data_6YH7
# 
_entry.id   6YH7 
# 
_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   6YH7         pdb_00006yh7 10.2210/pdb6yh7/pdb 
WWPDB D_1292106472 ?            ?                   
# 
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' Advisory                 
3 3 'Structure model' 'Data collection'        
4 3 'Structure model' 'Database references'    
5 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 
7 3 'Structure model' pdbx_unobs_or_zero_occ_atoms  
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                   
2  2 'Structure model' '_citation.journal_abbrev'            
3  2 'Structure model' '_citation.journal_id_CSD'            
4  2 'Structure model' '_citation.journal_id_ISSN'           
5  2 'Structure model' '_citation.journal_volume'            
6  2 'Structure model' '_citation.page_first'                
7  2 'Structure model' '_citation.page_last'                 
8  2 'Structure model' '_citation.pdbx_database_id_DOI'      
9  2 'Structure model' '_citation.pdbx_database_id_PubMed'   
10 2 'Structure model' '_citation.title'                     
11 2 'Structure model' '_citation.year'                      
12 3 'Structure model' '_database_2.pdbx_DOI'                
13 3 'Structure model' '_database_2.pdbx_database_accession' 
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   '5EF A 304 HAS WRONG CHIRALITY AT ATOM C21' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6YH7 
_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 'DIMETHYL SULFOXIDE'                                                                                     78.133 
1   ?       ?                                       ? ? 
4 non-polymer syn '3-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 450.452 
2   ?       ?                                       ? ? 
5 water       nat water                                                                                                    18.015 
284 ?       ?                                       ? ? 
# 
_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 'DIMETHYL SULFOXIDE'                                                                                     DMS 
4 '3-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 5EF 
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 
5EF non-polymer         . '3-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 
? 'C17 H17 F3 N2 O5 S2' 450.452 
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 
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 DMS 1   302 1   DMS DMS A . 
D 4 5EF 1   303 1   5EF V13 A . 
E 4 5EF 1   304 2   5EF V13 A . 
F 5 HOH 1   401 221 HOH HOH A . 
F 5 HOH 2   402 134 HOH HOH A . 
F 5 HOH 3   403 187 HOH HOH A . 
F 5 HOH 4   404 24  HOH HOH A . 
F 5 HOH 5   405 244 HOH HOH A . 
F 5 HOH 6   406 165 HOH HOH A . 
F 5 HOH 7   407 179 HOH HOH A . 
F 5 HOH 8   408 168 HOH HOH A . 
F 5 HOH 9   409 171 HOH HOH A . 
F 5 HOH 10  410 153 HOH HOH A . 
F 5 HOH 11  411 68  HOH HOH A . 
F 5 HOH 12  412 101 HOH HOH A . 
F 5 HOH 13  413 64  HOH HOH A . 
F 5 HOH 14  414 88  HOH HOH A . 
F 5 HOH 15  415 55  HOH HOH A . 
F 5 HOH 16  416 217 HOH HOH A . 
F 5 HOH 17  417 99  HOH HOH A . 
F 5 HOH 18  418 156 HOH HOH A . 
F 5 HOH 19  419 188 HOH HOH A . 
F 5 HOH 20  420 209 HOH HOH A . 
F 5 HOH 21  421 159 HOH HOH A . 
F 5 HOH 22  422 237 HOH HOH A . 
F 5 HOH 23  423 124 HOH HOH A . 
F 5 HOH 24  424 196 HOH HOH A . 
F 5 HOH 25  425 40  HOH HOH A . 
F 5 HOH 26  426 98  HOH HOH A . 
F 5 HOH 27  427 126 HOH HOH A . 
F 5 HOH 28  428 83  HOH HOH A . 
F 5 HOH 29  429 97  HOH HOH A . 
F 5 HOH 30  430 200 HOH HOH A . 
F 5 HOH 31  431 231 HOH HOH A . 
F 5 HOH 32  432 185 HOH HOH A . 
F 5 HOH 33  433 28  HOH HOH A . 
F 5 HOH 34  434 136 HOH HOH A . 
F 5 HOH 35  435 113 HOH HOH A . 
F 5 HOH 36  436 161 HOH HOH A . 
F 5 HOH 37  437 103 HOH HOH A . 
F 5 HOH 38  438 19  HOH HOH A . 
F 5 HOH 39  439 16  HOH HOH A . 
F 5 HOH 40  440 50  HOH HOH A . 
F 5 HOH 41  441 47  HOH HOH A . 
F 5 HOH 42  442 138 HOH HOH A . 
F 5 HOH 43  443 74  HOH HOH A . 
F 5 HOH 44  444 223 HOH HOH A . 
F 5 HOH 45  445 85  HOH HOH A . 
F 5 HOH 46  446 26  HOH HOH A . 
F 5 HOH 47  447 227 HOH HOH A . 
F 5 HOH 48  448 279 HOH HOH A . 
F 5 HOH 49  449 34  HOH HOH A . 
F 5 HOH 50  450 270 HOH HOH A . 
F 5 HOH 51  451 114 HOH HOH A . 
F 5 HOH 52  452 219 HOH HOH A . 
F 5 HOH 53  453 20  HOH HOH A . 
F 5 HOH 54  454 10  HOH HOH A . 
F 5 HOH 55  455 119 HOH HOH A . 
F 5 HOH 56  456 33  HOH HOH A . 
F 5 HOH 57  457 109 HOH HOH A . 
F 5 HOH 58  458 122 HOH HOH A . 
F 5 HOH 59  459 89  HOH HOH A . 
F 5 HOH 60  460 199 HOH HOH A . 
F 5 HOH 61  461 264 HOH HOH A . 
F 5 HOH 62  462 13  HOH HOH A . 
F 5 HOH 63  463 70  HOH HOH A . 
F 5 HOH 64  464 87  HOH HOH A . 
F 5 HOH 65  465 21  HOH HOH A . 
F 5 HOH 66  466 173 HOH HOH A . 
F 5 HOH 67  467 252 HOH HOH A . 
F 5 HOH 68  468 218 HOH HOH A . 
F 5 HOH 69  469 130 HOH HOH A . 
F 5 HOH 70  470 58  HOH HOH A . 
F 5 HOH 71  471 92  HOH HOH A . 
F 5 HOH 72  472 62  HOH HOH A . 
F 5 HOH 73  473 15  HOH HOH A . 
F 5 HOH 74  474 118 HOH HOH A . 
F 5 HOH 75  475 31  HOH HOH A . 
F 5 HOH 76  476 205 HOH HOH A . 
F 5 HOH 77  477 240 HOH HOH A . 
F 5 HOH 78  478 175 HOH HOH A . 
F 5 HOH 79  479 195 HOH HOH A . 
F 5 HOH 80  480 262 HOH HOH A . 
F 5 HOH 81  481 204 HOH HOH A . 
F 5 HOH 82  482 6   HOH HOH A . 
F 5 HOH 83  483 94  HOH HOH A . 
F 5 HOH 84  484 167 HOH HOH A . 
F 5 HOH 85  485 35  HOH HOH A . 
F 5 HOH 86  486 115 HOH HOH A . 
F 5 HOH 87  487 105 HOH HOH A . 
F 5 HOH 88  488 82  HOH HOH A . 
F 5 HOH 89  489 117 HOH HOH A . 
F 5 HOH 90  490 157 HOH HOH A . 
F 5 HOH 91  491 123 HOH HOH A . 
F 5 HOH 92  492 137 HOH HOH A . 
F 5 HOH 93  493 41  HOH HOH A . 
F 5 HOH 94  494 127 HOH HOH A . 
F 5 HOH 95  495 135 HOH HOH A . 
F 5 HOH 96  496 12  HOH HOH A . 
F 5 HOH 97  497 1   HOH HOH A . 
F 5 HOH 98  498 45  HOH HOH A . 
F 5 HOH 99  499 224 HOH HOH A . 
F 5 HOH 100 500 80  HOH HOH A . 
F 5 HOH 101 501 9   HOH HOH A . 
F 5 HOH 102 502 148 HOH HOH A . 
F 5 HOH 103 503 2   HOH HOH A . 
F 5 HOH 104 504 67  HOH HOH A . 
F 5 HOH 105 505 133 HOH HOH A . 
F 5 HOH 106 506 60  HOH HOH A . 
F 5 HOH 107 507 22  HOH HOH A . 
F 5 HOH 108 508 43  HOH HOH A . 
F 5 HOH 109 509 72  HOH HOH A . 
F 5 HOH 110 510 214 HOH HOH A . 
F 5 HOH 111 511 17  HOH HOH A . 
F 5 HOH 112 512 18  HOH HOH A . 
F 5 HOH 113 513 71  HOH HOH A . 
F 5 HOH 114 514 166 HOH HOH A . 
F 5 HOH 115 515 8   HOH HOH A . 
F 5 HOH 116 516 11  HOH HOH A . 
F 5 HOH 117 517 30  HOH HOH A . 
F 5 HOH 118 518 197 HOH HOH A . 
F 5 HOH 119 519 236 HOH HOH A . 
F 5 HOH 120 520 54  HOH HOH A . 
F 5 HOH 121 521 190 HOH HOH A . 
F 5 HOH 122 522 79  HOH HOH A . 
F 5 HOH 123 523 36  HOH HOH A . 
F 5 HOH 124 524 106 HOH HOH A . 
F 5 HOH 125 525 29  HOH HOH A . 
F 5 HOH 126 526 120 HOH HOH A . 
F 5 HOH 127 527 3   HOH HOH A . 
F 5 HOH 128 528 93  HOH HOH A . 
F 5 HOH 129 529 170 HOH HOH A . 
F 5 HOH 130 530 268 HOH HOH A . 
F 5 HOH 131 531 14  HOH HOH A . 
F 5 HOH 132 532 38  HOH HOH A . 
F 5 HOH 133 533 277 HOH HOH A . 
F 5 HOH 134 534 59  HOH HOH A . 
F 5 HOH 135 535 102 HOH HOH A . 
F 5 HOH 136 536 129 HOH HOH A . 
F 5 HOH 137 537 69  HOH HOH A . 
F 5 HOH 138 538 162 HOH HOH A . 
F 5 HOH 139 539 267 HOH HOH A . 
F 5 HOH 140 540 125 HOH HOH A . 
F 5 HOH 141 541 149 HOH HOH A . 
F 5 HOH 142 542 46  HOH HOH A . 
F 5 HOH 143 543 66  HOH HOH A . 
F 5 HOH 144 544 271 HOH HOH A . 
F 5 HOH 145 545 81  HOH HOH A . 
F 5 HOH 146 546 57  HOH HOH A . 
F 5 HOH 147 547 174 HOH HOH A . 
F 5 HOH 148 548 155 HOH HOH A . 
F 5 HOH 149 549 247 HOH HOH A . 
F 5 HOH 150 550 110 HOH HOH A . 
F 5 HOH 151 551 281 HOH HOH A . 
F 5 HOH 152 552 234 HOH HOH A . 
F 5 HOH 153 553 265 HOH HOH A . 
F 5 HOH 154 554 48  HOH HOH A . 
F 5 HOH 155 555 150 HOH HOH A . 
F 5 HOH 156 556 23  HOH HOH A . 
F 5 HOH 157 557 220 HOH HOH A . 
F 5 HOH 158 558 180 HOH HOH A . 
F 5 HOH 159 559 25  HOH HOH A . 
F 5 HOH 160 560 78  HOH HOH A . 
F 5 HOH 161 561 241 HOH HOH A . 
F 5 HOH 162 562 202 HOH HOH A . 
F 5 HOH 163 563 86  HOH HOH A . 
F 5 HOH 164 564 63  HOH HOH A . 
F 5 HOH 165 565 233 HOH HOH A . 
F 5 HOH 166 566 42  HOH HOH A . 
F 5 HOH 167 567 91  HOH HOH A . 
F 5 HOH 168 568 7   HOH HOH A . 
F 5 HOH 169 569 61  HOH HOH A . 
F 5 HOH 170 570 73  HOH HOH A . 
F 5 HOH 171 571 128 HOH HOH A . 
F 5 HOH 172 572 249 HOH HOH A . 
F 5 HOH 173 573 256 HOH HOH A . 
F 5 HOH 174 574 49  HOH HOH A . 
F 5 HOH 175 575 143 HOH HOH A . 
F 5 HOH 176 576 222 HOH HOH A . 
F 5 HOH 177 577 84  HOH HOH A . 
F 5 HOH 178 578 95  HOH HOH A . 
F 5 HOH 179 579 53  HOH HOH A . 
F 5 HOH 180 580 76  HOH HOH A . 
F 5 HOH 181 581 108 HOH HOH A . 
F 5 HOH 182 582 248 HOH HOH A . 
F 5 HOH 183 583 107 HOH HOH A . 
F 5 HOH 184 584 104 HOH HOH A . 
F 5 HOH 185 585 44  HOH HOH A . 
F 5 HOH 186 586 257 HOH HOH A . 
F 5 HOH 187 587 56  HOH HOH A . 
F 5 HOH 188 588 147 HOH HOH A . 
F 5 HOH 189 589 261 HOH HOH A . 
F 5 HOH 190 590 207 HOH HOH A . 
F 5 HOH 191 591 75  HOH HOH A . 
F 5 HOH 192 592 226 HOH HOH A . 
F 5 HOH 193 593 51  HOH HOH A . 
F 5 HOH 194 594 5   HOH HOH A . 
F 5 HOH 195 595 206 HOH HOH A . 
F 5 HOH 196 596 235 HOH HOH A . 
F 5 HOH 197 597 151 HOH HOH A . 
F 5 HOH 198 598 142 HOH HOH A . 
F 5 HOH 199 599 216 HOH HOH A . 
F 5 HOH 200 600 27  HOH HOH A . 
F 5 HOH 201 601 32  HOH HOH A . 
F 5 HOH 202 602 158 HOH HOH A . 
F 5 HOH 203 603 96  HOH HOH A . 
F 5 HOH 204 604 228 HOH HOH A . 
F 5 HOH 205 605 39  HOH HOH A . 
F 5 HOH 206 606 181 HOH HOH A . 
F 5 HOH 207 607 275 HOH HOH A . 
F 5 HOH 208 608 258 HOH HOH A . 
F 5 HOH 209 609 192 HOH HOH A . 
F 5 HOH 210 610 208 HOH HOH A . 
F 5 HOH 211 611 259 HOH HOH A . 
F 5 HOH 212 612 283 HOH HOH A . 
F 5 HOH 213 613 211 HOH HOH A . 
F 5 HOH 214 614 253 HOH HOH A . 
F 5 HOH 215 615 186 HOH HOH A . 
F 5 HOH 216 616 100 HOH HOH A . 
F 5 HOH 217 617 52  HOH HOH A . 
F 5 HOH 218 618 229 HOH HOH A . 
F 5 HOH 219 619 193 HOH HOH A . 
F 5 HOH 220 620 144 HOH HOH A . 
F 5 HOH 221 621 139 HOH HOH A . 
F 5 HOH 222 622 4   HOH HOH A . 
F 5 HOH 223 623 140 HOH HOH A . 
F 5 HOH 224 624 194 HOH HOH A . 
F 5 HOH 225 625 212 HOH HOH A . 
F 5 HOH 226 626 37  HOH HOH A . 
F 5 HOH 227 627 245 HOH HOH A . 
F 5 HOH 228 628 274 HOH HOH A . 
F 5 HOH 229 629 255 HOH HOH A . 
F 5 HOH 230 630 250 HOH HOH A . 
F 5 HOH 231 631 182 HOH HOH A . 
F 5 HOH 232 632 280 HOH HOH A . 
F 5 HOH 233 633 203 HOH HOH A . 
F 5 HOH 234 634 90  HOH HOH A . 
F 5 HOH 235 635 112 HOH HOH A . 
F 5 HOH 236 636 132 HOH HOH A . 
F 5 HOH 237 637 239 HOH HOH A . 
F 5 HOH 238 638 254 HOH HOH A . 
F 5 HOH 239 639 263 HOH HOH A . 
F 5 HOH 240 640 154 HOH HOH A . 
F 5 HOH 241 641 183 HOH HOH A . 
F 5 HOH 242 642 272 HOH HOH A . 
F 5 HOH 243 643 225 HOH HOH A . 
F 5 HOH 244 644 278 HOH HOH A . 
F 5 HOH 245 645 172 HOH HOH A . 
F 5 HOH 246 646 215 HOH HOH A . 
F 5 HOH 247 647 131 HOH HOH A . 
F 5 HOH 248 648 273 HOH HOH A . 
F 5 HOH 249 649 210 HOH HOH A . 
F 5 HOH 250 650 230 HOH HOH A . 
F 5 HOH 251 651 111 HOH HOH A . 
F 5 HOH 252 652 238 HOH HOH A . 
F 5 HOH 253 653 282 HOH HOH A . 
F 5 HOH 254 654 191 HOH HOH A . 
F 5 HOH 255 655 163 HOH HOH A . 
F 5 HOH 256 656 164 HOH HOH A . 
F 5 HOH 257 657 242 HOH HOH A . 
F 5 HOH 258 658 260 HOH HOH A . 
F 5 HOH 259 659 152 HOH HOH A . 
F 5 HOH 260 660 189 HOH HOH A . 
F 5 HOH 261 661 121 HOH HOH A . 
F 5 HOH 262 662 246 HOH HOH A . 
F 5 HOH 263 663 243 HOH HOH A . 
F 5 HOH 264 664 145 HOH HOH A . 
F 5 HOH 265 665 65  HOH HOH A . 
F 5 HOH 266 666 116 HOH HOH A . 
F 5 HOH 267 667 178 HOH HOH A . 
F 5 HOH 268 668 201 HOH HOH A . 
F 5 HOH 269 669 269 HOH HOH A . 
F 5 HOH 270 670 169 HOH HOH A . 
F 5 HOH 271 671 176 HOH HOH A . 
F 5 HOH 272 672 232 HOH HOH A . 
F 5 HOH 273 673 276 HOH HOH A . 
F 5 HOH 274 674 160 HOH HOH A . 
F 5 HOH 275 675 77  HOH HOH A . 
F 5 HOH 276 676 184 HOH HOH A . 
F 5 HOH 277 677 266 HOH HOH A . 
F 5 HOH 278 678 177 HOH HOH A . 
F 5 HOH 279 679 251 HOH HOH A . 
F 5 HOH 280 680 284 HOH HOH A . 
F 5 HOH 281 681 213 HOH HOH A . 
F 5 HOH 282 682 198 HOH HOH A . 
F 5 HOH 283 683 141 HOH HOH A . 
F 5 HOH 284 684 146 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
3  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
4  1 Y 1 A LYS 45  ? CE  ? A LYS 45  CE  
5  1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
6  1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
7  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
8  1 Y 1 A LYS 133 ? CE  ? A LYS 132 CE  
9  1 Y 1 A LYS 133 ? NZ  ? A LYS 132 NZ  
10 1 Y 1 A LYS 213 ? CE  ? A LYS 212 CE  
11 1 Y 1 A LYS 213 ? NZ  ? A LYS 212 NZ  
12 1 Y 0 A LEU 224 ? CD1 A A LEU 223 CD1 
13 1 Y 1 A GLN 255 ? CD  ? A GLN 254 CD  
14 1 Y 1 A GLN 255 ? OE1 ? A GLN 254 OE1 
15 1 Y 1 A GLN 255 ? NE2 ? A GLN 254 NE2 
16 1 Y 1 A LYS 257 ? CE  ? A LYS 256 CE  
17 1 Y 1 A LYS 257 ? NZ  ? A LYS 256 NZ  
18 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
19 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       ? ? ? 3.3.20   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                   103.570 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6YH7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.786 
_cell.length_a_esd                 ? 
_cell.length_b                     40.969 
_cell.length_b_esd                 ? 
_cell.length_c                     71.267 
_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                         6YH7 
_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                   6YH7 
_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            2.03 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.39 
_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                         6YH7 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.120 
_reflns.d_resolution_low                 40.969 
_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                       87438 
_reflns.number_obs                       87438 
_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             97.000 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  4.700 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.051 
_reflns.pdbx_netI_over_av_sigmaI         5.900 
_reflns.pdbx_netI_over_sigmaI            10.300 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.064 
_reflns.pdbx_Rpim_I_all                  0.028 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         407845 
_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 
1.120 1.180  ? 2.100  42710 ? ? ? 11577 88.800 ? ? ? ? 0.342 ? ? ? ? ? ? ? ? 3.700 0.342 ? ? 3.100  0.421 0.212 ? 1  1 ? ? ? 
1.180 1.250  ? 2.700  46934 ? ? ? 11666 94.200 ? ? ? ? 0.269 ? ? ? ? ? ? ? ? 4.000 0.269 ? ? 3.900  0.330 0.160 ? 2  1 ? ? ? 
1.250 1.340  ? 3.300  55497 ? ? ? 11572 99.000 ? ? ? ? 0.218 ? ? ? ? ? ? ? ? 4.800 0.218 ? ? 5.100  0.263 0.118 ? 3  1 ? ? ? 
1.340 1.450  ? 4.900  52508 ? ? ? 10744 98.900 ? ? ? ? 0.146 ? ? ? ? ? ? ? ? 4.900 0.146 ? ? 6.600  0.182 0.081 ? 4  1 ? ? ? 
1.450 1.580  ? 7.000  48319 ? ? ? 9932  99.200 ? ? ? ? 0.099 ? ? ? ? ? ? ? ? 4.900 0.099 ? ? 8.800  0.126 0.057 ? 5  1 ? ? ? 
1.580 1.770  ? 8.500  45668 ? ? ? 8978  99.300 ? ? ? ? 0.076 ? ? ? ? ? ? ? ? 5.100 0.076 ? ? 12.100 0.097 0.043 ? 6  1 ? ? ? 
1.770 2.040  ? 10.000 40864 ? ? ? 7991  99.400 ? ? ? ? 0.060 ? ? ? ? ? ? ? ? 5.100 0.060 ? ? 17.000 0.077 0.034 ? 7  1 ? ? ? 
2.040 2.500  ? 11.600 34238 ? ? ? 6731  99.500 ? ? ? ? 0.053 ? ? ? ? ? ? ? ? 5.100 0.053 ? ? 21.300 0.066 0.029 ? 8  1 ? ? ? 
2.500 3.540  ? 14.000 26532 ? ? ? 5272  99.500 ? ? ? ? 0.040 ? ? ? ? ? ? ? ? 5.000 0.040 ? ? 24.800 0.050 0.022 ? 9  1 ? ? ? 
3.540 40.969 ? 13.500 14575 ? ? ? 2975  99.600 ? ? ? ? 0.033 ? ? ? ? ? ? ? ? 4.900 0.033 ? ? 27.000 0.040 0.018 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.5000 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.0400 
_refine.aniso_B[2][2]                            -0.5800 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.9900 
_refine.B_iso_max                                108.280 
_refine.B_iso_mean                               17.5130 
_refine.B_iso_min                                7.280 
_refine.correlation_coeff_Fo_to_Fc               0.9790 
_refine.correlation_coeff_Fo_to_Fc_free          0.9730 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 6YH7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.1200 
_refine.ls_d_res_low                             40.6200 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     78541 
_refine.ls_number_reflns_R_free                  8787 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.8100 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1364 
_refine.ls_R_factor_R_free                       0.1629 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1334 
_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                       0.0330 
_refine.pdbx_overall_ESU_R_Free                  0.0340 
_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             0.0326 
_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                       1.1200 
_refine_hist.d_res_low                        40.6200 
_refine_hist.number_atoms_solvent             284 
_refine_hist.number_atoms_total               2372 
_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           24.74 
_refine_hist.pdbx_B_iso_mean_solvent          30.13 
_refine_hist.pdbx_number_atoms_protein        2025 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         63 
_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' ? 0.015  0.012  2238 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.135  1.675  3068 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.944  5.000  277  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.196 23.868 106  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.423 15.000 354  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 17.985 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.359  0.200  274  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.020  1759 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 6.118  3.000  2238 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 25.197 5.000  154  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 12.910 5.000  2296 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.1200 
_refine_ls_shell.d_res_low                        1.1490 
_refine_ls_shell.number_reflns_all                5822 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             549 
_refine_ls_shell.number_reflns_R_work             5273 
_refine_ls_shell.percent_reflns_obs               87.7100 
_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                  0.2070 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1900 
_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                     6YH7 
_struct.title                        
;Crystal structure of chimeric carbonic anhydrase XII with 3-[(1S)-2,3-Dihydro-1H-inden-1-ylamino]-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6YH7 
_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 4 ? 
F 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              6YH7 
_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 6YH7 SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6YH7 LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6YH7 THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 6YH7 ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 4 
1 6YH7 SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 5 
1 6YH7 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)'  11250 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 HIS A 15  ? ASP A 19  ? HIS A 15  ASP A 19  5 ? 5 
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 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.010 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 1.985 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 D 5EF . N4 ? ? A ZN  301 A 5EF 303 1_555 ? ? ? ? ? ? ? 1.950 ? ? 
# 
_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_555 103.7 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 111.4 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 100.6 ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? D 5EF .   ? A 5EF 303 ? 1_555 113.7 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? D 5EF .   ? A 5EF 303 ? 1_555 117.6 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? D 5EF .   ? A 5EF 303 ? 1_555 109.2 ? 
# 
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 -1.41 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 9.41  
# 
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 GLN A 92  ? N GLN A 92  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A DMS 302 ? 4  'binding site for residue DMS A 302' 
AC3 Software A 5EF 303 ? 15 'binding site for residue 5EF A 303' 
AC4 Software A 5EF 304 ? 12 'binding site for residue 5EF A 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  5EF D .   ? 5EF A 303 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  PRO A 246 ? PRO A 247 . ? 1_555 ? 
9  AC3 15 ASN A 62  ? ASN A 62  . ? 1_555 ? 
10 AC3 15 LYS A 67  ? LYS A 67  . ? 1_555 ? 
11 AC3 15 GLN A 92  ? GLN A 92  . ? 1_555 ? 
12 AC3 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
13 AC3 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
14 AC3 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
15 AC3 15 VAL A 121 ? VAL A 121 . ? 1_555 ? 
16 AC3 15 ALA A 130 ? ALA A 131 . ? 1_555 ? 
17 AC3 15 SER A 134 ? SER A 135 . ? 1_555 ? 
18 AC3 15 LEU A 140 ? LEU A 141 . ? 1_555 ? 
19 AC3 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
20 AC3 15 THR A 198 ? THR A 199 . ? 1_555 ? 
21 AC3 15 THR A 199 ? THR A 200 . ? 1_555 ? 
22 AC3 15 PRO A 200 ? PRO A 201 . ? 1_555 ? 
23 AC3 15 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
24 AC4 12 HIS A 4   ? HIS A 4   . ? 1_455 ? 
25 AC4 12 HIS A 10  ? HIS A 10  . ? 1_455 ? 
26 AC4 12 ASN A 11  ? ASN A 11  . ? 1_455 ? 
27 AC4 12 ASP A 19  ? ASP A 19  . ? 1_455 ? 
28 AC4 12 PRO A 154 ? PRO A 155 . ? 1_555 ? 
29 AC4 12 GLY A 155 ? GLY A 156 . ? 1_555 ? 
30 AC4 12 PHE A 178 ? PHE A 179 . ? 1_555 ? 
31 AC4 12 ASP A 179 ? ASP A 180 . ? 1_555 ? 
32 AC4 12 ARG A 181 ? ARG A 182 . ? 1_555 ? 
33 AC4 12 GLY A 182 ? GLY A 183 . ? 1_555 ? 
34 AC4 12 HOH F .   ? HOH A 512 . ? 1_555 ? 
35 AC4 12 HOH F .   ? HOH A 608 . ? 1_455 ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    34 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   A 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.80 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -144.10 56.12   
2 1 GLU A 106 ? ? -90.99  -60.90  
3 1 LYS A 111 ? ? 76.14   -5.04   
4 1 PHE A 176 ? ? -151.53 73.06   
5 1 PHE A 176 ? ? -155.68 73.06   
6 1 ASN A 244 ? ? -94.66  49.58   
7 1 LYS A 252 ? ? 55.04   -137.55 
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C21 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    5EF 
_pdbx_validate_chiral.auth_seq_id     304 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         PLANAR 
_pdbx_validate_chiral.omega           . 
# 
_pdbx_entry_details.entry_id                 6YH7 
_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         ? 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       684 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.57 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
5EF O19  O  N N 1   
5EF C17  C  N N 2   
5EF C6   C  Y N 3   
5EF F11  F  N N 4   
5EF C5   C  Y N 5   
5EF F12  F  N N 6   
5EF F13  F  N N 7   
5EF O16  O  N N 8   
5EF S14  S  N N 9   
5EF O15  O  N N 10  
5EF C18  C  N N 11  
5EF C8   C  Y N 12  
5EF C7   C  Y N 13  
5EF C9   C  Y N 14  
5EF C10  C  Y N 15  
5EF S1   S  N N 16  
5EF O3   O  N N 17  
5EF N4   N  N N 18  
5EF O2   O  N N 19  
5EF N20  N  N N 20  
5EF C21  C  N S 21  
5EF C25  C  N N 22  
5EF C24  C  N N 23  
5EF C23  C  Y N 24  
5EF C29  C  Y N 25  
5EF C28  C  Y N 26  
5EF C27  C  Y N 27  
5EF C26  C  Y N 28  
5EF C22  C  Y N 29  
5EF H1   H  N N 30  
5EF H2   H  N N 31  
5EF H3   H  N N 32  
5EF H4   H  N N 33  
5EF H5   H  N N 34  
5EF H6   H  N N 35  
5EF H7   H  N N 36  
5EF H8   H  N N 37  
5EF H9   H  N N 38  
5EF H10  H  N N 39  
5EF H11  H  N N 40  
5EF H12  H  N N 41  
5EF H13  H  N N 42  
5EF H14  H  N N 43  
5EF H15  H  N N 44  
5EF H16  H  N N 45  
5EF H17  H  N N 46  
ALA N    N  N N 47  
ALA CA   C  N S 48  
ALA C    C  N N 49  
ALA O    O  N N 50  
ALA CB   C  N N 51  
ALA OXT  O  N N 52  
ALA H    H  N N 53  
ALA H2   H  N N 54  
ALA HA   H  N N 55  
ALA HB1  H  N N 56  
ALA HB2  H  N N 57  
ALA HB3  H  N N 58  
ALA HXT  H  N N 59  
ARG N    N  N N 60  
ARG CA   C  N S 61  
ARG C    C  N N 62  
ARG O    O  N N 63  
ARG CB   C  N N 64  
ARG CG   C  N N 65  
ARG CD   C  N N 66  
ARG NE   N  N N 67  
ARG CZ   C  N N 68  
ARG NH1  N  N N 69  
ARG NH2  N  N N 70  
ARG OXT  O  N N 71  
ARG H    H  N N 72  
ARG H2   H  N N 73  
ARG HA   H  N N 74  
ARG HB2  H  N N 75  
ARG HB3  H  N N 76  
ARG HG2  H  N N 77  
ARG HG3  H  N N 78  
ARG HD2  H  N N 79  
ARG HD3  H  N N 80  
ARG HE   H  N N 81  
ARG HH11 H  N N 82  
ARG HH12 H  N N 83  
ARG HH21 H  N N 84  
ARG HH22 H  N N 85  
ARG HXT  H  N N 86  
ASN N    N  N N 87  
ASN CA   C  N S 88  
ASN C    C  N N 89  
ASN O    O  N N 90  
ASN CB   C  N N 91  
ASN CG   C  N N 92  
ASN OD1  O  N N 93  
ASN ND2  N  N N 94  
ASN OXT  O  N N 95  
ASN H    H  N N 96  
ASN H2   H  N N 97  
ASN HA   H  N N 98  
ASN HB2  H  N N 99  
ASN HB3  H  N N 100 
ASN HD21 H  N N 101 
ASN HD22 H  N N 102 
ASN HXT  H  N N 103 
ASP N    N  N N 104 
ASP CA   C  N S 105 
ASP C    C  N N 106 
ASP O    O  N N 107 
ASP CB   C  N N 108 
ASP CG   C  N N 109 
ASP OD1  O  N N 110 
ASP OD2  O  N N 111 
ASP OXT  O  N N 112 
ASP H    H  N N 113 
ASP H2   H  N N 114 
ASP HA   H  N N 115 
ASP HB2  H  N N 116 
ASP HB3  H  N N 117 
ASP HD2  H  N N 118 
ASP HXT  H  N N 119 
CYS N    N  N N 120 
CYS CA   C  N R 121 
CYS C    C  N N 122 
CYS O    O  N N 123 
CYS CB   C  N N 124 
CYS SG   S  N N 125 
CYS OXT  O  N N 126 
CYS H    H  N N 127 
CYS H2   H  N N 128 
CYS HA   H  N N 129 
CYS HB2  H  N N 130 
CYS HB3  H  N N 131 
CYS HG   H  N N 132 
CYS HXT  H  N N 133 
DMS S    S  N N 134 
DMS O    O  N N 135 
DMS C1   C  N N 136 
DMS C2   C  N N 137 
DMS H11  H  N N 138 
DMS H12  H  N N 139 
DMS H13  H  N N 140 
DMS H21  H  N N 141 
DMS H22  H  N N 142 
DMS H23  H  N N 143 
GLN N    N  N N 144 
GLN CA   C  N S 145 
GLN C    C  N N 146 
GLN O    O  N N 147 
GLN CB   C  N N 148 
GLN CG   C  N N 149 
GLN CD   C  N N 150 
GLN OE1  O  N N 151 
GLN NE2  N  N N 152 
GLN OXT  O  N N 153 
GLN H    H  N N 154 
GLN H2   H  N N 155 
GLN HA   H  N N 156 
GLN HB2  H  N N 157 
GLN HB3  H  N N 158 
GLN HG2  H  N N 159 
GLN HG3  H  N N 160 
GLN HE21 H  N N 161 
GLN HE22 H  N N 162 
GLN HXT  H  N N 163 
GLU N    N  N N 164 
GLU CA   C  N S 165 
GLU C    C  N N 166 
GLU O    O  N N 167 
GLU CB   C  N N 168 
GLU CG   C  N N 169 
GLU CD   C  N N 170 
GLU OE1  O  N N 171 
GLU OE2  O  N N 172 
GLU OXT  O  N N 173 
GLU H    H  N N 174 
GLU H2   H  N N 175 
GLU HA   H  N N 176 
GLU HB2  H  N N 177 
GLU HB3  H  N N 178 
GLU HG2  H  N N 179 
GLU HG3  H  N N 180 
GLU HE2  H  N N 181 
GLU HXT  H  N N 182 
GLY N    N  N N 183 
GLY CA   C  N N 184 
GLY C    C  N N 185 
GLY O    O  N N 186 
GLY OXT  O  N N 187 
GLY H    H  N N 188 
GLY H2   H  N N 189 
GLY HA2  H  N N 190 
GLY HA3  H  N N 191 
GLY HXT  H  N N 192 
HIS N    N  N N 193 
HIS CA   C  N S 194 
HIS C    C  N N 195 
HIS O    O  N N 196 
HIS CB   C  N N 197 
HIS CG   C  Y N 198 
HIS ND1  N  Y N 199 
HIS CD2  C  Y N 200 
HIS CE1  C  Y N 201 
HIS NE2  N  Y N 202 
HIS OXT  O  N N 203 
HIS H    H  N N 204 
HIS H2   H  N N 205 
HIS HA   H  N N 206 
HIS HB2  H  N N 207 
HIS HB3  H  N N 208 
HIS HD1  H  N N 209 
HIS HD2  H  N N 210 
HIS HE1  H  N N 211 
HIS HE2  H  N N 212 
HIS HXT  H  N N 213 
HOH O    O  N N 214 
HOH H1   H  N N 215 
HOH H2   H  N N 216 
ILE N    N  N N 217 
ILE CA   C  N S 218 
ILE C    C  N N 219 
ILE O    O  N N 220 
ILE CB   C  N S 221 
ILE CG1  C  N N 222 
ILE CG2  C  N N 223 
ILE CD1  C  N N 224 
ILE OXT  O  N N 225 
ILE H    H  N N 226 
ILE H2   H  N N 227 
ILE HA   H  N N 228 
ILE HB   H  N N 229 
ILE HG12 H  N N 230 
ILE HG13 H  N N 231 
ILE HG21 H  N N 232 
ILE HG22 H  N N 233 
ILE HG23 H  N N 234 
ILE HD11 H  N N 235 
ILE HD12 H  N N 236 
ILE HD13 H  N N 237 
ILE HXT  H  N N 238 
LEU N    N  N N 239 
LEU CA   C  N S 240 
LEU C    C  N N 241 
LEU O    O  N N 242 
LEU CB   C  N N 243 
LEU CG   C  N N 244 
LEU CD1  C  N N 245 
LEU CD2  C  N N 246 
LEU OXT  O  N N 247 
LEU H    H  N N 248 
LEU H2   H  N N 249 
LEU HA   H  N N 250 
LEU HB2  H  N N 251 
LEU HB3  H  N N 252 
LEU HG   H  N N 253 
LEU HD11 H  N N 254 
LEU HD12 H  N N 255 
LEU HD13 H  N N 256 
LEU HD21 H  N N 257 
LEU HD22 H  N N 258 
LEU HD23 H  N N 259 
LEU HXT  H  N N 260 
LYS N    N  N N 261 
LYS CA   C  N S 262 
LYS C    C  N N 263 
LYS O    O  N N 264 
LYS CB   C  N N 265 
LYS CG   C  N N 266 
LYS CD   C  N N 267 
LYS CE   C  N N 268 
LYS NZ   N  N N 269 
LYS OXT  O  N N 270 
LYS H    H  N N 271 
LYS H2   H  N N 272 
LYS HA   H  N N 273 
LYS HB2  H  N N 274 
LYS HB3  H  N N 275 
LYS HG2  H  N N 276 
LYS HG3  H  N N 277 
LYS HD2  H  N N 278 
LYS HD3  H  N N 279 
LYS HE2  H  N N 280 
LYS HE3  H  N N 281 
LYS HZ1  H  N N 282 
LYS HZ2  H  N N 283 
LYS HZ3  H  N N 284 
LYS HXT  H  N N 285 
MET N    N  N N 286 
MET CA   C  N S 287 
MET C    C  N N 288 
MET O    O  N N 289 
MET CB   C  N N 290 
MET CG   C  N N 291 
MET SD   S  N N 292 
MET CE   C  N N 293 
MET OXT  O  N N 294 
MET H    H  N N 295 
MET H2   H  N N 296 
MET HA   H  N N 297 
MET HB2  H  N N 298 
MET HB3  H  N N 299 
MET HG2  H  N N 300 
MET HG3  H  N N 301 
MET HE1  H  N N 302 
MET HE2  H  N N 303 
MET HE3  H  N N 304 
MET HXT  H  N N 305 
PHE N    N  N N 306 
PHE CA   C  N S 307 
PHE C    C  N N 308 
PHE O    O  N N 309 
PHE CB   C  N N 310 
PHE CG   C  Y N 311 
PHE CD1  C  Y N 312 
PHE CD2  C  Y N 313 
PHE CE1  C  Y N 314 
PHE CE2  C  Y N 315 
PHE CZ   C  Y N 316 
PHE OXT  O  N N 317 
PHE H    H  N N 318 
PHE H2   H  N N 319 
PHE HA   H  N N 320 
PHE HB2  H  N N 321 
PHE HB3  H  N N 322 
PHE HD1  H  N N 323 
PHE HD2  H  N N 324 
PHE HE1  H  N N 325 
PHE HE2  H  N N 326 
PHE HZ   H  N N 327 
PHE HXT  H  N N 328 
PRO N    N  N N 329 
PRO CA   C  N S 330 
PRO C    C  N N 331 
PRO O    O  N N 332 
PRO CB   C  N N 333 
PRO CG   C  N N 334 
PRO CD   C  N N 335 
PRO OXT  O  N N 336 
PRO H    H  N N 337 
PRO HA   H  N N 338 
PRO HB2  H  N N 339 
PRO HB3  H  N N 340 
PRO HG2  H  N N 341 
PRO HG3  H  N N 342 
PRO HD2  H  N N 343 
PRO HD3  H  N N 344 
PRO HXT  H  N N 345 
SER N    N  N N 346 
SER CA   C  N S 347 
SER C    C  N N 348 
SER O    O  N N 349 
SER CB   C  N N 350 
SER OG   O  N N 351 
SER OXT  O  N N 352 
SER H    H  N N 353 
SER H2   H  N N 354 
SER HA   H  N N 355 
SER HB2  H  N N 356 
SER HB3  H  N N 357 
SER HG   H  N N 358 
SER HXT  H  N N 359 
THR N    N  N N 360 
THR CA   C  N S 361 
THR C    C  N N 362 
THR O    O  N N 363 
THR CB   C  N R 364 
THR OG1  O  N N 365 
THR CG2  C  N N 366 
THR OXT  O  N N 367 
THR H    H  N N 368 
THR H2   H  N N 369 
THR HA   H  N N 370 
THR HB   H  N N 371 
THR HG1  H  N N 372 
THR HG21 H  N N 373 
THR HG22 H  N N 374 
THR HG23 H  N N 375 
THR HXT  H  N N 376 
TRP N    N  N N 377 
TRP CA   C  N S 378 
TRP C    C  N N 379 
TRP O    O  N N 380 
TRP CB   C  N N 381 
TRP CG   C  Y N 382 
TRP CD1  C  Y N 383 
TRP CD2  C  Y N 384 
TRP NE1  N  Y N 385 
TRP CE2  C  Y N 386 
TRP CE3  C  Y N 387 
TRP CZ2  C  Y N 388 
TRP CZ3  C  Y N 389 
TRP CH2  C  Y N 390 
TRP OXT  O  N N 391 
TRP H    H  N N 392 
TRP H2   H  N N 393 
TRP HA   H  N N 394 
TRP HB2  H  N N 395 
TRP HB3  H  N N 396 
TRP HD1  H  N N 397 
TRP HE1  H  N N 398 
TRP HE3  H  N N 399 
TRP HZ2  H  N N 400 
TRP HZ3  H  N N 401 
TRP HH2  H  N N 402 
TRP HXT  H  N N 403 
TYR N    N  N N 404 
TYR CA   C  N S 405 
TYR C    C  N N 406 
TYR O    O  N N 407 
TYR CB   C  N N 408 
TYR CG   C  Y N 409 
TYR CD1  C  Y N 410 
TYR CD2  C  Y N 411 
TYR CE1  C  Y N 412 
TYR CE2  C  Y N 413 
TYR CZ   C  Y N 414 
TYR OH   O  N N 415 
TYR OXT  O  N N 416 
TYR H    H  N N 417 
TYR H2   H  N N 418 
TYR HA   H  N N 419 
TYR HB2  H  N N 420 
TYR HB3  H  N N 421 
TYR HD1  H  N N 422 
TYR HD2  H  N N 423 
TYR HE1  H  N N 424 
TYR HE2  H  N N 425 
TYR HH   H  N N 426 
TYR HXT  H  N N 427 
VAL N    N  N N 428 
VAL CA   C  N S 429 
VAL C    C  N N 430 
VAL O    O  N N 431 
VAL CB   C  N N 432 
VAL CG1  C  N N 433 
VAL CG2  C  N N 434 
VAL OXT  O  N N 435 
VAL H    H  N N 436 
VAL H2   H  N N 437 
VAL HA   H  N N 438 
VAL HB   H  N N 439 
VAL HG11 H  N N 440 
VAL HG12 H  N N 441 
VAL HG13 H  N N 442 
VAL HG21 H  N N 443 
VAL HG22 H  N N 444 
VAL HG23 H  N N 445 
VAL HXT  H  N N 446 
ZN  ZN   ZN N N 447 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
5EF C28 C29  doub Y N 1   
5EF C28 C27  sing Y N 2   
5EF C29 C23  sing Y N 3   
5EF C27 C26  doub Y N 4   
5EF C23 C24  sing N N 5   
5EF C23 C22  doub Y N 6   
5EF O19 C18  sing N N 7   
5EF C24 C25  sing N N 8   
5EF C26 C22  sing Y N 9   
5EF C18 C17  sing N N 10  
5EF C22 C21  sing N N 11  
5EF C25 C21  sing N N 12  
5EF C17 S14  sing N N 13  
5EF C21 N20  sing N N 14  
5EF O15 S14  doub N N 15  
5EF S14 C8   sing N N 16  
5EF S14 O16  doub N N 17  
5EF N20 C9   sing N N 18  
5EF C9  C8   doub Y N 19  
5EF C9  C10  sing Y N 20  
5EF C8  C7   sing Y N 21  
5EF C7  F12  sing N N 22  
5EF C7  C6   doub Y N 23  
5EF F13 C10  sing N N 24  
5EF C10 C5   doub Y N 25  
5EF C6  C5   sing Y N 26  
5EF C6  F11  sing N N 27  
5EF C5  S1   sing N N 28  
5EF N4  S1   sing N N 29  
5EF S1  O3   doub N N 30  
5EF S1  O2   doub N N 31  
5EF O19 H1   sing N N 32  
5EF C17 H2   sing N N 33  
5EF C17 H3   sing N N 34  
5EF C18 H4   sing N N 35  
5EF C18 H5   sing N N 36  
5EF N4  H6   sing N N 37  
5EF N4  H7   sing N N 38  
5EF N20 H8   sing N N 39  
5EF C21 H9   sing N N 40  
5EF C25 H10  sing N N 41  
5EF C25 H11  sing N N 42  
5EF C24 H12  sing N N 43  
5EF C24 H13  sing N N 44  
5EF C29 H14  sing N N 45  
5EF C28 H15  sing N N 46  
5EF C27 H16  sing N N 47  
5EF C26 H17  sing N N 48  
ALA N   CA   sing N N 49  
ALA N   H    sing N N 50  
ALA N   H2   sing N N 51  
ALA CA  C    sing N N 52  
ALA CA  CB   sing N N 53  
ALA CA  HA   sing N N 54  
ALA C   O    doub N N 55  
ALA C   OXT  sing N N 56  
ALA CB  HB1  sing N N 57  
ALA CB  HB2  sing N N 58  
ALA CB  HB3  sing N N 59  
ALA OXT HXT  sing N N 60  
ARG N   CA   sing N N 61  
ARG N   H    sing N N 62  
ARG N   H2   sing N N 63  
ARG CA  C    sing N N 64  
ARG CA  CB   sing N N 65  
ARG CA  HA   sing N N 66  
ARG C   O    doub N N 67  
ARG C   OXT  sing N N 68  
ARG CB  CG   sing N N 69  
ARG CB  HB2  sing N N 70  
ARG CB  HB3  sing N N 71  
ARG CG  CD   sing N N 72  
ARG CG  HG2  sing N N 73  
ARG CG  HG3  sing N N 74  
ARG CD  NE   sing N N 75  
ARG CD  HD2  sing N N 76  
ARG CD  HD3  sing N N 77  
ARG NE  CZ   sing N N 78  
ARG NE  HE   sing N N 79  
ARG CZ  NH1  sing N N 80  
ARG CZ  NH2  doub N N 81  
ARG NH1 HH11 sing N N 82  
ARG NH1 HH12 sing N N 83  
ARG NH2 HH21 sing N N 84  
ARG NH2 HH22 sing N N 85  
ARG OXT HXT  sing N N 86  
ASN N   CA   sing N N 87  
ASN N   H    sing N N 88  
ASN N   H2   sing N N 89  
ASN CA  C    sing N N 90  
ASN CA  CB   sing N N 91  
ASN CA  HA   sing N N 92  
ASN C   O    doub N N 93  
ASN C   OXT  sing N N 94  
ASN CB  CG   sing N N 95  
ASN CB  HB2  sing N N 96  
ASN CB  HB3  sing N N 97  
ASN CG  OD1  doub N N 98  
ASN CG  ND2  sing N N 99  
ASN ND2 HD21 sing N N 100 
ASN ND2 HD22 sing N N 101 
ASN OXT HXT  sing N N 102 
ASP N   CA   sing N N 103 
ASP N   H    sing N N 104 
ASP N   H2   sing N N 105 
ASP CA  C    sing N N 106 
ASP CA  CB   sing N N 107 
ASP CA  HA   sing N N 108 
ASP C   O    doub N N 109 
ASP C   OXT  sing N N 110 
ASP CB  CG   sing N N 111 
ASP CB  HB2  sing N N 112 
ASP CB  HB3  sing N N 113 
ASP CG  OD1  doub N N 114 
ASP CG  OD2  sing N N 115 
ASP OD2 HD2  sing N N 116 
ASP OXT HXT  sing N N 117 
CYS N   CA   sing N N 118 
CYS N   H    sing N N 119 
CYS N   H2   sing N N 120 
CYS CA  C    sing N N 121 
CYS CA  CB   sing N N 122 
CYS CA  HA   sing N N 123 
CYS C   O    doub N N 124 
CYS C   OXT  sing N N 125 
CYS CB  SG   sing N N 126 
CYS CB  HB2  sing N N 127 
CYS CB  HB3  sing N N 128 
CYS SG  HG   sing N N 129 
CYS OXT HXT  sing N N 130 
DMS S   O    doub N N 131 
DMS S   C1   sing N N 132 
DMS S   C2   sing N N 133 
DMS C1  H11  sing N N 134 
DMS C1  H12  sing N N 135 
DMS C1  H13  sing N N 136 
DMS C2  H21  sing N N 137 
DMS C2  H22  sing N N 138 
DMS C2  H23  sing N N 139 
GLN N   CA   sing N N 140 
GLN N   H    sing N N 141 
GLN N   H2   sing N N 142 
GLN CA  C    sing N N 143 
GLN CA  CB   sing N N 144 
GLN CA  HA   sing N N 145 
GLN C   O    doub N N 146 
GLN C   OXT  sing N N 147 
GLN CB  CG   sing N N 148 
GLN CB  HB2  sing N N 149 
GLN CB  HB3  sing N N 150 
GLN CG  CD   sing N N 151 
GLN CG  HG2  sing N N 152 
GLN CG  HG3  sing N N 153 
GLN CD  OE1  doub N N 154 
GLN CD  NE2  sing N N 155 
GLN NE2 HE21 sing N N 156 
GLN NE2 HE22 sing N N 157 
GLN OXT HXT  sing N N 158 
GLU N   CA   sing N N 159 
GLU N   H    sing N N 160 
GLU N   H2   sing N N 161 
GLU CA  C    sing N N 162 
GLU CA  CB   sing N N 163 
GLU CA  HA   sing N N 164 
GLU C   O    doub N N 165 
GLU C   OXT  sing N N 166 
GLU CB  CG   sing N N 167 
GLU CB  HB2  sing N N 168 
GLU CB  HB3  sing N N 169 
GLU CG  CD   sing N N 170 
GLU CG  HG2  sing N N 171 
GLU CG  HG3  sing N N 172 
GLU CD  OE1  doub N N 173 
GLU CD  OE2  sing N N 174 
GLU OE2 HE2  sing N N 175 
GLU OXT HXT  sing N N 176 
GLY N   CA   sing N N 177 
GLY N   H    sing N N 178 
GLY N   H2   sing N N 179 
GLY CA  C    sing N N 180 
GLY CA  HA2  sing N N 181 
GLY CA  HA3  sing N N 182 
GLY C   O    doub N N 183 
GLY C   OXT  sing N N 184 
GLY OXT HXT  sing N N 185 
HIS N   CA   sing N N 186 
HIS N   H    sing N N 187 
HIS N   H2   sing N N 188 
HIS CA  C    sing N N 189 
HIS CA  CB   sing N N 190 
HIS CA  HA   sing N N 191 
HIS C   O    doub N N 192 
HIS C   OXT  sing N N 193 
HIS CB  CG   sing N N 194 
HIS CB  HB2  sing N N 195 
HIS CB  HB3  sing N N 196 
HIS CG  ND1  sing Y N 197 
HIS CG  CD2  doub Y N 198 
HIS ND1 CE1  doub Y N 199 
HIS ND1 HD1  sing N N 200 
HIS CD2 NE2  sing Y N 201 
HIS CD2 HD2  sing N N 202 
HIS CE1 NE2  sing Y N 203 
HIS CE1 HE1  sing N N 204 
HIS NE2 HE2  sing N N 205 
HIS OXT HXT  sing N N 206 
HOH O   H1   sing N N 207 
HOH O   H2   sing N N 208 
ILE N   CA   sing N N 209 
ILE N   H    sing N N 210 
ILE N   H2   sing N N 211 
ILE CA  C    sing N N 212 
ILE CA  CB   sing N N 213 
ILE CA  HA   sing N N 214 
ILE C   O    doub N N 215 
ILE C   OXT  sing N N 216 
ILE CB  CG1  sing N N 217 
ILE CB  CG2  sing N N 218 
ILE CB  HB   sing N N 219 
ILE CG1 CD1  sing N N 220 
ILE CG1 HG12 sing N N 221 
ILE CG1 HG13 sing N N 222 
ILE CG2 HG21 sing N N 223 
ILE CG2 HG22 sing N N 224 
ILE CG2 HG23 sing N N 225 
ILE CD1 HD11 sing N N 226 
ILE CD1 HD12 sing N N 227 
ILE CD1 HD13 sing N N 228 
ILE OXT HXT  sing N N 229 
LEU N   CA   sing N N 230 
LEU N   H    sing N N 231 
LEU N   H2   sing N N 232 
LEU CA  C    sing N N 233 
LEU CA  CB   sing N N 234 
LEU CA  HA   sing N N 235 
LEU C   O    doub N N 236 
LEU C   OXT  sing N N 237 
LEU CB  CG   sing N N 238 
LEU CB  HB2  sing N N 239 
LEU CB  HB3  sing N N 240 
LEU CG  CD1  sing N N 241 
LEU CG  CD2  sing N N 242 
LEU CG  HG   sing N N 243 
LEU CD1 HD11 sing N N 244 
LEU CD1 HD12 sing N N 245 
LEU CD1 HD13 sing N N 246 
LEU CD2 HD21 sing N N 247 
LEU CD2 HD22 sing N N 248 
LEU CD2 HD23 sing N N 249 
LEU OXT HXT  sing N N 250 
LYS N   CA   sing N N 251 
LYS N   H    sing N N 252 
LYS N   H2   sing N N 253 
LYS CA  C    sing N N 254 
LYS CA  CB   sing N N 255 
LYS CA  HA   sing N N 256 
LYS C   O    doub N N 257 
LYS C   OXT  sing N N 258 
LYS CB  CG   sing N N 259 
LYS CB  HB2  sing N N 260 
LYS CB  HB3  sing N N 261 
LYS CG  CD   sing N N 262 
LYS CG  HG2  sing N N 263 
LYS CG  HG3  sing N N 264 
LYS CD  CE   sing N N 265 
LYS CD  HD2  sing N N 266 
LYS CD  HD3  sing N N 267 
LYS CE  NZ   sing N N 268 
LYS CE  HE2  sing N N 269 
LYS CE  HE3  sing N N 270 
LYS NZ  HZ1  sing N N 271 
LYS NZ  HZ2  sing N N 272 
LYS NZ  HZ3  sing N N 273 
LYS OXT HXT  sing N N 274 
MET N   CA   sing N N 275 
MET N   H    sing N N 276 
MET N   H2   sing N N 277 
MET CA  C    sing N N 278 
MET CA  CB   sing N N 279 
MET CA  HA   sing N N 280 
MET C   O    doub N N 281 
MET C   OXT  sing N N 282 
MET CB  CG   sing N N 283 
MET CB  HB2  sing N N 284 
MET CB  HB3  sing N N 285 
MET CG  SD   sing N N 286 
MET CG  HG2  sing N N 287 
MET CG  HG3  sing N N 288 
MET SD  CE   sing N N 289 
MET CE  HE1  sing N N 290 
MET CE  HE2  sing N N 291 
MET CE  HE3  sing N N 292 
MET OXT HXT  sing N N 293 
PHE N   CA   sing N N 294 
PHE N   H    sing N N 295 
PHE N   H2   sing N N 296 
PHE CA  C    sing N N 297 
PHE CA  CB   sing N N 298 
PHE CA  HA   sing N N 299 
PHE C   O    doub N N 300 
PHE C   OXT  sing N N 301 
PHE CB  CG   sing N N 302 
PHE CB  HB2  sing N N 303 
PHE CB  HB3  sing N N 304 
PHE CG  CD1  doub Y N 305 
PHE CG  CD2  sing Y N 306 
PHE CD1 CE1  sing Y N 307 
PHE CD1 HD1  sing N N 308 
PHE CD2 CE2  doub Y N 309 
PHE CD2 HD2  sing N N 310 
PHE CE1 CZ   doub Y N 311 
PHE CE1 HE1  sing N N 312 
PHE CE2 CZ   sing Y N 313 
PHE CE2 HE2  sing N N 314 
PHE CZ  HZ   sing N N 315 
PHE OXT HXT  sing N N 316 
PRO N   CA   sing N N 317 
PRO N   CD   sing N N 318 
PRO N   H    sing N N 319 
PRO CA  C    sing N N 320 
PRO CA  CB   sing N N 321 
PRO CA  HA   sing N N 322 
PRO C   O    doub N N 323 
PRO C   OXT  sing N N 324 
PRO CB  CG   sing N N 325 
PRO CB  HB2  sing N N 326 
PRO CB  HB3  sing N N 327 
PRO CG  CD   sing N N 328 
PRO CG  HG2  sing N N 329 
PRO CG  HG3  sing N N 330 
PRO CD  HD2  sing N N 331 
PRO CD  HD3  sing N N 332 
PRO OXT HXT  sing N N 333 
SER N   CA   sing N N 334 
SER N   H    sing N N 335 
SER N   H2   sing N N 336 
SER CA  C    sing N N 337 
SER CA  CB   sing N N 338 
SER CA  HA   sing N N 339 
SER C   O    doub N N 340 
SER C   OXT  sing N N 341 
SER CB  OG   sing N N 342 
SER CB  HB2  sing N N 343 
SER CB  HB3  sing N N 344 
SER OG  HG   sing N N 345 
SER OXT HXT  sing N N 346 
THR N   CA   sing N N 347 
THR N   H    sing N N 348 
THR N   H2   sing N N 349 
THR CA  C    sing N N 350 
THR CA  CB   sing N N 351 
THR CA  HA   sing N N 352 
THR C   O    doub N N 353 
THR C   OXT  sing N N 354 
THR CB  OG1  sing N N 355 
THR CB  CG2  sing N N 356 
THR CB  HB   sing N N 357 
THR OG1 HG1  sing N N 358 
THR CG2 HG21 sing N N 359 
THR CG2 HG22 sing N N 360 
THR CG2 HG23 sing N N 361 
THR OXT HXT  sing N N 362 
TRP N   CA   sing N N 363 
TRP N   H    sing N N 364 
TRP N   H2   sing N N 365 
TRP CA  C    sing N N 366 
TRP CA  CB   sing N N 367 
TRP CA  HA   sing N N 368 
TRP C   O    doub N N 369 
TRP C   OXT  sing N N 370 
TRP CB  CG   sing N N 371 
TRP CB  HB2  sing N N 372 
TRP CB  HB3  sing N N 373 
TRP CG  CD1  doub Y N 374 
TRP CG  CD2  sing Y N 375 
TRP CD1 NE1  sing Y N 376 
TRP CD1 HD1  sing N N 377 
TRP CD2 CE2  doub Y N 378 
TRP CD2 CE3  sing Y N 379 
TRP NE1 CE2  sing Y N 380 
TRP NE1 HE1  sing N N 381 
TRP CE2 CZ2  sing Y N 382 
TRP CE3 CZ3  doub Y N 383 
TRP CE3 HE3  sing N N 384 
TRP CZ2 CH2  doub Y N 385 
TRP CZ2 HZ2  sing N N 386 
TRP CZ3 CH2  sing Y N 387 
TRP CZ3 HZ3  sing N N 388 
TRP CH2 HH2  sing N N 389 
TRP OXT HXT  sing N N 390 
TYR N   CA   sing N N 391 
TYR N   H    sing N N 392 
TYR N   H2   sing N N 393 
TYR CA  C    sing N N 394 
TYR CA  CB   sing N N 395 
TYR CA  HA   sing N N 396 
TYR C   O    doub N N 397 
TYR C   OXT  sing N N 398 
TYR CB  CG   sing N N 399 
TYR CB  HB2  sing N N 400 
TYR CB  HB3  sing N N 401 
TYR CG  CD1  doub Y N 402 
TYR CG  CD2  sing Y N 403 
TYR CD1 CE1  sing Y N 404 
TYR CD1 HD1  sing N N 405 
TYR CD2 CE2  doub Y N 406 
TYR CD2 HD2  sing N N 407 
TYR CE1 CZ   doub Y N 408 
TYR CE1 HE1  sing N N 409 
TYR CE2 CZ   sing Y N 410 
TYR CE2 HE2  sing N N 411 
TYR CZ  OH   sing N N 412 
TYR OH  HH   sing N N 413 
TYR OXT HXT  sing N N 414 
VAL N   CA   sing N N 415 
VAL N   H    sing N N 416 
VAL N   H2   sing N N 417 
VAL CA  C    sing N N 418 
VAL CA  CB   sing N N 419 
VAL CA  HA   sing N N 420 
VAL C   O    doub N N 421 
VAL C   OXT  sing N N 422 
VAL CB  CG1  sing N N 423 
VAL CB  CG2  sing N N 424 
VAL CB  HB   sing N N 425 
VAL CG1 HG11 sing N N 426 
VAL CG1 HG12 sing N N 427 
VAL CG1 HG13 sing N N 428 
VAL CG2 HG21 sing N N 429 
VAL CG2 HG22 sing N N 430 
VAL CG2 HG23 sing N N 431 
VAL OXT HXT  sing N N 432 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        5EF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   5EF 
_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                    6YH7 
_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]   0.023931 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005776 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024409 
_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]   0.014435 
_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   ? 11.396  -0.600  7.370   1.00 91.26  ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.106  -0.022  7.857   1.00 69.82  ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.496   -0.912  8.962   1.00 39.80  ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.918   -2.079  9.035   1.00 37.02  ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 9.202   0.235   6.645   1.00 65.79  ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 8.317   1.426   6.799   1.00 66.91  ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 8.746   2.592   7.405   1.00 45.81  ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 7.035   1.640   6.433   1.00 50.86  ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 7.766   3.472   7.405   1.00 67.00  ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 6.704   2.912   6.813   1.00 70.09  ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.520   -0.425  9.780   1.00 25.40  ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 8.059   -1.303  10.840  1.00 18.05  ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 7.025   -2.194  10.160  1.00 16.97  ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.461   -1.799  9.124   1.00 20.13  ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.410   -0.614  12.058  1.00 18.61  ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 6.152   0.127   11.744  1.00 16.72  ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 6.078   1.457   11.405  1.00 20.20  ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.820   -0.398  11.711  1.00 15.18  ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.774   1.793   11.150  1.00 18.68  ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.981   0.695   11.401  1.00 15.62  ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 4.242   -1.650  12.035  1.00 15.43  ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.596   0.540   11.308  1.00 16.78  ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.874   -1.783  11.970  1.00 14.11  ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 2.065   -0.693  11.604  1.00 15.26  ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.845   -3.402  10.709  1.00 16.54  ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.882   -4.354  10.171  1.00 16.29  ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.527   -5.393  11.221  1.00 14.74  ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.511   -5.122  12.404  1.00 14.58  ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 5.170   -6.590  10.744  1.00 15.37  ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.742   -7.693  11.566  1.00 15.96  ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.619   -8.921  11.366  1.00 19.11  ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.351   -9.957  11.976  1.00 25.74  ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.281   -8.022  11.274  1.00 16.00  ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.343   -6.943  11.751  1.00 13.83  ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.971   -6.900  13.100  1.00 12.38  ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.890   -5.947  10.905  1.00 14.25  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 1.080   -5.937  13.535  1.00 12.59  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 1.006   -4.990  11.329  1.00 13.69  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.616   -4.983  12.655  1.00 12.94  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.268  -4.024  13.042  1.00 14.24  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.708   -8.774  10.598  1.00 17.61  ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.590   -9.915  10.356  1.00 22.84  ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.634   -10.127 11.465  1.00 20.41  ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.743   -9.378  12.432  1.00 19.04  ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.430   -11.180 11.296  1.00 20.88  ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.469  -11.528 12.250  1.00 22.02  ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.468  -10.391 12.474  1.00 19.64  ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.958  -10.213 13.584  1.00 20.01  ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.260  -12.744 11.718  1.00 27.25  ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.493  -13.094 12.538  1.00 29.21  ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? 11.761  -9.642  11.407  1.00 19.19  ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? 12.830  -8.675  11.544  1.00 20.93  ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? 12.360  -7.268  11.848  1.00 18.62  ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? 13.205  -6.399  12.123  1.00 20.35  ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? 13.801  -8.720  10.362  1.00 25.20  ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? 14.518  -10.043 10.333  1.00 24.24  ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? 15.549  -10.385 11.192  1.00 29.71  ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? 14.244  -11.100 9.573   1.00 28.91  ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? 15.931  -11.626 10.926  1.00 25.82  ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? 15.092  -12.082 9.913   1.00 23.07  ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? 11.042  -7.005  11.740  1.00 16.48  ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? 10.560  -5.630  11.928  1.00 14.58  ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? 9.258   -5.608  12.713  1.00 14.09  ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? 8.614   -4.563  12.715  1.00 14.75  ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? 10.386  -4.901  10.594  1.00 17.33  ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? 9.345   -5.537  9.699   1.00 19.18  ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? 8.717   -6.553  10.063  1.00 21.22  ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? 9.108   -4.938  8.545   1.00 25.05  ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? 8.887   -6.735  13.359  1.00 14.57  ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? 7.588   -6.869  14.000  1.00 14.95  ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? 7.606   -6.348  15.406  1.00 12.27  ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? 8.527   -5.631  15.841  1.00 12.63  ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? 6.522   -6.665  16.145  1.00 12.32  ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? 6.304   -6.115  17.454  1.00 11.39  ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? 7.467   -6.129  18.428  1.00 11.26  ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? 7.546   -5.202  19.224  1.00 12.43  ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? 5.116   -6.954  17.967  1.00 13.10  ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? 4.311   -7.186  16.722  1.00 13.66  ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? 5.366   -7.422  15.645  1.00 13.61  ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? 8.309   -7.160  18.376  1.00 12.75  ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? 9.427   -7.215  19.330  1.00 13.93  ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? 10.519  -6.193  19.007  1.00 12.49  ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? 11.425  -5.978  19.803  1.00 14.33  ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? 10.066  -8.630  19.331  1.00 19.01  ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? 9.080   -9.738  19.738  1.00 24.17  ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? 8.234   -9.374  20.953  1.00 37.11  ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? 8.843   -8.942  21.934  1.00 38.17  ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? 6.949   -9.435  20.891  1.00 35.65  ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? 10.474  -5.608  17.807  1.00 11.96  ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? 11.442  -4.613  17.367  1.00 12.07  ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? 10.978  -3.178  17.546  1.00 11.14  ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? 11.764  -2.239  17.478  1.00 12.84  ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? 11.806  -4.755  15.887  1.00 12.74  ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? 12.548  -5.984  15.575  1.00 14.77  ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? 13.937  -6.026  15.634  1.00 15.13  ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? 12.106  -7.221  15.266  1.00 14.82  ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? 14.313  -7.240  15.304  1.00 19.02  ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? 13.241  -8.009  15.060  1.00 17.23  ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? 9.660   -2.959  17.714  1.00 11.18  ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? 9.103   -1.621  17.634  1.00 11.39  ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? 9.643   -0.671  18.678  1.00 11.06  ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? 9.741   0.530   18.381  1.00 11.51  ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? 7.541   -1.685  17.768  1.00 10.74  ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? 6.902   -2.374  16.615  1.00 10.42  ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? 7.418   -2.764  15.418  1.00 11.41  ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? 5.503   -2.739  16.580  1.00 10.32  ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? 6.448   -3.381  14.654  1.00 12.05  ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? 5.267   -3.346  15.335  1.00 10.92  ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? 4.451   -2.585  17.497  1.00 10.05  ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? 3.999   -3.829  14.951  1.00 11.36  ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? 3.211   -3.055  17.108  1.00 10.74  ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? 2.995   -3.635  15.859  1.00 11.70  ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? 10.024  -1.206  19.844  1.00 11.06  ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? 10.503  -0.314  20.897  1.00 11.76  ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? 11.741  0.470   20.511  1.00 12.36  ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? 12.016  1.508   21.094  1.00 12.89  ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? 10.772  -1.108  22.175  1.00 12.15  ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? 11.999  -1.943  22.079  1.00 13.52  ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? 13.199  -1.527  22.650  1.00 13.77  ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? 12.196  -3.130  21.503  1.00 13.54  ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? 14.081  -2.457  22.392  1.00 14.89  ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? 13.542  -3.445  21.668  1.00 14.89  ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? 12.509  -0.020  19.521  1.00 12.20  ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? 13.708  0.735   19.185  1.00 13.39  ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? 13.389  2.076   18.552  1.00 14.93  ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? 14.031  3.061   18.860  1.00 21.20  ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? 14.580  -0.128  18.299  1.00 13.38  ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? 15.209  -1.342  18.970  1.00 14.47  ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? 15.939  -2.263  18.077  1.00 15.44  ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? 15.041  -3.261  17.402  1.00 14.77  ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? 15.691  -4.056  16.345  1.00 14.64  ? 18  LYS A NZ  1 
ATOM   132  N  N   A ASP A 1 19  ? 12.383  2.147   17.684  0.50 13.20  ? 19  ASP A N   1 
ATOM   133  N  N   B ASP A 1 19  ? 12.394  2.122   17.678  0.50 13.33  ? 19  ASP A N   1 
ATOM   134  C  CA  A ASP A 1 19  ? 11.987  3.416   17.099  0.50 14.20  ? 19  ASP A CA  1 
ATOM   135  C  CA  B ASP A 1 19  ? 11.952  3.365   17.082  0.50 13.49  ? 19  ASP A CA  1 
ATOM   136  C  C   A ASP A 1 19  ? 10.886  4.083   17.899  0.50 13.26  ? 19  ASP A C   1 
ATOM   137  C  C   B ASP A 1 19  ? 10.984  4.088   18.004  0.50 13.52  ? 19  ASP A C   1 
ATOM   138  O  O   A ASP A 1 19  ? 10.672  5.270   17.719  0.50 13.26  ? 19  ASP A O   1 
ATOM   139  O  O   B ASP A 1 19  ? 10.993  5.306   18.068  0.50 14.99  ? 19  ASP A O   1 
ATOM   140  C  CB  A ASP A 1 19  ? 11.492  3.254   15.673  0.50 17.29  ? 19  ASP A CB  1 
ATOM   141  C  CB  B ASP A 1 19  ? 11.357  3.092   15.714  0.50 15.60  ? 19  ASP A CB  1 
ATOM   142  C  CG  A ASP A 1 19  ? 12.633  2.862   14.768  0.50 20.88  ? 19  ASP A CG  1 
ATOM   143  C  CG  B ASP A 1 19  ? 12.421  3.184   14.635  0.50 18.10  ? 19  ASP A CG  1 
ATOM   144  O  OD1 A ASP A 1 19  ? 13.460  3.782   14.467  0.50 17.75  ? 19  ASP A OD1 1 
ATOM   145  O  OD1 B ASP A 1 19  ? 13.627  3.435   14.983  0.50 24.55  ? 19  ASP A OD1 1 
ATOM   146  O  OD2 A ASP A 1 19  ? 12.715  1.636   14.443  0.50 25.61  ? 19  ASP A OD2 1 
ATOM   147  O  OD2 B ASP A 1 19  ? 12.066  2.962   13.479  0.50 22.57  ? 19  ASP A OD2 1 
ATOM   148  N  N   . PHE A 1 20  ? 10.200  3.314   18.773  1.00 12.51  ? 20  PHE A N   1 
ATOM   149  C  CA  . PHE A 1 20  ? 9.062   3.864   19.516  1.00 12.10  ? 20  PHE A CA  1 
ATOM   150  C  C   . PHE A 1 20  ? 9.161   3.375   20.933  1.00 11.36  ? 20  PHE A C   1 
ATOM   151  O  O   . PHE A 1 20  ? 8.537   2.363   21.322  1.00 11.92  ? 20  PHE A O   1 
ATOM   152  C  CB  . PHE A 1 20  ? 7.715   3.441   18.868  1.00 13.27  ? 20  PHE A CB  1 
ATOM   153  C  CG  . PHE A 1 20  ? 7.646   3.878   17.436  1.00 14.40  ? 20  PHE A CG  1 
ATOM   154  C  CD1 . PHE A 1 20  ? 7.307   5.178   17.102  1.00 16.84  ? 20  PHE A CD1 1 
ATOM   155  C  CD2 . PHE A 1 20  ? 7.991   2.996   16.422  1.00 16.76  ? 20  PHE A CD2 1 
ATOM   156  C  CE1 . PHE A 1 20  ? 7.315   5.561   15.772  1.00 20.25  ? 20  PHE A CE1 1 
ATOM   157  C  CE2 . PHE A 1 20  ? 8.017   3.370   15.079  1.00 19.13  ? 20  PHE A CE2 1 
ATOM   158  C  CZ  . PHE A 1 20  ? 7.662   4.662   14.776  1.00 21.21  ? 20  PHE A CZ  1 
ATOM   159  N  N   . PRO A 1 21  ? 10.050  3.964   21.758  1.00 13.03  ? 21  PRO A N   1 
ATOM   160  C  CA  . PRO A 1 21  ? 10.290  3.435   23.086  1.00 13.79  ? 21  PRO A CA  1 
ATOM   161  C  C   . PRO A 1 21  ? 9.088   3.313   24.000  1.00 12.55  ? 21  PRO A C   1 
ATOM   162  O  O   . PRO A 1 21  ? 9.137   2.570   24.993  1.00 13.64  ? 21  PRO A O   1 
ATOM   163  C  CB  . PRO A 1 21  ? 11.355  4.354   23.735  1.00 17.38  ? 21  PRO A CB  1 
ATOM   164  C  CG  . PRO A 1 21  ? 11.530  5.424   22.756  1.00 25.11  ? 21  PRO A CG  1 
