data_5OGO
# 
_entry.id   5OGO 
# 
_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   5OGO         pdb_00005ogo 10.2210/pdb5ogo/pdb 
WWPDB D_1200005781 ?            ?                   
# 
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 2018-08-01 
2 'Structure model' 1 1 2024-01-17 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' pdbx_initial_refinement_model 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_database_2.pdbx_DOI'                
2 2 'Structure model' '_database_2.pdbx_database_accession' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5OGO 
_pdbx_database_status.recvd_initial_deposition_date   2017-07-13 
_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            ? 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'same manuscript' 
_pdbx_database_related.db_id          5OGJ 
_pdbx_database_related.content_type   unspecified 
# 
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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Crystal structure of chimeric carbonic anhydrase I with 3-(Benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnov, A.'  1 ? 
primary 'Manakova, E.' 2 ? 
primary 'Grazulis, S.' 3 ? 
primary 'Matulis, D.'  4 ? 
# 
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'                                                           29329.086 1   4.2.1.1 
'N62V, N67H, I91F, V121A, F130L, V134A, T199H, L203Y' 'chimeric carbonic anhydrase I' 
;The active site of human carbonic anhydrase I in carbonic anhydrase II was reconstructed by means of eight point mutations: N62V, N67H, I91F, V121A, F130L, V134A, T199H, and L203Y.
;
2 non-polymer syn 'ZINC ION'                                                                       65.409    1   ?       ? ? ? 
3 non-polymer syn '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 424.415   2   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                             78.133    1   ?       ? ? ? 
5 non-polymer syn BICINE                                                                           163.172   3   ?       ? ? ? 
6 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                          106.120   1   ?       ? ? ? 
7 non-polymer syn 1,2-ETHANEDIOL                                                                   62.068    2   ?       ? ? ? 
8 water       nat water                                                                            18.015    333 ?       ? ? ? 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNVGHAFHVEFDDSQDKAVLK
GGPLDGTYRLFQFHFHWGSLDGQGSEHTVDKKKYAAELHLAHWNTKYGDLGKAAQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTHPPLYECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNVGHAFHVEFDDSQDKAVLK
GGPLDGTYRLFQFHFHWGSLDGQGSEHTVDKKKYAAELHLAHWNTKYGDLGKAAQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTHPPLYECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
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 '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' WWO 
4 'DIMETHYL SULFOXIDE'                                                             DMS 
5 BICINE                                                                           BCN 
6 'DI(HYDROXYETHYL)ETHER'                                                          PEG 
7 1,2-ETHANEDIOL                                                                   EDO 
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  VAL n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  HIS 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  PHE 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 ALA 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 LEU n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 ALA 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 HIS n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 TYR n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                          ?                 
'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE                                                                         ?                 
'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                       ?                 
'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                  ?                 
'C4 H7 N O4'          133.103 
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  
GLN 'L-peptide linking' y GLUTAMINE                                                                        ?                 
'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                  ?                 
'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                                                          ?                 
'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                        ?                 
'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                                            ?                 
'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                       ?                 
'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                                                          ?                 
'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                                           ?                 
'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                                       ?                 
'C5 H11 N O2 S'       149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                          ?                 
'C4 H10 O3'           106.120 
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 
WWO non-polymer         . '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ?                 
'C15 H15 F3 N2 O5 S2' 424.415 
ZN  non-polymer         . 'ZINC ION'                                                                       ?                 
'Zn 2'                65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  HIS 67  67  67  HIS HIS 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  PHE 91  91  91  PHE PHE 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 ALA 121 121 121 ALA ALA 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 LEU 130 131 131 LEU LEU 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 ALA 134 135 135 ALA ALA 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 HIS 199 200 200 HIS HIS 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 TYR 203 204 204 TYR TYR 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 WWO 1   302 1   WWO WWO A . 
D 3 WWO 1   303 2   WWO WWO A . 
E 4 DMS 1   304 1   DMS DMS A . 
F 5 BCN 1   305 2   BCN BCN A . 
G 6 PEG 1   306 3   PEG PEG A . 
H 7 EDO 1   307 4   EDO EDO A . 
I 7 EDO 1   308 5   EDO EDO A . 
J 5 BCN 1   309 6   BCN BCN A . 
K 5 BCN 1   310 7   BCN BCN A . 
L 8 HOH 1   401 231 HOH HOH A . 
L 8 HOH 2   402 303 HOH HOH A . 
L 8 HOH 3   403 209 HOH HOH A . 
L 8 HOH 4   404 178 HOH HOH A . 
L 8 HOH 5   405 292 HOH HOH A . 
L 8 HOH 6   406 161 HOH HOH A . 
L 8 HOH 7   407 275 HOH HOH A . 
L 8 HOH 8   408 264 HOH HOH A . 
L 8 HOH 9   409 328 HOH HOH A . 
L 8 HOH 10  410 270 HOH HOH A . 
L 8 HOH 11  411 102 HOH HOH A . 
L 8 HOH 12  412 56  HOH HOH A . 
L 8 HOH 13  413 259 HOH HOH A . 
L 8 HOH 14  414 136 HOH HOH A . 
L 8 HOH 15  415 191 HOH HOH A . 
L 8 HOH 16  416 69  HOH HOH A . 
L 8 HOH 17  417 95  HOH HOH A . 
L 8 HOH 18  418 267 HOH HOH A . 
L 8 HOH 19  419 117 HOH HOH A . 
L 8 HOH 20  420 154 HOH HOH A . 
L 8 HOH 21  421 84  HOH HOH A . 
L 8 HOH 22  422 312 HOH HOH A . 
L 8 HOH 23  423 163 HOH HOH A . 
L 8 HOH 24  424 64  HOH HOH A . 
L 8 HOH 25  425 262 HOH HOH A . 
L 8 HOH 26  426 187 HOH HOH A . 
L 8 HOH 27  427 225 HOH HOH A . 
L 8 HOH 28  428 256 HOH HOH A . 
L 8 HOH 29  429 132 HOH HOH A . 
L 8 HOH 30  430 65  HOH HOH A . 
L 8 HOH 31  431 230 HOH HOH A . 
L 8 HOH 32  432 189 HOH HOH A . 
L 8 HOH 33  433 218 HOH HOH A . 
L 8 HOH 34  434 309 HOH HOH A . 
L 8 HOH 35  435 271 HOH HOH A . 
L 8 HOH 36  436 121 HOH HOH A . 
L 8 HOH 37  437 286 HOH HOH A . 
L 8 HOH 38  438 201 HOH HOH A . 
L 8 HOH 39  439 5   HOH HOH A . 
L 8 HOH 40  440 183 HOH HOH A . 
L 8 HOH 41  441 16  HOH HOH A . 
L 8 HOH 42  442 81  HOH HOH A . 
L 8 HOH 43  443 101 HOH HOH A . 
L 8 HOH 44  444 76  HOH HOH A . 
L 8 HOH 45  445 168 HOH HOH A . 
L 8 HOH 46  446 265 HOH HOH A . 
L 8 HOH 47  447 281 HOH HOH A . 
L 8 HOH 48  448 215 HOH HOH A . 
L 8 HOH 49  449 79  HOH HOH A . 
L 8 HOH 50  450 15  HOH HOH A . 
L 8 HOH 51  451 229 HOH HOH A . 
L 8 HOH 52  452 131 HOH HOH A . 
L 8 HOH 53  453 260 HOH HOH A . 
L 8 HOH 54  454 99  HOH HOH A . 
L 8 HOH 55  455 237 HOH HOH A . 
L 8 HOH 56  456 207 HOH HOH A . 
L 8 HOH 57  457 333 HOH HOH A . 
L 8 HOH 58  458 242 HOH HOH A . 
L 8 HOH 59  459 97  HOH HOH A . 
L 8 HOH 60  460 20  HOH HOH A . 
L 8 HOH 61  461 330 HOH HOH A . 
L 8 HOH 62  462 135 HOH HOH A . 
L 8 HOH 63  463 13  HOH HOH A . 
L 8 HOH 64  464 85  HOH HOH A . 
L 8 HOH 65  465 302 HOH HOH A . 
L 8 HOH 66  466 105 HOH HOH A . 
L 8 HOH 67  467 68  HOH HOH A . 
L 8 HOH 68  468 324 HOH HOH A . 
L 8 HOH 69  469 39  HOH HOH A . 
L 8 HOH 70  470 284 HOH HOH A . 
L 8 HOH 71  471 119 HOH HOH A . 
L 8 HOH 72  472 28  HOH HOH A . 
L 8 HOH 73  473 67  HOH HOH A . 
L 8 HOH 74  474 254 HOH HOH A . 
L 8 HOH 75  475 70  HOH HOH A . 
L 8 HOH 76  476 52  HOH HOH A . 
L 8 HOH 77  477 36  HOH HOH A . 
L 8 HOH 78  478 304 HOH HOH A . 
L 8 HOH 79  479 87  HOH HOH A . 
L 8 HOH 80  480 25  HOH HOH A . 
L 8 HOH 81  481 48  HOH HOH A . 
L 8 HOH 82  482 92  HOH HOH A . 
L 8 HOH 83  483 40  HOH HOH A . 
L 8 HOH 84  484 22  HOH HOH A . 
L 8 HOH 85  485 126 HOH HOH A . 
L 8 HOH 86  486 54  HOH HOH A . 
L 8 HOH 87  487 43  HOH HOH A . 
L 8 HOH 88  488 107 HOH HOH A . 
L 8 HOH 89  489 31  HOH HOH A . 
L 8 HOH 90  490 82  HOH HOH A . 
L 8 HOH 91  491 61  HOH HOH A . 
L 8 HOH 92  492 11  HOH HOH A . 
L 8 HOH 93  493 91  HOH HOH A . 
L 8 HOH 94  494 124 HOH HOH A . 
L 8 HOH 95  495 29  HOH HOH A . 
L 8 HOH 96  496 113 HOH HOH A . 
L 8 HOH 97  497 90  HOH HOH A . 
L 8 HOH 98  498 111 HOH HOH A . 
L 8 HOH 99  499 301 HOH HOH A . 
L 8 HOH 100 500 26  HOH HOH A . 
L 8 HOH 101 501 197 HOH HOH A . 
L 8 HOH 102 502 46  HOH HOH A . 
L 8 HOH 103 503 9   HOH HOH A . 
L 8 HOH 104 504 228 HOH HOH A . 
L 8 HOH 105 505 47  HOH HOH A . 
L 8 HOH 106 506 158 HOH HOH A . 
L 8 HOH 107 507 34  HOH HOH A . 
L 8 HOH 108 508 3   HOH HOH A . 
L 8 HOH 109 509 38  HOH HOH A . 
L 8 HOH 110 510 30  HOH HOH A . 
L 8 HOH 111 511 285 HOH HOH A . 
L 8 HOH 112 512 10  HOH HOH A . 
L 8 HOH 113 513 12  HOH HOH A . 
L 8 HOH 114 514 71  HOH HOH A . 
L 8 HOH 115 515 273 HOH HOH A . 
L 8 HOH 116 516 74  HOH HOH A . 
