data_6QL2
# 
_entry.id   6QL2 
# 
_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   6QL2         pdb_00006ql2 10.2210/pdb6ql2/pdb 
WWPDB D_1292100364 ?            ?                   
# 
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 2019-09-25 
2 'Structure model' 2 0 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' Advisory                 
2 2 'Structure model' 'Atomic model'           
3 2 'Structure model' 'Data collection'        
4 2 'Structure model' 'Database references'    
5 2 'Structure model' 'Refinement description' 
6 2 'Structure model' 'Structure summary'      
# 
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' atom_site                     
2 2 'Structure model' atom_site_anisotrop           
3 2 'Structure model' chem_comp_atom                
4 2 'Structure model' chem_comp_bond                
5 2 'Structure model' database_2                    
6 2 'Structure model' entity                        
7 2 'Structure model' pdbx_distant_solvent_atoms    
8 2 'Structure model' pdbx_initial_refinement_model 
9 2 'Structure model' pdbx_nonpoly_scheme           
# 
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' '_database_2.pdbx_DOI'                
2 2 'Structure model' '_database_2.pdbx_database_accession' 
3 2 'Structure model' '_entity.pdbx_number_of_molecules'    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6QL2 
_pdbx_database_status.recvd_initial_deposition_date   2019-01-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 ? 
'Manakova, E.' 2 ? 
'Grazulis, S.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Rep' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2045-2322 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            9 
_citation.language                  ? 
_citation.page_first                12710 
_citation.page_last                 12710 
_citation.title                     
'Engineered Carbonic Anhydrase VI-Mimic Enzyme Switched the Structure and Affinities of Inhibitors.' 
_citation.year                      2019 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41598-019-49094-0 
_citation.pdbx_database_id_PubMed   31481705 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kazokaite, J.'   1 ?                   
primary 'Kairys, V.'      2 ?                   
primary 'Smirnoviene, J.' 3 ?                   
primary 'Smirnov, A.'     4 ?                   
primary 'Manakova, E.'    5 ?                   
primary 'Tolvanen, M.'    6 ?                   
primary 'Parkkila, S.'    7 ?                   
primary 'Matulis, D.'     8 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'                   29366.055 1   4.2.1.1 'A65T, N67Q, F130Y, V134Q, L203T' 
'human carbonic anhydrase II'             ? 
2 non-polymer syn 'ZINC ION'                               65.409    1   ?       ?                                 
6-Ethoxy-1,3-benzothiazole-2-sulfonamide  ? 
3 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'   195.237   1   ?       ?                                 Zn ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                     78.133    1   ?       ?                                 
'Dimethyl sulfoxide'                      ? 
5 non-polymer syn BICINE                                   163.172   1   ?       ?                                 
'2-(Bis(2-hydroxyethyl)amino)acetic acid' ? 
6 non-polymer syn 1,2-ETHANEDIOL                           62.068    1   ?       ?                                 ethane-1,2-diol 
? 
7 non-polymer syn 6-ethoxy-1,3-benzothiazole-2-sulfonamide 258.317   1   ?       ?                                 
'2-morpholin-4-ylethanesulfonic acid'     ? 
8 water       nat water                                    18.015    225 ?       ?                                 ? ? 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHTFQVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAQQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLTECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHTFQVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAQQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLTECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                               ZN  
3 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'   MES 
4 'DIMETHYL SULFOXIDE'                     DMS 
5 BICINE                                   BCN 
6 1,2-ETHANEDIOL                           EDO 
7 6-ethoxy-1,3-benzothiazole-2-sulfonamide EZL 
8 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  THR n 
1 66  PHE n 
1 67  GLN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 TYR n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 GLN 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 THR n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                  ?                 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                 ?                 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                               ?                 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                          ?                 'C4 H7 N O4'      133.103 
BCN non-polymer         . BICINE                                   ?                 'C6 H13 N O4'     163.172 
CYS 'L-peptide linking' y CYSTEINE                                 ?                 'C3 H7 N O2 S'    121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                     ?                 'C2 H6 O S'       78.133  
EDO non-polymer         . 1,2-ETHANEDIOL                           'ETHYLENE GLYCOL' 'C2 H6 O2'        62.068  
EZL non-polymer         . 6-ethoxy-1,3-benzothiazole-2-sulfonamide Ethoxzolamide     'C9 H10 N2 O3 S2' 258.317 
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 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'   ?                 'C6 H13 N O4 S'   195.237 
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  THR 65  65  65  THR THR A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 TYR 130 131 131 TYR TYR 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 GLN 134 135 135 GLN GLN 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 THR 203 204 204 THR THR 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 MES 1   302 1   MES MES A . 
D 4 DMS 1   303 2   DMS DMS A . 
E 5 BCN 1   304 3   BCN BCN A . 
F 6 EDO 1   305 4   EDO EDO A . 
G 7 EZL 1   306 1   EZL EZA A . 
H 8 HOH 1   401 126 HOH HOH A . 
H 8 HOH 2   402 183 HOH HOH A . 
H 8 HOH 3   403 149 HOH HOH A . 
H 8 HOH 4   404 165 HOH HOH A . 
H 8 HOH 5   405 57  HOH HOH A . 
H 8 HOH 6   406 141 HOH HOH A . 
H 8 HOH 7   407 172 HOH HOH A . 
H 8 HOH 8   408 153 HOH HOH A . 
H 8 HOH 9   409 82  HOH HOH A . 
H 8 HOH 10  410 174 HOH HOH A . 
H 8 HOH 11  411 28  HOH HOH A . 
H 8 HOH 12  412 199 HOH HOH A . 
H 8 HOH 13  413 169 HOH HOH A . 
H 8 HOH 14  414 181 HOH HOH A . 
H 8 HOH 15  415 157 HOH HOH A . 
H 8 HOH 16  416 36  HOH HOH A . 
H 8 HOH 17  417 202 HOH HOH A . 
H 8 HOH 18  418 87  HOH HOH A . 
H 8 HOH 19  419 127 HOH HOH A . 
H 8 HOH 20  420 2   HOH HOH A . 
H 8 HOH 21  421 70  HOH HOH A . 
H 8 HOH 22  422 145 HOH HOH A . 
H 8 HOH 23  423 35  HOH HOH A . 
H 8 HOH 24  424 211 HOH HOH A . 
H 8 HOH 25  425 223 HOH HOH A . 
H 8 HOH 26  426 134 HOH HOH A . 
H 8 HOH 27  427 15  HOH HOH A . 
H 8 HOH 28  428 190 HOH HOH A . 
H 8 HOH 29  429 61  HOH HOH A . 
H 8 HOH 30  430 62  HOH HOH A . 
H 8 HOH 31  431 147 HOH HOH A . 
H 8 HOH 32  432 107 HOH HOH A . 
H 8 HOH 33  433 50  HOH HOH A . 
H 8 HOH 34  434 29  HOH HOH A . 
H 8 HOH 35  435 88  HOH HOH A . 
H 8 HOH 36  436 81  HOH HOH A . 
H 8 HOH 37  437 27  HOH HOH A . 
H 8 HOH 38  438 51  HOH HOH A . 
H 8 HOH 39  439 83  HOH HOH A . 
H 8 HOH 40  440 173 HOH HOH A . 
H 8 HOH 41  441 13  HOH HOH A . 
H 8 HOH 42  442 178 HOH HOH A . 
H 8 HOH 43  443 180 HOH HOH A . 
H 8 HOH 44  444 71  HOH HOH A . 
H 8 HOH 45  445 92  HOH HOH A . 
H 8 HOH 46  446 224 HOH HOH A . 
H 8 HOH 47  447 124 HOH HOH A . 
H 8 HOH 48  448 5   HOH HOH A . 
H 8 HOH 49  449 31  HOH HOH A . 
H 8 HOH 50  450 203 HOH HOH A . 
H 8 HOH 51  451 198 HOH HOH A . 
H 8 HOH 52  452 34  HOH HOH A . 
H 8 HOH 53  453 97  HOH HOH A . 
H 8 HOH 54  454 156 HOH HOH A . 
H 8 HOH 55  455 189 HOH HOH A . 
H 8 HOH 56  456 123 HOH HOH A . 
H 8 HOH 57  457 23  HOH HOH A . 
H 8 HOH 58  458 80  HOH HOH A . 
H 8 HOH 59  459 21  HOH HOH A . 
H 8 HOH 60  460 32  HOH HOH A . 
H 8 HOH 61  461 150 HOH HOH A . 
H 8 HOH 62  462 16  HOH HOH A . 
H 8 HOH 63  463 106 HOH HOH A . 
H 8 HOH 64  464 161 HOH HOH A . 
H 8 HOH 65  465 37  HOH HOH A . 
H 8 HOH 66  466 47  HOH HOH A . 
H 8 HOH 67  467 120 HOH HOH A . 
H 8 HOH 68  468 44  HOH HOH A . 
H 8 HOH 69  469 128 HOH HOH A . 
H 8 HOH 70  470 105 HOH HOH A . 
H 8 HOH 71  471 58  HOH HOH A . 
H 8 HOH 72  472 4   HOH HOH A . 
H 8 HOH 73  473 95  HOH HOH A . 
H 8 HOH 74  474 146 HOH HOH A . 
H 8 HOH 75  475 117 HOH HOH A . 
H 8 HOH 76  476 135 HOH HOH A . 
H 8 HOH 77  477 48  HOH HOH A . 
H 8 HOH 78  478 222 HOH HOH A . 
H 8 HOH 79  479 171 HOH HOH A . 
H 8 HOH 80  480 42  HOH HOH A . 
H 8 HOH 81  481 7   HOH HOH A . 
H 8 HOH 82  482 17  HOH HOH A . 
H 8 HOH 83  483 26  HOH HOH A . 
H 8 HOH 84  484 121 HOH HOH A . 
H 8 HOH 85  485 184 HOH HOH A . 
H 8 HOH 86  486 170 HOH HOH A . 
H 8 HOH 87  487 102 HOH HOH A . 
H 8 HOH 88  488 39  HOH HOH A . 
H 8 HOH 89  489 10  HOH HOH A . 
H 8 HOH 90  490 159 HOH HOH A . 
H 8 HOH 91  491 1   HOH HOH A . 
H 8 HOH 92  492 65  HOH HOH A . 
H 8 HOH 93  493 6   HOH HOH A . 
H 8 HOH 94  494 33  HOH HOH A . 
H 8 HOH 95  495 60  HOH HOH A . 
H 8 HOH 96  496 160 HOH HOH A . 
H 8 HOH 97  497 151 HOH HOH A . 
H 8 HOH 98  498 66  HOH HOH A . 
H 8 HOH 99  499 77  HOH HOH A . 
H 8 HOH 100 500 55  HOH HOH A . 
H 8 HOH 101 501 103 HOH HOH A . 
H 8 HOH 102 502 86  HOH HOH A . 
H 8 HOH 103 503 46  HOH HOH A . 
H 8 HOH 104 504 104 HOH HOH A . 
H 8 HOH 105 505 53  HOH HOH A . 
H 8 HOH 106 506 54  HOH HOH A . 
H 8 HOH 107 507 63  HOH HOH A . 
H 8 HOH 108 508 201 HOH HOH A . 
H 8 HOH 109 509 142 HOH HOH A . 
H 8 HOH 110 510 12  HOH HOH A . 
H 8 HOH 111 511 67  HOH HOH A . 
H 8 HOH 112 512 14  HOH HOH A . 
H 8 HOH 113 513 22  HOH HOH A . 
H 8 HOH 114 514 144 HOH HOH A . 
H 8 HOH 115 515 3   HOH HOH A . 
H 8 HOH 116 516 75  HOH HOH A . 
H 8 HOH 117 517 122 HOH HOH A . 
H 8 HOH 118 518 90  HOH HOH A . 
H 8 HOH 119 519 38  HOH HOH A . 
H 8 HOH 120 520 162 HOH HOH A . 
H 8 HOH 121 521 98  HOH HOH A . 
H 8 HOH 122 522 78  HOH HOH A . 
H 8 HOH 123 523 164 HOH HOH A . 
H 8 HOH 124 524 30  HOH HOH A . 
H 8 HOH 125 525 200 HOH HOH A . 
H 8 HOH 126 526 204 HOH HOH A . 
H 8 HOH 127 527 20  HOH HOH A . 
H 8 HOH 128 528 76  HOH HOH A . 
H 8 HOH 129 529 69  HOH HOH A . 
H 8 HOH 130 530 194 HOH HOH A . 
H 8 HOH 131 531 225 HOH HOH A . 
H 8 HOH 132 532 52  HOH HOH A . 
H 8 HOH 133 533 68  HOH HOH A . 
H 8 HOH 134 534 185 HOH HOH A . 
H 8 HOH 135 535 206 HOH HOH A . 
H 8 HOH 136 536 119 HOH HOH A . 
H 8 HOH 137 537 40  HOH HOH A . 
H 8 HOH 138 538 191 HOH HOH A . 
H 8 HOH 139 539 19  HOH HOH A . 
H 8 HOH 140 540 43  HOH HOH A . 
H 8 HOH 141 541 101 HOH HOH A . 
H 8 HOH 142 542 100 HOH HOH A . 
H 8 HOH 143 543 143 HOH HOH A . 
H 8 HOH 144 544 99  HOH HOH A . 
H 8 HOH 145 545 59  HOH HOH A . 
H 8 HOH 146 546 116 HOH HOH A . 
H 8 HOH 147 547 216 HOH HOH A . 
H 8 HOH 148 548 166 HOH HOH A . 
H 8 HOH 149 549 49  HOH HOH A . 
H 8 HOH 150 550 118 HOH HOH A . 
H 8 HOH 151 551 72  HOH HOH A . 
H 8 HOH 152 552 74  HOH HOH A . 
H 8 HOH 153 553 131 HOH HOH A . 
H 8 HOH 154 554 212 HOH HOH A . 
H 8 HOH 155 555 73  HOH HOH A . 
H 8 HOH 156 556 93  HOH HOH A . 
H 8 HOH 157 557 25  HOH HOH A . 
H 8 HOH 158 558 115 HOH HOH A . 
H 8 HOH 159 559 114 HOH HOH A . 
H 8 HOH 160 560 152 HOH HOH A . 
H 8 HOH 161 561 8   HOH HOH A . 
H 8 HOH 162 562 148 HOH HOH A . 
H 8 HOH 163 563 89  HOH HOH A . 
H 8 HOH 164 564 45  HOH HOH A . 
H 8 HOH 165 565 11  HOH HOH A . 
H 8 HOH 166 566 9   HOH HOH A . 
H 8 HOH 167 567 195 HOH HOH A . 
H 8 HOH 168 568 18  HOH HOH A . 
H 8 HOH 169 569 196 HOH HOH A . 
H 8 HOH 170 570 110 HOH HOH A . 
H 8 HOH 171 571 218 HOH HOH A . 
H 8 HOH 172 572 217 HOH HOH A . 
H 8 HOH 173 573 96  HOH HOH A . 
H 8 HOH 174 574 207 HOH HOH A . 
H 8 HOH 175 575 85  HOH HOH A . 
H 8 HOH 176 576 186 HOH HOH A . 
H 8 HOH 177 577 205 HOH HOH A . 
H 8 HOH 178 578 137 HOH HOH A . 
H 8 HOH 179 579 176 HOH HOH A . 
H 8 HOH 180 580 129 HOH HOH A . 
H 8 HOH 181 581 108 HOH HOH A . 
H 8 HOH 182 582 220 HOH HOH A . 
H 8 HOH 183 583 64  HOH HOH A . 
H 8 HOH 184 584 24  HOH HOH A . 
H 8 HOH 185 585 154 HOH HOH A . 
H 8 HOH 186 586 193 HOH HOH A . 
H 8 HOH 187 587 56  HOH HOH A . 
H 8 HOH 188 588 221 HOH HOH A . 
H 8 HOH 189 589 167 HOH HOH A . 
H 8 HOH 190 590 133 HOH HOH A . 
H 8 HOH 191 591 226 HOH HOH A . 
H 8 HOH 192 592 197 HOH HOH A . 
H 8 HOH 193 593 208 HOH HOH A . 
H 8 HOH 194 594 168 HOH HOH A . 
H 8 HOH 195 595 182 HOH HOH A . 
H 8 HOH 196 596 91  HOH HOH A . 
H 8 HOH 197 597 112 HOH HOH A . 
H 8 HOH 198 598 163 HOH HOH A . 
H 8 HOH 199 599 158 HOH HOH A . 
H 8 HOH 200 600 192 HOH HOH A . 
H 8 HOH 201 601 125 HOH HOH A . 
H 8 HOH 202 602 113 HOH HOH A . 
H 8 HOH 203 603 210 HOH HOH A . 
H 8 HOH 204 604 136 HOH HOH A . 
H 8 HOH 205 605 215 HOH HOH A . 
H 8 HOH 206 606 41  HOH HOH A . 
H 8 HOH 207 607 175 HOH HOH A . 
H 8 HOH 208 608 177 HOH HOH A . 
H 8 HOH 209 609 111 HOH HOH A . 
H 8 HOH 210 610 219 HOH HOH A . 
H 8 HOH 211 611 188 HOH HOH A . 
H 8 HOH 212 612 139 HOH HOH A . 
H 8 HOH 213 613 138 HOH HOH A . 
H 8 HOH 214 614 209 HOH HOH A . 
H 8 HOH 215 615 130 HOH HOH A . 
H 8 HOH 216 616 214 HOH HOH A . 
H 8 HOH 217 617 179 HOH HOH A . 
H 8 HOH 218 618 94  HOH HOH A . 
H 8 HOH 219 619 79  HOH HOH A . 
H 8 HOH 220 620 109 HOH HOH A . 
H 8 HOH 221 621 187 HOH HOH A . 
H 8 HOH 222 622 155 HOH HOH A . 
H 8 HOH 223 623 132 HOH HOH A . 
H 8 HOH 224 624 84  HOH HOH A . 
H 8 HOH 225 625 213 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 N 1 A MES 302 ? C8  ? C MES 1 C8  
2 1 N 1 A MES 302 ? S   ? C MES 1 S   
3 1 N 1 A MES 302 ? O1S ? C MES 1 O1S 
4 1 N 1 A MES 302 ? O2S ? C MES 1 O2S 
5 1 N 1 A MES 302 ? O3S ? C MES 1 O3S 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? .    1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.10 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .    3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .    4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .    5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .    6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.220 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6QL2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.136 
_cell.length_a_esd                 ? 
_cell.length_b                     41.309 
_cell.length_b_esd                 ? 
_cell.length_c                     71.368 
_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                         6QL2 
_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                   6QL2 
_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            2.05 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.01 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer was 0.1M sodium BICINE (pH 9), 0.2M ammonium sulfate and 2M sodium malonate (pH 7)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-21 
_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   0.975522 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.975522 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6QL2 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.300 
_reflns.d_resolution_low                 40.845 
_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                       56403 
_reflns.number_obs                       56403 
_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             96.400 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.900 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.067 
_reflns.pdbx_netI_over_av_sigmaI         4.251 
_reflns.pdbx_netI_over_sigmaI            13.100 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.079 
_reflns.pdbx_Rpim_I_all                  0.030 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         389087 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.300 1.370  ? 2.0  ? ? ? ? ? 94.500 ? ? ? ? 0.334 ? ? ? ? ? ? ? ? 6.900 0.334 ? ? ? 0.389 0.145 ? 1  1 ? ? 
1.370 1.450  ? 2.9  ? ? ? ? ? 94.900 ? ? ? ? 0.231 ? ? ? ? ? ? ? ? 6.900 0.231 ? ? ? 0.272 0.102 ? 2  1 ? ? 
1.450 1.550  ? 4.5  ? ? ? ? ? 95.600 ? ? ? ? 0.150 ? ? ? ? ? ? ? ? 6.900 0.150 ? ? ? 0.180 0.068 ? 3  1 ? ? 
1.550 1.680  ? 6.5  ? ? ? ? ? 95.800 ? ? ? ? 0.105 ? ? ? ? ? ? ? ? 6.700 0.105 ? ? ? 0.130 0.050 ? 4  1 ? ? 
1.680 1.840  ? 8.1  ? ? ? ? ? 96.800 ? ? ? ? 0.082 ? ? ? ? ? ? ? ? 7.000 0.082 ? ? ? 0.101 0.038 ? 5  1 ? ? 
1.840 2.060  ? 9.0  ? ? ? ? ? 97.800 ? ? ? ? 0.071 ? ? ? ? ? ? ? ? 7.000 0.071 ? ? ? 0.087 0.032 ? 6  1 ? ? 
2.060 2.370  ? 10.0 ? ? ? ? ? 98.300 ? ? ? ? 0.065 ? ? ? ? ? ? ? ? 7.000 0.065 ? ? ? 0.078 0.029 ? 7  1 ? ? 
2.370 2.910  ? 10.3 ? ? ? ? ? 98.300 ? ? ? ? 0.062 ? ? ? ? ? ? ? ? 6.900 0.062 ? ? ? 0.073 0.027 ? 8  1 ? ? 
2.910 4.110  ? 10.1 ? ? ? ? ? 98.800 ? ? ? ? 0.058 ? ? ? ? ? ? ? ? 6.800 0.058 ? ? ? 0.067 0.025 ? 9  1 ? ? 
4.110 40.845 ? 8.4  ? ? ? ? ? 97.400 ? ? ? ? 0.059 ? ? ? ? ? ? ? ? 6.600 0.059 ? ? ? 0.068 0.026 ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            0.1200 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            0.1300 
_refine.aniso_B[2][2]                            -0.3500 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.1400 
_refine.B_iso_max                                109.310 
_refine.B_iso_mean                               20.4793 
_refine.B_iso_min                                5.470 
_refine.correlation_coeff_Fo_to_Fc               0.9810 
_refine.correlation_coeff_Fo_to_Fc_free          0.9740 
_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                                 6QL2 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.3000 
_refine.ls_d_res_low                             39.7000 
_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                     56387 
_refine.ls_number_reflns_R_free                  5693 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.9800 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1227 
_refine.ls_R_factor_R_free                       0.1573 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1189 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4HT0 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0460 
_refine.pdbx_overall_ESU_R_Free                  0.0470 
_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             0.0463 
_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                         LAST 
_refine_hist.pdbx_number_atoms_protein        2054 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.number_atoms_solvent             226 
_refine_hist.number_atoms_total               2323 
_refine_hist.d_res_high                       1.3000 
_refine_hist.d_res_low                        39.7000 
# 
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' ? 0.013  0.012  2221 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.991  1.657  3026 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.638  5.000  269  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 35.440 23.578 109  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.387 15.000 367  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 23.838 15.000 8    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.128  0.200  269  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  1725 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 2.164  1.593  1061 ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.539  2.405  1335 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 5.117  2.038  1160 ? r_scbond_it            ? ? 
'X-RAY DIFFRACTION' ? 6.206  3.000  2221 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 29.850 5.000  138  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 16.480 5.000  2242 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.3000 
_refine_ls_shell.d_res_low                        1.3340 
_refine_ls_shell.number_reflns_all                4059 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             414 
_refine_ls_shell.number_reflns_R_work             3645 
_refine_ls_shell.percent_reflns_obs               94.0500 
_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                  0.1850 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1300 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     6QL2 
_struct.title                        'Crystal structure of chimeric carbonic anhydrase VI with ethoxzolamide.' 
_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        6QL2 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 8 ? 
# 
_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              6QL2 
_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 6QL2 THR A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6QL2 GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6QL2 TYR A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 3 
1 6QL2 GLN A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 4 
1 6QL2 THR A 203 ? UNP P00918 LEU 203 'engineered mutation' 204 5 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1050  ? 
1 MORE         3     ? 
1 'SSA (A^2)'  11560 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? GLN A 134 ? ASP A 130 GLN 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 ? ? ? ? ? ? ? 2.008 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
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 G EZL . N1 ? ? A ZN  301 A EZL 306 1_555 ? ? ? ? ? ? ? 1.927 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 104.8 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 112.1 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.6  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  ? G EZL .   ? A EZL 306 ? 1_555 112.1 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  ? G EZL .   ? A EZL 306 ? 1_555 111.7 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  ? G EZL .   ? A EZL 306 ? 1_555 116.2 ? 
# 
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 2.07  
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 10.61 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
AA2 7 8  O ILE A 91  ? O ILE A 91  N PHE A 70  ? N PHE A 70  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N 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 MES 302 ? 4  'binding site for residue MES A 302' 
AC3 Software A DMS 303 ? 4  'binding site for residue DMS A 303' 
AC4 Software A BCN 304 ? 8  'binding site for residue BCN A 304' 
AC5 Software A EDO 305 ? 8  'binding site for residue EDO A 305' 
AC6 Software A EZL 306 ? 12 'binding site for residue EZL A 306' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  EZL G .   ? EZL A 306 . ? 1_555 ? 
5  AC2 4  LEU A 163 ? LEU A 164 . ? 1_555 ? 
6  AC2 4  ASP A 164 ? ASP A 165 . ? 1_555 ? 
7  AC2 4  LYS A 224 ? LYS A 225 . ? 1_555 ? 
8  AC2 4  LYS A 227 ? LYS A 228 . ? 1_555 ? 
9  AC3 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
10 AC3 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
11 AC3 4  HOH H .   ? HOH A 404 . ? 1_555 ? 
12 AC3 4  HOH H .   ? HOH A 534 . ? 1_555 ? 
13 AC4 8  ASP A 72  ? ASP A 72  . ? 1_555 ? 
14 AC4 8  ASP A 101 ? ASP A 101 . ? 1_565 ? 
15 AC4 8  ASP A 129 ? ASP A 130 . ? 1_555 ? 
16 AC4 8  TYR A 130 ? TYR A 131 . ? 1_555 ? 
17 AC4 8  GLY A 131 ? GLY A 132 . ? 1_555 ? 
18 AC4 8  HOH H .   ? HOH A 465 . ? 1_555 ? 
19 AC4 8  HOH H .   ? HOH A 573 . ? 1_555 ? 
20 AC4 8  HOH H .   ? HOH A 586 . ? 1_555 ? 
21 AC5 8  ASN A 62  ? ASN A 62  . ? 1_555 ? 
22 AC5 8  THR A 65  ? THR A 65  . ? 1_555 ? 
23 AC5 8  GLN A 67  ? GLN A 67  . ? 1_555 ? 
24 AC5 8  GLN A 92  ? GLN A 92  . ? 1_555 ? 
25 AC5 8  HIS A 94  ? HIS A 94  . ? 1_555 ? 
26 AC5 8  THR A 199 ? THR A 200 . ? 1_555 ? 
27 AC5 8  EZL G .   ? EZL A 306 . ? 1_555 ? 
28 AC5 8  HOH H .   ? HOH A 401 . ? 1_555 ? 
29 AC6 12 HIS A 94  ? HIS A 94  . ? 1_555 ? 
30 AC6 12 HIS A 96  ? HIS A 96  . ? 1_555 ? 
31 AC6 12 HIS A 119 ? HIS A 119 . ? 1_555 ? 
32 AC6 12 TYR A 130 ? TYR A 131 . ? 1_555 ? 
33 AC6 12 GLN A 134 ? GLN A 135 . ? 1_555 ? 
34 AC6 12 LEU A 197 ? LEU A 198 . ? 1_555 ? 
35 AC6 12 THR A 198 ? THR A 199 . ? 1_555 ? 
36 AC6 12 THR A 199 ? THR A 200 . ? 1_555 ? 
37 AC6 12 PRO A 200 ? PRO A 201 . ? 1_555 ? 
38 AC6 12 TRP A 208 ? TRP A 209 . ? 1_555 ? 
39 AC6 12 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
40 AC6 12 EDO F .   ? EDO A 305 . ? 1_555 ? 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              89 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              89 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              89 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                87.18 
_pdbx_validate_rmsd_angle.angle_target_value         111.80 
_pdbx_validate_rmsd_angle.angle_deviation            -24.62 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? B -140.95 59.75   
2 1 LYS A 76  ? ? -106.33 -91.60  
3 1 LYS A 111 ? ? 74.89   -3.84   
4 1 PHE A 176 ? ? -154.68 71.78   
5 1 ASN A 244 ? ? -93.66  49.45   
6 1 LYS A 252 ? ? 63.35   -135.21 
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
EDO C1   C  N N 122 
EDO O1   O  N N 123 
EDO C2   C  N N 124 
EDO O2   O  N N 125 
EDO H11  H  N N 126 
EDO H12  H  N N 127 
EDO HO1  H  N N 128 
EDO H21  H  N N 129 
EDO H22  H  N N 130 
EDO HO2  H  N N 131 
EZL N1   N  N N 132 
EZL C2   C  Y N 133 
EZL C3   C  Y N 134 
EZL C4   C  Y N 135 
EZL C5   C  Y N 136 
EZL C8   C  N N 137 
EZL O1   O  N N 138 
EZL O2   O  N N 139 
EZL S1   S  N N 140 
EZL C1   C  Y N 141 
EZL N2   N  Y N 142 
EZL S2   S  Y N 143 
EZL C6   C  Y N 144 
EZL C7   C  Y N 145 
EZL O3   O  N N 146 
EZL C9   C  N N 147 
EZL HN1  H  N N 148 
EZL HN1A H  N N 149 
EZL H4   H  N N 150 
EZL H8   H  N N 151 
EZL H8A  H  N N 152 
EZL H6   H  N N 153 
EZL H7   H  N N 154 
EZL H9   H  N N 155 
EZL H9A  H  N N 156 
EZL H9B  H  N N 157 
GLN N    N  N N 158 
GLN CA   C  N S 159 
GLN C    C  N N 160 
GLN O    O  N N 161 
GLN CB   C  N N 162 
GLN CG   C  N N 163 
GLN CD   C  N N 164 
GLN OE1  O  N N 165 
GLN NE2  N  N N 166 
GLN OXT  O  N N 167 
GLN H    H  N N 168 
GLN H2   H  N N 169 
GLN HA   H  N N 170 
GLN HB2  H  N N 171 
GLN HB3  H  N N 172 
GLN HG2  H  N N 173 
GLN HG3  H  N N 174 
GLN HE21 H  N N 175 
GLN HE22 H  N N 176 
GLN HXT  H  N N 177 
GLU N    N  N N 178 
GLU CA   C  N S 179 
GLU C    C  N N 180 
GLU O    O  N N 181 
GLU CB   C  N N 182 
GLU CG   C  N N 183 
GLU CD   C  N N 184 
GLU OE1  O  N N 185 
GLU OE2  O  N N 186 
GLU OXT  O  N N 187 
GLU H    H  N N 188 
GLU H2   H  N N 189 
GLU HA   H  N N 190 
GLU HB2  H  N N 191 
GLU HB3  H  N N 192 
GLU HG2  H  N N 193 
GLU HG3  H  N N 194 
GLU HE2  H  N N 195 
GLU HXT  H  N N 196 
GLY N    N  N N 197 
GLY CA   C  N N 198 
GLY C    C  N N 199 
GLY O    O  N N 200 
GLY OXT  O  N N 201 
GLY H    H  N N 202 
GLY H2   H  N N 203 
GLY HA2  H  N N 204 
GLY HA3  H  N N 205 
GLY HXT  H  N N 206 
HIS N    N  N N 207 
HIS CA   C  N S 208 
HIS C    C  N N 209 
HIS O    O  N N 210 
HIS CB   C  N N 211 
HIS CG   C  Y N 212 
HIS ND1  N  Y N 213 
HIS CD2  C  Y N 214 
HIS CE1  C  Y N 215 
HIS NE2  N  Y N 216 
HIS OXT  O  N N 217 
HIS H    H  N N 218 
HIS H2   H  N N 219 
HIS HA   H  N N 220 
HIS HB2  H  N N 221 
HIS HB3  H  N N 222 
HIS HD1  H  N N 223 
HIS HD2  H  N N 224 
HIS HE1  H  N N 225 
HIS HE2  H  N N 226 
HIS HXT  H  N N 227 
HOH O    O  N N 228 
HOH H1   H  N N 229 
HOH H2   H  N N 230 
ILE N    N  N N 231 
ILE CA   C  N S 232 
ILE C    C  N N 233 
ILE O    O  N N 234 
ILE CB   C  N S 235 
ILE CG1  C  N N 236 
ILE CG2  C  N N 237 
ILE CD1  C  N N 238 
ILE OXT  O  N N 239 
ILE H    H  N N 240 
ILE H2   H  N N 241 
ILE HA   H  N N 242 
ILE HB   H  N N 243 
ILE HG12 H  N N 244 
ILE HG13 H  N N 245 
ILE HG21 H  N N 246 
ILE HG22 H  N N 247 
ILE HG23 H  N N 248 
ILE HD11 H  N N 249 
ILE HD12 H  N N 250 
ILE HD13 H  N N 251 
ILE HXT  H  N N 252 
LEU N    N  N N 253 
LEU CA   C  N S 254 
LEU C    C  N N 255 
LEU O    O  N N 256 
LEU CB   C  N N 257 
LEU CG   C  N N 258 
LEU CD1  C  N N 259 
LEU CD2  C  N N 260 
LEU OXT  O  N N 261 
LEU H    H  N N 262 
LEU H2   H  N N 263 
LEU HA   H  N N 264 
LEU HB2  H  N N 265 
LEU HB3  H  N N 266 
LEU HG   H  N N 267 
LEU HD11 H  N N 268 
LEU HD12 H  N N 269 
LEU HD13 H  N N 270 
LEU HD21 H  N N 271 
LEU HD22 H  N N 272 
LEU HD23 H  N N 273 
LEU HXT  H  N N 274 
LYS N    N  N N 275 
LYS CA   C  N S 276 
LYS C    C  N N 277 
LYS O    O  N N 278 
LYS CB   C  N N 279 
LYS CG   C  N N 280 
LYS CD   C  N N 281 
LYS CE   C  N N 282 
LYS NZ   N  N N 283 
LYS OXT  O  N N 284 
LYS H    H  N N 285 
LYS H2   H  N N 286 
LYS HA   H  N N 287 
LYS HB2  H  N N 288 
LYS HB3  H  N N 289 
LYS HG2  H  N N 290 
LYS HG3  H  N N 291 
LYS HD2  H  N N 292 
LYS HD3  H  N N 293 
LYS HE2  H  N N 294 
LYS HE3  H  N N 295 
LYS HZ1  H  N N 296 
LYS HZ2  H  N N 297 
LYS HZ3  H  N N 298 
LYS HXT  H  N N 299 
MES O1   O  N N 300 
MES C2   C  N N 301 
MES C3   C  N N 302 
MES N4   N  N N 303 
MES C5   C  N N 304 
MES C6   C  N N 305 
MES C7   C  N N 306 
MES C8   C  N N 307 
MES S    S  N N 308 
MES O1S  O  N N 309 
MES O2S  O  N N 310 
MES O3S  O  N N 311 
MES H21  H  N N 312 
MES H22  H  N N 313 
MES H31  H  N N 314 
MES H32  H  N N 315 
MES HN4  H  N N 316 
MES H51  H  N N 317 
MES H52  H  N N 318 
MES H61  H  N N 319 
MES H62  H  N N 320 
MES H71  H  N N 321 
MES H72  H  N N 322 
MES H81  H  N N 323 
MES H82  H  N N 324 
MET N    N  N N 325 
MET CA   C  N S 326 
MET C    C  N N 327 
MET O    O  N N 328 
MET CB   C  N N 329 
MET CG   C  N N 330 
MET SD   S  N N 331 
MET CE   C  N N 332 
MET OXT  O  N N 333 
MET H    H  N N 334 
MET H2   H  N N 335 
MET HA   H  N N 336 
MET HB2  H  N N 337 
MET HB3  H  N N 338 
MET HG2  H  N N 339 
MET HG3  H  N N 340 
MET HE1  H  N N 341 
MET HE2  H  N N 342 
MET HE3  H  N N 343 
MET HXT  H  N N 344 
PHE N    N  N N 345 
PHE CA   C  N S 346 
PHE C    C  N N 347 
PHE O    O  N N 348 
PHE CB   C  N N 349 
PHE CG   C  Y N 350 
PHE CD1  C  Y N 351 
PHE CD2  C  Y N 352 
PHE CE1  C  Y N 353 
PHE CE2  C  Y N 354 
PHE CZ   C  Y N 355 
PHE OXT  O  N N 356 
PHE H    H  N N 357 
PHE H2   H  N N 358 
PHE HA   H  N N 359 
PHE HB2  H  N N 360 
PHE HB3  H  N N 361 
PHE HD1  H  N N 362 
PHE HD2  H  N N 363 
PHE HE1  H  N N 364 
PHE HE2  H  N N 365 
PHE HZ   H  N N 366 
PHE HXT  H  N N 367 
PRO N    N  N N 368 
PRO CA   C  N S 369 
PRO C    C  N N 370 
PRO O    O  N N 371 
PRO CB   C  N N 372 
PRO CG   C  N N 373 
PRO CD   C  N N 374 
PRO OXT  O  N N 375 
PRO H    H  N N 376 
PRO HA   H  N N 377 
PRO HB2  H  N N 378 
PRO HB3  H  N N 379 
PRO HG2  H  N N 380 
PRO HG3  H  N N 381 
PRO HD2  H  N N 382 
PRO HD3  H  N N 383 
PRO HXT  H  N N 384 
SER N    N  N N 385 
SER CA   C  N S 386 
SER C    C  N N 387 
SER O    O  N N 388 
SER CB   C  N N 389 
SER OG   O  N N 390 
SER OXT  O  N N 391 
SER H    H  N N 392 
SER H2   H  N N 393 
SER HA   H  N N 394 
SER HB2  H  N N 395 
SER HB3  H  N N 396 
SER HG   H  N N 397 
SER HXT  H  N N 398 
THR N    N  N N 399 
THR CA   C  N S 400 
THR C    C  N N 401 
THR O    O  N N 402 
THR CB   C  N R 403 
THR OG1  O  N N 404 
THR CG2  C  N N 405 
THR OXT  O  N N 406 
THR H    H  N N 407 
THR H2   H  N N 408 
THR HA   H  N N 409 
THR HB   H  N N 410 
THR HG1  H  N N 411 
THR HG21 H  N N 412 
THR HG22 H  N N 413 
THR HG23 H  N N 414 
THR HXT  H  N N 415 
TRP N    N  N N 416 
TRP CA   C  N S 417 
TRP C    C  N N 418 
TRP O    O  N N 419 
TRP CB   C  N N 420 
TRP CG   C  Y N 421 
TRP CD1  C  Y N 422 
TRP CD2  C  Y N 423 
TRP NE1  N  Y N 424 
TRP CE2  C  Y N 425 
TRP CE3  C  Y N 426 
TRP CZ2  C  Y N 427 
TRP CZ3  C  Y N 428 
TRP CH2  C  Y N 429 
TRP OXT  O  N N 430 
TRP H    H  N N 431 
TRP H2   H  N N 432 
TRP HA   H  N N 433 
TRP HB2  H  N N 434 
TRP HB3  H  N N 435 
TRP HD1  H  N N 436 
TRP HE1  H  N N 437 
TRP HE3  H  N N 438 
TRP HZ2  H  N N 439 
TRP HZ3  H  N N 440 
TRP HH2  H  N N 441 
TRP HXT  H  N N 442 
TYR N    N  N N 443 
TYR CA   C  N S 444 
TYR C    C  N N 445 
TYR O    O  N N 446 
TYR CB   C  N N 447 
TYR CG   C  Y N 448 
TYR CD1  C  Y N 449 
TYR CD2  C  Y N 450 
TYR CE1  C  Y N 451 
TYR CE2  C  Y N 452 
TYR CZ   C  Y N 453 
TYR OH   O  N N 454 
TYR OXT  O  N N 455 
TYR H    H  N N 456 
TYR H2   H  N N 457 
TYR HA   H  N N 458 
TYR HB2  H  N N 459 
TYR HB3  H  N N 460 
TYR HD1  H  N N 461 
TYR HD2  H  N N 462 
TYR HE1  H  N N 463 
TYR HE2  H  N N 464 
TYR HH   H  N N 465 
TYR HXT  H  N N 466 
VAL N    N  N N 467 
VAL CA   C  N S 468 
VAL C    C  N N 469 
VAL O    O  N N 470 
VAL CB   C  N N 471 
VAL CG1  C  N N 472 
VAL CG2  C  N N 473 
VAL OXT  O  N N 474 
VAL H    H  N N 475 
VAL H2   H  N N 476 
VAL HA   H  N N 477 
VAL HB   H  N N 478 
VAL HG11 H  N N 479 
VAL HG12 H  N N 480 
VAL HG13 H  N N 481 
VAL HG21 H  N N 482 
VAL HG22 H  N N 483 
VAL HG23 H  N N 484 
VAL HXT  H  N N 485 
ZN  ZN   ZN N N 486 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
EDO C1  O1   sing N N 115 
EDO C1  C2   sing N N 116 
EDO C1  H11  sing N N 117 
EDO C1  H12  sing N N 118 
EDO O1  HO1  sing N N 119 
EDO C2  O2   sing N N 120 
EDO C2  H21  sing N N 121 
EDO C2  H22  sing N N 122 
EDO O2  HO2  sing N N 123 
EZL N1  S1   sing N N 124 
EZL C2  C3   doub Y N 125 
EZL C2  N2   sing Y N 126 
EZL C2  C7   sing Y N 127 
EZL C3  C4   sing Y N 128 
EZL C3  S2   sing Y N 129 
EZL C4  C5   doub Y N 130 
EZL C5  C6   sing Y N 131 
EZL C5  O3   sing N N 132 
EZL C8  O3   sing N N 133 
EZL C8  C9   sing N N 134 
EZL O1  S1   doub N N 135 
EZL O2  S1   doub N N 136 
EZL S1  C1   sing N N 137 
EZL C1  N2   doub Y N 138 
EZL C1  S2   sing Y N 139 
EZL C6  C7   doub Y N 140 
EZL N1  HN1  sing N N 141 
EZL N1  HN1A sing N N 142 
EZL C4  H4   sing N N 143 
EZL C8  H8   sing N N 144 
EZL C8  H8A  sing N N 145 
EZL C6  H6   sing N N 146 
EZL C7  H7   sing N N 147 
EZL C9  H9   sing N N 148 
EZL C9  H9A  sing N N 149 
EZL C9  H9B  sing N N 150 
GLN N   CA   sing N N 151 
GLN N   H    sing N N 152 
GLN N   H2   sing N N 153 
GLN CA  C    sing N N 154 
GLN CA  CB   sing N N 155 
GLN CA  HA   sing N N 156 
GLN C   O    doub N N 157 
GLN C   OXT  sing N N 158 
GLN CB  CG   sing N N 159 
GLN CB  HB2  sing N N 160 
GLN CB  HB3  sing N N 161 
GLN CG  CD   sing N N 162 
GLN CG  HG2  sing N N 163 
GLN CG  HG3  sing N N 164 
GLN CD  OE1  doub N N 165 
GLN CD  NE2  sing N N 166 
GLN NE2 HE21 sing N N 167 
GLN NE2 HE22 sing N N 168 
GLN OXT HXT  sing N N 169 
GLU N   CA   sing N N 170 
GLU N   H    sing N N 171 
GLU N   H2   sing N N 172 
GLU CA  C    sing N N 173 
GLU CA  CB   sing N N 174 
GLU CA  HA   sing N N 175 
GLU C   O    doub N N 176 
GLU C   OXT  sing N N 177 
GLU CB  CG   sing N N 178 
GLU CB  HB2  sing N N 179 
GLU CB  HB3  sing N N 180 
GLU CG  CD   sing N N 181 
GLU CG  HG2  sing N N 182 
GLU CG  HG3  sing N N 183 
GLU CD  OE1  doub N N 184 
GLU CD  OE2  sing N N 185 
GLU OE2 HE2  sing N N 186 
GLU OXT HXT  sing N N 187 
GLY N   CA   sing N N 188 
GLY N   H    sing N N 189 
GLY N   H2   sing N N 190 
GLY CA  C    sing N N 191 
GLY CA  HA2  sing N N 192 
GLY CA  HA3  sing N N 193 
GLY C   O    doub N N 194 
GLY C   OXT  sing N N 195 
GLY OXT HXT  sing N N 196 
HIS N   CA   sing N N 197 
HIS N   H    sing N N 198 
HIS N   H2   sing N N 199 
HIS CA  C    sing N N 200 
HIS CA  CB   sing N N 201 
HIS CA  HA   sing N N 202 
HIS C   O    doub N N 203 
HIS C   OXT  sing N N 204 
HIS CB  CG   sing N N 205 
HIS CB  HB2  sing N N 206 
HIS CB  HB3  sing N N 207 
HIS CG  ND1  sing Y N 208 
HIS CG  CD2  doub Y N 209 
HIS ND1 CE1  doub Y N 210 
HIS ND1 HD1  sing N N 211 
HIS CD2 NE2  sing Y N 212 
HIS CD2 HD2  sing N N 213 
HIS CE1 NE2  sing Y N 214 
HIS CE1 HE1  sing N N 215 
HIS NE2 HE2  sing N N 216 
HIS OXT HXT  sing N N 217 
HOH O   H1   sing N N 218 
HOH O   H2   sing N N 219 
ILE N   CA   sing N N 220 
ILE N   H    sing N N 221 
ILE N   H2   sing N N 222 
ILE CA  C    sing N N 223 
ILE CA  CB   sing N N 224 
ILE CA  HA   sing N N 225 
ILE C   O    doub N N 226 
ILE C   OXT  sing N N 227 
ILE CB  CG1  sing N N 228 
ILE CB  CG2  sing N N 229 
ILE CB  HB   sing N N 230 
ILE CG1 CD1  sing N N 231 
ILE CG1 HG12 sing N N 232 
ILE CG1 HG13 sing N N 233 
ILE CG2 HG21 sing N N 234 
ILE CG2 HG22 sing N N 235 
ILE CG2 HG23 sing N N 236 
ILE CD1 HD11 sing N N 237 
ILE CD1 HD12 sing N N 238 
ILE CD1 HD13 sing N N 239 
ILE OXT HXT  sing N N 240 
LEU N   CA   sing N N 241 
LEU N   H    sing N N 242 
LEU N   H2   sing N N 243 
LEU CA  C    sing N N 244 
LEU CA  CB   sing N N 245 
LEU CA  HA   sing N N 246 
LEU C   O    doub N N 247 
LEU C   OXT  sing N N 248 
LEU CB  CG   sing N N 249 
LEU CB  HB2  sing N N 250 
LEU CB  HB3  sing N N 251 
LEU CG  CD1  sing N N 252 
LEU CG  CD2  sing N N 253 
LEU CG  HG   sing N N 254 
LEU CD1 HD11 sing N N 255 
LEU CD1 HD12 sing N N 256 
LEU CD1 HD13 sing N N 257 
LEU CD2 HD21 sing N N 258 
LEU CD2 HD22 sing N N 259 
LEU CD2 HD23 sing N N 260 
LEU OXT HXT  sing N N 261 
LYS N   CA   sing N N 262 
LYS N   H    sing N N 263 
LYS N   H2   sing N N 264 
LYS CA  C    sing N N 265 
LYS CA  CB   sing N N 266 
LYS CA  HA   sing N N 267 
LYS C   O    doub N N 268 
LYS C   OXT  sing N N 269 
LYS CB  CG   sing N N 270 
LYS CB  HB2  sing N N 271 
LYS CB  HB3  sing N N 272 
LYS CG  CD   sing N N 273 
LYS CG  HG2  sing N N 274 
LYS CG  HG3  sing N N 275 
LYS CD  CE   sing N N 276 
LYS CD  HD2  sing N N 277 
LYS CD  HD3  sing N N 278 
LYS CE  NZ   sing N N 279 
LYS CE  HE2  sing N N 280 
LYS CE  HE3  sing N N 281 
LYS NZ  HZ1  sing N N 282 
LYS NZ  HZ2  sing N N 283 
LYS NZ  HZ3  sing N N 284 
LYS OXT HXT  sing N N 285 
MES O1  C2   sing N N 286 
MES O1  C6   sing N N 287 
MES C2  C3   sing N N 288 
MES C2  H21  sing N N 289 
MES C2  H22  sing N N 290 
MES C3  N4   sing N N 291 
MES C3  H31  sing N N 292 
MES C3  H32  sing N N 293 
MES N4  C5   sing N N 294 
MES N4  C7   sing N N 295 
MES N4  HN4  sing N N 296 
MES C5  C6   sing N N 297 
MES C5  H51  sing N N 298 
MES C5  H52  sing N N 299 
MES C6  H61  sing N N 300 
MES C6  H62  sing N N 301 
MES C7  C8   sing N N 302 
MES C7  H71  sing N N 303 
MES C7  H72  sing N N 304 
MES C8  S    sing N N 305 
MES C8  H81  sing N N 306 
MES C8  H82  sing N N 307 
MES S   O1S  doub N N 308 
MES S   O2S  doub N N 309 
MES S   O3S  sing N N 310 
MET N   CA   sing N N 311 
MET N   H    sing N N 312 
MET N   H2   sing N N 313 
MET CA  C    sing N N 314 
MET CA  CB   sing N N 315 
MET CA  HA   sing N N 316 
MET C   O    doub N N 317 
MET C   OXT  sing N N 318 
MET CB  CG   sing N N 319 
MET CB  HB2  sing N N 320 
MET CB  HB3  sing N N 321 
MET CG  SD   sing N N 322 
MET CG  HG2  sing N N 323 
MET CG  HG3  sing N N 324 
MET SD  CE   sing N N 325 
MET CE  HE1  sing N N 326 
MET CE  HE2  sing N N 327 
MET CE  HE3  sing N N 328 
MET OXT HXT  sing N N 329 
PHE N   CA   sing N N 330 
PHE N   H    sing N N 331 
PHE N   H2   sing N N 332 
PHE CA  C    sing N N 333 
PHE CA  CB   sing N N 334 
PHE CA  HA   sing N N 335 
PHE C   O    doub N N 336 
PHE C   OXT  sing N N 337 
PHE CB  CG   sing N N 338 
PHE CB  HB2  sing N N 339 
PHE CB  HB3  sing N N 340 
PHE CG  CD1  doub Y N 341 
PHE CG  CD2  sing Y N 342 
PHE CD1 CE1  sing Y N 343 
PHE CD1 HD1  sing N N 344 
PHE CD2 CE2  doub Y N 345 
PHE CD2 HD2  sing N N 346 
PHE CE1 CZ   doub Y N 347 
PHE CE1 HE1  sing N N 348 
PHE CE2 CZ   sing Y N 349 
PHE CE2 HE2  sing N N 350 
PHE CZ  HZ   sing N N 351 
PHE OXT HXT  sing N N 352 
PRO N   CA   sing N N 353 
PRO N   CD   sing N N 354 
PRO N   H    sing N N 355 
PRO CA  C    sing N N 356 
PRO CA  CB   sing N N 357 
PRO CA  HA   sing N N 358 
PRO C   O    doub N N 359 
PRO C   OXT  sing N N 360 
PRO CB  CG   sing N N 361 
PRO CB  HB2  sing N N 362 
PRO CB  HB3  sing N N 363 
PRO CG  CD   sing N N 364 
PRO CG  HG2  sing N N 365 
PRO CG  HG3  sing N N 366 
PRO CD  HD2  sing N N 367 
PRO CD  HD3  sing N N 368 
PRO OXT HXT  sing N N 369 
SER N   CA   sing N N 370 
SER N   H    sing N N 371 
SER N   H2   sing N N 372 
SER CA  C    sing N N 373 
SER CA  CB   sing N N 374 
SER CA  HA   sing N N 375 
SER C   O    doub N N 376 
SER C   OXT  sing N N 377 
SER CB  OG   sing N N 378 
SER CB  HB2  sing N N 379 
SER CB  HB3  sing N N 380 
SER OG  HG   sing N N 381 
SER OXT HXT  sing N N 382 
THR N   CA   sing N N 383 
THR N   H    sing N N 384 
THR N   H2   sing N N 385 
THR CA  C    sing N N 386 
THR CA  CB   sing N N 387 
THR CA  HA   sing N N 388 
THR C   O    doub N N 389 
THR C   OXT  sing N N 390 
THR CB  OG1  sing N N 391 
THR CB  CG2  sing N N 392 
THR CB  HB   sing N N 393 
THR OG1 HG1  sing N N 394 
THR CG2 HG21 sing N N 395 
THR CG2 HG22 sing N N 396 
THR CG2 HG23 sing N N 397 
THR OXT HXT  sing N N 398 
TRP N   CA   sing N N 399 
TRP N   H    sing N N 400 
TRP N   H2   sing N N 401 
TRP CA  C    sing N N 402 
TRP CA  CB   sing N N 403 
TRP CA  HA   sing N N 404 
TRP C   O    doub N N 405 
TRP C   OXT  sing N N 406 
TRP CB  CG   sing N N 407 
TRP CB  HB2  sing N N 408 
TRP CB  HB3  sing N N 409 
TRP CG  CD1  doub Y N 410 
TRP CG  CD2  sing Y N 411 
TRP CD1 NE1  sing Y N 412 
TRP CD1 HD1  sing N N 413 
TRP CD2 CE2  doub Y N 414 
TRP CD2 CE3  sing Y N 415 
TRP NE1 CE2  sing Y N 416 
TRP NE1 HE1  sing N N 417 
TRP CE2 CZ2  sing Y N 418 
TRP CE3 CZ3  doub Y N 419 
TRP CE3 HE3  sing N N 420 
TRP CZ2 CH2  doub Y N 421 
TRP CZ2 HZ2  sing N N 422 
TRP CZ3 CH2  sing Y N 423 
TRP CZ3 HZ3  sing N N 424 
TRP CH2 HH2  sing N N 425 
TRP OXT HXT  sing N N 426 
TYR N   CA   sing N N 427 
TYR N   H    sing N N 428 
TYR N   H2   sing N N 429 
TYR CA  C    sing N N 430 
TYR CA  CB   sing N N 431 
TYR CA  HA   sing N N 432 
TYR C   O    doub N N 433 
TYR C   OXT  sing N N 434 
TYR CB  CG   sing N N 435 
TYR CB  HB2  sing N N 436 
TYR CB  HB3  sing N N 437 
TYR CG  CD1  doub Y N 438 
TYR CG  CD2  sing Y N 439 
TYR CD1 CE1  sing Y N 440 
TYR CD1 HD1  sing N N 441 
TYR CD2 CE2  doub Y N 442 
TYR CD2 HD2  sing N N 443 
TYR CE1 CZ   doub Y N 444 
TYR CE1 HE1  sing N N 445 
TYR CE2 CZ   sing Y N 446 
TYR CE2 HE2  sing N N 447 
TYR CZ  OH   sing N N 448 
TYR OH  HH   sing N N 449 
TYR OXT HXT  sing N N 450 
VAL N   CA   sing N N 451 
VAL N   H    sing N N 452 
VAL N   H2   sing N N 453 
VAL CA  C    sing N N 454 
VAL CA  CB   sing N N 455 
VAL CA  HA   sing N N 456 
VAL C   O    doub N N 457 
VAL C   OXT  sing N N 458 
VAL CB  CG1  sing N N 459 
VAL CB  CG2  sing N N 460 
VAL CB  HB   sing N N 461 
VAL CG1 HG11 sing N N 462 
VAL CG1 HG12 sing N N 463 
VAL CG1 HG13 sing N N 464 
VAL CG2 HG21 sing N N 465 
VAL CG2 HG22 sing N N 466 
VAL CG2 HG23 sing N N 467 
VAL OXT HXT  sing N N 468 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4HT0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6QL2 
_atom_sites.fract_transf_matrix[1][1]   0.023733 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006013 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024208 
_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]   0.014455 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 30.503  2.296   7.444   1.00 50.41  ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 31.169  2.108   8.750   1.00 38.17  ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.483  0.978   9.510   1.00 29.11  ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.730  -0.207  9.300   1.00 32.60  ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 31.227  3.443   9.522   1.00 43.05  ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 30.119  4.377   9.189   1.00 56.09  ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 29.641  5.298   10.105  1.00 72.12  ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 29.403  4.545   8.057   1.00 58.00  ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 28.670  5.998   9.547   1.00 81.88  ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 28.503  5.551   8.289   1.00 84.71  ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.576  1.348   10.397  1.00 24.15  ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 28.899  0.364   11.226  1.00 18.85  ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 27.863  -0.439  10.433  1.00 18.97  ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.313  0.032   9.434   1.00 20.56  ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.240  1.055   12.416  1.00 19.72  ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 27.040  1.891   12.073  1.00 18.76  ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 27.024  3.233   11.774  1.00 20.67  ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.664  1.442   12.006  1.00 16.77  ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.738  3.654   11.549  1.00 20.72  ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.888  2.569   11.641  1.00 19.31  ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 25.032  0.206   12.213  1.00 15.92  ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.499  2.489   11.550  1.00 20.35  ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.647  0.120   12.078  1.00 16.61  ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 22.905  1.262   11.775  1.00 17.82  ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.571  -1.652  10.914  1.00 16.72  ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.509  -2.445  10.292  1.00 18.73  ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.197  -3.590  11.242  1.00 16.67  ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.214  -3.439  12.463  1.00 17.24  ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 25.876  -4.749  10.676  1.00 17.97  ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.442  -5.899  11.447  1.00 19.16  ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.302  -7.127  11.207  1.00 23.84  ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 25.897  -8.223  11.610  1.00 33.40  ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 23.968  -6.152  11.132  1.00 18.99  ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.076  -5.106  11.755  1.00 14.45  ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.756  -5.160  13.117  1.00 15.10  ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.566  -4.067  10.977  1.00 16.11  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 21.868  -4.215  13.642  1.00 13.71  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 21.686  -3.135  11.509  1.00 15.79  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.383  -3.184  12.858  1.00 14.23  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.486  -2.294  13.327  1.00 16.20  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.453  -6.951  10.546  1.00 22.85  ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 28.300  -8.112  10.272  1.00 28.00  ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.282  -8.429  11.405  1.00 27.16  ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.441  -7.703  12.391  1.00 31.12  ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 30.089  -9.465  11.195  1.00 34.73  ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 31.144  -9.890  12.108  1.00 36.51  ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 32.135  -8.750  12.331  1.00 34.99  ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 32.665  -8.598  13.431  1.00 33.82  ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 31.858  -11.122 11.532  1.00 44.89  ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 33.180  -11.484 12.199  1.00 42.94  ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 33.036  -12.566 13.248  1.00 58.44  ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 32.597  -13.886 12.649  1.00 71.96  ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 31.571  -14.586 13.467  1.00 73.09  ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 32.389  -7.948  11.280  1.00 30.24  ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 33.451  -6.979  11.360  1.00 25.70  ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 32.985  -5.599  11.775  1.00 22.17  ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 33.812  -4.767  12.149  1.00 27.50  ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 34.209  -6.951  10.037  1.00 29.74  ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 34.758  -8.303  9.741   1.00 28.67  ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 35.708  -8.867  10.579  1.00 31.16  ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 34.463  -9.236  8.793   1.00 34.30  ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 36.004  -10.089 10.168  1.00 25.17  ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 35.260  -10.339 9.039   1.00 36.16  ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 31.674  -5.344  11.713  1.00 20.69  ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 31.209  -3.986  11.974  1.00 19.19  ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 29.922  -3.982  12.805  1.00 19.08  ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 29.284  -2.948  12.914  1.00 18.41  ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 31.027  -3.188  10.690  1.00 20.90  ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 29.964  -3.806  9.799   1.00 22.52  ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 29.373  -4.831  10.176  1.00 26.14  ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 29.666  -3.181  8.663   1.00 24.14  ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 29.573  -5.139  13.407  1.00 19.42  ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 28.296  -5.301  14.095  1.00 17.20  ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 28.297  -4.756  15.508  1.00 16.03  ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 29.189  -4.049  15.940  1.00 16.68  ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 27.218  -5.053  16.247  1.00 14.61  ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 26.991  -4.524  17.582  1.00 14.82  ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 28.146  -4.547  18.571  1.00 15.45  ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 28.270  -3.623  19.354  1.00 15.90  ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 25.782  -5.347  18.069  1.00 16.97  ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 24.984  -5.557  16.827  1.00 16.22  ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 26.048  -5.773  15.738  1.00 15.72  ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 14  ? 29.010  -5.563  18.531  1.00 16.46  ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 14  ? 30.113  -5.679  19.473  1.00 19.92  ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 14  ? 31.198  -4.629  19.166  1.00 17.82  ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 14  ? 32.108  -4.422  19.969  1.00 19.94  ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 14  ? 30.629  -7.114  19.413  1.00 29.80  ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 14  ? 31.218  -7.450  18.036  1.00 35.91  ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 14  ? 30.452  -8.055  16.850  1.00 41.86  ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 14  ? 29.302  -7.634  16.614  1.00 27.68  ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 14  ? 31.013  -8.941  16.175  1.00 34.43  ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 15  ? 31.151  -4.029  17.969  1.00 16.09  ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 15  ? 32.136  -3.040  17.565  1.00 18.20  ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 15  ? 31.657  -1.605  17.723  1.00 14.23  ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 15  ? 32.501  -0.696  17.703  1.00 16.15  ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 15  ? 32.480  -3.173  16.085  1.00 18.87  ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 15  ? 33.188  -4.433  15.742  1.00 19.42  ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 15  ? 34.566  -4.515  15.778  1.00 22.17  ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 15  ? 32.714  -5.645  15.377  1.00 22.21  ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 15  ? 34.922  -5.750  15.456  1.00 27.82  ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 15  ? 33.796  -6.460  15.213  1.00 27.39  ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 16  ? 30.344  -1.390  17.931  1.00 14.69  ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 16  ? 29.847  -0.036  17.836  1.00 13.91  ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 16  ? 30.419  0.922   18.867  1.00 14.21  ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 16  ? 30.523  2.119   18.634  1.00 15.31  ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 16  ? 28.316  -0.087  17.965  1.00 14.09  ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 16  ? 27.621  -0.783  16.835  1.00 13.11  ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 16  ? 28.122  -1.133  15.609  1.00 14.20  ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 16  ? 26.223  -1.101  16.783  1.00 11.96  ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 16  ? 27.176  -1.726  14.832  1.00 13.99  ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 16  ? 25.983  -1.708  15.521  1.00 13.08  ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 16  ? 25.182  -0.959  17.691  1.00 11.90  ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 16  ? 24.713  -2.138  15.148  1.00 11.76  ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 16  ? 23.935  -1.394  17.316  1.00 12.13  ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 16  ? 23.721  -1.963  16.072  1.00 12.30  ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 17  ? 30.796  0.379   20.037  1.00 13.85  ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 17  ? 31.257  1.230   21.122  1.00 15.38  ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 17  ? 32.513  2.015   20.736  1.00 18.05  ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 17  ? 32.779  3.051   21.340  1.00 17.26  ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 17  ? 31.539  0.425   22.413  1.00 15.63  ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 17  ? 32.747  -0.439  22.311  1.00 16.89  ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 17  ? 33.971  -0.014  22.794  1.00 19.70  ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 17  ? 32.956  -1.617  21.676  1.00 18.42  ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 17  ? 34.891  -0.913  22.476  1.00 20.45  ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 17  ? 34.310  -1.921  21.802  1.00 19.84  ? 17  HIS A NE2 1 
ATOM   126  N  N   . LYS A 1 18  ? 33.287  1.531   19.758  1.00 17.45  ? 18  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 18  ? 34.516  2.247   19.445  1.00 18.89  ? 18  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 18  ? 34.213  3.581   18.773  1.00 20.60  ? 18  LYS A C   1 
ATOM   129  O  O   . LYS A 1 18  ? 34.923  4.558   19.002  1.00 26.79  ? 18  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 18  ? 35.358  1.394   18.500  1.00 19.49  ? 18  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 18  ? 35.899  0.112   19.167  1.00 18.32  ? 18  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 18  ? 36.653  -0.798  18.212  1.00 18.97  ? 18  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 18  ? 35.713  -1.729  17.492  1.00 19.66  ? 18  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 18  ? 36.410  -2.486  16.429  1.00 19.47  ? 18  LYS A NZ  1 
ATOM   135  N  N   . ASP A 1 19  ? 33.154  3.695   17.944  1.00 17.68  ? 19  ASP A N   1 
ATOM   136  C  CA  . ASP A 1 19  ? 32.774  4.980   17.374  1.00 17.52  ? 19  ASP A CA  1 
ATOM   137  C  C   . ASP A 1 19  ? 31.734  5.689   18.237  1.00 16.87  ? 19  ASP A C   1 
ATOM   138  O  O   . ASP A 1 19  ? 31.553  6.890   18.115  1.00 20.77  ? 19  ASP A O   1 
ATOM   139  C  CB  . ASP A 1 19  ? 32.372  4.835   15.901  1.00 21.83  ? 19  ASP A CB  1 
ATOM   140  C  CG  . ASP A 1 19  ? 33.595  4.573   15.029  1.00 33.73  ? 19  ASP A CG  1 
ATOM   141  O  OD1 . ASP A 1 19  ? 34.282  5.547   14.729  1.00 35.54  ? 19  ASP A OD1 1 
ATOM   142  O  OD2 . ASP A 1 19  ? 33.923  3.376   14.793  1.00 46.75  ? 19  ASP A OD2 1 
ATOM   143  N  N   . PHE A 1 20  ? 30.976  4.913   19.034  1.00 15.62  ? 20  PHE A N   1 
ATOM   144  C  CA  . PHE A 1 20  ? 29.825  5.433   19.747  1.00 17.22  ? 20  PHE A CA  1 
ATOM   145  C  C   . PHE A 1 20  ? 29.922  4.949   21.185  1.00 17.67  ? 20  PHE A C   1 
ATOM   146  O  O   . PHE A 1 20  ? 29.281  3.959   21.548  1.00 16.52  ? 20  PHE A O   1 
ATOM   147  C  CB  . PHE A 1 20  ? 28.514  4.944   19.082  1.00 16.10  ? 20  PHE A CB  1 
ATOM   148  C  CG  . PHE A 1 20  ? 28.454  5.294   17.613  1.00 16.01  ? 20  PHE A CG  1 
ATOM   149  C  CD1 . PHE A 1 20  ? 28.110  6.579   17.213  1.00 18.32  ? 20  PHE A CD1 1 
ATOM   150  C  CD2 . PHE A 1 20  ? 28.835  4.371   16.647  1.00 16.60  ? 20  PHE A CD2 1 
ATOM   151  C  CE1 . PHE A 1 20  ? 28.121  6.934   15.863  1.00 20.24  ? 20  PHE A CE1 1 
ATOM   152  C  CE2 . PHE A 1 20  ? 28.829  4.693   15.296  1.00 19.24  ? 20  PHE A CE2 1 
ATOM   153  C  CZ  . PHE A 1 20  ? 28.515  5.993   14.918  1.00 20.67  ? 20  PHE A CZ  1 
ATOM   154  N  N   . PRO A 1 21  ? 30.776  5.576   22.027  1.00 16.58  ? 21  PRO A N   1 
ATOM   155  C  CA  . PRO A 1 21  ? 31.041  5.055   23.372  1.00 18.75  ? 21  PRO A CA  1 
ATOM   156  C  C   . PRO A 1 21  ? 29.812  4.930   24.269  1.00 15.94  ? 21  PRO A C   1 
ATOM   157  O  O   . PRO A 1 21  ? 29.871  4.118   25.205  1.00 17.33  ? 21  PRO A O   1 
ATOM   158  C  CB  . PRO A 1 21  ? 32.113  5.978   23.991  1.00 23.48  ? 21  PRO A CB  1 
ATOM   159  C  CG  . PRO A 1 21  ? 32.302  7.075   22.973  1.00 26.85  ? 21  PRO A CG  1 
ATOM   160  C  CD  . PRO A 1 21  ? 31.719  6.648   21.650  1.00 21.06  ? 21  PRO A CD  1 
ATOM   161  N  N   . ILE A 1 22  ? 28.748  5.698   23.985  1.00 15.43  ? 22  ILE A N   1 
ATOM   162  C  CA  . ILE A 1 22  ? 27.534  5.522   24.778  1.00 14.78  ? 22  ILE A CA  1 