ATOM   165  C  CD  . PRO A 1 21  ? 10.992  5.047   21.407  1.00 15.53  ? 21  PRO A CD  1 
ATOM   166  N  N   A ILE A 1 22  ? 8.019   4.067   23.699  0.50 11.85  ? 22  ILE A N   1 
ATOM   167  N  N   B ILE A 1 22  ? 8.013   4.066   23.706  0.50 12.89  ? 22  ILE A N   1 
ATOM   168  C  CA  A ILE A 1 22  ? 6.775   3.936   24.447  0.50 10.79  ? 22  ILE A CA  1 
ATOM   169  C  CA  B ILE A 1 22  ? 6.775   3.935   24.468  0.50 13.12  ? 22  ILE A CA  1 
ATOM   170  C  C   A ILE A 1 22  ? 6.192   2.519   24.332  0.50 11.04  ? 22  ILE A C   1 
ATOM   171  C  C   B ILE A 1 22  ? 6.197   2.516   24.339  0.50 11.73  ? 22  ILE A C   1 
ATOM   172  O  O   A ILE A 1 22  ? 5.303   2.159   25.107  0.50 11.83  ? 22  ILE A O   1 
ATOM   173  O  O   B ILE A 1 22  ? 5.304   2.156   25.105  0.50 12.08  ? 22  ILE A O   1 
ATOM   174  C  CB  A ILE A 1 22  ? 5.763   5.008   24.006  0.50 11.38  ? 22  ILE A CB  1 
ATOM   175  C  CB  B ILE A 1 22  ? 5.747   5.001   24.041  0.50 13.76  ? 22  ILE A CB  1 
ATOM   176  C  CG1 A ILE A 1 22  ? 4.704   5.288   25.066  0.50 10.71  ? 22  ILE A CG1 1 
ATOM   177  C  CG1 B ILE A 1 22  ? 4.676   5.239   25.110  0.50 17.37  ? 22  ILE A CG1 1 
ATOM   178  C  CG2 A ILE A 1 22  ? 5.134   4.653   22.673  0.50 11.26  ? 22  ILE A CG2 1 
ATOM   179  C  CG2 B ILE A 1 22  ? 5.136   4.639   22.698  0.50 14.58  ? 22  ILE A CG2 1 
ATOM   180  C  CD1 A ILE A 1 22  ? 3.846   6.486   24.747  0.50 14.20  ? 22  ILE A CD1 1 
ATOM   181  C  CD1 B ILE A 1 22  ? 5.213   5.762   26.428  0.50 16.78  ? 22  ILE A CD1 1 
ATOM   182  N  N   . ALA A 1 23  ? 6.728   1.691   23.430  1.00 11.14  ? 23  ALA A N   1 
ATOM   183  C  CA  . ALA A 1 23  ? 6.290   0.312   23.305  1.00 11.39  ? 23  ALA A CA  1 
ATOM   184  C  C   . ALA A 1 23  ? 6.417   -0.416  24.617  1.00 11.73  ? 23  ALA A C   1 
ATOM   185  O  O   . ALA A 1 23  ? 5.718   -1.423  24.784  1.00 12.94  ? 23  ALA A O   1 
ATOM   186  C  CB  . ALA A 1 23  ? 7.103   -0.418  22.259  1.00 12.16  ? 23  ALA A CB  1 
ATOM   187  N  N   . LYS A 1 24  ? 7.351   0.057   25.487  1.00 12.85  ? 24  LYS A N   1 
ATOM   188  C  CA  . LYS A 1 24  ? 7.519   -0.578  26.779  1.00 13.88  ? 24  LYS A CA  1 
ATOM   189  C  C   . LYS A 1 24  ? 6.912   0.275   27.895  1.00 14.40  ? 24  LYS A C   1 
ATOM   190  O  O   . LYS A 1 24  ? 7.308   0.160   29.068  1.00 16.00  ? 24  LYS A O   1 
ATOM   191  C  CB  . LYS A 1 24  ? 9.010   -0.813  27.048  1.00 15.88  ? 24  LYS A CB  1 
ATOM   192  C  CG  . LYS A 1 24  ? 9.667   -1.831  26.124  1.00 16.43  ? 24  LYS A CG  1 
ATOM   193  C  CD  . LYS A 1 24  ? 11.114  -2.005  26.480  1.00 21.83  ? 24  LYS A CD  1 
ATOM   194  C  CE  . LYS A 1 24  ? 11.781  -3.018  25.572  1.00 22.04  ? 24  LYS A CE  1 
ATOM   195  N  NZ  . LYS A 1 24  ? 11.333  -4.389  25.934  1.00 29.03  ? 24  LYS A NZ  1 
ATOM   196  N  N   . GLY A 1 25  ? 5.903   1.084   27.544  1.00 13.24  ? 25  GLY A N   1 
ATOM   197  C  CA  . GLY A 1 25  ? 5.275   2.021   28.461  1.00 15.28  ? 25  GLY A CA  1 
ATOM   198  C  C   . GLY A 1 25  ? 4.340   1.351   29.456  1.00 12.88  ? 25  GLY A C   1 
ATOM   199  O  O   . GLY A 1 25  ? 4.172   0.137   29.516  1.00 14.54  ? 25  GLY A O   1 
ATOM   200  N  N   . GLU A 1 26  ? 3.685   2.222   30.198  1.00 14.04  ? 26  GLU A N   1 
ATOM   201  C  CA  . GLU A 1 26  ? 2.846   1.788   31.288  1.00 14.77  ? 26  GLU A CA  1 
ATOM   202  C  C   . GLU A 1 26  ? 1.387   1.577   30.879  1.00 13.39  ? 26  GLU A C   1 
ATOM   203  O  O   . GLU A 1 26  ? 0.621   1.063   31.702  1.00 14.77  ? 26  GLU A O   1 
ATOM   204  C  CB  . GLU A 1 26  ? 2.875   2.862   32.388  1.00 19.45  ? 26  GLU A CB  1 
ATOM   205  C  CG  . GLU A 1 26  ? 4.244   3.147   32.952  1.00 22.96  ? 26  GLU A CG  1 
ATOM   206  C  CD  . GLU A 1 26  ? 4.926   1.895   33.525  1.00 31.48  ? 26  GLU A CD  1 
ATOM   207  O  OE1 . GLU A 1 26  ? 4.317   1.182   34.350  1.00 39.05  ? 26  GLU A OE1 1 
ATOM   208  O  OE2 . GLU A 1 26  ? 6.076   1.607   33.113  1.00 39.14  ? 26  GLU A OE2 1 
ATOM   209  N  N   . ARG A 1 27  ? 1.016   1.906   29.647  1.00 10.81  ? 27  ARG A N   1 
ATOM   210  C  CA  . ARG A 1 27  ? -0.397  1.693   29.284  1.00 9.80   ? 27  ARG A CA  1 
ATOM   211  C  C   . ARG A 1 27  ? -0.467  1.255   27.829  1.00 9.58   ? 27  ARG A C   1 
ATOM   212  O  O   . ARG A 1 27  ? -1.213  1.818   27.037  1.00 10.44  ? 27  ARG A O   1 
ATOM   213  C  CB  . ARG A 1 27  ? -1.295  2.895   29.584  1.00 14.02  ? 27  ARG A CB  1 
ATOM   214  C  CG  . ARG A 1 27  ? -0.913  4.256   29.042  1.00 17.39  ? 27  ARG A CG  1 
ATOM   215  C  CD  . ARG A 1 27  ? -1.927  5.430   29.185  1.00 22.98  ? 27  ARG A CD  1 
ATOM   216  N  NE  . ARG A 1 27  ? -3.092  5.345   28.270  1.00 17.49  ? 27  ARG A NE  1 
ATOM   217  C  CZ  . ARG A 1 27  ? -4.000  6.302   28.117  1.00 15.64  ? 27  ARG A CZ  1 
ATOM   218  N  NH1 . ARG A 1 27  ? -3.900  7.426   28.806  1.00 18.00  ? 27  ARG A NH1 1 
ATOM   219  N  NH2 . ARG A 1 27  ? -5.004  6.133   27.275  1.00 17.35  ? 27  ARG A NH2 1 
ATOM   220  N  N   . GLN A 1 28  ? 0.244   0.173   27.518  1.00 8.99   ? 28  GLN A N   1 
ATOM   221  C  CA  . GLN A 1 28  ? 0.263   -0.333  26.155  1.00 8.86   ? 28  GLN A CA  1 
ATOM   222  C  C   . GLN A 1 28  ? -0.900  -1.322  25.906  1.00 8.17   ? 28  GLN A C   1 
ATOM   223  O  O   . GLN A 1 28  ? -1.386  -1.987  26.791  1.00 9.81   ? 28  GLN A O   1 
ATOM   224  C  CB  . GLN A 1 28  ? 1.630   -1.001  25.896  1.00 9.81   ? 28  GLN A CB  1 
ATOM   225  C  CG  . GLN A 1 28  ? 2.738   0.055   25.798  1.00 9.91   ? 28  GLN A CG  1 
ATOM   226  C  CD  . GLN A 1 28  ? 2.613   0.831   24.517  1.00 9.25   ? 28  GLN A CD  1 
ATOM   227  O  OE1 . GLN A 1 28  ? 2.783   0.312   23.426  1.00 9.97   ? 28  GLN A OE1 1 
ATOM   228  N  NE2 . GLN A 1 28  ? 2.235   2.123   24.643  1.00 9.86   ? 28  GLN A NE2 1 
ATOM   229  N  N   . SER A 1 29  ? -1.250  -1.396  24.639  1.00 8.32   ? 29  SER A N   1 
ATOM   230  C  CA  . SER A 1 29  ? -2.331  -2.263  24.162  1.00 7.96   ? 29  SER A CA  1 
ATOM   231  C  C   . SER A 1 29  ? -1.801  -3.121  23.032  1.00 8.10   ? 29  SER A C   1 
ATOM   232  O  O   . SER A 1 29  ? -0.839  -2.788  22.341  1.00 9.12   ? 29  SER A O   1 
ATOM   233  C  CB  . SER A 1 29  ? -3.451  -1.375  23.638  1.00 8.87   ? 29  SER A CB  1 
ATOM   234  O  OG  . SER A 1 29  ? -4.050  -0.675  24.702  1.00 8.98   ? 29  SER A OG  1 
ATOM   235  N  N   . PRO A 1 30  ? -2.455  -4.257  22.756  1.00 8.10   ? 30  PRO A N   1 
ATOM   236  C  CA  . PRO A 1 30  ? -3.645  -4.778  23.476  1.00 8.69   ? 30  PRO A CA  1 
ATOM   237  C  C   . PRO A 1 30  ? -3.205  -5.454  24.785  1.00 8.18   ? 30  PRO A C   1 
ATOM   238  O  O   . PRO A 1 30  ? -2.024  -5.502  25.114  1.00 9.14   ? 30  PRO A O   1 
ATOM   239  C  CB  . PRO A 1 30  ? -4.156  -5.811  22.472  1.00 8.59   ? 30  PRO A CB  1 
ATOM   240  C  CG  . PRO A 1 30  ? -2.877  -6.380  21.887  1.00 9.02   ? 30  PRO A CG  1 
ATOM   241  C  CD  . PRO A 1 30  ? -1.981  -5.154  21.710  1.00 8.80   ? 30  PRO A CD  1 
ATOM   242  N  N   . VAL A 1 31  ? -4.186  -6.010  25.461  1.00 8.71   ? 31  VAL A N   1 
ATOM   243  C  CA  . VAL A 1 31  ? -4.014  -6.754  26.687  1.00 9.10   ? 31  VAL A CA  1 
ATOM   244  C  C   . VAL A 1 31  ? -4.888  -7.988  26.648  1.00 9.57   ? 31  VAL A C   1 
ATOM   245  O  O   . VAL A 1 31  ? -5.864  -8.056  25.889  1.00 10.11  ? 31  VAL A O   1 
ATOM   246  C  CB  . VAL A 1 31  ? -4.339  -5.935  27.951  1.00 9.88   ? 31  VAL A CB  1 
ATOM   247  C  CG1 . VAL A 1 31  ? -3.399  -4.736  28.066  1.00 11.44  ? 31  VAL A CG1 1 
ATOM   248  C  CG2 . VAL A 1 31  ? -5.817  -5.483  27.966  1.00 10.65  ? 31  VAL A CG2 1 
ATOM   249  N  N   . ASP A 1 32  ? -4.532  -8.958  27.501  1.00 9.43   ? 32  ASP A N   1 
ATOM   250  C  CA  . ASP A 1 32  ? -5.479  -10.025 27.800  1.00 10.12  ? 32  ASP A CA  1 
ATOM   251  C  C   . ASP A 1 32  ? -6.518  -9.510  28.781  1.00 10.02  ? 32  ASP A C   1 
ATOM   252  O  O   . ASP A 1 32  ? -6.206  -8.908  29.797  1.00 12.01  ? 32  ASP A O   1 
ATOM   253  C  CB  . ASP A 1 32  ? -4.746  -11.200 28.432  1.00 11.77  ? 32  ASP A CB  1 
ATOM   254  C  CG  . ASP A 1 32  ? -5.680  -12.352 28.719  1.00 11.91  ? 32  ASP A CG  1 
ATOM   255  O  OD1 . ASP A 1 32  ? -6.389  -12.808 27.791  1.00 11.50  ? 32  ASP A OD1 1 
ATOM   256  O  OD2 . ASP A 1 32  ? -5.740  -12.796 29.913  1.00 14.80  ? 32  ASP A OD2 1 
ATOM   257  N  N   . ILE A 1 33  ? -7.771  -9.805  28.455  1.00 10.20  ? 33  ILE A N   1 
ATOM   258  C  CA  . ILE A 1 33  ? -8.885  -9.465  29.319  1.00 10.80  ? 33  ILE A CA  1 
ATOM   259  C  C   . ILE A 1 33  ? -9.209  -10.674 30.175  1.00 11.65  ? 33  ILE A C   1 
ATOM   260  O  O   . ILE A 1 33  ? -9.759  -11.663 29.677  1.00 13.31  ? 33  ILE A O   1 
ATOM   261  C  CB  . ILE A 1 33  ? -10.087 -9.013  28.473  1.00 11.03  ? 33  ILE A CB  1 
ATOM   262  C  CG1 . ILE A 1 33  ? -9.699  -7.805  27.612  1.00 11.52  ? 33  ILE A CG1 1 
ATOM   263  C  CG2 . ILE A 1 33  ? -11.289 -8.751  29.397  1.00 13.90  ? 33  ILE A CG2 1 
ATOM   264  C  CD1 . ILE A 1 33  ? -10.737 -7.494  26.551  1.00 12.79  ? 33  ILE A CD1 1 
ATOM   265  N  N   A ASP A 1 34  ? -8.803  -10.626 31.442  0.50 12.98  ? 34  ASP A N   1 
ATOM   266  N  N   B ASP A 1 34  ? -8.852  -10.585 31.467  0.50 12.21  ? 34  ASP A N   1 
ATOM   267  C  CA  A ASP A 1 34  ? -9.121  -11.704 32.347  0.50 14.23  ? 34  ASP A CA  1 
ATOM   268  C  CA  B ASP A 1 34  ? -9.167  -11.599 32.451  0.50 12.59  ? 34  ASP A CA  1 
ATOM   269  C  C   A ASP A 1 34  ? -10.508 -11.417 32.887  0.50 13.54  ? 34  ASP A C   1 
ATOM   270  C  C   B ASP A 1 34  ? -10.590 -11.333 32.881  0.50 13.04  ? 34  ASP A C   1 
ATOM   271  O  O   A ASP A 1 34  ? -10.661 -10.522 33.716  0.50 15.61  ? 34  ASP A O   1 
ATOM   272  O  O   B ASP A 1 34  ? -10.869 -10.371 33.598  0.50 14.91  ? 34  ASP A O   1 
ATOM   273  C  CB  A ASP A 1 34  ? -8.061  -11.746 33.449  0.50 16.45  ? 34  ASP A CB  1 
ATOM   274  C  CB  B ASP A 1 34  ? -8.126  -11.577 33.581  0.50 14.90  ? 34  ASP A CB  1 
ATOM   275  C  CG  A ASP A 1 34  ? -8.228  -12.994 34.285  0.50 19.38  ? 34  ASP A CG  1 
ATOM   276  C  CG  B ASP A 1 34  ? -8.387  -12.653 34.622  0.50 13.39  ? 34  ASP A CG  1 
ATOM   277  O  OD1 A ASP A 1 34  ? -7.679  -14.025 33.869  0.50 23.36  ? 34  ASP A OD1 1 
ATOM   278  O  OD1 B ASP A 1 34  ? -9.532  -13.074 34.756  0.50 15.04  ? 34  ASP A OD1 1 
ATOM   279  O  OD2 A ASP A 1 34  ? -8.885  -12.929 35.327  0.50 21.01  ? 34  ASP A OD2 1 
ATOM   280  O  OD2 B ASP A 1 34  ? -7.423  -13.089 35.283  0.50 19.55  ? 34  ASP A OD2 1 
ATOM   281  N  N   . THR A 1 35  ? -11.501 -12.185 32.428  1.00 15.19  ? 35  THR A N   1 
ATOM   282  C  CA  . THR A 1 35  ? -12.893 -11.854 32.649  1.00 16.31  ? 35  THR A CA  1 
ATOM   283  C  C   . THR A 1 35  ? -13.274 -11.965 34.096  1.00 17.22  ? 35  THR A C   1 
ATOM   284  O  O   . THR A 1 35  ? -14.238 -11.322 34.518  1.00 18.35  ? 35  THR A O   1 
ATOM   285  C  CB  . THR A 1 35  ? -13.816 -12.741 31.831  1.00 17.96  ? 35  THR A CB  1 
ATOM   286  O  OG1 . THR A 1 35  ? -13.697 -14.079 32.286  1.00 17.85  ? 35  THR A OG1 1 
ATOM   287  C  CG2 . THR A 1 35  ? -13.551 -12.635 30.361  1.00 18.78  ? 35  THR A CG2 1 
ATOM   288  N  N   . HIS A 1 36  ? -12.554 -12.825 34.831  1.00 19.04  ? 36  HIS A N   1 
ATOM   289  C  CA  . HIS A 1 36  ? -12.889 -13.037 36.193  1.00 20.64  ? 36  HIS A CA  1 
ATOM   290  C  C   . HIS A 1 36  ? -12.426 -11.871 37.035  1.00 21.93  ? 36  HIS A C   1 
ATOM   291  O  O   . HIS A 1 36  ? -13.166 -11.580 37.989  1.00 25.87  ? 36  HIS A O   1 
ATOM   292  C  CB  . HIS A 1 36  ? -12.368 -14.410 36.619  1.00 21.34  ? 36  HIS A CB  1 
ATOM   293  C  CG  . HIS A 1 36  ? -13.188 -15.542 36.045  1.00 26.38  ? 36  HIS A CG  1 
ATOM   294  N  ND1 . HIS A 1 36  ? -14.527 -15.708 36.341  1.00 30.45  ? 36  HIS A ND1 1 
ATOM   295  C  CD2 . HIS A 1 36  ? -12.858 -16.547 35.206  1.00 30.57  ? 36  HIS A CD2 1 
ATOM   296  C  CE1 . HIS A 1 36  ? -14.988 -16.768 35.708  1.00 29.60  ? 36  HIS A CE1 1 
ATOM   297  N  NE2 . HIS A 1 36  ? -13.982 -17.301 35.004  1.00 37.52  ? 36  HIS A NE2 1 
ATOM   298  N  N   . THR A 1 37  ? -11.338 -11.180 36.639  1.00 21.26  ? 37  THR A N   1 
ATOM   299  C  CA  . THR A 1 37  ? -10.672 -10.094 37.360  1.00 20.98  ? 37  THR A CA  1 
ATOM   300  C  C   . THR A 1 37  ? -11.273 -8.731  36.980  1.00 17.84  ? 37  THR A C   1 
ATOM   301  O  O   . THR A 1 37  ? -11.188 -7.806  37.741  1.00 23.81  ? 37  THR A O   1 
ATOM   302  C  CB  . THR A 1 37  ? -9.153  -10.173 37.066  1.00 27.89  ? 37  THR A CB  1 
ATOM   303  O  OG1 . THR A 1 37  ? -8.795  -11.355 37.754  1.00 38.22  ? 37  THR A OG1 1 
ATOM   304  C  CG2 . THR A 1 37  ? -8.348  -9.094  37.751  1.00 35.23  ? 37  THR A CG2 1 
ATOM   305  N  N   . ALA A 1 38  ? -11.924 -8.657  35.835  1.00 16.08  ? 38  ALA A N   1 
ATOM   306  C  CA  . ALA A 1 38  ? -12.523 -7.398  35.401  1.00 15.97  ? 38  ALA A CA  1 
ATOM   307  C  C   . ALA A 1 38  ? -13.601 -7.014  36.400  1.00 19.61  ? 38  ALA A C   1 
ATOM   308  O  O   . ALA A 1 38  ? -14.278 -7.853  36.944  1.00 26.82  ? 38  ALA A O   1 
ATOM   309  C  CB  . ALA A 1 38  ? -12.993 -7.547  33.968  1.00 16.46  ? 38  ALA A CB  1 
ATOM   310  N  N   . LYS A 1 39  ? -13.630 -5.731  36.788  1.00 17.48  ? 39  LYS A N   1 
ATOM   311  C  CA  . LYS A 1 39  ? -14.532 -5.239  37.814  1.00 20.83  ? 39  LYS A CA  1 
ATOM   312  C  C   . LYS A 1 39  ? -15.798 -4.714  37.151  1.00 16.92  ? 39  LYS A C   1 
ATOM   313  O  O   . LYS A 1 39  ? -15.707 -3.770  36.367  1.00 15.20  ? 39  LYS A O   1 
ATOM   314  C  CB  . LYS A 1 39  ? -13.852 -4.113  38.609  1.00 25.28  ? 39  LYS A CB  1 
ATOM   315  C  CG  . LYS A 1 39  ? -14.723 -3.268  39.503  1.00 28.47  ? 39  LYS A CG  1 
ATOM   316  C  CD  . LYS A 1 39  ? -14.885 -3.959  40.854  1.00 24.57  ? 39  LYS A CD  1 
ATOM   317  C  CE  . LYS A 1 39  ? -15.635 -3.085  41.822  1.00 28.27  ? 39  LYS A CE  1 
ATOM   318  N  NZ  . LYS A 1 39  ? -15.900 -3.838  43.071  1.00 32.13  ? 39  LYS A NZ  1 
ATOM   319  N  N   . TYR A 1 40  ? -16.944 -5.265  37.511  1.00 17.10  ? 40  TYR A N   1 
ATOM   320  C  CA  . TYR A 1 40  ? -18.209 -4.714  37.047  1.00 16.58  ? 40  TYR A CA  1 
ATOM   321  C  C   . TYR A 1 40  ? -18.369 -3.327  37.641  1.00 15.27  ? 40  TYR A C   1 
ATOM   322  O  O   . TYR A 1 40  ? -18.227 -3.185  38.861  1.00 19.09  ? 40  TYR A O   1 
ATOM   323  C  CB  . TYR A 1 40  ? -19.362 -5.627  37.460  1.00 19.37  ? 40  TYR A CB  1 
ATOM   324  C  CG  . TYR A 1 40  ? -20.690 -4.938  37.299  1.00 19.36  ? 40  TYR A CG  1 
ATOM   325  C  CD1 . TYR A 1 40  ? -21.124 -4.459  36.057  1.00 20.00  ? 40  TYR A CD1 1 
ATOM   326  C  CD2 . TYR A 1 40  ? -21.540 -4.802  38.390  1.00 26.61  ? 40  TYR A CD2 1 
ATOM   327  C  CE1 . TYR A 1 40  ? -22.368 -3.870  35.929  1.00 21.06  ? 40  TYR A CE1 1 
ATOM   328  C  CE2 . TYR A 1 40  ? -22.789 -4.195  38.245  1.00 25.56  ? 40  TYR A CE2 1 
ATOM   329  C  CZ  . TYR A 1 40  ? -23.161 -3.676  37.034  1.00 27.16  ? 40  TYR A CZ  1 
ATOM   330  O  OH  . TYR A 1 40  ? -24.423 -3.147  36.955  1.00 32.63  ? 40  TYR A OH  1 
ATOM   331  N  N   . ASP A 1 41  ? -18.616 -2.299  36.842  1.00 15.63  ? 41  ASP A N   1 
ATOM   332  C  CA  . ASP A 1 41  ? -18.707 -0.947  37.329  1.00 16.97  ? 41  ASP A CA  1 
ATOM   333  C  C   . ASP A 1 41  ? -20.114 -0.461  37.056  1.00 18.54  ? 41  ASP A C   1 
ATOM   334  O  O   . ASP A 1 41  ? -20.410 -0.125  35.927  1.00 17.79  ? 41  ASP A O   1 
ATOM   335  C  CB  . ASP A 1 41  ? -17.679 -0.045  36.653  1.00 19.61  ? 41  ASP A CB  1 
ATOM   336  C  CG  . ASP A 1 41  ? -17.686 1.359   37.223  1.00 24.25  ? 41  ASP A CG  1 
ATOM   337  O  OD1 . ASP A 1 41  ? -18.645 1.682   38.008  1.00 29.69  ? 41  ASP A OD1 1 
ATOM   338  O  OD2 . ASP A 1 41  ? -16.713 2.115   36.917  1.00 29.66  ? 41  ASP A OD2 1 
ATOM   339  N  N   . PRO A 1 42  ? -21.010 -0.514  38.063  1.00 24.11  ? 42  PRO A N   1 
ATOM   340  C  CA  . PRO A 1 42  ? -22.379 -0.093  37.796  1.00 26.01  ? 42  PRO A CA  1 
ATOM   341  C  C   . PRO A 1 42  ? -22.472 1.409   37.537  1.00 26.59  ? 42  PRO A C   1 
ATOM   342  O  O   . PRO A 1 42  ? -23.509 1.913   37.090  1.00 35.59  ? 42  PRO A O   1 
ATOM   343  C  CB  . PRO A 1 42  ? -23.127 -0.487  39.068  1.00 30.57  ? 42  PRO A CB  1 
ATOM   344  C  CG  . PRO A 1 42  ? -22.050 -0.467  40.130  1.00 37.36  ? 42  PRO A CG  1 
ATOM   345  C  CD  . PRO A 1 42  ? -20.794 -0.977  39.461  1.00 26.34  ? 42  PRO A CD  1 
ATOM   346  N  N   . SER A 1 43  ? -21.358 2.136   37.714  1.00 25.31  ? 43  SER A N   1 
ATOM   347  C  CA  . SER A 1 43  ? -21.425 3.550   37.307  1.00 27.68  ? 43  SER A CA  1 
ATOM   348  C  C   . SER A 1 43  ? -21.196 3.782   35.800  1.00 23.19  ? 43  SER A C   1 
ATOM   349  O  O   . SER A 1 43  ? -21.451 4.911   35.267  1.00 30.80  ? 43  SER A O   1 
ATOM   350  C  CB  . SER A 1 43  ? -20.457 4.362   38.091  1.00 33.23  ? 43  SER A CB  1 
ATOM   351  O  OG  . SER A 1 43  ? -19.120 4.219   37.604  1.00 33.17  ? 43  SER A OG  1 
ATOM   352  N  N   . LEU A 1 44  ? -20.759 2.736   35.076  1.00 23.10  ? 44  LEU A N   1 
ATOM   353  C  CA  . LEU A 1 44  ? -20.508 2.899   33.640  1.00 23.14  ? 44  LEU A CA  1 
ATOM   354  C  C   . LEU A 1 44  ? -21.844 3.088   32.923  1.00 25.98  ? 44  LEU A C   1 
ATOM   355  O  O   . LEU A 1 44  ? -22.808 2.383   33.199  1.00 29.09  ? 44  LEU A O   1 
ATOM   356  C  CB  . LEU A 1 44  ? -19.796 1.683   33.065  1.00 20.50  ? 44  LEU A CB  1 
ATOM   357  C  CG  . LEU A 1 44  ? -18.306 1.601   33.295  1.00 18.88  ? 44  LEU A CG  1 
ATOM   358  C  CD1 . LEU A 1 44  ? -17.800 0.263   32.883  1.00 20.40  ? 44  LEU A CD1 1 
ATOM   359  C  CD2 . LEU A 1 44  ? -17.571 2.712   32.640  1.00 21.68  ? 44  LEU A CD2 1 
ATOM   360  N  N   . LYS A 1 45  ? -21.875 3.949   31.915  1.00 22.50  ? 45  LYS A N   1 
ATOM   361  C  CA  . LYS A 1 45  ? -23.068 4.135   31.102  1.00 24.77  ? 45  LYS A CA  1 
ATOM   362  C  C   . LYS A 1 45  ? -23.082 3.198   29.913  1.00 20.97  ? 45  LYS A C   1 
ATOM   363  O  O   . LYS A 1 45  ? -22.054 2.639   29.458  1.00 22.27  ? 45  LYS A O   1 
ATOM   364  C  CB  . LYS A 1 45  ? -23.175 5.561   30.594  1.00 23.40  ? 45  LYS A CB  1 
ATOM   365  C  CG  . LYS A 1 45  ? -22.970 6.656   31.641  1.00 26.28  ? 45  LYS A CG  1 
ATOM   366  C  CD  . LYS A 1 45  ? -23.228 8.018   30.985  1.00 38.29  ? 45  LYS A CD  1 
ATOM   367  N  N   . PRO A 1 46  ? -24.324 2.966   29.388  1.00 18.60  ? 46  PRO A N   1 
ATOM   368  C  CA  . PRO A 1 46  ? -24.426 2.300   28.093  1.00 18.17  ? 46  PRO A CA  1 
ATOM   369  C  C   . PRO A 1 46  ? -23.588 3.101   27.116  1.00 15.70  ? 46  PRO A C   1 
ATOM   370  O  O   . PRO A 1 46  ? -23.552 4.309   27.183  1.00 17.73  ? 46  PRO A O   1 
ATOM   371  C  CB  . PRO A 1 46  ? -25.910 2.345   27.731  1.00 20.78  ? 46  PRO A CB  1 
ATOM   372  C  CG  . PRO A 1 46  ? -26.607 2.577   29.023  1.00 24.98  ? 46  PRO A CG  1 
ATOM   373  C  CD  . PRO A 1 46  ? -25.632 3.341   29.924  1.00 23.38  ? 46  PRO A CD  1 
ATOM   374  N  N   A LEU A 1 47  ? -22.827 2.410   26.276  0.50 20.67  ? 47  LEU A N   1 
ATOM   375  N  N   B LEU A 1 47  ? -23.024 2.386   26.122  0.50 16.00  ? 47  LEU A N   1 
ATOM   376  C  CA  A LEU A 1 47  ? -22.193 3.117   25.202  0.50 16.94  ? 47  LEU A CA  1 
ATOM   377  C  CA  B LEU A 1 47  ? -22.312 2.950   24.999  0.50 13.64  ? 47  LEU A CA  1 
ATOM   378  C  C   A LEU A 1 47  ? -23.351 3.699   24.375  0.50 17.95  ? 47  LEU A C   1 
ATOM   379  C  C   B LEU A 1 47  ? -23.330 3.569   24.054  0.50 17.14  ? 47  LEU A C   1 
ATOM   380  O  O   A LEU A 1 47  ? -24.457 3.169   24.423  0.50 19.28  ? 47  LEU A O   1 
ATOM   381  O  O   B LEU A 1 47  ? -24.227 2.869   23.579  0.50 14.40  ? 47  LEU A O   1 
ATOM   382  C  CB  A LEU A 1 47  ? -21.328 2.057   24.512  0.50 18.68  ? 47  LEU A CB  1 
ATOM   383  C  CB  B LEU A 1 47  ? -21.672 1.804   24.214  0.50 18.93  ? 47  LEU A CB  1 
ATOM   384  C  CG  A LEU A 1 47  ? -20.485 2.557   23.364  0.50 19.32  ? 47  LEU A CG  1 
ATOM   385  C  CG  B LEU A 1 47  ? -20.216 1.469   24.451  0.50 22.03  ? 47  LEU A CG  1 
ATOM   386  C  CD1 A LEU A 1 47  ? -19.358 3.407   23.935  0.50 19.03  ? 47  LEU A CD1 1 
ATOM   387  C  CD1 B LEU A 1 47  ? -19.685 0.838   23.185  0.50 22.76  ? 47  LEU A CD1 1 
ATOM   388  C  CD2 A LEU A 1 47  ? -19.873 1.426   22.547  0.50 20.50  ? 47  LEU A CD2 1 
ATOM   389  C  CD2 B LEU A 1 47  ? -19.392 2.714   24.829  0.50 24.01  ? 47  LEU A CD2 1 
ATOM   390  N  N   . SER A 1 48  ? -23.114 4.829   23.691  1.00 14.81  ? 48  SER A N   1 
ATOM   391  C  CA  . SER A 1 48  ? -23.924 5.401   22.635  1.00 15.03  ? 48  SER A CA  1 
ATOM   392  C  C   . SER A 1 48  ? -23.155 5.364   21.323  1.00 14.59  ? 48  SER A C   1 
ATOM   393  O  O   . SER A 1 48  ? -22.146 6.041   21.165  1.00 16.30  ? 48  SER A O   1 
ATOM   394  C  CB  . SER A 1 48  ? -24.346 6.806   23.039  1.00 17.63  ? 48  SER A CB  1 
ATOM   395  O  OG  . SER A 1 48  ? -24.943 7.493   21.980  1.00 21.89  ? 48  SER A OG  1 
ATOM   396  N  N   . VAL A 1 49  ? -23.621 4.561   20.404  1.00 16.13  ? 49  VAL A N   1 
ATOM   397  C  CA  . VAL A 1 49  ? -23.019 4.455   19.098  1.00 17.46  ? 49  VAL A CA  1 
ATOM   398  C  C   . VAL A 1 49  ? -24.001 5.096   18.128  1.00 19.22  ? 49  VAL A C   1 
ATOM   399  O  O   . VAL A 1 49  ? -25.081 4.553   18.002  1.00 23.63  ? 49  VAL A O   1 
ATOM   400  C  CB  . VAL A 1 49  ? -22.762 2.994   18.715  1.00 18.33  ? 49  VAL A CB  1 
ATOM   401  C  CG1 . VAL A 1 49  ? -22.210 2.947   17.341  1.00 25.05  ? 49  VAL A CG1 1 
ATOM   402  C  CG2 . VAL A 1 49  ? -21.907 2.279   19.744  1.00 23.14  ? 49  VAL A CG2 1 
ATOM   403  N  N   . SER A 1 50  ? -23.669 6.240   17.522  1.00 17.23  ? 50  SER A N   1 
ATOM   404  C  CA  . SER A 1 50  ? -24.613 6.951   16.669  1.00 17.92  ? 50  SER A CA  1 
ATOM   405  C  C   . SER A 1 50  ? -24.010 7.044   15.277  1.00 16.10  ? 50  SER A C   1 
ATOM   406  O  O   . SER A 1 50  ? -23.290 7.996   14.980  1.00 17.08  ? 50  SER A O   1 
ATOM   407  C  CB  . SER A 1 50  ? -24.955 8.337   17.226  1.00 25.21  ? 50  SER A CB  1 
ATOM   408  O  OG  . SER A 1 50  ? -25.614 8.253   18.478  1.00 27.60  ? 50  SER A OG  1 
ATOM   409  N  N   . TYR A 1 51  ? -24.241 6.010   14.474  1.00 16.93  ? 51  TYR A N   1 
ATOM   410  C  CA  . TYR A 1 51  ? -23.626 5.875   13.160  1.00 16.15  ? 51  TYR A CA  1 
ATOM   411  C  C   . TYR A 1 51  ? -24.587 6.163   11.994  1.00 15.96  ? 51  TYR A C   1 
ATOM   412  O  O   . TYR A 1 51  ? -24.177 5.988   10.860  1.00 16.12  ? 51  TYR A O   1 
ATOM   413  C  CB  . TYR A 1 51  ? -23.035 4.483   13.003  1.00 15.14  ? 51  TYR A CB  1 
ATOM   414  C  CG  . TYR A 1 51  ? -21.749 4.209   13.779  1.00 13.31  ? 51  TYR A CG  1 
ATOM   415  C  CD1 . TYR A 1 51  ? -21.044 5.187   14.474  1.00 14.02  ? 51  TYR A CD1 1 
ATOM   416  C  CD2 . TYR A 1 51  ? -21.243 2.916   13.778  1.00 13.27  ? 51  TYR A CD2 1 
ATOM   417  C  CE1 . TYR A 1 51  ? -19.833 4.879   15.113  1.00 13.58  ? 51  TYR A CE1 1 
ATOM   418  C  CE2 . TYR A 1 51  ? -20.045 2.604   14.386  1.00 12.25  ? 51  TYR A CE2 1 
ATOM   419  C  CZ  . TYR A 1 51  ? -19.350 3.583   15.076  1.00 13.23  ? 51  TYR A CZ  1 
ATOM   420  O  OH  . TYR A 1 51  ? -18.175 3.257   15.681  1.00 13.69  ? 51  TYR A OH  1 
ATOM   421  N  N   . ASP A 1 52  ? -25.807 6.678   12.246  1.00 19.33  ? 52  ASP A N   1 
ATOM   422  C  CA  . ASP A 1 52  ? -26.779 6.850   11.176  1.00 19.50  ? 52  ASP A CA  1 
ATOM   423  C  C   . ASP A 1 52  ? -26.359 7.763   10.015  1.00 20.47  ? 52  ASP A C   1 
ATOM   424  O  O   . ASP A 1 52  ? -26.753 7.501   8.879   1.00 24.72  ? 52  ASP A O   1 
ATOM   425  C  CB  . ASP A 1 52  ? -28.121 7.280   11.772  1.00 23.71  ? 52  ASP A CB  1 
ATOM   426  C  CG  . ASP A 1 52  ? -28.077 8.435   12.769  1.00 35.37  ? 52  ASP A CG  1 
ATOM   427  O  OD1 . ASP A 1 52  ? -27.417 8.292   13.838  1.00 43.21  ? 52  ASP A OD1 1 
ATOM   428  O  OD2 . ASP A 1 52  ? -28.765 9.462   12.501  1.00 48.37  ? 52  ASP A OD2 1 
ATOM   429  N  N   . GLN A 1 53  ? -25.558 8.794   10.282  1.00 18.01  ? 53  GLN A N   1 
ATOM   430  C  CA  . GLN A 1 53  ? -25.145 9.713   9.218   1.00 16.56  ? 53  GLN A CA  1 
ATOM   431  C  C   . GLN A 1 53  ? -23.698 9.477   8.802   1.00 14.43  ? 53  GLN A C   1 
ATOM   432  O  O   . GLN A 1 53  ? -23.105 10.334  8.147   1.00 15.64  ? 53  GLN A O   1 
ATOM   433  C  CB  . GLN A 1 53  ? -25.287 11.186  9.633   1.00 18.60  ? 53  GLN A CB  1 
ATOM   434  C  CG  . GLN A 1 53  ? -26.737 11.544  9.931   1.00 21.41  ? 53  GLN A CG  1 
ATOM   435  C  CD  . GLN A 1 53  ? -27.647 11.377  8.743   1.00 27.53  ? 53  GLN A CD  1 
ATOM   436  O  OE1 . GLN A 1 53  ? -28.765 10.883  8.890   1.00 42.71  ? 53  GLN A OE1 1 
ATOM   437  N  NE2 . GLN A 1 53  ? -27.206 11.854  7.575   1.00 23.19  ? 53  GLN A NE2 1 
ATOM   438  N  N   . ALA A 1 54  ? -23.178 8.277   9.031   1.00 13.80  ? 54  ALA A N   1 
ATOM   439  C  CA  . ALA A 1 54  ? -21.787 8.047   8.603   1.00 12.51  ? 54  ALA A CA  1 
ATOM   440  C  C   . ALA A 1 54  ? -21.604 8.226   7.114   1.00 13.02  ? 54  ALA A C   1 
ATOM   441  O  O   . ALA A 1 54  ? -22.464 7.804   6.325   1.00 15.27  ? 54  ALA A O   1 
ATOM   442  C  CB  . ALA A 1 54  ? -21.430 6.640   9.030   1.00 15.57  ? 54  ALA A CB  1 
ATOM   443  N  N   . THR A 1 55  ? -20.446 8.770   6.754   1.00 11.96  ? 55  THR A N   1 
ATOM   444  C  CA  . THR A 1 55  ? -20.095 8.946   5.337   1.00 11.84  ? 55  THR A CA  1 
ATOM   445  C  C   . THR A 1 55  ? -18.747 8.301   5.113   1.00 10.57  ? 55  THR A C   1 
ATOM   446  O  O   . THR A 1 55  ? -17.705 8.900   5.410   1.00 11.47  ? 55  THR A O   1 
ATOM   447  C  CB  . THR A 1 55  ? -20.001 10.446  4.956   1.00 14.04  ? 55  THR A CB  1 
ATOM   448  O  OG1 . THR A 1 55  ? -21.313 10.999  5.060   1.00 15.06  ? 55  THR A OG1 1 
ATOM   449  C  CG2 . THR A 1 55  ? -19.542 10.639  3.511   1.00 14.79  ? 55  THR A CG2 1 
ATOM   450  N  N   . SER A 1 56  ? -18.739 7.058   4.659   1.00 9.68   ? 56  SER A N   1 
ATOM   451  C  CA  . SER A 1 56  ? -17.482 6.465   4.245   1.00 10.10  ? 56  SER A CA  1 
ATOM   452  C  C   . SER A 1 56  ? -17.004 7.139   2.983   1.00 10.05  ? 56  SER A C   1 
ATOM   453  O  O   . SER A 1 56  ? -17.800 7.572   2.155   1.00 11.04  ? 56  SER A O   1 
ATOM   454  C  CB  . SER A 1 56  ? -17.651 4.973   4.094   1.00 10.80  ? 56  SER A CB  1 
ATOM   455  O  OG  . SER A 1 56  ? -18.475 4.622   2.991   1.00 10.72  ? 56  SER A OG  1 
ATOM   456  N  N   . LEU A 1 57  ? -15.687 7.180   2.819   1.00 10.64  ? 57  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 57  ? -15.111 7.835   1.656   1.00 11.23  ? 57  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 57  ? -14.288 6.883   0.800   1.00 10.52  ? 57  LEU A C   1 
ATOM   459  O  O   . LEU A 1 57  ? -14.470 6.830   -0.414  1.00 12.15  ? 57  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 57  ? -14.214 9.015   2.066   1.00 12.83  ? 57  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 57  ? -14.984 10.122  2.729   1.00 13.33  ? 57  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 57  ? -14.011 11.124  3.294   1.00 16.62  ? 57  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 57  ? -15.959 10.762  1.756   1.00 17.52  ? 57  LEU A CD2 1 
ATOM   464  N  N   . ARG A 1 58  ? -13.281 6.201   1.380   1.00 11.51  ? 58  ARG A N   1 
ATOM   465  C  CA  . ARG A 1 58  ? -12.284 5.474   0.597   1.00 12.07  ? 58  ARG A CA  1 
ATOM   466  C  C   . ARG A 1 58  ? -11.855 4.272   1.433   1.00 10.27  ? 58  ARG A C   1 
ATOM   467  O  O   . ARG A 1 58  ? -12.000 4.250   2.664   1.00 11.96  ? 58  ARG A O   1 
ATOM   468  C  CB  . ARG A 1 58  ? -11.069 6.347   0.250   1.00 13.28  ? 58  ARG A CB  1 
ATOM   469  C  CG  . ARG A 1 58  ? -11.394 7.580   -0.586  1.00 16.30  ? 58  ARG A CG  1 
ATOM   470  C  CD  . ARG A 1 58  ? -10.149 8.263   -1.174  1.00 20.39  ? 58  ARG A CD  1 
ATOM   471  N  NE  . ARG A 1 58  ? -9.392  7.321   -1.973  1.00 25.84  ? 58  ARG A NE  1 
ATOM   472  C  CZ  . ARG A 1 58  ? -9.692  7.038   -3.251  1.00 24.21  ? 58  ARG A CZ  1 
ATOM   473  N  NH1 . ARG A 1 58  ? -8.896  6.284   -3.990  1.00 26.16  ? 58  ARG A NH1 1 
ATOM   474  N  NH2 . ARG A 1 58  ? -10.737 7.628   -3.829  1.00 29.57  ? 58  ARG A NH2 1 
ATOM   475  N  N   . ILE A 1 59  ? -11.268 3.289   0.734   1.00 10.57  ? 59  ILE A N   1 
ATOM   476  C  CA  . ILE A 1 59  ? -10.629 2.140   1.379   1.00 11.00  ? 59  ILE A CA  1 
ATOM   477  C  C   . ILE A 1 59  ? -9.219  2.053   0.825   1.00 11.11  ? 59  ILE A C   1 
ATOM   478  O  O   . ILE A 1 59  ? -9.005  2.269   -0.372  1.00 11.74  ? 59  ILE A O   1 
ATOM   479  C  CB  . ILE A 1 59  ? -11.478 0.877   1.112   1.00 11.33  ? 59  ILE A CB  1 
ATOM   480  C  CG1 . ILE A 1 59  ? -11.002 -0.305  1.999   1.00 11.51  ? 59  ILE A CG1 1 
ATOM   481  C  CG2 . ILE A 1 59  ? -11.550 0.510   -0.371  1.00 11.66  ? 59  ILE A CG2 1 
ATOM   482  C  CD1 . ILE A 1 59  ? -11.900 -1.511  1.949   1.00 13.36  ? 59  ILE A CD1 1 
ATOM   483  N  N   . LEU A 1 60  ? -8.261  1.686   1.681   1.00 11.35  ? 60  LEU A N   1 
ATOM   484  C  CA  . LEU A 1 60  ? -6.882  1.644   1.201   1.00 12.85  ? 60  LEU A CA  1 
ATOM   485  C  C   . LEU A 1 60  ? -6.147  0.501   1.908   1.00 10.31  ? 60  LEU A C   1 
ATOM   486  O  O   . LEU A 1 60  ? -6.442  0.137   3.041   1.00 13.28  ? 60  LEU A O   1 
ATOM   487  C  CB  . LEU A 1 60  ? -6.190  2.975   1.426   1.00 17.79  ? 60  LEU A CB  1 
ATOM   488  C  CG  . LEU A 1 60  ? -5.946  3.297   2.865   1.00 21.32  ? 60  LEU A CG  1 
ATOM   489  C  CD1 . LEU A 1 60  ? -4.580  3.952   2.979   1.00 30.24  ? 60  LEU A CD1 1 
ATOM   490  C  CD2 . LEU A 1 60  ? -6.968  4.321   3.313   1.00 36.42  ? 60  LEU A CD2 1 
ATOM   491  N  N   . ASN A 1 61  ? -5.134  -0.007  1.216   1.00 10.75  ? 61  ASN A N   1 
ATOM   492  C  CA  . ASN A 1 61  ? -4.153  -0.966  1.767   1.00 11.09  ? 61  ASN A CA  1 
ATOM   493  C  C   . ASN A 1 61  ? -2.894  -0.147  2.048   1.00 11.77  ? 61  ASN A C   1 
ATOM   494  O  O   . ASN A 1 61  ? -2.317  0.392   1.117   1.00 12.22  ? 61  ASN A O   1 
ATOM   495  C  CB  . ASN A 1 61  ? -3.862  -2.040  0.711   1.00 12.48  ? 61  ASN A CB  1 
ATOM   496  C  CG  . ASN A 1 61  ? -2.859  -3.068  1.156   1.00 11.67  ? 61  ASN A CG  1 
ATOM   497  O  OD1 . ASN A 1 61  ? -1.975  -2.728  1.959   1.00 13.48  ? 61  ASN A OD1 1 
ATOM   498  N  ND2 . ASN A 1 61  ? -2.885  -4.247  0.552   1.00 12.83  ? 61  ASN A ND2 1 
ATOM   499  N  N   . ASN A 1 62  ? -2.549  -0.037  3.326   1.00 11.65  ? 62  ASN A N   1 
ATOM   500  C  CA  . ASN A 1 62  ? -1.357  0.756   3.667   1.00 12.67  ? 62  ASN A CA  1 
ATOM   501  C  C   . ASN A 1 62  ? -0.152  -0.139  3.969   1.00 13.65  ? 62  ASN A C   1 
ATOM   502  O  O   . ASN A 1 62  ? 0.857   0.367   4.502   1.00 17.02  ? 62  ASN A O   1 
ATOM   503  C  CB  . ASN A 1 62  ? -1.658  1.680   4.834   1.00 13.87  ? 62  ASN A CB  1 
ATOM   504  C  CG  . ASN A 1 62  ? -2.072  0.926   6.075   1.00 13.23  ? 62  ASN A CG  1 
ATOM   505  O  OD1 . ASN A 1 62  ? -1.880  -0.279  6.177   1.00 13.60  ? 62  ASN A OD1 1 
ATOM   506  N  ND2 . ASN A 1 62  ? -2.627  1.654   7.020   1.00 19.73  ? 62  ASN A ND2 1 
ATOM   507  N  N   . GLY A 1 63  ? -0.215  -1.411  3.615   1.00 13.68  ? 63  GLY A N   1 
ATOM   508  C  CA  . GLY A 1 63  ? 0.945   -2.284  3.832   1.00 15.64  ? 63  GLY A CA  1 
ATOM   509  C  C   . GLY A 1 63  ? 0.937   -2.932  5.204   1.00 14.48  ? 63  GLY A C   1 
ATOM   510  O  O   . GLY A 1 63  ? 1.818   -3.749  5.478   1.00 17.39  ? 63  GLY A O   1 
ATOM   511  N  N   . HIS A 1 64  ? 0.000   -2.508  6.078   1.00 12.94  ? 64  HIS A N   1 
ATOM   512  C  CA  . HIS A 1 64  ? -0.110  -3.015  7.450   1.00 13.54  ? 64  HIS A CA  1 
ATOM   513  C  C   . HIS A 1 64  ? -1.453  -3.687  7.655   1.00 12.49  ? 64  HIS A C   1 
ATOM   514  O  O   . HIS A 1 64  ? -1.538  -4.744  8.255   1.00 16.19  ? 64  HIS A O   1 
ATOM   515  C  CB  . HIS A 1 64  ? 0.093   -1.883  8.464   1.00 15.49  ? 64  HIS A CB  1 
ATOM   516  C  CG  . HIS A 1 64  ? 1.365   -1.162  8.306   1.00 16.04  ? 64  HIS A CG  1 
ATOM   517  N  ND1 . HIS A 1 64  ? 2.608   -1.753  8.520   1.00 18.25  ? 64  HIS A ND1 1 
ATOM   518  C  CD2 . HIS A 1 64  ? 1.604   0.143   7.997   1.00 17.61  ? 64  HIS A CD2 1 
ATOM   519  C  CE1 . HIS A 1 64  ? 3.554   -0.860  8.321   1.00 22.00  ? 64  HIS A CE1 1 
ATOM   520  N  NE2 . HIS A 1 64  ? 2.949   0.355   8.035   1.00 21.94  ? 64  HIS A NE2 1 
ATOM   521  N  N   . SER A 1 65  ? -2.495  -3.002  7.165   1.00 12.50  ? 65  SER A N   1 
ATOM   522  C  CA  . SER A 1 65  ? -3.879  -3.451  7.237   1.00 12.11  ? 65  SER A CA  1 
ATOM   523  C  C   . SER A 1 65  ? -4.586  -2.827  6.024   1.00 11.11  ? 65  SER A C   1 
ATOM   524  O  O   . SER A 1 65  ? -3.968  -2.232  5.161   1.00 11.91  ? 65  SER A O   1 
ATOM   525  C  CB  . SER A 1 65  ? -4.486  -3.039  8.567   1.00 13.81  ? 65  SER A CB  1 
ATOM   526  O  OG  . SER A 1 65  ? -5.792  -3.539  8.705   1.00 17.60  ? 65  SER A OG  1 
ATOM   527  N  N   . PHE A 1 66  ? -5.912  -2.965  5.998   1.00 10.76  ? 66  PHE A N   1 
ATOM   528  C  CA  . PHE A 1 66  ? -6.711  -2.110  5.131   1.00 11.62  ? 66  PHE A CA  1 
ATOM   529  C  C   . PHE A 1 66  ? -7.558  -1.274  6.058   1.00 9.79   ? 66  PHE A C   1 
ATOM   530  O  O   . PHE A 1 66  ? -7.978  -1.657  7.143   1.00 11.13  ? 66  PHE A O   1 
ATOM   531  C  CB  . PHE A 1 66  ? -7.507  -2.880  4.078   1.00 12.12  ? 66  PHE A CB  1 
ATOM   532  C  CG  . PHE A 1 66  ? -8.650  -3.698  4.618   1.00 11.49  ? 66  PHE A CG  1 
ATOM   533  C  CD1 . PHE A 1 66  ? -9.899  -3.099  4.813   1.00 12.06  ? 66  PHE A CD1 1 
ATOM   534  C  CD2 . PHE A 1 66  ? -8.479  -5.014  5.007   1.00 13.82  ? 66  PHE A CD2 1 
ATOM   535  C  CE1 . PHE A 1 66  ? -10.934 -3.854  5.326   1.00 13.07  ? 66  PHE A CE1 1 
ATOM   536  C  CE2 . PHE A 1 66  ? -9.543  -5.771  5.500   1.00 13.51  ? 66  PHE A CE2 1 
ATOM   537  C  CZ  . PHE A 1 66  ? -10.781 -5.194  5.645   1.00 13.54  ? 66  PHE A CZ  1 
ATOM   538  N  N   . LYS A 1 67  ? -7.875  -0.060  5.528   1.00 11.34  ? 67  LYS A N   1 
ATOM   539  C  CA  . LYS A 1 67  ? -8.612  0.894   6.330   1.00 11.59  ? 67  LYS A CA  1 
ATOM   540  C  C   . LYS A 1 67  ? -9.683  1.556   5.475   1.00 10.23  ? 67  LYS A C   1 
ATOM   541  O  O   . LYS A 1 67  ? -9.459  1.896   4.326   1.00 11.69  ? 67  LYS A O   1 
ATOM   542  C  CB  . LYS A 1 67  ? -7.613  1.948   6.801   1.00 17.54  ? 67  LYS A CB  1 
ATOM   543  C  CG  . LYS A 1 67  ? -8.134  3.085   7.580   1.00 19.52  ? 67  LYS A CG  1 
ATOM   544  C  CD  . LYS A 1 67  ? -7.060  4.236   7.644   1.00 20.42  ? 67  LYS A CD  1 
ATOM   545  C  CE  . LYS A 1 67  ? -5.649  3.920   8.038   1.00 25.29  ? 67  LYS A CE  1 
ATOM   546  N  NZ  . LYS A 1 67  ? -4.844  5.181   8.178   1.00 25.66  ? 67  LYS A NZ  1 
ATOM   547  N  N   . VAL A 1 68  ? -10.859 1.719   6.119   1.00 9.46   ? 68  VAL A N   1 
ATOM   548  C  CA  . VAL A 1 68  ? -11.936 2.505   5.502   1.00 9.53   ? 68  VAL A CA  1 
ATOM   549  C  C   . VAL A 1 68  ? -11.973 3.846   6.247   1.00 8.86   ? 68  VAL A C   1 
ATOM   550  O  O   . VAL A 1 68  ? -12.084 3.875   7.472   1.00 9.91   ? 68  VAL A O   1 
ATOM   551  C  CB  . VAL A 1 68  ? -13.269 1.784   5.651   1.00 10.15  ? 68  VAL A CB  1 
ATOM   552  C  CG1 . VAL A 1 68  ? -14.431 2.687   5.189   1.00 11.55  ? 68  VAL A CG1 1 
ATOM   553  C  CG2 . VAL A 1 68  ? -13.286 0.488   4.814   1.00 11.35  ? 68  VAL A CG2 1 
ATOM   554  N  N   . GLU A 1 69  ? -11.800 4.923   5.472   1.00 10.04  ? 69  GLU A N   1 
ATOM   555  C  CA  . GLU A 1 69  ? -11.816 6.269   6.022   1.00 10.20  ? 69  GLU A CA  1 
ATOM   556  C  C   . GLU A 1 69  ? -13.163 6.951   5.836   1.00 9.99   ? 69  GLU A C   1 
ATOM   557  O  O   . GLU A 1 69  ? -13.814 6.758   4.801   1.00 12.49  ? 69  GLU A O   1 
ATOM   558  C  CB  . GLU A 1 69  ? -10.726 7.135   5.400   1.00 14.95  ? 69  GLU A CB  1 
ATOM   559  C  CG  . GLU A 1 69  ? -9.342  6.576   5.778   1.00 22.59  ? 69  GLU A CG  1 
ATOM   560  C  CD  . GLU A 1 69  ? -8.095  7.447   5.669   1.00 23.83  ? 69  GLU A CD  1 
ATOM   561  O  OE1 . GLU A 1 69  ? -7.406  7.363   4.633   1.00 25.14  ? 69  GLU A OE1 1 
ATOM   562  O  OE2 . GLU A 1 69  ? -7.820  8.205   6.620   1.00 33.33  ? 69  GLU A OE2 1 
ATOM   563  N  N   . PHE A 1 70  ? -13.527 7.740   6.838   1.00 10.57  ? 70  PHE A N   1 
ATOM   564  C  CA  . PHE A 1 70  ? -14.788 8.451   6.891   1.00 9.93   ? 70  PHE A CA  1 
ATOM   565  C  C   . PHE A 1 70  ? -14.620 9.941   6.809   1.00 10.39  ? 70  PHE A C   1 
ATOM   566  O  O   . PHE A 1 70  ? -13.556 10.476  7.177   1.00 12.10  ? 70  PHE A O   1 
ATOM   567  C  CB  . PHE A 1 70  ? -15.529 8.103   8.177   1.00 11.01  ? 70  PHE A CB  1 
ATOM   568  C  CG  . PHE A 1 70  ? -16.070 6.694   8.167   1.00 9.67   ? 70  PHE A CG  1 
ATOM   569  C  CD1 . PHE A 1 70  ? -15.206 5.609   8.340   1.00 11.49  ? 70  PHE A CD1 1 
ATOM   570  C  CD2 . PHE A 1 70  ? -17.398 6.456   7.866   1.00 11.13  ? 70  PHE A CD2 1 
ATOM   571  C  CE1 . PHE A 1 70  ? -15.697 4.314   8.297   1.00 12.96  ? 70  PHE A CE1 1 
ATOM   572  C  CE2 . PHE A 1 70  ? -17.910 5.179   7.794   1.00 11.29  ? 70  PHE A CE2 1 
ATOM   573  C  CZ  . PHE A 1 70  ? -17.049 4.109   7.996   1.00 12.38  ? 70  PHE A CZ  1 
ATOM   574  N  N   . ASP A 1 71  ? -15.701 10.634  6.410   1.00 10.69  ? 71  ASP A N   1 
ATOM   575  C  CA  . ASP A 1 71  ? -15.725 12.083  6.486   1.00 11.71  ? 71  ASP A CA  1 
ATOM   576  C  C   . ASP A 1 71  ? -15.967 12.428  7.941   1.00 12.24  ? 71  ASP A C   1 
ATOM   577  O  O   . ASP A 1 71  ? -17.024 12.144  8.481   1.00 13.72  ? 71  ASP A O   1 
ATOM   578  C  CB  . ASP A 1 71  ? -16.871 12.616  5.633   1.00 13.14  ? 71  ASP A CB  1 
ATOM   579  C  CG  . ASP A 1 71  ? -17.037 14.115  5.854   1.00 17.51  ? 71  ASP A CG  1 
ATOM   580  O  OD1 . ASP A 1 71  ? -16.162 14.770  6.442   1.00 15.87  ? 71  ASP A OD1 1 
ATOM   581  O  OD2 . ASP A 1 71  ? -18.151 14.609  5.570   1.00 20.10  ? 71  ASP A OD2 1 
ATOM   582  N  N   . ASP A 1 72  ? -14.947 12.913  8.617   1.00 12.64  ? 72  ASP A N   1 
ATOM   583  C  CA  . ASP A 1 72  ? -15.054 13.277  10.024  1.00 12.70  ? 72  ASP A CA  1 
ATOM   584  C  C   . ASP A 1 72  ? -14.956 14.805  10.194  1.00 14.93  ? 72  ASP A C   1 
ATOM   585  O  O   . ASP A 1 72  ? -14.559 15.283  11.264  1.00 16.31  ? 72  ASP A O   1 
ATOM   586  C  CB  . ASP A 1 72  ? -13.963 12.616  10.862  1.00 13.66  ? 72  ASP A CB  1 
ATOM   587  C  CG  . ASP A 1 72  ? -12.567 12.878  10.464  1.00 15.32  ? 72  ASP A CG  1 
ATOM   588  O  OD1 . ASP A 1 72  ? -12.380 13.601  9.445   1.00 16.41  ? 72  ASP A OD1 1 
ATOM   589  O  OD2 . ASP A 1 72  ? -11.701 12.385  11.176  1.00 18.36  ? 72  ASP A OD2 1 
ATOM   590  N  N   . SER A 1 73  ? -15.380 15.543  9.169   1.00 14.07  ? 73  SER A N   1 
ATOM   591  C  CA  . SER A 1 73  ? -15.377 16.995  9.233   1.00 17.05  ? 73  SER A CA  1 
ATOM   592  C  C   . SER A 1 73  ? -16.631 17.579  9.872   1.00 18.11  ? 73  SER A C   1 
ATOM   593  O  O   . SER A 1 73  ? -16.726 18.816  9.978   1.00 20.08  ? 73  SER A O   1 
ATOM   594  C  CB  . SER A 1 73  ? -15.119 17.552  7.910   1.00 18.11  ? 73  SER A CB  1 
ATOM   595  O  OG  . SER A 1 73  ? -16.275 17.397  7.065   1.00 19.00  ? 73  SER A OG  1 
ATOM   596  N  N   . GLN A 1 74  ? -17.597 16.773  10.237  1.00 19.37  ? 74  GLN A N   1 
ATOM   597  C  CA  . GLN A 1 74  ? -18.650 17.201  11.120  1.00 22.51  ? 74  GLN A CA  1 
ATOM   598  C  C   . GLN A 1 74  ? -19.132 16.033  11.959  1.00 20.77  ? 74  GLN A C   1 
ATOM   599  O  O   . GLN A 1 74  ? -18.640 14.935  11.762  1.00 18.61  ? 74  GLN A O   1 
ATOM   600  C  CB  . GLN A 1 74  ? -19.754 17.879  10.322  1.00 30.75  ? 74  GLN A CB  1 
ATOM   601  C  CG  . GLN A 1 74  ? -20.248 17.091  9.141   1.00 28.89  ? 74  GLN A CG  1 
ATOM   602  C  CD  . GLN A 1 74  ? -21.258 17.964  8.405   1.00 35.79  ? 74  GLN A CD  1 
ATOM   603  O  OE1 . GLN A 1 74  ? -21.961 18.779  9.009   1.00 40.69  ? 74  GLN A OE1 1 
ATOM   604  N  NE2 . GLN A 1 74  ? -21.373 17.811  7.095   1.00 32.62  ? 74  GLN A NE2 1 
ATOM   605  N  N   . ASP A 1 75  ? -20.075 16.281  12.873  1.00 24.55  ? 75  ASP A N   1 
ATOM   606  C  CA  . ASP A 1 75  ? -20.507 15.230  13.774  1.00 28.48  ? 75  ASP A CA  1 
ATOM   607  C  C   . ASP A 1 75  ? -21.497 14.403  12.985  1.00 25.31  ? 75  ASP A C   1 
ATOM   608  O  O   . ASP A 1 75  ? -22.593 14.893  12.700  1.00 31.26  ? 75  ASP A O   1 
ATOM   609  C  CB  . ASP A 1 75  ? -21.195 15.737  15.046  1.00 38.32  ? 75  ASP A CB  1 
ATOM   610  C  CG  . ASP A 1 75  ? -20.261 16.247  16.130  1.00 33.65  ? 75  ASP A CG  1 
ATOM   611  O  OD1 . ASP A 1 75  ? -19.023 15.969  16.043  1.00 33.77  ? 75  ASP A OD1 1 
ATOM   612  O  OD2 . ASP A 1 75  ? -20.785 16.954  17.059  1.00 37.55  ? 75  ASP A OD2 1 
ATOM   613  N  N   . LYS A 1 76  ? -21.023 13.290  12.456  1.00 20.55  ? 76  LYS A N   1 
ATOM   614  C  CA  . LYS A 1 76  ? -21.779 12.390  11.582  1.00 23.03  ? 76  LYS A CA  1 
ATOM   615  C  C   . LYS A 1 76  ? -21.922 10.937  12.065  1.00 20.22  ? 76  LYS A C   1 
ATOM   616  O  O   . LYS A 1 76  ? -22.861 10.236  11.743  1.00 27.71  ? 76  LYS A O   1 
ATOM   617  C  CB  . LYS A 1 76  ? -21.064 12.265  10.234  1.00 23.99  ? 76  LYS A CB  1 
ATOM   618  C  CG  . LYS A 1 76  ? -21.449 13.322  9.211   1.00 27.21  ? 76  LYS A CG  1 
ATOM   619  C  CD  . LYS A 1 76  ? -20.779 13.065  7.874   1.00 24.18  ? 76  LYS A CD  1 
ATOM   620  C  CE  . LYS A 1 76  ? -21.417 14.016  6.868   1.00 27.88  ? 76  LYS A CE  1 
ATOM   621  N  NZ  . LYS A 1 76  ? -20.861 13.812  5.531   1.00 31.36  ? 76  LYS A NZ  1 
ATOM   622  N  N   . ALA A 1 77  ? -20.880 10.426  12.643  1.00 19.80  ? 77  ALA A N   1 
ATOM   623  C  CA  . ALA A 1 77  ? -20.738 9.051   13.171  1.00 15.56  ? 77  ALA A CA  1 
ATOM   624  C  C   . ALA A 1 77  ? -19.961 9.222   14.468  1.00 15.36  ? 77  ALA A C   1 
ATOM   625  O  O   . ALA A 1 77  ? -18.750 9.410   14.447  1.00 19.68  ? 77  ALA A O   1 
ATOM   626  C  CB  . ALA A 1 77  ? -19.991 8.213   12.188  1.00 16.82  ? 77  ALA A CB  1 
ATOM   627  N  N   . VAL A 1 78  ? -20.622 9.123   15.605  1.00 15.10  ? 78  VAL A N   1 
ATOM   628  C  CA  . VAL A 1 78  ? -20.012 9.468   16.877  1.00 16.97  ? 78  VAL A CA  1 
ATOM   629  C  C   . VAL A 1 78  ? -20.290 8.418   17.946  1.00 15.80  ? 78  VAL A C   1 
ATOM   630  O  O   . VAL A 1 78  ? -21.329 7.737   17.990  1.00 18.05  ? 78  VAL A O   1 
ATOM   631  C  CB  . VAL A 1 78  ? -20.298 10.876  17.371  1.00 20.01  ? 78  VAL A CB  1 
ATOM   632  C  CG1 . VAL A 1 78  ? -20.044 11.976  16.346  1.00 22.93  ? 78  VAL A CG1 1 
ATOM   633  C  CG2 . VAL A 1 78  ? -21.697 10.895  17.857  1.00 22.01  ? 78  VAL A CG2 1 
ATOM   634  N  N   . LEU A 1 79  ? -19.310 8.300   18.819  1.00 13.60  ? 79  LEU A N   1 
ATOM   635  C  CA  . LEU A 1 79  ? -19.361 7.477   19.999  1.00 14.19  ? 79  LEU A CA  1 
ATOM   636  C  C   . LEU A 1 79  ? -19.363 8.390   21.210  1.00 16.56  ? 79  LEU A C   1 
ATOM   637  O  O   . LEU A 1 79  ? -18.556 9.344   21.285  1.00 17.77  ? 79  LEU A O   1 
ATOM   638  C  CB  . LEU A 1 79  ? -18.097 6.604   19.932  1.00 17.00  ? 79  LEU A CB  1 
ATOM   639  C  CG  . LEU A 1 79  ? -17.958 5.516   20.958  1.00 17.30  ? 79  LEU A CG  1 
ATOM   640  C  CD1 . LEU A 1 79  ? -19.006 4.445   20.711  1.00 22.22  ? 79  LEU A CD1 1 
ATOM   641  C  CD2 . LEU A 1 79  ? -16.577 4.922   20.791  1.00 17.42  ? 79  LEU A CD2 1 
ATOM   642  N  N   . LYS A 1 80  ? -20.257 8.104   22.150  1.00 16.25  ? 80  LYS A N   1 
ATOM   643  C  CA  . LYS A 1 80  ? -20.215 8.735   23.454  1.00 18.29  ? 80  LYS A CA  1 
ATOM   644  C  C   . LYS A 1 80  ? -20.763 7.828   24.534  1.00 17.09  ? 80  LYS A C   1 
ATOM   645  O  O   . LYS A 1 80  ? -21.091 6.693   24.276  1.00 17.73  ? 80  LYS A O   1 
ATOM   646  C  CB  . LYS A 1 80  ? -20.931 10.071  23.532  1.00 22.32  ? 80  LYS A CB  1 
ATOM   647  C  CG  . LYS A 1 80  ? -22.406 9.978   23.249  1.00 24.48  ? 80  LYS A CG  1 
ATOM   648  C  CD  . LYS A 1 80  ? -23.047 11.338  22.889  1.00 34.02  ? 80  LYS A CD  1 
ATOM   649  N  N   . GLY A 1 81  ? -20.794 8.344   25.767  1.00 18.28  ? 81  GLY A N   1 
ATOM   650  C  CA  . GLY A 1 81  ? -21.293 7.587   26.902  1.00 19.14  ? 81  GLY A CA  1 
ATOM   651  C  C   . GLY A 1 81  ? -20.283 6.493   27.232  1.00 18.17  ? 81  GLY A C   1 
ATOM   652  O  O   . GLY A 1 81  ? -19.102 6.645   26.940  1.00 17.99  ? 81  GLY A O   1 
ATOM   653  N  N   . GLY A 1 82  ? -20.762 5.380   27.772  1.00 23.04  ? 82  GLY A N   1 
ATOM   654  C  CA  . GLY A 1 82  ? -19.844 4.370   28.253  1.00 23.77  ? 82  GLY A CA  1 
ATOM   655  C  C   . GLY A 1 82  ? -18.907 4.988   29.273  1.00 22.24  ? 82  GLY A C   1 
ATOM   656  O  O   . GLY A 1 82  ? -19.322 5.742   30.146  1.00 26.87  ? 82  GLY A O   1 
ATOM   657  N  N   . PRO A 1 83  ? -17.596 4.733   29.130  1.00 19.31  ? 83  PRO A N   1 
ATOM   658  C  CA  . PRO A 1 83  ? -16.596 5.365   29.954  1.00 18.89  ? 83  PRO A CA  1 
ATOM   659  C  C   . PRO A 1 83  ? -16.224 6.773   29.529  1.00 18.47  ? 83  PRO A C   1 
ATOM   660  O  O   . PRO A 1 83  ? -15.372 7.351   30.189  1.00 23.42  ? 83  PRO A O   1 
ATOM   661  C  CB  . PRO A 1 83  ? -15.380 4.457   29.781  1.00 19.48  ? 83  PRO A CB  1 
ATOM   662  C  CG  . PRO A 1 83  ? -15.493 4.057   28.337  1.00 18.37  ? 83  PRO A CG  1 
ATOM   663  C  CD  . PRO A 1 83  ? -16.989 3.898   28.090  1.00 18.41  ? 83  PRO A CD  1 
ATOM   664  N  N   . LEU A 1 84  ? -16.786 7.278   28.426  1.00 15.97  ? 84  LEU A N   1 
ATOM   665  C  CA  . LEU A 1 84  ? -16.202 8.454   27.800  1.00 15.05  ? 84  LEU A CA  1 
ATOM   666  C  C   . LEU A 1 84  ? -16.862 9.698   28.371  1.00 16.27  ? 84  LEU A C   1 
ATOM   667  O  O   . LEU A 1 84  ? -18.028 9.712   28.707  1.00 19.08  ? 84  LEU A O   1 
ATOM   668  C  CB  . LEU A 1 84  ? -16.517 8.406   26.300  1.00 15.22  ? 84  LEU A CB  1 
ATOM   669  C  CG  . LEU A 1 84  ? -15.950 7.177   25.579  1.00 14.21  ? 84  LEU A CG  1 
ATOM   670  C  CD1 . LEU A 1 84  ? -16.423 7.090   24.134  1.00 15.83  ? 84  LEU A CD1 1 
ATOM   671  C  CD2 . LEU A 1 84  ? -14.408 7.145   25.680  1.00 14.08  ? 84  LEU A CD2 1 
ATOM   672  N  N   . ASP A 1 85  ? -16.084 10.761  28.384  1.00 19.97  ? 85  ASP A N   1 
ATOM   673  C  CA  . ASP A 1 85  ? -16.637 12.069  28.682  1.00 22.96  ? 85  ASP A CA  1 
ATOM   674  C  C   . ASP A 1 85  ? -16.505 12.833  27.372  1.00 25.11  ? 85  ASP A C   1 
ATOM   675  O  O   . ASP A 1 85  ? -15.459 12.763  26.726  1.00 29.34  ? 85  ASP A O   1 
ATOM   676  C  CB  . ASP A 1 85  ? -15.766 12.736  29.759  1.00 27.74  ? 85  ASP A CB  1 
ATOM   677  C  CG  . ASP A 1 85  ? -15.866 12.197  31.190  1.00 31.02  ? 85  ASP A CG  1 
ATOM   678  O  OD1 . ASP A 1 85  ? -16.987 11.814  31.620  1.00 48.02  ? 85  ASP A OD1 1 
ATOM   679  O  OD2 . ASP A 1 85  ? -14.823 12.235  31.910  1.00 35.08  ? 85  ASP A OD2 1 
ATOM   680  N  N   . GLY A 1 86  ? -17.548 13.531  26.961  1.00 30.58  ? 86  GLY A N   1 
ATOM   681  C  CA  . GLY A 1 86  ? -17.563 14.104  25.625  1.00 30.44  ? 86  GLY A CA  1 
ATOM   682  C  C   . GLY A 1 86  ? -17.848 13.156  24.447  1.00 22.99  ? 86  GLY A C   1 
ATOM   683  O  O   . GLY A 1 86  ? -18.345 12.034  24.585  1.00 30.85  ? 86  GLY A O   1 
ATOM   684  N  N   . THR A 1 87  ? -17.611 13.683  23.236  1.00 19.19  ? 87  THR A N   1 
ATOM   685  C  CA  . THR A 1 87  ? -18.044 13.112  21.952  1.00 19.87  ? 87  THR A CA  1 
ATOM   686  C  C   . THR A 1 87  ? -16.806 12.738  21.140  1.00 17.10  ? 87  THR A C   1 
ATOM   687  O  O   . THR A 1 87  ? -15.866 13.542  21.033  1.00 17.34  ? 87  THR A O   1 
ATOM   688  C  CB  . THR A 1 87  ? -18.818 14.204  21.183  1.00 27.28  ? 87  THR A CB  1 
ATOM   689  O  OG1 . THR A 1 87  ? -19.983 14.504  21.945  1.00 32.06  ? 87  THR A OG1 1 
ATOM   690  C  CG2 . THR A 1 87  ? -19.236 13.759  19.776  1.00 25.77  ? 87  THR A CG2 1 
ATOM   691  N  N   . TYR A 1 88  ? -16.834 11.559  20.535  1.00 16.08  ? 88  TYR A N   1 
ATOM   692  C  CA  . TYR A 1 88  ? -15.720 11.060  19.758  1.00 13.88  ? 88  TYR A CA  1 
ATOM   693  C  C   . TYR A 1 88  ? -16.223 10.745  18.352  1.00 14.71  ? 88  TYR A C   1 
ATOM   694  O  O   . TYR A 1 88  ? -17.174 9.992   18.174  1.00 17.70  ? 88  TYR A O   1 
ATOM   695  C  CB  . TYR A 1 88  ? -15.145 9.800   20.399  1.00 14.81  ? 88  TYR A CB  1 
ATOM   696  C  CG  . TYR A 1 88  ? -14.386 10.070  21.680  1.00 12.92  ? 88  TYR A CG  1 
ATOM   697  C  CD1 . TYR A 1 88  ? -14.984 10.458  22.853  1.00 14.29  ? 88  TYR A CD1 1 
ATOM   698  C  CD2 . TYR A 1 88  ? -13.018 9.811   21.713  1.00 11.47  ? 88  TYR A CD2 1 
ATOM   699  C  CE1 . TYR A 1 88  ? -14.267 10.645  24.024  1.00 13.53  ? 88  TYR A CE1 1 
ATOM   700  C  CE2 . TYR A 1 88  ? -12.291 9.981   22.880  1.00 11.78  ? 88  TYR A CE2 1 
ATOM   701  C  CZ  . TYR A 1 88  ? -12.882 10.394  24.051  1.00 12.36  ? 88  TYR A CZ  1 
ATOM   702  O  OH  . TYR A 1 88  ? -12.209 10.505  25.237  1.00 13.66  ? 88  TYR A OH  1 
ATOM   703  N  N   . ARG A 1 89  ? -15.571 11.266  17.338  1.00 14.40  ? 89  ARG A N   1 
ATOM   704  C  CA  . ARG A 1 89  ? -15.981 11.104  15.958  1.00 14.18  ? 89  ARG A CA  1 
ATOM   705  C  C   . ARG A 1 89  ? -15.217 9.994   15.269  1.00 10.30  ? 89  ARG A C   1 
ATOM   706  O  O   . ARG A 1 89  ? -14.004 9.900   15.395  1.00 10.27  ? 89  ARG A O   1 
ATOM   707  C  CB  . ARG A 1 89  ? -15.630 12.398  15.267  1.00 18.05  ? 89  ARG A CB  1 
ATOM   708  C  CG  . ARG A 1 89  ? -16.625 12.570  14.169  1.00 21.55  ? 89  ARG A CG  1 
ATOM   709  C  CD  . ARG A 1 89  ? -16.274 13.963  13.636  1.00 25.88  ? 89  ARG A CD  1 
ATOM   710  N  NE  . ARG A 1 89  ? -16.900 14.948  14.435  1.00 27.21  ? 89  ARG A NE  1 
ATOM   711  C  CZ  . ARG A 1 89  ? -16.745 16.257  14.276  1.00 17.50  ? 89  ARG A CZ  1 
ATOM   712  N  NH1 . ARG A 1 89  ? -15.961 16.720  13.317  1.00 26.04  ? 89  ARG A NH1 1 
ATOM   713  N  NH2 . ARG A 1 89  ? -17.375 17.100  15.075  1.00 24.52  ? 89  ARG A NH2 1 
ATOM   714  N  N   . LEU A 1 90  ? -15.978 9.156   14.521  1.00 11.11  ? 90  LEU A N   1 
ATOM   715  C  CA  . LEU A 1 90  ? -15.363 8.062   13.802  1.00 10.25  ? 90  LEU A CA  1 
ATOM   716  C  C   . LEU A 1 90  ? -14.529 8.619   12.653  1.00 10.27  ? 90  LEU A C   1 
ATOM   717  O  O   . LEU A 1 90  ? -15.003 9.378   11.805  1.00 13.25  ? 90  LEU A O   1 
ATOM   718  C  CB  . LEU A 1 90  ? -16.480 7.173   13.232  1.00 10.49  ? 90  LEU A CB  1 
ATOM   719  C  CG  . LEU A 1 90  ? -16.001 6.004   12.356  1.00 10.97  ? 90  LEU A CG  1 
ATOM   720  C  CD1 . LEU A 1 90  ? -15.246 4.970   13.163  1.00 11.51  ? 90  LEU A CD1 1 
ATOM   721  C  CD2 . LEU A 1 90  ? -17.223 5.342   11.696  1.00 13.26  ? 90  LEU A CD2 1 
ATOM   722  N  N   . THR A 1 91  ? -13.256 8.190   12.567  1.00 9.96   ? 91  THR A N   1 
ATOM   723  C  CA  . THR A 1 91  ? -12.421 8.576   11.456  1.00 10.85  ? 91  THR A CA  1 
ATOM   724  C  C   . THR A 1 91  ? -12.093 7.407   10.539  1.00 9.32   ? 91  THR A C   1 
ATOM   725  O  O   . THR A 1 91  ? -12.004 7.620   9.341   1.00 10.05  ? 91  THR A O   1 
ATOM   726  C  CB  . THR A 1 91  ? -11.147 9.264   11.971  1.00 12.88  ? 91  THR A CB  1 
ATOM   727  O  OG1 . THR A 1 91  ? -10.368 9.707   10.840  1.00 18.05  ? 91  THR A OG1 1 
ATOM   728  C  CG2 . THR A 1 91  ? -10.257 8.420   12.872  1.00 13.13  ? 91  THR A CG2 1 
ATOM   729  N  N   . GLN A 1 92  ? -11.954 6.177   11.058  1.00 9.71   ? 92  GLN A N   1 
ATOM   730  C  CA  . GLN A 1 92  ? -11.604 5.054   10.196  1.00 8.73   ? 92  GLN A CA  1 
ATOM   731  C  C   . GLN A 1 92  ? -11.915 3.776   10.935  1.00 8.40   ? 92  GLN A C   1 
ATOM   732  O  O   . GLN A 1 92  ? -11.998 3.786   12.180  1.00 9.16   ? 92  GLN A O   1 
ATOM   733  C  CB  . GLN A 1 92  ? -10.144 5.086   9.763   1.00 10.44  ? 92  GLN A CB  1 
ATOM   734  C  CG  . GLN A 1 92  ? -9.165  5.164   10.960  1.00 11.65  ? 92  GLN A CG  1 
ATOM   735  C  CD  . GLN A 1 92  ? -8.401  3.869   11.112  1.00 12.21  ? 92  GLN A CD  1 
ATOM   736  O  OE1 . GLN A 1 92  ? -8.962  2.797   11.155  1.00 12.34  ? 92  GLN A OE1 1 
ATOM   737  N  NE2 . GLN A 1 92  ? -7.110  3.984   11.369  1.00 17.43  ? 92  GLN A NE2 1 
ATOM   738  N  N   . PHE A 1 93  ? -12.063 2.678   10.184  1.00 8.70   ? 93  PHE A N   1 
ATOM   739  C  CA  . PHE A 1 93  ? -11.933 1.391   10.839  1.00 8.57   ? 93  PHE A CA  1 
ATOM   740  C  C   . PHE A 1 93  ? -10.946 0.559   10.013  1.00 7.98   ? 93  PHE A C   1 
ATOM   741  O  O   . PHE A 1 93  ? -10.698 0.779   8.831   1.00 8.72   ? 93  PHE A O   1 
ATOM   742  C  CB  . PHE A 1 93  ? -13.302 0.677   10.979  1.00 8.95   ? 93  PHE A CB  1 
ATOM   743  C  CG  . PHE A 1 93  ? -14.003 0.237   9.722   1.00 8.65   ? 93  PHE A CG  1 
ATOM   744  C  CD1 . PHE A 1 93  ? -13.576 -0.863  9.004   1.00 9.48   ? 93  PHE A CD1 1 
ATOM   745  C  CD2 . PHE A 1 93  ? -15.141 0.934   9.306   1.00 9.35   ? 93  PHE A CD2 1 
ATOM   746  C  CE1 . PHE A 1 93  ? -14.239 -1.264  7.846   1.00 10.07  ? 93  PHE A CE1 1 
ATOM   747  C  CE2 . PHE A 1 93  ? -15.840 0.501   8.174   1.00 10.06  ? 93  PHE A CE2 1 
ATOM   748  C  CZ  . PHE A 1 93  ? -15.394 -0.590  7.450   1.00 10.39  ? 93  PHE A CZ  1 
ATOM   749  N  N   . HIS A 1 94  ? -10.434 -0.466  10.709  1.00 8.21   ? 94  HIS A N   1 
ATOM   750  C  CA  . HIS A 1 94  ? -9.530  -1.421  10.099  1.00 8.48   ? 94  HIS A CA  1 
ATOM   751  C  C   . HIS A 1 94  ? -9.667  -2.706  10.895  1.00 7.62   ? 94  HIS A C   1 
ATOM   752  O  O   . HIS A 1 94  ? -10.299 -2.777  11.916  1.00 8.54   ? 94  HIS A O   1 
ATOM   753  C  CB  . HIS A 1 94  ? -8.075  -0.878  10.081  1.00 8.95   ? 94  HIS A CB  1 
ATOM   754  C  CG  . HIS A 1 94  ? -7.594  -0.655  11.468  1.00 8.56   ? 94  HIS A CG  1 
ATOM   755  N  ND1 . HIS A 1 94  ? -7.840  0.513   12.161  1.00 8.99   ? 94  HIS A ND1 1 
ATOM   756  C  CD2 . HIS A 1 94  ? -6.992  -1.481  12.376  1.00 8.51   ? 94  HIS A CD2 1 
ATOM   757  C  CE1 . HIS A 1 94  ? -7.419  0.380   13.409  1.00 8.56   ? 94  HIS A CE1 1 
ATOM   758  N  NE2 . HIS A 1 94  ? -6.891  -0.859  13.581  1.00 8.09   ? 94  HIS A NE2 1 
ATOM   759  N  N   . PHE A 1 95  ? -8.922  -3.734  10.428  1.00 8.94   ? 95  PHE A N   1 
ATOM   760  C  CA  . PHE A 1 95  ? -8.946  -5.040  11.076  1.00 9.00   ? 95  PHE A CA  1 
ATOM   761  C  C   . PHE A 1 95  ? -7.531  -5.536  11.297  1.00 8.57   ? 95  PHE A C   1 
ATOM   762  O  O   . PHE A 1 95  ? -6.582  -5.098  10.660  1.00 9.78   ? 95  PHE A O   1 
ATOM   763  C  CB  . PHE A 1 95  ? -9.663  -6.084  10.170  1.00 9.16   ? 95  PHE A CB  1 
ATOM   764  C  CG  . PHE A 1 95  ? -11.117 -5.799  9.900   1.00 9.37   ? 95  PHE A CG  1 
ATOM   765  C  CD1 . PHE A 1 95  ? -11.486 -4.892  8.915   1.00 10.27  ? 95  PHE A CD1 1 
ATOM   766  C  CD2 . PHE A 1 95  ? -12.115 -6.500  10.572  1.00 10.37  ? 95  PHE A CD2 1 
ATOM   767  C  CE1 . PHE A 1 95  ? -12.835 -4.705  8.613   1.00 11.79  ? 95  PHE A CE1 1 
ATOM   768  C  CE2 . PHE A 1 95  ? -13.451 -6.323  10.239  1.00 11.41  ? 95  PHE A CE2 1 
ATOM   769  C  CZ  . PHE A 1 95  ? -13.808 -5.407  9.256   1.00 11.83  ? 95  PHE A CZ  1 
ATOM   770  N  N   . HIS A 1 96  ? -7.467  -6.525  12.205  1.00 8.57   ? 96  HIS A N   1 
ATOM   771  C  CA  . HIS A 1 96  ? -6.254  -7.338  12.392  1.00 8.82   ? 96  HIS A CA  1 
ATOM   772  C  C   . HIS A 1 96  ? -6.740  -8.772  12.270  1.00 8.92   ? 96  HIS A C   1 
ATOM   773  O  O   . HIS A 1 96  ? -7.812  -9.086  12.769  1.00 9.19   ? 96  HIS A O   1 
ATOM   774  C  CB  . HIS A 1 96  ? -5.660  -7.097  13.792  1.00 9.09   ? 96  HIS A CB  1 
ATOM   775  C  CG  . HIS A 1 96  ? -5.366  -5.664  14.056  1.00 8.68   ? 96  HIS A CG  1 
ATOM   776  N  ND1 . HIS A 1 96  ? -4.120  -5.089  13.855  1.00 9.36   ? 96  HIS A ND1 1 
ATOM   777  C  CD2 . HIS A 1 96  ? -6.142  -4.666  14.487  1.00 8.91   ? 96  HIS A CD2 1 
ATOM   778  C  CE1 . HIS A 1 96  ? -4.180  -3.802  14.178  1.00 8.71   ? 96  HIS A CE1 1 
ATOM   779  N  NE2 . HIS A 1 96  ? -5.434  -3.468  14.551  1.00 8.61   ? 96  HIS A NE2 1 
ATOM   780  N  N   . TRP A 1 97  ? -5.927  -9.634  11.658  1.00 8.82   ? 97  TRP A N   1 
ATOM   781  C  CA  . TRP A 1 97  ? -6.366  -11.021 11.479  1.00 9.56   ? 97  TRP A CA  1 
ATOM   782  C  C   . TRP A 1 97  ? -5.160  -11.932 11.343  1.00 8.73   ? 97  TRP A C   1 
ATOM   783  O  O   . TRP A 1 97  ? -3.992  -11.500 11.302  1.00 9.98   ? 97  TRP A O   1 
ATOM   784  C  CB  . TRP A 1 97  ? -7.281  -11.142 10.236  1.00 9.86   ? 97  TRP A CB  1 
ATOM   785  C  CG  . TRP A 1 97  ? -6.612  -10.801 8.951   1.00 9.25   ? 97  TRP A CG  1 
ATOM   786  C  CD1 . TRP A 1 97  ? -5.898  -11.639 8.148   1.00 10.61  ? 97  TRP A CD1 1 
ATOM   787  C  CD2 . TRP A 1 97  ? -6.508  -9.506  8.360   1.00 9.39   ? 97  TRP A CD2 1 
ATOM   788  N  NE1 . TRP A 1 97  ? -5.408  -10.964 7.062   1.00 10.69  ? 97  TRP A NE1 1 
ATOM   789  C  CE2 . TRP A 1 97  ? -5.801  -9.637  7.174   1.00 9.72   ? 97  TRP A CE2 1 
ATOM   790  C  CE3 . TRP A 1 97  ? -6.999  -8.237  8.709   1.00 9.42   ? 97  TRP A CE3 1 
ATOM   791  C  CZ2 . TRP A 1 97  ? -5.519  -8.566  6.332   1.00 10.12  ? 97  TRP A CZ2 1 
ATOM   792  C  CZ3 . TRP A 1 97  ? -6.741  -7.165  7.887   1.00 10.33  ? 97  TRP A CZ3 1 
ATOM   793  C  CH2 . TRP A 1 97  ? -6.034  -7.312  6.701   1.00 10.18  ? 97  TRP A CH2 1 
ATOM   794  N  N   . GLY A 1 98  ? -5.458  -13.210 11.354  1.00 10.06  ? 98  GLY A N   1 
ATOM   795  C  CA  . GLY A 1 98  ? -4.441  -14.265 11.452  1.00 10.40  ? 98  GLY A CA  1 
ATOM   796  C  C   . GLY A 1 98  ? -4.267  -14.996 10.141  1.00 10.81  ? 98  GLY A C   1 
ATOM   797  O  O   . GLY A 1 98  ? -4.968  -14.825 9.148   1.00 13.02  ? 98  GLY A O   1 
ATOM   798  N  N   . SER A 1 99  ? -3.235  -15.869 10.130  1.00 12.45  ? 99  SER A N   1 
ATOM   799  C  CA  . SER A 1 99  ? -2.985  -16.822 9.068   1.00 14.66  ? 99  SER A CA  1 
ATOM   800  C  C   . SER A 1 99  ? -3.960  -18.019 9.178   1.00 13.09  ? 99  SER A C   1 
ATOM   801  O  O   . SER A 1 99  ? -4.129  -18.718 8.193   1.00 20.75  ? 99  SER A O   1 
ATOM   802  C  CB  . SER A 1 99  ? -1.531  -17.222 9.087   1.00 16.04  ? 99  SER A CB  1 
ATOM   803  O  OG  . SER A 1 99  ? -1.108  -17.628 10.380  1.00 15.41  ? 99  SER A OG  1 
ATOM   804  N  N   . LEU A 1 100 ? -4.496  -18.281 10.354  1.00 15.03  ? 100 LEU A N   1 
ATOM   805  C  CA  . LEU A 1 100 ? -5.377  -19.409 10.652  1.00 18.72  ? 100 LEU A CA  1 
ATOM   806  C  C   . LEU A 1 100 ? -6.425  -18.889 11.611  1.00 15.00  ? 100 LEU A C   1 
ATOM   807  O  O   . LEU A 1 100 ? -6.208  -17.859 12.231  1.00 16.01  ? 100 LEU A O   1 
ATOM   808  C  CB  . LEU A 1 100 ? -4.574  -20.542 11.319  1.00 28.15  ? 100 LEU A CB  1 
ATOM   809  C  CG  . LEU A 1 100 ? -3.745  -21.343 10.338  1.00 33.64  ? 100 LEU A CG  1 
ATOM   810  C  CD1 . LEU A 1 100 ? -3.277  -22.587 11.029  1.00 41.19  ? 100 LEU A CD1 1 
ATOM   811  C  CD2 . LEU A 1 100 ? -4.511  -21.689 9.056   1.00 44.16  ? 100 LEU A CD2 1 
ATOM   812  N  N   . ASP A 1 101 ? -7.550  -19.601 11.779  1.00 17.47  ? 101 ASP A N   1 
ATOM   813  C  CA  . ASP A 1 101 ? -8.697  -19.035 12.478  1.00 15.70  ? 101 ASP A CA  1 
ATOM   814  C  C   . ASP A 1 101 ? -8.443  -18.990 13.968  1.00 15.29  ? 101 ASP A C   1 
ATOM   815  O  O   . ASP A 1 101 ? -9.125  -18.243 14.652  1.00 18.75  ? 101 ASP A O   1 
ATOM   816  C  CB  . ASP A 1 101 ? -9.948  -19.880 12.252  1.00 16.88  ? 101 ASP A CB  1 
ATOM   817  C  CG  . ASP A 1 101 ? -10.472 -19.925 10.831  1.00 18.96  ? 101 ASP A CG  1 
ATOM   818  O  OD1 . ASP A 1 101 ? -10.036 -19.139 10.009  1.00 19.93  ? 101 ASP A OD1 1 
ATOM   819  O  OD2 . ASP A 1 101 ? -11.371 -20.737 10.594  1.00 23.85  ? 101 ASP A OD2 1 
ATOM   820  N  N   . GLY A 1 102 ? -7.434  -19.733 14.477  1.00 16.88  ? 102 GLY A N   1 
ATOM   821  C  CA  . GLY A 1 102 ? -7.152  -19.674 15.906  1.00 17.17  ? 102 GLY A CA  1 
ATOM   822  C  C   . GLY A 1 102 ? -6.211  -18.571 16.355  1.00 15.03  ? 102 GLY A C   1 
ATOM   823  O  O   . GLY A 1 102 ? -5.839  -18.526 17.525  1.00 16.23  ? 102 GLY A O   1 
ATOM   824  N  N   . GLN A 1 103 ? -5.936  -17.574 15.514  1.00 14.30  ? 103 GLN A N   1 
ATOM   825  C  CA  . GLN A 1 103 ? -5.247  -16.399 15.950  1.00 11.82  ? 103 GLN A CA  1 