L 8 HOH 117 517 6   HOH HOH A . 
L 8 HOH 118 518 4   HOH HOH A . 
L 8 HOH 119 519 185 HOH HOH A . 
L 8 HOH 120 520 2   HOH HOH A . 
L 8 HOH 121 521 103 HOH HOH A . 
L 8 HOH 122 522 202 HOH HOH A . 
L 8 HOH 123 523 157 HOH HOH A . 
L 8 HOH 124 524 164 HOH HOH A . 
L 8 HOH 125 525 44  HOH HOH A . 
L 8 HOH 126 526 249 HOH HOH A . 
L 8 HOH 127 527 289 HOH HOH A . 
L 8 HOH 128 528 171 HOH HOH A . 
L 8 HOH 129 529 93  HOH HOH A . 
L 8 HOH 130 530 109 HOH HOH A . 
L 8 HOH 131 531 96  HOH HOH A . 
L 8 HOH 132 532 19  HOH HOH A . 
L 8 HOH 133 533 51  HOH HOH A . 
L 8 HOH 134 534 66  HOH HOH A . 
L 8 HOH 135 535 299 HOH HOH A . 
L 8 HOH 136 536 23  HOH HOH A . 
L 8 HOH 137 537 89  HOH HOH A . 
L 8 HOH 138 538 300 HOH HOH A . 
L 8 HOH 139 539 332 HOH HOH A . 
L 8 HOH 140 540 139 HOH HOH A . 
L 8 HOH 141 541 53  HOH HOH A . 
L 8 HOH 142 542 50  HOH HOH A . 
L 8 HOH 143 543 130 HOH HOH A . 
L 8 HOH 144 544 37  HOH HOH A . 
L 8 HOH 145 545 151 HOH HOH A . 
L 8 HOH 146 546 269 HOH HOH A . 
L 8 HOH 147 547 186 HOH HOH A . 
L 8 HOH 148 548 227 HOH HOH A . 
L 8 HOH 149 549 21  HOH HOH A . 
L 8 HOH 150 550 252 HOH HOH A . 
L 8 HOH 151 551 277 HOH HOH A . 
L 8 HOH 152 552 59  HOH HOH A . 
L 8 HOH 153 553 125 HOH HOH A . 
L 8 HOH 154 554 83  HOH HOH A . 
L 8 HOH 155 555 196 HOH HOH A . 
L 8 HOH 156 556 27  HOH HOH A . 
L 8 HOH 157 557 35  HOH HOH A . 
L 8 HOH 158 558 98  HOH HOH A . 
L 8 HOH 159 559 14  HOH HOH A . 
L 8 HOH 160 560 73  HOH HOH A . 
L 8 HOH 161 561 290 HOH HOH A . 
L 8 HOH 162 562 153 HOH HOH A . 
L 8 HOH 163 563 172 HOH HOH A . 
L 8 HOH 164 564 77  HOH HOH A . 
L 8 HOH 165 565 251 HOH HOH A . 
L 8 HOH 166 566 311 HOH HOH A . 
L 8 HOH 167 567 236 HOH HOH A . 
L 8 HOH 168 568 160 HOH HOH A . 
L 8 HOH 169 569 213 HOH HOH A . 
L 8 HOH 170 570 148 HOH HOH A . 
L 8 HOH 171 571 190 HOH HOH A . 
L 8 HOH 172 572 184 HOH HOH A . 
L 8 HOH 173 573 78  HOH HOH A . 
L 8 HOH 174 574 150 HOH HOH A . 
L 8 HOH 175 575 33  HOH HOH A . 
L 8 HOH 176 576 32  HOH HOH A . 
L 8 HOH 177 577 62  HOH HOH A . 
L 8 HOH 178 578 75  HOH HOH A . 
L 8 HOH 179 579 115 HOH HOH A . 
L 8 HOH 180 580 325 HOH HOH A . 
L 8 HOH 181 581 88  HOH HOH A . 
L 8 HOH 182 582 204 HOH HOH A . 
L 8 HOH 183 583 129 HOH HOH A . 
L 8 HOH 184 584 45  HOH HOH A . 
L 8 HOH 185 585 250 HOH HOH A . 
L 8 HOH 186 586 8   HOH HOH A . 
L 8 HOH 187 587 323 HOH HOH A . 
L 8 HOH 188 588 159 HOH HOH A . 
L 8 HOH 189 589 175 HOH HOH A . 
L 8 HOH 190 590 17  HOH HOH A . 
L 8 HOH 191 591 80  HOH HOH A . 
L 8 HOH 192 592 199 HOH HOH A . 
L 8 HOH 193 593 58  HOH HOH A . 
L 8 HOH 194 594 86  HOH HOH A . 
L 8 HOH 195 595 193 HOH HOH A . 
L 8 HOH 196 596 170 HOH HOH A . 
L 8 HOH 197 597 155 HOH HOH A . 
L 8 HOH 198 598 72  HOH HOH A . 
L 8 HOH 199 599 108 HOH HOH A . 
L 8 HOH 200 600 180 HOH HOH A . 
L 8 HOH 201 601 316 HOH HOH A . 
L 8 HOH 202 602 194 HOH HOH A . 
L 8 HOH 203 603 226 HOH HOH A . 
L 8 HOH 204 604 203 HOH HOH A . 
L 8 HOH 205 605 133 HOH HOH A . 
L 8 HOH 206 606 233 HOH HOH A . 
L 8 HOH 207 607 179 HOH HOH A . 
L 8 HOH 208 608 123 HOH HOH A . 
L 8 HOH 209 609 110 HOH HOH A . 
L 8 HOH 210 610 7   HOH HOH A . 
L 8 HOH 211 611 144 HOH HOH A . 
L 8 HOH 212 612 156 HOH HOH A . 
L 8 HOH 213 613 315 HOH HOH A . 
L 8 HOH 214 614 1   HOH HOH A . 
L 8 HOH 215 615 258 HOH HOH A . 
L 8 HOH 216 616 181 HOH HOH A . 
L 8 HOH 217 617 106 HOH HOH A . 
L 8 HOH 218 618 176 HOH HOH A . 
L 8 HOH 219 619 116 HOH HOH A . 
L 8 HOH 220 620 120 HOH HOH A . 
L 8 HOH 221 621 182 HOH HOH A . 
L 8 HOH 222 622 41  HOH HOH A . 
L 8 HOH 223 623 174 HOH HOH A . 
L 8 HOH 224 624 244 HOH HOH A . 
L 8 HOH 225 625 317 HOH HOH A . 
L 8 HOH 226 626 24  HOH HOH A . 
L 8 HOH 227 627 331 HOH HOH A . 
L 8 HOH 228 628 279 HOH HOH A . 
L 8 HOH 229 629 114 HOH HOH A . 
L 8 HOH 230 630 104 HOH HOH A . 
L 8 HOH 231 631 313 HOH HOH A . 
L 8 HOH 232 632 55  HOH HOH A . 
L 8 HOH 233 633 241 HOH HOH A . 
L 8 HOH 234 634 318 HOH HOH A . 
L 8 HOH 235 635 141 HOH HOH A . 
L 8 HOH 236 636 278 HOH HOH A . 
L 8 HOH 237 637 232 HOH HOH A . 
L 8 HOH 238 638 306 HOH HOH A . 
L 8 HOH 239 639 293 HOH HOH A . 
L 8 HOH 240 640 169 HOH HOH A . 
L 8 HOH 241 641 235 HOH HOH A . 
L 8 HOH 242 642 60  HOH HOH A . 
L 8 HOH 243 643 122 HOH HOH A . 
L 8 HOH 244 644 326 HOH HOH A . 
L 8 HOH 245 645 206 HOH HOH A . 
L 8 HOH 246 646 173 HOH HOH A . 
L 8 HOH 247 647 239 HOH HOH A . 
L 8 HOH 248 648 274 HOH HOH A . 
L 8 HOH 249 649 42  HOH HOH A . 
L 8 HOH 250 650 147 HOH HOH A . 
L 8 HOH 251 651 266 HOH HOH A . 
L 8 HOH 252 652 298 HOH HOH A . 
L 8 HOH 253 653 295 HOH HOH A . 
L 8 HOH 254 654 208 HOH HOH A . 
L 8 HOH 255 655 283 HOH HOH A . 
L 8 HOH 256 656 282 HOH HOH A . 
L 8 HOH 257 657 188 HOH HOH A . 
L 8 HOH 258 658 140 HOH HOH A . 
L 8 HOH 259 659 296 HOH HOH A . 
L 8 HOH 260 660 152 HOH HOH A . 
L 8 HOH 261 661 18  HOH HOH A . 
L 8 HOH 262 662 287 HOH HOH A . 
L 8 HOH 263 663 137 HOH HOH A . 
L 8 HOH 264 664 307 HOH HOH A . 
L 8 HOH 265 665 205 HOH HOH A . 
L 8 HOH 266 666 276 HOH HOH A . 
L 8 HOH 267 667 322 HOH HOH A . 
L 8 HOH 268 668 63  HOH HOH A . 
L 8 HOH 269 669 291 HOH HOH A . 
L 8 HOH 270 670 272 HOH HOH A . 
L 8 HOH 271 671 177 HOH HOH A . 
L 8 HOH 272 672 145 HOH HOH A . 
L 8 HOH 273 673 238 HOH HOH A . 
L 8 HOH 274 674 319 HOH HOH A . 
L 8 HOH 275 675 165 HOH HOH A . 
L 8 HOH 276 676 167 HOH HOH A . 
L 8 HOH 277 677 314 HOH HOH A . 
L 8 HOH 278 678 210 HOH HOH A . 
L 8 HOH 279 679 200 HOH HOH A . 
L 8 HOH 280 680 257 HOH HOH A . 
L 8 HOH 281 681 128 HOH HOH A . 
L 8 HOH 282 682 305 HOH HOH A . 
L 8 HOH 283 683 211 HOH HOH A . 
L 8 HOH 284 684 243 HOH HOH A . 
L 8 HOH 285 685 198 HOH HOH A . 
L 8 HOH 286 686 57  HOH HOH A . 
L 8 HOH 287 687 212 HOH HOH A . 
L 8 HOH 288 688 297 HOH HOH A . 
L 8 HOH 289 689 162 HOH HOH A . 
L 8 HOH 290 690 166 HOH HOH A . 
L 8 HOH 291 691 310 HOH HOH A . 
L 8 HOH 292 692 138 HOH HOH A . 
L 8 HOH 293 693 100 HOH HOH A . 
L 8 HOH 294 694 118 HOH HOH A . 
L 8 HOH 295 695 216 HOH HOH A . 
L 8 HOH 296 696 219 HOH HOH A . 
L 8 HOH 297 697 112 HOH HOH A . 
L 8 HOH 298 698 143 HOH HOH A . 
L 8 HOH 299 699 263 HOH HOH A . 
L 8 HOH 300 700 240 HOH HOH A . 
L 8 HOH 301 701 320 HOH HOH A . 
L 8 HOH 302 702 146 HOH HOH A . 
L 8 HOH 303 703 329 HOH HOH A . 
L 8 HOH 304 704 308 HOH HOH A . 
