514 0.3269 0.3914 0.1156  0.1945  0.0841  552 HOH A O   
2316 O  O   . HOH E .   ? 0.2894 0.3021 0.4356 0.0436  0.0234  0.0069  553 HOH A O   
2317 O  O   . HOH E .   ? 0.4966 0.6612 0.7126 -0.0003 0.0921  0.0113  554 HOH A O   
2318 O  O   . HOH E .   ? 0.3428 0.5337 0.7119 0.0930  -0.0963 0.0491  555 HOH A O   
2319 O  O   . HOH E .   ? 0.3299 0.2944 0.4097 0.0282  -0.0519 -0.0309 556 HOH A O   
2320 O  O   . HOH E .   ? 0.2983 0.3333 0.4180 0.1661  -0.0222 0.0463  557 HOH A O   
2321 O  O   . HOH E .   ? 0.3044 0.3535 0.3686 0.0358  -0.1094 -0.0290 558 HOH A O   
2322 O  O   . HOH E .   ? 0.4697 0.5496 0.5442 -0.1591 -0.1536 0.1498  559 HOH A O   
2323 O  O   . HOH E .   ? 0.3810 0.3091 0.6809 -0.0560 -0.0582 0.0783  560 HOH A O   
2324 O  O   . HOH E .   ? 0.3206 0.8544 0.6463 -0.1037 0.1072  0.1147  561 HOH A O   
2325 O  O   . HOH E .   ? 0.4373 0.4792 0.2611 0.0340  -0.0234 0.0142  562 HOH A O   
2326 O  O   . HOH E .   ? 0.4378 0.2360 0.4228 0.0741  0.1328  0.0771  563 HOH A O   
2327 O  O   . HOH E .   ? 0.3881 0.1458 0.3316 0.0534  0.0394  0.0018  564 HOH A O   
2328 O  O   . HOH E .   ? 0.6118 0.3052 0.2691 0.1096  -0.0693 0.0252  565 HOH A O   
2329 O  O   . HOH E .   ? 0.6068 0.6485 0.6503 0.0570  -0.0092 0.0591  566 HOH A O   
2330 O  O   . HOH E .   ? 0.1412 0.2348 0.4055 0.0008  -0.0032 0.0313  567 HOH A O   
2331 O  O   . HOH E .   ? 0.5898 0.7874 0.4746 -0.1441 0.2195  -0.2464 568 HOH A O   
2332 O  O   . HOH E .   ? 0.2444 0.3904 0.4502 -0.0178 -0.0339 0.0026  569 HOH A O   
2333 O  O   . HOH E .   ? 0.4521 0.6249 0.3603 0.1958  -0.2374 -0.1332 570 HOH A O   
2334 O  O   . HOH E .   ? 0.3065 0.1848 1.0741 0.0548  -0.0268 -0.1395 571 HOH A O   
2335 O  O   . HOH E .   ? 0.5512 0.5608 0.5900 0.2514  -0.1104 -0.1708 572 HOH A O   
2336 O  O   . HOH E .   ? 0.7155 0.4548 0.6427 0.1124  -0.1020 -0.0829 573 HOH A O   
2337 O  O   . HOH E .   ? 0.5256 0.4639 0.5698 -0.1450 -0.2606 -0.0511 574 HOH A O   
2338 O  O   . HOH E .   ? 0.2232 0.4137 1.0305 -0.0217 -0.2171 0.0956  575 HOH A O   
2339 O  O   . HOH E .   ? 0.3226 0.4029 0.4819 0.0308  -0.0697 -0.1265 576 HOH A O   
2340 O  O   . HOH E .   ? 0.5059 0.6656 0.7251 0.0039  0.3133  -0.2077 577 HOH A O   
2341 O  O   . HOH E .   ? 0.9701 1.2862 0.5503 0.6007  0.1670  -0.3458 578 HOH A O   
2342 O  O   . HOH E .   ? 0.4811 0.6852 0.4953 -0.2500 0.1297  -0.2315 579 HOH A O   
2343 O  O   . HOH E .   ? 0.4417 0.7007 0.6186 0.0446  -0.1089 0.1533  580 HOH A O   
2344 O  O   . HOH E .   ? 0.4541 0.4015 0.5346 -0.0038 0.1744  0.1815  581 HOH A O   
2345 O  O   . HOH E .   ? 0.3704 0.3076 0.4216 0.0771  -0.2265 -0.0352 582 HOH A O   
2346 O  O   . HOH E .   ? 0.3540 0.4922 0.6132 0.0900  -0.0591 -0.0159 583 HOH A O   
2347 O  O   . HOH E .   ? 0.2804 0.3862 0.4236 -0.0380 0.0362  0.0578  584 HOH A O   
2348 O  O   . HOH E .   ? 0.2681 0.2384 0.2391 -0.0428 -0.0489 0.0174  585 HOH A O   
2349 O  O   . HOH E .   ? 0.5169 0.5311 0.3509 -0.0033 -0.0375 0.1034  586 HOH A O   
2350 O  O   . HOH E .   ? 0.4290 0.3360 0.7781 0.0054  0.1147  -0.0604 587 HOH A O   
2351 O  O   . HOH E .   ? 0.3935 0.5598 0.7753 -0.0261 0.0399  -0.0744 588 HOH A O   
2352 O  O   . HOH E .   ? 0.4895 0.9289 0.5115 0.0577  -0.0430 -0.0117 589 HOH A O   
2353 O  O   . HOH E .   ? 0.3137 0.3563 0.3975 -0.0134 0.0259  0.0201  590 HOH A O   
2354 O  O   . HOH E .   ? 0.1421 0.4627 0.5410 -0.0405 -0.0298 0.1077  591 HOH A O   