ATOM   826  C  C   . GLN A 1 103 ? -5.662  -15.262 15.053  1.00 10.35  ? 103 GLN A C   1 
ATOM   827  O  O   . GLN A 1 103 ? -6.188  -15.475 13.966  1.00 11.75  ? 103 GLN A O   1 
ATOM   828  C  CB  . GLN A 1 103 ? -3.743  -16.624 15.954  1.00 12.02  ? 103 GLN A CB  1 
ATOM   829  C  CG  . GLN A 1 103 ? -3.178  -16.885 14.552  1.00 13.19  ? 103 GLN A CG  1 
ATOM   830  C  CD  . GLN A 1 103 ? -1.753  -17.414 14.594  1.00 17.07  ? 103 GLN A CD  1 
ATOM   831  O  OE1 . GLN A 1 103 ? -0.857  -17.012 13.860  1.00 17.99  ? 103 GLN A OE1 1 
ATOM   832  N  NE2 . GLN A 1 103 ? -1.493  -18.350 15.456  1.00 23.71  ? 103 GLN A NE2 1 
ATOM   833  N  N   . GLY A 1 104 ? -5.331  -14.035 15.463  1.00 9.95   ? 104 GLY A N   1 
ATOM   834  C  CA  . GLY A 1 104 ? -5.605  -12.865 14.638  1.00 10.17  ? 104 GLY A CA  1 
ATOM   835  C  C   . GLY A 1 104 ? -6.075  -11.692 15.485  1.00 8.95   ? 104 GLY A C   1 
ATOM   836  O  O   . GLY A 1 104 ? -5.797  -10.535 15.079  1.00 10.36  ? 104 GLY A O   1 
ATOM   837  N  N   . SER A 1 105 ? -6.753  -11.916 16.616  1.00 9.35   ? 105 SER A N   1 
ATOM   838  C  CA  . SER A 1 105 ? -7.160  -10.789 17.440  1.00 9.17   ? 105 SER A CA  1 
ATOM   839  C  C   . SER A 1 105 ? -5.946  -10.240 18.188  1.00 8.72   ? 105 SER A C   1 
ATOM   840  O  O   . SER A 1 105 ? -4.939  -10.924 18.420  1.00 10.20  ? 105 SER A O   1 
ATOM   841  C  CB  . SER A 1 105 ? -8.300  -11.138 18.383  1.00 9.64   ? 105 SER A CB  1 
ATOM   842  O  OG  . SER A 1 105 ? -7.919  -12.107 19.351  1.00 9.87   ? 105 SER A OG  1 
ATOM   843  N  N   . GLU A 1 106 ? -6.080  -9.010  18.581  1.00 8.73   ? 106 GLU A N   1 
ATOM   844  C  CA  . GLU A 1 106 ? -5.100  -8.307  19.398  1.00 8.47   ? 106 GLU A CA  1 
ATOM   845  C  C   . GLU A 1 106 ? -5.425  -8.485  20.854  1.00 8.32   ? 106 GLU A C   1 
ATOM   846  O  O   . GLU A 1 106 ? -4.614  -9.056  21.635  1.00 9.48   ? 106 GLU A O   1 
ATOM   847  C  CB  . GLU A 1 106 ? -5.044  -6.827  18.969  1.00 8.74   ? 106 GLU A CB  1 
ATOM   848  C  CG  . GLU A 1 106 ? -4.588  -6.713  17.562  1.00 10.02  ? 106 GLU A CG  1 
ATOM   849  C  CD  . GLU A 1 106 ? -3.904  -5.420  17.244  1.00 8.65   ? 106 GLU A CD  1 
ATOM   850  O  OE1 . GLU A 1 106 ? -4.478  -4.342  17.512  1.00 9.76   ? 106 GLU A OE1 1 
ATOM   851  O  OE2 . GLU A 1 106 ? -2.750  -5.464  16.773  1.00 10.32  ? 106 GLU A OE2 1 
ATOM   852  N  N   . HIS A 1 107 ? -6.595  -8.032  21.286  1.00 8.36   ? 107 HIS A N   1 
ATOM   853  C  CA  . HIS A 1 107 ? -7.035  -8.411  22.602  1.00 8.47   ? 107 HIS A CA  1 
ATOM   854  C  C   . HIS A 1 107 ? -7.319  -9.917  22.621  1.00 8.47   ? 107 HIS A C   1 
ATOM   855  O  O   . HIS A 1 107 ? -7.665  -10.511 21.612  1.00 9.11   ? 107 HIS A O   1 
ATOM   856  C  CB  . HIS A 1 107 ? -8.287  -7.624  23.020  1.00 9.07   ? 107 HIS A CB  1 
ATOM   857  C  CG  . HIS A 1 107 ? -7.977  -6.178  23.135  1.00 8.05   ? 107 HIS A CG  1 
ATOM   858  N  ND1 . HIS A 1 107 ? -8.037  -5.290  22.093  1.00 9.26   ? 107 HIS A ND1 1 
ATOM   859  C  CD2 . HIS A 1 107 ? -7.506  -5.479  24.183  1.00 8.64   ? 107 HIS A CD2 1 
ATOM   860  C  CE1 . HIS A 1 107 ? -7.606  -4.105  22.528  1.00 8.89   ? 107 HIS A CE1 1 
ATOM   861  N  NE2 . HIS A 1 107 ? -7.291  -4.173  23.808  1.00 8.27   ? 107 HIS A NE2 1 
ATOM   862  N  N   . THR A 1 108 ? -7.193  -10.462 23.827  1.00 9.24   ? 108 THR A N   1 
ATOM   863  C  CA  . THR A 1 108 ? -7.590  -11.853 24.074  1.00 9.54   ? 108 THR A CA  1 
ATOM   864  C  C   . THR A 1 108 ? -8.530  -11.845 25.281  1.00 9.23   ? 108 THR A C   1 
ATOM   865  O  O   . THR A 1 108 ? -8.584  -10.882 26.028  1.00 10.23  ? 108 THR A O   1 
ATOM   866  C  CB  . THR A 1 108 ? -6.380  -12.758 24.294  1.00 10.19  ? 108 THR A CB  1 
ATOM   867  O  OG1 . THR A 1 108 ? -5.558  -12.259 25.342  1.00 10.63  ? 108 THR A OG1 1 
ATOM   868  C  CG2 . THR A 1 108 ? -5.604  -12.847 23.026  1.00 11.21  ? 108 THR A CG2 1 
ATOM   869  N  N   . VAL A 1 109 ? -9.301  -12.926 25.397  1.00 10.44  ? 109 VAL A N   1 
ATOM   870  C  CA  . VAL A 1 109 ? -10.291 -13.013 26.459  1.00 11.49  ? 109 VAL A CA  1 
ATOM   871  C  C   . VAL A 1 109 ? -9.980  -14.291 27.215  1.00 11.55  ? 109 VAL A C   1 
ATOM   872  O  O   . VAL A 1 109 ? -10.150 -15.402 26.677  1.00 12.06  ? 109 VAL A O   1 
ATOM   873  C  CB  . VAL A 1 109 ? -11.743 -13.024 25.908  1.00 12.09  ? 109 VAL A CB  1 
ATOM   874  C  CG1 . VAL A 1 109 ? -12.730 -13.122 27.047  1.00 14.10  ? 109 VAL A CG1 1 
ATOM   875  C  CG2 . VAL A 1 109 ? -12.000 -11.746 25.105  1.00 13.24  ? 109 VAL A CG2 1 
ATOM   876  N  N   . ASP A 1 110 ? -9.491  -14.180 28.450  1.00 11.87  ? 110 ASP A N   1 
ATOM   877  C  CA  . ASP A 1 110 ? -9.030  -15.369 29.183  1.00 13.21  ? 110 ASP A CA  1 
ATOM   878  C  C   . ASP A 1 110 ? -8.064  -16.186 28.320  1.00 13.11  ? 110 ASP A C   1 
ATOM   879  O  O   . ASP A 1 110 ? -8.135  -17.405 28.280  1.00 14.44  ? 110 ASP A O   1 
ATOM   880  C  CB  . ASP A 1 110 ? -10.207 -16.182 29.692  1.00 15.63  ? 110 ASP A CB  1 
ATOM   881  C  CG  . ASP A 1 110 ? -11.029 -15.435 30.704  1.00 15.62  ? 110 ASP A CG  1 
ATOM   882  O  OD1 . ASP A 1 110 ? -10.502 -14.557 31.368  1.00 17.58  ? 110 ASP A OD1 1 
ATOM   883  O  OD2 . ASP A 1 110 ? -12.226 -15.731 30.761  1.00 19.94  ? 110 ASP A OD2 1 
ATOM   884  N  N   . LYS A 1 111 ? -7.183  -15.486 27.600  1.00 12.21  ? 111 LYS A N   1 
ATOM   885  C  CA  . LYS A 1 111 ? -6.162  -16.021 26.712  1.00 13.13  ? 111 LYS A CA  1 
ATOM   886  C  C   . LYS A 1 111 ? -6.709  -16.514 25.382  1.00 12.91  ? 111 LYS A C   1 
ATOM   887  O  O   . LYS A 1 111 ? -5.923  -16.858 24.512  1.00 13.99  ? 111 LYS A O   1 
ATOM   888  C  CB  . LYS A 1 111 ? -5.267  -17.065 27.383  1.00 14.38  ? 111 LYS A CB  1 
ATOM   889  C  CG  . LYS A 1 111 ? -4.602  -16.584 28.661  1.00 17.75  ? 111 LYS A CG  1 
ATOM   890  C  CD  . LYS A 1 111 ? -3.578  -15.512 28.370  1.00 22.23  ? 111 LYS A CD  1 
ATOM   891  C  CE  . LYS A 1 111 ? -2.912  -14.923 29.594  1.00 31.21  ? 111 LYS A CE  1 
ATOM   892  N  NZ  . LYS A 1 111 ? -1.483  -15.312 29.641  1.00 32.63  ? 111 LYS A NZ  1 
ATOM   893  N  N   . LYS A 1 112 ? -8.030  -16.513 25.192  1.00 11.41  ? 112 LYS A N   1 
ATOM   894  C  CA  . LYS A 1 112 ? -8.563  -16.936 23.901  1.00 12.84  ? 112 LYS A CA  1 
ATOM   895  C  C   . LYS A 1 112 ? -8.283  -15.861 22.850  1.00 11.11  ? 112 LYS A C   1 
ATOM   896  O  O   . LYS A 1 112 ? -8.553  -14.677 23.076  1.00 11.68  ? 112 LYS A O   1 
ATOM   897  C  CB  . LYS A 1 112 ? -10.090 -17.062 24.011  1.00 14.49  ? 112 LYS A CB  1 
ATOM   898  C  CG  . LYS A 1 112 ? -10.759 -17.381 22.674  1.00 17.10  ? 112 LYS A CG  1 
ATOM   899  C  CD  . LYS A 1 112 ? -12.267 -17.414 22.693  1.00 19.12  ? 112 LYS A CD  1 
ATOM   900  C  CE  . LYS A 1 112 ? -12.709 -17.593 21.271  1.00 24.23  ? 112 LYS A CE  1 
ATOM   901  N  NZ  . LYS A 1 112 ? -12.586 -18.975 20.791  1.00 27.38  ? 112 LYS A NZ  1 
ATOM   902  N  N   A LYS A 1 113 ? -7.781  -16.327 21.707  0.50 11.06  ? 113 LYS A N   1 
ATOM   903  N  N   B LYS A 1 113 ? -7.737  -16.304 21.723  0.50 10.84  ? 113 LYS A N   1 
ATOM   904  C  CA  A LYS A 1 113 ? -7.543  -15.521 20.525  0.50 12.48  ? 113 LYS A CA  1 
ATOM   905  C  CA  B LYS A 1 113 ? -7.556  -15.518 20.528  0.50 12.20  ? 113 LYS A CA  1 
ATOM   906  C  C   A LYS A 1 113 ? -8.671  -15.761 19.547  0.50 12.09  ? 113 LYS A C   1 
ATOM   907  C  C   B LYS A 1 113 ? -8.719  -15.766 19.597  0.50 11.75  ? 113 LYS A C   1 
ATOM   908  O  O   A LYS A 1 113 ? -9.045  -16.900 19.304  0.50 14.77  ? 113 LYS A O   1 
ATOM   909  O  O   B LYS A 1 113 ? -9.064  -16.904 19.314  0.50 15.61  ? 113 LYS A O   1 
ATOM   910  C  CB  A LYS A 1 113 ? -6.246  -15.910 19.815  0.50 12.13  ? 113 LYS A CB  1 
ATOM   911  C  CB  B LYS A 1 113 ? -6.250  -15.887 19.825  0.50 11.94  ? 113 LYS A CB  1 
ATOM   912  C  CG  A LYS A 1 113 ? -4.975  -15.598 20.590  0.50 13.36  ? 113 LYS A CG  1 
ATOM   913  C  CG  B LYS A 1 113 ? -5.018  -15.585 20.663  0.50 13.33  ? 113 LYS A CG  1 
ATOM   914  C  CD  A LYS A 1 113 ? -3.763  -16.227 19.950  0.50 14.53  ? 113 LYS A CD  1 
ATOM   915  C  CD  B LYS A 1 113 ? -3.740  -16.168 20.116  0.50 13.39  ? 113 LYS A CD  1 
ATOM   916  C  CE  A LYS A 1 113 ? -2.456  -15.774 20.570  0.50 16.67  ? 113 LYS A CE  1 
ATOM   917  C  CE  B LYS A 1 113 ? -2.537  -15.452 20.706  0.50 16.18  ? 113 LYS A CE  1 
ATOM   918  N  NZ  A LYS A 1 113 ? -2.194  -16.465 21.855  0.50 16.31  ? 113 LYS A NZ  1 
ATOM   919  N  NZ  B LYS A 1 113 ? -1.295  -16.257 20.637  0.50 18.97  ? 113 LYS A NZ  1 
ATOM   920  N  N   . TYR A 1 114 ? -9.260  -14.669 19.067  1.00 10.02  ? 114 TYR A N   1 
ATOM   921  C  CA  . TYR A 1 114 ? -10.235 -14.737 18.011  1.00 10.81  ? 114 TYR A CA  1 
ATOM   922  C  C   . TYR A 1 114 ? -9.584  -14.699 16.650  1.00 9.62   ? 114 TYR A C   1 
ATOM   923  O  O   . TYR A 1 114 ? -8.372  -14.393 16.488  1.00 10.81  ? 114 TYR A O   1 
ATOM   924  C  CB  . TYR A 1 114 ? -11.298 -13.648 18.159  1.00 10.59  ? 114 TYR A CB  1 
ATOM   925  C  CG  . TYR A 1 114 ? -12.212 -13.858 19.311  1.00 10.01  ? 114 TYR A CG  1 
ATOM   926  C  CD1 . TYR A 1 114 ? -11.874 -13.421 20.581  1.00 12.33  ? 114 TYR A CD1 1 
ATOM   927  C  CD2 . TYR A 1 114 ? -13.430 -14.497 19.150  1.00 11.73  ? 114 TYR A CD2 1 
ATOM   928  C  CE1 . TYR A 1 114 ? -12.720 -13.613 21.661  1.00 14.71  ? 114 TYR A CE1 1 
ATOM   929  C  CE2 . TYR A 1 114 ? -14.289 -14.697 20.219  1.00 14.73  ? 114 TYR A CE2 1 
ATOM   930  C  CZ  . TYR A 1 114 ? -13.933 -14.253 21.479  1.00 15.62  ? 114 TYR A CZ  1 
ATOM   931  O  OH  . TYR A 1 114 ? -14.773 -14.446 22.538  1.00 22.16  ? 114 TYR A OH  1 
ATOM   932  N  N   . ALA A 1 115 ? -10.341 -15.001 15.590  1.00 10.23  ? 115 ALA A N   1 
ATOM   933  C  CA  . ALA A 1 115 ? -9.812  -15.056 14.232  1.00 9.83   ? 115 ALA A CA  1 
ATOM   934  C  C   . ALA A 1 115 ? -9.425  -13.657 13.749  1.00 10.54  ? 115 ALA A C   1 
ATOM   935  O  O   . ALA A 1 115 ? -8.550  -13.531 12.863  1.00 10.60  ? 115 ALA A O   1 
ATOM   936  C  CB  . ALA A 1 115 ? -10.812 -15.673 13.310  1.00 11.54  ? 115 ALA A CB  1 
ATOM   937  N  N   . ALA A 1 116 ? -10.084 -12.617 14.245  1.00 9.32   ? 116 ALA A N   1 
ATOM   938  C  CA  . ALA A 1 116 ? -9.766  -11.265 13.799  1.00 9.11   ? 116 ALA A CA  1 
ATOM   939  C  C   . ALA A 1 116 ? -10.359 -10.312 14.807  1.00 8.39   ? 116 ALA A C   1 
ATOM   940  O  O   . ALA A 1 116 ? -11.102 -10.688 15.696  1.00 8.82   ? 116 ALA A O   1 
ATOM   941  C  CB  . ALA A 1 116 ? -10.326 -10.999 12.385  1.00 10.08  ? 116 ALA A CB  1 
ATOM   942  N  N   . GLU A 1 117 ? -10.005 -9.028  14.633  1.00 9.29   ? 117 GLU A N   1 
ATOM   943  C  CA  . GLU A 1 117 ? -10.520 -7.977  15.496  1.00 8.62   ? 117 GLU A CA  1 
ATOM   944  C  C   . GLU A 1 117 ? -10.695 -6.738  14.645  1.00 8.60   ? 117 GLU A C   1 
ATOM   945  O  O   . GLU A 1 117 ? -9.815  -6.364  13.897  1.00 9.20   ? 117 GLU A O   1 
ATOM   946  C  CB  . GLU A 1 117 ? -9.572  -7.709  16.668  1.00 9.20   ? 117 GLU A CB  1 
ATOM   947  C  CG  . GLU A 1 117 ? -10.135 -6.822  17.760  1.00 9.34   ? 117 GLU A CG  1 
ATOM   948  C  CD  . GLU A 1 117 ? -9.206  -6.752  18.961  1.00 9.42   ? 117 GLU A CD  1 
ATOM   949  O  OE1 . GLU A 1 117 ? -8.526  -7.770  19.249  1.00 9.72   ? 117 GLU A OE1 1 
ATOM   950  O  OE2 . GLU A 1 117 ? -9.183  -5.697  19.631  1.00 10.18  ? 117 GLU A OE2 1 
ATOM   951  N  N   . LEU A 1 118 ? -11.886 -6.163  14.759  1.00 7.99   ? 118 LEU A N   1 
ATOM   952  C  CA  . LEU A 1 118 ? -12.256 -4.910  14.063  1.00 8.29   ? 118 LEU A CA  1 
ATOM   953  C  C   . LEU A 1 118 ? -12.050 -3.768  15.063  1.00 7.35   ? 118 LEU A C   1 
ATOM   954  O  O   . LEU A 1 118 ? -12.466 -3.853  16.207  1.00 7.78   ? 118 LEU A O   1 
ATOM   955  C  CB  . LEU A 1 118 ? -13.736 -5.018  13.688  1.00 9.43   ? 118 LEU A CB  1 
ATOM   956  C  CG  . LEU A 1 118 ? -14.475 -3.712  13.349  1.00 8.99   ? 118 LEU A CG  1 
ATOM   957  C  CD1 . LEU A 1 118 ? -13.871 -3.031  12.127  1.00 9.68   ? 118 LEU A CD1 1 
ATOM   958  C  CD2 . LEU A 1 118 ? -15.937 -4.032  13.083  1.00 10.26  ? 118 LEU A CD2 1 
ATOM   959  N  N   . HIS A 1 119 ? -11.411 -2.700  14.560  1.00 7.78   ? 119 HIS A N   1 
ATOM   960  C  CA  . HIS A 1 119 ? -11.193 -1.493  15.351  1.00 7.87   ? 119 HIS A CA  1 
ATOM   961  C  C   . HIS A 1 119 ? -11.814 -0.304  14.659  1.00 7.65   ? 119 HIS A C   1 
ATOM   962  O  O   . HIS A 1 119 ? -11.429 0.022   13.542  1.00 8.26   ? 119 HIS A O   1 
ATOM   963  C  CB  . HIS A 1 119 ? -9.694  -1.223  15.511  1.00 8.41   ? 119 HIS A CB  1 
ATOM   964  C  CG  . HIS A 1 119 ? -9.047  -2.240  16.407  1.00 7.75   ? 119 HIS A CG  1 
ATOM   965  N  ND1 . HIS A 1 119 ? -7.719  -2.480  16.372  1.00 8.35   ? 119 HIS A ND1 1 
ATOM   966  C  CD2 . HIS A 1 119 ? -9.606  -3.006  17.366  1.00 8.62   ? 119 HIS A CD2 1 
ATOM   967  C  CE1 . HIS A 1 119 ? -7.438  -3.385  17.325  1.00 8.51   ? 119 HIS A CE1 1 
ATOM   968  N  NE2 . HIS A 1 119 ? -8.571  -3.741  17.917  1.00 8.52   ? 119 HIS A NE2 1 
ATOM   969  N  N   . LEU A 1 120 ? -12.775 0.313   15.336  1.00 7.28   ? 120 LEU A N   1 
ATOM   970  C  CA  . LEU A 1 120 ? -13.394 1.543   14.885  1.00 8.52   ? 120 LEU A CA  1 
ATOM   971  C  C   . LEU A 1 120 ? -12.759 2.681   15.684  1.00 7.31   ? 120 LEU A C   1 
ATOM   972  O  O   . LEU A 1 120 ? -12.899 2.707   16.902  1.00 7.58   ? 120 LEU A O   1 
ATOM   973  C  CB  . LEU A 1 120 ? -14.901 1.477   15.074  1.00 9.14   ? 120 LEU A CB  1 
ATOM   974  C  CG  . LEU A 1 120 ? -15.597 0.437   14.186  1.00 9.20   ? 120 LEU A CG  1 
ATOM   975  C  CD1 . LEU A 1 120 ? -16.391 -0.546  15.025  1.00 14.17  ? 120 LEU A CD1 1 
ATOM   976  C  CD2 . LEU A 1 120 ? -16.422 1.104   13.100  1.00 11.03  ? 120 LEU A CD2 1 
ATOM   977  N  N   . VAL A 1 121 ? -12.021 3.532   15.015  1.00 8.40   ? 121 VAL A N   1 
ATOM   978  C  CA  . VAL A 1 121 ? -11.180 4.551   15.649  1.00 8.26   ? 121 VAL A CA  1 
ATOM   979  C  C   . VAL A 1 121 ? -11.887 5.894   15.660  1.00 8.27   ? 121 VAL A C   1 
ATOM   980  O  O   . VAL A 1 121 ? -12.294 6.364   14.598  1.00 9.51   ? 121 VAL A O   1 
ATOM   981  C  CB  . VAL A 1 121 ? -9.830  4.674   14.919  1.00 8.91   ? 121 VAL A CB  1 
ATOM   982  C  CG1 . VAL A 1 121 ? -8.946  5.719   15.630  1.00 10.36  ? 121 VAL A CG1 1 
ATOM   983  C  CG2 . VAL A 1 121 ? -9.108  3.337   14.855  1.00 10.17  ? 121 VAL A CG2 1 
ATOM   984  N  N   . HIS A 1 122 ? -12.003 6.475   16.852  1.00 8.92   ? 122 HIS A N   1 
ATOM   985  C  CA  . HIS A 1 122 ? -12.709 7.729   17.024  1.00 9.53   ? 122 HIS A CA  1 
ATOM   986  C  C   . HIS A 1 122 ? -11.836 8.711   17.776  1.00 9.77   ? 122 HIS A C   1 
ATOM   987  O  O   . HIS A 1 122 ? -11.040 8.311   18.627  1.00 10.21  ? 122 HIS A O   1 
ATOM   988  C  CB  . HIS A 1 122 ? -13.981 7.535   17.881  1.00 9.87   ? 122 HIS A CB  1 
ATOM   989  C  CG  . HIS A 1 122 ? -14.868 6.417   17.459  1.00 9.25   ? 122 HIS A CG  1 
ATOM   990  N  ND1 . HIS A 1 122 ? -14.559 5.112   17.679  1.00 9.42   ? 122 HIS A ND1 1 
ATOM   991  C  CD2 . HIS A 1 122 ? -16.076 6.383   16.863  1.00 10.41  ? 122 HIS A CD2 1 
ATOM   992  C  CE1 . HIS A 1 122 ? -15.551 4.347   17.246  1.00 10.04  ? 122 HIS A CE1 1 
ATOM   993  N  NE2 . HIS A 1 122 ? -16.503 5.086   16.707  1.00 10.39  ? 122 HIS A NE2 1 
ATOM   994  N  N   . TRP A 1 123 ? -12.005 10.012  17.506  1.00 9.61   ? 123 TRP A N   1 
ATOM   995  C  CA  . TRP A 1 123 ? -11.220 11.034  18.194  1.00 9.66   ? 123 TRP A CA  1 
ATOM   996  C  C   . TRP A 1 123 ? -12.120 11.992  18.939  1.00 10.47  ? 123 TRP A C   1 
ATOM   997  O  O   . TRP A 1 123 ? -13.199 12.346  18.486  1.00 12.68  ? 123 TRP A O   1 
ATOM   998  C  CB  . TRP A 1 123 ? -10.265 11.763  17.240  1.00 11.35  ? 123 TRP A CB  1 
ATOM   999  C  CG  . TRP A 1 123 ? -10.942 12.364  16.048  1.00 12.48  ? 123 TRP A CG  1 
ATOM   1000 C  CD1 . TRP A 1 123 ? -11.115 11.740  14.850  1.00 14.59  ? 123 TRP A CD1 1 
ATOM   1001 C  CD2 . TRP A 1 123 ? -11.397 13.719  15.869  1.00 13.46  ? 123 TRP A CD2 1 
ATOM   1002 N  NE1 . TRP A 1 123 ? -11.680 12.570  13.930  1.00 15.67  ? 123 TRP A NE1 1 
ATOM   1003 C  CE2 . TRP A 1 123 ? -11.854 13.805  14.522  1.00 15.63  ? 123 TRP A CE2 1 
ATOM   1004 C  CE3 . TRP A 1 123 ? -11.420 14.853  16.676  1.00 14.91  ? 123 TRP A CE3 1 
ATOM   1005 C  CZ2 . TRP A 1 123 ? -12.393 14.982  14.004  1.00 18.64  ? 123 TRP A CZ2 1 
ATOM   1006 C  CZ3 . TRP A 1 123 ? -11.954 16.004  16.151  1.00 15.97  ? 123 TRP A CZ3 1 
ATOM   1007 C  CH2 . TRP A 1 123 ? -12.417 16.077  14.828  1.00 17.97  ? 123 TRP A CH2 1 
ATOM   1008 N  N   . ASN A 1 124 ? -11.593 12.468  20.057  1.00 11.04  ? 124 ASN A N   1 
ATOM   1009 C  CA  . ASN A 1 124 ? -12.333 13.357  20.951  1.00 12.91  ? 124 ASN A CA  1 
ATOM   1010 C  C   . ASN A 1 124 ? -12.419 14.729  20.297  1.00 12.21  ? 124 ASN A C   1 
ATOM   1011 O  O   . ASN A 1 124 ? -11.400 15.363  20.043  1.00 12.35  ? 124 ASN A O   1 
ATOM   1012 C  CB  . ASN A 1 124 ? -11.537 13.410  22.266  1.00 13.18  ? 124 ASN A CB  1 
ATOM   1013 C  CG  . ASN A 1 124 ? -12.267 14.047  23.390  1.00 14.59  ? 124 ASN A CG  1 
ATOM   1014 O  OD1 . ASN A 1 124 ? -13.081 14.972  23.151  1.00 15.46  ? 124 ASN A OD1 1 
ATOM   1015 N  ND2 . ASN A 1 124 ? -11.973 13.627  24.612  1.00 15.14  ? 124 ASN A ND2 1 
ATOM   1016 N  N   . THR A 1 125 ? -13.639 15.184  20.071  1.00 13.91  ? 125 THR A N   1 
ATOM   1017 C  CA  . THR A 1 125 ? -13.828 16.430  19.304  1.00 15.39  ? 125 THR A CA  1 
ATOM   1018 C  C   . THR A 1 125 ? -13.295 17.628  20.083  1.00 15.06  ? 125 THR A C   1 
ATOM   1019 O  O   . THR A 1 125 ? -13.096 18.679  19.511  1.00 18.09  ? 125 THR A O   1 
ATOM   1020 C  CB  . THR A 1 125 ? -15.317 16.626  19.000  1.00 19.41  ? 125 THR A CB  1 
ATOM   1021 O  OG1 . THR A 1 125 ? -16.049 16.664  20.232  1.00 22.10  ? 125 THR A OG1 1 
ATOM   1022 C  CG2 . THR A 1 125 ? -15.812 15.527  18.081  1.00 22.25  ? 125 THR A CG2 1 
ATOM   1023 N  N   . LYS A 1 126 ? -13.037 17.508  21.447  1.00 15.39  ? 127 LYS A N   1 
ATOM   1024 C  CA  . LYS A 1 126 ? -12.468 18.659  22.161  1.00 18.83  ? 127 LYS A CA  1 
ATOM   1025 C  C   . LYS A 1 126 ? -11.059 18.969  21.658  1.00 16.55  ? 127 LYS A C   1 
ATOM   1026 O  O   . LYS A 1 126 ? -10.573 20.066  21.922  1.00 19.42  ? 127 LYS A O   1 
ATOM   1027 C  CB  . LYS A 1 126 ? -12.599 18.447  23.670  1.00 21.54  ? 127 LYS A CB  1 
ATOM   1028 C  CG  . LYS A 1 126 ? -11.508 17.593  24.264  1.00 20.74  ? 127 LYS A CG  1 
ATOM   1029 C  CD  . LYS A 1 126 ? -11.831 17.342  25.719  1.00 26.74  ? 127 LYS A CD  1 
ATOM   1030 C  CE  . LYS A 1 126 ? -10.832 16.430  26.360  1.00 30.44  ? 127 LYS A CE  1 
ATOM   1031 N  NZ  . LYS A 1 126 ? -10.970 16.331  27.835  1.00 43.58  ? 127 LYS A NZ  1 
ATOM   1032 N  N   . TYR A 1 127 ? -10.404 18.087  20.875  1.00 13.09  ? 128 TYR A N   1 
ATOM   1033 C  CA  . TYR A 1 127 ? -9.063  18.315  20.367  1.00 12.75  ? 128 TYR A CA  1 
ATOM   1034 C  C   . TYR A 1 127 ? -9.067  18.667  18.881  1.00 13.19  ? 128 TYR A C   1 
ATOM   1035 O  O   . TYR A 1 127 ? -7.999  18.879  18.299  1.00 14.46  ? 128 TYR A O   1 
ATOM   1036 C  CB  . TYR A 1 127 ? -8.111  17.135  20.630  1.00 13.54  ? 128 TYR A CB  1 
ATOM   1037 C  CG  . TYR A 1 127 ? -8.025  16.860  22.113  1.00 12.92  ? 128 TYR A CG  1 
ATOM   1038 C  CD1 . TYR A 1 127 ? -7.573  17.850  23.003  1.00 14.63  ? 128 TYR A CD1 1 
ATOM   1039 C  CD2 . TYR A 1 127 ? -8.383  15.629  22.621  1.00 12.79  ? 128 TYR A CD2 1 
ATOM   1040 C  CE1 . TYR A 1 127 ? -7.528  17.593  24.350  1.00 15.80  ? 128 TYR A CE1 1 
ATOM   1041 C  CE2 . TYR A 1 127 ? -8.301  15.346  23.989  1.00 13.28  ? 128 TYR A CE2 1 
ATOM   1042 C  CZ  . TYR A 1 127 ? -7.870  16.361  24.859  1.00 15.24  ? 128 TYR A CZ  1 
ATOM   1043 O  OH  . TYR A 1 127 ? -7.766  16.178  26.197  1.00 16.76  ? 128 TYR A OH  1 
ATOM   1044 N  N   . GLY A 1 128 ? -10.264 18.750  18.262  1.00 14.30  ? 129 GLY A N   1 
ATOM   1045 C  CA  . GLY A 1 128 ? -10.350 19.399  16.966  1.00 14.95  ? 129 GLY A CA  1 
ATOM   1046 C  C   . GLY A 1 128 ? -9.955  18.560  15.740  1.00 14.58  ? 129 GLY A C   1 
ATOM   1047 O  O   . GLY A 1 128 ? -10.532 18.690  14.670  1.00 18.16  ? 129 GLY A O   1 
ATOM   1048 N  N   . ASP A 1 129 ? -8.933  17.704  15.863  1.00 15.39  ? 130 ASP A N   1 
ATOM   1049 C  CA  . ASP A 1 129 ? -8.503  16.838  14.770  1.00 15.83  ? 130 ASP A CA  1 
ATOM   1050 C  C   . ASP A 1 129 ? -7.874  15.582  15.364  1.00 15.48  ? 130 ASP A C   1 
ATOM   1051 O  O   . ASP A 1 129 ? -7.473  15.584  16.516  1.00 15.90  ? 130 ASP A O   1 
ATOM   1052 C  CB  . ASP A 1 129 ? -7.524  17.544  13.790  1.00 17.98  ? 130 ASP A CB  1 
ATOM   1053 C  CG  . ASP A 1 129 ? -6.128  17.870  14.276  1.00 23.32  ? 130 ASP A CG  1 
ATOM   1054 O  OD1 . ASP A 1 129 ? -5.229  16.970  14.357  1.00 23.40  ? 130 ASP A OD1 1 
ATOM   1055 O  OD2 . ASP A 1 129 ? -5.849  19.090  14.425  1.00 25.63  ? 130 ASP A OD2 1 
ATOM   1056 N  N   . ALA A 1 130 ? -7.860  14.521  14.545  1.00 16.33  ? 131 ALA A N   1 
ATOM   1057 C  CA  . ALA A 1 130 ? -7.436  13.234  15.042  1.00 14.86  ? 131 ALA A CA  1 
ATOM   1058 C  C   . ALA A 1 130 ? -5.954  13.242  15.394  1.00 13.89  ? 131 ALA A C   1 
ATOM   1059 O  O   . ALA A 1 130 ? -5.582  12.570  16.351  1.00 13.58  ? 131 ALA A O   1 
ATOM   1060 C  CB  . ALA A 1 130 ? -7.716  12.215  13.957  1.00 16.48  ? 131 ALA A CB  1 
ATOM   1061 N  N   . GLY A 1 131 ? -5.111  13.960  14.611  1.00 16.42  ? 132 GLY A N   1 
ATOM   1062 C  CA  . GLY A 1 131 ? -3.678  14.004  14.947  1.00 17.52  ? 132 GLY A CA  1 
ATOM   1063 C  C   . GLY A 1 131 ? -3.481  14.633  16.307  1.00 13.97  ? 132 GLY A C   1 
ATOM   1064 O  O   . GLY A 1 131 ? -2.720  14.121  17.134  1.00 16.89  ? 132 GLY A O   1 
ATOM   1065 N  N   . LYS A 1 132 ? -4.099  15.800  16.528  1.00 15.85  ? 133 LYS A N   1 
ATOM   1066 C  CA  . LYS A 1 132 ? -3.921  16.430  17.814  1.00 14.77  ? 133 LYS A CA  1 
ATOM   1067 C  C   . LYS A 1 132 ? -4.486  15.560  18.909  1.00 12.63  ? 133 LYS A C   1 
ATOM   1068 O  O   . LYS A 1 132 ? -3.918  15.469  19.988  1.00 13.73  ? 133 LYS A O   1 
ATOM   1069 C  CB  . LYS A 1 132 ? -4.602  17.811  17.819  1.00 16.31  ? 133 LYS A CB  1 
ATOM   1070 C  CG  . LYS A 1 132 ? -3.965  18.881  16.967  1.00 23.11  ? 133 LYS A CG  1 
ATOM   1071 C  CD  . LYS A 1 132 ? -2.507  19.202  17.283  1.00 31.69  ? 133 LYS A CD  1 
ATOM   1072 N  N   . ALA A 1 133 ? -5.624  14.910  18.628  1.00 11.81  ? 134 ALA A N   1 
ATOM   1073 C  CA  . ALA A 1 133 ? -6.203  14.048  19.641  1.00 11.69  ? 134 ALA A CA  1 
ATOM   1074 C  C   . ALA A 1 133 ? -5.224  12.936  20.039  1.00 11.24  ? 134 ALA A C   1 
ATOM   1075 O  O   . ALA A 1 133 ? -5.176  12.557  21.183  1.00 11.57  ? 134 ALA A O   1 
ATOM   1076 C  CB  . ALA A 1 133 ? -7.520  13.450  19.156  1.00 11.49  ? 134 ALA A CB  1 
ATOM   1077 N  N   . SER A 1 134 ? -4.464  12.430  19.079  1.00 11.69  ? 135 SER A N   1 
ATOM   1078 C  CA  . SER A 1 134 ? -3.572  11.304  19.362  1.00 11.63  ? 135 SER A CA  1 
ATOM   1079 C  C   . SER A 1 134 ? -2.422  11.704  20.284  1.00 12.49  ? 135 SER A C   1 
ATOM   1080 O  O   . SER A 1 134 ? -1.697  10.823  20.746  1.00 14.06  ? 135 SER A O   1 
ATOM   1081 C  CB  . SER A 1 134 ? -3.070  10.691  18.119  1.00 14.21  ? 135 SER A CB  1 
ATOM   1082 O  OG  . SER A 1 134 ? -2.071  11.493  17.481  1.00 15.63  ? 135 SER A OG  1 
ATOM   1083 N  N   . GLN A 1 135 ? -2.253  12.998  20.539  1.00 12.25  ? 136 GLN A N   1 
ATOM   1084 C  CA  . GLN A 1 135 ? -1.220  13.486  21.455  1.00 13.57  ? 136 GLN A CA  1 
ATOM   1085 C  C   . GLN A 1 135 ? -1.743  13.648  22.880  1.00 13.31  ? 136 GLN A C   1 
ATOM   1086 O  O   . GLN A 1 135 ? -1.028  14.183  23.734  1.00 18.25  ? 136 GLN A O   1 
ATOM   1087 C  CB  . GLN A 1 135 ? -0.666  14.838  20.966  1.00 17.90  ? 136 GLN A CB  1 
ATOM   1088 C  CG  . GLN A 1 135 ? -0.220  14.803  19.542  1.00 20.72  ? 136 GLN A CG  1 
ATOM   1089 C  CD  . GLN A 1 135 ? 0.828   13.769  19.248  1.00 28.71  ? 136 GLN A CD  1 
ATOM   1090 O  OE1 . GLN A 1 135 ? 1.738   13.515  20.042  1.00 41.87  ? 136 GLN A OE1 1 
ATOM   1091 N  NE2 . GLN A 1 135 ? 0.689   13.144  18.105  1.00 39.00  ? 136 GLN A NE2 1 
ATOM   1092 N  N   . GLN A 1 136 ? -2.990  13.234  23.148  1.00 12.50  ? 137 GLN A N   1 
ATOM   1093 C  CA  . GLN A 1 136 ? -3.626  13.492  24.447  1.00 12.58  ? 137 GLN A CA  1 
ATOM   1094 C  C   . GLN A 1 136 ? -3.964  12.168  25.084  1.00 12.04  ? 137 GLN A C   1 
ATOM   1095 O  O   . GLN A 1 136 ? -4.386  11.229  24.391  1.00 12.62  ? 137 GLN A O   1 
ATOM   1096 C  CB  . GLN A 1 136 ? -4.904  14.307  24.272  1.00 14.13  ? 137 GLN A CB  1 
ATOM   1097 C  CG  . GLN A 1 136 ? -4.705  15.567  23.440  1.00 17.61  ? 137 GLN A CG  1 
ATOM   1098 C  CD  . GLN A 1 136 ? -3.652  16.469  24.017  1.00 22.59  ? 137 GLN A CD  1 
ATOM   1099 O  OE1 . GLN A 1 136 ? -3.493  16.553  25.218  1.00 20.18  ? 137 GLN A OE1 1 
ATOM   1100 N  NE2 . GLN A 1 136 ? -2.963  17.193  23.140  1.00 30.63  ? 137 GLN A NE2 1 
ATOM   1101 N  N   . PRO A 1 137 ? -3.946  12.098  26.427  1.00 13.13  ? 138 PRO A N   1 
ATOM   1102 C  CA  . PRO A 1 137 ? -4.214  10.843  27.097  1.00 14.46  ? 138 PRO A CA  1 
ATOM   1103 C  C   . PRO A 1 137 ? -5.630  10.333  26.919  1.00 14.36  ? 138 PRO A C   1 
ATOM   1104 O  O   . PRO A 1 137 ? -5.832  9.140   27.060  1.00 18.60  ? 138 PRO A O   1 
ATOM   1105 C  CB  . PRO A 1 137 ? -3.915  11.166  28.573  1.00 19.70  ? 138 PRO A CB  1 
ATOM   1106 C  CG  . PRO A 1 137 ? -3.972  12.681  28.670  1.00 24.86  ? 138 PRO A CG  1 
ATOM   1107 C  CD  . PRO A 1 137 ? -3.478  13.154  27.333  1.00 17.74  ? 138 PRO A CD  1 
ATOM   1108 N  N   . ASP A 1 138 ? -6.591  11.240  26.657  1.00 12.62  ? 139 ASP A N   1 
ATOM   1109 C  CA  . ASP A 1 138 ? -8.004  10.911  26.431  1.00 13.61  ? 139 ASP A CA  1 
ATOM   1110 C  C   . ASP A 1 138 ? -8.373  11.292  25.007  1.00 11.35  ? 139 ASP A C   1 
ATOM   1111 O  O   . ASP A 1 138 ? -9.495  11.743  24.764  1.00 13.16  ? 139 ASP A O   1 
ATOM   1112 C  CB  . ASP A 1 138 ? -8.920  11.578  27.463  1.00 15.27  ? 139 ASP A CB  1 
ATOM   1113 C  CG  . ASP A 1 138 ? -8.819  13.069  27.447  1.00 16.72  ? 139 ASP A CG  1 
ATOM   1114 O  OD1 . ASP A 1 138 ? -7.879  13.647  26.837  1.00 16.70  ? 139 ASP A OD1 1 
ATOM   1115 O  OD2 . ASP A 1 138 ? -9.693  13.682  28.084  1.00 22.15  ? 139 ASP A OD2 1 
ATOM   1116 N  N   . GLY A 1 139 ? -7.442  11.173  24.056  1.00 10.04  ? 140 GLY A N   1 
ATOM   1117 C  CA  . GLY A 1 139 ? -7.700  11.678  22.731  1.00 10.53  ? 140 GLY A CA  1 
ATOM   1118 C  C   . GLY A 1 139 ? -8.533  10.781  21.834  1.00 9.04   ? 140 GLY A C   1 
ATOM   1119 O  O   . GLY A 1 139 ? -9.245  11.289  20.986  1.00 10.33  ? 140 GLY A O   1 
ATOM   1120 N  N   . LEU A 1 140 ? -8.329  9.473   21.941  1.00 9.39   ? 141 LEU A N   1 
ATOM   1121 C  CA  . LEU A 1 140 ? -8.985  8.522   21.048  1.00 8.56   ? 141 LEU A CA  1 
ATOM   1122 C  C   . LEU A 1 140 ? -9.803  7.543   21.854  1.00 8.85   ? 141 LEU A C   1 
ATOM   1123 O  O   . LEU A 1 140 ? -9.540  7.250   23.009  1.00 9.22   ? 141 LEU A O   1 
ATOM   1124 C  CB  . LEU A 1 140 ? -7.968  7.757   20.191  1.00 9.39   ? 141 LEU A CB  1 
ATOM   1125 C  CG  . LEU A 1 140 ? -7.023  8.568   19.354  1.00 11.68  ? 141 LEU A CG  1 
ATOM   1126 C  CD1 . LEU A 1 140 ? -6.135  7.628   18.531  1.00 11.95  ? 141 LEU A CD1 1 
ATOM   1127 C  CD2 . LEU A 1 140 ? -7.724  9.549   18.446  1.00 12.67  ? 141 LEU A CD2 1 
ATOM   1128 N  N   . ALA A 1 141 ? -10.837 7.004   21.174  1.00 8.85   ? 142 ALA A N   1 
ATOM   1129 C  CA  . ALA A 1 141 ? -11.597 5.876   21.701  1.00 9.54   ? 142 ALA A CA  1 
ATOM   1130 C  C   . ALA A 1 141 ? -11.683 4.901   20.581  1.00 8.81   ? 142 ALA A C   1 
ATOM   1131 O  O   . ALA A 1 141 ? -12.095 5.226   19.469  1.00 9.67   ? 142 ALA A O   1 
ATOM   1132 C  CB  . ALA A 1 141 ? -12.987 6.316   22.151  1.00 11.34  ? 142 ALA A CB  1 
ATOM   1133 N  N   . VAL A 1 142 ? -11.228 3.672   20.854  1.00 8.11   ? 143 VAL A N   1 
ATOM   1134 C  CA  . VAL A 1 142 ? -11.274 2.633   19.835  1.00 8.51   ? 143 VAL A CA  1 
ATOM   1135 C  C   . VAL A 1 142 ? -12.242 1.572   20.324  1.00 7.38   ? 143 VAL A C   1 
ATOM   1136 O  O   . VAL A 1 142 ? -12.131 1.083   21.439  1.00 8.48   ? 143 VAL A O   1 
ATOM   1137 C  CB  . VAL A 1 142 ? -9.891  2.045   19.505  1.00 9.04   ? 143 VAL A CB  1 
ATOM   1138 C  CG1 . VAL A 1 142 ? -10.062 1.022   18.382  1.00 9.97   ? 143 VAL A CG1 1 
ATOM   1139 C  CG2 . VAL A 1 142 ? -8.932  3.139   19.054  1.00 9.98   ? 143 VAL A CG2 1 
ATOM   1140 N  N   . LEU A 1 143 ? -13.262 1.328   19.473  1.00 8.35   ? 144 LEU A N   1 
ATOM   1141 C  CA  . LEU A 1 143 ? -14.225 0.295   19.724  1.00 8.93   ? 144 LEU A CA  1 
ATOM   1142 C  C   . LEU A 1 143 ? -13.732 -0.959  19.051  1.00 7.59   ? 144 LEU A C   1 
ATOM   1143 O  O   . LEU A 1 143 ? -13.553 -0.970  17.831  1.00 8.64   ? 144 LEU A O   1 
ATOM   1144 C  CB  . LEU A 1 143 ? -15.576 0.774   19.149  1.00 10.03  ? 144 LEU A CB  1 
ATOM   1145 C  CG  . LEU A 1 143 ? -16.761 -0.183  19.324  1.00 10.78  ? 144 LEU A CG  1 
ATOM   1146 C  CD1 . LEU A 1 143 ? -17.043 -0.382  20.790  1.00 13.04  ? 144 LEU A CD1 1 
ATOM   1147 C  CD2 . LEU A 1 143 ? -18.007 0.390   18.631  1.00 13.29  ? 144 LEU A CD2 1 
ATOM   1148 N  N   . GLY A 1 144 ? -13.486 -1.984  19.848  1.00 8.37   ? 145 GLY A N   1 
ATOM   1149 C  CA  . GLY A 1 144 ? -12.952 -3.243  19.345  1.00 8.90   ? 145 GLY A CA  1 
ATOM   1150 C  C   . GLY A 1 144 ? -14.017 -4.333  19.374  1.00 7.67   ? 145 GLY A C   1 
ATOM   1151 O  O   . GLY A 1 144 ? -14.733 -4.457  20.334  1.00 9.39   ? 145 GLY A O   1 
ATOM   1152 N  N   . ILE A 1 145 ? -14.043 -5.055  18.265  1.00 7.66   ? 146 ILE A N   1 
ATOM   1153 C  CA  . ILE A 1 145 ? -15.070 -6.110  18.085  1.00 8.83   ? 146 ILE A CA  1 
ATOM   1154 C  C   . ILE A 1 145 ? -14.341 -7.344  17.608  1.00 8.37   ? 146 ILE A C   1 
ATOM   1155 O  O   . ILE A 1 145 ? -13.632 -7.306  16.606  1.00 8.85   ? 146 ILE A O   1 
ATOM   1156 C  CB  . ILE A 1 145 ? -16.145 -5.633  17.091  1.00 9.27   ? 146 ILE A CB  1 
ATOM   1157 C  CG1 . ILE A 1 145 ? -16.790 -4.355  17.576  1.00 11.12  ? 146 ILE A CG1 1 
ATOM   1158 C  CG2 . ILE A 1 145 ? -17.155 -6.747  16.836  1.00 11.43  ? 146 ILE A CG2 1 
ATOM   1159 C  CD1 . ILE A 1 145 ? -17.821 -3.759  16.665  1.00 12.13  ? 146 ILE A CD1 1 
ATOM   1160 N  N   . PHE A 1 146 ? -14.550 -8.455  18.298  1.00 8.25   ? 147 PHE A N   1 
ATOM   1161 C  CA  . PHE A 1 146 ? -13.934 -9.718  17.883  1.00 8.52   ? 147 PHE A CA  1 
ATOM   1162 C  C   . PHE A 1 146 ? -14.706 -10.359 16.751  1.00 8.94   ? 147 PHE A C   1 
ATOM   1163 O  O   . PHE A 1 146 ? -15.933 -10.217 16.659  1.00 10.01  ? 147 PHE A O   1 
ATOM   1164 C  CB  . PHE A 1 146 ? -13.970 -10.670 19.081  1.00 9.33   ? 147 PHE A CB  1 
ATOM   1165 C  CG  . PHE A 1 146 ? -13.124 -10.199 20.237  1.00 8.22   ? 147 PHE A CG  1 
ATOM   1166 C  CD1 . PHE A 1 146 ? -11.746 -10.051 20.049  1.00 10.02  ? 147 PHE A CD1 1 
ATOM   1167 C  CD2 . PHE A 1 146 ? -13.664 -9.940  21.477  1.00 9.61   ? 147 PHE A CD2 1 
ATOM   1168 C  CE1 . PHE A 1 146 ? -10.942 -9.681  21.117  1.00 9.47   ? 147 PHE A CE1 1 
ATOM   1169 C  CE2 . PHE A 1 146 ? -12.862 -9.535  22.549  1.00 10.07  ? 147 PHE A CE2 1 
ATOM   1170 C  CZ  . PHE A 1 146 ? -11.489 -9.437  22.340  1.00 9.92   ? 147 PHE A CZ  1 
ATOM   1171 N  N   . LEU A 1 147 ? -13.986 -11.045 15.898  1.00 9.09   ? 148 LEU A N   1 
ATOM   1172 C  CA  . LEU A 1 147 ? -14.583 -11.837 14.817  1.00 9.46   ? 148 LEU A CA  1 
ATOM   1173 C  C   . LEU A 1 147 ? -14.264 -13.299 15.066  1.00 9.53   ? 148 LEU A C   1 
ATOM   1174 O  O   . LEU A 1 147 ? -13.100 -13.671 15.278  1.00 10.53  ? 148 LEU A O   1 
ATOM   1175 C  CB  . LEU A 1 147 ? -14.011 -11.480 13.437  1.00 9.73   ? 148 LEU A CB  1 
ATOM   1176 C  CG  . LEU A 1 147 ? -14.542 -10.212 12.774  1.00 10.34  ? 148 LEU A CG  1 
ATOM   1177 C  CD1 . LEU A 1 147 ? -14.355 -8.951  13.649  1.00 11.63  ? 148 LEU A CD1 1 
ATOM   1178 C  CD2 . LEU A 1 147 ? -13.934 -10.041 11.413  1.00 10.38  ? 148 LEU A CD2 1 
ATOM   1179 N  N   . LYS A 1 148 ? -15.316 -14.145 15.030  1.00 10.47  ? 149 LYS A N   1 
ATOM   1180 C  CA  . LYS A 1 148 ? -15.147 -15.588 15.006  1.00 11.00  ? 149 LYS A CA  1 
ATOM   1181 C  C   . LYS A 1 148 ? -15.643 -16.084 13.656  1.00 11.29  ? 149 LYS A C   1 
ATOM   1182 O  O   . LYS A 1 148 ? -16.457 -15.439 13.007  1.00 12.29  ? 149 LYS A O   1 
ATOM   1183 C  CB  . LYS A 1 148 ? -15.870 -16.244 16.164  1.00 13.58  ? 149 LYS A CB  1 
ATOM   1184 C  CG  . LYS A 1 148 ? -17.376 -16.098 16.158  1.00 15.34  ? 149 LYS A CG  1 
ATOM   1185 C  CD  . LYS A 1 148 ? -18.027 -16.812 17.344  1.00 21.64  ? 149 LYS A CD  1 
ATOM   1186 C  CE  . LYS A 1 148 ? -19.518 -16.972 17.158  1.00 31.12  ? 149 LYS A CE  1 
ATOM   1187 N  NZ  . LYS A 1 148 ? -20.172 -17.430 18.417  1.00 42.21  ? 149 LYS A NZ  1 
ATOM   1188 N  N   . VAL A 1 149 ? -15.185 -17.276 13.287  1.00 12.12  ? 150 VAL A N   1 
ATOM   1189 C  CA  . VAL A 1 149 ? -15.524 -17.826 11.976  1.00 11.82  ? 150 VAL A CA  1 
ATOM   1190 C  C   . VAL A 1 149 ? -16.700 -18.797 12.120  1.00 13.23  ? 150 VAL A C   1 
ATOM   1191 O  O   . VAL A 1 149 ? -16.682 -19.747 12.921  1.00 15.18  ? 150 VAL A O   1 
ATOM   1192 C  CB  . VAL A 1 149 ? -14.320 -18.514 11.338  1.00 12.86  ? 150 VAL A CB  1 
ATOM   1193 C  CG1 . VAL A 1 149 ? -14.714 -19.243 10.053  1.00 15.42  ? 150 VAL A CG1 1 
ATOM   1194 C  CG2 . VAL A 1 149 ? -13.260 -17.483 11.086  1.00 15.85  ? 150 VAL A CG2 1 
ATOM   1195 N  N   . GLY A 1 150 ? -17.768 -18.505 11.388  1.00 12.60  ? 151 GLY A N   1 
ATOM   1196 C  CA  . GLY A 1 150 ? -18.944 -19.375 11.395  1.00 14.52  ? 151 GLY A CA  1 
ATOM   1197 C  C   . GLY A 1 150 ? -19.871 -18.878 10.300  1.00 13.13  ? 151 GLY A C   1 
ATOM   1198 O  O   . GLY A 1 150 ? -19.514 -18.945 9.142   1.00 13.05  ? 151 GLY A O   1 
ATOM   1199 N  N   A SER A 1 151 ? -21.053 -18.348 10.660  0.50 14.03  ? 152 SER A N   1 
ATOM   1200 N  N   B SER A 1 151 ? -21.032 -18.330 10.696  0.50 13.64  ? 152 SER A N   1 
ATOM   1201 C  CA  A SER A 1 151 ? -21.944 -17.793 9.632   0.50 13.95  ? 152 SER A CA  1 
ATOM   1202 C  CA  B SER A 1 151 ? -21.942 -17.717 9.727   0.50 14.85  ? 152 SER A CA  1 
ATOM   1203 C  C   A SER A 1 151 ? -21.422 -16.446 9.156   0.50 12.23  ? 152 SER A C   1 
ATOM   1204 C  C   B SER A 1 151 ? -21.284 -16.485 9.105   0.50 12.94  ? 152 SER A C   1 
ATOM   1205 O  O   A SER A 1 151 ? -20.788 -15.713 9.917   0.50 11.47  ? 152 SER A O   1 
ATOM   1206 O  O   B SER A 1 151 ? -20.407 -15.862 9.711   0.50 12.28  ? 152 SER A O   1 
ATOM   1207 C  CB  A SER A 1 151 ? -23.312 -17.594 10.179  0.50 17.67  ? 152 SER A CB  1 
ATOM   1208 C  CB  B SER A 1 151 ? -23.244 -17.361 10.399  0.50 15.74  ? 152 SER A CB  1 
ATOM   1209 O  OG  A SER A 1 151 ? -23.253 -16.712 11.290  0.50 20.27  ? 152 SER A OG  1 
ATOM   1210 O  OG  B SER A 1 151 ? -23.874 -18.527 10.921  0.50 22.03  ? 152 SER A OG  1 
ATOM   1211 N  N   . ALA A 1 152 ? -21.717 -16.113 7.895   1.00 12.10  ? 153 ALA A N   1 
ATOM   1212 C  CA  . ALA A 1 152 ? -21.260 -14.857 7.306   1.00 12.57  ? 153 ALA A CA  1 
ATOM   1213 C  C   . ALA A 1 152 ? -21.933 -13.665 7.979   1.00 11.42  ? 153 ALA A C   1 
ATOM   1214 O  O   . ALA A 1 152 ? -23.030 -13.730 8.505   1.00 14.09  ? 153 ALA A O   1 
ATOM   1215 C  CB  . ALA A 1 152 ? -21.609 -14.861 5.822   1.00 14.38  ? 153 ALA A CB  1 
ATOM   1216 N  N   . LYS A 1 153 ? -21.223 -12.536 7.908   1.00 11.23  ? 154 LYS A N   1 
ATOM   1217 C  CA  . LYS A 1 153 ? -21.752 -11.266 8.372   1.00 10.94  ? 154 LYS A CA  1 
ATOM   1218 C  C   . LYS A 1 153 ? -22.159 -10.505 7.101   1.00 11.25  ? 154 LYS A C   1 
ATOM   1219 O  O   . LYS A 1 153 ? -21.289 -10.060 6.321   1.00 11.04  ? 154 LYS A O   1 
ATOM   1220 C  CB  . LYS A 1 153 ? -20.647 -10.483 9.122   1.00 11.29  ? 154 LYS A CB  1 
ATOM   1221 C  CG  . LYS A 1 153 ? -21.196 -9.261  9.838   1.00 12.87  ? 154 LYS A CG  1 
ATOM   1222 C  CD  . LYS A 1 153 ? -22.113 -9.591  11.007  1.00 14.88  ? 154 LYS A CD  1 
ATOM   1223 C  CE  . LYS A 1 153 ? -22.304 -8.382  11.883  1.00 16.70  ? 154 LYS A CE  1 
ATOM   1224 N  NZ  . LYS A 1 153 ? -23.197 -8.718  12.984  1.00 21.57  ? 154 LYS A NZ  1 
ATOM   1225 N  N   . PRO A 1 154 ? -23.455 -10.336 6.813   1.00 11.32  ? 155 PRO A N   1 
ATOM   1226 C  CA  . PRO A 1 154 ? -23.801 -9.729  5.532   1.00 12.16  ? 155 PRO A CA  1 
ATOM   1227 C  C   . PRO A 1 154 ? -23.258 -8.322  5.384   1.00 11.44  ? 155 PRO A C   1 
ATOM   1228 O  O   . PRO A 1 154 ? -22.862 -7.970  4.295   1.00 12.44  ? 155 PRO A O   1 
ATOM   1229 C  CB  . PRO A 1 154 ? -25.351 -9.785  5.588   1.00 14.68  ? 155 PRO A CB  1 
ATOM   1230 C  CG  . PRO A 1 154 ? -25.637 -10.987 6.421   1.00 18.83  ? 155 PRO A CG  1 
ATOM   1231 C  CD  . PRO A 1 154 ? -24.627 -10.884 7.564   1.00 13.61  ? 155 PRO A CD  1 
ATOM   1232 N  N   . GLY A 1 155 ? -23.183 -7.578  6.481   1.00 11.90  ? 156 GLY A N   1 
ATOM   1233 C  CA  . GLY A 1 155 ? -22.692 -6.197  6.455   1.00 13.38  ? 156 GLY A CA  1 
ATOM   1234 C  C   . GLY A 1 155 ? -21.199 -6.081  6.159   1.00 11.73  ? 156 GLY A C   1 
ATOM   1235 O  O   . GLY A 1 155 ? -20.730 -4.974  5.927   1.00 14.12  ? 156 GLY A O   1 
ATOM   1236 N  N   . LEU A 1 156 ? -20.462 -7.182  6.240   1.00 10.09  ? 157 LEU A N   1 
ATOM   1237 C  CA  . LEU A 1 156 ? -19.060 -7.147  5.875   1.00 10.39  ? 157 LEU A CA  1 
ATOM   1238 C  C   . LEU A 1 156 ? -18.850 -7.366  4.396   1.00 9.28   ? 157 LEU A C   1 
ATOM   1239 O  O   . LEU A 1 156 ? -17.737 -7.147  3.857   1.00 10.65  ? 157 LEU A O   1 
ATOM   1240 C  CB  . LEU A 1 156 ? -18.371 -8.225  6.707   1.00 11.62  ? 157 LEU A CB  1 
ATOM   1241 C  CG  . LEU A 1 156 ? -16.842 -8.346  6.521   1.00 11.45  ? 157 LEU A CG  1 
ATOM   1242 C  CD1 . LEU A 1 156 ? -16.094 -7.042  6.863   1.00 12.98  ? 157 LEU A CD1 1 
ATOM   1243 C  CD2 . LEU A 1 156 ? -16.319 -9.503  7.360   1.00 12.51  ? 157 LEU A CD2 1 
ATOM   1244 N  N   . GLN A 1 157 ? -19.849 -7.928  3.674   1.00 10.10  ? 158 GLN A N   1 
ATOM   1245 C  CA  . GLN A 1 157 ? -19.582 -8.407  2.345   1.00 10.17  ? 158 GLN A CA  1 
ATOM   1246 C  C   . GLN A 1 157 ? -19.139 -7.300  1.396   1.00 10.66  ? 158 GLN A C   1 
ATOM   1247 O  O   . GLN A 1 157 ? -18.297 -7.544  0.539   1.00 10.85  ? 158 GLN A O   1 
ATOM   1248 C  CB  . GLN A 1 157 ? -20.806 -9.164  1.800   1.00 11.46  ? 158 GLN A CB  1 
ATOM   1249 C  CG  . GLN A 1 157 ? -20.444 -9.917  0.527   1.00 12.38  ? 158 GLN A CG  1 
ATOM   1250 C  CD  . GLN A 1 157 ? -19.440 -11.018 0.747   1.00 11.48  ? 158 GLN A CD  1 
ATOM   1251 O  OE1 . GLN A 1 157 ? -19.313 -11.550 1.870   1.00 12.23  ? 158 GLN A OE1 1 
ATOM   1252 N  NE2 . GLN A 1 157 ? -18.707 -11.296 -0.290  1.00 13.20  ? 158 GLN A NE2 1 
ATOM   1253 N  N   . LYS A 1 158 ? -19.672 -6.078  1.534   1.00 10.63  ? 159 LYS A N   1 
ATOM   1254 C  CA  . LYS A 1 158 ? -19.254 -5.001  0.634   1.00 12.28  ? 159 LYS A CA  1 
ATOM   1255 C  C   . LYS A 1 158 ? -17.749 -4.718  0.770   1.00 11.16  ? 159 LYS A C   1 
ATOM   1256 O  O   . LYS A 1 158 ? -17.114 -4.391  -0.213  1.00 12.43  ? 159 LYS A O   1 
ATOM   1257 C  CB  . LYS A 1 158 ? -20.077 -3.749  0.940   1.00 14.29  ? 159 LYS A CB  1 
ATOM   1258 C  CG  . LYS A 1 158 ? -19.841 -2.522  0.080   1.00 18.64  ? 159 LYS A CG  1 
ATOM   1259 C  CD  . LYS A 1 158 ? -20.868 -1.336  0.360   1.00 22.08  ? 159 LYS A CD  1 
ATOM   1260 C  CE  . LYS A 1 158 ? -20.486 -0.026  -0.330  1.00 30.22  ? 159 LYS A CE  1 
ATOM   1261 N  NZ  . LYS A 1 158 ? -20.853 -0.016  -1.777  1.00 27.66  ? 159 LYS A NZ  1 
ATOM   1262 N  N   . VAL A 1 159 ? -17.230 -4.846  2.007   1.00 10.74  ? 160 VAL A N   1 
ATOM   1263 C  CA  . VAL A 1 159 ? -15.813 -4.676  2.205   1.00 10.40  ? 160 VAL A CA  1 
ATOM   1264 C  C   . VAL A 1 159 ? -15.064 -5.811  1.513   1.00 10.32  ? 160 VAL A C   1 
ATOM   1265 O  O   . VAL A 1 159 ? -14.119 -5.559  0.768   1.00 11.99  ? 160 VAL A O   1 
ATOM   1266 C  CB  . VAL A 1 159 ? -15.494 -4.658  3.697   1.00 11.24  ? 160 VAL A CB  1 
ATOM   1267 C  CG1 . VAL A 1 159 ? -13.980 -4.776  3.909   1.00 13.56  ? 160 VAL A CG1 1 
ATOM   1268 C  CG2 . VAL A 1 159 ? -16.053 -3.418  4.338   1.00 14.40  ? 160 VAL A CG2 1 
ATOM   1269 N  N   . VAL A 1 160 ? -15.442 -7.047  1.817   1.00 10.07  ? 161 VAL A N   1 
ATOM   1270 C  CA  . VAL A 1 160 ? -14.613 -8.126  1.290   1.00 11.90  ? 161 VAL A CA  1 
ATOM   1271 C  C   . VAL A 1 160 ? -14.625 -8.140  -0.227  1.00 10.69  ? 161 VAL A C   1 
ATOM   1272 O  O   . VAL A 1 160 ? -13.611 -8.472  -0.837  1.00 12.05  ? 161 VAL A O   1 
ATOM   1273 C  CB  . VAL A 1 160 ? -14.742 -9.482  1.966   1.00 17.29  ? 161 VAL A CB  1 
ATOM   1274 C  CG1 . VAL A 1 160 ? -14.417 -9.404  3.441   1.00 21.95  ? 161 VAL A CG1 1 
ATOM   1275 C  CG2 . VAL A 1 160 ? -16.123 -9.890  1.772   1.00 17.25  ? 161 VAL A CG2 1 
ATOM   1276 N  N   . ASP A 1 161 ? -15.714 -7.762  -0.881  1.00 11.38  ? 162 ASP A N   1 
ATOM   1277 C  CA  . ASP A 1 161 ? -15.785 -7.820  -2.321  1.00 12.10  ? 162 ASP A CA  1 
ATOM   1278 C  C   . ASP A 1 161 ? -14.931 -6.779  -3.034  1.00 12.90  ? 162 ASP A C   1 
ATOM   1279 O  O   . ASP A 1 161 ? -14.681 -6.954  -4.214  1.00 16.10  ? 162 ASP A O   1 
ATOM   1280 C  CB  . ASP A 1 161 ? -17.244 -7.662  -2.735  1.00 14.69  ? 162 ASP A CB  1 
ATOM   1281 C  CG  . ASP A 1 161 ? -17.990 -8.988  -2.683  1.00 15.57  ? 162 ASP A CG  1 
ATOM   1282 O  OD1 . ASP A 1 161 ? -17.362 -10.071 -2.685  1.00 17.59  ? 162 ASP A OD1 1 
ATOM   1283 O  OD2 . ASP A 1 161 ? -19.211 -8.967  -2.642  1.00 17.19  ? 162 ASP A OD2 1 
ATOM   1284 N  N   A VAL A 1 162 ? -14.519 -5.729  -2.303  0.50 12.73  ? 163 VAL A N   1 
ATOM   1285 N  N   B VAL A 1 162 ? -14.435 -5.748  -2.354  0.50 12.00  ? 163 VAL A N   1 
ATOM   1286 C  CA  A VAL A 1 162 ? -13.662 -4.677  -2.834  0.50 13.48  ? 163 VAL A CA  1 
ATOM   1287 C  CA  B VAL A 1 162 ? -13.557 -4.813  -3.066  0.50 12.28  ? 163 VAL A CA  1 
ATOM   1288 C  C   A VAL A 1 162 ? -12.180 -4.977  -2.619  0.50 12.86  ? 163 VAL A C   1 
ATOM   1289 C  C   B VAL A 1 162 ? -12.097 -5.074  -2.750  0.50 11.34  ? 163 VAL A C   1 
ATOM   1290 O  O   A VAL A 1 162 ? -11.358 -4.245  -3.164  0.50 12.65  ? 163 VAL A O   1 
ATOM   1291 O  O   B VAL A 1 162 ? -11.232 -4.413  -3.333  0.50 12.87  ? 163 VAL A O   1 
ATOM   1292 C  CB  A VAL A 1 162 ? -14.042 -3.285  -2.268  0.50 15.36  ? 163 VAL A CB  1 
ATOM   1293 C  CB  B VAL A 1 162 ? -13.915 -3.340  -2.779  0.50 12.16  ? 163 VAL A CB  1 
ATOM   1294 C  CG1 A VAL A 1 162 ? -13.459 -3.020  -0.899  0.50 15.70  ? 163 VAL A CG1 1 
ATOM   1295 C  CG1 B VAL A 1 162 ? -15.358 -3.041  -3.209  0.50 14.06  ? 163 VAL A CG1 1 
ATOM   1296 C  CG2 A VAL A 1 162 ? -13.685 -2.155  -3.232  0.50 17.62  ? 163 VAL A CG2 1 
ATOM   1297 C  CG2 B VAL A 1 162 ? -13.645 -2.928  -1.341  0.50 13.23  ? 163 VAL A CG2 1 
ATOM   1298 N  N   . LEU A 1 163 ? -11.800 -5.993  -1.815  1.00 11.38  ? 164 LEU A N   1 
ATOM   1299 C  CA  . LEU A 1 163 ? -10.406 -6.186  -1.461  1.00 11.70  ? 164 LEU A CA  1 
ATOM   1300 C  C   . LEU A 1 163 ? -9.531  -6.545  -2.655  1.00 11.85  ? 164 LEU A C   1 
ATOM   1301 O  O   . LEU A 1 163 ? -8.340  -6.185  -2.649  1.00 12.44  ? 164 LEU A O   1 
ATOM   1302 C  CB  . LEU A 1 163 ? -10.293 -7.137  -0.299  1.00 11.43  ? 164 LEU A CB  1 
ATOM   1303 C  CG  . LEU A 1 163 ? -10.915 -6.730  1.016   1.00 11.54  ? 164 LEU A CG  1 
ATOM   1304 C  CD1 . LEU A 1 163 ? -10.675 -7.826  2.033   1.00 13.44  ? 164 LEU A CD1 1 
ATOM   1305 C  CD2 . LEU A 1 163 ? -10.344 -5.407  1.452   1.00 12.19  ? 164 LEU A CD2 1 
ATOM   1306 N  N   . ASP A 1 164 ? -10.046 -7.245  -3.660  1.00 12.69  ? 165 ASP A N   1 
ATOM   1307 C  CA  . ASP A 1 164 ? -9.228  -7.609  -4.797  1.00 15.41  ? 165 ASP A CA  1 
ATOM   1308 C  C   . ASP A 1 164 ? -8.748  -6.343  -5.531  1.00 15.11  ? 165 ASP A C   1 
ATOM   1309 O  O   . ASP A 1 164 ? -7.795  -6.396  -6.281  1.00 18.94  ? 165 ASP A O   1 
ATOM   1310 C  CB  . ASP A 1 164 ? -9.998  -8.480  -5.813  1.00 19.41  ? 165 ASP A CB  1 
ATOM   1311 C  CG  . ASP A 1 164 ? -11.050 -7.631  -6.542  1.00 22.85  ? 165 ASP A CG  1 
ATOM   1312 O  OD1 . ASP A 1 164 ? -12.079 -7.190  -5.881  1.00 27.07  ? 165 ASP A OD1 1 
ATOM   1313 O  OD2 . ASP A 1 164 ? -10.845 -7.388  -7.764  1.00 32.08  ? 165 ASP A OD2 1 
ATOM   1314 N  N   . SER A 1 165 ? -9.400  -5.182  -5.325  1.00 13.49  ? 166 SER A N   1 
ATOM   1315 C  CA  . SER A 1 165 ? -8.968  -3.945  -5.960  1.00 14.95  ? 166 SER A CA  1 
ATOM   1316 C  C   . SER A 1 165 ? -7.847  -3.218  -5.203  1.00 12.78  ? 166 SER A C   1 
ATOM   1317 O  O   . SER A 1 165 ? -7.376  -2.207  -5.722  1.00 15.05  ? 166 SER A O   1 
ATOM   1318 C  CB  . SER A 1 165 ? -10.136 -3.045  -6.253  1.00 16.32  ? 166 SER A CB  1 
ATOM   1319 O  OG  . SER A 1 165 ? -10.619 -2.454  -5.049  1.00 16.22  ? 166 SER A OG  1 
ATOM   1320 N  N   . ILE A 1 166 ? -7.603  -3.636  -3.977  1.00 11.72  ? 167 ILE A N   1 
ATOM   1321 C  CA  . ILE A 1 166 ? -6.553  -3.001  -3.152  1.00 12.49  ? 167 ILE A CA  1 
ATOM   1322 C  C   . ILE A 1 166 ? -5.541  -4.052  -2.652  1.00 11.90  ? 167 ILE A C   1 
ATOM   1323 O  O   . ILE A 1 166 ? -5.172  -4.068  -1.467  1.00 12.46  ? 167 ILE A O   1 
ATOM   1324 C  CB  . ILE A 1 166 ? -7.153  -2.157  -2.026  1.00 12.62  ? 167 ILE A CB  1 
ATOM   1325 C  CG1 . ILE A 1 166 ? -8.079  -2.951  -1.114  1.00 11.96  ? 167 ILE A CG1 1 
ATOM   1326 C  CG2 . ILE A 1 166 ? -7.914  -0.954  -2.638  1.00 14.01  ? 167 ILE A CG2 1 
ATOM   1327 C  CD1 . ILE A 1 166 ? -8.210  -2.245  0.233   1.00 13.51  ? 167 ILE A CD1 1 
ATOM   1328 N  N   . LYS A 1 167 ? -5.124  -4.976  -3.541  1.00 13.18  ? 168 LYS A N   1 
ATOM   1329 C  CA  . LYS A 1 167 ? -4.415  -6.155  -3.059  1.00 13.63  ? 168 LYS A CA  1 
ATOM   1330 C  C   . LYS A 1 167 ? -3.076  -5.779  -2.436  1.00 14.59  ? 168 LYS A C   1 
ATOM   1331 O  O   . LYS A 1 167 ? -2.684  -6.415  -1.464  1.00 15.42  ? 168 LYS A O   1 
ATOM   1332 C  CB  . LYS A 1 167 ? -4.190  -7.101  -4.248  1.00 17.55  ? 168 LYS A CB  1 
ATOM   1333 C  CG  . LYS A 1 167 ? -3.357  -8.327  -3.874  1.00 20.28  ? 168 LYS A CG  1 
ATOM   1334 C  CD  . LYS A 1 167 ? -3.158  -9.251  -5.087  1.00 22.71  ? 168 LYS A CD  1 
ATOM   1335 C  CE  . LYS A 1 167 ? -1.941  -10.152 -4.981  1.00 36.84  ? 168 LYS A CE  1 
ATOM   1336 N  NZ  . LYS A 1 167 ? -1.516  -10.608 -6.328  1.00 45.21  ? 168 LYS A NZ  1 
ATOM   1337 N  N   . THR A 1 168 ? -2.413  -4.740  -2.957  1.00 14.66  ? 169 THR A N   1 
ATOM   1338 C  CA  . THR A 1 168 ? -1.023  -4.529  -2.519  1.00 14.37  ? 169 THR A CA  1 
ATOM   1339 C  C   . THR A 1 168 ? -0.931  -3.130  -1.927  1.00 15.09  ? 169 THR A C   1 
ATOM   1340 O  O   . THR A 1 168 ? -1.801  -2.238  -2.070  1.00 14.04  ? 169 THR A O   1 
ATOM   1341 C  CB  . THR A 1 168 ? -0.103  -4.635  -3.730  1.00 16.60  ? 169 THR A CB  1 
ATOM   1342 O  OG1 . THR A 1 168 ? -0.625  -3.843  -4.808  1.00 18.25  ? 169 THR A OG1 1 
ATOM   1343 C  CG2 . THR A 1 168 ? 0.091   -6.062  -4.199  1.00 19.45  ? 169 THR A CG2 1 
ATOM   1344 N  N   . LYS A 1 169 ? 0.153   -2.971  -1.182  1.00 15.36  ? 170 LYS A N   1 
ATOM   1345 C  CA  . LYS A 1 169 ? 0.379   -1.751  -0.433  1.00 14.20  ? 170 LYS A CA  1 
ATOM   1346 C  C   . LYS A 1 169 ? 0.338   -0.560  -1.360  1.00 15.59  ? 170 LYS A C   1 
ATOM   1347 O  O   . LYS A 1 169 ? 0.964   -0.546  -2.442  1.00 17.60  ? 170 LYS A O   1 
ATOM   1348 C  CB  . LYS A 1 169 ? 1.805   -1.784  0.128   1.00 16.74  ? 170 LYS A CB  1 
ATOM   1349 C  CG  . LYS A 1 169 ? 2.222   -0.573  0.930   1.00 17.39  ? 170 LYS A CG  1 
ATOM   1350 C  CD  . LYS A 1 169 ? 3.652   -0.680  1.445   1.00 23.81  ? 170 LYS A CD  1 
ATOM   1351 C  CE  . LYS A 1 169 ? 4.148   0.646   1.982   1.00 32.50  ? 170 LYS A CE  1 
ATOM   1352 N  NZ  . LYS A 1 169 ? 5.634   0.738   2.013   1.00 41.30  ? 170 LYS A NZ  1 
ATOM   1353 N  N   . GLY A 1 170 ? -0.392  0.464   -0.928  1.00 14.24  ? 171 GLY A N   1 
ATOM   1354 C  CA  . GLY A 1 170 ? -0.486  1.721   -1.658  1.00 16.72  ? 171 GLY A CA  1 
ATOM   1355 C  C   . GLY A 1 170 ? -1.737  1.824   -2.513  1.00 17.35  ? 171 GLY A C   1 
ATOM   1356 O  O   . GLY A 1 170 ? -1.967  2.862   -3.075  1.00 20.58  ? 171 GLY A O   1 
ATOM   1357 N  N   . LYS A 1 171 ? -2.459  0.739   -2.734  1.00 14.03  ? 172 LYS A N   1 
ATOM   1358 C  CA  . LYS A 1 171 ? -3.683  0.822   -3.536  1.00 13.84  ? 172 LYS A CA  1 
ATOM   1359 C  C   . LYS A 1 171 ? -4.839  1.353   -2.679  1.00 12.71  ? 172 LYS A C   1 
ATOM   1360 O  O   . LYS A 1 171 ? -4.993  1.019   -1.523  1.00 14.14  ? 172 LYS A O   1 
ATOM   1361 C  CB  . LYS A 1 171 ? -3.995  -0.526  -4.154  1.00 15.04  ? 172 LYS A CB  1 
ATOM   1362 C  CG  . LYS A 1 171 ? -2.997  -0.903  -5.241  1.00 20.97  ? 172 LYS A CG  1 
ATOM   1363 C  CD  . LYS A 1 171 ? -3.411  -1.986  -6.114  1.00 22.69  ? 172 LYS A CD  1 
ATOM   1364 C  CE  . LYS A 1 171 ? -4.347  -1.446  -7.204  1.00 33.11  ? 172 LYS A CE  1 
ATOM   1365 N  NZ  . LYS A 1 171 ? -5.277  -2.423  -7.846  1.00 37.57  ? 172 LYS A NZ  1 
ATOM   1366 N  N   . SER A 1 172 ? -5.685  2.131   -3.349  1.00 14.56  ? 173 SER A N   1 
ATOM   1367 C  CA  . SER A 1 172 ? -6.857  2.644   -2.675  1.00 13.48  ? 173 SER A CA  1 
ATOM   1368 C  C   . SER A 1 172 ? -8.019  2.635   -3.665  1.00 13.68  ? 173 SER A C   1 
ATOM   1369 O  O   . SER A 1 172 ? -7.840  2.591   -4.900  1.00 15.57  ? 173 SER A O   1 
ATOM   1370 C  CB  . SER A 1 172 ? -6.606  4.008   -2.038  1.00 16.80  ? 173 SER A CB  1 
ATOM   1371 O  OG  . SER A 1 172 ? -6.431  5.021   -3.025  1.00 20.18  ? 173 SER A OG  1 
ATOM   1372 N  N   . ALA A 1 173 ? -9.247  2.816   -3.171  1.00 13.60  ? 174 ALA A N   1 
ATOM   1373 C  CA  . ALA A 1 173 ? -10.410 2.908   -4.045  1.00 14.99  ? 174 ALA A CA  1 
ATOM   1374 C  C   . ALA A 1 173 ? -11.472 3.750   -3.325  1.00 13.83  ? 174 ALA A C   1 
ATOM   1375 O  O   . ALA A 1 173 ? -11.534 3.803   -2.094  1.00 13.63  ? 174 ALA A O   1 
ATOM   1376 C  CB  . ALA A 1 173 ? -10.996 1.534   -4.278  1.00 17.52  ? 174 ALA A CB  1 
ATOM   1377 N  N   A ASP A 1 174 ? -12.360 4.290   -4.149  0.50 17.49  ? 175 ASP A N   1 
ATOM   1378 N  N   B ASP A 1 174 ? -12.285 4.457   -4.096  0.50 16.49  ? 175 ASP A N   1 
ATOM   1379 C  CA  A ASP A 1 174 ? -13.579 4.906   -3.673  0.50 18.06  ? 175 ASP A CA  1 
ATOM   1380 C  CA  B ASP A 1 174 ? -13.410 5.074   -3.430  0.50 14.62  ? 175 ASP A CA  1 
ATOM   1381 C  C   A ASP A 1 174 ? -14.408 3.885   -2.895  0.50 15.53  ? 175 ASP A C   1 
ATOM   1382 C  C   B ASP A 1 174 ? -14.303 3.979   -2.865  0.50 14.16  ? 175 ASP A C   1 
ATOM   1383 O  O   A ASP A 1 174 ? -14.511 2.710   -3.241  0.50 17.74  ? 175 ASP A O   1 
ATOM   1384 O  O   B ASP A 1 174 ? -14.363 2.863   -3.357  0.50 16.07  ? 175 ASP A O   1 
ATOM   1385 C  CB  A ASP A 1 174 ? -14.273 5.591   -4.846  0.50 22.43  ? 175 ASP A CB  1 
ATOM   1386 C  CB  B ASP A 1 174 ? -14.181 6.044   -4.319  0.50 18.42  ? 175 ASP A CB  1 
ATOM   1387 C  CG  A ASP A 1 174 ? -13.371 6.680   -5.407  0.50 25.53  ? 175 ASP A CG  1 
ATOM   1388 C  CG  B ASP A 1 174 ? -14.823 5.419   -5.552  0.50 22.94  ? 175 ASP A CG  1 
ATOM   1389 O  OD1 A ASP A 1 174 ? -12.870 7.497   -4.633  0.50 30.94  ? 175 ASP A OD1 1 
ATOM   1390 O  OD1 B ASP A 1 174 ? -15.871 4.755   -5.390  0.50 31.45  ? 175 ASP A OD1 1 
ATOM   1391 O  OD2 A ASP A 1 174 ? -13.202 6.733   -6.622  0.50 36.96  ? 175 ASP A OD2 1 
ATOM   1392 O  OD2 B ASP A 1 174 ? -14.337 5.716   -6.661  0.50 29.82  ? 175 ASP A OD2 1 
ATOM   1393 N  N   . PHE A 1 175 ? -14.976 4.322   -1.769  1.00 12.63  ? 176 PHE A N   1 
ATOM   1394 C  CA  . PHE A 1 175 ? -15.738 3.392   -0.965  1.00 11.83  ? 176 PHE A CA  1 
ATOM   1395 C  C   . PHE A 1 175 ? -16.815 4.130   -0.202  1.00 11.53  ? 176 PHE A C   1 
ATOM   1396 O  O   . PHE A 1 175 ? -16.717 4.353   0.981   1.00 13.25  ? 176 PHE A O   1 
ATOM   1397 C  CB  . PHE A 1 175 ? -14.794 2.590   -0.050  1.00 11.81  ? 176 PHE A CB  1 
ATOM   1398 C  CG  . PHE A 1 175 ? -15.443 1.345   0.497   1.00 11.68  ? 176 PHE A CG  1 
ATOM   1399 C  CD1 . PHE A 1 175 ? -15.751 0.299   -0.331  1.00 13.57  ? 176 PHE A CD1 1 
ATOM   1400 C  CD2 . PHE A 1 175 ? -15.742 1.228   1.832   1.00 11.86  ? 176 PHE A CD2 1 
ATOM   1401 C  CE1 . PHE A 1 175 ? -16.310 -0.887  0.148   1.00 13.85  ? 176 PHE A CE1 1 
ATOM   1402 C  CE2 . PHE A 1 175 ? -16.292 0.046   2.362   1.00 14.00  ? 176 PHE A CE2 1 
ATOM   1403 C  CZ  . PHE A 1 175 ? -16.594 -0.980  1.486   1.00 13.82  ? 176 PHE A CZ  1 
ATOM   1404 N  N   . THR A 1 176 ? -17.849 4.556   -0.919  1.00 12.30  ? 177 THR A N   1 
ATOM   1405 C  CA  . THR A 1 176 ? -18.912 5.368   -0.347  1.00 11.71  ? 177 THR A CA  1 
ATOM   1406 C  C   . THR A 1 176 ? -20.100 4.508   0.056   1.00 10.66  ? 177 THR A C   1 
ATOM   1407 O  O   . THR A 1 176 ? -20.253 3.356   -0.361  1.00 12.10  ? 177 THR A O   1 
ATOM   1408 C  CB  . THR A 1 176 ? -19.391 6.455   -1.336  1.00 13.90  ? 177 THR A CB  1 
ATOM   1409 O  OG1 . THR A 1 176 ? -19.765 5.854   -2.564  1.00 15.46  ? 177 THR A OG1 1 
ATOM   1410 C  CG2 . THR A 1 176 ? -18.290 7.461   -1.622  1.00 20.24  ? 177 THR A CG2 1 
ATOM   1411 N  N   . ASN A 1 177 ? -20.913 5.065   0.936   1.00 10.91  ? 178 ASN A N   1 
ATOM   1412 C  CA  . ASN A 1 177 ? -22.178 4.487   1.351   1.00 11.54  ? 178 ASN A CA  1 
ATOM   1413 C  C   . ASN A 1 177 ? -22.016 3.164   2.090   1.00 13.38  ? 178 ASN A C   1 
ATOM   1414 O  O   . ASN A 1 177 ? -22.929 2.346   2.075   1.00 17.11  ? 178 ASN A O   1 
ATOM   1415 C  CB  . ASN A 1 177 ? -23.196 4.362   0.210   1.00 13.67  ? 178 ASN A CB  1 
ATOM   1416 C  CG  . ASN A 1 177 ? -23.518 5.754   -0.312  1.00 12.69  ? 178 ASN A CG  1 
ATOM   1417 O  OD1 . ASN A 1 177 ? -24.251 6.502   0.303   1.00 16.00  ? 178 ASN A OD1 1 
ATOM   1418 N  ND2 . ASN A 1 177 ? -22.962 6.058   -1.464  1.00 13.57  ? 178 ASN A ND2 1 
ATOM   1419 N  N   . PHE A 1 178 ? -20.877 2.945   2.745   1.00 11.16  ? 179 PHE A N   1 
ATOM   1420 C  CA  . PHE A 1 178 ? -20.726 1.765   3.576   1.00 10.59  ? 179 PHE A CA  1 
ATOM   1421 C  C   . PHE A 1 178 ? -21.225 2.107   4.967   1.00 10.47  ? 179 PHE A C   1 
ATOM   1422 O  O   . PHE A 1 178 ? -20.792 3.095   5.589   1.00 12.50  ? 179 PHE A O   1 
ATOM   1423 C  CB  . PHE A 1 178 ? -19.272 1.351   3.645   1.00 11.66  ? 179 PHE A CB  1 
ATOM   1424 C  CG  . PHE A 1 178 ? -19.150 0.130   4.514   1.00 11.45  ? 179 PHE A CG  1 
ATOM   1425 C  CD1 . PHE A 1 178 ? -19.472 -1.130  4.030   1.00 11.95  ? 179 PHE A CD1 1 
ATOM   1426 C  CD2 . PHE A 1 178 ? -18.804 0.233   5.862   1.00 10.29  ? 179 PHE A CD2 1 
ATOM   1427 C  CE1 . PHE A 1 178 ? -19.486 -2.255  4.829   1.00 12.42  ? 179 PHE A CE1 1 
ATOM   1428 C  CE2 . PHE A 1 178 ? -18.803 -0.899  6.698   1.00 11.39  ? 179 PHE A CE2 1 
ATOM   1429 C  CZ  . PHE A 1 178 ? -19.127 -2.122  6.171   1.00 11.49  ? 179 PHE A CZ  1 
ATOM   1430 N  N   . ASP A 1 179 ? -22.151 1.292   5.484   1.00 10.11  ? 180 ASP A N   1 
ATOM   1431 C  CA  . ASP A 1 179 ? -22.759 1.562   6.765   1.00 10.55  ? 180 ASP A CA  1 
ATOM   1432 C  C   . ASP A 1 179 ? -22.096 0.716   7.839   1.00 10.47  ? 180 ASP A C   1 
ATOM   1433 O  O   . ASP A 1 179 ? -22.306 -0.480  7.905   1.00 10.63  ? 180 ASP A O   1 
ATOM   1434 C  CB  . ASP A 1 179 ? -24.243 1.239   6.674   1.00 13.11  ? 180 ASP A CB  1 
ATOM   1435 C  CG  . ASP A 1 179 ? -25.001 1.681   7.890   1.00 15.54  ? 180 ASP A CG  1 
ATOM   1436 O  OD1 . ASP A 1 179 ? -24.447 1.891   8.955   1.00 13.53  ? 180 ASP A OD1 1 
ATOM   1437 O  OD2 . ASP A 1 179 ? -26.242 1.824   7.772   1.00 25.42  ? 180 ASP A OD2 1 
ATOM   1438 N  N   . PRO A 1 180 ? -21.315 1.329   8.748   1.00 10.42  ? 181 PRO A N   1 
ATOM   1439 C  CA  . PRO A 1 180 ? -20.616 0.516   9.756   1.00 11.22  ? 181 PRO A CA  1 
ATOM   1440 C  C   . PRO A 1 180 ? -21.561 -0.088  10.777  1.00 10.55  ? 181 PRO A C   1 
ATOM   1441 O  O   . PRO A 1 180 ? -21.121 -0.970  11.553  1.00 11.75  ? 181 PRO A O   1 
ATOM   1442 C  CB  . PRO A 1 180 ? -19.626 1.498   10.369  1.00 12.66  ? 181 PRO A CB  1 
ATOM   1443 C  CG  . PRO A 1 180 ? -20.341 2.864   10.193  1.00 13.01  ? 181 PRO A CG  1 
ATOM   1444 C  CD  . PRO A 1 180 ? -21.010 2.768   8.839   1.00 11.68  ? 181 PRO A CD  1 
ATOM   1445 N  N   . ARG A 1 181 ? -22.825 0.342   10.839  1.00 10.57  ? 182 ARG A N   1 
ATOM   1446 C  CA  . ARG A 1 181 ? -23.750 -0.363  11.718  1.00 11.04  ? 182 ARG A CA  1 
ATOM   1447 C  C   . ARG A 1 181 ? -23.851 -1.849  11.368  1.00 10.35  ? 182 ARG A C   1 
ATOM   1448 O  O   . ARG A 1 181 ? -24.213 -2.644  12.240  1.00 11.80  ? 182 ARG A O   1 
ATOM   1449 C  CB  . ARG A 1 181 ? -25.129 0.269   11.632  1.00 12.18  ? 182 ARG A CB  1 
ATOM   1450 C  CG  . ARG A 1 181 ? -25.155 1.663   12.226  1.00 13.30  ? 182 ARG A CG  1 
ATOM   1451 C  CD  . ARG A 1 181 ? -26.471 2.342   12.119  1.00 16.20  ? 182 ARG A CD  1 
ATOM   1452 N  NE  . ARG A 1 181 ? -26.774 2.632   10.733  1.00 15.82  ? 182 ARG A NE  1 
ATOM   1453 C  CZ  . ARG A 1 181 ? -27.833 3.349   10.362  1.00 17.74  ? 182 ARG A CZ  1 
ATOM   1454 N  NH1 . ARG A 1 181 ? -28.677 3.824   11.272  1.00 23.93  ? 182 ARG A NH1 1 
ATOM   1455 N  NH2 . ARG A 1 181 ? -28.032 3.569   9.066   1.00 20.94  ? 182 ARG A NH2 1 
ATOM   1456 N  N   . GLY A 1 182 ? -23.590 -2.184  10.098  1.00 10.87  ? 183 GLY A N   1 
ATOM   1457 C  CA  . GLY A 1 182 ? -23.648 -3.603  9.712   1.00 12.27  ? 183 GLY A CA  1 
ATOM   1458 C  C   . GLY A 1 182 ? -22.506 -4.478  10.224  1.00 12.51  ? 183 GLY A C   1 
ATOM   1459 O  O   . GLY A 1 182 ? -22.515 -5.657  9.939   1.00 12.86  ? 183 GLY A O   1 
ATOM   1460 N  N   . LEU A 1 183 ? -21.558 -3.905  10.990  1.00 11.03  ? 184 LEU A N   1 
ATOM   1461 C  CA  . LEU A 1 183 ? -20.442 -4.657  11.572  1.00 11.12  ? 184 LEU A CA  1 
ATOM   1462 C  C   . LEU A 1 183 ? -20.615 -4.891  13.062  1.00 11.39  ? 184 LEU A C   1 
ATOM   1463 O  O   . LEU A 1 183 ? -19.733 -5.500  13.676  1.00 13.37  ? 184 LEU A O   1 
ATOM   1464 C  CB  . LEU A 1 183 ? -19.152 -3.901  11.296  1.00 11.33  ? 184 LEU A CB  1 
ATOM   1465 C  CG  . LEU A 1 183 ? -18.776 -3.766  9.829   1.00 12.01  ? 184 LEU A CG  1 
ATOM   1466 C  CD1 . LEU A 1 183 ? -17.483 -2.991  9.675   1.00 13.74  ? 184 LEU A CD1 1 
ATOM   1467 C  CD2 . LEU A 1 183 ? -18.717 -5.085  9.101   1.00 14.65  ? 184 LEU A CD2 1 
ATOM   1468 N  N   . LEU A 1 184 ? -21.704 -4.435  13.656  1.00 11.20  ? 185 LEU A N   1 
ATOM   1469 C  CA  . LEU A 1 184 ? -21.797 -4.508  15.096  1.00 11.25  ? 185 LEU A CA  1 
ATOM   1470 C  C   . LEU A 1 184 ? -22.569 -5.761  15.532  1.00 11.72  ? 185 LEU A C   1 
ATOM   1471 O  O   . LEU A 1 184 ? -23.528 -6.176  14.891  1.00 17.31  ? 185 LEU A O   1 
ATOM   1472 C  CB  . LEU A 1 184 ? -22.552 -3.255  15.640  1.00 11.60  ? 185 LEU A CB  1 
ATOM   1473 C  CG  . LEU A 1 184 ? -21.998 -1.895  15.227  1.00 13.59  ? 185 LEU A CG  1 
ATOM   1474 C  CD1 . LEU A 1 184 ? -22.836 -0.760  15.770  1.00 16.54  ? 185 LEU A CD1 1 
ATOM   1475 C  CD2 . LEU A 1 184 ? -20.558 -1.800  15.628  1.00 16.55  ? 185 LEU A CD2 1 
ATOM   1476 N  N   . PRO A 1 185 ? -22.261 -6.317  16.704  1.00 11.00  ? 186 PRO A N   1 
ATOM   1477 C  CA  . PRO A 1 185 ? -23.048 -7.398  17.282  1.00 11.19  ? 186 PRO A CA  1 
ATOM   1478 C  C   . PRO A 1 185 ? -24.326 -6.821  17.899  1.00 10.65  ? 186 PRO A C   1 
ATOM   1479 O  O   . PRO A 1 185 ? -24.495 -5.627  17.992  1.00 12.85  ? 186 PRO A O   1 
ATOM   1480 C  CB  . PRO A 1 185 ? -22.112 -7.990  18.339  1.00 12.63  ? 186 PRO A CB  1 
ATOM   1481 C  CG  . PRO A 1 185 ? -21.350 -6.762  18.814  1.00 11.09  ? 186 PRO A CG  1 
ATOM   1482 C  CD  . PRO A 1 185 ? -21.150 -5.909  17.571  1.00 10.92  ? 186 PRO A CD  1 
ATOM   1483 N  N   . GLU A 1 186 ? -25.188 -7.689  18.426  1.00 11.94  ? 187 GLU A N   1 
ATOM   1484 C  CA  . GLU A 1 186 ? -26.424 -7.213  19.047  1.00 13.07  ? 187 GLU A CA  1 
ATOM   1485 C  C   . GLU A 1 186 ? -26.155 -6.431  20.304  1.00 13.04  ? 187 GLU A C   1 
ATOM   1486 O  O   . GLU A 1 186 ? -26.707 -5.339  20.486  1.00 15.11  ? 187 GLU A O   1 
ATOM   1487 C  CB  . GLU A 1 186 ? -27.280 -8.409  19.488  1.00 15.47  ? 187 GLU A CB  1 