ATOM   163  C  C   . ILE A 1 22  ? 26.935  4.134   24.588  1.00 13.84  ? 22  ILE A C   1 
ATOM   164  O  O   . ILE A 1 22  ? 26.066  3.754   25.350  1.00 14.95  ? 22  ILE A O   1 
ATOM   165  C  CB  . ILE A 1 22  ? 26.529  6.620   24.384  1.00 15.37  ? 22  ILE A CB  1 
ATOM   166  C  CG1 . ILE A 1 22  ? 25.396  6.822   25.393  1.00 19.49  ? 22  ILE A CG1 1 
ATOM   167  C  CG2 . ILE A 1 22  ? 25.926  6.316   22.993  1.00 15.15  ? 22  ILE A CG2 1 
ATOM   168  C  CD1 . ILE A 1 22  ? 25.859  7.290   26.760  1.00 24.49  ? 22  ILE A CD1 1 
ATOM   169  N  N   . ALA A 1 23  ? 27.470  3.312   23.668  1.00 14.53  ? 23  ALA A N   1 
ATOM   170  C  CA  . ALA A 1 23  ? 27.046  1.931   23.554  1.00 14.20  ? 23  ALA A CA  1 
ATOM   171  C  C   . ALA A 1 23  ? 27.156  1.201   24.891  1.00 14.59  ? 23  ALA A C   1 
ATOM   172  O  O   . ALA A 1 23  ? 26.439  0.199   25.058  1.00 15.61  ? 23  ALA A O   1 
ATOM   173  C  CB  . ALA A 1 23  ? 27.851  1.205   22.485  1.00 15.80  ? 23  ALA A CB  1 
ATOM   174  N  N   . LYS A 1 24  ? 28.087  1.656   25.787  1.00 16.14  ? 24  LYS A N   1 
ATOM   175  C  CA  . LYS A 1 24  ? 28.294  1.030   27.080  1.00 16.64  ? 24  LYS A CA  1 
ATOM   176  C  C   . LYS A 1 24  ? 27.671  1.878   28.195  1.00 18.85  ? 24  LYS A C   1 
ATOM   177  O  O   . LYS A 1 24  ? 28.083  1.748   29.360  1.00 20.90  ? 24  LYS A O   1 
ATOM   178  C  CB  . LYS A 1 24  ? 29.784  0.799   27.331  1.00 19.42  ? 24  LYS A CB  1 
ATOM   179  C  CG  . LYS A 1 24  ? 30.405  -0.212  26.374  1.00 23.16  ? 24  LYS A CG  1 
ATOM   180  C  CD  . LYS A 1 24  ? 31.882  -0.427  26.708  1.00 28.79  ? 24  LYS A CD  1 
ATOM   181  C  CE  . LYS A 1 24  ? 32.582  -1.411  25.805  1.00 28.82  ? 24  LYS A CE  1 
ATOM   182  N  NZ  . LYS A 1 24  ? 32.007  -2.767  25.935  1.00 38.26  ? 24  LYS A NZ  1 
ATOM   183  N  N   . GLY A 1 25  ? 26.655  2.692   27.840  1.00 17.18  ? 25  GLY A N   1 
ATOM   184  C  CA  . GLY A 1 25  ? 25.990  3.597   28.763  1.00 17.65  ? 25  GLY A CA  1 
ATOM   185  C  C   . GLY A 1 25  ? 25.043  2.882   29.717  1.00 16.69  ? 25  GLY A C   1 
ATOM   186  O  O   . GLY A 1 25  ? 24.872  1.664   29.695  1.00 18.02  ? 25  GLY A O   1 
ATOM   187  N  N   . GLU A 1 26  ? 24.335  3.712   30.476  1.00 17.67  ? 26  GLU A N   1 
ATOM   188  C  CA  . GLU A 1 26  ? 23.487  3.258   31.551  1.00 19.52  ? 26  GLU A CA  1 
ATOM   189  C  C   . GLU A 1 26  ? 22.044  3.057   31.127  1.00 15.11  ? 26  GLU A C   1 
ATOM   190  O  O   . GLU A 1 26  ? 21.282  2.514   31.927  1.00 17.12  ? 26  GLU A O   1 
ATOM   191  C  CB  . GLU A 1 26  ? 23.547  4.274   32.703  1.00 25.67  ? 26  GLU A CB  1 
ATOM   192  C  CG  . GLU A 1 26  ? 24.949  4.457   33.322  1.00 36.03  ? 26  GLU A CG  1 
ATOM   193  C  CD  . GLU A 1 26  ? 25.588  3.162   33.797  1.00 46.44  ? 26  GLU A CD  1 
ATOM   194  O  OE1 . GLU A 1 26  ? 25.013  2.492   34.719  1.00 46.37  ? 26  GLU A OE1 1 
ATOM   195  O  OE2 . GLU A 1 26  ? 26.657  2.825   33.241  1.00 50.15  ? 26  GLU A OE2 1 
ATOM   196  N  N   A ARG A 1 27  ? 21.711  3.453   29.886  0.50 12.72  ? 27  ARG A N   1 
ATOM   197  N  N   B ARG A 1 27  ? 21.691  3.494   29.917  0.50 14.24  ? 27  ARG A N   1 
ATOM   198  C  CA  A ARG A 1 27  ? 20.325  3.446   29.458  0.50 11.33  ? 27  ARG A CA  1 
ATOM   199  C  CA  B ARG A 1 27  ? 20.316  3.301   29.523  0.50 14.67  ? 27  ARG A CA  1 
ATOM   200  C  C   A ARG A 1 27  ? 20.203  2.879   28.043  0.50 10.48  ? 27  ARG A C   1 
ATOM   201  C  C   B ARG A 1 27  ? 20.271  2.916   28.051  0.50 11.71  ? 27  ARG A C   1 
ATOM   202  O  O   A ARG A 1 27  ? 19.389  3.349   27.263  0.50 10.98  ? 27  ARG A O   1 
ATOM   203  O  O   B ARG A 1 27  ? 19.619  3.567   27.248  0.50 13.05  ? 27  ARG A O   1 
ATOM   204  C  CB  A ARG A 1 27  ? 19.689  4.831   29.546  0.50 11.14  ? 27  ARG A CB  1 
ATOM   205  C  CB  B ARG A 1 27  ? 19.425  4.474   29.919  0.50 19.24  ? 27  ARG A CB  1 
ATOM   206  C  CG  A ARG A 1 27  ? 19.944  5.585   30.840  0.50 13.05  ? 27  ARG A CG  1 
ATOM   207  C  CG  B ARG A 1 27  ? 19.739  5.779   29.215  0.50 21.60  ? 27  ARG A CG  1 
ATOM   208  C  CD  A ARG A 1 27  ? 19.468  7.008   30.656  0.50 14.12  ? 27  ARG A CD  1 
ATOM   209  C  CD  B ARG A 1 27  ? 18.319  6.298   29.163  0.50 26.43  ? 27  ARG A CD  1 
ATOM   210  N  NE  A ARG A 1 27  ? 19.709  7.846   31.826  0.50 14.65  ? 27  ARG A NE  1 
ATOM   211  N  NE  B ARG A 1 27  ? 18.087  7.725   28.995  0.50 36.82  ? 27  ARG A NE  1 
ATOM   212  C  CZ  A ARG A 1 27  ? 20.778  8.606   31.965  0.50 16.54  ? 27  ARG A CZ  1 
ATOM   213  C  CZ  B ARG A 1 27  ? 16.997  8.300   28.467  0.50 17.90  ? 27  ARG A CZ  1 
ATOM   214  N  NH1 A ARG A 1 27  ? 20.867  9.408   33.006  0.50 19.63  ? 27  ARG A NH1 1 
ATOM   215  N  NH1 B ARG A 1 27  ? 16.892  9.607   28.423  0.50 5.47   ? 27  ARG A NH1 1 
ATOM   216  N  NH2 A ARG A 1 27  ? 21.673  8.674   30.992  0.50 19.29  ? 27  ARG A NH2 1 
ATOM   217  N  NH2 B ARG A 1 27  ? 16.041  7.604   27.952  0.50 13.34  ? 27  ARG A NH2 1 
ATOM   218  N  N   . GLN A 1 28  ? 20.924  1.803   27.736  1.00 11.33  ? 28  GLN A N   1 
ATOM   219  C  CA  . GLN A 1 28  ? 20.956  1.293   26.371  1.00 11.10  ? 28  GLN A CA  1 
ATOM   220  C  C   . GLN A 1 28  ? 19.776  0.371   26.118  1.00 10.16  ? 28  GLN A C   1 
ATOM   221  O  O   . GLN A 1 28  ? 19.284  -0.333  26.986  1.00 11.66  ? 28  GLN A O   1 
ATOM   222  C  CB  . GLN A 1 28  ? 22.297  0.593   26.137  1.00 12.00  ? 28  GLN A CB  1 
ATOM   223  C  CG  . GLN A 1 28  ? 23.434  1.603   26.053  1.00 12.65  ? 28  GLN A CG  1 
ATOM   224  C  CD  . GLN A 1 28  ? 23.313  2.452   24.815  1.00 11.68  ? 28  GLN A CD  1 
ATOM   225  O  OE1 . GLN A 1 28  ? 23.522  1.940   23.714  1.00 12.20  ? 28  GLN A OE1 1 
ATOM   226  N  NE2 . GLN A 1 28  ? 22.998  3.746   24.905  1.00 12.60  ? 28  GLN A NE2 1 
ATOM   227  N  N   . SER A 1 29  ? 19.415  0.296   24.839  1.00 9.66   ? 29  SER A N   1 
ATOM   228  C  CA  . SER A 1 29  ? 18.334  -0.543  24.351  1.00 9.54   ? 29  SER A CA  1 
ATOM   229  C  C   . SER A 1 29  ? 18.821  -1.394  23.208  1.00 9.21   ? 29  SER A C   1 
ATOM   230  O  O   . SER A 1 29  ? 19.799  -1.053  22.524  1.00 10.31  ? 29  SER A O   1 
ATOM   231  C  CB  . SER A 1 29  ? 17.180  0.339   23.822  1.00 10.35  ? 29  SER A CB  1 
ATOM   232  O  OG  . SER A 1 29  ? 16.607  1.070   24.919  1.00 10.37  ? 29  SER A OG  1 
ATOM   233  N  N   . PRO A 1 30  ? 18.206  -2.543  22.924  1.00 9.29   ? 30  PRO A N   1 
ATOM   234  C  CA  . PRO A 1 30  ? 17.018  -3.046  23.638  1.00 9.16   ? 30  PRO A CA  1 
ATOM   235  C  C   . PRO A 1 30  ? 17.417  -3.762  24.921  1.00 9.21   ? 30  PRO A C   1 
ATOM   236  O  O   . PRO A 1 30  ? 18.588  -3.807  25.254  1.00 10.43  ? 30  PRO A O   1 
ATOM   237  C  CB  . PRO A 1 30  ? 16.508  -4.080  22.614  1.00 9.70   ? 30  PRO A CB  1 
ATOM   238  C  CG  . PRO A 1 30  ? 17.771  -4.656  22.052  1.00 10.51  ? 30  PRO A CG  1 
ATOM   239  C  CD  . PRO A 1 30  ? 18.656  -3.459  21.848  1.00 9.59   ? 30  PRO A CD  1 
ATOM   240  N  N   . VAL A 1 31  ? 16.401  -4.280  25.632  1.00 10.27  ? 31  VAL A N   1 
ATOM   241  C  CA  . VAL A 1 31  ? 16.601  -5.050  26.836  1.00 11.36  ? 31  VAL A CA  1 
ATOM   242  C  C   . VAL A 1 31  ? 15.724  -6.291  26.774  1.00 10.84  ? 31  VAL A C   1 
ATOM   243  O  O   . VAL A 1 31  ? 14.753  -6.324  26.011  1.00 11.29  ? 31  VAL A O   1 
ATOM   244  C  CB  . VAL A 1 31  ? 16.258  -4.219  28.097  1.00 11.94  ? 31  VAL A CB  1 
ATOM   245  C  CG1 . VAL A 1 31  ? 17.194  -2.989  28.208  1.00 12.15  ? 31  VAL A CG1 1 
ATOM   246  C  CG2 . VAL A 1 31  ? 14.802  -3.796  28.166  1.00 12.64  ? 31  VAL A CG2 1 
ATOM   247  N  N   . ASP A 1 32  ? 16.037  -7.253  27.630  1.00 11.06  ? 32  ASP A N   1 
ATOM   248  C  CA  . ASP A 1 32  ? 15.112  -8.303  27.936  1.00 11.30  ? 32  ASP A CA  1 
ATOM   249  C  C   . ASP A 1 32  ? 14.056  -7.784  28.910  1.00 11.61  ? 32  ASP A C   1 
ATOM   250  O  O   . ASP A 1 32  ? 14.338  -7.162  29.940  1.00 14.78  ? 32  ASP A O   1 
ATOM   251  C  CB  . ASP A 1 32  ? 15.826  -9.500  28.539  1.00 14.32  ? 32  ASP A CB  1 
ATOM   252  C  CG  . ASP A 1 32  ? 14.865  -10.645 28.825  1.00 14.50  ? 32  ASP A CG  1 
ATOM   253  O  OD1 . ASP A 1 32  ? 14.188  -11.102 27.884  1.00 14.61  ? 32  ASP A OD1 1 
ATOM   254  O  OD2 . ASP A 1 32  ? 14.870  -11.106 30.024  1.00 18.23  ? 32  ASP A OD2 1 
ATOM   255  N  N   . ILE A 1 33  ? 12.795  -8.056  28.591  1.00 11.60  ? 33  ILE A N   1 
ATOM   256  C  CA  . ILE A 1 33  ? 11.674  -7.677  29.447  1.00 12.68  ? 33  ILE A CA  1 
ATOM   257  C  C   . ILE A 1 33  ? 11.366  -8.891  30.303  1.00 13.34  ? 33  ILE A C   1 
ATOM   258  O  O   . ILE A 1 33  ? 10.812  -9.877  29.820  1.00 14.23  ? 33  ILE A O   1 
ATOM   259  C  CB  . ILE A 1 33  ? 10.473  -7.234  28.607  1.00 13.07  ? 33  ILE A CB  1 
ATOM   260  C  CG1 . ILE A 1 33  ? 10.880  -6.022  27.730  1.00 13.35  ? 33  ILE A CG1 1 
ATOM   261  C  CG2 . ILE A 1 33  ? 9.287   -6.932  29.533  1.00 13.55  ? 33  ILE A CG2 1 
ATOM   262  C  CD1 . ILE A 1 33  ? 9.875   -5.771  26.625  1.00 15.97  ? 33  ILE A CD1 1 
ATOM   263  N  N   . ASP A 1 34  ? 11.779  -8.801  31.560  1.00 14.63  ? 34  ASP A N   1 
ATOM   264  C  CA  . ASP A 1 34  ? 11.469  -9.844  32.519  1.00 15.63  ? 34  ASP A CA  1 
ATOM   265  C  C   . ASP A 1 34  ? 10.071  -9.551  33.057  1.00 14.70  ? 34  ASP A C   1 
ATOM   266  O  O   . ASP A 1 34  ? 9.893   -8.605  33.848  1.00 16.75  ? 34  ASP A O   1 
ATOM   267  C  CB  . ASP A 1 34  ? 12.564  -9.876  33.608  1.00 18.38  ? 34  ASP A CB  1 
ATOM   268  C  CG  . ASP A 1 34  ? 12.378  -10.956 34.660  1.00 23.74  ? 34  ASP A CG  1 
ATOM   269  O  OD1 . ASP A 1 34  ? 11.242  -11.386 34.888  1.00 22.64  ? 34  ASP A OD1 1 
ATOM   270  O  OD2 . ASP A 1 34  ? 13.373  -11.325 35.274  1.00 37.02  ? 34  ASP A OD2 1 
ATOM   271  N  N   . THR A 1 35  ? 9.115   -10.357 32.621  1.00 15.71  ? 35  THR A N   1 
ATOM   272  C  CA  . THR A 1 35  ? 7.741   -10.043 32.937  1.00 18.47  ? 35  THR A CA  1 
ATOM   273  C  C   . THR A 1 35  ? 7.436   -10.237 34.407  1.00 18.10  ? 35  THR A C   1 
ATOM   274  O  O   . THR A 1 35  ? 6.453   -9.662  34.888  1.00 21.28  ? 35  THR A O   1 
ATOM   275  C  CB  . THR A 1 35  ? 6.797   -10.848 32.052  1.00 18.86  ? 35  THR A CB  1 
ATOM   276  O  OG1 . THR A 1 35  ? 6.892   -12.208 32.486  1.00 20.42  ? 35  THR A OG1 1 
ATOM   277  C  CG2 . THR A 1 35  ? 7.128   -10.730 30.576  1.00 21.71  ? 35  THR A CG2 1 
ATOM   278  N  N   . HIS A 1 36  ? 8.300   -10.978 35.135  1.00 18.98  ? 36  HIS A N   1 
ATOM   279  C  CA  . HIS A 1 36  ? 8.153   -11.249 36.556  1.00 21.70  ? 36  HIS A CA  1 
ATOM   280  C  C   . HIS A 1 36  ? 8.819   -10.211 37.447  1.00 23.79  ? 36  HIS A C   1 
ATOM   281  O  O   . HIS A 1 36  ? 8.663   -10.271 38.689  1.00 23.42  ? 36  HIS A O   1 
ATOM   282  C  CB  . HIS A 1 36  ? 8.830   -12.580 36.839  1.00 20.65  ? 36  HIS A CB  1 
ATOM   283  C  CG  . HIS A 1 36  ? 8.274   -13.611 35.921  1.00 23.60  ? 36  HIS A CG  1 
ATOM   284  N  ND1 . HIS A 1 36  ? 8.994   -14.194 34.861  1.00 25.97  ? 36  HIS A ND1 1 
ATOM   285  C  CD2 . HIS A 1 36  ? 7.031   -14.162 35.917  1.00 24.13  ? 36  HIS A CD2 1 
ATOM   286  C  CE1 . HIS A 1 36  ? 8.215   -15.100 34.288  1.00 26.24  ? 36  HIS A CE1 1 
ATOM   287  N  NE2 . HIS A 1 36  ? 7.007   -15.065 34.905  1.00 27.78  ? 36  HIS A NE2 1 
ATOM   288  N  N   . THR A 1 37  ? 9.590   -9.299  36.886  1.00 19.97  ? 37  THR A N   1 
ATOM   289  C  CA  . THR A 1 37  ? 10.124  -8.181  37.651  1.00 17.69  ? 37  THR A CA  1 
ATOM   290  C  C   . THR A 1 37  ? 9.502   -6.871  37.192  1.00 20.09  ? 37  THR A C   1 
ATOM   291  O  O   . THR A 1 37  ? 9.584   -5.880  37.926  1.00 24.40  ? 37  THR A O   1 
ATOM   292  C  CB  . THR A 1 37  ? 11.643  -8.230  37.771  1.00 24.37  ? 37  THR A CB  1 
ATOM   293  O  OG1 . THR A 1 37  ? 12.239  -8.216  36.495  1.00 31.55  ? 37  THR A OG1 1 
ATOM   294  C  CG2 . THR A 1 37  ? 12.076  -9.570  38.291  1.00 26.34  ? 37  THR A CG2 1 
ATOM   295  N  N   . ALA A 1 38  ? 8.836   -6.846  36.027  1.00 16.89  ? 38  ALA A N   1 
ATOM   296  C  CA  . ALA A 1 38  ? 8.214   -5.579  35.608  1.00 18.03  ? 38  ALA A CA  1 
ATOM   297  C  C   . ALA A 1 38  ? 7.127   -5.226  36.623  1.00 19.39  ? 38  ALA A C   1 
ATOM   298  O  O   . ALA A 1 38  ? 6.525   -6.084  37.223  1.00 22.40  ? 38  ALA A O   1 
ATOM   299  C  CB  . ALA A 1 38  ? 7.629   -5.751  34.225  1.00 17.78  ? 38  ALA A CB  1 
ATOM   300  N  N   . LYS A 1 39  ? 6.995   -3.953  36.919  1.00 17.91  ? 39  LYS A N   1 
ATOM   301  C  CA  . LYS A 1 39  ? 6.055   -3.463  37.920  1.00 21.42  ? 39  LYS A CA  1 
ATOM   302  C  C   . LYS A 1 39  ? 4.784   -2.953  37.234  1.00 18.00  ? 39  LYS A C   1 
ATOM   303  O  O   . LYS A 1 39  ? 4.840   -1.989  36.473  1.00 17.77  ? 39  LYS A O   1 
ATOM   304  C  CB  . LYS A 1 39  ? 6.787   -2.335  38.670  1.00 25.02  ? 39  LYS A CB  1 
ATOM   305  C  CG  . LYS A 1 39  ? 5.995   -1.463  39.625  1.00 29.51  ? 39  LYS A CG  1 
ATOM   306  C  CD  . LYS A 1 39  ? 5.741   -2.186  40.899  1.00 28.29  ? 39  LYS A CD  1 
ATOM   307  C  CE  . LYS A 1 39  ? 5.015   -1.308  41.895  1.00 34.95  ? 39  LYS A CE  1 
ATOM   308  N  NZ  . LYS A 1 39  ? 4.584   -2.092  43.064  1.00 39.31  ? 39  LYS A NZ  1 
ATOM   309  N  N   . TYR A 1 40  ? 3.626   -3.517  37.601  1.00 21.01  ? 40  TYR A N   1 
ATOM   310  C  CA  . TYR A 1 40  ? 2.367   -2.927  37.195  1.00 19.77  ? 40  TYR A CA  1 
ATOM   311  C  C   . TYR A 1 40  ? 2.264   -1.535  37.802  1.00 19.26  ? 40  TYR A C   1 
ATOM   312  O  O   . TYR A 1 40  ? 2.392   -1.371  39.029  1.00 22.67  ? 40  TYR A O   1 
ATOM   313  C  CB  . TYR A 1 40  ? 1.178   -3.821  37.535  1.00 25.75  ? 40  TYR A CB  1 
ATOM   314  C  CG  . TYR A 1 40  ? -0.147  -3.112  37.439  1.00 26.19  ? 40  TYR A CG  1 
ATOM   315  C  CD1 . TYR A 1 40  ? -0.601  -2.594  36.236  1.00 26.97  ? 40  TYR A CD1 1 
ATOM   316  C  CD2 . TYR A 1 40  ? -0.999  -3.015  38.538  1.00 34.47  ? 40  TYR A CD2 1 
ATOM   317  C  CE1 . TYR A 1 40  ? -1.822  -1.964  36.123  1.00 33.94  ? 40  TYR A CE1 1 
ATOM   318  C  CE2 . TYR A 1 40  ? -2.228  -2.370  38.451  1.00 33.06  ? 40  TYR A CE2 1 
ATOM   319  C  CZ  . TYR A 1 40  ? -2.645  -1.857  37.227  1.00 33.55  ? 40  TYR A CZ  1 
ATOM   320  O  OH  . TYR A 1 40  ? -3.838  -1.218  37.094  1.00 45.61  ? 40  TYR A OH  1 
ATOM   321  N  N   . ASP A 1 41  ? 1.963   -0.556  36.945  1.00 19.96  ? 41  ASP A N   1 
ATOM   322  C  CA  . ASP A 1 41  ? 1.827   0.797   37.436  1.00 19.19  ? 41  ASP A CA  1 
ATOM   323  C  C   . ASP A 1 41  ? 0.400   1.267   37.211  1.00 26.90  ? 41  ASP A C   1 
ATOM   324  O  O   . ASP A 1 41  ? 0.107   1.675   36.087  1.00 24.92  ? 41  ASP A O   1 
ATOM   325  C  CB  . ASP A 1 41  ? 2.875   1.752   36.866  1.00 23.01  ? 41  ASP A CB  1 
ATOM   326  C  CG  . ASP A 1 41  ? 2.801   3.139   37.499  1.00 31.74  ? 41  ASP A CG  1 
ATOM   327  O  OD1 . ASP A 1 41  ? 1.751   3.443   38.164  1.00 34.27  ? 41  ASP A OD1 1 
ATOM   328  O  OD2 . ASP A 1 41  ? 3.780   3.909   37.331  1.00 41.42  ? 41  ASP A OD2 1 
ATOM   329  N  N   . PRO A 1 42  ? -0.471  1.262   38.264  1.00 31.87  ? 42  PRO A N   1 
ATOM   330  C  CA  . PRO A 1 42  ? -1.878  1.559   38.038  1.00 35.10  ? 42  PRO A CA  1 
ATOM   331  C  C   . PRO A 1 42  ? -2.049  3.014   37.623  1.00 36.77  ? 42  PRO A C   1 
ATOM   332  O  O   . PRO A 1 42  ? -3.103  3.376   37.120  1.00 43.58  ? 42  PRO A O   1 
ATOM   333  C  CB  . PRO A 1 42  ? -2.555  1.213   39.366  1.00 37.47  ? 42  PRO A CB  1 
ATOM   334  C  CG  . PRO A 1 42  ? -1.432  1.349   40.389  1.00 44.44  ? 42  PRO A CG  1 
ATOM   335  C  CD  . PRO A 1 42  ? -0.174  0.899   39.672  1.00 33.40  ? 42  PRO A CD  1 
ATOM   336  N  N   . SER A 1 43  ? -1.003  3.845   37.768  1.00 34.06  ? 43  SER A N   1 
ATOM   337  C  CA  . SER A 1 43  ? -1.189  5.250   37.397  1.00 36.25  ? 43  SER A CA  1 
ATOM   338  C  C   . SER A 1 43  ? -0.860  5.496   35.910  1.00 31.56  ? 43  SER A C   1 
ATOM   339  O  O   . SER A 1 43  ? -1.099  6.598   35.421  1.00 38.51  ? 43  SER A O   1 
ATOM   340  C  CB  . SER A 1 43  ? -0.412  6.165   38.324  1.00 44.36  ? 43  SER A CB  1 
ATOM   341  O  OG  . SER A 1 43  ? 0.992   5.977   38.158  1.00 40.79  ? 43  SER A OG  1 
ATOM   342  N  N   . LEU A 1 44  ? -0.262  4.529   35.199  1.00 32.34  ? 44  LEU A N   1 
ATOM   343  C  CA  . LEU A 1 44  ? 0.012   4.707   33.777  1.00 28.64  ? 44  LEU A CA  1 
ATOM   344  C  C   . LEU A 1 44  ? -1.307  4.803   33.022  1.00 28.42  ? 44  LEU A C   1 
ATOM   345  O  O   . LEU A 1 44  ? -2.238  4.038   33.287  1.00 33.63  ? 44  LEU A O   1 
ATOM   346  C  CB  . LEU A 1 44  ? 0.749   3.494   33.238  1.00 24.51  ? 44  LEU A CB  1 
ATOM   347  C  CG  . LEU A 1 44  ? 2.245   3.429   33.501  1.00 21.03  ? 44  LEU A CG  1 
ATOM   348  C  CD1 . LEU A 1 44  ? 2.694   2.051   33.021  1.00 21.41  ? 44  LEU A CD1 1 
ATOM   349  C  CD2 . LEU A 1 44  ? 2.978   4.546   32.748  1.00 20.18  ? 44  LEU A CD2 1 
ATOM   350  N  N   . LYS A 1 45  ? -1.351  5.757   32.100  1.00 31.01  ? 45  LYS A N   1 
ATOM   351  C  CA  . LYS A 1 45  ? -2.522  5.962   31.252  1.00 28.06  ? 45  LYS A CA  1 
ATOM   352  C  C   . LYS A 1 45  ? -2.569  4.998   30.077  1.00 24.73  ? 45  LYS A C   1 
ATOM   353  O  O   . LYS A 1 45  ? -1.572  4.389   29.677  1.00 25.99  ? 45  LYS A O   1 
ATOM   354  C  CB  . LYS A 1 45  ? -2.563  7.382   30.727  1.00 28.93  ? 45  LYS A CB  1 
ATOM   355  C  CG  . LYS A 1 45  ? -2.552  8.450   31.817  1.00 33.90  ? 45  LYS A CG  1 
ATOM   356  C  CD  . LYS A 1 45  ? -2.959  9.806   31.291  1.00 55.11  ? 45  LYS A CD  1 
ATOM   357  C  CE  . LYS A 1 45  ? -1.804  10.770  31.106  1.00 64.83  ? 45  LYS A CE  1 
ATOM   358  N  NZ  . LYS A 1 45  ? -1.046  10.971  32.367  1.00 68.59  ? 45  LYS A NZ  1 
ATOM   359  N  N   . PRO A 1 46  ? -3.765  4.794   29.483  1.00 25.86  ? 46  PRO A N   1 
ATOM   360  C  CA  . PRO A 1 46  ? -3.836  4.042   28.239  1.00 23.82  ? 46  PRO A CA  1 
ATOM   361  C  C   . PRO A 1 46  ? -3.027  4.867   27.264  1.00 21.00  ? 46  PRO A C   1 
ATOM   362  O  O   . PRO A 1 46  ? -3.008  6.077   27.341  1.00 22.26  ? 46  PRO A O   1 
ATOM   363  C  CB  . PRO A 1 46  ? -5.331  4.065   27.846  1.00 23.23  ? 46  PRO A CB  1 
ATOM   364  C  CG  . PRO A 1 46  ? -6.077  4.481   29.088  1.00 33.10  ? 46  PRO A CG  1 
ATOM   365  C  CD  . PRO A 1 46  ? -5.084  5.266   29.921  1.00 31.93  ? 46  PRO A CD  1 
ATOM   366  N  N   . LEU A 1 47  ? -2.436  4.169   26.301  1.00 21.11  ? 47  LEU A N   1 
ATOM   367  C  CA  . LEU A 1 47  ? -1.756  4.858   25.250  1.00 20.39  ? 47  LEU A CA  1 
ATOM   368  C  C   . LEU A 1 47  ? -2.836  5.463   24.359  1.00 21.55  ? 47  LEU A C   1 
ATOM   369  O  O   . LEU A 1 47  ? -3.860  4.838   24.107  1.00 25.53  ? 47  LEU A O   1 
ATOM   370  C  CB  . LEU A 1 47  ? -1.047  3.758   24.467  1.00 27.30  ? 47  LEU A CB  1 
ATOM   371  C  CG  . LEU A 1 47  ? 0.163   4.097   23.646  1.00 30.10  ? 47  LEU A CG  1 
ATOM   372  C  CD1 . LEU A 1 47  ? 1.210   4.772   24.543  1.00 32.74  ? 47  LEU A CD1 1 
ATOM   373  C  CD2 . LEU A 1 47  ? 0.666   2.771   23.051  1.00 31.81  ? 47  LEU A CD2 1 
ATOM   374  N  N   . SER A 1 48  ? -2.543  6.622   23.806  1.00 16.96  ? 48  SER A N   1 
ATOM   375  C  CA  . SER A 1 48  ? -3.402  7.242   22.809  1.00 17.84  ? 48  SER A CA  1 
ATOM   376  C  C   . SER A 1 48  ? -2.621  7.237   21.499  1.00 17.18  ? 48  SER A C   1 
ATOM   377  O  O   . SER A 1 48  ? -1.607  7.934   21.369  1.00 17.88  ? 48  SER A O   1 
ATOM   378  C  CB  . SER A 1 48  ? -3.695  8.703   23.195  1.00 19.97  ? 48  SER A CB  1 
ATOM   379  O  OG  . SER A 1 48  ? -4.406  9.354   22.168  1.00 25.73  ? 48  SER A OG  1 
ATOM   380  N  N   . VAL A 1 49  ? -3.026  6.377   20.597  1.00 18.63  ? 49  VAL A N   1 
ATOM   381  C  CA  . VAL A 1 49  ? -2.417  6.306   19.285  1.00 20.33  ? 49  VAL A CA  1 
ATOM   382  C  C   . VAL A 1 49  ? -3.394  6.936   18.309  1.00 21.83  ? 49  VAL A C   1 
ATOM   383  O  O   . VAL A 1 49  ? -4.489  6.432   18.110  1.00 26.56  ? 49  VAL A O   1 
ATOM   384  C  CB  . VAL A 1 49  ? -2.168  4.841   18.902  1.00 24.57  ? 49  VAL A CB  1 
ATOM   385  C  CG1 . VAL A 1 49  ? -1.580  4.732   17.499  1.00 28.92  ? 49  VAL A CG1 1 
ATOM   386  C  CG2 . VAL A 1 49  ? -1.377  4.071   19.966  1.00 25.94  ? 49  VAL A CG2 1 
ATOM   387  N  N   . SER A 1 50  ? -3.023  8.049   17.699  1.00 20.19  ? 50  SER A N   1 
ATOM   388  C  CA  . SER A 1 50  ? -3.964  8.837   16.915  1.00 20.56  ? 50  SER A CA  1 
ATOM   389  C  C   . SER A 1 50  ? -3.390  8.956   15.508  1.00 18.55  ? 50  SER A C   1 
ATOM   390  O  O   . SER A 1 50  ? -2.726  9.934   15.231  1.00 20.52  ? 50  SER A O   1 
ATOM   391  C  CB  . SER A 1 50  ? -4.272  10.231  17.489  1.00 26.17  ? 50  SER A CB  1 
ATOM   392  O  OG  . SER A 1 50  ? -4.946  10.122  18.710  1.00 33.15  ? 50  SER A OG  1 
ATOM   393  N  N   . TYR A 1 51  ? -3.622  7.944   14.661  1.00 19.25  ? 51  TYR A N   1 
ATOM   394  C  CA  . TYR A 1 51  ? -3.037  7.825   13.340  1.00 20.02  ? 51  TYR A CA  1 
ATOM   395  C  C   . TYR A 1 51  ? -4.044  8.067   12.219  1.00 22.80  ? 51  TYR A C   1 
ATOM   396  O  O   . TYR A 1 51  ? -3.676  7.883   11.067  1.00 22.82  ? 51  TYR A O   1 
ATOM   397  C  CB  . TYR A 1 51  ? -2.422  6.430   13.186  1.00 18.83  ? 51  TYR A CB  1 
ATOM   398  C  CG  . TYR A 1 51  ? -1.136  6.147   13.959  1.00 17.39  ? 51  TYR A CG  1 
ATOM   399  C  CD1 . TYR A 1 51  ? -0.466  7.158   14.627  1.00 17.71  ? 51  TYR A CD1 1 
ATOM   400  C  CD2 . TYR A 1 51  ? -0.600  4.871   14.013  1.00 16.54  ? 51  TYR A CD2 1 
ATOM   401  C  CE1 . TYR A 1 51  ? 0.701   6.911   15.330  1.00 15.69  ? 51  TYR A CE1 1 
ATOM   402  C  CE2 . TYR A 1 51  ? 0.567   4.606   14.711  1.00 15.05  ? 51  TYR A CE2 1 
ATOM   403  C  CZ  . TYR A 1 51  ? 1.220   5.630   15.373  1.00 13.98  ? 51  TYR A CZ  1 
ATOM   404  O  OH  . TYR A 1 51  ? 2.370   5.377   16.063  1.00 15.35  ? 51  TYR A OH  1 
ATOM   405  N  N   . ASP A 1 52  ? -5.283  8.500   12.527  1.00 25.37  ? 52  ASP A N   1 
ATOM   406  C  CA  . ASP A 1 52  ? -6.287  8.746   11.505  1.00 26.87  ? 52  ASP A CA  1 
ATOM   407  C  C   . ASP A 1 52  ? -5.835  9.702   10.399  1.00 24.88  ? 52  ASP A C   1 
ATOM   408  O  O   . ASP A 1 52  ? -6.210  9.488   9.240   1.00 28.79  ? 52  ASP A O   1 
ATOM   409  C  CB  . ASP A 1 52  ? -7.642  9.061   12.129  1.00 35.31  ? 52  ASP A CB  1 
ATOM   410  C  CG  . ASP A 1 52  ? -7.606  10.013  13.312  1.00 56.56  ? 52  ASP A CG  1 
ATOM   411  O  OD1 . ASP A 1 52  ? -6.703  9.843   14.198  1.00 59.23  ? 52  ASP A OD1 1 
ATOM   412  O  OD2 . ASP A 1 52  ? -8.489  10.906  13.349  1.00 70.95  ? 52  ASP A OD2 1 
ATOM   413  N  N   . GLN A 1 53  ? -5.018  10.718  10.726  1.00 25.21  ? 53  GLN A N   1 
ATOM   414  C  CA  . GLN A 1 53  ? -4.638  11.672  9.678   1.00 30.60  ? 53  GLN A CA  1 
ATOM   415  C  C   . GLN A 1 53  ? -3.220  11.431  9.162   1.00 23.73  ? 53  GLN A C   1 
ATOM   416  O  O   . GLN A 1 53  ? -2.599  12.315  8.581   1.00 26.65  ? 53  GLN A O   1 
ATOM   417  C  CB  . GLN A 1 53  ? -4.852  13.134  10.097  1.00 39.49  ? 53  GLN A CB  1 
ATOM   418  C  CG  . GLN A 1 53  ? -6.321  13.562  10.090  1.00 52.11  ? 53  GLN A CG  1 
ATOM   419  C  CD  . GLN A 1 53  ? -7.002  13.333  8.759   1.00 56.71  ? 53  GLN A CD  1 
ATOM   420  O  OE1 . GLN A 1 53  ? -6.539  13.782  7.692   1.00 58.94  ? 53  GLN A OE1 1 
ATOM   421  N  NE2 . GLN A 1 53  ? -8.121  12.629  8.813   1.00 53.01  ? 53  GLN A NE2 1 
ATOM   422  N  N   . ALA A 1 54  ? -2.662  10.245  9.397   1.00 21.23  ? 54  ALA A N   1 
ATOM   423  C  CA  . ALA A 1 54  ? -1.302  9.995   8.961   1.00 16.79  ? 54  ALA A CA  1 
ATOM   424  C  C   . ALA A 1 54  ? -1.131  10.172  7.454   1.00 19.46  ? 54  ALA A C   1 
ATOM   425  O  O   . ALA A 1 54  ? -1.974  9.755   6.665   1.00 25.09  ? 54  ALA A O   1 
ATOM   426  C  CB  . ALA A 1 54  ? -0.831  8.614   9.409   1.00 20.03  ? 54  ALA A CB  1 
ATOM   427  N  N   . THR A 1 55  ? 0.002   10.769  7.062   1.00 17.69  ? 55  THR A N   1 
ATOM   428  C  CA  . THR A 1 55  ? 0.298   10.997  5.649   1.00 18.66  ? 55  THR A CA  1 
ATOM   429  C  C   . THR A 1 55  ? 1.639   10.345  5.377   1.00 15.75  ? 55  THR A C   1 
ATOM   430  O  O   . THR A 1 55  ? 2.669   10.948  5.633   1.00 17.07  ? 55  THR A O   1 
ATOM   431  C  CB  . THR A 1 55  ? 0.399   12.493  5.290   1.00 21.61  ? 55  THR A CB  1 
ATOM   432  O  OG1 . THR A 1 55  ? -0.867  13.067  5.592   1.00 30.59  ? 55  THR A OG1 1 
ATOM   433  C  CG2 . THR A 1 55  ? 0.813   12.683  3.844   1.00 27.11  ? 55  THR A CG2 1 
ATOM   434  N  N   . SER A 1 56  ? 1.603   9.114   4.885   1.00 17.03  ? 56  SER A N   1 
ATOM   435  C  CA  . SER A 1 56  ? 2.860   8.492   4.478   1.00 15.92  ? 56  SER A CA  1 
ATOM   436  C  C   . SER A 1 56  ? 3.337   9.158   3.184   1.00 18.80  ? 56  SER A C   1 
ATOM   437  O  O   . SER A 1 56  ? 2.518   9.588   2.355   1.00 21.23  ? 56  SER A O   1 
ATOM   438  C  CB  . SER A 1 56  ? 2.750   6.988   4.289   1.00 18.40  ? 56  SER A CB  1 
ATOM   439  O  OG  . SER A 1 56  ? 1.862   6.673   3.209   1.00 18.95  ? 56  SER A OG  1 
ATOM   440  N  N   . LEU A 1 57  ? 4.659   9.222   2.993   1.00 16.00  ? 57  LEU A N   1 
ATOM   441  C  CA  . LEU A 1 57  ? 5.210   9.830   1.803   1.00 18.42  ? 57  LEU A CA  1 
ATOM   442  C  C   . LEU A 1 57  ? 6.052   8.859   0.990   1.00 18.42  ? 57  LEU A C   1 
ATOM   443  O  O   . LEU A 1 57  ? 5.984   8.889   -0.236  1.00 19.08  ? 57  LEU A O   1 
ATOM   444  C  CB  . LEU A 1 57  ? 6.025   11.040  2.250   1.00 21.51  ? 57  LEU A CB  1 
ATOM   445  C  CG  . LEU A 1 57  ? 5.253   12.186  2.917   1.00 24.43  ? 57  LEU A CG  1 
ATOM   446  C  CD1 . LEU A 1 57  ? 6.228   13.240  3.460   1.00 32.15  ? 57  LEU A CD1 1 
ATOM   447  C  CD2 . LEU A 1 57  ? 4.247   12.840  1.955   1.00 29.62  ? 57  LEU A CD2 1 
ATOM   448  N  N   . ARG A 1 58  ? 6.916   8.053   1.616   1.00 17.13  ? 58  ARG A N   1 
ATOM   449  C  CA  . ARG A 1 58  ? 7.977   7.386   0.899   1.00 17.92  ? 58  ARG A CA  1 
ATOM   450  C  C   . ARG A 1 58  ? 8.451   6.178   1.680   1.00 15.53  ? 58  ARG A C   1 
ATOM   451  O  O   . ARG A 1 58  ? 8.348   6.180   2.913   1.00 17.49  ? 58  ARG A O   1 
ATOM   452  C  CB  . ARG A 1 58  ? 9.101   8.411   0.781   1.00 21.39  ? 58  ARG A CB  1 
ATOM   453  C  CG  . ARG A 1 58  ? 10.191  8.044   -0.196  1.00 25.13  ? 58  ARG A CG  1 
ATOM   454  C  CD  . ARG A 1 58  ? 11.141  9.223   -0.256  1.00 28.78  ? 58  ARG A CD  1 
ATOM   455  N  NE  . ARG A 1 58  ? 11.938  9.246   0.937   1.00 25.99  ? 58  ARG A NE  1 
ATOM   456  C  CZ  . ARG A 1 58  ? 13.239  9.412   0.897   1.00 20.72  ? 58  ARG A CZ  1 
ATOM   457  N  NH1 . ARG A 1 58  ? 13.846  9.729   -0.238  1.00 22.86  ? 58  ARG A NH1 1 
ATOM   458  N  NH2 . ARG A 1 58  ? 13.920  9.388   2.023   1.00 21.25  ? 58  ARG A NH2 1 
ATOM   459  N  N   . ILE A 1 59  ? 9.063   5.241   0.960   1.00 15.11  ? 59  ILE A N   1 
ATOM   460  C  CA  . ILE A 1 59  ? 9.717   4.106   1.596   1.00 14.43  ? 59  ILE A CA  1 
ATOM   461  C  C   . ILE A 1 59  ? 11.153  4.099   1.102   1.00 13.80  ? 59  ILE A C   1 
ATOM   462  O  O   . ILE A 1 59  ? 11.421  4.357   -0.069  1.00 16.95  ? 59  ILE A O   1 
ATOM   463  C  CB  . ILE A 1 59  ? 8.951   2.810   1.339   1.00 15.38  ? 59  ILE A CB  1 
ATOM   464  C  CG1 . ILE A 1 59  ? 9.496   1.662   2.199   1.00 15.83  ? 59  ILE A CG1 1 
ATOM   465  C  CG2 . ILE A 1 59  ? 8.963   2.454   -0.177  1.00 15.83  ? 59  ILE A CG2 1 
ATOM   466  C  CD1 . ILE A 1 59  ? 8.551   0.439   2.148   1.00 15.70  ? 59  ILE A CD1 1 
ATOM   467  N  N   . LEU A 1 60  ? 12.087  3.787   1.997   1.00 16.00  ? 60  LEU A N   1 
ATOM   468  C  CA  . LEU A 1 60  ? 13.513  3.961   1.748   1.00 14.52  ? 60  LEU A CA  1 
ATOM   469  C  C   . LEU A 1 60  ? 14.264  2.743   2.303   1.00 14.35  ? 60  LEU A C   1 
ATOM   470  O  O   . LEU A 1 60  ? 14.042  2.361   3.443   1.00 14.75  ? 60  LEU A O   1 
ATOM   471  C  CB  . LEU A 1 60  ? 14.004  5.259   2.470   1.00 17.03  ? 60  LEU A CB  1 
ATOM   472  C  CG  . LEU A 1 60  ? 15.518  5.427   2.479   1.00 16.90  ? 60  LEU A CG  1 
ATOM   473  C  CD1 . LEU A 1 60  ? 16.090  5.714   1.070   1.00 19.23  ? 60  LEU A CD1 1 
ATOM   474  C  CD2 . LEU A 1 60  ? 15.901  6.549   3.439   1.00 19.07  ? 60  LEU A CD2 1 
ATOM   475  N  N   . ASN A 1 61  ? 15.183  2.159   1.511   1.00 15.13  ? 61  ASN A N   1 
ATOM   476  C  CA  . ASN A 1 61  ? 16.179  1.221   1.984   1.00 13.77  ? 61  ASN A CA  1 
ATOM   477  C  C   . ASN A 1 61  ? 17.407  2.038   2.403   1.00 14.46  ? 61  ASN A C   1 
ATOM   478  O  O   . ASN A 1 61  ? 18.018  2.665   1.539   1.00 17.09  ? 61  ASN A O   1 
ATOM   479  C  CB  . ASN A 1 61  ? 16.504  0.182   0.916   1.00 16.06  ? 61  ASN A CB  1 
ATOM   480  C  CG  . ASN A 1 61  ? 17.598  -0.778  1.322   1.00 13.74  ? 61  ASN A CG  1 
ATOM   481  O  OD1 . ASN A 1 61  ? 18.432  -0.484  2.218   1.00 17.27  ? 61  ASN A OD1 1 
ATOM   482  N  ND2 . ASN A 1 61  ? 17.587  -1.966  0.733   1.00 16.68  ? 61  ASN A ND2 1 
ATOM   483  N  N   . ASN A 1 62  ? 17.725  2.115   3.712   1.00 14.58  ? 62  ASN A N   1 
ATOM   484  C  CA  . ASN A 1 62  ? 18.790  3.007   4.166   1.00 16.22  ? 62  ASN A CA  1 
ATOM   485  C  C   . ASN A 1 62  ? 20.079  2.235   4.407   1.00 15.46  ? 62  ASN A C   1 
ATOM   486  O  O   . ASN A 1 62  ? 21.085  2.769   4.910   1.00 20.68  ? 62  ASN A O   1 
ATOM   487  C  CB  . ASN A 1 62  ? 18.405  3.833   5.380   1.00 19.73  ? 62  ASN A CB  1 
ATOM   488  C  CG  . ASN A 1 62  ? 18.269  2.977   6.626   1.00 18.60  ? 62  ASN A CG  1 
ATOM   489  O  OD1 . ASN A 1 62  ? 18.557  1.779   6.617   1.00 15.34  ? 62  ASN A OD1 1 
ATOM   490  N  ND2 . ASN A 1 62  ? 18.055  3.637   7.730   1.00 25.53  ? 62  ASN A ND2 1 
ATOM   491  N  N   . GLY A 1 63  ? 20.132  0.978   3.938   1.00 16.36  ? 63  GLY A N   1 
ATOM   492  C  CA  . GLY A 1 63  ? 21.289  0.132   4.100   1.00 15.81  ? 63  GLY A CA  1 
ATOM   493  C  C   . GLY A 1 63  ? 21.336  -0.653  5.402   1.00 17.70  ? 63  GLY A C   1 
ATOM   494  O  O   . GLY A 1 63  ? 22.221  -1.478  5.570   1.00 17.97  ? 63  GLY A O   1 
ATOM   495  N  N   . HIS A 1 64  ? 20.433  -0.352  6.333   1.00 14.81  ? 64  HIS A N   1 
ATOM   496  C  CA  . HIS A 1 64  ? 20.370  -1.039  7.620   1.00 13.83  ? 64  HIS A CA  1 
ATOM   497  C  C   . HIS A 1 64  ? 19.012  -1.684  7.866   1.00 12.91  ? 64  HIS A C   1 
ATOM   498  O  O   . HIS A 1 64  ? 18.930  -2.690  8.561   1.00 18.46  ? 64  HIS A O   1 
ATOM   499  C  CB  . HIS A 1 64  ? 20.667  -0.069  8.807   1.00 16.42  ? 64  HIS A CB  1 
ATOM   500  C  CG  . HIS A 1 64  ? 21.877  0.761   8.559   1.00 18.78  ? 64  HIS A CG  1 
ATOM   501  N  ND1 . HIS A 1 64  ? 23.150  0.190   8.618   1.00 23.36  ? 64  HIS A ND1 1 
ATOM   502  C  CD2 . HIS A 1 64  ? 22.055  2.079   8.340   1.00 20.10  ? 64  HIS A CD2 1 
ATOM   503  C  CE1 . HIS A 1 64  ? 24.094  1.110   8.411   1.00 24.18  ? 64  HIS A CE1 1 
ATOM   504  N  NE2 . HIS A 1 64  ? 23.443  2.300   8.242   1.00 24.42  ? 64  HIS A NE2 1 
ATOM   505  N  N   . THR A 1 65  ? 17.961  -1.091  7.326   1.00 12.99  ? 65  THR A N   1 
ATOM   506  C  CA  . THR A 1 65  ? 16.577  -1.504  7.403   1.00 12.90  ? 65  THR A CA  1 
ATOM   507  C  C   . THR A 1 65  ? 15.881  -0.849  6.210   1.00 12.34  ? 65  THR A C   1 
ATOM   508  O  O   . THR A 1 65  ? 16.539  -0.193  5.382   1.00 14.06  ? 65  THR A O   1 
ATOM   509  C  CB  . THR A 1 65  ? 15.988  -1.161  8.778   1.00 13.56  ? 65  THR A CB  1 
ATOM   510  O  OG1 . THR A 1 65  ? 14.672  -1.675  8.795   1.00 16.75  ? 65  THR A OG1 1 
ATOM   511  C  CG2 . THR A 1 65  ? 15.907  0.337   8.948   1.00 15.55  ? 65  THR A CG2 1 
ATOM   512  N  N   . PHE A 1 66  ? 14.572  -1.036  6.139   1.00 12.37  ? 66  PHE A N   1 
ATOM   513  C  CA  . PHE A 1 66  ? 13.776  -0.136  5.330   1.00 13.80  ? 66  PHE A CA  1 
ATOM   514  C  C   . PHE A 1 66  ? 12.870  0.687   6.246   1.00 11.98  ? 66  PHE A C   1 
ATOM   515  O  O   . PHE A 1 66  ? 12.458  0.213   7.312   1.00 12.84  ? 66  PHE A O   1 
ATOM   516  C  CB  . PHE A 1 66  ? 13.003  -0.902  4.244   1.00 15.67  ? 66  PHE A CB  1 
ATOM   517  C  CG  . PHE A 1 66  ? 11.881  -1.740  4.789   1.00 15.19  ? 66  PHE A CG  1 
ATOM   518  C  CD1 . PHE A 1 66  ? 10.613  -1.204  4.974   1.00 15.80  ? 66  PHE A CD1 1 
ATOM   519  C  CD2 . PHE A 1 66  ? 12.092  -3.083  5.119   1.00 14.96  ? 66  PHE A CD2 1 
ATOM   520  C  CE1 . PHE A 1 66  ? 9.574   -1.980  5.433   1.00 16.50  ? 66  PHE A CE1 1 
ATOM   521  C  CE2 . PHE A 1 66  ? 11.048  -3.892  5.591   1.00 15.74  ? 66  PHE A CE2 1 
ATOM   522  C  CZ  . PHE A 1 66  ? 9.773   -3.321  5.706   1.00 15.77  ? 66  PHE A CZ  1 
ATOM   523  N  N   . GLN A 1 67  ? 12.530  1.899   5.809   1.00 14.21  ? 67  GLN A N   1 
ATOM   524  C  CA  . GLN A 1 67  ? 11.714  2.787   6.623   1.00 14.17  ? 67  GLN A CA  1 
ATOM   525  C  C   . GLN A 1 67  ? 10.635  3.425   5.767   1.00 14.48  ? 67  GLN A C   1 
ATOM   526  O  O   . GLN A 1 67  ? 10.866  3.826   4.617   1.00 15.42  ? 67  GLN A O   1 
ATOM   527  C  CB  . GLN A 1 67  ? 12.551  3.848   7.366   1.00 18.72  ? 67  GLN A CB  1 
ATOM   528  C  CG  . GLN A 1 67  ? 13.188  4.853   6.456   1.00 20.26  ? 67  GLN A CG  1 
ATOM   529  C  CD  . GLN A 1 67  ? 14.040  5.860   7.214   1.00 22.41  ? 67  GLN A CD  1 
ATOM   530  O  OE1 . GLN A 1 67  ? 13.984  7.078   6.996   1.00 29.07  ? 67  GLN A OE1 1 
ATOM   531  N  NE2 . GLN A 1 67  ? 14.848  5.344   8.117   1.00 23.62  ? 67  GLN A NE2 1 
ATOM   532  N  N   . VAL A 1 68  ? 9.462   3.558   6.356   1.00 14.38  ? 68  VAL A N   1 
ATOM   533  C  CA  . VAL A 1 68  ? 8.377   4.279   5.737   1.00 14.56  ? 68  VAL A CA  1 
ATOM   534  C  C   . VAL A 1 68  ? 8.297   5.613   6.483   1.00 14.45  ? 68  VAL A C   1 
ATOM   535  O  O   . VAL A 1 68  ? 8.166   5.635   7.709   1.00 14.68  ? 68  VAL A O   1 
ATOM   536  C  CB  . VAL A 1 68  ? 7.049   3.506   5.866   1.00 14.96  ? 68  VAL A CB  1 
ATOM   537  C  CG1 . VAL A 1 68  ? 5.874   4.389   5.445   1.00 17.02  ? 68  VAL A CG1 1 
ATOM   538  C  CG2 . VAL A 1 68  ? 7.080   2.214   5.057   1.00 15.12  ? 68  VAL A CG2 1 
ATOM   539  N  N   . GLU A 1 69  ? 8.305   6.701   5.723   1.00 15.27  ? 69  GLU A N   1 
ATOM   540  C  CA  . GLU A 1 69  ? 8.402   8.033   6.295   1.00 14.03  ? 69  GLU A CA  1 
ATOM   541  C  C   . GLU A 1 69  ? 7.060   8.745   6.136   1.00 14.48  ? 69  GLU A C   1 
ATOM   542  O  O   . GLU A 1 69  ? 6.323   8.516   5.153   1.00 18.18  ? 69  GLU A O   1 
ATOM   543  C  CB  . GLU A 1 69  ? 9.420   8.841   5.528   1.00 18.22  ? 69  GLU A CB  1 
ATOM   544  C  CG  . GLU A 1 69  ? 10.762  8.199   5.581   1.00 19.53  ? 69  GLU A CG  1 
ATOM   545  C  CD  . GLU A 1 69  ? 11.700  8.748   4.530   1.00 22.36  ? 69  GLU A CD  1 
ATOM   546  O  OE1 . GLU A 1 69  ? 11.227  9.446   3.575   1.00 29.82  ? 69  GLU A OE1 1 
ATOM   547  O  OE2 . GLU A 1 69  ? 12.889  8.450   4.640   1.00 26.95  ? 69  GLU A OE2 1 
ATOM   548  N  N   . PHE A 1 70  ? 6.799   9.673   7.079   1.00 13.95  ? 70  PHE A N   1 
ATOM   549  C  CA  . PHE A 1 70  ? 5.545   10.387  7.093   1.00 13.93  ? 70  PHE A CA  1 
ATOM   550  C  C   . PHE A 1 70  ? 5.786   11.882  7.093   1.00 14.80  ? 70  PHE A C   1 
ATOM   551  O  O   . PHE A 1 70  ? 6.876   12.352  7.448   1.00 16.86  ? 70  PHE A O   1 
ATOM   552  C  CB  . PHE A 1 70  ? 4.813   10.030  8.388   1.00 13.49  ? 70  PHE A CB  1 
ATOM   553  C  CG  . PHE A 1 70  ? 4.309   8.610   8.348   1.00 14.02  ? 70  PHE A CG  1 
ATOM   554  C  CD1 . PHE A 1 70  ? 5.152   7.519   8.598   1.00 14.21  ? 70  PHE A CD1 1 
ATOM   555  C  CD2 . PHE A 1 70  ? 2.967   8.371   8.047   1.00 14.60  ? 70  PHE A CD2 1 
ATOM   556  C  CE1 . PHE A 1 70  ? 4.687   6.212   8.511   1.00 16.24  ? 70  PHE A CE1 1 
ATOM   557  C  CE2 . PHE A 1 70  ? 2.488   7.063   7.978   1.00 15.79  ? 70  PHE A CE2 1 
ATOM   558  C  CZ  . PHE A 1 70  ? 3.369   5.992   8.170   1.00 15.36  ? 70  PHE A CZ  1 
ATOM   559  N  N   . ASP A 1 71  ? 4.761   12.623  6.684   1.00 17.95  ? 71  ASP A N   1 
ATOM   560  C  CA  . ASP A 1 71  ? 4.762   14.063  6.840   1.00 17.10  ? 71  ASP A CA  1 
ATOM   561  C  C   . ASP A 1 71  ? 4.562   14.427  8.326   1.00 16.66  ? 71  ASP A C   1 
ATOM   562  O  O   . ASP A 1 71  ? 3.485   14.206  8.896   1.00 22.04  ? 71  ASP A O   1 
ATOM   563  C  CB  . ASP A 1 71  ? 3.653   14.680  5.980   1.00 22.61  ? 71  ASP A CB  1 
ATOM   564  C  CG  . ASP A 1 71  ? 3.449   16.167  6.255   1.00 23.72  ? 71  ASP A CG  1 
ATOM   565  O  OD1 . ASP A 1 71  ? 4.358   16.811  6.829   1.00 22.51  ? 71  ASP A OD1 1 
ATOM   566  O  OD2 . ASP A 1 71  ? 2.395   16.699  5.841   1.00 35.01  ? 71  ASP A OD2 1 
ATOM   567  N  N   . ASP A 1 72  ? 5.607   14.967  8.955   1.00 16.44  ? 72  ASP A N   1 
ATOM   568  C  CA  . ASP A 1 72  ? 5.573   15.339  10.362  1.00 17.65  ? 72  ASP A CA  1 
ATOM   569  C  C   . ASP A 1 72  ? 5.612   16.869  10.496  1.00 19.47  ? 72  ASP A C   1 
ATOM   570  O  O   . ASP A 1 72  ? 6.042   17.386  11.518  1.00 21.04  ? 72  ASP A O   1 
ATOM   571  C  CB  . ASP A 1 72  ? 6.743   14.696  11.104  1.00 18.11  ? 72  ASP A CB  1 
ATOM   572  C  CG  . ASP A 1 72  ? 8.069   15.308  10.681  1.00 18.64  ? 72  ASP A CG  1 
ATOM   573  O  OD1 . ASP A 1 72  ? 8.139   15.928  9.544   1.00 21.03  ? 72  ASP A OD1 1 
ATOM   574  O  OD2 . ASP A 1 72  ? 9.074   15.127  11.431  1.00 18.42  ? 72  ASP A OD2 1 
ATOM   575  N  N   . SER A 1 73  ? 5.122   17.606  9.492   1.00 21.13  ? 73  SER A N   1 
ATOM   576  C  CA  . SER A 1 73  ? 5.207   19.074  9.560   1.00 21.25  ? 73  SER A CA  1 
ATOM   577  C  C   . SER A 1 73  ? 3.926   19.686  10.161  1.00 23.74  ? 73  SER A C   1 
ATOM   578  O  O   . SER A 1 73  ? 3.782   20.899  10.266  1.00 25.19  ? 73  SER A O   1 
ATOM   579  C  CB  . SER A 1 73  ? 5.521   19.653  8.202   1.00 26.83  ? 73  SER A CB  1 
ATOM   580  O  OG  . SER A 1 73  ? 4.367   19.491  7.370   1.00 23.89  ? 73  SER A OG  1 
ATOM   581  N  N   . GLN A 1 74  ? 2.983   18.855  10.596  1.00 23.94  ? 74  GLN A N   1 
ATOM   582  C  CA  . GLN A 1 74  ? 1.770   19.275  11.286  1.00 26.20  ? 74  GLN A CA  1 
ATOM   583  C  C   . GLN A 1 74  ? 1.402   18.131  12.223  1.00 23.82  ? 74  GLN A C   1 
ATOM   584  O  O   . GLN A 1 74  ? 1.906   17.040  12.013  1.00 21.62  ? 74  GLN A O   1 
ATOM   585  C  CB  . GLN A 1 74  ? 0.595   19.396  10.302  1.00 29.79  ? 74  GLN A CB  1 
ATOM   586  C  CG  . GLN A 1 74  ? 0.524   20.704  9.547   1.00 33.47  ? 74  GLN A CG  1 
ATOM   587  C  CD  . GLN A 1 74  ? -0.696  20.799  8.660   1.00 42.69  ? 74  GLN A CD  1 
ATOM   588  O  OE1 . GLN A 1 74  ? -1.723  21.387  9.027   1.00 51.55  ? 74  GLN A OE1 1 
ATOM   589  N  NE2 . GLN A 1 74  ? -0.593  20.192  7.483   1.00 42.88  ? 74  GLN A NE2 1 
ATOM   590  N  N   . ASP A 1 75  ? 0.557   18.413  13.240  1.00 31.14  ? 75  ASP A N   1 
ATOM   591  C  CA  . ASP A 1 75  ? 0.105   17.382  14.158  1.00 32.81  ? 75  ASP A CA  1 
ATOM   592  C  C   . ASP A 1 75  ? -0.942  16.549  13.433  1.00 28.20  ? 75  ASP A C   1 
ATOM   593  O  O   . ASP A 1 75  ? -2.102  16.943  13.360  1.00 43.26  ? 75  ASP A O   1 
ATOM   594  C  CB  . ASP A 1 75  ? -0.465  17.930  15.479  1.00 36.85  ? 75  ASP A CB  1 
ATOM   595  C  CG  . ASP A 1 75  ? 0.547   18.202  16.584  1.00 40.66  ? 75  ASP A CG  1 
ATOM   596  O  OD1 . ASP A 1 75  ? 1.643   17.561  16.596  1.00 41.62  ? 75  ASP A OD1 1 
ATOM   597  O  OD2 . ASP A 1 75  ? 0.218   19.026  17.475  1.00 57.13  ? 75  ASP A OD2 1 
ATOM   598  N  N   . LYS A 1 76  ? -0.468  15.453  12.823  1.00 25.63  ? 76  LYS A N   1 
ATOM   599  C  CA  . LYS A 1 76  ? -1.276  14.473  12.122  1.00 25.42  ? 76  LYS A CA  1 
ATOM   600  C  C   . LYS A 1 76  ? -1.330  13.239  13.011  1.00 30.25  ? 76  LYS A C   1 
ATOM   601  O  O   . LYS A 1 76  ? -2.112  13.155  13.975  1.00 37.87  ? 76  LYS A O   1 
ATOM   602  C  CB  . LYS A 1 76  ? -0.732  14.276  10.696  1.00 24.47  ? 76  LYS A CB  1 
ATOM   603  C  CG  . LYS A 1 76  ? -0.851  15.494  9.785   1.00 31.37  ? 76  LYS A CG  1 
ATOM   604  C  CD  . LYS A 1 76  ? -0.273  15.207  8.417   1.00 28.28  ? 76  LYS A CD  1 
ATOM   605  C  CE  . LYS A 1 76  ? -0.820  16.197  7.415   1.00 30.83  ? 76  LYS A CE  1 
ATOM   606  N  NZ  . LYS A 1 76  ? -0.427  15.915  6.018   1.00 32.92  ? 76  LYS A NZ  1 
ATOM   607  N  N   . ALA A 1 77  ? -0.386  12.359  12.769  1.00 22.71  ? 77  ALA A N   1 
ATOM   608  C  CA  . ALA A 1 77  ? -0.295  11.078  13.458  1.00 19.40  ? 77  ALA A CA  1 
ATOM   609  C  C   . ALA A 1 77  ? 0.539   11.278  14.723  1.00 17.05  ? 77  ALA A C   1 
ATOM   610  O  O   . ALA A 1 77  ? 1.726   11.610  14.629  1.00 21.12  ? 77  ALA A O   1 
ATOM   611  C  CB  . ALA A 1 77  ? 0.398   10.147  12.492  1.00 25.32  ? 77  ALA A CB  1 
ATOM   612  N  N   . VAL A 1 78  ? -0.091  11.113  15.887  1.00 15.94  ? 78  VAL A N   1 
ATOM   613  C  CA  . VAL A 1 78  ? 0.606   11.420  17.128  1.00 16.29  ? 78  VAL A CA  1 
ATOM   614  C  C   . VAL A 1 78  ? 0.346   10.321  18.144  1.00 14.80  ? 78  VAL A C   1 
ATOM   615  O  O   . VAL A 1 78  ? -0.664  9.611   18.131  1.00 17.89  ? 78  VAL A O   1 
ATOM   616  C  CB  . VAL A 1 78  ? 0.173   12.753  17.722  1.00 21.09  ? 78  VAL A CB  1 
ATOM   617  C  CG1 . VAL A 1 78  ? 0.479   13.945  16.810  1.00 22.40  ? 78  VAL A CG1 1 
ATOM   618  C  CG2 . VAL A 1 78  ? -1.273  12.708  18.078  1.00 25.39  ? 78  VAL A CG2 1 
ATOM   619  N  N   . LEU A 1 79  ? 1.327   10.181  19.031  1.00 14.77  ? 79  LEU A N   1 
ATOM   620  C  CA  . LEU A 1 79  ? 1.265   9.289   20.183  1.00 14.61  ? 79  LEU A CA  1 
ATOM   621  C  C   . LEU A 1 79  ? 1.241   10.197  21.396  1.00 14.11  ? 79  LEU A C   1 
ATOM   622  O  O   . LEU A 1 79  ? 2.075   11.094  21.527  1.00 16.43  ? 79  LEU A O   1 
ATOM   623  C  CB  . LEU A 1 79  ? 2.502   8.397   20.112  1.00 16.12  ? 79  LEU A CB  1 
ATOM   624  C  CG  . LEU A 1 79  ? 2.659   7.365   21.211  1.00 17.22  ? 79  LEU A CG  1 
ATOM   625  C  CD1 . LEU A 1 79  ? 1.551   6.340   21.119  1.00 21.61  ? 79  LEU A CD1 1 
ATOM   626  C  CD2 . LEU A 1 79  ? 4.011   6.706   21.018  1.00 17.27  ? 79  LEU A CD2 1 
ATOM   627  N  N   . LYS A 1 80  ? 0.384   9.874   22.343  1.00 16.46  ? 80  LYS A N   1 
ATOM   628  C  CA  . LYS A 1 80  ? 0.401   10.606  23.606  1.00 18.09  ? 80  LYS A CA  1 
ATOM   629  C  C   . LYS A 1 80  ? -0.101  9.685   24.702  1.00 16.34  ? 80  LYS A C   1 
ATOM   630  O  O   . LYS A 1 80  ? -0.472  8.542   24.406  1.00 16.85  ? 80  LYS A O   1 
ATOM   631  C  CB  . LYS A 1 80  ? -0.356  11.930  23.543  1.00 23.44  ? 80  LYS A CB  1 
ATOM   632  C  CG  . LYS A 1 80  ? -1.817  11.775  23.212  1.00 27.45  ? 80  LYS A CG  1 
ATOM   633  C  CD  . LYS A 1 80  ? -2.495  13.142  23.201  1.00 38.34  ? 80  LYS A CD  1 
ATOM   634  C  CE  . LYS A 1 80  ? -2.655  13.723  21.814  1.00 53.28  ? 80  LYS A CE  1 
ATOM   635  N  NZ  . LYS A 1 80  ? -3.054  15.154  21.850  1.00 71.15  ? 80  LYS A NZ  1 
ATOM   636  N  N   . GLY A 1 81  ? -0.207  10.213  25.926  1.00 18.93  ? 81  GLY A N   1 
ATOM   637  C  CA  . GLY A 1 81  ? -0.701  9.395   27.030  1.00 19.47  ? 81  GLY A CA  1 
ATOM   638  C  C   . GLY A 1 81  ? 0.320   8.340   27.435  1.00 19.56  ? 81  GLY A C   1 
ATOM   639  O  O   . GLY A 1 81  ? 1.529   8.484   27.229  1.00 19.34  ? 81  GLY A O   1 
ATOM   640  N  N   . GLY A 1 82  ? -0.145  7.211   27.960  1.00 23.10  ? 82  GLY A N   1 
ATOM   641  C  CA  . GLY A 1 82  ? 0.772   6.225   28.498  1.00 27.89  ? 82  GLY A CA  1 
ATOM   642  C  C   . GLY A 1 82  ? 1.719   6.906   29.479  1.00 24.41  ? 82  GLY A C   1 
ATOM   643  O  O   . GLY A 1 82  ? 1.282   7.703   30.304  1.00 25.87  ? 82  GLY A O   1 
ATOM   644  N  N   . PRO A 1 83  ? 3.046   6.650   29.373  1.00 20.24  ? 83  PRO A N   1 
ATOM   645  C  CA  . PRO A 1 83  ? 4.024   7.275   30.260  1.00 22.77  ? 83  PRO A CA  1 
ATOM   646  C  C   . PRO A 1 83  ? 4.460   8.652   29.776  1.00 20.56  ? 83  PRO A C   1 
ATOM   647  O  O   . PRO A 1 83  ? 5.322   9.259   30.407  1.00 25.47  ? 83  PRO A O   1 
ATOM   648  C  CB  . PRO A 1 83  ? 5.202   6.301   30.152  1.00 22.29  ? 83  PRO A CB  1 
ATOM   649  C  CG  . PRO A 1 83  ? 5.132   5.869   28.694  1.00 18.49  ? 83  PRO A CG  1 
ATOM   650  C  CD  . PRO A 1 83  ? 3.650   5.732   28.395  1.00 19.67  ? 83  PRO A CD  1 
ATOM   651  N  N   . LEU A 1 84  ? 3.890   9.137   28.660  1.00 17.40  ? 84  LEU A N   1 
ATOM   652  C  CA  . LEU A 1 84  ? 4.476   10.322  28.012  1.00 18.30  ? 84  LEU A CA  1 
ATOM   653  C  C   . LEU A 1 84  ? 3.868   11.605  28.593  1.00 18.89  ? 84  LEU A C   1 
ATOM   654  O  O   . LEU A 1 84  ? 2.668   11.641  28.876  1.00 22.04  ? 84  LEU A O   1 
ATOM   655  C  CB  . LEU A 1 84  ? 4.167   10.235  26.513  1.00 15.23  ? 84  LEU A CB  1 
ATOM   656  C  CG  . LEU A 1 84  ? 4.715   8.977   25.835  1.00 14.81  ? 84  LEU A CG  1 
ATOM   657  C  CD1 . LEU A 1 84  ? 4.251   8.901   24.396  1.00 16.75  ? 84  LEU A CD1 1 
ATOM   658  C  CD2 . LEU A 1 84  ? 6.243   8.940   25.906  1.00 15.48  ? 84  LEU A CD2 1 
ATOM   659  N  N   . ASP A 1 85  ? 4.609   12.696  28.504  1.00 20.27  ? 85  ASP A N   1 
ATOM   660  C  CA  . ASP A 1 85  ? 4.053   13.942  29.071  1.00 21.01  ? 85  ASP A CA  1 
ATOM   661  C  C   . ASP A 1 85  ? 3.436   14.827  27.995  1.00 22.78  ? 85  ASP A C   1 
ATOM   662  O  O   . ASP A 1 85  ? 2.389   15.448  28.267  1.00 40.60  ? 85  ASP A O   1 
ATOM   663  C  CB  . ASP A 1 85  ? 5.138   14.638  29.862  1.00 26.26  ? 85  ASP A CB  1 
ATOM   664  C  CG  . ASP A 1 85  ? 5.043   14.162  31.312  1.00 37.26  ? 85  ASP A CG  1 
ATOM   665  O  OD1 . ASP A 1 85  ? 3.886   13.872  31.750  1.00 38.09  ? 85  ASP A OD1 1 
ATOM   666  O  OD2 . ASP A 1 85  ? 6.106   14.024  31.987  1.00 45.12  ? 85  ASP A OD2 1 
ATOM   667  N  N   . GLY A 1 86  ? 4.063   14.880  26.824  1.00 27.23  ? 86  GLY A N   1 
ATOM   668  C  CA  . GLY A 1 86  ? 3.522   15.753  25.775  1.00 35.04  ? 86  GLY A CA  1 
ATOM   669  C  C   . GLY A 1 86  ? 2.941   14.986  24.607  1.00 25.85  ? 86  GLY A C   1 
ATOM   670  O  O   . GLY A 1 86  ? 2.156   14.056  24.827  1.00 30.10  ? 86  GLY A O   1 
ATOM   671  N  N   A THR A 1 87  ? 3.121   15.533  23.474  0.50 19.78  ? 87  THR A N   1 
ATOM   672  N  N   B THR A 1 87  ? 3.140   15.532  23.477  0.50 20.02  ? 87  THR A N   1 
ATOM   673  C  CA  A THR A 1 87  ? 2.609   14.951  22.252  0.50 18.15  ? 87  THR A CA  1 
ATOM   674  C  CA  B THR A 1 87  ? 2.641   14.922  22.269  0.50 18.15  ? 87  THR A CA  1 
ATOM   675  C  C   A THR A 1 87  ? 3.825   14.599  21.416  0.50 14.78  ? 87  THR A C   1 
ATOM   676  C  C   B THR A 1 87  ? 3.857   14.590  21.424  0.50 14.93  ? 87  THR A C   1 
ATOM   677  O  O   A THR A 1 87  ? 4.743   15.393  21.303  0.50 15.50  ? 87  THR A O   1 
ATOM   678  O  O   B THR A 1 87  ? 4.798   15.366  21.321  0.50 15.57  ? 87  THR A O   1 
ATOM   679  C  CB  A THR A 1 87  ? 1.780   15.975  21.460  0.50 22.37  ? 87  THR A CB  1 
ATOM   680  C  CB  B THR A 1 87  ? 1.656   15.844  21.531  0.50 23.42  ? 87  THR A CB  1 
ATOM   681  O  OG1 A THR A 1 87  ? 0.624   16.274  22.238  0.50 27.99  ? 87  THR A OG1 1 
ATOM   682  O  OG1 B THR A 1 87  ? 2.299   17.088  21.297  0.50 31.19  ? 87  THR A OG1 1 
ATOM   683  C  CG2 A THR A 1 87  ? 1.317   15.447  20.121  0.50 18.87  ? 87  THR A CG2 1 
ATOM   684  C  CG2 B THR A 1 87  ? 0.408   16.139  22.327  0.50 24.90  ? 87  THR A CG2 1 
ATOM   685  N  N   . TYR A 1 88  ? 3.824   13.392  20.855  1.00 13.07  ? 88  TYR A N   1 
ATOM   686  C  CA  . TYR A 1 88  ? 4.919   12.930  20.032  1.00 12.15  ? 88  TYR A CA  1 
ATOM   687  C  C   . TYR A 1 88  ? 4.416   12.645  18.630  1.00 12.53  ? 88  TYR A C   1 
ATOM   688  O  O   . TYR A 1 88  ? 3.436   11.895  18.450  1.00 17.05  ? 88  TYR A O   1 
ATOM   689  C  CB  . TYR A 1 88  ? 5.552   11.686  20.662  1.00 13.21  ? 88  TYR A CB  1 
ATOM   690  C  CG  . TYR A 1 88  ? 6.343   11.887  21.930  1.00 11.03  ? 88  TYR A CG  1 
ATOM   691  C  CD1 . TYR A 1 88  ? 5.742   12.300  23.116  1.00 13.30  ? 88  TYR A CD1 1 
ATOM   692  C  CD2 . TYR A 1 88  ? 7.726   11.683  21.921  1.00 11.63  ? 88  TYR A CD2 1 
ATOM   693  C  CE1 . TYR A 1 88  ? 6.488   12.464  24.279  1.00 13.43  ? 88  TYR A CE1 1 
ATOM   694  C  CE2 . TYR A 1 88  ? 8.474   11.816  23.069  1.00 12.14  ? 88  TYR A CE2 1 
ATOM   695  C  CZ  . TYR A 1 88  ? 7.849   12.173  24.241  1.00 11.75  ? 88  TYR A CZ  1 
ATOM   696  O  OH  . TYR A 1 88  ? 8.577   12.293  25.382  1.00 13.76  ? 88  TYR A OH  1 
ATOM   697  N  N   . ARG A 1 89  ? 5.081   13.183  17.628  1.00 12.58  ? 89  ARG A N   1 
ATOM   698  C  CA  . ARG A 1 89  ? 4.638   13.058  16.265  1.00 12.33  ? 89  ARG A CA  1 
ATOM   699  C  C   . ARG A 1 89  ? 5.340   11.916  15.532  1.00 9.78   ? 89  ARG A C   1 
ATOM   700  O  O   . ARG A 1 89  ? 6.558   11.771  15.597  1.00 10.71  ? 89  ARG A O   1 
ATOM   701  C  CB  . ARG A 1 89  ? 5.053   14.319  15.494  1.00 16.81  ? 89  ARG A CB  1 
ATOM   702  C  CG  . ARG A 1 89  ? 4.078   15.450  15.483  1.00 26.73  ? 89  ARG A CG  1 
ATOM   703  C  CD  . ARG A 1 89  ? 4.374   16.276  14.234  1.00 24.60  ? 89  ARG A CD  1 
ATOM   704  N  NE  . ARG A 1 89  ? 3.722   17.352  14.876  1.00 23.47  ? 89  ARG A NE  1 
ATOM   705  C  CZ  . ARG A 1 89  ? 3.952   18.634  14.617  1.00 24.21  ? 89  ARG A CZ  1 
ATOM   706  N  NH1 . ARG A 1 89  ? 4.845   18.975  13.703  1.00 22.16  ? 89  ARG A NH1 1 
ATOM   707  N  NH2 . ARG A 1 89  ? 3.290   19.571  15.272  1.00 26.37  ? 89  ARG A NH2 1 
ATOM   708  N  N   . LEU A 1 90  ? 4.562   11.090  14.787  1.00 11.93  ? 90  LEU A N   1 
ATOM   709  C  CA  . LEU A 1 90  ? 5.136   9.988   14.034  1.00 11.29  ? 90  LEU A CA  1 
ATOM   710  C  C   . LEU A 1 90  ? 5.961   10.545  12.870  1.00 11.76  ? 90  LEU A C   1 
ATOM   711  O  O   . LEU A 1 90  ? 5.478   11.365  12.097  1.00 14.13  ? 90  LEU A O   1 
ATOM   712  C  CB  . LEU A 1 90  ? 4.006   9.152   13.428  1.00 12.69  ? 90  LEU A CB  1 
ATOM   713  C  CG  . LEU A 1 90  ? 4.434   7.968   12.544  1.00 12.78  ? 90  LEU A CG  1 
ATOM   714  C  CD1 . LEU A 1 90  ? 5.207   6.903   13.329  1.00 13.78  ? 90  LEU A CD1 1 
ATOM   715  C  CD2 . LEU A 1 90  ? 3.181   7.339   11.933  1.00 15.64  ? 90  LEU A CD2 1 
ATOM   716  N  N   . ILE A 1 91  ? 7.199   10.074  12.725  1.00 11.00  ? 91  ILE A N   1 
ATOM   717  C  CA  . ILE A 1 91  ? 8.023   10.444  11.580  1.00 10.82  ? 91  ILE A CA  1 
ATOM   718  C  C   . ILE A 1 91  ? 8.318   9.238   10.704  1.00 11.04  ? 91  ILE A C   1 
ATOM   719  O  O   . ILE A 1 91  ? 8.317   9.361   9.481   1.00 11.81  ? 91  ILE A O   1 
ATOM   720  C  CB  . ILE A 1 91  ? 9.346   11.186  11.987  1.00 12.06  ? 91  ILE A CB  1 
ATOM   721  C  CG1 . ILE A 1 91  ? 10.261  11.441  10.778  1.00 15.18  ? 91  ILE A CG1 1 
ATOM   722  C  CG2 . ILE A 1 91  ? 10.143  10.426  13.050  1.00 12.01  ? 91  ILE A CG2 1 
ATOM   723  C  CD1 . ILE A 1 91  ? 9.662   12.249  9.636   1.00 17.75  ? 91  ILE A CD1 1 
ATOM   724  N  N   . GLN A 1 92  ? 8.538   8.040   11.288  1.00 10.86  ? 92  GLN A N   1 
ATOM   725  C  CA  . GLN A 1 92  ? 8.821   6.907   10.411  1.00 11.41  ? 92  GLN A CA  1 
ATOM   726  C  C   . GLN A 1 92  ? 8.558   5.605   11.159  1.00 10.31  ? 92  GLN A C   1 
ATOM   727  O  O   . GLN A 1 92  ? 8.530   5.635   12.382  1.00 10.51  ? 92  GLN A O   1 
ATOM   728  C  CB  . GLN A 1 92  ? 10.279  6.924   9.910   1.00 12.76  ? 92  GLN A CB  1 
ATOM   729  C  CG  . GLN A 1 92  ? 11.376  7.007   10.984  1.00 12.64  ? 92  GLN A CG  1 
ATOM   730  C  CD  . GLN A 1 92  ? 12.089  5.677   11.209  1.00 12.37  ? 92  GLN A CD  1 
ATOM   731  O  OE1 . GLN A 1 92  ? 11.455  4.612   11.200  1.00 13.56  ? 92  GLN A OE1 1 
ATOM   732  N  NE2 . GLN A 1 92  ? 13.391  5.737   11.438  1.00 17.27  ? 92  GLN A NE2 1 
ATOM   733  N  N   . PHE A 1 93  ? 8.356   4.509   10.397  1.00 10.29  ? 93  PHE A N   1 
ATOM   734  C  CA  . PHE A 1 93  ? 8.511   3.213   11.019  1.00 9.96   ? 93  PHE A CA  1 
ATOM   735  C  C   . PHE A 1 93  ? 9.490   2.372   10.219  1.00 9.72   ? 93  PHE A C   1 
ATOM   736  O  O   . PHE A 1 93  ? 9.702   2.593   9.037   1.00 11.52  ? 93  PHE A O   1 
ATOM   737  C  CB  . PHE A 1 93  ? 7.140   2.553   11.245  1.00 11.10  ? 93  PHE A CB  1 
ATOM   738  C  CG  . PHE A 1 93  ? 6.418   2.095   9.997   1.00 11.71  ? 93  PHE A CG  1 
ATOM   739  C  CD1 . PHE A 1 93  ? 6.787   0.952   9.305   1.00 13.16  ? 93  PHE A CD1 1 
ATOM   740  C  CD2 . PHE A 1 93  ? 5.311   2.784   9.540   1.00 12.64  ? 93  PHE A CD2 1 
ATOM   741  C  CE1 . PHE A 1 93  ? 6.108   0.537   8.166   1.00 13.50  ? 93  PHE A CE1 1 
ATOM   742  C  CE2 . PHE A 1 93  ? 4.615   2.368   8.419   1.00 12.48  ? 93  PHE A CE2 1 
ATOM   743  C  CZ  . PHE A 1 93  ? 5.030   1.260   7.726   1.00 12.67  ? 93  PHE A CZ  1 
ATOM   744  N  N   . HIS A 1 94  ? 10.042  1.360   10.891  1.00 9.49   ? 94  HIS A N   1 
ATOM   745  C  CA  . HIS A 1 94  ? 10.986  0.441   10.243  1.00 9.41   ? 94  HIS A CA  1 
ATOM   746  C  C   . HIS A 1 94  ? 10.935  -0.859  11.014  1.00 8.94   ? 94  HIS A C   1 
ATOM   747  O  O   . HIS A 1 94  ? 10.263  -0.973  12.034  1.00 9.65   ? 94  HIS A O   1 
ATOM   748  C  CB  . HIS A 1 94  ? 12.415  1.034   10.224  1.00 10.31  ? 94  HIS A CB  1 
ATOM   749  C  CG  . HIS A 1 94  ? 12.916  1.266   11.619  1.00 9.24   ? 94  HIS A CG  1 
ATOM   750  N  ND1 . HIS A 1 94  ? 12.707  2.431   12.324  1.00 9.59   ? 94  HIS A ND1 1 
ATOM   751  C  CD2 . HIS A 1 94  ? 13.569  0.433   12.462  1.00 9.26   ? 94  HIS A CD2 1 
ATOM   752  C  CE1 . HIS A 1 94  ? 13.227  2.311   13.536  1.00 9.34   ? 94  HIS A CE1 1 
ATOM   753  N  NE2 . HIS A 1 94  ? 13.780  1.062   13.659  1.00 9.32   ? 94  HIS A NE2 1 
ATOM   754  N  N   . PHE A 1 95  ? 11.688  -1.874  10.557  1.00 9.74   ? 95  PHE A N   1 
ATOM   755  C  CA  . PHE A 1 95  ? 11.682  -3.182  11.173  1.00 9.47   ? 95  PHE A CA  1 
ATOM   756  C  C   . PHE A 1 95  ? 13.096  -3.672  11.401  1.00 9.12   ? 95  PHE A C   1 
ATOM   757  O  O   . PHE A 1 95  ? 14.054  -3.231  10.782  1.00 11.21  ? 95  PHE A O   1 
ATOM   758  C  CB  . PHE A 1 95  ? 10.965  -4.198  10.279  1.00 11.39  ? 95  PHE A CB  1 
ATOM   759  C  CG  . PHE A 1 95  ? 9.506   -3.934  9.992   1.00 11.12  ? 95  PHE A CG  1 
ATOM   760  C  CD1 . PHE A 1 95  ? 9.154   -3.023  9.011   1.00 12.12  ? 95  PHE A CD1 1 
ATOM   761  C  CD2 . PHE A 1 95  ? 8.476   -4.575  10.684  1.00 11.81  ? 95  PHE A CD2 1 
ATOM   762  C  CE1 . PHE A 1 95  ? 7.815   -2.802  8.700   1.00 13.11  ? 95  PHE A CE1 1 
ATOM   763  C  CE2 . PHE A 1 95  ? 7.155   -4.383  10.350  1.00 12.35  ? 95  PHE A CE2 1 
ATOM   764  C  CZ  . PHE A 1 95  ? 6.834   -3.469  9.377   1.00 13.09  ? 95  PHE A CZ  1 
ATOM   765  N  N   . HIS A 1 96  ? 13.203  -4.631  12.327  1.00 9.17   ? 96  HIS A N   1 
ATOM   766  C  CA  . HIS A 1 96  ? 14.380  -5.460  12.540  1.00 8.95   ? 96  HIS A CA  1 
ATOM   767  C  C   . HIS A 1 96  ? 13.929  -6.906  12.385  1.00 9.28   ? 96  HIS A C   1 
ATOM   768  O  O   . HIS A 1 96  ? 12.844  -7.241  12.861  1.00 10.21  ? 96  HIS A O   1 
ATOM   769  C  CB  . HIS A 1 96  ? 15.033  -5.219  13.908  1.00 9.64   ? 96  HIS A CB  1 
ATOM   770  C  CG  . HIS A 1 96  ? 15.344  -3.781  14.145  1.00 8.78   ? 96  HIS A CG  1 
ATOM   771  N  ND1 . HIS A 1 96  ? 16.572  -3.220  13.943  1.00 10.06  ? 96  HIS A ND1 1 
ATOM   772  C  CD2 . HIS A 1 96  ? 14.523  -2.779  14.579  1.00 9.77   ? 96  HIS A CD2 1 
ATOM   773  C  CE1 . HIS A 1 96  ? 16.519  -1.913  14.252  1.00 10.71  ? 96  HIS A CE1 1 
ATOM   774  N  NE2 . HIS A 1 96  ? 15.271  -1.608  14.625  1.00 9.30   ? 96  HIS A NE2 1 
ATOM   775  N  N   . TRP A 1 97  ? 14.722  -7.762  11.724  1.00 9.66   ? 97  TRP A N   1 
ATOM   776  C  CA  . TRP A 1 97  ? 14.295  -9.139  11.541  1.00 9.57   ? 97  TRP A CA  1 
ATOM   777  C  C   . TRP A 1 97  ? 15.495  -10.060 11.426  1.00 9.72   ? 97  TRP A C   1 
ATOM   778  O  O   . TRP A 1 97  ? 16.658  -9.642  11.353  1.00 10.99  ? 97  TRP A O   1 
ATOM   779  C  CB  . TRP A 1 97  ? 13.376  -9.253  10.307  1.00 10.66  ? 97  TRP A CB  1 
ATOM   780  C  CG  . TRP A 1 97  ? 14.092  -8.871  9.036   1.00 10.17  ? 97  TRP A CG  1 
ATOM   781  C  CD1 . TRP A 1 97  ? 14.797  -9.709  8.213   1.00 11.62  ? 97  TRP A CD1 1 
ATOM   782  C  CD2 . TRP A 1 97  ? 14.142  -7.568  8.435   1.00 9.82   ? 97  TRP A CD2 1 
ATOM   783  N  NE1 . TRP A 1 97  ? 15.294  -8.998  7.135   1.00 12.09  ? 97  TRP A NE1 1 
ATOM   784  C  CE2 . TRP A 1 97  ? 14.935  -7.672  7.262   1.00 11.83  ? 97  TRP A CE2 1 
ATOM   785  C  CE3 . TRP A 1 97  ? 13.645  -6.297  8.780   1.00 11.01  ? 97  TRP A CE3 1 
ATOM   786  C  CZ2 . TRP A 1 97  ? 15.123  -6.593  6.378   1.00 12.15  ? 97  TRP A CZ2 1 
ATOM   787  C  CZ3 . TRP A 1 97  ? 13.871  -5.212  7.978   1.00 12.08  ? 97  TRP A CZ3 1 
ATOM   788  C  CH2 . TRP A 1 97  ? 14.629  -5.362  6.805   1.00 12.77  ? 97  TRP A CH2 1 
ATOM   789  N  N   . GLY A 1 98  ? 15.199  -11.369 11.427  1.00 10.48  ? 98  GLY A N   1 
ATOM   790  C  CA  . GLY A 1 98  ? 16.230  -12.370 11.511  1.00 11.58  ? 98  GLY A CA  1 
ATOM   791  C  C   . GLY A 1 98  ? 16.441  -13.095 10.183  1.00 11.75  ? 98  GLY A C   1 
ATOM   792  O  O   . GLY A 1 98  ? 15.731  -12.913 9.186   1.00 13.74  ? 98  GLY A O   1 
ATOM   793  N  N   . SER A 1 99  ? 17.414  -13.995 10.190  1.00 13.60  ? 99  SER A N   1 
ATOM   794  C  CA  . SER A 1 99  ? 17.630  -14.899 9.063   1.00 15.85  ? 99  SER A CA  1 
ATOM   795  C  C   . SER A 1 99  ? 16.753  -16.138 9.181   1.00 15.55  ? 99  SER A C   1 
ATOM   796  O  O   . SER A 1 99  ? 16.641  -16.883 8.211   1.00 20.54  ? 99  SER A O   1 
ATOM   797  C  CB  . SER A 1 99  ? 19.088  -15.211 8.982   1.00 18.18  ? 99  SER A CB  1 
ATOM   798  O  OG  . SER A 1 99  ? 19.529  -15.773 10.239  1.00 17.29  ? 99  SER A OG  1 
ATOM   799  N  N   . LEU A 1 100 ? 16.142  -16.358 10.364  1.00 14.79  ? 100 LEU A N   1 
ATOM   800  C  CA  . LEU A 1 100 ? 15.300  -17.508 10.665  1.00 16.74  ? 100 LEU A CA  1 
ATOM   801  C  C   . LEU A 1 100 ? 14.145  -16.998 11.494  1.00 16.65  ? 100 LEU A C   1 
ATOM   802  O  O   . LEU A 1 100 ? 14.294  -16.011 12.193  1.00 15.65  ? 100 LEU A O   1 
ATOM   803  C  CB  . LEU A 1 100 ? 16.088  -18.472 11.564  1.00 19.91  ? 100 LEU A CB  1 
ATOM   804  C  CG  . LEU A 1 100 ? 17.430  -18.923 11.023  1.00 20.97  ? 100 LEU A CG  1 