L 8 HOH 305 705 142 HOH HOH A . 
L 8 HOH 306 706 288 HOH HOH A . 
L 8 HOH 307 707 94  HOH HOH A . 
L 8 HOH 308 708 221 HOH HOH A . 
L 8 HOH 309 709 149 HOH HOH A . 
L 8 HOH 310 710 280 HOH HOH A . 
L 8 HOH 311 711 214 HOH HOH A . 
L 8 HOH 312 712 49  HOH HOH A . 
L 8 HOH 313 713 327 HOH HOH A . 
L 8 HOH 314 714 253 HOH HOH A . 
L 8 HOH 315 715 192 HOH HOH A . 
L 8 HOH 316 716 127 HOH HOH A . 
L 8 HOH 317 717 217 HOH HOH A . 
L 8 HOH 318 718 195 HOH HOH A . 
L 8 HOH 319 719 255 HOH HOH A . 
L 8 HOH 320 720 321 HOH HOH A . 
L 8 HOH 321 721 134 HOH HOH A . 
L 8 HOH 322 722 248 HOH HOH A . 
L 8 HOH 323 723 222 HOH HOH A . 
L 8 HOH 324 724 234 HOH HOH A . 
L 8 HOH 325 725 246 HOH HOH A . 
L 8 HOH 326 726 268 HOH HOH A . 
L 8 HOH 327 727 294 HOH HOH A . 
L 8 HOH 328 728 247 HOH HOH A . 
L 8 HOH 329 729 261 HOH HOH A . 
L 8 HOH 330 730 224 HOH HOH A . 
L 8 HOH 331 731 223 HOH HOH A . 
L 8 HOH 332 732 245 HOH HOH A . 
L 8 HOH 333 733 220 HOH HOH A . 
# 
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 scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20   3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .      4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .      5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.350 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5OGO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.094 
_cell.length_a_esd                 ? 
_cell.length_b                     41.426 
_cell.length_b_esd                 ? 
_cell.length_c                     71.654 
_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                         5OGO 
_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                   5OGO 
_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            2.06 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.40 
_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              0.000 
_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          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer: 0.1M sodium bicine (pH 9.0), 0.2M  ammonium sulfate and 2M sodium malonate (pH 7.0)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 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         2013-05-22 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.976300 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976300 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5OGO 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                0.988 
_reflns.d_resolution_low                 41.426 
_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                       128596 
_reflns.number_obs                       128596 
_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                  3.200 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.039 
_reflns.pdbx_netI_over_av_sigmaI         4.107 
_reflns.pdbx_netI_over_sigmaI            14.100 
_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                  0.056 
_reflns.pdbx_Rpim_I_all                  0.030 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         410103 
_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 
0.990 1.040  ? 2.900  ? ? ? ? ? 85.000 ? ? ? ? 0.262 ? ? ? ? ? ? ? ? 2.800 0.262 ? ? ? 0.353 0.204 ? 1  1 ? ? 
1.040 1.110  ? 4.800  ? ? ? ? ? 96.200 ? ? ? ? 0.160 ? ? ? ? ? ? ? ? 3.000 0.160 ? ? ? 0.216 0.123 ? 2  1 ? ? 
1.110 1.180  ? 7.400  ? ? ? ? ? 98.300 ? ? ? ? 0.102 ? ? ? ? ? ? ? ? 3.100 0.102 ? ? ? 0.140 0.078 ? 3  1 ? ? 
1.180 1.280  ? 9.700  ? ? ? ? ? 97.900 ? ? ? ? 0.077 ? ? ? ? ? ? ? ? 3.200 0.077 ? ? ? 0.110 0.061 ? 4  1 ? ? 
1.280 1.400  ? 12.100 ? ? ? ? ? 99.000 ? ? ? ? 0.059 ? ? ? ? ? ? ? ? 3.400 0.059 ? ? ? 0.087 0.047 ? 5  1 ? ? 
1.400 1.560  ? 15.300 ? ? ? ? ? 98.500 ? ? ? ? 0.045 ? ? ? ? ? ? ? ? 3.300 0.045 ? ? ? 0.069 0.037 ? 6  1 ? ? 
1.560 1.800  ? 18.400 ? ? ? ? ? 99.400 ? ? ? ? 0.035 ? ? ? ? ? ? ? ? 3.500 0.035 ? ? ? 0.055 0.029 ? 7  1 ? ? 
1.800 2.210  ? 20.100 ? ? ? ? ? 98.700 ? ? ? ? 0.030 ? ? ? ? ? ? ? ? 3.300 0.030 ? ? ? 0.045 0.024 ? 8  1 ? ? 
2.210 3.130  ? 20.500 ? ? ? ? ? 99.700 ? ? ? ? 0.027 ? ? ? ? ? ? ? ? 3.500 0.027 ? ? ? 0.041 0.022 ? 9  1 ? ? 
3.130 41.426 ? 9.200  ? ? ? ? ? 99.200 ? ? ? ? 0.040 ? ? ? ? ? ? ? ? 3.400 0.040 ? ? ? 0.054 0.029 ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            0.1000 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.1400 
_refine.aniso_B[2][2]                            -0.0900 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.0600 
_refine.B_iso_max                                151.120 
_refine.B_iso_mean                               14.4340 
_refine.B_iso_min                                4.920 
_refine.correlation_coeff_Fo_to_Fc               0.9800 
_refine.correlation_coeff_Fo_to_Fc_free          0.9720 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 5OGO 
_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                            0.9900 
_refine.ls_d_res_low                             39.7200 
_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                     115769 
_refine.ls_number_reflns_R_free                  12806 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.2400 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1268 
_refine.ls_R_factor_R_free                       0.1484 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1244 
_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                       0.0220 
_refine.pdbx_overall_ESU_R_Free                  0.0240 
_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             0.0225 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9900 
_refine_hist.d_res_low                        39.7200 
_refine_hist.pdbx_number_atoms_ligand         134 
_refine_hist.number_atoms_solvent             333 
_refine_hist.number_atoms_total               2530 
_refine_hist.pdbx_number_residues_total       258 
_refine_hist.pdbx_B_iso_mean_ligand           25.67 
_refine_hist.pdbx_B_iso_mean_solvent          25.41 
_refine_hist.pdbx_number_atoms_protein        2063 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.025  0.020  2518 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.834  2.003  3451 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.151  5.000  310  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 37.498 24.587 109  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.183 15.000 400  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 19.951 15.000 8    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.268  0.200  341  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.021  1989 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 9.464  3.000  2518 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 22.998 5.000  334  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 14.126 5.000  2427 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       0.9880 
_refine_ls_shell.d_res_low                        1.0140 
_refine_ls_shell.number_reflns_all                7114 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             679 
_refine_ls_shell.number_reflns_R_work             6435 
_refine_ls_shell.percent_reflns_obs               72.6100 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.1960 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1830 
_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                     5OGO 
_struct.title                        
;Crystal structure of chimeric carbonic anhydrase I with 3-(Benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        5OGO 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, double binding, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 7 ? 
I N N 7 ? 
J N N 5 ? 
K N N 5 ? 
L 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              5OGO 
_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 5OGO VAL A 62  ? UNP P00918 ASN 62  'engineered mutation' 62  1 
1 5OGO HIS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 5OGO PHE A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 5OGO ALA A 121 ? UNP P00918 VAL 121 'engineered mutation' 121 4 
1 5OGO LEU A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 5 
1 5OGO ALA A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 6 
1 5OGO HIS A 199 ? UNP P00918 THR 199 'engineered mutation' 200 7 
1 5OGO TYR A 203 ? UNP P00918 LEU 203 'engineered mutation' 204 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1630  ? 
1 MORE         11    ? 
1 'SSA (A^2)'  11930 ? 
# 
_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,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ASP A 19  ? HIS A 15  ASP A 19  5 ? 5 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? ALA A 134 ? ASP A 130 ALA 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 ? ILE A 166 ? ASP A 165 ILE A 167 5 ? 3 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.989 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.004 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C WWO . N10 ? ? A ZN  301 A WWO 302 1_555 ? ? ? ? ? ? ? 1.948 ? ? 
# 
_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_555 105.5 ? 
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_555 110.6 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 100.0 ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C WWO .   ? A WWO 302 ? 1_555 111.0 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C WWO .   ? A WWO 302 ? 1_555 114.2 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C WWO .   ? A WWO 302 ? 1_555 114.9 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -2.45 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 16.71 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  SER A 48  ? SER A 50  ? SER A 48  SER A 50  
AA3 2  VAL A 78  ? LYS A 80  ? VAL A 78  LYS A 80  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A WWO 302 ? 15 'binding site for residue WWO A 302' 
AC3 Software A WWO 303 ? 12 'binding site for residue WWO A 303' 
AC4 Software A DMS 304 ? 3  'binding site for residue DMS A 304' 
AC5 Software A BCN 305 ? 8  'binding site for residue BCN A 305' 
AC6 Software A PEG 306 ? 9  'binding site for residue PEG A 306' 
AC7 Software A EDO 307 ? 6  'binding site for residue EDO A 307' 
AC8 Software A EDO 308 ? 6  'binding site for residue EDO A 308' 
AC9 Software A BCN 309 ? 6  'binding site for residue BCN A 309' 
AD1 Software A BCN 310 ? 8  'binding site for residue BCN A 310' 
# 
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  WWO C .   ? WWO A 302 . ? 1_555 ? 