ATOM   1488 C  CG  . GLU A 1 186 ? -27.912 -9.157  18.323  1.00 18.09  ? 187 GLU A CG  1 
ATOM   1489 C  CD  . GLU A 1 186 ? -28.714 -10.373 18.770  1.00 19.27  ? 187 GLU A CD  1 
ATOM   1490 O  OE1 . GLU A 1 186 ? -28.726 -10.705 19.987  1.00 21.76  ? 187 GLU A OE1 1 
ATOM   1491 O  OE2 . GLU A 1 186 ? -29.190 -11.077 17.882  1.00 25.40  ? 187 GLU A OE2 1 
ATOM   1492 N  N   . SER A 1 187 ? -25.291 -6.980  21.178  1.00 12.42  ? 188 SER A N   1 
ATOM   1493 C  CA  . SER A 1 187 ? -25.084 -6.387  22.467  1.00 12.72  ? 188 SER A CA  1 
ATOM   1494 C  C   . SER A 1 187 ? -23.965 -5.343  22.423  1.00 12.19  ? 188 SER A C   1 
ATOM   1495 O  O   . SER A 1 187 ? -22.942 -5.598  21.797  1.00 13.66  ? 188 SER A O   1 
ATOM   1496 C  CB  . SER A 1 187 ? -24.664 -7.452  23.483  1.00 15.31  ? 188 SER A CB  1 
ATOM   1497 O  OG  . SER A 1 187 ? -24.459 -6.881  24.758  1.00 15.34  ? 188 SER A OG  1 
ATOM   1498 N  N   . LEU A 1 188 ? -24.121 -4.271  23.206  1.00 12.86  ? 189 LEU A N   1 
ATOM   1499 C  CA  . LEU A 1 188 ? -23.038 -3.319  23.436  1.00 12.76  ? 189 LEU A CA  1 
ATOM   1500 C  C   . LEU A 1 188 ? -22.434 -3.484  24.829  1.00 12.92  ? 189 LEU A C   1 
ATOM   1501 O  O   . LEU A 1 188 ? -21.735 -2.590  25.282  1.00 15.81  ? 189 LEU A O   1 
ATOM   1502 C  CB  . LEU A 1 188 ? -23.534 -1.868  23.202  1.00 14.88  ? 189 LEU A CB  1 
ATOM   1503 C  CG  . LEU A 1 188 ? -23.926 -1.500  21.770  1.00 15.53  ? 189 LEU A CG  1 
ATOM   1504 C  CD1 . LEU A 1 188 ? -24.410 -0.030  21.726  1.00 18.97  ? 189 LEU A CD1 1 
ATOM   1505 C  CD2 . LEU A 1 188 ? -22.780 -1.742  20.798  1.00 18.18  ? 189 LEU A CD2 1 
ATOM   1506 N  N   . ASP A 1 189 ? -22.586 -4.660  25.436  1.00 13.07  ? 190 ASP A N   1 
ATOM   1507 C  CA  . ASP A 1 189 ? -21.829 -4.882  26.679  1.00 12.87  ? 190 ASP A CA  1 
ATOM   1508 C  C   . ASP A 1 189 ? -20.328 -4.867  26.353  1.00 11.19  ? 190 ASP A C   1 
ATOM   1509 O  O   . ASP A 1 189 ? -19.916 -5.388  25.337  1.00 11.05  ? 190 ASP A O   1 
ATOM   1510 C  CB  . ASP A 1 189 ? -22.155 -6.236  27.254  1.00 16.23  ? 190 ASP A CB  1 
ATOM   1511 C  CG  . ASP A 1 189 ? -23.558 -6.333  27.867  1.00 21.01  ? 190 ASP A CG  1 
ATOM   1512 O  OD1 . ASP A 1 189 ? -24.166 -5.315  28.012  1.00 29.66  ? 190 ASP A OD1 1 
ATOM   1513 O  OD2 . ASP A 1 189 ? -23.941 -7.417  28.216  1.00 27.94  ? 190 ASP A OD2 1 
ATOM   1514 N  N   . TYR A 1 190 ? -19.554 -4.297  27.276  1.00 11.79  ? 191 TYR A N   1 
ATOM   1515 C  CA  . TYR A 1 190 ? -18.148 -4.039  26.942  1.00 10.37  ? 191 TYR A CA  1 
ATOM   1516 C  C   . TYR A 1 190 ? -17.270 -4.135  28.165  1.00 9.76   ? 191 TYR A C   1 
ATOM   1517 O  O   . TYR A 1 190 ? -17.694 -3.998  29.302  1.00 11.15  ? 191 TYR A O   1 
ATOM   1518 C  CB  . TYR A 1 190 ? -17.986 -2.668  26.280  1.00 10.84  ? 191 TYR A CB  1 
ATOM   1519 C  CG  . TYR A 1 190 ? -18.363 -1.496  27.137  1.00 11.34  ? 191 TYR A CG  1 
ATOM   1520 C  CD1 . TYR A 1 190 ? -17.457 -0.909  28.031  1.00 12.19  ? 191 TYR A CD1 1 
ATOM   1521 C  CD2 . TYR A 1 190 ? -19.641 -0.967  27.099  1.00 11.88  ? 191 TYR A CD2 1 
ATOM   1522 C  CE1 . TYR A 1 190 ? -17.837 0.176   28.826  1.00 12.51  ? 191 TYR A CE1 1 
ATOM   1523 C  CE2 . TYR A 1 190 ? -20.009 0.103   27.887  1.00 12.89  ? 191 TYR A CE2 1 
ATOM   1524 C  CZ  . TYR A 1 190 ? -19.126 0.669   28.781  1.00 13.33  ? 191 TYR A CZ  1 
ATOM   1525 O  OH  . TYR A 1 190 ? -19.435 1.681   29.604  1.00 15.09  ? 191 TYR A OH  1 
ATOM   1526 N  N   . TRP A 1 191 ? -15.966 -4.293  27.859  1.00 9.70   ? 192 TRP A N   1 
ATOM   1527 C  CA  . TRP A 1 191 ? -14.872 -4.021  28.797  1.00 9.78   ? 192 TRP A CA  1 
ATOM   1528 C  C   . TRP A 1 191 ? -14.174 -2.730  28.364  1.00 8.88   ? 192 TRP A C   1 
ATOM   1529 O  O   . TRP A 1 191 ? -14.137 -2.422  27.191  1.00 10.19  ? 192 TRP A O   1 
ATOM   1530 C  CB  . TRP A 1 191 ? -13.831 -5.173  28.776  1.00 10.25  ? 192 TRP A CB  1 
ATOM   1531 C  CG  . TRP A 1 191 ? -14.398 -6.502  29.200  1.00 10.25  ? 192 TRP A CG  1 
ATOM   1532 C  CD1 . TRP A 1 191 ? -14.639 -6.903  30.500  1.00 11.17  ? 192 TRP A CD1 1 
ATOM   1533 C  CD2 . TRP A 1 191 ? -14.668 -7.627  28.341  1.00 10.48  ? 192 TRP A CD2 1 
ATOM   1534 N  NE1 . TRP A 1 191 ? -15.073 -8.222  30.468  1.00 12.83  ? 192 TRP A NE1 1 
ATOM   1535 C  CE2 . TRP A 1 191 ? -15.095 -8.688  29.166  1.00 11.03  ? 192 TRP A CE2 1 
ATOM   1536 C  CE3 . TRP A 1 191 ? -14.559 -7.818  26.952  1.00 11.04  ? 192 TRP A CE3 1 
ATOM   1537 C  CZ2 . TRP A 1 191 ? -15.428 -9.947  28.661  1.00 13.24  ? 192 TRP A CZ2 1 
ATOM   1538 C  CZ3 . TRP A 1 191 ? -14.848 -9.079  26.470  1.00 12.79  ? 192 TRP A CZ3 1 
ATOM   1539 C  CH2 . TRP A 1 191 ? -15.266 -10.101 27.303  1.00 12.43  ? 192 TRP A CH2 1 
ATOM   1540 N  N   . THR A 1 192 ? -13.598 -2.042  29.366  1.00 9.66   ? 193 THR A N   1 
ATOM   1541 C  CA  . THR A 1 192 ? -12.887 -0.824  29.026  1.00 9.50   ? 193 THR A CA  1 
ATOM   1542 C  C   . THR A 1 192 ? -11.654 -0.682  29.883  1.00 9.61   ? 193 THR A C   1 
ATOM   1543 O  O   . THR A 1 192 ? -11.642 -1.054  31.044  1.00 9.85   ? 193 THR A O   1 
ATOM   1544 C  CB  . THR A 1 192 ? -13.816 0.393   29.118  1.00 9.93   ? 193 THR A CB  1 
ATOM   1545 O  OG1 . THR A 1 192 ? -13.104 1.581   28.694  1.00 10.54  ? 193 THR A OG1 1 
ATOM   1546 C  CG2 . THR A 1 192 ? -14.370 0.603   30.504  1.00 11.20  ? 193 THR A CG2 1 
ATOM   1547 N  N   . TYR A 1 193 ? -10.623 -0.069  29.292  1.00 9.37   ? 194 TYR A N   1 
ATOM   1548 C  CA  . TYR A 1 193 ? -9.402  0.189   30.032  1.00 9.40   ? 194 TYR A CA  1 
ATOM   1549 C  C   . TYR A 1 193 ? -8.645  1.266   29.266  1.00 8.67   ? 194 TYR A C   1 
ATOM   1550 O  O   . TYR A 1 193 ? -8.818  1.436   28.066  1.00 9.11   ? 194 TYR A O   1 
ATOM   1551 C  CB  . TYR A 1 193 ? -8.564  -1.094  30.222  1.00 9.76   ? 194 TYR A CB  1 
ATOM   1552 C  CG  . TYR A 1 193 ? -7.875  -1.562  28.977  1.00 9.42   ? 194 TYR A CG  1 
ATOM   1553 C  CD1 . TYR A 1 193 ? -8.570  -2.312  27.996  1.00 9.32   ? 194 TYR A CD1 1 
ATOM   1554 C  CD2 . TYR A 1 193 ? -6.531  -1.224  28.743  1.00 9.74   ? 194 TYR A CD2 1 
ATOM   1555 C  CE1 . TYR A 1 193 ? -7.953  -2.635  26.811  1.00 8.98   ? 194 TYR A CE1 1 
ATOM   1556 C  CE2 . TYR A 1 193 ? -5.926  -1.581  27.564  1.00 9.15   ? 194 TYR A CE2 1 
ATOM   1557 C  CZ  . TYR A 1 193 ? -6.620  -2.289  26.594  1.00 8.38   ? 194 TYR A CZ  1 
ATOM   1558 O  OH  . TYR A 1 193 ? -5.965  -2.563  25.447  1.00 8.64   ? 194 TYR A OH  1 
ATOM   1559 N  N   . PRO A 1 194 ? -7.688  1.943   29.950  1.00 9.19   ? 195 PRO A N   1 
ATOM   1560 C  CA  . PRO A 1 194 ? -6.836  2.929   29.276  1.00 9.66   ? 195 PRO A CA  1 
ATOM   1561 C  C   . PRO A 1 194 ? -5.651  2.270   28.601  1.00 8.61   ? 195 PRO A C   1 
ATOM   1562 O  O   . PRO A 1 194 ? -4.940  1.502   29.270  1.00 9.67   ? 195 PRO A O   1 
ATOM   1563 C  CB  . PRO A 1 194 ? -6.393  3.832   30.417  1.00 11.19  ? 195 PRO A CB  1 
ATOM   1564 C  CG  . PRO A 1 194 ? -6.383  2.915   31.650  1.00 12.34  ? 195 PRO A CG  1 
ATOM   1565 C  CD  . PRO A 1 194 ? -7.536  1.949   31.405  1.00 11.24  ? 195 PRO A CD  1 
ATOM   1566 N  N   . GLY A 1 195 ? -5.414  2.579   27.344  1.00 8.65   ? 196 GLY A N   1 
ATOM   1567 C  CA  . GLY A 1 195 ? -4.304  1.958   26.659  1.00 9.09   ? 196 GLY A CA  1 
ATOM   1568 C  C   . GLY A 1 195 ? -3.757  2.832   25.563  1.00 7.89   ? 196 GLY A C   1 
ATOM   1569 O  O   . GLY A 1 195 ? -3.649  4.056   25.679  1.00 9.04   ? 196 GLY A O   1 
ATOM   1570 N  N   . SER A 1 196 ? -3.345  2.166   24.497  1.00 7.96   ? 197 SER A N   1 
ATOM   1571 C  CA  . SER A 1 196 ? -2.530  2.763   23.460  1.00 8.36   ? 197 SER A CA  1 
ATOM   1572 C  C   . SER A 1 196 ? -2.962  2.387   22.049  1.00 7.76   ? 197 SER A C   1 
ATOM   1573 O  O   . SER A 1 196 ? -3.751  1.415   21.887  1.00 8.57   ? 197 SER A O   1 
ATOM   1574 C  CB  . SER A 1 196 ? -1.056  2.406   23.619  1.00 9.37   ? 197 SER A CB  1 
ATOM   1575 O  OG  . SER A 1 196 ? -0.804  1.063   23.218  1.00 9.09   ? 197 SER A OG  1 
ATOM   1576 N  N   . LEU A 1 197 ? -2.424  3.048   21.054  1.00 8.04   ? 198 LEU A N   1 
ATOM   1577 C  CA  . LEU A 1 197 ? -2.440  2.517   19.708  1.00 8.33   ? 198 LEU A CA  1 
ATOM   1578 C  C   . LEU A 1 197 ? -1.735  1.178   19.762  1.00 8.92   ? 198 LEU A C   1 
ATOM   1579 O  O   . LEU A 1 197 ? -0.750  1.010   20.483  1.00 9.31   ? 198 LEU A O   1 
ATOM   1580 C  CB  . LEU A 1 197 ? -1.708  3.444   18.765  1.00 10.10  ? 198 LEU A CB  1 
ATOM   1581 C  CG  . LEU A 1 197 ? -2.251  4.851   18.686  1.00 11.39  ? 198 LEU A CG  1 
ATOM   1582 C  CD1 . LEU A 1 197 ? -1.360  5.666   17.735  1.00 12.48  ? 198 LEU A CD1 1 
ATOM   1583 C  CD2 . LEU A 1 197 ? -3.711  4.845   18.225  1.00 12.33  ? 198 LEU A CD2 1 
ATOM   1584 N  N   . THR A 1 198 ? -2.137  0.240   18.879  1.00 8.78   ? 199 THR A N   1 
ATOM   1585 C  CA  . THR A 1 198 ? -1.481  -1.057  18.800  1.00 8.70   ? 199 THR A CA  1 
ATOM   1586 C  C   . THR A 1 198 ? -0.477  -1.117  17.690  1.00 8.86   ? 199 THR A C   1 
ATOM   1587 O  O   . THR A 1 198 ? 0.128   -2.180  17.499  1.00 9.90   ? 199 THR A O   1 
ATOM   1588 C  CB  . THR A 1 198 ? -2.462  -2.214  18.749  1.00 8.81   ? 199 THR A CB  1 
ATOM   1589 O  OG1 . THR A 1 198 ? -3.022  -2.196  17.446  1.00 8.35   ? 199 THR A OG1 1 
ATOM   1590 C  CG2 . THR A 1 198 ? -3.488  -2.192  19.851  1.00 9.78   ? 199 THR A CG2 1 
ATOM   1591 N  N   . THR A 1 199 ? -0.327  -0.021  16.932  1.00 9.47   ? 200 THR A N   1 
ATOM   1592 C  CA  . THR A 1 199 ? 0.684   0.105   15.916  1.00 9.94   ? 200 THR A CA  1 
ATOM   1593 C  C   . THR A 1 199 ? 1.521   1.310   16.266  1.00 10.09  ? 200 THR A C   1 
ATOM   1594 O  O   . THR A 1 199 ? 1.031   2.256   16.856  1.00 10.44  ? 200 THR A O   1 
ATOM   1595 C  CB  . THR A 1 199 ? 0.117   0.311   14.501  1.00 11.87  ? 200 THR A CB  1 
ATOM   1596 O  OG1 . THR A 1 199 ? -0.812  1.407   14.546  1.00 15.35  ? 200 THR A OG1 1 
ATOM   1597 C  CG2 . THR A 1 199 ? -0.643  -0.912  14.052  1.00 13.21  ? 200 THR A CG2 1 
ATOM   1598 N  N   . PRO A 1 200 ? 2.777   1.366   15.769  1.00 10.89  ? 201 PRO A N   1 
ATOM   1599 C  CA  . PRO A 1 200 ? 3.526   2.597   15.810  1.00 11.10  ? 201 PRO A CA  1 
ATOM   1600 C  C   . PRO A 1 200 ? 2.623   3.725   15.338  1.00 11.91  ? 201 PRO A C   1 
ATOM   1601 O  O   . PRO A 1 200 ? 1.924   3.577   14.317  1.00 12.71  ? 201 PRO A O   1 
ATOM   1602 C  CB  . PRO A 1 200 ? 4.686   2.285   14.833  1.00 13.11  ? 201 PRO A CB  1 
ATOM   1603 C  CG  . PRO A 1 200 ? 4.946   0.838   15.056  1.00 13.22  ? 201 PRO A CG  1 
ATOM   1604 C  CD  . PRO A 1 200 ? 3.525   0.296   15.130  1.00 11.68  ? 201 PRO A CD  1 
ATOM   1605 N  N   . PRO A 1 201 ? 2.659   4.900   15.988  1.00 11.78  ? 202 PRO A N   1 
ATOM   1606 C  CA  . PRO A 1 201 ? 3.637   5.273   17.008  1.00 11.60  ? 202 PRO A CA  1 
ATOM   1607 C  C   . PRO A 1 201 ? 3.351   4.810   18.437  1.00 10.87  ? 202 PRO A C   1 
ATOM   1608 O  O   . PRO A 1 201 ? 4.071   5.213   19.380  1.00 11.73  ? 202 PRO A O   1 
ATOM   1609 C  CB  . PRO A 1 201 ? 3.673   6.804   16.927  1.00 13.26  ? 202 PRO A CB  1 
ATOM   1610 C  CG  . PRO A 1 201 ? 2.222   7.117   16.519  1.00 16.43  ? 202 PRO A CG  1 
ATOM   1611 C  CD  . PRO A 1 201 ? 1.840   6.041   15.532  1.00 14.55  ? 202 PRO A CD  1 
ATOM   1612 N  N   . LEU A 1 202 ? 2.307   4.005   18.655  1.00 10.29  ? 203 LEU A N   1 
ATOM   1613 C  CA  . LEU A 1 202 ? 2.082   3.390   19.952  1.00 9.70   ? 203 LEU A CA  1 
ATOM   1614 C  C   . LEU A 1 202 ? 1.682   4.372   21.024  1.00 9.96   ? 203 LEU A C   1 
ATOM   1615 O  O   . LEU A 1 202 ? 1.724   4.067   22.232  1.00 9.85   ? 203 LEU A O   1 
ATOM   1616 C  CB  . LEU A 1 202 ? 3.202   2.472   20.435  1.00 10.31  ? 203 LEU A CB  1 
ATOM   1617 C  CG  . LEU A 1 202 ? 3.547   1.358   19.441  1.00 10.00  ? 203 LEU A CG  1 
ATOM   1618 C  CD1 . LEU A 1 202 ? 4.826   0.679   19.881  1.00 12.00  ? 203 LEU A CD1 1 
ATOM   1619 C  CD2 . LEU A 1 202 ? 2.454   0.309   19.351  1.00 11.29  ? 203 LEU A CD2 1 
ATOM   1620 N  N   . ASN A 1 203 ? 1.155   5.550   20.629  1.00 10.39  ? 204 ASN A N   1 
ATOM   1621 C  CA  . ASN A 1 203 ? 0.808   6.608   21.568  1.00 10.84  ? 204 ASN A CA  1 
ATOM   1622 C  C   . ASN A 1 203 ? -0.177  6.115   22.606  1.00 9.51   ? 204 ASN A C   1 
ATOM   1623 O  O   . ASN A 1 203 ? -1.140  5.370   22.294  1.00 10.13  ? 204 ASN A O   1 
ATOM   1624 C  CB  . ASN A 1 203 ? 0.135   7.771   20.843  1.00 12.02  ? 204 ASN A CB  1 
ATOM   1625 C  CG  . ASN A 1 203 ? 1.054   8.478   19.880  1.00 14.15  ? 204 ASN A CG  1 
ATOM   1626 O  OD1 . ASN A 1 203 ? 2.156   8.072   19.595  1.00 17.93  ? 204 ASN A OD1 1 
ATOM   1627 N  ND2 . ASN A 1 203 ? 0.597   9.641   19.430  1.00 18.70  ? 204 ASN A ND2 1 
ATOM   1628 N  N   . GLU A 1 204 ? 0.001   6.552   23.844  1.00 10.28  ? 205 GLU A N   1 
ATOM   1629 C  CA  . GLU A 1 204 ? -0.840  6.172   24.964  1.00 10.39  ? 205 GLU A CA  1 
ATOM   1630 C  C   . GLU A 1 204 ? -2.033  7.143   25.072  1.00 10.27  ? 205 GLU A C   1 
ATOM   1631 O  O   . GLU A 1 204 ? -2.145  7.920   26.012  1.00 13.55  ? 205 GLU A O   1 
ATOM   1632 C  CB  . GLU A 1 204 ? 0.001   6.075   26.238  1.00 11.93  ? 205 GLU A CB  1 
ATOM   1633 C  CG  . GLU A 1 204 ? 0.884   4.829   26.106  1.00 12.04  ? 205 GLU A CG  1 
ATOM   1634 C  CD  . GLU A 1 204 ? 1.795   4.535   27.296  1.00 11.87  ? 205 GLU A CD  1 
ATOM   1635 O  OE1 . GLU A 1 204 ? 2.055   5.467   28.080  1.00 14.88  ? 205 GLU A OE1 1 
ATOM   1636 O  OE2 . GLU A 1 204 ? 2.198   3.375   27.440  1.00 11.91  ? 205 GLU A OE2 1 
ATOM   1637 N  N   . CYS A 1 205 ? -2.901  7.070   24.080  1.00 9.83   ? 206 CYS A N   1 
ATOM   1638 C  CA  . CYS A 1 205 ? -3.929  8.087   23.897  1.00 9.24   ? 206 CYS A CA  1 
ATOM   1639 C  C   . CYS A 1 205 ? -5.310  7.454   23.754  1.00 9.59   ? 206 CYS A C   1 
ATOM   1640 O  O   . CYS A 1 205 ? -6.255  8.152   23.393  1.00 11.59  ? 206 CYS A O   1 
ATOM   1641 C  CB  . CYS A 1 205 ? -3.653  8.894   22.638  1.00 11.05  ? 206 CYS A CB  1 
ATOM   1642 S  SG  . CYS A 1 205 ? -3.575  7.913   21.123  1.00 11.42  ? 206 CYS A SG  1 
ATOM   1643 N  N   . VAL A 1 206 ? -5.458  6.157   24.046  1.00 9.12   ? 207 VAL A N   1 
ATOM   1644 C  CA  . VAL A 1 206 ? -6.697  5.444   23.692  1.00 9.44   ? 207 VAL A CA  1 
ATOM   1645 C  C   . VAL A 1 206 ? -7.456  5.009   24.928  1.00 8.91   ? 207 VAL A C   1 
ATOM   1646 O  O   . VAL A 1 206 ? -6.930  4.348   25.808  1.00 10.55  ? 207 VAL A O   1 
ATOM   1647 C  CB  . VAL A 1 206 ? -6.387  4.200   22.844  1.00 9.39   ? 207 VAL A CB  1 
ATOM   1648 C  CG1 . VAL A 1 206 ? -7.729  3.503   22.497  1.00 9.73   ? 207 VAL A CG1 1 
ATOM   1649 C  CG2 . VAL A 1 206 ? -5.666  4.567   21.570  1.00 9.95   ? 207 VAL A CG2 1 
ATOM   1650 N  N   . THR A 1 207 ? -8.775  5.323   24.963  1.00 9.43   ? 208 THR A N   1 
ATOM   1651 C  CA  . THR A 1 207 ? -9.706  4.595   25.827  1.00 9.90   ? 208 THR A CA  1 
ATOM   1652 C  C   . THR A 1 207 ? -10.267 3.435   25.003  1.00 8.82   ? 208 THR A C   1 
ATOM   1653 O  O   . THR A 1 207 ? -10.908 3.639   23.953  1.00 9.65   ? 208 THR A O   1 
ATOM   1654 C  CB  . THR A 1 207 ? -10.893 5.480   26.245  1.00 10.15  ? 208 THR A CB  1 
ATOM   1655 O  OG1 . THR A 1 207 ? -10.344 6.596   26.979  1.00 11.45  ? 208 THR A OG1 1 
ATOM   1656 C  CG2 . THR A 1 207 ? -11.810 4.704   27.152  1.00 11.86  ? 208 THR A CG2 1 
ATOM   1657 N  N   . TRP A 1 208 ? -9.879  2.226   25.415  1.00 8.61   ? 209 TRP A N   1 
ATOM   1658 C  CA  . TRP A 1 208 ? -10.344 1.035   24.686  1.00 8.39   ? 209 TRP A CA  1 
ATOM   1659 C  C   . TRP A 1 208 ? -11.720 0.627   25.217  1.00 7.50   ? 209 TRP A C   1 
ATOM   1660 O  O   . TRP A 1 208 ? -11.928 0.601   26.415  1.00 8.67   ? 209 TRP A O   1 
ATOM   1661 C  CB  . TRP A 1 208 ? -9.371  -0.132  24.913  1.00 8.61   ? 209 TRP A CB  1 
ATOM   1662 C  CG  . TRP A 1 208 ? -8.215  -0.030  23.967  1.00 8.17   ? 209 TRP A CG  1 
ATOM   1663 C  CD1 . TRP A 1 208 ? -6.972  0.569   24.163  1.00 8.94   ? 209 TRP A CD1 1 
ATOM   1664 C  CD2 . TRP A 1 208 ? -8.246  -0.418  22.607  1.00 8.02   ? 209 TRP A CD2 1 
ATOM   1665 N  NE1 . TRP A 1 208 ? -6.282  0.537   23.017  1.00 9.04   ? 209 TRP A NE1 1 
ATOM   1666 C  CE2 . TRP A 1 208 ? -7.008  -0.074  22.008  1.00 8.52   ? 209 TRP A CE2 1 
ATOM   1667 C  CE3 . TRP A 1 208 ? -9.213  -1.065  21.803  1.00 8.14   ? 209 TRP A CE3 1 
ATOM   1668 C  CZ2 . TRP A 1 208 ? -6.725  -0.325  20.678  1.00 9.41   ? 209 TRP A CZ2 1 
ATOM   1669 C  CZ3 . TRP A 1 208 ? -8.925  -1.331  20.497  1.00 9.42   ? 209 TRP A CZ3 1 
ATOM   1670 C  CH2 . TRP A 1 208 ? -7.693  -0.996  19.945  1.00 9.68   ? 209 TRP A CH2 1 
ATOM   1671 N  N   . ILE A 1 209 ? -12.601 0.276   24.258  1.00 8.57   ? 210 ILE A N   1 
ATOM   1672 C  CA  . ILE A 1 209 ? -13.919 -0.237  24.576  1.00 8.24   ? 210 ILE A CA  1 
ATOM   1673 C  C   . ILE A 1 209 ? -14.032 -1.501  23.713  1.00 7.55   ? 210 ILE A C   1 
ATOM   1674 O  O   . ILE A 1 209 ? -14.095 -1.407  22.503  1.00 8.85   ? 210 ILE A O   1 
ATOM   1675 C  CB  . ILE A 1 209 ? -14.986 0.785   24.204  1.00 9.42   ? 210 ILE A CB  1 
ATOM   1676 C  CG1 . ILE A 1 209 ? -14.760 2.089   25.008  1.00 12.04  ? 210 ILE A CG1 1 
ATOM   1677 C  CG2 . ILE A 1 209 ? -16.387 0.203   24.469  1.00 11.15  ? 210 ILE A CG2 1 
ATOM   1678 C  CD1 . ILE A 1 209 ? -15.588 3.254   24.560  1.00 14.26  ? 210 ILE A CD1 1 
ATOM   1679 N  N   . VAL A 1 210 ? -13.995 -2.659  24.380  1.00 8.23   ? 211 VAL A N   1 
ATOM   1680 C  CA  . VAL A 1 210 ? -13.957 -3.932  23.688  1.00 8.14   ? 211 VAL A CA  1 
ATOM   1681 C  C   . VAL A 1 210 ? -15.284 -4.638  23.931  1.00 7.94   ? 211 VAL A C   1 
ATOM   1682 O  O   . VAL A 1 210 ? -15.627 -4.886  25.072  1.00 8.89   ? 211 VAL A O   1 
ATOM   1683 C  CB  . VAL A 1 210 ? -12.756 -4.786  24.146  1.00 8.99   ? 211 VAL A CB  1 
ATOM   1684 C  CG1 . VAL A 1 210 ? -12.791 -6.141  23.462  1.00 10.10  ? 211 VAL A CG1 1 
ATOM   1685 C  CG2 . VAL A 1 210 ? -11.432 -4.081  23.842  1.00 10.24  ? 211 VAL A CG2 1 
ATOM   1686 N  N   . LEU A 1 211 ? -16.029 -4.892  22.864  1.00 9.14   ? 212 LEU A N   1 
ATOM   1687 C  CA  . LEU A 1 211 ? -17.330 -5.521  23.082  1.00 9.59   ? 212 LEU A CA  1 
ATOM   1688 C  C   . LEU A 1 211 ? -17.175 -6.986  23.446  1.00 9.53   ? 212 LEU A C   1 
ATOM   1689 O  O   . LEU A 1 211 ? -16.316 -7.721  22.933  1.00 10.15  ? 212 LEU A O   1 
ATOM   1690 C  CB  . LEU A 1 211 ? -18.154 -5.405  21.776  1.00 9.82   ? 212 LEU A CB  1 
ATOM   1691 C  CG  . LEU A 1 211 ? -18.506 -3.983  21.361  1.00 10.35  ? 212 LEU A CG  1 
ATOM   1692 C  CD1 . LEU A 1 211 ? -19.514 -4.003  20.221  1.00 12.93  ? 212 LEU A CD1 1 
ATOM   1693 C  CD2 . LEU A 1 211 ? -19.016 -3.121  22.516  1.00 11.26  ? 212 LEU A CD2 1 
ATOM   1694 N  N   . LYS A 1 212 ? -18.030 -7.434  24.352  1.00 10.16  ? 213 LYS A N   1 
ATOM   1695 C  CA  . LYS A 1 212 ? -18.006 -8.820  24.786  1.00 11.52  ? 213 LYS A CA  1 
ATOM   1696 C  C   . LYS A 1 212 ? -18.466 -9.781  23.706  1.00 10.39  ? 213 LYS A C   1 
ATOM   1697 O  O   . LYS A 1 212 ? -17.973 -10.897 23.624  1.00 13.10  ? 213 LYS A O   1 
ATOM   1698 C  CB  . LYS A 1 212 ? -18.841 -8.965  26.037  1.00 15.82  ? 213 LYS A CB  1 
ATOM   1699 C  CG  . LYS A 1 212 ? -19.157 -10.372 26.495  1.00 24.17  ? 213 LYS A CG  1 
ATOM   1700 C  CD  . LYS A 1 212 ? -20.226 -10.283 27.578  1.00 36.38  ? 213 LYS A CD  1 
ATOM   1701 N  N   . GLU A 1 213 ? -19.468 -9.378  22.922  1.00 10.23  ? 214 GLU A N   1 
ATOM   1702 C  CA  . GLU A 1 213 ? -20.035 -10.299 21.940  1.00 10.40  ? 214 GLU A CA  1 
ATOM   1703 C  C   . GLU A 1 213 ? -19.278 -10.205 20.630  1.00 9.98   ? 214 GLU A C   1 
ATOM   1704 O  O   . GLU A 1 213 ? -19.203 -9.137  20.034  1.00 10.28  ? 214 GLU A O   1 
ATOM   1705 C  CB  . GLU A 1 213 ? -21.505 -9.892  21.672  1.00 11.58  ? 214 GLU A CB  1 
ATOM   1706 C  CG  . GLU A 1 213 ? -22.282 -10.823 20.769  1.00 15.22  ? 214 GLU A CG  1 
ATOM   1707 C  CD  . GLU A 1 213 ? -23.736 -10.325 20.489  1.00 17.55  ? 214 GLU A CD  1 
ATOM   1708 O  OE1 . GLU A 1 213 ? -24.325 -9.690  21.386  1.00 18.11  ? 214 GLU A OE1 1 
ATOM   1709 O  OE2 . GLU A 1 213 ? -24.245 -10.584 19.380  1.00 26.60  ? 214 GLU A OE2 1 
ATOM   1710 N  N   . PRO A 1 214 ? -18.712 -11.313 20.141  1.00 10.56  ? 215 PRO A N   1 
ATOM   1711 C  CA  . PRO A 1 214 ? -18.095 -11.294 18.831  1.00 10.58  ? 215 PRO A CA  1 
ATOM   1712 C  C   . PRO A 1 214 ? -19.142 -11.225 17.747  1.00 10.34  ? 215 PRO A C   1 
ATOM   1713 O  O   . PRO A 1 214 ? -20.299 -11.634 17.972  1.00 12.48  ? 215 PRO A O   1 
ATOM   1714 C  CB  . PRO A 1 214 ? -17.351 -12.637 18.759  1.00 11.66  ? 215 PRO A CB  1 
ATOM   1715 C  CG  . PRO A 1 214 ? -18.118 -13.531 19.713  1.00 20.26  ? 215 PRO A CG  1 
ATOM   1716 C  CD  . PRO A 1 214 ? -18.669 -12.634 20.804  1.00 13.35  ? 215 PRO A CD  1 
ATOM   1717 N  N   . ILE A 1 215 ? -18.710 -10.822 16.564  1.00 9.71   ? 216 ILE A N   1 
ATOM   1718 C  CA  . ILE A 1 215 ? -19.515 -11.077 15.349  1.00 10.93  ? 216 ILE A CA  1 
ATOM   1719 C  C   . ILE A 1 215 ? -19.003 -12.348 14.733  1.00 10.52  ? 216 ILE A C   1 
ATOM   1720 O  O   . ILE A 1 215 ? -17.830 -12.680 14.857  1.00 11.82  ? 216 ILE A O   1 
ATOM   1721 C  CB  . ILE A 1 215 ? -19.500 -9.863  14.385  1.00 10.96  ? 216 ILE A CB  1 
ATOM   1722 C  CG1 . ILE A 1 215 ? -18.098 -9.510  13.903  1.00 11.00  ? 216 ILE A CG1 1 
ATOM   1723 C  CG2 . ILE A 1 215 ? -20.171 -8.669  15.044  1.00 11.72  ? 216 ILE A CG2 1 
ATOM   1724 C  CD1 . ILE A 1 215 ? -18.093 -8.604  12.699  1.00 12.94  ? 216 ILE A CD1 1 
ATOM   1725 N  N   . SER A 1 216 ? -19.879 -12.996 13.986  1.00 11.26  ? 217 SER A N   1 
ATOM   1726 C  CA  A SER A 1 216 ? -19.535 -14.142 13.166  0.50 11.39  ? 217 SER A CA  1 
ATOM   1727 C  CA  B SER A 1 216 ? -19.479 -14.124 13.190  0.50 11.65  ? 217 SER A CA  1 
ATOM   1728 C  C   . SER A 1 216 ? -19.290 -13.678 11.753  1.00 10.25  ? 217 SER A C   1 
ATOM   1729 O  O   . SER A 1 216 ? -20.119 -12.938 11.199  1.00 11.74  ? 217 SER A O   1 
ATOM   1730 C  CB  A SER A 1 216 ? -20.670 -15.162 13.143  0.50 12.85  ? 217 SER A CB  1 
ATOM   1731 C  CB  B SER A 1 216 ? -20.545 -15.193 13.328  0.50 15.54  ? 217 SER A CB  1 
ATOM   1732 O  OG  A SER A 1 216 ? -20.732 -15.837 14.377  0.50 14.51  ? 217 SER A OG  1 
ATOM   1733 O  OG  B SER A 1 216 ? -20.229 -16.282 12.515  0.50 18.43  ? 217 SER A OG  1 
ATOM   1734 N  N   . VAL A 1 217 ? -18.209 -14.159 11.137  1.00 10.85  ? 218 VAL A N   1 
ATOM   1735 C  CA  . VAL A 1 217 ? -17.935 -13.960 9.739   1.00 10.40  ? 218 VAL A CA  1 
ATOM   1736 C  C   . VAL A 1 217 ? -17.711 -15.337 9.126   1.00 10.34  ? 218 VAL A C   1 
ATOM   1737 O  O   . VAL A 1 217 ? -17.331 -16.269 9.838   1.00 11.39  ? 218 VAL A O   1 
ATOM   1738 C  CB  . VAL A 1 217 ? -16.735 -13.032 9.501   1.00 11.73  ? 218 VAL A CB  1 
ATOM   1739 C  CG1 . VAL A 1 217 ? -16.992 -11.684 10.203  1.00 12.99  ? 218 VAL A CG1 1 
ATOM   1740 C  CG2 . VAL A 1 217 ? -15.453 -13.666 10.043  1.00 13.91  ? 218 VAL A CG2 1 
ATOM   1741 N  N   . SER A 1 218 ? -17.851 -15.470 7.833   1.00 10.82  ? 219 SER A N   1 
ATOM   1742 C  CA  . SER A 1 218 ? -17.670 -16.795 7.262   1.00 11.08  ? 219 SER A CA  1 
ATOM   1743 C  C   . SER A 1 218 ? -16.201 -17.019 6.957   1.00 10.67  ? 219 SER A C   1 
ATOM   1744 O  O   . SER A 1 218 ? -15.401 -16.091 6.771   1.00 11.75  ? 219 SER A O   1 
ATOM   1745 C  CB  . SER A 1 218 ? -18.489 -16.989 6.008   1.00 12.36  ? 219 SER A CB  1 
ATOM   1746 O  OG  . SER A 1 218 ? -18.080 -16.082 5.034   1.00 12.07  ? 219 SER A OG  1 
ATOM   1747 N  N   . SER A 1 219 ? -15.859 -18.298 6.757   1.00 12.10  ? 220 SER A N   1 
ATOM   1748 C  CA  . SER A 1 219 ? -14.520 -18.652 6.296   1.00 12.98  ? 220 SER A CA  1 
ATOM   1749 C  C   . SER A 1 219 ? -14.215 -17.965 4.978   1.00 13.30  ? 220 SER A C   1 
ATOM   1750 O  O   . SER A 1 219 ? -13.087 -17.526 4.760   1.00 14.75  ? 220 SER A O   1 
ATOM   1751 C  CB  . SER A 1 219 ? -14.382 -20.162 6.230   1.00 16.05  ? 220 SER A CB  1 
ATOM   1752 O  OG  . SER A 1 219 ? -15.318 -20.729 5.287   1.00 19.29  ? 220 SER A OG  1 
ATOM   1753 N  N   . GLU A 1 220 ? -15.200 -17.879 4.074   1.00 12.45  ? 221 GLU A N   1 
ATOM   1754 C  CA  . GLU A 1 220 ? -14.904 -17.245 2.803   1.00 13.71  ? 221 GLU A CA  1 
ATOM   1755 C  C   . GLU A 1 220 ? -14.597 -15.754 2.952   1.00 12.12  ? 221 GLU A C   1 
ATOM   1756 O  O   . GLU A 1 220 ? -13.801 -15.200 2.201   1.00 13.60  ? 221 GLU A O   1 
ATOM   1757 C  CB  . GLU A 1 220 ? -16.080 -17.357 1.815   1.00 15.16  ? 221 GLU A CB  1 
ATOM   1758 C  CG  . GLU A 1 220 ? -16.392 -18.799 1.385   1.00 20.01  ? 221 GLU A CG  1 
ATOM   1759 C  CD  . GLU A 1 220 ? -17.414 -19.532 2.248   1.00 23.56  ? 221 GLU A CD  1 
ATOM   1760 O  OE1 . GLU A 1 220 ? -17.732 -19.095 3.363   1.00 21.06  ? 221 GLU A OE1 1 
ATOM   1761 O  OE2 . GLU A 1 220 ? -17.942 -20.574 1.779   1.00 31.23  ? 221 GLU A OE2 1 
ATOM   1762 N  N   . GLN A 1 221 ? -15.244 -15.095 3.915   1.00 11.22  ? 222 GLN A N   1 
ATOM   1763 C  CA  . GLN A 1 221 ? -14.972 -13.691 4.134   1.00 11.21  ? 222 GLN A CA  1 
ATOM   1764 C  C   . GLN A 1 221 ? -13.536 -13.507 4.681   1.00 11.48  ? 222 GLN A C   1 
ATOM   1765 O  O   . GLN A 1 221 ? -12.808 -12.673 4.171   1.00 11.26  ? 222 GLN A O   1 
ATOM   1766 C  CB  . GLN A 1 221 ? -15.995 -13.112 5.091   1.00 10.59  ? 222 GLN A CB  1 
ATOM   1767 C  CG  . GLN A 1 221 ? -17.364 -12.984 4.422   1.00 10.69  ? 222 GLN A CG  1 
ATOM   1768 C  CD  . GLN A 1 221 ? -18.438 -12.460 5.329   1.00 10.03  ? 222 GLN A CD  1 
ATOM   1769 O  OE1 . GLN A 1 221 ? -18.553 -12.798 6.518   1.00 10.37  ? 222 GLN A OE1 1 
ATOM   1770 N  NE2 . GLN A 1 221 ? -19.255 -11.562 4.790   1.00 11.16  ? 222 GLN A NE2 1 
ATOM   1771 N  N   . VAL A 1 222 ? -13.142 -14.269 5.679   1.00 11.07  ? 223 VAL A N   1 
ATOM   1772 C  CA  . VAL A 1 222 ? -11.792 -14.085 6.216   1.00 12.94  ? 223 VAL A CA  1 
ATOM   1773 C  C   . VAL A 1 222 ? -10.746 -14.543 5.202   1.00 13.08  ? 223 VAL A C   1 
ATOM   1774 O  O   . VAL A 1 222 ? -9.663  -13.989 5.160   1.00 13.75  ? 223 VAL A O   1 
ATOM   1775 C  CB  . VAL A 1 222 ? -11.654 -14.730 7.591   1.00 16.34  ? 223 VAL A CB  1 
ATOM   1776 C  CG1 . VAL A 1 222 ? -11.663 -16.219 7.550   1.00 20.91  ? 223 VAL A CG1 1 
ATOM   1777 C  CG2 . VAL A 1 222 ? -10.385 -14.195 8.283   1.00 22.48  ? 223 VAL A CG2 1 
ATOM   1778 N  N   A LEU A 1 223 ? -11.060 -15.541 4.365   0.50 14.15  ? 224 LEU A N   1 
ATOM   1779 N  N   B LEU A 1 223 ? -11.040 -15.527 4.348   0.50 13.63  ? 224 LEU A N   1 
ATOM   1780 C  CA  A LEU A 1 223 ? -10.160 -15.960 3.306   0.50 15.05  ? 224 LEU A CA  1 
ATOM   1781 C  CA  B LEU A 1 223 ? -10.030 -15.926 3.386   0.50 15.74  ? 224 LEU A CA  1 
ATOM   1782 C  C   A LEU A 1 223 ? -9.759  -14.762 2.457   0.50 14.50  ? 224 LEU A C   1 
ATOM   1783 C  C   B LEU A 1 223 ? -9.760  -14.802 2.382   0.50 14.64  ? 224 LEU A C   1 
ATOM   1784 O  O   A LEU A 1 223 ? -8.590  -14.599 2.074   0.50 13.80  ? 224 LEU A O   1 
ATOM   1785 O  O   B LEU A 1 223 ? -8.642  -14.696 1.854   0.50 15.27  ? 224 LEU A O   1 
ATOM   1786 C  CB  A LEU A 1 223 ? -10.858 -17.000 2.427   0.50 17.47  ? 224 LEU A CB  1 
ATOM   1787 C  CB  B LEU A 1 223 ? -10.432 -17.246 2.710   0.50 16.84  ? 224 LEU A CB  1 
ATOM   1788 C  CG  A LEU A 1 223 ? -10.157 -17.323 1.108   0.50 21.63  ? 224 LEU A CG  1 
ATOM   1789 C  CG  B LEU A 1 223 ? -10.305 -18.495 3.581   0.50 17.42  ? 224 LEU A CG  1 
ATOM   1790 C  CD1 A LEU A 1 223 ? -8.784  -17.926 1.358   0.00 25.22  ? 224 LEU A CD1 1 
ATOM   1791 C  CD1 B LEU A 1 223 ? -11.031 -19.673 2.949   0.50 21.82  ? 224 LEU A CD1 1 
ATOM   1792 C  CD2 A LEU A 1 223 ? -11.004 -18.259 0.260   0.50 24.79  ? 224 LEU A CD2 1 
ATOM   1793 C  CD2 B LEU A 1 223 ? -8.844  -18.838 3.827   0.50 21.93  ? 224 LEU A CD2 1 
ATOM   1794 N  N   . LYS A 1 224 ? -10.743 -13.925 2.153   1.00 13.30  ? 225 LYS A N   1 
ATOM   1795 C  CA  . LYS A 1 224 ? -10.445 -12.779 1.319   1.00 14.36  ? 225 LYS A CA  1 
ATOM   1796 C  C   . LYS A 1 224 ? -9.510  -11.773 2.005   1.00 12.56  ? 225 LYS A C   1 
ATOM   1797 O  O   . LYS A 1 224 ? -8.692  -11.160 1.352   1.00 13.66  ? 225 LYS A O   1 
ATOM   1798 C  CB  . LYS A 1 224 ? -11.740 -12.126 0.822   1.00 17.54  ? 225 LYS A CB  1 
ATOM   1799 C  CG  . LYS A 1 224 ? -12.514 -13.057 -0.105  1.00 21.88  ? 225 LYS A CG  1 
ATOM   1800 C  CD  . LYS A 1 224 ? -13.898 -12.481 -0.496  1.00 34.41  ? 225 LYS A CD  1 
ATOM   1801 C  CE  . LYS A 1 224 ? -14.318 -12.636 -1.945  1.00 36.48  ? 225 LYS A CE  1 
ATOM   1802 N  NZ  . LYS A 1 224 ? -14.857 -14.001 -2.195  1.00 43.06  ? 225 LYS A NZ  1 
ATOM   1803 N  N   . PHE A 1 225 ? -9.622  -11.573 3.329   1.00 11.44  ? 226 PHE A N   1 
ATOM   1804 C  CA  . PHE A 1 225 ? -8.655  -10.755 4.066   1.00 11.65  ? 226 PHE A CA  1 
ATOM   1805 C  C   . PHE A 1 225 ? -7.262  -11.331 3.788   1.00 11.51  ? 226 PHE A C   1 
ATOM   1806 O  O   . PHE A 1 225 ? -6.316  -10.574 3.599   1.00 12.48  ? 226 PHE A O   1 
ATOM   1807 C  CB  . PHE A 1 225 ? -8.847  -10.797 5.578   1.00 12.13  ? 226 PHE A CB  1 
ATOM   1808 C  CG  . PHE A 1 225 ? -10.027 -10.039 6.143   1.00 11.81  ? 226 PHE A CG  1 
ATOM   1809 C  CD1 . PHE A 1 225 ? -11.005 -9.522  5.309   1.00 13.32  ? 226 PHE A CD1 1 
ATOM   1810 C  CD2 . PHE A 1 225 ? -10.158 -9.843  7.509   1.00 14.07  ? 226 PHE A CD2 1 
ATOM   1811 C  CE1 . PHE A 1 225 ? -12.087 -8.828  5.827   1.00 14.28  ? 226 PHE A CE1 1 
ATOM   1812 C  CE2 . PHE A 1 225 ? -11.239 -9.149  8.026   1.00 16.52  ? 226 PHE A CE2 1 
ATOM   1813 C  CZ  . PHE A 1 225 ? -12.202 -8.642  7.185   1.00 13.51  ? 226 PHE A CZ  1 
ATOM   1814 N  N   . ARG A 1 226 ? -7.130  -12.665 3.855   1.00 11.89  ? 227 ARG A N   1 
ATOM   1815 C  CA  . ARG A 1 226 ? -5.801  -13.276 3.817   1.00 12.69  ? 227 ARG A CA  1 
ATOM   1816 C  C   . ARG A 1 226 ? -5.240  -13.293 2.412   1.00 11.76  ? 227 ARG A C   1 
ATOM   1817 O  O   . ARG A 1 226 ? -4.086  -13.710 2.220   1.00 15.29  ? 227 ARG A O   1 
ATOM   1818 C  CB  . ARG A 1 226 ? -5.913  -14.715 4.311   1.00 12.48  ? 227 ARG A CB  1 
ATOM   1819 C  CG  . ARG A 1 226 ? -6.326  -14.820 5.747   1.00 12.64  ? 227 ARG A CG  1 
ATOM   1820 C  CD  . ARG A 1 226 ? -6.304  -16.243 6.210   1.00 15.16  ? 227 ARG A CD  1 
ATOM   1821 N  NE  . ARG A 1 226 ? -6.806  -16.403 7.582   1.00 13.25  ? 227 ARG A NE  1 
ATOM   1822 C  CZ  . ARG A 1 226 ? -7.670  -17.337 7.963   1.00 14.13  ? 227 ARG A CZ  1 
ATOM   1823 N  NH1 . ARG A 1 226 ? -8.138  -18.205 7.083   1.00 19.45  ? 227 ARG A NH1 1 
ATOM   1824 N  NH2 . ARG A 1 226 ? -8.062  -17.400 9.223   1.00 16.76  ? 227 ARG A NH2 1 
ATOM   1825 N  N   . LYS A 1 227 ? -5.971  -12.817 1.386   1.00 13.23  ? 228 LYS A N   1 
ATOM   1826 C  CA  . LYS A 1 227 ? -5.436  -12.657 0.066   1.00 13.90  ? 228 LYS A CA  1 
ATOM   1827 C  C   . LYS A 1 227 ? -4.787  -11.315 -0.177  1.00 14.04  ? 228 LYS A C   1 
ATOM   1828 O  O   . LYS A 1 227 ? -4.076  -11.115 -1.161  1.00 15.38  ? 228 LYS A O   1 
ATOM   1829 C  CB  . LYS A 1 227 ? -6.557  -12.819 -0.987  1.00 16.67  ? 228 LYS A CB  1 
ATOM   1830 C  CG  . LYS A 1 227 ? -7.117  -14.220 -1.131  1.00 21.23  ? 228 LYS A CG  1 
ATOM   1831 C  CD  . LYS A 1 227 ? -8.246  -14.345 -2.172  1.00 27.23  ? 228 LYS A CD  1 
ATOM   1832 C  CE  . LYS A 1 227 ? -8.859  -15.743 -2.193  1.00 38.80  ? 228 LYS A CE  1 
ATOM   1833 N  NZ  . LYS A 1 227 ? -10.336 -15.772 -2.418  1.00 48.15  ? 228 LYS A NZ  1 
ATOM   1834 N  N   . LEU A 1 228 ? -4.922  -10.391 0.766   1.00 12.86  ? 229 LEU A N   1 
ATOM   1835 C  CA  . LEU A 1 228 ? -4.218  -9.135  0.662   1.00 12.16  ? 229 LEU A CA  1 
ATOM   1836 C  C   . LEU A 1 228 ? -2.716  -9.368  0.857   1.00 13.85  ? 229 LEU A C   1 
ATOM   1837 O  O   . LEU A 1 228 ? -2.263  -10.407 1.323   1.00 14.89  ? 229 LEU A O   1 
ATOM   1838 C  CB  . LEU A 1 228 ? -4.721  -8.206  1.799   1.00 12.79  ? 229 LEU A CB  1 
ATOM   1839 C  CG  . LEU A 1 228 ? -6.148  -7.706  1.565   1.00 12.26  ? 229 LEU A CG  1 
ATOM   1840 C  CD1 . LEU A 1 228 ? -6.623  -7.029  2.851   1.00 12.66  ? 229 LEU A CD1 1 
ATOM   1841 C  CD2 . LEU A 1 228 ? -6.198  -6.739  0.406   1.00 14.70  ? 229 LEU A CD2 1 
ATOM   1842 N  N   . ASN A 1 229 ? -1.931  -8.408  0.389   1.00 13.65  ? 230 ASN A N   1 
ATOM   1843 C  CA  . ASN A 1 229 ? -0.468  -8.465  0.449   1.00 13.21  ? 230 ASN A CA  1 
ATOM   1844 C  C   . ASN A 1 229 ? 0.039   -7.319  1.294   1.00 14.60  ? 230 ASN A C   1 
ATOM   1845 O  O   . ASN A 1 229 ? -0.417  -6.179  1.236   1.00 13.91  ? 230 ASN A O   1 
ATOM   1846 C  CB  . ASN A 1 229 ? 0.107   -8.225  -0.919  1.00 15.26  ? 230 ASN A CB  1 
ATOM   1847 C  CG  . ASN A 1 229 ? 0.072   -9.433  -1.813  1.00 18.21  ? 230 ASN A CG  1 
ATOM   1848 O  OD1 . ASN A 1 229 ? 0.654   -9.367  -2.872  1.00 24.97  ? 230 ASN A OD1 1 
ATOM   1849 N  ND2 . ASN A 1 229 ? -0.673  -10.472 -1.491  1.00 20.67  ? 230 ASN A ND2 1 
ATOM   1850 N  N   . PHE A 1 230 ? 1.074   -7.631  2.087   1.00 14.00  ? 231 PHE A N   1 
ATOM   1851 C  CA  . PHE A 1 230 ? 1.782   -6.569  2.798   1.00 14.51  ? 231 PHE A CA  1 
ATOM   1852 C  C   . PHE A 1 230 ? 2.584   -5.717  1.829   1.00 15.69  ? 231 PHE A C   1 
ATOM   1853 O  O   . PHE A 1 230 ? 2.844   -4.543  2.026   1.00 15.37  ? 231 PHE A O   1 
ATOM   1854 C  CB  . PHE A 1 230 ? 2.794   -7.196  3.783   1.00 15.12  ? 231 PHE A CB  1 
ATOM   1855 C  CG  . PHE A 1 230 ? 2.282   -7.744  5.085   1.00 14.01  ? 231 PHE A CG  1 
ATOM   1856 C  CD1 . PHE A 1 230 ? 1.491   -6.937  5.927   1.00 14.88  ? 231 PHE A CD1 1 
ATOM   1857 C  CD2 . PHE A 1 230 ? 2.578   -9.041  5.515   1.00 15.12  ? 231 PHE A CD2 1 
ATOM   1858 C  CE1 . PHE A 1 230 ? 1.117   -7.407  7.175   1.00 13.77  ? 231 PHE A CE1 1 
ATOM   1859 C  CE2 . PHE A 1 230 ? 2.176   -9.507  6.747   1.00 15.32  ? 231 PHE A CE2 1 
ATOM   1860 C  CZ  . PHE A 1 230 ? 1.378   -8.704  7.568   1.00 15.31  ? 231 PHE A CZ  1 
ATOM   1861 N  N   . ASN A 1 231 ? 3.167   -6.375  0.835   1.00 16.13  ? 232 ASN A N   1 
ATOM   1862 C  CA  . ASN A 1 231 ? 4.101   -5.785  -0.087  1.00 17.12  ? 232 ASN A CA  1 
ATOM   1863 C  C   . ASN A 1 231 ? 3.409   -4.921  -1.139  1.00 16.46  ? 232 ASN A C   1 
ATOM   1864 O  O   . ASN A 1 231 ? 2.215   -5.074  -1.447  1.00 15.69  ? 232 ASN A O   1 
ATOM   1865 C  CB  . ASN A 1 231 ? 4.854   -6.919  -0.827  1.00 19.20  ? 232 ASN A CB  1 
ATOM   1866 C  CG  . ASN A 1 231 ? 3.882   -7.869  -1.508  1.00 16.09  ? 232 ASN A CG  1 
ATOM   1867 O  OD1 . ASN A 1 231 ? 3.291   -8.753  -0.869  1.00 16.97  ? 232 ASN A OD1 1 
ATOM   1868 N  ND2 . ASN A 1 231 ? 3.761   -7.693  -2.827  1.00 21.41  ? 232 ASN A ND2 1 
ATOM   1869 N  N   . GLY A 1 232 ? 4.191   -4.019  -1.733  1.00 16.89  ? 233 GLY A N   1 
ATOM   1870 C  CA  . GLY A 1 232 ? 3.801   -3.293  -2.919  1.00 18.87  ? 233 GLY A CA  1 
ATOM   1871 C  C   . GLY A 1 232 ? 3.872   -4.224  -4.160  1.00 19.84  ? 233 GLY A C   1 
ATOM   1872 O  O   . GLY A 1 232 ? 4.544   -5.275  -4.146  1.00 19.32  ? 233 GLY A O   1 
ATOM   1873 N  N   . GLU A 1 233 ? 3.091   -3.857  -5.174  1.00 23.73  ? 234 GLU A N   1 
ATOM   1874 C  CA  . GLU A 1 233 ? 3.104   -4.573  -6.453  1.00 29.28  ? 234 GLU A CA  1 
ATOM   1875 C  C   . GLU A 1 233 ? 4.537   -4.595  -7.009  1.00 33.39  ? 234 GLU A C   1 
ATOM   1876 O  O   . GLU A 1 233 ? 5.212   -3.584  -6.965  1.00 29.92  ? 234 GLU A O   1 
ATOM   1877 C  CB  . GLU A 1 233 ? 2.187   -3.890  -7.459  1.00 36.88  ? 234 GLU A CB  1 
ATOM   1878 C  CG  . GLU A 1 233 ? 2.051   -4.682  -8.766  1.00 58.48  ? 234 GLU A CG  1 
ATOM   1879 C  CD  . GLU A 1 233 ? 0.900   -4.215  -9.649  1.00 61.46  ? 234 GLU A CD  1 
ATOM   1880 O  OE1 . GLU A 1 233 ? 0.276   -3.164  -9.340  1.00 48.07  ? 234 GLU A OE1 1 
ATOM   1881 O  OE2 . GLU A 1 233 ? 0.638   -4.890  -10.657 1.00 79.34  ? 234 GLU A OE2 1 
ATOM   1882 N  N   . GLY A 1 234 ? 5.047   -5.770  -7.395  1.00 40.92  ? 235 GLY A N   1 
ATOM   1883 C  CA  . GLY A 1 234 ? 6.420   -5.848  -7.899  1.00 50.74  ? 235 GLY A CA  1 
ATOM   1884 C  C   . GLY A 1 234 ? 7.348   -6.569  -6.921  1.00 74.18  ? 235 GLY A C   1 
ATOM   1885 O  O   . GLY A 1 234 ? 8.192   -7.368  -7.327  1.00 108.28 ? 235 GLY A O   1 
ATOM   1886 N  N   . GLU A 1 235 ? 7.163   -6.291  -5.625  1.00 61.13  ? 236 GLU A N   1 
ATOM   1887 C  CA  . GLU A 1 235 ? 8.012   -6.794  -4.558  1.00 28.65  ? 236 GLU A CA  1 
ATOM   1888 C  C   . GLU A 1 235 ? 7.674   -8.224  -4.195  1.00 20.52  ? 236 GLU A C   1 
ATOM   1889 O  O   . GLU A 1 235 ? 6.571   -8.649  -4.592  1.00 23.28  ? 236 GLU A O   1 
ATOM   1890 C  CB  . GLU A 1 235 ? 7.827   -5.937  -3.299  1.00 22.03  ? 236 GLU A CB  1 
ATOM   1891 C  CG  . GLU A 1 235 ? 7.856   -4.429  -3.586  1.00 23.99  ? 236 GLU A CG  1 
ATOM   1892 C  CD  . GLU A 1 235 ? 7.401   -3.461  -2.477  1.00 35.04  ? 236 GLU A CD  1 
ATOM   1893 O  OE1 . GLU A 1 235 ? 7.104   -3.886  -1.282  1.00 32.58  ? 236 GLU A OE1 1 
ATOM   1894 O  OE2 . GLU A 1 235 ? 7.258   -2.243  -2.804  1.00 36.96  ? 236 GLU A OE2 1 
ATOM   1895 N  N   . PRO A 1 236 ? 8.564   -8.982  -3.502  1.00 21.28  ? 237 PRO A N   1 
ATOM   1896 C  CA  . PRO A 1 236 ? 8.204   -10.371 -3.174  1.00 22.62  ? 237 PRO A CA  1 
ATOM   1897 C  C   . PRO A 1 236 ? 6.844   -10.423 -2.477  1.00 18.80  ? 237 PRO A C   1 
ATOM   1898 O  O   . PRO A 1 236 ? 6.501   -9.632  -1.580  1.00 19.67  ? 237 PRO A O   1 
ATOM   1899 C  CB  . PRO A 1 236 ? 9.364   -10.842 -2.279  1.00 27.55  ? 237 PRO A CB  1 
ATOM   1900 C  CG  . PRO A 1 236 ? 10.499  -10.002 -2.794  1.00 25.91  ? 237 PRO A CG  1 
ATOM   1901 C  CD  . PRO A 1 236 ? 9.959   -8.633  -3.073  1.00 24.41  ? 237 PRO A CD  1 
ATOM   1902 N  N   . GLU A 1 237 ? 6.066   -11.437 -2.845  1.00 17.52  ? 238 GLU A N   1 
ATOM   1903 C  CA  . GLU A 1 237 ? 4.709   -11.567 -2.339  1.00 16.74  ? 238 GLU A CA  1 
ATOM   1904 C  C   . GLU A 1 237 ? 4.695   -12.134 -0.913  1.00 16.15  ? 238 GLU A C   1 
ATOM   1905 O  O   . GLU A 1 237 ? 5.127   -13.290 -0.663  1.00 18.62  ? 238 GLU A O   1 
ATOM   1906 C  CB  . GLU A 1 237 ? 4.033   -12.496 -3.331  1.00 19.27  ? 238 GLU A CB  1 
ATOM   1907 C  CG  . GLU A 1 237 ? 2.587   -12.760 -2.997  1.00 23.84  ? 238 GLU A CG  1 
ATOM   1908 C  CD  . GLU A 1 237 ? 2.057   -13.789 -3.985  1.00 29.60  ? 238 GLU A CD  1 
ATOM   1909 O  OE1 . GLU A 1 237 ? 2.790   -14.120 -4.975  1.00 33.24  ? 238 GLU A OE1 1 
ATOM   1910 O  OE2 . GLU A 1 237 ? 0.979   -14.354 -3.690  1.00 29.51  ? 238 GLU A OE2 1 
ATOM   1911 N  N   . GLU A 1 238 ? 4.173   -11.333 0.019   1.00 15.78  ? 239 GLU A N   1 
ATOM   1912 C  CA  . GLU A 1 238 ? 4.034   -11.738 1.392   1.00 16.57  ? 239 GLU A CA  1 
ATOM   1913 C  C   . GLU A 1 238 ? 2.598   -11.463 1.790   1.00 14.20  ? 239 GLU A C   1 
ATOM   1914 O  O   . GLU A 1 238 ? 2.136   -10.315 1.799   1.00 17.49  ? 239 GLU A O   1 
ATOM   1915 C  CB  . GLU A 1 238 ? 4.976   -10.919 2.277   1.00 19.87  ? 239 GLU A CB  1 
ATOM   1916 C  CG  . GLU A 1 238 ? 6.436   -11.276 2.062   1.00 25.02  ? 239 GLU A CG  1 
ATOM   1917 C  CD  . GLU A 1 238 ? 7.379   -10.565 3.024   1.00 23.75  ? 239 GLU A CD  1 
ATOM   1918 O  OE1 . GLU A 1 238 ? 7.378   -10.942 4.230   1.00 31.37  ? 239 GLU A OE1 1 
ATOM   1919 O  OE2 . GLU A 1 238 ? 8.093   -9.591  2.616   1.00 32.83  ? 239 GLU A OE2 1 
ATOM   1920 N  N   . LEU A 1 239 ? 1.808   -12.525 2.008   1.00 15.91  ? 240 LEU A N   1 
ATOM   1921 C  CA  . LEU A 1 239 ? 0.418   -12.336 2.348   1.00 15.33  ? 240 LEU A CA  1 
ATOM   1922 C  C   . LEU A 1 239 ? 0.289   -11.509 3.608   1.00 13.94  ? 240 LEU A C   1 
ATOM   1923 O  O   . LEU A 1 239 ? 1.010   -11.703 4.594   1.00 15.19  ? 240 LEU A O   1 
ATOM   1924 C  CB  . LEU A 1 239 ? -0.257  -13.692 2.536   1.00 17.69  ? 240 LEU A CB  1 
ATOM   1925 C  CG  . LEU A 1 239 ? -0.386  -14.561 1.297   1.00 19.08  ? 240 LEU A CG  1 
ATOM   1926 C  CD1 . LEU A 1 239 ? -1.179  -15.798 1.703   1.00 25.36  ? 240 LEU A CD1 1 
ATOM   1927 C  CD2 . LEU A 1 239 ? -1.097  -13.729 0.233   1.00 22.08  ? 240 LEU A CD2 1 
ATOM   1928 N  N   . MET A 1 240 ? -0.725  -10.631 3.602   1.00 14.39  ? 241 MET A N   1 
ATOM   1929 C  CA  . MET A 1 240 ? -1.062  -9.828  4.773   1.00 13.02  ? 241 MET A CA  1 
ATOM   1930 C  C   . MET A 1 240 ? -1.871  -10.693 5.713   1.00 12.08  ? 241 MET A C   1 
ATOM   1931 O  O   . MET A 1 240 ? -3.072  -10.817 5.553   1.00 13.14  ? 241 MET A O   1 
ATOM   1932 C  CB  . MET A 1 240 ? -1.844  -8.585  4.339   1.00 13.13  ? 241 MET A CB  1 
ATOM   1933 C  CG  . MET A 1 240 ? -2.138  -7.637  5.492   1.00 12.90  ? 241 MET A CG  1 
ATOM   1934 S  SD  . MET A 1 240 ? -3.120  -6.202  4.984   1.00 13.18  ? 241 MET A SD  1 
ATOM   1935 C  CE  . MET A 1 240 ? -1.807  -5.183  4.315   1.00 14.69  ? 241 MET A CE  1 
ATOM   1936 N  N   . VAL A 1 241 ? -1.150  -11.362 6.613   1.00 11.60  ? 242 VAL A N   1 
ATOM   1937 C  CA  . VAL A 1 241 ? -1.744  -12.185 7.660   1.00 12.03  ? 242 VAL A CA  1 
ATOM   1938 C  C   . VAL A 1 241 ? -0.936  -11.971 8.912   1.00 9.75   ? 242 VAL A C   1 
ATOM   1939 O  O   . VAL A 1 241 ? 0.262   -11.569 8.831   1.00 12.31  ? 242 VAL A O   1 
ATOM   1940 C  CB  . VAL A 1 241 ? -1.738  -13.680 7.269   1.00 12.63  ? 242 VAL A CB  1 
ATOM   1941 C  CG1 . VAL A 1 241 ? -2.661  -13.886 6.071   1.00 14.73  ? 242 VAL A CG1 1 
ATOM   1942 C  CG2 . VAL A 1 241 ? -0.323  -14.200 6.972   1.00 14.46  ? 242 VAL A CG2 1 
ATOM   1943 N  N   . ASP A 1 242 ? -1.509  -12.239 10.059  1.00 10.83  ? 243 ASP A N   1 
ATOM   1944 C  CA  . ASP A 1 242 ? -0.869  -12.099 11.337  1.00 10.72  ? 243 ASP A CA  1 
ATOM   1945 C  C   . ASP A 1 242 ? -0.370  -10.685 11.547  1.00 10.47  ? 243 ASP A C   1 
ATOM   1946 O  O   . ASP A 1 242 ? 0.723   -10.440 12.082  1.00 11.75  ? 243 ASP A O   1 
ATOM   1947 C  CB  . ASP A 1 242 ? 0.220   -13.176 11.521  1.00 11.72  ? 243 ASP A CB  1 
ATOM   1948 C  CG  . ASP A 1 242 ? -0.397  -14.522 11.598  1.00 11.92  ? 243 ASP A CG  1 
ATOM   1949 O  OD1 . ASP A 1 242 ? -1.403  -14.691 12.310  1.00 11.49  ? 243 ASP A OD1 1 
ATOM   1950 O  OD2 . ASP A 1 242 ? 0.247   -15.466 11.055  1.00 14.25  ? 243 ASP A OD2 1 
ATOM   1951 N  N   . ASN A 1 243 ? -1.236  -9.732  11.243  1.00 9.70   ? 244 ASN A N   1 
ATOM   1952 C  CA  . ASN A 1 243 ? -0.984  -8.300  11.438  1.00 9.18   ? 244 ASN A CA  1 
ATOM   1953 C  C   . ASN A 1 243 ? -1.552  -7.845  12.782  1.00 8.73   ? 244 ASN A C   1 
ATOM   1954 O  O   . ASN A 1 243 ? -2.285  -6.848  12.858  1.00 10.64  ? 244 ASN A O   1 
ATOM   1955 C  CB  . ASN A 1 243 ? -1.469  -7.457  10.262  1.00 9.97   ? 244 ASN A CB  1 
ATOM   1956 C  CG  . ASN A 1 243 ? -2.953  -7.642  9.990   1.00 9.71   ? 244 ASN A CG  1 
ATOM   1957 O  OD1 . ASN A 1 243 ? -3.611  -8.500  10.546  1.00 11.61  ? 244 ASN A OD1 1 
ATOM   1958 N  ND2 . ASN A 1 243 ? -3.466  -6.738  9.156   1.00 12.63  ? 244 ASN A ND2 1 
ATOM   1959 N  N   . TRP A 1 244 ? -1.239  -8.569  13.858  1.00 9.37   ? 245 TRP A N   1 
ATOM   1960 C  CA  . TRP A 1 244 ? -1.681  -8.325  15.206  1.00 9.07   ? 245 TRP A CA  1 
ATOM   1961 C  C   . TRP A 1 244 ? -0.462  -8.169  16.099  1.00 9.80   ? 245 TRP A C   1 
ATOM   1962 O  O   . TRP A 1 244 ? 0.494   -8.924  15.998  1.00 10.90  ? 245 TRP A O   1 
ATOM   1963 C  CB  . TRP A 1 244 ? -2.656  -9.408  15.708  1.00 9.40   ? 245 TRP A CB  1 
ATOM   1964 C  CG  . TRP A 1 244 ? -2.177  -10.815 15.535  1.00 8.85   ? 245 TRP A CG  1 
ATOM   1965 C  CD1 . TRP A 1 244 ? -2.289  -11.562 14.411  1.00 10.25  ? 245 TRP A CD1 1 
ATOM   1966 C  CD2 . TRP A 1 244 ? -1.576  -11.653 16.516  1.00 9.63   ? 245 TRP A CD2 1 
ATOM   1967 N  NE1 . TRP A 1 244 ? -1.787  -12.818 14.589  1.00 10.78  ? 245 TRP A NE1 1 
ATOM   1968 C  CE2 . TRP A 1 244 ? -1.358  -12.899 15.892  1.00 10.34  ? 245 TRP A CE2 1 
ATOM   1969 C  CE3 . TRP A 1 244 ? -1.305  -11.502 17.889  1.00 10.29  ? 245 TRP A CE3 1 
ATOM   1970 C  CZ2 . TRP A 1 244 ? -0.763  -13.986 16.565  1.00 11.65  ? 245 TRP A CZ2 1 
ATOM   1971 C  CZ3 . TRP A 1 244 ? -0.735  -12.574 18.551  1.00 12.05  ? 245 TRP A CZ3 1 
ATOM   1972 C  CH2 . TRP A 1 244 ? -0.464  -13.774 17.896  1.00 12.41  ? 245 TRP A CH2 1 
ATOM   1973 N  N   . ARG A 1 245 ? -0.606  -7.244  17.052  1.00 9.75   ? 246 ARG A N   1 
ATOM   1974 C  CA  . ARG A 1 245 ? 0.342   -7.137  18.159  1.00 9.40   ? 246 ARG A CA  1 
ATOM   1975 C  C   . ARG A 1 245 ? -0.136  -8.057  19.266  1.00 9.31   ? 246 ARG A C   1 
ATOM   1976 O  O   . ARG A 1 245 ? -1.310  -8.082  19.600  1.00 10.69  ? 246 ARG A O   1 
ATOM   1977 C  CB  . ARG A 1 245 ? 0.365   -5.685  18.660  1.00 9.57   ? 246 ARG A CB  1 
ATOM   1978 C  CG  . ARG A 1 245 ? 1.502   -5.440  19.676  1.00 9.83   ? 246 ARG A CG  1 
ATOM   1979 C  CD  . ARG A 1 245 ? 1.370   -4.083  20.271  1.00 10.20  ? 246 ARG A CD  1 
ATOM   1980 N  NE  . ARG A 1 245 ? 2.668   -3.777  20.965  1.00 9.89   ? 246 ARG A NE  1 
ATOM   1981 C  CZ  . ARG A 1 245 ? 2.851   -2.765  21.805  1.00 10.40  ? 246 ARG A CZ  1 
ATOM   1982 N  NH1 . ARG A 1 245 ? 1.853   -1.943  22.079  1.00 11.02  ? 246 ARG A NH1 1 
ATOM   1983 N  NH2 . ARG A 1 245 ? 4.032   -2.578  22.367  1.00 11.87  ? 246 ARG A NH2 1 
ATOM   1984 N  N   . PRO A 1 246 ? 0.776   -8.855  19.878  1.00 10.59  ? 247 PRO A N   1 
ATOM   1985 C  CA  . PRO A 1 246 ? 0.336   -9.660  21.001  1.00 11.13  ? 247 PRO A CA  1 
ATOM   1986 C  C   . PRO A 1 246 ? 0.007   -8.832  22.249  1.00 10.56  ? 247 PRO A C   1 
ATOM   1987 O  O   . PRO A 1 246 ? 0.357   -7.659  22.393  1.00 10.57  ? 247 PRO A O   1 
ATOM   1988 C  CB  . PRO A 1 246 ? 1.557   -10.562 21.274  1.00 13.27  ? 247 PRO A CB  1 
ATOM   1989 C  CG  . PRO A 1 246 ? 2.398   -10.418 20.065  1.00 18.49  ? 247 PRO A CG  1 
ATOM   1990 C  CD  . PRO A 1 246 ? 2.194   -9.028  19.542  1.00 12.11  ? 247 PRO A CD  1 
ATOM   1991 N  N   . ALA A 1 247 ? -0.645  -9.471  23.223  1.00 10.90  ? 248 ALA A N   1 
ATOM   1992 C  CA  . ALA A 1 247 ? -0.982  -8.871  24.492  1.00 10.52  ? 248 ALA A CA  1 
ATOM   1993 C  C   . ALA A 1 247 ? 0.259   -8.341  25.189  1.00 10.02  ? 248 ALA A C   1 
ATOM   1994 O  O   . ALA A 1 247 ? 1.293   -9.024  25.240  1.00 12.31  ? 248 ALA A O   1 
ATOM   1995 C  CB  . ALA A 1 247 ? -1.703  -9.871  25.378  1.00 12.81  ? 248 ALA A CB  1 
ATOM   1996 N  N   . GLN A 1 248 ? 0.106   -7.175  25.773  1.00 9.91   ? 249 GLN A N   1 
ATOM   1997 C  CA  . GLN A 1 248 ? 1.144   -6.444  26.487  1.00 9.70   ? 249 GLN A CA  1 
ATOM   1998 C  C   . GLN A 1 248 ? 0.844   -6.445  27.962  1.00 11.00  ? 249 GLN A C   1 
ATOM   1999 O  O   . GLN A 1 248 ? -0.283  -6.689  28.396  1.00 11.66  ? 249 GLN A O   1 
ATOM   2000 C  CB  . GLN A 1 248 ? 1.191   -5.017  25.930  1.00 10.90  ? 249 GLN A CB  1 
ATOM   2001 C  CG  . GLN A 1 248 ? 1.489   -4.943  24.460  1.00 10.94  ? 249 GLN A CG  1 
ATOM   2002 C  CD  . GLN A 1 248 ? 2.808   -5.608  24.120  1.00 11.96  ? 249 GLN A CD  1 
ATOM   2003 O  OE1 . GLN A 1 248 ? 3.873   -5.290  24.686  1.00 14.89  ? 249 GLN A OE1 1 
ATOM   2004 N  NE2 . GLN A 1 248 ? 2.806   -6.538  23.179  1.00 12.56  ? 249 GLN A NE2 1 
ATOM   2005 N  N   . PRO A 1 249 ? 1.854   -6.145  28.807  1.00 12.29  ? 250 PRO A N   1 
ATOM   2006 C  CA  . PRO A 1 249 ? 1.648   -6.212  30.247  1.00 14.23  ? 250 PRO A CA  1 
ATOM   2007 C  C   . PRO A 1 249 ? 0.575   -5.231  30.691  1.00 12.14  ? 250 PRO A C   1 
ATOM   2008 O  O   . PRO A 1 249 ? 0.602   -4.053  30.358  1.00 12.46  ? 250 PRO A O   1 
ATOM   2009 C  CB  . PRO A 1 249 ? 3.031   -5.771  30.797  1.00 17.86  ? 250 PRO A CB  1 
ATOM   2010 C  CG  . PRO A 1 249 ? 3.992   -6.246  29.753  1.00 18.97  ? 250 PRO A CG  1 
ATOM   2011 C  CD  . PRO A 1 249 ? 3.278   -5.908  28.453  1.00 15.18  ? 250 PRO A CD  1 
ATOM   2012 N  N   . LEU A 1 250 ? -0.285  -5.695  31.582  1.00 12.71  ? 251 LEU A N   1 
ATOM   2013 C  CA  . LEU A 1 250 ? -1.370  -4.875  32.081  1.00 12.11  ? 251 LEU A CA  1 
ATOM   2014 C  C   . LEU A 1 250 ? -0.836  -3.793  33.006  1.00 12.15  ? 251 LEU A C   1 
ATOM   2015 O  O   . LEU A 1 250 ? -1.400  -2.708  33.122  1.00 12.12  ? 251 LEU A O   1 
ATOM   2016 C  CB  . LEU A 1 250 ? -2.383  -5.766  32.813  1.00 14.63  ? 251 LEU A CB  1 
ATOM   2017 C  CG  . LEU A 1 250 ? -3.679  -5.053  33.240  1.00 15.01  ? 251 LEU A CG  1 
ATOM   2018 C  CD1 . LEU A 1 250 ? -4.428  -4.467  32.027  1.00 15.31  ? 251 LEU A CD1 1 
ATOM   2019 C  CD2 . LEU A 1 250 ? -4.568  -6.029  33.987  1.00 19.61  ? 251 LEU A CD2 1 
ATOM   2020 N  N   . LYS A 1 251 ? 0.244   -4.093  33.742  1.00 13.68  ? 252 LYS A N   1 
ATOM   2021 C  CA  . LYS A 1 251 ? 0.858   -3.086  34.641  1.00 15.06  ? 252 LYS A CA  1 
ATOM   2022 C  C   . LYS A 1 251 ? -0.186  -2.535  35.611  1.00 15.75  ? 252 LYS A C   1 
ATOM   2023 O  O   . LYS A 1 251 ? -0.918  -3.355  36.145  1.00 20.26  ? 252 LYS A O   1 
ATOM   2024 C  CB  . LYS A 1 251 ? 1.676   -2.020  33.893  1.00 17.65  ? 252 LYS A CB  1 
ATOM   2025 C  CG  . LYS A 1 251 ? 2.794   -2.676  33.080  1.00 21.86  ? 252 LYS A CG  1 
ATOM   2026 C  CD  . LYS A 1 251 ? 3.684   -1.785  32.351  1.00 22.35  ? 252 LYS A CD  1 
ATOM   2027 C  CE  . LYS A 1 251 ? 5.017   -2.457  32.117  1.00 25.47  ? 252 LYS A CE  1 
ATOM   2028 N  NZ  . LYS A 1 251 ? 5.879   -1.581  31.267  1.00 32.74  ? 252 LYS A NZ  1 
ATOM   2029 N  N   . ASN A 1 252 ? -0.212  -1.235  35.862  1.00 15.08  ? 253 ASN A N   1 
ATOM   2030 C  CA  . ASN A 1 252 ? -1.061  -0.785  36.938  1.00 23.92  ? 253 ASN A CA  1 
ATOM   2031 C  C   . ASN A 1 252 ? -2.405  -0.377  36.334  1.00 22.76  ? 253 ASN A C   1 
ATOM   2032 O  O   . ASN A 1 252 ? -2.667  0.877   36.368  1.00 30.87  ? 253 ASN A O   1 
ATOM   2033 C  CB  . ASN A 1 252 ? -0.298  0.293   37.712  1.00 29.92  ? 253 ASN A CB  1 
ATOM   2034 C  CG  . ASN A 1 252 ? -1.090  0.951   38.820  1.00 35.65  ? 253 ASN A CG  1 
ATOM   2035 O  OD1 . ASN A 1 252 ? -1.789  0.276   39.560  1.00 51.02  ? 253 ASN A OD1 1 
ATOM   2036 N  ND2 . ASN A 1 252 ? -1.040  2.269   38.907  1.00 35.84  ? 253 ASN A ND2 1 
ATOM   2037 N  N   . ARG A 1 253 ? -3.123  -1.380  35.672  1.00 16.16  ? 254 ARG A N   1 
ATOM   2038 C  CA  . ARG A 1 253 ? -4.422  -1.010  35.144  1.00 12.69  ? 254 ARG A CA  1 
ATOM   2039 C  C   . ARG A 1 253 ? -5.478  -2.001  35.572  1.00 14.44  ? 254 ARG A C   1 
ATOM   2040 O  O   . ARG A 1 253 ? -5.256  -3.187  35.779  1.00 20.39  ? 254 ARG A O   1 
ATOM   2041 C  CB  . ARG A 1 253 ? -4.340  -0.959  33.635  1.00 11.96  ? 254 ARG A CB  1 
ATOM   2042 C  CG  . ARG A 1 253 ? -3.434  0.171   33.154  1.00 11.65  ? 254 ARG A CG  1 
ATOM   2043 C  CD  . ARG A 1 253 ? -3.310  0.187   31.666  1.00 11.33  ? 254 ARG A CD  1 
ATOM   2044 N  NE  . ARG A 1 253 ? -2.520  -0.942  31.214  1.00 9.72   ? 254 ARG A NE  1 
ATOM   2045 C  CZ  . ARG A 1 253 ? -2.298  -1.192  29.932  1.00 9.22   ? 254 ARG A CZ  1 
ATOM   2046 N  NH1 . ARG A 1 253 ? -2.907  -0.507  28.953  1.00 9.67   ? 254 ARG A NH1 1 
ATOM   2047 N  NH2 . ARG A 1 253 ? -1.463  -2.180  29.593  1.00 9.76   ? 254 ARG A NH2 1 
ATOM   2048 N  N   A GLN A 1 254 ? -6.677  -1.461  35.663  0.50 12.90  ? 255 GLN A N   1 
ATOM   2049 N  N   B GLN A 1 254 ? -6.672  -1.471  35.709  0.50 16.04  ? 255 GLN A N   1 
ATOM   2050 C  CA  A GLN A 1 254 ? -7.882  -2.212  35.967  0.50 15.37  ? 255 GLN A CA  1 
ATOM   2051 C  CA  B GLN A 1 254 ? -7.840  -2.290  35.965  0.50 16.76  ? 255 GLN A CA  1 
ATOM   2052 C  C   A GLN A 1 254 ? -8.716  -2.197  34.685  0.50 14.00  ? 255 GLN A C   1 
ATOM   2053 C  C   B GLN A 1 254 ? -8.724  -2.212  34.730  0.50 15.51  ? 255 GLN A C   1 
ATOM   2054 O  O   A GLN A 1 254 ? -8.893  -1.171  33.991  0.50 15.36  ? 255 GLN A O   1 
ATOM   2055 O  O   B GLN A 1 254 ? -8.964  -1.145  34.150  0.50 21.48  ? 255 GLN A O   1 
ATOM   2056 C  CB  A GLN A 1 254 ? -8.668  -1.567  37.111  0.50 19.32  ? 255 GLN A CB  1 
ATOM   2057 C  CB  B GLN A 1 254 ? -8.642  -1.679  37.093  0.50 20.79  ? 255 GLN A CB  1 
ATOM   2058 C  CG  A GLN A 1 254 ? -9.761  -2.468  37.697  0.50 21.51  ? 255 GLN A CG  1 
ATOM   2059 C  CG  B GLN A 1 254 ? -7.889  -1.790  38.388  0.50 20.95  ? 255 GLN A CG  1 
ATOM   2060 N  N   . ILE A 1 255 ? -9.229  -3.378  34.346  1.00 12.25  ? 256 ILE A N   1 
ATOM   2061 C  CA  . ILE A 1 255 ? -10.214 -3.462  33.262  1.00 11.57  ? 256 ILE A CA  1 
ATOM   2062 C  C   . ILE A 1 255 ? -11.577 -3.457  33.935  1.00 11.80  ? 256 ILE A C   1 
ATOM   2063 O  O   . ILE A 1 255 ? -11.806 -4.194  34.908  1.00 13.14  ? 256 ILE A O   1 
ATOM   2064 C  CB  . ILE A 1 255 ? -10.019 -4.716  32.450  1.00 12.59  ? 256 ILE A CB  1 
ATOM   2065 C  CG1 . ILE A 1 255 ? -8.581  -4.743  31.908  1.00 14.01  ? 256 ILE A CG1 1 
ATOM   2066 C  CG2 . ILE A 1 255 ? -11.064 -4.778  31.312  1.00 13.70  ? 256 ILE A CG2 1 
ATOM   2067 C  CD1 . ILE A 1 255 ? -8.293  -5.933  30.993  1.00 15.36  ? 256 ILE A CD1 1 
ATOM   2068 N  N   . LYS A 1 256 ? -12.466 -2.606  33.421  1.00 11.19  ? 257 LYS A N   1 
ATOM   2069 C  CA  . LYS A 1 256 ? -13.802 -2.491  33.964  1.00 11.65  ? 257 LYS A CA  1 
ATOM   2070 C  C   . LYS A 1 256 ? -14.783 -3.145  33.014  1.00 11.14  ? 257 LYS A C   1 
ATOM   2071 O  O   . LYS A 1 256 ? -14.596 -3.071  31.813  1.00 13.27  ? 257 LYS A O   1 
ATOM   2072 C  CB  . LYS A 1 256 ? -14.193 -1.031  34.186  1.00 13.19  ? 257 LYS A CB  1 
ATOM   2073 C  CG  . LYS A 1 256 ? -13.264 -0.333  35.214  1.00 19.28  ? 257 LYS A CG  1 
ATOM   2074 C  CD  . LYS A 1 256 ? -13.699 1.077   35.535  1.00 30.71  ? 257 LYS A CD  1 
ATOM   2075 N  N   . ALA A 1 257 ? -15.840 -3.768  33.518  1.00 12.02  ? 258 ALA A N   1 
ATOM   2076 C  CA  . ALA A 1 257 ? -16.925 -4.371  32.746  1.00 12.86  ? 258 ALA A CA  1 
ATOM   2077 C  C   . ALA A 1 257 ? -18.179 -3.531  32.909  1.00 12.51  ? 258 ALA A C   1 
ATOM   2078 O  O   . ALA A 1 257 ? -18.507 -3.119  34.006  1.00 13.56  ? 258 ALA A O   1 
ATOM   2079 C  CB  . ALA A 1 257 ? -17.165 -5.794  33.169  1.00 15.27  ? 258 ALA A CB  1 
ATOM   2080 N  N   . SER A 1 258 ? -18.915 -3.407  31.786  1.00 12.47  ? 259 SER A N   1 
ATOM   2081 C  CA  . SER A 1 258 ? -20.187 -2.674  31.847  1.00 13.19  ? 259 SER A CA  1 
ATOM   2082 C  C   . SER A 1 258 ? -21.323 -3.599  32.286  1.00 13.56  ? 259 SER A C   1 
ATOM   2083 O  O   . SER A 1 258 ? -22.460 -3.109  32.382  1.00 19.43  ? 259 SER A O   1 
ATOM   2084 C  CB  . SER A 1 258 ? -20.501 -2.102  30.489  1.00 14.35  ? 259 SER A CB  1 
ATOM   2085 O  OG  . SER A 1 258 ? -20.909 -3.100  29.590  1.00 13.99  ? 259 SER A OG  1 
ATOM   2086 N  N   . PHE A 1 259 ? -21.032 -4.880  32.546  1.00 15.09  ? 260 PHE A N   1 
ATOM   2087 C  CA  . PHE A 1 259 ? -22.047 -5.927  32.673  1.00 17.83  ? 260 PHE A CA  1 
ATOM   2088 C  C   . PHE A 1 259 ? -21.579 -6.873  33.766  1.00 20.20  ? 260 PHE A C   1 
ATOM   2089 O  O   . PHE A 1 259 ? -20.369 -7.035  34.024  1.00 19.72  ? 260 PHE A O   1 
ATOM   2090 C  CB  . PHE A 1 259 ? -22.294 -6.692  31.383  1.00 18.69  ? 260 PHE A CB  1 
ATOM   2091 C  CG  . PHE A 1 259 ? -21.029 -7.366  30.903  1.00 16.58  ? 260 PHE A CG  1 
ATOM   2092 C  CD1 . PHE A 1 259 ? -20.033 -6.665  30.242  1.00 14.54  ? 260 PHE A CD1 1 
ATOM   2093 C  CD2 . PHE A 1 259 ? -20.833 -8.724  31.204  1.00 21.05  ? 260 PHE A CD2 1 
ATOM   2094 C  CE1 . PHE A 1 259 ? -18.835 -7.333  29.890  1.00 16.81  ? 260 PHE A CE1 1 
ATOM   2095 C  CE2 . PHE A 1 259 ? -19.634 -9.375  30.915  1.00 22.87  ? 260 PHE A CE2 1 
ATOM   2096 C  CZ  . PHE A 1 259 ? -18.653 -8.677  30.212  1.00 19.66  ? 260 PHE A CZ  1 
ATOM   2097 N  N   . LYS A 1 260 ? -22.631 -7.440  34.364  1.00 29.53  ? 261 LYS A N   1 
ATOM   2098 C  CA  . LYS A 1 260 ? -22.776 -8.537  35.308  1.00 37.98  ? 261 LYS A CA  1 
ATOM   2099 C  C   . LYS A 1 260 ? -23.003 -8.057  36.751  1.00 46.84  ? 261 LYS A C   1 
ATOM   2100 O  O   . LYS A 1 260 ? -23.979 -7.344  37.062  1.00 59.87  ? 261 LYS A O   1 
ATOM   2101 C  CB  . LYS A 1 260 ? -21.910 -9.776  35.031  1.00 47.04  ? 261 LYS A CB  1 
ATOM   2102 C  CG  . LYS A 1 260 ? -22.297 -10.531 33.744  1.00 43.87  ? 261 LYS A CG  1 
ATOM   2103 C  CD  . LYS A 1 260 ? -23.745 -10.099 33.165  1.00 49.20  ? 261 LYS A CD  1 
ATOM   2104 O  OXT . LYS A 1 260 ? -22.255 -8.355  37.680  1.00 67.53  ? 261 LYS A OXT 1 
HETATM 2105 ZN ZN  . ZN  B 2 .   ? -6.202  -1.770  15.235  1.00 8.10   ? 301 ZN  A ZN  1 
HETATM 2106 S  S   . DMS C 3 .   ? 1.778   -11.672 14.874  1.00 22.37  ? 302 DMS A S   1 
HETATM 2107 O  O   . DMS C 3 .   ? 2.384   -12.966 14.385  1.00 31.67  ? 302 DMS A O   1 
HETATM 2108 C  C1  . DMS C 3 .   ? 2.074   -11.585 16.574  1.00 21.27  ? 302 DMS A C1  1 
HETATM 2109 C  C2  . DMS C 3 .   ? 2.935   -10.427 14.443  1.00 28.49  ? 302 DMS A C2  1 
HETATM 2110 O  O19 . 5EF D 4 .   ? -0.381  3.334   13.073  1.00 28.50  ? 303 5EF A O19 1 
HETATM 2111 C  C17 . 5EF D 4 .   ? -1.021  2.670   10.850  1.00 21.62  ? 303 5EF A C17 1 
HETATM 2112 C  C6  . 5EF D 4 .   ? -3.934  0.654   13.782  1.00 12.22  ? 303 5EF A C6  1 
HETATM 2113 F  F11 . 5EF D 4 .   ? -3.841  -0.672  13.896  1.00 12.89  ? 303 5EF A F11 1 
HETATM 2114 C  C5  . 5EF D 4 .   ? -4.480  1.453   14.779  1.00 10.86  ? 303 5EF A C5  1 
HETATM 2115 F  F12 . 5EF D 4 .   ? -3.021  0.287   11.633  1.00 17.27  ? 303 5EF A F12 1 
HETATM 2116 F  F13 . 5EF D 4 .   ? -5.030  3.605   15.360  1.00 13.91  ? 303 5EF A F13 1 
HETATM 2117 O  O16 . 5EF D 4 .   ? -3.053  4.389   10.543  1.00 24.04  ? 303 5EF A O16 1 
HETATM 2118 S  S14 . 5EF D 4 .   ? -2.854  3.023   10.729  1.00 19.82  ? 303 5EF A S14 1 
HETATM 2119 O  O15 . 5EF D 4 .   ? -3.492  2.222   9.763   1.00 22.60  ? 303 5EF A O15 1 
HETATM 2120 C  C18 . 5EF D 4 .   ? -0.162  3.616   11.649  1.00 22.39  ? 303 5EF A C18 1 
HETATM 2121 C  C8  . 5EF D 4 .   ? -3.542  2.505   12.271  1.00 15.21  ? 303 5EF A C8  1 
HETATM 2122 C  C7  . 5EF D 4 .   ? -3.494  1.137   12.558  1.00 14.28  ? 303 5EF A C7  1 
HETATM 2123 C  C9  . 5EF D 4 .   ? -3.989  3.335   13.255  1.00 12.58  ? 303 5EF A C9  1 
HETATM 2124 C  C10 . 5EF D 4 .   ? -4.473  2.806   14.448  1.00 12.36  ? 303 5EF A C10 1 
HETATM 2125 S  S1  . 5EF D 4 .   ? -5.146  0.881   16.340  1.00 10.09  ? 303 5EF A S1  1 
HETATM 2126 O  O3  . 5EF D 4 .   ? -6.503  1.304   16.275  1.00 10.39  ? 303 5EF A O3  1 
HETATM 2127 N  N4  . 5EF D 4 .   ? -5.055  -0.637  16.332  1.00 9.31   ? 303 5EF A N4  1 
HETATM 2128 O  O2  . 5EF D 4 .   ? -4.285  1.435   17.344  1.00 11.33  ? 303 5EF A O2  1 
HETATM 2129 N  N20 . 5EF D 4 .   ? -3.957  4.757   13.098  1.00 15.50  ? 303 5EF A N20 1 
HETATM 2130 C  C21 . 5EF D 4 .   ? -3.251  5.603   13.978  1.00 14.30  ? 303 5EF A C21 1 
HETATM 2131 C  C25 . 5EF D 4 .   ? -1.883  6.135   13.643  1.00 15.76  ? 303 5EF A C25 1 
HETATM 2132 C  C24 . 5EF D 4 .   ? -1.756  7.440   14.333  1.00 17.20  ? 303 5EF A C24 1 
HETATM 2133 C  C23 . 5EF D 4 .   ? -3.188  7.887   14.610  1.00 15.42  ? 303 5EF A C23 1 
HETATM 2134 C  C29 . 5EF D 4 .   ? -3.648  9.147   14.917  1.00 17.50  ? 303 5EF A C29 1 
HETATM 2135 C  C28 . 5EF D 4 .   ? -5.017  9.304   15.149  1.00 18.81  ? 303 5EF A C28 1 
HETATM 2136 C  C27 . 5EF D 4 .   ? -5.892  8.214   14.952  1.00 18.77  ? 303 5EF A C27 1 
HETATM 2137 C  C26 . 5EF D 4 .   ? -5.374  6.956   14.536  1.00 16.94  ? 303 5EF A C26 1 
HETATM 2138 C  C22 . 5EF D 4 .   ? -4.013  6.764   14.401  1.00 14.74  ? 303 5EF A C22 1 
HETATM 2139 O  O19 . 5EF E 4 .   ? -31.604 -5.787  5.633   1.00 68.30  ? 304 5EF A O19 1 
HETATM 2140 C  C17 . 5EF E 4 .   ? -29.348 -6.355  5.944   1.00 49.10  ? 304 5EF A C17 1 
HETATM 2141 C  C6  . 5EF E 4 .   ? -25.297 -4.556  4.564   1.00 28.49  ? 304 5EF A C6  1 
HETATM 2142 F  F11 . 5EF E 4 .   ? -24.909 -5.013  3.353   1.00 33.58  ? 304 5EF A F11 1 
HETATM 2143 C  C5  . 5EF E 4 .   ? -24.882 -3.333  5.141   1.00 29.35  ? 304 5EF A C5  1 
HETATM 2144 F  F12 . 5EF E 4 .   ? -26.654 -6.481  4.560   1.00 30.85  ? 304 5EF A F12 1 
HETATM 2145 F  F13 . 5EF E 4 .   ? -24.964 -1.913  6.986   1.00 35.61  ? 304 5EF A F13 1 
HETATM 2146 O  O16 . 5EF E 4 .   ? -28.609 -5.665  8.344   1.00 49.68  ? 304 5EF A O16 1 
HETATM 2147 S  S14 . 5EF E 4 .   ? -28.002 -6.163  7.097   1.00 33.09  ? 304 5EF A S14 1 
HETATM 2148 O  O15 . 5EF E 4 .   ? -27.201 -7.411  7.101   1.00 45.97  ? 304 5EF A O15 1 
HETATM 2149 C  C18 . 5EF E 4 .   ? -30.740 -6.467  6.552   1.00 57.25  ? 304 5EF A C18 1 