ATOM   805  C  CD1 . LEU A 1 100 ? 18.281  -19.550 12.125  1.00 31.75  ? 100 LEU A CD1 1 
ATOM   806  C  CD2 . LEU A 1 100 ? 17.209  -19.935 9.895   1.00 26.98  ? 100 LEU A CD2 1 
ATOM   807  N  N   . ASP A 1 101 ? 13.034  -17.723 11.542  1.00 16.08  ? 101 ASP A N   1 
ATOM   808  C  CA  . ASP A 1 101 ? 11.836  -17.238 12.203  1.00 16.11  ? 101 ASP A CA  1 
ATOM   809  C  C   . ASP A 1 101 ? 12.073  -17.150 13.725  1.00 15.28  ? 101 ASP A C   1 
ATOM   810  O  O   . ASP A 1 101 ? 11.366  -16.453 14.412  1.00 22.11  ? 101 ASP A O   1 
ATOM   811  C  CB  . ASP A 1 101 ? 10.617  -18.106 11.869  1.00 17.87  ? 101 ASP A CB  1 
ATOM   812  C  CG  . ASP A 1 101 ? 10.136  -18.099 10.422  1.00 21.62  ? 101 ASP A CG  1 
ATOM   813  O  OD1 . ASP A 1 101 ? 10.548  -17.248 9.623   1.00 19.78  ? 101 ASP A OD1 1 
ATOM   814  O  OD2 . ASP A 1 101 ? 9.301   -18.932 10.113  1.00 25.04  ? 101 ASP A OD2 1 
ATOM   815  N  N   . GLY A 1 102 ? 13.032  -17.902 14.264  1.00 17.88  ? 102 GLY A N   1 
ATOM   816  C  CA  . GLY A 1 102 ? 13.331  -17.923 15.687  1.00 20.50  ? 102 GLY A CA  1 
ATOM   817  C  C   . GLY A 1 102 ? 14.195  -16.781 16.255  1.00 19.32  ? 102 GLY A C   1 
ATOM   818  O  O   . GLY A 1 102 ? 14.557  -16.795 17.424  1.00 18.08  ? 102 GLY A O   1 
ATOM   819  N  N   A GLN A 1 103 ? 14.480  -15.765 15.439  0.50 14.44  ? 103 GLN A N   1 
ATOM   820  N  N   B GLN A 1 103 ? 14.529  -15.768 15.458  0.50 15.94  ? 103 GLN A N   1 
ATOM   821  C  CA  A GLN A 1 103 ? 15.259  -14.620 15.882  0.50 12.86  ? 103 GLN A CA  1 
ATOM   822  C  CA  B GLN A 1 103 ? 15.290  -14.634 15.965  0.50 13.60  ? 103 GLN A CA  1 
ATOM   823  C  C   A GLN A 1 103 ? 14.853  -13.417 15.049  0.50 11.16  ? 103 GLN A C   1 
ATOM   824  C  C   B GLN A 1 103 ? 14.985  -13.462 15.047  0.50 11.34  ? 103 GLN A C   1 
ATOM   825  O  O   A GLN A 1 103 ? 14.232  -13.562 13.990  0.50 12.09  ? 103 GLN A O   1 
ATOM   826  O  O   B GLN A 1 103 ? 14.545  -13.687 13.920  0.50 12.34  ? 103 GLN A O   1 
ATOM   827  C  CB  A GLN A 1 103 ? 16.770  -14.864 15.832  0.50 13.29  ? 103 GLN A CB  1 
ATOM   828  C  CB  B GLN A 1 103 ? 16.790  -14.933 16.037  0.50 14.75  ? 103 GLN A CB  1 
ATOM   829  C  CG  A GLN A 1 103 ? 17.297  -15.052 14.415  0.50 14.37  ? 103 GLN A CG  1 
ATOM   830  C  CG  B GLN A 1 103 ? 17.388  -15.199 14.658  0.50 16.34  ? 103 GLN A CG  1 
ATOM   831  C  CD  A GLN A 1 103 ? 18.556  -15.884 14.443  0.50 15.22  ? 103 GLN A CD  1 
ATOM   832  C  CD  B GLN A 1 103 ? 18.864  -15.518 14.727  0.50 20.54  ? 103 GLN A CD  1 
ATOM   833  O  OE1 A GLN A 1 103 ? 18.555  -16.986 14.985  0.50 14.34  ? 103 GLN A OE1 1 
ATOM   834  O  OE1 B GLN A 1 103 ? 19.312  -16.165 15.679  0.50 21.79  ? 103 GLN A OE1 1 
ATOM   835  N  NE2 A GLN A 1 103 ? 19.661  -15.327 13.962  0.50 14.83  ? 103 GLN A NE2 1 
ATOM   836  N  NE2 B GLN A 1 103 ? 19.617  -15.058 13.732  0.50 20.09  ? 103 GLN A NE2 1 
ATOM   837  N  N   . GLY A 1 104 ? 15.267  -12.232 15.520  1.00 10.49  ? 104 GLY A N   1 
ATOM   838  C  CA  . GLY A 1 104 ? 15.024  -11.051 14.723  1.00 11.05  ? 104 GLY A CA  1 
ATOM   839  C  C   . GLY A 1 104 ? 14.570  -9.883  15.578  1.00 9.78   ? 104 GLY A C   1 
ATOM   840  O  O   . GLY A 1 104 ? 14.848  -8.746  15.188  1.00 10.69  ? 104 GLY A O   1 
ATOM   841  N  N   . SER A 1 105 ? 13.840  -10.145 16.675  1.00 9.65   ? 105 SER A N   1 
ATOM   842  C  CA  . SER A 1 105 ? 13.455  -9.016  17.502  1.00 10.01  ? 105 SER A CA  1 
ATOM   843  C  C   . SER A 1 105 ? 14.644  -8.461  18.279  1.00 9.31   ? 105 SER A C   1 
ATOM   844  O  O   . SER A 1 105 ? 15.669  -9.131  18.463  1.00 11.11  ? 105 SER A O   1 
ATOM   845  C  CB  . SER A 1 105 ? 12.310  -9.355  18.420  1.00 9.84   ? 105 SER A CB  1 
ATOM   846  O  OG  . SER A 1 105 ? 12.673  -10.339 19.396  1.00 10.61  ? 105 SER A OG  1 
ATOM   847  N  N   . GLU A 1 106 ? 14.519  -7.198  18.668  1.00 9.86   ? 106 GLU A N   1 
ATOM   848  C  CA  . GLU A 1 106 ? 15.544  -6.523  19.473  1.00 10.22  ? 106 GLU A CA  1 
ATOM   849  C  C   . GLU A 1 106 ? 15.236  -6.747  20.951  1.00 9.57   ? 106 GLU A C   1 
ATOM   850  O  O   . GLU A 1 106 ? 16.021  -7.304  21.726  1.00 10.68  ? 106 GLU A O   1 
ATOM   851  C  CB  . GLU A 1 106 ? 15.637  -5.060  19.074  1.00 10.56  ? 106 GLU A CB  1 
ATOM   852  C  CG  . GLU A 1 106 ? 16.024  -4.909  17.619  1.00 11.92  ? 106 GLU A CG  1 
ATOM   853  C  CD  . GLU A 1 106 ? 16.792  -3.678  17.360  1.00 10.70  ? 106 GLU A CD  1 
ATOM   854  O  OE1 . GLU A 1 106 ? 16.230  -2.596  17.601  1.00 11.43  ? 106 GLU A OE1 1 
ATOM   855  O  OE2 . GLU A 1 106 ? 17.920  -3.761  16.912  1.00 12.66  ? 106 GLU A OE2 1 
ATOM   856  N  N   . HIS A 1 107 ? 14.063  -6.289  21.373  1.00 9.08   ? 107 HIS A N   1 
ATOM   857  C  CA  . HIS A 1 107 ? 13.602  -6.660  22.700  1.00 9.15   ? 107 HIS A CA  1 
ATOM   858  C  C   . HIS A 1 107 ? 13.288  -8.149  22.727  1.00 9.25   ? 107 HIS A C   1 
ATOM   859  O  O   . HIS A 1 107 ? 12.958  -8.742  21.696  1.00 10.09  ? 107 HIS A O   1 
ATOM   860  C  CB  . HIS A 1 107 ? 12.359  -5.840  23.070  1.00 9.19   ? 107 HIS A CB  1 
ATOM   861  C  CG  . HIS A 1 107 ? 12.690  -4.392  23.252  1.00 8.38   ? 107 HIS A CG  1 
ATOM   862  N  ND1 . HIS A 1 107 ? 12.630  -3.493  22.202  1.00 9.98   ? 107 HIS A ND1 1 
ATOM   863  C  CD2 . HIS A 1 107 ? 13.131  -3.699  24.322  1.00 9.27   ? 107 HIS A CD2 1 
ATOM   864  C  CE1 . HIS A 1 107 ? 13.046  -2.299  22.669  1.00 10.33  ? 107 HIS A CE1 1 
ATOM   865  N  NE2 . HIS A 1 107 ? 13.353  -2.394  23.961  1.00 10.52  ? 107 HIS A NE2 1 
ATOM   866  N  N   . THR A 1 108 ? 13.354  -8.729  23.930  1.00 10.80  ? 108 THR A N   1 
ATOM   867  C  CA  . THR A 1 108 ? 12.944  -10.105 24.153  1.00 11.28  ? 108 THR A CA  1 
ATOM   868  C  C   . THR A 1 108 ? 12.004  -10.096 25.349  1.00 10.74  ? 108 THR A C   1 
ATOM   869  O  O   . THR A 1 108 ? 12.004  -9.134  26.123  1.00 11.54  ? 108 THR A O   1 
ATOM   870  C  CB  . THR A 1 108 ? 14.164  -11.037 24.351  1.00 12.36  ? 108 THR A CB  1 
ATOM   871  O  OG1 . THR A 1 108 ? 14.980  -10.562 25.420  1.00 12.93  ? 108 THR A OG1 1 
ATOM   872  C  CG2 . THR A 1 108 ? 15.031  -11.119 23.094  1.00 13.38  ? 108 THR A CG2 1 
ATOM   873  N  N   . VAL A 1 109 ? 11.216  -11.160 25.491  1.00 11.52  ? 109 VAL A N   1 
ATOM   874  C  CA  . VAL A 1 109 ? 10.255  -11.219 26.590  1.00 12.33  ? 109 VAL A CA  1 
ATOM   875  C  C   . VAL A 1 109 ? 10.557  -12.502 27.350  1.00 12.48  ? 109 VAL A C   1 
ATOM   876  O  O   . VAL A 1 109 ? 10.370  -13.589 26.784  1.00 13.18  ? 109 VAL A O   1 
ATOM   877  C  CB  . VAL A 1 109 ? 8.811   -11.205 26.045  1.00 13.62  ? 109 VAL A CB  1 
ATOM   878  C  CG1 . VAL A 1 109 ? 7.800   -11.324 27.189  1.00 15.35  ? 109 VAL A CG1 1 
ATOM   879  C  CG2 . VAL A 1 109 ? 8.526   -9.941  25.248  1.00 14.94  ? 109 VAL A CG2 1 
ATOM   880  N  N   . ASP A 1 110 ? 11.070  -12.398 28.577  1.00 14.24  ? 110 ASP A N   1 
ATOM   881  C  CA  . ASP A 1 110 ? 11.497  -13.616 29.276  1.00 14.94  ? 110 ASP A CA  1 
ATOM   882  C  C   . ASP A 1 110 ? 12.416  -14.440 28.393  1.00 13.99  ? 110 ASP A C   1 
ATOM   883  O  O   . ASP A 1 110 ? 12.328  -15.678 28.336  1.00 15.88  ? 110 ASP A O   1 
ATOM   884  C  CB  . ASP A 1 110 ? 10.310  -14.426 29.808  1.00 17.99  ? 110 ASP A CB  1 
ATOM   885  C  CG  . ASP A 1 110 ? 9.453   -13.630 30.777  1.00 17.76  ? 110 ASP A CG  1 
ATOM   886  O  OD1 . ASP A 1 110 ? 10.067  -12.845 31.488  1.00 20.18  ? 110 ASP A OD1 1 
ATOM   887  O  OD2 . ASP A 1 110 ? 8.205   -13.810 30.791  1.00 23.71  ? 110 ASP A OD2 1 
ATOM   888  N  N   . LYS A 1 111 ? 13.325  -13.738 27.682  1.00 13.60  ? 111 LYS A N   1 
ATOM   889  C  CA  . LYS A 1 111 ? 14.376  -14.276 26.812  1.00 14.64  ? 111 LYS A CA  1 
ATOM   890  C  C   . LYS A 1 111 ? 13.822  -14.798 25.476  1.00 14.16  ? 111 LYS A C   1 
ATOM   891  O  O   . LYS A 1 111 ? 14.606  -15.148 24.603  1.00 14.76  ? 111 LYS A O   1 
ATOM   892  C  CB  . LYS A 1 111 ? 15.272  -15.368 27.448  1.00 17.24  ? 111 LYS A CB  1 
ATOM   893  C  CG  . LYS A 1 111 ? 15.917  -14.938 28.754  1.00 20.84  ? 111 LYS A CG  1 
ATOM   894  C  CD  . LYS A 1 111 ? 16.873  -13.812 28.500  1.00 23.69  ? 111 LYS A CD  1 
ATOM   895  C  CE  . LYS A 1 111 ? 17.576  -13.415 29.771  1.00 38.03  ? 111 LYS A CE  1 
ATOM   896  N  NZ  . LYS A 1 111 ? 19.001  -13.300 29.438  1.00 42.42  ? 111 LYS A NZ  1 
ATOM   897  N  N   . LYS A 1 112 ? 12.513  -14.792 25.271  1.00 13.21  ? 112 LYS A N   1 
ATOM   898  C  CA  . LYS A 1 112 ? 11.939  -15.145 23.974  1.00 14.08  ? 112 LYS A CA  1 
ATOM   899  C  C   . LYS A 1 112 ? 12.259  -14.112 22.910  1.00 12.06  ? 112 LYS A C   1 
ATOM   900  O  O   . LYS A 1 112 ? 11.999  -12.919 23.094  1.00 12.74  ? 112 LYS A O   1 
ATOM   901  C  CB  . LYS A 1 112 ? 10.421  -15.242 24.050  1.00 15.55  ? 112 LYS A CB  1 
ATOM   902  C  CG  . LYS A 1 112 ? 9.814   -15.800 22.760  1.00 17.18  ? 112 LYS A CG  1 
ATOM   903  C  CD  . LYS A 1 112 ? 8.268   -15.821 22.788  1.00 23.92  ? 112 LYS A CD  1 
ATOM   904  C  CE  . LYS A 1 112 ? 7.723   -15.974 21.390  1.00 24.91  ? 112 LYS A CE  1 
ATOM   905  N  NZ  . LYS A 1 112 ? 8.087   -17.273 20.788  1.00 29.85  ? 112 LYS A NZ  1 
ATOM   906  N  N   A LYS A 1 113 ? 12.745  -14.613 21.765  0.50 13.11  ? 113 LYS A N   1 
ATOM   907  N  N   B LYS A 1 113 ? 12.783  -14.584 21.763  0.50 12.76  ? 113 LYS A N   1 
ATOM   908  C  CA  A LYS A 1 113 ? 12.972  -13.801 20.588  0.50 13.09  ? 113 LYS A CA  1 
ATOM   909  C  CA  B LYS A 1 113 ? 13.025  -13.751 20.597  0.50 12.64  ? 113 LYS A CA  1 
ATOM   910  C  C   A LYS A 1 113 ? 11.800  -14.015 19.642  0.50 11.99  ? 113 LYS A C   1 
ATOM   911  C  C   B LYS A 1 113 ? 11.903  -14.003 19.593  0.50 12.10  ? 113 LYS A C   1 
ATOM   912  O  O   A LYS A 1 113 ? 11.342  -15.139 19.421  0.50 16.33  ? 113 LYS A O   1 
ATOM   913  O  O   B LYS A 1 113 ? 11.565  -15.148 19.287  0.50 16.82  ? 113 LYS A O   1 
ATOM   914  C  CB  A LYS A 1 113 ? 14.255  -14.240 19.870  0.50 13.58  ? 113 LYS A CB  1 
ATOM   915  C  CB  B LYS A 1 113 ? 14.365  -14.110 19.933  0.50 14.67  ? 113 LYS A CB  1 
ATOM   916  C  CG  A LYS A 1 113 ? 15.547  -13.949 20.623  0.50 14.31  ? 113 LYS A CG  1 
ATOM   917  C  CG  B LYS A 1 113 ? 15.607  -13.892 20.793  0.50 15.75  ? 113 LYS A CG  1 
ATOM   918  C  CD  A LYS A 1 113 ? 16.786  -14.522 19.935  0.50 15.69  ? 113 LYS A CD  1 
ATOM   919  C  CD  B LYS A 1 113 ? 16.906  -14.461 20.198  0.50 17.35  ? 113 LYS A CD  1 
ATOM   920  C  CE  A LYS A 1 113 ? 18.090  -14.089 20.576  0.50 18.17  ? 113 LYS A CE  1 
ATOM   921  C  CE  B LYS A 1 113 ? 18.159  -13.848 20.803  0.50 20.22  ? 113 LYS A CE  1 
ATOM   922  N  NZ  A LYS A 1 113 ? 18.392  -14.860 21.806  0.50 19.74  ? 113 LYS A NZ  1 
ATOM   923  N  NZ  B LYS A 1 113 ? 19.361  -14.699 20.613  0.50 21.93  ? 113 LYS A NZ  1 
ATOM   924  N  N   . TYR A 1 114 ? 11.347  -12.923 19.040  1.00 11.27  ? 114 TYR A N   1 
ATOM   925  C  CA  . TYR A 1 114 ? 10.342  -12.977 17.988  1.00 10.74  ? 114 TYR A CA  1 
ATOM   926  C  C   . TYR A 1 114 ? 11.014  -12.913 16.617  1.00 10.63  ? 114 TYR A C   1 
ATOM   927  O  O   . TYR A 1 114 ? 12.218  -12.631 16.509  1.00 11.43  ? 114 TYR A O   1 
ATOM   928  C  CB  . TYR A 1 114 ? 9.309   -11.863 18.168  1.00 11.51  ? 114 TYR A CB  1 
ATOM   929  C  CG  . TYR A 1 114 ? 8.382   -12.131 19.326  1.00 11.52  ? 114 TYR A CG  1 
ATOM   930  C  CD1 . TYR A 1 114 ? 8.675   -11.718 20.620  1.00 13.85  ? 114 TYR A CD1 1 
ATOM   931  C  CD2 . TYR A 1 114 ? 7.184   -12.750 19.112  1.00 13.70  ? 114 TYR A CD2 1 
ATOM   932  C  CE1 . TYR A 1 114 ? 7.785   -11.944 21.666  1.00 16.40  ? 114 TYR A CE1 1 
ATOM   933  C  CE2 . TYR A 1 114 ? 6.286   -13.030 20.129  1.00 16.67  ? 114 TYR A CE2 1 
ATOM   934  C  CZ  . TYR A 1 114 ? 6.583   -12.599 21.416  1.00 18.62  ? 114 TYR A CZ  1 
ATOM   935  O  OH  . TYR A 1 114 ? 5.721   -12.835 22.443  1.00 24.91  ? 114 TYR A OH  1 
ATOM   936  N  N   . ALA A 1 115 ? 10.269  -13.177 15.542  1.00 11.23  ? 115 ALA A N   1 
ATOM   937  C  CA  . ALA A 1 115 ? 10.841  -13.211 14.200  1.00 11.05  ? 115 ALA A CA  1 
ATOM   938  C  C   . ALA A 1 115 ? 11.238  -11.812 13.753  1.00 11.77  ? 115 ALA A C   1 
ATOM   939  O  O   . ALA A 1 115 ? 12.080  -11.654 12.851  1.00 11.37  ? 115 ALA A O   1 
ATOM   940  C  CB  . ALA A 1 115 ? 9.797   -13.803 13.277  1.00 14.94  ? 115 ALA A CB  1 
ATOM   941  N  N   . ALA A 1 116 ? 10.580  -10.754 14.281  1.00 10.51  ? 116 ALA A N   1 
ATOM   942  C  CA  . ALA A 1 116 ? 10.903  -9.402  13.816  1.00 9.76   ? 116 ALA A CA  1 
ATOM   943  C  C   . ALA A 1 116 ? 10.331  -8.458  14.865  1.00 9.25   ? 116 ALA A C   1 
ATOM   944  O  O   . ALA A 1 116 ? 9.573   -8.848  15.760  1.00 9.86   ? 116 ALA A O   1 
ATOM   945  C  CB  . ALA A 1 116 ? 10.339  -9.128  12.421  1.00 11.04  ? 116 ALA A CB  1 
ATOM   946  N  N   . GLU A 1 117 ? 10.661  -7.197  14.719  1.00 9.58   ? 117 GLU A N   1 
ATOM   947  C  CA  . GLU A 1 117 ? 10.138  -6.139  15.571  1.00 9.35   ? 117 GLU A CA  1 
ATOM   948  C  C   . GLU A 1 117 ? 9.922   -4.905  14.719  1.00 8.94   ? 117 GLU A C   1 
ATOM   949  O  O   . GLU A 1 117 ? 10.812  -4.496  13.979  1.00 11.12  ? 117 GLU A O   1 
ATOM   950  C  CB  . GLU A 1 117 ? 11.081  -5.887  16.744  1.00 10.42  ? 117 GLU A CB  1 
ATOM   951  C  CG  . GLU A 1 117 ? 10.569  -4.925  17.801  1.00 10.71  ? 117 GLU A CG  1 
ATOM   952  C  CD  . GLU A 1 117 ? 11.485  -4.888  19.036  1.00 10.79  ? 117 GLU A CD  1 
ATOM   953  O  OE1 . GLU A 1 117 ? 12.093  -5.935  19.384  1.00 11.47  ? 117 GLU A OE1 1 
ATOM   954  O  OE2 . GLU A 1 117 ? 11.552  -3.833  19.708  1.00 11.65  ? 117 GLU A OE2 1 
ATOM   955  N  N   . LEU A 1 118 ? 8.760   -4.302  14.880  1.00 9.24   ? 118 LEU A N   1 
ATOM   956  C  CA  . LEU A 1 118 ? 8.376   -3.068  14.226  1.00 8.89   ? 118 LEU A CA  1 
ATOM   957  C  C   . LEU A 1 118 ? 8.591   -1.925  15.214  1.00 8.88   ? 118 LEU A C   1 
ATOM   958  O  O   . LEU A 1 118 ? 8.176   -1.989  16.382  1.00 9.12   ? 118 LEU A O   1 
ATOM   959  C  CB  . LEU A 1 118 ? 6.891   -3.176  13.865  1.00 10.12  ? 118 LEU A CB  1 
ATOM   960  C  CG  . LEU A 1 118 ? 6.153   -1.878  13.530  1.00 10.83  ? 118 LEU A CG  1 
ATOM   961  C  CD1 . LEU A 1 118 ? 6.720   -1.148  12.341  1.00 12.52  ? 118 LEU A CD1 1 
ATOM   962  C  CD2 . LEU A 1 118 ? 4.694   -2.225  13.281  1.00 12.37  ? 118 LEU A CD2 1 
ATOM   963  N  N   . HIS A 1 119 ? 9.259   -0.841  14.721  1.00 8.47   ? 119 HIS A N   1 
ATOM   964  C  CA  . HIS A 1 119 ? 9.485   0.352   15.537  1.00 8.40   ? 119 HIS A CA  1 
ATOM   965  C  C   . HIS A 1 119 ? 8.811   1.519   14.849  1.00 8.26   ? 119 HIS A C   1 
ATOM   966  O  O   . HIS A 1 119 ? 9.189   1.850   13.708  1.00 9.80   ? 119 HIS A O   1 
ATOM   967  C  CB  . HIS A 1 119 ? 10.998  0.618   15.601  1.00 8.62   ? 119 HIS A CB  1 
ATOM   968  C  CG  . HIS A 1 119 ? 11.662  -0.374  16.490  1.00 8.30   ? 119 HIS A CG  1 
ATOM   969  N  ND1 . HIS A 1 119 ? 13.050  -0.568  16.487  1.00 9.11   ? 119 HIS A ND1 1 
ATOM   970  C  CD2 . HIS A 1 119 ? 11.139  -1.205  17.446  1.00 8.85   ? 119 HIS A CD2 1 
ATOM   971  C  CE1 . HIS A 1 119 ? 13.338  -1.449  17.393  1.00 8.66   ? 119 HIS A CE1 1 
ATOM   972  N  NE2 . HIS A 1 119 ? 12.204  -1.865  18.020  1.00 8.96   ? 119 HIS A NE2 1 
ATOM   973  N  N   . LEU A 1 120 ? 7.857   2.151   15.555  1.00 8.53   ? 120 LEU A N   1 
ATOM   974  C  CA  . LEU A 1 120 ? 7.214   3.380   15.097  1.00 9.00   ? 120 LEU A CA  1 
ATOM   975  C  C   . LEU A 1 120 ? 7.850   4.528   15.875  1.00 8.83   ? 120 LEU A C   1 
ATOM   976  O  O   . LEU A 1 120 ? 7.711   4.569   17.105  1.00 9.12   ? 120 LEU A O   1 
ATOM   977  C  CB  . LEU A 1 120 ? 5.699   3.284   15.288  1.00 10.00  ? 120 LEU A CB  1 
ATOM   978  C  CG  . LEU A 1 120 ? 5.017   2.222   14.434  1.00 11.15  ? 120 LEU A CG  1 
ATOM   979  C  CD1 . LEU A 1 120 ? 4.284   1.222   15.342  1.00 15.70  ? 120 LEU A CD1 1 
ATOM   980  C  CD2 . LEU A 1 120 ? 4.060   2.890   13.449  1.00 14.65  ? 120 LEU A CD2 1 
ATOM   981  N  N   . VAL A 1 121 ? 8.556   5.402   15.150  1.00 9.43   ? 121 VAL A N   1 
ATOM   982  C  CA  . VAL A 1 121 ? 9.401   6.400   15.817  1.00 9.21   ? 121 VAL A CA  1 
ATOM   983  C  C   . VAL A 1 121 ? 8.650   7.736   15.822  1.00 8.95   ? 121 VAL A C   1 
ATOM   984  O  O   . VAL A 1 121 ? 8.218   8.211   14.783  1.00 9.93   ? 121 VAL A O   1 
ATOM   985  C  CB  . VAL A 1 121 ? 10.735  6.541   15.052  1.00 9.23   ? 121 VAL A CB  1 
ATOM   986  C  CG1 . VAL A 1 121 ? 11.646  7.573   15.681  1.00 10.89  ? 121 VAL A CG1 1 
ATOM   987  C  CG2 . VAL A 1 121 ? 11.438  5.184   14.913  1.00 10.98  ? 121 VAL A CG2 1 
ATOM   988  N  N   . HIS A 1 122 ? 8.567   8.345   17.015  1.00 8.91   ? 122 HIS A N   1 
ATOM   989  C  CA  . HIS A 1 122 ? 7.872   9.613   17.215  1.00 9.15   ? 122 HIS A CA  1 
ATOM   990  C  C   . HIS A 1 122 ? 8.763   10.594  17.963  1.00 8.76   ? 122 HIS A C   1 
ATOM   991  O  O   . HIS A 1 122 ? 9.571   10.182  18.821  1.00 10.55  ? 122 HIS A O   1 
ATOM   992  C  CB  . HIS A 1 122 ? 6.614   9.401   18.093  1.00 10.40  ? 122 HIS A CB  1 
ATOM   993  C  CG  . HIS A 1 122 ? 5.724   8.272   17.691  1.00 9.96   ? 122 HIS A CG  1 
ATOM   994  N  ND1 . HIS A 1 122 ? 6.047   6.953   17.901  1.00 10.71  ? 122 HIS A ND1 1 
ATOM   995  C  CD2 . HIS A 1 122 ? 4.520   8.237   17.083  1.00 11.49  ? 122 HIS A CD2 1 
ATOM   996  C  CE1 . HIS A 1 122 ? 5.063   6.182   17.476  1.00 11.74  ? 122 HIS A CE1 1 
ATOM   997  N  NE2 . HIS A 1 122 ? 4.111   6.926   16.939  1.00 11.97  ? 122 HIS A NE2 1 
ATOM   998  N  N   . TRP A 1 123 ? 8.600   11.891  17.657  1.00 9.74   ? 123 TRP A N   1 
ATOM   999  C  CA  . TRP A 1 123 ? 9.434   12.892  18.341  1.00 9.84   ? 123 TRP A CA  1 
ATOM   1000 C  C   . TRP A 1 123 ? 8.578   13.876  19.115  1.00 9.90   ? 123 TRP A C   1 
ATOM   1001 O  O   . TRP A 1 123 ? 7.440   14.230  18.741  1.00 11.04  ? 123 TRP A O   1 
ATOM   1002 C  CB  . TRP A 1 123 ? 10.387  13.591  17.359  1.00 11.39  ? 123 TRP A CB  1 
ATOM   1003 C  CG  . TRP A 1 123 ? 9.712   14.277  16.212  1.00 11.62  ? 123 TRP A CG  1 
ATOM   1004 C  CD1 . TRP A 1 123 ? 9.422   13.721  14.987  1.00 11.40  ? 123 TRP A CD1 1 
ATOM   1005 C  CD2 . TRP A 1 123 ? 9.261   15.642  16.129  1.00 12.33  ? 123 TRP A CD2 1 
ATOM   1006 N  NE1 . TRP A 1 123 ? 8.849   14.637  14.149  1.00 13.18  ? 123 TRP A NE1 1 
ATOM   1007 C  CE2 . TRP A 1 123 ? 8.754   15.825  14.821  1.00 13.81  ? 123 TRP A CE2 1 
ATOM   1008 C  CE3 . TRP A 1 123 ? 9.309   16.729  17.017  1.00 13.45  ? 123 TRP A CE3 1 
ATOM   1009 C  CZ2 . TRP A 1 123 ? 8.190   17.020  14.403  1.00 14.03  ? 123 TRP A CZ2 1 
ATOM   1010 C  CZ3 . TRP A 1 123 ? 8.793   17.936  16.587  1.00 15.11  ? 123 TRP A CZ3 1 
ATOM   1011 C  CH2 . TRP A 1 123 ? 8.257   18.073  15.300  1.00 14.98  ? 123 TRP A CH2 1 
ATOM   1012 N  N   . ASN A 1 124 ? 9.128   14.321  20.241  1.00 10.24  ? 124 ASN A N   1 
ATOM   1013 C  CA  . ASN A 1 124 ? 8.444   15.180  21.205  1.00 11.27  ? 124 ASN A CA  1 
ATOM   1014 C  C   . ASN A 1 124 ? 8.304   16.579  20.599  1.00 11.71  ? 124 ASN A C   1 
ATOM   1015 O  O   . ASN A 1 124 ? 9.284   17.284  20.315  1.00 12.01  ? 124 ASN A O   1 
ATOM   1016 C  CB  . ASN A 1 124 ? 9.284   15.245  22.481  1.00 12.65  ? 124 ASN A CB  1 
ATOM   1017 C  CG  . ASN A 1 124 ? 8.533   15.847  23.649  1.00 13.60  ? 124 ASN A CG  1 
ATOM   1018 O  OD1 . ASN A 1 124 ? 7.715   16.759  23.413  1.00 15.28  ? 124 ASN A OD1 1 
ATOM   1019 N  ND2 . ASN A 1 124 ? 8.876   15.388  24.840  1.00 16.05  ? 124 ASN A ND2 1 
ATOM   1020 N  N   . THR A 1 125 ? 7.050   17.039  20.390  1.00 12.38  ? 125 THR A N   1 
ATOM   1021 C  CA  . THR A 1 125 ? 6.836   18.306  19.686  1.00 13.91  ? 125 THR A CA  1 
ATOM   1022 C  C   . THR A 1 125 ? 7.374   19.492  20.498  1.00 13.53  ? 125 THR A C   1 
ATOM   1023 O  O   . THR A 1 125 ? 7.554   20.572  19.872  1.00 15.25  ? 125 THR A O   1 
ATOM   1024 C  CB  . THR A 1 125 ? 5.345   18.476  19.368  1.00 17.38  ? 125 THR A CB  1 
ATOM   1025 O  OG1 . THR A 1 125 ? 4.624   18.537  20.595  1.00 20.29  ? 125 THR A OG1 1 
ATOM   1026 C  CG2 . THR A 1 125 ? 4.820   17.418  18.426  1.00 20.74  ? 125 THR A CG2 1 
ATOM   1027 N  N   . LYS A 1 126 ? 7.667   19.389  21.789  1.00 13.26  ? 127 LYS A N   1 
ATOM   1028 C  CA  . LYS A 1 126 ? 8.266   20.507  22.530  1.00 15.37  ? 127 LYS A CA  1 
ATOM   1029 C  C   . LYS A 1 126 ? 9.649   20.882  21.982  1.00 14.35  ? 127 LYS A C   1 
ATOM   1030 O  O   . LYS A 1 126 ? 10.135  21.979  22.269  1.00 16.35  ? 127 LYS A O   1 
ATOM   1031 C  CB  . LYS A 1 126 ? 8.279   20.222  24.028  1.00 18.92  ? 127 LYS A CB  1 
ATOM   1032 C  CG  . LYS A 1 126 ? 9.376   19.315  24.538  1.00 19.99  ? 127 LYS A CG  1 
ATOM   1033 C  CD  . LYS A 1 126 ? 9.335   18.892  26.054  1.00 34.61  ? 127 LYS A CD  1 
ATOM   1034 C  CE  . LYS A 1 126 ? 9.894   19.919  27.035  1.00 48.25  ? 127 LYS A CE  1 
ATOM   1035 N  NZ  . LYS A 1 126 ? 9.693   19.541  28.470  1.00 57.30  ? 127 LYS A NZ  1 
ATOM   1036 N  N   . TYR A 1 127 ? 10.254  20.006  21.183  1.00 12.89  ? 128 TYR A N   1 
ATOM   1037 C  CA  . TYR A 1 127 ? 11.559  20.252  20.591  1.00 12.45  ? 128 TYR A CA  1 
ATOM   1038 C  C   . TYR A 1 127 ? 11.518  20.708  19.137  1.00 12.29  ? 128 TYR A C   1 
ATOM   1039 O  O   . TYR A 1 127 ? 12.612  20.931  18.557  1.00 14.09  ? 128 TYR A O   1 
ATOM   1040 C  CB  . TYR A 1 127 ? 12.504  19.063  20.822  1.00 13.32  ? 128 TYR A CB  1 
ATOM   1041 C  CG  . TYR A 1 127 ? 12.716  18.743  22.278  1.00 13.51  ? 128 TYR A CG  1 
ATOM   1042 C  CD1 . TYR A 1 127 ? 13.159  19.729  23.165  1.00 15.39  ? 128 TYR A CD1 1 
ATOM   1043 C  CD2 . TYR A 1 127 ? 12.385  17.511  22.794  1.00 13.91  ? 128 TYR A CD2 1 
ATOM   1044 C  CE1 . TYR A 1 127 ? 13.268  19.459  24.516  1.00 16.89  ? 128 TYR A CE1 1 
ATOM   1045 C  CE2 . TYR A 1 127 ? 12.527  17.192  24.136  1.00 14.83  ? 128 TYR A CE2 1 
ATOM   1046 C  CZ  . TYR A 1 127 ? 12.996  18.191  24.985  1.00 15.51  ? 128 TYR A CZ  1 
ATOM   1047 O  OH  . TYR A 1 127 ? 13.125  17.960  26.300  1.00 18.87  ? 128 TYR A OH  1 
ATOM   1048 N  N   . GLY A 1 128 ? 10.319  20.865  18.557  1.00 13.75  ? 129 GLY A N   1 
ATOM   1049 C  CA  . GLY A 1 128 ? 10.180  21.585  17.288  1.00 13.74  ? 129 GLY A CA  1 
ATOM   1050 C  C   . GLY A 1 128 ? 10.533  20.784  16.034  1.00 13.19  ? 129 GLY A C   1 
ATOM   1051 O  O   . GLY A 1 128 ? 9.892   20.985  15.018  1.00 15.71  ? 129 GLY A O   1 
ATOM   1052 N  N   . ASP A 1 129 ? 11.566  19.935  16.078  1.00 13.83  ? 130 ASP A N   1 
ATOM   1053 C  CA  . ASP A 1 129 ? 11.847  19.099  14.904  1.00 13.80  ? 130 ASP A CA  1 
ATOM   1054 C  C   . ASP A 1 129 ? 12.483  17.801  15.415  1.00 13.03  ? 130 ASP A C   1 
ATOM   1055 O  O   . ASP A 1 129 ? 13.060  17.714  16.518  1.00 13.96  ? 130 ASP A O   1 
ATOM   1056 C  CB  . ASP A 1 129 ? 12.739  19.798  13.825  1.00 16.21  ? 130 ASP A CB  1 
ATOM   1057 C  CG  . ASP A 1 129 ? 14.154  20.124  14.277  1.00 19.05  ? 130 ASP A CG  1 
ATOM   1058 O  OD1 . ASP A 1 129 ? 14.954  19.228  14.378  1.00 22.35  ? 130 ASP A OD1 1 
ATOM   1059 O  OD2 . ASP A 1 129 ? 14.509  21.356  14.424  1.00 25.19  ? 130 ASP A OD2 1 
ATOM   1060 N  N   . TYR A 1 130 ? 12.451  16.787  14.522  1.00 13.48  ? 131 TYR A N   1 
ATOM   1061 C  CA  . TYR A 1 130 ? 12.992  15.468  14.824  1.00 12.16  ? 131 TYR A CA  1 
ATOM   1062 C  C   . TYR A 1 130 ? 14.498  15.532  15.163  1.00 12.73  ? 131 TYR A C   1 
ATOM   1063 O  O   . TYR A 1 130 ? 14.934  14.816  16.087  1.00 12.52  ? 131 TYR A O   1 
ATOM   1064 C  CB  . TYR A 1 130 ? 12.706  14.585  13.608  1.00 14.28  ? 131 TYR A CB  1 
ATOM   1065 C  CG  . TYR A 1 130 ? 13.201  13.152  13.625  1.00 11.49  ? 131 TYR A CG  1 
ATOM   1066 C  CD1 . TYR A 1 130 ? 13.144  12.323  14.759  1.00 11.77  ? 131 TYR A CD1 1 
ATOM   1067 C  CD2 . TYR A 1 130 ? 13.607  12.583  12.416  1.00 13.10  ? 131 TYR A CD2 1 
ATOM   1068 C  CE1 . TYR A 1 130 ? 13.515  10.984  14.685  1.00 13.36  ? 131 TYR A CE1 1 
ATOM   1069 C  CE2 . TYR A 1 130 ? 13.981  11.251  12.326  1.00 13.98  ? 131 TYR A CE2 1 
ATOM   1070 C  CZ  . TYR A 1 130 ? 13.875  10.455  13.449  1.00 12.91  ? 131 TYR A CZ  1 
ATOM   1071 O  OH  . TYR A 1 130 ? 14.208  9.135   13.429  1.00 14.45  ? 131 TYR A OH  1 
ATOM   1072 N  N   . GLY A 1 131 ? 15.284  16.321  14.404  1.00 13.75  ? 132 GLY A N   1 
ATOM   1073 C  CA  . GLY A 1 131 ? 16.720  16.330  14.660  1.00 15.42  ? 132 GLY A CA  1 
ATOM   1074 C  C   . GLY A 1 131 ? 17.055  16.909  16.037  1.00 14.21  ? 132 GLY A C   1 
ATOM   1075 O  O   . GLY A 1 131 ? 17.945  16.394  16.736  1.00 16.68  ? 132 GLY A O   1 
ATOM   1076 N  N   . LYS A 1 132 ? 16.352  17.979  16.458  1.00 14.40  ? 133 LYS A N   1 
ATOM   1077 C  CA  . LYS A 1 132 ? 16.583  18.497  17.810  1.00 13.86  ? 133 LYS A CA  1 
ATOM   1078 C  C   . LYS A 1 132 ? 16.119  17.500  18.871  1.00 13.13  ? 133 LYS A C   1 
ATOM   1079 O  O   . LYS A 1 132 ? 16.783  17.317  19.888  1.00 15.47  ? 133 LYS A O   1 
ATOM   1080 C  CB  . LYS A 1 132 ? 15.832  19.836  17.983  1.00 16.34  ? 133 LYS A CB  1 
ATOM   1081 C  CG  . LYS A 1 132 ? 16.467  21.161  17.574  1.00 30.61  ? 133 LYS A CG  1 
ATOM   1082 C  CD  . LYS A 1 132 ? 17.554  21.136  16.626  1.00 32.06  ? 133 LYS A CD  1 
ATOM   1083 C  CE  . LYS A 1 132 ? 17.093  22.093  15.557  1.00 25.91  ? 133 LYS A CE  1 
ATOM   1084 N  NZ  . LYS A 1 132 ? 18.086  22.094  14.462  1.00 53.07  ? 133 LYS A NZ  1 
ATOM   1085 N  N   . ALA A 1 133 ? 14.959  16.857  18.623  1.00 12.34  ? 134 ALA A N   1 
ATOM   1086 C  CA  . ALA A 1 133 ? 14.457  15.868  19.585  1.00 12.36  ? 134 ALA A CA  1 
ATOM   1087 C  C   . ALA A 1 133 ? 15.479  14.737  19.807  1.00 11.77  ? 134 ALA A C   1 
ATOM   1088 O  O   . ALA A 1 133 ? 15.572  14.209  20.917  1.00 13.86  ? 134 ALA A O   1 
ATOM   1089 C  CB  . ALA A 1 133 ? 13.095  15.353  19.110  1.00 11.65  ? 134 ALA A CB  1 
ATOM   1090 N  N   . GLN A 1 134 ? 16.204  14.342  18.751  1.00 12.86  ? 135 GLN A N   1 
ATOM   1091 C  CA  . GLN A 1 134 ? 17.182  13.261  18.852  1.00 14.44  ? 135 GLN A CA  1 
ATOM   1092 C  C   . GLN A 1 134 ? 18.304  13.566  19.819  1.00 16.09  ? 135 GLN A C   1 
ATOM   1093 O  O   . GLN A 1 134 ? 19.049  12.655  20.187  1.00 19.50  ? 135 GLN A O   1 
ATOM   1094 C  CB  . GLN A 1 134 ? 17.810  13.028  17.482  1.00 17.33  ? 135 GLN A CB  1 
ATOM   1095 C  CG  . GLN A 1 134 ? 16.879  12.344  16.454  1.00 18.07  ? 135 GLN A CG  1 
ATOM   1096 C  CD  . GLN A 1 134 ? 17.419  12.565  15.052  1.00 18.64  ? 135 GLN A CD  1 
ATOM   1097 O  OE1 . GLN A 1 134 ? 18.641  12.545  14.825  1.00 23.50  ? 135 GLN A OE1 1 
ATOM   1098 N  NE2 . GLN A 1 134 ? 16.522  12.760  14.102  1.00 18.00  ? 135 GLN A NE2 1 
ATOM   1099 N  N   . GLN A 1 135 ? 18.437  14.824  20.278  1.00 14.95  ? 136 GLN A N   1 
ATOM   1100 C  CA  . GLN A 1 135 ? 19.511  15.252  21.169  1.00 17.20  ? 136 GLN A CA  1 
ATOM   1101 C  C   . GLN A 1 135 ? 19.014  15.442  22.603  1.00 16.98  ? 136 GLN A C   1 
ATOM   1102 O  O   . GLN A 1 135 ? 19.757  15.870  23.478  1.00 23.71  ? 136 GLN A O   1 
ATOM   1103 C  CB  . GLN A 1 135 ? 20.087  16.596  20.689  1.00 19.20  ? 136 GLN A CB  1 
ATOM   1104 C  CG  . GLN A 1 135 ? 20.542  16.531  19.235  1.00 26.52  ? 136 GLN A CG  1 
ATOM   1105 C  CD  . GLN A 1 135 ? 21.533  15.414  18.991  1.00 38.94  ? 136 GLN A CD  1 
ATOM   1106 O  OE1 . GLN A 1 135 ? 22.368  15.075  19.848  1.00 56.29  ? 136 GLN A OE1 1 
ATOM   1107 N  NE2 . GLN A 1 135 ? 21.421  14.796  17.820  1.00 54.85  ? 136 GLN A NE2 1 
ATOM   1108 N  N   . GLN A 1 136 ? 17.759  15.049  22.883  1.00 14.18  ? 137 GLN A N   1 
ATOM   1109 C  CA  . GLN A 1 136 ? 17.192  15.342  24.215  1.00 13.25  ? 137 GLN A CA  1 
ATOM   1110 C  C   . GLN A 1 136 ? 16.873  14.045  24.958  1.00 13.24  ? 137 GLN A C   1 
ATOM   1111 O  O   . GLN A 1 136 ? 16.478  13.075  24.317  1.00 13.04  ? 137 GLN A O   1 
ATOM   1112 C  CB  . GLN A 1 136 ? 15.880  16.131  24.080  1.00 14.69  ? 137 GLN A CB  1 
ATOM   1113 C  CG  . GLN A 1 136 ? 15.979  17.389  23.240  1.00 17.31  ? 137 GLN A CG  1 
ATOM   1114 C  CD  . GLN A 1 136 ? 17.011  18.326  23.792  1.00 20.66  ? 137 GLN A CD  1 
ATOM   1115 O  OE1 . GLN A 1 136 ? 17.173  18.449  25.009  1.00 23.25  ? 137 GLN A OE1 1 
ATOM   1116 N  NE2 . GLN A 1 136 ? 17.728  18.999  22.879  1.00 31.55  ? 137 GLN A NE2 1 
ATOM   1117 N  N   . PRO A 1 137 ? 16.916  14.037  26.313  1.00 13.72  ? 138 PRO A N   1 
ATOM   1118 C  CA  . PRO A 1 137 ? 16.735  12.806  27.070  1.00 14.81  ? 138 PRO A CA  1 
ATOM   1119 C  C   . PRO A 1 137 ? 15.334  12.206  26.919  1.00 14.54  ? 138 PRO A C   1 
ATOM   1120 O  O   . PRO A 1 137 ? 15.167  11.000  27.050  1.00 16.14  ? 138 PRO A O   1 
ATOM   1121 C  CB  . PRO A 1 137 ? 17.075  13.197  28.508  1.00 19.62  ? 138 PRO A CB  1 
ATOM   1122 C  CG  . PRO A 1 137 ? 17.052  14.720  28.517  1.00 25.56  ? 138 PRO A CG  1 
ATOM   1123 C  CD  . PRO A 1 137 ? 17.386  15.172  27.120  1.00 19.85  ? 138 PRO A CD  1 
ATOM   1124 N  N   . ASP A 1 138 ? 14.346  13.073  26.643  1.00 13.63  ? 139 ASP A N   1 
ATOM   1125 C  CA  . ASP A 1 138 ? 12.935  12.695  26.438  1.00 14.22  ? 139 ASP A CA  1 
ATOM   1126 C  C   . ASP A 1 138 ? 12.506  13.108  25.026  1.00 11.75  ? 139 ASP A C   1 
ATOM   1127 O  O   . ASP A 1 138 ? 11.364  13.513  24.797  1.00 13.34  ? 139 ASP A O   1 
ATOM   1128 C  CB  . ASP A 1 138 ? 12.015  13.351  27.485  1.00 15.34  ? 139 ASP A CB  1 
ATOM   1129 C  CG  . ASP A 1 138 ? 12.016  14.854  27.434  1.00 17.84  ? 139 ASP A CG  1 
ATOM   1130 O  OD1 . ASP A 1 138 ? 12.989  15.450  26.885  1.00 17.86  ? 139 ASP A OD1 1 
ATOM   1131 O  OD2 . ASP A 1 138 ? 11.147  15.426  28.087  1.00 21.93  ? 139 ASP A OD2 1 
ATOM   1132 N  N   . GLY A 1 139 ? 13.409  13.020  24.055  1.00 11.16  ? 140 GLY A N   1 
ATOM   1133 C  CA  . GLY A 1 139 ? 13.138  13.505  22.716  1.00 10.99  ? 140 GLY A CA  1 
ATOM   1134 C  C   . GLY A 1 139 ? 12.228  12.577  21.890  1.00 9.95   ? 140 GLY A C   1 
ATOM   1135 O  O   . GLY A 1 139 ? 11.486  13.059  21.055  1.00 10.61  ? 140 GLY A O   1 
ATOM   1136 N  N   . LEU A 1 140 ? 12.408  11.269  22.045  1.00 9.68   ? 141 LEU A N   1 
ATOM   1137 C  CA  . LEU A 1 140 ? 11.717  10.338  21.167  1.00 9.51   ? 141 LEU A CA  1 
ATOM   1138 C  C   . LEU A 1 140 ? 10.890  9.366   21.980  1.00 8.92   ? 141 LEU A C   1 
ATOM   1139 O  O   . LEU A 1 140 ? 11.189  9.062   23.137  1.00 10.11  ? 141 LEU A O   1 
ATOM   1140 C  CB  . LEU A 1 140 ? 12.694  9.532   20.311  1.00 10.74  ? 141 LEU A CB  1 
ATOM   1141 C  CG  . LEU A 1 140 ? 13.633  10.321  19.402  1.00 13.14  ? 141 LEU A CG  1 
ATOM   1142 C  CD1 . LEU A 1 140 ? 14.456  9.329   18.566  1.00 13.80  ? 141 LEU A CD1 1 
ATOM   1143 C  CD2 . LEU A 1 140 ? 12.973  11.337  18.529  1.00 13.28  ? 141 LEU A CD2 1 
ATOM   1144 N  N   . ALA A 1 141 ? 9.841   8.852   21.332  1.00 9.73   ? 142 ALA A N   1 
ATOM   1145 C  CA  . ALA A 1 141 ? 9.075   7.729   21.895  1.00 9.40   ? 142 ALA A CA  1 
ATOM   1146 C  C   . ALA A 1 141 ? 8.993   6.727   20.756  1.00 8.89   ? 142 ALA A C   1 
ATOM   1147 O  O   . ALA A 1 141 ? 8.559   7.076   19.652  1.00 10.26  ? 142 ALA A O   1 
ATOM   1148 C  CB  . ALA A 1 141 ? 7.687   8.187   22.332  1.00 12.09  ? 142 ALA A CB  1 
ATOM   1149 N  N   . VAL A 1 142 ? 9.463   5.500   21.049  1.00 9.11   ? 143 VAL A N   1 
ATOM   1150 C  CA  . VAL A 1 142 ? 9.401   4.474   20.016  1.00 9.13   ? 143 VAL A CA  1 
ATOM   1151 C  C   . VAL A 1 142 ? 8.432   3.416   20.513  1.00 8.80   ? 143 VAL A C   1 
ATOM   1152 O  O   . VAL A 1 142 ? 8.548   2.893   21.611  1.00 9.33   ? 143 VAL A O   1 
ATOM   1153 C  CB  . VAL A 1 142 ? 10.775  3.866   19.651  1.00 9.22   ? 143 VAL A CB  1 
ATOM   1154 C  CG1 . VAL A 1 142 ? 10.607  2.848   18.505  1.00 10.22  ? 143 VAL A CG1 1 
ATOM   1155 C  CG2 . VAL A 1 142 ? 11.735  4.946   19.221  1.00 10.44  ? 143 VAL A CG2 1 
ATOM   1156 N  N   . LEU A 1 143 ? 7.410   3.165   19.668  1.00 9.23   ? 144 LEU A N   1 
ATOM   1157 C  CA  . LEU A 1 143 ? 6.436   2.118   19.916  1.00 9.63   ? 144 LEU A CA  1 
ATOM   1158 C  C   . LEU A 1 143 ? 6.963   0.848   19.225  1.00 9.41   ? 144 LEU A C   1 
ATOM   1159 O  O   . LEU A 1 143 ? 7.116   0.834   18.008  1.00 10.20  ? 144 LEU A O   1 
ATOM   1160 C  CB  . LEU A 1 143 ? 5.078   2.596   19.372  1.00 12.45  ? 144 LEU A CB  1 
ATOM   1161 C  CG  . LEU A 1 143 ? 3.916   1.630   19.512  1.00 13.18  ? 144 LEU A CG  1 
ATOM   1162 C  CD1 . LEU A 1 143 ? 3.651   1.344   20.980  1.00 14.38  ? 144 LEU A CD1 1 
ATOM   1163 C  CD2 . LEU A 1 143 ? 2.685   2.246   18.863  1.00 15.25  ? 144 LEU A CD2 1 
ATOM   1164 N  N   . GLY A 1 144 ? 7.240   -0.182  20.045  1.00 9.11   ? 145 GLY A N   1 
ATOM   1165 C  CA  . GLY A 1 144 ? 7.764   -1.456  19.526  1.00 9.48   ? 145 GLY A CA  1 
ATOM   1166 C  C   . GLY A 1 144 ? 6.667   -2.514  19.534  1.00 8.90   ? 145 GLY A C   1 
ATOM   1167 O  O   . GLY A 1 144 ? 5.948   -2.649  20.511  1.00 10.15  ? 145 GLY A O   1 
ATOM   1168 N  N   . ILE A 1 145 ? 6.608   -3.268  18.434  1.00 8.87   ? 146 ILE A N   1 
ATOM   1169 C  CA  . ILE A 1 145 ? 5.575   -4.279  18.245  1.00 8.92   ? 146 ILE A CA  1 
ATOM   1170 C  C   . ILE A 1 145 ? 6.288   -5.531  17.743  1.00 9.46   ? 146 ILE A C   1 
ATOM   1171 O  O   . ILE A 1 145 ? 7.020   -5.494  16.742  1.00 9.88   ? 146 ILE A O   1 
ATOM   1172 C  CB  . ILE A 1 145 ? 4.520   -3.789  17.266  1.00 10.05  ? 146 ILE A CB  1 
ATOM   1173 C  CG1 . ILE A 1 145 ? 3.877   -2.490  17.778  1.00 12.82  ? 146 ILE A CG1 1 
ATOM   1174 C  CG2 . ILE A 1 145 ? 3.460   -4.889  17.051  1.00 13.11  ? 146 ILE A CG2 1 
ATOM   1175 C  CD1 . ILE A 1 145 ? 2.847   -1.880  16.841  1.00 13.26  ? 146 ILE A CD1 1 
ATOM   1176 N  N   . PHE A 1 146 ? 6.073   -6.650  18.424  1.00 9.14   ? 147 PHE A N   1 
ATOM   1177 C  CA  . PHE A 1 146 ? 6.696   -7.897  18.005  1.00 9.35   ? 147 PHE A CA  1 
ATOM   1178 C  C   . PHE A 1 146 ? 5.932   -8.506  16.838  1.00 9.70   ? 147 PHE A C   1 
ATOM   1179 O  O   . PHE A 1 146 ? 4.707   -8.386  16.764  1.00 10.40  ? 147 PHE A O   1 
ATOM   1180 C  CB  . PHE A 1 146 ? 6.704   -8.872  19.151  1.00 10.58  ? 147 PHE A CB  1 
ATOM   1181 C  CG  . PHE A 1 146 ? 7.520   -8.437  20.336  1.00 9.09   ? 147 PHE A CG  1 
ATOM   1182 C  CD1 . PHE A 1 146 ? 8.896   -8.288  20.158  1.00 9.62   ? 147 PHE A CD1 1 
ATOM   1183 C  CD2 . PHE A 1 146 ? 6.980   -8.137  21.562  1.00 10.46  ? 147 PHE A CD2 1 
ATOM   1184 C  CE1 . PHE A 1 146 ? 9.702   -7.936  21.238  1.00 10.69  ? 147 PHE A CE1 1 
ATOM   1185 C  CE2 . PHE A 1 146 ? 7.760   -7.755  22.646  1.00 10.18  ? 147 PHE A CE2 1 
ATOM   1186 C  CZ  . PHE A 1 146 ? 9.129   -7.668  22.476  1.00 10.71  ? 147 PHE A CZ  1 
ATOM   1187 N  N   . LEU A 1 147 ? 6.644   -9.207  15.951  1.00 10.23  ? 148 LEU A N   1 
ATOM   1188 C  CA  . LEU A 1 147 ? 6.060   -9.985  14.864  1.00 10.16  ? 148 LEU A CA  1 
ATOM   1189 C  C   . LEU A 1 147 ? 6.376   -11.456 15.113  1.00 10.65  ? 148 LEU A C   1 
ATOM   1190 O  O   . LEU A 1 147 ? 7.542   -11.815 15.282  1.00 11.99  ? 148 LEU A O   1 
ATOM   1191 C  CB  . LEU A 1 147 ? 6.666   -9.575  13.511  1.00 10.96  ? 148 LEU A CB  1 
ATOM   1192 C  CG  . LEU A 1 147 ? 6.126   -8.313  12.851  1.00 10.71  ? 148 LEU A CG  1 
ATOM   1193 C  CD1 . LEU A 1 147 ? 6.335   -7.050  13.709  1.00 12.04  ? 148 LEU A CD1 1 
ATOM   1194 C  CD2 . LEU A 1 147 ? 6.769   -8.124  11.478  1.00 13.44  ? 148 LEU A CD2 1 
ATOM   1195 N  N   . LYS A 1 148 ? 5.331   -12.286 15.103  1.00 11.56  ? 149 LYS A N   1 
ATOM   1196 C  CA  . LYS A 1 148 ? 5.504   -13.718 15.078  1.00 12.83  ? 149 LYS A CA  1 
ATOM   1197 C  C   . LYS A 1 148 ? 4.993   -14.249 13.744  1.00 13.85  ? 149 LYS A C   1 
ATOM   1198 O  O   . LYS A 1 148 ? 4.151   -13.621 13.087  1.00 15.72  ? 149 LYS A O   1 
ATOM   1199 C  CB  . LYS A 1 148 ? 4.776   -14.379 16.243  1.00 17.10  ? 149 LYS A CB  1 
ATOM   1200 C  CG  . LYS A 1 148 ? 3.279   -14.223 16.181  1.00 18.58  ? 149 LYS A CG  1 
ATOM   1201 C  CD  . LYS A 1 148 ? 2.613   -14.936 17.370  1.00 25.36  ? 149 LYS A CD  1 
ATOM   1202 C  CE  . LYS A 1 148 ? 1.309   -15.555 16.925  1.00 38.97  ? 149 LYS A CE  1 
ATOM   1203 N  NZ  . LYS A 1 148 ? 0.460   -15.933 18.076  1.00 47.90  ? 149 LYS A NZ  1 
ATOM   1204 N  N   . VAL A 1 149 ? 5.524   -15.382 13.306  1.00 14.06  ? 150 VAL A N   1 
ATOM   1205 C  CA  . VAL A 1 149 ? 5.124   -15.982 12.062  1.00 14.14  ? 150 VAL A CA  1 
ATOM   1206 C  C   . VAL A 1 149 ? 3.916   -16.885 12.297  1.00 14.50  ? 150 VAL A C   1 
ATOM   1207 O  O   . VAL A 1 149 ? 3.939   -17.797 13.137  1.00 16.82  ? 150 VAL A O   1 
ATOM   1208 C  CB  . VAL A 1 149 ? 6.321   -16.725 11.437  1.00 15.00  ? 150 VAL A CB  1 
ATOM   1209 C  CG1 . VAL A 1 149 ? 5.877   -17.525 10.224  1.00 16.49  ? 150 VAL A CG1 1 
ATOM   1210 C  CG2 . VAL A 1 149 ? 7.388   -15.745 10.989  1.00 18.32  ? 150 VAL A CG2 1 
ATOM   1211 N  N   . GLY A 1 150 ? 2.889   -16.626 11.496  1.00 14.20  ? 151 GLY A N   1 
ATOM   1212 C  CA  . GLY A 1 150 ? 1.651   -17.374 11.574  1.00 17.04  ? 151 GLY A CA  1 
ATOM   1213 C  C   . GLY A 1 150 ? 0.742   -16.990 10.418  1.00 15.35  ? 151 GLY A C   1 
ATOM   1214 O  O   . GLY A 1 150 ? 1.158   -17.103 9.274   1.00 16.13  ? 151 GLY A O   1 
ATOM   1215 N  N   . SER A 1 151 ? -0.453  -16.454 10.718  1.00 17.22  ? 152 SER A N   1 
ATOM   1216 C  CA  . SER A 1 151 ? -1.333  -15.906 9.692   1.00 16.51  ? 152 SER A CA  1 
ATOM   1217 C  C   . SER A 1 151 ? -0.730  -14.631 9.094   1.00 16.76  ? 152 SER A C   1 
ATOM   1218 O  O   . SER A 1 151 ? 0.020   -13.918 9.772   1.00 16.54  ? 152 SER A O   1 
ATOM   1219 C  CB  . SER A 1 151 ? -2.631  -15.539 10.348  1.00 25.63  ? 152 SER A CB  1 
ATOM   1220 O  OG  . SER A 1 151 ? -3.275  -16.733 10.692  1.00 35.73  ? 152 SER A OG  1 
ATOM   1221 N  N   . ALA A 1 152 ? -1.026  -14.316 7.828   1.00 15.71  ? 153 ALA A N   1 
ATOM   1222 C  CA  . ALA A 1 152 ? -0.622  -13.045 7.253   1.00 15.10  ? 153 ALA A CA  1 
ATOM   1223 C  C   . ALA A 1 152 ? -1.236  -11.867 7.991   1.00 14.34  ? 153 ALA A C   1 
ATOM   1224 O  O   . ALA A 1 152 ? -2.345  -11.919 8.505   1.00 17.89  ? 153 ALA A O   1 
ATOM   1225 C  CB  . ALA A 1 152 ? -0.963  -12.986 5.781   1.00 18.99  ? 153 ALA A CB  1 
ATOM   1226 N  N   . LYS A 1 153 ? -0.519  -10.741 7.930   1.00 16.36  ? 154 LYS A N   1 
ATOM   1227 C  CA  . LYS A 1 153 ? -1.061  -9.459  8.391   1.00 15.26  ? 154 LYS A CA  1 
ATOM   1228 C  C   . LYS A 1 153 ? -1.475  -8.692  7.126   1.00 15.21  ? 154 LYS A C   1 
ATOM   1229 O  O   . LYS A 1 153 ? -0.636  -8.216  6.353   1.00 15.54  ? 154 LYS A O   1 
ATOM   1230 C  CB  . LYS A 1 153 ? 0.034   -8.667  9.113   1.00 15.56  ? 154 LYS A CB  1 
ATOM   1231 C  CG  . LYS A 1 153 ? -0.455  -7.431  9.869   1.00 16.14  ? 154 LYS A CG  1 
ATOM   1232 C  CD  . LYS A 1 153 ? -1.309  -7.833  11.067  1.00 18.74  ? 154 LYS A CD  1 
ATOM   1233 C  CE  . LYS A 1 153 ? -1.477  -6.631  11.981  1.00 20.39  ? 154 LYS A CE  1 
ATOM   1234 N  NZ  . LYS A 1 153 ? -2.432  -6.966  13.041  1.00 24.10  ? 154 LYS A NZ  1 
ATOM   1235 N  N   . PRO A 1 154 ? -2.786  -8.552  6.852   1.00 16.33  ? 155 PRO A N   1 
ATOM   1236 C  CA  . PRO A 1 154 ? -3.200  -7.934  5.568   1.00 16.69  ? 155 PRO A CA  1 
ATOM   1237 C  C   . PRO A 1 154 ? -2.674  -6.499  5.436   1.00 17.25  ? 155 PRO A C   1 
ATOM   1238 O  O   . PRO A 1 154 ? -2.247  -6.091  4.352   1.00 20.31  ? 155 PRO A O   1 
ATOM   1239 C  CB  . PRO A 1 154 ? -4.736  -7.999  5.630   1.00 20.60  ? 155 PRO A CB  1 
ATOM   1240 C  CG  . PRO A 1 154 ? -5.031  -9.055  6.666   1.00 26.90  ? 155 PRO A CG  1 
ATOM   1241 C  CD  . PRO A 1 154 ? -3.904  -9.086  7.657   1.00 17.80  ? 155 PRO A CD  1 
ATOM   1242 N  N   . GLY A 1 155 ? -2.588  -5.782  6.564   1.00 17.60  ? 156 GLY A N   1 
ATOM   1243 C  CA  . GLY A 1 155 ? -2.155  -4.380  6.560   1.00 18.58  ? 156 GLY A CA  1 
ATOM   1244 C  C   . GLY A 1 155 ? -0.680  -4.183  6.245   1.00 17.13  ? 156 GLY A C   1 
ATOM   1245 O  O   . GLY A 1 155 ? -0.227  -3.072  6.056   1.00 20.92  ? 156 GLY A O   1 
ATOM   1246 N  N   . LEU A 1 156 ? 0.068   -5.275  6.287   1.00 15.55  ? 157 LEU A N   1 
ATOM   1247 C  CA  . LEU A 1 156 ? 1.483   -5.260  5.969   1.00 14.38  ? 157 LEU A CA  1 
ATOM   1248 C  C   . LEU A 1 156 ? 1.738   -5.502  4.490   1.00 14.54  ? 157 LEU A C   1 
ATOM   1249 O  O   . LEU A 1 156 ? 2.836   -5.219  3.976   1.00 15.45  ? 157 LEU A O   1 
ATOM   1250 C  CB  . LEU A 1 156 ? 2.232   -6.298  6.828   1.00 15.01  ? 157 LEU A CB  1 
ATOM   1251 C  CG  . LEU A 1 156 ? 3.752   -6.418  6.620   1.00 14.10  ? 157 LEU A CG  1 
ATOM   1252 C  CD1 . LEU A 1 156 ? 4.485   -5.109  7.001   1.00 16.02  ? 157 LEU A CD1 1 
ATOM   1253 C  CD2 . LEU A 1 156 ? 4.300   -7.573  7.468   1.00 15.75  ? 157 LEU A CD2 1 
ATOM   1254 N  N   . GLN A 1 157 ? 0.753   -6.053  3.777   1.00 15.29  ? 158 GLN A N   1 
ATOM   1255 C  CA  . GLN A 1 157 ? 1.053   -6.526  2.444   1.00 16.82  ? 158 GLN A CA  1 
ATOM   1256 C  C   . GLN A 1 157 ? 1.452   -5.392  1.500   1.00 16.56  ? 158 GLN A C   1 
ATOM   1257 O  O   . GLN A 1 157 ? 2.299   -5.638  0.657   1.00 16.87  ? 158 GLN A O   1 
ATOM   1258 C  CB  . GLN A 1 157 ? -0.042  -7.444  1.882   1.00 19.41  ? 158 GLN A CB  1 
ATOM   1259 C  CG  . GLN A 1 157 ? 0.366   -8.115  0.566   1.00 22.31  ? 158 GLN A CG  1 
ATOM   1260 C  CD  . GLN A 1 157 ? 1.485   -9.106  0.803   1.00 20.26  ? 158 GLN A CD  1 
ATOM   1261 O  OE1 . GLN A 1 157 ? 1.630   -9.657  1.907   1.00 21.06  ? 158 GLN A OE1 1 
ATOM   1262 N  NE2 . GLN A 1 157 ? 2.284   -9.376  -0.247  1.00 22.25  ? 158 GLN A NE2 1 
ATOM   1263 N  N   . LYS A 1 158 ? 0.867   -4.178  1.617   1.00 17.53  ? 159 LYS A N   1 
ATOM   1264 C  CA  . LYS A 1 158 ? 1.250   -3.082  0.730   1.00 17.01  ? 159 LYS A CA  1 
ATOM   1265 C  C   . LYS A 1 158 ? 2.759   -2.768  0.879   1.00 16.73  ? 159 LYS A C   1 
ATOM   1266 O  O   . LYS A 1 158 ? 3.417   -2.377  -0.082  1.00 17.32  ? 159 LYS A O   1 
ATOM   1267 C  CB  . LYS A 1 158 ? 0.418   -1.822  1.021   1.00 22.23  ? 159 LYS A CB  1 
ATOM   1268 C  CG  . LYS A 1 158 ? 0.658   -0.575  0.156   1.00 35.24  ? 159 LYS A CG  1 
ATOM   1269 C  CD  . LYS A 1 158 ? -0.185  0.702   0.497   1.00 40.81  ? 159 LYS A CD  1 
ATOM   1270 C  CE  . LYS A 1 158 ? 0.258   2.034   -0.111  1.00 46.28  ? 159 LYS A CE  1 
ATOM   1271 N  NZ  . LYS A 1 158 ? 0.066   2.125   -1.588  1.00 47.97  ? 159 LYS A NZ  1 
ATOM   1272 N  N   . VAL A 1 159 ? 3.283   -2.933  2.106   1.00 15.00  ? 160 VAL A N   1 
ATOM   1273 C  CA  . VAL A 1 159 ? 4.709   -2.716  2.359   1.00 15.62  ? 160 VAL A CA  1 
ATOM   1274 C  C   . VAL A 1 159 ? 5.514   -3.826  1.700   1.00 15.94  ? 160 VAL A C   1 
ATOM   1275 O  O   . VAL A 1 159 ? 6.444   -3.557  0.965   1.00 16.39  ? 160 VAL A O   1 
ATOM   1276 C  CB  . VAL A 1 159 ? 4.998   -2.693  3.860   1.00 15.77  ? 160 VAL A CB  1 
ATOM   1277 C  CG1 . VAL A 1 159 ? 6.500   -2.730  4.132   1.00 18.26  ? 160 VAL A CG1 1 
ATOM   1278 C  CG2 . VAL A 1 159 ? 4.356   -1.468  4.491   1.00 19.89  ? 160 VAL A CG2 1 
ATOM   1279 N  N   . VAL A 1 160 ? 5.143   -5.084  1.949   1.00 16.12  ? 161 VAL A N   1 
ATOM   1280 C  CA  . VAL A 1 160 ? 5.904   -6.206  1.402   1.00 17.89  ? 161 VAL A CA  1 
ATOM   1281 C  C   . VAL A 1 160 ? 5.978   -6.114  -0.129  1.00 16.30  ? 161 VAL A C   1 
ATOM   1282 O  O   . VAL A 1 160 ? 7.001   -6.407  -0.748  1.00 18.24  ? 161 VAL A O   1 
ATOM   1283 C  CB  . VAL A 1 160 ? 5.261   -7.559  1.847   1.00 21.57  ? 161 VAL A CB  1 
ATOM   1284 C  CG1 . VAL A 1 160 ? 5.649   -8.798  1.051   1.00 20.77  ? 161 VAL A CG1 1 
ATOM   1285 C  CG2 . VAL A 1 160 ? 5.522   -7.746  3.329   1.00 25.77  ? 161 VAL A CG2 1 
ATOM   1286 N  N   . ASP A 1 161 ? 4.852   -5.731  -0.770  1.00 18.91  ? 162 ASP A N   1 
ATOM   1287 C  CA  . ASP A 1 161 ? 4.796   -5.743  -2.236  1.00 21.53  ? 162 ASP A CA  1 
ATOM   1288 C  C   . ASP A 1 161 ? 5.676   -4.688  -2.907  1.00 22.42  ? 162 ASP A C   1 
ATOM   1289 O  O   . ASP A 1 161 ? 5.962   -4.811  -4.094  1.00 28.61  ? 162 ASP A O   1 
ATOM   1290 C  CB  . ASP A 1 161 ? 3.350   -5.661  -2.686  1.00 25.60  ? 162 ASP A CB  1 
ATOM   1291 C  CG  . ASP A 1 161 ? 2.714   -7.050  -2.652  1.00 27.29  ? 162 ASP A CG  1 
ATOM   1292 O  OD1 . ASP A 1 161 ? 3.465   -8.081  -2.821  1.00 38.81  ? 162 ASP A OD1 1 
ATOM   1293 O  OD2 . ASP A 1 161 ? 1.512   -7.107  -2.399  1.00 34.72  ? 162 ASP A OD2 1 
ATOM   1294 N  N   . VAL A 1 162 ? 6.088   -3.633  -2.172  1.00 19.92  ? 163 VAL A N   1 
ATOM   1295 C  CA  . VAL A 1 162 ? 6.872   -2.589  -2.794  1.00 20.36  ? 163 VAL A CA  1 
ATOM   1296 C  C   . VAL A 1 162 ? 8.355   -2.885  -2.547  1.00 18.37  ? 163 VAL A C   1 
ATOM   1297 O  O   . VAL A 1 162 ? 9.182   -2.196  -3.119  1.00 20.37  ? 163 VAL A O   1 
ATOM   1298 C  CB  . VAL A 1 162 ? 6.483   -1.209  -2.209  1.00 23.07  ? 163 VAL A CB  1 
ATOM   1299 C  CG1 . VAL A 1 162 ? 7.040   -0.951  -0.831  1.00 23.29  ? 163 VAL A CG1 1 
ATOM   1300 C  CG2 . VAL A 1 162 ? 6.794   -0.010  -3.087  1.00 24.18  ? 163 VAL A CG2 1 
ATOM   1301 N  N   . LEU A 1 163 ? 8.738   -3.895  -1.736  1.00 18.98  ? 164 LEU A N   1 
ATOM   1302 C  CA  . LEU A 1 163 ? 10.154  -4.042  -1.378  1.00 17.15  ? 164 LEU A CA  1 
ATOM   1303 C  C   . LEU A 1 163 ? 11.094  -4.372  -2.547  1.00 18.93  ? 164 LEU A C   1 
ATOM   1304 O  O   . LEU A 1 163 ? 12.268  -3.982  -2.536  1.00 20.23  ? 164 LEU A O   1 
ATOM   1305 C  CB  . LEU A 1 163 ? 10.289  -5.107  -0.291  1.00 17.05  ? 164 LEU A CB  1 
ATOM   1306 C  CG  . LEU A 1 163 ? 9.640   -4.761  1.049   1.00 16.23  ? 164 LEU A CG  1 
ATOM   1307 C  CD1 . LEU A 1 163 ? 9.991   -5.867  2.053   1.00 18.09  ? 164 LEU A CD1 1 
ATOM   1308 C  CD2 . LEU A 1 163 ? 10.194  -3.424  1.585   1.00 16.97  ? 164 LEU A CD2 1 
ATOM   1309 N  N   . ASP A 1 164 ? 10.603  -5.072  -3.562  1.00 20.22  ? 165 ASP A N   1 
ATOM   1310 C  CA  . ASP A 1 164 ? 11.412  -5.323  -4.757  1.00 23.22  ? 165 ASP A CA  1 
ATOM   1311 C  C   . ASP A 1 164 ? 11.832  -4.002  -5.424  1.00 22.64  ? 165 ASP A C   1 
ATOM   1312 O  O   . ASP A 1 164 ? 12.813  -3.989  -6.168  1.00 30.17  ? 165 ASP A O   1 
ATOM   1313 C  CB  . ASP A 1 164 ? 10.657  -6.279  -5.698  1.00 35.33  ? 165 ASP A CB  1 
ATOM   1314 C  CG  . ASP A 1 164 ? 9.632   -5.515  -6.518  1.00 34.03  ? 165 ASP A CG  1 
ATOM   1315 O  OD1 . ASP A 1 164 ? 8.682   -4.998  -5.891  1.00 40.69  ? 165 ASP A OD1 1 
ATOM   1316 O  OD2 . ASP A 1 164 ? 9.873   -5.315  -7.770  1.00 51.00  ? 165 ASP A OD2 1 
ATOM   1317 N  N   . SER A 1 165 ? 11.083  -2.891  -5.221  1.00 20.51  ? 166 SER A N   1 
ATOM   1318 C  CA  . SER A 1 165 ? 11.496  -1.641  -5.859  1.00 22.60  ? 166 SER A CA  1 
ATOM   1319 C  C   . SER A 1 165 ? 12.554  -0.896  -5.040  1.00 19.64  ? 166 SER A C   1 
ATOM   1320 O  O   . SER A 1 165 ? 13.118  0.098   -5.513  1.00 22.63  ? 166 SER A O   1 
ATOM   1321 C  CB  . SER A 1 165 ? 10.304  -0.799  -6.161  1.00 28.05  ? 166 SER A CB  1 
ATOM   1322 O  OG  . SER A 1 165 ? 9.763   -0.318  -4.953  1.00 26.80  ? 166 SER A OG  1 
ATOM   1323 N  N   . ILE A 1 166 ? 12.858  -1.396  -3.816  1.00 19.13  ? 167 ILE A N   1 
ATOM   1324 C  CA  . ILE A 1 166 ? 13.879  -0.767  -3.009  1.00 16.39  ? 167 ILE A CA  1 
ATOM   1325 C  C   . ILE A 1 166 ? 14.873  -1.810  -2.492  1.00 15.50  ? 167 ILE A C   1 
ATOM   1326 O  O   . ILE A 1 166 ? 15.286  -1.811  -1.324  1.00 16.81  ? 167 ILE A O   1 
ATOM   1327 C  CB  . ILE A 1 166 ? 13.285  0.071   -1.864  1.00 16.92  ? 167 ILE A CB  1 
ATOM   1328 C  CG1 . ILE A 1 166 ? 12.422  -0.794  -0.941  1.00 16.54  ? 167 ILE A CG1 1 
ATOM   1329 C  CG2 . ILE A 1 166 ? 12.528  1.296   -2.398  1.00 18.99  ? 167 ILE A CG2 1 
ATOM   1330 C  CD1 . ILE A 1 166 ? 12.378  -0.242  0.502   1.00 17.35  ? 167 ILE A CD1 1 
ATOM   1331 N  N   . LYS A 1 167 ? 15.316  -2.651  -3.413  1.00 17.66  ? 168 LYS A N   1 
ATOM   1332 C  CA  . LYS A 1 167 ? 16.110  -3.795  -3.017  1.00 15.83  ? 168 LYS A CA  1 
ATOM   1333 C  C   . LYS A 1 167 ? 17.403  -3.410  -2.323  1.00 17.49  ? 168 LYS A C   1 
ATOM   1334 O  O   . LYS A 1 167 ? 17.840  -4.099  -1.408  1.00 17.67  ? 168 LYS A O   1 
ATOM   1335 C  CB  . LYS A 1 167 ? 16.399  -4.722  -4.218  1.00 19.81  ? 168 LYS A CB  1 
ATOM   1336 C  CG  . LYS A 1 167 ? 17.167  -5.983  -3.823  1.00 19.86  ? 168 LYS A CG  1 
ATOM   1337 C  CD  . LYS A 1 167 ? 17.365  -6.901  -5.054  1.00 25.17  ? 168 LYS A CD  1 
ATOM   1338 C  CE  . LYS A 1 167 ? 18.240  -8.094  -4.717  1.00 30.53  ? 168 LYS A CE  1 
ATOM   1339 N  NZ  . LYS A 1 167 ? 18.264  -9.097  -5.809  1.00 43.39  ? 168 LYS A NZ  1 
ATOM   1340 N  N   . THR A 1 168 ? 18.035  -2.361  -2.831  1.00 17.67  ? 169 THR A N   1 
ATOM   1341 C  CA  . THR A 1 168 ? 19.376  -2.063  -2.422  1.00 17.19  ? 169 THR A CA  1 
ATOM   1342 C  C   . THR A 1 168 ? 19.436  -0.691  -1.733  1.00 14.40  ? 169 THR A C   1 
ATOM   1343 O  O   . THR A 1 168 ? 18.568  0.195   -1.836  1.00 17.71  ? 169 THR A O   1 
ATOM   1344 C  CB  . THR A 1 168 ? 20.294  -2.067  -3.662  1.00 18.14  ? 169 THR A CB  1 
ATOM   1345 O  OG1 . THR A 1 168 ? 19.710  -1.278  -4.690  1.00 18.50  ? 169 THR A OG1 1 
ATOM   1346 C  CG2 . THR A 1 168 ? 20.507  -3.496  -4.130  1.00 21.11  ? 169 THR A CG2 1 
ATOM   1347 N  N   . LYS A 1 169 ? 20.514  -0.559  -0.979  1.00 17.94  ? 170 LYS A N   1 
ATOM   1348 C  CA  . LYS A 1 169 ? 20.762  0.634   -0.185  1.00 15.66  ? 170 LYS A CA  1 
ATOM   1349 C  C   . LYS A 1 169 ? 20.670  1.937   -0.985  1.00 15.38  ? 170 LYS A C   1 
ATOM   1350 O  O   . LYS A 1 169 ? 21.304  2.050   -2.056  1.00 22.16  ? 170 LYS A O   1 
ATOM   1351 C  CB  . LYS A 1 169 ? 22.185  0.561   0.384   1.00 17.31  ? 170 LYS A CB  1 
ATOM   1352 C  CG  . LYS A 1 169 ? 22.656  1.785   1.185   1.00 19.22  ? 170 LYS A CG  1 
ATOM   1353 C  CD  . LYS A 1 169 ? 24.001  1.561   1.888   1.00 22.96  ? 170 LYS A CD  1 
ATOM   1354 C  CE  . LYS A 1 169 ? 24.695  2.857   2.257   1.00 42.99  ? 170 LYS A CE  1 
ATOM   1355 N  NZ  . LYS A 1 169 ? 26.136  2.676   2.581   1.00 46.88  ? 170 LYS A NZ  1 
ATOM   1356 N  N   . GLY A 1 170 ? 19.874  2.908   -0.482  1.00 17.78  ? 171 GLY A N   1 
ATOM   1357 C  CA  . GLY A 1 170 ? 19.700  4.210   -1.132  1.00 21.07  ? 171 GLY A CA  1 
ATOM   1358 C  C   . GLY A 1 170 ? 18.498  4.315   -2.082  1.00 19.09  ? 171 GLY A C   1 
ATOM   1359 O  O   . GLY A 1 170 ? 18.128  5.417   -2.538  1.00 23.27  ? 171 GLY A O   1 
ATOM   1360 N  N   . LYS A 1 171 ? 17.874  3.150   -2.386  1.00 17.49  ? 172 LYS A N   1 
ATOM   1361 C  CA  . LYS A 1 171 ? 16.675  3.208   -3.217  1.00 19.54  ? 172 LYS A CA  1 
ATOM   1362 C  C   . LYS A 1 171 ? 15.471  3.644   -2.394  1.00 16.14  ? 172 LYS A C   1 
ATOM   1363 O  O   . LYS A 1 171 ? 15.293  3.194   -1.250  1.00 18.10  ? 172 LYS A O   1 
ATOM   1364 C  CB  . LYS A 1 171 ? 16.455  1.848   -3.852  1.00 18.67  ? 172 LYS A CB  1 
ATOM   1365 C  CG  . LYS A 1 171 ? 17.496  1.515   -4.920  1.00 23.27  ? 172 LYS A CG  1 
ATOM   1366 C  CD  . LYS A 1 171 ? 17.130  0.386   -5.870  1.00 28.08  ? 172 LYS A CD  1 
ATOM   1367 C  CE  . LYS A 1 171 ? 17.904  0.439   -7.177  1.00 42.58  ? 172 LYS A CE  1 
ATOM   1368 N  NZ  . LYS A 1 171 ? 17.295  -0.423  -8.222  1.00 54.17  ? 172 LYS A NZ  1 
ATOM   1369 N  N   . SER A 1 172 ? 14.642  4.516   -2.939  1.00 18.52  ? 173 SER A N   1 
ATOM   1370 C  CA  . SER A 1 172 ? 13.366  4.903   -2.374  1.00 20.32  ? 173 SER A CA  1 
ATOM   1371 C  C   . SER A 1 172 ? 12.255  4.773   -3.414  1.00 18.11  ? 173 SER A C   1 
ATOM   1372 O  O   . SER A 1 172 ? 12.482  4.797   -4.652  1.00 22.39  ? 173 SER A O   1 
ATOM   1373 C  CB  . SER A 1 172 ? 13.440  6.286   -1.825  1.00 19.29  ? 173 SER A CB  1 
ATOM   1374 O  OG  . SER A 1 172 ? 13.613  7.250   -2.828  1.00 24.82  ? 173 SER A OG  1 
ATOM   1375 N  N   . ALA A 1 173 ? 11.015  4.807   -2.907  1.00 19.55  ? 174 ALA A N   1 
ATOM   1376 C  CA  . ALA A 1 173 ? 9.859   4.810   -3.791  1.00 20.25  ? 174 ALA A CA  1 
ATOM   1377 C  C   . ALA A 1 173 ? 8.712   5.589   -3.138  1.00 19.45  ? 174 ALA A C   1 
ATOM   1378 O  O   . ALA A 1 173 ? 8.644   5.681   -1.898  1.00 18.03  ? 174 ALA A O   1 
ATOM   1379 C  CB  . ALA A 1 173 ? 9.489   3.380   -4.048  1.00 26.73  ? 174 ALA A CB  1 
ATOM   1380 N  N   . ASP A 1 174 ? 7.860   6.220   -3.933  1.00 22.99  ? 175 ASP A N   1 
ATOM   1381 C  CA  . ASP A 1 174 ? 6.718   6.935   -3.374  1.00 24.37  ? 175 ASP A CA  1 
ATOM   1382 C  C   . ASP A 1 174 ? 5.920   5.894   -2.620  1.00 22.23  ? 175 ASP A C   1 
ATOM   1383 O  O   . ASP A 1 174 ? 5.874   4.745   -3.028  1.00 25.63  ? 175 ASP A O   1 
ATOM   1384 C  CB  . ASP A 1 174 ? 5.836   7.518   -4.484  1.00 29.57  ? 175 ASP A CB  1 
ATOM   1385 C  CG  . ASP A 1 174 ? 6.476   8.679   -5.229  1.00 40.79  ? 175 ASP A CG  1 
ATOM   1386 O  OD1 . ASP A 1 174 ? 7.371   9.367   -4.631  1.00 44.64  ? 175 ASP A OD1 1 
ATOM   1387 O  OD2 . ASP A 1 174 ? 6.105   8.872   -6.414  1.00 56.30  ? 175 ASP A OD2 1 
ATOM   1388 N  N   . PHE A 1 175 ? 5.303   6.311   -1.523  1.00 18.18  ? 176 PHE A N   1 
ATOM   1389 C  CA  . PHE A 1 175 ? 4.602   5.369   -0.685  1.00 17.77  ? 176 PHE A CA  1 
ATOM   1390 C  C   . PHE A 1 175 ? 3.548   6.163   0.040   1.00 20.52  ? 176 PHE A C   1 
ATOM   1391 O  O   . PHE A 1 175 ? 3.667   6.426   1.213   1.00 22.17  ? 176 PHE A O   1 
ATOM   1392 C  CB  . PHE A 1 175 ? 5.550   4.532   0.168   1.00 19.81  ? 176 PHE A CB  1 
ATOM   1393 C  CG  . PHE A 1 175 ? 4.915   3.279   0.692   1.00 18.37  ? 176 PHE A CG  1 
ATOM   1394 C  CD1 . PHE A 1 175 ? 4.693   2.197   -0.147  1.00 20.34  ? 176 PHE A CD1 1 
ATOM   1395 C  CD2 . PHE A 1 175 ? 4.574   3.163   2.031   1.00 18.00  ? 176 PHE A CD2 1 
ATOM   1396 C  CE1 . PHE A 1 175 ? 4.140   1.034   0.367   1.00 19.89  ? 176 PHE A CE1 1 
ATOM   1397 C  CE2 . PHE A 1 175 ? 4.054   1.974   2.542   1.00 19.64  ? 176 PHE A CE2 1 
ATOM   1398 C  CZ  . PHE A 1 175 ? 3.815   0.929   1.693   1.00 19.69  ? 176 PHE A CZ  1 
ATOM   1399 N  N   . THR A 1 176 ? 2.524   6.576   -0.692  1.00 21.50  ? 177 THR A N   1 
ATOM   1400 C  CA  . THR A 1 176 ? 1.500   7.435   -0.153  1.00 20.73  ? 177 THR A CA  1 
ATOM   1401 C  C   . THR A 1 176 ? 0.302   6.597   0.270   1.00 15.60  ? 177 THR A C   1 
ATOM   1402 O  O   . THR A 1 176 ? 0.134   5.460   -0.173  1.00 18.39  ? 177 THR A O   1 
ATOM   1403 C  CB  . THR A 1 176 ? 1.074   8.473   -1.200  1.00 21.38  ? 177 THR A CB  1 
ATOM   1404 O  OG1 . THR A 1 176 ? 0.586   7.818   -2.385  1.00 24.05  ? 177 THR A OG1 1 
ATOM   1405 C  CG2 . THR A 1 176 ? 2.162   9.481   -1.493  1.00 30.13  ? 177 THR A CG2 1 
ATOM   1406 N  N   . ASN A 1 177 ? -0.525  7.147   1.151   1.00 17.24  ? 178 ASN A N   1 
ATOM   1407 C  CA  . ASN A 1 177 ? -1.799  6.593   1.547   1.00 18.04  ? 178 ASN A CA  1 
ATOM   1408 C  C   . ASN A 1 177 ? -1.644  5.253   2.251   1.00 18.19  ? 178 ASN A C   1 
ATOM   1409 O  O   . ASN A 1 177 ? -2.543  4.410   2.169   1.00 24.02  ? 178 ASN A O   1 
ATOM   1410 C  CB  . ASN A 1 177 ? -2.767  6.506   0.367   1.00 19.84  ? 178 ASN A CB  1 
ATOM   1411 C  CG  . ASN A 1 177 ? -2.992  7.885   -0.234  1.00 18.73  ? 178 ASN A CG  1 
ATOM   1412 O  OD1 . ASN A 1 177 ? -3.610  8.758   0.386   1.00 24.62  ? 178 ASN A OD1 1 
ATOM   1413 N  ND2 . ASN A 1 177 ? -2.387  8.124   -1.376  1.00 20.31  ? 178 ASN A ND2 1 
ATOM   1414 N  N   . PHE A 1 178 ? -0.519  5.053   2.940   1.00 16.09  ? 179 PHE A N   1 
ATOM   1415 C  CA  . PHE A 1 178 ? -0.420  3.835   3.723   1.00 16.75  ? 179 PHE A CA  1 
ATOM   1416 C  C   . PHE A 1 178 ? -0.925  4.105   5.146   1.00 16.09  ? 179 PHE A C   1 
ATOM   1417 O  O   . PHE A 1 178 ? -0.541  5.101   5.750   1.00 17.97  ? 179 PHE A O   1 
ATOM   1418 C  CB  . PHE A 1 178 ? 1.040   3.394   3.813   1.00 18.12  ? 179 PHE A CB  1 
ATOM   1419 C  CG  . PHE A 1 178 ? 1.205   2.165   4.671   1.00 16.28  ? 179 PHE A CG  1 
ATOM   1420 C  CD1 . PHE A 1 178 ? 0.786   0.943   4.182   1.00 17.97  ? 179 PHE A CD1 1 
ATOM   1421 C  CD2 . PHE A 1 178 ? 1.590   2.244   5.998   1.00 15.27  ? 179 PHE A CD2 1 
ATOM   1422 C  CE1 . PHE A 1 178 ? 0.841   -0.180  4.974   1.00 20.00  ? 179 PHE A CE1 1 
ATOM   1423 C  CE2 . PHE A 1 178 ? 1.625   1.101   6.792   1.00 14.50  ? 179 PHE A CE2 1 
ATOM   1424 C  CZ  . PHE A 1 178 ? 1.301   -0.124  6.262   1.00 16.69  ? 179 PHE A CZ  1 
ATOM   1425 N  N   . ASP A 1 179 ? -1.790  3.252   5.690   1.00 17.22  ? 180 ASP A N   1 
ATOM   1426 C  CA  . ASP A 1 179 ? -2.381  3.487   6.991   1.00 16.60  ? 180 ASP A CA  1 
ATOM   1427 C  C   . ASP A 1 179 ? -1.689  2.634   8.038   1.00 16.51  ? 180 ASP A C   1 
ATOM   1428 O  O   . ASP A 1 179 ? -1.867  1.424   8.076   1.00 17.13  ? 180 ASP A O   1 
ATOM   1429 C  CB  . ASP A 1 179 ? -3.864  3.114   6.937   1.00 18.65  ? 180 ASP A CB  1 
ATOM   1430 C  CG  . ASP A 1 179 ? -4.654  3.491   8.172   1.00 23.09  ? 180 ASP A CG  1 
ATOM   1431 O  OD1 . ASP A 1 179 ? -4.059  3.705   9.227   1.00 19.95  ? 180 ASP A OD1 1 
ATOM   1432 O  OD2 . ASP A 1 179 ? -5.874  3.610   8.037   1.00 28.69  ? 180 ASP A OD2 1 
ATOM   1433 N  N   . PRO A 1 180 ? -0.852  3.218   8.922   1.00 15.44  ? 181 PRO A N   1 
ATOM   1434 C  CA  . PRO A 1 180 ? -0.124  2.390   9.893   1.00 14.84  ? 181 PRO A CA  1 
ATOM   1435 C  C   . PRO A 1 180 ? -1.007  1.790   10.983  1.00 13.95  ? 181 PRO A C   1 
ATOM   1436 O  O   . PRO A 1 180 ? -0.562  0.874   11.667  1.00 14.73  ? 181 PRO A O   1 
ATOM   1437 C  CB  . PRO A 1 180 ? 0.901   3.395   10.414  1.00 17.14  ? 181 PRO A CB  1 
ATOM   1438 C  CG  . PRO A 1 180 ? 0.164   4.699   10.371  1.00 17.08  ? 181 PRO A CG  1 
ATOM   1439 C  CD  . PRO A 1 180 ? -0.517  4.641   9.011   1.00 16.87  ? 181 PRO A CD  1 
ATOM   1440 N  N   . ARG A 1 181 ? -2.291  2.160   11.018  1.00 14.62  ? 182 ARG A N   1 
ATOM   1441 C  CA  . ARG A 1 181 ? -3.220  1.488   11.928  1.00 15.59  ? 182 ARG A CA  1 
ATOM   1442 C  C   . ARG A 1 181 ? -3.335  0.005   11.589  1.00 15.39  ? 182 ARG A C   1 
ATOM   1443 O  O   . ARG A 1 181 ? -3.661  -0.804  12.490  1.00 17.38  ? 182 ARG A O   1 
ATOM   1444 C  CB  . ARG A 1 181 ? -4.595  2.164   11.887  1.00 16.95  ? 182 ARG A CB  1 
ATOM   1445 C  CG  . ARG A 1 181 ? -4.518  3.569   12.433  1.00 18.75  ? 182 ARG A CG  1 
ATOM   1446 C  CD  . ARG A 1 181 ? -5.836  4.258   12.460  1.00 20.65  ? 182 ARG A CD  1 
ATOM   1447 N  NE  . ARG A 1 181 ? -6.266  4.495   11.085  1.00 21.12  ? 182 ARG A NE  1 