5  AC2 15 HIS A 64  ? HIS A 64  . ? 1_555 ? 
6  AC2 15 HIS A 67  ? HIS A 67  . ? 1_555 ? 
7  AC2 15 PHE A 91  ? PHE A 91  . ? 1_555 ? 
8  AC2 15 GLN A 92  ? GLN A 92  . ? 1_555 ? 
9  AC2 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
10 AC2 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
11 AC2 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
12 AC2 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
13 AC2 15 THR A 198 ? THR A 199 . ? 1_555 ? 
14 AC2 15 HIS A 199 ? HIS A 200 . ? 1_555 ? 
15 AC2 15 PRO A 200 ? PRO A 201 . ? 1_555 ? 
16 AC2 15 PRO A 201 ? PRO A 202 . ? 1_555 ? 
17 AC2 15 TRP A 208 ? TRP A 209 . ? 1_555 ? 
18 AC2 15 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
19 AC2 15 WWO D .   ? WWO A 303 . ? 1_555 ? 
20 AC3 12 HIS A 67  ? HIS A 67  . ? 1_555 ? 
21 AC3 12 GLU A 69  ? GLU A 69  . ? 1_555 ? 
22 AC3 12 PHE A 91  ? PHE A 91  . ? 1_555 ? 
23 AC3 12 GLN A 92  ? GLN A 92  . ? 1_555 ? 
24 AC3 12 ASP A 129 ? ASP A 130 . ? 1_555 ? 
25 AC3 12 LEU A 130 ? LEU A 131 . ? 1_555 ? 
26 AC3 12 GLY A 131 ? GLY A 132 . ? 1_555 ? 
27 AC3 12 WWO C .   ? WWO A 302 . ? 1_555 ? 
28 AC3 12 BCN K .   ? BCN A 310 . ? 1_565 ? 
29 AC3 12 HOH L .   ? HOH A 539 . ? 1_555 ? 
30 AC3 12 HOH L .   ? HOH A 582 . ? 1_555 ? 
31 AC3 12 HOH L .   ? HOH A 627 . ? 1_555 ? 
32 AC4 3  TYR A 7   ? TYR A 7   . ? 1_555 ? 
33 AC4 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
34 AC4 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
35 AC5 8  LYS A 148 ? LYS A 149 . ? 1_555 ? 
36 AC5 8  LYS A 212 ? LYS A 213 . ? 1_555 ? 
37 AC5 8  GLU A 213 ? GLU A 214 . ? 1_555 ? 
38 AC5 8  PRO A 214 ? PRO A 215 . ? 1_555 ? 
39 AC5 8  HOH L .   ? HOH A 448 . ? 1_555 ? 
40 AC5 8  HOH L .   ? HOH A 451 . ? 1_555 ? 
41 AC5 8  HOH L .   ? HOH A 560 . ? 1_555 ? 
42 AC5 8  HOH L .   ? HOH A 651 . ? 1_555 ? 
43 AC6 9  HIS A 17  ? HIS A 17  . ? 1_555 ? 
44 AC6 9  PRO A 21  ? PRO A 21  . ? 1_555 ? 
45 AC6 9  PRO A 46  ? PRO A 46  . ? 1_655 ? 
46 AC6 9  LEU A 47  ? LEU A 47  . ? 1_655 ? 
47 AC6 9  SER A 48  ? SER A 48  . ? 1_655 ? 
48 AC6 9  HOH L .   ? HOH A 404 . ? 1_655 ? 
49 AC6 9  HOH L .   ? HOH A 417 . ? 1_555 ? 
50 AC6 9  HOH L .   ? HOH A 473 . ? 1_655 ? 
51 AC6 9  HOH L .   ? HOH A 669 . ? 1_555 ? 
52 AC7 6  PRO A 83  ? PRO A 83  . ? 1_555 ? 
53 AC7 6  LEU A 84  ? LEU A 84  . ? 1_555 ? 
54 AC7 6  THR A 207 ? THR A 208 . ? 1_555 ? 
55 AC7 6  HOH L .   ? HOH A 408 . ? 1_555 ? 
56 AC7 6  HOH L .   ? HOH A 500 . ? 1_555 ? 
57 AC7 6  HOH L .   ? HOH A 663 . ? 1_555 ? 
58 AC8 6  PRO A 46  ? PRO A 46  . ? 1_555 ? 
59 AC8 6  LEU A 47  ? LEU A 47  . ? 1_555 ? 
60 AC8 6  LEU A 188 ? LEU A 189 . ? 1_555 ? 
61 AC8 6  ASP A 189 ? ASP A 190 . ? 1_555 ? 
62 AC8 6  SER A 258 ? SER A 259 . ? 1_555 ? 
63 AC8 6  HOH L .   ? HOH A 694 . ? 1_455 ? 
64 AC9 6  SER A 99  ? SER A 99  . ? 1_555 ? 
65 AC9 6  ARG A 226 ? ARG A 227 . ? 1_555 ? 
66 AC9 6  BCN K .   ? BCN A 310 . ? 1_555 ? 
67 AC9 6  HOH L .   ? HOH A 461 . ? 1_555 ? 
68 AC9 6  HOH L .   ? HOH A 462 . ? 1_555 ? 
69 AC9 6  HOH L .   ? HOH A 475 . ? 1_555 ? 
70 AD1 8  SER A 99  ? SER A 99  . ? 1_555 ? 
71 AD1 8  LEU A 100 ? LEU A 100 . ? 1_555 ? 
72 AD1 8  ASP A 101 ? ASP A 101 . ? 1_555 ? 
73 AD1 8  ASP A 129 ? ASP A 130 . ? 1_545 ? 
74 AD1 8  LEU A 223 ? LEU A 224 . ? 1_555 ? 
75 AD1 8  ARG A 226 ? ARG A 227 . ? 1_555 ? 
76 AD1 8  WWO D .   ? WWO A 303 . ? 1_545 ? 
77 AD1 8  BCN J .   ? BCN A 309 . ? 1_555 ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OE1 A GLU 214 ? A O A HOH 401 ? ? 1.91 
2  1 NE2 A GLN 103 ? B O A HOH 402 ? ? 1.92 
3  1 O   A HOH 596 ? ? O A HOH 632 ? ? 1.92 
4  1 O   A HOH 596 ? ? O A HOH 621 ? ? 2.10 
5  1 CG  A LYS 133 ? A O A HOH 458 ? ? 2.12 
6  1 OD1 A ASP 52  ? ? O A HOH 403 ? ? 2.16 
7  1 O   A PRO 46  ? A O A HOH 404 ? ? 2.16 
8  1 CD1 A LEU 224 ? B O A HOH 462 ? ? 2.16 
9  1 O   A ASP 19  ? ? O A HOH 405 ? ? 2.17 
10 1 N   A ARG 254 ? ? O A HOH 406 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 C6  A BCN 309 ? ? 1_555 O A HOH 642 ? ? 2_645 1.97 
2 1 O25 A WWO 303 ? A 1_555 O A HOH 457 ? ? 2_655 2.13 
3 1 O   A HOH 693 ? ? 1_555 O A HOH 705 ? ? 2_646 2.14 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A HIS 3   ? ? CD2 A HIS 3   ? ? 1.415 1.354 0.061 0.009 N 
2 1 CG A HIS 4   ? ? CD2 A HIS 4   ? ? 1.421 1.354 0.067 0.009 N 
3 1 C  A THR 125 ? ? N   A LYS 127 ? B 1.524 1.336 0.188 0.023 Y 
4 1 C  A ASP 130 ? B O   A ASP 130 ? B 1.367 1.229 0.138 0.019 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 O A THR 125 ? ? C A THR 125 ? ? N  A LYS 127 ? B 109.48 122.70 -13.22 1.60 Y 
2 1 C A THR 125 ? ? N A LYS 127 ? A CA A LYS 127 ? A 100.76 121.70 -20.94 2.50 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 11  ? ? -179.44 7.85    
2  1 ASN A 11  ? ? -153.04 7.85    
3  1 ARG A 27  ? ? -144.29 55.43   
4  1 ALA A 65  ? ? -170.02 -176.33 
5  1 LYS A 76  ? ? -107.86 -96.57  
6  1 LYS A 76  ? ? -122.46 -96.57  
7  1 GLU A 106 ? ? -91.23  -61.73  
8  1 LYS A 111 ? ? 74.98   -5.60   
9  1 THR A 125 ? ? -64.10  1.26    
10 1 PHE A 176 ? ? -151.64 60.61   
11 1 ASN A 244 ? ? -97.47  45.92   
12 1 LYS A 252 ? ? 56.52   -143.30 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 THR A 125 ? ? -13.96 
2 1 THR A 125 ? ? -13.88 
# 
_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 
# 
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 
GLN N    N  N N 132 
GLN CA   C  N S 133 
GLN C    C  N N 134 
GLN O    O  N N 135 
GLN CB   C  N N 136 
GLN CG   C  N N 137 
GLN CD   C  N N 138 
GLN OE1  O  N N 139 
GLN NE2  N  N N 140 
GLN OXT  O  N N 141 
GLN H    H  N N 142 
GLN H2   H  N N 143 
GLN HA   H  N N 144 
GLN HB2  H  N N 145 
GLN HB3  H  N N 146 
GLN HG2  H  N N 147 
GLN HG3  H  N N 148 
GLN HE21 H  N N 149 
GLN HE22 H  N N 150 
GLN HXT  H  N N 151 
GLU N    N  N N 152 
GLU CA   C  N S 153 
GLU C    C  N N 154 
GLU O    O  N N 155 
GLU CB   C  N N 156 
GLU CG   C  N N 157 
GLU CD   C  N N 158 
GLU OE1  O  N N 159 
GLU OE2  O  N N 160 
GLU OXT  O  N N 161 
GLU H    H  N N 162 
GLU H2   H  N N 163 
GLU HA   H  N N 164 
GLU HB2  H  N N 165 
GLU HB3  H  N N 166 
GLU HG2  H  N N 167 
GLU HG3  H  N N 168 
GLU HE2  H  N N 169 
GLU HXT  H  N N 170 
GLY N    N  N N 171 
GLY CA   C  N N 172 
GLY C    C  N N 173 
GLY O    O  N N 174 
GLY OXT  O  N N 175 
GLY H    H  N N 176 
GLY H2   H  N N 177 
GLY HA2  H  N N 178 
GLY HA3  H  N N 179 
GLY HXT  H  N N 180 
HIS N    N  N N 181 
HIS CA   C  N S 182 
HIS C    C  N N 183 
HIS O    O  N N 184 
HIS CB   C  N N 185 
HIS CG   C  Y N 186 
HIS ND1  N  Y N 187 
HIS CD2  C  Y N 188 
HIS CE1  C  Y N 189 
HIS NE2  N  Y N 190 
HIS OXT  O  N N 191 
HIS H    H  N N 192 
HIS H2   H  N N 193 
HIS HA   H  N N 194 
HIS HB2  H  N N 195 
HIS HB3  H  N N 196 
HIS HD1  H  N N 197 
HIS HD2  H  N N 198 
HIS HE1  H  N N 199 
HIS HE2  H  N N 200 
HIS HXT  H  N N 201 
HOH O    O  N N 202 
HOH H1   H  N N 203 
HOH H2   H  N N 204 
ILE N    N  N N 205 
ILE CA   C  N S 206 
ILE C    C  N N 207 
ILE O    O  N N 208 
ILE CB   C  N S 209 
ILE CG1  C  N N 210 
ILE CG2  C  N N 211 
ILE CD1  C  N N 212 
ILE OXT  O  N N 213 
ILE H    H  N N 214 
ILE H2   H  N N 215 
ILE HA   H  N N 216 
ILE HB   H  N N 217 
ILE HG12 H  N N 218 
ILE HG13 H  N N 219 
ILE HG21 H  N N 220 
ILE HG22 H  N N 221 
ILE HG23 H  N N 222 
ILE HD11 H  N N 223 
ILE HD12 H  N N 224 
ILE HD13 H  N N 225 
ILE HXT  H  N N 226 
LEU N    N  N N 227 
LEU CA   C  N S 228 
LEU C    C  N N 229 
LEU O    O  N N 230 
LEU CB   C  N N 231 
LEU CG   C  N N 232 
LEU CD1  C  N N 233 
LEU CD2  C  N N 234 
LEU OXT  O  N N 235 
LEU H    H  N N 236 
LEU H2   H  N N 237 
LEU HA   H  N N 238 
LEU HB2  H  N N 239 
LEU HB3  H  N N 240 
LEU HG   H  N N 241 
LEU HD11 H  N N 242 
LEU HD12 H  N N 243 
LEU HD13 H  N N 244 
LEU HD21 H  N N 245 
LEU HD22 H  N N 246 