2355 O  O   . HOH E .   ? 0.4845 0.7582 0.4913 -0.0390 0.1353  0.0712  592 HOH A O   
2356 O  O   . HOH E .   ? 0.4796 0.4686 0.7278 0.0834  -0.0173 0.0895  593 HOH A O   
2357 O  O   . HOH E .   ? 0.5192 0.5252 0.3759 -0.1722 0.0741  0.1087  594 HOH A O   
2358 O  O   . HOH E .   ? 0.2355 0.3328 0.8211 -0.0387 0.0167  -0.1750 595 HOH A O   
2359 O  O   . HOH E .   ? 0.5634 0.4825 1.0030 0.0167  0.0864  0.0413  596 HOH A O   
2360 O  O   . HOH E .   ? 0.2584 0.7189 1.0407 -0.0365 0.0789  0.4122  597 HOH A O   
2361 O  O   . HOH E .   ? 0.1936 0.6455 0.7545 -0.0039 0.1045  0.0651  598 HOH A O   
2362 O  O   . HOH E .   ? 0.4318 0.6447 0.3119 -0.1893 -0.0146 0.0708  599 HOH A O   
2363 O  O   . HOH E .   ? 0.3440 0.6783 0.3596 0.0196  0.0006  0.1280  600 HOH A O   
2364 O  O   . HOH E .   ? 0.2920 0.5084 0.5296 0.2050  -0.0996 0.0585  601 HOH A O   
2365 O  O   . HOH E .   ? 0.6327 0.3757 0.4308 0.0728  -0.0987 -0.1780 602 HOH A O   
2366 O  O   . HOH E .   ? 0.5155 0.5265 0.3559 0.1456  -0.0390 -0.0148 603 HOH A O   
2367 O  O   . HOH E .   ? 0.4797 0.2682 0.7030 0.1252  0.0546  -0.0476 604 HOH A O   
2368 O  O   . HOH E .   ? 0.3077 0.5137 0.5708 0.1207  -0.0737 0.0675  605 HOH A O   
2369 O  O   . HOH E .   ? 0.2922 0.3933 0.4642 0.0210  0.0819  0.1684  606 HOH A O   
2370 O  O   . HOH E .   ? 0.2503 0.3612 0.5302 0.0087  0.1263  0.0673  607 HOH A O   
2371 O  O   . HOH E .   ? 0.5061 0.3392 0.6427 -0.0485 -0.2001 0.0485  608 HOH A O   
2372 O  O   . HOH E .   ? 0.5279 0.3864 0.4917 0.0272  0.1076  -0.1638 609 HOH A O   
2373 O  O   . HOH E .   ? 0.3486 1.2778 1.2330 -0.1216 0.0057  0.5241  610 HOH A O   
2374 O  O   . HOH E .   ? 0.4336 0.6129 0.5993 0.3283  0.0823  0.0219  611 HOH A O   
2375 O  O   . HOH E .   ? 0.4555 0.3662 0.5326 0.0930  0.1138  0.0385  612 HOH A O   
2376 O  O   . HOH E .   ? 0.3662 0.4833 0.5610 -0.0216 0.0826  0.0904  613 HOH A O   
2377 O  O   . HOH E .   ? 0.5103 0.4154 0.2458 -0.1348 0.0210  0.0346  614 HOH A O   
2378 O  O   . HOH E .   ? 0.2749 0.3499 0.8542 0.0005  0.0406  0.0866  615 HOH A O   
2379 O  O   . HOH E .   ? 0.6898 0.3990 0.4421 0.0388  -0.1265 0.0077  616 HOH A O   
2380 O  O   . HOH E .   ? 0.3180 0.2560 0.3332 0.0853  -0.0514 -0.0201 617 HOH A O   
2381 O  O   . HOH E .   ? 0.4726 0.7857 0.3342 -0.1904 0.0562  0.0419  618 HOH A O   
2382 O  O   . HOH E .   ? 0.9036 0.5799 0.4888 0.2550  -0.2938 -0.1559 619 HOH A O   
2383 O  O   . HOH E .   ? 0.4146 0.4314 0.7128 0.0026  -0.0184 0.0482  620 HOH A O   
2384 O  O   . HOH E .   ? 0.3799 0.7332 0.5517 0.0239  0.0245  -0.3533 621 HOH A O   
2385 O  O   . HOH E .   ? 0.2531 0.3468 0.3746 0.0322  0.0100  -0.0237 622 HOH A O   
2386 O  O   . HOH E .   ? 0.3413 0.5601 0.5101 -0.0132 0.0943  -0.1997 623 HOH A O   
2387 O  O   . HOH E .   ? 0.3039 0.2780 0.5619 0.0080  0.1421  -0.0036 624 HOH A O   
2388 O  O   . HOH E .   ? 0.5110 0.5686 0.5329 0.2550  0.2149  0.1720  625 HOH A O   
2389 O  O   . HOH E .   ? 0.3578 0.3535 0.2169 -0.0416 0.0137  -0.0190 626 HOH A O   
2390 O  O   . HOH E .   ? 0.4108 0.3841 0.7265 -0.0890 0.1322  0.0168  627 HOH A O   
2391 O  O   . HOH E .   ? 0.6626 0.4952 0.3609 0.0359  -0.1158 -0.1907 628 HOH A O   
2392 O  O   . HOH E .   ? 0.4797 0.5212 0.3540 0.0619  -0.1595 -0.0242 629 HOH A O   
2393 O  O   . HOH E .   ? 1.0421 1.0680 0.9614 -0.3290 -0.2581 0.2633  630 HOH A O   
2394 O  O   . HOH E .   ? 0.4003 0.4096 0.2773 -0.0027 -0.1425 0.0351  631 HOH A O   
# 