ATOM   1448 C  CZ  . ARG A 1 181 ? -7.349  5.172   10.741  1.00 21.73  ? 182 ARG A CZ  1 
ATOM   1449 N  NH1 . ARG A 1 181 ? -8.134  5.684   11.685  1.00 28.56  ? 182 ARG A NH1 1 
ATOM   1450 N  NH2 . ARG A 1 181 ? -7.614  5.347   9.462   1.00 26.73  ? 182 ARG A NH2 1 
ATOM   1451 N  N   . GLY A 1 182 ? -3.075  -0.360  10.332  1.00 14.77  ? 183 GLY A N   1 
ATOM   1452 C  CA  . GLY A 1 182 ? -3.186  -1.762  9.933   1.00 17.29  ? 183 GLY A CA  1 
ATOM   1453 C  C   . GLY A 1 182 ? -2.028  -2.626  10.428  1.00 17.08  ? 183 GLY A C   1 
ATOM   1454 O  O   . GLY A 1 182 ? -2.009  -3.834  10.147  1.00 19.56  ? 183 GLY A O   1 
ATOM   1455 N  N   . LEU A 1 183 ? -1.070  -2.028  11.152  1.00 15.84  ? 184 LEU A N   1 
ATOM   1456 C  CA  . LEU A 1 183 ? 0.056   -2.797  11.675  1.00 14.60  ? 184 LEU A CA  1 
ATOM   1457 C  C   . LEU A 1 183 ? -0.061  -3.035  13.177  1.00 14.34  ? 184 LEU A C   1 
ATOM   1458 O  O   . LEU A 1 183 ? 0.825   -3.654  13.777  1.00 15.97  ? 184 LEU A O   1 
ATOM   1459 C  CB  . LEU A 1 183 ? 1.359   -2.047  11.409  1.00 14.93  ? 184 LEU A CB  1 
ATOM   1460 C  CG  . LEU A 1 183 ? 1.705   -1.871  9.929   1.00 16.66  ? 184 LEU A CG  1 
ATOM   1461 C  CD1 . LEU A 1 183 ? 2.953   -1.057  9.768   1.00 18.51  ? 184 LEU A CD1 1 
ATOM   1462 C  CD2 . LEU A 1 183 ? 1.856   -3.243  9.210   1.00 20.92  ? 184 LEU A CD2 1 
ATOM   1463 N  N   . LEU A 1 184 ? -1.146  -2.544  13.797  1.00 14.91  ? 185 LEU A N   1 
ATOM   1464 C  CA  . LEU A 1 184 ? -1.296  -2.656  15.243  1.00 13.95  ? 185 LEU A CA  1 
ATOM   1465 C  C   . LEU A 1 184 ? -2.019  -3.937  15.652  1.00 17.06  ? 185 LEU A C   1 
ATOM   1466 O  O   . LEU A 1 184 ? -2.921  -4.418  14.977  1.00 22.31  ? 185 LEU A O   1 
ATOM   1467 C  CB  . LEU A 1 184 ? -2.081  -1.446  15.777  1.00 15.05  ? 185 LEU A CB  1 
ATOM   1468 C  CG  . LEU A 1 184 ? -1.508  -0.074  15.411  1.00 15.48  ? 185 LEU A CG  1 
ATOM   1469 C  CD1 . LEU A 1 184 ? -2.393  1.058   15.925  1.00 19.44  ? 185 LEU A CD1 1 
ATOM   1470 C  CD2 . LEU A 1 184 ? -0.119  0.031   15.995  1.00 19.45  ? 185 LEU A CD2 1 
ATOM   1471 N  N   . PRO A 1 185 ? -1.670  -4.515  16.828  1.00 13.88  ? 186 PRO A N   1 
ATOM   1472 C  CA  . PRO A 1 185 ? -2.442  -5.639  17.399  1.00 14.63  ? 186 PRO A CA  1 
ATOM   1473 C  C   . PRO A 1 185 ? -3.728  -5.097  17.985  1.00 15.31  ? 186 PRO A C   1 
ATOM   1474 O  O   . PRO A 1 185 ? -3.942  -3.892  18.054  1.00 18.22  ? 186 PRO A O   1 
ATOM   1475 C  CB  . PRO A 1 185 ? -1.458  -6.218  18.430  1.00 14.04  ? 186 PRO A CB  1 
ATOM   1476 C  CG  . PRO A 1 185 ? -0.759  -5.001  18.897  1.00 12.94  ? 186 PRO A CG  1 
ATOM   1477 C  CD  . PRO A 1 185 ? -0.581  -4.045  17.720  1.00 12.40  ? 186 PRO A CD  1 
ATOM   1478 N  N   . GLU A 1 186 ? -4.570  -6.017  18.478  1.00 17.40  ? 187 GLU A N   1 
ATOM   1479 C  CA  . GLU A 1 186 ? -5.853  -5.625  19.039  1.00 18.67  ? 187 GLU A CA  1 
ATOM   1480 C  C   . GLU A 1 186 ? -5.621  -4.846  20.324  1.00 16.14  ? 187 GLU A C   1 
ATOM   1481 O  O   . GLU A 1 186 ? -6.259  -3.803  20.530  1.00 20.39  ? 187 GLU A O   1 
ATOM   1482 C  CB  . GLU A 1 186 ? -6.503  -6.958  19.403  1.00 25.59  ? 187 GLU A CB  1 
ATOM   1483 C  CG  . GLU A 1 186 ? -7.930  -7.132  19.100  1.00 39.14  ? 187 GLU A CG  1 
ATOM   1484 C  CD  . GLU A 1 186 ? -8.235  -8.606  19.398  1.00 31.68  ? 187 GLU A CD  1 
ATOM   1485 O  OE1 . GLU A 1 186 ? -8.415  -9.367  18.414  1.00 48.31  ? 187 GLU A OE1 1 
ATOM   1486 O  OE2 . GLU A 1 186 ? -8.281  -8.986  20.580  1.00 51.98  ? 187 GLU A OE2 1 
ATOM   1487 N  N   . SER A 1 187 ? -4.732  -5.342  21.201  1.00 16.20  ? 188 SER A N   1 
ATOM   1488 C  CA  . SER A 1 187 ? -4.549  -4.739  22.506  1.00 15.99  ? 188 SER A CA  1 
ATOM   1489 C  C   . SER A 1 187 ? -3.441  -3.693  22.504  1.00 15.41  ? 188 SER A C   1 
ATOM   1490 O  O   . SER A 1 187 ? -2.421  -3.862  21.813  1.00 17.09  ? 188 SER A O   1 
ATOM   1491 C  CB  . SER A 1 187 ? -4.134  -5.822  23.537  1.00 19.41  ? 188 SER A CB  1 
ATOM   1492 O  OG  . SER A 1 187 ? -3.900  -5.224  24.844  1.00 19.65  ? 188 SER A OG  1 
ATOM   1493 N  N   . LEU A 1 188 ? -3.607  -2.593  23.274  1.00 16.11  ? 189 LEU A N   1 
ATOM   1494 C  CA  . LEU A 1 188 ? -2.524  -1.627  23.472  1.00 16.29  ? 189 LEU A CA  1 
ATOM   1495 C  C   . LEU A 1 188 ? -1.898  -1.757  24.868  1.00 15.39  ? 189 LEU A C   1 
ATOM   1496 O  O   . LEU A 1 188 ? -1.210  -0.832  25.318  1.00 18.07  ? 189 LEU A O   1 
ATOM   1497 C  CB  . LEU A 1 188 ? -3.063  -0.206  23.212  1.00 19.26  ? 189 LEU A CB  1 
ATOM   1498 C  CG  . LEU A 1 188 ? -3.448  0.126   21.772  1.00 21.01  ? 189 LEU A CG  1 
ATOM   1499 C  CD1 . LEU A 1 188 ? -3.920  1.568   21.666  1.00 24.14  ? 189 LEU A CD1 1 
ATOM   1500 C  CD2 . LEU A 1 188 ? -2.278  -0.128  20.830  1.00 21.87  ? 189 LEU A CD2 1 
ATOM   1501 N  N   . ASP A 1 189 ? -2.059  -2.904  25.545  1.00 15.79  ? 190 ASP A N   1 
ATOM   1502 C  CA  . ASP A 1 189 ? -1.296  -3.172  26.760  1.00 15.79  ? 190 ASP A CA  1 
ATOM   1503 C  C   . ASP A 1 189 ? 0.201   -3.122  26.476  1.00 13.08  ? 190 ASP A C   1 
ATOM   1504 O  O   . ASP A 1 189 ? 0.647   -3.611  25.413  1.00 12.99  ? 190 ASP A O   1 
ATOM   1505 C  CB  . ASP A 1 189 ? -1.652  -4.542  27.334  1.00 18.43  ? 190 ASP A CB  1 
ATOM   1506 C  CG  . ASP A 1 189 ? -3.047  -4.694  27.938  1.00 29.50  ? 190 ASP A CG  1 
ATOM   1507 O  OD1 . ASP A 1 189 ? -3.677  -3.655  28.226  1.00 32.80  ? 190 ASP A OD1 1 
ATOM   1508 O  OD2 . ASP A 1 189 ? -3.468  -5.859  28.179  1.00 36.54  ? 190 ASP A OD2 1 
ATOM   1509 N  N   . TYR A 1 190 ? 1.011   -2.556  27.411  1.00 12.68  ? 191 TYR A N   1 
ATOM   1510 C  CA  . TYR A 1 190 ? 2.417   -2.291  27.062  1.00 11.64  ? 191 TYR A CA  1 
ATOM   1511 C  C   . TYR A 1 190 ? 3.307   -2.366  28.286  1.00 11.49  ? 191 TYR A C   1 
ATOM   1512 O  O   . TYR A 1 190 ? 2.882   -2.264  29.445  1.00 13.01  ? 191 TYR A O   1 
ATOM   1513 C  CB  . TYR A 1 190 ? 2.565   -0.915  26.385  1.00 12.32  ? 191 TYR A CB  1 
ATOM   1514 C  CG  . TYR A 1 190 ? 2.155   0.239   27.278  1.00 12.59  ? 191 TYR A CG  1 
ATOM   1515 C  CD1 . TYR A 1 190 ? 3.070   0.861   28.113  1.00 13.47  ? 191 TYR A CD1 1 
ATOM   1516 C  CD2 . TYR A 1 190 ? 0.869   0.774   27.240  1.00 13.61  ? 191 TYR A CD2 1 
ATOM   1517 C  CE1 . TYR A 1 190 ? 2.702   1.908   28.960  1.00 13.50  ? 191 TYR A CE1 1 
ATOM   1518 C  CE2 . TYR A 1 190 ? 0.473   1.827   28.053  1.00 15.21  ? 191 TYR A CE2 1 
ATOM   1519 C  CZ  . TYR A 1 190 ? 1.396   2.389   28.914  1.00 14.39  ? 191 TYR A CZ  1 
ATOM   1520 O  OH  . TYR A 1 190 ? 1.067   3.415   29.752  1.00 16.55  ? 191 TYR A OH  1 
ATOM   1521 N  N   . TRP A 1 191 ? 4.600   -2.504  27.982  1.00 10.73  ? 192 TRP A N   1 
ATOM   1522 C  CA  . TRP A 1 191 ? 5.668   -2.248  28.937  1.00 10.54  ? 192 TRP A CA  1 
ATOM   1523 C  C   . TRP A 1 191 ? 6.351   -0.948  28.531  1.00 10.28  ? 192 TRP A C   1 
ATOM   1524 O  O   . TRP A 1 191 ? 6.354   -0.596  27.353  1.00 11.05  ? 192 TRP A O   1 
ATOM   1525 C  CB  . TRP A 1 191 ? 6.718   -3.361  28.935  1.00 11.53  ? 192 TRP A CB  1 
ATOM   1526 C  CG  . TRP A 1 191 ? 6.201   -4.703  29.360  1.00 11.54  ? 192 TRP A CG  1 
ATOM   1527 C  CD1 . TRP A 1 191 ? 5.955   -5.160  30.646  1.00 14.29  ? 192 TRP A CD1 1 
ATOM   1528 C  CD2 . TRP A 1 191 ? 5.910   -5.814  28.469  1.00 12.17  ? 192 TRP A CD2 1 
ATOM   1529 N  NE1 . TRP A 1 191 ? 5.535   -6.472  30.596  1.00 14.21  ? 192 TRP A NE1 1 
ATOM   1530 C  CE2 . TRP A 1 191 ? 5.518   -6.901  29.284  1.00 13.55  ? 192 TRP A CE2 1 
ATOM   1531 C  CE3 . TRP A 1 191 ? 5.997   -5.999  27.064  1.00 12.87  ? 192 TRP A CE3 1 
ATOM   1532 C  CZ2 . TRP A 1 191 ? 5.200   -8.152  28.728  1.00 13.96  ? 192 TRP A CZ2 1 
ATOM   1533 C  CZ3 . TRP A 1 191 ? 5.719   -7.244  26.527  1.00 15.18  ? 192 TRP A CZ3 1 
ATOM   1534 C  CH2 . TRP A 1 191 ? 5.296   -8.297  27.353  1.00 14.86  ? 192 TRP A CH2 1 
ATOM   1535 N  N   . THR A 1 192 ? 6.925   -0.243  29.492  1.00 10.79  ? 193 THR A N   1 
ATOM   1536 C  CA  . THR A 1 192 ? 7.670   0.967   29.167  1.00 10.60  ? 193 THR A CA  1 
ATOM   1537 C  C   . THR A 1 192 ? 8.902   1.091   30.044  1.00 9.96   ? 193 THR A C   1 
ATOM   1538 O  O   . THR A 1 192 ? 8.897   0.703   31.212  1.00 11.38  ? 193 THR A O   1 
ATOM   1539 C  CB  . THR A 1 192 ? 6.770   2.189   29.265  1.00 11.15  ? 193 THR A CB  1 
ATOM   1540 O  OG1 . THR A 1 192 ? 7.461   3.365   28.843  1.00 11.76  ? 193 THR A OG1 1 
ATOM   1541 C  CG2 . THR A 1 192 ? 6.196   2.429   30.656  1.00 12.42  ? 193 THR A CG2 1 
ATOM   1542 N  N   . TYR A 1 193 ? 9.952   1.680   29.454  1.00 10.37  ? 194 TYR A N   1 
ATOM   1543 C  CA  . TYR A 1 193 ? 11.191  1.923   30.214  1.00 11.22  ? 194 TYR A CA  1 
ATOM   1544 C  C   . TYR A 1 193 ? 11.987  2.979   29.457  1.00 9.82   ? 194 TYR A C   1 
ATOM   1545 O  O   . TYR A 1 193 ? 11.771  3.204   28.251  1.00 10.63  ? 194 TYR A O   1 
ATOM   1546 C  CB  . TYR A 1 193 ? 12.017  0.616   30.415  1.00 12.13  ? 194 TYR A CB  1 
ATOM   1547 C  CG  . TYR A 1 193 ? 12.722  0.164   29.143  1.00 9.60   ? 194 TYR A CG  1 
ATOM   1548 C  CD1 . TYR A 1 193 ? 12.062  -0.571  28.155  1.00 10.35  ? 194 TYR A CD1 1 
ATOM   1549 C  CD2 . TYR A 1 193 ? 14.058  0.478   28.959  1.00 11.20  ? 194 TYR A CD2 1 
ATOM   1550 C  CE1 . TYR A 1 193 ? 12.685  -0.907  26.959  1.00 10.38  ? 194 TYR A CE1 1 
ATOM   1551 C  CE2 . TYR A 1 193 ? 14.700  0.154   27.772  1.00 10.80  ? 194 TYR A CE2 1 
ATOM   1552 C  CZ  . TYR A 1 193 ? 14.008  -0.518  26.773  1.00 9.38   ? 194 TYR A CZ  1 
ATOM   1553 O  OH  . TYR A 1 193 ? 14.659  -0.826  25.619  1.00 9.89   ? 194 TYR A OH  1 
ATOM   1554 N  N   . PRO A 1 194 ? 12.940  3.659   30.128  1.00 11.25  ? 195 PRO A N   1 
ATOM   1555 C  CA  . PRO A 1 194 ? 13.779  4.635   29.459  1.00 12.26  ? 195 PRO A CA  1 
ATOM   1556 C  C   . PRO A 1 194 ? 14.997  3.992   28.807  1.00 10.53  ? 195 PRO A C   1 
ATOM   1557 O  O   . PRO A 1 194 ? 15.702  3.197   29.453  1.00 11.74  ? 195 PRO A O   1 
ATOM   1558 C  CB  . PRO A 1 194 ? 14.240  5.534   30.617  1.00 13.96  ? 195 PRO A CB  1 
ATOM   1559 C  CG  . PRO A 1 194 ? 14.274  4.607   31.813  1.00 15.88  ? 195 PRO A CG  1 
ATOM   1560 C  CD  . PRO A 1 194 ? 13.103  3.667   31.589  1.00 14.99  ? 195 PRO A CD  1 
ATOM   1561 N  N   . GLY A 1 195 ? 15.248  4.361   27.538  1.00 10.34  ? 196 GLY A N   1 
ATOM   1562 C  CA  . GLY A 1 195 ? 16.356  3.726   26.852  1.00 10.70  ? 196 GLY A CA  1 
ATOM   1563 C  C   . GLY A 1 195 ? 16.935  4.601   25.767  1.00 9.54   ? 196 GLY A C   1 
ATOM   1564 O  O   . GLY A 1 195 ? 17.029  5.823   25.892  1.00 10.45  ? 196 GLY A O   1 
ATOM   1565 N  N   . SER A 1 196 ? 17.327  3.911   24.686  1.00 9.77   ? 197 SER A N   1 
ATOM   1566 C  CA  . SER A 1 196 ? 18.196  4.518   23.690  1.00 9.55   ? 197 SER A CA  1 
ATOM   1567 C  C   . SER A 1 196 ? 17.739  4.131   22.294  1.00 9.31   ? 197 SER A C   1 
ATOM   1568 O  O   . SER A 1 196 ? 16.936  3.191   22.106  1.00 9.64   ? 197 SER A O   1 
ATOM   1569 C  CB  . SER A 1 196 ? 19.645  4.071   23.867  1.00 10.44  ? 197 SER A CB  1 
ATOM   1570 O  OG  . SER A 1 196 ? 19.874  2.748   23.398  1.00 10.57  ? 197 SER A OG  1 
ATOM   1571 N  N   . LEU A 1 197 ? 18.311  4.813   21.281  1.00 9.63   ? 198 LEU A N   1 
ATOM   1572 C  CA  . LEU A 1 197 ? 18.295  4.278   19.923  1.00 9.30   ? 198 LEU A CA  1 
ATOM   1573 C  C   . LEU A 1 197 ? 18.988  2.942   19.955  1.00 9.29   ? 198 LEU A C   1 
ATOM   1574 O  O   . LEU A 1 197 ? 20.039  2.779   20.630  1.00 10.60  ? 198 LEU A O   1 
ATOM   1575 C  CB  . LEU A 1 197 ? 19.047  5.261   19.009  1.00 10.58  ? 198 LEU A CB  1 
ATOM   1576 C  CG  . LEU A 1 197 ? 18.536  6.689   19.025  1.00 11.68  ? 198 LEU A CG  1 
ATOM   1577 C  CD1 . LEU A 1 197 ? 19.467  7.568   18.145  1.00 15.19  ? 198 LEU A CD1 1 
ATOM   1578 C  CD2 . LEU A 1 197 ? 17.100  6.766   18.609  1.00 12.88  ? 198 LEU A CD2 1 
ATOM   1579 N  N   . THR A 1 198 ? 18.535  1.988   19.123  1.00 9.29   ? 199 THR A N   1 
ATOM   1580 C  CA  . THR A 1 198 ? 19.177  0.678   19.091  1.00 10.13  ? 199 THR A CA  1 
ATOM   1581 C  C   . THR A 1 198 ? 20.211  0.582   17.958  1.00 10.31  ? 199 THR A C   1 
ATOM   1582 O  O   . THR A 1 198 ? 20.773  -0.494  17.805  1.00 11.67  ? 199 THR A O   1 
ATOM   1583 C  CB  . THR A 1 198 ? 18.164  -0.481  18.973  1.00 9.91   ? 199 THR A CB  1 
ATOM   1584 O  OG1 . THR A 1 198 ? 17.626  -0.426  17.640  1.00 9.46   ? 199 THR A OG1 1 
ATOM   1585 C  CG2 . THR A 1 198 ? 17.080  -0.415  20.014  1.00 11.14  ? 199 THR A CG2 1 
ATOM   1586 N  N   . THR A 1 199 ? 20.338  1.620   17.151  1.00 11.08  ? 200 THR A N   1 
ATOM   1587 C  CA  . THR A 1 199 ? 21.418  1.678   16.194  1.00 11.74  ? 200 THR A CA  1 
ATOM   1588 C  C   . THR A 1 199 ? 22.243  2.927   16.430  1.00 11.89  ? 200 THR A C   1 
ATOM   1589 O  O   . THR A 1 199 ? 21.758  3.852   17.069  1.00 12.59  ? 200 THR A O   1 
ATOM   1590 C  CB  . THR A 1 199 ? 20.941  1.688   14.747  1.00 13.34  ? 200 THR A CB  1 
ATOM   1591 O  OG1 . THR A 1 199 ? 20.348  2.915   14.370  1.00 19.37  ? 200 THR A OG1 1 
ATOM   1592 C  CG2 . THR A 1 199 ? 19.916  0.645   14.474  1.00 17.52  ? 200 THR A CG2 1 
ATOM   1593 N  N   . PRO A 1 200 ? 23.492  3.009   15.939  1.00 12.63  ? 201 PRO A N   1 
ATOM   1594 C  CA  . PRO A 1 200 ? 24.268  4.252   16.112  1.00 12.73  ? 201 PRO A CA  1 
ATOM   1595 C  C   . PRO A 1 200 ? 23.410  5.424   15.638  1.00 12.93  ? 201 PRO A C   1 
ATOM   1596 O  O   . PRO A 1 200 ? 22.703  5.327   14.629  1.00 14.31  ? 201 PRO A O   1 
ATOM   1597 C  CB  . PRO A 1 200 ? 25.429  3.959   15.131  1.00 14.75  ? 201 PRO A CB  1 
ATOM   1598 C  CG  . PRO A 1 200 ? 25.670  2.496   15.348  1.00 15.31  ? 201 PRO A CG  1 
ATOM   1599 C  CD  . PRO A 1 200 ? 24.260  1.918   15.312  1.00 14.40  ? 201 PRO A CD  1 
ATOM   1600 N  N   . PRO A 1 201 ? 23.462  6.580   16.337  1.00 12.59  ? 202 PRO A N   1 
ATOM   1601 C  CA  . PRO A 1 201 ? 24.453  6.854   17.385  1.00 12.65  ? 202 PRO A CA  1 
ATOM   1602 C  C   . PRO A 1 201 ? 24.132  6.384   18.803  1.00 11.98  ? 202 PRO A C   1 
ATOM   1603 O  O   . PRO A 1 201 ? 24.868  6.728   19.718  1.00 13.11  ? 202 PRO A O   1 
ATOM   1604 C  CB  . PRO A 1 201 ? 24.555  8.373   17.351  1.00 15.14  ? 202 PRO A CB  1 
ATOM   1605 C  CG  . PRO A 1 201 ? 23.137  8.800   16.928  1.00 15.26  ? 202 PRO A CG  1 
ATOM   1606 C  CD  . PRO A 1 201 ? 22.741  7.778   15.899  1.00 13.84  ? 202 PRO A CD  1 
ATOM   1607 N  N   . LEU A 1 202 ? 23.076  5.570   18.975  1.00 11.26  ? 203 LEU A N   1 
ATOM   1608 C  CA  . LEU A 1 202 ? 22.804  4.941   20.281  1.00 11.59  ? 203 LEU A CA  1 
ATOM   1609 C  C   . LEU A 1 202 ? 22.478  5.943   21.388  1.00 10.32  ? 203 LEU A C   1 
ATOM   1610 O  O   . LEU A 1 202 ? 22.516  5.583   22.571  1.00 11.54  ? 203 LEU A O   1 
ATOM   1611 C  CB  . LEU A 1 202 ? 23.943  4.002   20.739  1.00 12.38  ? 203 LEU A CB  1 
ATOM   1612 C  CG  . LEU A 1 202 ? 24.301  2.918   19.696  1.00 11.24  ? 203 LEU A CG  1 
ATOM   1613 C  CD1 . LEU A 1 202 ? 25.614  2.238   20.085  1.00 14.88  ? 203 LEU A CD1 1 
ATOM   1614 C  CD2 . LEU A 1 202 ? 23.200  1.903   19.540  1.00 13.15  ? 203 LEU A CD2 1 
ATOM   1615 N  N   . THR A 1 203 ? 22.012  7.131   20.989  1.00 11.88  ? 204 THR A N   1 
ATOM   1616 C  CA  . THR A 1 203 ? 21.718  8.193   21.951  1.00 11.82  ? 204 THR A CA  1 
ATOM   1617 C  C   . THR A 1 203 ? 20.605  7.777   22.920  1.00 11.64  ? 204 THR A C   1 
ATOM   1618 O  O   . THR A 1 203 ? 19.631  7.118   22.519  1.00 11.59  ? 204 THR A O   1 
ATOM   1619 C  CB  . THR A 1 203 ? 21.221  9.398   21.164  1.00 13.77  ? 204 THR A CB  1 
ATOM   1620 O  OG1 . THR A 1 203 ? 22.200  9.638   20.168  1.00 14.41  ? 204 THR A OG1 1 
ATOM   1621 C  CG2 . THR A 1 203 ? 21.107  10.642  22.010  1.00 15.25  ? 204 THR A CG2 1 
ATOM   1622 N  N   . GLU A 1 204 ? 20.732  8.182   24.185  1.00 12.46  ? 205 GLU A N   1 
ATOM   1623 C  CA  . GLU A 1 204 ? 19.806  7.800   25.251  1.00 13.00  ? 205 GLU A CA  1 
ATOM   1624 C  C   . GLU A 1 204 ? 18.648  8.804   25.287  1.00 12.89  ? 205 GLU A C   1 
ATOM   1625 O  O   . GLU A 1 204 ? 18.445  9.472   26.284  1.00 16.52  ? 205 GLU A O   1 
ATOM   1626 C  CB  . GLU A 1 204 ? 20.611  7.668   26.565  1.00 13.41  ? 205 GLU A CB  1 
ATOM   1627 C  CG  . GLU A 1 204 ? 21.565  6.482   26.441  1.00 14.55  ? 205 GLU A CG  1 
ATOM   1628 C  CD  . GLU A 1 204 ? 22.435  6.151   27.645  1.00 14.86  ? 205 GLU A CD  1 
ATOM   1629 O  OE1 . GLU A 1 204 ? 22.616  7.049   28.541  1.00 17.24  ? 205 GLU A OE1 1 
ATOM   1630 O  OE2 . GLU A 1 204 ? 22.878  4.998   27.766  1.00 14.81  ? 205 GLU A OE2 1 
ATOM   1631 N  N   . CYS A 1 205 ? 17.848  8.833   24.213  1.00 10.80  ? 206 CYS A N   1 
ATOM   1632 C  CA  . CYS A 1 205 ? 16.834  9.832   23.995  1.00 11.09  ? 206 CYS A CA  1 
ATOM   1633 C  C   . CYS A 1 205 ? 15.430  9.244   23.861  1.00 10.67  ? 206 CYS A C   1 
ATOM   1634 O  O   . CYS A 1 205 ? 14.518  9.958   23.449  1.00 12.61  ? 206 CYS A O   1 
ATOM   1635 C  CB  . CYS A 1 205 ? 17.153  10.657  22.729  1.00 12.28  ? 206 CYS A CB  1 
ATOM   1636 S  SG  . CYS A 1 205 ? 17.247  9.680   21.223  1.00 13.25  ? 206 CYS A SG  1 
ATOM   1637 N  N   . VAL A 1 206 ? 15.249  7.949   24.208  1.00 9.98   ? 207 VAL A N   1 
ATOM   1638 C  CA  . VAL A 1 206 ? 14.016  7.240   23.852  1.00 9.30   ? 207 VAL A CA  1 
ATOM   1639 C  C   . VAL A 1 206 ? 13.241  6.816   25.101  1.00 9.23   ? 207 VAL A C   1 
ATOM   1640 O  O   . VAL A 1 206 ? 13.773  6.158   26.001  1.00 11.86  ? 207 VAL A O   1 
ATOM   1641 C  CB  . VAL A 1 206 ? 14.301  5.987   23.013  1.00 9.67   ? 207 VAL A CB  1 
ATOM   1642 C  CG1 . VAL A 1 206 ? 12.956  5.296   22.661  1.00 10.02  ? 207 VAL A CG1 1 
ATOM   1643 C  CG2 . VAL A 1 206 ? 15.080  6.342   21.758  1.00 10.54  ? 207 VAL A CG2 1 
ATOM   1644 N  N   . THR A 1 207 ? 11.926  7.111   25.139  1.00 9.60   ? 208 THR A N   1 
ATOM   1645 C  CA  . THR A 1 207 ? 11.010  6.406   26.008  1.00 9.85   ? 208 THR A CA  1 
ATOM   1646 C  C   . THR A 1 207 ? 10.454  5.250   25.174  1.00 9.38   ? 208 THR A C   1 
ATOM   1647 O  O   . THR A 1 207 ? 9.826   5.449   24.133  1.00 9.77   ? 208 THR A O   1 
ATOM   1648 C  CB  . THR A 1 207 ? 9.820   7.290   26.439  1.00 10.96  ? 208 THR A CB  1 
ATOM   1649 O  OG1 . THR A 1 207 ? 10.350  8.404   27.171  1.00 12.32  ? 208 THR A OG1 1 
ATOM   1650 C  CG2 . THR A 1 207 ? 8.908   6.491   27.328  1.00 13.02  ? 208 THR A CG2 1 
ATOM   1651 N  N   . TRP A 1 208 ? 10.760  4.007   25.611  1.00 8.91   ? 209 TRP A N   1 
ATOM   1652 C  CA  . TRP A 1 208 ? 10.307  2.831   24.886  1.00 8.98   ? 209 TRP A CA  1 
ATOM   1653 C  C   . TRP A 1 208 ? 8.938   2.418   25.383  1.00 8.96   ? 209 TRP A C   1 
ATOM   1654 O  O   . TRP A 1 208 ? 8.676   2.390   26.610  1.00 10.18  ? 209 TRP A O   1 
ATOM   1655 C  CB  . TRP A 1 208 ? 11.312  1.673   25.111  1.00 9.31   ? 209 TRP A CB  1 
ATOM   1656 C  CG  . TRP A 1 208 ? 12.444  1.769   24.158  1.00 8.72   ? 209 TRP A CG  1 
ATOM   1657 C  CD1 . TRP A 1 208 ? 13.671  2.338   24.377  1.00 9.41   ? 209 TRP A CD1 1 
ATOM   1658 C  CD2 . TRP A 1 208 ? 12.392  1.366   22.778  1.00 8.36   ? 209 TRP A CD2 1 
ATOM   1659 N  NE1 . TRP A 1 208 ? 14.374  2.304   23.197  1.00 9.92   ? 209 TRP A NE1 1 
ATOM   1660 C  CE2 . TRP A 1 208 ? 13.641  1.724   22.195  1.00 9.09   ? 209 TRP A CE2 1 
ATOM   1661 C  CE3 . TRP A 1 208 ? 11.430  0.725   21.982  1.00 9.11   ? 209 TRP A CE3 1 
ATOM   1662 C  CZ2 . TRP A 1 208 ? 13.937  1.488   20.855  1.00 9.65   ? 209 TRP A CZ2 1 
ATOM   1663 C  CZ3 . TRP A 1 208 ? 11.734  0.469   20.659  1.00 10.04  ? 209 TRP A CZ3 1 
ATOM   1664 C  CH2 . TRP A 1 208 ? 12.976  0.826   20.096  1.00 10.49  ? 209 TRP A CH2 1 
ATOM   1665 N  N   . ILE A 1 209 ? 8.063   2.086   24.442  1.00 9.11   ? 210 ILE A N   1 
ATOM   1666 C  CA  . ILE A 1 209 ? 6.720   1.558   24.755  1.00 8.94   ? 210 ILE A CA  1 
ATOM   1667 C  C   . ILE A 1 209 ? 6.610   0.299   23.906  1.00 9.25   ? 210 ILE A C   1 
ATOM   1668 O  O   . ILE A 1 209 ? 6.585   0.378   22.683  1.00 10.42  ? 210 ILE A O   1 
ATOM   1669 C  CB  . ILE A 1 209 ? 5.632   2.576   24.414  1.00 10.01  ? 210 ILE A CB  1 
ATOM   1670 C  CG1 . ILE A 1 209 ? 5.850   3.856   25.226  1.00 12.11  ? 210 ILE A CG1 1 
ATOM   1671 C  CG2 . ILE A 1 209 ? 4.242   1.966   24.658  1.00 11.94  ? 210 ILE A CG2 1 
ATOM   1672 C  CD1 . ILE A 1 209 ? 5.019   5.030   24.799  1.00 14.37  ? 210 ILE A CD1 1 
ATOM   1673 N  N   . VAL A 1 210 ? 6.634   -0.865  24.563  1.00 9.50   ? 211 VAL A N   1 
ATOM   1674 C  CA  . VAL A 1 210 ? 6.659   -2.144  23.838  1.00 9.09   ? 211 VAL A CA  1 
ATOM   1675 C  C   . VAL A 1 210 ? 5.332   -2.865  24.088  1.00 9.12   ? 211 VAL A C   1 
ATOM   1676 O  O   . VAL A 1 210 ? 4.960   -3.102  25.227  1.00 10.50  ? 211 VAL A O   1 
ATOM   1677 C  CB  . VAL A 1 210 ? 7.838   -3.010  24.280  1.00 9.69   ? 211 VAL A CB  1 
ATOM   1678 C  CG1 . VAL A 1 210 ? 7.768   -4.358  23.581  1.00 10.56  ? 211 VAL A CG1 1 
ATOM   1679 C  CG2 . VAL A 1 210 ? 9.160   -2.304  23.984  1.00 11.43  ? 211 VAL A CG2 1 
ATOM   1680 N  N   . LEU A 1 211 ? 4.593   -3.131  23.012  1.00 10.18  ? 212 LEU A N   1 
ATOM   1681 C  CA  . LEU A 1 211 ? 3.272   -3.739  23.186  1.00 11.07  ? 212 LEU A CA  1 
ATOM   1682 C  C   . LEU A 1 211 ? 3.430   -5.198  23.572  1.00 11.36  ? 212 LEU A C   1 
ATOM   1683 O  O   . LEU A 1 211 ? 4.270   -5.939  23.068  1.00 11.19  ? 212 LEU A O   1 
ATOM   1684 C  CB  . LEU A 1 211 ? 2.454   -3.623  21.901  1.00 10.85  ? 212 LEU A CB  1 
ATOM   1685 C  CG  . LEU A 1 211 ? 2.084   -2.212  21.444  1.00 11.73  ? 212 LEU A CG  1 
ATOM   1686 C  CD1 . LEU A 1 211 ? 1.074   -2.206  20.276  1.00 14.13  ? 212 LEU A CD1 1 
ATOM   1687 C  CD2 . LEU A 1 211 ? 1.591   -1.357  22.609  1.00 13.72  ? 212 LEU A CD2 1 
ATOM   1688 N  N   . LYS A 1 212 ? 2.542   -5.646  24.472  1.00 12.04  ? 213 LYS A N   1 
ATOM   1689 C  CA  . LYS A 1 212 ? 2.563   -7.040  24.916  1.00 13.56  ? 213 LYS A CA  1 
ATOM   1690 C  C   . LYS A 1 212 ? 2.103   -8.007  23.842  1.00 12.97  ? 213 LYS A C   1 
ATOM   1691 O  O   . LYS A 1 212 ? 2.631   -9.108  23.738  1.00 15.61  ? 213 LYS A O   1 
ATOM   1692 C  CB  . LYS A 1 212 ? 1.630   -7.122  26.118  1.00 17.70  ? 213 LYS A CB  1 
ATOM   1693 C  CG  . LYS A 1 212 ? 1.258   -8.523  26.577  1.00 26.29  ? 213 LYS A CG  1 
ATOM   1694 C  CD  . LYS A 1 212 ? 0.136   -8.505  27.619  1.00 37.74  ? 213 LYS A CD  1 
ATOM   1695 C  CE  . LYS A 1 212 ? -1.288  -8.786  27.153  1.00 40.68  ? 213 LYS A CE  1 
ATOM   1696 N  NZ  . LYS A 1 212 ? -1.783  -7.957  26.014  1.00 50.10  ? 213 LYS A NZ  1 
ATOM   1697 N  N   . GLU A 1 213 ? 1.128   -7.622  23.011  1.00 12.26  ? 214 GLU A N   1 
ATOM   1698 C  CA  . GLU A 1 213 ? 0.560   -8.549  22.046  1.00 12.73  ? 214 GLU A CA  1 
ATOM   1699 C  C   . GLU A 1 213 ? 1.325   -8.452  20.735  1.00 11.63  ? 214 GLU A C   1 
ATOM   1700 O  O   . GLU A 1 213 ? 1.408   -7.371  20.132  1.00 11.72  ? 214 GLU A O   1 
ATOM   1701 C  CB  . GLU A 1 213 ? -0.901  -8.165  21.786  1.00 13.73  ? 214 GLU A CB  1 
ATOM   1702 C  CG  . GLU A 1 213 ? -1.583  -9.128  20.873  1.00 17.61  ? 214 GLU A CG  1 
ATOM   1703 C  CD  . GLU A 1 213 ? -3.040  -8.857  20.583  1.00 26.33  ? 214 GLU A CD  1 
ATOM   1704 O  OE1 . GLU A 1 213 ? -3.669  -8.029  21.247  1.00 21.27  ? 214 GLU A OE1 1 
ATOM   1705 O  OE2 . GLU A 1 213 ? -3.581  -9.578  19.712  1.00 43.80  ? 214 GLU A OE2 1 
ATOM   1706 N  N   A PRO A 1 214 ? 1.870   -9.572  20.221  0.50 11.64  ? 215 PRO A N   1 
ATOM   1707 N  N   B PRO A 1 214 ? 1.964   -9.537  20.267  0.50 11.96  ? 215 PRO A N   1 
ATOM   1708 C  CA  A PRO A 1 214 ? 2.541   -9.523  18.934  0.50 11.37  ? 215 PRO A CA  1 
ATOM   1709 C  CA  B PRO A 1 214 ? 2.591   -9.514  18.949  0.50 11.79  ? 215 PRO A CA  1 
ATOM   1710 C  C   A PRO A 1 214 ? 1.501   -9.464  17.838  0.50 12.59  ? 215 PRO A C   1 
ATOM   1711 C  C   B PRO A 1 214 ? 1.544   -9.482  17.850  0.50 12.56  ? 215 PRO A C   1 
ATOM   1712 O  O   A PRO A 1 214 ? 0.346   -9.838  18.032  0.50 14.89  ? 215 PRO A O   1 
ATOM   1713 O  O   B PRO A 1 214 ? 0.399   -9.868  18.060  0.50 14.87  ? 215 PRO A O   1 
ATOM   1714 C  CB  A PRO A 1 214 ? 3.252   -10.867 18.789  0.50 12.62  ? 215 PRO A CB  1 
ATOM   1715 C  CB  B PRO A 1 214 ? 3.375   -10.824 18.862  0.50 13.42  ? 215 PRO A CB  1 
ATOM   1716 C  CG  A PRO A 1 214 ? 2.398   -11.793 19.644  0.50 15.33  ? 215 PRO A CG  1 
ATOM   1717 C  CG  B PRO A 1 214 ? 3.498   -11.243 20.330  0.50 18.55  ? 215 PRO A CG  1 
ATOM   1718 C  CD  A PRO A 1 214 ? 1.861   -10.937 20.791  0.50 14.27  ? 215 PRO A CD  1 
ATOM   1719 C  CD  B PRO A 1 214 ? 2.222   -10.789 21.008  0.50 15.16  ? 215 PRO A CD  1 
ATOM   1720 N  N   . ILE A 1 215 ? 1.937   -9.011  16.667  1.00 12.80  ? 216 ILE A N   1 
ATOM   1721 C  CA  . ILE A 1 215 ? 1.138   -9.215  15.462  1.00 13.38  ? 216 ILE A CA  1 
ATOM   1722 C  C   . ILE A 1 215 ? 1.641   -10.473 14.774  1.00 12.35  ? 216 ILE A C   1 
ATOM   1723 O  O   . ILE A 1 215 ? 2.802   -10.874 14.904  1.00 13.78  ? 216 ILE A O   1 
ATOM   1724 C  CB  . ILE A 1 215 ? 1.143   -7.995  14.502  1.00 12.59  ? 216 ILE A CB  1 
ATOM   1725 C  CG1 . ILE A 1 215 ? 2.578   -7.691  14.022  1.00 12.91  ? 216 ILE A CG1 1 
ATOM   1726 C  CG2 . ILE A 1 215 ? 0.458   -6.803  15.224  1.00 15.99  ? 216 ILE A CG2 1 
ATOM   1727 C  CD1 . ILE A 1 215 ? 2.595   -6.666  12.866  1.00 15.15  ? 216 ILE A CD1 1 
ATOM   1728 N  N   A SER A 1 216 ? 0.732   -11.050 13.987  0.50 13.15  ? 217 SER A N   1 
ATOM   1729 N  N   B SER A 1 216 ? 0.744   -11.194 14.101  0.50 14.31  ? 217 SER A N   1 
ATOM   1730 C  CA  A SER A 1 216 ? 1.061   -12.239 13.203  0.50 12.97  ? 217 SER A CA  1 
ATOM   1731 C  CA  B SER A 1 216 ? 1.232   -12.329 13.309  0.50 15.13  ? 217 SER A CA  1 
ATOM   1732 C  C   A SER A 1 216 ? 1.323   -11.837 11.761  0.50 12.40  ? 217 SER A C   1 
ATOM   1733 C  C   B SER A 1 216 ? 1.360   -11.880 11.863  0.50 12.37  ? 217 SER A C   1 
ATOM   1734 O  O   A SER A 1 216 ? 0.530   -11.084 11.166  0.50 14.20  ? 217 SER A O   1 
ATOM   1735 O  O   B SER A 1 216 ? 0.503   -11.128 11.373  0.50 16.01  ? 217 SER A O   1 
ATOM   1736 C  CB  A SER A 1 216 ? -0.046  -13.259 13.265  0.50 14.36  ? 217 SER A CB  1 
ATOM   1737 C  CB  B SER A 1 216 ? 0.330   -13.530 13.389  0.50 20.29  ? 217 SER A CB  1 
ATOM   1738 O  OG  A SER A 1 216 ? -0.061  -13.893 14.525  0.50 19.19  ? 217 SER A OG  1 
ATOM   1739 O  OG  B SER A 1 216 ? -0.964  -13.151 12.973  0.50 25.32  ? 217 SER A OG  1 
ATOM   1740 N  N   . VAL A 1 217 ? 2.446   -12.321 11.218  1.00 13.60  ? 218 VAL A N   1 
ATOM   1741 C  CA  . VAL A 1 217 ? 2.700   -12.119 9.809   1.00 13.31  ? 218 VAL A CA  1 
ATOM   1742 C  C   . VAL A 1 217 ? 2.951   -13.487 9.183   1.00 13.68  ? 218 VAL A C   1 
ATOM   1743 O  O   . VAL A 1 217 ? 3.321   -14.440 9.901   1.00 14.14  ? 218 VAL A O   1 
ATOM   1744 C  CB  . VAL A 1 217 ? 3.884   -11.172 9.585   1.00 13.90  ? 218 VAL A CB  1 
ATOM   1745 C  CG1 . VAL A 1 217 ? 3.625   -9.852  10.318  1.00 14.71  ? 218 VAL A CG1 1 
ATOM   1746 C  CG2 . VAL A 1 217 ? 5.194   -11.803 10.073  1.00 16.85  ? 218 VAL A CG2 1 
ATOM   1747 N  N   . SER A 1 218 ? 2.840   -13.626 7.867   1.00 13.81  ? 219 SER A N   1 
ATOM   1748 C  CA  . SER A 1 218 ? 3.021   -14.967 7.305   1.00 13.92  ? 219 SER A CA  1 
ATOM   1749 C  C   . SER A 1 218 ? 4.507   -15.222 7.051   1.00 14.06  ? 219 SER A C   1 
ATOM   1750 O  O   . SER A 1 218 ? 5.319   -14.282 6.932   1.00 14.41  ? 219 SER A O   1 
ATOM   1751 C  CB  . SER A 1 218 ? 2.223   -15.159 6.064   1.00 16.12  ? 219 SER A CB  1 
ATOM   1752 O  OG  . SER A 1 218 ? 2.720   -14.270 5.068   1.00 17.16  ? 219 SER A OG  1 
ATOM   1753 N  N   . SER A 1 219 ? 4.851   -16.497 6.902   1.00 14.71  ? 220 SER A N   1 
ATOM   1754 C  CA  . SER A 1 219 ? 6.225   -16.841 6.572   1.00 15.41  ? 220 SER A CA  1 
ATOM   1755 C  C   . SER A 1 219 ? 6.610   -16.165 5.262   1.00 14.94  ? 220 SER A C   1 
ATOM   1756 O  O   . SER A 1 219 ? 7.739   -15.710 5.130   1.00 17.80  ? 220 SER A O   1 
ATOM   1757 C  CB  . SER A 1 219 ? 6.420   -18.348 6.494   1.00 20.71  ? 220 SER A CB  1 
ATOM   1758 O  OG  . SER A 1 219 ? 5.420   -18.915 5.704   1.00 23.25  ? 220 SER A OG  1 
ATOM   1759 N  N   . GLU A 1 220 ? 5.662   -16.039 4.311   1.00 16.25  ? 221 GLU A N   1 
ATOM   1760 C  CA  . GLU A 1 220 ? 5.952   -15.405 3.039   1.00 17.50  ? 221 GLU A CA  1 
ATOM   1761 C  C   . GLU A 1 220 ? 6.262   -13.922 3.208   1.00 16.72  ? 221 GLU A C   1 
ATOM   1762 O  O   . GLU A 1 220 ? 7.084   -13.361 2.468   1.00 18.80  ? 221 GLU A O   1 
ATOM   1763 C  CB  . GLU A 1 220 ? 4.828   -15.588 2.013   1.00 21.66  ? 221 GLU A CB  1 
ATOM   1764 C  CG  . GLU A 1 220 ? 4.668   -17.039 1.576   1.00 26.71  ? 221 GLU A CG  1 
ATOM   1765 C  CD  . GLU A 1 220 ? 3.779   -17.894 2.481   1.00 28.27  ? 221 GLU A CD  1 
ATOM   1766 O  OE1 . GLU A 1 220 ? 3.194   -17.388 3.494   1.00 25.87  ? 221 GLU A OE1 1 
ATOM   1767 O  OE2 . GLU A 1 220 ? 3.659   -19.080 2.203   1.00 40.88  ? 221 GLU A OE2 1 
ATOM   1768 N  N   . GLN A 1 221 ? 5.532   -13.253 4.100   1.00 15.21  ? 222 GLN A N   1 
ATOM   1769 C  CA  . GLN A 1 221 ? 5.785   -11.839 4.310   1.00 14.45  ? 222 GLN A CA  1 
ATOM   1770 C  C   . GLN A 1 221 ? 7.211   -11.630 4.823   1.00 14.83  ? 222 GLN A C   1 
ATOM   1771 O  O   . GLN A 1 221 ? 7.956   -10.760 4.317   1.00 15.45  ? 222 GLN A O   1 
ATOM   1772 C  CB  . GLN A 1 221 ? 4.738   -11.249 5.250   1.00 14.83  ? 222 GLN A CB  1 
ATOM   1773 C  CG  . GLN A 1 221 ? 3.392   -11.125 4.520   1.00 15.94  ? 222 GLN A CG  1 
ATOM   1774 C  CD  . GLN A 1 221 ? 2.282   -10.579 5.396   1.00 14.68  ? 222 GLN A CD  1 
ATOM   1775 O  OE1 . GLN A 1 221 ? 2.151   -10.966 6.573   1.00 14.08  ? 222 GLN A OE1 1 
ATOM   1776 N  NE2 . GLN A 1 221 ? 1.461   -9.702  4.815   1.00 15.44  ? 222 GLN A NE2 1 
ATOM   1777 N  N   . VAL A 1 222 ? 7.613   -12.406 5.842   1.00 14.04  ? 223 VAL A N   1 
ATOM   1778 C  CA  . VAL A 1 222 ? 8.935   -12.162 6.402   1.00 15.58  ? 223 VAL A CA  1 
ATOM   1779 C  C   . VAL A 1 222 ? 10.019  -12.613 5.418   1.00 15.31  ? 223 VAL A C   1 
ATOM   1780 O  O   . VAL A 1 222 ? 11.093  -12.010 5.363   1.00 16.22  ? 223 VAL A O   1 
ATOM   1781 C  CB  . VAL A 1 222 ? 9.100   -12.770 7.803   1.00 18.94  ? 223 VAL A CB  1 
ATOM   1782 C  CG1 . VAL A 1 222 ? 9.069   -14.259 7.778   1.00 22.88  ? 223 VAL A CG1 1 
ATOM   1783 C  CG2 . VAL A 1 222 ? 10.373  -12.274 8.496   1.00 20.83  ? 223 VAL A CG2 1 
ATOM   1784 N  N   A LEU A 1 223 ? 9.767   -13.673 4.628   0.50 15.98  ? 224 LEU A N   1 
ATOM   1785 N  N   B LEU A 1 223 ? 9.718   -13.670 4.651   0.50 16.19  ? 224 LEU A N   1 
ATOM   1786 C  CA  A LEU A 1 223 ? 10.728  -14.050 3.601   0.50 17.72  ? 224 LEU A CA  1 
ATOM   1787 C  CA  B LEU A 1 223 ? 10.621  -14.085 3.598   0.50 18.74  ? 224 LEU A CA  1 
ATOM   1788 C  C   A LEU A 1 223 ? 11.041  -12.891 2.649   0.50 17.88  ? 224 LEU A C   1 
ATOM   1789 C  C   B LEU A 1 223 ? 11.004  -12.925 2.673   0.50 16.99  ? 224 LEU A C   1 
ATOM   1790 O  O   A LEU A 1 223 ? 12.171  -12.777 2.164   0.50 17.52  ? 224 LEU A O   1 
ATOM   1791 O  O   B LEU A 1 223 ? 12.156  -12.845 2.236   0.50 18.59  ? 224 LEU A O   1 
ATOM   1792 C  CB  A LEU A 1 223 ? 10.171  -15.230 2.797   0.50 22.95  ? 224 LEU A CB  1 
ATOM   1793 C  CB  B LEU A 1 223 ? 9.969   -15.197 2.774   0.50 22.22  ? 224 LEU A CB  1 
ATOM   1794 C  CG  A LEU A 1 223 ? 10.212  -16.570 3.517   0.50 23.07  ? 224 LEU A CG  1 
ATOM   1795 C  CG  B LEU A 1 223 ? 10.980  -15.899 1.880   0.50 25.30  ? 224 LEU A CG  1 
ATOM   1796 C  CD1 A LEU A 1 223 ? 9.387   -17.609 2.772   0.50 26.07  ? 224 LEU A CD1 1 
ATOM   1797 C  CD1 B LEU A 1 223 ? 12.195  -16.277 2.724   0.50 28.42  ? 224 LEU A CD1 1 
ATOM   1798 C  CD2 A LEU A 1 223 ? 11.645  -17.044 3.692   0.50 27.22  ? 224 LEU A CD2 1 
ATOM   1799 C  CD2 B LEU A 1 223 ? 10.367  -17.142 1.265   0.50 30.27  ? 224 LEU A CD2 1 
ATOM   1800 N  N   . LYS A 1 224 ? 10.039  -12.060 2.329   1.00 16.35  ? 225 LYS A N   1 
ATOM   1801 C  CA  . LYS A 1 224 ? 10.259  -10.941 1.421   1.00 17.77  ? 225 LYS A CA  1 
ATOM   1802 C  C   . LYS A 1 224 ? 11.147  -9.883  2.101   1.00 16.00  ? 225 LYS A C   1 
ATOM   1803 O  O   . LYS A 1 224 ? 11.958  -9.243  1.433   1.00 16.49  ? 225 LYS A O   1 
ATOM   1804 C  CB  . LYS A 1 224 ? 8.931   -10.400 0.867   1.00 20.59  ? 225 LYS A CB  1 
ATOM   1805 C  CG  . LYS A 1 224 ? 8.207   -11.371 -0.082  1.00 27.48  ? 225 LYS A CG  1 
ATOM   1806 C  CD  . LYS A 1 224 ? 7.227   -10.720 -1.051  1.00 39.46  ? 225 LYS A CD  1 
ATOM   1807 C  CE  . LYS A 1 224 ? 7.003   -11.477 -2.341  1.00 54.77  ? 225 LYS A CE  1 
ATOM   1808 N  NZ  . LYS A 1 224 ? 5.913   -12.472 -2.174  1.00 55.01  ? 225 LYS A NZ  1 
ATOM   1809 N  N   . PHE A 1 225 ? 11.064  -9.681  3.427   1.00 13.91  ? 226 PHE A N   1 
ATOM   1810 C  CA  . PHE A 1 225 ? 12.016  -8.815  4.107   1.00 13.52  ? 226 PHE A CA  1 
ATOM   1811 C  C   . PHE A 1 225 ? 13.439  -9.305  3.871   1.00 15.01  ? 226 PHE A C   1 
ATOM   1812 O  O   . PHE A 1 225 ? 14.342  -8.509  3.676   1.00 15.08  ? 226 PHE A O   1 
ATOM   1813 C  CB  . PHE A 1 225 ? 11.834  -8.825  5.645   1.00 14.25  ? 226 PHE A CB  1 
ATOM   1814 C  CG  . PHE A 1 225 ? 10.610  -8.150  6.221   1.00 14.25  ? 226 PHE A CG  1 
ATOM   1815 C  CD1 . PHE A 1 225 ? 9.563   -7.634  5.450   1.00 17.58  ? 226 PHE A CD1 1 
ATOM   1816 C  CD2 . PHE A 1 225 ? 10.563  -7.936  7.592   1.00 16.65  ? 226 PHE A CD2 1 
ATOM   1817 C  CE1 . PHE A 1 225 ? 8.473   -6.966  6.032   1.00 17.50  ? 226 PHE A CE1 1 
ATOM   1818 C  CE2 . PHE A 1 225 ? 9.473   -7.297  8.172   1.00 18.00  ? 226 PHE A CE2 1 
ATOM   1819 C  CZ  . PHE A 1 225 ? 8.460   -6.792  7.393   1.00 17.50  ? 226 PHE A CZ  1 
ATOM   1820 N  N   . ARG A 1 226 ? 13.633  -10.635 3.892   1.00 14.30  ? 227 ARG A N   1 
ATOM   1821 C  CA  . ARG A 1 226 ? 14.964  -11.214 3.839   1.00 15.11  ? 227 ARG A CA  1 
ATOM   1822 C  C   . ARG A 1 226 ? 15.533  -11.214 2.415   1.00 15.16  ? 227 ARG A C   1 
ATOM   1823 O  O   . ARG A 1 226 ? 16.724  -11.591 2.255   1.00 18.65  ? 227 ARG A O   1 
ATOM   1824 C  CB  . ARG A 1 226 ? 14.933  -12.672 4.333   1.00 14.94  ? 227 ARG A CB  1 
ATOM   1825 C  CG  . ARG A 1 226 ? 14.471  -12.823 5.776   1.00 15.29  ? 227 ARG A CG  1 
ATOM   1826 C  CD  . ARG A 1 226 ? 14.576  -14.270 6.198   1.00 16.70  ? 227 ARG A CD  1 
ATOM   1827 N  NE  . ARG A 1 226 ? 13.965  -14.420 7.527   1.00 15.63  ? 227 ARG A NE  1 
ATOM   1828 C  CZ  . ARG A 1 226 ? 12.989  -15.241 7.843   1.00 15.55  ? 227 ARG A CZ  1 
ATOM   1829 N  NH1 . ARG A 1 226 ? 12.479  -16.017 6.884   1.00 21.85  ? 227 ARG A NH1 1 
ATOM   1830 N  NH2 . ARG A 1 226 ? 12.474  -15.250 9.058   1.00 16.97  ? 227 ARG A NH2 1 
ATOM   1831 N  N   . LYS A 1 227 ? 14.759  -10.726 1.419   1.00 15.13  ? 228 LYS A N   1 
ATOM   1832 C  CA  . LYS A 1 227 ? 15.313  -10.609 0.071   1.00 18.06  ? 228 LYS A CA  1 
ATOM   1833 C  C   . LYS A 1 227 ? 15.923  -9.224  -0.153  1.00 18.06  ? 228 LYS A C   1 
ATOM   1834 O  O   . LYS A 1 227 ? 16.591  -9.029  -1.161  1.00 19.08  ? 228 LYS A O   1 
ATOM   1835 C  CB  . LYS A 1 227 ? 14.189  -10.839 -0.941  1.00 18.53  ? 228 LYS A CB  1 
ATOM   1836 C  CG  . LYS A 1 227 ? 13.675  -12.268 -0.992  1.00 22.98  ? 228 LYS A CG  1 
ATOM   1837 C  CD  . LYS A 1 227 ? 12.524  -12.443 -1.986  1.00 27.39  ? 228 LYS A CD  1 
ATOM   1838 C  CE  . LYS A 1 227 ? 12.914  -12.782 -3.417  1.00 46.23  ? 228 LYS A CE  1 
ATOM   1839 N  NZ  . LYS A 1 227 ? 12.530  -14.168 -3.785  1.00 60.49  ? 228 LYS A NZ  1 
ATOM   1840 N  N   . LEU A 1 228 ? 15.685  -8.281  0.792   1.00 16.23  ? 229 LEU A N   1 
ATOM   1841 C  CA  . LEU A 1 228 ? 16.327  -6.989  0.726   1.00 15.99  ? 229 LEU A CA  1 
ATOM   1842 C  C   . LEU A 1 228 ? 17.833  -7.156  0.867   1.00 17.34  ? 229 LEU A C   1 
ATOM   1843 O  O   . LEU A 1 228 ? 18.328  -8.214  1.253   1.00 16.08  ? 229 LEU A O   1 
ATOM   1844 C  CB  . LEU A 1 228 ? 15.833  -6.059  1.824   1.00 14.31  ? 229 LEU A CB  1 
ATOM   1845 C  CG  . LEU A 1 228 ? 14.400  -5.585  1.622   1.00 15.55  ? 229 LEU A CG  1 
ATOM   1846 C  CD1 . LEU A 1 228 ? 13.914  -4.958  2.931   1.00 17.19  ? 229 LEU A CD1 1 
ATOM   1847 C  CD2 . LEU A 1 228 ? 14.307  -4.606  0.453   1.00 17.69  ? 229 LEU A CD2 1 
ATOM   1848 N  N   . ASN A 1 229 ? 18.573  -6.117  0.452   1.00 16.17  ? 230 ASN A N   1 
ATOM   1849 C  CA  . ASN A 1 229 ? 20.017  -6.141  0.477   1.00 15.88  ? 230 ASN A CA  1 
ATOM   1850 C  C   . ASN A 1 229 ? 20.565  -4.995  1.328   1.00 16.33  ? 230 ASN A C   1 
ATOM   1851 O  O   . ASN A 1 229 ? 20.080  -3.868  1.285   1.00 17.48  ? 230 ASN A O   1 
ATOM   1852 C  CB  . ASN A 1 229 ? 20.638  -5.936  -0.913  1.00 19.09  ? 230 ASN A CB  1 
ATOM   1853 C  CG  . ASN A 1 229 ? 20.578  -7.095  -1.877  1.00 20.18  ? 230 ASN A CG  1 
ATOM   1854 O  OD1 . ASN A 1 229 ? 21.112  -6.944  -2.985  1.00 26.53  ? 230 ASN A OD1 1 
ATOM   1855 N  ND2 . ASN A 1 229 ? 20.003  -8.226  -1.496  1.00 21.86  ? 230 ASN A ND2 1 
ATOM   1856 N  N   . PHE A 1 230 ? 21.644  -5.319  2.063   1.00 16.76  ? 231 PHE A N   1 
ATOM   1857 C  CA  . PHE A 1 230 ? 22.342  -4.246  2.772   1.00 16.52  ? 231 PHE A CA  1 
ATOM   1858 C  C   . PHE A 1 230 ? 23.171  -3.348  1.851   1.00 18.71  ? 231 PHE A C   1 
ATOM   1859 O  O   . PHE A 1 230 ? 23.395  -2.151  2.107   1.00 20.49  ? 231 PHE A O   1 
ATOM   1860 C  CB  . PHE A 1 230 ? 23.341  -4.840  3.759   1.00 17.07  ? 231 PHE A CB  1 
ATOM   1861 C  CG  . PHE A 1 230 ? 22.798  -5.436  5.053   1.00 16.62  ? 231 PHE A CG  1 
ATOM   1862 C  CD1 . PHE A 1 230 ? 22.071  -4.672  5.970   1.00 16.65  ? 231 PHE A CD1 1 
ATOM   1863 C  CD2 . PHE A 1 230 ? 23.102  -6.760  5.403   1.00 18.11  ? 231 PHE A CD2 1 
ATOM   1864 C  CE1 . PHE A 1 230 ? 21.635  -5.193  7.182   1.00 17.29  ? 231 PHE A CE1 1 
ATOM   1865 C  CE2 . PHE A 1 230 ? 22.620  -7.303  6.599   1.00 18.39  ? 231 PHE A CE2 1 
ATOM   1866 C  CZ  . PHE A 1 230 ? 21.955  -6.495  7.522   1.00 16.12  ? 231 PHE A CZ  1 
ATOM   1867 N  N   . ASN A 1 231 ? 23.687  -3.955  0.786   1.00 17.35  ? 232 ASN A N   1 
ATOM   1868 C  CA  . ASN A 1 231 ? 24.543  -3.310  -0.192  1.00 18.37  ? 232 ASN A CA  1 
ATOM   1869 C  C   . ASN A 1 231 ? 23.746  -2.386  -1.114  1.00 18.97  ? 232 ASN A C   1 
ATOM   1870 O  O   . ASN A 1 231 ? 22.532  -2.511  -1.340  1.00 19.43  ? 232 ASN A O   1 
ATOM   1871 C  CB  . ASN A 1 231 ? 25.237  -4.380  -1.017  1.00 20.87  ? 232 ASN A CB  1 
ATOM   1872 C  CG  . ASN A 1 231 ? 24.256  -5.313  -1.684  1.00 19.70  ? 232 ASN A CG  1 
ATOM   1873 O  OD1 . ASN A 1 231 ? 23.772  -6.263  -1.043  1.00 22.83  ? 232 ASN A OD1 1 
ATOM   1874 N  ND2 . ASN A 1 231 ? 24.002  -5.081  -2.985  1.00 21.14  ? 232 ASN A ND2 1 
ATOM   1875 N  N   . GLY A 1 232 ? 24.520  -1.504  -1.795  1.00 19.55  ? 233 GLY A N   1 
ATOM   1876 C  CA  . GLY A 1 232 ? 23.978  -0.701  -2.876  1.00 20.38  ? 233 GLY A CA  1 
ATOM   1877 C  C   . GLY A 1 232 ? 23.952  -1.484  -4.179  1.00 20.61  ? 233 GLY A C   1 
ATOM   1878 O  O   . GLY A 1 232 ? 24.635  -2.493  -4.298  1.00 21.03  ? 233 GLY A O   1 
ATOM   1879 N  N   . GLU A 1 233 ? 23.213  -0.965  -5.163  1.00 19.81  ? 234 GLU A N   1 
ATOM   1880 C  CA  . GLU A 1 233 ? 23.211  -1.549  -6.496  1.00 20.08  ? 234 GLU A CA  1 
ATOM   1881 C  C   . GLU A 1 233 ? 24.628  -1.591  -7.063  1.00 19.63  ? 234 GLU A C   1 
ATOM   1882 O  O   . GLU A 1 233 ? 25.385  -0.632  -6.968  1.00 22.23  ? 234 GLU A O   1 
ATOM   1883 C  CB  . GLU A 1 233 ? 22.279  -0.739  -7.403  1.00 21.77  ? 234 GLU A CB  1 
ATOM   1884 C  CG  . GLU A 1 233 ? 22.100  -1.338  -8.794  1.00 23.51  ? 234 GLU A CG  1 
ATOM   1885 C  CD  . GLU A 1 233 ? 21.266  -0.490  -9.723  1.00 37.60  ? 234 GLU A CD  1 
ATOM   1886 O  OE1 . GLU A 1 233 ? 20.868  0.661   -9.313  1.00 36.89  ? 234 GLU A OE1 1 
ATOM   1887 O  OE2 . GLU A 1 233 ? 21.013  -0.985  -10.843 1.00 34.63  ? 234 GLU A OE2 1 
ATOM   1888 N  N   . GLY A 1 234 ? 24.984  -2.736  -7.632  1.00 24.36  ? 235 GLY A N   1 
ATOM   1889 C  CA  . GLY A 1 234 ? 26.268  -2.866  -8.306  1.00 26.65  ? 235 GLY A CA  1 
ATOM   1890 C  C   . GLY A 1 234 ? 27.369  -3.358  -7.366  1.00 28.60  ? 235 GLY A C   1 
ATOM   1891 O  O   . GLY A 1 234 ? 28.490  -3.625  -7.809  1.00 33.71  ? 235 GLY A O   1 
ATOM   1892 N  N   . GLU A 1 235 ? 27.053  -3.518  -6.070  1.00 26.72  ? 236 GLU A N   1 
ATOM   1893 C  CA  . GLU A 1 235 ? 28.006  -4.059  -5.098  1.00 23.68  ? 236 GLU A CA  1 
ATOM   1894 C  C   . GLU A 1 235 ? 27.654  -5.518  -4.836  1.00 27.10  ? 236 GLU A C   1 
ATOM   1895 O  O   . GLU A 1 235 ? 26.560  -6.005  -5.172  1.00 25.93  ? 236 GLU A O   1 
ATOM   1896 C  CB  . GLU A 1 235 ? 27.906  -3.321  -3.750  1.00 22.86  ? 236 GLU A CB  1 
ATOM   1897 C  CG  . GLU A 1 235 ? 28.358  -1.855  -3.792  1.00 29.88  ? 236 GLU A CG  1 
ATOM   1898 C  CD  . GLU A 1 235 ? 28.170  -1.029  -2.514  1.00 40.02  ? 236 GLU A CD  1 
ATOM   1899 O  OE1 . GLU A 1 235 ? 27.384  -1.452  -1.576  1.00 38.99  ? 236 GLU A OE1 1 
ATOM   1900 O  OE2 . GLU A 1 235 ? 28.821  0.042   -2.420  1.00 47.63  ? 236 GLU A OE2 1 
ATOM   1901 N  N   . PRO A 1 236 ? 28.576  -6.279  -4.229  1.00 21.41  ? 237 PRO A N   1 
ATOM   1902 C  CA  . PRO A 1 236 ? 28.320  -7.677  -3.942  1.00 22.74  ? 237 PRO A CA  1 
ATOM   1903 C  C   . PRO A 1 236 ? 27.065  -7.770  -3.076  1.00 21.28  ? 237 PRO A C   1 
ATOM   1904 O  O   . PRO A 1 236 ? 26.851  -7.040  -2.100  1.00 21.61  ? 237 PRO A O   1 
ATOM   1905 C  CB  . PRO A 1 236 ? 29.530  -8.112  -3.141  1.00 22.57  ? 237 PRO A CB  1 
ATOM   1906 C  CG  . PRO A 1 236 ? 30.599  -7.150  -3.543  1.00 22.59  ? 237 PRO A CG  1 
ATOM   1907 C  CD  . PRO A 1 236 ? 29.914  -5.832  -3.828  1.00 26.00  ? 237 PRO A CD  1 
ATOM   1908 N  N   . GLU A 1 237 ? 26.271  -8.789  -3.377  1.00 19.94  ? 238 GLU A N   1 
ATOM   1909 C  CA  . GLU A 1 237 ? 25.005  -8.960  -2.675  1.00 21.36  ? 238 GLU A CA  1 
ATOM   1910 C  C   . GLU A 1 237 ? 25.190  -9.510  -1.253  1.00 20.99  ? 238 GLU A C   1 
ATOM   1911 O  O   . GLU A 1 237 ? 25.708  -10.610 -1.024  1.00 20.13  ? 238 GLU A O   1 
ATOM   1912 C  CB  . GLU A 1 237 ? 24.106  -9.961  -3.425  1.00 24.17  ? 238 GLU A CB  1 
ATOM   1913 C  CG  . GLU A 1 237 ? 22.687  -10.036 -2.839  1.00 30.38  ? 238 GLU A CG  1 
ATOM   1914 C  CD  . GLU A 1 237 ? 21.561  -10.624 -3.682  1.00 41.67  ? 238 GLU A CD  1 
ATOM   1915 O  OE1 . GLU A 1 237 ? 21.855  -11.136 -4.801  1.00 45.95  ? 238 GLU A OE1 1 
ATOM   1916 O  OE2 . GLU A 1 237 ? 20.373  -10.486 -3.275  1.00 30.75  ? 238 GLU A OE2 1 
ATOM   1917 N  N   . GLU A 1 238 ? 24.592  -8.798  -0.306  1.00 19.74  ? 239 GLU A N   1 
ATOM   1918 C  CA  . GLU A 1 238 ? 24.593  -9.206  1.080   1.00 19.98  ? 239 GLU A CA  1 
ATOM   1919 C  C   . GLU A 1 238 ? 23.161  -9.083  1.583   1.00 17.24  ? 239 GLU A C   1 
ATOM   1920 O  O   . GLU A 1 238 ? 22.637  -7.972  1.649   1.00 19.85  ? 239 GLU A O   1 
ATOM   1921 C  CB  . GLU A 1 238 ? 25.466  -8.245  1.881   1.00 23.96  ? 239 GLU A CB  1 
ATOM   1922 C  CG  . GLU A 1 238 ? 25.688  -8.745  3.288   1.00 32.89  ? 239 GLU A CG  1 
ATOM   1923 C  CD  . GLU A 1 238 ? 26.502  -10.037 3.335   1.00 39.87  ? 239 GLU A CD  1 
ATOM   1924 O  OE1 . GLU A 1 238 ? 27.596  -10.054 2.719   1.00 56.23  ? 239 GLU A OE1 1 
ATOM   1925 O  OE2 . GLU A 1 238 ? 26.041  -11.034 3.967   1.00 49.07  ? 239 GLU A OE2 1 
ATOM   1926 N  N   . LEU A 1 239 ? 22.499  -10.217 1.859   1.00 18.99  ? 240 LEU A N   1 
ATOM   1927 C  CA  . LEU A 1 239 ? 21.093  -10.152 2.251   1.00 16.26  ? 240 LEU A CA  1 
ATOM   1928 C  C   . LEU A 1 239 ? 20.940  -9.400  3.574   1.00 15.01  ? 240 LEU A C   1 
ATOM   1929 O  O   . LEU A 1 239 ? 21.686  -9.619  4.513   1.00 17.97  ? 240 LEU A O   1 
ATOM   1930 C  CB  . LEU A 1 239 ? 20.527  -11.571 2.396   1.00 16.56  ? 240 LEU A CB  1 
ATOM   1931 C  CG  . LEU A 1 239 ? 20.456  -12.388 1.126   1.00 17.73  ? 240 LEU A CG  1 
ATOM   1932 C  CD1 . LEU A 1 239 ? 19.915  -13.787 1.430   1.00 22.27  ? 240 LEU A CD1 1 
ATOM   1933 C  CD2 . LEU A 1 239 ? 19.614  -11.736 0.064   1.00 20.88  ? 240 LEU A CD2 1 
ATOM   1934 N  N   . MET A 1 240 ? 19.927  -8.541  3.612   1.00 14.86  ? 241 MET A N   1 
ATOM   1935 C  CA  . MET A 1 240 ? 19.553  -7.753  4.792   1.00 13.99  ? 241 MET A CA  1 
ATOM   1936 C  C   . MET A 1 240 ? 18.785  -8.697  5.708   1.00 14.63  ? 241 MET A C   1 
ATOM   1937 O  O   . MET A 1 240 ? 17.580  -8.905  5.544   1.00 15.07  ? 241 MET A O   1 
ATOM   1938 C  CB  . MET A 1 240 ? 18.731  -6.540  4.357   1.00 16.00  ? 241 MET A CB  1 
ATOM   1939 C  CG  . MET A 1 240 ? 18.426  -5.573  5.569   1.00 14.59  ? 241 MET A CG  1 
ATOM   1940 S  SD  . MET A 1 240 ? 17.454  -4.201  5.111   1.00 16.84  ? 241 MET A SD  1 
ATOM   1941 C  CE  . MET A 1 240 ? 18.703  -3.121  4.405   1.00 17.07  ? 241 MET A CE  1 
ATOM   1942 N  N   . VAL A 1 241 ? 19.545  -9.361  6.600   1.00 13.78  ? 242 VAL A N   1 
ATOM   1943 C  CA  . VAL A 1 241 ? 18.976  -10.243 7.629   1.00 13.73  ? 242 VAL A CA  1 
ATOM   1944 C  C   . VAL A 1 241 ? 19.762  -10.005 8.906   1.00 12.31  ? 242 VAL A C   1 
ATOM   1945 O  O   . VAL A 1 241 ? 20.951  -9.609  8.854   1.00 13.89  ? 242 VAL A O   1 
ATOM   1946 C  CB  . VAL A 1 241 ? 19.058  -11.741 7.252   1.00 14.80  ? 242 VAL A CB  1 
ATOM   1947 C  CG1 . VAL A 1 241 ? 18.139  -12.038 6.068   1.00 16.05  ? 242 VAL A CG1 1 
ATOM   1948 C  CG2 . VAL A 1 241 ? 20.495  -12.225 6.968   1.00 16.06  ? 242 VAL A CG2 1 
ATOM   1949 N  N   . ASP A 1 242 ? 19.148  -10.336 10.053  1.00 11.68  ? 243 ASP A N   1 
ATOM   1950 C  CA  . ASP A 1 242 ? 19.822  -10.229 11.348  1.00 11.69  ? 243 ASP A CA  1 
ATOM   1951 C  C   . ASP A 1 242 ? 20.288  -8.793  11.588  1.00 10.73  ? 243 ASP A C   1 
ATOM   1952 O  O   . ASP A 1 242 ? 21.382  -8.552  12.082  1.00 13.41  ? 243 ASP A O   1 
ATOM   1953 C  CB  . ASP A 1 242 ? 20.914  -11.278 11.530  1.00 13.01  ? 243 ASP A CB  1 
ATOM   1954 C  CG  . ASP A 1 242 ? 20.294  -12.648 11.605  1.00 12.99  ? 243 ASP A CG  1 
ATOM   1955 O  OD1 . ASP A 1 242 ? 19.253  -12.816 12.312  1.00 13.29  ? 243 ASP A OD1 1 
ATOM   1956 O  OD2 . ASP A 1 242 ? 20.904  -13.597 11.083  1.00 16.39  ? 243 ASP A OD2 1 
ATOM   1957 N  N   . ASN A 1 243 ? 19.409  -7.834  11.284  1.00 10.44  ? 244 ASN A N   1 
ATOM   1958 C  CA  . ASN A 1 243 ? 19.686  -6.418  11.523  1.00 10.31  ? 244 ASN A CA  1 
ATOM   1959 C  C   . ASN A 1 243 ? 19.123  -5.991  12.904  1.00 10.20  ? 244 ASN A C   1 
ATOM   1960 O  O   . ASN A 1 243 ? 18.396  -5.019  13.002  1.00 11.59  ? 244 ASN A O   1 
ATOM   1961 C  CB  . ASN A 1 243 ? 19.161  -5.530  10.388  1.00 11.20  ? 244 ASN A CB  1 
ATOM   1962 C  CG  . ASN A 1 243 ? 17.695  -5.737  10.088  1.00 10.89  ? 244 ASN A CG  1 
ATOM   1963 O  OD1 . ASN A 1 243 ? 17.058  -6.631  10.622  1.00 12.68  ? 244 ASN A OD1 1 
ATOM   1964 N  ND2 . ASN A 1 243 ? 17.121  -4.833  9.303   1.00 13.91  ? 244 ASN A ND2 1 
ATOM   1965 N  N   . TRP A 1 244 ? 19.438  -6.768  13.929  1.00 9.99   ? 245 TRP A N   1 
ATOM   1966 C  CA  . TRP A 1 244 ? 18.980  -6.508  15.305  1.00 10.17  ? 245 TRP A CA  1 
ATOM   1967 C  C   . TRP A 1 244 ? 20.180  -6.416  16.238  1.00 10.25  ? 245 TRP A C   1 
ATOM   1968 O  O   . TRP A 1 244 ? 21.193  -7.116  16.043  1.00 11.48  ? 245 TRP A O   1 
ATOM   1969 C  CB  . TRP A 1 244 ? 18.005  -7.603  15.777  1.00 10.38  ? 245 TRP A CB  1 
ATOM   1970 C  CG  . TRP A 1 244 ? 18.473  -9.006  15.577  1.00 9.89   ? 245 TRP A CG  1 
ATOM   1971 C  CD1 . TRP A 1 244 ? 18.337  -9.729  14.421  1.00 10.51  ? 245 TRP A CD1 1 
ATOM   1972 C  CD2 . TRP A 1 244 ? 19.017  -9.887  16.570  1.00 10.11  ? 245 TRP A CD2 1 
ATOM   1973 N  NE1 . TRP A 1 244 ? 18.820  -11.000 14.630  1.00 10.84  ? 245 TRP A NE1 1 
ATOM   1974 C  CE2 . TRP A 1 244 ? 19.251  -11.133 15.929  1.00 11.29  ? 245 TRP A CE2 1 
ATOM   1975 C  CE3 . TRP A 1 244 ? 19.290  -9.740  17.949  1.00 12.12  ? 245 TRP A CE3 1 
ATOM   1976 C  CZ2 . TRP A 1 244 ? 19.752  -12.242 16.626  1.00 13.27  ? 245 TRP A CZ2 1 
ATOM   1977 C  CZ3 . TRP A 1 244 ? 19.799  -10.841 18.624  1.00 13.63  ? 245 TRP A CZ3 1 
ATOM   1978 C  CH2 . TRP A 1 244 ? 20.046  -12.060 17.965  1.00 14.21  ? 245 TRP A CH2 1 
ATOM   1979 N  N   . ARG A 1 245 ? 20.047  -5.542  17.240  1.00 10.07  ? 246 ARG A N   1 
ATOM   1980 C  CA  . ARG A 1 245 ? 21.009  -5.458  18.340  1.00 10.34  ? 246 ARG A CA  1 
ATOM   1981 C  C   . ARG A 1 245 ? 20.541  -6.393  19.441  1.00 10.92  ? 246 ARG A C   1 
ATOM   1982 O  O   . ARG A 1 245 ? 19.356  -6.370  19.777  1.00 12.29  ? 246 ARG A O   1 
ATOM   1983 C  CB  . ARG A 1 245 ? 21.085  -4.011  18.861  1.00 10.91  ? 246 ARG A CB  1 
ATOM   1984 C  CG  . ARG A 1 245 ? 22.222  -3.782  19.836  1.00 10.62  ? 246 ARG A CG  1 
ATOM   1985 C  CD  . ARG A 1 245 ? 22.117  -2.436  20.509  1.00 11.22  ? 246 ARG A CD  1 
ATOM   1986 N  NE  . ARG A 1 245 ? 23.364  -2.034  21.143  1.00 10.92  ? 246 ARG A NE  1 
ATOM   1987 C  CZ  . ARG A 1 245 ? 23.477  -1.044  22.021  1.00 10.52  ? 246 ARG A CZ  1 
ATOM   1988 N  NH1 . ARG A 1 245 ? 22.410  -0.347  22.374  1.00 12.19  ? 246 ARG A NH1 1 
ATOM   1989 N  NH2 . ARG A 1 245 ? 24.655  -0.754  22.543  1.00 13.69  ? 246 ARG A NH2 1 
ATOM   1990 N  N   . PRO A 1 246 ? 21.433  -7.192  20.055  1.00 11.64  ? 247 PRO A N   1 
ATOM   1991 C  CA  . PRO A 1 246 ? 21.039  -8.031  21.184  1.00 12.35  ? 247 PRO A CA  1 
ATOM   1992 C  C   . PRO A 1 246 ? 20.683  -7.191  22.410  1.00 12.71  ? 247 PRO A C   1 
ATOM   1993 O  O   . PRO A 1 246 ? 21.014  -6.003  22.550  1.00 12.53  ? 247 PRO A O   1 
ATOM   1994 C  CB  . PRO A 1 246 ? 22.297  -8.830  21.485  1.00 18.15  ? 247 PRO A CB  1 
ATOM   1995 C  CG  . PRO A 1 246 ? 23.105  -8.764  20.196  1.00 20.82  ? 247 PRO A CG  1 
ATOM   1996 C  CD  . PRO A 1 246 ? 22.863  -7.368  19.657  1.00 15.01  ? 247 PRO A CD  1 
ATOM   1997 N  N   . ALA A 1 247 ? 20.008  -7.854  23.355  1.00 13.03  ? 248 ALA A N   1 
ATOM   1998 C  CA  . ALA A 1 247 ? 19.620  -7.206  24.619  1.00 12.39  ? 248 ALA A CA  1 
ATOM   1999 C  C   . ALA A 1 247 ? 20.836  -6.695  25.399  1.00 12.35  ? 248 ALA A C   1 
ATOM   2000 O  O   . ALA A 1 247 ? 21.893  -7.346  25.414  1.00 14.60  ? 248 ALA A O   1 
ATOM   2001 C  CB  . ALA A 1 247 ? 18.843  -8.202  25.479  1.00 15.36  ? 248 ALA A CB  1 
ATOM   2002 N  N   . GLN A 1 248 ? 20.712  -5.491  25.965  1.00 12.00  ? 249 GLN A N   1 
ATOM   2003 C  CA  . GLN A 1 248 ? 21.744  -4.781  26.674  1.00 12.72  ? 249 GLN A CA  1 
ATOM   2004 C  C   . GLN A 1 248 ? 21.418  -4.818  28.164  1.00 13.25  ? 249 GLN A C   1 
ATOM   2005 O  O   . GLN A 1 248 ? 20.245  -5.026  28.580  1.00 14.47  ? 249 GLN A O   1 
ATOM   2006 C  CB  . GLN A 1 248 ? 21.793  -3.337  26.172  1.00 13.84  ? 249 GLN A CB  1 
ATOM   2007 C  CG  . GLN A 1 248 ? 22.132  -3.280  24.672  1.00 13.93  ? 249 GLN A CG  1 
ATOM   2008 C  CD  . GLN A 1 248 ? 23.455  -3.959  24.338  1.00 15.37  ? 249 GLN A CD  1 
ATOM   2009 O  OE1 . GLN A 1 248 ? 24.487  -3.614  24.939  1.00 18.26  ? 249 GLN A OE1 1 
ATOM   2010 N  NE2 . GLN A 1 248 ? 23.440  -4.903  23.421  1.00 16.25  ? 249 GLN A NE2 1 
ATOM   2011 N  N   . PRO A 1 249 ? 22.396  -4.560  29.039  1.00 16.08  ? 250 PRO A N   1 
ATOM   2012 C  CA  . PRO A 1 249 ? 22.135  -4.659  30.475  1.00 18.16  ? 250 PRO A CA  1 
ATOM   2013 C  C   . PRO A 1 249 ? 21.123  -3.625  30.944  1.00 14.41  ? 250 PRO A C   1 
ATOM   2014 O  O   . PRO A 1 249 ? 21.190  -2.440  30.626  1.00 15.44  ? 250 PRO A O   1 
ATOM   2015 C  CB  . PRO A 1 249 ? 23.530  -4.403  31.110  1.00 24.07  ? 250 PRO A CB  1 
ATOM   2016 C  CG  . PRO A 1 249 ? 24.532  -4.624  30.007  1.00 23.03  ? 250 PRO A CG  1 
ATOM   2017 C  CD  . PRO A 1 249 ? 23.807  -4.286  28.733  1.00 19.81  ? 250 PRO A CD  1 
ATOM   2018 N  N   . LEU A 1 250 ? 20.199  -4.104  31.772  1.00 16.21  ? 251 LEU A N   1 
ATOM   2019 C  CA  . LEU A 1 250 ? 19.173  -3.220  32.299  1.00 15.29  ? 251 LEU A CA  1 
ATOM   2020 C  C   . LEU A 1 250 ? 19.737  -2.152  33.243  1.00 14.91  ? 251 LEU A C   1 
ATOM   2021 O  O   . LEU A 1 250 ? 19.216  -1.047  33.394  1.00 16.41  ? 251 LEU A O   1 
ATOM   2022 C  CB  . LEU A 1 250 ? 18.075  -4.056  32.954  1.00 18.58  ? 251 LEU A CB  1 
ATOM   2023 C  CG  . LEU A 1 250 ? 16.800  -3.313  33.355  1.00 17.04  ? 251 LEU A CG  1 
ATOM   2024 C  CD1 . LEU A 1 250 ? 16.098  -2.719  32.131  1.00 18.48  ? 251 LEU A CD1 1 
ATOM   2025 C  CD2 . LEU A 1 250 ? 15.853  -4.267  34.088  1.00 22.76  ? 251 LEU A CD2 1 
ATOM   2026 N  N   . LYS A 1 251 ? 20.819  -2.468  33.961  1.00 19.04  ? 252 LYS A N   1 
ATOM   2027 C  CA  . LYS A 1 251 ? 21.423  -1.471  34.874  1.00 21.87  ? 252 LYS A CA  1 
ATOM   2028 C  C   . LYS A 1 251 ? 20.429  -1.107  35.981  1.00 24.05  ? 252 LYS A C   1 
ATOM   2029 O  O   . LYS A 1 251 ? 19.786  -1.970  36.554  1.00 32.73  ? 252 LYS A O   1 
ATOM   2030 C  CB  . LYS A 1 251 ? 21.854  -0.226  34.092  1.00 24.62  ? 252 LYS A CB  1 
ATOM   2031 C  CG  . LYS A 1 251 ? 22.876  -0.471  32.990  1.00 25.61  ? 252 LYS A CG  1 
ATOM   2032 C  CD  . LYS A 1 251 ? 24.286  -0.660  33.510  1.00 35.19  ? 252 LYS A CD  1 
ATOM   2033 C  CE  . LYS A 1 251 ? 25.168  -1.445  32.563  1.00 32.74  ? 252 LYS A CE  1 
ATOM   2034 N  NZ  . LYS A 1 251 ? 26.161  -0.575  31.889  1.00 40.75  ? 252 LYS A NZ  1 
ATOM   2035 N  N   . ASN A 1 252 ? 20.291  0.160   36.279  1.00 24.04  ? 253 ASN A N   1 
ATOM   2036 C  CA  . ASN A 1 252 ? 19.433  0.358   37.460  1.00 41.19  ? 253 ASN A CA  1 
ATOM   2037 C  C   . ASN A 1 252 ? 17.919  0.405   37.117  1.00 30.99  ? 253 ASN A C   1 
ATOM   2038 O  O   . ASN A 1 252 ? 17.086  0.653   37.990  1.00 34.29  ? 253 ASN A O   1 
ATOM   2039 C  CB  . ASN A 1 252 ? 20.007  1.353   38.503  1.00 85.25  ? 253 ASN A CB  1 
ATOM   2040 C  CG  . ASN A 1 252 ? 21.385  0.958   39.003  1.00 81.43  ? 253 ASN A CG  1 
ATOM   2041 O  OD1 . ASN A 1 252 ? 21.669  -0.254  39.205  1.00 93.40  ? 253 ASN A OD1 1 
ATOM   2042 N  ND2 . ASN A 1 252 ? 22.251  1.977   39.205  1.00 109.31 ? 253 ASN A ND2 1 
ATOM   2043 N  N   . ARG A 1 253 ? 17.549  0.159   35.852  1.00 17.96  ? 254 ARG A N   1 
ATOM   2044 C  CA  . ARG A 1 253 ? 16.268  0.663   35.374  1.00 14.99  ? 254 ARG A CA  1 
ATOM   2045 C  C   . ARG A 1 253 ? 15.142  -0.255  35.820  1.00 16.15  ? 254 ARG A C   1 
ATOM   2046 O  O   . ARG A 1 253 ? 15.365  -1.443  35.940  1.00 22.64  ? 254 ARG A O   1 
ATOM   2047 C  CB  . ARG A 1 253 ? 16.304  0.811   33.851  1.00 13.48  ? 254 ARG A CB  1 
ATOM   2048 C  CG  . ARG A 1 253 ? 17.184  1.942   33.365  1.00 14.87  ? 254 ARG A CG  1 
ATOM   2049 C  CD  . ARG A 1 253 ? 17.354  1.932   31.858  1.00 13.49  ? 254 ARG A CD  1 
ATOM   2050 N  NE  . ARG A 1 253 ? 18.116  0.777   31.391  1.00 13.44  ? 254 ARG A NE  1 
ATOM   2051 C  CZ  . ARG A 1 253 ? 18.358  0.501   30.113  1.00 11.57  ? 254 ARG A CZ  1 
ATOM   2052 N  NH1 . ARG A 1 253 ? 17.732  1.184   29.168  1.00 11.85  ? 254 ARG A NH1 1 
ATOM   2053 N  NH2 . ARG A 1 253 ? 19.180  -0.479  29.801  1.00 11.85  ? 254 ARG A NH2 1 
ATOM   2054 N  N   . GLN A 1 254 ? 13.923  0.284   35.884  1.00 16.29  ? 255 GLN A N   1 
ATOM   2055 C  CA  . GLN A 1 254 ? 12.711  -0.489  36.125  1.00 18.70  ? 255 GLN A CA  1 
ATOM   2056 C  C   . GLN A 1 254 ? 11.882  -0.463  34.854  1.00 15.50  ? 255 GLN A C   1 
ATOM   2057 O  O   . GLN A 1 254 ? 11.739  0.592   34.208  1.00 20.78  ? 255 GLN A O   1 
ATOM   2058 C  CB  . GLN A 1 254 ? 11.878  0.137   37.253  1.00 23.42  ? 255 GLN A CB  1 
ATOM   2059 C  CG  . GLN A 1 254 ? 12.562  -0.046  38.592  1.00 38.87  ? 255 GLN A CG  1 
ATOM   2060 C  CD  . GLN A 1 254 ? 11.528  -0.085  39.691  1.00 54.09  ? 255 GLN A CD  1 
ATOM   2061 O  OE1 . GLN A 1 254 ? 10.354  -0.423  39.474  1.00 67.71  ? 255 GLN A OE1 1 
ATOM   2062 N  NE2 . GLN A 1 254 ? 11.970  0.255   40.888  1.00 52.03  ? 255 GLN A NE2 1 
ATOM   2063 N  N   . ILE A 1 255 ? 11.370  -1.600  34.474  1.00 13.81  ? 256 ILE A N   1 
ATOM   2064 C  CA  . ILE A 1 255 ? 10.372  -1.710  33.419  1.00 12.81  ? 256 ILE A CA  1 
ATOM   2065 C  C   . ILE A 1 255 ? 9.005   -1.674  34.099  1.00 13.43  ? 256 ILE A C   1 
ATOM   2066 O  O   . ILE A 1 255 ? 8.776   -2.410  35.058  1.00 15.11  ? 256 ILE A O   1 
ATOM   2067 C  CB  . ILE A 1 255 ? 10.591  -2.976  32.591  1.00 13.12  ? 256 ILE A CB  1 
ATOM   2068 C  CG1 . ILE A 1 255 ? 12.044  -3.005  32.060  1.00 14.86  ? 256 ILE A CG1 1 
ATOM   2069 C  CG2 . ILE A 1 255 ? 9.506   -3.020  31.454  1.00 15.19  ? 256 ILE A CG2 1 
ATOM   2070 C  CD1 . ILE A 1 255 ? 12.318  -4.207  31.138  1.00 17.03  ? 256 ILE A CD1 1 
ATOM   2071 N  N   . LYS A 1 256 ? 8.102   -0.815  33.601  1.00 13.56  ? 257 LYS A N   1 
ATOM   2072 C  CA  . LYS A 1 256 ? 6.741   -0.724  34.124  1.00 12.91  ? 257 LYS A CA  1 
ATOM   2073 C  C   . LYS A 1 256 ? 5.794   -1.372  33.142  1.00 13.63  ? 257 LYS A C   1 
ATOM   2074 O  O   . LYS A 1 256 ? 6.029   -1.327  31.947  1.00 15.67  ? 257 LYS A O   1 
ATOM   2075 C  CB  . LYS A 1 256 ? 6.365   0.755   34.334  1.00 16.38  ? 257 LYS A CB  1 
ATOM   2076 C  CG  . LYS A 1 256 ? 7.219   1.411   35.418  1.00 23.86  ? 257 LYS A CG  1 
ATOM   2077 C  CD  . LYS A 1 256 ? 6.734   2.713   35.961  1.00 39.06  ? 257 LYS A CD  1 
ATOM   2078 C  CE  . LYS A 1 256 ? 7.434   3.127   37.245  1.00 57.19  ? 257 LYS A CE  1 
ATOM   2079 N  NZ  . LYS A 1 256 ? 7.060   4.501   37.656  1.00 66.84  ? 257 LYS A NZ  1 
ATOM   2080 N  N   . ALA A 1 257 ? 4.721   -1.973  33.654  1.00 14.79  ? 258 ALA A N   1 
ATOM   2081 C  CA  . ALA A 1 257 ? 3.645   -2.577  32.858  1.00 14.57  ? 258 ALA A CA  1 
ATOM   2082 C  C   . ALA A 1 257 ? 2.366   -1.769  33.023  1.00 14.00  ? 258 ALA A C   1 
ATOM   2083 O  O   . ALA A 1 257 ? 2.015   -1.342  34.125  1.00 15.63  ? 258 ALA A O   1 
ATOM   2084 C  CB  . ALA A 1 257 ? 3.429   -4.025  33.242  1.00 16.33  ? 258 ALA A CB  1 
ATOM   2085 N  N   . SER A 1 258 ? 1.600   -1.637  31.945  1.00 14.58  ? 259 SER A N   1 
ATOM   2086 C  CA  . SER A 1 258 ? 0.300   -0.982  31.992  1.00 16.33  ? 259 SER A CA  1 
ATOM   2087 C  C   . SER A 1 258 ? -0.819  -1.940  32.404  1.00 16.53  ? 259 SER A C   1 
ATOM   2088 O  O   . SER A 1 258 ? -1.948  -1.483  32.552  1.00 22.19  ? 259 SER A O   1 
ATOM   2089 C  CB  . SER A 1 258 ? 0.006   -0.385  30.622  1.00 16.14  ? 259 SER A CB  1 