LEU HD23 H  N N 247 
LEU HXT  H  N N 248 
LYS N    N  N N 249 
LYS CA   C  N S 250 
LYS C    C  N N 251 
LYS O    O  N N 252 
LYS CB   C  N N 253 
LYS CG   C  N N 254 
LYS CD   C  N N 255 
LYS CE   C  N N 256 
LYS NZ   N  N N 257 
LYS OXT  O  N N 258 
LYS H    H  N N 259 
LYS H2   H  N N 260 
LYS HA   H  N N 261 
LYS HB2  H  N N 262 
LYS HB3  H  N N 263 
LYS HG2  H  N N 264 
LYS HG3  H  N N 265 
LYS HD2  H  N N 266 
LYS HD3  H  N N 267 
LYS HE2  H  N N 268 
LYS HE3  H  N N 269 
LYS HZ1  H  N N 270 
LYS HZ2  H  N N 271 
LYS HZ3  H  N N 272 
LYS HXT  H  N N 273 
MET N    N  N N 274 
MET CA   C  N S 275 
MET C    C  N N 276 
MET O    O  N N 277 
MET CB   C  N N 278 
MET CG   C  N N 279 
MET SD   S  N N 280 
MET CE   C  N N 281 
MET OXT  O  N N 282 
MET H    H  N N 283 
MET H2   H  N N 284 
MET HA   H  N N 285 
MET HB2  H  N N 286 
MET HB3  H  N N 287 
MET HG2  H  N N 288 
MET HG3  H  N N 289 
MET HE1  H  N N 290 
MET HE2  H  N N 291 
MET HE3  H  N N 292 
MET HXT  H  N N 293 
PEG C1   C  N N 294 
PEG O1   O  N N 295 
PEG C2   C  N N 296 
PEG O2   O  N N 297 
PEG C3   C  N N 298 
PEG C4   C  N N 299 
PEG O4   O  N N 300 
PEG H11  H  N N 301 
PEG H12  H  N N 302 
PEG HO1  H  N N 303 
PEG H21  H  N N 304 
PEG H22  H  N N 305 
PEG H31  H  N N 306 
PEG H32  H  N N 307 
PEG H41  H  N N 308 
PEG H42  H  N N 309 
PEG HO4  H  N N 310 
PHE N    N  N N 311 
PHE CA   C  N S 312 
PHE C    C  N N 313 
PHE O    O  N N 314 
PHE CB   C  N N 315 
PHE CG   C  Y N 316 
PHE CD1  C  Y N 317 
PHE CD2  C  Y N 318 
PHE CE1  C  Y N 319 
PHE CE2  C  Y N 320 
PHE CZ   C  Y N 321 
PHE OXT  O  N N 322 
PHE H    H  N N 323 
PHE H2   H  N N 324 
PHE HA   H  N N 325 
PHE HB2  H  N N 326 
PHE HB3  H  N N 327 
PHE HD1  H  N N 328 
PHE HD2  H  N N 329 
PHE HE1  H  N N 330 
PHE HE2  H  N N 331 
PHE HZ   H  N N 332 
PHE HXT  H  N N 333 
PRO N    N  N N 334 
PRO CA   C  N S 335 
PRO C    C  N N 336 
PRO O    O  N N 337 
PRO CB   C  N N 338 
PRO CG   C  N N 339 
PRO CD   C  N N 340 
PRO OXT  O  N N 341 
PRO H    H  N N 342 
PRO HA   H  N N 343 
PRO HB2  H  N N 344 
PRO HB3  H  N N 345 
PRO HG2  H  N N 346 
PRO HG3  H  N N 347 
PRO HD2  H  N N 348 
PRO HD3  H  N N 349 
PRO HXT  H  N N 350 
SER N    N  N N 351 
SER CA   C  N S 352 
SER C    C  N N 353 
SER O    O  N N 354 
SER CB   C  N N 355 
SER OG   O  N N 356 
SER OXT  O  N N 357 
SER H    H  N N 358 
SER H2   H  N N 359 
SER HA   H  N N 360 
SER HB2  H  N N 361 
SER HB3  H  N N 362 
SER HG   H  N N 363 
SER HXT  H  N N 364 
THR N    N  N N 365 
THR CA   C  N S 366 
THR C    C  N N 367 
THR O    O  N N 368 
THR CB   C  N R 369 
THR OG1  O  N N 370 
THR CG2  C  N N 371 
THR OXT  O  N N 372 
THR H    H  N N 373 
THR H2   H  N N 374 
THR HA   H  N N 375 
THR HB   H  N N 376 
THR HG1  H  N N 377 
THR HG21 H  N N 378 
THR HG22 H  N N 379 
THR HG23 H  N N 380 
THR HXT  H  N N 381 
TRP N    N  N N 382 
TRP CA   C  N S 383 
TRP C    C  N N 384 
TRP O    O  N N 385 
TRP CB   C  N N 386 
TRP CG   C  Y N 387 
TRP CD1  C  Y N 388 
TRP CD2  C  Y N 389 
TRP NE1  N  Y N 390 
TRP CE2  C  Y N 391 
TRP CE3  C  Y N 392 
TRP CZ2  C  Y N 393 
TRP CZ3  C  Y N 394 
TRP CH2  C  Y N 395 
TRP OXT  O  N N 396 
TRP H    H  N N 397 
TRP H2   H  N N 398 
TRP HA   H  N N 399 
TRP HB2  H  N N 400 
TRP HB3  H  N N 401 
TRP HD1  H  N N 402 
TRP HE1  H  N N 403 
TRP HE3  H  N N 404 
TRP HZ2  H  N N 405 
TRP HZ3  H  N N 406 
TRP HH2  H  N N 407 
TRP HXT  H  N N 408 
TYR N    N  N N 409 
TYR CA   C  N S 410 
TYR C    C  N N 411 
TYR O    O  N N 412 
TYR CB   C  N N 413 
TYR CG   C  Y N 414 
TYR CD1  C  Y N 415 
TYR CD2  C  Y N 416 
TYR CE1  C  Y N 417 
TYR CE2  C  Y N 418 
TYR CZ   C  Y N 419 
TYR OH   O  N N 420 
TYR OXT  O  N N 421 
TYR H    H  N N 422 
TYR H2   H  N N 423 
TYR HA   H  N N 424 
TYR HB2  H  N N 425 
TYR HB3  H  N N 426 
TYR HD1  H  N N 427 
TYR HD2  H  N N 428 
TYR HE1  H  N N 429 
TYR HE2  H  N N 430 
TYR HH   H  N N 431 
TYR HXT  H  N N 432 
VAL N    N  N N 433 
VAL CA   C  N S 434 
VAL C    C  N N 435 
VAL O    O  N N 436 
VAL CB   C  N N 437 
VAL CG1  C  N N 438 
VAL CG2  C  N N 439 
VAL OXT  O  N N 440 
VAL H    H  N N 441 
VAL H2   H  N N 442 
VAL HA   H  N N 443 
VAL HB   H  N N 444 
VAL HG11 H  N N 445 
VAL HG12 H  N N 446 
VAL HG13 H  N N 447 
VAL HG21 H  N N 448 
VAL HG22 H  N N 449 
VAL HG23 H  N N 450 
VAL HXT  H  N N 451 
WWO F27  F  N N 452 
WWO C5   C  Y N 453 
WWO C4   C  Y N 454 
WWO S7   S  N N 455 
WWO O9   O  N N 456 
WWO N10  N  N N 457 
WWO O8   O  N N 458 
WWO C3   C  Y N 459 
WWO F12  F  N N 460 
WWO C2   C  Y N 461 
WWO F13  F  N N 462 
WWO C6   C  Y N 463 
WWO C1   C  Y N 464 
WWO S11  S  N N 465 
WWO O22  O  N N 466 
WWO O23  O  N N 467 
WWO C21  C  N N 468 
WWO C24  C  N N 469 
WWO O25  O  N N 470 
WWO N26  N  N N 471 
WWO C14  C  N N 472 
WWO C15  C  Y N 473 
WWO C20  C  Y N 474 
WWO C19  C  Y N 475 
WWO C18  C  Y N 476 
WWO C17  C  Y N 477 
WWO C16  C  Y N 478 
WWO H1   H  N N 479 
WWO H2   H  N N 480 
WWO H3   H  N N 481 
WWO H4   H  N N 482 
WWO H5   H  N N 483 
WWO H6   H  N N 484 
WWO H7   H  N N 485 
WWO H8   H  N N 486 
WWO H9   H  N N 487 
WWO H10  H  N N 488 
WWO H11  H  N N 489 
WWO H12  H  N N 490 
WWO H13  H  N N 491 
WWO H14  H  N N 492 
WWO H15  H  N N 493 
ZN  ZN   ZN N N 494 
# 
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 
GLN N   CA   sing N N 124 
GLN N   H    sing N N 125 
GLN N   H2   sing N N 126 
GLN CA  C    sing N N 127 
GLN CA  CB   sing N N 128 
GLN CA  HA   sing N N 129 
GLN C   O    doub N N 130 
GLN C   OXT  sing N N 131 
GLN CB  CG   sing N N 132 
GLN CB  HB2  sing N N 133 
GLN CB  HB3  sing N N 134 
GLN CG  CD   sing N N 135 
GLN CG  HG2  sing N N 136 
GLN CG  HG3  sing N N 137 
GLN CD  OE1  doub N N 138 
GLN CD  NE2  sing N N 139 
GLN NE2 HE21 sing N N 140 
GLN NE2 HE22 sing N N 141 
GLN OXT HXT  sing N N 142 
GLU N   CA   sing N N 143 
GLU N   H    sing N N 144 
GLU N   H2   sing N N 145 
GLU CA  C    sing N N 146 
GLU CA  CB   sing N N 147 
GLU CA  HA   sing N N 148 
GLU C   O    doub N N 149 
GLU C   OXT  sing N N 150 
GLU CB  CG   sing N N 151 
GLU CB  HB2  sing N N 152 
GLU CB  HB3  sing N N 153 
GLU CG  CD   sing N N 154 
GLU CG  HG2  sing N N 155 
GLU CG  HG3  sing N N 156 
GLU CD  OE1  doub N N 157 
GLU CD  OE2  sing N N 158 
GLU OE2 HE2  sing N N 159 
GLU OXT HXT  sing N N 160 
GLY N   CA   sing N N 161 
GLY N   H    sing N N 162 
GLY N   H2   sing N N 163 
GLY CA  C    sing N N 164 
GLY CA  HA2  sing N N 165 
GLY CA  HA3  sing N N 166 
GLY C   O    doub N N 167 
GLY C   OXT  sing N N 168 
GLY OXT HXT  sing N N 169 
HIS N   CA   sing N N 170 
HIS N   H    sing N N 171 
HIS N   H2   sing N N 172 
HIS CA  C    sing N N 173 
HIS CA  CB   sing N N 174 
HIS CA  HA   sing N N 175 
HIS C   O    doub N N 176 
HIS C   OXT  sing N N 177 
HIS CB  CG   sing N N 178 
HIS CB  HB2  sing N N 179 
HIS CB  HB3  sing N N 180 
HIS CG  ND1  sing Y N 181 
HIS CG  CD2  doub Y N 182 
HIS ND1 CE1  doub Y N 183 
HIS ND1 HD1  sing N N 184 
HIS CD2 NE2  sing Y N 185 
HIS CD2 HD2  sing N N 186 
HIS CE1 NE2  sing Y N 187 
HIS CE1 HE1  sing N N 188 
HIS NE2 HE2  sing N N 189 
HIS OXT HXT  sing N N 190 
HOH O   H1   sing N N 191 
HOH O   H2   sing N N 192 
ILE N   CA   sing N N 193 
ILE N   H    sing N N 194 
ILE N   H2   sing N N 195 
ILE CA  C    sing N N 196 
ILE CA  CB   sing N N 197 
ILE CA  HA   sing N N 198 
ILE C   O    doub N N 199 
ILE C   OXT  sing N N 200 
ILE CB  CG1  sing N N 201 
ILE CB  CG2  sing N N 202 
ILE CB  HB   sing N N 203 
ILE CG1 CD1  sing N N 204 
ILE CG1 HG12 sing N N 205 
ILE CG1 HG13 sing N N 206 
ILE CG2 HG21 sing N N 207 
ILE CG2 HG22 sing N N 208 
ILE CG2 HG23 sing N N 209 
ILE CD1 HD11 sing N N 210 
ILE CD1 HD12 sing N N 211 
ILE CD1 HD13 sing N N 212 
ILE OXT HXT  sing N N 213 
LEU N   CA   sing N N 214 