HETATM 2150 C  C8  . 5EF E 4 .   ? -26.840 -5.026  6.398   1.00 26.80  ? 304 5EF A C8  1 
HETATM 2151 C  C7  . 5EF E 4 .   ? -26.255 -5.377  5.184   1.00 26.08  ? 304 5EF A C7  1 
HETATM 2152 C  C9  . 5EF E 4 .   ? -26.386 -3.856  7.031   1.00 26.51  ? 304 5EF A C9  1 
HETATM 2153 C  C10 . 5EF E 4 .   ? -25.410 -3.050  6.372   1.00 26.69  ? 304 5EF A C10 1 
HETATM 2154 S  S1  . 5EF E 4 .   ? -23.483 -2.338  4.597   1.00 37.09  ? 304 5EF A S1  1 
HETATM 2155 O  O3  . 5EF E 4 .   ? -23.948 -0.990  4.380   1.00 26.77  ? 304 5EF A O3  1 
HETATM 2156 N  N4  . 5EF E 4 .   ? -22.470 -2.291  5.935   1.00 22.58  ? 304 5EF A N4  1 
HETATM 2157 O  O2  . 5EF E 4 .   ? -22.715 -3.064  3.613   1.00 29.61  ? 304 5EF A O2  1 
HETATM 2158 N  N20 . 5EF E 4 .   ? -26.884 -3.558  8.303   1.00 23.50  ? 304 5EF A N20 1 
HETATM 2159 C  C21 . 5EF E 4 .   ? -27.234 -2.247  8.871   1.00 23.95  ? 304 5EF A C21 1 
HETATM 2160 C  C25 . 5EF E 4 .   ? -27.306 -0.803  8.356   1.00 37.77  ? 304 5EF A C25 1 
HETATM 2161 C  C24 . 5EF E 4 .   ? -28.394 -0.209  9.307   1.00 30.80  ? 304 5EF A C24 1 
HETATM 2162 C  C23 . 5EF E 4 .   ? -28.392 -1.122  10.516  1.00 32.89  ? 304 5EF A C23 1 
HETATM 2163 C  C29 . 5EF E 4 .   ? -28.977 -0.939  11.800  1.00 31.55  ? 304 5EF A C29 1 
HETATM 2164 C  C28 . 5EF E 4 .   ? -28.782 -1.989  12.730  1.00 31.90  ? 304 5EF A C28 1 
HETATM 2165 C  C27 . 5EF E 4 .   ? -28.095 -3.194  12.493  1.00 31.14  ? 304 5EF A C27 1 
HETATM 2166 C  C26 . 5EF E 4 .   ? -27.488 -3.336  11.211  1.00 27.32  ? 304 5EF A C26 1 
HETATM 2167 C  C22 . 5EF E 4 .   ? -27.607 -2.284  10.281  1.00 26.07  ? 304 5EF A C22 1 
HETATM 2168 O  O   . HOH F 5 .   ? -8.240  -15.371 32.816  1.00 33.57  ? 401 HOH A O   1 
HETATM 2169 O  O   . HOH F 5 .   ? 12.067  -0.004  15.769  1.00 24.10  ? 402 HOH A O   1 
HETATM 2170 O  O   . HOH F 5 .   ? -25.136 -10.518 17.295  1.00 29.87  ? 403 HOH A O   1 
HETATM 2171 O  O   . HOH F 5 .   ? -17.414 19.012  5.946   1.00 14.11  ? 404 HOH A O   1 
HETATM 2172 O  O   . HOH F 5 .   ? 2.004   -4.503  -12.446 1.00 43.17  ? 405 HOH A O   1 
HETATM 2173 O  O   . HOH F 5 .   ? -10.667 -14.939 34.037  1.00 41.02  ? 406 HOH A O   1 
HETATM 2174 O  O   . HOH F 5 .   ? -24.666 9.633   13.035  1.00 35.36  ? 407 HOH A O   1 
HETATM 2175 O  O   . HOH F 5 .   ? -14.967 -10.194 37.573  1.00 27.40  ? 408 HOH A O   1 
HETATM 2176 O  O   . HOH F 5 .   ? -10.125 -5.779  38.152  1.00 34.67  ? 409 HOH A O   1 
HETATM 2177 O  O   . HOH F 5 .   ? 7.519   2.813   31.647  1.00 46.90  ? 410 HOH A O   1 
HETATM 2178 O  O   . HOH F 5 .   ? 4.910   -13.932 -6.063  1.00 35.46  ? 411 HOH A O   1 
HETATM 2179 O  O   . HOH F 5 .   ? 10.453  -7.369  -8.170  1.00 23.68  ? 412 HOH A O   1 
HETATM 2180 O  O   . HOH F 5 .   ? -12.785 -22.358 11.707  1.00 36.74  ? 413 HOH A O   1 
HETATM 2181 O  O   . HOH F 5 .   ? -0.799  -12.628 -3.465  1.00 26.67  ? 414 HOH A O   1 
HETATM 2182 O  O   . HOH F 5 .   ? -13.675 -9.015  -5.296  1.00 16.26  ? 415 HOH A O   1 
HETATM 2183 O  O   . HOH F 5 .   ? -2.660  17.908  20.757  1.00 32.68  ? 416 HOH A O   1 
HETATM 2184 O  O   . HOH F 5 .   ? -13.481 14.288  26.993  1.00 28.12  ? 417 HOH A O   1 
HETATM 2185 O  O   . HOH F 5 .   ? -7.355  7.174   27.476  1.00 27.95  ? 418 HOH A O   1 
HETATM 2186 O  O   . HOH F 5 .   ? -11.768 12.632  29.076  1.00 32.46  ? 419 HOH A O   1 
HETATM 2187 O  O   . HOH F 5 .   ? 1.935   -9.455  -5.056  1.00 37.39  ? 420 HOH A O   1 
HETATM 2188 O  O   . HOH F 5 .   ? -25.816 13.746  6.615   1.00 24.34  ? 421 HOH A O   1 
HETATM 2189 O  O   . HOH F 5 .   ? -13.685 -5.384  -6.657  1.00 35.72  ? 422 HOH A O   1 
HETATM 2190 O  O   . HOH F 5 .   ? -0.422  -15.657 -5.370  1.00 39.48  ? 423 HOH A O   1 
HETATM 2191 O  O   . HOH F 5 .   ? -18.834 11.920  12.917  1.00 37.53  ? 424 HOH A O   1 
HETATM 2192 O  O   . HOH F 5 .   ? -6.251  -20.276 19.357  1.00 17.00  ? 425 HOH A O   1 
HETATM 2193 O  O   . HOH F 5 .   ? -16.070 -14.843 32.917  1.00 36.54  ? 426 HOH A O   1 
HETATM 2194 O  O   . HOH F 5 .   ? -26.905 2.970   23.625  1.00 25.55  ? 427 HOH A O   1 
HETATM 2195 O  O   . HOH F 5 .   ? -10.042 -18.236 17.074  1.00 18.52  ? 428 HOH A O   1 
HETATM 2196 O  O   . HOH F 5 .   ? 14.900  0.298   14.842  1.00 22.19  ? 429 HOH A O   1 
HETATM 2197 O  O   . HOH F 5 .   ? -12.277 -21.937 8.465   1.00 31.89  ? 430 HOH A O   1 
HETATM 2198 O  O   . HOH F 5 .   ? -20.003 8.437   29.842  1.00 32.38  ? 431 HOH A O   1 
HETATM 2199 O  O   . HOH F 5 .   ? 2.480   8.033   27.825  1.00 33.07  ? 432 HOH A O   1 
HETATM 2200 O  O   . HOH F 5 .   ? -13.840 -16.527 28.860  1.00 23.32  ? 433 HOH A O   1 
HETATM 2201 O  O   . HOH F 5 .   ? -2.011  -3.342  11.210  1.00 28.97  ? 434 HOH A O   1 
HETATM 2202 O  O   . HOH F 5 .   ? -7.943  -15.452 36.292  1.00 30.34  ? 435 HOH A O   1 
HETATM 2203 O  O   . HOH F 5 .   ? -23.548 -3.044  29.197  1.00 34.47  ? 436 HOH A O   1 
HETATM 2204 O  O   . HOH F 5 .   ? -8.588  5.916   28.823  1.00 24.13  ? 437 HOH A O   1 
HETATM 2205 O  O   . HOH F 5 .   ? -0.849  -4.043  15.627  1.00 11.90  ? 438 HOH A O   1 
HETATM 2206 O  O   . HOH F 5 .   ? -17.796 4.086   -3.718  1.00 37.84  ? 439 HOH A O   1 
HETATM 2207 O  O   . HOH F 5 .   ? -20.537 -6.710  -2.320  1.00 27.28  ? 440 HOH A O   1 
HETATM 2208 O  O   . HOH F 5 .   ? -23.542 8.691   20.052  1.00 22.00  ? 441 HOH A O   1 
HETATM 2209 O  O   . HOH F 5 .   ? -14.963 19.148  13.039  1.00 25.53  ? 442 HOH A O   1 
HETATM 2210 O  O   . HOH F 5 .   ? -19.069 -20.735 4.951   1.00 22.36  ? 443 HOH A O   1 
HETATM 2211 O  O   . HOH F 5 .   ? 8.137   -8.411  0.245   1.00 30.18  ? 444 HOH A O   1 
HETATM 2212 O  O   . HOH F 5 .   ? 4.699   -3.405  26.360  1.00 19.16  ? 445 HOH A O   1 
HETATM 2213 O  O   . HOH F 5 .   ? -9.998  8.688   25.378  1.00 14.04  ? 446 HOH A O   1 
HETATM 2214 O  O   . HOH F 5 .   ? -24.275 4.561   8.616   1.00 30.66  ? 447 HOH A O   1 
HETATM 2215 O  O   . HOH F 5 .   ? -14.616 1.027   -5.301  1.00 32.00  ? 448 HOH A O   1 
HETATM 2216 O  O   . HOH F 5 .   ? -4.245  -11.957 31.955  1.00 23.50  ? 449 HOH A O   1 
HETATM 2217 O  O   . HOH F 5 .   ? 0.169   1.113   34.331  1.00 27.18  ? 450 HOH A O   1 
HETATM 2218 O  O   . HOH F 5 .   ? 11.868  -6.890  22.273  1.00 27.41  ? 451 HOH A O   1 
HETATM 2219 O  O   . HOH F 5 .   ? 6.051   -10.390 -6.551  1.00 44.81  ? 452 HOH A O   1 
HETATM 2220 O  O   . HOH F 5 .   ? 1.014   -1.733  -4.837  1.00 21.72  ? 453 HOH A O   1 
HETATM 2221 O  O   . HOH F 5 .   ? -7.529  -15.494 11.364  1.00 13.54  ? 454 HOH A O   1 
HETATM 2222 O  O   . HOH F 5 .   ? 10.777  -10.647 15.947  1.00 19.86  ? 455 HOH A O   1 
HETATM 2223 O  O   . HOH F 5 .   ? -21.650 -18.334 13.487  1.00 24.07  ? 456 HOH A O   1 
HETATM 2224 O  O   . HOH F 5 .   ? 6.077   -11.301 19.159  1.00 37.77  ? 457 HOH A O   1 
HETATM 2225 O  O   . HOH F 5 .   ? -14.208 -18.444 18.708  1.00 21.04  ? 458 HOH A O   1 
HETATM 2226 O  O   . HOH F 5 .   ? -6.483  -14.852 31.486  1.00 25.86  ? 459 HOH A O   1 
HETATM 2227 O  O   . HOH F 5 .   ? -19.072 17.249  5.811   1.00 32.51  ? 460 HOH A O   1 
HETATM 2228 O  O   . HOH F 5 .   ? -21.262 -14.051 18.685  1.00 37.23  ? 461 HOH A O   1 
HETATM 2229 O  O   . HOH F 5 .   ? -2.038  -8.659  28.962  1.00 12.81  ? 462 HOH A O   1 
HETATM 2230 O  O   . HOH F 5 .   ? -5.551  -4.904  -6.503  1.00 21.41  ? 463 HOH A O   1 
HETATM 2231 O  O   . HOH F 5 .   ? -15.538 -10.480 -4.643  1.00 25.76  ? 464 HOH A O   1 
HETATM 2232 O  O   . HOH F 5 .   ? 4.040   5.005   29.863  1.00 22.61  ? 465 HOH A O   1 
HETATM 2233 O  O   . HOH F 5 .   ? -10.294 1.137   33.541  1.00 48.50  ? 466 HOH A O   1 
HETATM 2234 O  O   . HOH F 5 .   ? -24.477 -10.963 23.777  1.00 37.82  ? 467 HOH A O   1 
HETATM 2235 O  O   . HOH F 5 .   ? -25.311 -15.095 7.959   1.00 40.54  ? 468 HOH A O   1 
HETATM 2236 O  O   . HOH F 5 .   ? -5.312  17.367  27.062  1.00 28.41  ? 469 HOH A O   1 
HETATM 2237 O  O   . HOH F 5 .   ? 15.793  3.423   20.895  1.00 33.20  ? 470 HOH A O   1 
HETATM 2238 O  O   . HOH F 5 .   ? -19.720 10.844  26.603  1.00 23.17  ? 471 HOH A O   1 
HETATM 2239 O  O   . HOH F 5 .   ? 3.115   -13.325 5.162   1.00 23.70  ? 472 HOH A O   1 
HETATM 2240 O  O   . HOH F 5 .   ? -3.063  -11.119 20.784  1.00 11.48  ? 473 HOH A O   1 
HETATM 2241 O  O   . HOH F 5 .   ? 3.205   -4.335  7.741   1.00 22.49  ? 474 HOH A O   1 
HETATM 2242 O  O   . HOH F 5 .   ? 5.543   7.267   20.393  1.00 18.74  ? 475 HOH A O   1 
HETATM 2243 O  O   . HOH F 5 .   ? -7.972  8.078   9.338   1.00 28.87  ? 476 HOH A O   1 
HETATM 2244 O  O   . HOH F 5 .   ? -27.748 6.391   15.765  1.00 52.90  ? 477 HOH A O   1 
HETATM 2245 O  O   . HOH F 5 .   ? -13.908 -21.163 2.991   1.00 43.69  ? 478 HOH A O   1 
HETATM 2246 O  O   . HOH F 5 .   ? 1.800   -6.297  34.159  1.00 35.77  ? 479 HOH A O   1 
HETATM 2247 O  O   . HOH F 5 .   ? 0.441   -19.799 10.977  1.00 36.15  ? 480 HOH A O   1 
HETATM 2248 O  O   . HOH F 5 .   ? -26.855 -7.449  25.944  1.00 36.33  ? 481 HOH A O   1 
HETATM 2249 O  O   . HOH F 5 .   ? -4.094  -13.481 17.947  1.00 11.21  ? 482 HOH A O   1 
HETATM 2250 O  O   . HOH F 5 .   ? -25.220 -5.627  12.814  1.00 34.85  ? 483 HOH A O   1 
HETATM 2251 O  O   . HOH F 5 .   ? 9.683   7.695   18.514  1.00 44.84  ? 484 HOH A O   1 
HETATM 2252 O  O   . HOH F 5 .   ? -13.260 10.449  27.764  1.00 21.01  ? 485 HOH A O   1 
HETATM 2253 O  O   . HOH F 5 .   ? -16.440 -14.036 37.361  1.00 29.65  ? 486 HOH A O   1 
HETATM 2254 O  O   . HOH F 5 .   ? 10.745  -9.190  8.905   1.00 32.66  ? 487 HOH A O   1 
HETATM 2255 O  O   . HOH F 5 .   ? -15.615 15.972  23.439  1.00 22.14  ? 488 HOH A O   1 
HETATM 2256 O  O   . HOH F 5 .   ? -0.664  9.119   27.983  1.00 36.23  ? 489 HOH A O   1 
HETATM 2257 O  O   . HOH F 5 .   ? -3.413  -13.142 -2.888  1.00 25.69  ? 490 HOH A O   1 
HETATM 2258 O  O   . HOH F 5 .   ? -19.322 -4.078  41.215  1.00 36.03  ? 491 HOH A O   1 
HETATM 2259 O  O   . HOH F 5 .   ? -22.877 -11.165 17.070  1.00 27.48  ? 492 HOH A O   1 
HETATM 2260 O  O   . HOH F 5 .   ? 13.728  0.512   24.414  1.00 18.74  ? 493 HOH A O   1 
HETATM 2261 O  O   . HOH F 5 .   ? -18.322 -20.811 14.856  1.00 36.09  ? 494 HOH A O   1 
HETATM 2262 O  O   . HOH F 5 .   ? -4.217  -16.070 0.810   1.00 30.60  ? 495 HOH A O   1 
HETATM 2263 O  O   . HOH F 5 .   ? 8.993   -3.606  20.940  1.00 14.63  ? 496 HOH A O   1 
HETATM 2264 O  O   . HOH F 5 .   ? -16.526 -8.299  20.248  1.00 10.31  ? 497 HOH A O   1 
HETATM 2265 O  O   . HOH F 5 .   ? -11.004 10.338  8.233   1.00 21.00  ? 498 HOH A O   1 
HETATM 2266 O  O   . HOH F 5 .   ? -17.444 6.205   38.534  1.00 49.63  ? 499 HOH A O   1 
HETATM 2267 O  O   . HOH F 5 .   ? -18.879 -12.256 -3.425  1.00 17.59  ? 500 HOH A O   1 
HETATM 2268 O  O   . HOH F 5 .   ? -18.672 9.937   8.702   1.00 12.69  ? 501 HOH A O   1 
HETATM 2269 O  O   . HOH F 5 .   ? -6.218  -5.341  37.220  1.00 23.94  ? 502 HOH A O   1 
HETATM 2270 O  O   . HOH F 5 .   ? -21.105 -6.990  23.423  1.00 13.42  ? 503 HOH A O   1 
HETATM 2271 O  O   . HOH F 5 .   ? 4.973   -2.499  28.821  1.00 27.78  ? 504 HOH A O   1 
HETATM 2272 O  O   . HOH F 5 .   ? -7.939  0.357   -6.605  1.00 25.62  ? 505 HOH A O   1 
HETATM 2273 O  O   . HOH F 5 .   ? 1.848   -11.716 24.896  1.00 24.70  ? 506 HOH A O   1 
HETATM 2274 O  O   . HOH F 5 .   ? -17.421 10.578  11.165  1.00 16.70  ? 507 HOH A O   1 
HETATM 2275 O  O   . HOH F 5 .   ? -12.460 -9.093  -3.284  1.00 16.95  ? 508 HOH A O   1 
HETATM 2276 O  O   . HOH F 5 .   ? -16.879 -16.153 21.944  1.00 28.66  ? 509 HOH A O   1 
HETATM 2277 O  O   . HOH F 5 .   ? 6.047   -3.212  6.767   1.00 32.68  ? 510 HOH A O   1 
HETATM 2278 O  O   . HOH F 5 .   ? -17.508 -20.423 7.904   1.00 14.60  ? 511 HOH A O   1 
HETATM 2279 O  O   . HOH F 5 .   ? -22.274 -5.767  2.700   1.00 18.46  ? 512 HOH A O   1 
HETATM 2280 O  O   . HOH F 5 .   ? -3.755  -8.500  31.058  1.00 21.76  ? 513 HOH A O   1 
HETATM 2281 O  O   . HOH F 5 .   ? 2.247   11.113  17.004  1.00 40.84  ? 514 HOH A O   1 
HETATM 2282 O  O   . HOH F 5 .   ? -3.341  -15.820 24.328  1.00 15.56  ? 515 HOH A O   1 
HETATM 2283 O  O   . HOH F 5 .   ? -2.938  -13.188 25.103  1.00 13.22  ? 516 HOH A O   1 
HETATM 2284 O  O   . HOH F 5 .   ? -15.636 -12.263 24.302  1.00 17.29  ? 517 HOH A O   1 
HETATM 2285 O  O   . HOH F 5 .   ? -12.831 -0.971  -5.888  1.00 24.62  ? 518 HOH A O   1 
HETATM 2286 O  O   . HOH F 5 .   ? -11.947 12.620  6.394   1.00 38.79  ? 519 HOH A O   1 
HETATM 2287 O  O   . HOH F 5 .   ? -24.261 11.881  6.128   1.00 21.25  ? 520 HOH A O   1 
HETATM 2288 O  O   . HOH F 5 .   ? -1.224  -5.223  -7.164  1.00 33.20  ? 521 HOH A O   1 
HETATM 2289 O  O   . HOH F 5 .   ? -25.817 -2.084  14.466  1.00 25.28  ? 522 HOH A O   1 
HETATM 2290 O  O   . HOH F 5 .   ? -12.584 -16.784 26.510  1.00 19.23  ? 523 HOH A O   1 
HETATM 2291 O  O   . HOH F 5 .   ? -22.910 -13.233 11.262  1.00 23.79  ? 524 HOH A O   1 
HETATM 2292 O  O   . HOH F 5 .   ? -24.375 -7.554  9.033   1.00 16.30  ? 525 HOH A O   1 
HETATM 2293 O  O   . HOH F 5 .   ? -18.259 -4.207  -2.770  1.00 25.95  ? 526 HOH A O   1 
HETATM 2294 O  O   . HOH F 5 .   ? -21.228 5.696   4.619   1.00 13.16  ? 527 HOH A O   1 
HETATM 2295 O  O   . HOH F 5 .   ? -6.856  -16.803 1.330   1.00 22.24  ? 528 HOH A O   1 
HETATM 2296 O  O   . HOH F 5 .   ? -25.272 7.914   6.219   1.00 25.33  ? 529 HOH A O   1 
HETATM 2297 O  O   . HOH F 5 .   ? -2.358  4.530   7.032   1.00 25.56  ? 530 HOH A O   1 
HETATM 2298 O  O   . HOH F 5 .   ? 5.326   -4.769  20.899  1.00 14.31  ? 531 HOH A O   1 
HETATM 2299 O  O   . HOH F 5 .   ? 11.618  1.586   25.891  1.00 22.74  ? 532 HOH A O   1 
HETATM 2300 O  O   . HOH F 5 .   ? 2.067   12.264  22.547  1.00 34.57  ? 533 HOH A O   1 
HETATM 2301 O  O   . HOH F 5 .   ? 2.437   -15.595 9.283   1.00 22.43  ? 534 HOH A O   1 
HETATM 2302 O  O   . HOH F 5 .   ? -7.015  -8.629  32.488  1.00 17.91  ? 535 HOH A O   1 
HETATM 2303 O  O   . HOH F 5 .   ? -10.631 -19.526 7.203   1.00 41.76  ? 536 HOH A O   1 
HETATM 2304 O  O   . HOH F 5 .   ? -14.513 20.144  17.552  1.00 26.25  ? 537 HOH A O   1 
HETATM 2305 O  O   . HOH F 5 .   ? 15.799  -7.067  11.211  1.00 33.72  ? 538 HOH A O   1 
HETATM 2306 O  O   . HOH F 5 .   ? 3.725   10.172  18.523  1.00 38.80  ? 539 HOH A O   1 
HETATM 2307 O  O   . HOH F 5 .   ? -3.533  5.223   -3.124  1.00 29.87  ? 540 HOH A O   1 
HETATM 2308 O  O   . HOH F 5 .   ? -25.822 -7.237  30.328  1.00 37.90  ? 541 HOH A O   1 
HETATM 2309 O  O   . HOH F 5 .   ? -11.490 2.876   30.632  1.00 21.18  ? 542 HOH A O   1 
HETATM 2310 O  O   . HOH F 5 .   ? -12.998 -18.527 14.587  1.00 22.25  ? 543 HOH A O   1 
HETATM 2311 O  O   . HOH F 5 .   ? 7.433   -3.607  30.028  1.00 32.52  ? 544 HOH A O   1 
HETATM 2312 O  O   . HOH F 5 .   ? -25.452 6.396   26.876  1.00 25.90  ? 545 HOH A O   1 
HETATM 2313 O  O   . HOH F 5 .   ? -26.217 -3.772  25.056  1.00 20.02  ? 546 HOH A O   1 
HETATM 2314 O  O   . HOH F 5 .   ? -22.719 -0.253  34.274  1.00 30.94  ? 547 HOH A O   1 
HETATM 2315 O  O   . HOH F 5 .   ? -12.129 13.110  31.616  1.00 50.87  ? 548 HOH A O   1 
HETATM 2316 O  O   . HOH F 5 .   ? -19.495 14.132  28.951  1.00 41.38  ? 549 HOH A O   1 
HETATM 2317 O  O   . HOH F 5 .   ? -25.750 3.475   15.452  1.00 24.53  ? 550 HOH A O   1 
HETATM 2318 O  O   . HOH F 5 .   ? -20.315 2.121   -3.583  1.00 33.56  ? 551 HOH A O   1 
HETATM 2319 O  O   . HOH F 5 .   ? -12.222 3.846   -7.058  1.00 33.15  ? 552 HOH A O   1 
HETATM 2320 O  O   . HOH F 5 .   ? 8.571   -5.914  0.092   1.00 45.87  ? 553 HOH A O   1 
HETATM 2321 O  O   . HOH F 5 .   ? -8.652  -5.767  35.800  1.00 19.49  ? 554 HOH A O   1 
HETATM 2322 O  O   . HOH F 5 .   ? -13.385 -16.190 -0.448  1.00 36.34  ? 555 HOH A O   1 
HETATM 2323 O  O   . HOH F 5 .   ? -5.943  6.482   10.476  1.00 21.43  ? 556 HOH A O   1 
HETATM 2324 O  O   . HOH F 5 .   ? -6.485  -8.751  -7.254  1.00 32.07  ? 557 HOH A O   1 
HETATM 2325 O  O   . HOH F 5 .   ? -8.058  -22.095 10.462  1.00 22.30  ? 558 HOH A O   1 
HETATM 2326 O  O   . HOH F 5 .   ? -15.941 -9.807  32.774  1.00 18.45  ? 559 HOH A O   1 
HETATM 2327 O  O   . HOH F 5 .   ? 3.048   -11.396 9.502   1.00 27.65  ? 560 HOH A O   1 
HETATM 2328 O  O   . HOH F 5 .   ? 3.361   -14.958 0.869   1.00 31.05  ? 561 HOH A O   1 
HETATM 2329 O  O   . HOH F 5 .   ? -12.188 -18.394 31.836  1.00 34.67  ? 562 HOH A O   1 
HETATM 2330 O  O   . HOH F 5 .   ? 1.924   8.693   23.932  1.00 22.13  ? 563 HOH A O   1 
HETATM 2331 O  O   . HOH F 5 .   ? 8.504   -9.100  16.251  1.00 21.50  ? 564 HOH A O   1 
HETATM 2332 O  O   . HOH F 5 .   ? -2.658  -19.310 21.969  1.00 42.46  ? 565 HOH A O   1 
HETATM 2333 O  O   . HOH F 5 .   ? -13.170 19.852  14.885  1.00 28.77  ? 566 HOH A O   1 
HETATM 2334 O  O   . HOH F 5 .   ? -21.896 3.911   -3.091  1.00 24.50  ? 567 HOH A O   1 
HETATM 2335 O  O   . HOH F 5 .   ? 1.730   -1.559  29.304  1.00 14.81  ? 568 HOH A O   1 
HETATM 2336 O  O   . HOH F 5 .   ? -9.028  14.759  11.899  1.00 41.77  ? 569 HOH A O   1 
HETATM 2337 O  O   . HOH F 5 .   ? 4.773   -6.818  7.877   1.00 23.61  ? 570 HOH A O   1 
HETATM 2338 O  O   . HOH F 5 .   ? 13.462  -5.686  24.434  1.00 24.65  ? 571 HOH A O   1 
HETATM 2339 O  O   . HOH F 5 .   ? -16.778 -7.240  39.661  1.00 38.82  ? 572 HOH A O   1 
HETATM 2340 O  O   . HOH F 5 .   ? 3.805   4.474   10.495  1.00 33.15  ? 573 HOH A O   1 
HETATM 2341 O  O   . HOH F 5 .   ? 0.241   -14.245 22.107  1.00 24.06  ? 574 HOH A O   1 
HETATM 2342 O  O   . HOH F 5 .   ? -7.771  6.523   0.331   1.00 21.77  ? 575 HOH A O   1 
HETATM 2343 O  O   . HOH F 5 .   ? -18.444 17.688  18.665  1.00 35.30  ? 576 HOH A O   1 
HETATM 2344 O  O   . HOH F 5 .   ? -0.167  10.628  23.242  1.00 23.51  ? 577 HOH A O   1 
HETATM 2345 O  O   . HOH F 5 .   ? -23.475 -0.529  26.442  1.00 19.24  ? 578 HOH A O   1 
HETATM 2346 O  O   . HOH F 5 .   ? 5.639   -7.169  22.224  1.00 28.87  ? 579 HOH A O   1 
HETATM 2347 O  O   . HOH F 5 .   ? -0.154  -8.523  32.383  1.00 26.90  ? 580 HOH A O   1 
HETATM 2348 O  O   . HOH F 5 .   ? -27.327 -12.074 15.831  1.00 47.27  ? 581 HOH A O   1 
HETATM 2349 O  O   . HOH F 5 .   ? 9.092   -10.115 -6.749  1.00 47.31  ? 582 HOH A O   1 
HETATM 2350 O  O   . HOH F 5 .   ? -5.717  -19.708 23.787  1.00 31.46  ? 583 HOH A O   1 
HETATM 2351 O  O   . HOH F 5 .   ? 8.594   3.337   27.788  1.00 30.47  ? 584 HOH A O   1 
HETATM 2352 O  O   . HOH F 5 .   ? -4.776  2.950   -6.033  1.00 24.51  ? 585 HOH A O   1 
HETATM 2353 O  O   . HOH F 5 .   ? 3.315   3.298   8.138   1.00 40.01  ? 586 HOH A O   1 
HETATM 2354 O  O   . HOH F 5 .   ? -9.168  -7.961  33.938  1.00 22.48  ? 587 HOH A O   1 
HETATM 2355 O  O   . HOH F 5 .   ? -23.752 -17.768 6.498   1.00 33.39  ? 588 HOH A O   1 
HETATM 2356 O  O   . HOH F 5 .   ? -11.787 16.498  9.815   1.00 33.73  ? 589 HOH A O   1 
HETATM 2357 O  O   . HOH F 5 .   ? -27.516 6.038   19.101  1.00 39.09  ? 590 HOH A O   1 
HETATM 2358 O  O   . HOH F 5 .   ? 15.124  -10.247 14.447  1.00 28.26  ? 591 HOH A O   1 
HETATM 2359 O  O   . HOH F 5 .   ? -15.325 9.094   -2.170  1.00 38.26  ? 592 HOH A O   1 
HETATM 2360 O  O   . HOH F 5 .   ? -8.792  -10.138 -1.457  1.00 30.25  ? 593 HOH A O   1 
HETATM 2361 O  O   . HOH F 5 .   ? -1.615  -12.265 22.749  1.00 12.48  ? 594 HOH A O   1 
HETATM 2362 O  O   . HOH F 5 .   ? -6.571  1.502   35.237  1.00 27.45  ? 595 HOH A O   1 
HETATM 2363 O  O   . HOH F 5 .   ? -6.753  4.927   -6.433  1.00 39.69  ? 596 HOH A O   1 
HETATM 2364 O  O   . HOH F 5 .   ? 2.024   -17.850 13.862  1.00 37.59  ? 597 HOH A O   1 
HETATM 2365 O  O   . HOH F 5 .   ? 4.492   -2.914  4.403   1.00 44.59  ? 598 HOH A O   1 
HETATM 2366 O  O   . HOH F 5 .   ? -10.316 17.413  11.949  1.00 26.24  ? 599 HOH A O   1 
HETATM 2367 O  O   . HOH F 5 .   ? -7.613  -19.331 21.510  1.00 20.29  ? 600 HOH A O   1 
HETATM 2368 O  O   . HOH F 5 .   ? 7.876   6.272   21.647  1.00 16.35  ? 601 HOH A O   1 
HETATM 2369 O  O   . HOH F 5 .   ? -0.270  2.722   -5.564  1.00 30.51  ? 602 HOH A O   1 
HETATM 2370 O  O   . HOH F 5 .   ? -12.284 7.945   28.858  1.00 27.50  ? 603 HOH A O   1 
HETATM 2371 O  O   . HOH F 5 .   ? -19.313 -13.491 24.397  1.00 42.11  ? 604 HOH A O   1 
HETATM 2372 O  O   . HOH F 5 .   ? -22.511 -11.506 13.955  1.00 22.45  ? 605 HOH A O   1 
HETATM 2373 O  O   . HOH F 5 .   ? -20.835 -19.527 6.478   1.00 23.40  ? 606 HOH A O   1 
HETATM 2374 O  O   . HOH F 5 .   ? 3.672   -0.618  5.133   1.00 35.39  ? 607 HOH A O   1 
HETATM 2375 O  O   . HOH F 5 .   ? 10.479  -2.320  13.607  1.00 38.64  ? 608 HOH A O   1 
HETATM 2376 O  O   . HOH F 5 .   ? 9.226   -7.566  -10.193 1.00 25.68  ? 609 HOH A O   1 
HETATM 2377 O  O   . HOH F 5 .   ? -10.117 20.702  24.875  1.00 27.01  ? 610 HOH A O   1 
HETATM 2378 O  O   . HOH F 5 .   ? -18.072 -9.045  34.394  1.00 31.43  ? 611 HOH A O   1 
HETATM 2379 O  O   . HOH F 5 .   ? -16.769 -22.955 3.664   1.00 34.09  ? 612 HOH A O   1 
HETATM 2380 O  O   . HOH F 5 .   ? -22.456 15.124  18.992  1.00 49.32  ? 613 HOH A O   1 
HETATM 2381 O  O   . HOH F 5 .   ? 8.913   -12.534 8.494   1.00 43.39  ? 614 HOH A O   1 
HETATM 2382 O  O   . HOH F 5 .   ? 6.720   -10.608 14.782  1.00 33.00  ? 615 HOH A O   1 
HETATM 2383 O  O   . HOH F 5 .   ? -1.038  11.129  25.526  1.00 33.64  ? 616 HOH A O   1 
HETATM 2384 O  O   . HOH F 5 .   ? -12.410 -17.143 16.781  1.00 17.21  ? 617 HOH A O   1 
HETATM 2385 O  O   . HOH F 5 .   ? 6.782   -2.679  1.684   1.00 49.08  ? 618 HOH A O   1 
HETATM 2386 O  O   . HOH F 5 .   ? 9.136   -4.586  23.551  1.00 29.88  ? 619 HOH A O   1 
HETATM 2387 O  O   . HOH F 5 .   ? -24.577 -9.247  1.848   1.00 31.76  ? 620 HOH A O   1 
HETATM 2388 O  O   . HOH F 5 .   ? -6.858  -9.080  -2.465  1.00 29.16  ? 621 HOH A O   1 
HETATM 2389 O  O   . HOH F 5 .   ? -21.248 -12.769 -1.740  1.00 12.48  ? 622 HOH A O   1 
HETATM 2390 O  O   . HOH F 5 .   ? -24.681 11.176  19.641  1.00 32.76  ? 623 HOH A O   1 
HETATM 2391 O  O   . HOH F 5 .   ? 10.505  5.782   12.862  1.00 36.27  ? 624 HOH A O   1 
HETATM 2392 O  O   . HOH F 5 .   ? 5.096   -10.276 8.129   1.00 40.42  ? 625 HOH A O   1 
HETATM 2393 O  O   . HOH F 5 .   ? -1.102  -13.099 27.135  1.00 26.02  ? 626 HOH A O   1 
HETATM 2394 O  O   . HOH F 5 .   ? -22.318 -9.447  25.163  1.00 31.56  ? 627 HOH A O   1 
HETATM 2395 O  O   . HOH F 5 .   ? 2.995   2.115   -2.845  1.00 31.04  ? 628 HOH A O   1 
HETATM 2396 O  O   . HOH F 5 .   ? -7.867  -21.454 8.184   1.00 44.35  ? 629 HOH A O   1 
HETATM 2397 O  O   . HOH F 5 .   ? -3.487  7.844   10.713  1.00 36.04  ? 630 HOH A O   1 
HETATM 2398 O  O   . HOH F 5 .   ? -2.359  -17.529 5.376   1.00 27.97  ? 631 HOH A O   1 
HETATM 2399 O  O   . HOH F 5 .   ? -16.926 0.202   -3.929  1.00 31.95  ? 632 HOH A O   1 
HETATM 2400 O  O   . HOH F 5 .   ? -8.011  -17.527 34.593  1.00 31.53  ? 633 HOH A O   1 
HETATM 2401 O  O   . HOH F 5 .   ? -17.366 19.884  17.409  1.00 27.65  ? 634 HOH A O   1 
HETATM 2402 O  O   . HOH F 5 .   ? 4.315   8.801   22.448  1.00 29.55  ? 635 HOH A O   1 
HETATM 2403 O  O   . HOH F 5 .   ? -27.392 5.196   25.238  1.00 28.24  ? 636 HOH A O   1 
HETATM 2404 O  O   . HOH F 5 .   ? -24.119 15.582  5.350   1.00 41.90  ? 637 HOH A O   1 
HETATM 2405 O  O   . HOH F 5 .   ? 6.713   -4.041  -10.411 1.00 35.69  ? 638 HOH A O   1 
HETATM 2406 O  O   . HOH F 5 .   ? -9.883  4.975   30.570  1.00 30.84  ? 639 HOH A O   1 
HETATM 2407 O  O   . HOH F 5 .   ? -1.779  -11.891 31.336  1.00 32.69  ? 640 HOH A O   1 
HETATM 2408 O  O   . HOH F 5 .   ? -1.477  -17.329 25.521  1.00 31.73  ? 641 HOH A O   1 
HETATM 2409 O  O   . HOH F 5 .   ? -24.650 8.748   26.017  1.00 34.32  ? 642 HOH A O   1 
HETATM 2410 O  O   . HOH F 5 .   ? -12.407 -11.052 -6.210  1.00 36.76  ? 643 HOH A O   1 
HETATM 2411 O  O   . HOH F 5 .   ? 0.011   18.339  20.828  1.00 35.81  ? 644 HOH A O   1 
HETATM 2412 O  O   . HOH F 5 .   ? -23.298 10.266  28.144  1.00 54.62  ? 645 HOH A O   1 
HETATM 2413 O  O   . HOH F 5 .   ? -16.411 -18.006 20.245  1.00 35.03  ? 646 HOH A O   1 
HETATM 2414 O  O   . HOH F 5 .   ? -14.902 20.748  22.845  1.00 36.07  ? 647 HOH A O   1 
HETATM 2415 O  O   . HOH F 5 .   ? -25.406 12.082  17.248  1.00 34.08  ? 648 HOH A O   1 
HETATM 2416 O  O   . HOH F 5 .   ? -3.571  -6.104  -7.992  1.00 33.21  ? 649 HOH A O   1 
HETATM 2417 O  O   . HOH F 5 .   ? 7.005   -5.246  27.270  1.00 38.98  ? 650 HOH A O   1 
HETATM 2418 O  O   . HOH F 5 .   ? -16.497 -13.954 26.200  1.00 25.75  ? 651 HOH A O   1 
HETATM 2419 O  O   . HOH F 5 .   ? -4.512  -9.663  33.454  1.00 38.06  ? 652 HOH A O   1 
HETATM 2420 O  O   . HOH F 5 .   ? -14.077 -3.029  -7.181  1.00 33.17  ? 653 HOH A O   1 
HETATM 2421 O  O   . HOH F 5 .   ? 0.744   0.075   -6.801  1.00 34.59  ? 654 HOH A O   1 
HETATM 2422 O  O   . HOH F 5 .   ? 5.054   -10.474 16.872  1.00 51.26  ? 655 HOH A O   1 
HETATM 2423 O  O   . HOH F 5 .   ? -23.936 -7.042  0.398   1.00 44.22  ? 656 HOH A O   1 
HETATM 2424 O  O   . HOH F 5 .   ? -4.275  -8.486  -8.681  1.00 52.70  ? 657 HOH A O   1 
HETATM 2425 O  O   . HOH F 5 .   ? -19.849 -2.285  43.112  1.00 45.38  ? 658 HOH A O   1 
HETATM 2426 O  O   . HOH F 5 .   ? -10.830 -11.386 -3.083  1.00 28.88  ? 659 HOH A O   1 
HETATM 2427 O  O   . HOH F 5 .   ? -15.652 17.271  26.035  1.00 37.88  ? 660 HOH A O   1 
HETATM 2428 O  O   . HOH F 5 .   ? 4.394   -11.765 23.482  1.00 41.40  ? 661 HOH A O   1 
HETATM 2429 O  O   . HOH F 5 .   ? -23.838 13.454  20.293  1.00 45.95  ? 662 HOH A O   1 
HETATM 2430 O  O   . HOH F 5 .   ? -16.177 -14.411 28.753  1.00 42.68  ? 663 HOH A O   1 
HETATM 2431 O  O   . HOH F 5 .   ? -19.603 -15.555 22.299  1.00 37.73  ? 664 HOH A O   1 
HETATM 2432 O  O   . HOH F 5 .   ? -0.704  -11.086 28.913  1.00 19.23  ? 665 HOH A O   1 
HETATM 2433 O  O   . HOH F 5 .   ? -17.463 -12.081 31.369  1.00 30.58  ? 666 HOH A O   1 
HETATM 2434 O  O   . HOH F 5 .   ? -21.519 -13.413 23.119  1.00 53.52  ? 667 HOH A O   1 
HETATM 2435 O  O   . HOH F 5 .   ? -20.367 -22.064 13.540  1.00 37.30  ? 668 HOH A O   1 
HETATM 2436 O  O   . HOH F 5 .   ? 6.611   5.457   29.364  1.00 33.17  ? 669 HOH A O   1 
HETATM 2437 O  O   . HOH F 5 .   ? 9.390   -12.857 16.069  1.00 37.02  ? 670 HOH A O   1 
HETATM 2438 O  O   . HOH F 5 .   ? 2.578   -14.038 20.616  1.00 31.43  ? 671 HOH A O   1 
HETATM 2439 O  O   . HOH F 5 .   ? 2.165   -17.328 7.311   1.00 41.84  ? 672 HOH A O   1 
HETATM 2440 O  O   . HOH F 5 .   ? -3.653  20.336  19.969  1.00 35.01  ? 673 HOH A O   1 
HETATM 2441 O  O   . HOH F 5 .   ? 2.602   9.579   26.265  1.00 34.28  ? 674 HOH A O   1 
HETATM 2442 O  O   . HOH F 5 .   ? -26.200 -1.054  25.876  1.00 21.18  ? 675 HOH A O   1 
HETATM 2443 O  O   . HOH F 5 .   ? -12.446 -19.432 26.000  1.00 28.41  ? 676 HOH A O   1 
HETATM 2444 O  O   . HOH F 5 .   ? 7.128   8.686   18.490  1.00 38.98  ? 677 HOH A O   1 
HETATM 2445 O  O   . HOH F 5 .   ? -3.405  -15.724 -1.986  1.00 30.60  ? 678 HOH A O   1 
HETATM 2446 O  O   . HOH F 5 .   ? -1.303  11.199  12.740  1.00 51.29  ? 679 HOH A O   1 
HETATM 2447 O  O   . HOH F 5 .   ? -2.259  -9.229  34.429  1.00 35.18  ? 680 HOH A O   1 
HETATM 2448 O  O   . HOH F 5 .   ? 14.423  -1.316  28.379  1.00 30.95  ? 681 HOH A O   1 
HETATM 2449 O  O   . HOH F 5 .   ? -9.295  1.485   38.852  1.00 32.19  ? 682 HOH A O   1 
HETATM 2450 O  O   . HOH F 5 .   ? -29.185 4.301   27.254  1.00 42.63  ? 683 HOH A O   1 
HETATM 2451 O  O   . HOH F 5 .   ? -8.667  0.647   42.697  1.00 27.87  ? 684 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   ? 1.2351 0.8893 1.3431 -0.2134 0.3169  0.0858  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.9431 0.8309 0.8788 -0.2421 0.1663  0.2430  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.3267 0.7331 0.4526 0.1345  0.0581  0.0533  4   HIS A C   
4    O  O   . HIS A 4   ? 0.5175 0.4652 0.4239 -0.1835 0.0666  0.0027  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.7151 0.6278 1.1568 -0.3370 0.5037  0.3648  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.9256 0.7619 0.8547 -0.2603 0.2487  -0.0252 4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.5766 0.5493 0.6147 0.0899  -0.0244 0.2402  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.6808 0.5497 0.7019 0.1371  -0.1126 0.1714  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 0.7091 0.8675 0.9691 0.1278  0.2052  0.1544  4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 0.7508 1.2059 0.7065 0.3131  0.0640  0.0323  4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.2949 0.4219 0.2483 -0.0722 0.0678  0.0237  5   TRP A N   
12   C  CA  . TRP A 5   ? 0.1802 0.2809 0.2249 -0.0063 0.0203  0.0205  5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1504 0.2855 0.2089 -0.0005 0.0368  -0.0098 5   TRP A C   
14   O  O   . TRP A 5   ? 0.2007 0.3307 0.2333 0.0336  0.0339  0.0356  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1873 0.2676 0.2521 -0.0268 0.0321  0.0026  5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1906 0.2344 0.2100 -0.0280 0.0236  0.0314  5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.2394 0.2796 0.2485 -0.0351 0.0222  0.1015  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1726 0.2284 0.1759 0.0111  0.0218  0.0016  5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.2212 0.2690 0.2194 -0.0167 0.0081  0.0297  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1937 0.2334 0.1662 0.0162  0.0453  0.0310  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1729 0.2547 0.1587 -0.0342 0.0172  -0.0490 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.2056 0.2957 0.1361 0.0466  -0.0210 0.0179  5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1673 0.2384 0.1302 0.0184  0.0049  -0.0425 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1561 0.2935 0.1302 0.0337  -0.0037 -0.0403 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1574 0.2483 0.2226 0.0154  0.0261  -0.0240 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1479 0.2724 0.1987 0.0192  0.0129  -0.0223 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1338 0.2694 0.1568 0.0263  0.0183  -0.0395 6   GLY A C   
28   O  O   . GLY A 6   ? 0.1291 0.2734 0.1514 0.0160  0.0060  -0.0445 6   GLY A O   
29   N  N   . TYR A 7   ? 0.1430 0.2492 0.1914 0.0190  0.0044  -0.0540 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.1452 0.2551 0.2061 0.0018  0.0058  -0.0370 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.1386 0.2827 0.3049 0.0002  0.0334  -0.0633 7   TYR A C   
32   O  O   . TYR A 7   ? 0.1809 0.3643 0.4328 -0.0039 0.0263  0.0003  7   TYR A O   
33   C  CB  . TYR A 7   ? 0.1423 0.2440 0.2215 -0.0044 0.0130  -0.0753 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1432 0.2269 0.1553 -0.0127 0.0114  -0.0617 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.1174 0.2075 0.1455 -0.0032 -0.0030 -0.0524 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.1664 0.2143 0.1607 -0.0293 0.0132  -0.0555 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.1195 0.1590 0.1999 -0.0188 -0.0153 -0.0329 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.1437 0.2182 0.1583 -0.0460 0.0165  -0.0513 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.1700 0.1697 0.1521 -0.0305 0.0068  -0.0366 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.2131 0.1673 0.1608 0.0061  -0.0020 -0.0249 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.1781 0.2766 0.2143 0.0379  0.0302  -0.0458 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.2321 0.2746 0.3610 0.0624  -0.0011 -0.0754 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.1921 0.2712 0.3119 0.0359  0.0462  -0.0487 8   GLY A C   
44   O  O   . GLY A 8   ? 0.1547 0.3173 0.2516 0.0053  0.0531  -0.0365 8   GLY A O   
45   N  N   . LYS A 9   ? 0.1905 0.2452 0.3574 0.0301  0.0114  -0.0294 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.2172 0.2534 0.3658 0.0153  -0.0083 -0.0159 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.1949 0.2518 0.2994 0.0272  0.0710  -0.0183 9   LYS A C   
48   O  O   . LYS A 9   ? 0.1967 0.2412 0.3225 -0.0139 0.0488  0.0020  9   LYS A O   
49   C  CB  . LYS A 9   ? 0.2703 0.1901 0.5751 0.0175  -0.0348 -0.0370 9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.3415 0.3204 0.4478 -0.0271 -0.0383 0.0321  9   LYS A CG  
51   N  N   . HIS A 10  ? 0.1808 0.2124 0.3361 0.0379  0.0886  0.0020  10  HIS A N   
52   C  CA  . HIS A 10  ? 0.1995 0.2207 0.3750 0.0171  0.1553  0.0216  10  HIS A CA  
53   C  C   . HIS A 10  ? 0.1610 0.2276 0.3190 0.0337  0.0813  0.0182  10  HIS A C   
54   O  O   . HIS A 10  ? 0.1524 0.2462 0.3746 0.0479  0.0770  0.0125  10  HIS A O   
55   C  CB  . HIS A 10  ? 0.3080 0.2541 0.3953 0.0594  0.2431  0.0527  10  HIS A CB  
56   C  CG  . HIS A 10  ? 0.2522 0.3343 0.3346 0.0757  0.1209  0.1101  10  HIS A CG  
57   N  ND1 . HIS A 10  ? 0.3299 0.2949 0.5041 0.1145  0.0829  0.0446  10  HIS A ND1 
58   C  CD2 . HIS A 10  ? 0.3233 0.3593 0.4157 0.0075  0.1846  0.1110  10  HIS A CD2 
59   C  CE1 . HIS A 10  ? 0.3249 0.2919 0.3644 0.0723  -0.0500 -0.0337 10  HIS A CE1 
60   N  NE2 . HIS A 10  ? 0.2145 0.3498 0.3123 0.0096  0.0756  -0.0447 10  HIS A NE2 
61   N  N   . ASN A 11  ? 0.1585 0.2239 0.2438 0.0346  0.0647  -0.0179 11  ASN A N   
62   C  CA  . ASN A 11  ? 0.1750 0.2041 0.1748 0.0195  0.0584  -0.0241 11  ASN A CA  
63   C  C   . ASN A 11  ? 0.1174 0.2348 0.1831 0.0145  0.0156  -0.0326 11  ASN A C   
64   O  O   . ASN A 11  ? 0.1443 0.2487 0.1676 0.0384  0.0176  -0.0151 11  ASN A O   
65   C  CB  . ASN A 11  ? 0.1967 0.2861 0.1755 0.0119  0.0680  -0.0130 11  ASN A CB  
66   C  CG  . ASN A 11  ? 0.1867 0.3442 0.1977 0.0377  0.0220  -0.0132 11  ASN A CG  
67   O  OD1 . ASN A 11  ? 0.2387 0.3685 0.1989 0.0364  0.0162  -0.0212 11  ASN A OD1 
68   N  ND2 . ASN A 11  ? 0.3080 0.3977 0.2462 0.1048  0.0277  0.0146  11  ASN A ND2 
69   N  N   . GLY A 12  ? 0.1389 0.2427 0.1719 0.0161  0.0390  -0.0273 12  GLY A N   
70   C  CA  . GLY A 12  ? 0.1293 0.2811 0.1575 0.0414  0.0357  -0.0396 12  GLY A CA  
71   C  C   . GLY A 12  ? 0.1109 0.2063 0.1491 0.0089  0.0198  -0.0095 12  GLY A C   
72   O  O   . GLY A 12  ? 0.1066 0.2056 0.1678 0.0078  0.0044  -0.0006 12  GLY A O   
73   N  N   . PRO A 13  ? 0.1177 0.2045 0.1458 0.0079  0.0195  -0.0179 13  PRO A N   
74   C  CA  . PRO A 13  ? 0.1136 0.1795 0.1394 0.0046  0.0219  -0.0083 13  PRO A CA  
75   C  C   . PRO A 13  ? 0.1174 0.1664 0.1438 0.0046  0.0280  -0.0030 13  PRO A C   
76   O  O   . PRO A 13  ? 0.1204 0.1878 0.1641 -0.0021 0.0125  -0.0279 13  PRO A O   
77   C  CB  . PRO A 13  ? 0.1408 0.1691 0.1880 -0.0305 -0.0003 -0.0080 13  PRO A CB  
78   C  CG  . PRO A 13  ? 0.1551 0.2092 0.1544 -0.0111 0.0204  -0.0223 13  PRO A CG  
79   C  CD  . PRO A 13  ? 0.1125 0.2195 0.1852 0.0068  0.0148  -0.0184 13  PRO A CD  
80   N  N   . GLU A 14  ? 0.1216 0.1747 0.1880 0.0078  0.0006  0.0061  14  GLU A N   
81   C  CA  . GLU A 14  ? 0.1439 0.1737 0.2116 0.0006  -0.0181 0.0096  14  GLU A CA  
82   C  C   . GLU A 14  ? 0.1241 0.1590 0.1914 0.0239  -0.0087 0.0019  14  GLU A C   
83   O  O   . GLU A 14  ? 0.1361 0.2011 0.2070 0.0247  -0.0313 0.0145  14  GLU A O   
84   C  CB  . GLU A 14  ? 0.1794 0.1921 0.3506 0.0129  -0.0604 0.0600  14  GLU A CB  
85   C  CG  . GLU A 14  ? 0.3574 0.2244 0.3364 -0.0774 -0.0534 0.0339  14  GLU A CG  
86   C  CD  . GLU A 14  ? 0.5921 0.4725 0.3454 -0.1432 0.0284  0.0158  14  GLU A CD  
87   O  OE1 . GLU A 14  ? 0.6343 0.4967 0.3193 -0.1468 -0.0354 0.0968  14  GLU A OE1 
88   O  OE2 . GLU A 14  ? 0.6401 0.3850 0.3295 0.0392  0.0845  -0.0395 14  GLU A OE2 
89   N  N   . HIS A 15  ? 0.1127 0.1744 0.1673 0.0089  -0.0008 -0.0044 15  HIS A N   
90   C  CA  . HIS A 15  ? 0.1067 0.1820 0.1698 0.0070  0.0115  0.0039  15  HIS A CA  
91   C  C   . HIS A 15  ? 0.0996 0.1952 0.1286 0.0146  -0.0053 -0.0078 15  HIS A C   
92   O  O   . HIS A 15  ? 0.0912 0.1975 0.1989 0.0059  0.0000  0.0001  15  HIS A O   
93   C  CB  . HIS A 15  ? 0.1189 0.1935 0.1716 0.0266  -0.0002 -0.0109 15  HIS A CB  
94   C  CG  . HIS A 15  ? 0.1324 0.2203 0.2085 0.0310  -0.0135 -0.0445 15  HIS A CG  
95   N  ND1 . HIS A 15  ? 0.1238 0.2398 0.2111 0.0231  0.0047  -0.0128 15  HIS A ND1 
96   C  CD2 . HIS A 15  ? 0.1788 0.2061 0.1780 0.0394  0.0085  -0.0078 15  HIS A CD2 
97   C  CE1 . HIS A 15  ? 0.1783 0.2799 0.2646 0.0702  -0.0381 -0.0455 15  HIS A CE1 
98   N  NE2 . HIS A 15  ? 0.1741 0.2307 0.2495 0.0570  0.0088  -0.0287 15  HIS A NE2 
99   N  N   . TRP A 16  ? 0.0924 0.1680 0.1641 0.0100  -0.0107 -0.0097 16  TRP A N   
100  C  CA  . TRP A 16  ? 0.0750 0.1636 0.1939 -0.0002 -0.0064 -0.0133 16  TRP A CA  
101  C  C   . TRP A 16  ? 0.0849 0.1741 0.1611 0.0078  -0.0074 -0.0036 16  TRP A C   
102  O  O   . TRP A 16  ? 0.1005 0.1569 0.1798 -0.0051 -0.0316 -0.0002 16  TRP A O   
103  C  CB  . TRP A 16  ? 0.0758 0.1806 0.1514 -0.0009 -0.0035 -0.0159 16  TRP A CB  
104  C  CG  . TRP A 16  ? 0.0969 0.1691 0.1298 0.0096  -0.0020 -0.0081 16  TRP A CG  
105  C  CD1 . TRP A 16  ? 0.1057 0.2092 0.1186 0.0093  0.0038  -0.0163 16  TRP A CD1 
106  C  CD2 . TRP A 16  ? 0.0934 0.1533 0.1454 0.0081  -0.0013 -0.0001 16  TRP A CD2 
107  N  NE1 . TRP A 16  ? 0.1071 0.1890 0.1619 0.0124  0.0029  -0.0199 16  TRP A NE1 
108  C  CE2 . TRP A 16  ? 0.0993 0.1905 0.1251 0.0182  -0.0042 0.0013  16  TRP A CE2 
109  C  CE3 . TRP A 16  ? 0.0842 0.1476 0.1500 0.0067  -0.0027 -0.0020 16  TRP A CE3 
110  C  CZ2 . TRP A 16  ? 0.1059 0.1689 0.1569 0.0067  0.0002  0.0027  16  TRP A CZ2 
111  C  CZ3 . TRP A 16  ? 0.0944 0.1612 0.1522 -0.0061 0.0034  -0.0019 16  TRP A CZ3 
112  C  CH2 . TRP A 16  ? 0.1347 0.1678 0.1420 0.0057  0.0046  0.0018  16  TRP A CH2 
113  N  N   . HIS A 17  ? 0.0908 0.1738 0.1554 0.0065  -0.0072 -0.0080 17  HIS A N   
114  C  CA  . HIS A 17  ? 0.1027 0.2066 0.1377 -0.0121 -0.0147 0.0027  17  HIS A CA  
115  C  C   . HIS A 17  ? 0.0919 0.1996 0.1780 0.0048  -0.0009 0.0009  17  HIS A C   
116  O  O   . HIS A 17  ? 0.0943 0.2124 0.1829 -0.0200 -0.0120 -0.0074 17  HIS A O   
117  C  CB  . HIS A 17  ? 0.1102 0.2068 0.1446 0.0104  0.0047  0.0008  17  HIS A CB  
118  C  CG  . HIS A 17  ? 0.1174 0.2222 0.1741 0.0128  -0.0110 0.0179  17  HIS A CG  
119  N  ND1 . HIS A 17  ? 0.1110 0.2353 0.1768 0.0024  -0.0154 0.0307  17  HIS A ND1 
120  C  CD2 . HIS A 17  ? 0.1201 0.2075 0.1867 0.0320  0.0067  0.0203  17  HIS A CD2 
121  C  CE1 . HIS A 17  ? 0.1198 0.2377 0.2082 0.0265  -0.0105 0.0176  17  HIS A CE1 
122  N  NE2 . HIS A 17  ? 0.1251 0.2507 0.1899 0.0392  0.0111  0.0379  17  HIS A NE2 
123  N  N   . LYS A 18  ? 0.0761 0.2249 0.1623 -0.0077 0.0013  0.0189  18  LYS A N   
124  C  CA  . LYS A 18  ? 0.0738 0.2206 0.2145 -0.0054 0.0104  0.0204  18  LYS A CA  
125  C  C   . LYS A 18  ? 0.1124 0.2305 0.2244 -0.0244 -0.0205 0.0436  18  LYS A C   
126  O  O   . LYS A 18  ? 0.1696 0.2627 0.3732 -0.0854 -0.0875 0.1058  18  LYS A O   
127  C  CB  . LYS A 18  ? 0.0985 0.2347 0.1750 0.0114  0.0008  0.0489  18  LYS A CB  
128  C  CG  . LYS A 18  ? 0.1213 0.2304 0.1980 0.0340  0.0167  0.0304  18  LYS A CG  
129  C  CD  . LYS A 18  ? 0.1279 0.2606 0.1980 0.0374  -0.0039 0.0075  18  LYS A CD  
130  C  CE  . LYS A 18  ? 0.1279 0.2311 0.2021 0.0379  0.0005  0.0403  18  LYS A CE  
131  N  NZ  . LYS A 18  ? 0.1172 0.2322 0.2068 0.0258  0.0126  0.0486  18  LYS A NZ  
132  N  N   A ASP A 19  ? 0.0961 0.2172 0.1881 0.0174  -0.0003 0.0209  19  ASP A N   
133  N  N   B ASP A 19  ? 0.0930 0.2258 0.1873 0.0105  0.0001  0.0258  19  ASP A N   
134  C  CA  A ASP A 19  ? 0.1382 0.2084 0.1931 -0.0073 0.0156  0.0172  19  ASP A CA  
135  C  CA  B ASP A 19  ? 0.0937 0.2182 0.2006 -0.0275 0.0044  0.0260  19  ASP A CA  
136  C  C   A ASP A 19  ? 0.1124 0.2020 0.1895 0.0006  0.0066  0.0364  19  ASP A C   
137  C  C   B ASP A 19  ? 0.1059 0.1910 0.2167 -0.0102 0.0040  0.0281  19  ASP A C   
138  O  O   A ASP A 19  ? 0.1346 0.2042 0.1648 -0.0232 -0.0069 0.0402  19  ASP A O   
139  O  O   B ASP A 19  ? 0.1169 0.1974 0.2554 -0.0239 -0.0277 0.0179  19  ASP A O   
140  C  CB  A ASP A 19  ? 0.2059 0.2771 0.1738 -0.0185 0.0206  -0.0168 19  ASP A CB  
141  C  CB  B ASP A 19  ? 0.0996 0.3190 0.1741 0.0368  -0.0150 0.0486  19  ASP A CB  
142  C  CG  A ASP A 19  ? 0.2497 0.3278 0.2158 0.0091  0.0399  -0.0534 19  ASP A CG  
143  C  CG  B ASP A 19  ? 0.1143 0.3342 0.2391 0.0009  0.0162  0.0562  19  ASP A CG  
144  O  OD1 A ASP A 19  ? 0.2332 0.2966 0.1448 0.0946  -0.0058 0.0653  19  ASP A OD1 
145  O  OD1 B ASP A 19  ? 0.1341 0.5544 0.2444 -0.0344 -0.0124 0.0990  19  ASP A OD1 
146  O  OD2 A ASP A 19  ? 0.3440 0.3383 0.2908 0.0985  0.0294  -0.0354 19  ASP A OD2 
147  O  OD2 B ASP A 19  ? 0.2229 0.3843 0.2504 0.0653  0.0063  0.0145  19  ASP A OD2 
148  N  N   . PHE A 20  ? 0.1172 0.1971 0.1610 -0.0083 0.0080  0.0225  20  PHE A N   
149  C  CA  . PHE A 20  ? 0.1146 0.1808 0.1644 -0.0127 0.0000  0.0026  20  PHE A CA  
150  C  C   . PHE A 20  ? 0.0991 0.1702 0.1622 -0.0049 0.0066  0.0075  20  PHE A C   
151  O  O   . PHE A 20  ? 0.1189 0.1590 0.1750 0.0006  0.0071  0.0079  20  PHE A O   
152  C  CB  . PHE A 20  ? 0.1067 0.2023 0.1953 -0.0141 -0.0185 0.0179  20  PHE A CB  
153  C  CG  . PHE A 20  ? 0.0807 0.2487 0.2175 -0.0212 -0.0201 0.0632  20  PHE A CG  
154  C  CD1 . PHE A 20  ? 0.1256 0.2493 0.2648 -0.0136 -0.0197 0.0564  20  PHE A CD1 
155  C  CD2 . PHE A 20  ? 0.1065 0.3509 0.1793 -0.0545 -0.0048 0.0429  20  PHE A CD2 
156  C  CE1 . PHE A 20  ? 0.1495 0.3276 0.2924 -0.0325 -0.0259 0.1174  20  PHE A CE1 
157  C  CE2 . PHE A 20  ? 0.1284 0.3996 0.1989 -0.0478 0.0002  0.0558  20  PHE A CE2 
158  C  CZ  . PHE A 20  ? 0.1196 0.3853 0.3008 -0.0592 -0.0488 0.0986  20  PHE A CZ  
159  N  N   . PRO A 21  ? 0.1243 0.1824 0.1884 -0.0223 -0.0120 0.0158  21  PRO A N   
160  C  CA  . PRO A 21  ? 0.1167 0.2305 0.1765 -0.0507 -0.0105 0.0190  21  PRO A CA  
161  C  C   . PRO A 21  ? 0.1137 0.2042 0.1589 -0.0377 -0.0166 -0.0168 21  PRO A C   
162  O  O   . PRO A 21  ? 0.1040 0.2297 0.1844 -0.0218 -0.0277 0.0083  21  PRO A O   
163  C  CB  . PRO A 21  ? 0.1318 0.3162 0.2122 -0.0899 -0.0209 0.0034  21  PRO A CB  
164  C  CG  . PRO A 21  ? 0.3377 0.3459 0.2703 -0.1729 -0.1120 0.0559  21  PRO A CG  
165  C  CD  . PRO A 21  ? 0.1384 0.2366 0.2152 -0.0514 0.0055  0.0319  21  PRO A CD  
166  N  N   A ILE A 22  ? 0.0962 0.1970 0.1571 -0.0290 -0.0051 -0.0146 22  ILE A N   
167  N  N   B ILE A 22  ? 0.1084 0.2032 0.1781 -0.0255 -0.0233 -0.0142 22  ILE A N   
168  C  CA  A ILE A 22  ? 0.1079 0.1702 0.1320 -0.0066 -0.0013 -0.0162 22  ILE A CA  
169  C  CA  B ILE A 22  ? 0.1201 0.1745 0.2036 -0.0186 -0.0106 0.0049  22  ILE A CA  
170  C  C   A ILE A 22  ? 0.0883 0.1732 0.1576 -0.0027 -0.0145 -0.0143 22  ILE A C   
171  C  C   B ILE A 22  ? 0.1070 0.1847 0.1540 -0.0214 0.0008  -0.0185 22  ILE A C   
172  O  O   A ILE A 22  ? 0.1134 0.1600 0.1762 0.0022  0.0040  -0.0011 22  ILE A O   
173  O  O   B ILE A 22  ? 0.0998 0.1816 0.1775 -0.0088 0.0071  -0.0004 22  ILE A O   
174  C  CB  A ILE A 22  ? 0.1349 0.1748 0.1224 0.0005  -0.0060 -0.0006 22  ILE A CB  
175  C  CB  B ILE A 22  ? 0.1490 0.1793 0.1946 -0.0021 -0.0100 0.0091  22  ILE A CB  
176  C  CG1 A ILE A 22  ? 0.1395 0.1458 0.1215 -0.0303 0.0011  -0.0335 22  ILE A CG1 
177  C  CG1 B ILE A 22  ? 0.2031 0.2131 0.2437 0.0161  0.0304  -0.0355 22  ILE A CG1 
178  C  CG2 A ILE A 22  ? 0.1226 0.1580 0.1472 -0.0428 -0.0081 -0.0288 22  ILE A CG2 
179  C  CG2 B ILE A 22  ? 0.1480 0.1910 0.2147 -0.0030 -0.0435 0.0107  22  ILE A CG2 
180  C  CD1 A ILE A 22  ? 0.1497 0.1860 0.2039 0.0177  -0.0039 -0.0313 22  ILE A CD1 
181  C  CD1 B ILE A 22  ? 0.1441 0.2253 0.2680 -0.0086 0.0061  -0.0061 22  ILE A CD1 
182  N  N   . ALA A 23  ? 0.0991 0.1727 0.1511 -0.0041 -0.0010 -0.0043 23  ALA A N   
183  C  CA  . ALA A 23  ? 0.1107 0.1650 0.1571 -0.0074 -0.0039 -0.0006 23  ALA A CA  
184  C  C   . ALA A 23  ? 0.1109 0.1673 0.1673 -0.0046 -0.0050 0.0016  23  ALA A C   
185  O  O   . ALA A 23  ? 0.1340 0.1697 0.1880 -0.0060 0.0037  -0.0037 23  ALA A O   
186  C  CB  . ALA A 23  ? 0.0930 0.1664 0.2024 0.0059  -0.0017 -0.0205 23  ALA A CB  
187  N  N   . LYS A 24  ? 0.1298 0.2165 0.1417 0.0335  -0.0164 -0.0075 24  LYS A N   
188  C  CA  . LYS A 24  ? 0.1240 0.2398 0.1636 0.0125  -0.0044 0.0023  24  LYS A CA  
189  C  C   . LYS A 24  ? 0.1379 0.2494 0.1597 -0.0064 -0.0082 -0.0047 24  LYS A C   
190  O  O   . LYS A 24  ? 0.1529 0.2817 0.1734 -0.0023 -0.0281 0.0027  24  LYS A O   
191  C  CB  . LYS A 24  ? 0.1344 0.2897 0.1794 0.0142  -0.0207 -0.0245 24  LYS A CB  
192  C  CG  . LYS A 24  ? 0.1518 0.3080 0.1646 0.0259  0.0262  0.0136  24  LYS A CG  
193  C  CD  . LYS A 24  ? 0.1835 0.2754 0.3705 0.0703  -0.0285 0.0257  24  LYS A CD  
194  C  CE  . LYS A 24  ? 0.1930 0.3031 0.3415 0.0878  0.0409  0.0710  24  LYS A CE  
195  N  NZ  . LYS A 24  ? 0.2861 0.3315 0.4854 0.0152  0.0441  0.0023  24  LYS A NZ  
196  N  N   . GLY A 25  ? 0.1181 0.2179 0.1669 0.0186  0.0013  -0.0093 25  GLY A N   
197  C  CA  . GLY A 25  ? 0.1562 0.2583 0.1661 -0.0134 0.0158  -0.0290 25  GLY A CA  
198  C  C   . GLY A 25  ? 0.1288 0.2321 0.1283 0.0022  -0.0124 -0.0306 25  GLY A C   
199  O  O   . GLY A 25  ? 0.1455 0.2476 0.1594 0.0063  -0.0278 -0.0157 25  GLY A O   
200  N  N   . GLU A 26  ? 0.1243 0.2860 0.1232 0.0021  -0.0108 -0.0535 26  GLU A N   
201  C  CA  . GLU A 26  ? 0.1601 0.3012 0.0996 -0.0079 -0.0147 -0.0290 26  GLU A CA  
202  C  C   . GLU A 26  ? 0.1511 0.2301 0.1276 -0.0138 -0.0207 -0.0226 26  GLU A C   
203  O  O   . GLU A 26  ? 0.1823 0.2442 0.1348 -0.0048 -0.0328 0.0092  26  GLU A O   
204  C  CB  . GLU A 26  ? 0.1737 0.3939 0.1712 -0.0514 -0.0126 -0.0973 26  GLU A CB  
205  C  CG  . GLU A 26  ? 0.1902 0.4852 0.1967 -0.0453 -0.0370 -0.0452 26  GLU A CG  
206  C  CD  . GLU A 26  ? 0.3359 0.5804 0.2797 0.0465  -0.0913 -0.0370 26  GLU A CD  
207  O  OE1 . GLU A 26  ? 0.4442 0.6414 0.3981 -0.0493 -0.2048 0.0559  26  GLU A OE1 
208  O  OE2 . GLU A 26  ? 0.3631 0.6353 0.4887 0.1837  -0.1052 -0.0424 26  GLU A OE2 
209  N  N   . ARG A 27  ? 0.1244 0.1722 0.1140 -0.0072 -0.0131 -0.0234 27  ARG A N   
210  C  CA  . ARG A 27  ? 0.1156 0.1465 0.1104 -0.0040 -0.0126 -0.0212 27  ARG A CA  
211  C  C   . ARG A 27  ? 0.1079 0.1451 0.1111 -0.0055 -0.0165 -0.0157 27  ARG A C   
212  O  O   . ARG A 27  ? 0.1128 0.1477 0.1361 0.0127  -0.0162 -0.0111 27  ARG A O   
213  C  CB  . ARG A 27  ? 0.2218 0.1822 0.1286 0.0299  -0.0320 -0.0675 27  ARG A CB  
214  C  CG  . ARG A 27  ? 0.2533 0.2156 0.1919 0.0106  -0.0054 -0.0270 27  ARG A CG  
215  C  CD  . ARG A 27  ? 0.3406 0.3169 0.2154 0.0678  -0.0540 -0.0469 27  ARG A CD  
216  N  NE  . ARG A 27  ? 0.2715 0.2138 0.1794 0.0222  0.0159  -0.0081 27  ARG A NE  
217  C  CZ  . ARG A 27  ? 0.2509 0.2122 0.1311 0.0410  0.0186  -0.0223 27  ARG A CZ  
218  N  NH1 . ARG A 27  ? 0.1804 0.2876 0.2158 0.0417  -0.0253 -0.1332 27  ARG A NH1 
219  N  NH2 . ARG A 27  ? 0.2062 0.2063 0.2467 -0.0200 0.0010  -0.0526 27  ARG A NH2 
220  N  N   . GLN A 28  ? 0.1068 0.1311 0.1038 0.0000  -0.0059 -0.0117 28  GLN A N   
221  C  CA  . GLN A 28  ? 0.0957 0.1404 0.1005 -0.0036 -0.0044 -0.0104 28  GLN A CA  
222  C  C   . GLN A 28  ? 0.0949 0.1192 0.0961 0.0050  -0.0053 0.0078  28  GLN A C   
223  O  O   . GLN A 28  ? 0.1217 0.1447 0.1064 -0.0234 -0.0100 0.0034  28  GLN A O   
224  C  CB  . GLN A 28  ? 0.0949 0.1521 0.1256 -0.0027 0.0059  -0.0044 28  GLN A CB  
225  C  CG  . GLN A 28  ? 0.1077 0.1494 0.1195 -0.0174 -0.0142 -0.0071 28  GLN A CG  
226  C  CD  . GLN A 28  ? 0.0906 0.1597 0.1013 -0.0098 -0.0082 -0.0187 28  GLN A CD  
227  O  OE1 . GLN A 28  ? 0.1118 0.1409 0.1261 -0.0120 0.0004  -0.0089 28  GLN A OE1 
228  N  NE2 . GLN A 28  ? 0.0935 0.1353 0.1456 0.0074  -0.0005 -0.0155 28  GLN A NE2 
229  N  N   . SER A 29  ? 0.1025 0.1174 0.0964 -0.0006 -0.0097 -0.0100 29  SER A N   
230  C  CA  . SER A 29  ? 0.0874 0.1061 0.1090 -0.0001 -0.0039 -0.0103 29  SER A CA  
231  C  C   . SER A 29  ? 0.0861 0.1155 0.1059 -0.0019 -0.0024 -0.0035 29  SER A C   
232  O  O   . SER A 29  ? 0.0960 0.1361 0.1143 -0.0039 0.0048  -0.0097 29  SER A O   
233  C  CB  . SER A 29  ? 0.0962 0.1135 0.1273 0.0100  -0.0088 -0.0175 29  SER A CB  
234  O  OG  . SER A 29  ? 0.0964 0.1210 0.1235 -0.0023 0.0010  -0.0083 29  SER A OG  
235  N  N   . PRO A 30  ? 0.0974 0.1149 0.0952 0.0034  0.0026  -0.0080 30  PRO A N   
236  C  CA  . PRO A 30  ? 0.1080 0.1220 0.1003 -0.0118 -0.0047 -0.0020 30  PRO A CA  
237  C  C   . PRO A 30  ? 0.1079 0.1089 0.0941 0.0000  0.0025  -0.0063 30  PRO A C   
238  O  O   . PRO A 30  ? 0.1046 0.1270 0.1156 0.0006  -0.0109 -0.0012 30  PRO A O   
239  C  CB  . PRO A 30  ? 0.1155 0.1210 0.0898 0.0177  -0.0171 -0.0106 30  PRO A CB  
240  C  CG  . PRO A 30  ? 0.1073 0.1246 0.1107 -0.0040 -0.0038 -0.0034 30  PRO A CG  
241  C  CD  . PRO A 30  ? 0.1072 0.1146 0.1124 0.0069  0.0000  -0.0231 30  PRO A CD  
242  N  N   . VAL A 31  ? 0.1185 0.1188 0.0935 0.0059  0.0084  0.0160  31  VAL A N   
243  C  CA  . VAL A 31  ? 0.1317 0.1198 0.0942 -0.0033 0.0065  0.0168  31  VAL A CA  
244  C  C   . VAL A 31  ? 0.1397 0.1264 0.0974 0.0005  0.0064  0.0089  31  VAL A C   
245  O  O   . VAL A 31  ? 0.1331 0.1256 0.1256 -0.0053 -0.0116 0.0168  31  VAL A O   
246  C  CB  . VAL A 31  ? 0.1187 0.1429 0.1137 -0.0035 0.0049  -0.0032 31  VAL A CB  
247  C  CG1 . VAL A 31  ? 0.1553 0.1358 0.1436 -0.0121 -0.0033 -0.0015 31  VAL A CG1 
248  C  CG2 . VAL A 31  ? 0.1333 0.1435 0.1276 0.0127  0.0084  -0.0033 31  VAL A CG2 
249  N  N   . ASP A 32  ? 0.1261 0.1234 0.1086 0.0005  -0.0013 0.0134  32  ASP A N   
250  C  CA  . ASP A 32  ? 0.1504 0.1221 0.1120 0.0092  0.0095  0.0236  32  ASP A CA  
251  C  C   . ASP A 32  ? 0.1436 0.1437 0.0935 -0.0059 0.0023  0.0219  32  ASP A C   
252  O  O   . ASP A 32  ? 0.1508 0.1835 0.1219 -0.0012 0.0010  -0.0192 32  ASP A O   
253  C  CB  . ASP A 32  ? 0.1862 0.1113 0.1495 0.0115  0.0158  0.0304  32  ASP A CB  
254  C  CG  . ASP A 32  ? 0.1675 0.1504 0.1346 0.0127  -0.0100 0.0309  32  ASP A CG  
255  O  OD1 . ASP A 32  ? 0.1801 0.1272 0.1296 0.0055  -0.0060 0.0243  32  ASP A OD1 
256  O  OD2 . ASP A 32  ? 0.2382 0.1640 0.1601 -0.0122 0.0010  0.0368  32  ASP A OD2 
257  N  N   . ILE A 33  ? 0.1315 0.1342 0.1219 -0.0031 0.0088  0.0125  33  ILE A N   
258  C  CA  . ILE A 33  ? 0.1443 0.1487 0.1174 -0.0041 0.0011  0.0308  33  ILE A CA  
259  C  C   . ILE A 33  ? 0.1687 0.1482 0.1258 0.0134  0.0323  0.0311  33  ILE A C   
260  O  O   . ILE A 33  ? 0.1967 0.1393 0.1698 0.0048  0.0017  0.0254  33  ILE A O   
261  C  CB  . ILE A 33  ? 0.1401 0.1410 0.1381 0.0135  0.0168  0.0329  33  ILE A CB  
262  C  CG1 . ILE A 33  ? 0.1544 0.1355 0.1477 -0.0041 -0.0184 0.0359  33  ILE A CG1 
263  C  CG2 . ILE A 33  ? 0.1690 0.1927 0.1666 0.0261  0.0464  0.0435  33  ILE A CG2 
264  C  CD1 . ILE A 33  ? 0.1384 0.1639 0.1837 0.0001  -0.0346 0.0402  33  ILE A CD1 
265  N  N   A ASP A 34  ? 0.1920 0.1626 0.1386 0.0150  0.0001  0.0330  34  ASP A N   
266  N  N   B ASP A 34  ? 0.1841 0.1611 0.1187 0.0050  0.0281  0.0396  34  ASP A N   
267  C  CA  A ASP A 34  ? 0.2025 0.1932 0.1448 0.0188  0.0098  0.0458  34  ASP A CA  
268  C  CA  B ASP A 34  ? 0.1851 0.1793 0.1141 0.0125  0.0434  0.0392  34  ASP A CA  
269  C  C   A ASP A 34  ? 0.2268 0.1757 0.1118 0.0519  0.0259  0.0520  34  ASP A C   
270  C  C   B ASP A 34  ? 0.2104 0.1787 0.1061 0.0464  0.0595  0.0427  34  ASP A C   
271  O  O   A ASP A 34  ? 0.2224 0.2398 0.1307 0.0547  0.0332  0.0133  34  ASP A O   
272  O  O   B ASP A 34  ? 0.2632 0.1820 0.1213 0.0605  0.0458  0.0364  34  ASP A O   
273  C  CB  A ASP A 34  ? 0.2762 0.1891 0.1599 0.0672  -0.0223 0.0491  34  ASP A CB  
274  C  CB  B ASP A 34  ? 0.2348 0.1985 0.1326 0.0460  0.0132  0.0417  34  ASP A CB  
275  C  CG  A ASP A 34  ? 0.3104 0.2438 0.1823 0.0706  0.0540  0.0846  34  ASP A CG  
276  C  CG  B ASP A 34  ? 0.2003 0.1788 0.1294 0.0450  0.0237  0.0257  34  ASP A CG  
277  O  OD1 A ASP A 34  ? 0.4145 0.2028 0.2703 0.0771  0.0582  0.0966  34  ASP A OD1 
278  O  OD1 B ASP A 34  ? 0.2210 0.2096 0.1410 0.0253  0.0141  0.0876  34  ASP A OD1 
279  O  OD2 A ASP A 34  ? 0.3283 0.2625 0.2075 0.0743  0.0666  0.0204  34  ASP A OD2 
280  O  OD2 B ASP A 34  ? 0.2933 0.2851 0.1644 0.0286  -0.0617 0.0638  34  ASP A OD2 
281  N  N   . THR A 35  ? 0.1975 0.2075 0.1719 0.0439  0.0455  0.0816  35  THR A N   
282  C  CA  . THR A 35  ? 0.2038 0.2165 0.1993 0.0737  0.0700  0.0796  35  THR A CA  
283  C  C   . THR A 35  ? 0.2611 0.2059 0.1872 0.0674  0.0886  0.0783  35  THR A C   
284  O  O   . THR A 35  ? 0.2375 0.2233 0.2363 0.0607  0.0661  0.0348  35  THR A O   
285  C  CB  . THR A 35  ? 0.2176 0.2434 0.2214 0.0569  0.0418  0.0768  35  THR A CB  
286  O  OG1 . THR A 35  ? 0.2014 0.2337 0.2429 0.0103  0.0471  0.0796  35  THR A OG1 
287  C  CG2 . THR A 35  ? 0.2343 0.2909 0.1884 0.0612  0.0355  0.0635  35  THR A CG2 
288  N  N   . HIS A 36  ? 0.3125 0.2221 0.1888 0.0746  0.1042  0.1111  36  HIS A N   
289  C  CA  . HIS A 36  ? 0.3783 0.2185 0.1876 0.0765  0.1004  0.1138  36  HIS A CA  
290  C  C   . HIS A 36  ? 0.3917 0.3010 0.1405 0.0539  0.0807  0.0730  36  HIS A C   
291  O  O   . HIS A 36  ? 0.3402 0.4937 0.1491 0.1209  0.0289  0.0447  36  HIS A O   
292  C  CB  . HIS A 36  ? 0.4168 0.2225 0.1716 0.0765  0.0678  0.0945  36  HIS A CB  
293  C  CG  . HIS A 36  ? 0.5914 0.1869 0.2242 0.0621  -0.0187 0.0491  36  HIS A CG  
294  N  ND1 . HIS A 36  ? 0.6338 0.3252 0.1981 -0.1377 -0.0991 0.0664  36  HIS A ND1 
295  C  CD2 . HIS A 36  ? 0.6425 0.2927 0.2262 0.0655  -0.1515 -0.0155 36  HIS A CD2 
296  C  CE1 . HIS A 36  ? 0.6174 0.3129 0.1942 -0.0567 -0.1632 0.0586  36  HIS A CE1 
297  N  NE2 . HIS A 36  ? 0.7862 0.2115 0.4280 0.0597  -0.0389 0.0392  36  HIS A NE2 
298  N  N   . THR A 37  ? 0.3731 0.2266 0.2080 0.1004  0.0665  0.0639  37  THR A N   
299  C  CA  . THR A 37  ? 0.3600 0.2741 0.1630 0.1165  0.0438  0.0612  37  THR A CA  
300  C  C   . THR A 37  ? 0.2750 0.2501 0.1529 0.0797  -0.0025 0.0272  37  THR A C   
301  O  O   . THR A 37  ? 0.4501 0.2599 0.1946 0.0995  -0.0201 0.0083  37  THR A O   
302  C  CB  . THR A 37  ? 0.3167 0.3156 0.4274 0.1175  -0.1067 0.0193  37  THR A CB  
303  O  OG1 . THR A 37  ? 0.4917 0.4061 0.5542 0.1655  0.0588  0.1045  37  THR A OG1 
304  C  CG2 . THR A 37  ? 0.4248 0.4704 0.4433 0.0838  -0.1544 0.0488  37  THR A CG2 
305  N  N   . ALA A 38  ? 0.2291 0.2407 0.1411 0.0709  0.0422  0.0529  38  ALA A N   
306  C  CA  . ALA A 38  ? 0.2513 0.1957 0.1596 0.0653  0.0577  0.0502  38  ALA A CA  
307  C  C   . ALA A 38  ? 0.2871 0.2373 0.2208 0.0551  0.0911  0.0447  38  ALA A C   
308  O  O   . ALA A 38  ? 0.3575 0.2520 0.4096 0.0662  0.1743  0.0868  38  ALA A O   
309  C  CB  . ALA A 38  ? 0.2361 0.2011 0.1881 0.0389  0.0155  0.0425  38  ALA A CB  
310  N  N   . LYS A 39  ? 0.2499 0.2477 0.1665 0.0840  0.0107  -0.0003 39  LYS A N   
311  C  CA  . LYS A 39  ? 0.2968 0.3065 0.1880 0.1496  -0.0193 -0.0573 39  LYS A CA  
312  C  C   . LYS A 39  ? 0.2096 0.3034 0.1298 0.0768  0.0489  0.0331  39  LYS A C   
313  O  O   . LYS A 39  ? 0.1744 0.2793 0.1238 0.0520  0.0027  0.0130  39  LYS A O   
314  C  CB  . LYS A 39  ? 0.3644 0.3601 0.2358 0.1728  -0.1137 -0.0972 39  LYS A CB  
315  C  CG  . LYS A 39  ? 0.4148 0.4916 0.1752 0.1074  -0.0469 -0.0706 39  LYS A CG  
316  C  CD  . LYS A 39  ? 0.2329 0.4303 0.2703 0.1129  0.0065  -0.0114 39  LYS A CD  
317  C  CE  . LYS A 39  ? 0.3319 0.4615 0.2807 0.0759  0.0290  -0.0394 39  LYS A CE  
318  N  NZ  . LYS A 39  ? 0.2588 0.5583 0.4037 0.0466  0.0260  0.0999  39  LYS A NZ  
319  N  N   . TYR A 40  ? 0.2375 0.2622 0.1500 0.0491  0.0253  0.0285  40  TYR A N   
320  C  CA  . TYR A 40  ? 0.2300 0.2470 0.1529 0.0159  0.0353  0.0122  40  TYR A CA  
321  C  C   . TYR A 40  ? 0.1824 0.2864 0.1113 0.0316  0.0295  -0.0026 40  TYR A C   
322  O  O   . TYR A 40  ? 0.2536 0.3528 0.1188 0.0754  0.0158  -0.0127 40  TYR A O   
323  C  CB  . TYR A 40  ? 0.2469 0.2603 0.2289 0.0041  0.0608  0.0397  40  TYR A CB  
324  C  CG  . TYR A 40  ? 0.2382 0.3001 0.1971 0.0006  0.0595  0.0533  40  TYR A CG  
325  C  CD1 . TYR A 40  ? 0.2091 0.3475 0.2032 -0.0611 0.0009  0.0311  40  TYR A CD1 
326  C  CD2 . TYR A 40  ? 0.2666 0.4832 0.2613 0.0012  0.0886  0.0171  40  TYR A CD2 
327  C  CE1 . TYR A 40  ? 0.2280 0.4449 0.1272 -0.0205 -0.0017 0.0019  40  TYR A CE1 
328  C  CE2 . TYR A 40  ? 0.2908 0.4841 0.1962 -0.0130 0.0385  -0.0281 40  TYR A CE2 
329  C  CZ  . TYR A 40  ? 0.1870 0.6575 0.1873 -0.0140 -0.0044 -0.0579 40  TYR A CZ  
330  O  OH  . TYR A 40  ? 0.2584 0.6612 0.3202 0.0946  0.0370  0.0356  40  TYR A OH  
331  N  N   . ASP A 41  ? 0.1880 0.2409 0.1648 0.0411  0.0130  -0.0083 41  ASP A N   
332  C  CA  . ASP A 41  ? 0.2274 0.2370 0.1802 0.0315  -0.0276 0.0072  41  ASP A CA  
333  C  C   . ASP A 41  ? 0.2492 0.2865 0.1687 0.0883  0.0021  -0.0326 41  ASP A C   
334  O  O   . ASP A 41  ? 0.2133 0.2743 0.1884 0.0564  -0.0100 -0.0249 41  ASP A O   
335  C  CB  . ASP A 41  ? 0.2484 0.2563 0.2405 0.0009  -0.0324 -0.0120 41  ASP A CB  
336  C  CG  . ASP A 41  ? 0.3913 0.2764 0.2538 -0.0576 -0.1042 -0.0478 41  ASP A CG  
337  O  OD1 . ASP A 41  ? 0.5541 0.3253 0.2488 0.0051  -0.0565 -0.1041 41  ASP A OD1 
338  O  OD2 . ASP A 41  ? 0.4292 0.3264 0.3715 -0.1295 -0.1169 0.0302  41  ASP A OD2 
339  N  N   . PRO A 42  ? 0.2689 0.4686 0.1787 0.1040  0.0159  -0.0060 42  PRO A N   
340  C  CA  . PRO A 42  ? 0.2427 0.4573 0.2883 0.1327  0.0846  0.0514  42  PRO A CA  
341  C  C   . PRO A 42  ? 0.3195 0.3949 0.2957 0.1138  0.0873  -0.0163 42  PRO A C   
342  O  O   . PRO A 42  ? 0.3345 0.5867 0.4312 0.2098  0.0164  -0.0719 42  PRO A O   
343  C  CB  . PRO A 42  ? 0.3563 0.5102 0.2950 0.0734  0.1372  0.0241  42  PRO A CB  
344  C  CG  . PRO A 42  ? 0.4410 0.6998 0.2785 0.2011  0.1233  0.0696  42  PRO A CG  
345  C  CD  . PRO A 42  ? 0.4649 0.3808 0.1551 0.1248  0.1208  0.0218  42  PRO A CD  
346  N  N   . SER A 43  ? 0.3978 0.3580 0.2060 0.0897  0.0734  -0.0618 43  SER A N   
347  C  CA  . SER A 43  ? 0.5212 0.3047 0.2257 0.0562  0.0186  -0.0886 43  SER A CA  
348  C  C   . SER A 43  ? 0.3552 0.2859 0.2400 0.0923  -0.0151 0.0022  43  SER A C   
349  O  O   . SER A 43  ? 0.5671 0.2898 0.3134 0.1606  -0.0650 -0.0331 43  SER A O   
350  C  CB  . SER A 43  ? 0.6027 0.3837 0.2761 0.0212  -0.0219 -0.1212 43  SER A CB  
351  O  OG  . SER A 43  ? 0.6005 0.4181 0.2416 0.0256  -0.0978 -0.0864 43  SER A OG  
352  N  N   . LEU A 44  ? 0.3437 0.2969 0.2370 0.1096  -0.0364 -0.0016 44  LEU A N   
353  C  CA  . LEU A 44  ? 0.2875 0.3570 0.2348 0.0902  -0.0445 0.0113  44  LEU A CA  
354  C  C   . LEU A 44  ? 0.2785 0.4114 0.2974 -0.0230 -0.0687 0.0924  44  LEU A C   
355  O  O   . LEU A 44  ? 0.2370 0.4623 0.4059 -0.0046 -0.0373 0.1275  44  LEU A O   
356  C  CB  . LEU A 44  ? 0.2312 0.3413 0.2064 0.0076  -0.0307 -0.0381 44  LEU A CB  
357  C  CG  . LEU A 44  ? 0.2141 0.3565 0.1465 0.0307  0.0089  0.0491  44  LEU A CG  
358  C  CD1 . LEU A 44  ? 0.2454 0.3359 0.1938 -0.0204 0.0029  -0.0245 44  LEU A CD1 
359  C  CD2 . LEU A 44  ? 0.3078 0.3245 0.1916 -0.0489 -0.0250 0.0021  44  LEU A CD2 
360  N  N   . LYS A 45  ? 0.2483 0.3501 0.2564 0.0117  -0.0280 0.0333  45  LYS A N   
361  C  CA  . LYS A 45  ? 0.2755 0.3123 0.3534 0.0013  -0.0906 -0.0402 45  LYS A CA  
362  C  C   . LYS A 45  ? 0.1967 0.4013 0.1989 0.0659  0.0034  0.0100  45  LYS A C   
363  O  O   . LYS A 45  ? 0.1672 0.3704 0.3085 -0.0049 0.0142  -0.0514 45  LYS A O   
364  C  CB  . LYS A 45  ? 0.3155 0.3227 0.2509 0.1267  0.0473  -0.0706 45  LYS A CB  
365  C  CG  . LYS A 45  ? 0.3105 0.4104 0.2776 0.0825  -0.0460 -0.1141 45  LYS A CG  
366  C  CD  . LYS A 45  ? 0.6506 0.3671 0.4370 -0.0410 -0.0097 -0.0455 45  LYS A CD  
367  N  N   . PRO A 46  ? 0.1719 0.2887 0.2460 -0.0211 0.0116  0.0190  46  PRO A N   
368  C  CA  . PRO A 46  ? 0.1844 0.3072 0.1987 -0.0186 -0.0036 0.0358  46  PRO A CA  
369  C  C   . PRO A 46  ? 0.1720 0.2665 0.1579 -0.0243 0.0052  0.0098  46  PRO A C   
370  O  O   . PRO A 46  ? 0.1633 0.2705 0.2397 -0.0247 -0.0141 0.0127  46  PRO A O   
371  C  CB  . PRO A 46  ? 0.1478 0.3571 0.2845 -0.0370 0.0272  -0.0122 46  PRO A CB  
372  C  CG  . PRO A 46  ? 0.2240 0.4576 0.2675 0.0307  0.0121  -0.0357 46  PRO A CG  