ATOM   2090 O  OG  . SER A 1 258 ? -0.397  -1.410  29.739  1.00 16.02  ? 259 SER A OG  1 
ATOM   2091 N  N   . PHE A 1 259 ? -0.480  -3.205  32.697  1.00 17.91  ? 260 PHE A N   1 
ATOM   2092 C  CA  . PHE A 1 259 ? -1.469  -4.252  32.940  1.00 19.38  ? 260 PHE A CA  1 
ATOM   2093 C  C   . PHE A 1 259 ? -0.920  -5.257  33.933  1.00 23.74  ? 260 PHE A C   1 
ATOM   2094 O  O   . PHE A 1 259 ? 0.293   -5.399  34.186  1.00 23.21  ? 260 PHE A O   1 
ATOM   2095 C  CB  . PHE A 1 259 ? -1.645  -5.055  31.638  1.00 20.94  ? 260 PHE A CB  1 
ATOM   2096 C  CG  . PHE A 1 259 ? -0.415  -5.734  31.056  1.00 19.00  ? 260 PHE A CG  1 
ATOM   2097 C  CD1 . PHE A 1 259 ? 0.501   -5.019  30.302  1.00 16.44  ? 260 PHE A CD1 1 
ATOM   2098 C  CD2 . PHE A 1 259 ? -0.182  -7.084  31.266  1.00 24.27  ? 260 PHE A CD2 1 
ATOM   2099 C  CE1 . PHE A 1 259 ? 1.622   -5.638  29.771  1.00 19.57  ? 260 PHE A CE1 1 
ATOM   2100 C  CE2 . PHE A 1 259 ? 0.939   -7.702  30.735  1.00 27.72  ? 260 PHE A CE2 1 
ATOM   2101 C  CZ  . PHE A 1 259 ? 1.839   -6.979  29.989  1.00 25.30  ? 260 PHE A CZ  1 
ATOM   2102 N  N   . LYS A 1 260 ? -1.880  -6.122  34.340  1.00 34.64  ? 261 LYS A N   1 
ATOM   2103 C  CA  . LYS A 1 260 ? -1.862  -7.342  35.225  1.00 47.42  ? 261 LYS A CA  1 
ATOM   2104 C  C   . LYS A 1 260 ? -2.123  -7.043  36.712  1.00 49.21  ? 261 LYS A C   1 
ATOM   2105 O  O   . LYS A 1 260 ? -1.298  -7.417  37.546  1.00 84.12  ? 261 LYS A O   1 
ATOM   2106 C  CB  . LYS A 1 260 ? -0.708  -8.324  34.970  1.00 49.40  ? 261 LYS A CB  1 
ATOM   2107 C  CG  . LYS A 1 260 ? -0.899  -9.258  33.782  1.00 66.77  ? 261 LYS A CG  1 
ATOM   2108 C  CD  . LYS A 1 260 ? -1.126  -10.700 34.184  1.00 76.12  ? 261 LYS A CD  1 
ATOM   2109 C  CE  . LYS A 1 260 ? -1.853  -11.503 33.126  1.00 75.73  ? 261 LYS A CE  1 
ATOM   2110 N  NZ  . LYS A 1 260 ? -1.281  -11.280 31.778  1.00 70.23  ? 261 LYS A NZ  1 
ATOM   2111 O  OXT . LYS A 1 260 ? -3.163  -6.432  36.998  1.00 63.02  ? 261 LYS A OXT 1 
HETATM 2112 ZN ZN  . ZN  B 2 .   ? 14.515  0.162   15.297  1.00 9.11   ? 301 ZN  A ZN  1 
HETATM 2113 O  O1  . MES C 3 .   ? 13.502  -7.382  -2.700  1.00 40.86  ? 302 MES A O1  1 
HETATM 2114 C  C2  . MES C 3 .   ? 13.604  -8.311  -3.796  1.00 33.39  ? 302 MES A C2  1 
HETATM 2115 C  C3  . MES C 3 .   ? 12.265  -8.717  -4.379  1.00 43.28  ? 302 MES A C3  1 
HETATM 2116 N  N4  . MES C 3 .   ? 11.334  -9.174  -3.296  1.00 33.62  ? 302 MES A N4  1 
HETATM 2117 C  C5  . MES C 3 .   ? 11.250  -8.208  -2.156  1.00 33.74  ? 302 MES A C5  1 
HETATM 2118 C  C6  . MES C 3 .   ? 12.633  -7.840  -1.663  1.00 29.51  ? 302 MES A C6  1 
HETATM 2119 C  C7  . MES C 3 .   ? 10.020  -9.773  -3.736  1.00 47.58  ? 302 MES A C7  1 
HETATM 2120 S  S   . DMS D 4 .   ? 22.431  -9.985  14.934  1.00 21.51  ? 303 DMS A S   1 
HETATM 2121 O  O   . DMS D 4 .   ? 23.108  -11.282 14.491  1.00 29.45  ? 303 DMS A O   1 
HETATM 2122 C  C1  . DMS D 4 .   ? 23.585  -8.722  14.597  1.00 25.22  ? 303 DMS A C1  1 
HETATM 2123 C  C2  . DMS D 4 .   ? 22.655  -9.934  16.649  1.00 21.87  ? 303 DMS A C2  1 
HETATM 2124 N  N1  . BCN E 5 .   ? 12.345  18.623  10.185  1.00 44.21  ? 304 BCN A N1  1 
HETATM 2125 C  C1  . BCN E 5 .   ? 12.819  17.193  10.300  1.00 21.51  ? 304 BCN A C1  1 
HETATM 2126 C  C2  . BCN E 5 .   ? 14.163  16.958  11.083  1.00 44.30  ? 304 BCN A C2  1 
HETATM 2127 O  O21 . BCN E 5 .   ? 14.696  15.848  10.994  1.00 38.36  ? 304 BCN A O21 1 
HETATM 2128 O  O22 . BCN E 5 .   ? 14.691  17.880  11.767  1.00 45.09  ? 304 BCN A O22 1 
HETATM 2129 C  C3  . BCN E 5 .   ? 13.347  19.699  10.389  1.00 42.39  ? 304 BCN A C3  1 
HETATM 2130 C  C4  . BCN E 5 .   ? 12.799  21.114  10.135  1.00 58.39  ? 304 BCN A C4  1 
HETATM 2131 O  O4  . BCN E 5 .   ? 12.800  21.683  8.793   1.00 39.56  ? 304 BCN A O4  1 
HETATM 2132 C  C5  . BCN E 5 .   ? 11.453  18.879  9.029   1.00 50.18  ? 304 BCN A C5  1 
HETATM 2133 C  C6  . BCN E 5 .   ? 10.548  17.770  8.523   1.00 36.80  ? 304 BCN A C6  1 
HETATM 2134 O  O6  . BCN E 5 .   ? 9.169   18.130  8.730   1.00 46.07  ? 304 BCN A O6  1 
HETATM 2135 C  C1  . EDO F 6 .   ? 16.327  3.298   12.412  1.00 33.71  ? 305 EDO A C1  1 
HETATM 2136 O  O1  . EDO F 6 .   ? 17.049  2.112   12.848  1.00 38.60  ? 305 EDO A O1  1 
HETATM 2137 C  C2  . EDO F 6 .   ? 16.331  3.460   10.937  1.00 36.41  ? 305 EDO A C2  1 
HETATM 2138 O  O2  . EDO F 6 .   ? 15.067  3.437   10.220  1.00 26.93  ? 305 EDO A O2  1 
HETATM 2139 N  N1  . EZL G 7 .   ? 15.863  1.230   16.166  1.00 9.66   ? 306 EZL A N1  1 
HETATM 2140 C  C2  . EZL G 7 .   ? 17.822  5.207   15.235  1.00 11.62  ? 306 EZL A C2  1 
HETATM 2141 C  C3  . EZL G 7 .   ? 16.773  5.985   14.846  1.00 12.11  ? 306 EZL A C3  1 
HETATM 2142 C  C4  . EZL G 7 .   ? 16.952  7.208   14.153  1.00 14.43  ? 306 EZL A C4  1 
HETATM 2143 C  C5  . EZL G 7 .   ? 18.308  7.535   13.896  1.00 14.49  ? 306 EZL A C5  1 
HETATM 2144 C  C8  . EZL G 7 .   ? 17.582  9.556   12.720  1.00 19.94  ? 306 EZL A C8  1 
HETATM 2145 O  O1  . EZL G 7 .   ? 13.993  2.846   16.601  1.00 9.93   ? 306 EZL A O1  1 
HETATM 2146 O  O2  . EZL G 7 .   ? 15.844  2.714   18.254  1.00 10.21  ? 306 EZL A O2  1 
HETATM 2147 S  S1  . EZL G 7 .   ? 15.392  2.612   16.867  1.00 10.05  ? 306 EZL A S1  1 
HETATM 2148 C  C1  . EZL G 7 .   ? 16.153  3.970   16.005  1.00 9.97   ? 306 EZL A C1  1 
HETATM 2149 N  N2  . EZL G 7 .   ? 17.489  4.028   15.909  1.00 10.84  ? 306 EZL A N2  1 
HETATM 2150 S  S2  . EZL G 7 .   ? 15.326  5.235   15.333  1.00 12.44  ? 306 EZL A S2  1 
HETATM 2151 C  C6  . EZL G 7 .   ? 19.372  6.718   14.269  1.00 13.14  ? 306 EZL A C6  1 
HETATM 2152 C  C7  . EZL G 7 .   ? 19.183  5.558   14.972  1.00 13.26  ? 306 EZL A C7  1 
HETATM 2153 O  O3  . EZL G 7 .   ? 18.628  8.701   13.188  1.00 17.80  ? 306 EZL A O3  1 
HETATM 2154 C  C9  . EZL G 7 .   ? 18.304  10.653  11.911  1.00 22.61  ? 306 EZL A C9  1 
HETATM 2155 O  O   . HOH H 8 .   ? 18.652  2.451   11.342  1.00 21.07  ? 401 HOH A O   1 
HETATM 2156 O  O   . HOH H 8 .   ? 35.805  2.047   15.107  1.00 47.65  ? 402 HOH A O   1 
HETATM 2157 O  O   . HOH H 8 .   ? 18.924  10.271  29.338  1.00 26.31  ? 403 HOH A O   1 
HETATM 2158 O  O   . HOH H 8 .   ? 22.459  -13.518 14.285  1.00 44.40  ? 404 HOH A O   1 
HETATM 2159 O  O   . HOH H 8 .   ? 19.637  -16.250 18.101  1.00 46.43  ? 405 HOH A O   1 
HETATM 2160 O  O   . HOH H 8 .   ? 3.376   -20.186 6.146   1.00 19.83  ? 406 HOH A O   1 
HETATM 2161 O  O   . HOH H 8 .   ? 2.107   19.344  19.002  1.00 46.95  ? 407 HOH A O   1 
HETATM 2162 O  O   . HOH H 8 .   ? 6.565   -14.509 29.044  1.00 38.78  ? 408 HOH A O   1 
HETATM 2163 O  O   . HOH H 8 .   ? 7.069   -6.819  -5.252  1.00 33.78  ? 409 HOH A O   1 
HETATM 2164 O  O   . HOH H 8 .   ? 36.320  -5.007  11.796  1.00 34.83  ? 410 HOH A O   1 
HETATM 2165 O  O   . HOH H 8 .   ? 7.648   -20.463 11.319  1.00 30.27  ? 411 HOH A O   1 
HETATM 2166 O  O   . HOH H 8 .   ? -2.020  -11.713 11.132  1.00 41.85  ? 412 HOH A O   1 
HETATM 2167 O  O   . HOH H 8 .   ? 4.635   7.404   -7.919  1.00 38.01  ? 413 HOH A O   1 
HETATM 2168 O  O   . HOH H 8 .   ? 32.548  -5.469  22.272  1.00 36.76  ? 414 HOH A O   1 
HETATM 2169 O  O   . HOH H 8 .   ? -3.118  -1.473  29.467  1.00 34.68  ? 415 HOH A O   1 
HETATM 2170 O  O   . HOH H 8 .   ? -3.016  10.588  20.366  1.00 28.14  ? 416 HOH A O   1 
HETATM 2171 O  O   . HOH H 8 .   ? 7.804   1.053   -5.955  1.00 40.79  ? 417 HOH A O   1 
HETATM 2172 O  O   . HOH H 8 .   ? 1.238   -14.896 3.027   1.00 30.69  ? 418 HOH A O   1 
HETATM 2173 O  O   . HOH H 8 .   ? 11.470  17.564  29.530  1.00 33.35  ? 419 HOH A O   1 
HETATM 2174 O  O   . HOH H 8 .   ? 19.881  -2.389  15.889  1.00 13.70  ? 420 HOH A O   1 
HETATM 2175 O  O   . HOH H 8 .   ? 25.497  -1.840  26.569  1.00 23.33  ? 421 HOH A O   1 
HETATM 2176 O  O   . HOH H 8 .   ? -4.498  -3.256  13.244  1.00 31.73  ? 422 HOH A O   1 
HETATM 2177 O  O   . HOH H 8 .   ? 14.996  -2.548  -6.383  1.00 30.45  ? 423 HOH A O   1 
HETATM 2178 O  O   . HOH H 8 .   ? 4.446   -12.800 33.232  1.00 42.36  ? 424 HOH A O   1 
HETATM 2179 O  O   . HOH H 8 .   ? 12.984  -13.442 36.777  1.00 47.04  ? 425 HOH A O   1 
HETATM 2180 O  O   . HOH H 8 .   ? 10.598  2.960   34.234  1.00 37.52  ? 426 HOH A O   1 
HETATM 2181 O  O   . HOH H 8 .   ? 24.523  6.542   30.289  1.00 26.67  ? 427 HOH A O   1 
HETATM 2182 O  O   . HOH H 8 .   ? -4.787  8.011   27.101  1.00 41.91  ? 428 HOH A O   1 
HETATM 2183 O  O   . HOH H 8 .   ? 10.587  -17.605 19.981  1.00 25.80  ? 429 HOH A O   1 
HETATM 2184 O  O   . HOH H 8 .   ? 16.240  -10.238 32.106  1.00 25.60  ? 430 HOH A O   1 
HETATM 2185 O  O   . HOH H 8 .   ? 1.755   -18.867 5.148   1.00 31.10  ? 431 HOH A O   1 
HETATM 2186 O  O   . HOH H 8 .   ? 8.984   12.725  5.892   1.00 27.68  ? 432 HOH A O   1 
HETATM 2187 O  O   . HOH H 8 .   ? 5.741   -8.609  37.355  1.00 23.31  ? 433 HOH A O   1 
HETATM 2188 O  O   . HOH H 8 .   ? 14.383  -18.529 19.427  1.00 20.07  ? 434 HOH A O   1 
HETATM 2189 O  O   . HOH H 8 .   ? 23.176  9.568   27.885  1.00 21.50  ? 435 HOH A O   1 
HETATM 2190 O  O   . HOH H 8 .   ? 9.067   14.226  29.242  1.00 27.95  ? 436 HOH A O   1 
HETATM 2191 O  O   . HOH H 8 .   ? 0.937   12.651  26.735  1.00 22.75  ? 437 HOH A O   1 
HETATM 2192 O  O   . HOH H 8 .   ? -0.108  9.790   1.936   1.00 22.21  ? 438 HOH A O   1 
HETATM 2193 O  O   . HOH H 8 .   ? 18.635  -1.348  11.656  1.00 27.54  ? 439 HOH A O   1 
HETATM 2194 O  O   . HOH H 8 .   ? -4.512  -1.416  31.819  1.00 43.11  ? 440 HOH A O   1 
HETATM 2195 O  O   . HOH H 8 .   ? 10.796  10.485  25.560  1.00 14.24  ? 441 HOH A O   1 
HETATM 2196 O  O   . HOH H 8 .   ? 2.305   -19.268 14.657  1.00 37.63  ? 442 HOH A O   1 
HETATM 2197 O  O   . HOH H 8 .   ? 6.451   -16.884 18.701  1.00 29.01  ? 443 HOH A O   1 
HETATM 2198 O  O   . HOH H 8 .   ? 10.559  -16.419 16.968  1.00 23.91  ? 444 HOH A O   1 
HETATM 2199 O  O   . HOH H 8 .   ? 23.632  -11.334 5.209   1.00 25.02  ? 445 HOH A O   1 
HETATM 2200 O  O   . HOH H 8 .   ? 20.798  11.294  15.824  1.00 36.04  ? 446 HOH A O   1 
HETATM 2201 O  O   . HOH H 8 .   ? -2.122  -9.460  17.040  1.00 40.20  ? 447 HOH A O   1 
HETATM 2202 O  O   . HOH H 8 .   ? 18.526  -7.011  29.158  1.00 16.91  ? 448 HOH A O   1 
HETATM 2203 O  O   . HOH H 8 .   ? -1.674  -3.947  2.829   1.00 26.56  ? 449 HOH A O   1 
HETATM 2204 O  O   . HOH H 8 .   ? 7.054   -19.021 3.559   1.00 43.15  ? 450 HOH A O   1 
HETATM 2205 O  O   . HOH H 8 .   ? 20.357  13.686  13.079  1.00 44.78  ? 451 HOH A O   1 
HETATM 2206 O  O   . HOH H 8 .   ? 20.950  11.373  18.513  1.00 25.17  ? 452 HOH A O   1 
HETATM 2207 O  O   . HOH H 8 .   ? 32.439  1.212   15.447  1.00 42.67  ? 453 HOH A O   1 
HETATM 2208 O  O   . HOH H 8 .   ? 1.605   19.391  6.126   1.00 36.44  ? 454 HOH A O   1 
HETATM 2209 O  O   . HOH H 8 .   ? 1.415   -2.388  41.339  1.00 39.00  ? 455 HOH A O   1 
HETATM 2210 O  O   . HOH H 8 .   ? 21.249  -17.801 10.748  1.00 38.16  ? 456 HOH A O   1 
HETATM 2211 O  O   . HOH H 8 .   ? 21.178  0.995   -4.554  1.00 21.55  ? 457 HOH A O   1 
HETATM 2212 O  O   . HOH H 8 .   ? 24.639  10.441  21.036  1.00 25.08  ? 458 HOH A O   1 
HETATM 2213 O  O   . HOH H 8 .   ? 13.094  -13.616 11.279  1.00 13.64  ? 459 HOH A O   1 
HETATM 2214 O  O   . HOH H 8 .   ? 26.672  8.664   20.328  1.00 19.99  ? 460 HOH A O   1 
HETATM 2215 O  O   . HOH H 8 .   ? 17.323  -10.961 -2.924  1.00 34.11  ? 461 HOH A O   1 
HETATM 2216 O  O   . HOH H 8 .   ? 17.573  -9.360  20.865  1.00 14.38  ? 462 HOH A O   1 
HETATM 2217 O  O   . HOH H 8 .   ? 22.987  -13.724 9.339   1.00 25.11  ? 463 HOH A O   1 
HETATM 2218 O  O   . HOH H 8 .   ? 6.760   11.279  31.528  1.00 47.55  ? 464 HOH A O   1 
HETATM 2219 O  O   . HOH H 8 .   ? 10.953  17.203  12.043  1.00 19.43  ? 465 HOH A O   1 
HETATM 2220 O  O   . HOH H 8 .   ? 12.704  2.642   -6.392  1.00 35.03  ? 466 HOH A O   1 
HETATM 2221 O  O   . HOH H 8 .   ? 17.690  -17.473 22.125  1.00 48.30  ? 467 HOH A O   1 
HETATM 2222 O  O   . HOH H 8 .   ? 5.746   -19.835 13.232  1.00 23.15  ? 468 HOH A O   1 
HETATM 2223 O  O   . HOH H 8 .   ? 12.195  7.804   29.086  1.00 28.86  ? 469 HOH A O   1 
HETATM 2224 O  O   . HOH H 8 .   ? 22.406  6.329   12.109  1.00 32.41  ? 470 HOH A O   1 
HETATM 2225 O  O   . HOH H 8 .   ? 14.145  -13.215 31.601  1.00 30.23  ? 471 HOH A O   1 
HETATM 2226 O  O   . HOH H 8 .   ? 14.761  8.259   10.901  1.00 18.48  ? 472 HOH A O   1 
HETATM 2227 O  O   . HOH H 8 .   ? 20.512  2.912   34.518  1.00 34.65  ? 473 HOH A O   1 
HETATM 2228 O  O   . HOH H 8 .   ? 15.045  9.968   5.357   1.00 28.62  ? 474 HOH A O   1 
HETATM 2229 O  O   . HOH H 8 .   ? 18.004  7.970   -1.569  1.00 30.86  ? 475 HOH A O   1 
HETATM 2230 O  O   . HOH H 8 .   ? 17.393  -2.808  37.576  1.00 45.16  ? 476 HOH A O   1 
HETATM 2231 O  O   . HOH H 8 .   ? 23.780  -2.375  7.903   1.00 23.71  ? 477 HOH A O   1 
HETATM 2232 O  O   . HOH H 8 .   ? 12.172  -13.618 33.057  1.00 36.31  ? 478 HOH A O   1 
HETATM 2233 O  O   . HOH H 8 .   ? -3.813  6.617   8.641   1.00 40.44  ? 479 HOH A O   1 
HETATM 2234 O  O   . HOH H 8 .   ? 3.050   12.469  11.469  1.00 23.77  ? 480 HOH A O   1 
HETATM 2235 O  O   . HOH H 8 .   ? 16.482  -11.716 18.038  1.00 12.55  ? 481 HOH A O   1 
HETATM 2236 O  O   . HOH H 8 .   ? 29.706  -2.104  21.131  1.00 18.37  ? 482 HOH A O   1 
HETATM 2237 O  O   . HOH H 8 .   ? 7.435   12.267  27.877  1.00 22.41  ? 483 HOH A O   1 
HETATM 2238 O  O   . HOH H 8 .   ? -0.791  -12.229 18.802  1.00 47.62  ? 484 HOH A O   1 
HETATM 2239 O  O   . HOH H 8 .   ? 35.313  7.274   19.130  1.00 48.17  ? 485 HOH A O   1 
HETATM 2240 O  O   . HOH H 8 .   ? -4.360  11.619  13.602  1.00 40.88  ? 486 HOH A O   1 
HETATM 2241 O  O   . HOH H 8 .   ? 3.619   -14.518 21.893  1.00 38.11  ? 487 HOH A O   1 
HETATM 2242 O  O   . HOH H 8 .   ? 8.040   -15.043 26.666  1.00 23.30  ? 488 HOH A O   1 
HETATM 2243 O  O   . HOH H 8 .   ? 17.165  -14.160 24.423  1.00 18.24  ? 489 HOH A O   1 
HETATM 2244 O  O   . HOH H 8 .   ? -10.525 6.866   12.363  1.00 52.98  ? 490 HOH A O   1 
HETATM 2245 O  O   . HOH H 8 .   ? 4.074   -6.534  20.386  1.00 11.48  ? 491 HOH A O   1 
HETATM 2246 O  O   . HOH H 8 .   ? 13.010  -17.355 30.420  1.00 37.47  ? 492 HOH A O   1 
HETATM 2247 O  O   . HOH H 8 .   ? -0.512  -5.186  23.463  1.00 15.96  ? 493 HOH A O   1 
HETATM 2248 O  O   . HOH H 8 .   ? 7.336   22.019  15.179  1.00 24.07  ? 494 HOH A O   1 
HETATM 2249 O  O   . HOH H 8 .   ? -3.728  -5.769  9.159   1.00 22.81  ? 495 HOH A O   1 
HETATM 2250 O  O   . HOH H 8 .   ? -2.043  1.451   34.354  1.00 38.57  ? 496 HOH A O   1 
HETATM 2251 O  O   . HOH H 8 .   ? 2.354   -1.796  -2.574  1.00 32.43  ? 497 HOH A O   1 
HETATM 2252 O  O   . HOH H 8 .   ? 16.581  -14.007 0.901   1.00 34.19  ? 498 HOH A O   1 
HETATM 2253 O  O   . HOH H 8 .   ? 4.956   -10.476 24.395  1.00 23.33  ? 499 HOH A O   1 
HETATM 2254 O  O   . HOH H 8 .   ? 19.032  -2.696  -6.982  1.00 34.46  ? 500 HOH A O   1 
HETATM 2255 O  O   . HOH H 8 .   ? 22.410  -10.056 25.067  1.00 29.30  ? 501 HOH A O   1 
HETATM 2256 O  O   . HOH H 8 .   ? -5.343  4.875   20.929  1.00 34.60  ? 502 HOH A O   1 
HETATM 2257 O  O   . HOH H 8 .   ? 36.630  -0.406  14.593  1.00 27.49  ? 503 HOH A O   1 
HETATM 2258 O  O   . HOH H 8 .   ? 9.148   11.289  3.411   1.00 24.66  ? 504 HOH A O   1 
HETATM 2259 O  O   . HOH H 8 .   ? -5.260  5.605   15.565  1.00 31.22  ? 505 HOH A O   1 
HETATM 2260 O  O   . HOH H 8 .   ? 13.661  -6.939  32.634  1.00 22.02  ? 506 HOH A O   1 
HETATM 2261 O  O   . HOH H 8 .   ? 34.556  2.064   24.559  1.00 28.49  ? 507 HOH A O   1 
HETATM 2262 O  O   . HOH H 8 .   ? -0.248  -5.049  -1.727  1.00 42.05  ? 508 HOH A O   1 
HETATM 2263 O  O   . HOH H 8 .   ? 8.237   -7.001  -3.179  1.00 27.24  ? 509 HOH A O   1 
HETATM 2264 O  O   . HOH H 8 .   ? 1.795   11.987  9.007   1.00 18.39  ? 510 HOH A O   1 
HETATM 2265 O  O   . HOH H 8 .   ? 5.534   10.881  -2.141  1.00 31.14  ? 511 HOH A O   1 
HETATM 2266 O  O   . HOH H 8 .   ? 17.596  -11.520 25.197  1.00 16.05  ? 512 HOH A O   1 
HETATM 2267 O  O   . HOH H 8 .   ? 3.136   -18.666 8.059   1.00 17.44  ? 513 HOH A O   1 
HETATM 2268 O  O   . HOH H 8 .   ? 25.706  -0.949  29.137  1.00 28.05  ? 514 HOH A O   1 
HETATM 2269 O  O   . HOH H 8 .   ? -0.937  7.729   4.855   1.00 22.76  ? 515 HOH A O   1 
HETATM 2270 O  O   . HOH H 8 .   ? 14.278  -3.670  37.255  1.00 24.93  ? 516 HOH A O   1 
HETATM 2271 O  O   . HOH H 8 .   ? 16.829  -6.928  31.210  1.00 25.62  ? 517 HOH A O   1 
HETATM 2272 O  O   . HOH H 8 .   ? 13.999  -14.821 1.459   1.00 26.94  ? 518 HOH A O   1 
HETATM 2273 O  O   . HOH H 8 .   ? 9.111   4.754   30.651  1.00 26.00  ? 519 HOH A O   1 
HETATM 2274 O  O   . HOH H 8 .   ? 17.693  6.414   7.420   1.00 50.32  ? 520 HOH A O   1 
HETATM 2275 O  O   . HOH H 8 .   ? 24.646  -7.280  26.020  1.00 42.32  ? 521 HOH A O   1 
HETATM 2276 O  O   . HOH H 8 .   ? 20.421  -6.788  32.622  1.00 32.22  ? 522 HOH A O   1 
HETATM 2277 O  O   . HOH H 8 .   ? 3.795   -21.150 4.129   1.00 35.52  ? 523 HOH A O   1 
HETATM 2278 O  O   . HOH H 8 .   ? -2.126  -1.092  6.804   1.00 25.38  ? 524 HOH A O   1 
HETATM 2279 O  O   . HOH H 8 .   ? -2.814  -15.965 6.378   1.00 37.64  ? 525 HOH A O   1 
HETATM 2280 O  O   . HOH H 8 .   ? 22.167  -4.902  34.497  1.00 46.57  ? 526 HOH A O   1 
HETATM 2281 O  O   . HOH H 8 .   ? 9.871   -17.215 6.868   1.00 27.39  ? 527 HOH A O   1 
HETATM 2282 O  O   . HOH H 8 .   ? 25.445  -4.636  7.869   1.00 27.42  ? 528 HOH A O   1 
HETATM 2283 O  O   . HOH H 8 .   ? -5.678  -2.147  25.179  1.00 25.21  ? 529 HOH A O   1 
HETATM 2284 O  O   . HOH H 8 .   ? 20.781  -18.756 14.762  1.00 49.47  ? 530 HOH A O   1 
HETATM 2285 O  O   . HOH H 8 .   ? 24.898  -0.839  4.776   1.00 37.62  ? 531 HOH A O   1 
HETATM 2286 O  O   . HOH H 8 .   ? 23.705  -9.560  9.648   1.00 26.05  ? 532 HOH A O   1 
HETATM 2287 O  O   . HOH H 8 .   ? 22.885  9.851   25.079  1.00 20.40  ? 533 HOH A O   1 
HETATM 2288 O  O   . HOH H 8 .   ? 24.545  -11.759 12.045  1.00 40.50  ? 534 HOH A O   1 
HETATM 2289 O  O   . HOH H 8 .   ? 25.379  4.427   8.162   1.00 57.39  ? 535 HOH A O   1 
HETATM 2290 O  O   . HOH H 8 .   ? 25.053  6.381   10.938  1.00 44.35  ? 536 HOH A O   1 
HETATM 2291 O  O   . HOH H 8 .   ? -2.868  1.210   3.973   1.00 29.05  ? 537 HOH A O   1 
HETATM 2292 O  O   . HOH H 8 .   ? -3.724  7.476   6.496   1.00 54.75  ? 538 HOH A O   1 
HETATM 2293 O  O   . HOH H 8 .   ? 26.011  -3.212  21.094  1.00 18.61  ? 539 HOH A O   1 
HETATM 2294 O  O   . HOH H 8 .   ? 32.446  3.135   26.066  1.00 28.40  ? 540 HOH A O   1 
HETATM 2295 O  O   . HOH H 8 .   ? 14.611  -17.974 24.001  1.00 36.13  ? 541 HOH A O   1 
HETATM 2296 O  O   . HOH H 8 .   ? 28.800  -5.867  -0.317  1.00 32.45  ? 542 HOH A O   1 
HETATM 2297 O  O   . HOH H 8 .   ? 7.650   15.949  27.403  1.00 29.61  ? 543 HOH A O   1 
HETATM 2298 O  O   . HOH H 8 .   ? 8.526   9.797   28.941  1.00 28.14  ? 544 HOH A O   1 
HETATM 2299 O  O   . HOH H 8 .   ? 9.665   19.796  12.384  1.00 22.69  ? 545 HOH A O   1 
HETATM 2300 O  O   . HOH H 8 .   ? 2.542   -7.159  34.691  1.00 33.62  ? 546 HOH A O   1 
HETATM 2301 O  O   . HOH H 8 .   ? 2.081   14.107  13.146  1.00 44.58  ? 547 HOH A O   1 
HETATM 2302 O  O   . HOH H 8 .   ? 3.828   -5.479  39.732  1.00 38.71  ? 548 HOH A O   1 
HETATM 2303 O  O   . HOH H 8 .   ? -2.940  1.208   26.452  1.00 21.43  ? 549 HOH A O   1 
HETATM 2304 O  O   . HOH H 8 .   ? -5.068  -5.642  30.595  1.00 43.21  ? 550 HOH A O   1 
HETATM 2305 O  O   . HOH H 8 .   ? -1.169  -16.456 13.535  1.00 31.40  ? 551 HOH A O   1 
HETATM 2306 O  O   . HOH H 8 .   ? 11.930  -4.093  35.860  1.00 22.51  ? 552 HOH A O   1 
HETATM 2307 O  O   . HOH H 8 .   ? 19.540  -11.481 27.234  1.00 33.28  ? 553 HOH A O   1 
HETATM 2308 O  O   . HOH H 8 .   ? -3.088  1.755   31.695  1.00 48.08  ? 554 HOH A O   1 
HETATM 2309 O  O   . HOH H 8 .   ? 4.998   17.787  23.603  1.00 24.73  ? 555 HOH A O   1 
HETATM 2310 O  O   . HOH H 8 .   ? 23.567  -12.566 -0.732  1.00 45.69  ? 556 HOH A O   1 
HETATM 2311 O  O   . HOH H 8 .   ? -1.883  -9.765  14.069  1.00 23.18  ? 557 HOH A O   1 
HETATM 2312 O  O   . HOH H 8 .   ? 34.221  -4.079  24.564  1.00 34.01  ? 558 HOH A O   1 
HETATM 2313 O  O   . HOH H 8 .   ? 6.342   13.124  34.752  1.00 37.68  ? 559 HOH A O   1 
HETATM 2314 O  O   . HOH H 8 .   ? 29.672  5.379   27.834  1.00 44.45  ? 560 HOH A O   1 
HETATM 2315 O  O   . HOH H 8 .   ? 22.429  0.049   29.529  1.00 17.80  ? 561 HOH A O   1 
HETATM 2316 O  O   . HOH H 8 .   ? 6.145   21.866  17.656  1.00 31.27  ? 562 HOH A O   1 
HETATM 2317 O  O   . HOH H 8 .   ? 7.758   -16.627 14.743  1.00 22.22  ? 563 HOH A O   1 
HETATM 2318 O  O   . HOH H 8 .   ? 11.569  -6.205  34.046  1.00 24.99  ? 564 HOH A O   1 
HETATM 2319 O  O   . HOH H 8 .   ? 4.743   -8.064  32.944  1.00 22.57  ? 565 HOH A O   1 
HETATM 2320 O  O   . HOH H 8 .   ? 18.971  -10.568 22.859  1.00 14.19  ? 566 HOH A O   1 
HETATM 2321 O  O   . HOH H 8 .   ? 12.510  -18.062 26.590  1.00 39.37  ? 567 HOH A O   1 
HETATM 2322 O  O   . HOH H 8 .   ? 13.000  -17.573 21.695  1.00 21.61  ? 568 HOH A O   1 
HETATM 2323 O  O   . HOH H 8 .   ? 10.411  -17.766 27.382  1.00 47.93  ? 569 HOH A O   1 
HETATM 2324 O  O   . HOH H 8 .   ? 2.197   5.444   -3.446  1.00 39.94  ? 570 HOH A O   1 
HETATM 2325 O  O   . HOH H 8 .   ? -0.085  -17.671 6.602   1.00 29.92  ? 571 HOH A O   1 
HETATM 2326 O  O   . HOH H 8 .   ? 7.098   18.101  28.939  1.00 40.66  ? 572 HOH A O   1 
HETATM 2327 O  O   . HOH H 8 .   ? 16.874  13.799  11.289  1.00 34.23  ? 573 HOH A O   1 
HETATM 2328 O  O   . HOH H 8 .   ? 26.829  -1.065  6.674   1.00 40.14  ? 574 HOH A O   1 
HETATM 2329 O  O   . HOH H 8 .   ? 28.718  8.013   22.053  1.00 20.74  ? 575 HOH A O   1 
HETATM 2330 O  O   . HOH H 8 .   ? 31.409  -6.949  8.587   1.00 44.33  ? 576 HOH A O   1 
HETATM 2331 O  O   . HOH H 8 .   ? 14.153  3.312   35.862  1.00 42.27  ? 577 HOH A O   1 
HETATM 2332 O  O   . HOH H 8 .   ? 35.129  3.999   23.019  1.00 31.97  ? 578 HOH A O   1 
HETATM 2333 O  O   . HOH H 8 .   ? 15.648  5.418   -5.662  1.00 38.13  ? 579 HOH A O   1 
HETATM 2334 O  O   . HOH H 8 .   ? 8.277   5.602   -6.888  1.00 32.39  ? 580 HOH A O   1 
HETATM 2335 O  O   . HOH H 8 .   ? 26.203  -5.651  22.356  1.00 34.15  ? 581 HOH A O   1 
HETATM 2336 O  O   . HOH H 8 .   ? 14.505  -6.294  -7.266  1.00 38.62  ? 582 HOH A O   1 
HETATM 2337 O  O   . HOH H 8 .   ? 8.230   -16.685 31.870  1.00 30.87  ? 583 HOH A O   1 
HETATM 2338 O  O   . HOH H 8 .   ? 24.169  3.230   -1.835  1.00 41.80  ? 584 HOH A O   1 
HETATM 2339 O  O   . HOH H 8 .   ? 20.832  -12.489 22.258  1.00 35.41  ? 585 HOH A O   1 
HETATM 2340 O  O   . HOH H 8 .   ? 11.862  14.945  10.032  1.00 27.17  ? 586 HOH A O   1 
HETATM 2341 O  O   . HOH H 8 .   ? 29.748  -2.873  23.773  1.00 35.55  ? 587 HOH A O   1 
HETATM 2342 O  O   . HOH H 8 .   ? 27.318  -9.121  14.318  1.00 49.01  ? 588 HOH A O   1 
HETATM 2343 O  O   . HOH H 8 .   ? 16.841  6.805   10.131  1.00 48.64  ? 589 HOH A O   1 
HETATM 2344 O  O   . HOH H 8 .   ? 27.409  -4.073  6.547   1.00 36.49  ? 590 HOH A O   1 
HETATM 2345 O  O   . HOH H 8 .   ? 3.508   21.770  17.652  1.00 35.68  ? 591 HOH A O   1 
HETATM 2346 O  O   . HOH H 8 .   ? 8.299   -15.476 16.804  1.00 24.84  ? 592 HOH A O   1 
HETATM 2347 O  O   . HOH H 8 .   ? 36.239  -8.577  14.582  1.00 41.61  ? 593 HOH A O   1 
HETATM 2348 O  O   . HOH H 8 .   ? -2.567  10.346  3.419   1.00 37.83  ? 594 HOH A O   1 
HETATM 2349 O  O   . HOH H 8 .   ? 33.572  -1.482  13.020  1.00 41.38  ? 595 HOH A O   1 
HETATM 2350 O  O   . HOH H 8 .   ? 21.400  2.756   -6.615  1.00 36.60  ? 596 HOH A O   1 
HETATM 2351 O  O   . HOH H 8 .   ? 4.632   21.746  21.978  1.00 45.75  ? 597 HOH A O   1 
HETATM 2352 O  O   . HOH H 8 .   ? 13.440  10.023  8.848   1.00 43.74  ? 598 HOH A O   1 
HETATM 2353 O  O   . HOH H 8 .   ? 18.706  -10.421 31.476  1.00 41.80  ? 599 HOH A O   1 
HETATM 2354 O  O   . HOH H 8 .   ? 17.232  8.449   6.208   1.00 42.55  ? 600 HOH A O   1 
HETATM 2355 O  O   . HOH H 8 .   ? 19.103  -15.814 25.299  1.00 40.46  ? 601 HOH A O   1 
HETATM 2356 O  O   . HOH H 8 .   ? 23.948  -11.591 8.012   1.00 37.64  ? 602 HOH A O   1 
HETATM 2357 O  O   . HOH H 8 .   ? 20.469  12.529  24.968  1.00 41.88  ? 603 HOH A O   1 
HETATM 2358 O  O   . HOH H 8 .   ? -5.997  -4.614  7.882   1.00 43.75  ? 604 HOH A O   1 
HETATM 2359 O  O   . HOH H 8 .   ? 12.112  11.564  6.852   1.00 46.43  ? 605 HOH A O   1 
HETATM 2360 O  O   . HOH H 8 .   ? 19.855  -9.423  28.987  1.00 25.55  ? 606 HOH A O   1 
HETATM 2361 O  O   . HOH H 8 .   ? 4.230   -16.213 20.225  1.00 43.39  ? 607 HOH A O   1 
HETATM 2362 O  O   . HOH H 8 .   ? 22.893  -12.549 20.819  1.00 51.76  ? 608 HOH A O   1 
HETATM 2363 O  O   . HOH H 8 .   ? 4.203   -12.096 26.289  1.00 33.31  ? 609 HOH A O   1 
HETATM 2364 O  O   . HOH H 8 .   ? -2.849  -5.493  0.160   1.00 41.75  ? 610 HOH A O   1 
HETATM 2365 O  O   . HOH H 8 .   ? 15.928  -8.072  33.833  1.00 40.33  ? 611 HOH A O   1 
HETATM 2366 O  O   . HOH H 8 .   ? 9.289   12.749  1.000   1.00 32.83  ? 612 HOH A O   1 
HETATM 2367 O  O   . HOH H 8 .   ? 15.975  -5.880  37.408  1.00 33.10  ? 613 HOH A O   1 
HETATM 2368 O  O   . HOH H 8 .   ? 25.649  10.376  28.861  1.00 42.49  ? 614 HOH A O   1 
HETATM 2369 O  O   . HOH H 8 .   ? 20.948  -5.121  -7.123  1.00 52.82  ? 615 HOH A O   1 
HETATM 2370 O  O   . HOH H 8 .   ? 8.633   15.638  4.810   1.00 35.02  ? 616 HOH A O   1 
HETATM 2371 O  O   . HOH H 8 .   ? -5.584  0.602   25.915  1.00 27.17  ? 617 HOH A O   1 
HETATM 2372 O  O   . HOH H 8 .   ? 25.045  10.622  23.646  1.00 33.81  ? 618 HOH A O   1 
HETATM 2373 O  O   . HOH H 8 .   ? 8.339   -17.766 26.357  1.00 39.02  ? 619 HOH A O   1 
HETATM 2374 O  O   . HOH H 8 .   ? 1.073   -13.663 22.460  1.00 48.44  ? 620 HOH A O   1 
HETATM 2375 O  O   . HOH H 8 .   ? 27.848  10.138  18.127  1.00 40.35  ? 621 HOH A O   1 
HETATM 2376 O  O   . HOH H 8 .   ? 19.518  4.962   -7.127  1.00 33.13  ? 622 HOH A O   1 
HETATM 2377 O  O   . HOH H 8 .   ? 25.159  -10.297 23.110  1.00 52.97  ? 623 HOH A O   1 
HETATM 2378 O  O   . HOH H 8 .   ? 3.597   13.011  -1.916  1.00 28.95  ? 624 HOH A O   1 
HETATM 2379 O  O   . HOH H 8 .   ? -6.879  0.432   28.384  1.00 35.94  ? 625 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS A 4   ? 0.7494 0.6315 0.5343 -0.2804 0.1808  0.0734  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.5485 0.4745 0.4274 -0.0999 0.3147  0.0108  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.4606 0.3700 0.2752 -0.0515 0.1524  -0.0046 4   HIS A C   
4    O  O   . HIS A 4   ? 0.4745 0.3509 0.4131 -0.0739 0.1843  0.0245  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.4907 0.3869 0.7580 0.0110  0.3549  0.0300  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.5374 0.7029 0.8909 0.0346  0.0422  0.3486  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.6680 1.0599 1.0125 0.0890  0.1198  0.2358  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.7904 0.9521 0.4611 -0.1826 0.1897  0.2037  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 1.0768 1.0355 0.9987 0.0820  0.0018  0.5059  4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 1.0082 1.1806 1.0296 0.1134  -0.0960 0.4203  4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.2727 0.3567 0.2879 -0.0958 0.0970  -0.0046 5   TRP A N   
12   C  CA  . TRP A 5   ? 0.2032 0.2518 0.2613 -0.0580 0.0820  -0.0276 5   TRP A CA  
13   C  C   . TRP A 5   ? 0.2025 0.2213 0.2970 -0.0210 0.0575  -0.0286 5   TRP A C   
14   O  O   . TRP A 5   ? 0.2260 0.2791 0.2760 -0.0538 0.0897  -0.0192 5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1890 0.2360 0.3241 -0.0058 0.1128  -0.0201 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.2222 0.2216 0.2688 -0.0275 0.0433  -0.0383 5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.2825 0.2363 0.2665 -0.0269 0.0760  -0.0196 5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1993 0.2319 0.2059 -0.0175 0.0114  -0.0370 5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.2659 0.2730 0.2484 -0.0079 0.0600  0.0597  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.2137 0.3068 0.2133 -0.0132 0.0387  0.0094  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1541 0.2434 0.2073 -0.0168 0.0574  -0.0483 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.2204 0.3227 0.2301 0.0092  0.0031  -0.0095 5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1682 0.2784 0.1844 0.0116  0.0373  -0.0444 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.2127 0.2910 0.1732 0.0223  -0.0129 -0.0471 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1648 0.2106 0.2597 -0.0239 0.0854  -0.0579 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.2158 0.2350 0.2609 -0.0584 0.0664  -0.0155 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.2034 0.1941 0.2357 0.0225  0.0803  -0.0113 6   GLY A C   
28   O  O   . GLY A 6   ? 0.1476 0.2706 0.2367 -0.0450 0.0513  -0.0297 6   GLY A O   
29   N  N   . TYR A 7   ? 0.1861 0.2346 0.2618 -0.0304 0.0974  -0.0401 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.2022 0.2345 0.2911 -0.0381 0.0922  -0.0321 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.2036 0.2802 0.4217 -0.0051 0.1027  -0.0154 7   TYR A C   
32   O  O   . TYR A 7   ? 0.2888 0.2724 0.7076 -0.0364 0.2215  -0.0309 7   TYR A O   
33   C  CB  . TYR A 7   ? 0.1983 0.2341 0.2889 -0.0290 0.0803  -0.0511 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1578 0.1998 0.1912 -0.0451 0.0374  -0.0397 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.1565 0.2221 0.1953 -0.0583 0.0496  -0.0543 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.1885 0.1933 0.2302 -0.0390 0.0359  -0.0252 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.1506 0.1799 0.1903 -0.0366 0.0009  -0.0305 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.1950 0.2213 0.1838 -0.0584 0.0449  -0.0358 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.1316 0.2291 0.1800 -0.0314 0.0430  -0.0140 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.1826 0.2400 0.1928 0.0082  0.0312  -0.0407 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.1580 0.2824 0.4278 0.0138  0.0790  -0.0779 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.2835 0.2027 0.5777 -0.0091 0.1620  -0.0974 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.2917 0.2561 0.4842 0.0538  0.1894  0.0055  8   GLY A C   
44   O  O   . GLY A 8   ? 0.3014 0.3186 0.5624 -0.0136 0.2624  -0.0658 8   GLY A O   
45   N  N   . LYS A 9   ? 0.3475 0.2518 0.7203 0.0453  0.2175  -0.0536 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.3189 0.3060 0.7623 0.0111  0.1505  -0.0282 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.2131 0.4041 0.7120 -0.0052 0.1337  0.1001  9   LYS A C   
48   O  O   . LYS A 9   ? 0.3521 0.3021 0.6308 0.0168  0.0732  -0.0223 9   LYS A O   
49   C  CB  . LYS A 9   ? 0.5161 0.3657 0.8237 0.1672  0.0916  0.0215  9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.5136 0.7043 0.4135 -0.1638 0.0168  0.0262  9   LYS A CG  
51   C  CD  . LYS A 9   ? 0.8779 0.6982 0.6442 -0.3890 -0.1805 0.1032  9   LYS A CD  
52   C  CE  . LYS A 9   ? 0.9256 0.6631 1.1454 -0.5071 0.0176  0.0632  9   LYS A CE  
53   N  NZ  . LYS A 9   ? 0.9128 1.0605 0.8038 -0.4834 -0.0265 0.0992  9   LYS A NZ  
54   N  N   . HIS A 10  ? 0.3053 0.2499 0.5939 0.0127  0.2461  -0.0599 10  HIS A N   
55   C  CA  . HIS A 10  ? 0.1865 0.3244 0.4652 0.0323  0.1263  -0.0739 10  HIS A CA  
56   C  C   . HIS A 10  ? 0.1513 0.2935 0.3973 0.0499  0.1274  0.0200  10  HIS A C   
57   O  O   . HIS A 10  ? 0.1951 0.2884 0.5614 -0.0122 0.1872  -0.0551 10  HIS A O   
58   C  CB  . HIS A 10  ? 0.2738 0.3324 0.5234 0.0078  0.2393  -0.0737 10  HIS A CB  
59   C  CG  . HIS A 10  ? 0.2496 0.3319 0.5079 -0.0069 0.1606  -0.0400 10  HIS A CG  
60   N  ND1 . HIS A 10  ? 0.3237 0.3100 0.5501 0.0951  0.2044  0.0832  10  HIS A ND1 
61   C  CD2 . HIS A 10  ? 0.3158 0.3306 0.6567 -0.0469 0.0943  -0.0696 10  HIS A CD2 
62   C  CE1 . HIS A 10  ? 0.3452 0.2748 0.3362 -0.0318 0.1463  0.0097  10  HIS A CE1 
63   N  NE2 . HIS A 10  ? 0.3631 0.4419 0.5690 0.0850  0.0750  -0.2172 10  HIS A NE2 
64   N  N   . ASN A 11  ? 0.1332 0.2744 0.3784 0.0138  0.1293  -0.0271 11  ASN A N   
65   C  CA  . ASN A 11  ? 0.1750 0.2449 0.3093 0.0122  0.1221  -0.0197 11  ASN A CA  
66   C  C   . ASN A 11  ? 0.1391 0.2355 0.3502 -0.0006 0.1083  -0.0431 11  ASN A C   
67   O  O   . ASN A 11  ? 0.1660 0.2332 0.3003 0.0036  0.0807  -0.0223 11  ASN A O   
68   C  CB  . ASN A 11  ? 0.2163 0.2409 0.3369 -0.0177 0.1485  -0.0119 11  ASN A CB  
69   C  CG  . ASN A 11  ? 0.2253 0.2796 0.3507 -0.0080 0.1224  -0.0233 11  ASN A CG  
70   O  OD1 . ASN A 11  ? 0.2626 0.3312 0.3991 -0.0822 0.1463  -0.0575 11  ASN A OD1 
71   N  ND2 . ASN A 11  ? 0.2676 0.3304 0.3191 -0.0178 0.1260  -0.0210 11  ASN A ND2 
72   N  N   . GLY A 12  ? 0.1462 0.2690 0.3226 -0.0104 0.1117  -0.0190 12  GLY A N   
73   C  CA  . GLY A 12  ? 0.1459 0.2666 0.2407 0.0093  0.0913  -0.0253 12  GLY A CA  
74   C  C   . GLY A 12  ? 0.1430 0.2212 0.2447 0.0046  0.0620  0.0051  12  GLY A C   
75   O  O   . GLY A 12  ? 0.1125 0.2357 0.2855 0.0120  0.0486  0.0179  12  GLY A O   
76   N  N   . PRO A 13  ? 0.1136 0.1815 0.2600 -0.0006 0.0540  -0.0334 13  PRO A N   
77   C  CA  . PRO A 13  ? 0.1361 0.1911 0.2357 -0.0141 0.0515  -0.0080 13  PRO A CA  
78   C  C   . PRO A 13  ? 0.1326 0.1904 0.2640 0.0057  0.0414  -0.0128 13  PRO A C   
79   O  O   . PRO A 13  ? 0.1037 0.2196 0.2809 -0.0012 0.0298  -0.0347 13  PRO A O   
80   C  CB  . PRO A 13  ? 0.1545 0.2293 0.2608 -0.0321 0.0800  -0.0296 13  PRO A CB  
81   C  CG  . PRO A 13  ? 0.1969 0.2027 0.2165 -0.0488 0.0681  -0.0553 13  PRO A CG  
82   C  CD  . PRO A 13  ? 0.1463 0.2456 0.2054 -0.0378 0.0363  -0.0228 13  PRO A CD  
83   N  N   . GLU A 14  ? 0.1400 0.1901 0.2952 0.0089  0.0340  0.0414  14  GLU A N   
84   C  CA  . GLU A 14  ? 0.1425 0.2091 0.4052 0.0135  -0.0265 0.0500  14  GLU A CA  
85   C  C   . GLU A 14  ? 0.1039 0.2328 0.3403 0.0323  0.0260  0.0158  14  GLU A C   
86   O  O   . GLU A 14  ? 0.1405 0.2672 0.3498 0.0282  -0.0114 0.0179  14  GLU A O   
87   C  CB  . GLU A 14  ? 0.3690 0.3033 0.4598 0.1749  -0.0637 0.0294  14  GLU A CB  
88   C  CG  . GLU A 14  ? 0.2217 0.5898 0.5528 -0.0471 -0.0159 -0.0403 14  GLU A CG  
89   C  CD  . GLU A 14  ? 0.4684 0.5261 0.5958 0.2349  -0.1082 -0.1879 14  GLU A CD  
90   O  OE1 . GLU A 14  ? 0.2914 0.2925 0.4674 0.0523  -0.0055 -0.1461 14  GLU A OE1 
91   O  OE2 . GLU A 14  ? 0.3898 0.3534 0.5650 0.0524  -0.0160 -0.1497 14  GLU A OE2 
92   N  N   . HIS A 15  ? 0.1177 0.1749 0.3189 0.0049  0.0226  -0.0042 15  HIS A N   
93   C  CA  . HIS A 15  ? 0.1181 0.1980 0.3754 0.0148  0.0430  0.0173  15  HIS A CA  
94   C  C   . HIS A 15  ? 0.0858 0.2001 0.2546 0.0111  0.0277  0.0132  15  HIS A C   
95   O  O   . HIS A 15  ? 0.0725 0.2274 0.3139 0.0008  0.0264  0.0143  15  HIS A O   
96   C  CB  . HIS A 15  ? 0.1014 0.2460 0.3696 0.0229  0.0520  0.0046  15  HIS A CB  
97   C  CG  . HIS A 15  ? 0.1217 0.2425 0.3736 0.0082  0.0640  -0.0143 15  HIS A CG  
98   N  ND1 . HIS A 15  ? 0.1391 0.2604 0.4426 0.0391  0.0490  -0.0564 15  HIS A ND1 
99   C  CD2 . HIS A 15  ? 0.2039 0.2142 0.4256 0.0467  0.1015  -0.0435 15  HIS A CD2 
100  C  CE1 . HIS A 15  ? 0.2813 0.2975 0.4784 0.0974  0.0377  -0.0983 15  HIS A CE1 
101  N  NE2 . HIS A 15  ? 0.2403 0.2965 0.5037 0.0983  0.1083  -0.0473 15  HIS A NE2 
102  N  N   . TRP A 16  ? 0.0813 0.1854 0.2916 0.0108  0.0258  0.0241  16  TRP A N   
103  C  CA  . TRP A 16  ? 0.0677 0.1825 0.2782 0.0186  0.0148  -0.0030 16  TRP A CA  
104  C  C   . TRP A 16  ? 0.0682 0.2009 0.2705 0.0037  0.0159  0.0127  16  TRP A C   
105  O  O   . TRP A 16  ? 0.0946 0.1903 0.2967 0.0024  0.0099  0.0095  16  TRP A O   
106  C  CB  . TRP A 16  ? 0.0628 0.2007 0.2719 0.0025  0.0089  -0.0243 16  TRP A CB  
107  C  CG  . TRP A 16  ? 0.0797 0.1716 0.2469 0.0034  0.0326  -0.0085 16  TRP A CG  
108  C  CD1 . TRP A 16  ? 0.0775 0.2185 0.2434 -0.0079 0.0480  -0.0133 16  TRP A CD1 
109  C  CD2 . TRP A 16  ? 0.0811 0.1757 0.1976 -0.0002 0.0286  0.0013  16  TRP A CD2 
110  N  NE1 . TRP A 16  ? 0.0847 0.1972 0.2496 0.0017  0.0452  -0.0306 16  TRP A NE1 
111  C  CE2 . TRP A 16  ? 0.0777 0.1887 0.2303 0.0142  0.0295  -0.0054 16  TRP A CE2 
112  C  CE3 . TRP A 16  ? 0.0714 0.1527 0.2278 -0.0099 0.0364  0.0006  16  TRP A CE3 
113  C  CZ2 . TRP A 16  ? 0.0863 0.1495 0.2112 -0.0027 0.0414  -0.0062 16  TRP A CZ2 
114  C  CZ3 . TRP A 16  ? 0.0844 0.1595 0.2168 -0.0149 0.0279  -0.0297 16  TRP A CZ3 
115  C  CH2 . TRP A 16  ? 0.0928 0.1656 0.2090 -0.0063 0.0505  -0.0233 16  TRP A CH2 
116  N  N   . HIS A 17  ? 0.0784 0.1951 0.2528 0.0032  0.0069  -0.0035 17  HIS A N   
117  C  CA  . HIS A 17  ? 0.0964 0.2239 0.2638 -0.0096 0.0012  -0.0015 17  HIS A CA  
118  C  C   . HIS A 17  ? 0.0833 0.2576 0.3450 -0.0109 0.0016  -0.0113 17  HIS A C   
119  O  O   . HIS A 17  ? 0.0856 0.2459 0.3243 -0.0140 0.0020  -0.0039 17  HIS A O   
120  C  CB  . HIS A 17  ? 0.0885 0.2296 0.2755 0.0223  0.0012  -0.0006 17  HIS A CB  
121  C  CG  . HIS A 17  ? 0.0880 0.2289 0.3247 0.0175  -0.0216 0.0209  17  HIS A CG  
122  N  ND1 . HIS A 17  ? 0.0883 0.3018 0.3583 0.0016  -0.0254 0.0339  17  HIS A ND1 
123  C  CD2 . HIS A 17  ? 0.1393 0.2321 0.3283 0.0623  0.0159  0.0323  17  HIS A CD2 
124  C  CE1 . HIS A 17  ? 0.1263 0.3129 0.3376 0.0468  -0.0276 0.0541  17  HIS A CE1 
125  N  NE2 . HIS A 17  ? 0.1469 0.2606 0.3460 0.0586  0.0148  0.0691  17  HIS A NE2 
126  N  N   . LYS A 18  ? 0.0704 0.2503 0.3421 0.0061  0.0009  0.0328  18  LYS A N   
127  C  CA  . LYS A 18  ? 0.0870 0.2562 0.3743 -0.0076 0.0358  0.0174  18  LYS A CA  
128  C  C   . LYS A 18  ? 0.1201 0.2676 0.3948 -0.0363 -0.0121 0.0379  18  LYS A C   
129  O  O   . LYS A 18  ? 0.1650 0.2856 0.5671 -0.0695 -0.0745 0.0927  18  LYS A O   
130  C  CB  . LYS A 18  ? 0.1145 0.2423 0.3836 0.0287  0.0315  0.0681  18  LYS A CB  
131  C  CG  . LYS A 18  ? 0.1195 0.2433 0.3333 0.0336  0.0055  0.0348  18  LYS A CG  
132  C  CD  . LYS A 18  ? 0.1014 0.2644 0.3549 0.0451  0.0167  0.0396  18  LYS A CD  
133  C  CE  . LYS A 18  ? 0.0996 0.2947 0.3527 0.0255  0.0302  0.0203  18  LYS A CE  
134  N  NZ  . LYS A 18  ? 0.1244 0.3089 0.3061 0.0565  0.0256  0.0431  18  LYS A NZ  
135  N  N   . ASP A 19  ? 0.1222 0.2381 0.3112 0.0042  0.0039  0.0411  19  ASP A N   
136  C  CA  . ASP A 19  ? 0.1490 0.1962 0.3205 -0.0030 0.0236  0.0105  19  ASP A CA  
137  C  C   . ASP A 19  ? 0.1113 0.1759 0.3536 -0.0464 0.0321  0.0025  19  ASP A C   
138  O  O   . ASP A 19  ? 0.1375 0.1876 0.4641 -0.0397 0.0431  0.0198  19  ASP A O   
139  C  CB  . ASP A 19  ? 0.1860 0.3557 0.2875 0.0545  -0.0111 0.0569  19  ASP A CB  
140  C  CG  . ASP A 19  ? 0.4200 0.4095 0.4516 0.0791  0.1981  0.0214  19  ASP A CG  
141  O  OD1 . ASP A 19  ? 0.4249 0.4164 0.5091 0.1002  0.1467  0.0882  19  ASP A OD1 
142  O  OD2 . ASP A 19  ? 0.7438 0.4782 0.5540 0.2584  0.0820  0.0077  19  ASP A OD2 
143  N  N   . PHE A 20  ? 0.0788 0.2161 0.2985 -0.0285 0.0150  0.0043  20  PHE A N   
144  C  CA  . PHE A 20  ? 0.0664 0.2375 0.3500 0.0051  0.0061  0.0096  20  PHE A CA  
145  C  C   . PHE A 20  ? 0.1063 0.2213 0.3435 -0.0113 0.0018  -0.0299 20  PHE A C   
146  O  O   . PHE A 20  ? 0.0974 0.2224 0.3075 -0.0275 -0.0029 -0.0330 20  PHE A O   
147  C  CB  . PHE A 20  ? 0.0989 0.2361 0.2766 -0.0289 0.0131  0.0082  20  PHE A CB  
148  C  CG  . PHE A 20  ? 0.0919 0.2378 0.2787 -0.0145 0.0166  0.0024  20  PHE A CG  
149  C  CD1 . PHE A 20  ? 0.0998 0.2684 0.3279 -0.0179 0.0048  0.0414  20  PHE A CD1 
150  C  CD2 . PHE A 20  ? 0.1059 0.2594 0.2651 -0.0152 0.0023  -0.0066 20  PHE A CD2 
151  C  CE1 . PHE A 20  ? 0.1025 0.3438 0.3226 -0.0040 0.0227  0.0505  20  PHE A CE1 
152  C  CE2 . PHE A 20  ? 0.1273 0.3147 0.2889 -0.0333 -0.0094 0.0291  20  PHE A CE2 
153  C  CZ  . PHE A 20  ? 0.1169 0.3273 0.3409 -0.0206 0.0401  0.0540  20  PHE A CZ  
154  N  N   . PRO A 21  ? 0.1100 0.2122 0.3079 -0.0267 0.0020  -0.0253 21  PRO A N   
155  C  CA  . PRO A 21  ? 0.0804 0.3324 0.2996 -0.0568 -0.0188 -0.0271 21  PRO A CA  
156  C  C   . PRO A 21  ? 0.1016 0.2230 0.2810 -0.0293 -0.0179 -0.0255 21  PRO A C   
157  O  O   . PRO A 21  ? 0.1217 0.2163 0.3204 -0.0170 -0.0531 0.0016  21  PRO A O   
158  C  CB  . PRO A 21  ? 0.1144 0.3039 0.4740 -0.1074 -0.0172 -0.0183 21  PRO A CB  
159  C  CG  . PRO A 21  ? 0.2312 0.3094 0.4795 -0.1647 -0.0782 -0.0339 21  PRO A CG  
160  C  CD  . PRO A 21  ? 0.1068 0.2546 0.4385 -0.0688 -0.0450 0.0131  21  PRO A CD  
161  N  N   . ILE A 22  ? 0.0885 0.2168 0.2807 -0.0239 -0.0131 -0.0578 22  ILE A N   
162  C  CA  . ILE A 22  ? 0.1238 0.1789 0.2590 -0.0100 -0.0091 -0.0299 22  ILE A CA  
163  C  C   . ILE A 22  ? 0.1110 0.1735 0.2413 -0.0065 -0.0210 -0.0054 22  ILE A C   
164  O  O   . ILE A 22  ? 0.1102 0.1951 0.2626 -0.0105 0.0031  -0.0265 22  ILE A O   
165  C  CB  . ILE A 22  ? 0.1152 0.1980 0.2706 0.0115  -0.0239 -0.0409 22  ILE A CB  
166  C  CG1 . ILE A 22  ? 0.1003 0.3075 0.3327 -0.0226 -0.0082 -0.1108 22  ILE A CG1 
167  C  CG2 . ILE A 22  ? 0.1194 0.2154 0.2407 -0.0179 -0.0113 0.0018  22  ILE A CG2 
168  C  CD1 . ILE A 22  ? 0.2005 0.3697 0.3600 -0.0134 -0.0577 -0.1483 22  ILE A CD1 
169  N  N   . ALA A 23  ? 0.1032 0.1759 0.2730 -0.0146 -0.0362 -0.0392 23  ALA A N   
170  C  CA  . ALA A 23  ? 0.1032 0.1828 0.2536 -0.0085 -0.0033 -0.0159 23  ALA A CA  
171  C  C   . ALA A 23  ? 0.1029 0.2137 0.2375 -0.0128 0.0083  -0.0227 23  ALA A C   
172  O  O   . ALA A 23  ? 0.1300 0.2041 0.2590 -0.0036 0.0057  -0.0122 23  ALA A O   
173  C  CB  . ALA A 23  ? 0.1093 0.2044 0.2867 0.0006  0.0353  -0.0499 23  ALA A CB  
174  N  N   . LYS A 24  ? 0.1217 0.2432 0.2481 0.0136  -0.0122 -0.0126 24  LYS A N   
175  C  CA  . LYS A 24  ? 0.1077 0.2863 0.2382 0.0126  -0.0009 0.0115  24  LYS A CA  
176  C  C   . LYS A 24  ? 0.1650 0.3147 0.2364 0.0205  -0.0229 -0.0232 24  LYS A C   
177  O  O   . LYS A 24  ? 0.1822 0.3718 0.2400 0.0150  -0.0207 -0.0553 24  LYS A O   
178  C  CB  . LYS A 24  ? 0.1242 0.3294 0.2843 0.0290  -0.0280 0.0086  24  LYS A CB  
179  C  CG  . LYS A 24  ? 0.1922 0.3524 0.3353 0.0849  0.0275  0.0290  24  LYS A CG  
180  C  CD  . LYS A 24  ? 0.2151 0.4177 0.4609 0.1314  0.0089  0.0590  24  LYS A CD  
181  C  CE  . LYS A 24  ? 0.2084 0.4304 0.4562 0.0679  -0.0116 0.0458  24  LYS A CE  
182  N  NZ  . LYS A 24  ? 0.3256 0.4882 0.6398 -0.0731 0.0656  0.0690  24  LYS A NZ  
183  N  N   . GLY A 25  ? 0.1380 0.2690 0.2457 0.0084  -0.0043 -0.0550 25  GLY A N   
184  C  CA  . GLY A 25  ? 0.1874 0.2439 0.2393 -0.0168 -0.0220 -0.0560 25  GLY A CA  
185  C  C   . GLY A 25  ? 0.1537 0.2738 0.2064 -0.0013 -0.0425 -0.0569 25  GLY A C   
186  O  O   . GLY A 25  ? 0.1501 0.2996 0.2348 -0.0201 -0.0217 -0.0408 25  GLY A O   
187  N  N   . GLU A 26  ? 0.1590 0.3327 0.1796 0.0285  -0.0562 -0.0672 26  GLU A N   
188  C  CA  . GLU A 26  ? 0.1714 0.4213 0.1490 0.0361  -0.0506 -0.0776 26  GLU A CA  
189  C  C   . GLU A 26  ? 0.1743 0.2541 0.1455 0.0208  -0.0340 -0.0473 26  GLU A C   
190  O  O   . GLU A 26  ? 0.2106 0.2881 0.1517 0.0049  -0.0391 -0.0237 26  GLU A O   
191  C  CB  . GLU A 26  ? 0.1912 0.5375 0.2468 -0.0043 -0.0332 -0.1881 26  GLU A CB  
192  C  CG  . GLU A 26  ? 0.2722 0.7507 0.3460 0.0163  -0.1410 -0.1894 26  GLU A CG  
193  C  CD  . GLU A 26  ? 0.4763 0.7860 0.5022 0.0241  -0.2199 -0.0536 26  GLU A CD  
194  O  OE1 . GLU A 26  ? 0.4494 0.7440 0.5683 -0.0704 -0.2569 -0.0116 26  GLU A OE1 
195  O  OE2 . GLU A 26  ? 0.5367 0.8374 0.5313 0.1542  -0.2556 -0.1217 26  GLU A OE2 
196  N  N   A ARG A 27  ? 0.1346 0.2156 0.1330 0.0066  -0.0198 -0.0592 27  ARG A N   
197  N  N   B ARG A 27  ? 0.1638 0.2342 0.1429 0.0111  -0.0350 -0.0606 27  ARG A N   
198  C  CA  A ARG A 27  ? 0.1368 0.1632 0.1303 -0.0077 -0.0276 -0.0287 27  ARG A CA  
199  C  CA  B ARG A 27  ? 0.1681 0.2199 0.1693 0.0015  -0.0442 -0.0744 27  ARG A CA  
200  C  C   A ARG A 27  ? 0.1093 0.1576 0.1313 -0.0114 -0.0009 -0.0289 27  ARG A C   
201  C  C   B ARG A 27  ? 0.1172 0.1772 0.1504 0.0065  -0.0070 -0.0325 27  ARG A C   
202  O  O   A ARG A 27  ? 0.1283 0.1427 0.1461 -0.0039 -0.0138 -0.0256 27  ARG A O   
203  O  O   B ARG A 27  ? 0.1444 0.2068 0.1445 -0.0041 -0.0188 -0.0083 27  ARG A O   
204  C  CB  A ARG A 27  ? 0.1560 0.1621 0.1050 -0.0040 -0.0020 -0.0097 27  ARG A CB  
205  C  CB  B ARG A 27  ? 0.2521 0.2583 0.2206 0.0466  -0.0076 -0.0785 27  ARG A CB  
206  C  CG  A ARG A 27  ? 0.1802 0.1459 0.1696 -0.0135 -0.0298 -0.0490 27  ARG A CG  
207  C  CG  B ARG A 27  ? 0.1910 0.3168 0.3129 0.0379  -0.0866 -0.0092 27  ARG A CG  
208  C  CD  A ARG A 27  ? 0.2228 0.1549 0.1587 0.0083  -0.0310 -0.0326 27  ARG A CD  
209  C  CD  B ARG A 27  ? 0.2533 0.4986 0.2519 0.1588  -0.0408 0.0389  27  ARG A CD  
210  N  NE  A ARG A 27  ? 0.1818 0.2113 0.1632 0.0220  0.0356  -0.0712 27  ARG A NE  
211  N  NE  B ARG A 27  ? 0.3068 0.5205 0.5717 0.2498  0.0840  0.0705  27  ARG A NE  
212  C  CZ  A ARG A 27  ? 0.1940 0.2654 0.1689 -0.0225 -0.0020 -0.0536 27  ARG A CZ  
213  C  CZ  B ARG A 27  ? 0.2471 0.1208 0.3122 0.0085  -0.0009 -0.0111 27  ARG A CZ  
214  N  NH1 A ARG A 27  ? 0.2061 0.3603 0.1793 0.0001  -0.0484 -0.0785 27  ARG A NH1 
215  N  NH1 B ARG A 27  ? 0.0731 0.0885 0.0461 -0.0030 -0.0055 -0.0413 27  ARG A NH1 
216  N  NH2 A ARG A 27  ? 0.1573 0.2925 0.2830 0.0148  0.0319  -0.0647 27  ARG A NH2 
217  N  NH2 B ARG A 27  ? 0.2382 0.0889 0.1797 -0.0206 0.0886  -0.0868 27  ARG A NH2 
218  N  N   . GLN A 28  ? 0.1145 0.1656 0.1502 -0.0031 -0.0182 -0.0486 28  GLN A N   
219  C  CA  . GLN A 28  ? 0.1018 0.1674 0.1526 0.0027  -0.0258 -0.0542 28  GLN A CA  
220  C  C   . GLN A 28  ? 0.1029 0.1463 0.1368 0.0000  -0.0013 -0.0231 28  GLN A C   
221  O  O   . GLN A 28  ? 0.1359 0.1745 0.1323 -0.0219 -0.0087 -0.0135 28  GLN A O   
222  C  CB  . GLN A 28  ? 0.0820 0.1853 0.1887 -0.0023 -0.0111 -0.0427 28  GLN A CB  
223  C  CG  . GLN A 28  ? 0.1016 0.1865 0.1923 0.0006  -0.0194 -0.0355 28  GLN A CG  
224  C  CD  . GLN A 28  ? 0.0953 0.1707 0.1777 -0.0186 -0.0150 -0.0352 28  GLN A CD  
225  O  OE1 . GLN A 28  ? 0.1254 0.1671 0.1707 -0.0127 0.0041  -0.0341 28  GLN A OE1 
226  N  NE2 . GLN A 28  ? 0.0876 0.1605 0.2306 -0.0147 -0.0237 -0.0348 28  GLN A NE2 
227  N  N   . SER A 29  ? 0.1007 0.1361 0.1304 0.0006  -0.0010 -0.0317 29  SER A N   
228  C  CA  . SER A 29  ? 0.0989 0.1143 0.1493 0.0042  -0.0086 -0.0282 29  SER A CA  
229  C  C   . SER A 29  ? 0.0970 0.1309 0.1222 0.0057  0.0050  0.0002  29  SER A C   
230  O  O   . SER A 29  ? 0.0874 0.1468 0.1574 -0.0062 0.0065  -0.0100 29  SER A O   
231  C  CB  . SER A 29  ? 0.1110 0.1509 0.1312 0.0174  0.0034  -0.0044 29  SER A CB  
232  O  OG  . SER A 29  ? 0.1045 0.1463 0.1433 0.0110  0.0141  -0.0206 29  SER A OG  
233  N  N   . PRO A 30  ? 0.0908 0.1412 0.1208 -0.0004 0.0146  -0.0124 30  PRO A N   
234  C  CA  . PRO A 30  ? 0.0865 0.1447 0.1169 -0.0142 0.0029  -0.0006 30  PRO A CA  
235  C  C   . PRO A 30  ? 0.1005 0.1312 0.1183 -0.0001 -0.0027 -0.0208 30  PRO A C   
236  O  O   . PRO A 30  ? 0.1070 0.1614 0.1279 0.0040  -0.0142 -0.0126 30  PRO A O   
237  C  CB  . PRO A 30  ? 0.0969 0.1463 0.1252 0.0060  0.0044  -0.0254 30  PRO A CB  
238  C  CG  . PRO A 30  ? 0.0806 0.1524 0.1663 -0.0096 0.0108  -0.0241 30  PRO A CG  
239  C  CD  . PRO A 30  ? 0.0885 0.1484 0.1275 -0.0083 0.0057  -0.0306 30  PRO A CD  
240  N  N   . VAL A 31  ? 0.1180 0.1418 0.1304 0.0044  0.0183  0.0109  31  VAL A N   
241  C  CA  . VAL A 31  ? 0.1700 0.1483 0.1133 -0.0162 0.0140  0.0178  31  VAL A CA  
242  C  C   . VAL A 31  ? 0.1275 0.1693 0.1150 -0.0052 0.0096  0.0206  31  VAL A C   
243  O  O   . VAL A 31  ? 0.1301 0.1657 0.1330 0.0041  -0.0058 0.0209  31  VAL A O   
244  C  CB  . VAL A 31  ? 0.1440 0.1585 0.1509 -0.0063 0.0145  -0.0040 31  VAL A CB  
245  C  CG1 . VAL A 31  ? 0.1355 0.1745 0.1513 -0.0194 -0.0116 0.0016  31  VAL A CG1 
246  C  CG2 . VAL A 31  ? 0.1606 0.1671 0.1524 0.0204  0.0174  -0.0061 31  VAL A CG2 
247  N  N   . ASP A 32  ? 0.1445 0.1566 0.1192 0.0099  0.0044  0.0142  32  ASP A N   
248  C  CA  . ASP A 32  ? 0.1682 0.1384 0.1225 0.0121  0.0236  0.0126  32  ASP A CA  
249  C  C   . ASP A 32  ? 0.1691 0.1612 0.1110 0.0186  0.0013  0.0082  32  ASP A C   
250  O  O   . ASP A 32  ? 0.1930 0.2316 0.1366 0.0005  0.0201  -0.0351 32  ASP A O   
251  C  CB  . ASP A 32  ? 0.2045 0.1646 0.1749 0.0285  -0.0091 0.0234  32  ASP A CB  
252  C  CG  . ASP A 32  ? 0.2105 0.1989 0.1416 0.0205  -0.0069 0.0105  32  ASP A CG  
253  O  OD1 . ASP A 32  ? 0.2224 0.1874 0.1454 -0.0046 -0.0062 0.0177  32  ASP A OD1 
254  O  OD2 . ASP A 32  ? 0.3197 0.2296 0.1430 -0.0236 -0.0303 0.0205  32  ASP A OD2 
255  N  N   . ILE A 33  ? 0.1506 0.1659 0.1240 0.0207  0.0106  0.0185  33  ILE A N   
256  C  CA  . ILE A 33  ? 0.1562 0.1793 0.1459 0.0185  0.0259  0.0294  33  ILE A CA  
257  C  C   . ILE A 33  ? 0.2066 0.1584 0.1418 0.0223  0.0460  0.0027  33  ILE A C   
258  O  O   . ILE A 33  ? 0.2109 0.1788 0.1506 0.0144  0.0337  0.0033  33  ILE A O   
259  C  CB  . ILE A 33  ? 0.1502 0.1930 0.1533 0.0219  0.0372  0.0217  33  ILE A CB  
260  C  CG1 . ILE A 33  ? 0.1968 0.1660 0.1444 0.0359  -0.0187 0.0260  33  ILE A CG1 
261  C  CG2 . ILE A 33  ? 0.1353 0.2053 0.1743 0.0329  0.0328  0.0208  33  ILE A CG2 
262  C  CD1 . ILE A 33  ? 0.1659 0.2306 0.2101 0.0385  -0.0358 0.0438  33  ILE A CD1 
263  N  N   . ASP A 34  ? 0.2228 0.1987 0.1344 0.0288  0.0232  0.0212  34  ASP A N   
264  C  CA  . ASP A 34  ? 0.2159 0.2226 0.1555 0.0465  0.0442  0.0447  34  ASP A CA  
265  C  C   . ASP A 34  ? 0.2238 0.2172 0.1174 0.0122  0.0499  0.0279  34  ASP A C   
266  O  O   . ASP A 34  ? 0.2575 0.2314 0.1476 0.0633  0.0417  0.0139  34  ASP A O   
267  C  CB  . ASP A 34  ? 0.2652 0.2496 0.1835 0.0436  0.0000  0.0339  34  ASP A CB  
268  C  CG  . ASP A 34  ? 0.2679 0.3642 0.2701 0.0355  0.0223  0.1284  34  ASP A CG  
269  O  OD1 . ASP A 34  ? 0.2949 0.3378 0.2275 0.0738  0.0444  0.1030  34  ASP A OD1 
270  O  OD2 . ASP A 34  ? 0.3493 0.6038 0.4534 0.0877  -0.0271 0.2507  34  ASP A OD2 
271  N  N   . THR A 35  ? 0.2197 0.2133 0.1638 0.0294  0.0405  0.0526  35  THR A N   
272  C  CA  . THR A 35  ? 0.2324 0.2846 0.1847 0.0961  0.0085  0.0385  35  THR A CA  
273  C  C   . THR A 35  ? 0.2548 0.2298 0.2030 0.0518  0.0788  0.0042  35  THR A C   
274  O  O   . THR A 35  ? 0.2472 0.3025 0.2587 0.0825  0.0788  -0.0033 35  THR A O   
275  C  CB  . THR A 35  ? 0.2555 0.2654 0.1955 0.0484  0.0308  0.0508  35  THR A CB  
276  O  OG1 . THR A 35  ? 0.2619 0.2293 0.2848 0.0231  0.0602  0.0308  35  THR A OG1 
277  C  CG2 . THR A 35  ? 0.3426 0.3047 0.1775 0.0555  0.0115  0.0332  35  THR A CG2 
278  N  N   . HIS A 36  ? 0.3265 0.2058 0.1887 0.0425  0.0778  0.0519  36  HIS A N   
279  C  CA  . HIS A 36  ? 0.4253 0.2014 0.1976 0.0081  0.1121  0.0535  36  HIS A CA  
280  C  C   . HIS A 36  ? 0.3855 0.3222 0.1961 0.0002  0.1246  -0.0156 36  HIS A C   
281  O  O   . HIS A 36  ? 0.3556 0.3326 0.2015 0.0285  0.0787  0.0263  36  HIS A O   
282  C  CB  . HIS A 36  ? 0.3539 0.2073 0.2233 -0.0027 0.0414  0.0690  36  HIS A CB  
283  C  CG  . HIS A 36  ? 0.4566 0.2168 0.2233 -0.0200 0.0313  0.0418  36  HIS A CG  
284  N  ND1 . HIS A 36  ? 0.4841 0.2958 0.2068 0.0749  -0.0124 0.0262  36  HIS A ND1 
285  C  CD2 . HIS A 36  ? 0.4713 0.2888 0.1567 -0.1157 -0.0076 0.0642  36  HIS A CD2 
286  C  CE1 . HIS A 36  ? 0.5012 0.2467 0.2490 0.0693  0.0242  -0.0078 36  HIS A CE1 
287  N  NE2 . HIS A 36  ? 0.5211 0.3089 0.2256 -0.0178 -0.0142 0.0089  36  HIS A NE2 
288  N  N   . THR A 37  ? 0.3347 0.2357 0.1883 0.0626  0.0549  0.0212  37  THR A N   
289  C  CA  . THR A 37  ? 0.2929 0.2420 0.1369 0.0490  0.0568  0.0345  37  THR A CA  
290  C  C   . THR A 37  ? 0.3194 0.2702 0.1736 0.0809  0.0479  0.0460  37  THR A C   
291  O  O   . THR A 37  ? 0.4332 0.2952 0.1987 0.0724  0.0383  0.0173  37  THR A O   
292  C  CB  . THR A 37  ? 0.3092 0.3940 0.2226 0.0932  0.0194  0.0334  37  THR A CB  
293  O  OG1 . THR A 37  ? 0.5071 0.4637 0.2278 0.0763  0.0636  -0.0050 37  THR A OG1 
294  C  CG2 . THR A 37  ? 0.3631 0.3111 0.3265 0.0725  0.0119  0.0221  37  THR A CG2 
295  N  N   . ALA A 38  ? 0.2317 0.2449 0.1653 0.0761  0.0738  0.0487  38  ALA A N   
296  C  CA  . ALA A 38  ? 0.2995 0.2115 0.1738 0.0688  0.0563  0.0407  38  ALA A CA  
297  C  C   . ALA A 38  ? 0.2982 0.1941 0.2443 0.0544  0.0972  0.0724  38  ALA A C   
298  O  O   . ALA A 38  ? 0.3032 0.2644 0.2834 0.0289  0.1030  0.0699  38  ALA A O   
299  C  CB  . ALA A 38  ? 0.2661 0.1997 0.2098 0.0653  0.0403  0.0325  38  ALA A CB  
300  N  N   . LYS A 39  ? 0.2983 0.2212 0.1610 0.0974  0.0372  0.0522  39  LYS A N   
301  C  CA  . LYS A 39  ? 0.2842 0.2914 0.2380 0.1339  0.0283  0.0093  39  LYS A CA  
302  C  C   . LYS A 39  ? 0.2562 0.2720 0.1556 0.0684  0.0552  0.0347  39  LYS A C   
303  O  O   . LYS A 39  ? 0.2453 0.2964 0.1335 0.0653  0.0490  0.0552  39  LYS A O   
304  C  CB  . LYS A 39  ? 0.2942 0.3868 0.2695 0.1508  -0.0366 -0.0672 39  LYS A CB  
305  C  CG  . LYS A 39  ? 0.3820 0.4990 0.2400 0.1637  0.0245  -0.0252 39  LYS A CG  
306  C  CD  . LYS A 39  ? 0.2476 0.5163 0.3110 0.1955  0.0197  0.1040  39  LYS A CD  
307  C  CE  . LYS A 39  ? 0.3284 0.7279 0.2715 0.1444  -0.0223 -0.0303 39  LYS A CE  
308  N  NZ  . LYS A 39  ? 0.2731 0.8987 0.3216 0.2104  0.0240  0.1013  39  LYS A NZ  
309  N  N   . TYR A 40  ? 0.3014 0.3197 0.1770 0.0603  0.0484  0.0737  40  TYR A N   
310  C  CA  . TYR A 40  ? 0.2364 0.3212 0.1933 0.0271  0.0741  0.0351  40  TYR A CA  
311  C  C   . TYR A 40  ? 0.2241 0.3622 0.1452 0.0366  0.0685  -0.0004 40  TYR A C   
312  O  O   . TYR A 40  ? 0.2885 0.4299 0.1429 0.0771  0.0644  -0.0012 40  TYR A O   
313  C  CB  . TYR A 40  ? 0.2766 0.4424 0.2594 -0.0428 0.1052  0.0673  40  TYR A CB  
314  C  CG  . TYR A 40  ? 0.2307 0.5170 0.2474 -0.0791 0.0897  0.0669  40  TYR A CG  
315  C  CD1 . TYR A 40  ? 0.3837 0.4394 0.2015 -0.1278 0.0683  0.0256  40  TYR A CD1 
316  C  CD2 . TYR A 40  ? 0.3150 0.7698 0.2248 0.0100  0.1053  0.0566  40  TYR A CD2 
317  C  CE1 . TYR A 40  ? 0.3432 0.6984 0.2478 -0.0419 0.0878  0.0131  40  TYR A CE1 
318  C  CE2 . TYR A 40  ? 0.3208 0.6381 0.2972 0.0054  0.1064  0.0100  40  TYR A CE2 
319  C  CZ  . TYR A 40  ? 0.2037 0.7471 0.3238 -0.0302 0.0759  0.0193  40  TYR A CZ  
320  O  OH  . TYR A 40  ? 0.2515 0.9948 0.4866 0.1062  0.1119  -0.1138 40  TYR A OH  
321  N  N   . ASP A 41  ? 0.2511 0.2975 0.2095 0.0423  0.0354  -0.0115 41  ASP A N   
322  C  CA  . ASP A 41  ? 0.2662 0.3015 0.1614 0.0280  0.0111  -0.0099 41  ASP A CA  
323  C  C   . ASP A 41  ? 0.3116 0.5175 0.1930 0.1158  0.0219  -0.0586 41  ASP A C   
324  O  O   . ASP A 41  ? 0.2386 0.4917 0.2163 0.1071  0.0620  -0.0166 41  ASP A O   
325  C  CB  . ASP A 41  ? 0.2792 0.2454 0.3493 0.0033  -0.0027 0.0077  41  ASP A CB  
326  C  CG  . ASP A 41  ? 0.4684 0.4028 0.3345 0.0132  -0.0414 -0.1643 41  ASP A CG  
327  O  OD1 . ASP A 41  ? 0.5134 0.5044 0.2842 0.1425  -0.0924 -0.1002 41  ASP A OD1 
328  O  OD2 . ASP A 41  ? 0.5019 0.5175 0.5542 -0.0660 -0.1511 0.0249  41  ASP A OD2 
329  N  N   . PRO A 42  ? 0.3431 0.6638 0.2041 0.1750  0.0348  -0.0358 42  PRO A N   
330  C  CA  . PRO A 42  ? 0.3844 0.6783 0.2709 0.2383  0.0662  0.0464  42  PRO A CA  
331  C  C   . PRO A 42  ? 0.4309 0.6833 0.2828 0.2478  0.0685  0.0573  42  PRO A C   
332  O  O   . PRO A 42  ? 0.3279 0.9024 0.4253 0.2373  0.0759  -0.0095 42  PRO A O   
333  C  CB  . PRO A 42  ? 0.4217 0.6537 0.3482 0.1993  0.1520  0.0512  42  PRO A CB  
334  C  CG  . PRO A 42  ? 0.5047 0.8693 0.3143 0.2733  0.1412  0.0029  42  PRO A CG  
335  C  CD  . PRO A 42  ? 0.5639 0.4885 0.2167 0.2625  0.1270  0.0013  42  PRO A CD  
336  N  N   . SER A 43  ? 0.4967 0.5314 0.2661 0.2873  0.0836  0.0419  43  SER A N   
337  C  CA  . SER A 43  ? 0.6475 0.5018 0.2281 0.2305  -0.0143 -0.0117 43  SER A CA  
338  C  C   . SER A 43  ? 0.5707 0.3996 0.2285 0.2649  0.0037  0.0115  43  SER A C   
339  O  O   . SER A 43  ? 0.6970 0.4285 0.3377 0.2900  -0.0287 0.0343  43  SER A O   
340  C  CB  . SER A 43  ? 0.6917 0.5955 0.3981 0.1086  0.0452  -0.0483 43  SER A CB  
341  O  OG  . SER A 43  ? 0.6459 0.4496 0.4544 -0.0018 0.0296  -0.1317 43  SER A OG  
342  N  N   . LEU A 44  ? 0.4742 0.4885 0.2659 0.2133  0.0174  -0.0480 44  LEU A N   
343  C  CA  . LEU A 44  ? 0.3062 0.4895 0.2921 0.1929  -0.0167 0.0602  44  LEU A CA  
344  C  C   . LEU A 44  ? 0.2235 0.5554 0.3008 0.0957  0.0477  0.0966  44  LEU A C   
345  O  O   . LEU A 44  ? 0.3406 0.6619 0.2752 -0.0200 0.0577  0.1064  44  LEU A O   
346  C  CB  . LEU A 44  ? 0.2615 0.4417 0.2281 0.0632  0.0091  0.0031  44  LEU A CB  
347  C  CG  . LEU A 44  ? 0.2518 0.2433 0.3039 0.0447  0.0476  0.0502  44  LEU A CG  
348  C  CD1 . LEU A 44  ? 0.2856 0.2605 0.2674 0.0013  0.0526  -0.0126 44  LEU A CD1 
349  C  CD2 . LEU A 44  ? 0.2600 0.2450 0.2619 0.0288  0.0066  0.0403  44  LEU A CD2 
350  N  N   . LYS A 45  ? 0.2809 0.5723 0.3250 0.0621  -0.0079 0.1543  45  LYS A N   
351  C  CA  . LYS A 45  ? 0.3468 0.3590 0.3600 0.0358  -0.0936 -0.0343 45  LYS A CA  
352  C  C   . LYS A 45  ? 0.2970 0.3597 0.2828 0.0851  0.0595  0.0238  45  LYS A C   
353  O  O   . LYS A 45  ? 0.1975 0.4388 0.3513 -0.0029 0.0785  -0.0727 45  LYS A O   
354  C  CB  . LYS A 45  ? 0.3919 0.3190 0.3880 0.1615  0.0223  -0.0703 45  LYS A CB  
355  C  CG  . LYS A 45  ? 0.4284 0.4964 0.3632 0.1561  -0.0704 -0.1377 45  LYS A CG  
356  C  CD  . LYS A 45  ? 0.7301 0.6291 0.7348 0.2080  -0.0912 -0.0242 45  LYS A CD  
357  C  CE  . LYS A 45  ? 0.6289 1.0698 0.7646 0.0858  -0.1398 -0.2664 45  LYS A CE  
358  N  NZ  . LYS A 45  ? 0.9944 1.1734 0.4379 0.3213  -0.0592 -0.2197 45  LYS A NZ  
359  N  N   . PRO A 46  ? 0.2393 0.3714 0.3715 -0.0359 0.0670  0.0157  46  PRO A N   
360  C  CA  . PRO A 46  ? 0.1941 0.3607 0.3503 0.0016  0.0606  0.0765  46  PRO A CA  
361  C  C   . PRO A 46  ? 0.1756 0.2927 0.3297 0.0205  0.0687  0.0573  46  PRO A C   
362  O  O   . PRO A 46  ? 0.1808 0.3312 0.3338 -0.0211 0.0104  0.0719  46  PRO A O   
363  C  CB  . PRO A 46  ? 0.1584 0.3700 0.3541 -0.0179 0.0897  0.0251  46  PRO A CB  