LEU N   H    sing N N 215 
LEU N   H2   sing N N 216 
LEU CA  C    sing N N 217 
LEU CA  CB   sing N N 218 
LEU CA  HA   sing N N 219 
LEU C   O    doub N N 220 
LEU C   OXT  sing N N 221 
LEU CB  CG   sing N N 222 
LEU CB  HB2  sing N N 223 
LEU CB  HB3  sing N N 224 
LEU CG  CD1  sing N N 225 
LEU CG  CD2  sing N N 226 
LEU CG  HG   sing N N 227 
LEU CD1 HD11 sing N N 228 
LEU CD1 HD12 sing N N 229 
LEU CD1 HD13 sing N N 230 
LEU CD2 HD21 sing N N 231 
LEU CD2 HD22 sing N N 232 
LEU CD2 HD23 sing N N 233 
LEU OXT HXT  sing N N 234 
LYS N   CA   sing N N 235 
LYS N   H    sing N N 236 
LYS N   H2   sing N N 237 
LYS CA  C    sing N N 238 
LYS CA  CB   sing N N 239 
LYS CA  HA   sing N N 240 
LYS C   O    doub N N 241 
LYS C   OXT  sing N N 242 
LYS CB  CG   sing N N 243 
LYS CB  HB2  sing N N 244 
LYS CB  HB3  sing N N 245 
LYS CG  CD   sing N N 246 
LYS CG  HG2  sing N N 247 
LYS CG  HG3  sing N N 248 
LYS CD  CE   sing N N 249 
LYS CD  HD2  sing N N 250 
LYS CD  HD3  sing N N 251 
LYS CE  NZ   sing N N 252 
LYS CE  HE2  sing N N 253 
LYS CE  HE3  sing N N 254 
LYS NZ  HZ1  sing N N 255 
LYS NZ  HZ2  sing N N 256 
LYS NZ  HZ3  sing N N 257 
LYS OXT HXT  sing N N 258 
MET N   CA   sing N N 259 
MET N   H    sing N N 260 
MET N   H2   sing N N 261 
MET CA  C    sing N N 262 
MET CA  CB   sing N N 263 
MET CA  HA   sing N N 264 
MET C   O    doub N N 265 
MET C   OXT  sing N N 266 
MET CB  CG   sing N N 267 
MET CB  HB2  sing N N 268 
MET CB  HB3  sing N N 269 
MET CG  SD   sing N N 270 
MET CG  HG2  sing N N 271 
MET CG  HG3  sing N N 272 
MET SD  CE   sing N N 273 
MET CE  HE1  sing N N 274 
MET CE  HE2  sing N N 275 
MET CE  HE3  sing N N 276 
MET OXT HXT  sing N N 277 
PEG C1  O1   sing N N 278 
PEG C1  C2   sing N N 279 
PEG C1  H11  sing N N 280 
PEG C1  H12  sing N N 281 
PEG O1  HO1  sing N N 282 
PEG C2  O2   sing N N 283 
PEG C2  H21  sing N N 284 
PEG C2  H22  sing N N 285 
PEG O2  C3   sing N N 286 
PEG C3  C4   sing N N 287 
PEG C3  H31  sing N N 288 
PEG C3  H32  sing N N 289 
PEG C4  O4   sing N N 290 
PEG C4  H41  sing N N 291 
PEG C4  H42  sing N N 292 
PEG O4  HO4  sing N N 293 
PHE N   CA   sing N N 294 
PHE N   H    sing N N 295 
PHE N   H2   sing N N 296 
PHE CA  C    sing N N 297 
PHE CA  CB   sing N N 298 
PHE CA  HA   sing N N 299 
PHE C   O    doub N N 300 
PHE C   OXT  sing N N 301 
PHE CB  CG   sing N N 302 
PHE CB  HB2  sing N N 303 
PHE CB  HB3  sing N N 304 
PHE CG  CD1  doub Y N 305 
PHE CG  CD2  sing Y N 306 
PHE CD1 CE1  sing Y N 307 
PHE CD1 HD1  sing N N 308 
PHE CD2 CE2  doub Y N 309 
PHE CD2 HD2  sing N N 310 
PHE CE1 CZ   doub Y N 311 
PHE CE1 HE1  sing N N 312 
PHE CE2 CZ   sing Y N 313 
PHE CE2 HE2  sing N N 314 
PHE CZ  HZ   sing N N 315 
PHE OXT HXT  sing N N 316 
PRO N   CA   sing N N 317 
PRO N   CD   sing N N 318 
PRO N   H    sing N N 319 
PRO CA  C    sing N N 320 
PRO CA  CB   sing N N 321 
PRO CA  HA   sing N N 322 
PRO C   O    doub N N 323 
PRO C   OXT  sing N N 324 
PRO CB  CG   sing N N 325 
PRO CB  HB2  sing N N 326 
PRO CB  HB3  sing N N 327 
PRO CG  CD   sing N N 328 
PRO CG  HG2  sing N N 329 
PRO CG  HG3  sing N N 330 
PRO CD  HD2  sing N N 331 
PRO CD  HD3  sing N N 332 
PRO OXT HXT  sing N N 333 
SER N   CA   sing N N 334 
SER N   H    sing N N 335 
SER N   H2   sing N N 336 
SER CA  C    sing N N 337 
SER CA  CB   sing N N 338 
SER CA  HA   sing N N 339 
SER C   O    doub N N 340 
SER C   OXT  sing N N 341 
SER CB  OG   sing N N 342 
SER CB  HB2  sing N N 343 
SER CB  HB3  sing N N 344 
SER OG  HG   sing N N 345 
SER OXT HXT  sing N N 346 
THR N   CA   sing N N 347 
THR N   H    sing N N 348 
THR N   H2   sing N N 349 
THR CA  C    sing N N 350 
THR CA  CB   sing N N 351 
THR CA  HA   sing N N 352 
THR C   O    doub N N 353 
THR C   OXT  sing N N 354 
THR CB  OG1  sing N N 355 
THR CB  CG2  sing N N 356 
THR CB  HB   sing N N 357 
THR OG1 HG1  sing N N 358 
THR CG2 HG21 sing N N 359 
THR CG2 HG22 sing N N 360 
THR CG2 HG23 sing N N 361 
THR OXT HXT  sing N N 362 
TRP N   CA   sing N N 363 
TRP N   H    sing N N 364 
TRP N   H2   sing N N 365 
TRP CA  C    sing N N 366 
TRP CA  CB   sing N N 367 
TRP CA  HA   sing N N 368 
TRP C   O    doub N N 369 
TRP C   OXT  sing N N 370 
TRP CB  CG   sing N N 371 
TRP CB  HB2  sing N N 372 
TRP CB  HB3  sing N N 373 
TRP CG  CD1  doub Y N 374 
TRP CG  CD2  sing Y N 375 
TRP CD1 NE1  sing Y N 376 
TRP CD1 HD1  sing N N 377 
TRP CD2 CE2  doub Y N 378 
TRP CD2 CE3  sing Y N 379 
TRP NE1 CE2  sing Y N 380 
TRP NE1 HE1  sing N N 381 
TRP CE2 CZ2  sing Y N 382 
TRP CE3 CZ3  doub Y N 383 
TRP CE3 HE3  sing N N 384 
TRP CZ2 CH2  doub Y N 385 
TRP CZ2 HZ2  sing N N 386 
TRP CZ3 CH2  sing Y N 387 
TRP CZ3 HZ3  sing N N 388 
TRP CH2 HH2  sing N N 389 
TRP OXT HXT  sing N N 390 
TYR N   CA   sing N N 391 
TYR N   H    sing N N 392 
TYR N   H2   sing N N 393 
TYR CA  C    sing N N 394 
TYR CA  CB   sing N N 395 
TYR CA  HA   sing N N 396 
TYR C   O    doub N N 397 
TYR C   OXT  sing N N 398 
TYR CB  CG   sing N N 399 
TYR CB  HB2  sing N N 400 
TYR CB  HB3  sing N N 401 
TYR CG  CD1  doub Y N 402 
TYR CG  CD2  sing Y N 403 
TYR CD1 CE1  sing Y N 404 
TYR CD1 HD1  sing N N 405 
TYR CD2 CE2  doub Y N 406 
TYR CD2 HD2  sing N N 407 
TYR CE1 CZ   doub Y N 408 
TYR CE1 HE1  sing N N 409 
TYR CE2 CZ   sing Y N 410 
TYR CE2 HE2  sing N N 411 
TYR CZ  OH   sing N N 412 
TYR OH  HH   sing N N 413 
TYR OXT HXT  sing N N 414 
VAL N   CA   sing N N 415 
VAL N   H    sing N N 416 
VAL N   H2   sing N N 417 
VAL CA  C    sing N N 418 
VAL CA  CB   sing N N 419 
VAL CA  HA   sing N N 420 
VAL C   O    doub N N 421 
VAL C   OXT  sing N N 422 
VAL CB  CG1  sing N N 423 
VAL CB  CG2  sing N N 424 
VAL CB  HB   sing N N 425 
VAL CG1 HG11 sing N N 426 
VAL CG1 HG12 sing N N 427 
VAL CG1 HG13 sing N N 428 
VAL CG2 HG21 sing N N 429 
VAL CG2 HG22 sing N N 430 
VAL CG2 HG23 sing N N 431 
VAL OXT HXT  sing N N 432 
WWO O9  S7   doub N N 433 
WWO S7  N10  sing N N 434 
WWO S7  C4   sing N N 435 
WWO S7  O8   doub N N 436 
WWO C16 C17  doub Y N 437 
WWO C16 C15  sing Y N 438 
WWO F27 C5   sing N N 439 
WWO C17 C18  sing Y N 440 
WWO C14 C15  sing N N 441 
WWO C14 N26  sing N N 442 
WWO C4  C5   doub Y N 443 
WWO C4  C3   sing Y N 444 
WWO C5  C6   sing Y N 445 
WWO C15 C20  doub Y N 446 
WWO C3  F12  sing N N 447 
WWO C3  C2   doub Y N 448 
WWO C6  N26  sing N N 449 
WWO C6  C1   doub Y N 450 
WWO O23 S11  doub N N 451 
WWO C18 C19  doub Y N 452 
WWO C2  C1   sing Y N 453 
WWO C2  F13  sing N N 454 
WWO C1  S11  sing N N 455 
WWO O22 S11  doub N N 456 
WWO C20 C19  sing Y N 457 
WWO S11 C21  sing N N 458 
WWO C21 C24  sing N N 459 
WWO O25 C24  sing N N 460 
WWO N10 H1   sing N N 461 
WWO N10 H2   sing N N 462 
WWO C21 H3   sing N N 463 
WWO C21 H4   sing N N 464 
WWO C24 H5   sing N N 465 
WWO C24 H6   sing N N 466 
WWO O25 H7   sing N N 467 
WWO N26 H8   sing N N 468 
WWO C14 H9   sing N N 469 
WWO C14 H10  sing N N 470 
WWO C20 H11  sing N N 471 
WWO C19 H12  sing N N 472 
WWO C18 H13  sing N N 473 
WWO C17 H14  sing N N 474 
WWO C16 H15  sing N N 475 
# 
_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                    5OGO 
_atom_sites.fract_transf_matrix[1][1]   0.023756 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006079 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024139 
_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]   0.014406 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 3   ? 34.559  1.870   6.482   1.00 26.28  ? 3   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 3   ? 34.332  0.825   7.521   1.00 22.74  ? 3   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 3   ? 33.325  1.287   8.587   1.00 25.51  ? 3   HIS A C   1 