373  C  CD  . PRO A 46  ? 0.2614 0.3707 0.2563 0.0837  0.0155  -0.0657 46  PRO A CD  
374  N  N   A LEU A 47  ? 0.2348 0.3040 0.2463 0.0247  0.0113  0.0003  47  LEU A N   
375  N  N   B LEU A 47  ? 0.1252 0.2800 0.2028 0.0001  -0.0081 0.0058  47  LEU A N   
376  C  CA  A LEU A 47  ? 0.1551 0.3062 0.1823 0.0038  -0.0026 -0.0379 47  LEU A CA  
377  C  CA  B LEU A 47  ? 0.1241 0.1865 0.2078 -0.0136 0.0171  -0.0263 47  LEU A CA  
378  C  C   A LEU A 47  ? 0.1046 0.2921 0.2855 -0.0363 0.0000  0.0384  47  LEU A C   
379  C  C   B LEU A 47  ? 0.1324 0.2210 0.2979 -0.0163 -0.0447 -0.0231 47  LEU A C   
380  O  O   A LEU A 47  ? 0.1070 0.3415 0.2841 -0.0502 0.0106  0.0036  47  LEU A O   
381  O  O   B LEU A 47  ? 0.1306 0.1872 0.2293 -0.0059 -0.0237 -0.0265 47  LEU A O   
382  C  CB  A LEU A 47  ? 0.1430 0.2515 0.3151 0.0253  -0.0233 -0.0158 47  LEU A CB  
383  C  CB  B LEU A 47  ? 0.2533 0.2253 0.2407 0.0439  0.0337  -0.0294 47  LEU A CB  
384  C  CG  A LEU A 47  ? 0.0632 0.3005 0.3703 -0.0187 0.0001  -0.0566 47  LEU A CG  
385  C  CG  B LEU A 47  ? 0.2368 0.2377 0.3624 -0.0221 -0.0174 0.0579  47  LEU A CG  
386  C  CD1 A LEU A 47  ? 0.1382 0.2171 0.3677 -0.0499 -0.0105 -0.0408 47  LEU A CD1 
387  C  CD1 B LEU A 47  ? 0.2455 0.2709 0.3482 0.0125  -0.1735 -0.0295 47  LEU A CD1 
388  C  CD2 A LEU A 47  ? 0.1435 0.2999 0.3353 0.0871  -0.0697 -0.0276 47  LEU A CD2 
389  C  CD2 B LEU A 47  ? 0.1337 0.3502 0.4285 -0.0507 -0.0420 -0.0003 47  LEU A CD2 
390  N  N   . SER A 48  ? 0.1361 0.2222 0.2045 -0.0241 -0.0241 0.0008  48  SER A N   
391  C  CA  . SER A 48  ? 0.1608 0.2443 0.1661 -0.0060 -0.0089 -0.0219 48  SER A CA  
392  C  C   . SER A 48  ? 0.1399 0.2398 0.1747 -0.0058 -0.0077 -0.0222 48  SER A C   
393  O  O   . SER A 48  ? 0.1549 0.2366 0.2276 -0.0341 0.0024  -0.0332 48  SER A O   
394  C  CB  . SER A 48  ? 0.1831 0.2637 0.2229 0.0110  -0.0201 -0.0249 48  SER A CB  
395  O  OG  . SER A 48  ? 0.2393 0.3198 0.2725 0.0760  0.0117  0.0294  48  SER A OG  
396  N  N   . VAL A 49  ? 0.1801 0.2687 0.1639 -0.0322 -0.0017 -0.0295 49  VAL A N   
397  C  CA  . VAL A 49  ? 0.2343 0.2298 0.1993 -0.0558 0.0255  -0.0593 49  VAL A CA  
398  C  C   . VAL A 49  ? 0.1779 0.3140 0.2384 -0.0849 0.0082  -0.0221 49  VAL A C   
399  O  O   . VAL A 49  ? 0.2581 0.4212 0.2183 -0.1867 -0.0033 -0.0088 49  VAL A O   
400  C  CB  . VAL A 49  ? 0.2545 0.2285 0.2134 -0.0653 0.0832  -0.0653 49  VAL A CB  
401  C  CG1 . VAL A 49  ? 0.4503 0.2340 0.2676 -0.1351 0.1798  -0.0765 49  VAL A CG1 
402  C  CG2 . VAL A 49  ? 0.2799 0.2361 0.3631 -0.0714 0.0291  -0.0189 49  VAL A CG2 
403  N  N   . SER A 50  ? 0.1752 0.2546 0.2246 -0.0245 0.0065  -0.0483 50  SER A N   
404  C  CA  . SER A 50  ? 0.1319 0.2803 0.2687 -0.0276 -0.0080 -0.0398 50  SER A CA  
405  C  C   . SER A 50  ? 0.1176 0.2693 0.2249 -0.0153 -0.0310 -0.0385 50  SER A C   
406  O  O   . SER A 50  ? 0.1632 0.2348 0.2509 -0.0133 -0.0435 -0.0127 50  SER A O   
407  C  CB  . SER A 50  ? 0.2817 0.3527 0.3236 0.0302  0.0445  -0.1178 50  SER A CB  
408  O  OG  . SER A 50  ? 0.2339 0.4301 0.3846 -0.0705 0.0370  -0.1342 50  SER A OG  
409  N  N   . TYR A 51  ? 0.1333 0.2701 0.2397 -0.0166 0.0006  -0.0460 51  TYR A N   
410  C  CA  . TYR A 51  ? 0.1804 0.2157 0.2176 -0.0080 -0.0004 -0.0374 51  TYR A CA  
411  C  C   . TYR A 51  ? 0.1533 0.2086 0.2445 0.0059  -0.0040 -0.0316 51  TYR A C   
412  O  O   . TYR A 51  ? 0.1575 0.2264 0.2287 0.0021  -0.0254 -0.0080 51  TYR A O   
413  C  CB  . TYR A 51  ? 0.1562 0.2359 0.1831 0.0000  -0.0303 -0.0385 51  TYR A CB  
414  C  CG  . TYR A 51  ? 0.1355 0.2002 0.1700 -0.0267 0.0017  -0.0144 51  TYR A CG  
415  C  CD1 . TYR A 51  ? 0.1311 0.1712 0.2305 -0.0157 -0.0088 -0.0281 51  TYR A CD1 
416  C  CD2 . TYR A 51  ? 0.1398 0.1905 0.1740 -0.0170 0.0064  0.0005  51  TYR A CD2 
417  C  CE1 . TYR A 51  ? 0.1273 0.1766 0.2120 -0.0125 0.0069  -0.0003 51  TYR A CE1 
418  C  CE2 . TYR A 51  ? 0.1342 0.1722 0.1587 -0.0310 0.0065  -0.0170 51  TYR A CE2 
419  C  CZ  . TYR A 51  ? 0.1301 0.1568 0.2159 -0.0351 -0.0205 -0.0067 51  TYR A CZ  
420  O  OH  . TYR A 51  ? 0.1381 0.1648 0.2171 -0.0152 -0.0280 -0.0250 51  TYR A OH  
421  N  N   . ASP A 52  ? 0.1223 0.2897 0.3226 0.0006  -0.0283 -0.0135 52  ASP A N   
422  C  CA  . ASP A 52  ? 0.1297 0.2964 0.3149 -0.0414 -0.0220 0.0606  52  ASP A CA  
423  C  C   . ASP A 52  ? 0.2006 0.2835 0.2937 -0.0027 -0.0595 0.0484  52  ASP A C   
424  O  O   . ASP A 52  ? 0.2443 0.3842 0.3106 -0.0644 -0.0912 0.0856  52  ASP A O   
425  C  CB  . ASP A 52  ? 0.1848 0.3644 0.3514 0.0026  0.0416  0.0647  52  ASP A CB  
426  C  CG  . ASP A 52  ? 0.2518 0.4747 0.6175 0.0992  0.0710  -0.0604 52  ASP A CG  
427  O  OD1 . ASP A 52  ? 0.3333 0.6426 0.6660 0.1279  0.1722  -0.0114 52  ASP A OD1 
428  O  OD2 . ASP A 52  ? 0.3729 0.5155 0.9493 0.1018  0.1043  0.1701  52  ASP A OD2 
429  N  N   . GLN A 53  ? 0.1294 0.2235 0.3315 0.0248  0.0000  0.0278  53  GLN A N   
430  C  CA  . GLN A 53  ? 0.1661 0.2366 0.2265 0.0109  -0.0146 0.0019  53  GLN A CA  
431  C  C   . GLN A 53  ? 0.1705 0.2043 0.1733 0.0177  -0.0215 0.0201  53  GLN A C   
432  O  O   . GLN A 53  ? 0.1761 0.2043 0.2140 0.0333  -0.0137 0.0218  53  GLN A O   
433  C  CB  . GLN A 53  ? 0.1795 0.2449 0.2824 0.0458  -0.0304 -0.0120 53  GLN A CB  
434  C  CG  . GLN A 53  ? 0.2297 0.3124 0.2713 0.0895  0.0361  0.0343  53  GLN A CG  
435  C  CD  . GLN A 53  ? 0.2307 0.4571 0.3581 0.0961  -0.0121 0.1437  53  GLN A CD  
436  O  OE1 . GLN A 53  ? 0.3116 0.7318 0.5794 -0.0220 0.1225  0.1336  53  GLN A OE1 
437  N  NE2 . GLN A 53  ? 0.2057 0.3200 0.3556 0.0560  -0.0294 0.1089  53  GLN A NE2 
438  N  N   . ALA A 54  ? 0.1471 0.1877 0.1896 0.0063  0.0084  -0.0100 54  ALA A N   
439  C  CA  . ALA A 54  ? 0.1319 0.1824 0.1610 0.0140  -0.0009 0.0016  54  ALA A CA  
440  C  C   . ALA A 54  ? 0.1504 0.1856 0.1585 -0.0033 -0.0115 -0.0340 54  ALA A C   
441  O  O   . ALA A 54  ? 0.1544 0.2404 0.1852 -0.0198 -0.0178 -0.0442 54  ALA A O   
442  C  CB  . ALA A 54  ? 0.1659 0.1869 0.2387 0.0258  0.0121  0.0115  54  ALA A CB  
443  N  N   . THR A 55  ? 0.1346 0.1546 0.1653 0.0075  -0.0129 -0.0093 55  THR A N   
444  C  CA  . THR A 55  ? 0.1390 0.1456 0.1650 0.0153  -0.0195 0.0095  55  THR A CA  
445  C  C   . THR A 55  ? 0.1366 0.1187 0.1464 0.0085  -0.0217 0.0301  55  THR A C   
446  O  O   . THR A 55  ? 0.1465 0.1280 0.1612 -0.0017 -0.0388 0.0159  55  THR A O   
447  C  CB  . THR A 55  ? 0.1454 0.1716 0.2165 0.0212  -0.0386 0.0400  55  THR A CB  
448  O  OG1 . THR A 55  ? 0.1738 0.1999 0.1982 0.0354  -0.0162 0.0190  55  THR A OG1 
449  C  CG2 . THR A 55  ? 0.2099 0.1704 0.1817 0.0133  -0.0537 0.0385  55  THR A CG2 
450  N  N   . SER A 56  ? 0.1159 0.1276 0.1244 -0.0120 -0.0125 0.0217  56  SER A N   
451  C  CA  . SER A 56  ? 0.1289 0.1203 0.1342 0.0131  -0.0136 0.0237  56  SER A CA  
452  C  C   . SER A 56  ? 0.1412 0.1222 0.1183 0.0075  -0.0207 0.0282  56  SER A C   
453  O  O   . SER A 56  ? 0.1416 0.1439 0.1338 0.0010  -0.0313 0.0376  56  SER A O   
454  C  CB  . SER A 56  ? 0.1655 0.1215 0.1232 -0.0076 -0.0403 0.0159  56  SER A CB  
455  O  OG  . SER A 56  ? 0.1487 0.1354 0.1232 -0.0016 -0.0183 0.0108  56  SER A OG  
456  N  N   . LEU A 57  ? 0.1321 0.1410 0.1310 0.0006  0.0003  0.0127  57  LEU A N   
457  C  CA  . LEU A 57  ? 0.1597 0.1362 0.1307 0.0040  -0.0074 0.0208  57  LEU A CA  
458  C  C   . LEU A 57  ? 0.1610 0.1278 0.1108 0.0046  0.0083  0.0351  57  LEU A C   
459  O  O   . LEU A 57  ? 0.1816 0.1605 0.1196 0.0131  -0.0039 0.0293  57  LEU A O   
460  C  CB  . LEU A 57  ? 0.1659 0.1490 0.1725 -0.0170 0.0058  0.0135  57  LEU A CB  
461  C  CG  . LEU A 57  ? 0.1783 0.1473 0.1809 -0.0168 0.0025  -0.0032 57  LEU A CG  
462  C  CD1 . LEU A 57  ? 0.2025 0.1945 0.2346 -0.0511 0.0077  -0.0392 57  LEU A CD1 
463  C  CD2 . LEU A 57  ? 0.2115 0.1877 0.2663 0.0276  -0.0162 0.0164  57  LEU A CD2 
464  N  N   . ARG A 58  ? 0.1579 0.1399 0.1394 -0.0013 -0.0192 0.0230  58  ARG A N   
465  C  CA  . ARG A 58  ? 0.1576 0.1468 0.1543 -0.0107 0.0136  0.0457  58  ARG A CA  
466  C  C   . ARG A 58  ? 0.1263 0.1474 0.1163 -0.0092 -0.0052 0.0214  58  ARG A C   
467  O  O   . ARG A 58  ? 0.1817 0.1528 0.1198 0.0211  -0.0024 0.0226  58  ARG A O   
468  C  CB  . ARG A 58  ? 0.1763 0.1515 0.1766 -0.0353 0.0005  0.0425  58  ARG A CB  
469  C  CG  . ARG A 58  ? 0.2139 0.1578 0.2477 -0.0240 0.0230  0.0582  58  ARG A CG  
470  C  CD  . ARG A 58  ? 0.2680 0.1899 0.3168 -0.0317 0.0719  0.0563  58  ARG A CD  
471  N  NE  . ARG A 58  ? 0.3946 0.2708 0.3165 -0.0233 0.1464  0.0576  58  ARG A NE  
472  C  CZ  . ARG A 58  ? 0.3820 0.2358 0.3021 -0.0060 0.0540  0.1263  58  ARG A CZ  
473  N  NH1 . ARG A 58  ? 0.3705 0.2437 0.3799 -0.0254 0.1198  0.0731  58  ARG A NH1 
474  N  NH2 . ARG A 58  ? 0.4041 0.2995 0.4201 0.0396  0.0540  0.1718  58  ARG A NH2 
475  N  N   . ILE A 59  ? 0.1542 0.1377 0.1097 0.0055  -0.0139 0.0132  59  ILE A N   
476  C  CA  . ILE A 59  ? 0.1617 0.1399 0.1163 0.0023  -0.0107 0.0321  59  ILE A CA  
477  C  C   . ILE A 59  ? 0.1729 0.1450 0.1041 -0.0128 -0.0106 0.0124  59  ILE A C   
478  O  O   . ILE A 59  ? 0.1718 0.1648 0.1093 0.0021  -0.0055 0.0144  59  ILE A O   
479  C  CB  . ILE A 59  ? 0.1874 0.1406 0.1025 -0.0081 -0.0189 0.0236  59  ILE A CB  
480  C  CG1 . ILE A 59  ? 0.1560 0.1532 0.1280 0.0011  -0.0013 0.0335  59  ILE A CG1 
481  C  CG2 . ILE A 59  ? 0.1696 0.1729 0.1005 0.0107  -0.0089 0.0159  59  ILE A CG2 
482  C  CD1 . ILE A 59  ? 0.2031 0.1544 0.1500 -0.0034 0.0046  -0.0010 59  ILE A CD1 
483  N  N   . LEU A 60  ? 0.1425 0.1641 0.1244 0.0135  -0.0065 0.0083  60  LEU A N   
484  C  CA  . LEU A 60  ? 0.1402 0.1784 0.1694 -0.0039 0.0042  0.0430  60  LEU A CA  
485  C  C   . LEU A 60  ? 0.1284 0.1752 0.0880 -0.0006 -0.0114 0.0079  60  LEU A C   
486  O  O   . LEU A 60  ? 0.1641 0.2286 0.1116 0.0314  0.0084  0.0351  60  LEU A O   
487  C  CB  . LEU A 60  ? 0.1917 0.2330 0.2511 -0.0548 0.0294  0.0170  60  LEU A CB  
488  C  CG  . LEU A 60  ? 0.3705 0.1567 0.2827 -0.0790 0.0394  -0.0233 60  LEU A CG  
489  C  CD1 . LEU A 60  ? 0.3106 0.5238 0.3146 -0.0385 -0.1142 -0.0328 60  LEU A CD1 
490  C  CD2 . LEU A 60  ? 0.3705 0.5092 0.5041 0.0613  0.0628  -0.0263 60  LEU A CD2 
491  N  N   . ASN A 61  ? 0.1430 0.1520 0.1133 -0.0021 0.0051  -0.0015 61  ASN A N   
492  C  CA  . ASN A 61  ? 0.1141 0.1723 0.1350 -0.0107 -0.0107 0.0039  61  ASN A CA  
493  C  C   . ASN A 61  ? 0.1289 0.2063 0.1118 -0.0142 0.0261  -0.0170 61  ASN A C   
494  O  O   . ASN A 61  ? 0.1336 0.2108 0.1199 -0.0201 0.0173  -0.0025 61  ASN A O   
495  C  CB  . ASN A 61  ? 0.1381 0.1885 0.1476 0.0034  -0.0035 -0.0153 61  ASN A CB  
496  C  CG  . ASN A 61  ? 0.1389 0.1833 0.1213 -0.0063 -0.0024 0.0005  61  ASN A CG  
497  O  OD1 . ASN A 61  ? 0.1474 0.2253 0.1393 0.0089  -0.0118 -0.0400 61  ASN A OD1 
498  N  ND2 . ASN A 61  ? 0.1666 0.1794 0.1416 -0.0042 0.0033  -0.0174 61  ASN A ND2 
499  N  N   . ASN A 62  ? 0.1274 0.2009 0.1143 -0.0266 -0.0005 -0.0023 62  ASN A N   
500  C  CA  . ASN A 62  ? 0.1415 0.1959 0.1439 -0.0412 0.0118  -0.0078 62  ASN A CA  
501  C  C   . ASN A 62  ? 0.1356 0.2289 0.1540 -0.0348 -0.0020 -0.0027 62  ASN A C   
502  O  O   . ASN A 62  ? 0.1443 0.2790 0.2232 -0.0274 -0.0301 -0.0385 62  ASN A O   
503  C  CB  . ASN A 62  ? 0.1977 0.1878 0.1416 -0.0372 -0.0042 -0.0064 62  ASN A CB  
504  C  CG  . ASN A 62  ? 0.1849 0.2064 0.1113 -0.0194 -0.0195 -0.0166 62  ASN A CG  
505  O  OD1 . ASN A 62  ? 0.1781 0.1998 0.1388 -0.0128 -0.0013 0.0078  62  ASN A OD1 
506  N  ND2 . ASN A 62  ? 0.3041 0.2329 0.2125 0.0136  0.0370  -0.0573 62  ASN A ND2 
507  N  N   . GLY A 63  ? 0.1340 0.2411 0.1448 -0.0089 0.0001  -0.0158 63  GLY A N   
508  C  CA  . GLY A 63  ? 0.1427 0.2987 0.1528 0.0332  -0.0033 -0.0010 63  GLY A CA  
509  C  C   . GLY A 63  ? 0.1614 0.2661 0.1226 0.0127  -0.0125 -0.0147 63  GLY A C   
510  O  O   . GLY A 63  ? 0.1557 0.3078 0.1973 0.0461  -0.0003 -0.0055 63  GLY A O   
511  N  N   . HIS A 64  ? 0.1398 0.2330 0.1187 -0.0154 -0.0093 -0.0076 64  HIS A N   
512  C  CA  . HIS A 64  ? 0.1648 0.2340 0.1156 -0.0221 -0.0009 -0.0042 64  HIS A CA  
513  C  C   . HIS A 64  ? 0.1340 0.1919 0.1487 0.0108  -0.0044 0.0008  64  HIS A C   
514  O  O   . HIS A 64  ? 0.1517 0.2265 0.2370 0.0032  -0.0321 0.0480  64  HIS A O   
515  C  CB  . HIS A 64  ? 0.1798 0.2950 0.1136 -0.0234 0.0019  -0.0376 64  HIS A CB  
516  C  CG  . HIS A 64  ? 0.2100 0.2892 0.1102 -0.0434 -0.0100 -0.0185 64  HIS A CG  
517  N  ND1 . HIS A 64  ? 0.1963 0.3263 0.1708 -0.0318 -0.0216 -0.0156 64  HIS A ND1 
518  C  CD2 . HIS A 64  ? 0.2344 0.2842 0.1506 -0.0538 -0.0135 0.0049  64  HIS A CD2 
519  C  CE1 . HIS A 64  ? 0.2108 0.3843 0.2409 -0.0763 0.0116  0.0153  64  HIS A CE1 
520  N  NE2 . HIS A 64  ? 0.2279 0.3848 0.2208 -0.0847 0.0036  -0.0288 64  HIS A NE2 
521  N  N   . SER A 65  ? 0.1239 0.1849 0.1661 -0.0006 0.0003  0.0004  65  SER A N   
522  C  CA  . SER A 65  ? 0.1307 0.1842 0.1451 -0.0130 -0.0105 0.0133  65  SER A CA  
523  C  C   . SER A 65  ? 0.1317 0.1781 0.1122 -0.0051 0.0070  0.0015  65  SER A C   
524  O  O   . SER A 65  ? 0.1293 0.1902 0.1332 0.0066  0.0105  0.0179  65  SER A O   
525  C  CB  . SER A 65  ? 0.1617 0.2136 0.1493 -0.0259 -0.0039 0.0205  65  SER A CB  
526  O  OG  . SER A 65  ? 0.1773 0.3004 0.1910 -0.0345 -0.0179 0.0814  65  SER A OG  
527  N  N   . PHE A 66  ? 0.1221 0.1528 0.1338 0.0196  -0.0177 -0.0003 66  PHE A N   
528  C  CA  . PHE A 66  ? 0.1439 0.1964 0.1012 0.0414  -0.0114 0.0013  66  PHE A CA  
529  C  C   . PHE A 66  ? 0.1263 0.1429 0.1025 0.0177  -0.0085 0.0019  66  PHE A C   
530  O  O   . PHE A 66  ? 0.1536 0.1691 0.0998 0.0164  0.0033  0.0036  66  PHE A O   
531  C  CB  . PHE A 66  ? 0.1669 0.1949 0.0986 0.0353  -0.0055 -0.0134 66  PHE A CB  
532  C  CG  . PHE A 66  ? 0.1590 0.1838 0.0937 0.0164  -0.0095 -0.0273 66  PHE A CG  
533  C  CD1 . PHE A 66  ? 0.1430 0.1775 0.1377 0.0168  -0.0381 -0.0140 66  PHE A CD1 
534  C  CD2 . PHE A 66  ? 0.1700 0.1752 0.1799 0.0317  -0.0355 -0.0156 66  PHE A CD2 
535  C  CE1 . PHE A 66  ? 0.1532 0.1761 0.1673 0.0115  -0.0438 -0.0146 66  PHE A CE1 
536  C  CE2 . PHE A 66  ? 0.1820 0.1793 0.1520 0.0087  -0.0332 -0.0307 66  PHE A CE2 
537  C  CZ  . PHE A 66  ? 0.1779 0.1666 0.1700 0.0172  -0.0536 -0.0313 66  PHE A CZ  
538  N  N   . LYS A 67  ? 0.1398 0.1597 0.1311 0.0227  -0.0032 0.0168  67  LYS A N   
539  C  CA  . LYS A 67  ? 0.1540 0.1611 0.1253 0.0340  -0.0304 0.0004  67  LYS A CA  
540  C  C   . LYS A 67  ? 0.1446 0.1383 0.1057 0.0188  0.0000  0.0140  67  LYS A C   
541  O  O   . LYS A 67  ? 0.1471 0.2007 0.0962 0.0454  0.0109  0.0195  67  LYS A O   
542  C  CB  . LYS A 67  ? 0.2248 0.2337 0.2077 0.0289  -0.0930 -0.0310 67  LYS A CB  
543  C  CG  . LYS A 67  ? 0.2580 0.2248 0.2590 -0.0234 -0.0401 -0.0414 67  LYS A CG  
544  C  CD  . LYS A 67  ? 0.3120 0.2229 0.2411 -0.0699 -0.0022 -0.0071 67  LYS A CD  
545  C  CE  . LYS A 67  ? 0.2998 0.2507 0.4104 -0.0021 0.0457  -0.0839 67  LYS A CE  
546  N  NZ  . LYS A 67  ? 0.3673 0.2930 0.3145 -0.0721 -0.0594 -0.0848 67  LYS A NZ  
547  N  N   . VAL A 68  ? 0.1235 0.1318 0.1041 0.0049  -0.0074 0.0242  68  VAL A N   
548  C  CA  . VAL A 68  ? 0.1284 0.1068 0.1269 0.0149  -0.0041 0.0138  68  VAL A CA  
549  C  C   . VAL A 68  ? 0.1138 0.1265 0.0962 0.0197  0.0141  0.0175  68  VAL A C   
550  O  O   . VAL A 68  ? 0.1571 0.1129 0.1067 0.0035  0.0002  0.0119  68  VAL A O   
551  C  CB  . VAL A 68  ? 0.1322 0.1289 0.1246 0.0006  -0.0053 0.0046  68  VAL A CB  
552  C  CG1 . VAL A 68  ? 0.1480 0.1417 0.1493 0.0138  -0.0152 -0.0020 68  VAL A CG1 
553  C  CG2 . VAL A 68  ? 0.1719 0.1421 0.1170 -0.0039 -0.0195 -0.0008 68  VAL A CG2 
554  N  N   . GLU A 69  ? 0.1241 0.1301 0.1273 0.0020  -0.0064 0.0270  69  GLU A N   
555  C  CA  . GLU A 69  ? 0.1240 0.1239 0.1397 0.0000  -0.0011 0.0243  69  GLU A CA  
556  C  C   . GLU A 69  ? 0.1333 0.1034 0.1427 0.0015  -0.0187 0.0216  69  GLU A C   
557  O  O   . GLU A 69  ? 0.1709 0.1608 0.1425 0.0354  -0.0412 0.0141  69  GLU A O   
558  C  CB  . GLU A 69  ? 0.1542 0.1518 0.2622 -0.0092 0.0499  0.0299  69  GLU A CB  
559  C  CG  . GLU A 69  ? 0.1424 0.3142 0.4017 0.0051  0.0475  0.0490  69  GLU A CG  
560  C  CD  . GLU A 69  ? 0.2873 0.3777 0.2404 -0.0683 0.0884  0.0579  69  GLU A CD  
561  O  OE1 . GLU A 69  ? 0.2676 0.4132 0.2743 -0.0017 0.0979  0.0989  69  GLU A OE1 
562  O  OE2 . GLU A 69  ? 0.4345 0.4602 0.3717 -0.0402 -0.1274 0.0397  69  GLU A OE2 
563  N  N   . PHE A 70  ? 0.1240 0.1183 0.1594 0.0032  -0.0146 0.0136  70  PHE A N   
564  C  CA  . PHE A 70  ? 0.1280 0.1170 0.1322 0.0080  -0.0209 0.0244  70  PHE A CA  
565  C  C   . PHE A 70  ? 0.1412 0.1312 0.1224 -0.0059 -0.0248 0.0064  70  PHE A C   
566  O  O   . PHE A 70  ? 0.1564 0.1274 0.1761 -0.0054 -0.0379 0.0143  70  PHE A O   
567  C  CB  . PHE A 70  ? 0.1514 0.1329 0.1341 -0.0050 -0.0088 0.0137  70  PHE A CB  
568  C  CG  . PHE A 70  ? 0.1385 0.1246 0.1045 0.0106  -0.0159 0.0136  70  PHE A CG  
569  C  CD1 . PHE A 70  ? 0.1741 0.1297 0.1328 0.0223  0.0044  0.0422  70  PHE A CD1 
570  C  CD2 . PHE A 70  ? 0.1533 0.1410 0.1285 -0.0116 -0.0156 0.0215  70  PHE A CD2 
571  C  CE1 . PHE A 70  ? 0.1733 0.1394 0.1798 0.0137  0.0228  0.0438  70  PHE A CE1 
572  C  CE2 . PHE A 70  ? 0.1770 0.1298 0.1219 -0.0129 -0.0055 0.0248  70  PHE A CE2 
573  C  CZ  . PHE A 70  ? 0.1738 0.1411 0.1556 -0.0036 0.0250  0.0330  70  PHE A CZ  
574  N  N   . ASP A 71  ? 0.1454 0.1088 0.1518 0.0015  -0.0205 0.0227  71  ASP A N   
575  C  CA  . ASP A 71  ? 0.1448 0.1213 0.1790 -0.0048 -0.0365 0.0269  71  ASP A CA  
576  C  C   . ASP A 71  ? 0.1702 0.1058 0.1888 -0.0277 -0.0159 0.0279  71  ASP A C   
577  O  O   . ASP A 71  ? 0.1831 0.1540 0.1841 -0.0311 0.0000  0.0013  71  ASP A O   
578  C  CB  . ASP A 71  ? 0.1727 0.1492 0.1773 0.0128  -0.0493 0.0236  71  ASP A CB  
579  C  CG  . ASP A 71  ? 0.2499 0.1544 0.2608 0.0387  -0.1243 0.0330  71  ASP A CG  
580  O  OD1 . ASP A 71  ? 0.2242 0.1596 0.2190 0.0193  -0.0556 0.0284  71  ASP A OD1 
581  O  OD2 . ASP A 71  ? 0.2629 0.1777 0.3231 0.0460  -0.1114 -0.0077 71  ASP A OD2 
582  N  N   . ASP A 72  ? 0.1905 0.1091 0.1804 -0.0139 -0.0324 0.0143  72  ASP A N   
583  C  CA  . ASP A 72  ? 0.2023 0.1014 0.1787 -0.0051 -0.0291 0.0139  72  ASP A CA  
584  C  C   . ASP A 72  ? 0.2488 0.1081 0.2102 -0.0104 -0.0587 0.0199  72  ASP A C   
585  O  O   . ASP A 72  ? 0.2835 0.1272 0.2091 0.0088  -0.0570 0.0128  72  ASP A O   
586  C  CB  . ASP A 72  ? 0.2197 0.0986 0.2007 0.0039  -0.0457 0.0109  72  ASP A CB  
587  C  CG  . ASP A 72  ? 0.2653 0.1526 0.1641 -0.0354 -0.0735 0.0131  72  ASP A CG  
588  O  OD1 . ASP A 72  ? 0.2251 0.2107 0.1876 -0.0257 -0.0446 0.0565  72  ASP A OD1 
589  O  OD2 . ASP A 72  ? 0.2988 0.2178 0.1808 -0.0210 -0.1000 0.0435  72  ASP A OD2 
590  N  N   . SER A 73  ? 0.2167 0.1068 0.2110 0.0162  -0.0438 0.0183  73  SER A N   
591  C  CA  . SER A 73  ? 0.2970 0.1064 0.2445 -0.0347 -0.0651 0.0397  73  SER A CA  
592  C  C   . SER A 73  ? 0.3175 0.1084 0.2623 -0.0194 -0.0884 -0.0102 73  SER A C   
593  O  O   . SER A 73  ? 0.3856 0.1041 0.2734 0.0037  -0.1109 -0.0040 73  SER A O   
594  C  CB  . SER A 73  ? 0.3215 0.1263 0.2402 -0.0354 -0.0468 0.0286  73  SER A CB  
595  O  OG  . SER A 73  ? 0.3310 0.1226 0.2683 0.0234  -0.0535 0.0177  73  SER A OG  
596  N  N   . GLN A 74  ? 0.2864 0.1547 0.2946 0.0023  -0.0100 -0.0323 74  GLN A N   
597  C  CA  . GLN A 74  ? 0.3529 0.2623 0.2398 0.0612  -0.0190 -0.0665 74  GLN A CA  
598  C  C   . GLN A 74  ? 0.2548 0.2257 0.3085 -0.0057 -0.0699 -0.1016 74  GLN A C   
599  O  O   . GLN A 74  ? 0.2358 0.1896 0.2817 -0.0234 -0.0607 -0.0286 74  GLN A O   
600  C  CB  . GLN A 74  ? 0.4202 0.4027 0.3454 0.0945  -0.1025 -0.0651 74  GLN A CB  
601  C  CG  . GLN A 74  ? 0.2879 0.3983 0.4116 0.0516  -0.1240 -0.0657 74  GLN A CG  
602  C  CD  . GLN A 74  ? 0.5243 0.3804 0.4551 0.0877  -0.1709 0.0355  74  GLN A CD  
603  O  OE1 . GLN A 74  ? 0.4657 0.6035 0.4769 0.0960  -0.0880 0.0211  74  GLN A OE1 
604  N  NE2 . GLN A 74  ? 0.4897 0.3386 0.4111 0.0885  -0.1082 0.0243  74  GLN A NE2 
605  N  N   . ASP A 75  ? 0.3262 0.2872 0.3195 -0.0496 -0.0582 -0.1547 75  ASP A N   
606  C  CA  . ASP A 75  ? 0.2872 0.3907 0.4043 -0.1106 -0.0672 -0.0917 75  ASP A CA  
607  C  C   . ASP A 75  ? 0.2251 0.3442 0.3922 0.0008  -0.1476 -0.0792 75  ASP A C   
608  O  O   . ASP A 75  ? 0.3383 0.2377 0.6117 0.0687  -0.2284 -0.0473 75  ASP A O   
609  C  CB  . ASP A 75  ? 0.4046 0.4682 0.5832 0.0334  -0.0983 -0.2625 75  ASP A CB  
610  C  CG  . ASP A 75  ? 0.3171 0.4696 0.4919 0.0259  -0.0604 -0.1005 75  ASP A CG  
611  O  OD1 . ASP A 75  ? 0.3360 0.6358 0.3112 0.1189  -0.0712 -0.1979 75  ASP A OD1 
612  O  OD2 . ASP A 75  ? 0.4226 0.4677 0.5364 0.0653  0.0602  -0.0677 75  ASP A OD2 
613  N  N   . LYS A 76  ? 0.2143 0.2603 0.3061 0.0100  -0.0675 0.0714  76  LYS A N   
614  C  CA  . LYS A 76  ? 0.2526 0.1572 0.4650 -0.0306 -0.0422 -0.0027 76  LYS A CA  
615  C  C   . LYS A 76  ? 0.2247 0.2075 0.3358 0.0356  -0.0605 0.0137  76  LYS A C   
616  O  O   . LYS A 76  ? 0.2564 0.4610 0.3355 -0.0747 -0.0872 -0.0237 76  LYS A O   
617  C  CB  . LYS A 76  ? 0.3309 0.2341 0.3466 0.0234  -0.1402 -0.0392 76  LYS A CB  
618  C  CG  . LYS A 76  ? 0.4279 0.2007 0.4051 0.0150  -0.0195 0.0068  76  LYS A CG  
619  C  CD  . LYS A 76  ? 0.3266 0.2523 0.3397 -0.0434 -0.0428 0.0037  76  LYS A CD  
620  C  CE  . LYS A 76  ? 0.3819 0.2240 0.4536 0.0789  0.0413  0.0472  76  LYS A CE  
621  N  NZ  . LYS A 76  ? 0.5621 0.2529 0.3765 0.0980  -0.0908 -0.0339 76  LYS A NZ  
622  N  N   . ALA A 77  ? 0.1863 0.2669 0.2991 0.0130  -0.0743 0.0675  77  ALA A N   
623  C  CA  . ALA A 77  ? 0.1848 0.1775 0.2287 0.0190  -0.0421 0.0076  77  ALA A CA  
624  C  C   . ALA A 77  ? 0.1546 0.1607 0.2683 0.0287  -0.0507 -0.0188 77  ALA A C   
625  O  O   . ALA A 77  ? 0.1377 0.2564 0.3536 0.0212  -0.0433 -0.0818 77  ALA A O   
626  C  CB  . ALA A 77  ? 0.1905 0.2139 0.2345 0.0324  -0.0062 0.0167  77  ALA A CB  
627  N  N   . VAL A 78  ? 0.1720 0.1736 0.2283 0.0120  -0.0413 -0.0059 78  VAL A N   
628  C  CA  . VAL A 78  ? 0.2269 0.1777 0.2402 0.0029  -0.0724 0.0140  78  VAL A CA  
629  C  C   . VAL A 78  ? 0.1748 0.1629 0.2625 -0.0135 -0.0727 -0.0053 78  VAL A C   
630  O  O   . VAL A 78  ? 0.1694 0.1913 0.3252 -0.0315 -0.0873 0.0212  78  VAL A O   
631  C  CB  . VAL A 78  ? 0.2570 0.2455 0.2579 0.0262  -0.0574 -0.0365 78  VAL A CB  
632  C  CG1 . VAL A 78  ? 0.3755 0.1659 0.3299 0.0593  -0.0712 -0.0032 78  VAL A CG1 
633  C  CG2 . VAL A 78  ? 0.2602 0.2461 0.3301 0.0271  0.0041  -0.0469 78  VAL A CG2 
634  N  N   . LEU A 79  ? 0.1432 0.1533 0.2201 0.0044  -0.0391 -0.0194 79  LEU A N   
635  C  CA  . LEU A 79  ? 0.1630 0.1709 0.2052 0.0156  -0.0091 -0.0173 79  LEU A CA  
636  C  C   . LEU A 79  ? 0.1831 0.2078 0.2383 0.0006  -0.0189 -0.0397 79  LEU A C   
637  O  O   . LEU A 79  ? 0.2217 0.2222 0.2310 -0.0539 -0.0031 -0.0528 79  LEU A O   
638  C  CB  . LEU A 79  ? 0.1316 0.2147 0.2997 -0.0085 -0.0370 0.0446  79  LEU A CB  
639  C  CG  . LEU A 79  ? 0.1768 0.1966 0.2838 0.0176  -0.0204 0.0151  79  LEU A CG  
640  C  CD1 . LEU A 79  ? 0.1630 0.1993 0.4817 0.0157  0.0315  0.0388  79  LEU A CD1 
641  C  CD2 . LEU A 79  ? 0.1831 0.2011 0.2774 0.0292  0.0313  0.0073  79  LEU A CD2 
642  N  N   . LYS A 80  ? 0.2057 0.2129 0.1989 -0.0002 -0.0024 -0.0479 80  LYS A N   
643  C  CA  . LYS A 80  ? 0.2529 0.2267 0.2153 0.0184  -0.0012 -0.0532 80  LYS A CA  
644  C  C   . LYS A 80  ? 0.1655 0.2260 0.2577 0.0006  0.0285  -0.0548 80  LYS A C   
645  O  O   . LYS A 80  ? 0.1916 0.2248 0.2574 -0.0277 -0.0187 -0.0282 80  LYS A O   
646  C  CB  . LYS A 80  ? 0.2942 0.2321 0.3218 0.0428  0.0065  0.0336  80  LYS A CB  
647  C  CG  . LYS A 80  ? 0.3306 0.2833 0.3164 0.0269  -0.0401 -0.0888 80  LYS A CG  
648  C  CD  . LYS A 80  ? 0.3129 0.3098 0.6699 0.0776  -0.0170 -0.0663 80  LYS A CD  
649  N  N   . GLY A 81  ? 0.2152 0.2291 0.2501 0.0131  0.0536  -0.0388 81  GLY A N   
650  C  CA  . GLY A 81  ? 0.2183 0.2394 0.2694 0.0330  0.0290  -0.0105 81  GLY A CA  
651  C  C   . GLY A 81  ? 0.1962 0.2264 0.2677 0.0336  0.0616  -0.0174 81  GLY A C   
652  O  O   . GLY A 81  ? 0.1797 0.2676 0.2362 -0.0125 0.0350  -0.0482 81  GLY A O   
653  N  N   . GLY A 82  ? 0.1919 0.2530 0.4307 0.0230  0.0609  0.0332  82  GLY A N   
654  C  CA  . GLY A 82  ? 0.2314 0.2028 0.4690 0.0290  0.0854  0.0158  82  GLY A CA  
655  C  C   . GLY A 82  ? 0.2267 0.2167 0.4017 0.0831  0.1005  0.0325  82  GLY A C   
656  O  O   . GLY A 82  ? 0.2712 0.4025 0.3471 0.1428  0.1037  0.0560  82  GLY A O   
657  N  N   . PRO A 83  ? 0.1970 0.2125 0.3243 0.0321  0.0673  -0.0044 83  PRO A N   
658  C  CA  . PRO A 83  ? 0.2637 0.2025 0.2513 0.0805  0.0381  -0.0020 83  PRO A CA  
659  C  C   . PRO A 83  ? 0.2182 0.2187 0.2647 0.0431  0.0032  -0.0192 83  PRO A C   
660  O  O   . PRO A 83  ? 0.2717 0.3162 0.3019 0.0429  -0.0708 -0.0073 83  PRO A O   
661  C  CB  . PRO A 83  ? 0.2310 0.2717 0.2373 0.0734  0.0514  0.0223  83  PRO A CB  
662  C  CG  . PRO A 83  ? 0.2034 0.2294 0.2651 0.0313  0.0120  0.0036  83  PRO A CG  
663  C  CD  . PRO A 83  ? 0.1772 0.1786 0.3437 0.0444  0.0644  -0.0034 83  PRO A CD  
664  N  N   . LEU A 84  ? 0.2035 0.1835 0.2197 0.0398  0.0359  -0.0336 84  LEU A N   
665  C  CA  . LEU A 84  ? 0.1859 0.1651 0.2207 0.0262  0.0042  -0.0524 84  LEU A CA  
666  C  C   . LEU A 84  ? 0.2021 0.2183 0.1975 0.0372  0.0219  -0.0749 84  LEU A C   
667  O  O   . LEU A 84  ? 0.2156 0.2193 0.2901 0.0228  0.0493  -0.0706 84  LEU A O   
668  C  CB  . LEU A 84  ? 0.1992 0.1617 0.2174 0.0267  0.0143  -0.0592 84  LEU A CB  
669  C  CG  . LEU A 84  ? 0.1511 0.1701 0.2187 0.0223  0.0230  -0.0591 84  LEU A CG  
670  C  CD1 . LEU A 84  ? 0.1632 0.2214 0.2170 0.0278  0.0031  -0.0379 84  LEU A CD1 
671  C  CD2 . LEU A 84  ? 0.1499 0.1486 0.2365 -0.0023 0.0250  -0.0254 84  LEU A CD2 
672  N  N   . ASP A 85  ? 0.2909 0.1817 0.2860 0.0031  0.0466  -0.0761 85  ASP A N   
673  C  CA  . ASP A 85  ? 0.3387 0.1855 0.3482 0.0228  0.0094  -0.1054 85  ASP A CA  
674  C  C   . ASP A 85  ? 0.2859 0.1432 0.5250 0.0230  0.0785  -0.0273 85  ASP A C   
675  O  O   . ASP A 85  ? 0.3352 0.3302 0.4492 0.0965  0.0633  -0.0688 85  ASP A O   
676  C  CB  . ASP A 85  ? 0.4995 0.1993 0.3552 0.0652  -0.0359 -0.1076 85  ASP A CB  
677  C  CG  . ASP A 85  ? 0.4355 0.3591 0.3838 0.1459  -0.0602 -0.0636 85  ASP A CG  
678  O  OD1 . ASP A 85  ? 0.5793 0.7965 0.4488 -0.0136 0.0335  0.0552  85  ASP A OD1 
679  O  OD2 . ASP A 85  ? 0.3560 0.5615 0.4155 -0.0237 -0.0108 0.0161  85  ASP A OD2 
680  N  N   . GLY A 86  ? 0.2889 0.2805 0.5924 0.0139  0.0199  0.0082  86  GLY A N   
681  C  CA  . GLY A 86  ? 0.4254 0.2863 0.4448 -0.1216 -0.0144 -0.1029 86  GLY A CA  
682  C  C   . GLY A 86  ? 0.3054 0.2329 0.3352 -0.0516 -0.1011 -0.0002 86  GLY A C   
683  O  O   . GLY A 86  ? 0.3817 0.3054 0.4850 -0.1662 -0.0524 0.0273  86  GLY A O   
684  N  N   . THR A 87  ? 0.2505 0.1736 0.3050 0.0320  0.0027  -0.0403 87  THR A N   
685  C  CA  . THR A 87  ? 0.1982 0.2304 0.3264 0.0328  0.0091  -0.0863 87  THR A CA  
686  C  C   . THR A 87  ? 0.1464 0.1363 0.3671 0.0274  0.0052  -0.0515 87  THR A C   
687  O  O   . THR A 87  ? 0.1738 0.1430 0.3418 0.0188  -0.0081 -0.0682 87  THR A O   
688  C  CB  . THR A 87  ? 0.1966 0.4680 0.3719 0.1491  -0.0474 -0.0491 87  THR A CB  
689  O  OG1 . THR A 87  ? 0.2859 0.4355 0.4967 0.1461  -0.0333 -0.1426 87  THR A OG1 
690  C  CG2 . THR A 87  ? 0.2170 0.3371 0.4250 0.0453  -0.0458 -0.0682 87  THR A CG2 
691  N  N   . TYR A 88  ? 0.1333 0.1342 0.3433 0.0163  -0.0122 -0.0559 88  TYR A N   
692  C  CA  . TYR A 88  ? 0.1397 0.1345 0.2533 0.0122  -0.0186 -0.0240 88  TYR A CA  
693  C  C   . TYR A 88  ? 0.1430 0.1389 0.2771 0.0314  -0.0576 -0.0427 88  TYR A C   
694  O  O   . TYR A 88  ? 0.1709 0.2020 0.2997 -0.0291 -0.0826 0.0069  88  TYR A O   
695  C  CB  . TYR A 88  ? 0.1824 0.1364 0.2440 0.0469  -0.0326 -0.0562 88  TYR A CB  
696  C  CG  . TYR A 88  ? 0.1576 0.1058 0.2275 0.0044  -0.0039 -0.0447 88  TYR A CG  
697  C  CD1 . TYR A 88  ? 0.1759 0.1424 0.2246 0.0092  -0.0124 -0.0462 88  TYR A CD1 
698  C  CD2 . TYR A 88  ? 0.1567 0.1045 0.1747 0.0143  0.0044  -0.0108 88  TYR A CD2 
699  C  CE1 . TYR A 88  ? 0.1542 0.1341 0.2257 0.0217  0.0076  -0.0379 88  TYR A CE1 
700  C  CE2 . TYR A 88  ? 0.1738 0.1082 0.1654 0.0000  0.0009  -0.0204 88  TYR A CE2 
701  C  CZ  . TYR A 88  ? 0.1599 0.1226 0.1873 -0.0052 0.0091  -0.0583 88  TYR A CZ  
702  O  OH  . TYR A 88  ? 0.1812 0.1657 0.1720 -0.0076 0.0102  -0.0465 88  TYR A OH  
703  N  N   . ARG A 89  ? 0.1543 0.1425 0.2502 0.0335  -0.0337 -0.0883 89  ARG A N   
704  C  CA  . ARG A 89  ? 0.1655 0.1147 0.2584 0.0418  -0.0670 -0.0388 89  ARG A CA  
705  C  C   . ARG A 89  ? 0.1271 0.0865 0.1777 0.0072  -0.0365 0.0034  89  ARG A C   
706  O  O   . ARG A 89  ? 0.1289 0.1029 0.1583 0.0104  -0.0284 -0.0008 89  ARG A O   
707  C  CB  . ARG A 89  ? 0.2337 0.0822 0.3699 0.0370  -0.1251 -0.0025 89  ARG A CB  
708  C  CG  . ARG A 89  ? 0.4097 0.2091 0.2000 0.0485  -0.0954 0.0230  89  ARG A CG  
709  C  CD  . ARG A 89  ? 0.2929 0.2336 0.4567 0.1297  -0.0022 0.0831  89  ARG A CD  
710  N  NE  . ARG A 89  ? 0.5661 0.2064 0.2613 0.0234  -0.1577 0.0468  89  ARG A NE  
711  C  CZ  . ARG A 89  ? 0.3155 0.1890 0.1605 0.0600  -0.0950 -0.0245 89  ARG A CZ  
712  N  NH1 . ARG A 89  ? 0.4468 0.2982 0.2445 0.1312  -0.1023 0.0460  89  ARG A NH1 
713  N  NH2 . ARG A 89  ? 0.3690 0.3386 0.2239 -0.0054 0.0435  0.0099  89  ARG A NH2 
714  N  N   . LEU A 90  ? 0.1420 0.0977 0.1824 0.0071  -0.0345 -0.0039 90  LEU A N   
715  C  CA  . LEU A 90  ? 0.1474 0.0912 0.1507 0.0018  -0.0249 0.0133  90  LEU A CA  
716  C  C   . LEU A 90  ? 0.1460 0.1122 0.1319 -0.0043 -0.0302 0.0247  90  LEU A C   
717  O  O   . LEU A 90  ? 0.1665 0.1402 0.1966 -0.0023 -0.0442 0.0526  90  LEU A O   
718  C  CB  . LEU A 90  ? 0.1322 0.1216 0.1449 0.0015  -0.0293 -0.0054 90  LEU A CB  
719  C  CG  . LEU A 90  ? 0.1562 0.1170 0.1435 0.0026  -0.0414 -0.0095 90  LEU A CG  
720  C  CD1 . LEU A 90  ? 0.1610 0.1170 0.1592 0.0097  -0.0370 -0.0194 90  LEU A CD1 
721  C  CD2 . LEU A 90  ? 0.1833 0.1574 0.1632 -0.0436 -0.0292 -0.0055 90  LEU A CD2 
722  N  N   . THR A 91  ? 0.1429 0.0982 0.1375 0.0100  -0.0230 0.0017  91  THR A N   
723  C  CA  . THR A 91  ? 0.1587 0.0989 0.1546 0.0044  -0.0326 0.0142  91  THR A CA  
724  C  C   . THR A 91  ? 0.1277 0.1031 0.1234 -0.0087 -0.0243 0.0221  91  THR A C   
725  O  O   . THR A 91  ? 0.1453 0.1125 0.1241 0.0009  -0.0232 0.0164  91  THR A O   
726  C  CB  . THR A 91  ? 0.1786 0.1383 0.1726 -0.0238 -0.0395 0.0133  91  THR A CB  
727  O  OG1 . THR A 91  ? 0.2371 0.2565 0.1923 -0.1050 -0.0604 0.0639  91  THR A OG1 
728  C  CG2 . THR A 91  ? 0.1932 0.1129 0.1928 -0.0137 -0.0525 0.0017  91  THR A CG2 
729  N  N   . GLN A 92  ? 0.1320 0.0860 0.1510 0.0044  -0.0217 0.0073  92  GLN A N   
730  C  CA  . GLN A 92  ? 0.1260 0.0988 0.1070 -0.0024 -0.0119 0.0158  92  GLN A CA  
731  C  C   . GLN A 92  ? 0.1014 0.1066 0.1111 -0.0036 -0.0054 0.0183  92  GLN A C   
732  O  O   . GLN A 92  ? 0.1518 0.0930 0.1030 -0.0009 -0.0100 0.0060  92  GLN A O   
733  C  CB  . GLN A 92  ? 0.1285 0.1455 0.1228 0.0040  0.0023  0.0082  92  GLN A CB  
734  C  CG  . GLN A 92  ? 0.1562 0.1265 0.1601 -0.0055 -0.0326 0.0192  92  GLN A CG  
735  C  CD  . GLN A 92  ? 0.1452 0.1363 0.1824 -0.0106 -0.0037 0.0285  92  GLN A CD  
736  O  OE1 . GLN A 92  ? 0.1599 0.1271 0.1820 0.0027  -0.0247 0.0414  92  GLN A OE1 
737  N  NE2 . GLN A 92  ? 0.1420 0.2114 0.3088 -0.0209 -0.0127 0.0908  92  GLN A NE2 
738  N  N   . PHE A 93  ? 0.1128 0.0903 0.1273 0.0032  -0.0114 0.0108  93  PHE A N   
739  C  CA  . PHE A 93  ? 0.1127 0.0912 0.1217 0.0006  0.0003  0.0070  93  PHE A CA  
740  C  C   . PHE A 93  ? 0.1099 0.1031 0.0901 -0.0022 -0.0044 0.0162  93  PHE A C   
741  O  O   . PHE A 93  ? 0.1318 0.1028 0.0969 0.0057  -0.0020 0.0144  93  PHE A O   
742  C  CB  . PHE A 93  ? 0.1239 0.1165 0.0995 -0.0072 -0.0111 0.0087  93  PHE A CB  
743  C  CG  . PHE A 93  ? 0.1186 0.1027 0.1072 -0.0079 -0.0043 0.0109  93  PHE A CG  
744  C  CD1 . PHE A 93  ? 0.1307 0.1186 0.1109 -0.0033 -0.0120 -0.0070 93  PHE A CD1 
745  C  CD2 . PHE A 93  ? 0.1231 0.1208 0.1111 0.0033  -0.0125 0.0233  93  PHE A CD2 
746  C  CE1 . PHE A 93  ? 0.1340 0.1162 0.1324 0.0020  -0.0300 -0.0129 93  PHE A CE1 
747  C  CE2 . PHE A 93  ? 0.1424 0.1324 0.1074 -0.0091 -0.0119 0.0155  93  PHE A CE2 
748  C  CZ  . PHE A 93  ? 0.1297 0.1007 0.1641 -0.0038 -0.0184 0.0141  93  PHE A CZ  
749  N  N   . HIS A 94  ? 0.1118 0.0903 0.1098 0.0084  -0.0219 0.0071  94  HIS A N   
750  C  CA  . HIS A 94  ? 0.1156 0.1152 0.0915 -0.0002 -0.0089 0.0109  94  HIS A CA  
751  C  C   . HIS A 94  ? 0.1108 0.1013 0.0776 -0.0055 -0.0161 -0.0002 94  HIS A C   
752  O  O   . HIS A 94  ? 0.1338 0.0980 0.0925 0.0086  0.0046  0.0071  94  HIS A O   
753  C  CB  . HIS A 94  ? 0.1254 0.1280 0.0867 -0.0118 -0.0094 0.0018  94  HIS A CB  
754  C  CG  . HIS A 94  ? 0.1129 0.1120 0.1000 -0.0043 -0.0035 -0.0048 94  HIS A CG  
755  N  ND1 . HIS A 94  ? 0.1127 0.1177 0.1111 -0.0111 -0.0095 -0.0009 94  HIS A ND1 
756  C  CD2 . HIS A 94  ? 0.1005 0.1461 0.0767 -0.0058 -0.0030 -0.0042 94  HIS A CD2 
757  C  CE1 . HIS A 94  ? 0.1111 0.1014 0.1127 0.0006  -0.0190 0.0025  94  HIS A CE1 
758  N  NE2 . HIS A 94  ? 0.0967 0.1233 0.0872 0.0019  -0.0068 0.0108  94  HIS A NE2 
759  N  N   . PHE A 95  ? 0.1190 0.0962 0.1243 0.0070  -0.0146 -0.0066 95  PHE A N   
760  C  CA  . PHE A 95  ? 0.1115 0.0895 0.1408 0.0011  -0.0166 -0.0009 95  PHE A CA  
761  C  C   . PHE A 95  ? 0.1102 0.1095 0.1059 -0.0002 -0.0019 -0.0075 95  PHE A C   
762  O  O   . PHE A 95  ? 0.1256 0.1174 0.1284 0.0015  0.0029  0.0189  95  PHE A O   
763  C  CB  . PHE A 95  ? 0.1160 0.1153 0.1167 -0.0012 -0.0153 -0.0070 95  PHE A CB  
764  C  CG  . PHE A 95  ? 0.1272 0.1120 0.1168 0.0132  -0.0196 -0.0193 95  PHE A CG  
765  C  CD1 . PHE A 95  ? 0.1483 0.1125 0.1292 0.0064  -0.0332 -0.0117 95  PHE A CD1 
766  C  CD2 . PHE A 95  ? 0.1251 0.1264 0.1427 -0.0037 -0.0091 -0.0365 95  PHE A CD2 
767  C  CE1 . PHE A 95  ? 0.1594 0.1201 0.1684 0.0179  -0.0412 -0.0286 95  PHE A CE1 
768  C  CE2 . PHE A 95  ? 0.1331 0.1353 0.1651 0.0119  -0.0094 -0.0489 95  PHE A CE2 
769  C  CZ  . PHE A 95  ? 0.1376 0.1276 0.1842 0.0066  -0.0408 -0.0518 95  PHE A CZ  
770  N  N   . HIS A 96  ? 0.1265 0.0983 0.1007 0.0127  -0.0029 -0.0120 96  HIS A N   
771  C  CA  . HIS A 96  ? 0.1188 0.0987 0.1178 0.0167  -0.0135 -0.0168 96  HIS A CA  
772  C  C   . HIS A 96  ? 0.1302 0.1016 0.1072 0.0111  0.0037  -0.0109 96  HIS A C   
773  O  O   . HIS A 96  ? 0.1162 0.1029 0.1298 0.0074  -0.0036 -0.0127 96  HIS A O   
774  C  CB  . HIS A 96  ? 0.1304 0.1070 0.1077 0.0199  -0.0163 -0.0069 96  HIS A CB  
775  C  CG  . HIS A 96  ? 0.1167 0.1077 0.1053 0.0080  -0.0207 -0.0024 96  HIS A CG  
776  N  ND1 . HIS A 96  ? 0.1126 0.1040 0.1390 0.0021  -0.0050 -0.0129 96  HIS A ND1 
777  C  CD2 . HIS A 96  ? 0.1377 0.0829 0.1176 0.0027  -0.0138 -0.0008 96  HIS A CD2 
778  C  CE1 . HIS A 96  ? 0.1098 0.1073 0.1140 0.0227  -0.0120 0.0001  96  HIS A CE1 
779  N  NE2 . HIS A 96  ? 0.1097 0.0962 0.1214 0.0068  -0.0200 0.0002  96  HIS A NE2 
780  N  N   . TRP A 97  ? 0.1271 0.0989 0.1090 0.0133  -0.0044 -0.0176 97  TRP A N   
781  C  CA  . TRP A 97  ? 0.1259 0.1000 0.1374 0.0131  -0.0208 -0.0073 97  TRP A CA  
782  C  C   . TRP A 97  ? 0.1312 0.1098 0.0907 0.0192  -0.0093 -0.0254 97  TRP A C   
783  O  O   . TRP A 97  ? 0.1268 0.1116 0.1409 0.0214  -0.0016 -0.0120 97  TRP A O   
784  C  CB  . TRP A 97  ? 0.1454 0.1205 0.1086 0.0185  -0.0132 -0.0192 97  TRP A CB  
785  C  CG  . TRP A 97  ? 0.1258 0.1122 0.1135 0.0250  -0.0261 -0.0236 97  TRP A CG  
786  C  CD1 . TRP A 97  ? 0.1428 0.1398 0.1204 0.0304  -0.0081 -0.0138 97  TRP A CD1 
787  C  CD2 . TRP A 97  ? 0.1275 0.1303 0.0989 0.0114  -0.0067 -0.0245 97  TRP A CD2 
788  N  NE1 . TRP A 97  ? 0.1417 0.1363 0.1283 0.0247  -0.0154 -0.0228 97  TRP A NE1 
789  C  CE2 . TRP A 97  ? 0.1318 0.1371 0.1004 0.0259  -0.0094 -0.0122 97  TRP A CE2 
790  C  CE3 . TRP A 97  ? 0.1244 0.1132 0.1203 0.0132  -0.0163 -0.0064 97  TRP A CE3 
791  C  CZ2 . TRP A 97  ? 0.1380 0.1481 0.0985 0.0083  -0.0020 -0.0105 97  TRP A CZ2 
792  C  CZ3 . TRP A 97  ? 0.1395 0.1536 0.0993 0.0193  -0.0070 -0.0075 97  TRP A CZ3 
793  C  CH2 . TRP A 97  ? 0.1586 0.1395 0.0885 0.0001  -0.0099 -0.0017 97  TRP A CH2 
794  N  N   . GLY A 98  ? 0.1580 0.1018 0.1223 0.0258  -0.0239 -0.0195 98  GLY A N   
795  C  CA  . GLY A 98  ? 0.1448 0.1251 0.1251 0.0302  -0.0140 -0.0151 98  GLY A CA  
796  C  C   . GLY A 98  ? 0.1587 0.1273 0.1248 0.0262  -0.0184 -0.0034 98  GLY A C   
797  O  O   . GLY A 98  ? 0.2093 0.1349 0.1504 0.0431  -0.0388 -0.0399 98  GLY A O   
798  N  N   . SER A 99  ? 0.2002 0.1231 0.1498 0.0494  -0.0277 -0.0375 99  SER A N   
799  C  CA  . SER A 99  ? 0.2206 0.1697 0.1666 0.0488  -0.0098 -0.0623 99  SER A CA  
800  C  C   . SER A 99  ? 0.1914 0.1459 0.1601 0.0439  -0.0364 -0.0496 99  SER A C   
801  O  O   . SER A 99  ? 0.3914 0.1840 0.2129 0.0323  -0.0753 -0.0822 99  SER A O   
802  C  CB  . SER A 99  ? 0.2427 0.2107 0.1561 0.0743  0.0066  -0.0663 99  SER A CB  
803  O  OG  . SER A 99  ? 0.2161 0.1784 0.1910 0.0677  -0.0102 -0.0472 99  SER A OG  
804  N  N   . LEU A 100 ? 0.1987 0.1259 0.2463 0.0348  -0.0055 -0.0420 100 LEU A N   
805  C  CA  . LEU A 100 ? 0.1962 0.1321 0.3829 0.0077  0.0098  -0.0631 100 LEU A CA  
806  C  C   . LEU A 100 ? 0.1903 0.1220 0.2577 0.0287  -0.0196 -0.0262 100 LEU A C   
807  O  O   . LEU A 100 ? 0.2139 0.1100 0.2843 0.0163  0.0083  -0.0318 100 LEU A O   
808  C  CB  . LEU A 100 ? 0.3106 0.1974 0.5614 0.0719  0.0981  0.0423  100 LEU A CB  
809  C  CG  . LEU A 100 ? 0.3683 0.4017 0.5083 0.0965  0.1476  0.0753  100 LEU A CG  
810  C  CD1 . LEU A 100 ? 0.4725 0.3770 0.7156 0.2389  0.1119  0.0346  100 LEU A CD1 
811  C  CD2 . LEU A 100 ? 0.6217 0.2072 0.8490 0.0916  -0.0259 -0.2173 100 LEU A CD2 
812  N  N   . ASP A 101 ? 0.2075 0.1280 0.3280 0.0048  -0.0256 -0.0128 101 ASP A N   
813  C  CA  . ASP A 101 ? 0.1863 0.1405 0.2696 0.0161  -0.0408 0.0068  101 ASP A CA  
814  C  C   . ASP A 101 ? 0.2089 0.1075 0.2646 -0.0011 -0.0509 0.0060  101 ASP A C   
815  O  O   . ASP A 101 ? 0.2514 0.1320 0.3292 0.0356  -0.0438 0.0108  101 ASP A O   
816  C  CB  . ASP A 101 ? 0.2116 0.1367 0.2931 -0.0098 -0.0460 0.0279  101 ASP A CB  
817  C  CG  . ASP A 101 ? 0.2377 0.1508 0.3318 0.0011  -0.0700 0.0418  101 ASP A CG  
818  O  OD1 . ASP A 101 ? 0.2437 0.1966 0.3168 -0.0313 -0.0361 0.0182  101 ASP A OD1 
819  O  OD2 . ASP A 101 ? 0.2966 0.2211 0.3884 -0.0685 -0.0915 0.0507  101 ASP A OD2 
820  N  N   . GLY A 102 ? 0.2190 0.1274 0.2947 0.0170  -0.0460 0.0122  102 GLY A N   
821  C  CA  . GLY A 102 ? 0.2042 0.1364 0.3119 0.0002  -0.0487 0.0353  102 GLY A CA  
822  C  C   . GLY A 102 ? 0.2298 0.0974 0.2437 0.0111  -0.0302 0.0111  102 GLY A C   
823  O  O   . GLY A 102 ? 0.2280 0.1491 0.2396 -0.0042 -0.0214 0.0375  102 GLY A O   
824  N  N   . GLN A 103 ? 0.1783 0.1068 0.2582 0.0230  -0.0034 0.0110  103 GLN A N   
825  C  CA  . GLN A 103 ? 0.1658 0.1122 0.1709 0.0179  -0.0016 0.0041  103 GLN A CA  
826  C  C   . GLN A 103 ? 0.1264 0.1137 0.1533 0.0064  0.0004  -0.0068 103 GLN A C   
827  O  O   . GLN A 103 ? 0.1791 0.1029 0.1643 0.0055  -0.0245 -0.0134 103 GLN A O   
828  C  CB  . GLN A 103 ? 0.1775 0.1320 0.1473 0.0174  0.0009  0.0134  103 GLN A CB  
829  C  CG  . GLN A 103 ? 0.1845 0.1474 0.1691 0.0334  0.0242  0.0092  103 GLN A CG  
830  C  CD  . GLN A 103 ? 0.2384 0.1999 0.2100 0.1002  0.0496  0.0408  103 GLN A CD  
831  O  OE1 . GLN A 103 ? 0.2221 0.2300 0.2314 0.0832  0.0394  0.0279  103 GLN A OE1 
832  N  NE2 . GLN A 103 ? 0.2581 0.3312 0.3115 0.1754  0.0991  0.1477  103 GLN A NE2 
833  N  N   . GLY A 104 ? 0.1317 0.1070 0.1392 0.0115  0.0066  -0.0048 104 GLY A N   
834  C  CA  . GLY A 104 ? 0.1426 0.1156 0.1280 0.0262  -0.0129 -0.0146 104 GLY A CA  
835  C  C   . GLY A 104 ? 0.1180 0.1009 0.1210 0.0066  -0.0068 -0.0185 104 GLY A C   
836  O  O   . GLY A 104 ? 0.1380 0.1146 0.1411 -0.0013 -0.0114 0.0063  104 GLY A O   
837  N  N   . SER A 105 ? 0.1212 0.1195 0.1147 0.0156  -0.0036 -0.0113 105 SER A N   
838  C  CA  . SER A 105 ? 0.1174 0.1111 0.1196 -0.0013 -0.0025 -0.0229 105 SER A CA  
839  C  C   . SER A 105 ? 0.1226 0.1022 0.1063 0.0083  -0.0048 0.0013  105 SER A C   
840  O  O   . SER A 105 ? 0.1342 0.1141 0.1391 0.0190  -0.0166 -0.0104 105 SER A O   
841  C  CB  . SER A 105 ? 0.1217 0.1132 0.1313 0.0021  -0.0143 0.0054  105 SER A CB  
842  O  OG  . SER A 105 ? 0.1513 0.0960 0.1278 -0.0006 -0.0015 0.0035  105 SER A OG  
843  N  N   . GLU A 106 ? 0.1215 0.0897 0.1204 -0.0084 -0.0054 -0.0048 106 GLU A N   
844  C  CA  . GLU A 106 ? 0.1199 0.1061 0.0958 0.0140  -0.0120 -0.0053 106 GLU A CA  
845  C  C   . GLU A 106 ? 0.1219 0.0937 0.1005 0.0006  -0.0049 0.0054  106 GLU A C   
846  O  O   . GLU A 106 ? 0.1223 0.1156 0.1222 0.0068  -0.0103 0.0113  106 GLU A O   
847  C  CB  . GLU A 106 ? 0.1346 0.1050 0.0926 -0.0063 0.0016  0.0050  106 GLU A CB  
848  C  CG  . GLU A 106 ? 0.1550 0.1183 0.1073 0.0023  0.0130  0.0000  106 GLU A CG  
849  C  CD  . GLU A 106 ? 0.1050 0.1280 0.0955 0.0143  0.0006  -0.0026 106 GLU A CD  
850  O  OE1 . GLU A 106 ? 0.1093 0.1107 0.1508 0.0069  -0.0012 -0.0093 106 GLU A OE1 
851  O  OE2 . GLU A 106 ? 0.1086 0.1307 0.1528 0.0080  0.0091  -0.0075 106 GLU A OE2 
852  N  N   . HIS A 107 ? 0.1122 0.1022 0.1032 0.0058  -0.0077 0.0053  107 HIS A N   
853  C  CA  . HIS A 107 ? 0.1174 0.1023 0.1018 0.0049  -0.0011 0.0055  107 HIS A CA  
854  C  C   . HIS A 107 ? 0.1159 0.1059 0.1000 0.0016  -0.0140 0.0041  107 HIS A C   
855  O  O   . HIS A 107 ? 0.1257 0.1034 0.1169 0.0064  -0.0172 0.0025  107 HIS A O   
856  C  CB  . HIS A 107 ? 0.1138 0.1047 0.1259 0.0069  0.0047  0.0002  107 HIS A CB  
857  C  CG  . HIS A 107 ? 0.1071 0.1039 0.0946 0.0074  0.0114  -0.0012 107 HIS A CG  
858  N  ND1 . HIS A 107 ? 0.1355 0.0985 0.1178 0.0016  0.0021  0.0151  107 HIS A ND1 
859  C  CD2 . HIS A 107 ? 0.1030 0.1131 0.1120 0.0074  0.0114  -0.0220 107 HIS A CD2 
860  C  CE1 . HIS A 107 ? 0.1307 0.1074 0.0996 0.0044  -0.0048 -0.0003 107 HIS A CE1 
861  N  NE2 . HIS A 107 ? 0.1053 0.1003 0.1088 0.0134  -0.0088 -0.0076 107 HIS A NE2 
862  N  N   . THR A 108 ? 0.1368 0.0996 0.1144 -0.0035 0.0025  0.0158  108 THR A N   
863  C  CA  . THR A 108 ? 0.1423 0.0860 0.1342 0.0025  0.0111  0.0120  108 THR A CA  
864  C  C   . THR A 108 ? 0.1291 0.0968 0.1248 -0.0061 -0.0044 0.0076  108 THR A C   
865  O  O   . THR A 108 ? 0.1474 0.1135 0.1278 -0.0021 -0.0060 0.0113  108 THR A O   
866  C  CB  . THR A 108 ? 0.1546 0.1201 0.1124 0.0226  -0.0190 0.0108  108 THR A CB  
867  O  OG1 . THR A 108 ? 0.1515 0.1322 0.1203 0.0148  -0.0110 0.0063  108 THR A OG1 
868  C  CG2 . THR A 108 ? 0.1562 0.1376 0.1322 0.0203  0.0021  0.0053  108 THR A CG2 
869  N  N   . VAL A 109 ? 0.1473 0.1071 0.1421 -0.0116 0.0097  0.0343  109 VAL A N   
870  C  CA  . VAL A 109 ? 0.1410 0.1294 0.1659 -0.0093 0.0085  0.0388  109 VAL A CA  
871  C  C   . VAL A 109 ? 0.1740 0.1203 0.1445 -0.0055 0.0092  0.0364  109 VAL A C   
872  O  O   . VAL A 109 ? 0.1711 0.1116 0.1756 0.0017  0.0041  0.0164  109 VAL A O   
873  C  CB  . VAL A 109 ? 0.1630 0.1341 0.1623 -0.0113 -0.0121 0.0203  109 VAL A CB  
874  C  CG1 . VAL A 109 ? 0.1524 0.1644 0.2189 -0.0026 0.0113  0.0417  109 VAL A CG1 
875  C  CG2 . VAL A 109 ? 0.1844 0.1421 0.1766 -0.0003 -0.0326 0.0357  109 VAL A CG2 
876  N  N   . ASP A 110 ? 0.1777 0.1329 0.1403 0.0035  -0.0010 0.0427  110 ASP A N   
877  C  CA  . ASP A 110 ? 0.2041 0.1458 0.1522 0.0284  0.0243  0.0578  110 ASP A CA  
878  C  C   . ASP A 110 ? 0.1946 0.1246 0.1787 0.0189  0.0115  0.0395  110 ASP A C   
879  O  O   . ASP A 110 ? 0.2456 0.1305 0.1723 0.0206  0.0031  0.0346  110 ASP A O   
880  C  CB  . ASP A 110 ? 0.2596 0.1590 0.1752 0.0084  0.0425  0.0531  110 ASP A CB  
881  C  CG  . ASP A 110 ? 0.2491 0.1572 0.1870 0.0073  0.0414  0.0612  110 ASP A CG  
882  O  OD1 . ASP A 110 ? 0.2746 0.1812 0.2121 0.0222  0.0427  0.0523  110 ASP A OD1 
883  O  OD2 . ASP A 110 ? 0.2576 0.2748 0.2253 0.0105  0.0621  0.0675  110 ASP A OD2 
884  N  N   . LYS A 111 ? 0.1673 0.1456 0.1508 0.0193  -0.0025 0.0313  111 LYS A N   
885  C  CA  . LYS A 111 ? 0.1551 0.1423 0.2013 0.0370  -0.0058 0.0205  111 LYS A CA  
886  C  C   . LYS A 111 ? 0.1899 0.1224 0.1781 0.0113  0.0059  0.0248  111 LYS A C   
887  O  O   . LYS A 111 ? 0.1877 0.1542 0.1895 0.0219  0.0155  0.0164  111 LYS A O   
888  C  CB  . LYS A 111 ? 0.2221 0.1668 0.1576 0.0675  -0.0082 0.0254  111 LYS A CB  
889  C  CG  . LYS A 111 ? 0.2537 0.2626 0.1581 0.0659  -0.0227 0.0207  111 LYS A CG  
890  C  CD  . LYS A 111 ? 0.2422 0.3001 0.3025 0.0318  -0.0519 -0.0209 111 LYS A CD  
891  C  CE  . LYS A 111 ? 0.3765 0.5213 0.2879 0.0912  -0.1160 -0.0484 111 LYS A CE  
892  N  NZ  . LYS A 111 ? 0.3838 0.4385 0.4174 0.0370  -0.0320 0.0558  111 LYS A NZ  
893  N  N   . LYS A 112 ? 0.1847 0.1084 0.1402 0.0008  0.0070  0.0176  112 LYS A N   
894  C  CA  . LYS A 112 ? 0.1863 0.1438 0.1575 0.0074  0.0127  0.0141  112 LYS A CA  
895  C  C   . LYS A 112 ? 0.1601 0.1300 0.1322 0.0013  -0.0078 0.0002  112 LYS A C   
896  O  O   . LYS A 112 ? 0.1705 0.1093 0.1637 0.0164  -0.0009 -0.0043 112 LYS A O   
897  C  CB  . LYS A 112 ? 0.1817 0.1802 0.1884 -0.0292 0.0227  -0.0159 112 LYS A CB  
898  C  CG  . LYS A 112 ? 0.2226 0.2170 0.2102 -0.0340 0.0088  -0.0478 112 LYS A CG  
899  C  CD  . LYS A 112 ? 0.2297 0.2904 0.2064 0.0026  -0.0392 0.0458  112 LYS A CD  
900  C  CE  . LYS A 112 ? 0.3650 0.3039 0.2519 0.0220  -0.1024 -0.0098 112 LYS A CE  
901  N  NZ  . LYS A 112 ? 0.3431 0.2569 0.4403 -0.0350 -0.1051 0.0568  112 LYS A NZ  
902  N  N   A LYS A 113 ? 0.1576 0.1327 0.1297 0.0260  -0.0156 0.0037  113 LYS A N   
903  N  N   B LYS A 113 ? 0.1558 0.1289 0.1271 0.0238  -0.0154 0.0042  113 LYS A N   
904  C  CA  A LYS A 113 ? 0.1762 0.1597 0.1381 0.0316  -0.0187 0.0220  113 LYS A CA  
905  C  CA  B LYS A 113 ? 0.1776 0.1524 0.1333 0.0309  -0.0147 0.0190  113 LYS A CA  
906  C  C   A LYS A 113 ? 0.1768 0.0991 0.1834 0.0071  -0.0286 0.0146  113 LYS A C   
907  C  C   B LYS A 113 ? 0.1720 0.1041 0.1704 0.0078  -0.0174 0.0193  113 LYS A C   
908  O  O   A LYS A 113 ? 0.2339 0.0978 0.2294 0.0033  -0.0646 0.0190  113 LYS A O   
909  O  O   B LYS A 113 ? 0.2423 0.1062 0.2445 0.0055  -0.0700 0.0147  113 LYS A O   
910  C  CB  A LYS A 113 ? 0.1605 0.1538 0.1465 0.0142  -0.0252 0.0094  113 LYS A CB  
911  C  CB  B LYS A 113 ? 0.1745 0.1452 0.1339 0.0126  -0.0121 0.0023  113 LYS A CB  
912  C  CG  A LYS A 113 ? 0.1791 0.1820 0.1465 0.0158  -0.0456 0.0009  113 LYS A CG  
913  C  CG  B LYS A 113 ? 0.1757 0.1819 0.1487 0.0071  -0.0153 -0.0253 113 LYS A CG  
914  C  CD  A LYS A 113 ? 0.1887 0.1544 0.2086 0.0099  -0.0253 -0.0206 113 LYS A CD  
915  C  CD  B LYS A 113 ? 0.2046 0.1730 0.1311 0.0125  0.0168  -0.0089 113 LYS A CD  
916  C  CE  A LYS A 113 ? 0.2091 0.1820 0.2423 -0.0044 -0.0630 0.0286  113 LYS A CE  
917  C  CE  B LYS A 113 ? 0.2111 0.2159 0.1876 0.0162  -0.0220 -0.0038 113 LYS A CE  
918  N  NZ  A LYS A 113 ? 0.1920 0.2366 0.1910 0.0544  -0.0592 -0.0262 113 LYS A NZ  
919  N  NZ  B LYS A 113 ? 0.2172 0.2476 0.2559 0.0321  0.0418  -0.0289 113 LYS A NZ  
920  N  N   . TYR A 114 ? 0.1522 0.0955 0.1329 0.0093  -0.0115 0.0072  114 TYR A N   
921  C  CA  . TYR A 114 ? 0.1669 0.0998 0.1439 -0.0044 -0.0192 0.0041  114 TYR A CA  
922  C  C   . TYR A 114 ? 0.1517 0.0813 0.1323 -0.0091 -0.0175 -0.0030 114 TYR A C   
923  O  O   . TYR A 114 ? 0.1403 0.1077 0.1628 -0.0024 -0.0109 0.0027  114 TYR A O   
924  C  CB  . TYR A 114 ? 0.1572 0.0991 0.1458 0.0013  0.0072  0.0006  114 TYR A CB  
925  C  CG  . TYR A 114 ? 0.1605 0.0924 0.1274 0.0013  -0.0006 0.0143  114 TYR A CG  
926  C  CD1 . TYR A 114 ? 0.2104 0.1386 0.1192 0.0522  -0.0049 0.0063  114 TYR A CD1 
927  C  CD2 . TYR A 114 ? 0.1551 0.1122 0.1781 -0.0082 -0.0021 0.0062  114 TYR A CD2 
928  C  CE1 . TYR A 114 ? 0.2332 0.1812 0.1447 0.0495  0.0196  0.0015  114 TYR A CE1 
929  C  CE2 . TYR A 114 ? 0.2078 0.1630 0.1888 0.0177  0.0384  0.0178  114 TYR A CE2 
930  C  CZ  . TYR A 114 ? 0.2546 0.1729 0.1659 0.0258  0.0399  0.0223  114 TYR A CZ  
931  O  OH  . TYR A 114 ? 0.3233 0.2613 0.2573 0.0365  0.1076  0.0418  114 TYR A OH  
932  N  N   . ALA A 115 ? 0.1596 0.0912 0.1377 -0.0005 -0.0282 -0.0183 115 ALA A N   
933  C  CA  . ALA A 115 ? 0.1480 0.0883 0.1371 0.0051  -0.0212 -0.0255 115 ALA A CA  
934  C  C   . ALA A 115 ? 0.1395 0.1031 0.1578 0.0177  -0.0044 -0.0164 115 ALA A C   
935  O  O   . ALA A 115 ? 0.1390 0.0989 0.1648 0.0155  -0.0044 -0.0159 115 ALA A O   
936  C  CB  . ALA A 115 ? 0.1590 0.1198 0.1597 0.0040  -0.0314 -0.0277 115 ALA A CB  
937  N  N   . ALA A 116 ? 0.1458 0.0840 0.1244 0.0131  -0.0073 -0.0091 116 ALA A N   
938  C  CA  . ALA A 116 ? 0.1226 0.1007 0.1228 0.0047  0.0027  -0.0111 116 ALA A CA  
939  C  C   . ALA A 116 ? 0.1025 0.0994 0.1170 0.0159  -0.0137 -0.0024 116 ALA A C   
940  O  O   . ALA A 116 ? 0.1151 0.0986 0.1213 0.0053  -0.0006 -0.0025 116 ALA A O   
941  C  CB  . ALA A 116 ? 0.1500 0.1142 0.1188 0.0179  -0.0029 -0.0122 116 ALA A CB  
942  N  N   . GLU A 117 ? 0.1189 0.0944 0.1394 0.0132  -0.0150 -0.0029 117 GLU A N   
943  C  CA  . GLU A 117 ? 0.1304 0.0761 0.1212 0.0108  -0.0173 -0.0063 117 GLU A CA  
944  C  C   . GLU A 117 ? 0.1250 0.1089 0.0928 0.0031  0.0137  0.0055  117 GLU A C   
945  O  O   . GLU A 117 ? 0.1333 0.1023 0.1137 0.0267  0.0244  0.0115  117 GLU A O   
946  C  CB  . GLU A 117 ? 0.1232 0.1174 0.1086 0.0092  -0.0084 0.0046  117 GLU A CB  
947  C  CG  . GLU A 117 ? 0.1377 0.1052 0.1118 0.0001  -0.0160 -0.0115 117 GLU A CG  
948  C  CD  . GLU A 117 ? 0.1307 0.1044 0.1229 0.0036  0.0000  -0.0052 117 GLU A CD  
949  O  OE1 . GLU A 117 ? 0.1259 0.1289 0.1143 0.0108  -0.0122 -0.0011 117 GLU A OE1 
950  O  OE2 . GLU A 117 ? 0.1535 0.1196 0.1138 0.0033  -0.0267 0.0043  117 GLU A OE2 
951  N  N   . LEU A 118 ? 0.1165 0.0908 0.0960 0.0049  -0.0044 0.0000  118 LEU A N   
952  C  CA  . LEU A 118 ? 0.1244 0.0844 0.1059 -0.0043 -0.0151 0.0006  118 LEU A CA  
953  C  C   . LEU A 118 ? 0.1025 0.0928 0.0837 0.0082  0.0001  0.0081  118 LEU A C   
954  O  O   . LEU A 118 ? 0.1183 0.0962 0.0812 0.0013  0.0037  0.0015  118 LEU A O   
955  C  CB  . LEU A 118 ? 0.1165 0.1023 0.1393 0.0011  -0.0024 0.0131  118 LEU A CB  
956  C  CG  . LEU A 118 ? 0.1045 0.1154 0.1216 0.0109  -0.0149 0.0125  118 LEU A CG  
957  C  CD1 . LEU A 118 ? 0.1423 0.0946 0.1310 0.0054  -0.0258 0.0189  118 LEU A CD1 
958  C  CD2 . LEU A 118 ? 0.1170 0.1521 0.1208 -0.0052 -0.0198 0.0117  118 LEU A CD2 
959  N  N   . HIS A 119 ? 0.1072 0.0854 0.1031 0.0023  -0.0046 0.0023  119 HIS A N   
960  C  CA  . HIS A 119 ? 0.1065 0.0829 0.1095 -0.0002 -0.0087 0.0001  119 HIS A CA  
961  C  C   . HIS A 119 ? 0.1047 0.0900 0.0961 -0.0020 0.0058  -0.0006 119 HIS A C   
962  O  O   . HIS A 119 ? 0.1135 0.0969 0.1032 0.0100  0.0019  0.0113  119 HIS A O   
963  C  CB  . HIS A 119 ? 0.0989 0.1028 0.1177 0.0092  -0.0133 0.0066  119 HIS A CB  
964  C  CG  . HIS A 119 ? 0.0979 0.1086 0.0878 -0.0035 -0.0054 -0.0060 119 HIS A CG  
965  N  ND1 . HIS A 119 ? 0.1027 0.1007 0.1140 -0.0076 -0.0142 -0.0037 119 HIS A ND1 
966  C  CD2 . HIS A 119 ? 0.1162 0.0989 0.1125 0.0069  -0.0095 -0.0011 119 HIS A CD2 
967  C  CE1 . HIS A 119 ? 0.1332 0.1197 0.0705 0.0047  0.0053  -0.0084 119 HIS A CE1 
968  N  NE2 . HIS A 119 ? 0.1128 0.1063 0.1046 0.0185  -0.0057 -0.0043 119 HIS A NE2 
969  N  N   . LEU A 120 ? 0.0944 0.0876 0.0946 0.0038  -0.0071 -0.0042 120 LEU A N   
970  C  CA  . LEU A 120 ? 0.1070 0.0812 0.1357 0.0022  -0.0064 -0.0046 120 LEU A CA  
971  C  C   . LEU A 120 ? 0.0974 0.0883 0.0917 0.0239  -0.0108 0.0106  120 LEU A C   
972  O  O   . LEU A 120 ? 0.1068 0.0912 0.0899 0.0012  -0.0109 0.0000  120 LEU A O   
973  C  CB  . LEU A 120 ? 0.1058 0.1109 0.1305 0.0059  -0.0145 -0.0200 120 LEU A CB  
974  C  CG  . LEU A 120 ? 0.1062 0.1198 0.1237 -0.0089 -0.0238 0.0057  120 LEU A CG  
975  C  CD1 . LEU A 120 ? 0.2142 0.1538 0.1704 -0.0765 -0.0143 0.0187  120 LEU A CD1 
976  C  CD2 . LEU A 120 ? 0.1372 0.1522 0.1298 0.0116  -0.0381 0.0111  120 LEU A CD2 
977  N  N   . VAL A 121 ? 0.1163 0.0838 0.1192 0.0027  -0.0125 0.0070  121 VAL A N   
978  C  CA  . VAL A 121 ? 0.1232 0.0835 0.1073 -0.0020 -0.0134 -0.0064 121 VAL A CA  
979  C  C   . VAL A 121 ? 0.1152 0.0900 0.1092 -0.0064 -0.0125 0.0025  121 VAL A C   
980  O  O   . VAL A 121 ? 0.1467 0.0943 0.1201 -0.0013 -0.0212 0.0074  121 VAL A O   
981  C  CB  . VAL A 121 ? 0.1117 0.0985 0.1282 -0.0040 -0.0076 0.0033  121 VAL A CB  
982  C  CG1 . VAL A 121 ? 0.1113 0.1141 0.1683 -0.0072 -0.0082 -0.0082 121 VAL A CG1 
983  C  CG2 . VAL A 121 ? 0.1363 0.1079 0.1421 0.0096  0.0117  0.0042  121 VAL A CG2 
984  N  N   . HIS A 122 ? 0.1145 0.0897 0.1346 0.0021  -0.0120 -0.0128 122 HIS A N   
985  C  CA  . HIS A 122 ? 0.1254 0.0885 0.1482 0.0067  -0.0189 -0.0232 122 HIS A CA  
986  C  C   . HIS A 122 ? 0.1409 0.0914 0.1389 0.0009  -0.0370 -0.0027 122 HIS A C   
987  O  O   . HIS A 122 ? 0.1455 0.1029 0.1395 -0.0062 -0.0430 0.0020  122 HIS A O   
988  C  CB  . HIS A 122 ? 0.1180 0.0833 0.1738 0.0096  -0.0027 -0.0025 122 HIS A CB  
989  C  CG  . HIS A 122 ? 0.1151 0.0979 0.1383 0.0145  -0.0088 -0.0110 122 HIS A CG  
990  N  ND1 . HIS A 122 ? 0.1167 0.0867 0.1544 0.0103  0.0013  -0.0081 122 HIS A ND1 
991  C  CD2 . HIS A 122 ? 0.1296 0.1150 0.1508 0.0120  -0.0219 -0.0006 122 HIS A CD2 
992  C  CE1 . HIS A 122 ? 0.1120 0.1133 0.1561 0.0061  -0.0057 -0.0132 122 HIS A CE1 
993  N  NE2 . HIS A 122 ? 0.1235 0.1253 0.1459 -0.0015 -0.0135 -0.0079 122 HIS A NE2 
994  N  N   . TRP A 123 ? 0.1486 0.0829 0.1337 0.0032  -0.0333 -0.0133 123 TRP A N   
995  C  CA  . TRP A 123 ? 0.1374 0.0749 0.1547 0.0052  -0.0343 -0.0139 123 TRP A CA  
996  C  C   . TRP A 123 ? 0.1549 0.0873 0.1557 0.0060  -0.0233 -0.0128 123 TRP A C   
997  O  O   . TRP A 123 ? 0.1491 0.1034 0.2292 0.0166  -0.0534 -0.0266 123 TRP A O   
998  C  CB  . TRP A 123 ? 0.1662 0.1115 0.1536 -0.0179 -0.0480 0.0046  123 TRP A CB  
999  C  CG  . TRP A 123 ? 0.1957 0.1088 0.1696 -0.0324 -0.0687 0.0102  123 TRP A CG  
1000 C  CD1 . TRP A 123 ? 0.2573 0.1306 0.1662 -0.0187 -0.0814 0.0091  123 TRP A CD1 
1001 C  CD2 . TRP A 123 ? 0.2379 0.1084 0.1651 -0.0183 -0.0624 0.0070  123 TRP A CD2 
1002 N  NE1 . TRP A 123 ? 0.3055 0.1025 0.1870 -0.0145 -0.1099 0.0048  123 TRP A NE1 
1003 C  CE2 . TRP A 123 ? 0.3103 0.0962 0.1874 -0.0291 -0.0993 0.0092  123 TRP A CE2 
1004 C  CE3 . TRP A 123 ? 0.2687 0.0953 0.2025 -0.0294 -0.0635 0.0107  123 TRP A CE3 
1005 C  CZ2 . TRP A 123 ? 0.3632 0.1041 0.2409 -0.0122 -0.1215 0.0036  123 TRP A CZ2 
1006 C  CZ3 . TRP A 123 ? 0.3194 0.0892 0.1980 -0.0245 -0.0533 0.0093  123 TRP A CZ3 
1007 C  CH2 . TRP A 123 ? 0.3745 0.1188 0.1896 -0.0200 -0.0751 0.0168  123 TRP A CH2 
1008 N  N   . ASN A 124 ? 0.1529 0.0970 0.1697 0.0086  -0.0283 -0.0323 124 ASN A N   
1009 C  CA  . ASN A 124 ? 0.1992 0.0983 0.1928 0.0243  -0.0434 -0.0516 124 ASN A CA  
1010 C  C   . ASN A 124 ? 0.1756 0.1081 0.1802 0.0160  -0.0236 -0.0406 124 ASN A C   
1011 O  O   . ASN A 124 ? 0.1852 0.1067 0.1773 0.0107  -0.0200 -0.0285 124 ASN A O   
1012 C  CB  . ASN A 124 ? 0.2131 0.1170 0.1707 -0.0027 -0.0051 -0.0414 124 ASN A CB  
1013 C  CG  . ASN A 124 ? 0.2366 0.1318 0.1859 -0.0176 0.0062  -0.0494 124 ASN A CG  
1014 O  OD1 . ASN A 124 ? 0.2174 0.1283 0.2416 0.0141  0.0259  -0.0480 124 ASN A OD1 
1015 N  ND2 . ASN A 124 ? 0.2455 0.1493 0.1806 0.0124  -0.0042 -0.0325 124 ASN A ND2 
1016 N  N   . THR A 125 ? 0.1812 0.1068 0.2402 0.0274  -0.0390 -0.0488 125 THR A N   
1017 C  CA  . THR A 125 ? 0.2063 0.1101 0.2683 0.0237  -0.0512 -0.0326 125 THR A CA  
1018 C  C   . THR A 125 ? 0.1914 0.1091 0.2717 0.0476  -0.0138 -0.0534 125 THR A C   
1019 O  O   . THR A 125 ? 0.2286 0.1127 0.3462 0.0372  -0.0473 -0.0278 125 THR A O   
1020 C  CB  . THR A 125 ? 0.2042 0.1795 0.3537 0.0121  -0.0641 -0.0392 125 THR A CB  
1021 O  OG1 . THR A 125 ? 0.2160 0.1801 0.4436 0.0465  -0.0186 -0.0520 125 THR A OG1 
1022 C  CG2 . THR A 125 ? 0.2523 0.1921 0.4008 0.0284  -0.1354 -0.0381 125 THR A CG2 
1023 N  N   . LYS A 126 ? 0.2020 0.1205 0.2623 0.0091  0.0120  -0.0688 127 LYS A N   
1024 C  CA  . LYS A 126 ? 0.3177 0.1335 0.2640 -0.0074 0.0344  -0.0899 127 LYS A CA  
1025 C  C   . LYS A 126 ? 0.2470 0.0983 0.2834 0.0049  -0.0201 -0.0523 127 LYS A C   
1026 O  O   . LYS A 126 ? 0.2613 0.1201 0.3563 -0.0064 -0.0103 -0.1013 127 LYS A O   
1027 C  CB  . LYS A 126 ? 0.3480 0.2179 0.2526 -0.0600 0.0105  -0.0935 127 LYS A CB  
1028 C  CG  . LYS A 126 ? 0.2816 0.2179 0.2884 -0.0741 0.0174  -0.0826 127 LYS A CG  
1029 C  CD  . LYS A 126 ? 0.3604 0.3679 0.2877 -0.0394 0.0738  -0.0996 127 LYS A CD  
1030 C  CE  . LYS A 126 ? 0.3133 0.5238 0.3193 0.0305  0.0941  -0.0297 127 LYS A CE  
1031 N  NZ  . LYS A 126 ? 0.6333 0.7235 0.2991 0.1638  0.0568  0.0903  127 LYS A NZ  
1032 N  N   . TYR A 127 ? 0.1977 0.1150 0.1848 -0.0011 -0.0245 -0.0233 128 TYR A N   
1033 C  CA  . TYR A 127 ? 0.2066 0.0942 0.1838 0.0050  -0.0300 -0.0359 128 TYR A CA  
1034 C  C   . TYR A 127 ? 0.2100 0.0989 0.1921 0.0040  -0.0243 -0.0314 128 TYR A C   
1035 O  O   . TYR A 127 ? 0.2122 0.1231 0.2139 0.0025  -0.0250 -0.0194 128 TYR A O   
1036 C  CB  . TYR A 127 ? 0.2078 0.1071 0.1993 0.0081  -0.0176 -0.0345 128 TYR A CB  
1037 C  CG  . TYR A 127 ? 0.1806 0.1201 0.1901 0.0048  -0.0187 -0.0388 128 TYR A CG  
1038 C  CD1 . TYR A 127 ? 0.2344 0.1389 0.1824 0.0148  -0.0543 -0.0370 128 TYR A CD1 
1039 C  CD2 . TYR A 127 ? 0.1890 0.1257 0.1714 0.0210  -0.0012 -0.0312 128 TYR A CD2 
1040 C  CE1 . TYR A 127 ? 0.2633 0.1612 0.1757 0.0315  -0.0697 -0.0442 128 TYR A CE1 
1041 C  CE2 . TYR A 127 ? 0.1920 0.1504 0.1622 0.0167  -0.0184 -0.0434 128 TYR A CE2 
1042 C  CZ  . TYR A 127 ? 0.2529 0.1716 0.1546 0.0220  -0.0141 -0.0578 128 TYR A CZ  
1043 O  OH  . TYR A 127 ? 0.2803 0.1805 0.1759 0.0348  -0.0319 -0.0535 128 TYR A OH  
1044 N  N   . GLY A 128 ? 0.2260 0.1111 0.2063 0.0240  -0.0527 -0.0109 129 GLY A N   
1045 C  CA  . GLY A 128 ? 0.2330 0.1293 0.2057 0.0061  -0.0369 -0.0068 129 GLY A CA  
1046 C  C   . GLY A 128 ? 0.2445 0.1339 0.1756 0.0038  -0.0497 -0.0003 129 GLY A C   
1047 O  O   . GLY A 128 ? 0.3478 0.1208 0.2213 0.0084  -0.0964 0.0220  129 GLY A O   
1048 N  N   . ASP A 129 ? 0.2722 0.1353 0.1773 0.0283  -0.0364 -0.0116 130 ASP A N   
1049 C  CA  . ASP A 129 ? 0.3180 0.1289 0.1544 0.0225  -0.0354 0.0142  130 ASP A CA  
1050 C  C   . ASP A 129 ? 0.3025 0.1333 0.1524 0.0183  -0.0418 -0.0036 130 ASP A C   
1051 O  O   . ASP A 129 ? 0.2958 0.1557 0.1526 0.0451  -0.0407 -0.0076 130 ASP A O   
1052 C  CB  . ASP A 129 ? 0.3753 0.1404 0.1673 0.0730  -0.0044 0.0165  130 ASP A CB  
1053 C  CG  . ASP A 129 ? 0.3391 0.2194 0.3274 0.1249  0.0083  -0.0359 130 ASP A CG  
1054 O  OD1 . ASP A 129 ? 0.3657 0.2454 0.2781 0.1104  -0.0230 0.0517  130 ASP A OD1 
1055 O  OD2 . ASP A 129 ? 0.3568 0.2398 0.3772 0.0986  -0.0776 0.0222  130 ASP A OD2 
1056 N  N   . ALA A 130 ? 0.3258 0.1294 0.1651 0.0247  -0.0276 0.0057  131 ALA A N   
1057 C  CA  . ALA A 130 ? 0.2779 0.1263 0.1605 0.0245  -0.0182 -0.0013 131 ALA A CA  
1058 C  C   . ALA A 130 ? 0.2636 0.1342 0.1301 0.0031  -0.0035 -0.0025 131 ALA A C   
1059 O  O   . ALA A 130 ? 0.2448 0.1273 0.1438 0.0081  -0.0100 -0.0053 131 ALA A O   
1060 C  CB  . ALA A 130 ? 0.2776 0.1239 0.2247 0.0070  -0.0168 -0.0114 131 ALA A CB  
1061 N  N   . GLY A 131 ? 0.3080 0.1712 0.1447 0.0183  0.0186  0.0136  132 GLY A N   
1062 C  CA  . GLY A 131 ? 0.3061 0.2092 0.1502 0.0388  0.0428  0.0040  132 GLY A CA  
1063 C  C   . GLY A 131 ? 0.2025 0.1590 0.1691 -0.0067 0.0347  0.0083  132 GLY A C   
1064 O  O   . GLY A 131 ? 0.2149 0.1813 0.2454 -0.0178 0.0025  0.0464  132 GLY A O   
1065 N  N   . LYS A 132 ? 0.2655 0.1452 0.1914 -0.0021 0.0630  0.0238  133 LYS A N   