364  C  CG  . PRO A 46  ? 0.2577 0.5035 0.4964 -0.0025 0.1668  -0.1339 46  PRO A CG  
365  C  CD  . PRO A 46  ? 0.3495 0.4130 0.4505 0.1015  0.0727  -0.1252 46  PRO A CD  
366  N  N   . LEU A 47  ? 0.1560 0.2968 0.3489 0.0389  0.0292  0.0812  47  LEU A N   
367  C  CA  . LEU A 47  ? 0.1125 0.2917 0.3704 -0.0309 0.0414  0.0716  47  LEU A CA  
368  C  C   . LEU A 47  ? 0.1243 0.2608 0.4335 -0.0458 0.0156  0.1251  47  LEU A C   
369  O  O   . LEU A 47  ? 0.1270 0.3463 0.4965 -0.0824 -0.0278 0.1949  47  LEU A O   
370  C  CB  . LEU A 47  ? 0.2947 0.3643 0.3780 0.0328  0.0592  0.0776  47  LEU A CB  
371  C  CG  . LEU A 47  ? 0.1835 0.4447 0.5152 -0.0267 0.0027  -0.0737 47  LEU A CG  
372  C  CD1 . LEU A 47  ? 0.1775 0.3711 0.6954 -0.0332 -0.0801 -0.0783 47  LEU A CD1 
373  C  CD2 . LEU A 47  ? 0.1289 0.3865 0.6933 0.0042  -0.0770 -0.0884 47  LEU A CD2 
374  N  N   . SER A 48  ? 0.1047 0.2484 0.2911 0.0009  0.0279  0.0787  48  SER A N   
375  C  CA  . SER A 48  ? 0.1402 0.2737 0.2637 0.0105  0.0234  0.0649  48  SER A CA  
376  C  C   . SER A 48  ? 0.1423 0.2751 0.2350 -0.0422 0.0134  0.0335  48  SER A C   
377  O  O   . SER A 48  ? 0.1384 0.2616 0.2792 -0.0362 0.0325  0.0154  48  SER A O   
378  C  CB  . SER A 48  ? 0.2192 0.2756 0.2637 0.0219  0.0297  0.0570  48  SER A CB  
379  O  OG  . SER A 48  ? 0.2583 0.3923 0.3268 0.0291  -0.0013 0.0831  48  SER A OG  
380  N  N   . VAL A 49  ? 0.1538 0.2820 0.2717 -0.0617 0.0234  0.0243  49  VAL A N   
381  C  CA  . VAL A 49  ? 0.1682 0.3089 0.2953 -0.0886 0.0629  -0.0208 49  VAL A CA  
382  C  C   . VAL A 49  ? 0.1728 0.3657 0.2907 -0.1225 0.0210  -0.0033 49  VAL A C   
383  O  O   . VAL A 49  ? 0.2120 0.4758 0.3213 -0.1972 -0.0100 0.0168  49  VAL A O   
384  C  CB  . VAL A 49  ? 0.2719 0.3025 0.3589 -0.0467 0.1053  -0.0201 49  VAL A CB  
385  C  CG1 . VAL A 49  ? 0.3955 0.3448 0.3585 -0.0679 0.1213  -0.0297 49  VAL A CG1 
386  C  CG2 . VAL A 49  ? 0.2174 0.3183 0.4500 -0.0981 0.0731  -0.0291 49  VAL A CG2 
387  N  N   . SER A 50  ? 0.1754 0.3017 0.2899 -0.0489 0.0357  -0.0029 50  SER A N   
388  C  CA  . SER A 50  ? 0.1530 0.2806 0.3474 -0.0423 0.0196  -0.0282 50  SER A CA  
389  C  C   . SER A 50  ? 0.1452 0.2651 0.2945 -0.0088 -0.0153 0.0029  50  SER A C   
390  O  O   . SER A 50  ? 0.1560 0.2940 0.3297 -0.0429 0.0034  0.0052  50  SER A O   
391  C  CB  . SER A 50  ? 0.2832 0.3383 0.3728 -0.0296 0.1093  -0.1090 50  SER A CB  
392  O  OG  . SER A 50  ? 0.3212 0.5374 0.4006 -0.0820 0.0591  -0.0801 50  SER A OG  
393  N  N   . TYR A 51  ? 0.1405 0.2350 0.3557 -0.0361 0.0037  -0.0061 51  TYR A N   
394  C  CA  . TYR A 51  ? 0.2037 0.2515 0.3054 0.0042  -0.0498 0.0195  51  TYR A CA  
395  C  C   . TYR A 51  ? 0.2133 0.2910 0.3620 0.0081  -0.0567 0.0476  51  TYR A C   
396  O  O   . TYR A 51  ? 0.2310 0.2841 0.3520 -0.0080 -0.0895 0.0353  51  TYR A O   
397  C  CB  . TYR A 51  ? 0.1208 0.2702 0.3244 -0.0039 -0.0373 -0.0239 51  TYR A CB  
398  C  CG  . TYR A 51  ? 0.1731 0.2226 0.2649 -0.0348 -0.0581 0.0144  51  TYR A CG  
399  C  CD1 . TYR A 51  ? 0.1452 0.2420 0.2856 -0.0370 -0.0342 0.0159  51  TYR A CD1 
400  C  CD2 . TYR A 51  ? 0.1432 0.2343 0.2511 -0.0125 -0.0337 0.0105  51  TYR A CD2 
401  C  CE1 . TYR A 51  ? 0.1303 0.2127 0.2530 -0.0216 -0.0104 0.0094  51  TYR A CE1 
402  C  CE2 . TYR A 51  ? 0.1301 0.2109 0.2306 -0.0268 -0.0179 0.0100  51  TYR A CE2 
403  C  CZ  . TYR A 51  ? 0.1330 0.2124 0.1856 -0.0201 0.0006  -0.0060 51  TYR A CZ  
404  O  OH  . TYR A 51  ? 0.1383 0.2089 0.2360 -0.0325 -0.0294 -0.0057 51  TYR A OH  
405  N  N   . ASP A 52  ? 0.1624 0.3736 0.4277 -0.0427 -0.0749 0.0377  52  ASP A N   
406  C  CA  . ASP A 52  ? 0.2310 0.4157 0.3740 0.0088  -0.0353 0.1018  52  ASP A CA  
407  C  C   . ASP A 52  ? 0.1628 0.3690 0.4131 0.0129  -0.0057 0.0534  52  ASP A C   
408  O  O   . ASP A 52  ? 0.3565 0.3916 0.3453 0.0353  -0.0241 0.1021  52  ASP A O   
409  C  CB  . ASP A 52  ? 0.1295 0.6225 0.5897 0.0362  -0.0960 0.1430  52  ASP A CB  
410  C  CG  . ASP A 52  ? 0.4864 0.6800 0.9826 0.0694  0.0856  -0.0964 52  ASP A CG  
411  O  OD1 . ASP A 52  ? 0.3766 0.8008 1.0729 0.0653  0.1702  -0.0220 52  ASP A OD1 
412  O  OD2 . ASP A 52  ? 0.4437 0.9428 1.3090 0.1958  0.0710  0.0347  52  ASP A OD2 
413  N  N   . GLN A 53  ? 0.1493 0.3529 0.4555 0.0031  -0.0199 0.0538  53  GLN A N   
414  C  CA  . GLN A 53  ? 0.2432 0.3416 0.5777 -0.0134 0.0734  0.0618  53  GLN A CA  
415  C  C   . GLN A 53  ? 0.2551 0.2899 0.3567 0.0497  0.0332  0.0558  53  GLN A C   
416  O  O   . GLN A 53  ? 0.2637 0.2913 0.4573 -0.0001 -0.0557 0.0834  53  GLN A O   
417  C  CB  . GLN A 53  ? 0.3481 0.4052 0.7471 0.1078  0.1428  0.0153  53  GLN A CB  
418  C  CG  . GLN A 53  ? 0.3999 0.7480 0.8318 0.2011  0.0622  0.2442  53  GLN A CG  
419  C  CD  . GLN A 53  ? 0.5518 0.8460 0.7569 0.1442  0.0878  0.4148  53  GLN A CD  
420  O  OE1 . GLN A 53  ? 0.4425 0.8718 0.9251 0.2632  0.1703  0.5962  53  GLN A OE1 
421  N  NE2 . GLN A 53  ? 0.4954 0.9308 0.5880 0.1777  0.1930  0.3019  53  GLN A NE2 
422  N  N   . ALA A 54  ? 0.1800 0.2318 0.3947 -0.0206 -0.0161 -0.0053 54  ALA A N   
423  C  CA  . ALA A 54  ? 0.1728 0.2037 0.2613 -0.0155 -0.0259 -0.0212 54  ALA A CA  
424  C  C   . ALA A 54  ? 0.2722 0.2105 0.2568 -0.0291 -0.0319 -0.0410 54  ALA A C   
425  O  O   . ALA A 54  ? 0.2823 0.2967 0.3743 -0.0679 -0.1007 -0.0234 54  ALA A O   
426  C  CB  . ALA A 54  ? 0.2181 0.2454 0.2974 0.0318  0.0075  0.0141  54  ALA A CB  
427  N  N   . THR A 55  ? 0.2308 0.1965 0.2447 -0.0037 -0.0634 0.0588  55  THR A N   
428  C  CA  . THR A 55  ? 0.2706 0.1930 0.2453 0.0616  -0.0771 0.0422  55  THR A CA  
429  C  C   . THR A 55  ? 0.2312 0.1840 0.1833 0.0026  -0.0765 0.0212  55  THR A C   
430  O  O   . THR A 55  ? 0.2898 0.1700 0.1887 0.0022  -0.0789 0.0194  55  THR A O   
431  C  CB  . THR A 55  ? 0.2598 0.2224 0.3385 0.0029  -0.0743 0.1175  55  THR A CB  
432  O  OG1 . THR A 55  ? 0.3248 0.3040 0.5332 0.0526  -0.1668 0.0002  55  THR A OG1 
433  C  CG2 . THR A 55  ? 0.4268 0.2609 0.3423 0.0356  -0.0946 0.1123  55  THR A CG2 
434  N  N   . SER A 56  ? 0.2651 0.1692 0.2127 0.0171  -0.0793 0.0232  56  SER A N   
435  C  CA  . SER A 56  ? 0.2547 0.1592 0.1907 -0.0027 -0.0577 0.0015  56  SER A CA  
436  C  C   . SER A 56  ? 0.3204 0.2023 0.1917 -0.0143 -0.0867 0.0013  56  SER A C   
437  O  O   . SER A 56  ? 0.3791 0.1993 0.2282 0.0136  -0.1188 0.0274  56  SER A O   
438  C  CB  . SER A 56  ? 0.3790 0.1585 0.1614 -0.0178 -0.1206 0.0158  56  SER A CB  
439  O  OG  . SER A 56  ? 0.3534 0.1768 0.1899 -0.0355 -0.1115 0.0379  56  SER A OG  
440  N  N   . LEU A 57  ? 0.3079 0.1555 0.1443 0.0116  -0.0406 0.0384  57  LEU A N   
441  C  CA  . LEU A 57  ? 0.3581 0.1793 0.1624 0.0154  -0.0181 0.0323  57  LEU A CA  
442  C  C   . LEU A 57  ? 0.3816 0.1754 0.1429 0.0485  -0.0388 0.0463  57  LEU A C   
443  O  O   . LEU A 57  ? 0.3711 0.2076 0.1461 0.0134  -0.0607 0.0468  57  LEU A O   
444  C  CB  . LEU A 57  ? 0.3966 0.2229 0.1976 -0.0181 -0.0054 0.0072  57  LEU A CB  
445  C  CG  . LEU A 57  ? 0.5080 0.2166 0.2034 0.0438  -0.0536 0.0011  57  LEU A CG  
446  C  CD1 . LEU A 57  ? 0.6208 0.2874 0.3130 -0.1319 -0.0334 0.0597  57  LEU A CD1 
447  C  CD2 . LEU A 57  ? 0.5906 0.2382 0.2965 0.0620  -0.0986 0.0660  57  LEU A CD2 
448  N  N   . ARG A 58  ? 0.3054 0.1739 0.1714 0.0432  -0.0519 0.0103  58  ARG A N   
449  C  CA  . ARG A 58  ? 0.2726 0.1849 0.2235 0.0444  -0.0441 0.0439  58  ARG A CA  
450  C  C   . ARG A 58  ? 0.2515 0.1835 0.1551 -0.0190 -0.0493 0.0239  58  ARG A C   
451  O  O   . ARG A 58  ? 0.3360 0.1998 0.1285 0.0248  -0.0392 0.0190  58  ARG A O   
452  C  CB  . ARG A 58  ? 0.3168 0.2221 0.2740 0.0196  0.0049  0.0866  58  ARG A CB  
453  C  CG  . ARG A 58  ? 0.1660 0.4039 0.3845 -0.0501 0.0195  0.0669  58  ARG A CG  
454  C  CD  . ARG A 58  ? 0.1890 0.5357 0.3689 -0.1169 -0.0037 0.0027  58  ARG A CD  
455  N  NE  . ARG A 58  ? 0.2246 0.3180 0.4447 -0.0167 -0.0534 0.0779  58  ARG A NE  
456  C  CZ  . ARG A 58  ? 0.2127 0.2978 0.2766 -0.0174 -0.0449 0.1229  58  ARG A CZ  
457  N  NH1 . ARG A 58  ? 0.3233 0.2767 0.2684 -0.0818 -0.0041 0.0204  58  ARG A NH1 
458  N  NH2 . ARG A 58  ? 0.2597 0.3186 0.2291 -0.0186 -0.0100 0.0457  58  ARG A NH2 
459  N  N   . ILE A 59  ? 0.2781 0.1713 0.1244 -0.0091 -0.0273 0.0241  59  ILE A N   
460  C  CA  . ILE A 59  ? 0.2238 0.1637 0.1609 -0.0072 -0.0192 0.0174  59  ILE A CA  
461  C  C   . ILE A 59  ? 0.2339 0.1772 0.1132 -0.0186 -0.0315 0.0192  59  ILE A C   
462  O  O   . ILE A 59  ? 0.2710 0.2594 0.1137 -0.0089 -0.0072 0.0504  59  ILE A O   
463  C  CB  . ILE A 59  ? 0.3046 0.1570 0.1226 -0.0004 -0.0534 0.0150  59  ILE A CB  
464  C  CG1 . ILE A 59  ? 0.2749 0.1650 0.1614 -0.0200 -0.0497 0.0413  59  ILE A CG1 
465  C  CG2 . ILE A 59  ? 0.2695 0.1976 0.1341 0.0420  -0.0573 0.0000  59  ILE A CG2 
466  C  CD1 . ILE A 59  ? 0.2638 0.1860 0.1465 -0.0276 -0.0276 0.0324  59  ILE A CD1 
467  N  N   . LEU A 60  ? 0.2172 0.2190 0.1717 -0.0170 -0.0497 0.0190  60  LEU A N   
468  C  CA  . LEU A 60  ? 0.2124 0.2162 0.1230 0.0107  -0.0611 0.0084  60  LEU A CA  
469  C  C   . LEU A 60  ? 0.2283 0.1908 0.1262 -0.0233 -0.0206 0.0315  60  LEU A C   
470  O  O   . LEU A 60  ? 0.1795 0.2530 0.1277 -0.0236 0.0057  0.0558  60  LEU A O   
471  C  CB  . LEU A 60  ? 0.2163 0.1610 0.2697 -0.0502 -0.0122 0.0192  60  LEU A CB  
472  C  CG  . LEU A 60  ? 0.2174 0.2215 0.2030 -0.0229 -0.0081 0.0044  60  LEU A CG  
473  C  CD1 . LEU A 60  ? 0.2613 0.2497 0.2194 -0.0636 0.0362  0.0305  60  LEU A CD1 
474  C  CD2 . LEU A 60  ? 0.2454 0.1923 0.2866 -0.0392 -0.0403 -0.0196 60  LEU A CD2 
475  N  N   . ASN A 61  ? 0.2486 0.1635 0.1627 -0.0219 0.0186  0.0100  61  ASN A N   
476  C  CA  . ASN A 61  ? 0.2071 0.1980 0.1181 -0.0364 0.0264  -0.0252 61  ASN A CA  
477  C  C   . ASN A 61  ? 0.2104 0.2160 0.1232 -0.0484 0.0255  -0.0226 61  ASN A C   
478  O  O   . ASN A 61  ? 0.2692 0.2318 0.1481 -0.0341 0.0258  0.0254  61  ASN A O   
479  C  CB  . ASN A 61  ? 0.3053 0.1896 0.1153 -0.0148 0.0316  -0.0072 61  ASN A CB  
480  C  CG  . ASN A 61  ? 0.2097 0.1900 0.1225 -0.0416 0.0498  -0.0129 61  ASN A CG  
481  O  OD1 . ASN A 61  ? 0.2855 0.2314 0.1390 -0.0271 0.0463  -0.0162 61  ASN A OD1 
482  N  ND2 . ASN A 61  ? 0.2831 0.2040 0.1466 -0.0658 0.0705  -0.0354 61  ASN A ND2 
483  N  N   . ASN A 62  ? 0.2471 0.1711 0.1359 -0.0499 -0.0177 0.0067  62  ASN A N   
484  C  CA  . ASN A 62  ? 0.2734 0.1856 0.1571 -0.0502 -0.0258 0.0116  62  ASN A CA  
485  C  C   . ASN A 62  ? 0.2310 0.2090 0.1473 -0.0399 0.0209  0.0060  62  ASN A C   
486  O  O   . ASN A 62  ? 0.3100 0.2762 0.1993 -0.1206 -0.0137 0.0049  62  ASN A O   
487  C  CB  . ASN A 62  ? 0.3750 0.1847 0.1900 -0.0774 -0.0012 0.0001  62  ASN A CB  
488  C  CG  . ASN A 62  ? 0.3466 0.1764 0.1835 -0.0497 0.0145  0.0055  62  ASN A CG  
489  O  OD1 . ASN A 62  ? 0.2362 0.1857 0.1610 -0.0486 0.0144  0.0129  62  ASN A OD1 
490  N  ND2 . ASN A 62  ? 0.5350 0.2202 0.2150 -0.0402 0.0292  -0.0315 62  ASN A ND2 
491  N  N   . GLY A 63  ? 0.2450 0.2169 0.1598 -0.0609 0.0674  0.0099  63  GLY A N   
492  C  CA  . GLY A 63  ? 0.2245 0.2192 0.1570 -0.0252 0.0588  0.0119  63  GLY A CA  
493  C  C   . GLY A 63  ? 0.2424 0.2565 0.1734 -0.0447 0.0428  0.0139  63  GLY A C   
494  O  O   . GLY A 63  ? 0.2080 0.2737 0.2009 -0.0473 0.0100  -0.0214 63  GLY A O   
495  N  N   . HIS A 64  ? 0.2069 0.2231 0.1329 -0.0438 0.0240  0.0113  64  HIS A N   
496  C  CA  . HIS A 64  ? 0.1707 0.2127 0.1420 -0.0550 0.0074  0.0149  64  HIS A CA  
497  C  C   . HIS A 64  ? 0.1526 0.1725 0.1655 -0.0303 0.0102  0.0029  64  HIS A C   
498  O  O   . HIS A 64  ? 0.1756 0.2265 0.2992 -0.0509 -0.0187 0.0914  64  HIS A O   
499  C  CB  . HIS A 64  ? 0.1872 0.2730 0.1635 -0.0908 0.0092  -0.0175 64  HIS A CB  
500  C  CG  . HIS A 64  ? 0.2393 0.2906 0.1835 -0.1165 -0.0198 0.0153  64  HIS A CG  
501  N  ND1 . HIS A 64  ? 0.2055 0.4277 0.2541 -0.1001 -0.0161 -0.0325 64  HIS A ND1 
502  C  CD2 . HIS A 64  ? 0.2716 0.2730 0.2188 -0.0734 -0.0003 -0.0222 64  HIS A CD2 
503  C  CE1 . HIS A 64  ? 0.2737 0.3319 0.3129 -0.0924 0.0457  -0.0579 64  HIS A CE1 
504  N  NE2 . HIS A 64  ? 0.2921 0.3653 0.2701 -0.1026 0.0351  -0.0253 64  HIS A NE2 
505  N  N   . THR A 65  ? 0.1565 0.1890 0.1481 -0.0255 0.0170  0.0181  65  THR A N   
506  C  CA  . THR A 65  ? 0.1650 0.1833 0.1418 -0.0420 0.0234  0.0154  65  THR A CA  
507  C  C   . THR A 65  ? 0.1578 0.1822 0.1288 -0.0229 0.0229  0.0063  65  THR A C   
508  O  O   . THR A 65  ? 0.1883 0.2115 0.1344 -0.0387 0.0283  0.0108  65  THR A O   
509  C  CB  . THR A 65  ? 0.1756 0.2071 0.1326 -0.0538 0.0207  0.0243  65  THR A CB  
510  O  OG1 . THR A 65  ? 0.1763 0.2977 0.1623 -0.0560 0.0103  0.0706  65  THR A OG1 
511  C  CG2 . THR A 65  ? 0.2032 0.1958 0.1917 -0.0098 0.0217  -0.0199 65  THR A CG2 
512  N  N   . PHE A 66  ? 0.1573 0.1903 0.1223 -0.0145 0.0218  0.0011  66  PHE A N   
513  C  CA  . PHE A 66  ? 0.2109 0.2380 0.0754 -0.0009 0.0040  0.0067  66  PHE A CA  
514  C  C   . PHE A 66  ? 0.2020 0.1644 0.0885 -0.0237 0.0077  -0.0022 66  PHE A C   
515  O  O   . PHE A 66  ? 0.1951 0.1865 0.1062 -0.0173 0.0125  -0.0027 66  PHE A O   
516  C  CB  . PHE A 66  ? 0.2178 0.2601 0.1172 -0.0513 0.0249  -0.0238 66  PHE A CB  
517  C  CG  . PHE A 66  ? 0.2248 0.2420 0.1104 -0.0357 0.0099  -0.0158 66  PHE A CG  
518  C  CD1 . PHE A 66  ? 0.2199 0.2532 0.1270 -0.0303 -0.0038 -0.0058 66  PHE A CD1 
519  C  CD2 . PHE A 66  ? 0.2126 0.2120 0.1437 -0.0230 -0.0038 -0.0309 66  PHE A CD2 
520  C  CE1 . PHE A 66  ? 0.2253 0.2495 0.1520 -0.0358 -0.0145 -0.0030 66  PHE A CE1 
521  C  CE2 . PHE A 66  ? 0.2300 0.2149 0.1530 -0.0287 -0.0027 -0.0386 66  PHE A CE2 
522  C  CZ  . PHE A 66  ? 0.2100 0.2217 0.1673 -0.0365 -0.0107 -0.0015 66  PHE A CZ  
523  N  N   . GLN A 67  ? 0.2005 0.2009 0.1384 0.0037  -0.0040 0.0368  67  GLN A N   
524  C  CA  . GLN A 67  ? 0.1868 0.2020 0.1495 0.0138  -0.0234 0.0096  67  GLN A CA  
525  C  C   . GLN A 67  ? 0.2488 0.1911 0.1102 0.0141  -0.0345 0.0108  67  GLN A C   
526  O  O   . GLN A 67  ? 0.2406 0.2259 0.1192 -0.0133 -0.0011 0.0290  67  GLN A O   
527  C  CB  . GLN A 67  ? 0.2177 0.2957 0.1979 -0.0293 -0.0628 0.0350  67  GLN A CB  
528  C  CG  . GLN A 67  ? 0.2160 0.3132 0.2406 -0.0358 -0.0317 0.0035  67  GLN A CG  
529  C  CD  . GLN A 67  ? 0.2992 0.3240 0.2278 -0.0535 -0.0429 -0.0212 67  GLN A CD  
530  O  OE1 . GLN A 67  ? 0.4601 0.3362 0.3080 -0.0595 -0.0084 -0.0172 67  GLN A OE1 
531  N  NE2 . GLN A 67  ? 0.2935 0.3531 0.2508 -0.0445 -0.0696 -0.0218 67  GLN A NE2 
532  N  N   . VAL A 68  ? 0.2469 0.1642 0.1351 0.0260  -0.0301 0.0149  68  VAL A N   
533  C  CA  . VAL A 68  ? 0.2827 0.1548 0.1159 0.0438  -0.0341 0.0233  68  VAL A CA  
534  C  C   . VAL A 68  ? 0.2676 0.1602 0.1212 0.0111  -0.0187 0.0178  68  VAL A C   
535  O  O   . VAL A 68  ? 0.2695 0.1732 0.1150 0.0203  -0.0364 0.0183  68  VAL A O   
536  C  CB  . VAL A 68  ? 0.2366 0.1815 0.1504 0.0367  -0.0340 -0.0122 68  VAL A CB  
537  C  CG1 . VAL A 68  ? 0.2943 0.1905 0.1619 0.0653  -0.0460 -0.0017 68  VAL A CG1 
538  C  CG2 . VAL A 68  ? 0.2518 0.1784 0.1443 0.0215  -0.0296 0.0000  68  VAL A CG2 
539  N  N   . GLU A 69  ? 0.3067 0.1472 0.1262 0.0458  0.0119  0.0156  69  GLU A N   
540  C  CA  . GLU A 69  ? 0.2400 0.1616 0.1313 0.0154  0.0013  0.0016  69  GLU A CA  
541  C  C   . GLU A 69  ? 0.2511 0.1477 0.1513 0.0319  -0.0452 0.0146  69  GLU A C   
542  O  O   . GLU A 69  ? 0.3554 0.1673 0.1678 0.0537  -0.0873 -0.0156 69  GLU A O   
543  C  CB  . GLU A 69  ? 0.2490 0.2204 0.2229 0.0201  0.0411  0.0229  69  GLU A CB  
544  C  CG  . GLU A 69  ? 0.1900 0.3014 0.2507 -0.0345 0.0150  0.0609  69  GLU A CG  
545  C  CD  . GLU A 69  ? 0.2906 0.2824 0.2764 -0.0209 0.0493  0.1070  69  GLU A CD  
546  O  OE1 . GLU A 69  ? 0.4327 0.3686 0.3316 0.0502  0.0271  0.1386  69  GLU A OE1 
547  O  OE2 . GLU A 69  ? 0.2799 0.4041 0.3401 0.0403  0.0704  0.0396  69  GLU A OE2 
548  N  N   . PHE A 70  ? 0.2413 0.1438 0.1450 -0.0003 -0.0160 0.0164  70  PHE A N   
549  C  CA  . PHE A 70  ? 0.2190 0.1323 0.1779 -0.0060 -0.0342 0.0296  70  PHE A CA  
550  C  C   . PHE A 70  ? 0.2363 0.1407 0.1854 -0.0084 -0.0261 0.0114  70  PHE A C   
551  O  O   . PHE A 70  ? 0.2519 0.1537 0.2349 -0.0272 -0.0351 0.0289  70  PHE A O   
552  C  CB  . PHE A 70  ? 0.1975 0.1445 0.1706 0.0187  -0.0269 0.0139  70  PHE A CB  
553  C  CG  . PHE A 70  ? 0.2298 0.1456 0.1571 0.0047  -0.0801 0.0234  70  PHE A CG  
554  C  CD1 . PHE A 70  ? 0.1937 0.1668 0.1795 0.0145  -0.0223 0.0201  70  PHE A CD1 
555  C  CD2 . PHE A 70  ? 0.2337 0.1626 0.1584 -0.0009 -0.0522 0.0296  70  PHE A CD2 
556  C  CE1 . PHE A 70  ? 0.2593 0.1840 0.1736 -0.0051 -0.0117 0.0116  70  PHE A CE1 
557  C  CE2 . PHE A 70  ? 0.2957 0.1531 0.1508 0.0132  -0.0577 0.0315  70  PHE A CE2 
558  C  CZ  . PHE A 70  ? 0.2493 0.1714 0.1628 0.0109  -0.0043 0.0337  70  PHE A CZ  
559  N  N   . ASP A 71  ? 0.3122 0.1445 0.2253 0.0137  -0.0665 0.0280  71  ASP A N   
560  C  CA  . ASP A 71  ? 0.2641 0.1362 0.2493 -0.0053 -0.0622 0.0245  71  ASP A CA  
561  C  C   . ASP A 71  ? 0.2227 0.1559 0.2544 -0.0006 -0.0225 -0.0022 71  ASP A C   
562  O  O   . ASP A 71  ? 0.2677 0.2317 0.3378 -0.0613 -0.0154 0.0176  71  ASP A O   
563  C  CB  . ASP A 71  ? 0.3689 0.1822 0.3079 0.0530  -0.1184 0.0453  71  ASP A CB  
564  C  CG  . ASP A 71  ? 0.4037 0.1808 0.3165 0.0097  -0.1670 0.0295  71  ASP A CG  
565  O  OD1 . ASP A 71  ? 0.3082 0.1993 0.3477 0.0091  -0.0973 0.0423  71  ASP A OD1 
566  O  OD2 . ASP A 71  ? 0.5209 0.2231 0.5862 0.0261  -0.3325 0.0439  71  ASP A OD2 
567  N  N   . ASP A 72  ? 0.2364 0.1560 0.2321 -0.0232 -0.0403 0.0270  72  ASP A N   
568  C  CA  . ASP A 72  ? 0.2575 0.1606 0.2525 -0.0099 -0.0152 0.0042  72  ASP A CA  
569  C  C   . ASP A 72  ? 0.3141 0.1571 0.2684 -0.0200 -0.0232 0.0033  72  ASP A C   
570  O  O   . ASP A 72  ? 0.3255 0.1890 0.2850 -0.0121 -0.0351 -0.0168 72  ASP A O   
571  C  CB  . ASP A 72  ? 0.2616 0.1867 0.2396 0.0060  0.0013  0.0322  72  ASP A CB  
572  C  CG  . ASP A 72  ? 0.2672 0.2314 0.2098 0.0006  -0.0096 0.0229  72  ASP A CG  
573  O  OD1 . ASP A 72  ? 0.2773 0.2644 0.2572 -0.0339 -0.0254 0.0691  72  ASP A OD1 
574  O  OD2 . ASP A 72  ? 0.2852 0.2206 0.1939 -0.0255 -0.0076 0.0138  72  ASP A OD2 
575  N  N   . SER A 73  ? 0.3130 0.1364 0.3532 -0.0134 -0.0250 0.0515  73  SER A N   
576  C  CA  . SER A 73  ? 0.3376 0.1470 0.3226 -0.0205 0.0107  -0.0071 73  SER A CA  
577  C  C   . SER A 73  ? 0.3132 0.1746 0.4141 -0.0186 0.0200  -0.0421 73  SER A C   
578  O  O   . SER A 73  ? 0.3837 0.1685 0.4046 -0.0011 -0.0763 -0.0204 73  SER A O   
579  C  CB  . SER A 73  ? 0.4014 0.2445 0.3732 -0.0741 -0.0571 0.0672  73  SER A CB  
580  O  OG  . SER A 73  ? 0.3653 0.2093 0.3330 0.0247  -0.0356 0.0356  73  SER A OG  
581  N  N   . GLN A 74  ? 0.2575 0.1960 0.4559 0.0092  0.0116  0.0013  74  GLN A N   
582  C  CA  . GLN A 74  ? 0.2831 0.2802 0.4321 0.0348  0.0395  0.0188  74  GLN A CA  
583  C  C   . GLN A 74  ? 0.3328 0.2705 0.3014 -0.0185 -0.0680 -0.0569 74  GLN A C   
584  O  O   . GLN A 74  ? 0.2676 0.2447 0.3089 -0.0314 -0.0491 0.0102  74  GLN A O   
585  C  CB  . GLN A 74  ? 0.3909 0.3349 0.4059 0.0329  -0.0099 0.0767  74  GLN A CB  
586  C  CG  . GLN A 74  ? 0.3743 0.3213 0.5758 -0.0121 -0.0693 0.0976  74  GLN A CG  
587  C  CD  . GLN A 74  ? 0.3822 0.5950 0.6448 0.1264  -0.0863 0.1066  74  GLN A CD  
588  O  OE1 . GLN A 74  ? 0.3231 0.6664 0.9691 0.0212  0.1224  0.1449  74  GLN A OE1 
589  N  NE2 . GLN A 74  ? 0.4522 0.5525 0.6246 0.0800  0.0370  0.1729  74  GLN A NE2 
590  N  N   . ASP A 75  ? 0.4644 0.3851 0.3335 0.0375  0.0127  -0.0832 75  ASP A N   
591  C  CA  . ASP A 75  ? 0.4216 0.4832 0.3417 -0.1649 -0.0072 -0.1117 75  ASP A CA  
592  C  C   . ASP A 75  ? 0.2753 0.4067 0.3891 0.0493  -0.1146 -0.1045 75  ASP A C   
593  O  O   . ASP A 75  ? 0.3201 0.6442 0.6794 0.1187  -0.1775 0.0469  75  ASP A O   
594  C  CB  . ASP A 75  ? 0.4734 0.5715 0.3553 0.0287  -0.0598 -0.1329 75  ASP A CB  
595  C  CG  . ASP A 75  ? 0.2860 0.6077 0.6510 -0.0080 -0.0833 -0.2582 75  ASP A CG  
596  O  OD1 . ASP A 75  ? 0.2856 0.7640 0.5316 0.0269  -0.0135 -0.1982 75  ASP A OD1 
597  O  OD2 . ASP A 75  ? 0.9066 0.7634 0.5006 0.0110  0.2114  -0.1713 75  ASP A OD2 
598  N  N   . LYS A 76  ? 0.3262 0.2801 0.3674 -0.0117 -0.0241 0.0085  76  LYS A N   
599  C  CA  . LYS A 76  ? 0.3378 0.2679 0.3599 0.0118  -0.0798 0.0480  76  LYS A CA  
600  C  C   . LYS A 76  ? 0.2916 0.3521 0.5054 0.0498  -0.0351 0.1415  76  LYS A C   
601  O  O   . LYS A 76  ? 0.3908 0.4932 0.5550 0.0717  0.0402  0.1053  76  LYS A O   
602  C  CB  . LYS A 76  ? 0.3359 0.2195 0.3740 -0.0391 -0.1138 0.0591  76  LYS A CB  
603  C  CG  . LYS A 76  ? 0.5700 0.3075 0.3143 -0.0588 -0.0952 0.0872  76  LYS A CG  
604  C  CD  . LYS A 76  ? 0.3750 0.3129 0.3865 -0.0074 -0.0359 0.0841  76  LYS A CD  
605  C  CE  . LYS A 76  ? 0.4906 0.3475 0.3330 0.0183  -0.1459 0.0188  76  LYS A CE  
606  N  NZ  . LYS A 76  ? 0.5253 0.3869 0.3385 0.0907  -0.0482 0.1089  76  LYS A NZ  
607  N  N   . ALA A 77  ? 0.1972 0.2939 0.3715 -0.0107 -0.0842 0.0750  77  ALA A N   
608  C  CA  . ALA A 77  ? 0.2241 0.2680 0.2451 -0.0460 -0.0529 0.0452  77  ALA A CA  
609  C  C   . ALA A 77  ? 0.1316 0.2799 0.2364 -0.0219 -0.0058 0.0261  77  ALA A C   
610  O  O   . ALA A 77  ? 0.1219 0.3729 0.3074 -0.0234 0.0000  0.0024  77  ALA A O   
611  C  CB  . ALA A 77  ? 0.3674 0.3450 0.2497 0.0398  -0.0844 -0.0059 77  ALA A CB  
612  N  N   . VAL A 78  ? 0.1757 0.2109 0.2190 -0.0150 -0.0337 0.0347  78  VAL A N   
613  C  CA  . VAL A 78  ? 0.2023 0.2188 0.1976 -0.0167 -0.0237 0.0468  78  VAL A CA  
614  C  C   . VAL A 78  ? 0.1513 0.2030 0.2077 -0.0453 -0.0234 0.0345  78  VAL A C   
615  O  O   . VAL A 78  ? 0.1619 0.2296 0.2879 -0.0675 -0.0381 0.0435  78  VAL A O   
616  C  CB  . VAL A 78  ? 0.2557 0.2673 0.2781 0.0055  0.0016  0.0170  78  VAL A CB  
617  C  CG1 . VAL A 78  ? 0.2744 0.2308 0.3457 0.0186  -0.0003 0.0386  78  VAL A CG1 
618  C  CG2 . VAL A 78  ? 0.2534 0.3037 0.4074 0.0753  0.1025  0.0051  78  VAL A CG2 
619  N  N   . LEU A 79  ? 0.1648 0.1881 0.2083 0.0130  -0.0255 0.0471  79  LEU A N   
620  C  CA  . LEU A 79  ? 0.1535 0.1804 0.2209 -0.0194 -0.0165 0.0362  79  LEU A CA  
621  C  C   . LEU A 79  ? 0.1341 0.1558 0.2461 -0.0199 0.0239  0.0306  79  LEU A C   
622  O  O   . LEU A 79  ? 0.1926 0.1969 0.2345 -0.0605 0.0331  -0.0156 79  LEU A O   
623  C  CB  . LEU A 79  ? 0.1333 0.1797 0.2992 -0.0353 0.0127  0.0463  79  LEU A CB  
624  C  CG  . LEU A 79  ? 0.1596 0.2063 0.2881 0.0173  0.0229  0.0307  79  LEU A CG  
625  C  CD1 . LEU A 79  ? 0.1835 0.2615 0.3758 -0.0300 0.0425  0.0911  79  LEU A CD1 
626  C  CD2 . LEU A 79  ? 0.1456 0.2212 0.2892 0.0345  0.0285  0.0303  79  LEU A CD2 
627  N  N   . LYS A 80  ? 0.1397 0.2410 0.2447 -0.0117 0.0311  0.0122  80  LYS A N   
628  C  CA  . LYS A 80  ? 0.2253 0.2186 0.2434 -0.0005 0.0731  0.0054  80  LYS A CA  
629  C  C   . LYS A 80  ? 0.1553 0.2009 0.2647 0.0022  0.0559  0.0184  80  LYS A C   
630  O  O   . LYS A 80  ? 0.1553 0.2065 0.2782 -0.0154 0.0201  0.0443  80  LYS A O   
631  C  CB  . LYS A 80  ? 0.2843 0.2830 0.3230 0.0558  0.0299  0.0433  80  LYS A CB  
632  C  CG  . LYS A 80  ? 0.2752 0.2816 0.4860 0.0264  0.0534  0.0686  80  LYS A CG  
633  C  CD  . LYS A 80  ? 0.3794 0.2924 0.7850 0.0599  0.1037  0.1626  80  LYS A CD  
634  C  CE  . LYS A 80  ? 0.7216 0.4465 0.8563 0.2232  0.2520  0.2666  80  LYS A CE  
635  N  NZ  . LYS A 80  ? 0.7593 0.5326 1.4114 0.2705  0.2289  -0.0938 80  LYS A NZ  
636  N  N   . GLY A 81  ? 0.2169 0.2391 0.2633 0.0131  0.1117  0.0367  81  GLY A N   
637  C  CA  . GLY A 81  ? 0.1771 0.2760 0.2866 0.0138  0.1016  0.0673  81  GLY A CA  
638  C  C   . GLY A 81  ? 0.2370 0.2195 0.2867 0.0297  0.1050  0.0644  81  GLY A C   
639  O  O   . GLY A 81  ? 0.2201 0.2580 0.2565 -0.0230 0.0900  -0.0060 81  GLY A O   
640  N  N   . GLY A 82  ? 0.2332 0.2637 0.3807 0.0262  0.1342  0.1167  82  GLY A N   
641  C  CA  . GLY A 82  ? 0.3128 0.2927 0.4541 0.0745  0.1547  0.1109  82  GLY A CA  
642  C  C   . GLY A 82  ? 0.2859 0.2727 0.3689 0.1349  0.1693  0.0886  82  GLY A C   
643  O  O   . GLY A 82  ? 0.2795 0.3432 0.3600 0.1529  0.1529  0.0650  82  GLY A O   
644  N  N   . PRO A 83  ? 0.2384 0.2002 0.3302 0.0725  0.1282  0.0671  83  PRO A N   
645  C  CA  . PRO A 83  ? 0.3108 0.2552 0.2988 0.0675  0.1496  0.0170  83  PRO A CA  
646  C  C   . PRO A 83  ? 0.2623 0.2471 0.2717 0.0666  0.0480  0.0140  83  PRO A C   
647  O  O   . PRO A 83  ? 0.3356 0.3452 0.2867 0.0582  0.0109  0.0068  83  PRO A O   
648  C  CB  . PRO A 83  ? 0.2504 0.3459 0.2504 0.0780  0.1062  0.0617  83  PRO A CB  
649  C  CG  . PRO A 83  ? 0.1932 0.2253 0.2838 0.0598  0.0935  0.0414  83  PRO A CG  
650  C  CD  . PRO A 83  ? 0.1897 0.2213 0.3363 0.0510  0.1110  0.0449  83  PRO A CD  
651  N  N   . LEU A 84  ? 0.2089 0.2091 0.2429 0.0322  0.0763  0.0179  84  LEU A N   
652  C  CA  . LEU A 84  ? 0.2623 0.1887 0.2443 0.0320  0.0762  -0.0035 84  LEU A CA  
653  C  C   . LEU A 84  ? 0.1775 0.2318 0.3082 0.0566  0.0088  -0.0493 84  LEU A C   
654  O  O   . LEU A 84  ? 0.2168 0.2602 0.3603 0.0675  0.0736  -0.0314 84  LEU A O   
655  C  CB  . LEU A 84  ? 0.1570 0.1657 0.2559 0.0084  0.0759  -0.0067 84  LEU A CB  
656  C  CG  . LEU A 84  ? 0.1698 0.1777 0.2154 0.0395  0.0598  0.0047  84  LEU A CG  
657  C  CD1 . LEU A 84  ? 0.1950 0.2129 0.2284 -0.0018 0.0264  0.0022  84  LEU A CD1 
658  C  CD2 . LEU A 84  ? 0.1666 0.1953 0.2264 0.0203  0.0606  -0.0188 84  LEU A CD2 
659  N  N   . ASP A 85  ? 0.3039 0.2082 0.2579 0.0087  0.0652  -0.0635 85  ASP A N   
660  C  CA  . ASP A 85  ? 0.3399 0.2095 0.2486 0.0048  0.0675  -0.0520 85  ASP A CA  
661  C  C   . ASP A 85  ? 0.3101 0.2420 0.3133 -0.0363 0.1141  -0.0170 85  ASP A C   
662  O  O   . ASP A 85  ? 0.3506 0.4225 0.7694 0.0592  -0.0317 -0.0717 85  ASP A O   
663  C  CB  . ASP A 85  ? 0.3725 0.3419 0.2832 -0.0544 0.1004  -0.1214 85  ASP A CB  
664  C  CG  . ASP A 85  ? 0.4490 0.5575 0.4089 -0.0218 0.2002  0.0139  85  ASP A CG  
665  O  OD1 . ASP A 85  ? 0.3554 0.7717 0.3198 -0.0748 0.0480  0.1476  85  ASP A OD1 
666  O  OD2 . ASP A 85  ? 0.5417 0.8490 0.3234 -0.0475 0.1104  -0.0758 85  ASP A OD2 
667  N  N   . GLY A 86  ? 0.5000 0.2320 0.3028 0.0403  0.1237  -0.0266 86  GLY A N   
668  C  CA  . GLY A 86  ? 0.6463 0.4444 0.2406 -0.2049 -0.0853 0.1089  86  GLY A CA  
669  C  C   . GLY A 86  ? 0.3920 0.2986 0.2913 -0.1386 0.0286  0.0078  86  GLY A C   
670  O  O   . GLY A 86  ? 0.4401 0.3826 0.3211 -0.1845 -0.0188 0.0726  86  GLY A O   
671  N  N   A THR A 87  ? 0.2547 0.2395 0.2572 0.0059  0.0885  -0.0118 87  THR A N   
672  N  N   B THR A 87  ? 0.2597 0.2522 0.2488 0.0073  0.0948  -0.0181 87  THR A N   
673  C  CA  A THR A 87  ? 0.1829 0.2367 0.2699 0.0249  0.0769  -0.0214 87  THR A CA  
674  C  CA  B THR A 87  ? 0.1863 0.2368 0.2666 0.0342  0.0726  -0.0266 87  THR A CA  
675  C  C   A THR A 87  ? 0.1427 0.1786 0.2400 -0.0145 0.0521  -0.0034 87  THR A C   
676  C  C   B THR A 87  ? 0.1480 0.1832 0.2362 -0.0145 0.0527  -0.0061 87  THR A C   
677  O  O   A THR A 87  ? 0.1682 0.1455 0.2751 -0.0155 0.0684  0.0047  87  THR A O   
678  O  O   B THR A 87  ? 0.1680 0.1520 0.2716 -0.0147 0.0616  0.0034  87  THR A O   
679  C  CB  A THR A 87  ? 0.1734 0.3657 0.3105 0.0926  0.0484  -0.0188 87  THR A CB  
680  C  CB  B THR A 87  ? 0.2130 0.3676 0.3092 0.0987  0.0390  -0.0272 87  THR A CB  
681  O  OG1 A THR A 87  ? 0.1950 0.4367 0.4318 0.0842  0.0941  -0.0858 87  THR A OG1 
682  O  OG1 B THR A 87  ? 0.4898 0.3470 0.3481 0.0307  -0.0318 0.0037  87  THR A OG1 
683  C  CG2 A THR A 87  ? 0.1185 0.2769 0.3215 0.0441  0.0365  0.0158  87  THR A CG2 
684  C  CG2 B THR A 87  ? 0.1998 0.3726 0.3735 0.0908  0.0497  -0.0373 87  THR A CG2 
685  N  N   . TYR A 88  ? 0.1213 0.1547 0.2206 0.0136  0.0337  0.0026  88  TYR A N   
686  C  CA  . TYR A 88  ? 0.0953 0.1711 0.1951 0.0113  0.0249  0.0128  88  TYR A CA  
687  C  C   . TYR A 88  ? 0.1028 0.1680 0.2054 -0.0053 -0.0008 0.0326  88  TYR A C   
688  O  O   . TYR A 88  ? 0.1513 0.2461 0.2504 -0.0750 -0.0133 0.0424  88  TYR A O   
689  C  CB  . TYR A 88  ? 0.1544 0.1520 0.1954 0.0231  -0.0003 0.0089  88  TYR A CB  
690  C  CG  . TYR A 88  ? 0.1292 0.1128 0.1771 0.0047  0.0286  0.0024  88  TYR A CG  
691  C  CD1 . TYR A 88  ? 0.1511 0.1678 0.1864 0.0124  0.0286  -0.0163 88  TYR A CD1 
692  C  CD2 . TYR A 88  ? 0.1307 0.1052 0.2057 0.0027  0.0153  -0.0005 88  TYR A CD2 
693  C  CE1 . TYR A 88  ? 0.1577 0.1710 0.1815 0.0013  0.0428  -0.0126 88  TYR A CE1 
694  C  CE2 . TYR A 88  ? 0.1559 0.1364 0.1688 -0.0099 0.0434  -0.0044 88  TYR A CE2 
695  C  CZ  . TYR A 88  ? 0.1494 0.1215 0.1754 -0.0060 0.0269  -0.0218 88  TYR A CZ  
696  O  OH  . TYR A 88  ? 0.1754 0.1685 0.1786 -0.0041 0.0319  -0.0170 88  TYR A OH  
697  N  N   . ARG A 89  ? 0.1513 0.1427 0.1838 -0.0100 0.0253  -0.0089 89  ARG A N   
698  C  CA  . ARG A 89  ? 0.1632 0.1207 0.1844 0.0019  0.0080  -0.0033 89  ARG A CA  
699  C  C   . ARG A 89  ? 0.1074 0.1269 0.1372 -0.0024 0.0077  0.0156  89  ARG A C   
700  O  O   . ARG A 89  ? 0.1072 0.1395 0.1602 -0.0016 -0.0057 0.0133  89  ARG A O   
701  C  CB  . ARG A 89  ? 0.2332 0.1317 0.2737 -0.0104 -0.0389 0.0403  89  ARG A CB  
702  C  CG  . ARG A 89  ? 0.2481 0.2819 0.4857 0.0368  -0.0515 0.1698  89  ARG A CG  
703  C  CD  . ARG A 89  ? 0.3007 0.1303 0.5036 0.0024  -0.0510 0.1492  89  ARG A CD  
704  N  NE  . ARG A 89  ? 0.3096 0.2709 0.3110 0.0240  -0.0605 0.1029  89  ARG A NE  
705  C  CZ  . ARG A 89  ? 0.4559 0.2336 0.2302 0.0131  -0.0462 0.0652  89  ARG A CZ  
706  N  NH1 . ARG A 89  ? 0.3833 0.2265 0.2320 0.0447  -0.0403 0.0574  89  ARG A NH1 
707  N  NH2 . ARG A 89  ? 0.3069 0.3898 0.3050 0.0009  -0.0726 -0.0306 89  ARG A NH2 
708  N  N   . LEU A 90  ? 0.1603 0.1289 0.1639 -0.0044 -0.0237 -0.0049 90  LEU A N   
709  C  CA  . LEU A 90  ? 0.1343 0.1395 0.1549 -0.0230 -0.0046 -0.0089 90  LEU A CA  
710  C  C   . LEU A 90  ? 0.1494 0.1341 0.1634 -0.0139 -0.0173 0.0275  90  LEU A C   
711  O  O   . LEU A 90  ? 0.1642 0.1858 0.1869 0.0172  -0.0137 0.0515  90  LEU A O   
712  C  CB  . LEU A 90  ? 0.1596 0.1506 0.1718 -0.0312 -0.0344 -0.0109 90  LEU A CB  
713  C  CG  . LEU A 90  ? 0.1699 0.1504 0.1652 -0.0237 -0.0401 -0.0133 90  LEU A CG  
714  C  CD1 . LEU A 90  ? 0.1738 0.1559 0.1940 -0.0179 -0.0145 0.0144  90  LEU A CD1 
715  C  CD2 . LEU A 90  ? 0.1599 0.2534 0.1808 -0.0560 -0.0304 -0.0127 90  LEU A CD2 
716  N  N   . ILE A 91  ? 0.1448 0.1304 0.1426 -0.0122 0.0062  0.0000  91  ILE A N   
717  C  CA  . ILE A 91  ? 0.1501 0.1391 0.1217 -0.0163 0.0049  -0.0003 91  ILE A CA  
718  C  C   . ILE A 91  ? 0.1481 0.1306 0.1408 -0.0006 0.0010  0.0156  91  ILE A C   
719  O  O   . ILE A 91  ? 0.1890 0.1347 0.1249 -0.0163 -0.0146 0.0127  91  ILE A O   
720  C  CB  . ILE A 91  ? 0.1650 0.1594 0.1336 -0.0278 -0.0013 0.0172  91  ILE A CB  
721  C  CG1 . ILE A 91  ? 0.2255 0.2099 0.1412 -0.0633 0.0148  0.0351  91  ILE A CG1 
722  C  CG2 . ILE A 91  ? 0.1422 0.1562 0.1577 -0.0197 -0.0173 -0.0016 91  ILE A CG2 
723  C  CD1 . ILE A 91  ? 0.2623 0.2271 0.1849 -0.0282 -0.0168 0.0417  91  ILE A CD1 
724  N  N   . GLN A 92  ? 0.1492 0.1217 0.1416 -0.0044 -0.0134 0.0119  92  GLN A N   
725  C  CA  . GLN A 92  ? 0.1890 0.1163 0.1282 -0.0040 0.0083  0.0243  92  GLN A CA  
726  C  C   . GLN A 92  ? 0.1578 0.1291 0.1047 -0.0231 -0.0023 0.0148  92  GLN A C   
727  O  O   . GLN A 92  ? 0.1628 0.1283 0.1082 -0.0005 -0.0076 0.0184  92  GLN A O   
728  C  CB  . GLN A 92  ? 0.1793 0.1725 0.1330 -0.0037 -0.0089 0.0121  92  GLN A CB  
729  C  CG  . GLN A 92  ? 0.1515 0.1635 0.1650 0.0061  -0.0138 0.0384  92  GLN A CG  
730  C  CD  . GLN A 92  ? 0.1587 0.1652 0.1462 -0.0199 -0.0076 0.0408  92  GLN A CD  
731  O  OE1 . GLN A 92  ? 0.2043 0.1596 0.1512 -0.0121 0.0020  0.0228  92  GLN A OE1 
732  N  NE2 . GLN A 92  ? 0.1397 0.2325 0.2838 -0.0190 0.0161  0.0622  92  GLN A NE2 
733  N  N   . PHE A 93  ? 0.1671 0.1122 0.1116 -0.0069 -0.0145 0.0141  93  PHE A N   
734  C  CA  . PHE A 93  ? 0.1570 0.0980 0.1235 -0.0109 -0.0208 0.0100  93  PHE A CA  
735  C  C   . PHE A 93  ? 0.1490 0.1234 0.0969 -0.0097 -0.0210 0.0116  93  PHE A C   
736  O  O   . PHE A 93  ? 0.2023 0.1275 0.1080 -0.0035 -0.0136 0.0116  93  PHE A O   
737  C  CB  . PHE A 93  ? 0.1498 0.1344 0.1373 -0.0220 -0.0307 0.0084  93  PHE A CB  
738  C  CG  . PHE A 93  ? 0.1632 0.1252 0.1563 -0.0260 -0.0364 0.0095  93  PHE A CG  
739  C  CD1 . PHE A 93  ? 0.1984 0.1380 0.1635 -0.0217 -0.0472 -0.0095 93  PHE A CD1 
740  C  CD2 . PHE A 93  ? 0.1966 0.1578 0.1260 0.0000  -0.0449 0.0172  93  PHE A CD2 
741  C  CE1 . PHE A 93  ? 0.1764 0.1481 0.1883 -0.0111 -0.0586 -0.0080 93  PHE A CE1 
742  C  CE2 . PHE A 93  ? 0.1971 0.1490 0.1280 -0.0050 -0.0365 -0.0030 93  PHE A CE2 
743  C  CZ  . PHE A 93  ? 0.1930 0.1307 0.1574 0.0025  -0.0321 0.0013  93  PHE A CZ  
744  N  N   . HIS A 94  ? 0.1322 0.1156 0.1125 0.0001  -0.0221 0.0019  94  HIS A N   
745  C  CA  . HIS A 94  ? 0.1234 0.1077 0.1263 -0.0003 -0.0161 0.0165  94  HIS A CA  
746  C  C   . HIS A 94  ? 0.1377 0.1129 0.0888 -0.0122 -0.0069 0.0003  94  HIS A C   
747  O  O   . HIS A 94  ? 0.1408 0.1350 0.0907 -0.0083 0.0052  0.0179  94  HIS A O   
748  C  CB  . HIS A 94  ? 0.1286 0.1540 0.1090 -0.0077 -0.0094 0.0002  94  HIS A CB  
749  C  CG  . HIS A 94  ? 0.1169 0.1257 0.1084 -0.0118 0.0025  0.0096  94  HIS A CG  
750  N  ND1 . HIS A 94  ? 0.1253 0.1418 0.0973 -0.0166 0.0119  0.0044  94  HIS A ND1 
751  C  CD2 . HIS A 94  ? 0.1194 0.1487 0.0838 -0.0151 0.0132  0.0016  94  HIS A CD2 
752  C  CE1 . HIS A 94  ? 0.1041 0.1359 0.1149 -0.0093 -0.0072 0.0179  94  HIS A CE1 
753  N  NE2 . HIS A 94  ? 0.1162 0.1398 0.0980 -0.0134 -0.0032 0.0016  94  HIS A NE2 
754  N  N   . PHE A 95  ? 0.1408 0.1138 0.1155 -0.0022 -0.0011 0.0004  95  PHE A N   
755  C  CA  . PHE A 95  ? 0.1408 0.1027 0.1163 0.0100  -0.0250 0.0018  95  PHE A CA  
756  C  C   . PHE A 95  ? 0.1217 0.1210 0.1039 -0.0057 0.0114  -0.0013 95  PHE A C   
757  O  O   . PHE A 95  ? 0.1470 0.1552 0.1238 -0.0245 0.0251  0.0156  95  PHE A O   
758  C  CB  . PHE A 95  ? 0.1419 0.1395 0.1513 -0.0111 -0.0155 -0.0216 95  PHE A CB  
759  C  CG  . PHE A 95  ? 0.1553 0.1423 0.1248 -0.0127 -0.0303 -0.0181 95  PHE A CG  
760  C  CD1 . PHE A 95  ? 0.1793 0.1544 0.1268 0.0000  -0.0300 -0.0182 95  PHE A CD1 
761  C  CD2 . PHE A 95  ? 0.1313 0.1535 0.1639 -0.0279 -0.0323 -0.0236 95  PHE A CD2 
762  C  CE1 . PHE A 95  ? 0.1858 0.1678 0.1444 0.0080  -0.0324 -0.0466 95  PHE A CE1 
763  C  CE2 . PHE A 95  ? 0.1495 0.1587 0.1609 -0.0082 -0.0361 -0.0332 95  PHE A CE2 
764  C  CZ  . PHE A 95  ? 0.1448 0.1872 0.1652 -0.0068 -0.0497 -0.0197 95  PHE A CZ  
765  N  N   . HIS A 96  ? 0.1303 0.1219 0.0961 0.0009  -0.0019 0.0027  96  HIS A N   
766  C  CA  . HIS A 96  ? 0.1355 0.1016 0.1028 -0.0027 -0.0052 -0.0120 96  HIS A CA  
767  C  C   . HIS A 96  ? 0.1117 0.1135 0.1273 -0.0223 0.0075  -0.0182 96  HIS A C   
768  O  O   . HIS A 96  ? 0.1098 0.1425 0.1357 -0.0122 0.0227  -0.0058 96  HIS A O   
769  C  CB  . HIS A 96  ? 0.1247 0.1244 0.1171 -0.0184 -0.0119 -0.0311 96  HIS A CB  
770  C  CG  . HIS A 96  ? 0.1032 0.1138 0.1164 -0.0189 0.0049  -0.0081 96  HIS A CG  
771  N  ND1 . HIS A 96  ? 0.1044 0.1359 0.1418 -0.0212 0.0189  -0.0161 96  HIS A ND1 
772  C  CD2 . HIS A 96  ? 0.1329 0.1185 0.1199 0.0001  -0.0079 -0.0120 96  HIS A CD2 
773  C  CE1 . HIS A 96  ? 0.1252 0.1451 0.1365 -0.0032 0.0294  -0.0144 96  HIS A CE1 
774  N  NE2 . HIS A 96  ? 0.1242 0.1084 0.1206 0.0055  0.0148  -0.0295 96  HIS A NE2 
775  N  N   . TRP A 97  ? 0.1368 0.1079 0.1223 -0.0111 0.0166  -0.0195 97  TRP A N   
776  C  CA  . TRP A 97  ? 0.1183 0.1125 0.1326 -0.0100 0.0053  -0.0214 97  TRP A CA  
777  C  C   . TRP A 97  ? 0.1210 0.1350 0.1133 -0.0064 0.0042  -0.0097 97  TRP A C   
778  O  O   . TRP A 97  ? 0.1260 0.1372 0.1544 -0.0159 0.0347  -0.0193 97  TRP A O   
779  C  CB  . TRP A 97  ? 0.1522 0.1544 0.0986 -0.0200 0.0025  -0.0070 97  TRP A CB  
780  C  CG  . TRP A 97  ? 0.1340 0.1348 0.1177 -0.0076 0.0140  -0.0132 97  TRP A CG  
781  C  CD1 . TRP A 97  ? 0.1754 0.1504 0.1156 -0.0055 0.0285  -0.0122 97  TRP A CD1 
782  C  CD2 . TRP A 97  ? 0.1215 0.1407 0.1111 -0.0085 0.0148  -0.0141 97  TRP A CD2 
783  N  NE1 . TRP A 97  ? 0.1886 0.1491 0.1216 -0.0245 0.0308  -0.0128 97  TRP A NE1 
784  C  CE2 . TRP A 97  ? 0.1637 0.1623 0.1234 -0.0391 0.0339  -0.0059 97  TRP A CE2 
785  C  CE3 . TRP A 97  ? 0.1678 0.1357 0.1149 -0.0255 -0.0022 -0.0227 97  TRP A CE3 
786  C  CZ2 . TRP A 97  ? 0.1754 0.1617 0.1244 -0.0419 0.0247  -0.0071 97  TRP A CZ2 
787  C  CZ3 . TRP A 97  ? 0.1882 0.1578 0.1129 -0.0210 0.0072  0.0027  97  TRP A CZ3 
788  C  CH2 . TRP A 97  ? 0.1964 0.1700 0.1186 -0.0321 0.0190  -0.0230 97  TRP A CH2 
789  N  N   . GLY A 98  ? 0.1423 0.1260 0.1297 -0.0130 0.0206  -0.0097 98  GLY A N   
790  C  CA  . GLY A 98  ? 0.1675 0.1423 0.1298 0.0105  0.0139  -0.0266 98  GLY A CA  
791  C  C   . GLY A 98  ? 0.1872 0.1343 0.1250 -0.0182 0.0216  -0.0187 98  GLY A C   
792  O  O   . GLY A 98  ? 0.2107 0.1666 0.1448 -0.0037 0.0148  -0.0302 98  GLY A O   
793  N  N   . SER A 99  ? 0.1918 0.1627 0.1623 0.0147  0.0124  -0.0438 99  SER A N   
794  C  CA  . SER A 99  ? 0.2393 0.1650 0.1976 0.0075  0.0232  -0.0659 99  SER A CA  
795  C  C   . SER A 99  ? 0.2486 0.1580 0.1844 0.0153  0.0450  -0.0466 99  SER A C   
796  O  O   . SER A 99  ? 0.3517 0.2112 0.2174 -0.0118 0.0184  -0.0682 99  SER A O   
797  C  CB  . SER A 99  ? 0.2644 0.2107 0.2155 0.0641  0.0423  -0.0621 99  SER A CB  
798  O  OG  . SER A 99  ? 0.2066 0.1821 0.2681 0.0243  0.0469  -0.0472 99  SER A OG  
799  N  N   . LEU A 100 ? 0.1781 0.1815 0.2023 -0.0060 0.0228  -0.0342 100 LEU A N   
800  C  CA  . LEU A 100 ? 0.2325 0.1319 0.2713 0.0029  -0.0069 -0.0259 100 LEU A CA  
801  C  C   . LEU A 100 ? 0.2493 0.1343 0.2490 -0.0378 0.0241  -0.0287 100 LEU A C   
802  O  O   . LEU A 100 ? 0.2541 0.1411 0.1993 -0.0209 0.0054  -0.0210 100 LEU A O   
803  C  CB  . LEU A 100 ? 0.2109 0.2253 0.3201 0.0104  0.0305  0.0551  100 LEU A CB  
804  C  CG  . LEU A 100 ? 0.2479 0.2196 0.3292 0.0454  0.0274  -0.0147 100 LEU A CG  
805  C  CD1 . LEU A 100 ? 0.3126 0.4819 0.4117 0.2392  -0.0038 -0.0372 100 LEU A CD1 
806  C  CD2 . LEU A 100 ? 0.4260 0.2427 0.3561 0.0562  0.0904  -0.0834 100 LEU A CD2 
807  N  N   . ASP A 101 ? 0.1993 0.1434 0.2680 -0.0148 0.0137  -0.0103 101 ASP A N   
808  C  CA  . ASP A 101 ? 0.1937 0.1832 0.2352 -0.0120 0.0036  -0.0002 101 ASP A CA  
809  C  C   . ASP A 101 ? 0.2683 0.0937 0.2186 -0.0130 0.0088  0.0027  101 ASP A C   
810  O  O   . ASP A 101 ? 0.4285 0.1531 0.2583 0.0328  0.0452  -0.0053 101 ASP A O   
811  C  CB  . ASP A 101 ? 0.2278 0.1955 0.2554 -0.0553 -0.0145 0.0152  101 ASP A CB  
812  C  CG  . ASP A 101 ? 0.3086 0.2518 0.2608 -0.0722 0.0039  -0.0307 101 ASP A CG  
813  O  OD1 . ASP A 101 ? 0.2546 0.2285 0.2683 -0.0313 0.0168  -0.0440 101 ASP A OD1 
814  O  OD2 . ASP A 101 ? 0.3245 0.2720 0.3549 -0.0889 0.0357  -0.0938 101 ASP A OD2 
815  N  N   . GLY A 102 ? 0.2899 0.1508 0.2388 -0.0569 -0.0054 0.0209  102 GLY A N   
816  C  CA  . GLY A 102 ? 0.3575 0.1789 0.2423 -0.0831 -0.0231 0.0301  102 GLY A CA  
817  C  C   . GLY A 102 ? 0.3215 0.1729 0.2393 -0.0578 0.0022  0.0188  102 GLY A C   
818  O  O   . GLY A 102 ? 0.2634 0.1849 0.2384 -0.0244 0.0094  0.0280  102 GLY A O   
819  N  N   A GLN A 103 ? 0.2429 0.1462 0.1594 -0.0400 0.0159  -0.0257 103 GLN A N   
820  N  N   B GLN A 103 ? 0.2615 0.1459 0.1983 -0.0328 0.0222  -0.0107 103 GLN A N   
821  C  CA  A GLN A 103 ? 0.1986 0.1448 0.1451 -0.0139 0.0051  -0.0412 103 GLN A CA  
822  C  CA  B GLN A 103 ? 0.1911 0.1393 0.1861 0.0049  0.0027  -0.0148 103 GLN A CA  
823  C  C   A GLN A 103 ? 0.1519 0.1445 0.1275 -0.0076 0.0483  -0.0384 103 GLN A C   
824  C  C   B GLN A 103 ? 0.1556 0.1430 0.1319 -0.0147 0.0160  -0.0247 103 GLN A C   
825  O  O   A GLN A 103 ? 0.1233 0.1486 0.1874 -0.0023 0.0297  -0.0442 103 GLN A O   
826  O  O   B GLN A 103 ? 0.2037 0.1427 0.1222 -0.0171 0.0364  -0.0261 103 GLN A O   
827  C  CB  A GLN A 103 ? 0.2161 0.1244 0.1642 -0.0079 0.0247  -0.0223 103 GLN A CB  
828  C  CB  B GLN A 103 ? 0.1971 0.1864 0.1768 0.0195  0.0401  -0.0084 103 GLN A CB  
829  C  CG  A GLN A 103 ? 0.2281 0.1743 0.1436 0.0147  0.0230  0.0111  103 GLN A CG  
830  C  CG  B GLN A 103 ? 0.2080 0.1954 0.2176 0.0461  0.1030  0.0105  103 GLN A CG  
831  C  CD  A GLN A 103 ? 0.2181 0.1509 0.2091 -0.0115 0.0166  0.0159  103 GLN A CD  
832  C  CD  B GLN A 103 ? 0.2260 0.2799 0.2741 0.0767  0.1061  0.0198  103 GLN A CD  
833  O  OE1 A GLN A 103 ? 0.2030 0.1459 0.1958 -0.0162 0.0504  0.0100  103 GLN A OE1 
834  O  OE1 B GLN A 103 ? 0.2221 0.2778 0.3277 0.0458  0.0150  0.0013  103 GLN A OE1 
835  N  NE2 A GLN A 103 ? 0.2326 0.1164 0.2145 -0.0033 0.0121  0.0571  103 GLN A NE2 
836  N  NE2 B GLN A 103 ? 0.1682 0.3345 0.2606 0.0485  0.1111  -0.0411 103 GLN A NE2 
837  N  N   . GLY A 104 ? 0.1350 0.1244 0.1393 0.0052  0.0234  -0.0095 104 GLY A N   
838  C  CA  . GLY A 104 ? 0.1351 0.1430 0.1419 0.0036  0.0198  -0.0106 104 GLY A CA  
839  C  C   . GLY A 104 ? 0.1468 0.1248 0.1000 -0.0022 0.0012  0.0044  104 GLY A C   
840  O  O   . GLY A 104 ? 0.1441 0.1372 0.1250 -0.0175 0.0068  0.0092  104 GLY A O   
841  N  N   . SER A 105 ? 0.1253 0.1386 0.1029 -0.0135 0.0044  -0.0147 105 SER A N   
842  C  CA  . SER A 105 ? 0.1150 0.1430 0.1222 -0.0293 0.0233  -0.0257 105 SER A CA  
843  C  C   . SER A 105 ? 0.1150 0.1220 0.1167 -0.0089 0.0015  0.0011  105 SER A C   
844  O  O   . SER A 105 ? 0.1341 0.1472 0.1409 0.0089  -0.0004 -0.0188 105 SER A O   
845  C  CB  . SER A 105 ? 0.1124 0.1341 0.1273 -0.0151 0.0203  0.0055  105 SER A CB  
846  O  OG  . SER A 105 ? 0.1456 0.1178 0.1398 -0.0164 0.0183  -0.0022 105 SER A OG  
847  N  N   . GLU A 106 ? 0.1309 0.1312 0.1127 -0.0091 0.0064  -0.0214 106 GLU A N   
848  C  CA  . GLU A 106 ? 0.1212 0.1422 0.1248 -0.0303 0.0096  0.0055  106 GLU A CA  
849  C  C   . GLU A 106 ? 0.1101 0.1377 0.1160 -0.0103 0.0002  0.0008  106 GLU A C   
850  O  O   . GLU A 106 ? 0.1230 0.1540 0.1288 0.0040  -0.0106 -0.0048 106 GLU A O   
851  C  CB  . GLU A 106 ? 0.1445 0.1494 0.1075 -0.0185 0.0138  0.0018  106 GLU A CB  
852  C  CG  . GLU A 106 ? 0.1840 0.1481 0.1208 -0.0295 0.0457  -0.0047 106 GLU A CG  
853  C  CD  . GLU A 106 ? 0.0995 0.1513 0.1558 -0.0044 0.0204  -0.0022 106 GLU A CD  
854  O  OE1 . GLU A 106 ? 0.1235 0.1451 0.1655 0.0022  0.0081  -0.0022 106 GLU A OE1 
855  O  OE2 . GLU A 106 ? 0.1172 0.1854 0.1785 -0.0001 0.0298  -0.0182 106 GLU A OE2 
856  N  N   . HIS A 107 ? 0.1081 0.1292 0.1077 -0.0055 0.0082  0.0011  107 HIS A N   
857  C  CA  . HIS A 107 ? 0.1238 0.1201 0.1037 0.0124  0.0134  0.0087  107 HIS A CA  
858  C  C   . HIS A 107 ? 0.1216 0.1133 0.1165 0.0079  0.0113  -0.0089 107 HIS A C   
859  O  O   . HIS A 107 ? 0.1226 0.1409 0.1198 -0.0052 0.0089  -0.0061 107 HIS A O   
860  C  CB  . HIS A 107 ? 0.1128 0.1226 0.1136 0.0059  0.0241  -0.0021 107 HIS A CB  
861  C  CG  . HIS A 107 ? 0.0948 0.1161 0.1075 0.0059  0.0018  -0.0038 107 HIS A CG  
862  N  ND1 . HIS A 107 ? 0.1402 0.1246 0.1143 -0.0025 0.0015  0.0105  107 HIS A ND1 
863  C  CD2 . HIS A 107 ? 0.1031 0.1319 0.1170 0.0098  0.0135  -0.0308 107 HIS A CD2 
864  C  CE1 . HIS A 107 ? 0.1411 0.1250 0.1265 0.0117  -0.0117 -0.0100 107 HIS A CE1 
865  N  NE2 . HIS A 107 ? 0.1351 0.1337 0.1309 0.0134  -0.0006 -0.0120 107 HIS A NE2 
866  N  N   . THR A 108 ? 0.1483 0.1369 0.1248 -0.0081 0.0081  0.0239  108 THR A N   
867  C  CA  . THR A 108 ? 0.1544 0.1277 0.1463 -0.0039 0.0234  0.0157  108 THR A CA  
868  C  C   . THR A 108 ? 0.1452 0.1423 0.1203 0.0063  0.0000  0.0060  108 THR A C   
869  O  O   . THR A 108 ? 0.1506 0.1552 0.1328 -0.0003 0.0079  0.0027  108 THR A O   
870  C  CB  . THR A 108 ? 0.1610 0.1786 0.1300 0.0176  -0.0087 0.0029  108 THR A CB  
871  O  OG1 . THR A 108 ? 0.1626 0.1741 0.1547 0.0212  -0.0102 0.0010  108 THR A OG1 
872  C  CG2 . THR A 108 ? 0.1668 0.2040 0.1377 0.0149  0.0182  0.0143  108 THR A CG2 
873  N  N   . VAL A 109 ? 0.1689 0.1260 0.1427 0.0025  0.0244  0.0222  109 VAL A N   
874  C  CA  . VAL A 109 ? 0.1470 0.1754 0.1461 -0.0117 0.0179  0.0209  109 VAL A CA  
875  C  C   . VAL A 109 ? 0.1634 0.1602 0.1505 -0.0248 0.0292  0.0182  109 VAL A C   
876  O  O   . VAL A 109 ? 0.1894 0.1505 0.1606 -0.0196 0.0280  0.0185  109 VAL A O   
877  C  CB  . VAL A 109 ? 0.1533 0.1954 0.1689 -0.0034 0.0177  0.0419  109 VAL A CB  
878  C  CG1 . VAL A 109 ? 0.1470 0.2382 0.1980 -0.0064 0.0331  0.0402  109 VAL A CG1 
879  C  CG2 . VAL A 109 ? 0.1901 0.1955 0.1817 0.0160  0.0198  0.0458  109 VAL A CG2 
880  N  N   . ASP A 110 ? 0.2280 0.1869 0.1261 0.0230  0.0359  0.0408  110 ASP A N   
881  C  CA  . ASP A 110 ? 0.2334 0.1696 0.1646 0.0312  0.0510  0.0468  110 ASP A CA  
882  C  C   . ASP A 110 ? 0.2303 0.1682 0.1329 0.0110  0.0275  0.0135  110 ASP A C   
883  O  O   . ASP A 110 ? 0.2580 0.1598 0.1854 0.0177  0.0074  0.0386  110 ASP A O   
884  C  CB  . ASP A 110 ? 0.2886 0.2112 0.1835 0.0027  0.0784  0.0565  110 ASP A CB  
885  C  CG  . ASP A 110 ? 0.2878 0.2255 0.1613 0.0406  0.0351  0.0576  110 ASP A CG  
886  O  OD1 . ASP A 110 ? 0.3153 0.2288 0.2224 0.0221  0.1062  0.0483  110 ASP A OD1 
887  O  OD2 . ASP A 110 ? 0.2928 0.3118 0.2960 0.0162  0.1007  0.0527  110 ASP A OD2 
888  N  N   . LYS A 111 ? 0.1793 0.1707 0.1666 0.0183  0.0024  0.0365  111 LYS A N   
889  C  CA  . LYS A 111 ? 0.2202 0.1721 0.1638 0.0511  -0.0053 0.0119  111 LYS A CA  
890  C  C   . LYS A 111 ? 0.2064 0.1756 0.1560 -0.0103 0.0212  0.0203  111 LYS A C   
891  O  O   . LYS A 111 ? 0.1900 0.1991 0.1717 0.0067  0.0255  -0.0149 111 LYS A O   
892  C  CB  . LYS A 111 ? 0.2019 0.2449 0.2081 0.0613  -0.0250 0.0383  111 LYS A CB  
893  C  CG  . LYS A 111 ? 0.3000 0.2760 0.2156 0.0655  -0.0463 0.0323  111 LYS A CG  
894  C  CD  . LYS A 111 ? 0.2575 0.3495 0.2931 0.0405  -0.0424 -0.0366 111 LYS A CD  
895  C  CE  . LYS A 111 ? 0.3937 0.7153 0.3358 0.0577  -0.0619 -0.1401 111 LYS A CE  
896  N  NZ  . LYS A 111 ? 0.3577 0.8011 0.4529 -0.0176 -0.1416 0.0602  111 LYS A NZ  
897  N  N   . LYS A 112 ? 0.2025 0.1535 0.1456 -0.0099 0.0125  0.0152  112 LYS A N   
898  C  CA  . LYS A 112 ? 0.2166 0.1731 0.1452 -0.0050 0.0099  0.0217  112 LYS A CA  
899  C  C   . LYS A 112 ? 0.1628 0.1513 0.1441 0.0183  0.0001  0.0086  112 LYS A C   
900  O  O   . LYS A 112 ? 0.1958 0.1391 0.1492 0.0137  0.0167  -0.0047 112 LYS A O   
901  C  CB  . LYS A 112 ? 0.2158 0.1886 0.1864 -0.0407 -0.0047 0.0223  112 LYS A CB  
902  C  CG  . LYS A 112 ? 0.2131 0.2533 0.1863 -0.0060 0.0140  -0.0345 112 LYS A CG  
903  C  CD  . LYS A 112 ? 0.2186 0.3765 0.3137 -0.0506 -0.0590 0.0071  112 LYS A CD  
904  C  CE  . LYS A 112 ? 0.2199 0.3987 0.3279 -0.0255 -0.0646 0.0046  112 LYS A CE  
905  N  NZ  . LYS A 112 ? 0.4153 0.3524 0.3661 -0.0082 -0.1078 0.0823  112 LYS A NZ  
906  N  N   A LYS A 113 ? 0.2117 0.1493 0.1371 0.0158  0.0118  0.0088  113 LYS A N   
907  N  N   B LYS A 113 ? 0.2029 0.1409 0.1409 0.0239  0.0107  0.0119  113 LYS A N   
908  C  CA  A LYS A 113 ? 0.1984 0.1653 0.1336 0.0198  0.0171  0.0203  113 LYS A CA  
909  C  CA  B LYS A 113 ? 0.1626 0.1754 0.1422 0.0079  0.0110  0.0300  113 LYS A CA  
910  C  C   A LYS A 113 ? 0.1707 0.1292 0.1558 -0.0154 0.0306  0.0209  113 LYS A C   
911  C  C   B LYS A 113 ? 0.1555 0.1307 0.1735 -0.0283 0.0062  0.0298  113 LYS A C   
912  O  O   A LYS A 113 ? 0.2518 0.1344 0.2343 -0.0364 0.0066  0.0143  113 LYS A O   
913  O  O   B LYS A 113 ? 0.2903 0.1289 0.2199 -0.0234 -0.0207 0.0055  113 LYS A O   
914  C  CB  A LYS A 113 ? 0.1811 0.2048 0.1300 0.0240  -0.0036 0.0042  113 LYS A CB  
915  C  CB  B LYS A 113 ? 0.1584 0.1889 0.2101 0.0324  0.0059  0.0012  113 LYS A CB  
916  C  CG  A LYS A 113 ? 0.1759 0.2034 0.1646 -0.0044 0.0000  0.0111  113 LYS A CG  
917  C  CG  B LYS A 113 ? 0.1644 0.2170 0.2170 0.0182  0.0042  -0.0075 113 LYS A CG  
918  C  CD  A LYS A 113 ? 0.1692 0.2188 0.2079 -0.0005 -0.0092 -0.0399 113 LYS A CD  
919  C  CD  B LYS A 113 ? 0.1707 0.2223 0.2661 0.0361  0.0181  0.0019  113 LYS A CD  
920  C  CE  A LYS A 113 ? 0.2262 0.2534 0.2105 -0.0411 -0.0402 -0.0374 113 LYS A CE  
921  C  CE  B LYS A 113 ? 0.1940 0.2881 0.2860 0.0151  0.0094  0.0070  113 LYS A CE  
922  N  NZ  A LYS A 113 ? 0.1548 0.3481 0.2472 0.0258  -0.0139 0.0089  113 LYS A NZ  
923  N  NZ  B LYS A 113 ? 0.2518 0.2361 0.3452 0.0414  0.0171  -0.0220 113 LYS A NZ  
924  N  N   . TYR A 114 ? 0.1384 0.1416 0.1480 -0.0002 0.0178  0.0122  114 TYR A N   
925  C  CA  . TYR A 114 ? 0.1337 0.1296 0.1445 0.0058  0.0063  0.0106  114 TYR A CA  
926  C  C   . TYR A 114 ? 0.1376 0.1160 0.1502 -0.0319 0.0082  0.0043  114 TYR A C   
927  O  O   . TYR A 114 ? 0.1250 0.1362 0.1731 -0.0242 0.0242  -0.0088 114 TYR A O   
928  C  CB  . TYR A 114 ? 0.1239 0.1264 0.1869 0.0053  0.0425  0.0216  114 TYR A CB  
929  C  CG  . TYR A 114 ? 0.1107 0.1659 0.1609 0.0013  0.0100  0.0201  114 TYR A CG  
930  C  CD1 . TYR A 114 ? 0.1840 0.1986 0.1434 0.0500  0.0245  0.0301  114 TYR A CD1 
931  C  CD2 . TYR A 114 ? 0.1041 0.1894 0.2270 0.0021  0.0267  0.0293  114 TYR A CD2 
932  C  CE1 . TYR A 114 ? 0.2229 0.2192 0.1811 0.0348  0.0358  0.0286  114 TYR A CE1 
933  C  CE2 . TYR A 114 ? 0.1562 0.2375 0.2396 -0.0205 0.0579  0.0171  114 TYR A CE2 
934  C  CZ  . TYR A 114 ? 0.2429 0.2627 0.2016 0.0044  0.0666  0.0390  114 TYR A CZ  
935  O  OH  . TYR A 114 ? 0.2505 0.3980 0.2978 0.0199  0.1058  0.1161  114 TYR A OH  
936  N  N   . ALA A 115 ? 0.1495 0.1298 0.1473 -0.0168 -0.0017 -0.0158 115 ALA A N   
937  C  CA  . ALA A 115 ? 0.1497 0.1201 0.1498 -0.0204 0.0019  -0.0118 115 ALA A CA  
938  C  C   . ALA A 115 ? 0.1639 0.1271 0.1560 -0.0095 0.0019  0.0057  115 ALA A C   
939  O  O   . ALA A 115 ? 0.1359 0.1368 0.1592 -0.0195 0.0082  -0.0138 115 ALA A O   
940  C  CB  . ALA A 115 ? 0.1897 0.1596 0.2184 -0.0201 -0.0441 -0.0348 115 ALA A CB  
941  N  N   . ALA A 116 ? 0.1404 0.1140 0.1448 -0.0199 0.0000  -0.0114 116 ALA A N   
942  C  CA  . ALA A 116 ? 0.1432 0.1167 0.1110 0.0125  0.0093  0.0058  116 ALA A CA  
943  C  C   . ALA A 116 ? 0.1192 0.1172 0.1152 0.0026  0.0044  0.0008  116 ALA A C   
944  O  O   . ALA A 116 ? 0.1140 0.1351 0.1254 -0.0087 0.0032  0.0109  116 ALA A O   
945  C  CB  . ALA A 116 ? 0.1448 0.1523 0.1222 0.0046  -0.0027 0.0223  116 ALA A CB  
946  N  N   . GLU A 117 ? 0.1326 0.1084 0.1226 0.0000  0.0022  -0.0055 117 GLU A N   
947  C  CA  . GLU A 117 ? 0.1312 0.1018 0.1220 -0.0003 -0.0121 -0.0068 117 GLU A CA  
948  C  C   . GLU A 117 ? 0.1174 0.1163 0.1058 0.0000  0.0031  -0.0006 117 GLU A C   
949  O  O   . GLU A 117 ? 0.1242 0.1552 0.1430 0.0027  0.0284  0.0100  117 GLU A O   
950  C  CB  . GLU A 117 ? 0.1304 0.1452 0.1204 -0.0107 -0.0065 -0.0166 117 GLU A CB  
951  C  CG  . GLU A 117 ? 0.1423 0.1492 0.1154 -0.0058 -0.0109 -0.0133 117 GLU A CG  
952  C  CD  . GLU A 117 ? 0.1357 0.1544 0.1199 0.0130  -0.0079 -0.0137 117 GLU A CD  
953  O  OE1 . GLU A 117 ? 0.1262 0.1793 0.1303 0.0004  -0.0057 0.0001  117 GLU A OE1 
954  O  OE2 . GLU A 117 ? 0.1707 0.1616 0.1102 -0.0117 -0.0066 -0.0033 117 GLU A OE2 
955  N  N   . LEU A 118 ? 0.1149 0.1152 0.1210 0.0040  -0.0190 -0.0006 118 LEU A N   
956  C  CA  . LEU A 118 ? 0.1100 0.1186 0.1091 -0.0131 -0.0165 0.0027  118 LEU A CA  
957  C  C   . LEU A 118 ? 0.1135 0.1144 0.1095 0.0017  0.0121  0.0036  118 LEU A C   
958  O  O   . LEU A 118 ? 0.1117 0.1233 0.1115 -0.0050 0.0115  0.0027  118 LEU A O   
959  C  CB  . LEU A 118 ? 0.0881 0.1332 0.1634 0.0047  -0.0046 0.0040  118 LEU A CB  
960  C  CG  . LEU A 118 ? 0.1192 0.1527 0.1395 0.0076  -0.0359 0.0207  118 LEU A CG  
961  C  CD1 . LEU A 118 ? 0.2000 0.1384 0.1373 0.0003  -0.0125 0.0168  118 LEU A CD1 
962  C  CD2 . LEU A 118 ? 0.1183 0.1929 0.1588 -0.0016 -0.0337 0.0070  118 LEU A CD2 
963  N  N   . HIS A 119 ? 0.0998 0.1025 0.1194 -0.0100 -0.0140 0.0086  119 HIS A N   
964  C  CA  . HIS A 119 ? 0.0862 0.1156 0.1172 -0.0044 -0.0033 0.0034  119 HIS A CA  
965  C  C   . HIS A 119 ? 0.0973 0.1183 0.0982 -0.0085 -0.0176 -0.0010 119 HIS A C   
966  O  O   . HIS A 119 ? 0.1192 0.1427 0.1102 0.0076  0.0025  0.0114  119 HIS A O   
967  C  CB  . HIS A 119 ? 0.0804 0.1280 0.1189 0.0035  -0.0097 0.0113  119 HIS A CB  
968  C  CG  . HIS A 119 ? 0.1041 0.1041 0.1068 0.0036  -0.0104 -0.0034 119 HIS A CG  
969  N  ND1 . HIS A 119 ? 0.0964 0.1405 0.1090 -0.0002 -0.0030 -0.0008 119 HIS A ND1 
970  C  CD2 . HIS A 119 ? 0.1181 0.1176 0.1004 0.0037  -0.0048 0.0059  119 HIS A CD2 
971  C  CE1 . HIS A 119 ? 0.1289 0.1214 0.0788 -0.0146 0.0111  0.0030  119 HIS A CE1 
972  N  NE2 . HIS A 119 ? 0.1149 0.1195 0.1061 0.0081  0.0042  0.0048  119 HIS A NE2 
973  N  N   . LEU A 120 ? 0.0961 0.1080 0.1199 -0.0026 -0.0021 0.0039  120 LEU A N   
974  C  CA  . LEU A 120 ? 0.0935 0.1111 0.1372 -0.0042 -0.0130 0.0061  120 LEU A CA  
975  C  C   . LEU A 120 ? 0.1064 0.1183 0.1107 0.0022  -0.0100 0.0130  120 LEU A C   
976  O  O   . LEU A 120 ? 0.1093 0.1238 0.1133 -0.0097 -0.0071 0.0070  120 LEU A O   
977  C  CB  . LEU A 120 ? 0.0889 0.1361 0.1548 0.0111  -0.0259 0.0010  120 LEU A CB  
978  C  CG  . LEU A 120 ? 0.1089 0.1502 0.1646 -0.0146 -0.0313 0.0107  120 LEU A CG  
979  C  CD1 . LEU A 120 ? 0.2418 0.1840 0.1706 -0.0776 -0.0076 0.0009  120 LEU A CD1 
980  C  CD2 . LEU A 120 ? 0.1405 0.2270 0.1892 0.0082  -0.0744 -0.0052 120 LEU A CD2 
981  N  N   . VAL A 121 ? 0.1104 0.1068 0.1409 -0.0149 -0.0022 0.0128  121 VAL A N   
982  C  CA  . VAL A 121 ? 0.1243 0.1011 0.1244 -0.0265 0.0232  0.0046  121 VAL A CA  
983  C  C   . VAL A 121 ? 0.1380 0.0985 0.1036 -0.0226 -0.0001 0.0179  121 VAL A C   
984  O  O   . VAL A 121 ? 0.1371 0.1286 0.1117 -0.0055 0.0044  0.0144  121 VAL A O   
985  C  CB  . VAL A 121 ? 0.1129 0.1080 0.1298 -0.0229 0.0157  0.0070  121 VAL A CB  
986  C  CG1 . VAL A 121 ? 0.1329 0.1234 0.1574 -0.0402 -0.0030 0.0111  121 VAL A CG1 
987  C  CG2 . VAL A 121 ? 0.1268 0.1244 0.1659 0.0020  0.0034  -0.0029 121 VAL A CG2 
988  N  N   . HIS A 122 ? 0.1108 0.1048 0.1229 -0.0088 0.0000  -0.0055 122 HIS A N   
989  C  CA  . HIS A 122 ? 0.1022 0.1016 0.1438 -0.0063 0.0052  0.0009  122 HIS A CA  
990  C  C   . HIS A 122 ? 0.1131 0.1056 0.1140 -0.0122 0.0179  -0.0058 122 HIS A C   
991  O  O   . HIS A 122 ? 0.1438 0.1174 0.1397 -0.0096 -0.0065 0.0025  122 HIS A O   
992  C  CB  . HIS A 122 ? 0.1248 0.1285 0.1416 -0.0110 0.0254  -0.0019 122 HIS A CB  
993  C  CG  . HIS A 122 ? 0.1083 0.1275 0.1427 -0.0049 0.0156  0.0050  122 HIS A CG  
994  N  ND1 . HIS A 122 ? 0.1124 0.1207 0.1738 -0.0109 0.0091  0.0070  122 HIS A ND1 
995  C  CD2 . HIS A 122 ? 0.1310 0.1477 0.1577 -0.0061 -0.0025 0.0058  122 HIS A CD2 
996  C  CE1 . HIS A 122 ? 0.0928 0.1659 0.1874 -0.0079 0.0143  -0.0177 122 HIS A CE1 
997  N  NE2 . HIS A 122 ? 0.1344 0.1573 0.1630 -0.0198 -0.0072 0.0047  122 HIS A NE2 
998  N  N   . TRP A 123 ? 0.1106 0.1007 0.1585 -0.0047 0.0230  -0.0131 123 TRP A N   
999  C  CA  . TRP A 123 ? 0.1306 0.1077 0.1353 -0.0171 0.0245  -0.0195 123 TRP A CA  
1000 C  C   . TRP A 123 ? 0.1119 0.1210 0.1430 -0.0067 0.0143  0.0010  123 TRP A C   
1001 O  O   . TRP A 123 ? 0.1136 0.1347 0.1713 -0.0084 0.0104  0.0091  123 TRP A O   
1002 C  CB  . TRP A 123 ? 0.1335 0.1438 0.1553 -0.0194 0.0189  0.0190  123 TRP A CB  
1003 C  CG  . TRP A 123 ? 0.1574 0.1339 0.1501 -0.0270 0.0253  0.0077  123 TRP A CG  
1004 C  CD1 . TRP A 123 ? 0.1566 0.1291 0.1474 -0.0322 -0.0108 0.0215  123 TRP A CD1 
1005 C  CD2 . TRP A 123 ? 0.1980 0.1359 0.1343 -0.0078 0.0359  0.0136  123 TRP A CD2 
1006 N  NE1 . TRP A 123 ? 0.1919 0.1391 0.1695 -0.0099 -0.0121 0.0095  123 TRP A NE1 
1007 C  CE2 . TRP A 123 ? 0.2409 0.1210 0.1626 -0.0093 0.0126  0.0187  123 TRP A CE2 
1008 C  CE3 . TRP A 123 ? 0.2029 0.1165 0.1918 -0.0305 0.0339  0.0003  123 TRP A CE3 
1009 C  CZ2 . TRP A 123 ? 0.2370 0.1418 0.1542 0.0075  0.0155  0.0149  123 TRP A CZ2 
1010 C  CZ3 . TRP A 123 ? 0.2392 0.1402 0.1947 -0.0384 0.0223  0.0275  123 TRP A CZ3 
1011 C  CH2 . TRP A 123 ? 0.2411 0.1305 0.1973 -0.0420 0.0013  -0.0060 123 TRP A CH2 
1012 N  N   . ASN A 124 ? 0.1257 0.1340 0.1295 -0.0087 0.0236  -0.0285 124 ASN A N   
1013 C  CA  . ASN A 124 ? 0.1544 0.1188 0.1549 0.0066  0.0267  -0.0136 124 ASN A CA  
1014 C  C   . ASN A 124 ? 0.1585 0.1314 0.1552 0.0094  0.0150  -0.0027 124 ASN A C   
1015 O  O   . ASN A 124 ? 0.1541 0.1243 0.1778 -0.0020 0.0298  -0.0146 124 ASN A O   
1016 C  CB  . ASN A 124 ? 0.2066 0.1556 0.1186 0.0000  0.0242  -0.0142 124 ASN A CB  
1017 C  CG  . ASN A 124 ? 0.2213 0.1495 0.1459 -0.0037 0.0381  -0.0170 124 ASN A CG  
1018 O  OD1 . ASN A 124 ? 0.2249 0.1519 0.2039 -0.0066 0.0487  -0.0367 124 ASN A OD1 
1019 N  ND2 . ASN A 124 ? 0.3172 0.1486 0.1438 -0.0022 0.0376  -0.0065 124 ASN A ND2 
1020 N  N   . THR A 125 ? 0.1497 0.1192 0.2015 0.0179  0.0135  -0.0116 125 THR A N   
1021 C  CA  . THR A 125 ? 0.1741 0.1129 0.2415 0.0047  0.0020  -0.0190 125 THR A CA  
1022 C  C   . THR A 125 ? 0.1808 0.1156 0.2177 0.0042  0.0133  -0.0190 125 THR A C   
1023 O  O   . THR A 125 ? 0.1709 0.1398 0.2684 0.0077  0.0170  0.0077  125 THR A O   
1024 C  CB  . THR A 125 ? 0.1828 0.1944 0.2830 0.0100  -0.0170 0.0351  125 THR A CB  
1025 O  OG1 . THR A 125 ? 0.1966 0.2131 0.3610 0.0353  0.0456  0.0078  125 THR A OG1 
1026 C  CG2 . THR A 125 ? 0.2318 0.1947 0.3614 -0.0070 -0.0536 0.0147  125 THR A CG2 
1027 N  N   . LYS A 126 ? 0.1638 0.1553 0.1847 0.0118  0.0403  -0.0085 127 LYS A N   
1028 C  CA  . LYS A 126 ? 0.2229 0.1416 0.2194 -0.0035 0.0339  -0.0267 127 LYS A CA  
1029 C  C   . LYS A 126 ? 0.2058 0.1470 0.1923 0.0035  0.0249  -0.0279 127 LYS A C   
1030 O  O   . LYS A 126 ? 0.2281 0.1481 0.2451 -0.0274 0.0499  -0.0359 127 LYS A O   
1031 C  CB  . LYS A 126 ? 0.3003 0.1817 0.2368 -0.0179 0.0422  -0.0165 127 LYS A CB  
1032 C  CG  . LYS A 126 ? 0.2950 0.2083 0.2562 0.0139  0.0422  -0.0107 127 LYS A CG  
1033 C  CD  . LYS A 126 ? 0.7221 0.3414 0.2514 0.0334  0.1879  0.0232  127 LYS A CD  
1034 C  CE  . LYS A 126 ? 0.9064 0.3820 0.5449 -0.0516 -0.0116 -0.0958 127 LYS A CE  
1035 N  NZ  . LYS A 126 ? 1.1481 0.6821 0.3470 -0.3395 -0.3120 0.2531  127 LYS A NZ  