ATOM   4    O  O   . HIS A 1 3   ? 33.672  1.498   9.815   1.00 35.36  ? 3   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 3   ? 35.595  0.395   8.204   1.00 24.35  ? 3   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 3   ? 35.379  -0.758  9.075   1.00 22.59  ? 3   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 3   ? 35.376  -2.056  8.573   1.00 28.42  ? 3   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 3   ? 34.986  -0.816  10.433  1.00 21.53  ? 3   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 3   ? 35.084  -2.892  9.646   1.00 24.71  ? 3   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 3   ? 34.870  -2.108  10.763  1.00 26.38  ? 3   HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 4   ? 32.099  1.440   8.075   1.00 32.80  ? 4   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 4   ? 30.977  2.000   8.725   1.00 29.41  ? 4   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 4   ? 30.351  0.871   9.593   1.00 20.64  ? 4   HIS A C   1 
ATOM   14   O  O   . HIS A 1 4   ? 30.572  -0.306  9.338   1.00 19.58  ? 4   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 4   ? 29.972  2.592   7.612   1.00 99.24  ? 4   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 4   ? 29.466  3.875   8.006   1.00 90.87  ? 4   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 4   ? 28.792  4.664   7.110   1.00 88.87  ? 4   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 4   ? 29.614  4.572   9.235   1.00 108.42 ? 4   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 4   ? 28.426  5.799   7.767   1.00 118.52 ? 4   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 4   ? 28.942  5.743   9.080   1.00 102.70 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 29.516  1.223   10.485  1.00 18.10  ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 28.853  0.291   11.359  1.00 14.26  ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 27.865  -0.526  10.613  1.00 12.70  ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 27.313  -0.115  9.547   1.00 14.40  ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 28.160  1.036   12.473  1.00 12.07  ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 26.929  1.793   12.068  1.00 10.97  ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 26.850  3.116   11.702  1.00 13.10  ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 25.589  1.288   12.005  1.00 10.06  ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 25.580  3.445   11.370  1.00 13.29  ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 24.749  2.369   11.561  1.00 11.04  ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 25.006  0.055   12.330  1.00 10.19  ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 23.379  2.210   11.411  1.00 12.49  ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 23.646  -0.108  12.154  1.00 10.71  ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 22.847  0.949   11.705  1.00 11.34  ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 27.590  -1.712  11.085  1.00 12.35  ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 26.568  -2.576  10.471  1.00 12.67  ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 26.194  -3.629  11.472  1.00 11.07  ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 26.209  -3.441  12.676  1.00 11.59  ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 25.801  -4.807  10.947  1.00 12.43  ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 25.402  -5.922  11.784  1.00 13.99  ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 26.331  -7.104  11.696  1.00 15.39  ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 26.023  -8.113  12.300  1.00 18.99  ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 23.910  -6.272  11.526  1.00 13.64  ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 22.995  -5.201  12.033  1.00 10.07  ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 22.573  -5.232  13.368  1.00 9.60   ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 22.568  -4.156  11.225  1.00 10.20  ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 21.732  -4.213  13.846  1.00 8.13   ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 21.730  -3.189  11.692  1.00 9.65   ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 21.298  -3.219  13.019  1.00 7.75   ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? 20.468  -2.219  13.423  1.00 8.20   ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 27.379  -7.011  10.899  1.00 17.47  ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 28.303  -8.180  10.764  1.00 20.40  ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 29.339  -8.351  11.834  1.00 17.29  ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 29.478  -7.587  12.766  1.00 15.73  ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 30.137  -9.391  11.693  1.00 17.47  ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 31.206  -9.680  12.607  1.00 17.30  ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 32.239  -8.481  12.908  1.00 15.05  ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 32.613  -8.283  14.061  1.00 15.78  ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 32.037  -10.867 12.067  1.00 21.49  ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 33.333  -11.161 12.825  1.00 26.75  ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 33.840  -12.561 12.574  1.00 31.80  ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 34.688  -13.038 13.762  1.00 40.24  ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 34.226  -14.351 14.319  1.00 61.38  ? 9   LYS A NZ  1 
ATOM   64   N  N   A HIS A 1 10  ? 32.491  -7.812  11.793  0.50 14.46  ? 10  HIS A N   1 
ATOM   65   N  N   B HIS A 1 10  ? 32.709  -7.787  11.870  0.50 11.59  ? 10  HIS A N   1 
ATOM   66   C  CA  A HIS A 1 10  ? 33.544  -6.922  11.514  0.50 11.71  ? 10  HIS A CA  1 
ATOM   67   C  CA  B HIS A 1 10  ? 33.726  -6.753  12.048  0.50 10.07  ? 10  HIS A CA  1 
ATOM   68   C  C   A HIS A 1 10  ? 33.002  -5.516  11.687  0.50 14.82  ? 10  HIS A C   1 
ATOM   69   C  C   B HIS A 1 10  ? 33.144  -5.410  12.207  0.50 10.51  ? 10  HIS A C   1 
ATOM   70   O  O   A HIS A 1 10  ? 33.653  -4.554  11.225  0.50 14.46  ? 10  HIS A O   1 
ATOM   71   O  O   B HIS A 1 10  ? 33.882  -4.402  12.217  0.50 11.54  ? 10  HIS A O   1 
ATOM   72   C  CB  A HIS A 1 10  ? 33.983  -7.149  10.037  0.50 11.80  ? 10  HIS A CB  1 
ATOM   73   C  CB  B HIS A 1 10  ? 34.718  -6.725  10.885  0.50 9.31   ? 10  HIS A CB  1 
ATOM   74   C  CG  A HIS A 1 10  ? 34.462  -8.514  9.714   0.50 11.77  ? 10  HIS A CG  1 
ATOM   75   C  CG  B HIS A 1 10  ? 35.362  -8.058  10.653  0.50 9.90   ? 10  HIS A CG  1 
ATOM   76   N  ND1 A HIS A 1 10  ? 35.416  -9.129  10.466  0.50 13.76  ? 10  HIS A ND1 1 
ATOM   77   N  ND1 B HIS A 1 10  ? 36.378  -8.526  11.403  0.50 10.75  ? 10  HIS A ND1 1 
ATOM   78   C  CD2 A HIS A 1 10  ? 34.068  -9.397  8.760   0.50 15.96  ? 10  HIS A CD2 1 
ATOM   79   C  CD2 B HIS A 1 10  ? 35.002  -9.104  9.788   0.50 11.66  ? 10  HIS A CD2 1 
ATOM   80   C  CE1 A HIS A 1 10  ? 35.637  -10.365 9.954   0.50 16.64  ? 10  HIS A CE1 1 
ATOM   81   C  CE1 B HIS A 1 10  ? 36.651  -9.800  11.041  0.50 11.84  ? 10  HIS A CE1 1 
ATOM   82   N  NE2 A HIS A 1 10  ? 34.822  -10.520 8.900   0.50 19.15  ? 10  HIS A NE2 1 
ATOM   83   N  NE2 B HIS A 1 10  ? 35.833  -10.133 10.031  0.50 12.68  ? 10  HIS A NE2 1 
ATOM   84   N  N   . ASN A 1 11  ? 31.828  -5.329  12.321  1.00 14.73  ? 11  ASN A N   1 
ATOM   85   C  CA  . ASN A 1 11  ? 31.276  -3.942  12.356  1.00 13.47  ? 11  ASN A CA  1 
ATOM   86   C  C   . ASN A 1 11  ? 29.980  -3.880  13.101  1.00 12.04  ? 11  ASN A C   1 
ATOM   87   O  O   . ASN A 1 11  ? 29.308  -2.852  13.128  1.00 12.35  ? 11  ASN A O   1 