1066 C  CA  . LYS A 132 ? 0.2147 0.1575 0.1890 0.0060  0.0185  0.0331  133 LYS A CA  
1067 C  C   . LYS A 132 ? 0.1953 0.1122 0.1725 -0.0211 -0.0139 0.0047  133 LYS A C   
1068 O  O   . LYS A 132 ? 0.1964 0.1420 0.1831 -0.0290 -0.0217 -0.0106 133 LYS A O   
1069 C  CB  . LYS A 132 ? 0.2291 0.1300 0.2605 0.0033  0.0009  0.0205  133 LYS A CB  
1070 C  CG  . LYS A 132 ? 0.2950 0.1923 0.3906 -0.0433 -0.0193 0.0842  133 LYS A CG  
1071 C  CD  . LYS A 132 ? 0.2336 0.3174 0.6529 -0.0540 0.0401  0.1558  133 LYS A CD  
1072 N  N   . ALA A 133 ? 0.1762 0.1201 0.1522 -0.0179 0.0042  -0.0089 134 ALA A N   
1073 C  CA  . ALA A 133 ? 0.1522 0.1538 0.1381 -0.0059 -0.0046 -0.0062 134 ALA A CA  
1074 C  C   . ALA A 133 ? 0.1720 0.1360 0.1190 -0.0252 0.0030  0.0142  134 ALA A C   
1075 O  O   . ALA A 133 ? 0.1621 0.1513 0.1263 -0.0127 -0.0029 -0.0055 134 ALA A O   
1076 C  CB  . ALA A 133 ? 0.1544 0.1285 0.1536 -0.0077 -0.0222 -0.0257 134 ALA A CB  
1077 N  N   . SER A 134 ? 0.1727 0.1224 0.1489 0.0000  -0.0079 -0.0043 135 SER A N   
1078 C  CA  . SER A 134 ? 0.1669 0.1449 0.1302 0.0072  0.0005  0.0060  135 SER A CA  
1079 C  C   . SER A 134 ? 0.1621 0.1551 0.1571 -0.0145 0.0033  0.0255  135 SER A C   
1080 O  O   . SER A 134 ? 0.1709 0.1712 0.1920 0.0041  -0.0003 0.0305  135 SER A O   
1081 C  CB  . SER A 134 ? 0.2240 0.1590 0.1569 0.0075  0.0449  -0.0037 135 SER A CB  
1082 O  OG  . SER A 134 ? 0.2344 0.1953 0.1641 0.0251  0.0401  0.0078  135 SER A OG  
1083 N  N   . GLN A 135 ? 0.1707 0.1533 0.1412 -0.0233 0.0002  -0.0018 136 GLN A N   
1084 C  CA  . GLN A 135 ? 0.1546 0.1704 0.1905 -0.0442 -0.0192 0.0103  136 GLN A CA  
1085 C  C   . GLN A 135 ? 0.1639 0.1581 0.1838 -0.0280 -0.0320 -0.0031 136 GLN A C   
1086 O  O   . GLN A 135 ? 0.2097 0.2451 0.2384 -0.0502 -0.0741 -0.0122 136 GLN A O   
1087 C  CB  . GLN A 135 ? 0.2345 0.2258 0.2199 -0.0885 -0.0072 0.0313  136 GLN A CB  
1088 C  CG  . GLN A 135 ? 0.3005 0.2368 0.2499 -0.0906 0.0304  0.0365  136 GLN A CG  
1089 C  CD  . GLN A 135 ? 0.3369 0.4101 0.3438 -0.0190 0.0726  0.0447  136 GLN A CD  
1090 O  OE1 . GLN A 135 ? 0.2604 0.5992 0.7313 0.0798  -0.0381 0.0066  136 GLN A OE1 
1091 N  NE2 . GLN A 135 ? 0.5310 0.4039 0.5467 -0.0596 -0.0653 -0.1274 136 GLN A NE2 
1092 N  N   . GLN A 136 ? 0.1666 0.1605 0.1478 -0.0211 -0.0044 -0.0098 137 GLN A N   
1093 C  CA  . GLN A 136 ? 0.1823 0.1795 0.1160 0.0006  -0.0335 -0.0240 137 GLN A CA  
1094 C  C   . GLN A 136 ? 0.1770 0.1766 0.1039 -0.0030 -0.0029 -0.0326 137 GLN A C   
1095 O  O   . GLN A 136 ? 0.1975 0.1536 0.1283 0.0055  -0.0277 -0.0152 137 GLN A O   
1096 C  CB  . GLN A 136 ? 0.1921 0.1745 0.1700 0.0085  -0.0530 -0.0277 137 GLN A CB  
1097 C  CG  . GLN A 136 ? 0.2658 0.2190 0.1842 0.0670  -0.0016 0.0141  137 GLN A CG  
1098 C  CD  . GLN A 136 ? 0.3435 0.2315 0.2834 -0.0013 0.0399  0.0703  137 GLN A CD  
1099 O  OE1 . GLN A 136 ? 0.2955 0.1675 0.3037 -0.0136 0.0072  -0.0498 137 GLN A OE1 
1100 N  NE2 . GLN A 136 ? 0.3499 0.3869 0.4270 0.0249  0.0844  0.1643  137 GLN A NE2 
1101 N  N   . PRO A 137 ? 0.1723 0.2242 0.1021 0.0124  -0.0187 -0.0267 138 PRO A N   
1102 C  CA  . PRO A 137 ? 0.2124 0.2377 0.0994 0.0452  -0.0308 0.0161  138 PRO A CA  
1103 C  C   . PRO A 137 ? 0.2294 0.2052 0.1111 0.0381  -0.0020 0.0143  138 PRO A C   
1104 O  O   . PRO A 137 ? 0.2455 0.2068 0.2543 0.0447  0.0369  0.0488  138 PRO A O   
1105 C  CB  . PRO A 137 ? 0.3125 0.3460 0.0900 0.0724  -0.0291 0.0251  138 PRO A CB  
1106 C  CG  . PRO A 137 ? 0.4254 0.3870 0.1323 -0.0675 -0.0744 -0.0546 138 PRO A CG  
1107 C  CD  . PRO A 137 ? 0.2251 0.3314 0.1174 -0.0037 -0.0519 -0.0816 138 PRO A CD  
1108 N  N   . ASP A 138 ? 0.1842 0.1833 0.1118 0.0204  -0.0030 -0.0077 139 ASP A N   
1109 C  CA  . ASP A 138 ? 0.1666 0.2450 0.1057 0.0036  0.0257  -0.0096 139 ASP A CA  
1110 C  C   . ASP A 138 ? 0.1657 0.1493 0.1164 -0.0190 0.0063  -0.0187 139 ASP A C   
1111 O  O   . ASP A 138 ? 0.1589 0.1756 0.1654 0.0063  -0.0070 -0.0172 139 ASP A O   
1112 C  CB  . ASP A 138 ? 0.2129 0.2536 0.1137 0.0353  0.0114  -0.0286 139 ASP A CB  
1113 C  CG  . ASP A 138 ? 0.2189 0.2613 0.1549 0.0392  0.0004  -0.0233 139 ASP A CG  
1114 O  OD1 . ASP A 138 ? 0.2724 0.1795 0.1824 0.0240  -0.0016 -0.0515 139 ASP A OD1 
1115 O  OD2 . ASP A 138 ? 0.2656 0.3389 0.2370 0.0839  0.0122  -0.1091 139 ASP A OD2 
1116 N  N   . GLY A 139 ? 0.1554 0.1331 0.0928 -0.0018 -0.0129 -0.0182 140 GLY A N   
1117 C  CA  . GLY A 139 ? 0.1603 0.1381 0.1018 -0.0165 -0.0212 -0.0114 140 GLY A CA  
1118 C  C   . GLY A 139 ? 0.1324 0.1076 0.1034 -0.0111 -0.0150 0.0025  140 GLY A C   
1119 O  O   . GLY A 139 ? 0.1648 0.1049 0.1229 0.0073  -0.0304 -0.0055 140 GLY A O   
1120 N  N   . LEU A 140 ? 0.1307 0.0983 0.1277 -0.0013 -0.0117 -0.0043 141 LEU A N   
1121 C  CA  . LEU A 140 ? 0.1198 0.0982 0.1071 0.0036  -0.0057 -0.0034 141 LEU A CA  
1122 C  C   . LEU A 140 ? 0.1183 0.1053 0.1125 0.0089  -0.0092 -0.0110 141 LEU A C   
1123 O  O   . LEU A 140 ? 0.1324 0.1041 0.1140 -0.0035 -0.0093 -0.0127 141 LEU A O   
1124 C  CB  . LEU A 140 ? 0.1167 0.1055 0.1345 0.0078  0.0040  -0.0089 141 LEU A CB  
1125 C  CG  . LEU A 140 ? 0.1432 0.1382 0.1625 0.0226  0.0223  0.0208  141 LEU A CG  
1126 C  CD1 . LEU A 140 ? 0.1399 0.1386 0.1756 0.0278  0.0163  0.0054  141 LEU A CD1 
1127 C  CD2 . LEU A 140 ? 0.1916 0.1149 0.1750 0.0092  -0.0118 0.0156  141 LEU A CD2 
1128 N  N   . ALA A 141 ? 0.1115 0.0932 0.1314 0.0013  -0.0113 -0.0134 142 ALA A N   
1129 C  CA  . ALA A 141 ? 0.1348 0.0921 0.1357 -0.0022 -0.0039 -0.0149 142 ALA A CA  
1130 C  C   . ALA A 141 ? 0.1217 0.1032 0.1099 0.0013  -0.0098 -0.0040 142 ALA A C   
1131 O  O   . ALA A 141 ? 0.1477 0.0964 0.1234 0.0061  -0.0212 -0.0006 142 ALA A O   
1132 C  CB  . ALA A 141 ? 0.1345 0.1263 0.1702 0.0008  0.0083  -0.0182 142 ALA A CB  
1133 N  N   . VAL A 142 ? 0.1163 0.0971 0.0944 -0.0060 -0.0118 -0.0051 143 VAL A N   
1134 C  CA  . VAL A 142 ? 0.1205 0.1043 0.0985 0.0029  -0.0108 -0.0106 143 VAL A CA  
1135 C  C   . VAL A 142 ? 0.1156 0.0840 0.0809 0.0054  -0.0023 -0.0042 143 VAL A C   
1136 O  O   . VAL A 142 ? 0.1201 0.1071 0.0951 -0.0020 -0.0124 0.0002  143 VAL A O   
1137 C  CB  . VAL A 142 ? 0.1092 0.1140 0.1201 0.0003  -0.0157 -0.0088 143 VAL A CB  
1138 C  CG1 . VAL A 142 ? 0.1374 0.1420 0.0993 0.0058  -0.0106 -0.0121 143 VAL A CG1 
1139 C  CG2 . VAL A 142 ? 0.1254 0.1487 0.1052 -0.0091 0.0108  -0.0021 143 VAL A CG2 
1140 N  N   . LEU A 143 ? 0.1048 0.0916 0.1207 -0.0065 -0.0106 -0.0077 144 LEU A N   
1141 C  CA  . LEU A 143 ? 0.1061 0.0906 0.1426 -0.0018 0.0004  0.0004  144 LEU A CA  
1142 C  C   . LEU A 143 ? 0.0973 0.1014 0.0897 -0.0135 -0.0074 0.0036  144 LEU A C   
1143 O  O   . LEU A 143 ? 0.1319 0.0998 0.0964 0.0051  0.0013  -0.0035 144 LEU A O   
1144 C  CB  . LEU A 143 ? 0.1232 0.1185 0.1394 0.0011  -0.0132 0.0055  144 LEU A CB  
1145 C  CG  . LEU A 143 ? 0.1149 0.1492 0.1456 -0.0041 -0.0080 -0.0023 144 LEU A CG  
1146 C  CD1 . LEU A 143 ? 0.1210 0.2400 0.1342 -0.0097 -0.0089 0.0441  144 LEU A CD1 
1147 C  CD2 . LEU A 143 ? 0.1107 0.1799 0.2141 0.0109  -0.0392 -0.0108 144 LEU A CD2 
1148 N  N   . GLY A 144 ? 0.1196 0.0946 0.1038 -0.0100 -0.0054 -0.0027 145 GLY A N   
1149 C  CA  . GLY A 144 ? 0.1146 0.0957 0.1279 -0.0062 -0.0038 -0.0086 145 GLY A CA  
1150 C  C   . GLY A 144 ? 0.1061 0.1003 0.0849 0.0087  0.0031  -0.0025 145 GLY A C   
1151 O  O   . GLY A 144 ? 0.1302 0.1122 0.1142 -0.0067 0.0221  -0.0081 145 GLY A O   
1152 N  N   . ILE A 145 ? 0.1118 0.0973 0.0820 0.0004  0.0016  -0.0016 146 ILE A N   
1153 C  CA  . ILE A 145 ? 0.1190 0.0974 0.1189 0.0004  -0.0100 -0.0025 146 ILE A CA  
1154 C  C   . ILE A 145 ? 0.1259 0.0985 0.0937 -0.0062 -0.0013 -0.0003 146 ILE A C   
1155 O  O   . ILE A 145 ? 0.1289 0.0878 0.1196 -0.0032 0.0076  0.0070  146 ILE A O   
1156 C  CB  . ILE A 145 ? 0.1220 0.1122 0.1180 0.0080  -0.0076 0.0000  146 ILE A CB  
1157 C  CG1 . ILE A 145 ? 0.1377 0.1329 0.1518 0.0367  -0.0144 0.0092  146 ILE A CG1 
1158 C  CG2 . ILE A 145 ? 0.1165 0.1248 0.1928 0.0025  -0.0478 0.0089  146 ILE A CG2 
1159 C  CD1 . ILE A 145 ? 0.1417 0.1436 0.1757 0.0309  -0.0241 0.0122  146 ILE A CD1 
1160 N  N   . PHE A 146 ? 0.1134 0.0873 0.1127 0.0065  -0.0036 0.0020  147 PHE A N   
1161 C  CA  . PHE A 146 ? 0.1262 0.0925 0.1049 0.0146  -0.0083 0.0025  147 PHE A CA  
1162 C  C   . PHE A 146 ? 0.1244 0.0806 0.1344 0.0036  -0.0181 -0.0124 147 PHE A C   
1163 O  O   . PHE A 146 ? 0.1147 0.1183 0.1470 0.0008  -0.0190 -0.0051 147 PHE A O   
1164 C  CB  . PHE A 146 ? 0.1452 0.1129 0.0962 0.0006  -0.0107 0.0117  147 PHE A CB  
1165 C  CG  . PHE A 146 ? 0.1228 0.0851 0.1043 -0.0078 -0.0087 0.0148  147 PHE A CG  
1166 C  CD1 . PHE A 146 ? 0.1198 0.1199 0.1411 0.0055  -0.0254 0.0000  147 PHE A CD1 
1167 C  CD2 . PHE A 146 ? 0.1564 0.0969 0.1118 0.0023  -0.0134 0.0072  147 PHE A CD2 
1168 C  CE1 . PHE A 146 ? 0.1280 0.1155 0.1161 0.0063  -0.0194 0.0136  147 PHE A CE1 
1169 C  CE2 . PHE A 146 ? 0.1384 0.1135 0.1306 -0.0022 -0.0105 0.0197  147 PHE A CE2 
1170 C  CZ  . PHE A 146 ? 0.1383 0.1199 0.1187 -0.0104 -0.0033 0.0280  147 PHE A CZ  
1171 N  N   . LEU A 147 ? 0.1310 0.0948 0.1197 -0.0011 -0.0078 -0.0140 148 LEU A N   
1172 C  CA  . LEU A 147 ? 0.1569 0.0946 0.1079 -0.0069 -0.0168 -0.0102 148 LEU A CA  
1173 C  C   . LEU A 147 ? 0.1244 0.1132 0.1246 0.0032  -0.0132 -0.0196 148 LEU A C   
1174 O  O   . LEU A 147 ? 0.1327 0.1073 0.1601 0.0068  -0.0199 -0.0057 148 LEU A O   
1175 C  CB  . LEU A 147 ? 0.1333 0.1025 0.1338 -0.0044 -0.0006 -0.0100 148 LEU A CB  
1176 C  CG  . LEU A 147 ? 0.1806 0.0967 0.1153 -0.0089 -0.0147 -0.0068 148 LEU A CG  
1177 C  CD1 . LEU A 147 ? 0.2085 0.1023 0.1310 -0.0097 -0.0221 -0.0149 148 LEU A CD1 
1178 C  CD2 . LEU A 147 ? 0.1421 0.1213 0.1309 -0.0126 -0.0137 -0.0130 148 LEU A CD2 
1179 N  N   . LYS A 148 ? 0.1551 0.0907 0.1518 -0.0168 -0.0218 -0.0121 149 LYS A N   
1180 C  CA  . LYS A 148 ? 0.1698 0.0995 0.1485 0.0031  -0.0328 -0.0065 149 LYS A CA  
1181 C  C   . LYS A 148 ? 0.1659 0.1007 0.1621 -0.0044 -0.0374 0.0016  149 LYS A C   
1182 O  O   . LYS A 148 ? 0.1804 0.1371 0.1496 0.0262  -0.0333 -0.0079 149 LYS A O   
1183 C  CB  . LYS A 148 ? 0.2062 0.1459 0.1639 -0.0326 -0.0212 0.0100  149 LYS A CB  
1184 C  CG  . LYS A 148 ? 0.2188 0.1675 0.1967 -0.0272 -0.0137 0.0152  149 LYS A CG  
1185 C  CD  . LYS A 148 ? 0.3325 0.2710 0.2189 -0.0531 0.0184  0.0563  149 LYS A CD  
1186 C  CE  . LYS A 148 ? 0.3711 0.4762 0.3352 -0.1280 0.0230  0.2168  149 LYS A CE  
1187 N  NZ  . LYS A 148 ? 0.5320 0.6925 0.3792 -0.2098 0.0977  0.1882  149 LYS A NZ  
1188 N  N   . VAL A 149 ? 0.1921 0.1002 0.1682 0.0122  -0.0527 -0.0163 150 VAL A N   
1189 C  CA  . VAL A 149 ? 0.1967 0.1063 0.1460 0.0168  -0.0321 -0.0161 150 VAL A CA  
1190 C  C   . VAL A 149 ? 0.2073 0.1037 0.1917 -0.0111 -0.0445 -0.0029 150 VAL A C   
1191 O  O   . VAL A 149 ? 0.2226 0.1375 0.2167 -0.0084 -0.0557 0.0187  150 VAL A O   
1192 C  CB  . VAL A 149 ? 0.2018 0.1217 0.1650 0.0158  -0.0314 -0.0118 150 VAL A CB  
1193 C  CG1 . VAL A 149 ? 0.2406 0.1726 0.1725 0.0168  -0.0536 -0.0274 150 VAL A CG1 
1194 C  CG2 . VAL A 149 ? 0.2028 0.1769 0.2226 -0.0057 -0.0316 -0.0012 150 VAL A CG2 
1195 N  N   . GLY A 150 ? 0.1860 0.1300 0.1629 -0.0055 -0.0372 -0.0071 151 GLY A N   
1196 C  CA  . GLY A 150 ? 0.2282 0.1497 0.1738 -0.0454 -0.0623 0.0186  151 GLY A CA  
1197 C  C   . GLY A 150 ? 0.2111 0.1278 0.1599 -0.0345 -0.0386 0.0077  151 GLY A C   
1198 O  O   . GLY A 150 ? 0.1887 0.1394 0.1676 -0.0154 -0.0277 0.0060  151 GLY A O   
1199 N  N   A SER A 151 ? 0.2110 0.1607 0.1612 -0.0348 -0.0261 0.0131  152 SER A N   
1200 N  N   B SER A 151 ? 0.2050 0.1430 0.1700 -0.0363 -0.0406 0.0145  152 SER A N   
1201 C  CA  A SER A 151 ? 0.1773 0.1612 0.1913 -0.0302 -0.0178 0.0240  152 SER A CA  
1202 C  CA  B SER A 151 ? 0.1920 0.1461 0.2262 -0.0267 -0.0617 0.0088  152 SER A CA  
1203 C  C   A SER A 151 ? 0.1768 0.1455 0.1423 -0.0298 0.0032  -0.0207 152 SER A C   
1204 C  C   B SER A 151 ? 0.2003 0.1201 0.1709 -0.0087 -0.0457 -0.0205 152 SER A C   
1205 O  O   A SER A 151 ? 0.1453 0.1504 0.1400 -0.0029 -0.0322 -0.0063 152 SER A O   
1206 O  O   B SER A 151 ? 0.1504 0.1451 0.1709 -0.0186 -0.0190 -0.0108 152 SER A O   
1207 C  CB  A SER A 151 ? 0.2020 0.2333 0.2362 -0.0548 0.0517  -0.0348 152 SER A CB  
1208 C  CB  B SER A 151 ? 0.1696 0.1590 0.2694 -0.0186 -0.0715 -0.0318 152 SER A CB  
1209 O  OG  A SER A 151 ? 0.1866 0.3636 0.2201 -0.0478 0.0396  -0.0759 152 SER A OG  
1210 O  OG  B SER A 151 ? 0.1705 0.3220 0.3444 -0.0571 -0.0223 0.0884  152 SER A OG  
1211 N  N   . ALA A 152 ? 0.1680 0.1326 0.1590 -0.0245 -0.0401 -0.0184 153 ALA A N   
1212 C  CA  . ALA A 152 ? 0.1808 0.1326 0.1641 -0.0065 -0.0368 -0.0095 153 ALA A CA  
1213 C  C   . ALA A 152 ? 0.1424 0.1368 0.1547 -0.0036 -0.0190 -0.0073 153 ALA A C   
1214 O  O   . ALA A 152 ? 0.1639 0.1406 0.2307 -0.0122 -0.0019 -0.0030 153 ALA A O   
1215 C  CB  . ALA A 152 ? 0.2253 0.1712 0.1498 -0.0154 -0.0414 -0.0179 153 ALA A CB  
1216 N  N   . LYS A 153 ? 0.1558 0.1129 0.1578 0.0000  -0.0372 -0.0113 154 LYS A N   
1217 C  CA  . LYS A 153 ? 0.1460 0.1226 0.1472 0.0025  -0.0214 -0.0059 154 LYS A CA  
1218 C  C   . LYS A 153 ? 0.1437 0.1388 0.1448 -0.0005 -0.0004 -0.0069 154 LYS A C   
1219 O  O   . LYS A 153 ? 0.1366 0.1320 0.1508 -0.0022 -0.0225 0.0037  154 LYS A O   
1220 C  CB  . LYS A 153 ? 0.1547 0.1289 0.1453 -0.0059 -0.0304 -0.0096 154 LYS A CB  
1221 C  CG  . LYS A 153 ? 0.2010 0.1195 0.1684 0.0139  -0.0165 -0.0139 154 LYS A CG  
1222 C  CD  . LYS A 153 ? 0.2666 0.1404 0.1585 0.0000  -0.0034 -0.0200 154 LYS A CD  
1223 C  CE  . LYS A 153 ? 0.2883 0.1856 0.1604 0.0318  -0.0042 -0.0311 154 LYS A CE  
1224 N  NZ  . LYS A 153 ? 0.4016 0.2329 0.1851 0.0016  0.0391  -0.0189 154 LYS A NZ  
1225 N  N   . PRO A 154 ? 0.1312 0.1669 0.1321 -0.0089 -0.0052 0.0000  155 PRO A N   
1226 C  CA  . PRO A 154 ? 0.1419 0.1745 0.1456 -0.0179 -0.0128 0.0082  155 PRO A CA  
1227 C  C   . PRO A 154 ? 0.1213 0.1704 0.1429 0.0218  -0.0107 0.0171  155 PRO A C   
1228 O  O   . PRO A 154 ? 0.1376 0.1932 0.1420 0.0187  -0.0103 0.0222  155 PRO A O   
1229 C  CB  . PRO A 154 ? 0.1226 0.2382 0.1969 -0.0114 -0.0359 0.0178  155 PRO A CB  
1230 C  CG  . PRO A 154 ? 0.1312 0.2989 0.2854 -0.0287 -0.0502 0.0849  155 PRO A CG  
1231 C  CD  . PRO A 154 ? 0.1567 0.1981 0.1623 -0.0073 0.0148  0.0217  155 PRO A CD  
1232 N  N   . GLY A 155 ? 0.1268 0.1402 0.1852 0.0223  -0.0122 -0.0094 156 GLY A N   
1233 C  CA  . GLY A 155 ? 0.1465 0.1368 0.2251 0.0114  -0.0047 0.0104  156 GLY A CA  
1234 C  C   . GLY A 155 ? 0.1533 0.1292 0.1630 0.0142  -0.0126 0.0071  156 GLY A C   
1235 O  O   . GLY A 155 ? 0.1687 0.1283 0.2394 0.0130  0.0012  0.0256  156 GLY A O   
1236 N  N   . LEU A 156 ? 0.1359 0.1277 0.1198 0.0077  -0.0205 -0.0022 157 LEU A N   
1237 C  CA  . LEU A 156 ? 0.1316 0.1420 0.1210 0.0013  -0.0066 0.0025  157 LEU A CA  
1238 C  C   . LEU A 156 ? 0.1258 0.1107 0.1161 0.0057  -0.0236 0.0023  157 LEU A C   
1239 O  O   . LEU A 156 ? 0.1234 0.1391 0.1421 -0.0095 -0.0117 0.0061  157 LEU A O   
1240 C  CB  . LEU A 156 ? 0.1518 0.1562 0.1333 -0.0039 -0.0237 0.0027  157 LEU A CB  
1241 C  CG  . LEU A 156 ? 0.1349 0.1453 0.1549 -0.0052 -0.0283 -0.0038 157 LEU A CG  
1242 C  CD1 . LEU A 156 ? 0.1434 0.1657 0.1841 -0.0367 -0.0160 0.0044  157 LEU A CD1 
1243 C  CD2 . LEU A 156 ? 0.1646 0.1776 0.1333 0.0165  -0.0287 -0.0050 157 LEU A CD2 
1244 N  N   . GLN A 157 ? 0.1368 0.1348 0.1119 -0.0156 -0.0218 -0.0141 158 GLN A N   
1245 C  CA  . GLN A 157 ? 0.1208 0.1333 0.1322 -0.0312 -0.0111 -0.0074 158 GLN A CA  
1246 C  C   . GLN A 157 ? 0.1244 0.1553 0.1251 -0.0011 -0.0171 0.0109  158 GLN A C   
1247 O  O   . GLN A 157 ? 0.1342 0.1539 0.1239 -0.0195 -0.0063 -0.0021 158 GLN A O   
1248 C  CB  . GLN A 157 ? 0.1134 0.1546 0.1676 -0.0217 -0.0208 -0.0151 158 GLN A CB  
1249 C  CG  . GLN A 157 ? 0.1581 0.1540 0.1581 -0.0093 -0.0288 -0.0243 158 GLN A CG  
1250 C  CD  . GLN A 157 ? 0.1902 0.1416 0.1044 -0.0276 -0.0055 -0.0150 158 GLN A CD  
1251 O  OE1 . GLN A 157 ? 0.2046 0.1357 0.1244 -0.0062 -0.0163 -0.0023 158 GLN A OE1 
1252 N  NE2 . GLN A 157 ? 0.1834 0.1648 0.1533 -0.0380 -0.0025 -0.0332 158 GLN A NE2 
1253 N  N   . LYS A 158 ? 0.1376 0.1350 0.1312 0.0042  -0.0275 0.0130  159 LYS A N   
1254 C  CA  . LYS A 158 ? 0.1533 0.1438 0.1694 -0.0032 -0.0274 0.0199  159 LYS A CA  
1255 C  C   . LYS A 158 ? 0.1779 0.1282 0.1180 -0.0047 -0.0111 0.0027  159 LYS A C   
1256 O  O   . LYS A 158 ? 0.1694 0.1594 0.1434 -0.0225 -0.0249 0.0075  159 LYS A O   
1257 C  CB  . LYS A 158 ? 0.2036 0.1617 0.1777 0.0266  -0.0469 0.0198  159 LYS A CB  
1258 C  CG  . LYS A 158 ? 0.2579 0.1738 0.2764 -0.0228 -0.0536 0.0367  159 LYS A CG  
1259 C  CD  . LYS A 158 ? 0.3231 0.1890 0.3270 0.0107  -0.0857 0.0326  159 LYS A CD  
1260 C  CE  . LYS A 158 ? 0.5381 0.3116 0.2985 -0.0828 -0.0534 0.0759  159 LYS A CE  
1261 N  NZ  . LYS A 158 ? 0.3592 0.3934 0.2984 0.0482  -0.0245 0.1459  159 LYS A NZ  
1262 N  N   . VAL A 159 ? 0.1464 0.1293 0.1322 -0.0077 -0.0324 0.0071  160 VAL A N   
1263 C  CA  . VAL A 159 ? 0.1392 0.1322 0.1237 -0.0227 -0.0085 0.0077  160 VAL A CA  
1264 C  C   . VAL A 159 ? 0.1309 0.1361 0.1250 -0.0223 -0.0264 0.0044  160 VAL A C   
1265 O  O   . VAL A 159 ? 0.1447 0.1363 0.1744 -0.0225 -0.0106 0.0111  160 VAL A O   
1266 C  CB  . VAL A 159 ? 0.1447 0.1514 0.1309 -0.0070 -0.0284 -0.0108 160 VAL A CB  
1267 C  CG1 . VAL A 159 ? 0.1520 0.1967 0.1662 -0.0399 -0.0436 0.0065  160 VAL A CG1 
1268 C  CG2 . VAL A 159 ? 0.2337 0.1781 0.1351 0.0283  -0.0198 -0.0325 160 VAL A CG2 
1269 N  N   . VAL A 160 ? 0.1392 0.1129 0.1303 -0.0098 -0.0241 -0.0060 161 VAL A N   
1270 C  CA  . VAL A 160 ? 0.1860 0.1357 0.1302 0.0038  -0.0059 -0.0047 161 VAL A CA  
1271 C  C   . VAL A 160 ? 0.1504 0.1213 0.1342 -0.0182 0.0087  -0.0094 161 VAL A C   
1272 O  O   . VAL A 160 ? 0.1669 0.1558 0.1350 0.0064  0.0204  -0.0055 161 VAL A O   
1273 C  CB  . VAL A 160 ? 0.2913 0.1491 0.2167 0.0029  0.0386  -0.0024 161 VAL A CB  
1274 C  CG1 . VAL A 160 ? 0.4134 0.2314 0.1892 0.1218  0.0697  0.0628  161 VAL A CG1 
1275 C  CG2 . VAL A 160 ? 0.2107 0.2143 0.2305 0.0857  0.0441  -0.0029 161 VAL A CG2 
1276 N  N   . ASP A 161 ? 0.1605 0.1529 0.1188 -0.0249 -0.0198 -0.0085 162 ASP A N   
1277 C  CA  . ASP A 161 ? 0.1479 0.1841 0.1278 -0.0348 -0.0078 -0.0083 162 ASP A CA  
1278 C  C   . ASP A 161 ? 0.1583 0.1852 0.1464 -0.0428 0.0070  -0.0095 162 ASP A C   
1279 O  O   . ASP A 161 ? 0.2142 0.2493 0.1483 -0.0532 0.0197  -0.0099 162 ASP A O   
1280 C  CB  . ASP A 161 ? 0.1474 0.2501 0.1605 -0.0565 -0.0168 -0.0111 162 ASP A CB  
1281 C  CG  . ASP A 161 ? 0.1643 0.2445 0.1824 -0.0451 -0.0331 0.0002  162 ASP A CG  
1282 O  OD1 . ASP A 161 ? 0.2280 0.2422 0.1981 -0.0458 -0.0232 0.0072  162 ASP A OD1 
1283 O  OD2 . ASP A 161 ? 0.1608 0.2989 0.1932 -0.0486 -0.0103 -0.0285 162 ASP A OD2 
1284 N  N   A VAL A 162 ? 0.1581 0.1568 0.1686 -0.0479 -0.0489 0.0226  163 VAL A N   
1285 N  N   B VAL A 162 ? 0.1632 0.1723 0.1203 -0.0414 -0.0206 0.0111  163 VAL A N   
1286 C  CA  A VAL A 162 ? 0.1775 0.1802 0.1542 -0.0446 -0.0335 0.0348  163 VAL A CA  
1287 C  CA  B VAL A 162 ? 0.1302 0.1550 0.1813 0.0008  0.0085  0.0262  163 VAL A CA  
1288 C  C   A VAL A 162 ? 0.1730 0.1471 0.1683 -0.0468 -0.0142 0.0185  163 VAL A C   
1289 C  C   B VAL A 162 ? 0.1329 0.1946 0.1031 -0.0403 -0.0198 0.0060  163 VAL A C   
1290 O  O   A VAL A 162 ? 0.1758 0.1698 0.1351 -0.0383 -0.0147 0.0332  163 VAL A O   
1291 O  O   B VAL A 162 ? 0.1246 0.1955 0.1687 -0.0385 -0.0097 0.0047  163 VAL A O   
1292 C  CB  A VAL A 162 ? 0.1949 0.1859 0.2029 -0.0243 -0.0185 0.0281  163 VAL A CB  
1293 C  CB  B VAL A 162 ? 0.1406 0.1395 0.1819 0.0063  0.0053  0.0666  163 VAL A CB  
1294 C  CG1 A VAL A 162 ? 0.1733 0.1985 0.2247 -0.0247 -0.0154 -0.0253 163 VAL A CG1 
1295 C  CG1 B VAL A 162 ? 0.1264 0.1558 0.2518 -0.0116 0.0013  0.0240  163 VAL A CG1 
1296 C  CG2 A VAL A 162 ? 0.2582 0.2207 0.1903 -0.0417 0.0268  0.0249  163 VAL A CG2 
1297 C  CG2 B VAL A 162 ? 0.1744 0.1305 0.1977 -0.0104 -0.0172 0.0322  163 VAL A CG2 
1298 N  N   . LEU A 163 ? 0.1386 0.1657 0.1278 -0.0184 -0.0091 -0.0003 164 LEU A N   
1299 C  CA  . LEU A 163 ? 0.1476 0.1756 0.1212 -0.0319 -0.0025 0.0035  164 LEU A CA  
1300 C  C   . LEU A 163 ? 0.1580 0.1838 0.1082 -0.0134 -0.0015 -0.0108 164 LEU A C   
1301 O  O   . LEU A 163 ? 0.1604 0.1896 0.1224 -0.0267 -0.0023 -0.0038 164 LEU A O   
1302 C  CB  . LEU A 163 ? 0.1473 0.1632 0.1237 -0.0137 0.0017  0.0125  164 LEU A CB  
1303 C  CG  . LEU A 163 ? 0.1630 0.1517 0.1238 -0.0108 0.0037  0.0111  164 LEU A CG  
1304 C  CD1 . LEU A 163 ? 0.1766 0.1788 0.1551 0.0144  -0.0005 0.0476  164 LEU A CD1 
1305 C  CD2 . LEU A 163 ? 0.1653 0.1694 0.1285 -0.0139 -0.0135 0.0050  164 LEU A CD2 
1306 N  N   . ASP A 164 ? 0.2010 0.1619 0.1190 -0.0176 0.0089  -0.0193 165 ASP A N   
1307 C  CA  . ASP A 164 ? 0.2498 0.2194 0.1164 -0.0292 0.0217  -0.0279 165 ASP A CA  
1308 C  C   . ASP A 164 ? 0.2174 0.2555 0.1012 -0.0345 0.0110  -0.0103 165 ASP A C   
1309 O  O   . ASP A 164 ? 0.2814 0.2601 0.1781 -0.0220 0.0741  -0.0221 165 ASP A O   
1310 C  CB  . ASP A 164 ? 0.2955 0.2817 0.1601 -0.0132 0.0026  -0.0873 165 ASP A CB  
1311 C  CG  . ASP A 164 ? 0.2902 0.3720 0.2060 -0.0949 -0.0302 -0.0179 165 ASP A CG  
1312 O  OD1 . ASP A 164 ? 0.2800 0.5032 0.2452 -0.1176 -0.0023 0.0049  165 ASP A OD1 
1313 O  OD2 . ASP A 164 ? 0.3888 0.6161 0.2141 -0.1034 0.0348  -0.0653 165 ASP A OD2 
1314 N  N   . SER A 165 ? 0.1514 0.2355 0.1256 -0.0285 -0.0076 0.0088  166 SER A N   
1315 C  CA  . SER A 165 ? 0.1565 0.2611 0.1504 -0.0458 -0.0143 0.0256  166 SER A CA  
1316 C  C   . SER A 165 ? 0.1617 0.2153 0.1086 -0.0387 0.0107  0.0238  166 SER A C   
1317 O  O   . SER A 165 ? 0.1829 0.2405 0.1483 -0.0469 -0.0046 0.0483  166 SER A O   
1318 C  CB  . SER A 165 ? 0.1880 0.2817 0.1502 -0.0311 -0.0326 0.0207  166 SER A CB  
1319 O  OG  . SER A 165 ? 0.1896 0.2426 0.1838 -0.0323 -0.0017 0.0355  166 SER A OG  
1320 N  N   . ILE A 166 ? 0.1529 0.1948 0.0976 -0.0297 0.0031  0.0035  167 ILE A N   
1321 C  CA  . ILE A 166 ? 0.1361 0.1971 0.1412 -0.0227 -0.0155 -0.0080 167 ILE A CA  
1322 C  C   . ILE A 166 ? 0.1551 0.1784 0.1186 -0.0190 0.0041  -0.0151 167 ILE A C   
1323 O  O   . ILE A 166 ? 0.1571 0.1975 0.1188 -0.0179 0.0037  -0.0047 167 ILE A O   
1324 C  CB  . ILE A 166 ? 0.1635 0.1698 0.1460 -0.0188 -0.0023 0.0122  167 ILE A CB  
1325 C  CG1 . ILE A 166 ? 0.1389 0.1910 0.1244 -0.0309 0.0044  -0.0072 167 ILE A CG1 
1326 C  CG2 . ILE A 166 ? 0.1866 0.1610 0.1845 -0.0403 -0.0054 0.0308  167 ILE A CG2 
1327 C  CD1 . ILE A 166 ? 0.1702 0.2068 0.1361 -0.0368 0.0113  -0.0211 167 ILE A CD1 
1328 N  N   . LYS A 167 ? 0.1805 0.1899 0.1302 0.0015  0.0051  -0.0165 168 LYS A N   
1329 C  CA  . LYS A 167 ? 0.1926 0.2086 0.1167 0.0057  -0.0051 -0.0162 168 LYS A CA  
1330 C  C   . LYS A 167 ? 0.2074 0.2070 0.1401 0.0048  -0.0117 -0.0087 168 LYS A C   
1331 O  O   . LYS A 167 ? 0.1757 0.2570 0.1531 0.0144  -0.0052 0.0054  168 LYS A O   
1332 C  CB  . LYS A 167 ? 0.2420 0.2567 0.1680 0.0155  0.0228  -0.0666 168 LYS A CB  
1333 C  CG  . LYS A 167 ? 0.2857 0.2518 0.2329 0.0254  -0.0344 -0.0573 168 LYS A CG  
1334 C  CD  . LYS A 167 ? 0.3432 0.2639 0.2559 0.0364  -0.0710 -0.0829 168 LYS A CD  
1335 C  CE  . LYS A 167 ? 0.5116 0.4797 0.4085 0.1919  -0.0986 -0.0928 168 LYS A CE  
1336 N  NZ  . LYS A 167 ? 0.6512 0.5375 0.5291 0.1324  0.1547  -0.0472 168 LYS A NZ  
1337 N  N   . THR A 168 ? 0.1623 0.2452 0.1497 0.0012  -0.0057 -0.0013 169 THR A N   
1338 C  CA  . THR A 168 ? 0.1630 0.2550 0.1280 -0.0158 0.0084  -0.0057 169 THR A CA  
1339 C  C   . THR A 168 ? 0.1531 0.2548 0.1655 -0.0027 0.0069  0.0147  169 THR A C   
1340 O  O   . THR A 168 ? 0.1650 0.2207 0.1479 -0.0093 0.0072  0.0035  169 THR A O   
1341 C  CB  . THR A 168 ? 0.2042 0.2986 0.1279 -0.0183 0.0177  -0.0035 169 THR A CB  
1342 O  OG1 . THR A 168 ? 0.2268 0.3371 0.1296 -0.0269 0.0134  0.0048  169 THR A OG1 
1343 C  CG2 . THR A 168 ? 0.2499 0.3373 0.1518 0.0272  0.0182  -0.0745 169 THR A CG2 
1344 N  N   . LYS A 169 ? 0.1571 0.2509 0.1756 -0.0148 -0.0074 -0.0262 170 LYS A N   
1345 C  CA  . LYS A 169 ? 0.1585 0.2355 0.1454 -0.0291 0.0210  -0.0026 170 LYS A CA  
1346 C  C   . LYS A 169 ? 0.1194 0.2792 0.1939 -0.0363 0.0413  0.0184  170 LYS A C   
1347 O  O   . LYS A 169 ? 0.1615 0.3343 0.1729 -0.0537 0.0316  0.0149  170 LYS A O   
1348 C  CB  . LYS A 169 ? 0.1532 0.3037 0.1790 -0.0005 -0.0041 -0.0237 170 LYS A CB  
1349 C  CG  . LYS A 169 ? 0.1788 0.3088 0.1732 -0.0324 0.0058  -0.0108 170 LYS A CG  
1350 C  CD  . LYS A 169 ? 0.2043 0.3841 0.3163 -0.0122 -0.0389 -0.0767 170 LYS A CD  
1351 C  CE  . LYS A 169 ? 0.2823 0.3869 0.5657 -0.0740 -0.1048 -0.0463 170 LYS A CE  
1352 N  NZ  . LYS A 169 ? 0.3022 0.5938 0.6732 -0.0926 -0.1251 0.1368  170 LYS A NZ  
1353 N  N   . GLY A 170 ? 0.1589 0.2049 0.1770 -0.0376 0.0013  0.0212  171 GLY A N   
1354 C  CA  . GLY A 170 ? 0.1823 0.2129 0.2401 -0.0571 -0.0167 0.0190  171 GLY A CA  
1355 C  C   . GLY A 170 ? 0.2187 0.2314 0.2091 -0.0677 0.0133  0.0683  171 GLY A C   
1356 O  O   . GLY A 170 ? 0.2746 0.2220 0.2854 -0.0841 -0.0682 0.0748  171 GLY A O   
1357 N  N   . LYS A 171 ? 0.1653 0.2188 0.1489 -0.0508 0.0077  0.0223  172 LYS A N   
1358 C  CA  . LYS A 171 ? 0.1700 0.1989 0.1569 -0.0226 0.0176  0.0348  172 LYS A CA  
1359 C  C   . LYS A 171 ? 0.1470 0.1884 0.1474 -0.0425 0.0175  0.0421  172 LYS A C   
1360 O  O   . LYS A 171 ? 0.1646 0.2311 0.1416 -0.0271 0.0172  0.0367  172 LYS A O   
1361 C  CB  . LYS A 171 ? 0.1683 0.2197 0.1831 -0.0193 -0.0168 0.0116  172 LYS A CB  
1362 C  CG  . LYS A 171 ? 0.1903 0.2775 0.3287 -0.0030 0.0182  -0.0961 172 LYS A CG  
1363 C  CD  . LYS A 171 ? 0.2476 0.3368 0.2778 -0.0208 0.0305  -0.0942 172 LYS A CD  
1364 C  CE  . LYS A 171 ? 0.3025 0.4332 0.5224 0.0573  -0.0725 -0.0073 172 LYS A CE  
1365 N  NZ  . LYS A 171 ? 0.5854 0.4967 0.3452 -0.1247 0.1653  -0.0827 172 LYS A NZ  
1366 N  N   . SER A 172 ? 0.1697 0.2052 0.1783 -0.0413 0.0066  0.0188  173 SER A N   
1367 C  CA  . SER A 172 ? 0.1732 0.1838 0.1550 -0.0144 0.0058  0.0409  173 SER A CA  
1368 C  C   . SER A 172 ? 0.1805 0.2147 0.1247 -0.0223 0.0182  0.0568  173 SER A C   
1369 O  O   . SER A 172 ? 0.2070 0.2594 0.1252 -0.0240 0.0116  0.0599  173 SER A O   
1370 C  CB  . SER A 172 ? 0.2523 0.1694 0.2165 -0.0388 0.0312  0.0467  173 SER A CB  
1371 O  OG  . SER A 172 ? 0.2605 0.2224 0.2840 -0.0288 0.0606  0.0800  173 SER A OG  
1372 N  N   . ALA A 173 ? 0.1686 0.1932 0.1551 -0.0040 -0.0074 0.0253  174 ALA A N   
1373 C  CA  . ALA A 173 ? 0.1928 0.2630 0.1138 0.0171  -0.0026 -0.0002 174 ALA A CA  
1374 C  C   . ALA A 173 ? 0.1562 0.2752 0.0939 0.0168  0.0034  0.0436  174 ALA A C   
1375 O  O   . ALA A 173 ? 0.2120 0.2017 0.1040 0.0212  0.0062  0.0381  174 ALA A O   
1376 C  CB  . ALA A 173 ? 0.1612 0.2856 0.2189 0.0117  -0.0295 -0.0413 174 ALA A CB  
1377 N  N   A ASP A 174 ? 0.2020 0.3063 0.1561 0.0884  0.0095  0.0560  175 ASP A N   
1378 N  N   B ASP A 174 ? 0.2214 0.2786 0.1264 0.0395  -0.0039 0.0589  175 ASP A N   
1379 C  CA  A ASP A 174 ? 0.1784 0.2922 0.2154 0.0826  0.0229  0.0761  175 ASP A CA  
1380 C  CA  B ASP A 174 ? 0.2283 0.2616 0.0655 0.0118  0.0148  0.0663  175 ASP A CA  
1381 C  C   A ASP A 174 ? 0.2034 0.2660 0.1208 0.0414  0.0072  0.0033  175 ASP A C   
1382 C  C   B ASP A 174 ? 0.1962 0.2422 0.0996 0.0013  0.0113  0.0143  175 ASP A C   
1383 O  O   A ASP A 174 ? 0.2262 0.3063 0.1415 0.0700  -0.0513 -0.0413 175 ASP A O   
1384 O  O   B ASP A 174 ? 0.1913 0.2614 0.1580 0.0147  0.0107  0.0047  175 ASP A O   
1385 C  CB  A ASP A 174 ? 0.1698 0.4458 0.2366 0.0937  0.0244  0.1207  175 ASP A CB  
1386 C  CB  B ASP A 174 ? 0.2982 0.3009 0.1007 0.0402  0.0081  0.0681  175 ASP A CB  
1387 C  CG  A ASP A 174 ? 0.3201 0.3990 0.2511 0.0601  -0.0752 0.2466  175 ASP A CG  
1388 C  CG  B ASP A 174 ? 0.4066 0.3041 0.1610 -0.0308 0.0184  0.0050  175 ASP A CG  
1389 O  OD1 A ASP A 174 ? 0.4579 0.4605 0.2573 -0.0294 0.1418  0.1153  175 ASP A OD1 
1390 O  OD1 B ASP A 174 ? 0.4991 0.5039 0.1917 -0.1347 0.0869  0.0518  175 ASP A OD1 
1391 O  OD2 A ASP A 174 ? 0.4372 0.6391 0.3278 -0.0370 0.0702  0.2130  175 ASP A OD2 
1392 O  OD2 B ASP A 174 ? 0.3368 0.5637 0.2326 -0.0955 0.1043  -0.0335 175 ASP A OD2 
1393 N  N   . PHE A 175 ? 0.1831 0.1874 0.1093 0.0157  0.0107  0.0430  176 PHE A N   
1394 C  CA  . PHE A 175 ? 0.1712 0.1775 0.1007 -0.0055 -0.0179 0.0237  176 PHE A CA  
1395 C  C   . PHE A 175 ? 0.1483 0.1479 0.1417 -0.0141 -0.0288 0.0165  176 PHE A C   
1396 O  O   . PHE A 175 ? 0.1741 0.1865 0.1429 0.0353  -0.0293 0.0010  176 PHE A O   
1397 C  CB  . PHE A 175 ? 0.1639 0.1450 0.1398 0.0001  -0.0284 0.0234  176 PHE A CB  
1398 C  CG  . PHE A 175 ? 0.1348 0.1503 0.1587 0.0029  -0.0040 0.0064  176 PHE A CG  
1399 C  CD1 . PHE A 175 ? 0.1725 0.1536 0.1896 0.0055  0.0070  -0.0083 176 PHE A CD1 
1400 C  CD2 . PHE A 175 ? 0.1346 0.1619 0.1540 0.0073  -0.0128 0.0248  176 PHE A CD2 
1401 C  CE1 . PHE A 175 ? 0.1913 0.1683 0.1666 -0.0146 0.0064  0.0163  176 PHE A CE1 
1402 C  CE2 . PHE A 175 ? 0.1837 0.1641 0.1840 0.0095  -0.0167 0.0307  176 PHE A CE2 
1403 C  CZ  . PHE A 175 ? 0.1998 0.1432 0.1820 0.0195  -0.0024 0.0223  176 PHE A CZ  
1404 N  N   . THR A 176 ? 0.1549 0.1786 0.1337 -0.0108 -0.0366 0.0140  177 THR A N   
1405 C  CA  . THR A 176 ? 0.1492 0.1495 0.1461 -0.0118 -0.0242 0.0439  177 THR A CA  
1406 C  C   . THR A 176 ? 0.1629 0.1320 0.1102 -0.0071 -0.0307 0.0381  177 THR A C   
1407 O  O   . THR A 176 ? 0.1898 0.1411 0.1287 -0.0068 -0.0163 0.0229  177 THR A O   
1408 C  CB  . THR A 176 ? 0.1985 0.1817 0.1479 -0.0284 -0.0537 0.0577  177 THR A CB  
1409 O  OG1 . THR A 176 ? 0.2451 0.2219 0.1205 0.0332  -0.0416 0.0458  177 THR A OG1 
1410 C  CG2 . THR A 176 ? 0.2253 0.2568 0.2868 -0.0765 -0.0688 0.1356  177 THR A CG2 
1411 N  N   . ASN A 177 ? 0.1410 0.1322 0.1412 -0.0190 -0.0226 0.0279  178 ASN A N   
1412 C  CA  . ASN A 177 ? 0.1295 0.1542 0.1547 -0.0046 -0.0190 0.0286  178 ASN A CA  
1413 C  C   . ASN A 177 ? 0.1779 0.1716 0.1590 -0.0381 -0.0432 0.0447  178 ASN A C   
1414 O  O   . ASN A 177 ? 0.1892 0.2036 0.2573 -0.0574 -0.0656 0.0897  178 ASN A O   
1415 C  CB  . ASN A 177 ? 0.1556 0.1646 0.1991 -0.0238 -0.0573 0.0601  178 ASN A CB  
1416 C  CG  . ASN A 177 ? 0.1502 0.1709 0.1608 0.0107  -0.0268 0.0226  178 ASN A CG  
1417 O  OD1 . ASN A 177 ? 0.1830 0.1949 0.2300 0.0155  0.0055  0.0494  178 ASN A OD1 
1418 N  ND2 . ASN A 177 ? 0.1939 0.1799 0.1415 -0.0031 -0.0447 0.0322  178 ASN A ND2 
1419 N  N   . PHE A 178 ? 0.1700 0.1471 0.1070 -0.0156 -0.0214 0.0343  179 PHE A N   
1420 C  CA  . PHE A 178 ? 0.1687 0.1458 0.0878 -0.0160 -0.0017 0.0367  179 PHE A CA  
1421 C  C   . PHE A 178 ? 0.1682 0.1285 0.1011 -0.0069 -0.0078 0.0281  179 PHE A C   
1422 O  O   . PHE A 178 ? 0.2106 0.1342 0.1301 -0.0151 -0.0140 0.0109  179 PHE A O   
1423 C  CB  . PHE A 178 ? 0.1637 0.1486 0.1307 0.0079  -0.0110 0.0368  179 PHE A CB  
1424 C  CG  . PHE A 178 ? 0.1757 0.1368 0.1224 -0.0039 -0.0125 0.0238  179 PHE A CG  
1425 C  CD1 . PHE A 178 ? 0.1820 0.1376 0.1342 -0.0139 0.0003  0.0209  179 PHE A CD1 
1426 C  CD2 . PHE A 178 ? 0.1411 0.1337 0.1161 0.0024  -0.0109 0.0170  179 PHE A CD2 
1427 C  CE1 . PHE A 178 ? 0.2084 0.1268 0.1368 -0.0122 0.0019  0.0166  179 PHE A CE1 
1428 C  CE2 . PHE A 178 ? 0.1234 0.1370 0.1723 0.0058  0.0013  0.0352  179 PHE A CE2 
1429 C  CZ  . PHE A 178 ? 0.1524 0.1506 0.1335 0.0013  -0.0044 0.0156  179 PHE A CZ  
1430 N  N   . ASP A 179 ? 0.1306 0.1465 0.1070 -0.0080 -0.0114 0.0272  180 ASP A N   
1431 C  CA  . ASP A 179 ? 0.1284 0.1538 0.1188 0.0060  -0.0023 0.0267  180 ASP A CA  
1432 C  C   . ASP A 179 ? 0.1499 0.1292 0.1188 0.0040  -0.0078 0.0111  180 ASP A C   
1433 O  O   . ASP A 179 ? 0.1395 0.1307 0.1337 -0.0006 -0.0087 0.0069  180 ASP A O   
1434 C  CB  . ASP A 179 ? 0.1403 0.2075 0.1504 -0.0070 -0.0132 0.0348  180 ASP A CB  
1435 C  CG  . ASP A 179 ? 0.1554 0.2469 0.1881 0.0223  -0.0187 0.0241  180 ASP A CG  
1436 O  OD1 . ASP A 179 ? 0.1513 0.1786 0.1842 0.0188  0.0073  0.0240  180 ASP A OD1 
1437 O  OD2 . ASP A 179 ? 0.1547 0.5263 0.2850 0.0620  -0.0256 -0.0399 180 ASP A OD2 
1438 N  N   . PRO A 180 ? 0.1506 0.1318 0.1136 -0.0053 -0.0100 0.0184  181 PRO A N   
1439 C  CA  . PRO A 180 ? 0.1449 0.1579 0.1235 -0.0151 -0.0185 0.0232  181 PRO A CA  
1440 C  C   . PRO A 180 ? 0.1298 0.1581 0.1129 0.0103  -0.0006 0.0100  181 PRO A C   
1441 O  O   . PRO A 180 ? 0.1653 0.1506 0.1306 0.0000  -0.0160 0.0217  181 PRO A O   
1442 C  CB  . PRO A 180 ? 0.1532 0.1668 0.1611 -0.0064 -0.0167 -0.0012 181 PRO A CB  
1443 C  CG  . PRO A 180 ? 0.2018 0.1385 0.1540 -0.0078 -0.0251 0.0114  181 PRO A CG  
1444 C  CD  . PRO A 180 ? 0.1698 0.1326 0.1411 -0.0151 -0.0223 0.0212  181 PRO A CD  
1445 N  N   . ARG A 181 ? 0.1293 0.1451 0.1272 0.0042  -0.0053 0.0100  182 ARG A N   
1446 C  CA  . ARG A 181 ? 0.1447 0.1476 0.1273 0.0013  0.0111  -0.0099 182 ARG A CA  
1447 C  C   . ARG A 181 ? 0.1180 0.1576 0.1174 0.0073  -0.0266 0.0185  182 ARG A C   
1448 O  O   . ARG A 181 ? 0.1615 0.1551 0.1316 0.0099  -0.0086 0.0245  182 ARG A O   
1449 C  CB  . ARG A 181 ? 0.1630 0.1390 0.1605 0.0192  0.0034  -0.0006 182 ARG A CB  
1450 C  CG  . ARG A 181 ? 0.2041 0.1377 0.1632 0.0311  0.0167  0.0057  182 ARG A CG  
1451 C  CD  . ARG A 181 ? 0.2079 0.1921 0.2156 0.0475  0.0476  0.0152  182 ARG A CD  
1452 N  NE  . ARG A 181 ? 0.1869 0.1877 0.2262 0.0435  0.0486  0.0311  182 ARG A NE  
1453 C  CZ  . ARG A 181 ? 0.2235 0.2024 0.2481 0.0545  0.0464  0.0288  182 ARG A CZ  
1454 N  NH1 . ARG A 181 ? 0.2181 0.2982 0.3929 0.0885  0.0873  0.0225  182 ARG A NH1 
1455 N  NH2 . ARG A 181 ? 0.2319 0.2996 0.2641 0.0847  0.0234  0.0646  182 ARG A NH2 
1456 N  N   . GLY A 182 ? 0.1381 0.1453 0.1295 0.0154  -0.0215 0.0012  183 GLY A N   
1457 C  CA  . GLY A 182 ? 0.1873 0.1346 0.1444 0.0282  -0.0247 0.0024  183 GLY A CA  
1458 C  C   . GLY A 182 ? 0.1837 0.1366 0.1550 0.0193  -0.0248 0.0096  183 GLY A C   
1459 O  O   . GLY A 182 ? 0.2031 0.1446 0.1410 0.0092  -0.0172 0.0049  183 GLY A O   
1460 N  N   . LEU A 183 ? 0.1433 0.1487 0.1272 0.0247  -0.0148 0.0124  184 LEU A N   
1461 C  CA  . LEU A 183 ? 0.1496 0.1453 0.1275 0.0228  -0.0058 0.0146  184 LEU A CA  
1462 C  C   . LEU A 183 ? 0.1507 0.1467 0.1353 0.0151  -0.0147 0.0026  184 LEU A C   
1463 O  O   . LEU A 183 ? 0.1885 0.1644 0.1550 0.0414  -0.0151 0.0242  184 LEU A O   
1464 C  CB  . LEU A 183 ? 0.1597 0.1536 0.1169 0.0102  -0.0200 0.0265  184 LEU A CB  
1465 C  CG  . LEU A 183 ? 0.1610 0.1702 0.1251 0.0359  -0.0030 0.0258  184 LEU A CG  
1466 C  CD1 . LEU A 183 ? 0.1664 0.2243 0.1312 0.0116  0.0063  0.0278  184 LEU A CD1 
1467 C  CD2 . LEU A 183 ? 0.2039 0.1751 0.1777 0.0533  -0.0083 0.0021  184 LEU A CD2 
1468 N  N   . LEU A 184 ? 0.1643 0.1467 0.1147 0.0078  0.0167  0.0252  185 LEU A N   
1469 C  CA  . LEU A 184 ? 0.1612 0.1504 0.1159 -0.0095 0.0107  0.0313  185 LEU A CA  
1470 C  C   . LEU A 184 ? 0.1770 0.1558 0.1122 -0.0273 -0.0110 0.0194  185 LEU A C   
1471 O  O   . LEU A 184 ? 0.2780 0.1898 0.1899 -0.0839 -0.1016 0.0534  185 LEU A O   
1472 C  CB  . LEU A 184 ? 0.1409 0.1536 0.1460 -0.0194 -0.0063 0.0055  185 LEU A CB  
1473 C  CG  . LEU A 184 ? 0.1398 0.1659 0.2108 -0.0178 0.0195  0.0102  185 LEU A CG  
1474 C  CD1 . LEU A 184 ? 0.2258 0.1522 0.2506 -0.0076 0.0450  0.0022  185 LEU A CD1 
1475 C  CD2 . LEU A 184 ? 0.1697 0.1727 0.2866 -0.0059 -0.0580 0.0113  185 LEU A CD2 
1476 N  N   . PRO A 185 ? 0.1406 0.1485 0.1289 -0.0128 -0.0215 0.0190  186 PRO A N   
1477 C  CA  . PRO A 185 ? 0.1504 0.1436 0.1313 -0.0089 -0.0103 0.0240  186 PRO A CA  
1478 C  C   . PRO A 185 ? 0.1393 0.1357 0.1298 -0.0071 -0.0304 0.0182  186 PRO A C   
1479 O  O   . PRO A 185 ? 0.1242 0.1418 0.2224 -0.0060 -0.0370 0.0298  186 PRO A O   
1480 C  CB  . PRO A 185 ? 0.1427 0.1651 0.1719 0.0088  -0.0179 0.0220  186 PRO A CB  
1481 C  CG  . PRO A 185 ? 0.1248 0.1744 0.1221 0.0145  -0.0227 0.0074  186 PRO A CG  
1482 C  CD  . PRO A 185 ? 0.1354 0.1745 0.1049 0.0118  -0.0193 0.0034  186 PRO A CD  
1483 N  N   . GLU A 186 ? 0.1610 0.1441 0.1483 -0.0140 -0.0149 0.0335  187 GLU A N   
1484 C  CA  . GLU A 186 ? 0.1233 0.1755 0.1978 -0.0099 -0.0204 0.0122  187 GLU A CA  
1485 C  C   . GLU A 186 ? 0.1169 0.1988 0.1799 -0.0012 -0.0181 0.0297  187 GLU A C   
1486 O  O   . GLU A 186 ? 0.1216 0.2226 0.2300 0.0142  -0.0144 -0.0012 187 GLU A O   
1487 C  CB  . GLU A 186 ? 0.1481 0.2185 0.2212 -0.0362 -0.0161 0.0273  187 GLU A CB  
1488 C  CG  . GLU A 186 ? 0.2242 0.1910 0.2721 -0.0152 -0.0646 0.0079  187 GLU A CG  
1489 C  CD  . GLU A 186 ? 0.1905 0.2143 0.3273 0.0067  -0.0616 0.0164  187 GLU A CD  
1490 O  OE1 . GLU A 186 ? 0.2167 0.2548 0.3552 -0.0651 -0.0630 0.0702  187 GLU A OE1 
1491 O  OE2 . GLU A 186 ? 0.2693 0.2233 0.4724 -0.0283 -0.1277 -0.0079 187 GLU A OE2 
1492 N  N   . SER A 187 ? 0.1025 0.2068 0.1623 -0.0170 -0.0269 0.0139  188 SER A N   
1493 C  CA  . SER A 187 ? 0.1286 0.1888 0.1659 -0.0298 -0.0253 0.0173  188 SER A CA  
1494 C  C   . SER A 187 ? 0.0973 0.2100 0.1557 -0.0201 -0.0065 0.0150  188 SER A C   
1495 O  O   . SER A 187 ? 0.1135 0.2229 0.1827 -0.0114 0.0075  -0.0198 188 SER A O   
1496 C  CB  . SER A 187 ? 0.1750 0.2597 0.1469 -0.0161 -0.0129 0.0462  188 SER A CB  
1497 O  OG  . SER A 187 ? 0.1557 0.2524 0.1745 -0.0114 -0.0231 0.0292  188 SER A OG  
1498 N  N   . LEU A 188 ? 0.1208 0.1827 0.1849 -0.0097 -0.0057 0.0010  189 LEU A N   
1499 C  CA  . LEU A 188 ? 0.1214 0.1813 0.1820 -0.0173 -0.0124 -0.0135 189 LEU A CA  
1500 C  C   . LEU A 188 ? 0.1075 0.1989 0.1845 0.0004  0.0031  -0.0211 189 LEU A C   
1501 O  O   . LEU A 188 ? 0.1365 0.2611 0.2032 -0.0314 -0.0125 -0.0425 189 LEU A O   
1502 C  CB  . LEU A 188 ? 0.1773 0.1740 0.2138 -0.0064 -0.0043 -0.0314 189 LEU A CB  
1503 C  CG  . LEU A 188 ? 0.1465 0.2014 0.2419 -0.0055 -0.0303 -0.0147 189 LEU A CG  
1504 C  CD1 . LEU A 188 ? 0.1679 0.2016 0.3513 -0.0021 -0.0184 0.0074  189 LEU A CD1 
1505 C  CD2 . LEU A 188 ? 0.1284 0.2845 0.2777 -0.0279 0.0011  0.0345  189 LEU A CD2 
1506 N  N   . ASP A 189 ? 0.1122 0.2318 0.1526 0.0065  0.0027  -0.0011 190 ASP A N   
1507 C  CA  . ASP A 189 ? 0.1100 0.2255 0.1535 -0.0250 -0.0015 -0.0305 190 ASP A CA  
1508 C  C   . ASP A 189 ? 0.1129 0.1860 0.1262 -0.0216 0.0125  -0.0155 190 ASP A C   
1509 O  O   . ASP A 189 ? 0.1124 0.1751 0.1322 -0.0093 -0.0029 -0.0154 190 ASP A O   
1510 C  CB  . ASP A 189 ? 0.1576 0.3096 0.1494 -0.1050 0.0190  0.0289  190 ASP A CB  
1511 C  CG  . ASP A 189 ? 0.1637 0.4346 0.2000 -0.0903 0.0033  0.0050  190 ASP A CG  
1512 O  OD1 . ASP A 189 ? 0.2565 0.5480 0.3226 -0.0785 0.0730  -0.0832 190 ASP A OD1 
1513 O  OD2 . ASP A 189 ? 0.2427 0.5630 0.2559 -0.1579 -0.0292 0.0949  190 ASP A OD2 
1514 N  N   . TYR A 190 ? 0.1097 0.2035 0.1346 -0.0276 0.0041  0.0005  191 TYR A N   
1515 C  CA  . TYR A 190 ? 0.1102 0.1820 0.1020 -0.0150 0.0115  0.0004  191 TYR A CA  
1516 C  C   . TYR A 190 ? 0.1217 0.1520 0.0970 -0.0066 0.0116  0.0003  191 TYR A C   
1517 O  O   . TYR A 190 ? 0.1144 0.2011 0.1080 -0.0032 0.0192  -0.0038 191 TYR A O   
1518 C  CB  . TYR A 190 ? 0.1223 0.1657 0.1237 -0.0179 -0.0042 0.0055  191 TYR A CB  
1519 C  CG  . TYR A 190 ? 0.1176 0.1737 0.1397 -0.0192 -0.0058 0.0008  191 TYR A CG  
1520 C  CD1 . TYR A 190 ? 0.1268 0.1888 0.1477 -0.0277 -0.0057 -0.0054 191 TYR A CD1 
1521 C  CD2 . TYR A 190 ? 0.1233 0.1920 0.1361 -0.0108 0.0008  0.0010  191 TYR A CD2 
1522 C  CE1 . TYR A 190 ? 0.1470 0.1719 0.1565 -0.0006 -0.0331 -0.0162 191 TYR A CE1 
1523 C  CE2 . TYR A 190 ? 0.1536 0.1957 0.1404 -0.0179 -0.0021 -0.0168 191 TYR A CE2 
1524 C  CZ  . TYR A 190 ? 0.1619 0.2098 0.1346 0.0089  -0.0107 -0.0170 191 TYR A CZ  
1525 O  OH  . TYR A 190 ? 0.1880 0.1913 0.1941 0.0150  -0.0102 -0.0383 191 TYR A OH  
1526 N  N   . TRP A 191 ? 0.1122 0.1536 0.1027 0.0004  -0.0008 -0.0062 192 TRP A N   
1527 C  CA  . TRP A 191 ? 0.1046 0.1647 0.1023 0.0018  0.0031  -0.0004 192 TRP A CA  
1528 C  C   . TRP A 191 ? 0.1068 0.1666 0.0639 0.0065  0.0125  -0.0081 192 TRP A C   
1529 O  O   . TRP A 191 ? 0.1444 0.1640 0.0786 -0.0260 0.0044  -0.0034 192 TRP A O   
1530 C  CB  . TRP A 191 ? 0.1241 0.1366 0.1288 -0.0074 0.0113  -0.0152 192 TRP A CB  
1531 C  CG  . TRP A 191 ? 0.1225 0.1500 0.1169 0.0105  -0.0034 0.0027  192 TRP A CG  
1532 C  CD1 . TRP A 191 ? 0.1338 0.1604 0.1301 0.0165  0.0122  0.0115  192 TRP A CD1 
1533 C  CD2 . TRP A 191 ? 0.1034 0.1596 0.1350 0.0135  -0.0166 0.0082  192 TRP A CD2 
1534 N  NE1 . TRP A 191 ? 0.1565 0.1665 0.1643 0.0157  0.0166  0.0189  192 TRP A NE1 
1535 C  CE2 . TRP A 191 ? 0.1318 0.1447 0.1424 0.0200  -0.0004 0.0162  192 TRP A CE2 
1536 C  CE3 . TRP A 191 ? 0.1097 0.1594 0.1502 0.0063  -0.0109 -0.0006 192 TRP A CE3 
1537 C  CZ2 . TRP A 191 ? 0.1551 0.1500 0.1978 0.0304  -0.0068 0.0089  192 TRP A CZ2 
1538 C  CZ3 . TRP A 191 ? 0.1128 0.1698 0.2034 -0.0109 -0.0053 -0.0237 192 TRP A CZ3 
1539 C  CH2 . TRP A 191 ? 0.1144 0.1571 0.2009 0.0034  -0.0070 -0.0030 192 TRP A CH2 
1540 N  N   . THR A 192 ? 0.1302 0.1473 0.0895 0.0074  -0.0157 -0.0008 193 THR A N   
1541 C  CA  . THR A 192 ? 0.1152 0.1487 0.0970 0.0004  -0.0094 0.0003  193 THR A CA  
1542 C  C   . THR A 192 ? 0.1260 0.1743 0.0650 0.0066  0.0074  -0.0140 193 THR A C   
1543 O  O   . THR A 192 ? 0.1189 0.1819 0.0734 -0.0037 0.0027  0.0042  193 THR A O   
1544 C  CB  . THR A 192 ? 0.1207 0.1587 0.0980 0.0071  0.0126  -0.0057 193 THR A CB  
1545 O  OG1 . THR A 192 ? 0.1190 0.1388 0.1428 0.0111  -0.0064 -0.0100 193 THR A OG1 
1546 C  CG2 . THR A 192 ? 0.1465 0.1891 0.0899 0.0141  0.0030  -0.0184 193 THR A CG2 
1547 N  N   . TYR A 193 ? 0.1153 0.1333 0.1073 -0.0010 -0.0018 -0.0109 194 TYR A N   
1548 C  CA  . TYR A 193 ? 0.1049 0.1429 0.1095 0.0039  0.0000  0.0048  194 TYR A CA  
1549 C  C   . TYR A 193 ? 0.1050 0.1366 0.0880 0.0152  -0.0151 -0.0035 194 TYR A C   
1550 O  O   . TYR A 193 ? 0.1146 0.1402 0.0912 0.0018  -0.0178 -0.0053 194 TYR A O   
1551 C  CB  . TYR A 193 ? 0.1220 0.1529 0.0959 0.0144  0.0023  -0.0013 194 TYR A CB  
1552 C  CG  . TYR A 193 ? 0.1189 0.1395 0.0994 0.0214  -0.0106 0.0043  194 TYR A CG  
1553 C  CD1 . TYR A 193 ? 0.1316 0.1263 0.0962 0.0145  0.0012  0.0042  194 TYR A CD1 
1554 C  CD2 . TYR A 193 ? 0.1276 0.1315 0.1111 0.0061  -0.0037 -0.0108 194 TYR A CD2 
1555 C  CE1 . TYR A 193 ? 0.1113 0.1252 0.1047 0.0141  0.0128  0.0170  194 TYR A CE1 
1556 C  CE2 . TYR A 193 ? 0.1185 0.1326 0.0967 0.0100  -0.0086 0.0003  194 TYR A CE2 
1557 C  CZ  . TYR A 193 ? 0.1205 0.1040 0.0937 0.0048  0.0058  0.0005  194 TYR A CZ  
1558 O  OH  . TYR A 193 ? 0.1165 0.1068 0.1048 0.0055  0.0068  0.0011  194 TYR A OH  
1559 N  N   . PRO A 194 ? 0.1059 0.1517 0.0914 0.0040  -0.0086 -0.0138 195 PRO A N   
1560 C  CA  . PRO A 194 ? 0.1201 0.1412 0.1058 0.0135  0.0039  -0.0174 195 PRO A CA  
1561 C  C   . PRO A 194 ? 0.1034 0.1254 0.0982 0.0017  -0.0114 -0.0214 195 PRO A C   
1562 O  O   . PRO A 194 ? 0.1201 0.1412 0.1062 0.0109  -0.0143 -0.0138 195 PRO A O   
1563 C  CB  . PRO A 194 ? 0.1358 0.1718 0.1174 0.0133  -0.0003 -0.0359 195 PRO A CB  
1564 C  CG  . PRO A 194 ? 0.1540 0.1952 0.1195 -0.0303 -0.0189 -0.0209 195 PRO A CG  
1565 C  CD  . PRO A 194 ? 0.1415 0.2025 0.0829 -0.0245 -0.0121 -0.0186 195 PRO A CD  
1566 N  N   . GLY A 195 ? 0.0989 0.1264 0.1032 -0.0054 0.0046  -0.0136 196 GLY A N   
1567 C  CA  . GLY A 195 ? 0.1080 0.1389 0.0986 0.0095  0.0183  0.0052  196 GLY A CA  
1568 C  C   . GLY A 195 ? 0.0883 0.1237 0.0876 0.0000  0.0020  -0.0084 196 GLY A C   
1569 O  O   . GLY A 195 ? 0.1045 0.1149 0.1240 -0.0004 -0.0078 -0.0119 196 GLY A O   
1570 N  N   . SER A 196 ? 0.1063 0.1235 0.0724 0.0011  0.0068  0.0001  197 SER A N   
1571 C  CA  . SER A 196 ? 0.1132 0.1320 0.0724 0.0060  0.0190  -0.0111 197 SER A CA  
1572 C  C   . SER A 196 ? 0.1144 0.1083 0.0721 0.0137  0.0150  -0.0009 197 SER A C   
1573 O  O   . SER A 196 ? 0.1083 0.1065 0.1109 -0.0047 -0.0164 -0.0089 197 SER A O   
1574 C  CB  . SER A 196 ? 0.1047 0.1106 0.1408 0.0038  -0.0210 -0.0128 197 SER A CB  
1575 O  OG  . SER A 196 ? 0.0973 0.1224 0.1254 -0.0046 -0.0093 -0.0034 197 SER A OG  
1576 N  N   . LEU A 197 ? 0.0900 0.1306 0.0847 -0.0019 0.0030  0.0018  198 LEU A N   
1577 C  CA  . LEU A 197 ? 0.1183 0.1199 0.0782 0.0011  -0.0013 0.0059  198 LEU A CA  
1578 C  C   . LEU A 197 ? 0.0833 0.1263 0.1293 -0.0038 0.0041  -0.0103 198 LEU A C   
1579 O  O   . LEU A 197 ? 0.1032 0.1342 0.1162 -0.0023 -0.0050 -0.0098 198 LEU A O   
1580 C  CB  . LEU A 197 ? 0.1333 0.1213 0.1289 -0.0031 0.0126  0.0201  198 LEU A CB  
1581 C  CG  . LEU A 197 ? 0.1522 0.1138 0.1666 -0.0221 -0.0099 0.0119  198 LEU A CG  
1582 C  CD1 . LEU A 197 ? 0.1849 0.1487 0.1406 -0.0325 -0.0187 0.0273  198 LEU A CD1 
1583 C  CD2 . LEU A 197 ? 0.1460 0.1560 0.1666 0.0186  0.0071  0.0232  198 LEU A CD2 
1584 N  N   . THR A 198 ? 0.1109 0.1111 0.1116 -0.0008 0.0039  -0.0195 199 THR A N   
1585 C  CA  . THR A 198 ? 0.1143 0.1091 0.1071 -0.0009 0.0076  -0.0001 199 THR A CA  
1586 C  C   . THR A 198 ? 0.0946 0.1309 0.1109 -0.0042 -0.0067 -0.0060 199 THR A C   
1587 O  O   . THR A 198 ? 0.0952 0.1332 0.1479 0.0004  -0.0008 -0.0060 199 THR A O   
1588 C  CB  . THR A 198 ? 0.1303 0.1183 0.0861 -0.0111 -0.0044 -0.0087 199 THR A CB  
1589 O  OG1 . THR A 198 ? 0.1004 0.1204 0.0964 -0.0027 -0.0063 0.0030  199 THR A OG1 
1590 C  CG2 . THR A 198 ? 0.1254 0.1451 0.1012 0.0055  0.0209  0.0055  199 THR A CG2 
1591 N  N   . THR A 199 ? 0.1052 0.1421 0.1126 -0.0094 0.0087  0.0017  200 THR A N   
1592 C  CA  . THR A 199 ? 0.1180 0.1437 0.1160 -0.0161 0.0143  -0.0011 200 THR A CA  
1593 C  C   . THR A 199 ? 0.1044 0.1589 0.1199 -0.0027 -0.0032 0.0039  200 THR A C   
1594 O  O   . THR A 199 ? 0.1190 0.1360 0.1415 -0.0121 0.0100  0.0050  200 THR A O   
1595 C  CB  . THR A 199 ? 0.1494 0.1621 0.1395 0.0053  -0.0283 -0.0151 200 THR A CB  
1596 O  OG1 . THR A 199 ? 0.2024 0.2293 0.1514 0.0613  -0.0407 -0.0212 200 THR A OG1 
1597 C  CG2 . THR A 199 ? 0.1384 0.1955 0.1679 -0.0335 0.0064  -0.0238 200 THR A CG2 
1598 N  N   . PRO A 200 ? 0.1169 0.1544 0.1423 -0.0147 0.0084  -0.0046 201 PRO A N   
1599 C  CA  . PRO A 200 ? 0.1252 0.1582 0.1382 -0.0337 0.0115  0.0129  201 PRO A CA  
1600 C  C   . PRO A 200 ? 0.1316 0.1628 0.1580 -0.0337 -0.0008 0.0143  201 PRO A C   
1601 O  O   . PRO A 200 ? 0.1434 0.1779 0.1615 -0.0171 -0.0111 0.0174  201 PRO A O   
1602 C  CB  . PRO A 200 ? 0.1261 0.2018 0.1702 -0.0103 0.0146  0.0102  201 PRO A CB  
1603 C  CG  . PRO A 200 ? 0.1161 0.2027 0.1834 -0.0325 -0.0069 0.0111  201 PRO A CG  
1604 C  CD  . PRO A 200 ? 0.0993 0.1903 0.1539 -0.0021 0.0109  -0.0139 201 PRO A CD  
1605 N  N   . PRO A 201 ? 0.1327 0.1653 0.1494 -0.0300 -0.0126 0.0263  202 PRO A N   
1606 C  CA  . PRO A 201 ? 0.1412 0.1533 0.1460 -0.0361 -0.0004 0.0236  202 PRO A CA  
1607 C  C   . PRO A 201 ? 0.1063 0.1403 0.1662 -0.0103 -0.0126 0.0238  202 PRO A C   
1608 O  O   . PRO A 201 ? 0.1242 0.1579 0.1636 -0.0190 -0.0044 -0.0021 202 PRO A O   
1609 C  CB  . PRO A 201 ? 0.1712 0.1579 0.1748 -0.0368 -0.0013 0.0258  202 PRO A CB  
1610 C  CG  . PRO A 201 ? 0.1946 0.1633 0.2662 -0.0179 -0.0531 0.0295  202 PRO A CG  
1611 C  CD  . PRO A 201 ? 0.1932 0.1571 0.2023 -0.0172 -0.0186 0.0505  202 PRO A CD  
1612 N  N   . LEU A 202 ? 0.1146 0.1361 0.1402 -0.0280 0.0121  0.0125  203 LEU A N   
1613 C  CA  . LEU A 202 ? 0.1028 0.1328 0.1331 -0.0050 -0.0111 -0.0067 203 LEU A CA  
1614 C  C   . LEU A 202 ? 0.1067 0.1263 0.1455 -0.0201 0.0030  -0.0081 203 LEU A C   
1615 O  O   . LEU A 202 ? 0.1014 0.1280 0.1447 -0.0079 -0.0002 -0.0055 203 LEU A O   
1616 C  CB  . LEU A 202 ? 0.1062 0.1462 0.1395 -0.0049 -0.0251 -0.0223 203 LEU A CB  
1617 C  CG  . LEU A 202 ? 0.0987 0.1370 0.1444 -0.0031 -0.0046 -0.0058 203 LEU A CG  
1618 C  CD1 . LEU A 202 ? 0.0959 0.1647 0.1952 0.0076  0.0047  -0.0253 203 LEU A CD1 
1619 C  CD2 . LEU A 202 ? 0.0969 0.1471 0.1848 -0.0038 -0.0113 -0.0048 203 LEU A CD2 
1620 N  N   . ASN A 203 ? 0.1259 0.1208 0.1482 -0.0116 0.0020  -0.0023 204 ASN A N   
1621 C  CA  . ASN A 203 ? 0.1345 0.1201 0.1571 -0.0086 0.0084  -0.0034 204 ASN A CA  
1622 C  C   . ASN A 203 ? 0.1273 0.1120 0.1219 -0.0042 0.0060  -0.0030 204 ASN A C   
1623 O  O   . ASN A 203 ? 0.1125 0.1306 0.1418 -0.0129 -0.0116 -0.0049 204 ASN A O   
1624 C  CB  . ASN A 203 ? 0.1551 0.1174 0.1841 -0.0043 0.0091  0.0250  204 ASN A CB  
1625 C  CG  . ASN A 203 ? 0.1720 0.1374 0.2280 0.0021  0.0358  0.0357  204 ASN A CG  
1626 O  OD1 . ASN A 203 ? 0.2141 0.1841 0.2829 -0.0040 0.0774  0.0164  204 ASN A OD1 
1627 N  ND2 . ASN A 203 ? 0.2590 0.1639 0.2878 0.0232  0.0462  0.0584  204 ASN A ND2 
1628 N  N   . GLU A 204 ? 0.1195 0.1329 0.1383 0.0006  -0.0034 -0.0262 205 GLU A N   
1629 C  CA  . GLU A 204 ? 0.1456 0.1491 0.1000 0.0060  -0.0093 -0.0306 205 GLU A CA  
1630 C  C   . GLU A 204 ? 0.1339 0.1138 0.1427 -0.0050 -0.0158 -0.0196 205 GLU A C   
1631 O  O   . GLU A 204 ? 0.1599 0.2029 0.1522 0.0400  -0.0479 -0.0496 205 GLU A O   
1632 C  CB  . GLU A 204 ? 0.1454 0.1542 0.1536 0.0075  -0.0436 -0.0368 205 GLU A CB  
1633 C  CG  . GLU A 204 ? 0.1491 0.1648 0.1434 0.0130  -0.0253 -0.0150 205 GLU A CG  
1634 C  CD  . GLU A 204 ? 0.1310 0.1565 0.1635 0.0064  -0.0231 -0.0282 205 GLU A CD  
1635 O  OE1 . GLU A 204 ? 0.1702 0.1945 0.2007 0.0150  -0.0726 -0.0476 205 GLU A OE1 
1636 O  OE2 . GLU A 204 ? 0.1258 0.1648 0.1618 0.0057  -0.0142 -0.0140 205 GLU A OE2 
1637 N  N   . CYS A 205 ? 0.1124 0.1128 0.1482 -0.0076 -0.0275 -0.0147 206 CYS A N   
1638 C  CA  . CYS A 205 ? 0.1115 0.1189 0.1207 0.0023  -0.0053 -0.0125 206 CYS A CA  
1639 C  C   . CYS A 205 ? 0.1155 0.1083 0.1407 0.0000  -0.0183 -0.0179 206 CYS A C   
1640 O  O   . CYS A 205 ? 0.1421 0.1059 0.1923 0.0079  -0.0411 -0.0031 206 CYS A O   
1641 C  CB  . CYS A 205 ? 0.1423 0.1529 0.1246 -0.0145 -0.0044 0.0009  206 CYS A CB  
1642 S  SG  . CYS A 205 ? 0.1560 0.1388 0.1390 -0.0021 -0.0212 -0.0003 206 CYS A SG  
1643 N  N   . VAL A 206 ? 0.1093 0.1062 0.1310 -0.0091 -0.0142 -0.0032 207 VAL A N   
1644 C  CA  . VAL A 206 ? 0.1021 0.1113 0.1452 -0.0081 -0.0040 -0.0069 207 VAL A CA  
1645 C  C   . VAL A 206 ? 0.1254 0.0969 0.1164 -0.0026 -0.0157 -0.0127 207 VAL A C   
1646 O  O   . VAL A 206 ? 0.1237 0.1383 0.1386 -0.0008 -0.0149 0.0196  207 VAL A O   
1647 C  CB  . VAL A 206 ? 0.1059 0.1092 0.1418 -0.0002 0.0031  -0.0020 207 VAL A CB  
1648 C  CG1 . VAL A 206 ? 0.1111 0.1224 0.1363 -0.0034 -0.0149 -0.0094 207 VAL A CG1 
1649 C  CG2 . VAL A 206 ? 0.1301 0.1259 0.1221 0.0135  -0.0060 0.0033  207 VAL A CG2 
1650 N  N   . THR A 207 ? 0.1034 0.0980 0.1567 -0.0052 -0.0066 -0.0116 208 THR A N   
1651 C  CA  . THR A 207 ? 0.1300 0.1223 0.1238 -0.0005 -0.0062 -0.0159 208 THR A CA  
1652 C  C   . THR A 207 ? 0.1120 0.1040 0.1192 -0.0143 -0.0055 -0.0058 208 THR A C   
1653 O  O   . THR A 207 ? 0.1324 0.1219 0.1122 -0.0073 -0.0245 -0.0063 208 THR A O   
1654 C  CB  . THR A 207 ? 0.1400 0.1128 0.1327 -0.0031 0.0111  -0.0150 208 THR A CB  
1655 O  OG1 . THR A 207 ? 0.1518 0.1274 0.1557 -0.0002 -0.0037 -0.0333 208 THR A OG1 
1656 C  CG2 . THR A 207 ? 0.1362 0.1456 0.1689 -0.0095 0.0077  -0.0066 208 THR A CG2 
1657 N  N   . TRP A 208 ? 0.0991 0.1041 0.1239 0.0003  -0.0020 -0.0078 209 TRP A N   
1658 C  CA  . TRP A 208 ? 0.1146 0.1045 0.0996 -0.0006 0.0031  -0.0015 209 TRP A CA  
1659 C  C   . TRP A 208 ? 0.1041 0.1054 0.0752 0.0098  0.0005  0.0029  209 TRP A C   
1660 O  O   . TRP A 208 ? 0.1174 0.1289 0.0831 -0.0059 0.0027  -0.0010 209 TRP A O   
1661 C  CB  . TRP A 208 ? 0.1098 0.1185 0.0987 0.0144  0.0000  0.0116  209 TRP A CB  
1662 C  CG  . TRP A 208 ? 0.0996 0.1212 0.0895 0.0098  -0.0058 0.0015  209 TRP A CG  
1663 C  CD1 . TRP A 208 ? 0.1093 0.1149 0.1156 -0.0023 -0.0008 0.0098  209 TRP A CD1 
1664 C  CD2 . TRP A 208 ? 0.1088 0.1083 0.0878 0.0198  0.0029  0.0035  209 TRP A CD2 
1665 N  NE1 . TRP A 208 ? 0.1179 0.1137 0.1118 0.0063  -0.0075 -0.0042 209 TRP A NE1 
1666 C  CE2 . TRP A 208 ? 0.1154 0.1072 0.1012 0.0190  0.0024  0.0036  209 TRP A CE2 
1667 C  CE3 . TRP A 208 ? 0.1150 0.1000 0.0942 0.0084  -0.0133 0.0103  209 TRP A CE3 
1668 C  CZ2 . TRP A 208 ? 0.1286 0.1194 0.1095 0.0304  0.0073  0.0064  209 TRP A CZ2 
1669 C  CZ3 . TRP A 208 ? 0.1385 0.1120 0.1075 0.0113  -0.0025 -0.0129 209 TRP A CZ3 
1670 C  CH2 . TRP A 208 ? 0.1515 0.1152 0.1009 0.0259  0.0025  -0.0119 209 TRP A CH2 
1671 N  N   . ILE A 209 ? 0.1004 0.1186 0.1067 0.0036  -0.0107 -0.0032 210 ILE A N   
1672 C  CA  . ILE A 209 ? 0.1043 0.1117 0.0971 0.0013  0.0012  -0.0113 210 ILE A CA  
1673 C  C   . ILE A 209 ? 0.0943 0.1160 0.0766 0.0006  0.0075  -0.0025 210 ILE A C   
1674 O  O   . ILE A 209 ? 0.1515 0.1071 0.0777 0.0000  0.0063  -0.0026 210 ILE A O   
1675 C  CB  . ILE A 209 ? 0.0961 0.1132 0.1488 0.0088  0.0156  -0.0119 210 ILE A CB  
1676 C  CG1 . ILE A 209 ? 0.1247 0.1104 0.2222 0.0263  -0.0012 -0.0337 210 ILE A CG1 
1677 C  CG2 . ILE A 209 ? 0.0858 0.1578 0.1799 0.0076  0.0073  -0.0038 210 ILE A CG2 
1678 C  CD1 . ILE A 209 ? 0.1589 0.1307 0.2523 0.0372  -0.0122 -0.0103 210 ILE A CD1 
1679 N  N   . VAL A 210 ? 0.1067 0.1070 0.0991 0.0013  0.0043  0.0031  211 VAL A N   
1680 C  CA  . VAL A 210 ? 0.0968 0.1089 0.1037 0.0061  0.0096  -0.0016 211 VAL A CA  
1681 C  C   . VAL A 210 ? 0.1045 0.1174 0.0797 0.0024  0.0138  0.0027  211 VAL A C   
1682 O  O   . VAL A 210 ? 0.1263 0.1270 0.0845 -0.0117 0.0041  0.0074  211 VAL A O   
1683 C  CB  . VAL A 210 ? 0.0998 0.1143 0.1273 0.0119  0.0042  -0.0043 211 VAL A CB  
1684 C  CG1 . VAL A 210 ? 0.1467 0.1110 0.1259 0.0060  0.0110  -0.0110 211 VAL A CG1 
1685 C  CG2 . VAL A 210 ? 0.1104 0.1297 0.1490 -0.0121 -0.0084 -0.0001 211 VAL A CG2 
1686 N  N   . LEU A 211 ? 0.0980 0.1219 0.1271 -0.0020 -0.0072 -0.0131 212 LEU A N   
1687 C  CA  . LEU A 211 ? 0.1204 0.1395 0.1044 -0.0232 0.0035  0.0021  212 LEU A CA  
1688 C  C   . LEU A 211 ? 0.1083 0.1488 0.1050 -0.0127 0.0062  0.0145  212 LEU A C   
1689 O  O   . LEU A 211 ? 0.1153 0.1490 0.1214 -0.0122 -0.0029 0.0037  212 LEU A O   
1690 C  CB  . LEU A 211 ? 0.1241 0.1412 0.1077 -0.0033 -0.0041 0.0052  212 LEU A CB  
1691 C  CG  . LEU A 211 ? 0.1178 0.1486 0.1269 -0.0072 -0.0039 0.0096  212 LEU A CG  
1692 C  CD1 . LEU A 211 ? 0.1328 0.1957 0.1626 0.0162  -0.0305 0.0058  212 LEU A CD1 
1693 C  CD2 . LEU A 211 ? 0.1190 0.1539 0.1549 0.0103  0.0094  -0.0093 212 LEU A CD2 
1694 N  N   . LYS A 212 ? 0.1162 0.1612 0.1084 -0.0239 0.0009  0.0307  213 LYS A N   
1695 C  CA  . LYS A 212 ? 0.1601 0.1666 0.1111 -0.0326 -0.0142 0.0410  213 LYS A CA  
1696 C  C   . LYS A 212 ? 0.1254 0.1456 0.1235 -0.0122 -0.0036 0.0227  213 LYS A C   
1697 O  O   . LYS A 212 ? 0.1490 0.1510 0.1977 -0.0115 -0.0359 0.0351  213 LYS A O   
1698 C  CB  . LYS A 212 ? 0.2576 0.2233 0.1201 -0.0841 0.0008  0.0521  213 LYS A CB  
1699 C  CG  . LYS A 212 ? 0.4977 0.2976 0.1229 -0.1549 -0.0485 0.0688  213 LYS A CG  
1700 C  CD  . LYS A 212 ? 0.6893 0.3912 0.3018 -0.2551 0.1189  -0.0348 213 LYS A CD  
1701 N  N   . GLU A 213 ? 0.1199 0.1540 0.1149 -0.0138 -0.0119 0.0086  214 GLU A N   
1702 C  CA  . GLU A 213 ? 0.1314 0.1340 0.1298 -0.0131 -0.0076 0.0092  214 GLU A CA  
1703 C  C   . GLU A 213 ? 0.1237 0.1282 0.1272 -0.0040 -0.0137 0.0179  214 GLU A C   
1704 O  O   . GLU A 213 ? 0.1311 0.1321 0.1275 -0.0044 -0.0071 0.0240  214 GLU A O   
1705 C  CB  . GLU A 213 ? 0.1188 0.1816 0.1397 -0.0159 -0.0111 0.0214  214 GLU A CB  
1706 C  CG  . GLU A 213 ? 0.1759 0.2099 0.1924 -0.0400 -0.0151 -0.0150 214 GLU A CG  
1707 C  CD  . GLU A 213 ? 0.1684 0.2635 0.2351 -0.0807 -0.0264 -0.0055 214 GLU A CD  
1708 O  OE1 . GLU A 213 ? 0.1562 0.2375 0.2943 -0.0197 -0.0195 0.0192  214 GLU A OE1 
1709 O  OE2 . GLU A 213 ? 0.2405 0.4980 0.2720 -0.0715 -0.0337 -0.0215 214 GLU A OE2 
1710 N  N   . PRO A 214 ? 0.1479 0.1206 0.1326 -0.0092 -0.0088 0.0151  215 PRO A N   
1711 C  CA  . PRO A 214 ? 0.1583 0.1289 0.1146 0.0062  -0.0107 -0.0001 215 PRO A CA  
1712 C  C   . PRO A 214 ? 0.1223 0.1324 0.1380 -0.0018 -0.0080 -0.0015 215 PRO A C   
1713 O  O   . PRO A 214 ? 0.1399 0.1874 0.1469 -0.0374 -0.0165 0.0211  215 PRO A O   
1714 C  CB  . PRO A 214 ? 0.1741 0.1225 0.1464 -0.0003 -0.0099 -0.0008 215 PRO A CB  
1715 C  CG  . PRO A 214 ? 0.3292 0.1885 0.2518 0.0647  0.0965  0.0411  215 PRO A CG  
1716 C  CD  . PRO A 214 ? 0.2115 0.1160 0.1797 0.0161  0.0220  0.0216  215 PRO A CD  
1717 N  N   . ILE A 215 ? 0.1275 0.1280 0.1136 0.0069  -0.0059 -0.0034 216 ILE A N   
1718 C  CA  . ILE A 215 ? 0.1583 0.1232 0.1339 -0.0008 -0.0223 -0.0139 216 ILE A CA  
1719 C  C   . ILE A 215 ? 0.1474 0.1291 0.1231 -0.0044 -0.0117 -0.0079 216 ILE A C   
1720 O  O   . ILE A 215 ? 0.1333 0.1153 0.2005 0.0008  -0.0166 -0.0120 216 ILE A O   
1721 C  CB  . ILE A 215 ? 0.1410 0.1225 0.1528 0.0070  -0.0105 -0.0055 216 ILE A CB  
1722 C  CG1 . ILE A 215 ? 0.1409 0.1426 0.1344 0.0051  -0.0034 0.0083  216 ILE A CG1 
1723 C  CG2 . ILE A 215 ? 0.1551 0.1264 0.1637 0.0212  -0.0102 -0.0111 216 ILE A CG2 
1724 C  CD1 . ILE A 215 ? 0.1827 0.1478 0.1612 0.0133  -0.0017 0.0259  216 ILE A CD1 
1725 N  N   . SER A 216 ? 0.1777 0.1240 0.1262 -0.0053 -0.0241 -0.0012 217 SER A N   
1726 C  CA  A SER A 216 ? 0.1709 0.1395 0.1221 0.0086  -0.0216 -0.0049 217 SER A CA  
1727 C  CA  B SER A 216 ? 0.1872 0.1217 0.1336 0.0009  -0.0109 0.0029  217 SER A CA  
1728 C  C   . SER A 216 ? 0.1599 0.1110 0.1183 -0.0061 -0.0315 -0.0116 217 SER A C   
1729 O  O   . SER A 216 ? 0.1589 0.1416 0.1456 0.0043  -0.0366 0.0060  217 SER A O   
1730 C  CB  A SER A 216 ? 0.2695 0.1180 0.1007 -0.0405 -0.0195 -0.0480 217 SER A CB  
1731 C  CB  B SER A 216 ? 0.2697 0.1180 0.2027 -0.0352 0.0002  0.0473  217 SER A CB  
1732 O  OG  A SER A 216 ? 0.2352 0.1901 0.1261 -0.0139 -0.0462 -0.0088 217 SER A OG  
1733 O  OG  B SER A 216 ? 0.2870 0.1579 0.2552 -0.0215 -0.0243 0.0109  217 SER A OG  
1734 N  N   . VAL A 217 ? 0.1605 0.1122 0.1394 -0.0104 -0.0047 -0.0114 218 VAL A N   
1735 C  CA  . VAL A 217 ? 0.1507 0.1057 0.1386 -0.0054 -0.0155 -0.0043 218 VAL A CA  
1736 C  C   . VAL A 217 ? 0.1585 0.1077 0.1264 -0.0080 -0.0243 -0.0117 218 VAL A C   
1737 O  O   . VAL A 217 ? 0.1693 0.1140 0.1494 -0.0111 -0.0311 -0.0036 218 VAL A O   
1738 C  CB  . VAL A 217 ? 0.1511 0.0937 0.2007 -0.0051 -0.0441 -0.0032 218 VAL A CB  
1739 C  CG1 . VAL A 217 ? 0.1813 0.1169 0.1952 -0.0106 -0.0388 -0.0228 218 VAL A CG1 
1740 C  CG2 . VAL A 217 ? 0.1510 0.1430 0.2343 0.0107  -0.0402 -0.0082 218 VAL A CG2 
1741 N  N   . SER A 218 ? 0.1711 0.1126 0.1276 -0.0121 -0.0256 -0.0173 219 SER A N   
1742 C  CA  . SER A 218 ? 0.1763 0.1090 0.1357 -0.0049 -0.0308 -0.0124 219 SER A CA  
1743 C  C   . SER A 218 ? 0.1770 0.1081 0.1204 -0.0117 -0.0215 0.0023  219 SER A C   
1744 O  O   . SER A 218 ? 0.1788 0.1005 0.1669 -0.0105 -0.0414 0.0073  219 SER A O   
1745 C  CB  . SER A 218 ? 0.1932 0.1152 0.1612 -0.0260 -0.0425 0.0099  219 SER A CB  
1746 O  OG  . SER A 218 ? 0.1662 0.1373 0.1551 -0.0177 -0.0392 -0.0054 219 SER A OG  
1747 N  N   . SER A 219 ? 0.1902 0.1007 0.1687 0.0021  -0.0289 -0.0024 220 SER A N   
1748 C  CA  . SER A 219 ? 0.1932 0.1047 0.1952 0.0042  -0.0321 -0.0025 220 SER A CA  
1749 C  C   . SER A 219 ? 0.1955 0.1027 0.2071 0.0108  -0.0380 0.0089  220 SER A C   
1750 O  O   . SER A 219 ? 0.1833 0.1359 0.2414 0.0061  -0.0165 0.0068  220 SER A O   
1751 C  CB  . SER A 219 ? 0.2414 0.1063 0.2622 -0.0154 -0.0040 -0.0155 220 SER A CB  
1752 O  OG  . SER A 219 ? 0.3321 0.1359 0.2648 -0.0047 -0.0458 -0.0091 220 SER A OG  
1753 N  N   . GLU A 220 ? 0.1939 0.1289 0.1500 0.0195  -0.0201 -0.0141 221 GLU A N   
1754 C  CA  . GLU A 220 ? 0.2345 0.1241 0.1622 0.0102  -0.0194 -0.0086 221 GLU A CA  
1755 C  C   . GLU A 220 ? 0.1768 0.1298 0.1536 0.0088  -0.0142 -0.0098 221 GLU A C   
1756 O  O   . GLU A 220 ? 0.2054 0.1499 0.1612 0.0178  0.0163  -0.0129 221 GLU A O   
1757 C  CB  . GLU A 220 ? 0.2023 0.1716 0.2020 0.0075  -0.0391 -0.0511 221 GLU A CB  
1758 C  CG  . GLU A 220 ? 0.2948 0.1980 0.2675 -0.0225 -0.0326 -0.0891 221 GLU A CG  