1036 N  N   . TYR A 127 ? 0.1713 0.1312 0.1872 -0.0150 0.0333  -0.0164 128 TYR A N   
1037 C  CA  . TYR A 127 ? 0.1509 0.1380 0.1840 -0.0131 0.0092  0.0284  128 TYR A CA  
1038 C  C   . TYR A 127 ? 0.1797 0.1137 0.1735 -0.0199 0.0226  -0.0136 128 TYR A C   
1039 O  O   . TYR A 127 ? 0.1856 0.1547 0.1951 -0.0250 0.0363  -0.0001 128 TYR A O   
1040 C  CB  . TYR A 127 ? 0.1883 0.1549 0.1627 0.0286  0.0298  -0.0005 128 TYR A CB  
1041 C  CG  . TYR A 127 ? 0.1847 0.1596 0.1689 -0.0006 0.0042  -0.0146 128 TYR A CG  
1042 C  CD1 . TYR A 127 ? 0.2300 0.1468 0.2079 0.0069  -0.0347 -0.0284 128 TYR A CD1 
1043 C  CD2 . TYR A 127 ? 0.1788 0.1529 0.1968 0.0264  0.0373  0.0012  128 TYR A CD2 
1044 C  CE1 . TYR A 127 ? 0.2841 0.1588 0.1987 0.0313  0.0154  -0.0086 128 TYR A CE1 
1045 C  CE2 . TYR A 127 ? 0.2252 0.1574 0.1808 0.0159  0.0044  -0.0290 128 TYR A CE2 
1046 C  CZ  . TYR A 127 ? 0.2659 0.1517 0.1714 0.0394  -0.0207 -0.0309 128 TYR A CZ  
1047 O  OH  . TYR A 127 ? 0.3299 0.2190 0.1681 0.0248  -0.0387 -0.0407 128 TYR A OH  
1048 N  N   . GLY A 128 ? 0.1993 0.1520 0.1711 0.0000  0.0031  0.0103  129 GLY A N   
1049 C  CA  . GLY A 128 ? 0.2019 0.1559 0.1644 -0.0012 0.0219  0.0001  129 GLY A CA  
1050 C  C   . GLY A 128 ? 0.1965 0.1273 0.1775 -0.0060 0.0396  0.0043  129 GLY A C   
1051 O  O   . GLY A 128 ? 0.2271 0.1655 0.2041 0.0086  -0.0117 0.0174  129 GLY A O   
1052 N  N   . ASP A 129 ? 0.1840 0.1573 0.1843 0.0091  0.0369  -0.0080 130 ASP A N   
1053 C  CA  . ASP A 129 ? 0.2206 0.1606 0.1430 0.0306  0.0268  0.0054  130 ASP A CA  
1054 C  C   . ASP A 129 ? 0.1779 0.1717 0.1452 0.0040  0.0040  -0.0055 130 ASP A C   
1055 O  O   . ASP A 129 ? 0.2071 0.1617 0.1616 0.0149  -0.0019 0.0001  130 ASP A O   
1056 C  CB  . ASP A 129 ? 0.2899 0.1962 0.1298 0.0276  0.0263  0.0408  130 ASP A CB  
1057 C  CG  . ASP A 129 ? 0.2776 0.1790 0.2672 0.0347  0.0368  -0.0206 130 ASP A CG  
1058 O  OD1 . ASP A 129 ? 0.3560 0.2100 0.2831 -0.0182 -0.0734 0.0361  130 ASP A OD1 
1059 O  OD2 . ASP A 129 ? 0.3231 0.2319 0.4020 -0.0164 0.0010  0.0522  130 ASP A OD2 
1060 N  N   . TYR A 130 ? 0.2418 0.1238 0.1465 0.0011  0.0299  0.0046  131 TYR A N   
1061 C  CA  . TYR A 130 ? 0.1595 0.1434 0.1590 0.0073  0.0087  0.0034  131 TYR A CA  
1062 C  C   . TYR A 130 ? 0.1591 0.1648 0.1596 -0.0262 0.0216  0.0141  131 TYR A C   
1063 O  O   . TYR A 130 ? 0.1376 0.1745 0.1637 -0.0099 0.0166  -0.0017 131 TYR A O   
1064 C  CB  . TYR A 130 ? 0.2418 0.1377 0.1628 -0.0130 0.0116  -0.0132 131 TYR A CB  
1065 C  CG  . TYR A 130 ? 0.1590 0.1469 0.1306 -0.0081 0.0091  0.0135  131 TYR A CG  
1066 C  CD1 . TYR A 130 ? 0.1264 0.1606 0.1601 -0.0177 0.0029  0.0306  131 TYR A CD1 
1067 C  CD2 . TYR A 130 ? 0.1926 0.1553 0.1495 -0.0115 0.0370  0.0134  131 TYR A CD2 
1068 C  CE1 . TYR A 130 ? 0.1666 0.1610 0.1800 -0.0271 0.0200  0.0040  131 TYR A CE1 
1069 C  CE2 . TYR A 130 ? 0.2107 0.1346 0.1858 -0.0351 0.0113  0.0012  131 TYR A CE2 
1070 C  CZ  . TYR A 130 ? 0.1595 0.1468 0.1842 -0.0189 0.0261  0.0058  131 TYR A CZ  
1071 O  OH  . TYR A 130 ? 0.1860 0.1468 0.2163 -0.0138 0.0104  0.0107  131 TYR A OH  
1072 N  N   . GLY A 131 ? 0.1885 0.1667 0.1673 -0.0370 0.0446  -0.0039 132 GLY A N   
1073 C  CA  . GLY A 131 ? 0.1696 0.2119 0.2043 -0.0414 0.0410  0.0034  132 GLY A CA  
1074 C  C   . GLY A 131 ? 0.1675 0.1754 0.1971 -0.0280 0.0346  0.0078  132 GLY A C   
1075 O  O   . GLY A 131 ? 0.1628 0.2129 0.2580 0.0031  0.0079  -0.0068 132 GLY A O   
1076 N  N   . LYS A 132 ? 0.1914 0.1699 0.1858 -0.0425 0.0341  -0.0076 133 LYS A N   
1077 C  CA  . LYS A 132 ? 0.1861 0.1548 0.1857 -0.0316 0.0024  0.0144  133 LYS A CA  
1078 C  C   . LYS A 132 ? 0.1495 0.1784 0.1707 -0.0262 0.0168  0.0044  133 LYS A C   
1079 O  O   . LYS A 132 ? 0.1833 0.2095 0.1948 -0.0453 -0.0129 0.0140  133 LYS A O   
1080 C  CB  . LYS A 132 ? 0.1703 0.1890 0.2615 0.0018  -0.0095 0.0084  133 LYS A CB  
1081 C  CG  . LYS A 132 ? 0.4647 0.2866 0.4119 -0.0263 0.0996  0.1548  133 LYS A CG  
1082 C  CD  . LYS A 132 ? 0.5341 0.3513 0.3324 -0.1149 0.0657  0.0743  133 LYS A CD  
1083 C  CE  . LYS A 132 ? 0.4313 0.2906 0.2626 -0.1114 0.0955  0.0651  133 LYS A CE  
1084 N  NZ  . LYS A 132 ? 0.7455 0.6901 0.5808 -0.0713 0.3864  -0.1511 133 LYS A NZ  
1085 N  N   . ALA A 133 ? 0.1451 0.1502 0.1732 -0.0318 0.0190  0.0005  134 ALA A N   
1086 C  CA  . ALA A 133 ? 0.1228 0.1914 0.1553 -0.0179 0.0188  0.0251  134 ALA A CA  
1087 C  C   . ALA A 133 ? 0.1405 0.1603 0.1463 -0.0168 0.0206  0.0170  134 ALA A C   
1088 O  O   . ALA A 133 ? 0.1404 0.2278 0.1585 -0.0252 0.0060  0.0210  134 ALA A O   
1089 C  CB  . ALA A 133 ? 0.1411 0.1617 0.1398 -0.0274 0.0138  0.0228  134 ALA A CB  
1090 N  N   . GLN A 134 ? 0.1336 0.1723 0.1826 -0.0134 0.0275  0.0139  135 GLN A N   
1091 C  CA  . GLN A 134 ? 0.1541 0.2039 0.1905 0.0124  0.0279  -0.0058 135 GLN A CA  
1092 C  C   . GLN A 134 ? 0.1983 0.2120 0.2009 -0.0233 -0.0040 0.0326  135 GLN A C   
1093 O  O   . GLN A 134 ? 0.2145 0.2620 0.2640 0.0120  -0.0149 0.0709  135 GLN A O   
1094 C  CB  . GLN A 134 ? 0.2210 0.2309 0.2064 0.0068  0.0620  -0.0397 135 GLN A CB  
1095 C  CG  . GLN A 134 ? 0.2277 0.2220 0.2367 -0.0214 0.0384  -0.0086 135 GLN A CG  
1096 C  CD  . GLN A 134 ? 0.2048 0.2792 0.2241 -0.0280 0.0413  0.0133  135 GLN A CD  
1097 O  OE1 . GLN A 134 ? 0.2082 0.3984 0.2861 0.0187  0.0658  -0.0166 135 GLN A OE1 
1098 N  NE2 . GLN A 134 ? 0.2262 0.2350 0.2228 0.0221  0.0359  -0.0065 135 GLN A NE2 
1099 N  N   . GLN A 135 ? 0.1516 0.2433 0.1732 -0.0350 0.0259  -0.0124 136 GLN A N   
1100 C  CA  . GLN A 135 ? 0.1558 0.2889 0.2086 -0.0638 0.0140  -0.0120 136 GLN A CA  
1101 C  C   . GLN A 135 ? 0.1386 0.3273 0.1790 -0.0375 -0.0078 0.0422  136 GLN A C   
1102 O  O   . GLN A 135 ? 0.2041 0.4612 0.2354 -0.0756 -0.0475 -0.0006 136 GLN A O   
1103 C  CB  . GLN A 135 ? 0.1603 0.3294 0.2397 -0.0857 0.0015  -0.0094 136 GLN A CB  
1104 C  CG  . GLN A 135 ? 0.2548 0.4956 0.2572 -0.1058 0.0333  0.0555  136 GLN A CG  
1105 C  CD  . GLN A 135 ? 0.3592 0.7267 0.3937 -0.0247 0.0006  -0.0705 136 GLN A CD  
1106 O  OE1 . GLN A 135 ? 0.4332 1.1701 0.5356 0.0239  -0.0993 -0.0384 136 GLN A OE1 
1107 N  NE2 . GLN A 135 ? 0.7212 1.0046 0.3581 0.0383  0.0476  -0.1429 136 GLN A NE2 
1108 N  N   . GLN A 136 ? 0.1456 0.2181 0.1747 -0.0079 0.0258  0.0250  137 GLN A N   
1109 C  CA  . GLN A 136 ? 0.1768 0.1838 0.1426 -0.0004 -0.0131 -0.0137 137 GLN A CA  
1110 C  C   . GLN A 136 ? 0.1948 0.1889 0.1194 0.0077  -0.0060 -0.0179 137 GLN A C   
1111 O  O   . GLN A 136 ? 0.1883 0.1846 0.1223 -0.0063 0.0088  -0.0247 137 GLN A O   
1112 C  CB  . GLN A 136 ? 0.1652 0.1684 0.2244 0.0044  -0.0057 0.0005  137 GLN A CB  
1113 C  CG  . GLN A 136 ? 0.2612 0.2126 0.1836 0.0131  -0.0029 0.0148  137 GLN A CG  
1114 C  CD  . GLN A 136 ? 0.2386 0.2609 0.2853 -0.0124 -0.0425 0.0961  137 GLN A CD  
1115 O  OE1 . GLN A 136 ? 0.3776 0.2298 0.2758 -0.0178 -0.1021 -0.0250 137 GLN A OE1 
1116 N  NE2 . GLN A 136 ? 0.3740 0.3793 0.4454 -0.0226 0.0353  0.2120  137 GLN A NE2 
1117 N  N   . PRO A 137 ? 0.2064 0.1976 0.1172 0.0003  -0.0314 -0.0192 138 PRO A N   
1118 C  CA  . PRO A 137 ? 0.2009 0.2440 0.1178 0.0230  -0.0006 0.0035  138 PRO A CA  
1119 C  C   . PRO A 137 ? 0.2276 0.1991 0.1258 0.0073  0.0001  -0.0186 138 PRO A C   
1120 O  O   . PRO A 137 ? 0.2294 0.2145 0.1693 0.0264  0.0409  0.0025  138 PRO A O   
1121 C  CB  . PRO A 137 ? 0.3347 0.2784 0.1325 0.0005  -0.0272 -0.0286 138 PRO A CB  
1122 C  CG  . PRO A 137 ? 0.4569 0.3262 0.1879 -0.1086 -0.0784 -0.0324 138 PRO A CG  
1123 C  CD  . PRO A 137 ? 0.3014 0.3061 0.1463 -0.0663 -0.0697 -0.0615 138 PRO A CD  
1124 N  N   . ASP A 138 ? 0.1800 0.2156 0.1223 0.0036  0.0057  -0.0181 139 ASP A N   
1125 C  CA  . ASP A 138 ? 0.1754 0.2409 0.1241 0.0059  0.0198  -0.0024 139 ASP A CA  
1126 C  C   . ASP A 138 ? 0.1693 0.1567 0.1201 -0.0068 0.0189  -0.0167 139 ASP A C   
1127 O  O   . ASP A 138 ? 0.1682 0.1926 0.1459 0.0032  0.0050  -0.0099 139 ASP A O   
1128 C  CB  . ASP A 138 ? 0.1861 0.2655 0.1309 0.0142  0.0348  0.0019  139 ASP A CB  
1129 C  CG  . ASP A 138 ? 0.2579 0.2842 0.1357 0.0157  0.0372  -0.0611 139 ASP A CG  
1130 O  OD1 . ASP A 138 ? 0.2296 0.2453 0.2037 0.0241  0.0032  -0.0473 139 ASP A OD1 
1131 O  OD2 . ASP A 138 ? 0.3082 0.3194 0.2054 0.0643  0.0587  -0.0748 139 ASP A OD2 
1132 N  N   . GLY A 139 ? 0.1632 0.1423 0.1185 -0.0174 0.0158  -0.0130 140 GLY A N   
1133 C  CA  . GLY A 139 ? 0.1678 0.1302 0.1197 -0.0089 -0.0069 -0.0001 140 GLY A CA  
1134 C  C   . GLY A 139 ? 0.1472 0.1288 0.1018 -0.0139 0.0110  0.0033  140 GLY A C   
1135 O  O   . GLY A 139 ? 0.1477 0.1208 0.1344 0.0038  0.0006  -0.0019 140 GLY A O   
1136 N  N   . LEU A 140 ? 0.1181 0.1165 0.1330 -0.0095 0.0203  -0.0170 141 LEU A N   
1137 C  CA  . LEU A 140 ? 0.1295 0.1091 0.1229 -0.0111 0.0286  -0.0170 141 LEU A CA  
1138 C  C   . LEU A 140 ? 0.1007 0.1137 0.1244 0.0006  0.0131  -0.0129 141 LEU A C   
1139 O  O   . LEU A 140 ? 0.1319 0.1315 0.1205 -0.0131 0.0067  -0.0113 141 LEU A O   
1140 C  CB  . LEU A 140 ? 0.1125 0.1524 0.1430 0.0130  0.0288  -0.0073 141 LEU A CB  
1141 C  CG  . LEU A 140 ? 0.1462 0.1675 0.1857 0.0373  0.0524  0.0168  141 LEU A CG  
1142 C  CD1 . LEU A 140 ? 0.1594 0.2048 0.1599 0.0436  0.0525  0.0042  141 LEU A CD1 
1143 C  CD2 . LEU A 140 ? 0.1800 0.1732 0.1513 0.0080  0.0173  0.0194  141 LEU A CD2 
1144 N  N   . ALA A 141 ? 0.1104 0.1230 0.1362 -0.0168 0.0017  -0.0137 142 ALA A N   
1145 C  CA  . ALA A 141 ? 0.1018 0.1247 0.1305 -0.0185 0.0075  -0.0055 142 ALA A CA  
1146 C  C   . ALA A 141 ? 0.0777 0.1408 0.1192 0.0015  0.0132  0.0000  142 ALA A C   
1147 O  O   . ALA A 141 ? 0.1470 0.1221 0.1208 -0.0089 -0.0066 0.0072  142 ALA A O   
1148 C  CB  . ALA A 141 ? 0.1156 0.1603 0.1835 -0.0035 0.0442  0.0074  142 ALA A CB  
1149 N  N   . VAL A 142 ? 0.0906 0.1276 0.1280 -0.0006 0.0038  -0.0044 143 VAL A N   
1150 C  CA  . VAL A 142 ? 0.1011 0.1224 0.1235 -0.0078 0.0040  -0.0048 143 VAL A CA  
1151 C  C   . VAL A 142 ? 0.1067 0.1291 0.0987 0.0002  0.0110  0.0204  143 VAL A C   
1152 O  O   . VAL A 142 ? 0.1224 0.1289 0.1030 0.0011  0.0016  0.0162  143 VAL A O   
1153 C  CB  . VAL A 142 ? 0.0881 0.1366 0.1257 -0.0012 0.0050  -0.0110 143 VAL A CB  
1154 C  CG1 . VAL A 142 ? 0.1108 0.1492 0.1282 0.0068  0.0072  -0.0280 143 VAL A CG1 
1155 C  CG2 . VAL A 142 ? 0.0989 0.1887 0.1091 -0.0273 0.0131  0.0118  143 VAL A CG2 
1156 N  N   . LEU A 143 ? 0.0974 0.1237 0.1296 -0.0063 -0.0022 0.0048  144 LEU A N   
1157 C  CA  . LEU A 143 ? 0.1044 0.1355 0.1260 -0.0127 0.0038  0.0074  144 LEU A CA  
1158 C  C   . LEU A 143 ? 0.1077 0.1506 0.0989 -0.0253 -0.0086 -0.0035 144 LEU A C   
1159 O  O   . LEU A 143 ? 0.1275 0.1384 0.1217 -0.0153 0.0076  0.0088  144 LEU A O   
1160 C  CB  . LEU A 143 ? 0.1217 0.1867 0.1644 -0.0077 -0.0177 0.0253  144 LEU A CB  
1161 C  CG  . LEU A 143 ? 0.1158 0.2170 0.1681 -0.0170 -0.0175 0.0265  144 LEU A CG  
1162 C  CD1 . LEU A 143 ? 0.1355 0.2201 0.1908 -0.0231 0.0083  0.0339  144 LEU A CD1 
1163 C  CD2 . LEU A 143 ? 0.0989 0.2427 0.2379 0.0042  -0.0057 0.0160  144 LEU A CD2 
1164 N  N   . GLY A 144 ? 0.1034 0.1253 0.1172 -0.0066 -0.0027 -0.0008 145 GLY A N   
1165 C  CA  . GLY A 144 ? 0.1014 0.1170 0.1419 -0.0245 0.0100  -0.0075 145 GLY A CA  
1166 C  C   . GLY A 144 ? 0.0987 0.1262 0.1132 -0.0181 0.0069  0.0156  145 GLY A C   
1167 O  O   . GLY A 144 ? 0.1307 0.1386 0.1160 -0.0240 0.0186  0.0073  145 GLY A O   
1168 N  N   . ILE A 145 ? 0.0925 0.1102 0.1341 -0.0004 -0.0084 0.0013  146 ILE A N   
1169 C  CA  . ILE A 145 ? 0.0882 0.1143 0.1364 -0.0075 -0.0099 -0.0008 146 ILE A CA  
1170 C  C   . ILE A 145 ? 0.1159 0.1140 0.1296 -0.0110 0.0058  -0.0003 146 ILE A C   
1171 O  O   . ILE A 145 ? 0.1180 0.1234 0.1339 -0.0148 0.0183  -0.0030 146 ILE A O   
1172 C  CB  . ILE A 145 ? 0.1210 0.1289 0.1317 -0.0016 -0.0161 0.0198  146 ILE A CB  
1173 C  CG1 . ILE A 145 ? 0.1515 0.1578 0.1777 0.0347  -0.0231 0.0002  146 ILE A CG1 
1174 C  CG2 . ILE A 145 ? 0.0985 0.1843 0.2154 -0.0134 -0.0394 -0.0024 146 ILE A CG2 
1175 C  CD1 . ILE A 145 ? 0.1430 0.1603 0.2005 0.0032  -0.0487 -0.0016 146 ILE A CD1 
1176 N  N   . PHE A 146 ? 0.1167 0.1086 0.1221 -0.0005 0.0009  0.0008  147 PHE A N   
1177 C  CA  . PHE A 146 ? 0.1325 0.1185 0.1041 0.0133  -0.0040 0.0004  147 PHE A CA  
1178 C  C   . PHE A 146 ? 0.1127 0.1303 0.1256 0.0033  -0.0140 -0.0024 147 PHE A C   
1179 O  O   . PHE A 146 ? 0.1029 0.1372 0.1552 -0.0054 -0.0024 -0.0190 147 PHE A O   
1180 C  CB  . PHE A 146 ? 0.1380 0.1322 0.1319 -0.0245 -0.0226 0.0284  147 PHE A CB  
1181 C  CG  . PHE A 146 ? 0.1025 0.1084 0.1341 -0.0022 -0.0082 0.0011  147 PHE A CG  
1182 C  CD1 . PHE A 146 ? 0.0979 0.1104 0.1574 0.0110  -0.0065 -0.0058 147 PHE A CD1 
1183 C  CD2 . PHE A 146 ? 0.1412 0.1369 0.1190 -0.0086 -0.0016 0.0212  147 PHE A CD2 
1184 C  CE1 . PHE A 146 ? 0.1234 0.1419 0.1408 -0.0032 -0.0033 -0.0247 147 PHE A CE1 
1185 C  CE2 . PHE A 146 ? 0.1224 0.1307 0.1337 -0.0039 -0.0027 0.0094  147 PHE A CE2 
1186 C  CZ  . PHE A 146 ? 0.1183 0.1448 0.1437 -0.0021 0.0192  0.0145  147 PHE A CZ  
1187 N  N   . LEU A 147 ? 0.1293 0.1284 0.1311 -0.0027 0.0079  -0.0168 148 LEU A N   
1188 C  CA  . LEU A 147 ? 0.1216 0.1326 0.1318 -0.0293 -0.0139 0.0021  148 LEU A CA  
1189 C  C   . LEU A 147 ? 0.1275 0.1491 0.1282 -0.0236 -0.0096 -0.0073 148 LEU A C   
1190 O  O   . LEU A 147 ? 0.1368 0.1477 0.1711 -0.0135 -0.0026 -0.0080 148 LEU A O   
1191 C  CB  . LEU A 147 ? 0.1594 0.1296 0.1276 -0.0084 0.0058  0.0005  148 LEU A CB  
1192 C  CG  . LEU A 147 ? 0.1364 0.1323 0.1383 -0.0217 -0.0077 -0.0115 148 LEU A CG  
1193 C  CD1 . LEU A 147 ? 0.1724 0.1330 0.1520 -0.0129 0.0058  -0.0256 148 LEU A CD1 
1194 C  CD2 . LEU A 147 ? 0.1782 0.1958 0.1365 0.0084  -0.0032 -0.0070 148 LEU A CD2 
1195 N  N   . LYS A 148 ? 0.1450 0.1394 0.1548 -0.0273 -0.0217 -0.0228 149 LYS A N   
1196 C  CA  . LYS A 148 ? 0.1829 0.1319 0.1725 0.0067  -0.0230 -0.0159 149 LYS A CA  
1197 C  C   . LYS A 148 ? 0.1857 0.1409 0.1993 -0.0134 -0.0429 -0.0052 149 LYS A C   
1198 O  O   . LYS A 148 ? 0.2270 0.1680 0.2023 0.0364  -0.0728 -0.0290 149 LYS A O   
1199 C  CB  . LYS A 148 ? 0.2009 0.2766 0.1720 -0.0506 -0.0323 0.0111  149 LYS A CB  
1200 C  CG  . LYS A 148 ? 0.2109 0.2421 0.2529 -0.0052 0.0219  0.0472  149 LYS A CG  
1201 C  CD  . LYS A 148 ? 0.3707 0.3092 0.2835 -0.0905 0.0435  0.0396  149 LYS A CD  
1202 C  CE  . LYS A 148 ? 0.3797 0.6384 0.4626 -0.1875 0.0107  0.1495  149 LYS A CE  
1203 N  NZ  . LYS A 148 ? 0.5040 0.6400 0.6760 -0.2297 0.1632  0.1787  149 LYS A NZ  
1204 N  N   . VAL A 149 ? 0.1991 0.1267 0.2086 -0.0065 -0.0454 -0.0057 150 VAL A N   
1205 C  CA  . VAL A 149 ? 0.1501 0.1821 0.2051 -0.0248 -0.0380 -0.0196 150 VAL A CA  
1206 C  C   . VAL A 149 ? 0.1857 0.1928 0.1724 -0.0363 -0.0352 -0.0024 150 VAL A C   
1207 O  O   . VAL A 149 ? 0.2346 0.2055 0.1987 -0.0207 -0.0394 0.0135  150 VAL A O   
1208 C  CB  . VAL A 149 ? 0.1720 0.1592 0.2386 -0.0135 -0.0243 -0.0185 150 VAL A CB  
1209 C  CG1 . VAL A 149 ? 0.2141 0.2095 0.2027 0.0066  -0.0585 -0.0053 150 VAL A CG1 
1210 C  CG2 . VAL A 149 ? 0.2206 0.2415 0.2339 -0.0474 0.0000  -0.0038 150 VAL A CG2 
1211 N  N   . GLY A 150 ? 0.1669 0.1605 0.2120 -0.0375 -0.0579 0.0041  151 GLY A N   
1212 C  CA  . GLY A 150 ? 0.1832 0.1868 0.2776 -0.0464 -0.0452 0.0491  151 GLY A CA  
1213 C  C   . GLY A 150 ? 0.1978 0.1626 0.2230 -0.0309 -0.0450 -0.0121 151 GLY A C   
1214 O  O   . GLY A 150 ? 0.1958 0.1797 0.2372 -0.0176 -0.0365 -0.0380 151 GLY A O   
1215 N  N   . SER A 151 ? 0.2163 0.1736 0.2644 -0.0172 -0.0354 0.0223  152 SER A N   
1216 C  CA  . SER A 151 ? 0.1976 0.1674 0.2623 -0.0082 -0.0617 0.0114  152 SER A CA  
1217 C  C   . SER A 151 ? 0.2323 0.1764 0.2281 -0.0389 -0.0585 -0.0093 152 SER A C   
1218 O  O   . SER A 151 ? 0.2278 0.1793 0.2213 -0.0185 -0.0636 -0.0240 152 SER A O   
1219 C  CB  . SER A 151 ? 0.0982 0.3966 0.4789 0.0002  -0.0439 0.1577  152 SER A CB  
1220 O  OG  . SER A 151 ? 0.3083 0.4504 0.5988 -0.0798 -0.0319 0.1043  152 SER A OG  
1221 N  N   . ALA A 152 ? 0.2012 0.1764 0.2191 -0.0139 -0.0335 0.0044  153 ALA A N   
1222 C  CA  . ALA A 152 ? 0.2198 0.1673 0.1865 -0.0168 -0.0534 -0.0122 153 ALA A CA  
1223 C  C   . ALA A 152 ? 0.2005 0.1753 0.1692 -0.0301 -0.0367 -0.0222 153 ALA A C   
1224 O  O   . ALA A 152 ? 0.2281 0.1946 0.2569 -0.0097 -0.0074 -0.0055 153 ALA A O   
1225 C  CB  . ALA A 152 ? 0.2834 0.2380 0.2001 0.0116  -0.0917 -0.0540 153 ALA A CB  
1226 N  N   . LYS A 153 ? 0.2318 0.1454 0.2445 -0.0294 -0.0907 -0.0080 154 LYS A N   
1227 C  CA  . LYS A 153 ? 0.2169 0.1743 0.1886 -0.0019 -0.0407 -0.0033 154 LYS A CA  
1228 C  C   . LYS A 153 ? 0.1813 0.1756 0.2210 -0.0089 -0.0604 0.0057  154 LYS A C   
1229 O  O   . LYS A 153 ? 0.2082 0.1804 0.2016 -0.0286 -0.0659 0.0114  154 LYS A O   
1230 C  CB  . LYS A 153 ? 0.2126 0.1741 0.2044 -0.0122 -0.0572 0.0121  154 LYS A CB  
1231 C  CG  . LYS A 153 ? 0.2459 0.1745 0.1930 -0.0109 -0.0707 0.0079  154 LYS A CG  
1232 C  CD  . LYS A 153 ? 0.3597 0.1858 0.1664 -0.0365 -0.0435 -0.0125 154 LYS A CD  
1233 C  CE  . LYS A 153 ? 0.3941 0.1955 0.1851 0.0076  -0.0930 -0.0157 154 LYS A CE  
1234 N  NZ  . LYS A 153 ? 0.3114 0.3207 0.2837 0.0318  -0.0336 0.0002  154 LYS A NZ  
1235 N  N   . PRO A 154 ? 0.1826 0.2134 0.2242 -0.0195 -0.0615 0.0053  155 PRO A N   
1236 C  CA  . PRO A 154 ? 0.1513 0.2525 0.2303 -0.0458 -0.0471 0.0355  155 PRO A CA  
1237 C  C   . PRO A 154 ? 0.1692 0.2384 0.2477 0.0075  -0.0842 0.0392  155 PRO A C   
1238 O  O   . PRO A 154 ? 0.2508 0.2957 0.2249 -0.0398 -0.0900 0.0603  155 PRO A O   
1239 C  CB  . PRO A 154 ? 0.1599 0.2873 0.3352 -0.0324 -0.0952 0.0493  155 PRO A CB  
1240 C  CG  . PRO A 154 ? 0.2644 0.4282 0.3294 -0.0447 -0.1011 0.1196  155 PRO A CG  
1241 C  CD  . PRO A 154 ? 0.2192 0.2095 0.2475 -0.0336 -0.0490 0.0450  155 PRO A CD  
1242 N  N   . GLY A 155 ? 0.1699 0.1869 0.3118 0.0095  -0.0782 -0.0116 156 GLY A N   
1243 C  CA  . GLY A 155 ? 0.1818 0.1986 0.3252 -0.0096 -0.0513 0.0384  156 GLY A CA  
1244 C  C   . GLY A 155 ? 0.2183 0.1761 0.2562 -0.0262 -0.0403 0.0173  156 GLY A C   
1245 O  O   . GLY A 155 ? 0.2493 0.1747 0.3708 -0.0223 -0.0584 0.0306  156 GLY A O   
1246 N  N   . LEU A 156 ? 0.1793 0.1753 0.2363 -0.0152 -0.0471 -0.0057 157 LEU A N   
1247 C  CA  . LEU A 156 ? 0.1845 0.1668 0.1951 -0.0156 -0.0616 -0.0121 157 LEU A CA  
1248 C  C   . LEU A 156 ? 0.1932 0.1797 0.1796 -0.0254 -0.0655 -0.0010 157 LEU A C   
1249 O  O   . LEU A 156 ? 0.1930 0.2016 0.1923 -0.0227 -0.0488 -0.0067 157 LEU A O   
1250 C  CB  . LEU A 156 ? 0.1777 0.1714 0.2210 -0.0367 -0.0666 0.0284  157 LEU A CB  
1251 C  CG  . LEU A 156 ? 0.1771 0.1808 0.1777 -0.0274 -0.0474 0.0096  157 LEU A CG  
1252 C  CD1 . LEU A 156 ? 0.1881 0.2217 0.1990 -0.0445 -0.0593 -0.0149 157 LEU A CD1 
1253 C  CD2 . LEU A 156 ? 0.2069 0.2093 0.1821 -0.0201 -0.0536 0.0208  157 LEU A CD2 
1254 N  N   . GLN A 157 ? 0.2093 0.1774 0.1941 -0.0420 -0.0648 0.0032  158 GLN A N   
1255 C  CA  . GLN A 157 ? 0.2264 0.2320 0.1806 -0.0603 -0.0608 -0.0280 158 GLN A CA  
1256 C  C   . GLN A 157 ? 0.2276 0.1994 0.2020 -0.0320 -0.0655 -0.0303 158 GLN A C   
1257 O  O   . GLN A 157 ? 0.2709 0.1936 0.1766 -0.0266 -0.0663 -0.0138 158 GLN A O   
1258 C  CB  . GLN A 157 ? 0.2658 0.2590 0.2125 -0.0925 -0.0756 -0.0197 158 GLN A CB  
1259 C  CG  . GLN A 157 ? 0.4074 0.2167 0.2233 -0.0293 -0.1047 -0.0186 158 GLN A CG  
1260 C  CD  . GLN A 157 ? 0.3953 0.1718 0.2023 -0.0544 -0.0916 0.0047  158 GLN A CD  
1261 O  OE1 . GLN A 157 ? 0.4304 0.1820 0.1875 -0.0298 -0.0717 0.0005  158 GLN A OE1 
1262 N  NE2 . GLN A 157 ? 0.4131 0.2326 0.1997 -0.0652 -0.0863 -0.0392 158 GLN A NE2 
1263 N  N   . LYS A 158 ? 0.2504 0.2113 0.2044 -0.0269 -0.0788 -0.0067 159 LYS A N   
1264 C  CA  . LYS A 158 ? 0.2420 0.2087 0.1955 -0.0136 -0.0758 0.0073  159 LYS A CA  
1265 C  C   . LYS A 158 ? 0.2552 0.2039 0.1763 -0.0240 -0.0482 0.0051  159 LYS A C   
1266 O  O   . LYS A 158 ? 0.2705 0.2082 0.1795 -0.0506 -0.0414 0.0132  159 LYS A O   
1267 C  CB  . LYS A 158 ? 0.2972 0.2205 0.3269 0.0488  -0.1526 0.0016  159 LYS A CB  
1268 C  CG  . LYS A 158 ? 0.5871 0.2899 0.4618 0.0398  -0.1650 0.0621  159 LYS A CG  
1269 C  CD  . LYS A 158 ? 0.6900 0.3556 0.5049 0.1432  -0.2286 0.0665  159 LYS A CD  
1270 C  CE  . LYS A 158 ? 0.9299 0.4039 0.4246 0.0601  -0.2876 0.1217  159 LYS A CE  
1271 N  NZ  . LYS A 158 ? 0.8855 0.4771 0.4601 0.0177  -0.2882 0.1645  159 LYS A NZ  
1272 N  N   . VAL A 159 ? 0.2126 0.1770 0.1804 -0.0175 -0.0647 -0.0020 160 VAL A N   
1273 C  CA  . VAL A 159 ? 0.2324 0.1806 0.1803 -0.0309 -0.0629 0.0020  160 VAL A CA  
1274 C  C   . VAL A 159 ? 0.2420 0.1839 0.1797 -0.0099 -0.0306 0.0280  160 VAL A C   
1275 O  O   . VAL A 159 ? 0.2344 0.1914 0.1969 -0.0201 -0.0567 0.0055  160 VAL A O   
1276 C  CB  . VAL A 159 ? 0.2391 0.1808 0.1793 -0.0140 -0.0677 0.0009  160 VAL A CB  
1277 C  CG1 . VAL A 159 ? 0.2174 0.2702 0.2061 -0.0712 -0.0579 0.0117  160 VAL A CG1 
1278 C  CG2 . VAL A 159 ? 0.3416 0.2378 0.1763 0.0299  -0.0748 -0.0575 160 VAL A CG2 
1279 N  N   . VAL A 160 ? 0.2694 0.1590 0.1839 -0.0241 -0.0761 0.0170  161 VAL A N   
1280 C  CA  . VAL A 160 ? 0.3255 0.1897 0.1645 0.0020  -0.0009 0.0175  161 VAL A CA  
1281 C  C   . VAL A 160 ? 0.2644 0.1983 0.1567 -0.0594 -0.0495 -0.0240 161 VAL A C   
1282 O  O   . VAL A 160 ? 0.3169 0.2088 0.1674 -0.0257 -0.0173 -0.0051 161 VAL A O   
1283 C  CB  . VAL A 160 ? 0.4740 0.1732 0.1721 0.0098  0.0331  0.0232  161 VAL A CB  
1284 C  CG1 . VAL A 160 ? 0.3636 0.2072 0.2181 -0.0620 -0.0586 -0.0017 161 VAL A CG1 
1285 C  CG2 . VAL A 160 ? 0.5912 0.2199 0.1678 0.0150  0.0185  -0.0220 161 VAL A CG2 
1286 N  N   . ASP A 161 ? 0.2993 0.2471 0.1718 -0.0759 -0.0655 -0.0004 162 ASP A N   
1287 C  CA  . ASP A 161 ? 0.3219 0.3276 0.1687 -0.1035 -0.0937 0.0046  162 ASP A CA  
1288 C  C   . ASP A 161 ? 0.3786 0.2938 0.1792 -0.0864 -0.0688 -0.0047 162 ASP A C   
1289 O  O   . ASP A 161 ? 0.5114 0.3711 0.2044 -0.1323 -0.0643 -0.0516 162 ASP A O   
1290 C  CB  . ASP A 161 ? 0.3462 0.4020 0.2242 -0.0889 -0.1052 -0.0108 162 ASP A CB  
1291 C  CG  . ASP A 161 ? 0.4177 0.4128 0.2064 -0.1216 -0.0403 -0.0994 162 ASP A CG  
1292 O  OD1 . ASP A 161 ? 0.5576 0.4974 0.4196 0.0000  0.0288  0.0225  162 ASP A OD1 
1293 O  OD2 . ASP A 161 ? 0.3845 0.5381 0.3966 -0.0133 -0.1192 -0.0339 162 ASP A OD2 
1294 N  N   . VAL A 162 ? 0.3498 0.2345 0.1725 -0.0724 -0.0699 0.0219  163 VAL A N   
1295 C  CA  . VAL A 162 ? 0.2988 0.2763 0.1986 -0.0618 -0.0735 0.0535  163 VAL A CA  
1296 C  C   . VAL A 162 ? 0.3021 0.2483 0.1477 -0.0389 -0.0239 0.0504  163 VAL A C   
1297 O  O   . VAL A 162 ? 0.3359 0.2823 0.1558 -0.0760 -0.0089 0.0302  163 VAL A O   
1298 C  CB  . VAL A 162 ? 0.3022 0.2590 0.3150 -0.0487 -0.0745 0.0658  163 VAL A CB  
1299 C  CG1 . VAL A 162 ? 0.3679 0.1754 0.3414 -0.0697 -0.0797 -0.0012 163 VAL A CG1 
1300 C  CG2 . VAL A 162 ? 0.2957 0.3258 0.2974 0.0129  0.0306  0.0864  163 VAL A CG2 
1301 N  N   . LEU A 163 ? 0.3384 0.2160 0.1668 -0.0451 -0.0680 0.0047  164 LEU A N   
1302 C  CA  . LEU A 163 ? 0.3179 0.2113 0.1225 -0.0199 0.0027  -0.0154 164 LEU A CA  
1303 C  C   . LEU A 163 ? 0.3643 0.2558 0.0991 -0.0259 0.0116  -0.0201 164 LEU A C   
1304 O  O   . LEU A 163 ? 0.3638 0.2345 0.1702 -0.0620 0.0428  -0.0013 164 LEU A O   
1305 C  CB  . LEU A 163 ? 0.2914 0.2041 0.1520 0.0055  0.0027  -0.0111 164 LEU A CB  
1306 C  CG  . LEU A 163 ? 0.2878 0.1944 0.1344 -0.0386 0.0032  0.0218  164 LEU A CG  
1307 C  CD1 . LEU A 163 ? 0.2702 0.2185 0.1987 0.0147  0.0189  0.0535  164 LEU A CD1 
1308 C  CD2 . LEU A 163 ? 0.2695 0.2341 0.1411 -0.0372 -0.0024 -0.0390 164 LEU A CD2 
1309 N  N   . ASP A 164 ? 0.4102 0.2346 0.1235 -0.0613 0.0135  -0.0243 165 ASP A N   
1310 C  CA  . ASP A 164 ? 0.4408 0.3103 0.1310 -0.1177 0.0529  -0.0298 165 ASP A CA  
1311 C  C   . ASP A 164 ? 0.4332 0.2749 0.1520 -0.0374 0.0357  -0.0165 165 ASP A C   
1312 O  O   . ASP A 164 ? 0.5550 0.3747 0.2168 -0.0796 0.1159  -0.0168 165 ASP A O   
1313 C  CB  . ASP A 164 ? 0.6609 0.4742 0.2073 -0.1170 -0.0156 -0.1759 165 ASP A CB  
1314 C  CG  . ASP A 164 ? 0.6042 0.4586 0.2300 -0.2676 0.0553  -0.0504 165 ASP A CG  
1315 O  OD1 . ASP A 164 ? 0.6720 0.6281 0.2459 -0.1272 0.0304  0.0069  165 ASP A OD1 
1316 O  OD2 . ASP A 164 ? 0.9176 0.8082 0.2119 -0.2663 0.1359  -0.0747 165 ASP A OD2 
1317 N  N   . SER A 165 ? 0.4008 0.2591 0.1190 -0.0479 -0.0305 -0.0042 166 SER A N   
1318 C  CA  . SER A 165 ? 0.4279 0.3072 0.1233 -0.0851 -0.0290 0.0091  166 SER A CA  
1319 C  C   . SER A 165 ? 0.3911 0.2196 0.1357 -0.0330 -0.0216 0.0146  166 SER A C   
1320 O  O   . SER A 165 ? 0.4422 0.2511 0.1666 -0.0419 0.0143  0.0440  166 SER A O   
1321 C  CB  . SER A 165 ? 0.5550 0.3358 0.1750 -0.0285 0.0359  0.0741  166 SER A CB  
1322 O  OG  . SER A 165 ? 0.5062 0.2868 0.2251 0.0067  0.0027  0.0403  166 SER A OG  
1323 N  N   . ILE A 166 ? 0.3837 0.2204 0.1226 -0.0374 -0.0584 0.0001  167 ILE A N   
1324 C  CA  . ILE A 166 ? 0.2737 0.2152 0.1337 -0.0353 0.0247  0.0006  167 ILE A CA  
1325 C  C   . ILE A 166 ? 0.2321 0.2167 0.1400 -0.0188 0.0317  -0.0308 167 ILE A C   
1326 O  O   . ILE A 166 ? 0.2713 0.2249 0.1423 -0.0279 0.0155  -0.0039 167 ILE A O   
1327 C  CB  . ILE A 166 ? 0.2985 0.2203 0.1241 -0.0319 0.0212  -0.0051 167 ILE A CB  
1328 C  CG1 . ILE A 166 ? 0.2690 0.2490 0.1104 -0.0712 0.0250  -0.0148 167 ILE A CG1 
1329 C  CG2 . ILE A 166 ? 0.3367 0.1964 0.1883 -0.0285 -0.0321 -0.0015 167 ILE A CG2 
1330 C  CD1 . ILE A 166 ? 0.2812 0.2326 0.1452 -0.0597 0.0385  -0.0469 167 ILE A CD1 
1331 N  N   . LYS A 167 ? 0.3287 0.2034 0.1387 -0.0140 0.0480  -0.0074 168 LYS A N   
1332 C  CA  . LYS A 167 ? 0.2389 0.2034 0.1591 -0.0165 0.0148  -0.0221 168 LYS A CA  
1333 C  C   . LYS A 167 ? 0.2760 0.2613 0.1270 -0.0485 0.0495  -0.0104 168 LYS A C   
1334 O  O   . LYS A 167 ? 0.2885 0.2305 0.1520 -0.0392 0.0317  -0.0037 168 LYS A O   
1335 C  CB  . LYS A 167 ? 0.3457 0.2442 0.1627 -0.0325 -0.0032 -0.0570 168 LYS A CB  
1336 C  CG  . LYS A 167 ? 0.3277 0.2658 0.1606 -0.0210 -0.0084 -0.0402 168 LYS A CG  
1337 C  CD  . LYS A 167 ? 0.3800 0.3158 0.2602 0.0346  -0.0156 -0.1061 168 LYS A CD  
1338 C  CE  . LYS A 167 ? 0.4547 0.3111 0.3940 0.0359  -0.0121 -0.0557 168 LYS A CE  
1339 N  NZ  . LYS A 167 ? 0.5329 0.6675 0.4482 0.0584  0.0069  -0.2153 168 LYS A NZ  
1340 N  N   . THR A 168 ? 0.2722 0.2724 0.1266 -0.0621 0.0461  0.0044  169 THR A N   
1341 C  CA  . THR A 168 ? 0.2615 0.2454 0.1459 -0.0735 0.0444  -0.0177 169 THR A CA  
1342 C  C   . THR A 168 ? 0.2318 0.1926 0.1228 -0.0030 0.0316  0.0175  169 THR A C   
1343 O  O   . THR A 168 ? 0.2726 0.2222 0.1781 -0.0147 0.0440  0.0212  169 THR A O   
1344 C  CB  . THR A 168 ? 0.3021 0.2495 0.1377 -0.0325 0.0358  0.0185  169 THR A CB  
1345 O  OG1 . THR A 168 ? 0.2806 0.2798 0.1423 -0.0065 0.0491  0.0181  169 THR A OG1 
1346 C  CG2 . THR A 168 ? 0.3477 0.2861 0.1681 -0.0282 0.1018  -0.0670 169 THR A CG2 
1347 N  N   . LYS A 169 ? 0.2712 0.2698 0.1407 -0.0820 0.0373  0.0015  170 LYS A N   
1348 C  CA  . LYS A 169 ? 0.2518 0.2026 0.1404 -0.0527 0.0004  0.0059  170 LYS A CA  
1349 C  C   . LYS A 169 ? 0.1705 0.2127 0.2011 -0.0618 0.0498  0.0462  170 LYS A C   
1350 O  O   . LYS A 169 ? 0.3732 0.3035 0.1650 -0.1170 0.0650  0.0342  170 LYS A O   
1351 C  CB  . LYS A 169 ? 0.2388 0.2490 0.1699 -0.0189 0.0409  -0.0192 170 LYS A CB  
1352 C  CG  . LYS A 169 ? 0.2143 0.3184 0.1973 -0.0775 0.0523  -0.0447 170 LYS A CG  
1353 C  CD  . LYS A 169 ? 0.2674 0.3575 0.2472 -0.0868 0.0341  -0.0378 170 LYS A CD  
1354 C  CE  . LYS A 169 ? 0.4037 0.5319 0.6978 -0.1877 -0.2069 -0.0876 170 LYS A CE  
1355 N  NZ  . LYS A 169 ? 0.4325 0.6825 0.6663 0.0614  -0.0934 -0.0233 170 LYS A NZ  
1356 N  N   . GLY A 170 ? 0.2733 0.2252 0.1768 -0.0435 0.0099  0.0250  171 GLY A N   
1357 C  CA  . GLY A 170 ? 0.2760 0.2389 0.2856 -0.0697 0.0088  0.0823  171 GLY A CA  
1358 C  C   . GLY A 170 ? 0.3273 0.1693 0.2285 -0.0036 0.0063  0.0424  171 GLY A C   
1359 O  O   . GLY A 170 ? 0.3694 0.1840 0.3305 -0.0255 -0.0017 0.0710  171 GLY A O   
1360 N  N   . LYS A 171 ? 0.2835 0.2066 0.1742 -0.0594 0.0432  0.0277  172 LYS A N   
1361 C  CA  . LYS A 171 ? 0.3037 0.2705 0.1678 -0.0502 0.0217  0.0356  172 LYS A CA  
1362 C  C   . LYS A 171 ? 0.2759 0.1993 0.1377 -0.0204 -0.0030 0.0225  172 LYS A C   
1363 O  O   . LYS A 171 ? 0.3187 0.2240 0.1448 -0.0142 0.0428  0.0308  172 LYS A O   
1364 C  CB  . LYS A 171 ? 0.2770 0.2512 0.1811 -0.0447 0.0178  0.0170  172 LYS A CB  
1365 C  CG  . LYS A 171 ? 0.2629 0.3078 0.3134 0.0153  0.0284  -0.0708 172 LYS A CG  
1366 C  CD  . LYS A 171 ? 0.4063 0.3391 0.3212 0.0061  0.0017  -0.0655 172 LYS A CD  
1367 C  CE  . LYS A 171 ? 0.6733 0.6497 0.2949 0.1331  0.0561  -0.0486 172 LYS A CE  
1368 N  NZ  . LYS A 171 ? 0.7046 0.8667 0.4871 0.0048  -0.3278 0.0587  172 LYS A NZ  
1369 N  N   . SER A 172 ? 0.3201 0.2158 0.1678 -0.0298 -0.0013 0.0386  173 SER A N   
1370 C  CA  . SER A 172 ? 0.3582 0.2593 0.1544 -0.0493 0.0345  0.0230  173 SER A CA  
1371 C  C   . SER A 172 ? 0.3323 0.2199 0.1357 0.0328  0.0322  0.0039  173 SER A C   
1372 O  O   . SER A 172 ? 0.3744 0.3430 0.1333 0.0491  0.0206  0.0447  173 SER A O   
1373 C  CB  . SER A 172 ? 0.3220 0.2573 0.1533 -0.0493 -0.0066 0.0370  173 SER A CB  
1374 O  OG  . SER A 172 ? 0.4834 0.2554 0.2041 -0.0145 -0.0199 0.0612  173 SER A OG  
1375 N  N   . ALA A 173 ? 0.3261 0.2713 0.1452 0.0696  -0.0042 0.0262  174 ALA A N   
1376 C  CA  . ALA A 173 ? 0.3261 0.2940 0.1491 0.1131  -0.0194 0.0719  174 ALA A CA  
1377 C  C   . ALA A 173 ? 0.2857 0.2956 0.1576 0.0621  -0.0516 -0.0008 174 ALA A C   
1378 O  O   . ALA A 173 ? 0.2899 0.2561 0.1391 0.0530  -0.0425 0.0132  174 ALA A O   
1379 C  CB  . ALA A 173 ? 0.4922 0.3158 0.2073 0.1225  -0.0030 -0.0128 174 ALA A CB  
1380 N  N   . ASP A 174 ? 0.2914 0.3786 0.2033 0.0501  -0.0623 0.0646  175 ASP A N   
1381 C  CA  . ASP A 174 ? 0.3380 0.3797 0.2080 0.0469  -0.0580 0.0739  175 ASP A CA  
1382 C  C   . ASP A 174 ? 0.2888 0.3086 0.2474 0.1169  0.0057  0.0222  175 ASP A C   
1383 O  O   . ASP A 174 ? 0.4641 0.3140 0.1957 0.0963  -0.0805 0.0015  175 ASP A O   
1384 C  CB  . ASP A 174 ? 0.4095 0.4255 0.2885 0.1288  -0.0618 0.1077  175 ASP A CB  
1385 C  CG  . ASP A 174 ? 0.6541 0.4687 0.4270 -0.0132 -0.2287 0.1776  175 ASP A CG  
1386 O  OD1 . ASP A 174 ? 0.5074 0.8186 0.3701 -0.0838 -0.1354 0.0418  175 ASP A OD1 
1387 O  OD2 . ASP A 174 ? 1.0146 0.7124 0.4123 -0.0672 -0.1912 0.3051  175 ASP A OD2 
1388 N  N   . PHE A 175 ? 0.2620 0.2496 0.1790 0.0137  -0.0115 0.0298  176 PHE A N   
1389 C  CA  . PHE A 175 ? 0.2932 0.2257 0.1560 0.0048  -0.0498 0.0375  176 PHE A CA  
1390 C  C   . PHE A 175 ? 0.3412 0.2486 0.1897 0.0254  -0.0753 0.0006  176 PHE A C   
1391 O  O   . PHE A 175 ? 0.3747 0.2637 0.2039 0.0730  -0.1158 -0.0229 176 PHE A O   
1392 C  CB  . PHE A 175 ? 0.3908 0.1684 0.1933 0.0134  -0.0820 0.0267  176 PHE A CB  
1393 C  CG  . PHE A 175 ? 0.3308 0.1833 0.1836 0.0168  -0.0873 0.0154  176 PHE A CG  
1394 C  CD1 . PHE A 175 ? 0.3611 0.1854 0.2262 -0.0161 -0.0651 0.0111  176 PHE A CD1 
1395 C  CD2 . PHE A 175 ? 0.2645 0.2138 0.2055 -0.0008 -0.0760 0.0289  176 PHE A CD2 
1396 C  CE1 . PHE A 175 ? 0.3441 0.2001 0.2113 -0.0141 -0.0688 0.0346  176 PHE A CE1 
1397 C  CE2 . PHE A 175 ? 0.3021 0.2129 0.2310 0.0053  -0.0661 0.0294  176 PHE A CE2 
1398 C  CZ  . PHE A 175 ? 0.3395 0.2037 0.2047 0.0151  -0.0637 0.0199  176 PHE A CZ  
1399 N  N   . THR A 176 ? 0.3980 0.2098 0.2091 0.0121  -0.1298 0.0406  177 THR A N   
1400 C  CA  . THR A 176 ? 0.3305 0.2015 0.2554 -0.0066 -0.1122 0.0642  177 THR A CA  
1401 C  C   . THR A 176 ? 0.2579 0.1662 0.1684 0.0164  -0.0853 0.0143  177 THR A C   
1402 O  O   . THR A 176 ? 0.3463 0.1724 0.1797 -0.0019 -0.1110 0.0139  177 THR A O   
1403 C  CB  . THR A 176 ? 0.3410 0.2346 0.2366 0.0058  -0.1377 0.0535  177 THR A CB  
1404 O  OG1 . THR A 176 ? 0.4523 0.2784 0.1829 0.0609  -0.0879 0.0325  177 THR A OG1 
1405 C  CG2 . THR A 176 ? 0.3683 0.3268 0.4497 -0.0051 -0.0688 0.1799  177 THR A CG2 
1406 N  N   . ASN A 177 ? 0.2938 0.2143 0.1470 0.0230  -0.0570 0.0167  178 ASN A N   
1407 C  CA  . ASN A 177 ? 0.2799 0.2228 0.1826 0.0378  -0.0510 0.0403  178 ASN A CA  
1408 C  C   . ASN A 177 ? 0.2824 0.2180 0.1905 0.0174  -0.0722 0.0419  178 ASN A C   
1409 O  O   . ASN A 177 ? 0.3159 0.2590 0.3374 -0.0381 -0.1293 0.1268  178 ASN A O   
1410 C  CB  . ASN A 177 ? 0.3069 0.2159 0.2310 -0.0099 -0.0961 0.0770  178 ASN A CB  
1411 C  CG  . ASN A 177 ? 0.3122 0.2079 0.1914 0.0263  -0.0776 0.0411  178 ASN A CG  
1412 O  OD1 . ASN A 177 ? 0.3647 0.2917 0.2788 0.0895  -0.0203 0.0443  178 ASN A OD1 
1413 N  ND2 . ASN A 177 ? 0.3312 0.2587 0.1815 0.0245  -0.0794 0.0677  178 ASN A ND2 
1414 N  N   . PHE A 178 ? 0.2950 0.1667 0.1497 -0.0048 -0.0743 0.0328  179 PHE A N   
1415 C  CA  . PHE A 178 ? 0.2970 0.1804 0.1590 -0.0192 -0.0866 0.0444  179 PHE A CA  
1416 C  C   . PHE A 178 ? 0.2860 0.1793 0.1459 -0.0085 -0.0839 0.0374  179 PHE A C   
1417 O  O   . PHE A 178 ? 0.3148 0.1972 0.1707 -0.0205 -0.0686 0.0194  179 PHE A O   
1418 C  CB  . PHE A 178 ? 0.2853 0.2291 0.1738 -0.0105 -0.0812 0.0659  179 PHE A CB  
1419 C  CG  . PHE A 178 ? 0.2443 0.1912 0.1829 -0.0216 -0.0780 0.0493  179 PHE A CG  
1420 C  CD1 . PHE A 178 ? 0.2834 0.1876 0.2115 -0.0164 -0.0901 0.0388  179 PHE A CD1 
1421 C  CD2 . PHE A 178 ? 0.2137 0.1930 0.1735 0.0170  -0.0597 0.0408  179 PHE A CD2 
1422 C  CE1 . PHE A 178 ? 0.3421 0.1951 0.2227 -0.0136 -0.1068 0.0493  179 PHE A CE1 
1423 C  CE2 . PHE A 178 ? 0.1666 0.1858 0.1987 0.0140  -0.0595 0.0429  179 PHE A CE2 
1424 C  CZ  . PHE A 178 ? 0.2341 0.2188 0.1810 -0.0267 -0.0586 0.0380  179 PHE A CZ  
1425 N  N   . ASP A 179 ? 0.2495 0.2104 0.1944 0.0022  -0.0723 0.0305  180 ASP A N   
1426 C  CA  . ASP A 179 ? 0.1946 0.2269 0.2094 -0.0107 -0.0765 0.0409  180 ASP A CA  
1427 C  C   . ASP A 179 ? 0.2064 0.2127 0.2081 -0.0203 -0.0592 0.0539  180 ASP A C   
1428 O  O   . ASP A 179 ? 0.2188 0.2023 0.2296 -0.0221 -0.0618 0.0158  180 ASP A O   
1429 C  CB  . ASP A 179 ? 0.1940 0.2495 0.2652 -0.0060 -0.1094 0.0352  180 ASP A CB  
1430 C  CG  . ASP A 179 ? 0.2192 0.3316 0.3262 0.0058  -0.0394 0.0664  180 ASP A CG  
1431 O  OD1 . ASP A 179 ? 0.2045 0.2551 0.2982 0.0256  -0.0478 0.0390  180 ASP A OD1 
1432 O  OD2 . ASP A 179 ? 0.2016 0.4935 0.3948 -0.0082 -0.0375 -0.0590 180 ASP A OD2 
1433 N  N   . PRO A 180 ? 0.1961 0.1833 0.2072 -0.0157 -0.0513 0.0340  181 PRO A N   
1434 C  CA  . PRO A 180 ? 0.1408 0.2345 0.1883 -0.0255 -0.0394 0.0474  181 PRO A CA  
1435 C  C   . PRO A 180 ? 0.1580 0.1720 0.1998 -0.0004 -0.0278 0.0333  181 PRO A C   
1436 O  O   . PRO A 180 ? 0.1942 0.1756 0.1899 -0.0009 -0.0517 0.0273  181 PRO A O   
1437 C  CB  . PRO A 180 ? 0.1950 0.2147 0.2415 -0.0100 -0.0451 0.0073  181 PRO A CB  
1438 C  CG  . PRO A 180 ? 0.1987 0.2244 0.2257 -0.0178 -0.0502 0.0433  181 PRO A CG  
1439 C  CD  . PRO A 180 ? 0.2285 0.1835 0.2288 -0.0422 -0.0803 0.0234  181 PRO A CD  
1440 N  N   . ARG A 181 ? 0.1631 0.1968 0.1955 -0.0036 -0.0287 0.0132  182 ARG A N   
1441 C  CA  . ARG A 181 ? 0.1570 0.2242 0.2109 -0.0050 -0.0154 0.0055  182 ARG A CA  
1442 C  C   . ARG A 181 ? 0.1599 0.2122 0.2127 0.0113  -0.0684 0.0242  182 ARG A C   
1443 O  O   . ARG A 181 ? 0.1732 0.2395 0.2477 -0.0064 -0.0587 0.0352  182 ARG A O   
1444 C  CB  . ARG A 181 ? 0.1659 0.2219 0.2561 0.0137  -0.0381 0.0306  182 ARG A CB  
1445 C  CG  . ARG A 181 ? 0.1989 0.2125 0.3010 0.0243  -0.0443 0.0240  182 ARG A CG  
1446 C  CD  . ARG A 181 ? 0.1894 0.2536 0.3414 0.0292  -0.0250 0.0317  182 ARG A CD  
1447 N  NE  . ARG A 181 ? 0.1968 0.2231 0.3826 0.0339  -0.0166 0.0861  182 ARG A NE  
1448 C  CZ  . ARG A 181 ? 0.2037 0.2436 0.3783 0.0276  -0.0352 0.0861  182 ARG A CZ  
1449 N  NH1 . ARG A 181 ? 0.2053 0.4439 0.4357 0.0344  0.0581  0.1105  182 ARG A NH1 
1450 N  NH2 . ARG A 181 ? 0.2605 0.3427 0.4124 0.0413  -0.0442 0.1432  182 ARG A NH2 
1451 N  N   . GLY A 182 ? 0.1653 0.1680 0.2278 0.0002  -0.0533 0.0147  183 GLY A N   
1452 C  CA  . GLY A 182 ? 0.2119 0.1806 0.2643 0.0125  -0.0971 0.0093  183 GLY A CA  
1453 C  C   . GLY A 182 ? 0.1689 0.2015 0.2784 0.0196  -0.0655 -0.0147 183 GLY A C   
1454 O  O   . GLY A 182 ? 0.2634 0.1973 0.2824 -0.0020 -0.1048 -0.0104 183 GLY A O   
1455 N  N   . LEU A 183 ? 0.1742 0.2156 0.2120 0.0033  -0.0816 0.0233  184 LEU A N   
1456 C  CA  . LEU A 183 ? 0.1614 0.2019 0.1915 -0.0040 -0.0636 0.0217  184 LEU A CA  
1457 C  C   . LEU A 183 ? 0.1499 0.2075 0.1872 0.0034  -0.0677 0.0150  184 LEU A C   
1458 O  O   . LEU A 183 ? 0.1646 0.2221 0.2199 0.0145  -0.0471 0.0634  184 LEU A O   
1459 C  CB  . LEU A 183 ? 0.1409 0.2206 0.2057 0.0155  -0.0477 0.0510  184 LEU A CB  
1460 C  CG  . LEU A 183 ? 0.1976 0.2486 0.1868 0.0301  -0.0333 0.0550  184 LEU A CG  
1461 C  CD1 . LEU A 183 ? 0.2037 0.3100 0.1893 0.0136  -0.0453 0.0807  184 LEU A CD1 
1462 C  CD2 . LEU A 183 ? 0.2220 0.2970 0.2756 0.0406  -0.0227 -0.0047 184 LEU A CD2 
1463 N  N   . LEU A 184 ? 0.1551 0.1881 0.2234 -0.0210 -0.0192 0.0403  185 LEU A N   
1464 C  CA  . LEU A 184 ? 0.1398 0.1825 0.2077 -0.0215 -0.0353 0.0249  185 LEU A CA  
1465 C  C   . LEU A 184 ? 0.1943 0.1793 0.2745 -0.0445 -0.0976 0.0508  185 LEU A C   
1466 O  O   . LEU A 184 ? 0.2612 0.2551 0.3310 -0.1173 -0.1676 0.1078  185 LEU A O   
1467 C  CB  . LEU A 184 ? 0.1481 0.1987 0.2249 -0.0071 -0.0027 0.0119  185 LEU A CB  
1468 C  CG  . LEU A 184 ? 0.1379 0.2150 0.2353 -0.0162 -0.0159 -0.0030 185 LEU A CG  
1469 C  CD1 . LEU A 184 ? 0.2108 0.2521 0.2759 0.0228  -0.0228 0.0066  185 LEU A CD1 
1470 C  CD2 . LEU A 184 ? 0.1426 0.2300 0.3665 0.0064  -0.0599 -0.0233 185 LEU A CD2 
1471 N  N   . PRO A 185 ? 0.1162 0.1878 0.2235 -0.0089 -0.0422 0.0272  186 PRO A N   
1472 C  CA  . PRO A 185 ? 0.1427 0.1571 0.2558 0.0079  -0.0305 0.0337  186 PRO A CA  
1473 C  C   . PRO A 185 ? 0.1159 0.1685 0.2974 -0.0089 -0.0428 0.0353  186 PRO A C   
1474 O  O   . PRO A 185 ? 0.1235 0.1761 0.3923 -0.0058 -0.0307 0.0529  186 PRO A O   
1475 C  CB  . PRO A 185 ? 0.1183 0.1684 0.2467 0.0038  -0.0137 0.0205  186 PRO A CB  
1476 C  CG  . PRO A 185 ? 0.1333 0.1596 0.1984 0.0206  -0.0009 0.0163  186 PRO A CG  
1477 C  CD  . PRO A 185 ? 0.1009 0.1867 0.1833 -0.0052 -0.0244 0.0326  186 PRO A CD  
1478 N  N   . GLU A 186 ? 0.1201 0.2231 0.3177 -0.0354 -0.0402 0.0442  187 GLU A N   
1479 C  CA  . GLU A 186 ? 0.1310 0.2471 0.3312 -0.0405 -0.0177 0.0137  187 GLU A CA  
1480 C  C   . GLU A 186 ? 0.0736 0.2364 0.3031 0.0037  0.0115  0.0285  187 GLU A C   
1481 O  O   . GLU A 186 ? 0.1143 0.2737 0.3868 0.0428  -0.0192 0.0042  187 GLU A O   
1482 C  CB  . GLU A 186 ? 0.2492 0.2924 0.4306 -0.0944 0.0312  0.0307  187 GLU A CB  
1483 C  CG  . GLU A 186 ? 0.3230 0.3455 0.8187 -0.1033 -0.0469 0.0859  187 GLU A CG  
1484 C  CD  . GLU A 186 ? 0.1315 0.3241 0.7479 -0.0199 0.0330  0.1252  187 GLU A CD  
1485 O  OE1 . GLU A 186 ? 0.4568 0.3161 1.0627 -0.0223 0.1066  -0.0358 187 GLU A OE1 
1486 O  OE2 . GLU A 186 ? 0.5290 0.5906 0.8553 -0.2435 -0.2868 0.4077  187 GLU A OE2 
1487 N  N   . SER A 187 ? 0.1104 0.2414 0.2637 -0.0253 -0.0263 0.0192  188 SER A N   
1488 C  CA  . SER A 187 ? 0.1065 0.2299 0.2709 -0.0171 -0.0050 0.0216  188 SER A CA  
1489 C  C   . SER A 187 ? 0.1027 0.2372 0.2454 -0.0268 0.0257  0.0105  188 SER A C   
1490 O  O   . SER A 187 ? 0.1258 0.2590 0.2647 -0.0122 0.0220  -0.0006 188 SER A O   
1491 C  CB  . SER A 187 ? 0.1723 0.3209 0.2443 0.0084  0.0095  0.0644  188 SER A CB  
1492 O  OG  . SER A 187 ? 0.2084 0.2716 0.2666 -0.0127 0.0044  0.0256  188 SER A OG  
1493 N  N   . LEU A 188 ? 0.1002 0.2230 0.2888 -0.0134 -0.0008 0.0022  189 LEU A N   
1494 C  CA  . LEU A 188 ? 0.1058 0.2186 0.2945 -0.0097 -0.0229 0.0060  189 LEU A CA  
1495 C  C   . LEU A 188 ? 0.0905 0.2231 0.2712 -0.0013 0.0154  -0.0029 189 LEU A C   
1496 O  O   . LEU A 188 ? 0.1261 0.2676 0.2927 -0.0137 0.0013  -0.0267 189 LEU A O   
1497 C  CB  . LEU A 188 ? 0.1729 0.1968 0.3621 -0.0339 -0.0129 0.0241  189 LEU A CB  
1498 C  CG  . LEU A 188 ? 0.1699 0.2680 0.3602 -0.0024 0.0245  0.0706  189 LEU A CG  
1499 C  CD1 . LEU A 188 ? 0.2288 0.2443 0.4440 -0.0153 -0.0616 0.0924  189 LEU A CD1 
1500 C  CD2 . LEU A 188 ? 0.1477 0.3838 0.2992 -0.0379 -0.0053 -0.0029 189 LEU A CD2 
1501 N  N   . ASP A 189 ? 0.1190 0.2292 0.2515 0.0134  0.0114  0.0023  190 ASP A N   
1502 C  CA  . ASP A 189 ? 0.0951 0.2546 0.2503 -0.0245 0.0166  0.0071  190 ASP A CA  
1503 C  C   . ASP A 189 ? 0.1046 0.1912 0.2011 -0.0060 0.0328  -0.0172 190 ASP A C   
1504 O  O   . ASP A 189 ? 0.1190 0.1936 0.1808 -0.0089 0.0269  -0.0117 190 ASP A O   
1505 C  CB  . ASP A 189 ? 0.1700 0.3000 0.2300 -0.0576 0.0707  0.0335  190 ASP A CB  
1506 C  CG  . ASP A 189 ? 0.1822 0.5370 0.4016 -0.0707 0.1133  0.0573  190 ASP A CG  
1507 O  OD1 . ASP A 189 ? 0.2170 0.6438 0.3855 -0.1073 0.1430  -0.0573 190 ASP A OD1 
1508 O  OD2 . ASP A 189 ? 0.2723 0.6570 0.4591 -0.2005 0.0684  0.1670  190 ASP A OD2 
1509 N  N   . TYR A 190 ? 0.1174 0.1932 0.1711 -0.0181 0.0472  0.0022  191 TYR A N   
1510 C  CA  . TYR A 190 ? 0.1034 0.1779 0.1610 -0.0066 0.0292  0.0223  191 TYR A CA  
1511 C  C   . TYR A 190 ? 0.1433 0.1581 0.1351 0.0069  0.0350  0.0362  191 TYR A C   
1512 O  O   . TYR A 190 ? 0.1535 0.1885 0.1523 0.0013  0.0511  0.0284  191 TYR A O   
1513 C  CB  . TYR A 190 ? 0.1412 0.1738 0.1531 -0.0046 0.0222  0.0325  191 TYR A CB  
1514 C  CG  . TYR A 190 ? 0.1438 0.1684 0.1660 -0.0166 0.0096  0.0260  191 TYR A CG  
1515 C  CD1 . TYR A 190 ? 0.1703 0.1890 0.1522 -0.0356 0.0258  0.0075  191 TYR A CD1 
1516 C  CD2 . TYR A 190 ? 0.1506 0.2077 0.1588 0.0116  0.0146  0.0124  191 TYR A CD2 
1517 C  CE1 . TYR A 190 ? 0.1682 0.1703 0.1743 -0.0037 0.0358  0.0155  191 TYR A CE1 
1518 C  CE2 . TYR A 190 ? 0.2095 0.2026 0.1656 -0.0208 0.0219  -0.0013 191 TYR A CE2 
1519 C  CZ  . TYR A 190 ? 0.1696 0.2091 0.1680 0.0072  0.0211  -0.0059 191 TYR A CZ  
1520 O  OH  . TYR A 190 ? 0.2457 0.1808 0.2022 0.0115  0.0168  -0.0086 191 TYR A OH  
1521 N  N   . TRP A 191 ? 0.1181 0.1401 0.1495 0.0078  0.0089  0.0100  192 TRP A N   
1522 C  CA  . TRP A 191 ? 0.1286 0.1447 0.1272 0.0012  0.0125  0.0031  192 TRP A CA  
1523 C  C   . TRP A 191 ? 0.1194 0.1637 0.1076 0.0079  0.0182  0.0189  192 TRP A C   
1524 O  O   . TRP A 191 ? 0.1419 0.1779 0.0998 -0.0120 0.0215  0.0071  192 TRP A O   
1525 C  CB  . TRP A 191 ? 0.1168 0.1614 0.1596 0.0097  0.0160  0.0055  192 TRP A CB  
1526 C  CG  . TRP A 191 ? 0.1113 0.1578 0.1695 0.0236  0.0381  0.0232  192 TRP A CG  
1527 C  CD1 . TRP A 191 ? 0.1899 0.1761 0.1770 0.0034  0.0463  0.0188  192 TRP A CD1 
1528 C  CD2 . TRP A 191 ? 0.1280 0.1833 0.1509 0.0111  0.0181  0.0154  192 TRP A CD2 
1529 N  NE1 . TRP A 191 ? 0.1987 0.1681 0.1729 0.0005  0.0185  0.0190  192 TRP A NE1 
1530 C  CE2 . TRP A 191 ? 0.1747 0.1668 0.1734 0.0121  0.0059  0.0135  192 TRP A CE2 
1531 C  CE3 . TRP A 191 ? 0.1146 0.2005 0.1738 0.0129  0.0275  -0.0006 192 TRP A CE3 
1532 C  CZ2 . TRP A 191 ? 0.1407 0.1832 0.2065 0.0161  0.0036  0.0030  192 TRP A CZ2 
1533 C  CZ3 . TRP A 191 ? 0.1293 0.2235 0.2238 -0.0166 0.0566  -0.0110 192 TRP A CZ3 
1534 C  CH2 . TRP A 191 ? 0.1488 0.2094 0.2066 0.0076  0.0106  -0.0032 192 TRP A CH2 
1535 N  N   . THR A 192 ? 0.1208 0.1617 0.1276 -0.0067 0.0086  0.0085  193 THR A N   
1536 C  CA  . THR A 192 ? 0.1041 0.1660 0.1326 0.0187  0.0103  0.0153  193 THR A CA  
1537 C  C   . THR A 192 ? 0.1113 0.1570 0.1102 -0.0021 0.0124  0.0080  193 THR A C   
1538 O  O   . THR A 192 ? 0.1448 0.1818 0.1058 0.0018  0.0052  0.0055  193 THR A O   
1539 C  CB  . THR A 192 ? 0.1429 0.1505 0.1304 0.0314  0.0328  0.0019  193 THR A CB  
1540 O  OG1 . THR A 192 ? 0.1368 0.1566 0.1535 0.0126  0.0184  -0.0016 193 THR A OG1 
1541 C  CG2 . THR A 192 ? 0.1509 0.1890 0.1319 0.0290  0.0380  -0.0065 193 THR A CG2 
1542 N  N   . TYR A 193 ? 0.1108 0.1659 0.1174 -0.0012 0.0183  -0.0179 194 TYR A N   
1543 C  CA  . TYR A 193 ? 0.0886 0.1861 0.1513 0.0150  0.0188  -0.0064 194 TYR A CA  
1544 C  C   . TYR A 193 ? 0.1084 0.1601 0.1045 0.0148  0.0129  -0.0227 194 TYR A C   
1545 O  O   . TYR A 193 ? 0.1438 0.1519 0.1081 0.0119  -0.0018 -0.0187 194 TYR A O   
1546 C  CB  . TYR A 193 ? 0.1670 0.1833 0.1104 0.0389  0.0030  -0.0346 194 TYR A CB  
1547 C  CG  . TYR A 193 ? 0.1168 0.1461 0.1016 0.0170  -0.0016 -0.0006 194 TYR A CG  
1548 C  CD1 . TYR A 193 ? 0.1441 0.1451 0.1040 0.0008  -0.0031 0.0027  194 TYR A CD1 
1549 C  CD2 . TYR A 193 ? 0.1086 0.1826 0.1343 0.0230  0.0060  -0.0074 194 TYR A CD2 
1550 C  CE1 . TYR A 193 ? 0.1070 0.1642 0.1232 0.0059  0.0108  0.0042  194 TYR A CE1 
1551 C  CE2 . TYR A 193 ? 0.1391 0.1499 0.1210 0.0049  -0.0070 -0.0159 194 TYR A CE2 
1552 C  CZ  . TYR A 193 ? 0.1151 0.1301 0.1111 0.0132  0.0049  -0.0182 194 TYR A CZ  
1553 O  OH  . TYR A 193 ? 0.1099 0.1438 0.1222 0.0011  0.0117  -0.0066 194 TYR A OH  
1554 N  N   . PRO A 194 ? 0.1244 0.1900 0.1131 0.0098  -0.0041 -0.0234 195 PRO A N   
1555 C  CA  . PRO A 194 ? 0.1272 0.1919 0.1466 -0.0003 0.0192  -0.0457 195 PRO A CA  
1556 C  C   . PRO A 194 ? 0.1147 0.1547 0.1307 0.0035  -0.0082 -0.0299 195 PRO A C   
1557 O  O   . PRO A 194 ? 0.1337 0.1822 0.1302 0.0253  -0.0024 -0.0165 195 PRO A O   
1558 C  CB  . PRO A 194 ? 0.1573 0.2131 0.1599 -0.0065 -0.0063 -0.0565 195 PRO A CB  
1559 C  CG  . PRO A 194 ? 0.1743 0.2643 0.1648 -0.0103 -0.0192 -0.0333 195 PRO A CG  
1560 C  CD  . PRO A 194 ? 0.1735 0.2963 0.0998 -0.0300 -0.0075 -0.0296 195 PRO A CD  
1561 N  N   . GLY A 195 ? 0.1064 0.1601 0.1265 -0.0002 0.0049  -0.0439 196 GLY A N   
1562 C  CA  . GLY A 195 ? 0.1027 0.1657 0.1382 0.0092  0.0100  -0.0096 196 GLY A CA  
1563 C  C   . GLY A 195 ? 0.0810 0.1451 0.1364 -0.0038 -0.0038 -0.0270 196 GLY A C   
1564 O  O   . GLY A 195 ? 0.1197 0.1380 0.1395 -0.0024 0.0030  -0.0220 196 GLY A O   
1565 N  N   . SER A 196 ? 0.0907 0.1581 0.1225 0.0027  0.0089  -0.0211 197 SER A N   
1566 C  CA  . SER A 196 ? 0.0668 0.1642 0.1317 0.0013  0.0177  -0.0245 197 SER A CA  
1567 C  C   . SER A 196 ? 0.1009 0.1161 0.1368 0.0037  -0.0006 -0.0188 197 SER A C   
1568 O  O   . SER A 196 ? 0.0779 0.1361 0.1520 -0.0047 -0.0035 -0.0223 197 SER A O   
1569 C  CB  . SER A 196 ? 0.0750 0.1578 0.1635 0.0116  0.0102  -0.0496 197 SER A CB  
1570 O  OG  . SER A 196 ? 0.0897 0.1409 0.1707 0.0016  0.0038  -0.0207 197 SER A OG  
1571 N  N   . LEU A 197 ? 0.0912 0.1445 0.1303 0.0063  0.0089  -0.0100 198 LEU A N   
1572 C  CA  . LEU A 197 ? 0.0847 0.1343 0.1344 -0.0077 0.0127  -0.0178 198 LEU A CA  
1573 C  C   . LEU A 197 ? 0.0569 0.1326 0.1635 -0.0196 -0.0030 -0.0192 198 LEU A C   
1574 O  O   . LEU A 197 ? 0.0712 0.1736 0.1580 -0.0034 -0.0055 -0.0370 198 LEU A O   
1575 C  CB  . LEU A 197 ? 0.0822 0.1492 0.1707 -0.0041 0.0189  -0.0005 198 LEU A CB  
1576 C  CG  . LEU A 197 ? 0.1259 0.1520 0.1659 -0.0089 0.0141  -0.0071 198 LEU A CG  
1577 C  CD1 . LEU A 197 ? 0.1978 0.1767 0.2027 -0.0207 0.0559  0.0205  198 LEU A CD1 
1578 C  CD2 . LEU A 197 ? 0.1153 0.1754 0.1987 -0.0096 0.0234  -0.0157 198 LEU A CD2 
1579 N  N   . THR A 198 ? 0.0817 0.1322 0.1391 -0.0080 -0.0064 -0.0166 199 THR A N   
1580 C  CA  . THR A 198 ? 0.0815 0.1409 0.1624 -0.0025 0.0067  -0.0302 199 THR A CA  
1581 C  C   . THR A 198 ? 0.0686 0.1432 0.1800 -0.0197 0.0111  -0.0166 199 THR A C   
1582 O  O   . THR A 198 ? 0.0979 0.1459 0.1994 -0.0029 0.0063  -0.0364 199 THR A O   
1583 C  CB  . THR A 198 ? 0.1046 0.1544 0.1177 -0.0168 0.0111  -0.0142 199 THR A CB  
1584 O  OG1 . THR A 198 ? 0.0939 0.1412 0.1244 -0.0038 0.0022  -0.0065 199 THR A OG1 
1585 C  CG2 . THR A 198 ? 0.1131 0.1729 0.1373 0.0114  0.0257  -0.0313 199 THR A CG2 
1586 N  N   . THR A 199 ? 0.0851 0.1560 0.1796 -0.0337 0.0211  -0.0037 200 THR A N   
1587 C  CA  . THR A 199 ? 0.1136 0.1756 0.1567 -0.0296 0.0231  -0.0145 200 THR A CA  
1588 C  C   . THR A 199 ? 0.0883 0.1896 0.1736 -0.0376 0.0337  -0.0290 200 THR A C   
1589 O  O   . THR A 199 ? 0.1106 0.1662 0.2016 -0.0119 0.0303  -0.0239 200 THR A O   
1590 C  CB  . THR A 199 ? 0.1432 0.1886 0.1750 -0.0129 -0.0074 -0.0139 200 THR A CB  
1591 O  OG1 . THR A 199 ? 0.3010 0.2055 0.2293 0.0341  -0.0295 -0.0115 200 THR A OG1 
1592 C  CG2 . THR A 199 ? 0.2814 0.1955 0.1886 -0.0831 -0.0836 -0.0100 200 THR A CG2 
1593 N  N   . PRO A 200 ? 0.0919 0.1761 0.2119 -0.0229 0.0507  -0.0295 201 PRO A N   
1594 C  CA  . PRO A 200 ? 0.1146 0.1743 0.1947 -0.0290 0.0478  -0.0115 201 PRO A CA  
1595 C  C   . PRO A 200 ? 0.0996 0.1901 0.2011 -0.0297 0.0174  -0.0190 201 PRO A C   
1596 O  O   . PRO A 200 ? 0.1057 0.2349 0.2033 -0.0133 0.0313  -0.0154 201 PRO A O   
1597 C  CB  . PRO A 200 ? 0.1205 0.2008 0.2392 -0.0044 0.0639  -0.0095 201 PRO A CB  
1598 C  CG  . PRO A 200 ? 0.1337 0.1890 0.2588 -0.0256 0.0381  -0.0497 201 PRO A CG  
1599 C  CD  . PRO A 200 ? 0.1208 0.1984 0.2277 -0.0087 0.0418  -0.0514 201 PRO A CD  
1600 N  N   . PRO A 201 ? 0.0964 0.1821 0.1997 -0.0240 0.0259  -0.0151 202 PRO A N   
1601 C  CA  . PRO A 201 ? 0.1326 0.1562 0.1915 -0.0205 0.0080  -0.0085 202 PRO A CA  
1602 C  C   . PRO A 201 ? 0.1009 0.1678 0.1861 -0.0134 0.0059  -0.0010 202 PRO A C   
1603 O  O   . PRO A 201 ? 0.1089 0.1720 0.2174 -0.0214 0.0052  -0.0322 202 PRO A O   
1604 C  CB  . PRO A 201 ? 0.1499 0.1562 0.2692 0.0000  0.0262  0.0036  202 PRO A CB  
1605 C  CG  . PRO A 201 ? 0.1375 0.1887 0.2536 -0.0318 0.0081  -0.0152 202 PRO A CG  
1606 C  CD  . PRO A 201 ? 0.1248 0.1616 0.2393 -0.0052 0.0342  -0.0156 202 PRO A CD  
1607 N  N   . LEU A 202 ? 0.0838 0.1588 0.1850 -0.0095 0.0162  -0.0190 203 LEU A N   
1608 C  CA  . LEU A 202 ? 0.1092 0.1355 0.1957 -0.0132 -0.0057 -0.0196 203 LEU A CA  
1609 C  C   . LEU A 202 ? 0.0779 0.1441 0.1700 -0.0281 0.0035  -0.0163 203 LEU A C   
1610 O  O   . LEU A 202 ? 0.0847 0.1727 0.1808 -0.0040 -0.0100 -0.0242 203 LEU A O   
1611 C  CB  . LEU A 202 ? 0.0919 0.1720 0.2064 0.0032  -0.0238 -0.0317 203 LEU A CB  
1612 C  CG  . LEU A 202 ? 0.0889 0.1432 0.1950 0.0049  -0.0016 -0.0251 203 LEU A CG  
1613 C  CD1 . LEU A 202 ? 0.1120 0.2174 0.2359 0.0307  -0.0161 -0.0079 203 LEU A CD1 
1614 C  CD2 . LEU A 202 ? 0.1142 0.1549 0.2306 -0.0079 -0.0009 -0.0165 203 LEU A CD2 
1615 N  N   . THR A 203 ? 0.1029 0.1382 0.2104 -0.0176 0.0268  -0.0341 204 THR A N   
1616 C  CA  . THR A 203 ? 0.1172 0.1382 0.1936 -0.0198 0.0146  -0.0381 204 THR A CA  
1617 C  C   . THR A 203 ? 0.1128 0.1538 0.1754 -0.0201 -0.0089 -0.0273 204 THR A C   
1618 O  O   . THR A 203 ? 0.0876 0.1571 0.1953 -0.0208 0.0017  -0.0387 204 THR A O   
1619 C  CB  . THR A 203 ? 0.1524 0.1441 0.2267 -0.0035 0.0552  -0.0049 204 THR A CB  
1620 O  OG1 . THR A 203 ? 0.1463 0.1707 0.2307 -0.0109 0.0491  -0.0184 204 THR A OG1 
1621 C  CG2 . THR A 203 ? 0.1628 0.1718 0.2449 -0.0035 0.0420  -0.0436 204 THR A CG2 
1622 N  N   . GLU A 204 ? 0.1434 0.1549 0.1750 -0.0058 -0.0122 -0.0427 205 GLU A N   
1623 C  CA  . GLU A 204 ? 0.1266 0.1813 0.1861 0.0108  -0.0187 -0.0265 205 GLU A CA  
1624 C  C   . GLU A 204 ? 0.1409 0.1796 0.1691 0.0077  -0.0301 -0.0642 205 GLU A C   
1625 O  O   . GLU A 204 ? 0.1964 0.2469 0.1843 0.0570  -0.0765 -0.1048 205 GLU A O   
1626 C  CB  . GLU A 204 ? 0.1329 0.1863 0.1905 0.0165  -0.0292 -0.0401 205 GLU A CB  
1627 C  CG  . GLU A 204 ? 0.1706 0.1929 0.1892 0.0422  -0.0187 -0.0322 205 GLU A CG  
1628 C  CD  . GLU A 204 ? 0.1481 0.2305 0.1861 0.0150  -0.0144 -0.0581 205 GLU A CD  
1629 O  OE1 . GLU A 204 ? 0.1822 0.2424 0.2303 0.0277  -0.0621 -0.0766 205 GLU A OE1 
1630 O  OE2 . GLU A 204 ? 0.1383 0.2256 0.1987 -0.0156 -0.0207 -0.0348 205 GLU A OE2 
1631 N  N   . CYS A 205 ? 0.0874 0.1594 0.1635 0.0036  -0.0182 -0.0372 206 CYS A N   
1632 C  CA  . CYS A 205 ? 0.1014 0.1612 0.1585 0.0013  -0.0151 -0.0142 206 CYS A CA  
1633 C  C   . CYS A 205 ? 0.1075 0.1433 0.1545 0.0013  0.0048  -0.0297 206 CYS A C   
1634 O  O   . CYS A 205 ? 0.1229 0.1560 0.2002 -0.0005 -0.0189 -0.0062 206 CYS A O   
1635 C  CB  . CYS A 205 ? 0.1317 0.1638 0.1710 -0.0104 -0.0122 -0.0216 206 CYS A CB  
1636 S  SG  . CYS A 205 ? 0.1585 0.1764 0.1682 0.0041  0.0072  -0.0248 206 CYS A SG  
1637 N  N   . VAL A 206 ? 0.0923 0.1391 0.1477 -0.0156 0.0044  -0.0241 207 VAL A N   
1638 C  CA  . VAL A 206 ? 0.0934 0.1549 0.1048 -0.0111 -0.0073 -0.0179 207 VAL A CA  
1639 C  C   . VAL A 206 ? 0.1031 0.1217 0.1259 -0.0041 0.0017  0.0011  207 VAL A C   
1640 O  O   . VAL A 206 ? 0.1151 0.1757 0.1596 0.0053  -0.0122 0.0055  207 VAL A O   
1641 C  CB  . VAL A 206 ? 0.0967 0.1456 0.1252 -0.0134 0.0107  -0.0274 207 VAL A CB  
1642 C  CG1 . VAL A 206 ? 0.0912 0.1556 0.1337 -0.0093 -0.0117 -0.0282 207 VAL A CG1 
1643 C  CG2 . VAL A 206 ? 0.1037 0.1585 0.1380 0.0243  0.0271  -0.0182 207 VAL A CG2 
1644 N  N   . THR A 207 ? 0.0998 0.1247 0.1401 -0.0019 0.0076  -0.0066 208 THR A N   
1645 C  CA  . THR A 207 ? 0.1237 0.1212 0.1293 -0.0012 0.0113  -0.0097 208 THR A CA  
1646 C  C   . THR A 207 ? 0.1027 0.1375 0.1161 -0.0092 0.0024  0.0066  208 THR A C   
1647 O  O   . THR A 207 ? 0.1142 0.1329 0.1240 0.0040  -0.0073 0.0035  208 THR A O   
1648 C  CB  . THR A 207 ? 0.1527 0.1270 0.1366 0.0104  0.0206  -0.0100 208 THR A CB  
1649 O  OG1 . THR A 207 ? 0.1685 0.1337 0.1659 -0.0022 0.0144  -0.0121 208 THR A OG1 
1650 C  CG2 . THR A 207 ? 0.1552 0.1699 0.1695 -0.0036 0.0401  0.0054  208 THR A CG2 
1651 N  N   . TRP A 208 ? 0.0968 0.1145 0.1274 0.0049  -0.0009 -0.0086 209 TRP A N   
1652 C  CA  . TRP A 208 ? 0.0962 0.1194 0.1256 0.0051  0.0092  -0.0144 209 TRP A CA  
1653 C  C   . TRP A 208 ? 0.0888 0.1423 0.1095 0.0146  0.0058  -0.0052 209 TRP A C   
1654 O  O   . TRP A 208 ? 0.1119 0.1599 0.1147 0.0000  0.0121  0.0083  209 TRP A O   
1655 C  CB  . TRP A 208 ? 0.0854 0.1361 0.1323 0.0054  0.0064  0.0128  209 TRP A CB  
1656 C  CG  . TRP A 208 ? 0.1037 0.1108 0.1169 -0.0081 0.0086  -0.0022 209 TRP A CG  
1657 C  CD1 . TRP A 208 ? 0.0926 0.1317 0.1333 -0.0033 0.0106  -0.0128 209 TRP A CD1 
1658 C  CD2 . TRP A 208 ? 0.0926 0.1038 0.1212 0.0006  0.0010  -0.0086 209 TRP A CD2 
1659 N  NE1 . TRP A 208 ? 0.0987 0.1409 0.1373 -0.0020 0.0050  -0.0141 209 TRP A NE1 
1660 C  CE2 . TRP A 208 ? 0.1045 0.1188 0.1221 0.0020  0.0096  -0.0043 209 TRP A CE2 
1661 C  CE3 . TRP A 208 ? 0.1220 0.1219 0.1023 0.0039  -0.0182 -0.0017 209 TRP A CE3 
1662 C  CZ2 . TRP A 208 ? 0.1310 0.1181 0.1174 0.0227  0.0150  -0.0166 209 TRP A CZ2 
1663 C  CZ3 . TRP A 208 ? 0.1443 0.1368 0.1003 0.0165  -0.0015 -0.0008 209 TRP A CZ3 
1664 C  CH2 . TRP A 208 ? 0.1470 0.1371 0.1146 0.0052  0.0165  -0.0087 209 TRP A CH2 
1665 N  N   . ILE A 209 ? 0.0925 0.1217 0.1321 -0.0099 0.0065  0.0098  210 ILE A N   
1666 C  CA  . ILE A 209 ? 0.0833 0.1405 0.1159 -0.0037 0.0127  -0.0050 210 ILE A CA  
1667 C  C   . ILE A 209 ? 0.1021 0.1441 0.1053 0.0020  0.0074  0.0049  210 ILE A C   
1668 O  O   . ILE A 209 ? 0.1371 0.1502 0.1086 -0.0026 0.0122  0.0034  210 ILE A O   
1669 C  CB  . ILE A 209 ? 0.0901 0.1616 0.1288 0.0023  0.0177  0.0066  210 ILE A CB  
1670 C  CG1 . ILE A 209 ? 0.1422 0.1328 0.1853 0.0244  0.0055  -0.0206 210 ILE A CG1 
1671 C  CG2 . ILE A 209 ? 0.0842 0.1993 0.1702 -0.0137 0.0139  0.0173  210 ILE A CG2 
1672 C  CD1 . ILE A 209 ? 0.1177 0.1792 0.2490 0.0321  -0.0111 -0.0051 210 ILE A CD1 
1673 N  N   . VAL A 210 ? 0.1072 0.1272 0.1267 0.0145  0.0094  0.0013  211 VAL A N   
1674 C  CA  . VAL A 210 ? 0.0885 0.1379 0.1189 0.0077  0.0005  -0.0111 211 VAL A CA  
1675 C  C   . VAL A 210 ? 0.1074 0.1229 0.1162 0.0005  0.0266  -0.0174 211 VAL A C   
1676 O  O   . VAL A 210 ? 0.1274 0.1535 0.1180 -0.0156 0.0252  -0.0051 211 VAL A O   
1677 C  CB  . VAL A 210 ? 0.0930 0.1307 0.1441 0.0083  0.0050  0.0026  211 VAL A CB  
1678 C  CG1 . VAL A 210 ? 0.1092 0.1232 0.1687 -0.0083 0.0082  -0.0165 211 VAL A CG1 
1679 C  CG2 . VAL A 210 ? 0.1120 0.1491 0.1729 -0.0164 0.0129  0.0078  211 VAL A CG2 
1680 N  N   . LEU A 211 ? 0.0961 0.1480 0.1427 -0.0181 0.0067  -0.0063 212 LEU A N   
1681 C  CA  . LEU A 211 ? 0.0968 0.1555 0.1684 -0.0243 -0.0055 0.0074  212 LEU A CA  
1682 C  C   . LEU A 211 ? 0.1102 0.1497 0.1716 -0.0292 0.0181  -0.0022 212 LEU A C   
1683 O  O   . LEU A 211 ? 0.1131 0.1685 0.1434 -0.0085 -0.0013 -0.0055 212 LEU A O   
1684 C  CB  . LEU A 211 ? 0.0968 0.1513 0.1641 -0.0242 -0.0074 0.0098  212 LEU A CB  
1685 C  CG  . LEU A 211 ? 0.1131 0.1775 0.1551 -0.0084 -0.0017 0.0032  212 LEU A CG  
1686 C  CD1 . LEU A 211 ? 0.1244 0.2177 0.1947 -0.0009 -0.0315 0.0177  212 LEU A CD1 
1687 C  CD2 . LEU A 211 ? 0.1445 0.2084 0.1682 0.0337  0.0236  0.0107  212 LEU A CD2 
1688 N  N   . LYS A 212 ? 0.1147 0.1847 0.1581 -0.0370 0.0072  0.0253  213 LYS A N   
1689 C  CA  . LYS A 212 ? 0.1905 0.1754 0.1491 -0.0200 0.0038  0.0142  213 LYS A CA  
1690 C  C   . LYS A 212 ? 0.1452 0.1889 0.1585 -0.0201 0.0376  0.0072  213 LYS A C   
1691 O  O   . LYS A 212 ? 0.1591 0.1813 0.2528 -0.0115 -0.0141 0.0335  213 LYS A O   
1692 C  CB  . LYS A 212 ? 0.3072 0.2309 0.1344 -0.0829 0.0408  0.0042  213 LYS A CB  
1693 C  CG  . LYS A 212 ? 0.4698 0.3216 0.2073 -0.1547 0.0182  0.0696  213 LYS A CG  
1694 C  CD  . LYS A 212 ? 0.5708 0.4494 0.4137 -0.2485 0.1560  0.0229  213 LYS A CD  
1695 C  CE  . LYS A 212 ? 0.4749 0.7307 0.3398 0.0520  0.1647  0.0059  213 LYS A CE  
1696 N  NZ  . LYS A 212 ? 0.4837 0.6246 0.7953 0.0675  -0.3920 -0.0280 213 LYS A NZ  
1697 N  N   . GLU A 213 ? 0.1375 0.1716 0.1569 -0.0260 0.0250  0.0152  214 GLU A N   
1698 C  CA  . GLU A 213 ? 0.1241 0.1847 0.1749 -0.0103 0.0168  0.0037  214 GLU A CA  
1699 C  C   . GLU A 213 ? 0.1165 0.1560 0.1693 -0.0218 0.0057  0.0151  214 GLU A C   
1700 O  O   . GLU A 213 ? 0.1084 0.1595 0.1774 -0.0086 0.0208  0.0138  214 GLU A O   
1701 C  CB  . GLU A 213 ? 0.1203 0.1863 0.2150 -0.0034 0.0324  -0.0002 214 GLU A CB  
1702 C  CG  . GLU A 213 ? 0.2117 0.2004 0.2570 -0.0460 -0.0208 -0.0071 214 GLU A CG  
1703 C  CD  . GLU A 213 ? 0.1788 0.3212 0.5004 -0.0974 0.0288  -0.1085 214 GLU A CD  
1704 O  OE1 . GLU A 213 ? 0.1670 0.2821 0.3589 -0.0313 0.0032  -0.0019 214 GLU A OE1 
1705 O  OE2 . GLU A 213 ? 0.3147 0.6838 0.6656 -0.0813 -0.1395 -0.2846 214 GLU A OE2 
1706 N  N   A PRO A 214 ? 0.1317 0.1484 0.1621 -0.0189 0.0063  0.0187  215 PRO A N   
1707 N  N   B PRO A 214 ? 0.1379 0.1465 0.1702 -0.0182 0.0100  0.0201  215 PRO A N   
1708 C  CA  A PRO A 214 ? 0.1149 0.1598 0.1571 -0.0109 -0.0051 -0.0006 215 PRO A CA  
1709 C  CA  B PRO A 214 ? 0.1264 0.1656 0.1559 0.0044  -0.0100 -0.0023 215 PRO A CA  
1710 C  C   A PRO A 214 ? 0.1307 0.1734 0.1743 -0.0270 -0.0204 0.0118  215 PRO A C   
1711 C  C   B PRO A 214 ? 0.1307 0.1734 0.1732 -0.0265 -0.0216 0.0138  215 PRO A C   
1712 O  O   A PRO A 214 ? 0.1300 0.2411 0.1948 -0.0467 -0.0168 0.0164  215 PRO A O   
1713 O  O   B PRO A 214 ? 0.1279 0.2404 0.1966 -0.0428 -0.0183 0.0212  215 PRO A O   
1714 C  CB  A PRO A 214 ? 0.1353 0.1459 0.1984 -0.0160 -0.0009 -0.0039 215 PRO A CB  
1715 C  CB  B PRO A 214 ? 0.1588 0.1323 0.2186 -0.0121 0.0095  -0.0097 215 PRO A CB  
1716 C  CG  A PRO A 214 ? 0.1793 0.1752 0.2278 0.0044  0.0374  0.0316  215 PRO A CG  
1717 C  CG  B PRO A 214 ? 0.2451 0.2238 0.2360 0.0313  0.0550  0.0372  215 PRO A CG  
1718 C  CD  A PRO A 214 ? 0.1723 0.1477 0.2221 0.0120  0.0092  0.0287  215 PRO A CD  
1719 C  CD  B PRO A 214 ? 0.1939 0.1246 0.2573 -0.0270 0.0392  0.0358  215 PRO A CD  
1720 N  N   . ILE A 215 ? 0.1745 0.1603 0.1513 -0.0065 -0.0221 0.0107  216 ILE A N   
1721 C  CA  . ILE A 215 ? 0.1653 0.1849 0.1581 0.0027  -0.0212 -0.0061 216 ILE A CA  
1722 C  C   . ILE A 215 ? 0.1480 0.1729 0.1483 -0.0219 -0.0102 -0.0005 216 ILE A C   
1723 O  O   . ILE A 215 ? 0.1545 0.1653 0.2037 0.0036  -0.0065 -0.0234 216 ILE A O   
1724 C  CB  . ILE A 215 ? 0.1432 0.1846 0.1504 0.0110  -0.0379 -0.0098 216 ILE A CB  
1725 C  CG1 . ILE A 215 ? 0.1549 0.1596 0.1757 0.0013  -0.0177 0.0109  216 ILE A CG1 
1726 C  CG2 . ILE A 215 ? 0.1980 0.1900 0.2194 0.0133  -0.0069 -0.0516 216 ILE A CG2 
1727 C  CD1 . ILE A 215 ? 0.2018 0.1786 0.1951 0.0025  0.0010  0.0124  216 ILE A CD1 
1728 N  N   A SER A 216 ? 0.1592 0.1391 0.2011 -0.0037 -0.0373 -0.0181 217 SER A N   
1729 N  N   B SER A 216 ? 0.1612 0.1983 0.1842 -0.0248 -0.0176 -0.0231 217 SER A N   
1730 C  CA  A SER A 216 ? 0.1797 0.1595 0.1535 -0.0238 -0.0501 -0.0302 217 SER A CA  
1731 C  CA  B SER A 216 ? 0.1756 0.2163 0.1829 0.0031  0.0000  -0.0133 217 SER A CA  
1732 C  C   A SER A 216 ? 0.1681 0.1389 0.1641 -0.0142 -0.0407 -0.0079 217 SER A C   
1733 C  C   B SER A 216 ? 0.1458 0.1409 0.1831 -0.0296 -0.0348 -0.0087 217 SER A C   
1734 O  O   A SER A 216 ? 0.1919 0.1754 0.1721 -0.0174 -0.0506 0.0304  217 SER A O   
1735 O  O   B SER A 216 ? 0.1739 0.2080 0.2264 0.0084  -0.0509 -0.0052 217 SER A O   
1736 C  CB  A SER A 216 ? 0.2091 0.1416 0.1950 -0.0305 -0.0507 -0.0127 217 SER A CB  
1737 C  CB  B SER A 216 ? 0.2705 0.2667 0.2338 -0.0430 0.0025  0.1485  217 SER A CB  
1738 O  OG  A SER A 216 ? 0.2935 0.2587 0.1770 -0.0413 -0.0226 -0.0058 217 SER A OG  
1739 O  OG  B SER A 216 ? 0.2427 0.3917 0.3276 -0.1333 -0.0550 0.0522  217 SER A OG  
1740 N  N   . VAL A 217 ? 0.1789 0.1559 0.1820 -0.0210 -0.0242 -0.0108 218 VAL A N   
1741 C  CA  . VAL A 217 ? 0.1923 0.1397 0.1738 -0.0232 -0.0302 -0.0121 218 VAL A CA  
1742 C  C   . VAL A 217 ? 0.1918 0.1420 0.1861 -0.0029 -0.0296 -0.0197 218 VAL A C   
1743 O  O   . VAL A 217 ? 0.1858 0.1465 0.2045 -0.0187 -0.0490 -0.0130 218 VAL A O   
1744 C  CB  . VAL A 217 ? 0.1627 0.1559 0.2095 -0.0189 -0.0477 -0.0181 218 VAL A CB  
1745 C  CG1 . VAL A 217 ? 0.2133 0.1280 0.2178 -0.0301 -0.0414 -0.0103 218 VAL A CG1 
1746 C  CG2 . VAL A 217 ? 0.1581 0.1797 0.3025 -0.0079 -0.0297 -0.0326 218 VAL A CG2 
1747 N  N   . SER A 218 ? 0.2223 0.1333 0.1689 -0.0182 -0.0290 -0.0210 219 SER A N   
1748 C  CA  . SER A 218 ? 0.1966 0.1418 0.1904 -0.0026 -0.0454 -0.0245 219 SER A CA  
1749 C  C   . SER A 218 ? 0.2061 0.1418 0.1864 -0.0089 -0.0044 0.0010  219 SER A C   
1750 O  O   . SER A 218 ? 0.2181 0.1391 0.1903 -0.0249 -0.0413 0.0111  219 SER A O   
1751 C  CB  . SER A 218 ? 0.2985 0.1490 0.1650 -0.0340 -0.0532 -0.0153 219 SER A CB  
1752 O  OG  . SER A 218 ? 0.2824 0.1775 0.1919 -0.0325 -0.0482 -0.0052 219 SER A OG  
1753 N  N   . SER A 219 ? 0.1979 0.1426 0.2183 0.0008  -0.0335 -0.0113 220 SER A N   
1754 C  CA  . SER A 219 ? 0.1894 0.1562 0.2397 -0.0218 -0.0025 0.0190  220 SER A CA  
1755 C  C   . SER A 219 ? 0.1847 0.1395 0.2434 -0.0097 -0.0033 -0.0042 220 SER A C   
1756 O  O   . SER A 219 ? 0.2127 0.1887 0.2749 -0.0570 0.0068  0.0111  220 SER A O   
1757 C  CB  . SER A 219 ? 0.3435 0.1584 0.2849 -0.0473 -0.0027 0.0184  220 SER A CB  
1758 O  OG  . SER A 219 ? 0.3204 0.2147 0.3482 -0.0010 0.0425  -0.0113 220 SER A OG  
1759 N  N   . GLU A 220 ? 0.2422 0.1621 0.2130 -0.0055 -0.0106 -0.0065 221 GLU A N   
1760 C  CA  . GLU A 220 ? 0.2752 0.1757 0.2140 -0.0125 -0.0241 -0.0029 221 GLU A CA  
1761 C  C   . GLU A 220 ? 0.2666 0.1720 0.1966 -0.0062 -0.0345 0.0116  221 GLU A C   
1762 O  O   . GLU A 220 ? 0.3139 0.1861 0.2143 -0.0175 0.0340  -0.0160 221 GLU A O   
1763 C  CB  . GLU A 220 ? 0.3373 0.2698 0.2160 -0.0410 -0.0528 -0.0841 221 GLU A CB  
1764 C  CG  . GLU A 220 ? 0.4023 0.2928 0.3197 -0.1147 -0.0510 -0.0989 221 GLU A CG  
1765 C  CD  . GLU A 220 ? 0.4986 0.2201 0.3553 -0.0571 -0.0409 -0.0476 221 GLU A CD  
1766 O  OE1 . GLU A 220 ? 0.3464 0.3018 0.3345 -0.0651 -0.0916 -0.0794 221 GLU A OE1 
1767 O  OE2 . GLU A 220 ? 0.7849 0.2608 0.5075 -0.1715 0.1034  -0.0889 221 GLU A OE2 
1768 N  N   . GLN A 221 ? 0.2346 0.1605 0.1828 -0.0119 -0.0163 0.0073  222 GLN A N   
1769 C  CA  . GLN A 221 ? 0.2069 0.1541 0.1879 -0.0088 -0.0228 0.0086  222 GLN A CA  
1770 C  C   . GLN A 221 ? 0.2082 0.1847 0.1705 -0.0189 -0.0057 0.0136  222 GLN A C   
1771 O  O   . GLN A 221 ? 0.2217 0.1786 0.1864 -0.0361 0.0011  0.0198  222 GLN A O   
1772 C  CB  . GLN A 221 ? 0.1923 0.1939 0.1772 -0.0127 -0.0266 -0.0013 222 GLN A CB  
1773 C  CG  . GLN A 221 ? 0.1725 0.1991 0.2339 -0.0287 -0.0332 0.0063  222 GLN A CG  
1774 C  CD  . GLN A 221 ? 0.2274 0.1422 0.1879 -0.0104 -0.0425 0.0107  222 GLN A CD  
1775 O  OE1 . GLN A 221 ? 0.1966 0.1486 0.1899 -0.0145 -0.0210 0.0100  222 GLN A OE1 
1776 N  NE2 . GLN A 221 ? 0.2320 0.1438 0.2108 -0.0134 -0.0538 0.0176  222 GLN A NE2 
1777 N  N   . VAL A 222 ? 0.2023 0.1666 0.1644 -0.0170 -0.0125 0.0060  223 VAL A N   
1778 C  CA  . VAL A 222 ? 0.2048 0.1997 0.1875 0.0061  -0.0266 0.0094  223 VAL A CA  
1779 C  C   . VAL A 222 ? 0.2162 0.1839 0.1817 -0.0389 -0.0052 0.0002  223 VAL A C   
1780 O  O   . VAL A 222 ? 0.1932 0.2256 0.1973 -0.0433 0.0072  0.0385  223 VAL A O   
1781 C  CB  . VAL A 222 ? 0.2330 0.2643 0.2222 -0.0270 -0.0641 0.0633  223 VAL A CB  
1782 C  CG1 . VAL A 222 ? 0.2695 0.2713 0.3283 -0.0790 -0.0381 0.1020  223 VAL A CG1 
1783 C  CG2 . VAL A 222 ? 0.2579 0.3151 0.2186 -0.0322 -0.0697 0.0350  223 VAL A CG2 
1784 N  N   A LEU A 223 ? 0.2235 0.1573 0.2265 -0.0030 0.0291  -0.0182 224 LEU A N   
1785 N  N   B LEU A 223 ? 0.2258 0.1781 0.2113 -0.0178 0.0307  -0.0239 224 LEU A N   
1786 C  CA  A LEU A 223 ? 0.2247 0.1955 0.2532 -0.0152 0.0515  -0.0298 224 LEU A CA  
1787 C  CA  B LEU A 223 ? 0.2813 0.2102 0.2204 -0.0110 0.0620  -0.0283 224 LEU A CA  
1788 C  C   A LEU A 223 ? 0.2483 0.2178 0.2133 -0.0263 0.0319  -0.0330 224 LEU A C   
1789 C  C   B LEU A 223 ? 0.2231 0.2256 0.1968 -0.0413 0.0288  -0.0365 224 LEU A C   
1790 O  O   A LEU A 223 ? 0.2338 0.2186 0.2132 0.0050  0.0293  -0.0084 224 LEU A O   
1791 O  O   B LEU A 223 ? 0.2127 0.2533 0.2404 -0.0337 0.0352  -0.0234 224 LEU A O   
1792 C  CB  A LEU A 223 ? 0.3378 0.2484 0.2856 -0.0269 0.0469  -0.0883 224 LEU A CB  
1793 C  CB  B LEU A 223 ? 0.3916 0.2223 0.2303 -0.0538 0.0317  -0.0173 224 LEU A CB  
1794 C  CG  A LEU A 223 ? 0.3528 0.2850 0.2388 -0.0534 0.0880  -0.0806 224 LEU A CG  
1795 C  CG  B LEU A 223 ? 0.3227 0.2709 0.3675 -0.0345 0.0021  -0.0974 224 LEU A CG  
1796 C  CD1 A LEU A 223 ? 0.2271 0.3948 0.3685 -0.0653 0.0285  -0.1031 224 LEU A CD1 
1797 C  CD1 B LEU A 223 ? 0.5161 0.3944 0.1693 -0.0391 -0.0341 0.0451  224 LEU A CD1 
1798 C  CD2 A LEU A 223 ? 0.3316 0.2917 0.4110 -0.0851 0.1038  -0.0155 224 LEU A CD2 
1799 C  CD2 B LEU A 223 ? 0.4562 0.2461 0.4476 -0.0363 0.0337  -0.1434 224 LEU A CD2 
1800 N  N   . LYS A 224 ? 0.2362 0.2242 0.1608 -0.0417 0.0085  -0.0321 225 LYS A N   
1801 C  CA  . LYS A 224 ? 0.2825 0.2249 0.1677 -0.0446 0.0089  -0.0263 225 LYS A CA  
1802 C  C   . LYS A 224 ? 0.2727 0.2026 0.1326 -0.0300 0.0064  -0.0037 225 LYS A C   
1803 O  O   . LYS A 224 ? 0.2602 0.2179 0.1484 -0.0482 0.0074  -0.0158 225 LYS A O   
1804 C  CB  . LYS A 224 ? 0.3294 0.2435 0.2093 -0.0233 0.0097  0.0193  225 LYS A CB  
1805 C  CG  . LYS A 224 ? 0.4174 0.3651 0.2613 -0.0831 -0.0062 -0.0311 225 LYS A CG  
1806 C  CD  . LYS A 224 ? 0.4993 0.6423 0.3577 -0.1094 -0.1213 -0.0769 225 LYS A CD  
1807 C  CE  . LYS A 224 ? 0.7057 0.8771 0.4982 -0.1675 -0.0406 -0.2663 225 LYS A CE  
1808 N  NZ  . LYS A 224 ? 1.0817 0.5729 0.4357 -0.2429 0.1982  -0.0413 225 LYS A NZ  
1809 N  N   . PHE A 225 ? 0.2209 0.1810 0.1267 -0.0313 0.0046  -0.0048 226 PHE A N   
1810 C  CA  . PHE A 225 ? 0.2253 0.1678 0.1206 -0.0060 0.0186  -0.0208 226 PHE A CA  
1811 C  C   . PHE A 225 ? 0.1989 0.1961 0.1753 -0.0335 0.0232  0.0034  226 PHE A C   
1812 O  O   . PHE A 225 ? 0.2271 0.1965 0.1492 -0.0434 0.0391  -0.0216 226 PHE A O   
1813 C  CB  . PHE A 225 ? 0.2161 0.2127 0.1127 -0.0318 0.0201  -0.0293 226 PHE A CB  
1814 C  CG  . PHE A 225 ? 0.2118 0.1759 0.1537 -0.0297 0.0308  -0.0100 226 PHE A CG  
1815 C  CD1 . PHE A 225 ? 0.2476 0.2104 0.2099 0.0124  0.0165  0.0035  226 PHE A CD1 
1816 C  CD2 . PHE A 225 ? 0.2087 0.2492 0.1746 -0.0192 0.0337  -0.0494 226 PHE A CD2 
1817 C  CE1 . PHE A 225 ? 0.2458 0.2334 0.1856 -0.0198 0.0285  0.0074  226 PHE A CE1 
1818 C  CE2 . PHE A 225 ? 0.1603 0.2794 0.2442 -0.0089 0.0138  -0.0653 226 PHE A CE2 
1819 C  CZ  . PHE A 225 ? 0.2264 0.2257 0.2127 -0.0116 0.0032  -0.0414 226 PHE A CZ  
1820 N  N   . ARG A 226 ? 0.2112 0.1865 0.1456 0.0046  0.0182  -0.0154 227 ARG A N   
1821 C  CA  . ARG A 226 ? 0.1965 0.2246 0.1531 -0.0222 0.0178  0.0117  227 ARG A CA  
1822 C  C   . ARG A 226 ? 0.2440 0.1861 0.1461 -0.0297 0.0223  -0.0330 227 ARG A C   
1823 O  O   . ARG A 226 ? 0.2558 0.2859 0.1669 -0.0154 0.0495  -0.0253 227 ARG A O   
1824 C  CB  . ARG A 226 ? 0.2263 0.2052 0.1362 0.0091  0.0311  0.0022  227 ARG A CB  
1825 C  CG  . ARG A 226 ? 0.2504 0.1944 0.1362 -0.0157 0.0498  0.0159  227 ARG A CG  
1826 C  CD  . ARG A 226 ? 0.3004 0.1933 0.1405 -0.0219 0.0210  0.0245  227 ARG A CD  
1827 N  NE  . ARG A 226 ? 0.2349 0.1966 0.1623 -0.0480 0.0013  0.0065  227 ARG A NE  
1828 C  CZ  . ARG A 226 ? 0.2546 0.1569 0.1792 -0.0416 0.0473  -0.0530 227 ARG A CZ  
1829 N  NH1 . ARG A 226 ? 0.3432 0.2547 0.2323 -0.0756 0.0140  -0.1029 227 ARG A NH1 
1830 N  NH2 . ARG A 226 ? 0.2620 0.1993 0.1831 -0.0330 0.0507  -0.0127 227 ARG A NH2 
1831 N  N   . LYS A 227 ? 0.2183 0.2312 0.1253 -0.0301 0.0377  -0.0477 228 LYS A N   
1832 C  CA  . LYS A 227 ? 0.2950 0.2680 0.1231 -0.0818 0.0443  -0.0356 228 LYS A CA  
1833 C  C   . LYS A 227 ? 0.3274 0.2470 0.1116 -0.0629 0.0551  -0.0340 228 LYS A C   
1834 O  O   . LYS A 227 ? 0.3272 0.2583 0.1391 -0.0779 0.0650  -0.0521 228 LYS A O   
1835 C  CB  . LYS A 227 ? 0.2888 0.2741 0.1409 -0.0517 0.0260  -0.0275 228 LYS A CB  
1836 C  CG  . LYS A 227 ? 0.3644 0.3003 0.2084 -0.1152 0.0236  -0.0115 228 LYS A CG  
1837 C  CD  . LYS A 227 ? 0.3718 0.4317 0.2372 -0.0928 0.0222  -0.0347 228 LYS A CD  
1838 C  CE  . LYS A 227 ? 0.6265 0.7435 0.3865 0.0539  0.1110  -0.1629 228 LYS A CE  
1839 N  NZ  . LYS A 227 ? 0.4799 0.7787 1.0396 0.0696  -0.1463 -0.1562 228 LYS A NZ  
1840 N  N   . LEU A 228 ? 0.2658 0.2118 0.1387 -0.0530 0.0207  -0.0256 229 LEU A N   
1841 C  CA  . LEU A 228 ? 0.2478 0.2014 0.1583 -0.0337 0.0458  -0.0462 229 LEU A CA  
1842 C  C   . LEU A 228 ? 0.2766 0.2339 0.1483 -0.0355 0.0482  -0.0138 229 LEU A C   
1843 O  O   . LEU A 228 ? 0.2361 0.2177 0.1570 -0.0248 0.0456  -0.0262 229 LEU A O   
1844 C  CB  . LEU A 228 ? 0.2468 0.1955 0.1016 -0.0041 -0.0006 -0.0233 229 LEU A CB  
1845 C  CG  . LEU A 228 ? 0.2446 0.2158 0.1305 0.0149  -0.0233 -0.0167 229 LEU A CG  
1846 C  CD1 . LEU A 228 ? 0.2708 0.2293 0.1531 -0.0174 0.0161  -0.0499 229 LEU A CD1 
1847 C  CD2 . LEU A 228 ? 0.2767 0.2302 0.1653 -0.0442 0.0309  0.0148  229 LEU A CD2 
1848 N  N   . ASN A 229 ? 0.2271 0.2468 0.1402 -0.0398 0.0674  -0.0122 230 ASN A N   
1849 C  CA  . ASN A 229 ? 0.2084 0.2695 0.1253 -0.0239 0.0495  -0.0544 230 ASN A CA  
1850 C  C   . ASN A 229 ? 0.2508 0.2057 0.1638 -0.0072 0.0444  -0.0190 230 ASN A C   
1851 O  O   . ASN A 229 ? 0.2461 0.2233 0.1947 -0.0389 0.0467  -0.0326 230 ASN A O   
1852 C  CB  . ASN A 229 ? 0.3021 0.2685 0.1545 -0.0269 0.0880  -0.0212 230 ASN A CB  
1853 C  CG  . ASN A 229 ? 0.2745 0.2954 0.1968 -0.0356 0.0980  -0.0443 230 ASN A CG  
1854 O  OD1 . ASN A 229 ? 0.4472 0.3646 0.1960 -0.0234 0.1329  -0.0653 230 ASN A OD1 
1855 N  ND2 . ASN A 229 ? 0.3179 0.3062 0.2062 -0.0716 0.1209  -0.0734 230 ASN A ND2 
1856 N  N   . PHE A 230 ? 0.2187 0.2839 0.1340 -0.0842 0.0434  -0.0267 231 PHE A N   
1857 C  CA  . PHE A 230 ? 0.2501 0.2397 0.1377 -0.0655 0.0205  0.0087  231 PHE A CA  
1858 C  C   . PHE A 230 ? 0.2597 0.2888 0.1623 -0.0364 0.0723  0.0055  231 PHE A C   
1859 O  O   . PHE A 230 ? 0.2985 0.2867 0.1932 -0.0871 0.0812  -0.0173 231 PHE A O   
1860 C  CB  . PHE A 230 ? 0.2422 0.2400 0.1663 -0.0234 0.0361  0.0179  231 PHE A CB  
1861 C  CG  . PHE A 230 ? 0.2127 0.2464 0.1723 -0.0611 0.0475  -0.0172 231 PHE A CG  
1862 C  CD1 . PHE A 230 ? 0.2314 0.2428 0.1583 -0.0356 0.0278  -0.0089 231 PHE A CD1 
1863 C  CD2 . PHE A 230 ? 0.2906 0.2385 0.1588 -0.0271 0.0637  -0.0414 231 PHE A CD2 
1864 C  CE1 . PHE A 230 ? 0.2590 0.2249 0.1732 -0.0850 0.0272  -0.0065 231 PHE A CE1 
1865 C  CE2 . PHE A 230 ? 0.2698 0.2669 0.1620 -0.0496 0.0455  -0.0468 231 PHE A CE2 
1866 C  CZ  . PHE A 230 ? 0.1820 0.2720 0.1581 -0.0348 0.0434  -0.0199 231 PHE A CZ  
1867 N  N   . ASN A 231 ? 0.2248 0.2961 0.1382 -0.0321 0.0565  0.0184  232 ASN A N   
1868 C  CA  . ASN A 231 ? 0.2626 0.2644 0.1709 -0.0431 0.0881  0.0062  232 ASN A CA  
1869 C  C   . ASN A 231 ? 0.2584 0.3722 0.0899 -0.0243 0.0369  0.0067  232 ASN A C   
1870 O  O   . ASN A 231 ? 0.2888 0.2529 0.1964 -0.0273 0.0434  -0.0164 232 ASN A O   
1871 C  CB  . ASN A 231 ? 0.2459 0.3169 0.2300 -0.0632 0.1241  -0.0319 232 ASN A CB  
1872 C  CG  . ASN A 231 ? 0.2090 0.3180 0.2213 -0.0439 0.0581  0.0322  232 ASN A CG  
1873 O  OD1 . ASN A 231 ? 0.3620 0.3053 0.2002 -0.0836 0.1177  -0.0592 232 ASN A OD1 
1874 N  ND2 . ASN A 231 ? 0.2873 0.3213 0.1944 0.0427  0.0632  -0.0055 232 ASN A ND2 
1875 N  N   . GLY A 232 ? 0.3186 0.2454 0.1788 0.0168  0.0575  0.0179  233 GLY A N   
1876 C  CA  . GLY A 232 ? 0.3299 0.2795 0.1649 -0.0018 0.0229  0.0249  233 GLY A CA  
1877 C  C   . GLY A 232 ? 0.3292 0.2618 0.1919 0.0335  -0.0095 0.0064  233 GLY A C   
1878 O  O   . GLY A 232 ? 0.2971 0.2874 0.2145 0.0140  0.1227  0.0106  233 GLY A O   
1879 N  N   . GLU A 233 ? 0.2497 0.3398 0.1631 -0.0144 0.0418  0.0034  234 GLU A N   
1880 C  CA  . GLU A 233 ? 0.2722 0.3153 0.1754 0.0124  0.0316  -0.0021 234 GLU A CA  
1881 C  C   . GLU A 233 ? 0.2777 0.2964 0.1717 0.0375  0.0527  0.0158  234 GLU A C   
1882 O  O   . GLU A 233 ? 0.2429 0.3743 0.2271 0.0144  0.0578  0.0436  234 GLU A O   
1883 C  CB  . GLU A 233 ? 0.3218 0.3158 0.1894 0.0361  0.0121  0.0068  234 GLU A CB  
1884 C  CG  . GLU A 233 ? 0.3575 0.3671 0.1682 -0.0798 0.0210  0.0104  234 GLU A CG  
1885 C  CD  . GLU A 233 ? 0.5453 0.5088 0.3747 0.0974  -0.0783 -0.0363 234 GLU A CD  
1886 O  OE1 . GLU A 233 ? 0.5499 0.5136 0.3380 0.1243  0.0706  0.0381  234 GLU A OE1 
1887 O  OE2 . GLU A 233 ? 0.3794 0.6361 0.3003 -0.1093 -0.0315 0.0268  234 GLU A OE2 
1888 N  N   . GLY A 234 ? 0.3571 0.3347 0.2337 0.0864  0.1399  0.0210  235 GLY A N   
1889 C  CA  . GLY A 234 ? 0.2946 0.4843 0.2335 0.1129  0.0533  0.0207  235 GLY A CA  
1890 C  C   . GLY A 234 ? 0.3865 0.5001 0.2000 0.1967  0.0551  0.0285  235 GLY A C   
1891 O  O   . GLY A 234 ? 0.3753 0.6318 0.2737 0.2262  0.0964  -0.0179 235 GLY A O   
1892 N  N   . GLU A 235 ? 0.3445 0.4656 0.2051 0.1444  0.0603  0.0526  236 GLU A N   
1893 C  CA  . GLU A 235 ? 0.3125 0.3755 0.2113 0.1114  0.0051  -0.0252 236 GLU A CA  
1894 C  C   . GLU A 235 ? 0.3171 0.4462 0.2662 0.0411  0.0397  -0.0069 236 GLU A C   
1895 O  O   . GLU A 235 ? 0.3053 0.4253 0.2547 0.0425  0.0311  -0.0075 236 GLU A O   
1896 C  CB  . GLU A 235 ? 0.2968 0.3334 0.2384 -0.0167 0.0546  -0.0506 236 GLU A CB  
1897 C  CG  . GLU A 235 ? 0.4375 0.3291 0.3686 -0.0858 0.1397  -0.0864 236 GLU A CG  
1898 C  CD  . GLU A 235 ? 0.5956 0.4902 0.4347 -0.1819 0.2958  -0.1472 236 GLU A CD  
1899 O  OE1 . GLU A 235 ? 0.4198 0.5250 0.5365 -0.2078 0.2073  -0.0310 236 GLU A OE1 
1900 O  OE2 . GLU A 235 ? 0.5516 0.6091 0.6492 -0.2619 0.1644  0.0131  236 GLU A OE2 
1901 N  N   . PRO A 236 ? 0.2354 0.3625 0.2156 0.0100  0.1009  -0.0212 237 PRO A N   
1902 C  CA  . PRO A 236 ? 0.2824 0.3737 0.2080 -0.0542 0.0620  0.0158  237 PRO A CA  
1903 C  C   . PRO A 236 ? 0.2842 0.3610 0.1634 -0.0184 0.0603  -0.0274 237 PRO A C   
1904 O  O   . PRO A 236 ? 0.2892 0.3378 0.1941 0.0125  0.0526  0.0030  237 PRO A O   
1905 C  CB  . PRO A 236 ? 0.2174 0.3721 0.2680 0.0039  0.0954  0.0085  237 PRO A CB  
1906 C  CG  . PRO A 236 ? 0.2504 0.3320 0.2759 0.0038  0.0493  0.0617  237 PRO A CG  
1907 C  CD  . PRO A 236 ? 0.2738 0.3850 0.3290 0.0102  0.0257  0.0239  237 PRO A CD  
1908 N  N   . GLU A 237 ? 0.2564 0.2819 0.2194 -0.0008 0.0798  -0.0176 238 GLU A N   
1909 C  CA  . GLU A 237 ? 0.3057 0.2942 0.2115 -0.0308 0.1135  -0.0439 238 GLU A CA  
1910 C  C   . GLU A 237 ? 0.2569 0.3204 0.2202 0.0037  0.0968  -0.0341 238 GLU A C   
1911 O  O   . GLU A 237 ? 0.2776 0.2884 0.1990 -0.0006 0.0449  -0.0433 238 GLU A O   
1912 C  CB  . GLU A 237 ? 0.1998 0.3972 0.3212 0.0052  0.0535  -0.1273 238 GLU A CB  
1913 C  CG  . GLU A 237 ? 0.2140 0.5028 0.4375 -0.0449 0.0863  -0.0910 238 GLU A CG  
1914 C  CD  . GLU A 237 ? 0.4128 0.7844 0.3861 -0.0387 0.0269  -0.2324 238 GLU A CD  
1915 O  OE1 . GLU A 237 ? 0.5759 0.7683 0.4016 -0.0458 0.0420  -0.2652 238 GLU A OE1 
1916 O  OE2 . GLU A 237 ? 0.4896 0.3755 0.3031 -0.0706 0.1364  -0.1418 238 GLU A OE2 
1917 N  N   . GLU A 238 ? 0.2072 0.3575 0.1851 -0.0312 0.1072  -0.0451 239 GLU A N   
1918 C  CA  . GLU A 238 ? 0.1871 0.3528 0.2192 -0.0666 0.0795  0.0036  239 GLU A CA  
1919 C  C   . GLU A 238 ? 0.1962 0.2764 0.1822 -0.0102 0.0936  -0.0122 239 GLU A C   
1920 O  O   . GLU A 238 ? 0.2638 0.2590 0.2312 -0.0384 0.0932  -0.0337 239 GLU A O   
1921 C  CB  . GLU A 238 ? 0.2594 0.3855 0.2654 -0.0981 0.0357  -0.0084 239 GLU A CB  
1922 C  CG  . GLU A 238 ? 0.3330 0.5229 0.3935 0.0253  -0.0905 0.1030  239 GLU A CG  
1923 C  CD  . GLU A 238 ? 0.3603 0.6120 0.5424 0.0819  0.1059  0.1032  239 GLU A CD  
1924 O  OE1 . GLU A 238 ? 0.3116 1.1371 0.6876 0.2881  0.1305  -0.0928 239 GLU A OE1 
1925 O  OE2 . GLU A 238 ? 0.3122 0.6898 0.8622 0.1209  0.0877  0.3274  239 GLU A OE2 
1926 N  N   . LEU A 239 ? 0.2601 0.3017 0.1598 -0.0477 0.0815  -0.0458 240 LEU A N   
1927 C  CA  . LEU A 239 ? 0.2370 0.2089 0.1718 -0.0366 0.0682  -0.0497 240 LEU A CA  
1928 C  C   . LEU A 239 ? 0.2247 0.1799 0.1656 -0.0017 0.0540  -0.0297 240 LEU A C   
1929 O  O   . LEU A 239 ? 0.2503 0.2827 0.1495 -0.0166 0.0609  -0.0418 240 LEU A O   
1930 C  CB  . LEU A 239 ? 0.2240 0.1872 0.2179 0.0111  0.0285  -0.0510 240 LEU A CB  
1931 C  CG  . LEU A 239 ? 0.2293 0.2136 0.2308 0.0196  0.0239  -0.0834 240 LEU A CG  
1932 C  CD1 . LEU A 239 ? 0.2079 0.2068 0.4314 0.0183  -0.0068 -0.0744 240 LEU A CD1 
1933 C  CD2 . LEU A 239 ? 0.2953 0.2709 0.2271 0.0165  -0.0121 -0.0809 240 LEU A CD2 
1934 N  N   . MET A 240 ? 0.2131 0.2106 0.1409 0.0122  0.0562  -0.0173 241 MET A N   
1935 C  CA  . MET A 240 ? 0.2104 0.2130 0.1081 0.0025  0.0650  -0.0016 241 MET A CA  
1936 C  C   . MET A 240 ? 0.1876 0.2289 0.1391 -0.0258 0.0564  -0.0247 241 MET A C   
1937 O  O   . MET A 240 ? 0.1966 0.2227 0.1534 -0.0211 0.0487  -0.0201 241 MET A O   
1938 C  CB  . MET A 240 ? 0.2271 0.2184 0.1624 0.0027  0.0527  -0.0309 241 MET A CB  
1939 C  CG  . MET A 240 ? 0.1948 0.2381 0.1215 -0.0282 0.0431  -0.0304 241 MET A CG  
1940 S  SD  . MET A 240 ? 0.2812 0.1840 0.1745 -0.0245 0.0741  -0.0167 241 MET A SD  
1941 C  CE  . MET A 240 ? 0.2691 0.2303 0.1493 -0.0664 0.0717  0.0075  241 MET A CE  
1942 N  N   . VAL A 241 ? 0.1887 0.1896 0.1452 -0.0152 0.0608  -0.0098 242 VAL A N   
1943 C  CA  . VAL A 241 ? 0.2238 0.1725 0.1253 -0.0521 0.0397  -0.0458 242 VAL A CA  
1944 C  C   . VAL A 241 ? 0.1757 0.1626 0.1296 0.0024  0.0268  -0.0322 242 VAL A C   
1945 O  O   . VAL A 241 ? 0.1689 0.2030 0.1556 -0.0146 0.0466  -0.0280 242 VAL A O   
1946 C  CB  . VAL A 241 ? 0.1695 0.1883 0.2045 -0.0411 0.0274  -0.0873 242 VAL A CB  
1947 C  CG1 . VAL A 241 ? 0.2209 0.1961 0.1926 -0.0301 0.0137  -0.0413 242 VAL A CG1 
1948 C  CG2 . VAL A 241 ? 0.2107 0.2088 0.1907 0.0150  0.0447  -0.0270 242 VAL A CG2 
1949 N  N   . ASP A 242 ? 0.1736 0.1524 0.1177 0.0078  0.0379  -0.0296 243 ASP A N   
1950 C  CA  . ASP A 242 ? 0.1504 0.1495 0.1441 -0.0040 0.0245  -0.0270 243 ASP A CA  
1951 C  C   . ASP A 242 ? 0.1355 0.1409 0.1312 -0.0155 0.0234  -0.0348 243 ASP A C   
1952 O  O   . ASP A 242 ? 0.1326 0.1603 0.2168 -0.0037 -0.0029 -0.0419 243 ASP A O   
1953 C  CB  . ASP A 242 ? 0.1624 0.1441 0.1879 0.0133  0.0190  -0.0129 243 ASP A CB  
1954 C  CG  . ASP A 242 ? 0.1857 0.1359 0.1718 0.0115  0.0355  -0.0084 243 ASP A CG  
1955 O  OD1 . ASP A 242 ? 0.1797 0.1547 0.1703 -0.0173 0.0283  -0.0331 243 ASP A OD1 
1956 O  OD2 . ASP A 242 ? 0.2086 0.1807 0.2332 0.0243  0.0330  -0.0570 243 ASP A OD2 
1957 N  N   . ASN A 243 ? 0.1383 0.1280 0.1303 0.0011  0.0339  -0.0230 244 ASN A N   
1958 C  CA  . ASN A 243 ? 0.1362 0.1386 0.1168 -0.0046 0.0255  -0.0131 244 ASN A CA  
1959 C  C   . ASN A 243 ? 0.1135 0.1430 0.1309 -0.0070 0.0201  -0.0214 244 ASN A C   
1960 O  O   . ASN A 243 ? 0.1423 0.1612 0.1368 0.0201  0.0278  -0.0033 244 ASN A O   
1961 C  CB  . ASN A 243 ? 0.1179 0.1802 0.1274 -0.0027 0.0307  0.0093  244 ASN A CB  
1962 C  CG  . ASN A 243 ? 0.1183 0.1650 0.1303 -0.0143 0.0468  -0.0143 244 ASN A CG  
1963 O  OD1 . ASN A 243 ? 0.1321 0.1943 0.1555 -0.0275 0.0223  0.0225  244 ASN A OD1 
1964 N  ND2 . ASN A 243 ? 0.1491 0.1826 0.1966 -0.0179 0.0082  0.0228  244 ASN A ND2 
1965 N  N   . TRP A 244 ? 0.1315 0.1440 0.1039 -0.0141 0.0206  -0.0174 245 TRP A N   
1966 C  CA  . TRP A 244 ? 0.1091 0.1673 0.1100 0.0038  0.0303  -0.0102 245 TRP A CA  
1967 C  C   . TRP A 244 ? 0.1208 0.1477 0.1207 0.0026  0.0215  -0.0089 245 TRP A C   
1968 O  O   . TRP A 244 ? 0.1153 0.1519 0.1691 0.0075  0.0064  -0.0333 245 TRP A O   
1969 C  CB  . TRP A 244 ? 0.1343 0.1316 0.1286 -0.0094 0.0240  -0.0122 245 TRP A CB  
1970 C  CG  . TRP A 244 ? 0.1050 0.1315 0.1391 -0.0048 0.0165  -0.0027 245 TRP A CG  
1971 C  CD1 . TRP A 244 ? 0.1161 0.1306 0.1526 -0.0079 0.0262  -0.0137 245 TRP A CD1 
1972 C  CD2 . TRP A 244 ? 0.1132 0.1434 0.1277 -0.0027 0.0339  -0.0037 245 TRP A CD2 
1973 N  NE1 . TRP A 244 ? 0.1161 0.1432 0.1524 -0.0118 0.0172  0.0068  245 TRP A NE1 
1974 C  CE2 . TRP A 244 ? 0.1366 0.1432 0.1491 0.0074  0.0142  -0.0060 245 TRP A CE2 
1975 C  CE3 . TRP A 244 ? 0.1329 0.1930 0.1344 -0.0024 0.0064  0.0212  245 TRP A CE3 
1976 C  CZ2 . TRP A 244 ? 0.1790 0.1703 0.1549 0.0084  0.0232  0.0094  245 TRP A CZ2 
1977 C  CZ3 . TRP A 244 ? 0.1890 0.1908 0.1379 0.0287  -0.0049 0.0032  245 TRP A CZ3 
1978 C  CH2 . TRP A 244 ? 0.1918 0.1874 0.1606 0.0353  0.0163  -0.0043 245 TRP A CH2 
1979 N  N   . ARG A 245 ? 0.0874 0.1601 0.1348 -0.0004 0.0164  -0.0301 246 ARG A N   
1980 C  CA  . ARG A 245 ? 0.1048 0.1436 0.1445 0.0046  0.0020  -0.0122 246 ARG A CA  
1981 C  C   . ARG A 245 ? 0.1220 0.1577 0.1351 0.0118  0.0117  -0.0159 246 ARG A C   
1982 O  O   . ARG A 245 ? 0.1252 0.1901 0.1517 -0.0067 0.0209  -0.0340 246 ARG A O   
1983 C  CB  . ARG A 245 ? 0.0924 0.1644 0.1576 0.0005  0.0067  -0.0365 246 ARG A CB  
1984 C  CG  . ARG A 245 ? 0.1090 0.1409 0.1537 -0.0088 -0.0016 -0.0257 246 ARG A CG  
1985 C  CD  . ARG A 245 ? 0.1004 0.1650 0.1608 -0.0140 -0.0125 -0.0419 246 ARG A CD  
1986 N  NE  . ARG A 245 ? 0.0944 0.1760 0.1443 -0.0145 0.0076  -0.0359 246 ARG A NE  
1987 C  CZ  . ARG A 245 ? 0.0828 0.1549 0.1619 -0.0260 0.0071  -0.0413 246 ARG A CZ  
1988 N  NH1 . ARG A 245 ? 0.1277 0.1707 0.1648 0.0034  0.0270  -0.0200 246 ARG A NH1 
1989 N  NH2 . ARG A 245 ? 0.1014 0.2117 0.2072 -0.0453 -0.0156 -0.0223 246 ARG A NH2 
1990 N  N   . PRO A 246 ? 0.1566 0.1513 0.1343 0.0122  0.0084  -0.0215 247 PRO A N   
1991 C  CA  . PRO A 246 ? 0.1577 0.1624 0.1488 0.0083  0.0032  -0.0078 247 PRO A CA  
1992 C  C   . PRO A 246 ? 0.1822 0.1463 0.1544 0.0418  0.0300  0.0021  247 PRO A C   
1993 O  O   . PRO A 246 ? 0.1468 0.1635 0.1656 0.0073  -0.0009 -0.0238 247 PRO A O   
1994 C  CB  . PRO A 246 ? 0.2598 0.2384 0.1914 0.1218  -0.0150 -0.0054 247 PRO A CB  
1995 C  CG  . PRO A 246 ? 0.2352 0.2647 0.2910 0.0469  0.0267  0.0803  247 PRO A CG  
1996 C  CD  . PRO A 246 ? 0.1486 0.1982 0.2234 0.0378  0.0162  0.0153  247 PRO A CD  
1997 N  N   . ALA A 247 ? 0.1652 0.1825 0.1473 -0.0021 0.0209  0.0048  248 ALA A N   
1998 C  CA  . ALA A 247 ? 0.1689 0.1638 0.1380 0.0176  -0.0039 -0.0129 248 ALA A CA  
1999 C  C   . ALA A 247 ? 0.1656 0.1563 0.1470 0.0306  0.0060  0.0201  248 ALA A C   
2000 O  O   . ALA A 247 ? 0.1858 0.1863 0.1828 0.0633  -0.0100 0.0071  248 ALA A O   
2001 C  CB  . ALA A 247 ? 0.2198 0.2095 0.1542 0.0171  0.0172  0.0249  248 ALA A CB  
2002 N  N   . GLN A 248 ? 0.1269 0.1660 0.1631 0.0060  -0.0061 -0.0052 249 GLN A N   
2003 C  CA  . GLN A 248 ? 0.1376 0.1842 0.1614 0.0000  -0.0207 -0.0103 249 GLN A CA  
2004 C  C   . GLN A 248 ? 0.1725 0.1674 0.1635 0.0262  -0.0363 -0.0086 249 GLN A C   
2005 O  O   . GLN A 248 ? 0.1767 0.2041 0.1691 0.0253  -0.0117 -0.0013 249 GLN A O   
2006 C  CB  . GLN A 248 ? 0.1689 0.1861 0.1709 0.0097  0.0104  0.0116  249 GLN A CB  
2007 C  CG  . GLN A 248 ? 0.1750 0.1822 0.1721 0.0185  0.0148  0.0158  249 GLN A CG  
2008 C  CD  . GLN A 248 ? 0.1419 0.2235 0.2186 -0.0094 -0.0171 -0.0227 249 GLN A CD  
2009 O  OE1 . GLN A 248 ? 0.1570 0.2975 0.2393 -0.0460 -0.0157 -0.0258 249 GLN A OE1 
2010 N  NE2 . GLN A 248 ? 0.1752 0.2357 0.2066 0.0197  -0.0065 -0.0027 249 GLN A NE2 
2011 N  N   . PRO A 249 ? 0.1616 0.2655 0.1836 0.0599  -0.0403 -0.0392 250 PRO A N   
2012 C  CA  . PRO A 249 ? 0.2018 0.3097 0.1782 0.0917  -0.0222 -0.0201 250 PRO A CA  
2013 C  C   . PRO A 249 ? 0.2047 0.2124 0.1303 0.0543  -0.0406 0.0098  250 PRO A C   
2014 O  O   . PRO A 249 ? 0.1821 0.2332 0.1714 0.0467  -0.0418 -0.0125 250 PRO A O   
2015 C  CB  . PRO A 249 ? 0.2422 0.4313 0.2409 0.1402  -0.1086 -0.0987 250 PRO A CB  
2016 C  CG  . PRO A 249 ? 0.2392 0.4106 0.2253 0.0176  -0.0804 -0.0286 250 PRO A CG  
2017 C  CD  . PRO A 249 ? 0.1316 0.3881 0.2330 0.0582  -0.0469 -0.0479 250 PRO A CD  
2018 N  N   . LEU A 250 ? 0.2141 0.2710 0.1306 0.0455  -0.0097 -0.0088 251 LEU A N   
2019 C  CA  . LEU A 250 ? 0.1747 0.2638 0.1423 0.0287  -0.0073 -0.0278 251 LEU A CA  
2020 C  C   . LEU A 250 ? 0.2073 0.2126 0.1466 0.0184  -0.0359 0.0095  251 LEU A C   
2021 O  O   . LEU A 250 ? 0.2253 0.2263 0.1720 0.0276  -0.0414 -0.0173 251 LEU A O   
2022 C  CB  . LEU A 250 ? 0.2460 0.2939 0.1660 0.0033  0.0138  -0.0027 251 LEU A CB  
2023 C  CG  . LEU A 250 ? 0.2467 0.2519 0.1486 -0.0055 0.0545  -0.0047 251 LEU A CG  
2024 C  CD1 . LEU A 250 ? 0.2514 0.3172 0.1333 -0.0226 0.0121  -0.0241 251 LEU A CD1 
2025 C  CD2 . LEU A 250 ? 0.3373 0.3101 0.2170 -0.0827 0.0767  -0.0080 251 LEU A CD2 
2026 N  N   . LYS A 251 ? 0.2476 0.3301 0.1456 0.0615  -0.0522 -0.0354 252 LYS A N   
2027 C  CA  . LYS A 251 ? 0.2756 0.4110 0.1441 0.0847  -0.0713 -0.0818 252 LYS A CA  
2028 C  C   . LYS A 251 ? 0.3121 0.4616 0.1398 0.0717  -0.0566 -0.0924 252 LYS A C   
2029 O  O   . LYS A 251 ? 0.4117 0.5802 0.2515 -0.0029 0.0337  -0.0832 252 LYS A O   
2030 C  CB  . LYS A 251 ? 0.3141 0.3811 0.2400 0.0790  -0.0861 -0.1020 252 LYS A CB  
2031 C  CG  . LYS A 251 ? 0.3798 0.3419 0.2514 0.0068  0.0253  -0.1055 252 LYS A CG  
2032 C  CD  . LYS A 251 ? 0.3155 0.5611 0.4602 0.0127  0.0779  -0.0302 252 LYS A CD  
2033 C  CE  . LYS A 251 ? 0.3146 0.4740 0.4552 0.0908  -0.0743 -0.0584 252 LYS A CE  
2034 N  NZ  . LYS A 251 ? 0.5655 0.3815 0.6013 -0.0079 -0.0422 -0.0704 252 LYS A NZ  
2035 N  N   . ASN A 252 ? 0.1962 0.4523 0.2648 0.0859  -0.0776 -0.1591 253 ASN A N   
2036 C  CA  . ASN A 252 ? 0.2217 0.8277 0.5156 0.2080  0.1022  -0.0319 253 ASN A CA  
2037 C  C   . ASN A 252 ? 0.2529 0.7400 0.1846 0.0920  0.0148  -0.1261 253 ASN A C   
2038 O  O   . ASN A 252 ? 0.3589 0.7906 0.1533 0.2278  0.0086  -0.0563 253 ASN A O   
2039 C  CB  . ASN A 252 ? 1.3926 1.0511 0.7953 -0.4734 -0.1205 -0.6498 253 ASN A CB  
2040 C  CG  . ASN A 252 ? 0.7653 1.0774 1.2512 0.0436  0.3396  -0.3212 253 ASN A CG  
2041 O  OD1 . ASN A 252 ? 1.2513 1.3660 0.9312 0.0732  -0.8823 0.1405  253 ASN A OD1 
2042 N  ND2 . ASN A 252 ? 2.1318 0.8471 1.1743 -0.5400 0.3050  -0.1539 253 ASN A ND2 
2043 N  N   . ARG A 253 ? 0.1868 0.3477 0.1477 0.0464  0.0006  -0.0190 254 ARG A N   
2044 C  CA  . ARG A 253 ? 0.1759 0.2638 0.1296 0.0203  0.0048  -0.0186 254 ARG A CA  
2045 C  C   . ARG A 253 ? 0.2274 0.2308 0.1553 0.0140  0.0275  -0.0418 254 ARG A C   
2046 O  O   . ARG A 253 ? 0.3416 0.2433 0.2751 0.0450  0.0951  0.0157  254 ARG A O   
2047 C  CB  . ARG A 253 ? 0.1707 0.2005 0.1409 0.0219  0.0060  0.0120  254 ARG A CB  
2048 C  CG  . ARG A 253 ? 0.2283 0.2055 0.1312 -0.0066 0.0190  -0.0053 254 ARG A CG  
2049 C  CD  . ARG A 253 ? 0.1713 0.2133 0.1278 0.0291  0.0160  -0.0226 254 ARG A CD  
2050 N  NE  . ARG A 253 ? 0.1621 0.1929 0.1556 0.0229  0.0024  -0.0223 254 ARG A NE  
2051 C  CZ  . ARG A 253 ? 0.1383 0.1648 0.1365 0.0152  0.0131  0.0008  254 ARG A CZ  
2052 N  NH1 . ARG A 253 ? 0.1258 0.1929 0.1317 -0.0059 -0.0219 -0.0058 254 ARG A NH1 
2053 N  NH2 . ARG A 253 ? 0.1474 0.1520 0.1509 0.0117  -0.0188 -0.0228 254 ARG A NH2 
2054 N  N   . GLN A 254 ? 0.1865 0.2605 0.1718 0.0133  -0.0156 -0.0495 255 GLN A N   
2055 C  CA  . GLN A 254 ? 0.2000 0.3475 0.1628 -0.0122 -0.0370 -0.0693 255 GLN A CA  
2056 C  C   . GLN A 254 ? 0.2224 0.2029 0.1637 -0.0008 -0.0278 -0.0154 255 GLN A C   
2057 O  O   . GLN A 254 ? 0.3559 0.2115 0.2223 0.0039  -0.0800 -0.0086 255 GLN A O   
2058 C  CB  . GLN A 254 ? 0.3710 0.3829 0.1359 -0.0508 0.0418  -0.0850 255 GLN A CB  
2059 C  CG  . GLN A 254 ? 0.5259 0.7465 0.2044 0.0249  -0.0243 -0.0664 255 GLN A CG  
2060 C  CD  . GLN A 254 ? 0.6914 1.0348 0.3291 0.0043  0.1241  -0.0691 255 GLN A CD  
2061 O  OE1 . GLN A 254 ? 0.7544 1.4239 0.3941 -0.1132 0.1791  -0.2733 255 GLN A OE1 
2062 N  NE2 . GLN A 254 ? 0.5704 0.9942 0.4124 0.1960  -0.0622 -0.0323 255 GLN A NE2 
2063 N  N   . ILE A 255 ? 0.1797 0.2161 0.1287 -0.0036 0.0021  -0.0091 256 ILE A N   
2064 C  CA  . ILE A 255 ? 0.1736 0.1978 0.1153 0.0171  0.0040  -0.0044 256 ILE A CA  
2065 C  C   . ILE A 255 ? 0.1930 0.1896 0.1276 0.0185  0.0234  0.0192  256 ILE A C   
2066 O  O   . ILE A 255 ? 0.2148 0.2059 0.1533 0.0257  0.0285  0.0413  256 ILE A O   
2067 C  CB  . ILE A 255 ? 0.1693 0.1900 0.1390 0.0023  0.0031  -0.0153 256 ILE A CB  
2068 C  CG1 . ILE A 255 ? 0.1741 0.2140 0.1767 0.0496  0.0247  -0.0210 256 ILE A CG1 
2069 C  CG2 . ILE A 255 ? 0.1874 0.2515 0.1382 0.0452  -0.0023 -0.0062 256 ILE A CG2 
2070 C  CD1 . ILE A 255 ? 0.2284 0.2414 0.1771 -0.0138 0.0444  -0.0320 256 ILE A CD1 
2071 N  N   . LYS A 256 ? 0.1635 0.2072 0.1445 0.0255  0.0164  0.0054  257 LYS A N   
2072 C  CA  . LYS A 256 ? 0.1743 0.1914 0.1250 0.0352  0.0177  -0.0061 257 LYS A CA  
2073 C  C   . LYS A 256 ? 0.1752 0.2169 0.1259 0.0116  0.0205  0.0036  257 LYS A C   
2074 O  O   . LYS A 256 ? 0.2106 0.2685 0.1163 -0.0334 0.0225  0.0030  257 LYS A O   
2075 C  CB  . LYS A 256 ? 0.2493 0.1968 0.1764 0.0281  0.0336  -0.0343 257 LYS A CB  
2076 C  CG  . LYS A 256 ? 0.3650 0.2652 0.2763 -0.0302 0.0095  -0.1040 257 LYS A CG  
2077 C  CD  . LYS A 256 ? 0.5912 0.2924 0.6003 0.0397  -0.0443 -0.1859 257 LYS A CD  
2078 C  CE  . LYS A 256 ? 0.8047 0.5691 0.7992 -0.2260 -0.1086 -0.3304 257 LYS A CE  
2079 N  NZ  . LYS A 256 ? 1.1360 0.6229 0.7808 0.0272  -0.5204 -0.2716 257 LYS A NZ  
2080 N  N   . ALA A 257 ? 0.1757 0.2534 0.1328 0.0188  0.0370  0.0329  258 ALA A N   
2081 C  CA  . ALA A 257 ? 0.1645 0.2539 0.1351 0.0303  0.0295  0.0460  258 ALA A CA  
2082 C  C   . ALA A 257 ? 0.1942 0.1961 0.1418 0.0259  0.0652  0.0322  258 ALA A C   
2083 O  O   . ALA A 257 ? 0.1775 0.2691 0.1472 0.0244  0.0532  0.0038  258 ALA A O   
2084 C  CB  . ALA A 257 ? 0.1965 0.2291 0.1948 0.0305  0.0592  0.0413  258 ALA A CB  
2085 N  N   . SER A 258 ? 0.1829 0.1929 0.1782 0.0065  0.0357  0.0325  259 SER A N   
2086 C  CA  . SER A 258 ? 0.1876 0.2447 0.1882 0.0197  0.0472  0.0302  259 SER A CA  
2087 C  C   . SER A 258 ? 0.1850 0.2666 0.1764 0.0194  0.0851  -0.0008 259 SER A C   
2088 O  O   . SER A 258 ? 0.2022 0.3513 0.2893 0.0560  0.1033  -0.0220 259 SER A O   
2089 C  CB  . SER A 258 ? 0.2192 0.1950 0.1987 0.0106  0.0053  0.0190  259 SER A CB  
2090 O  OG  . SER A 258 ? 0.1747 0.2554 0.1782 0.0037  0.0539  0.0050  259 SER A OG  
2091 N  N   . PHE A 259 ? 0.1846 0.2688 0.2271 -0.0320 0.0712  0.0159  260 PHE A N   
2092 C  CA  . PHE A 259 ? 0.1829 0.2823 0.2712 -0.0424 0.0651  -0.0006 260 PHE A CA  
2093 C  C   . PHE A 259 ? 0.2845 0.3326 0.2849 -0.0573 0.0904  0.0187  260 PHE A C   
2094 O  O   . PHE A 259 ? 0.3154 0.3233 0.2428 -0.0656 0.0657  0.0511  260 PHE A O   
2095 C  CB  . PHE A 259 ? 0.2391 0.2522 0.3040 -0.0201 0.0679  -0.0063 260 PHE A CB  
2096 C  CG  . PHE A 259 ? 0.1736 0.2909 0.2573 -0.0029 0.0394  0.0710  260 PHE A CG  
2097 C  CD1 . PHE A 259 ? 0.1434 0.2637 0.2174 -0.0256 0.0300  0.0034  260 PHE A CD1 
2098 C  CD2 . PHE A 259 ? 0.2514 0.2708 0.4001 -0.0312 0.0205  0.0851  260 PHE A CD2 
2099 C  CE1 . PHE A 259 ? 0.2158 0.2889 0.2389 0.0179  0.0562  -0.0128 260 PHE A CE1 
2100 C  CE2 . PHE A 259 ? 0.3101 0.3240 0.4188 -0.0182 0.0917  0.0244  260 PHE A CE2 
2101 C  CZ  . PHE A 259 ? 0.2242 0.2619 0.4749 -0.0106 0.0647  -0.0400 260 PHE A CZ  
2102 N  N   . LYS A 260 ? 0.4528 0.5035 0.3596 -0.2061 0.1249  0.0505  261 LYS A N   
2103 C  CA  . LYS A 260 ? 0.7898 0.5669 0.4449 -0.0469 0.0403  0.1641  261 LYS A CA  
2104 C  C   . LYS A 260 ? 0.7741 0.6646 0.4311 -0.0125 -0.0234 0.1854  261 LYS A C   
2105 O  O   . LYS A 260 ? 0.9771 1.1212 1.0976 0.0276  -0.3820 0.2265  261 LYS A O   
2106 C  CB  . LYS A 260 ? 0.8400 0.4335 0.6035 -0.0355 0.1786  0.3167  261 LYS A CB  
2107 C  CG  . LYS A 260 ? 0.9618 0.5977 0.9775 -0.3796 0.2685  -0.0402 261 LYS A CG  
2108 C  CD  . LYS A 260 ? 1.2703 0.6600 0.9618 -0.1287 0.2277  -0.3792 261 LYS A CD  
2109 C  CE  . LYS A 260 ? 0.8945 1.0511 0.9316 0.0905  0.4737  -0.1470 261 LYS A CE  
2110 N  NZ  . LYS A 260 ? 0.7868 1.1207 0.7610 -0.0266 0.4500  -0.1394 261 LYS A NZ  
2111 O  OXT . LYS A 260 ? 0.5440 0.9089 0.9414 -0.0713 0.0226  0.0894  261 LYS A OXT 
2112 ZN ZN  . ZN  B .   ? 0.1050 0.1284 0.1126 -0.0081 0.0044  -0.0059 301 ZN  A ZN  
2113 O  O1  . MES C .   ? 0.7158 0.4828 0.3536 -0.0431 0.0335  0.1000  302 MES A O1  
2114 C  C2  . MES C .   ? 0.3255 0.5610 0.3819 0.0840  0.0277  0.0424  302 MES A C2  
2115 C  C3  . MES C .   ? 0.5019 0.5949 0.5474 -0.1571 -0.0118 0.0293  302 MES A C3  
2116 N  N4  . MES C .   ? 0.5266 0.3068 0.4439 -0.0259 -0.0209 0.0194  302 MES A N4  
2117 C  C5  . MES C .   ? 0.4428 0.3076 0.5313 0.0328  0.0768  -0.0405 302 MES A C5  
2118 C  C6  . MES C .   ? 0.5888 0.2929 0.2396 0.0233  -0.0798 0.0372  302 MES A C6  
2119 C  C7  . MES C .   ? 0.6937 0.4356 0.6785 -0.2283 -0.2395 0.2212  302 MES A C7  
2120 S  S   . DMS D .   ? 0.2471 0.2988 0.2715 -0.0087 0.0094  -0.0238 303 DMS A S   
2121 O  O   . DMS D .   ? 0.3507 0.3556 0.4127 0.0557  0.0780  -0.1142 303 DMS A O   
2122 C  C1  . DMS D .   ? 0.2618 0.2461 0.4504 -0.0633 -0.0001 -0.0447 303 DMS A C1  
2123 C  C2  . DMS D .   ? 0.2860 0.3107 0.2339 0.0425  0.0366  0.0248  303 DMS A C2  
2124 N  N1  . BCN E .   ? 0.7263 0.4020 0.5515 0.0688  -0.0614 0.0234  304 BCN A N1  
2125 C  C1  . BCN E .   ? 0.2606 0.3635 0.1929 0.0006  0.1045  0.0458  304 BCN A C1  
2126 C  C2  . BCN E .   ? 0.5225 0.6552 0.5055 0.1954  -0.0751 0.0737  304 BCN A C2  
2127 O  O21 . BCN E .   ? 0.4595 0.5705 0.4273 0.1069  0.1349  0.2927  304 BCN A O21 
2128 O  O22 . BCN E .   ? 0.8870 0.6029 0.2233 0.2161  0.1349  0.1079  304 BCN A O22 
2129 C  C3  . BCN E .   ? 0.4946 0.9187 0.1975 -0.1715 0.0784  -0.0105 304 BCN A C3  
2130 C  C4  . BCN E .   ? 0.9493 0.3438 0.9252 -0.2128 0.1395  -0.4115 304 BCN A C4  
2131 O  O4  . BCN E .   ? 0.2878 0.3151 0.9001 0.0348  0.2278  -0.1208 304 BCN A O4  
2132 C  C5  . BCN E .   ? 0.4195 0.7440 0.7432 -0.1243 -0.1566 0.0468  304 BCN A C5  
2133 C  C6  . BCN E .   ? 0.5824 0.3744 0.4415 0.1358  -0.1888 -0.1538 304 BCN A C6  
2134 O  O6  . BCN E .   ? 0.4963 0.6328 0.6212 -0.1202 0.0155  0.2487  304 BCN A O6  
2135 C  C1  . EDO F .   ? 0.2979 0.5606 0.4221 -0.1640 0.0747  -0.0620 305 EDO A C1  
2136 O  O1  . EDO F .   ? 0.2838 0.6409 0.5416 0.0420  0.1344  -0.1180 305 EDO A O1  
2137 C  C2  . EDO F .   ? 0.5169 0.3887 0.4777 -0.2258 -0.1923 0.1539  305 EDO A C2  
2138 O  O2  . EDO F .   ? 0.2972 0.3377 0.3883 -0.0326 0.0379  -0.0421 305 EDO A O2  
2139 N  N1  . EZL G .   ? 0.0930 0.1258 0.1481 -0.0196 0.0135  -0.0171 306 EZL A N1  
2140 C  C2  . EZL G .   ? 0.1336 0.1366 0.1713 -0.0120 0.0074  -0.0092 306 EZL A C2  
2141 C  C3  . EZL G .   ? 0.1101 0.1779 0.1720 -0.0084 0.0092  -0.0036 306 EZL A C3  
2142 C  C4  . EZL G .   ? 0.1599 0.1914 0.1969 -0.0147 0.0138  0.0178  306 EZL A C4  
2143 C  C5  . EZL G .   ? 0.1562 0.2213 0.1728 -0.0067 0.0039  0.0182  306 EZL A C5  
2144 C  C8  . EZL G .   ? 0.1893 0.2655 0.3028 0.0043  0.0397  0.0767  306 EZL A C8  
2145 O  O1  . EZL G .   ? 0.1020 0.1361 0.1391 -0.0043 -0.0041 -0.0118 306 EZL A O1  
2146 O  O2  . EZL G .   ? 0.0964 0.1628 0.1286 -0.0006 -0.0049 -0.0252 306 EZL A O2  
2147 S  S1  . EZL G .   ? 0.1037 0.1390 0.1390 -0.0111 -0.0044 -0.0160 306 EZL A S1  
2148 C  C1  . EZL G .   ? 0.0908 0.1544 0.1335 0.0001  0.0100  0.0004  306 EZL A C1  
2149 N  N2  . EZL G .   ? 0.1025 0.1402 0.1692 -0.0012 0.0106  -0.0103 306 EZL A N2  
2150 S  S2  . EZL G .   ? 0.1204 0.1668 0.1854 -0.0078 -0.0055 0.0114  306 EZL A S2  
2151 C  C6  . EZL G .   ? 0.1343 0.1905 0.1743 -0.0190 0.0168  -0.0092 306 EZL A C6  
2152 C  C7  . EZL G .   ? 0.1490 0.1666 0.1883 -0.0278 0.0171  -0.0217 306 EZL A C7  
2153 O  O3  . EZL G .   ? 0.2149 0.2562 0.2051 -0.0186 0.0107  0.0515  306 EZL A O3  
2154 C  C9  . EZL G .   ? 0.3093 0.2807 0.2690 -0.0195 0.1328  0.0462  306 EZL A C9  
2155 O  O   . HOH H .   ? 0.2536 0.3074 0.2396 -0.0283 -0.0061 0.0248  401 HOH A O   
2156 O  O   . HOH H .   ? 0.8612 0.5209 0.4282 0.3522  0.1814  0.2034  402 HOH A O   
2157 O  O   . HOH H .   ? 0.2727 0.3854 0.3416 0.0004  -0.0704 -0.1297 403 HOH A O   
2158 O  O   . HOH H .   ? 0.6318 0.6082 0.4469 0.0800  -0.0504 -0.1186 404 HOH A O   
2159 O  O   . HOH H .   ? 0.7368 0.6244 0.4028 0.2410  -0.0273 -0.1434 405 HOH A O   
2160 O  O   . HOH H .   ? 0.3373 0.1517 0.2641 -0.0115 -0.0705 0.0212  406 HOH A O   
2161 O  O   . HOH H .   ? 0.2986 0.7719 0.7134 0.0542  0.0165  0.0482  407 HOH A O   
2162 O  O   . HOH H .   ? 0.5235 0.5588 0.3912 -0.2002 0.1768  -0.0876 408 HOH A O   
2163 O  O   . HOH H .   ? 0.6269 0.4817 0.1747 -0.1955 -0.0119 -0.0908 409 HOH A O   
2164 O  O   . HOH H .   ? 0.2037 0.5401 0.5794 0.0084  -0.0198 -0.1227 410 HOH A O   
2165 O  O   . HOH H .   ? 0.4317 0.2744 0.4440 -0.0120 -0.0747 0.0141  411 HOH A O   
2166 O  O   . HOH H .   ? 0.5146 0.7843 0.2910 -0.4087 -0.1693 0.1540  412 HOH A O   
2167 O  O   . HOH H .   ? 0.3352 0.4426 0.6662 0.1391  -0.1782 -0.1114 413 HOH A O   
2168 O  O   . HOH H .   ? 0.4429 0.5098 0.4439 0.0442  -0.0625 0.1087  414 HOH A O   
2169 O  O   . HOH H .   ? 0.2030 0.6844 0.4303 -0.0050 0.0301  -0.2098 415 HOH A O   
2170 O  O   . HOH H .   ? 0.2913 0.3858 0.3917 0.0145  0.0173  0.0465  416 HOH A O   
2171 O  O   . HOH H .   ? 0.6433 0.4056 0.5008 -0.0857 0.1586  -0.1256 417 HOH A O   
2172 O  O   . HOH H .   ? 0.3492 0.6262 0.1908 -0.2271 -0.0752 0.0293  418 HOH A O   
2173 O  O   . HOH H .   ? 0.5423 0.3962 0.3287 -0.0822 0.0783  -0.0969 419 HOH A O   
2174 O  O   . HOH H .   ? 0.1537 0.1778 0.1890 0.0021  0.0089  -0.0278 420 HOH A O   
2175 O  O   . HOH H .   ? 0.3380 0.2843 0.2641 -0.0652 -0.0553 -0.0291 421 HOH A O   
2176 O  O   . HOH H .   ? 0.3366 0.4487 0.4202 0.0456  -0.1154 0.0870  422 HOH A O   
2177 O  O   . HOH H .   ? 0.6195 0.3593 0.1779 -0.0032 0.0181  0.0012  423 HOH A O   
2178 O  O   . HOH H .   ? 0.3162 0.6432 0.6500 0.0081  0.1177  0.3521  424 HOH A O   
2179 O  O   . HOH H .   ? 0.3171 0.6415 0.8287 0.0593  0.0939  0.4597  425 HOH A O   
2180 O  O   . HOH H .   ? 0.4674 0.3804 0.5777 0.1386  0.2225  0.1459  426 HOH A O   
2181 O  O   . HOH H .   ? 0.2709 0.3589 0.3833 0.0754  -0.1747 -0.1757 427 HOH A O   
2182 O  O   . HOH H .   ? 0.2878 0.5751 0.7295 0.1960  -0.1152 -0.1384 428 HOH A O   
2183 O  O   . HOH H .   ? 0.4325 0.2490 0.2988 -0.0499 0.0547  -0.0281 429 HOH A O   
2184 O  O   . HOH H .   ? 0.3503 0.3876 0.2345 -0.0197 -0.0455 0.0132  430 HOH A O   
2185 O  O   . HOH H .   ? 0.4789 0.2759 0.4268 -0.0565 -0.0651 -0.0260 431 HOH A O   
2186 O  O   . HOH H .   ? 0.2605 0.4594 0.3319 0.0127  0.1242  -0.0080 432 HOH A O   
2187 O  O   . HOH H .   ? 0.3502 0.2636 0.2716 0.0156  0.0828  0.0661  433 HOH A O   
2188 O  O   . HOH H .   ? 0.2717 0.2727 0.2178 -0.0399 -0.0066 -0.0064 434 HOH A O   
2189 O  O   . HOH H .   ? 0.2456 0.3291 0.2420 -0.0337 -0.0466 -0.0722 435 HOH A O   
2190 O  O   . HOH H .   ? 0.3223 0.4001 0.3395 0.0144  0.0891  -0.1280 436 HOH A O   
2191 O  O   . HOH H .   ? 0.2564 0.2770 0.3309 -0.0046 0.0647  -0.0274 437 HOH A O   
2192 O  O   . HOH H .   ? 0.3699 0.2197 0.2541 0.0373  -0.1345 0.0238  438 HOH A O   
2193 O  O   . HOH H .   ? 0.2223 0.5713 0.2529 -0.0212 0.0353  -0.0299 439 HOH A O   
2194 O  O   . HOH H .   ? 0.2508 0.8303 0.5570 0.0364  0.0057  -0.1949 440 HOH A O   
2195 O  O   . HOH H .   ? 0.2244 0.1488 0.1678 -0.0197 0.0390  -0.0179 441 HOH A O   
2196 O  O   . HOH H .   ? 0.2957 0.5666 0.5675 -0.0380 0.0370  0.2464  442 HOH A O   
2197 O  O   . HOH H .   ? 0.3226 0.3897 0.3897 -0.0719 -0.0263 0.0856  443 HOH A O   
2198 O  O   . HOH H .   ? 0.4519 0.1926 0.2636 -0.0652 0.0255  0.0080  444 HOH A O   
2199 O  O   . HOH H .   ? 0.3098 0.3412 0.2996 0.0589  0.0321  -0.0535 445 HOH A O   
2200 O  O   . HOH H .   ? 0.3414 0.6892 0.3388 0.1703  0.0107  0.0345  446 HOH A O   
2201 O  O   . HOH H .   ? 0.3315 0.6899 0.5062 -0.1700 -0.1562 0.1897  447 HOH A O   
2202 O  O   . HOH H .   ? 0.1833 0.2508 0.2083 -0.0075 -0.0422 0.0262  448 HOH A O   
2203 O  O   . HOH H .   ? 0.3269 0.3194 0.3628 0.0223  0.0042  0.1381  449 HOH A O   
2204 O  O   . HOH H .   ? 0.5565 0.6391 0.4437 0.1867  0.1775  0.0993  450 HOH A O   
2205 O  O   . HOH H .   ? 0.4185 0.6268 0.6562 -0.1076 -0.0142 0.1650  451 HOH A O   
2206 O  O   . HOH H .   ? 0.3571 0.3003 0.2989 0.0666  0.0722  0.0564  452 HOH A O   
2207 O  O   . HOH H .   ? 0.3356 0.3094 0.9762 0.0959  0.3160  0.1856  453 HOH A O   
2208 O  O   . HOH H .   ? 0.5136 0.3549 0.5161 -0.0662 -0.1034 0.1417  454 HOH A O   
2209 O  O   . HOH H .   ? 0.5876 0.6526 0.2416 -0.1181 0.1146  0.0754  455 HOH A O   
2210 O  O   . HOH H .   ? 0.4806 0.3237 0.6456 0.1349  -0.0473 -0.0008 456 HOH A O   
2211 O  O   . HOH H .   ? 0.3226 0.3067 0.1894 -0.0490 0.0748  0.0098  457 HOH A O   
2212 O  O   . HOH H .   ? 0.1653 0.3646 0.4230 -0.0564 0.0441  -0.0586 458 HOH A O   
2213 O  O   . HOH H .   ? 0.1822 0.1768 0.1592 -0.0006 0.0069  -0.0300 459 HOH A O   
2214 O  O   . HOH H .   ? 0.2037 0.2355 0.3202 -0.0795 -0.0280 0.0041  460 HOH A O   
2215 O  O   . HOH H .   ? 0.6429 0.4069 0.2461 0.0105  0.1119  -0.0992 461 HOH A O   
2216 O  O   . HOH H .   ? 0.1674 0.2237 0.1553 0.0421  0.0243  0.0068  462 HOH A O   
2217 O  O   . HOH H .   ? 0.2411 0.3664 0.3463 0.0176  0.0413  -0.0390 463 HOH A O   
2218 O  O   . HOH H .   ? 0.9772 0.3783 0.4511 -0.0367 0.1675  -0.0266 464 HOH A O   
2219 O  O   . HOH H .   ? 0.3352 0.2102 0.1929 0.0375  -0.0194 0.0146  465 HOH A O   
2220 O  O   . HOH H .   ? 0.7584 0.2989 0.2735 -0.0135 0.0671  0.0762  466 HOH A O   
2221 O  O   . HOH H .   ? 0.9395 0.3987 0.4968 -0.0802 -0.2218 0.0149  467 HOH A O   
2222 O  O   . HOH H .   ? 0.3119 0.2451 0.3226 -0.0060 -0.0411 0.0245  468 HOH A O   
2223 O  O   . HOH H .   ? 0.4119 0.3719 0.3125 0.0416  -0.1087 -0.0192 469 HOH A O   
2224 O  O   . HOH H .   ? 0.5153 0.4781 0.2380 0.1370  0.1008  0.0903  470 HOH A O   
2225 O  O   . HOH H .   ? 0.5813 0.3079 0.2593 -0.0358 0.0044  0.0626  471 HOH A O   
2226 O  O   . HOH H .   ? 0.2659 0.1817 0.2544 -0.0593 0.0697  -0.0563 472 HOH A O   
2227 O  O   . HOH H .   ? 0.3306 0.7119 0.2737 -0.1439 0.0484  -0.2318 473 HOH A O   
2228 O  O   . HOH H .   ? 0.3629 0.4453 0.2791 -0.0732 0.0449  0.1351  474 HOH A O   
2229 O  O   . HOH H .   ? 0.2850 0.3534 0.5341 -0.0552 0.0789  0.0781  475 HOH A O   
2230 O  O   . HOH H .   ? 0.7496 0.6499 0.3162 0.2722  0.0306  0.0454  476 HOH A O   
2231 O  O   . HOH H .   ? 0.2576 0.3355 0.3076 -0.0384 -0.0062 -0.0625 477 HOH A O   
2232 O  O   . HOH H .   ? 0.5727 0.4322 0.3746 -0.0133 -0.0243 0.2000  478 HOH A O   
2233 O  O   . HOH H .   ? 0.6190 0.3280 0.5894 -0.0430 -0.2302 -0.0292 479 HOH A O   
2234 O  O   . HOH H .   ? 0.2728 0.2957 0.3345 0.0141  -0.1087 0.0148  480 HOH A O   
2235 O  O   . HOH H .   ? 0.1556 0.1703 0.1509 0.0069  -0.0044 -0.0190 481 HOH A O   
2236 O  O   . HOH H .   ? 0.1531 0.2145 0.3302 -0.0250 0.0115  0.0024  482 HOH A O   
2237 O  O   . HOH H .   ? 0.2896 0.3243 0.2373 0.0111  0.0910  -0.0281 483 HOH A O   
2238 O  O   . HOH H .   ? 0.6396 0.4340 0.7355 -0.2943 -0.1119 0.2028  484 HOH A O   
2239 O  O   . HOH H .   ? 0.4425 0.5163 0.8713 -0.1797 0.0128  0.1982  485 HOH A O   
2240 O  O   . HOH H .   ? 0.4166 0.3323 0.8042 0.0119  -0.2157 0.0566  486 HOH A O   
2241 O  O   . HOH H .   ? 0.3985 0.5302 0.5191 -0.1075 0.0889  0.2343  487 HOH A O   
2242 O  O   . HOH H .   ? 0.2935 0.2648 0.3269 -0.0528 0.1091  -0.0370 488 HOH A O   
2243 O  O   . HOH H .   ? 0.2082 0.2204 0.2644 0.0199  -0.0117 0.0092  489 HOH A O   
2244 O  O   . HOH H .   ? 0.3154 0.6050 1.0926 0.1090  0.2093  0.2773  490 HOH A O   
2245 O  O   . HOH H .   ? 0.1344 0.1517 0.1497 -0.0075 0.0334  -0.0048 491 HOH A O   
2246 O  O   . HOH H .   ? 0.7682 0.4171 0.2382 0.0414  0.0304  0.1194  492 HOH A O   
2247 O  O   . HOH H .   ? 0.1215 0.2244 0.2604 0.0079  0.0189  -0.0289 493 HOH A O   
2248 O  O   . HOH H .   ? 0.3107 0.2385 0.3653 0.0414  -0.0588 -0.0192 494 HOH A O   
2249 O  O   . HOH H .   ? 0.2812 0.2730 0.3123 -0.0080 -0.1198 0.0151  495 HOH A O   
2250 O  O   . HOH H .   ? 0.3327 0.7013 0.4311 0.0608  -0.0038 0.1593  496 HOH A O   
2251 O  O   . HOH H .   ? 0.4737 0.4647 0.2938 -0.1117 -0.1417 0.1286  497 HOH A O   
2252 O  O   . HOH H .   ? 0.3211 0.3136 0.6645 -0.0288 0.0873  -0.1335 498 HOH A O   
2253 O  O   . HOH H .   ? 0.2134 0.3608 0.3122 0.0631  -0.0299 -0.0741 499 HOH A O   
2254 O  O   . HOH H .   ? 0.5942 0.4562 0.2586 -0.1256 -0.0222 -0.0491 500 HOH A O   
2255 O  O   . HOH H .   ? 0.4893 0.2626 0.3610 0.1600  -0.0754 -0.0348 501 HOH A O   
2256 O  O   . HOH H .   ? 0.3137 0.5662 0.4345 -0.2666 -0.0367 0.1348  502 HOH A O   
2257 O  O   . HOH H .   ? 0.3140 0.4268 0.3036 0.1370  0.0574  0.1295  503 HOH A O   
2258 O  O   . HOH H .   ? 0.3398 0.2977 0.2995 -0.0096 0.0243  0.0275  504 HOH A O   
2259 O  O   . HOH H .   ? 0.2946 0.5260 0.3653 -0.1688 -0.0039 0.0039  505 HOH A O   
2260 O  O   . HOH H .   ? 0.3420 0.2834 0.2113 0.0032  0.0122  0.0094  506 HOH A O   
2261 O  O   . HOH H .   ? 0.1766 0.4523 0.4536 -0.0500 -0.0611 0.0475  507 HOH A O   
2262 O  O   . HOH H .   ? 0.4205 0.6208 0.5562 -0.0497 -0.2379 -0.1622 508 HOH A O   
2263 O  O   . HOH H .   ? 0.5108 0.3137 0.2104 -0.1059 0.0115  -0.0322 509 HOH A O   
2264 O  O   . HOH H .   ? 0.2391 0.2120 0.2475 0.0026  -0.0685 0.0066  510 HOH A O   
2265 O  O   . HOH H .   ? 0.5130 0.3585 0.3115 -0.0249 -0.1168 0.1703  511 HOH A O   
2266 O  O   . HOH H .   ? 0.1960 0.2009 0.2130 0.0161  -0.0049 0.0214  512 HOH A O   
2267 O  O   . HOH H .   ? 0.2152 0.1778 0.2694 -0.0286 -0.0044 -0.0103 513 HOH A O   
2268 O  O   . HOH H .   ? 0.3815 0.3495 0.3345 -0.0525 0.0365  -0.1207 514 HOH A O   
2269 O  O   . HOH H .   ? 0.3222 0.2354 0.3072 -0.0249 -0.1421 0.0006  515 HOH A O   
2270 O  O   . HOH H .   ? 0.4013 0.3074 0.2385 0.0435  0.0022  0.0071  516 HOH A O   
2271 O  O   . HOH H .   ? 0.3013 0.4442 0.2278 -0.0189 -0.0114 -0.0798 517 HOH A O   
2272 O  O   . HOH H .   ? 0.3546 0.3053 0.3638 0.0151  0.0258  -0.0508 518 HOH A O   
2273 O  O   . HOH H .   ? 0.4415 0.3047 0.2414 -0.0797 -0.0286 -0.0522 519 HOH A O   
2274 O  O   . HOH H .   ? 0.9303 0.2839 0.6978 -0.0524 -0.1469 -0.1146 520 HOH A O   
2275 O  O   . HOH H .   ? 0.2425 0.5183 0.8469 0.0893  -0.1235 0.0974  521 HOH A O   
2276 O  O   . HOH H .   ? 0.6000 0.2802 0.3438 0.0790  -0.0219 0.0818  522 HOH A O   
2277 O  O   . HOH H .   ? 0.5242 0.4184 0.4069 0.0033  -0.1027 -0.0476 523 HOH A O   
2278 O  O   . HOH H .   ? 0.3417 0.2669 0.3554 -0.0468 -0.0172 -0.0487 524 HOH A O   
2279 O  O   . HOH H .   ? 0.5599 0.4099 0.4605 -0.2112 -0.2098 -0.0427 525 HOH A O   
2280 O  O   . HOH H .   ? 0.8379 0.6291 0.3022 0.4925  -0.1918 -0.0472 526 HOH A O   
2281 O  O   . HOH H .   ? 0.2979 0.4128 0.3298 -0.0241 -0.0291 -0.0798 527 HOH A O   
2282 O  O   . HOH H .   ? 0.3891 0.3851 0.2674 -0.0167 0.0554  -0.0653 528 HOH A O   
2283 O  O   . HOH H .   ? 0.2160 0.3624 0.3793 0.0718  0.1128  0.0141  529 HOH A O   
2284 O  O   . HOH H .   ? 0.4483 0.5317 0.8996 0.2144  -0.0233 -0.1433 530 HOH A O   
2285 O  O   . HOH H .   ? 0.3807 0.5781 0.4704 -0.0310 0.1130  0.0493  531 HOH A O   
2286 O  O   . HOH H .   ? 0.2278 0.4095 0.3524 0.0089  0.0164  -0.0362 532 HOH A O   
2287 O  O   . HOH H .   ? 0.1919 0.2842 0.2989 -0.0847 -0.0588 -0.0402 533 HOH A O   
2288 O  O   . HOH H .   ? 0.2816 0.7420 0.5151 0.0029  0.0803  -0.0485 534 HOH A O   
2289 O  O   . HOH H .   ? 1.2723 0.6172 0.2910 -0.4176 -0.0178 0.0352  535 HOH A O   
2290 O  O   . HOH H .   ? 0.7896 0.3974 0.4979 0.2081  0.2885  0.2060  536 HOH A O   
2291 O  O   . HOH H .   ? 0.4769 0.3065 0.3204 -0.0834 -0.1647 0.0174  537 HOH A O   
2292 O  O   . HOH H .   ? 0.5346 0.6909 0.8549 -0.3512 -0.2196 0.1429  538 HOH A O   
2293 O  O   . HOH H .   ? 0.0955 0.3326 0.2789 0.0193  0.0140  -0.0570 539 HOH A O   
2294 O  O   . HOH H .   ? 0.1955 0.4451 0.4383 0.0289  -0.0320 0.0576  540 HOH A O   
2295 O  O   . HOH H .   ? 0.6896 0.2554 0.4278 0.1262  -0.1289 -0.1242 541 HOH A O   
2296 O  O   . HOH H .   ? 0.3470 0.5202 0.3656 -0.0724 0.0031  -0.1852 542 HOH A O   
2297 O  O   . HOH H .   ? 0.5360 0.3590 0.2298 -0.0989 0.1923  -0.1048 543 HOH A O   
2298 O  O   . HOH H .   ? 0.3226 0.4093 0.3370 -0.0376 0.0640  -0.0534 544 HOH A O   
2299 O  O   . HOH H .   ? 0.3183 0.2741 0.2697 -0.0686 0.0069  0.0092  545 HOH A O   
2300 O  O   . HOH H .   ? 0.5430 0.3873 0.3470 0.0888  0.2036  0.1159  546 HOH A O   
2301 O  O   . HOH H .   ? 0.8598 0.4142 0.4196 0.1262  -0.3065 0.0057  547 HOH A O   
2302 O  O   . HOH H .   ? 0.5572 0.4805 0.4329 0.1524  0.1884  0.2101  548 HOH A O   
2303 O  O   . HOH H .   ? 0.2283 0.2924 0.2936 -0.0100 0.0259  -0.0016 549 HOH A O   
2304 O  O   . HOH H .   ? 0.2791 0.9129 0.4498 -0.0483 0.1641  0.0718  550 HOH A O   
2305 O  O   . HOH H .   ? 0.4717 0.4255 0.2957 -0.0564 0.0754  -0.0266 551 HOH A O   
2306 O  O   . HOH H .   ? 0.3031 0.3050 0.2471 0.0697  -0.0097 0.0554  552 HOH A O   
2307 O  O   . HOH H .   ? 0.4318 0.3270 0.5054 0.0600  -0.2754 0.0162  553 HOH A O   
2308 O  O   . HOH H .   ? 0.9080 0.3754 0.5435 0.0514  0.4268  -0.0168 554 HOH A O   
2309 O  O   . HOH H .   ? 0.3542 0.2240 0.3614 -0.0538 0.0736  -0.0336 555 HOH A O   
2310 O  O   . HOH H .   ? 0.2630 0.2935 1.1794 0.0172  0.1366  0.0788  556 HOH A O   
2311 O  O   . HOH H .   ? 0.1972 0.3353 0.3481 0.0355  -0.0848 -0.0096 557 HOH A O   
2312 O  O   . HOH H .   ? 0.3459 0.4458 0.5005 0.0078  0.1289  0.1094  558 HOH A O   
2313 O  O   . HOH H .   ? 0.6001 0.3753 0.4561 -0.0885 0.0518  -0.0758 559 HOH A O   
2314 O  O   . HOH H .   ? 0.3775 0.8678 0.4436 0.1002  -0.1014 -0.0600 560 HOH A O   
2315 O  O   . HOH H .   ? 0.1838 0.2921 0.2002 0.0110  -0.0447 0.0050  561 HOH A O   
2316 O  O   . HOH H .   ? 0.3013 0.6000 0.2867 -0.1335 -0.0346 0.1135  562 HOH A O   
2317 O  O   . HOH H .   ? 0.2503 0.2855 0.3082 0.0491  -0.0068 0.0724  563 HOH A O   
2318 O  O   . HOH H .   ? 0.3973 0.2561 0.2958 0.0278  0.0617  0.0390  564 HOH A O   
2319 O  O   . HOH H .   ? 0.3078 0.2713 0.2781 0.0290  0.0776  0.1096  565 HOH A O   
2320 O  O   . HOH H .   ? 0.1731 0.1786 0.1876 0.0113  -0.0046 -0.0091 566 HOH A O   
2321 O  O   . HOH H .   ? 0.7888 0.3273 0.3796 0.0161  -0.0458 -0.0603 567 HOH A O   
2322 O  O   . HOH H .   ? 0.4246 0.1685 0.2280 0.0496  -0.0020 -0.0138 568 HOH A O   
2323 O  O   . HOH H .   ? 0.4397 0.4250 0.9564 -0.1100 -0.0204 0.1479  569 HOH A O   
2324 O  O   . HOH H .   ? 0.7220 0.5488 0.2467 0.1971  -0.2285 -0.0540 570 HOH A O   
2325 O  O   . HOH H .   ? 0.4340 0.3495 0.3532 0.0700  -0.0750 -0.0247 571 HOH A O   
2326 O  O   . HOH H .   ? 0.4515 0.4411 0.6522 -0.1454 0.3143  -0.2288 572 HOH A O   
2327 O  O   . HOH H .   ? 0.4539 0.6132 0.2335 -0.1474 0.0884  -0.0078 573 HOH A O   
2328 O  O   . HOH H .   ? 0.3209 0.7307 0.4735 0.0566  0.0565  -0.0199 574 HOH A O   
2329 O  O   . HOH H .   ? 0.1711 0.2573 0.3596 -0.0260 -0.0286 -0.0089 575 HOH A O   
2330 O  O   . HOH H .   ? 0.4119 0.6759 0.5964 -0.0967 0.1689  -0.1391 576 HOH A O   
2331 O  O   . HOH H .   ? 0.4307 0.3212 0.8540 0.1113  0.0629  0.1354  577 HOH A O   
2332 O  O   . HOH H .   ? 0.2813 0.4352 0.4981 0.1302  0.0707  0.1446  578 HOH A O   
2333 O  O   . HOH H .   ? 0.5359 0.6287 0.2839 -0.0030 0.0990  0.2194  579 HOH A O   
2334 O  O   . HOH H .   ? 0.4641 0.4838 0.2827 0.1316  -0.0425 -0.0032 580 HOH A O   
2335 O  O   . HOH H .   ? 0.2845 0.6171 0.3960 0.0672  0.0727  0.1028  581 HOH A O   
2336 O  O   . HOH H .   ? 0.5778 0.4551 0.4345 -0.0099 -0.0080 -0.0270 582 HOH A O   
2337 O  O   . HOH H .   ? 0.3962 0.3388 0.4379 -0.0652 -0.0323 0.0773  583 HOH A O   
2338 O  O   . HOH H .   ? 0.5211 0.6990 0.3679 -0.0414 0.1159  0.0151  584 HOH A O   
2339 O  O   . HOH H .   ? 0.4220 0.4763 0.4469 0.2630  -0.0554 -0.0825 585 HOH A O   
2340 O  O   . HOH H .   ? 0.4289 0.3650 0.2384 -0.0153 0.0184  0.0276  586 HOH A O   
2341 O  O   . HOH H .   ? 0.2788 0.5983 0.4735 -0.0516 -0.0432 -0.0939 587 HOH A O   
2342 O  O   . HOH H .   ? 0.4828 0.5499 0.8293 0.1297  0.1114  0.0850  588 HOH A O   
2343 O  O   . HOH H .   ? 0.5590 0.7720 0.5168 0.2148  0.0394  -0.3313 589 HOH A O   
2344 O  O   . HOH H .   ? 0.6645 0.4361 0.2860 0.0083  0.0281  0.0414  590 HOH A O   
2345 O  O   . HOH H .   ? 0.3875 0.4770 0.4910 0.0744  -0.0114 0.0005  591 HOH A O   
2346 O  O   . HOH H .   ? 0.2968 0.2896 0.3574 -0.0476 -0.0761 0.0064  592 HOH A O   
2347 O  O   . HOH H .   ? 0.6355 0.3930 0.5522 0.1881  0.0788  0.0751  593 HOH A O   
2348 O  O   . HOH H .   ? 0.3944 0.7565 0.2864 0.1368  -0.1063 -0.1233 594 HOH A O   
2349 O  O   . HOH H .   ? 0.5679 0.4159 0.5885 -0.2127 0.2102  -0.0798 595 HOH A O   
2350 O  O   . HOH H .   ? 0.5037 0.4774 0.4095 -0.0442 0.1728  0.1848  596 HOH A O   
2351 O  O   . HOH H .   ? 0.5057 0.5757 0.6569 0.2025  0.0370  0.0297  597 HOH A O   
2352 O  O   . HOH H .   ? 0.4771 0.9376 0.2472 -0.0212 0.1116  -0.1036 598 HOH A O   
2353 O  O   . HOH H .   ? 0.6179 0.4465 0.5238 -0.0135 -0.0839 0.1349  599 HOH A O   
2354 O  O   . HOH H .   ? 0.6087 0.5054 0.5026 -0.0526 -0.1897 0.0370  600 HOH A O   
2355 O  O   . HOH H .   ? 0.4198 0.5091 0.6082 0.1615  -0.1345 0.1075  601 HOH A O   
2356 O  O   . HOH H .   ? 0.4853 0.4393 0.5056 -0.1312 -0.0232 0.1499  602 HOH A O   
2357 O  O   . HOH H .   ? 0.4206 0.6778 0.4928 -0.0430 -0.0381 -0.3486 603 HOH A O   
2358 O  O   . HOH H .   ? 0.4181 0.5264 0.7177 0.1241  -0.1305 0.0357  604 HOH A O   
2359 O  O   . HOH H .   ? 0.3992 0.9890 0.3758 -0.2531 0.0629  -0.1718 605 HOH A O   
2360 O  O   . HOH H .   ? 0.3039 0.3013 0.3653 0.0849  -0.0846 -0.0124 606 HOH A O   
2361 O  O   . HOH H .   ? 0.3100 0.5586 0.7798 -0.0491 0.0452  -0.1508 607 HOH A O   
2362 O  O   . HOH H .   ? 0.5674 0.3643 1.0348 0.1195  -0.2207 0.1020  608 HOH A O   
2363 O  O   . HOH H .   ? 0.3360 0.4066 0.5229 -0.0170 0.0678  0.0067  609 HOH A O   
2364 O  O   . HOH H .   ? 0.5461 0.6113 0.4289 -0.1570 -0.1982 0.1412  610 HOH A O   
2365 O  O   . HOH H .   ? 0.4795 0.4773 0.5757 -0.0978 -0.2419 0.0741  611 HOH A O   
2366 O  O   . HOH H .   ? 0.4092 0.4347 0.4031 -0.1223 -0.0738 0.1452  612 HOH A O   
2367 O  O   . HOH H .   ? 0.4038 0.5931 0.2605 0.1480  0.0190  0.1365  613 HOH A O   
2368 O  O   . HOH H .   ? 0.4593 0.5599 0.5954 -0.1377 -0.2159 0.0052  614 HOH A O   
2369 O  O   . HOH H .   ? 1.1770 0.4910 0.3389 -0.0384 0.0177  -0.1289 615 HOH A O   
2370 O  O   . HOH H .   ? 0.4550 0.4044 0.4710 -0.0322 0.0520  0.0142  616 HOH A O   
2371 O  O   . HOH H .   ? 0.2377 0.3881 0.4064 0.0141  0.0218  0.0238  617 HOH A O   
2372 O  O   . HOH H .   ? 0.3078 0.6079 0.3689 -0.2031 0.0189  0.0328  618 HOH A O   
2373 O  O   . HOH H .   ? 0.4403 0.2885 0.7537 -0.0735 0.1635  0.0230  619 HOH A O   
2374 O  O   . HOH H .   ? 0.5615 0.6104 0.6686 -0.1214 0.0522  0.3265  620 HOH A O   
2375 O  O   . HOH H .   ? 0.3826 0.4591 0.6914 -0.1592 0.0048  0.1876  621 HOH A O   
2376 O  O   . HOH H .   ? 0.4092 0.4246 0.4248 -0.0282 0.0563  0.0641  622 HOH A O   
2377 O  O   . HOH H .   ? 0.4097 0.6445 0.9582 0.0625  -0.0829 0.3819  623 HOH A O   
2378 O  O   . HOH H .   ? 0.3834 0.4268 0.2896 -0.0030 -0.0717 0.0439  624 HOH A O   
2379 O  O   . HOH H .   ? 0.2746 0.5719 0.5191 0.0399  0.0725  0.0974  625 HOH A O   
# 