1759 C  CD  . GLU A 220 ? 0.4199 0.1576 0.3174 -0.0486 -0.0293 -0.0496 221 GLU A CD  
1760 O  OE1 . GLU A 220 ? 0.2663 0.2172 0.3167 -0.0660 -0.0138 -0.0575 221 GLU A OE1 
1761 O  OE2 . GLU A 220 ? 0.5384 0.2312 0.4170 -0.1553 -0.0044 -0.1070 221 GLU A OE2 
1762 N  N   . GLN A 221 ? 0.1658 0.1101 0.1504 0.0128  -0.0159 -0.0098 222 GLN A N   
1763 C  CA  . GLN A 221 ? 0.1424 0.1111 0.1725 -0.0110 -0.0121 -0.0178 222 GLN A CA  
1764 C  C   . GLN A 221 ? 0.1662 0.1061 0.1640 -0.0153 -0.0301 0.0091  222 GLN A C   
1765 O  O   . GLN A 221 ? 0.1459 0.1289 0.1529 0.0006  -0.0065 0.0128  222 GLN A O   
1766 C  CB  . GLN A 221 ? 0.1433 0.1258 0.1333 -0.0012 -0.0194 0.0039  222 GLN A CB  
1767 C  CG  . GLN A 221 ? 0.1359 0.1356 0.1345 -0.0042 -0.0156 0.0019  222 GLN A CG  
1768 C  CD  . GLN A 221 ? 0.1435 0.1120 0.1254 -0.0052 -0.0088 -0.0043 222 GLN A CD  
1769 O  OE1 . GLN A 221 ? 0.1531 0.1217 0.1192 0.0063  -0.0129 -0.0047 222 GLN A OE1 
1770 N  NE2 . GLN A 221 ? 0.1544 0.1216 0.1480 0.0071  -0.0319 0.0006  222 GLN A NE2 
1771 N  N   . VAL A 222 ? 0.1368 0.1433 0.1404 -0.0013 -0.0151 0.0162  223 VAL A N   
1772 C  CA  . VAL A 222 ? 0.1412 0.1680 0.1820 0.0005  -0.0262 0.0223  223 VAL A CA  
1773 C  C   . VAL A 222 ? 0.1424 0.1490 0.2056 0.0043  -0.0210 0.0129  223 VAL A C   
1774 O  O   . VAL A 222 ? 0.1478 0.1955 0.1790 0.0058  -0.0134 0.0267  223 VAL A O   
1775 C  CB  . VAL A 222 ? 0.1820 0.2664 0.1723 0.0284  -0.0685 0.0257  223 VAL A CB  
1776 C  CG1 . VAL A 222 ? 0.2590 0.2634 0.2720 -0.0193 -0.0300 0.0019  223 VAL A CG1 
1777 C  CG2 . VAL A 222 ? 0.2376 0.3632 0.2535 -0.0557 -0.0987 0.0941  223 VAL A CG2 
1778 N  N   A LEU A 223 ? 0.1744 0.1562 0.2071 0.0178  0.0061  0.0131  224 LEU A N   
1779 N  N   B LEU A 223 ? 0.1679 0.1589 0.1910 0.0263  0.0115  0.0158  224 LEU A N   
1780 C  CA  A LEU A 223 ? 0.1762 0.1657 0.2300 0.0097  0.0022  -0.0124 224 LEU A CA  
1781 C  CA  B LEU A 223 ? 0.1948 0.1720 0.2312 0.0265  0.0308  -0.0054 224 LEU A CA  
1782 C  C   A LEU A 223 ? 0.1654 0.1831 0.2024 0.0081  -0.0084 -0.0059 224 LEU A C   
1783 C  C   B LEU A 223 ? 0.1744 0.1903 0.1914 0.0145  -0.0085 -0.0063 224 LEU A C   
1784 O  O   A LEU A 223 ? 0.1672 0.1848 0.1725 0.0067  0.0066  -0.0259 224 LEU A O   
1785 O  O   B LEU A 223 ? 0.1434 0.2242 0.2125 0.0110  -0.0229 -0.0230 224 LEU A O   
1786 C  CB  A LEU A 223 ? 0.2451 0.1091 0.3096 -0.0120 0.0011  -0.0304 224 LEU A CB  
1787 C  CB  B LEU A 223 ? 0.1971 0.1797 0.2629 0.0607  -0.0135 -0.0384 224 LEU A CB  
1788 C  CG  A LEU A 223 ? 0.2567 0.2382 0.3270 0.0039  0.0166  -0.0009 224 LEU A CG  
1789 C  CG  B LEU A 223 ? 0.2350 0.1662 0.2606 -0.0117 0.0447  -0.0281 224 LEU A CG  
1790 C  CD1 A LEU A 223 ? 0.3194 0.3194 0.3194 0.0000  0.0000  0.0000  224 LEU A CD1 
1791 C  CD1 B LEU A 223 ? 0.2577 0.1935 0.3778 -0.0332 0.0113  -0.0452 224 LEU A CD1 
1792 C  CD2 A LEU A 223 ? 0.3353 0.3206 0.2860 -0.0509 -0.0177 0.0071  224 LEU A CD2 
1793 C  CD2 B LEU A 223 ? 0.2280 0.1515 0.4539 0.0366  0.1174  -0.0601 224 LEU A CD2 
1794 N  N   . LYS A 224 ? 0.1583 0.1847 0.1622 0.0042  -0.0128 0.0012  225 LYS A N   
1795 C  CA  . LYS A 224 ? 0.1617 0.2251 0.1587 -0.0094 -0.0206 0.0082  225 LYS A CA  
1796 C  C   . LYS A 224 ? 0.1838 0.1684 0.1250 0.0282  -0.0122 -0.0078 225 LYS A C   
1797 O  O   . LYS A 224 ? 0.1820 0.1662 0.1707 0.0152  -0.0179 0.0029  225 LYS A O   
1798 C  CB  . LYS A 224 ? 0.1829 0.2943 0.1894 0.0279  -0.0487 0.0184  225 LYS A CB  
1799 C  CG  . LYS A 224 ? 0.2268 0.3583 0.2463 -0.0375 -0.0971 0.0502  225 LYS A CG  
1800 C  CD  . LYS A 224 ? 0.2667 0.5440 0.4966 0.0005  -0.1529 0.0142  225 LYS A CD  
1801 C  CE  . LYS A 224 ? 0.4878 0.3480 0.5502 -0.0449 -0.2330 -0.0362 225 LYS A CE  
1802 N  NZ  . LYS A 224 ? 0.8600 0.3218 0.4543 -0.0912 -0.0592 -0.1146 225 LYS A NZ  
1803 N  N   . PHE A 225 ? 0.1754 0.1424 0.1169 0.0178  -0.0044 -0.0048 226 PHE A N   
1804 C  CA  . PHE A 225 ? 0.1612 0.1403 0.1412 0.0272  -0.0003 -0.0138 226 PHE A CA  
1805 C  C   . PHE A 225 ? 0.1732 0.1493 0.1147 0.0171  -0.0087 0.0013  226 PHE A C   
1806 O  O   . PHE A 225 ? 0.1815 0.1529 0.1399 0.0204  0.0161  -0.0122 226 PHE A O   
1807 C  CB  . PHE A 225 ? 0.1553 0.1646 0.1409 0.0354  -0.0091 -0.0074 226 PHE A CB  
1808 C  CG  . PHE A 225 ? 0.1428 0.1393 0.1665 0.0122  0.0085  -0.0120 226 PHE A CG  
1809 C  CD1 . PHE A 225 ? 0.1657 0.1827 0.1576 0.0379  0.0251  -0.0009 226 PHE A CD1 
1810 C  CD2 . PHE A 225 ? 0.1540 0.2133 0.1673 0.0051  0.0023  -0.0239 226 PHE A CD2 
1811 C  CE1 . PHE A 225 ? 0.2005 0.1830 0.1592 0.0431  0.0434  -0.0005 226 PHE A CE1 
1812 C  CE2 . PHE A 225 ? 0.1447 0.2438 0.2393 0.0265  -0.0187 -0.0487 226 PHE A CE2 
1813 C  CZ  . PHE A 225 ? 0.1581 0.1763 0.1788 0.0048  -0.0003 -0.0546 226 PHE A CZ  
1814 N  N   . ARG A 226 ? 0.1698 0.1526 0.1291 0.0374  -0.0027 -0.0122 227 ARG A N   
1815 C  CA  . ARG A 226 ? 0.1741 0.1826 0.1253 0.0454  0.0153  0.0075  227 ARG A CA  
1816 C  C   . ARG A 226 ? 0.1507 0.1571 0.1391 0.0188  0.0103  0.0095  227 ARG A C   
1817 O  O   . ARG A 226 ? 0.1716 0.2330 0.1763 0.0530  0.0162  -0.0170 227 ARG A O   
1818 C  CB  . ARG A 226 ? 0.1867 0.1536 0.1340 0.0460  0.0087  -0.0058 227 ARG A CB  
1819 C  CG  . ARG A 226 ? 0.1960 0.1648 0.1192 0.0298  -0.0088 -0.0172 227 ARG A CG  
1820 C  CD  . ARG A 226 ? 0.2483 0.1507 0.1770 0.0440  -0.0162 -0.0106 227 ARG A CD  
1821 N  NE  . ARG A 226 ? 0.2215 0.1379 0.1439 0.0136  -0.0391 -0.0094 227 ARG A NE  
1822 C  CZ  . ARG A 226 ? 0.2158 0.1636 0.1576 -0.0137 -0.0149 -0.0342 227 ARG A CZ  
1823 N  NH1 . ARG A 226 ? 0.2260 0.2353 0.2777 -0.0451 -0.0166 -0.1112 227 ARG A NH1 
1824 N  NH2 . ARG A 226 ? 0.2603 0.1863 0.1901 -0.0431 0.0300  -0.0441 227 ARG A NH2 
1825 N  N   . LYS A 227 ? 0.1977 0.1928 0.1120 0.0181  -0.0153 -0.0221 228 LYS A N   
1826 C  CA  . LYS A 227 ? 0.2143 0.1939 0.1196 0.0193  -0.0156 -0.0488 228 LYS A CA  
1827 C  C   . LYS A 227 ? 0.2145 0.2258 0.0930 0.0306  -0.0033 -0.0411 228 LYS A C   
1828 O  O   . LYS A 227 ? 0.2269 0.2194 0.1381 0.0227  0.0267  -0.0384 228 LYS A O   
1829 C  CB  . LYS A 227 ? 0.2420 0.2484 0.1430 0.0245  -0.0245 -0.0385 228 LYS A CB  
1830 C  CG  . LYS A 227 ? 0.2614 0.3076 0.2377 -0.0201 -0.0439 -0.0820 228 LYS A CG  
1831 C  CD  . LYS A 227 ? 0.2675 0.4455 0.3218 0.0444  -0.0845 -0.1135 228 LYS A CD  
1832 C  CE  . LYS A 227 ? 0.3596 0.5213 0.5933 -0.0759 -0.1342 -0.1802 228 LYS A CE  
1833 N  NZ  . LYS A 227 ? 0.4113 0.6189 0.7991 -0.0412 -0.2374 -0.1791 228 LYS A NZ  
1834 N  N   . LEU A 228 ? 0.1794 0.1837 0.1254 0.0229  -0.0066 -0.0372 229 LEU A N   
1835 C  CA  . LEU A 228 ? 0.1691 0.1895 0.1032 0.0239  0.0041  -0.0086 229 LEU A CA  
1836 C  C   . LEU A 228 ? 0.1842 0.2061 0.1357 0.0524  0.0055  -0.0260 229 LEU A C   
1837 O  O   . LEU A 228 ? 0.2000 0.2138 0.1521 0.0588  -0.0178 -0.0283 229 LEU A O   
1838 C  CB  . LEU A 228 ? 0.1461 0.2125 0.1272 0.0400  0.0064  -0.0234 229 LEU A CB  
1839 C  CG  . LEU A 228 ? 0.1543 0.2010 0.1106 0.0392  -0.0021 -0.0042 229 LEU A CG  
1840 C  CD1 . LEU A 228 ? 0.1614 0.2247 0.0949 0.0193  0.0084  0.0012  229 LEU A CD1 
1841 C  CD2 . LEU A 228 ? 0.2062 0.2212 0.1312 0.0201  0.0238  0.0259  229 LEU A CD2 
1842 N  N   . ASN A 229 ? 0.1662 0.2355 0.1167 0.0407  -0.0063 -0.0092 230 ASN A N   
1843 C  CA  . ASN A 229 ? 0.1637 0.2416 0.0964 0.0476  0.0041  -0.0347 230 ASN A CA  
1844 C  C   . ASN A 229 ? 0.1458 0.2433 0.1657 0.0342  0.0115  -0.0296 230 ASN A C   
1845 O  O   . ASN A 229 ? 0.1673 0.2197 0.1414 0.0283  0.0020  -0.0262 230 ASN A O   
1846 C  CB  . ASN A 229 ? 0.1594 0.2856 0.1346 0.0317  0.0275  -0.0286 230 ASN A CB  
1847 C  CG  . ASN A 229 ? 0.2291 0.3335 0.1294 0.0767  0.0015  -0.0731 230 ASN A CG  
1848 O  OD1 . ASN A 229 ? 0.3283 0.4487 0.1718 0.0924  0.0642  -0.1079 230 ASN A OD1 
1849 N  ND2 . ASN A 229 ? 0.3039 0.3227 0.1587 0.0763  0.0042  -0.0885 230 ASN A ND2 
1850 N  N   . PHE A 230 ? 0.1488 0.2328 0.1504 0.0204  0.0013  -0.0209 231 PHE A N   
1851 C  CA  . PHE A 230 ? 0.1287 0.2516 0.1711 0.0124  0.0089  -0.0288 231 PHE A CA  
1852 C  C   . PHE A 230 ? 0.1777 0.2690 0.1495 0.0133  -0.0064 -0.0337 231 PHE A C   
1853 O  O   . PHE A 230 ? 0.1666 0.2659 0.1515 0.0081  0.0209  -0.0286 231 PHE A O   
1854 C  CB  . PHE A 230 ? 0.1664 0.2976 0.1106 0.0396  0.0141  -0.0316 231 PHE A CB  
1855 C  CG  . PHE A 230 ? 0.1705 0.2580 0.1038 0.0047  0.0010  -0.0204 231 PHE A CG  
1856 C  CD1 . PHE A 230 ? 0.1576 0.2820 0.1259 0.0038  -0.0025 -0.0495 231 PHE A CD1 
1857 C  CD2 . PHE A 230 ? 0.1646 0.2431 0.1666 0.0227  0.0120  -0.0218 231 PHE A CD2 
1858 C  CE1 . PHE A 230 ? 0.1605 0.2298 0.1328 -0.0149 0.0195  -0.0554 231 PHE A CE1 
1859 C  CE2 . PHE A 230 ? 0.1862 0.2728 0.1230 0.0231  -0.0198 -0.0319 231 PHE A CE2 
1860 C  CZ  . PHE A 230 ? 0.1689 0.2146 0.1982 0.0166  -0.0057 -0.0513 231 PHE A CZ  
1861 N  N   . ASN A 231 ? 0.1474 0.3165 0.1488 0.0239  0.0260  -0.0244 232 ASN A N   
1862 C  CA  . ASN A 231 ? 0.1971 0.2809 0.1725 0.0172  0.0255  -0.0121 232 ASN A CA  
1863 C  C   . ASN A 231 ? 0.1948 0.2609 0.1698 0.0115  0.0201  -0.0152 232 ASN A C   
1864 O  O   . ASN A 231 ? 0.1662 0.2400 0.1899 0.0234  0.0262  -0.0039 232 ASN A O   
1865 C  CB  . ASN A 231 ? 0.1921 0.3353 0.2018 0.0175  0.0335  -0.0606 232 ASN A CB  
1866 C  CG  . ASN A 231 ? 0.1580 0.2797 0.1737 0.0364  -0.0042 0.0154  232 ASN A CG  
1867 O  OD1 . ASN A 231 ? 0.1768 0.2629 0.2050 0.0384  0.0359  -0.0201 232 ASN A OD1 
1868 N  ND2 . ASN A 231 ? 0.2376 0.3885 0.1872 0.0862  -0.0075 -0.0205 232 ASN A ND2 
1869 N  N   . GLY A 232 ? 0.1865 0.2855 0.1698 -0.0161 0.0128  -0.0168 233 GLY A N   
1870 C  CA  . GLY A 232 ? 0.2922 0.2591 0.1657 0.0167  0.0286  -0.0118 233 GLY A CA  
1871 C  C   . GLY A 232 ? 0.3576 0.2391 0.1571 0.0414  0.0245  -0.0179 233 GLY A C   
1872 O  O   . GLY A 232 ? 0.2843 0.2808 0.1691 0.0039  0.0480  -0.0251 233 GLY A O   
1873 N  N   . GLU A 233 ? 0.3376 0.4028 0.1614 -0.0438 0.0398  0.0403  234 GLU A N   
1874 C  CA  . GLU A 233 ? 0.3500 0.5738 0.1885 0.0057  0.0515  -0.0612 234 GLU A CA  
1875 C  C   . GLU A 233 ? 0.4036 0.5740 0.2912 -0.1043 0.1223  -0.0342 234 GLU A C   
1876 O  O   . GLU A 233 ? 0.3539 0.5457 0.2370 -0.0882 0.1345  -0.0631 234 GLU A O   
1877 C  CB  . GLU A 233 ? 0.4282 0.6320 0.3410 0.0547  0.0634  0.1237  234 GLU A CB  
1878 C  CG  . GLU A 233 ? 0.9696 0.9307 0.3218 0.0845  0.0691  -0.1787 234 GLU A CG  
1879 C  CD  . GLU A 233 ? 0.8863 0.9389 0.5100 -0.0536 0.0069  -0.0661 234 GLU A CD  
1880 O  OE1 . GLU A 233 ? 0.4618 1.0434 0.3213 -0.0476 -0.0243 0.0562  234 GLU A OE1 
1881 O  OE2 . GLU A 233 ? 1.3662 1.2482 0.4001 -0.1670 -0.0792 -0.0952 234 GLU A OE2 
1882 N  N   . GLY A 234 ? 0.7030 0.6522 0.1996 0.0879  0.0465  -0.0570 235 GLY A N   
1883 C  CA  . GLY A 234 ? 0.7105 1.0113 0.2060 0.2473  0.1529  -0.1782 235 GLY A CA  
1884 C  C   . GLY A 234 ? 1.2685 0.8094 0.7407 -0.2370 0.0490  -0.0557 235 GLY A C   
1885 O  O   . GLY A 234 ? 1.5229 2.2408 0.3504 0.3186  0.5256  -0.3881 235 GLY A O   
1886 N  N   . GLU A 235 ? 0.9269 0.7488 0.6468 0.3531  -0.3479 -0.2649 236 GLU A N   
1887 C  CA  . GLU A 235 ? 0.4135 0.2629 0.4123 -0.0966 0.2363  -0.1442 236 GLU A CA  
1888 C  C   . GLU A 235 ? 0.2737 0.2676 0.2384 0.0430  0.0562  -0.0039 236 GLU A C   
1889 O  O   . GLU A 235 ? 0.2970 0.4016 0.1858 0.0731  0.0172  -0.0258 236 GLU A O   
1890 C  CB  . GLU A 235 ? 0.3699 0.2486 0.2186 -0.0080 0.0461  -0.0121 236 GLU A CB  
1891 C  CG  . GLU A 235 ? 0.3447 0.2174 0.3496 -0.0685 0.0783  -0.0411 236 GLU A CG  
1892 C  CD  . GLU A 235 ? 0.6493 0.3278 0.3541 -0.0132 0.0364  -0.0885 236 GLU A CD  
1893 O  OE1 . GLU A 235 ? 0.2873 0.5019 0.4488 -0.0710 -0.0655 0.0963  236 GLU A OE1 
1894 O  OE2 . GLU A 235 ? 0.4040 0.3557 0.6447 0.0392  -0.2175 -0.0396 236 GLU A OE2 
1895 N  N   . PRO A 236 ? 0.1974 0.2985 0.3125 0.0336  0.0171  -0.0356 237 PRO A N   
1896 C  CA  . PRO A 236 ? 0.2560 0.3279 0.2755 0.0469  0.0761  -0.0055 237 PRO A CA  
1897 C  C   . PRO A 236 ? 0.2010 0.3027 0.2108 0.0455  0.0361  -0.0702 237 PRO A C   
1898 O  O   . PRO A 236 ? 0.2751 0.2666 0.2057 0.0212  0.0392  -0.0411 237 PRO A O   
1899 C  CB  . PRO A 236 ? 0.1382 0.4083 0.5001 0.0276  0.0288  -0.0151 237 PRO A CB  
1900 C  CG  . PRO A 236 ? 0.1781 0.3707 0.4354 0.0227  -0.0331 0.0340  237 PRO A CG  
1901 C  CD  . PRO A 236 ? 0.2060 0.3540 0.3676 0.0663  -0.0203 -0.0283 237 PRO A CD  
1902 N  N   . GLU A 237 ? 0.2194 0.2794 0.1669 0.0291  0.0494  -0.0128 238 GLU A N   
1903 C  CA  . GLU A 237 ? 0.2239 0.2630 0.1493 0.0116  0.0421  -0.0276 238 GLU A CA  
1904 C  C   . GLU A 237 ? 0.2194 0.2153 0.1788 0.0201  0.0628  -0.0225 238 GLU A C   
1905 O  O   . GLU A 237 ? 0.2779 0.2340 0.1957 0.0591  0.0168  -0.0305 238 GLU A O   
1906 C  CB  . GLU A 237 ? 0.2462 0.2673 0.2187 0.0428  -0.0223 -0.0525 238 GLU A CB  
1907 C  CG  . GLU A 237 ? 0.2595 0.3597 0.2868 -0.0378 -0.0352 0.0295  238 GLU A CG  
1908 C  CD  . GLU A 237 ? 0.3118 0.4100 0.4028 0.0607  0.0622  -0.1498 238 GLU A CD  
1909 O  OE1 . GLU A 237 ? 0.3899 0.4705 0.4025 -0.0107 0.0802  -0.1001 238 GLU A OE1 
1910 O  OE2 . GLU A 237 ? 0.2894 0.4488 0.3832 0.0233  -0.0787 -0.0042 238 GLU A OE2 
1911 N  N   . GLU A 238 ? 0.2072 0.2472 0.1450 0.0407  0.0648  -0.0167 239 GLU A N   
1912 C  CA  . GLU A 238 ? 0.2261 0.2567 0.1468 0.0427  0.0421  -0.0155 239 GLU A CA  
1913 C  C   . GLU A 238 ? 0.1963 0.1953 0.1479 0.0559  0.0285  0.0099  239 GLU A C   
1914 O  O   . GLU A 238 ? 0.2441 0.2172 0.2032 0.0650  0.0262  0.0122  239 GLU A O   
1915 C  CB  . GLU A 238 ? 0.1964 0.2610 0.2976 0.0339  0.0346  -0.0749 239 GLU A CB  
1916 C  CG  . GLU A 238 ? 0.2135 0.4374 0.2996 0.0266  0.0436  -0.0569 239 GLU A CG  
1917 C  CD  . GLU A 238 ? 0.3172 0.3853 0.1999 0.0468  0.0510  -0.0611 239 GLU A CD  
1918 O  OE1 . GLU A 238 ? 0.4311 0.5220 0.2387 0.0979  0.0714  0.0313  239 GLU A OE1 
1919 O  OE2 . GLU A 238 ? 0.4265 0.4697 0.3513 -0.0274 0.0704  0.0064  239 GLU A OE2 
1920 N  N   . LEU A 239 ? 0.2167 0.2312 0.1567 0.0455  0.0316  -0.0242 240 LEU A N   
1921 C  CA  . LEU A 239 ? 0.1991 0.2570 0.1264 0.0717  0.0305  -0.0205 240 LEU A CA  
1922 C  C   . LEU A 239 ? 0.1902 0.2233 0.1161 0.0412  0.0129  0.0020  240 LEU A C   
1923 O  O   . LEU A 239 ? 0.2082 0.2411 0.1279 0.0710  0.0087  -0.0037 240 LEU A O   
1924 C  CB  . LEU A 239 ? 0.2386 0.2474 0.1860 0.0289  -0.0009 -0.0248 240 LEU A CB  
1925 C  CG  . LEU A 239 ? 0.2133 0.2514 0.2604 0.0617  -0.0098 -0.0661 240 LEU A CG  
1926 C  CD1 . LEU A 239 ? 0.2721 0.2057 0.4857 0.0524  -0.0658 -0.0736 240 LEU A CD1 
1927 C  CD2 . LEU A 239 ? 0.3204 0.2817 0.2368 0.0861  -0.0574 -0.0911 240 LEU A CD2 
1928 N  N   . MET A 240 ? 0.2038 0.2156 0.1275 0.0692  0.0275  -0.0192 241 MET A N   
1929 C  CA  . MET A 240 ? 0.1855 0.2021 0.1070 0.0511  0.0205  -0.0024 241 MET A CA  
1930 C  C   . MET A 240 ? 0.1553 0.1830 0.1206 0.0354  0.0003  -0.0319 241 MET A C   
1931 O  O   . MET A 240 ? 0.1506 0.2075 0.1410 0.0364  -0.0190 -0.0194 241 MET A O   
1932 C  CB  . MET A 240 ? 0.1636 0.1980 0.1372 0.0500  0.0043  -0.0239 241 MET A CB  
1933 C  CG  . MET A 240 ? 0.1556 0.1927 0.1417 0.0348  0.0052  -0.0203 241 MET A CG  
1934 S  SD  . MET A 240 ? 0.1524 0.1844 0.1639 0.0178  0.0209  -0.0073 241 MET A SD  
1935 C  CE  . MET A 240 ? 0.1867 0.2114 0.1599 0.0469  0.0359  0.0033  241 MET A CE  
1936 N  N   . VAL A 241 ? 0.1561 0.1694 0.1153 0.0414  -0.0103 -0.0223 242 VAL A N   
1937 C  CA  . VAL A 241 ? 0.1906 0.1777 0.0885 0.0381  -0.0132 -0.0190 242 VAL A CA  
1938 C  C   . VAL A 241 ? 0.1324 0.1321 0.1059 0.0414  -0.0097 -0.0212 242 VAL A C   
1939 O  O   . VAL A 241 ? 0.1317 0.1941 0.1420 0.0264  -0.0043 -0.0385 242 VAL A O   
1940 C  CB  . VAL A 241 ? 0.1809 0.1743 0.1244 0.0263  -0.0132 -0.0358 242 VAL A CB  
1941 C  CG1 . VAL A 241 ? 0.2258 0.1863 0.1476 0.0263  -0.0486 -0.0495 242 VAL A CG1 
1942 C  CG2 . VAL A 241 ? 0.1957 0.1734 0.1802 0.0460  0.0251  -0.0425 242 VAL A CG2 
1943 N  N   . ASP A 242 ? 0.1747 0.1521 0.0845 0.0387  0.0055  -0.0337 243 ASP A N   
1944 C  CA  . ASP A 242 ? 0.1540 0.1420 0.1115 0.0483  -0.0163 -0.0359 243 ASP A CA  
1945 C  C   . ASP A 242 ? 0.1322 0.1471 0.1186 0.0392  -0.0092 -0.0291 243 ASP A C   
1946 O  O   . ASP A 242 ? 0.1350 0.1593 0.1522 0.0256  -0.0364 -0.0226 243 ASP A O   
1947 C  CB  . ASP A 242 ? 0.1461 0.1522 0.1470 0.0454  -0.0356 -0.0321 243 ASP A CB  
1948 C  CG  . ASP A 242 ? 0.1903 0.1393 0.1232 0.0499  -0.0009 -0.0194 243 ASP A CG  
1949 O  OD1 . ASP A 242 ? 0.1632 0.1361 0.1370 0.0462  -0.0058 -0.0280 243 ASP A OD1 
1950 O  OD2 . ASP A 242 ? 0.1883 0.1601 0.1928 0.0569  0.0022  -0.0469 243 ASP A OD2 
1951 N  N   . ASN A 243 ? 0.1279 0.1307 0.1098 0.0240  -0.0008 -0.0239 244 ASN A N   
1952 C  CA  . ASN A 243 ? 0.1351 0.1393 0.0745 -0.0060 0.0030  0.0002  244 ASN A CA  
1953 C  C   . ASN A 243 ? 0.1304 0.1187 0.0826 -0.0041 0.0194  0.0044  244 ASN A C   
1954 O  O   . ASN A 243 ? 0.1504 0.1273 0.1266 0.0306  0.0068  -0.0022 244 ASN A O   
1955 C  CB  . ASN A 243 ? 0.1156 0.1632 0.1000 0.0125  0.0047  0.0030  244 ASN A CB  
1956 C  CG  . ASN A 243 ? 0.1186 0.1544 0.0960 0.0073  0.0102  -0.0001 244 ASN A CG  
1957 O  OD1 . ASN A 243 ? 0.1203 0.1658 0.1549 0.0096  -0.0060 0.0076  244 ASN A OD1 
1958 N  ND2 . ASN A 243 ? 0.1546 0.1727 0.1526 0.0087  -0.0256 0.0265  244 ASN A ND2 
1959 N  N   . TRP A 244 ? 0.1301 0.1367 0.0894 -0.0027 -0.0047 -0.0005 245 TRP A N   
1960 C  CA  . TRP A 244 ? 0.1256 0.1293 0.0895 0.0058  -0.0024 0.0055  245 TRP A CA  
1961 C  C   . TRP A 244 ? 0.1023 0.1364 0.1335 0.0111  -0.0006 -0.0139 245 TRP A C   
1962 O  O   . TRP A 244 ? 0.1174 0.1392 0.1572 0.0345  -0.0170 -0.0319 245 TRP A O   
1963 C  CB  . TRP A 244 ? 0.1276 0.1138 0.1159 0.0069  -0.0055 0.0017  245 TRP A CB  
1964 C  CG  . TRP A 244 ? 0.1058 0.1226 0.1080 0.0027  -0.0016 -0.0018 245 TRP A CG  
1965 C  CD1 . TRP A 244 ? 0.1433 0.1187 0.1274 0.0088  -0.0154 -0.0166 245 TRP A CD1 
1966 C  CD2 . TRP A 244 ? 0.1342 0.1197 0.1119 0.0170  0.0063  -0.0015 245 TRP A CD2 
1967 N  NE1 . TRP A 244 ? 0.1433 0.1289 0.1374 0.0185  -0.0156 -0.0138 245 TRP A NE1 
1968 C  CE2 . TRP A 244 ? 0.1251 0.1226 0.1450 0.0179  -0.0118 -0.0129 245 TRP A CE2 
1969 C  CE3 . TRP A 244 ? 0.1322 0.1448 0.1138 0.0086  -0.0089 0.0139  245 TRP A CE3 
1970 C  CZ2 . TRP A 244 ? 0.1471 0.1278 0.1676 0.0173  -0.0245 -0.0033 245 TRP A CZ2 
1971 C  CZ3 . TRP A 244 ? 0.1694 0.1409 0.1476 0.0177  -0.0204 0.0125  245 TRP A CZ3 
1972 C  CH2 . TRP A 244 ? 0.1535 0.1556 0.1623 0.0438  -0.0195 0.0030  245 TRP A CH2 
1973 N  N   . ARG A 245 ? 0.1185 0.1349 0.1169 -0.0055 0.0020  -0.0150 246 ARG A N   
1974 C  CA  . ARG A 245 ? 0.1045 0.1271 0.1254 0.0103  -0.0086 -0.0068 246 ARG A CA  
1975 C  C   . ARG A 245 ? 0.1180 0.1199 0.1159 0.0040  0.0025  -0.0264 246 ARG A C   
1976 O  O   . ARG A 245 ? 0.1172 0.1471 0.1420 -0.0070 0.0098  -0.0124 246 ARG A O   
1977 C  CB  . ARG A 245 ? 0.1041 0.1452 0.1142 -0.0097 0.0046  -0.0276 246 ARG A CB  
1978 C  CG  . ARG A 245 ? 0.0955 0.1294 0.1485 -0.0020 -0.0089 -0.0077 246 ARG A CG  
1979 C  CD  . ARG A 245 ? 0.1076 0.1280 0.1521 -0.0064 -0.0255 -0.0140 246 ARG A CD  
1980 N  NE  . ARG A 245 ? 0.1183 0.1490 0.1086 -0.0115 -0.0061 -0.0150 246 ARG A NE  
1981 C  CZ  . ARG A 245 ? 0.1151 0.1653 0.1147 -0.0173 0.0170  -0.0203 246 ARG A CZ  
1982 N  NH1 . ARG A 245 ? 0.1333 0.1723 0.1129 -0.0067 0.0239  -0.0065 246 ARG A NH1 
1983 N  NH2 . ARG A 245 ? 0.1313 0.1830 0.1367 -0.0359 -0.0137 -0.0119 246 ARG A NH2 
1984 N  N   . PRO A 246 ? 0.1248 0.1340 0.1434 0.0108  -0.0037 -0.0039 247 PRO A N   
1985 C  CA  . PRO A 246 ? 0.1611 0.1447 0.1172 0.0378  0.0024  -0.0034 247 PRO A CA  
1986 C  C   . PRO A 246 ? 0.1311 0.1536 0.1165 0.0109  0.0036  -0.0075 247 PRO A C   
1987 O  O   . PRO A 246 ? 0.1397 0.1330 0.1288 0.0106  -0.0131 -0.0132 247 PRO A O   
1988 C  CB  . PRO A 246 ? 0.1650 0.1863 0.1526 0.0541  0.0051  0.0244  247 PRO A CB  
1989 C  CG  . PRO A 246 ? 0.2201 0.2547 0.2278 0.0745  0.0472  0.0956  247 PRO A CG  
1990 C  CD  . PRO A 246 ? 0.1237 0.1734 0.1632 0.0509  0.0108  0.0055  247 PRO A CD  
1991 N  N   . ALA A 247 ? 0.1540 0.1498 0.1104 0.0200  0.0152  0.0046  248 ALA A N   
1992 C  CA  . ALA A 247 ? 0.1533 0.1633 0.0828 0.0041  0.0067  -0.0044 248 ALA A CA  
1993 C  C   . ALA A 247 ? 0.1276 0.1324 0.1208 0.0277  0.0016  0.0087  248 ALA A C   
1994 O  O   . ALA A 247 ? 0.1511 0.1637 0.1526 0.0475  -0.0086 0.0044  248 ALA A O   
1995 C  CB  . ALA A 247 ? 0.1953 0.1740 0.1172 -0.0013 0.0234  0.0149  248 ALA A CB  
1996 N  N   . GLN A 248 ? 0.1283 0.1288 0.1196 0.0005  -0.0107 0.0031  249 GLN A N   
1997 C  CA  . GLN A 248 ? 0.1029 0.1436 0.1221 0.0156  -0.0081 0.0018  249 GLN A CA  
1998 C  C   . GLN A 248 ? 0.1372 0.1502 0.1307 0.0271  -0.0127 0.0012  249 GLN A C   
1999 O  O   . GLN A 248 ? 0.1714 0.1619 0.1097 0.0226  0.0102  0.0128  249 GLN A O   
2000 C  CB  . GLN A 248 ? 0.1445 0.1417 0.1278 -0.0015 -0.0199 0.0091  249 GLN A CB  
2001 C  CG  . GLN A 248 ? 0.1324 0.1683 0.1147 -0.0019 -0.0072 0.0080  249 GLN A CG  
2002 C  CD  . GLN A 248 ? 0.1210 0.1917 0.1415 -0.0162 0.0121  0.0044  249 GLN A CD  
2003 O  OE1 . GLN A 248 ? 0.1368 0.2480 0.1808 -0.0334 0.0044  -0.0208 249 GLN A OE1 
2004 N  NE2 . GLN A 248 ? 0.1707 0.1872 0.1192 0.0107  0.0008  0.0066  249 GLN A NE2 
2005 N  N   . PRO A 249 ? 0.1553 0.1849 0.1267 0.0337  -0.0200 -0.0109 250 PRO A N   
2006 C  CA  . PRO A 249 ? 0.1896 0.2303 0.1208 0.0700  -0.0322 -0.0105 250 PRO A CA  
2007 C  C   . PRO A 249 ? 0.1723 0.1673 0.1216 0.0356  -0.0190 -0.0102 250 PRO A C   
2008 O  O   . PRO A 249 ? 0.1473 0.1806 0.1456 0.0340  -0.0162 0.0159  250 PRO A O   
2009 C  CB  . PRO A 249 ? 0.1848 0.3353 0.1583 0.0961  -0.0515 -0.0380 250 PRO A CB  
2010 C  CG  . PRO A 249 ? 0.2233 0.3705 0.1268 0.0302  -0.0291 -0.0162 250 PRO A CG  
2011 C  CD  . PRO A 249 ? 0.1305 0.2731 0.1730 0.0337  -0.0323 0.0051  250 PRO A CD  
2012 N  N   . LEU A 250 ? 0.1985 0.1712 0.1132 0.0483  -0.0013 0.0005  251 LEU A N   
2013 C  CA  . LEU A 250 ? 0.1641 0.1655 0.1303 0.0309  0.0058  0.0035  251 LEU A CA  
2014 C  C   . LEU A 250 ? 0.1738 0.1712 0.1168 0.0417  -0.0176 0.0092  251 LEU A C   
2015 O  O   . LEU A 250 ? 0.1587 0.1455 0.1562 0.0178  -0.0267 0.0015  251 LEU A O   
2016 C  CB  . LEU A 250 ? 0.2325 0.1619 0.1612 0.0013  0.0242  -0.0021 251 LEU A CB  
2017 C  CG  . LEU A 250 ? 0.2384 0.2243 0.1077 -0.0142 0.0334  -0.0093 251 LEU A CG  
2018 C  CD1 . LEU A 250 ? 0.2222 0.2481 0.1111 -0.0181 -0.0006 -0.0219 251 LEU A CD1 
2019 C  CD2 . LEU A 250 ? 0.3262 0.2147 0.2042 -0.0450 0.0544  0.0147  251 LEU A CD2 
2020 N  N   . LYS A 251 ? 0.1687 0.2183 0.1328 0.0343  -0.0164 0.0073  252 LYS A N   
2021 C  CA  . LYS A 251 ? 0.1727 0.2463 0.1533 0.0306  -0.0274 -0.0044 252 LYS A CA  
2022 C  C   . LYS A 251 ? 0.1673 0.2278 0.2032 0.0423  -0.0335 -0.0098 252 LYS A C   
2023 O  O   . LYS A 251 ? 0.2347 0.3710 0.1641 -0.0127 0.0166  -0.0124 252 LYS A O   
2024 C  CB  . LYS A 251 ? 0.1762 0.2886 0.2059 -0.0357 0.0062  -0.0476 252 LYS A CB  
2025 C  CG  . LYS A 251 ? 0.2861 0.3489 0.1956 0.0100  0.0776  -0.0377 252 LYS A CG  
2026 C  CD  . LYS A 251 ? 0.2468 0.3779 0.2244 0.0002  0.0288  -0.0307 252 LYS A CD  
2027 C  CE  . LYS A 251 ? 0.2169 0.4255 0.3254 0.0083  0.0368  -0.0923 252 LYS A CE  
2028 N  NZ  . LYS A 251 ? 0.2195 0.4670 0.5576 -0.0105 0.0571  -0.0079 252 LYS A NZ  
2029 N  N   . ASN A 252 ? 0.1805 0.2597 0.1329 0.0376  -0.0254 -0.0239 253 ASN A N   
2030 C  CA  . ASN A 252 ? 0.2753 0.4418 0.1917 0.0820  -0.0493 -0.1353 253 ASN A CA  
2031 C  C   . ASN A 252 ? 0.2606 0.3820 0.2220 0.1044  -0.0333 -0.1312 253 ASN A C   
2032 O  O   . ASN A 252 ? 0.4078 0.3659 0.3993 0.1293  0.0693  -0.0663 253 ASN A O   
2033 C  CB  . ASN A 252 ? 0.3302 0.4615 0.3450 0.0288  -0.0441 -0.1723 253 ASN A CB  
2034 C  CG  . ASN A 252 ? 0.5384 0.4226 0.3937 0.0216  0.0974  -0.1153 253 ASN A CG  
2035 O  OD1 . ASN A 252 ? 0.8099 0.6846 0.4439 -0.0524 0.1703  0.0527  253 ASN A OD1 
2036 N  ND2 . ASN A 252 ? 0.4012 0.4397 0.5208 -0.0194 -0.0301 -0.2171 253 ASN A ND2 
2037 N  N   . ARG A 253 ? 0.1902 0.3118 0.1120 0.0495  -0.0128 0.0104  254 ARG A N   
2038 C  CA  . ARG A 253 ? 0.1569 0.2067 0.1186 0.0155  -0.0039 0.0039  254 ARG A CA  
2039 C  C   . ARG A 253 ? 0.2118 0.2048 0.1322 0.0218  0.0380  0.0088  254 ARG A C   
2040 O  O   . ARG A 253 ? 0.2694 0.2208 0.2847 0.0427  0.0958  0.0573  254 ARG A O   
2041 C  CB  . ARG A 253 ? 0.1618 0.1874 0.1050 -0.0030 -0.0073 -0.0023 254 ARG A CB  
2042 C  CG  . ARG A 253 ? 0.1795 0.1698 0.0932 -0.0027 -0.0024 -0.0065 254 ARG A CG  
2043 C  CD  . ARG A 253 ? 0.1820 0.1536 0.0949 0.0229  0.0132  -0.0120 254 ARG A CD  
2044 N  NE  . ARG A 253 ? 0.1246 0.1399 0.1047 0.0054  0.0031  -0.0012 254 ARG A NE  
2045 C  CZ  . ARG A 253 ? 0.1228 0.1397 0.0880 -0.0108 -0.0006 0.0051  254 ARG A CZ  
2046 N  NH1 . ARG A 253 ? 0.1064 0.1494 0.1115 -0.0184 -0.0120 0.0055  254 ARG A NH1 
2047 N  NH2 . ARG A 253 ? 0.1168 0.1533 0.1005 0.0065  -0.0024 -0.0074 254 ARG A NH2 
2048 N  N   A GLN A 254 ? 0.1655 0.2068 0.1179 -0.0127 -0.0023 -0.0386 255 GLN A N   
2049 N  N   B GLN A 254 ? 0.1633 0.2445 0.2014 -0.0138 0.0082  -0.0491 255 GLN A N   
2050 C  CA  A GLN A 254 ? 0.1506 0.2890 0.1442 -0.0266 0.0049  -0.0447 255 GLN A CA  
2051 C  CA  B GLN A 254 ? 0.1597 0.3218 0.1551 -0.0398 -0.0168 -0.0307 255 GLN A CA  
2052 C  C   A GLN A 254 ? 0.2005 0.1973 0.1342 -0.0005 -0.0143 -0.0082 255 GLN A C   
2053 C  C   B GLN A 254 ? 0.2210 0.2268 0.1416 -0.0250 -0.0356 -0.0100 255 GLN A C   
2054 O  O   A GLN A 254 ? 0.2088 0.2133 0.1615 -0.0228 -0.0177 -0.0030 255 GLN A O   
2055 O  O   B GLN A 254 ? 0.3161 0.2118 0.2881 -0.0168 -0.0822 -0.0290 255 GLN A O   
2056 C  CB  A GLN A 254 ? 0.1845 0.3655 0.1838 -0.0264 0.0150  -0.1098 255 GLN A CB  
2057 C  CB  B GLN A 254 ? 0.2451 0.3890 0.1558 -0.0417 -0.0127 -0.0916 255 GLN A CB  
2058 C  CG  A GLN A 254 ? 0.1220 0.4621 0.2330 -0.0456 -0.0083 -0.1059 255 GLN A CG  
2059 C  CG  B GLN A 254 ? 0.3090 0.3877 0.0993 -0.0150 0.0289  -0.0040 255 GLN A CG  
2060 N  N   . ILE A 255 ? 0.1468 0.2078 0.1109 -0.0070 0.0016  -0.0004 256 ILE A N   
2061 C  CA  . ILE A 255 ? 0.1311 0.1738 0.1346 0.0302  -0.0157 -0.0013 256 ILE A CA  
2062 C  C   . ILE A 255 ? 0.1344 0.1633 0.1507 -0.0055 -0.0015 0.0248  256 ILE A C   
2063 O  O   . ILE A 255 ? 0.1702 0.1768 0.1524 0.0181  0.0185  0.0391  256 ILE A O   
2064 C  CB  . ILE A 255 ? 0.1469 0.1664 0.1650 0.0230  -0.0222 -0.0142 256 ILE A CB  
2065 C  CG1 . ILE A 255 ? 0.1720 0.2030 0.1571 0.0532  0.0006  -0.0083 256 ILE A CG1 
2066 C  CG2 . ILE A 255 ? 0.1668 0.2197 0.1339 0.0212  -0.0120 -0.0270 256 ILE A CG2 
2067 C  CD1 . ILE A 255 ? 0.1878 0.2229 0.1727 0.0244  0.0388  -0.0194 256 ILE A CD1 
2068 N  N   . LYS A 256 ? 0.1263 0.1845 0.1144 0.0115  -0.0120 0.0184  257 LYS A N   
2069 C  CA  . LYS A 256 ? 0.1455 0.1984 0.0989 0.0108  0.0009  0.0020  257 LYS A CA  
2070 C  C   . LYS A 256 ? 0.1468 0.1987 0.0777 -0.0050 -0.0012 0.0209  257 LYS A C   
2071 O  O   . LYS A 256 ? 0.1788 0.2441 0.0813 -0.0630 0.0062  0.0070  257 LYS A O   
2072 C  CB  . LYS A 256 ? 0.1452 0.2131 0.1427 0.0163  0.0079  -0.0114 257 LYS A CB  
2073 C  CG  . LYS A 256 ? 0.2528 0.2841 0.1956 -0.0259 -0.0050 -0.0444 257 LYS A CG  
2074 C  CD  . LYS A 256 ? 0.4083 0.3455 0.4132 -0.0219 -0.0277 -0.1544 257 LYS A CD  
2075 N  N   . ALA A 257 ? 0.1465 0.2091 0.1009 -0.0141 0.0216  0.0216  258 ALA A N   
2076 C  CA  . ALA A 257 ? 0.1300 0.2073 0.1514 -0.0032 0.0091  0.0017  258 ALA A CA  
2077 C  C   . ALA A 257 ? 0.1504 0.2090 0.1160 -0.0032 0.0133  -0.0234 258 ALA A C   
2078 O  O   . ALA A 257 ? 0.1587 0.2424 0.1141 -0.0023 0.0093  -0.0265 258 ALA A O   
2079 C  CB  . ALA A 257 ? 0.1690 0.2014 0.2096 0.0082  0.0135  0.0175  258 ALA A CB  
2080 N  N   . SER A 258 ? 0.1333 0.2043 0.1360 -0.0031 0.0029  0.0025  259 SER A N   
2081 C  CA  . SER A 258 ? 0.1317 0.2175 0.1520 -0.0108 0.0122  -0.0041 259 SER A CA  
2082 C  C   . SER A 258 ? 0.1574 0.2560 0.1020 -0.0255 0.0255  -0.0134 259 SER A C   
2083 O  O   . SER A 258 ? 0.1492 0.3504 0.2384 0.0262  0.0348  0.0105  259 SER A O   
2084 C  CB  . SER A 258 ? 0.1684 0.2573 0.1196 0.0068  -0.0079 -0.0107 259 SER A CB  
2085 O  OG  . SER A 258 ? 0.1342 0.2675 0.1297 0.0193  0.0228  -0.0063 259 SER A OG  
2086 N  N   . PHE A 259 ? 0.1666 0.2557 0.1511 -0.0322 0.0100  0.0063  260 PHE A N   
2087 C  CA  . PHE A 259 ? 0.1896 0.2803 0.2075 -0.0615 0.0179  -0.0040 260 PHE A CA  
2088 C  C   . PHE A 259 ? 0.2375 0.3744 0.1554 -0.0722 0.0402  0.0272  260 PHE A C   
2089 O  O   . PHE A 259 ? 0.2738 0.2366 0.2388 -0.0785 0.0005  0.0397  260 PHE A O   
2090 C  CB  . PHE A 259 ? 0.1719 0.2974 0.2408 -0.0527 0.0334  -0.0467 260 PHE A CB  
2091 C  CG  . PHE A 259 ? 0.1733 0.2649 0.1916 -0.0181 0.0139  0.0129  260 PHE A CG  
2092 C  CD1 . PHE A 259 ? 0.1601 0.2311 0.1611 -0.0263 -0.0033 -0.0044 260 PHE A CD1 
2093 C  CD2 . PHE A 259 ? 0.2429 0.2415 0.3154 -0.0163 -0.0034 0.0062  260 PHE A CD2 
2094 C  CE1 . PHE A 259 ? 0.1768 0.2469 0.2151 -0.0219 0.0069  -0.0066 260 PHE A CE1 
2095 C  CE2 . PHE A 259 ? 0.2451 0.2632 0.3606 -0.0376 0.0268  0.0247  260 PHE A CE2 
2096 C  CZ  . PHE A 259 ? 0.1959 0.2440 0.3071 -0.0173 -0.0019 -0.0077 260 PHE A CZ  
2097 N  N   . LYS A 260 ? 0.3836 0.5256 0.2125 -0.2170 0.0477  0.0767  261 LYS A N   
2098 C  CA  . LYS A 260 ? 0.4901 0.6670 0.2858 0.0176  0.0941  0.2357  261 LYS A CA  
2099 C  C   . LYS A 260 ? 0.5673 0.8584 0.3541 -0.0141 0.0640  0.1620  261 LYS A C   
2100 O  O   . LYS A 260 ? 0.4678 0.9787 0.8282 -0.0381 0.2631  -0.0243 261 LYS A O   
2101 C  CB  . LYS A 260 ? 0.5608 0.8362 0.3903 0.0781  0.1888  0.0077  261 LYS A CB  
2102 C  CG  . LYS A 260 ? 0.5873 0.5035 0.5759 -0.1078 -0.0236 0.0936  261 LYS A CG  
2103 C  CD  . LYS A 260 ? 0.5664 0.4967 0.8061 -0.3106 0.1130  0.1433  261 LYS A CD  
2104 O  OXT . LYS A 260 ? 0.5911 1.0711 0.9038 -0.0203 -0.2768 0.2284  261 LYS A OXT 
2105 ZN ZN  . ZN  B .   ? 0.1040 0.0996 0.1039 0.0023  -0.0114 -0.0036 301 ZN  A ZN  
2106 S  S   . DMS C .   ? 0.2467 0.3218 0.2815 -0.0034 -0.0058 -0.0375 302 DMS A S   
2107 O  O   . DMS C .   ? 0.3571 0.4940 0.3522 0.1050  0.0225  -0.1992 302 DMS A O   
2108 C  C1  . DMS C .   ? 0.2199 0.3312 0.2570 0.0773  -0.0374 -0.0574 302 DMS A C1  
2109 C  C2  . DMS C .   ? 0.1881 0.3542 0.5403 -0.0408 0.0289  -0.0217 302 DMS A C2  
2110 O  O19 . 5EF D .   ? 0.3345 0.3570 0.3914 0.0272  0.0333  0.1142  303 5EF A O19 
2111 C  C17 . 5EF D .   ? 0.2115 0.3669 0.2430 -0.0558 0.0206  0.0260  303 5EF A C17 
2112 C  C6  . 5EF D .   ? 0.1254 0.1508 0.1878 -0.0012 -0.0061 0.0110  303 5EF A C6  
2113 F  F11 . 5EF D .   ? 0.1401 0.1522 0.1975 0.0159  0.0108  0.0062  303 5EF A F11 
2114 C  C5  . 5EF D .   ? 0.1296 0.1260 0.1569 -0.0098 -0.0407 -0.0048 303 5EF A C5  
2115 F  F12 . 5EF D .   ? 0.2527 0.2220 0.1813 0.0190  0.0326  0.0181  303 5EF A F12 
2116 F  F13 . 5EF D .   ? 0.2474 0.1347 0.1465 -0.0041 -0.0507 -0.0168 303 5EF A F13 
2117 O  O16 . 5EF D .   ? 0.4118 0.2147 0.2869 0.0209  0.0446  0.0989  303 5EF A O16 
2118 S  S14 . 5EF D .   ? 0.3048 0.2426 0.2056 0.0046  0.0201  0.0556  303 5EF A S14 
2119 O  O15 . 5EF D .   ? 0.2477 0.3993 0.2115 0.0017  -0.0440 0.0156  303 5EF A O15 
2120 C  C18 . 5EF D .   ? 0.2149 0.3186 0.3172 -0.0165 0.0321  -0.0042 303 5EF A C18 
2121 C  C8  . 5EF D .   ? 0.2427 0.1722 0.1630 0.0108  -0.0230 -0.0038 303 5EF A C8  
2122 C  C7  . 5EF D .   ? 0.1851 0.1684 0.1888 -0.0030 -0.0023 -0.0004 303 5EF A C7  
2123 C  C9  . 5EF D .   ? 0.1844 0.1571 0.1363 0.0019  -0.0373 0.0179  303 5EF A C9  
2124 C  C10 . 5EF D .   ? 0.2140 0.1480 0.1077 -0.0149 -0.0443 -0.0089 303 5EF A C10 
2125 S  S1  . 5EF D .   ? 0.1340 0.1063 0.1432 0.0053  -0.0384 -0.0118 303 5EF A S1  
2126 O  O3  . 5EF D .   ? 0.1172 0.1283 0.1492 0.0162  -0.0358 -0.0115 303 5EF A O3  
2127 N  N4  . 5EF D .   ? 0.1154 0.0993 0.1391 -0.0150 -0.0333 -0.0095 303 5EF A N4  
2128 O  O2  . 5EF D .   ? 0.1619 0.1084 0.1600 0.0171  -0.0670 -0.0182 303 5EF A O2  
2129 N  N20 . 5EF D .   ? 0.2797 0.1437 0.1655 -0.0064 -0.0644 -0.0054 303 5EF A N20 
2130 C  C21 . 5EF D .   ? 0.1899 0.1659 0.1877 -0.0173 -0.0168 0.0114  303 5EF A C21 
2131 C  C25 . 5EF D .   ? 0.1978 0.1963 0.2045 -0.0325 -0.0168 -0.0020 303 5EF A C25 
2132 C  C24 . 5EF D .   ? 0.2325 0.2111 0.2100 -0.0370 -0.0020 -0.0252 303 5EF A C24 
2133 C  C23 . 5EF D .   ? 0.2376 0.1529 0.1953 -0.0316 -0.0237 0.0030  303 5EF A C23 
2134 C  C29 . 5EF D .   ? 0.2753 0.2098 0.1797 0.0174  -0.0289 -0.0104 303 5EF A C29 
2135 C  C28 . 5EF D .   ? 0.2506 0.2128 0.2513 -0.0190 -0.0452 -0.0229 303 5EF A C28 
2136 C  C27 . 5EF D .   ? 0.2353 0.2300 0.2479 -0.0201 0.0271  -0.0684 303 5EF A C27 
2137 C  C26 . 5EF D .   ? 0.2183 0.2427 0.1826 -0.0015 -0.0053 -0.0650 303 5EF A C26 
2138 C  C22 . 5EF D .   ? 0.2309 0.1919 0.1371 -0.0274 0.0175  -0.0077 303 5EF A C22 
2139 O  O19 . 5EF E .   ? 0.7258 0.9460 0.9232 0.2299  0.0762  -0.3188 304 5EF A O19 
2140 C  C17 . 5EF E .   ? 0.3713 0.7991 0.6952 -0.1844 -0.0488 -0.2477 304 5EF A C17 
2141 C  C6  . 5EF E .   ? 0.2698 0.3728 0.4400 -0.0584 0.0095  -0.0832 304 5EF A C6  
2142 F  F11 . 5EF E .   ? 0.3781 0.4930 0.4049 0.0741  -0.0334 -0.0585 304 5EF A F11 
2143 C  C5  . 5EF E .   ? 0.3639 0.2746 0.4765 -0.0037 -0.0015 -0.0727 304 5EF A C5  
2144 F  F12 . 5EF E .   ? 0.3165 0.3596 0.4959 0.0095  0.0061  -0.1268 304 5EF A F12 
2145 F  F13 . 5EF E .   ? 0.4808 0.3026 0.5695 -0.0092 0.0321  -0.0925 304 5EF A F13 
2146 O  O16 . 5EF E .   ? 0.6595 0.7607 0.4674 0.1452  0.2256  -0.0731 304 5EF A O16 
2147 S  S14 . 5EF E .   ? 0.3565 0.3587 0.5421 -0.0201 0.0293  -0.0776 304 5EF A S14 
2148 O  O15 . 5EF E .   ? 0.5256 0.4044 0.8167 0.1375  0.3210  0.0173  304 5EF A O15 
2149 C  C18 . 5EF E .   ? 0.3945 0.9826 0.7983 0.0921  0.0687  -0.2679 304 5EF A C18 
2150 C  C8  . 5EF E .   ? 0.2199 0.3307 0.4675 -0.0340 0.0341  -0.1204 304 5EF A C8  
2151 C  C7  . 5EF E .   ? 0.2551 0.3098 0.4261 0.0206  0.0185  -0.0812 304 5EF A C7  
2152 C  C9  . 5EF E .   ? 0.2588 0.3008 0.4477 0.0487  -0.0292 -0.1394 304 5EF A C9  
2153 C  C10 . 5EF E .   ? 0.2605 0.2658 0.4878 0.0620  -0.0206 -0.0342 304 5EF A C10 
2154 S  S1  . 5EF E .   ? 0.4173 0.3163 0.6758 0.0240  0.0419  -0.0140 304 5EF A S1  
2155 O  O3  . 5EF E .   ? 0.4117 0.1653 0.4400 0.0388  -0.2050 -0.0810 304 5EF A O3  
2156 N  N4  . 5EF E .   ? 0.1723 0.2108 0.4748 0.0222  -0.0388 -0.1183 304 5EF A N4  
2157 O  O2  . 5EF E .   ? 0.3875 0.2404 0.4972 0.0789  -0.0614 0.0040  304 5EF A O2  
2158 N  N20 . 5EF E .   ? 0.2221 0.2958 0.3748 0.0385  -0.0430 -0.0691 304 5EF A N20 
2159 C  C21 . 5EF E .   ? 0.2658 0.2871 0.3572 0.0950  -0.1100 -0.0512 304 5EF A C21 
2160 C  C25 . 5EF E .   ? 0.5360 0.3974 0.5015 0.1033  0.1514  0.0921  304 5EF A C25 
2161 C  C24 . 5EF E .   ? 0.4433 0.3922 0.3349 0.1454  -0.0064 -0.0017 304 5EF A C24 
2162 C  C23 . 5EF E .   ? 0.4976 0.3576 0.3946 0.0589  0.0735  0.0081  304 5EF A C23 
2163 C  C29 . 5EF E .   ? 0.3199 0.4473 0.4314 0.0185  0.1060  0.0067  304 5EF A C29 
2164 C  C28 . 5EF E .   ? 0.4233 0.2952 0.4936 0.0430  0.0502  -0.0361 304 5EF A C28 
2165 C  C27 . 5EF E .   ? 0.3453 0.3776 0.4601 0.0715  -0.0228 -0.1664 304 5EF A C27 
2166 C  C26 . 5EF E .   ? 0.2414 0.3334 0.4633 0.0019  -0.0070 -0.0137 304 5EF A C26 
2167 C  C22 . 5EF E .   ? 0.3251 0.3343 0.3310 -0.0017 -0.0803 -0.0926 304 5EF A C22 
2168 O  O   . HOH F .   ? 0.4136 0.3585 0.5034 0.0058  0.0013  0.1852  401 HOH A O   
2169 O  O   . HOH F .   ? 0.2798 0.4022 0.2337 0.0486  0.0198  0.0179  402 HOH A O   
2170 O  O   . HOH F .   ? 0.3215 0.2450 0.5685 -0.0526 0.0138  -0.0456 403 HOH A O   
2171 O  O   . HOH F .   ? 0.2132 0.1144 0.2084 -0.0013 -0.0587 0.0018  404 HOH A O   
2172 O  O   . HOH F .   ? 0.4712 0.4313 0.7377 0.0396  0.0727  -0.2614 405 HOH A O   
2173 O  O   . HOH F .   ? 0.5953 0.6067 0.3565 -0.1232 0.0491  0.2251  406 HOH A O   
2174 O  O   . HOH F .   ? 0.4220 0.3422 0.5795 -0.0037 -0.1297 0.1737  407 HOH A O   
2175 O  O   . HOH F .   ? 0.3428 0.2512 0.4471 -0.0534 -0.0483 0.0361  408 HOH A O   
2176 O  O   . HOH F .   ? 0.3834 0.6292 0.3048 -0.0666 0.0364  -0.0517 409 HOH A O   
2177 O  O   . HOH F .   ? 0.2786 1.2269 0.2763 0.1412  0.0011  0.1495  410 HOH A O   
2178 O  O   . HOH F .   ? 0.5224 0.5109 0.3139 -0.0243 -0.0268 -0.0587 411 HOH A O   
2179 O  O   . HOH F .   ? 0.2067 0.3838 0.3093 0.0583  0.0140  -0.0493 412 HOH A O   
2180 O  O   . HOH F .   ? 0.4548 0.2393 0.7020 -0.0622 0.1811  -0.0848 413 HOH A O   
2181 O  O   . HOH F .   ? 0.3993 0.3224 0.2916 0.0414  0.0454  -0.1177 414 HOH A O   
2182 O  O   . HOH F .   ? 0.1763 0.2437 0.1978 -0.0008 -0.0013 -0.0295 415 HOH A O   
2183 O  O   . HOH F .   ? 0.3723 0.3037 0.5656 -0.0596 -0.1059 -0.0869 416 HOH A O   
2184 O  O   . HOH F .   ? 0.3828 0.3749 0.3107 -0.0713 0.1371  -0.1351 417 HOH A O   
2185 O  O   . HOH F .   ? 0.3173 0.3004 0.4444 0.0259  -0.0900 -0.0818 418 HOH A O   
2186 O  O   . HOH F .   ? 0.3407 0.4988 0.3939 -0.0758 0.0972  -0.2187 419 HOH A O   
2187 O  O   . HOH F .   ? 0.4231 0.6297 0.3678 0.1264  0.1364  0.0055  420 HOH A O   
2188 O  O   . HOH F .   ? 0.3561 0.3272 0.2415 0.0650  -0.0109 0.0302  421 HOH A O   
2189 O  O   . HOH F .   ? 0.6197 0.4065 0.3309 0.0392  0.1761  0.0443  422 HOH A O   
2190 O  O   . HOH F .   ? 0.6709 0.3802 0.4488 0.0530  0.0280  -0.1201 423 HOH A O   
2191 O  O   . HOH F .   ? 0.7626 0.2391 0.4243 0.3378  -0.1087 -0.0655 424 HOH A O   
2192 O  O   . HOH F .   ? 0.2260 0.1730 0.2468 0.0063  -0.0310 0.0093  425 HOH A O   
2193 O  O   . HOH F .   ? 0.2621 0.5343 0.5917 -0.0137 0.0731  0.2567  426 HOH A O   
2194 O  O   . HOH F .   ? 0.2063 0.3536 0.4110 -0.0005 0.0538  0.0482  427 HOH A O   
2195 O  O   . HOH F .   ? 0.2473 0.1365 0.3197 -0.0018 -0.0221 0.0037  428 HOH A O   
2196 O  O   . HOH F .   ? 0.2769 0.3375 0.2287 0.0607  0.0467  0.0639  429 HOH A O   
2197 O  O   . HOH F .   ? 0.3488 0.3957 0.4673 0.0868  -0.1544 -0.0608 430 HOH A O   
2198 O  O   . HOH F .   ? 0.3767 0.4144 0.4391 0.0938  0.0989  -0.0256 431 HOH A O   
2199 O  O   . HOH F .   ? 0.5980 0.2038 0.4548 -0.0469 -0.1056 -0.0081 432 HOH A O   
2200 O  O   . HOH F .   ? 0.2793 0.3561 0.2505 -0.0419 0.0216  0.0284  433 HOH A O   
2201 O  O   . HOH F .   ? 0.3309 0.5113 0.2584 0.0217  0.0060  -0.0403 434 HOH A O   
2202 O  O   . HOH F .   ? 0.3815 0.3873 0.3840 -0.0239 -0.1172 0.1556  435 HOH A O   
2203 O  O   . HOH F .   ? 0.3034 0.6194 0.3868 0.0603  0.0277  -0.2293 436 HOH A O   
2204 O  O   . HOH F .   ? 0.3931 0.2517 0.2720 0.0558  -0.0851 -0.0548 437 HOH A O   
2205 O  O   . HOH F .   ? 0.1500 0.1469 0.1553 0.0057  0.0027  -0.0232 438 HOH A O   
2206 O  O   . HOH F .   ? 0.3966 0.6312 0.4100 0.1690  -0.0525 -0.0983 439 HOH A O   
2207 O  O   . HOH F .   ? 0.2929 0.2955 0.4482 0.0127  -0.1629 -0.1145 440 HOH A O   
2208 O  O   . HOH F .   ? 0.3006 0.2910 0.2444 0.0322  -0.0051 -0.0502 441 HOH A O   
2209 O  O   . HOH F .   ? 0.3494 0.2545 0.3662 0.0124  -0.0855 0.0265  442 HOH A O   
2210 O  O   . HOH F .   ? 0.3322 0.2116 0.3058 -0.0489 0.0140  -0.0198 443 HOH A O   
2211 O  O   . HOH F .   ? 0.3291 0.4405 0.3771 -0.0908 0.0053  -0.0369 444 HOH A O   
2212 O  O   . HOH F .   ? 0.3006 0.2197 0.2077 -0.0541 -0.0218 -0.0001 445 HOH A O   
2213 O  O   . HOH F .   ? 0.2167 0.1533 0.1632 -0.0201 0.0097  -0.0241 446 HOH A O   
2214 O  O   . HOH F .   ? 0.5565 0.2584 0.3499 -0.0496 0.0935  -0.0669 447 HOH A O   
2215 O  O   . HOH F .   ? 0.3655 0.4463 0.4039 0.0341  -0.0509 -0.0577 448 HOH A O   
2216 O  O   . HOH F .   ? 0.3544 0.2984 0.2400 0.0081  -0.0701 0.0047  449 HOH A O   
2217 O  O   . HOH F .   ? 0.4558 0.3690 0.2080 -0.0428 0.0288  -0.0255 450 HOH A O   
2218 O  O   . HOH F .   ? 0.4364 0.3592 0.2460 -0.0284 -0.0337 0.0595  451 HOH A O   
2219 O  O   . HOH F .   ? 0.7231 0.5717 0.4078 0.2218  -0.0822 0.0950  452 HOH A O   
2220 O  O   . HOH F .   ? 0.2515 0.3465 0.2271 -0.0717 0.0295  -0.0053 453 HOH A O   
2221 O  O   . HOH F .   ? 0.1612 0.1716 0.1815 0.0128  -0.0148 -0.0491 454 HOH A O   
2222 O  O   . HOH F .   ? 0.1718 0.2157 0.3671 0.0083  0.0000  -0.0140 455 HOH A O   
2223 O  O   . HOH F .   ? 0.4171 0.2536 0.2438 -0.0807 0.0370  -0.0261 456 HOH A O   
2224 O  O   . HOH F .   ? 0.2833 0.5056 0.6461 -0.1058 0.0597  -0.0451 457 HOH A O   
2225 O  O   . HOH F .   ? 0.2756 0.2768 0.2472 -0.0043 -0.0236 0.0239  458 HOH A O   
2226 O  O   . HOH F .   ? 0.5097 0.2358 0.2372 -0.0719 -0.0372 0.0917  459 HOH A O   
2227 O  O   . HOH F .   ? 0.4513 0.2838 0.5000 -0.0351 -0.1803 0.1443  460 HOH A O   
2228 O  O   . HOH F .   ? 0.5370 0.4002 0.4773 -0.2469 0.0133  0.0956  461 HOH A O   
2229 O  O   . HOH F .   ? 0.1594 0.1704 0.1569 0.0006  -0.0192 0.0233  462 HOH A O   
2230 O  O   . HOH F .   ? 0.2767 0.3603 0.1765 -0.0475 -0.0121 0.0111  463 HOH A O   
2231 O  O   . HOH F .   ? 0.3585 0.3049 0.3155 -0.0420 0.0425  -0.1289 464 HOH A O   
2232 O  O   . HOH F .   ? 0.2720 0.2520 0.3352 0.0302  -0.1837 -0.0642 465 HOH A O   
2233 O  O   . HOH F .   ? 0.8027 0.4347 0.6054 0.0076  0.4186  0.1249  466 HOH A O   
2234 O  O   . HOH F .   ? 0.5932 0.3983 0.4455 -0.0174 0.1693  0.0380  467 HOH A O   
2235 O  O   . HOH F .   ? 0.3254 0.5337 0.6814 -0.1022 -0.1910 0.0920  468 HOH A O   
2236 O  O   . HOH F .   ? 0.3474 0.3982 0.3338 0.0159  -0.0294 -0.0779 469 HOH A O   
2237 O  O   . HOH F .   ? 0.4375 0.5500 0.2741 -0.3106 -0.0291 0.0231  470 HOH A O   
2238 O  O   . HOH F .   ? 0.2501 0.2617 0.3687 0.0104  0.0010  -0.0771 471 HOH A O   
2239 O  O   . HOH F .   ? 0.2486 0.3891 0.2628 0.1460  0.0087  0.0365  472 HOH A O   
2240 O  O   . HOH F .   ? 0.1538 0.1580 0.1244 0.0315  -0.0086 -0.0012 473 HOH A O   
2241 O  O   . HOH F .   ? 0.2742 0.3550 0.2254 0.0139  -0.0778 -0.0027 474 HOH A O   
2242 O  O   . HOH F .   ? 0.2224 0.2034 0.2861 -0.0420 -0.0672 0.0011  475 HOH A O   
2243 O  O   . HOH F .   ? 0.3865 0.3709 0.3394 -0.1201 -0.0578 0.1359  476 HOH A O   
2244 O  O   . HOH F .   ? 0.5551 0.4137 1.0413 0.0000  -0.2336 0.1967  477 HOH A O   
2245 O  O   . HOH F .   ? 0.7587 0.5148 0.3866 0.3195  0.0231  0.0272  478 HOH A O   
2246 O  O   . HOH F .   ? 0.6493 0.4716 0.2382 0.2881  -0.0671 -0.0385 479 HOH A O   
2247 O  O   . HOH F .   ? 0.6386 0.3243 0.4108 0.2770  -0.2356 -0.0800 480 HOH A O   
2248 O  O   . HOH F .   ? 0.2667 0.6332 0.4805 -0.0860 0.0651  0.0961  481 HOH A O   
2249 O  O   . HOH F .   ? 0.1469 0.1295 0.1495 0.0111  -0.0145 -0.0032 482 HOH A O   
2250 O  O   . HOH F .   ? 0.4065 0.6202 0.2973 0.2215  0.0351  0.1166  483 HOH A O   
2251 O  O   . HOH F .   ? 0.6317 0.2629 0.8092 -0.0041 -0.1529 -0.0165 484 HOH A O   
2252 O  O   . HOH F .   ? 0.2580 0.3190 0.2211 -0.0044 0.0702  -0.0675 485 HOH A O   
2253 O  O   . HOH F .   ? 0.5113 0.3673 0.2479 -0.0741 0.0199  0.0848  486 HOH A O   
2254 O  O   . HOH F .   ? 0.5332 0.4344 0.2735 0.0510  0.0744  0.0416  487 HOH A O   
2255 O  O   . HOH F .   ? 0.2672 0.1644 0.4096 0.0044  0.0579  -0.0594 488 HOH A O   
2256 O  O   . HOH F .   ? 0.5126 0.3802 0.4837 0.1582  -0.2417 -0.2572 489 HOH A O   
2257 O  O   . HOH F .   ? 0.3705 0.3664 0.2391 0.0306  0.0848  -0.1066 490 HOH A O   
2258 O  O   . HOH F .   ? 0.5281 0.6193 0.2215 -0.1090 -0.0057 0.0939  491 HOH A O   
2259 O  O   . HOH F .   ? 0.3348 0.4407 0.2687 -0.0589 -0.0816 -0.0089 492 HOH A O   
2260 O  O   . HOH F .   ? 0.1438 0.3052 0.2629 -0.0298 -0.0139 -0.0212 493 HOH A O   
2261 O  O   . HOH F .   ? 0.4862 0.4662 0.4187 -0.0430 0.0161  0.2413  494 HOH A O   
2262 O  O   . HOH F .   ? 0.3437 0.4161 0.4027 0.1189  0.0312  -0.0747 495 HOH A O   
2263 O  O   . HOH F .   ? 0.1385 0.1901 0.2272 -0.0084 -0.0010 0.0085  496 HOH A O   
2264 O  O   . HOH F .   ? 0.1270 0.1337 0.1312 -0.0032 0.0097  0.0084  497 HOH A O   
2265 O  O   . HOH F .   ? 0.2238 0.3392 0.2348 -0.0412 -0.0281 0.1204  498 HOH A O   
2266 O  O   . HOH F .   ? 0.7508 0.3610 0.7738 -0.0584 -0.3007 -0.0551 499 HOH A O   
2267 O  O   . HOH F .   ? 0.2215 0.2574 0.1895 -0.0428 -0.0447 -0.0034 500 HOH A O   
2268 O  O   . HOH F .   ? 0.1435 0.1661 0.1723 0.0029  -0.0254 0.0116  501 HOH A O   
2269 O  O   . HOH F .   ? 0.2681 0.3926 0.2490 0.0465  -0.0032 0.0206  502 HOH A O   
2270 O  O   . HOH F .   ? 0.1176 0.1885 0.2038 0.0055  -0.0038 -0.0292 503 HOH A O   
2271 O  O   . HOH F .   ? 0.4335 0.2920 0.3302 -0.0832 0.0886  -0.0945 504 HOH A O   
2272 O  O   . HOH F .   ? 0.4686 0.2535 0.2515 0.0348  0.0740  0.0740  505 HOH A O   
2273 O  O   . HOH F .   ? 0.4010 0.1912 0.3461 0.0930  -0.0775 -0.0113 506 HOH A O   
2274 O  O   . HOH F .   ? 0.2090 0.2332 0.1921 0.0080  -0.0687 0.0215  507 HOH A O   
2275 O  O   . HOH F .   ? 0.2142 0.2362 0.1935 -0.0325 0.0343  -0.0516 508 HOH A O   
2276 O  O   . HOH F .   ? 0.3297 0.3674 0.3917 -0.0230 0.0354  0.0897  509 HOH A O   
2277 O  O   . HOH F .   ? 0.3948 0.5705 0.2763 -0.0514 -0.0723 0.0223  510 HOH A O   
2278 O  O   . HOH F .   ? 0.2120 0.1254 0.2172 -0.0124 -0.0334 0.0136  511 HOH A O   
2279 O  O   . HOH F .   ? 0.1862 0.2481 0.2671 0.0552  0.0458  0.0885  512 HOH A O   
2280 O  O   . HOH F .   ? 0.2208 0.3813 0.2246 0.0223  -0.0019 -0.0719 513 HOH A O   
2281 O  O   . HOH F .   ? 0.4618 0.3480 0.7419 0.0211  0.1030  0.1159  514 HOH A O   
2282 O  O   . HOH F .   ? 0.1988 0.1770 0.2153 0.0304  0.0029  0.0102  515 HOH A O   
2283 O  O   . HOH F .   ? 0.1600 0.1632 0.1791 0.0051  -0.0151 0.0152  516 HOH A O   
2284 O  O   . HOH F .   ? 0.1927 0.2262 0.2380 0.0403  -0.0424 0.0096  517 HOH A O   
2285 O  O   . HOH F .   ? 0.3028 0.2459 0.3867 0.0298  -0.0013 0.0201  518 HOH A O   
2286 O  O   . HOH F .   ? 0.6147 0.5829 0.2762 -0.3666 -0.0670 0.1459  519 HOH A O   
2287 O  O   . HOH F .   ? 0.2814 0.3136 0.2125 -0.0073 0.0065  0.0549  520 HOH A O   
2288 O  O   . HOH F .   ? 0.6067 0.4274 0.2274 -0.0632 -0.1275 -0.0643 521 HOH A O   
2289 O  O   . HOH F .   ? 0.3780 0.3278 0.2547 0.1789  0.1430  0.1340  522 HOH A O   
2290 O  O   . HOH F .   ? 0.2228 0.1855 0.3222 -0.0190 0.0221  -0.0011 523 HOH A O   
2291 O  O   . HOH F .   ? 0.2562 0.4025 0.2454 -0.0751 -0.0392 0.0688  524 HOH A O   
2292 O  O   . HOH F .   ? 0.2039 0.2318 0.1835 0.0291  0.0220  0.0270  525 HOH A O   
2293 O  O   . HOH F .   ? 0.4433 0.3778 0.1648 0.1079  -0.0858 0.0139  526 HOH A O   
2294 O  O   . HOH F .   ? 0.1507 0.1488 0.2005 -0.0184 -0.0100 0.0124  527 HOH A O   
2295 O  O   . HOH F .   ? 0.2800 0.2301 0.3350 0.0368  -0.0065 -0.0337 528 HOH A O   
2296 O  O   . HOH F .   ? 0.2681 0.3782 0.3161 -0.0130 -0.0247 0.0771  529 HOH A O   
2297 O  O   . HOH F .   ? 0.4248 0.2450 0.3012 -0.0092 0.0674  -0.0043 530 HOH A O   
2298 O  O   . HOH F .   ? 0.1190 0.2483 0.1763 0.0287  -0.0065 -0.0215 531 HOH A O   
2299 O  O   . HOH F .   ? 0.1526 0.3715 0.3400 0.0386  -0.0124 0.0736  532 HOH A O   
2300 O  O   . HOH F .   ? 0.4098 0.4326 0.4711 -0.0216 0.0085  0.0099  533 HOH A O   
2301 O  O   . HOH F .   ? 0.2637 0.3341 0.2544 0.1000  0.0071  -0.0497 534 HOH A O   
2302 O  O   . HOH F .   ? 0.2524 0.2470 0.1808 -0.0018 -0.0179 -0.0044 535 HOH A O   
2303 O  O   . HOH F .   ? 0.6836 0.4296 0.4733 -0.0908 -0.3476 0.1058  536 HOH A O   
2304 O  O   . HOH F .   ? 0.2792 0.4958 0.2224 -0.0400 -0.0610 -0.0355 537 HOH A O   
2305 O  O   . HOH F .   ? 0.2870 0.5331 0.4610 -0.0326 -0.0586 -0.0823 538 HOH A O   
2306 O  O   . HOH F .   ? 0.5249 0.3897 0.5597 -0.1838 0.1747  -0.0714 539 HOH A O   
2307 O  O   . HOH F .   ? 0.3233 0.2621 0.5495 -0.0628 0.1561  0.0532  540 HOH A O   
2308 O  O   . HOH F .   ? 0.2645 0.8420 0.3335 -0.0620 0.0736  0.1467  541 HOH A O   
2309 O  O   . HOH F .   ? 0.3066 0.2427 0.2555 0.0042  -0.0712 -0.0741 542 HOH A O   
2310 O  O   . HOH F .   ? 0.3055 0.2459 0.2939 0.1009  -0.1103 -0.0337 543 HOH A O   
2311 O  O   . HOH F .   ? 0.3683 0.4187 0.4485 0.0395  -0.0044 -0.0148 544 HOH A O   
2312 O  O   . HOH F .   ? 0.2536 0.3022 0.4282 0.0103  -0.0665 -0.0176 545 HOH A O   
2313 O  O   . HOH F .   ? 0.1812 0.3037 0.2757 0.0372  0.0379  0.0192  546 HOH A O   
2314 O  O   . HOH F .   ? 0.2713 0.6215 0.2829 -0.0794 -0.0531 0.1493  547 HOH A O   
2315 O  O   . HOH F .   ? 0.7695 0.6262 0.5371 -0.2982 0.3991  -0.1825 548 HOH A O   
2316 O  O   . HOH F .   ? 0.4742 0.5301 0.5680 0.1540  0.1478  -0.1127 549 HOH A O   
2317 O  O   . HOH F .   ? 0.1791 0.4869 0.2658 -0.0325 -0.0087 -0.0740 550 HOH A O   
2318 O  O   . HOH F .   ? 0.4353 0.3258 0.5141 0.0218  0.0398  0.0168  551 HOH A O   
2319 O  O   . HOH F .   ? 0.4430 0.6421 0.1745 0.0776  -0.0068 0.0663  552 HOH A O   
2320 O  O   . HOH F .   ? 0.7495 0.4376 0.5559 0.1227  -0.2049 -0.0485 553 HOH A O   
2321 O  O   . HOH F .   ? 0.2328 0.2536 0.2542 0.0682  0.0036  0.0598  554 HOH A O   
2322 O  O   . HOH F .   ? 0.5486 0.4470 0.3851 -0.0613 0.1562  -0.2031 555 HOH A O   
2323 O  O   . HOH F .   ? 0.2443 0.2171 0.3528 -0.0744 0.0102  0.0502  556 HOH A O   
2324 O  O   . HOH F .   ? 0.3049 0.4521 0.4616 0.0293  0.0066  -0.1421 557 HOH A O   
2325 O  O   . HOH F .   ? 0.3698 0.1981 0.2793 -0.0037 -0.0681 -0.0469 558 HOH A O   
2326 O  O   . HOH F .   ? 0.2280 0.2325 0.2405 0.0234  0.0355  0.0919  559 HOH A O   
2327 O  O   . HOH F .   ? 0.2197 0.5234 0.3076 0.0964  -0.0507 -0.0071 560 HOH A O   
2328 O  O   . HOH F .   ? 0.3404 0.3721 0.4674 0.0871  0.1011  0.0629  561 HOH A O   
2329 O  O   . HOH F .   ? 0.3468 0.2902 0.6803 -0.0615 -0.0171 0.1908  562 HOH A O   
2330 O  O   . HOH F .   ? 0.2301 0.2601 0.3504 -0.1143 0.0585  -0.1306 563 HOH A O   
2331 O  O   . HOH F .   ? 0.2068 0.2749 0.3351 0.0731  -0.0626 -0.1097 564 HOH A O   
2332 O  O   . HOH F .   ? 0.7425 0.2803 0.5906 0.0780  -0.3179 -0.0567 565 HOH A O   
2333 O  O   . HOH F .   ? 0.3949 0.1459 0.5523 0.0125  -0.2240 -0.0021 566 HOH A O   
2334 O  O   . HOH F .   ? 0.2554 0.5187 0.1565 0.1362  -0.0675 -0.0162 567 HOH A O   
2335 O  O   . HOH F .   ? 0.1380 0.2599 0.1648 -0.0065 -0.0240 0.0425  568 HOH A O   
2336 O  O   . HOH F .   ? 0.7978 0.3853 0.4039 0.0110  -0.0055 -0.2118 569 HOH A O   
2337 O  O   . HOH F .   ? 0.2674 0.4346 0.1949 0.0473  -0.0136 -0.1118 570 HOH A O   
2338 O  O   . HOH F .   ? 0.2901 0.3277 0.3188 0.0556  0.0521  0.0006  571 HOH A O   
2339 O  O   . HOH F .   ? 0.4503 0.5069 0.5177 0.1084  0.1056  0.2488  572 HOH A O   
2340 O  O   . HOH F .   ? 0.5030 0.3464 0.4101 0.1011  0.0303  0.0662  573 HOH A O   
2341 O  O   . HOH F .   ? 0.2737 0.2477 0.3925 0.0876  -0.0306 -0.0370 574 HOH A O   
2342 O  O   . HOH F .   ? 0.2208 0.3276 0.2786 -0.0164 0.0302  0.0254  575 HOH A O   
2343 O  O   . HOH F .   ? 0.2860 0.4624 0.5929 0.0589  0.0502  0.0366  576 HOH A O   
2344 O  O   . HOH F .   ? 0.3162 0.2781 0.2989 0.0204  -0.0921 -0.0219 577 HOH A O   
2345 O  O   . HOH F .   ? 0.1607 0.3116 0.2588 0.0166  -0.0192 -0.0495 578 HOH A O   
2346 O  O   . HOH F .   ? 0.3429 0.3298 0.4244 0.0952  0.0596  0.0925  579 HOH A O   
2347 O  O   . HOH F .   ? 0.4364 0.2301 0.3554 0.0842  0.0447  0.0820  580 HOH A O   
2348 O  O   . HOH F .   ? 0.4943 0.4871 0.8144 0.1150  -0.0446 -0.2118 581 HOH A O   
2349 O  O   . HOH F .   ? 0.3190 0.8893 0.5894 -0.0098 0.0122  -0.2861 582 HOH A O   
2350 O  O   . HOH F .   ? 0.5671 0.2213 0.4070 0.1186  -0.1736 -0.0801 583 HOH A O   
2351 O  O   . HOH F .   ? 0.4011 0.4248 0.3318 -0.1261 -0.0190 0.0399  584 HOH A O   
2352 O  O   . HOH F .   ? 0.3050 0.4433 0.1829 -0.0562 0.0526  0.1321  585 HOH A O   
2353 O  O   . HOH F .   ? 0.3916 0.7011 0.4274 -0.1177 -0.0082 -0.0247 586 HOH A O   
2354 O  O   . HOH F .   ? 0.3202 0.2317 0.3021 0.0397  0.0478  0.0269  587 HOH A O   
2355 O  O   . HOH F .   ? 0.5623 0.4431 0.2631 -0.2300 -0.1778 -0.0088 588 HOH A O   
2356 O  O   . HOH F .   ? 0.3358 0.2523 0.6936 -0.0516 0.0190  0.0569  589 HOH A O   
2357 O  O   . HOH F .   ? 0.3230 0.2661 0.8960 -0.0717 0.1972  -0.0316 590 HOH A O   
2358 O  O   . HOH F .   ? 0.2465 0.3063 0.5208 0.0785  -0.1007 -0.0954 591 HOH A O   
2359 O  O   . HOH F .   ? 0.5343 0.5991 0.3203 -0.0119 -0.0350 0.2706  592 HOH A O   
2360 O  O   . HOH F .   ? 0.5610 0.2978 0.2906 0.2116  -0.0709 -0.0261 593 HOH A O   
2361 O  O   . HOH F .   ? 0.1669 0.1368 0.1702 0.0222  -0.0188 0.0064  594 HOH A O   
2362 O  O   . HOH F .   ? 0.2660 0.2215 0.5556 -0.0097 0.0277  -0.0052 595 HOH A O   
2363 O  O   . HOH F .   ? 0.5208 0.6183 0.3691 0.2315  0.0493  0.1634  596 HOH A O   
2364 O  O   . HOH F .   ? 0.3039 0.4546 0.6696 0.0590  0.0172  0.0584  597 HOH A O   
2365 O  O   . HOH F .   ? 0.2604 1.0019 0.4318 0.1392  0.0121  0.1335  598 HOH A O   
2366 O  O   . HOH F .   ? 0.4596 0.2366 0.3007 0.0077  -0.1052 0.0212  599 HOH A O   
2367 O  O   . HOH F .   ? 0.3154 0.1304 0.3251 0.0285  -0.0267 -0.0099 600 HOH A O   
2368 O  O   . HOH F .   ? 0.1428 0.2132 0.2653 -0.0156 0.0120  0.0183  601 HOH A O   
2369 O  O   . HOH F .   ? 0.3810 0.4827 0.2954 -0.1054 0.0469  0.1747  602 HOH A O   
2370 O  O   . HOH F .   ? 0.2226 0.3046 0.5176 0.0054  0.0059  0.0316  603 HOH A O   
2371 O  O   . HOH F .   ? 0.6531 0.4882 0.4586 -0.1100 0.1265  0.1372  604 HOH A O   
2372 O  O   . HOH F .   ? 0.2098 0.3601 0.2831 0.0571  -0.0334 0.0622  605 HOH A O   
2373 O  O   . HOH F .   ? 0.3011 0.2601 0.3280 0.0017  -0.0861 0.0158  606 HOH A O   
2374 O  O   . HOH F .   ? 0.4153 0.4694 0.4600 -0.0275 -0.0545 -0.0465 607 HOH A O   
2375 O  O   . HOH F .   ? 0.4940 0.4151 0.5590 -0.1517 -0.1397 0.0201  608 HOH A O   
2376 O  O   . HOH F .   ? 0.3687 0.3455 0.2617 0.0210  -0.0025 0.0825  609 HOH A O   
2377 O  O   . HOH F .   ? 0.4971 0.2258 0.3033 -0.0127 -0.0396 -0.0098 610 HOH A O   
2378 O  O   . HOH F .   ? 0.4393 0.2926 0.4624 0.0685  0.1351  0.0381  611 HOH A O   
2379 O  O   . HOH F .   ? 0.3915 0.4354 0.4682 0.0261  -0.0627 -0.0279 612 HOH A O   
2380 O  O   . HOH F .   ? 0.3292 0.5290 1.0158 0.0936  0.1728  0.0739  613 HOH A O   
2381 O  O   . HOH F .   ? 0.3550 0.5660 0.7275 0.1118  -0.1179 -0.3193 614 HOH A O   
2382 O  O   . HOH F .   ? 0.2868 0.3563 0.6108 -0.0524 -0.0820 0.0207  615 HOH A O   
2383 O  O   . HOH F .   ? 0.2491 0.6274 0.4014 0.1284  0.0343  0.0592  616 HOH A O   
2384 O  O   . HOH F .   ? 0.2488 0.1931 0.2120 -0.0361 -0.0519 -0.0041 617 HOH A O   
2385 O  O   . HOH F .   ? 0.5807 0.6335 0.6508 -0.1007 -0.1883 -0.1359 618 HOH A O   
2386 O  O   . HOH F .   ? 0.4857 0.3992 0.2504 -0.0824 -0.0542 0.0069  619 HOH A O   
2387 O  O   . HOH F .   ? 0.3790 0.5029 0.3249 0.0319  -0.0597 -0.1344 620 HOH A O   
2388 O  O   . HOH F .   ? 0.3465 0.4593 0.3021 -0.0373 -0.0761 0.0378  621 HOH A O   
2389 O  O   . HOH F .   ? 0.1641 0.1513 0.1587 -0.0130 -0.0450 -0.0053 622 HOH A O   
2390 O  O   . HOH F .   ? 0.3858 0.2980 0.5610 0.0801  0.0483  -0.0721 623 HOH A O   
2391 O  O   . HOH F .   ? 0.2512 0.5713 0.5557 -0.0747 -0.0103 0.2175  624 HOH A O   
2392 O  O   . HOH F .   ? 0.3217 0.8420 0.3720 -0.0155 -0.0357 -0.0160 625 HOH A O   
2393 O  O   . HOH F .   ? 0.3674 0.2300 0.3911 0.0734  -0.1960 -0.0474 626 HOH A O   
2394 O  O   . HOH F .   ? 0.3032 0.4268 0.4692 -0.1032 -0.0139 -0.0229 627 HOH A O   
2395 O  O   . HOH F .   ? 0.3551 0.4183 0.4060 -0.0047 0.0134  0.0254  628 HOH A O   
2396 O  O   . HOH F .   ? 0.9646 0.2394 0.4812 -0.0469 -0.0443 0.0763  629 HOH A O   
2397 O  O   . HOH F .   ? 0.3341 0.5060 0.5292 0.0111  -0.0575 0.0273  630 HOH A O   
2398 O  O   . HOH F .   ? 0.4314 0.2570 0.3743 0.0386  -0.0757 -0.0575 631 HOH A O   
2399 O  O   . HOH F .   ? 0.4113 0.4204 0.3824 0.0621  -0.0328 0.0427  632 HOH A O   
2400 O  O   . HOH F .   ? 0.4688 0.4002 0.3291 -0.0519 -0.0506 0.1223  633 HOH A O   
2401 O  O   . HOH F .   ? 0.3623 0.3015 0.3869 -0.0569 0.0168  0.0333  634 HOH A O   
2402 O  O   . HOH F .   ? 0.2466 0.3565 0.5194 -0.0701 0.0826  -0.1330 635 HOH A O   
2403 O  O   . HOH F .   ? 0.1641 0.5156 0.3931 -0.0778 -0.0881 0.1122  636 HOH A O   
2404 O  O   . HOH F .   ? 0.9224 0.4220 0.2474 -0.0254 -0.1145 -0.0291 637 HOH A O   
2405 O  O   . HOH F .   ? 0.8097 0.2838 0.2627 -0.0513 0.0021  0.0017  638 HOH A O   
2406 O  O   . HOH F .   ? 0.3423 0.3640 0.4654 -0.0315 -0.0780 -0.0730 639 HOH A O   
2407 O  O   . HOH F .   ? 0.4014 0.5365 0.3041 0.0147  -0.0144 0.0640  640 HOH A O   
2408 O  O   . HOH F .   ? 0.3618 0.4046 0.4393 0.1888  -0.0945 0.0239  641 HOH A O   
2409 O  O   . HOH F .   ? 0.3754 0.4516 0.4771 0.0271  0.0236  0.0027  642 HOH A O   
2410 O  O   . HOH F .   ? 0.4858 0.4823 0.4286 0.1794  -0.0306 0.0631  643 HOH A O   
2411 O  O   . HOH F .   ? 0.4624 0.3873 0.5108 0.0017  -0.0135 0.0348  644 HOH A O   
2412 O  O   . HOH F .   ? 0.6466 0.5632 0.8656 0.0134  0.0614  -0.0945 645 HOH A O   
2413 O  O   . HOH F .   ? 0.3964 0.4617 0.4729 0.0004  0.1013  0.0222  646 HOH A O   
2414 O  O   . HOH F .   ? 0.4225 0.2902 0.6579 0.1118  0.1627  0.0732  647 HOH A O   
2415 O  O   . HOH F .   ? 0.3947 0.4318 0.4684 -0.0002 0.0066  0.0454  648 HOH A O   
2416 O  O   . HOH F .   ? 0.3557 0.5686 0.3376 -0.0424 -0.0324 -0.1137 649 HOH A O   
2417 O  O   . HOH F .   ? 0.3601 0.6133 0.5077 0.0500  -0.0475 0.1989  650 HOH A O   
2418 O  O   . HOH F .   ? 0.2832 0.3124 0.3827 0.0094  -0.0004 0.1283  651 HOH A O   
2419 O  O   . HOH F .   ? 0.4613 0.3646 0.6202 -0.0528 -0.2346 0.0970  652 HOH A O   
2420 O  O   . HOH F .   ? 0.4612 0.3878 0.4113 -0.0285 -0.0376 -0.0345 653 HOH A O   
2421 O  O   . HOH F .   ? 0.5337 0.5208 0.2596 -0.1342 0.0854  0.0987  654 HOH A O   
2422 O  O   . HOH F .   ? 0.5780 0.3241 1.0454 0.0771  0.2195  -0.0236 655 HOH A O   
2423 O  O   . HOH F .   ? 0.7347 0.4241 0.5213 0.1192  -0.2216 -0.1468 656 HOH A O   
2424 O  O   . HOH F .   ? 0.4865 0.8612 0.6547 0.0212  0.0234  -0.2141 657 HOH A O   
2425 O  O   . HOH F .   ? 0.6857 0.4989 0.5396 0.1063  -0.1018 0.0780  658 HOH A O   
2426 O  O   . HOH F .   ? 0.4034 0.2807 0.4131 0.0130  -0.0712 0.0635  659 HOH A O   
2427 O  O   . HOH F .   ? 0.3657 0.7137 0.3600 0.0306  -0.0471 -0.2412 660 HOH A O   
2428 O  O   . HOH F .   ? 0.4488 0.5679 0.5563 0.2885  0.0015  0.0439  661 HOH A O   
2429 O  O   . HOH F .   ? 0.6158 0.5044 0.6256 0.1687  -0.1464 -0.0770 662 HOH A O   
2430 O  O   . HOH F .   ? 0.3419 0.7891 0.4907 -0.1199 -0.0376 0.3111  663 HOH A O   
2431 O  O   . HOH F .   ? 0.3276 0.3858 0.7201 -0.0936 0.0008  0.2743  664 HOH A O   
2432 O  O   . HOH F .   ? 0.2536 0.2143 0.2627 0.0450  -0.0576 0.0186  665 HOH A O   
2433 O  O   . HOH F .   ? 0.2654 0.4058 0.4906 -0.0443 -0.0184 0.0970  666 HOH A O   
2434 O  O   . HOH F .   ? 0.8280 0.8201 0.3856 -0.2339 -0.1870 0.5547  667 HOH A O   
2435 O  O   . HOH F .   ? 0.6520 0.2587 0.5065 0.1815  0.0020  -0.0484 668 HOH A O   
2436 O  O   . HOH F .   ? 0.2677 0.4819 0.5107 -0.0600 -0.0563 -0.0373 669 HOH A O   
2437 O  O   . HOH F .   ? 0.5824 0.2978 0.5263 -0.0871 -0.1379 -0.0287 670 HOH A O   
2438 O  O   . HOH F .   ? 0.3391 0.3525 0.5025 0.0314  0.0765  0.0518  671 HOH A O   
2439 O  O   . HOH F .   ? 0.3595 0.8649 0.3654 0.1236  -0.0057 -0.2353 672 HOH A O   
2440 O  O   . HOH F .   ? 0.4592 0.3736 0.4975 0.0122  -0.0238 -0.0124 673 HOH A O   
2441 O  O   . HOH F .   ? 0.5049 0.4096 0.3878 -0.0083 -0.1286 -0.1533 674 HOH A O   
2442 O  O   . HOH F .   ? 0.1967 0.3473 0.2608 0.0174  -0.0412 -0.0307 675 HOH A O   
2443 O  O   . HOH F .   ? 0.3486 0.1860 0.5446 -0.0416 0.0301  -0.0040 676 HOH A O   
2444 O  O   . HOH F .   ? 0.4527 0.4332 0.5951 -0.1630 0.0195  0.1324  677 HOH A O   
2445 O  O   . HOH F .   ? 0.3094 0.3787 0.4746 0.0462  -0.0077 -0.1932 678 HOH A O   
2446 O  O   . HOH F .   ? 0.7855 0.4524 0.7106 -0.1826 0.1632  0.1042  679 HOH A O   
2447 O  O   . HOH F .   ? 0.4722 0.4071 0.4572 -0.0085 0.0512  0.0022  680 HOH A O   
2448 O  O   . HOH F .   ? 0.2770 0.5586 0.3405 -0.0001 0.0456  0.0322  681 HOH A O   
2449 O  O   . HOH F .   ? 0.7232 0.2606 0.2391 -0.0559 -0.0204 -0.0961 682 HOH A O   
2450 O  O   . HOH F .   ? 0.3928 0.8542 0.3729 -0.0579 -0.1140 -0.0245 683 HOH A O   
2451 O  O   . HOH F .   ? 0.5399 0.2246 0.2946 0.0203  -0.1021 0.0005  684 HOH A O   
# 