ATOM   88   C  CB  . ASN A 1 11  ? 31.145  -3.236  10.967  1.00 14.57  ? 11  ASN A CB  1 
ATOM   89   C  CG  . ASN A 1 11  ? 30.011  -3.793  10.114  1.00 15.50  ? 11  ASN A CG  1 
ATOM   90   O  OD1 . ASN A 1 11  ? 29.361  -4.751  10.504  1.00 17.07  ? 11  ASN A OD1 1 
ATOM   91   N  ND2 . ASN A 1 11  ? 29.795  -3.209  8.931   1.00 20.48  ? 11  ASN A ND2 1 
ATOM   92   N  N   . GLY A 1 12  ? 29.649  -4.999  13.720  1.00 12.45  ? 12  GLY A N   1 
ATOM   93   C  CA  . GLY A 1 12  ? 28.330  -5.172  14.338  1.00 12.05  ? 12  GLY A CA  1 
ATOM   94   C  C   . GLY A 1 12  ? 28.335  -4.631  15.748  1.00 10.27  ? 12  GLY A C   1 
ATOM   95   O  O   . GLY A 1 12  ? 29.195  -3.886  16.199  1.00 10.44  ? 12  GLY A O   1 
ATOM   96   N  N   . PRO A 1 13  ? 27.256  -5.005  16.478  1.00 9.58   ? 13  PRO A N   1 
ATOM   97   C  CA  . PRO A 1 13  ? 26.973  -4.480  17.834  1.00 9.43   ? 13  PRO A CA  1 
ATOM   98   C  C   . PRO A 1 13  ? 28.141  -4.456  18.755  1.00 9.65   ? 13  PRO A C   1 
ATOM   99   O  O   . PRO A 1 13  ? 28.221  -3.541  19.543  1.00 10.85  ? 13  PRO A O   1 
ATOM   100  C  CB  . PRO A 1 13  ? 25.841  -5.356  18.310  1.00 9.68   ? 13  PRO A CB  1 
ATOM   101  C  CG  . PRO A 1 13  ? 25.042  -5.585  17.062  1.00 10.77  ? 13  PRO A CG  1 
ATOM   102  C  CD  . PRO A 1 13  ? 26.105  -5.794  15.971  1.00 11.38  ? 13  PRO A CD  1 
ATOM   103  N  N   . GLU A 1 14  ? 29.048  -5.446  18.720  1.00 10.86  ? 14  GLU A N   1 
ATOM   104  C  CA  . GLU A 1 14  ? 30.197  -5.475  19.646  1.00 12.38  ? 14  GLU A CA  1 
ATOM   105  C  C   . GLU A 1 14  ? 31.270  -4.435  19.313  1.00 10.79  ? 14  GLU A C   1 
ATOM   106  O  O   . GLU A 1 14  ? 32.180  -4.210  20.128  1.00 11.91  ? 14  GLU A O   1 
ATOM   107  C  CB  . GLU A 1 14  ? 30.827  -6.870  19.636  1.00 16.98  ? 14  GLU A CB  1 
ATOM   108  C  CG  . GLU A 1 14  ? 29.934  -8.039  19.954  1.00 21.01  ? 14  GLU A CG  1 
ATOM   109  C  CD  . GLU A 1 14  ? 29.619  -8.119  21.399  1.00 34.58  ? 14  GLU A CD  1 
ATOM   110  O  OE1 . GLU A 1 14  ? 30.358  -7.504  22.172  1.00 37.41  ? 14  GLU A OE1 1 
ATOM   111  O  OE2 . GLU A 1 14  ? 28.697  -8.830  21.772  1.00 45.37  ? 14  GLU A OE2 1 
ATOM   112  N  N   . HIS A 1 15  ? 31.168  -3.852  18.103  1.00 10.07  ? 15  HIS A N   1 
ATOM   113  C  CA  . HIS A 1 15  ? 32.123  -2.868  17.632  1.00 9.46   ? 15  HIS A CA  1 
ATOM   114  C  C   . HIS A 1 15  ? 31.630  -1.455  17.815  1.00 9.01   ? 15  HIS A C   1 
ATOM   115  O  O   . HIS A 1 15  ? 32.437  -0.508  17.772  1.00 9.89   ? 15  HIS A O   1 
ATOM   116  C  CB  . HIS A 1 15  ? 32.455  -3.066  16.188  1.00 10.84  ? 15  HIS A CB  1 
ATOM   117  C  CG  . HIS A 1 15  ? 33.241  -4.259  15.929  1.00 10.68  ? 15  HIS A CG  1 
ATOM   118  N  ND1 . HIS A 1 15  ? 34.639  -4.234  16.016  1.00 11.84  ? 15  HIS A ND1 1 
ATOM   119  C  CD2 . HIS A 1 15  ? 32.851  -5.496  15.559  1.00 11.78  ? 15  HIS A CD2 1 
ATOM   120  C  CE1 . HIS A 1 15  ? 35.095  -5.451  15.651  1.00 12.50  ? 15  HIS A CE1 1 
ATOM   121  N  NE2 . HIS A 1 15  ? 34.025  -6.253  15.391  1.00 13.18  ? 15  HIS A NE2 1 
ATOM   122  N  N   . TRP A 1 16  ? 30.298  -1.249  17.984  1.00 8.87   ? 16  TRP A N   1 
ATOM   123  C  CA  . TRP A 1 16  ? 29.749  0.098   17.877  1.00 8.30   ? 16  TRP A CA  1 
ATOM   124  C  C   . TRP A 1 16  ? 30.308  1.051   18.906  1.00 7.98   ? 16  TRP A C   1 
ATOM   125  O  O   . TRP A 1 16  ? 30.407  2.241   18.615  1.00 8.67   ? 16  TRP A O   1 
ATOM   126  C  CB  . TRP A 1 16  ? 28.232  0.042   18.040  1.00 8.40   ? 16  TRP A CB  1 
ATOM   127  C  CG  . TRP A 1 16  ? 27.530  -0.695  16.914  1.00 7.59   ? 16  TRP A CG  1 
ATOM   128  C  CD1 . TRP A 1 16  ? 28.027  -1.092  15.700  1.00 8.98   ? 16  TRP A CD1 1 
ATOM   129  C  CD2 . TRP A 1 16  ? 26.147  -1.096  16.924  1.00 7.51   ? 16  TRP A CD2 1 
ATOM   130  N  NE1 . TRP A 1 16  ? 27.068  -1.711  14.976  1.00 8.91   ? 16  TRP A NE1 1 
ATOM   131  C  CE2 . TRP A 1 16  ? 25.893  -1.730  15.685  1.00 7.89   ? 16  TRP A CE2 1 
ATOM   132  C  CE3 . TRP A 1 16  ? 25.130  -1.001  17.865  1.00 7.37   ? 16  TRP A CE3 1 
ATOM   133  C  CZ2 . TRP A 1 16  ? 24.633  -2.200  15.347  1.00 7.93   ? 16  TRP A CZ2 1 
ATOM   134  C  CZ3 . TRP A 1 16  ? 23.888  -1.484  17.528  1.00 7.84   ? 16  TRP A CZ3 1 
ATOM   135  C  CH2 . TRP A 1 16  ? 23.643  -2.069  16.296  1.00 7.84   ? 16  TRP A CH2 1 
ATOM   136  N  N   . HIS A 1 17  ? 30.682  0.556   20.093  1.00 8.51   ? 17  HIS A N   1 
ATOM   137  C  CA  . HIS A 1 17  ? 31.144  1.442   21.158  1.00 8.69   ? 17  HIS A CA  1 
ATOM   138  C  C   . HIS A 1 17  ? 32.371  2.255   20.777  1.00 9.34   ? 17  HIS A C   1 
ATOM   139  O  O   . HIS A 1 17  ? 32.611  3.328   21.364  1.00 10.35  ? 17  HIS A O   1 
ATOM   140  C  CB  . HIS A 1 17  ? 31.424  0.676   22.452  1.00 9.60   ? 17  HIS A CB  1 
ATOM   141  C  CG  . HIS A 1 17  ? 32.658  -0.182  22.365  1.00 10.40  ? 17  HIS A CG  1 
ATOM   142  N  ND1 . HIS A 1 17  ? 33.850  0.233   22.909  1.00 11.71  ? 17  HIS A ND1 1 
ATOM   143  C  CD2 . HIS A 1 17  ? 32.843  -1.382  21.763  1.00 11.53  ? 17  HIS A CD2 1 
ATOM   144  C  CE1 . HIS A 1 17  ? 34.723  -0.665  22.650  1.00 12.37  ? 17  HIS A CE1 1 
ATOM   145  N  NE2 . HIS A 1 17  ? 34.189  -1.651  21.931  1.00 11.79  ? 17  HIS A NE2 1 
ATOM   146  N  N   . LYS A 1 18  ? 33.173  1.778   19.811  1.00 9.17   ? 18  LYS A N   1 
ATOM   147  C  CA  . LYS A 1 18  ? 34.393  2.542   19.438  1.00 10.06  ? 18  LYS A CA  1 
ATOM   148  C  C   . LYS A 1 18  ? 34.057  3.877   18.815  1.00 10.68  ? 18  LYS A C   1 
ATOM   149  O  O   . LYS A 1 18  ? 34.667  4.870   19.140  1.00 15.41  ? 18  LYS A O   1 
ATOM   150  C  CB  . LYS A 1 18  ? 35.255  1.682   18.554  1.00 11.03  ? 18  LYS A CB  1 
ATOM   151  C  CG  . LYS A 1 18  ? 35.877  0.490   19.319  1.00 12.10  ? 18  LYS A CG  1 
ATOM   152  C  CD  . LYS A 1 18  ? 36.618  -0.430  18.383  1.00 11.92  ? 18  LYS A CD  1 
ATOM   153  C  CE  . LYS A 1 18  ? 35.704  -1.409  17.749  1.00 10.83  ? 18  LYS A CE  1 
ATOM   154  N  NZ  . LYS A 1 18  ? 36.340  -2.218  16.680  1.00 11.33  ? 18  LYS A NZ  1 
ATOM   155  N  N   . ASP A 1 19  ? 33.065  3.907   17.932  1.00 10.47  ? 19  ASP A N   1 
ATOM   156  C  CA  . ASP A 1 19  ? 32.650  5.150   17.313  1.00 11.21  ? 19  ASP A CA  1 
ATOM   157  C  C   . ASP A 1 19  ? 31.573  5.846   18.152  1.00 10.69  ? 19  ASP A C   1 
ATOM   158  O  O   . ASP A 1 19  ? 31.434  7.051   18.058  1.00 12.58  ? 19  ASP A O   1 
ATOM   159  C  CB  . ASP A 1 19  ? 32.121  4.938   15.915  1.00 12.18  ? 19  ASP A CB  1 
ATOM   160  C  CG  . ASP A 1 19  ? 33.213  4.843   14.870  1.00 17.18  ? 19  ASP A CG  1 
ATOM   161  O  OD1 . ASP A 1 19  ? 34.248  5.524   15.012  1.00 17.99  ? 19  ASP A OD1 1 
ATOM   162  O  OD2 . ASP A 1 19  ? 33.014  4.101   13.886  1.00 31.63  ? 19  ASP A OD2 1 
ATOM   163  N  N   . PHE A 1 20  ? 30.810  5.087   18.932  1.00 9.47   ? 20  PHE A N   1 
ATOM   164  C  CA  . PHE A 1 20  ? 29.664  5.604   19.657  1.00 9.62   ? 20  PHE A CA  1 
ATOM   165  C  C   . PHE A 1 20  ? 29.766  5.096   21.091  1.00 9.39   ? 20  PHE A C   1 
ATOM   166  O  O   . PHE A 1 20  ? 29.141  4.097   21.465  1.00 9.10   ? 20  PHE A O   1 
ATOM   167  C  CB  . PHE A 1 20  ? 28.368  5.089   19.011  1.00 9.65   ? 20  PHE A CB  1 
ATOM   168  C  CG  . PHE A 1 20  ? 28.246  5.500   17.569  1.00 10.37  ? 20  PHE A CG  1 
ATOM   169  C  CD1 . PHE A 1 20  ? 27.795  6.749   17.230  1.00 12.94  ? 20  PHE A CD1 1 
ATOM   170  C  CD2 . PHE A 1 20  ? 28.653  4.632   16.552  1.00 11.56  ? 20  PHE A CD2 1 
ATOM   171  C  CE1 . PHE A 1 20  ? 27.784  7.150   15.877  1.00 14.48  ? 20  PHE A CE1 1 
ATOM   172  C  CE2 . PHE A 1 20  ? 28.654  5.039   15.241  1.00 12.79  ? 20  PHE A CE2 1 
ATOM   173  C  CZ  . PHE A 1 20  ? 28.203  6.257   14.911  1.00 14.69  ? 20  PHE A CZ  1 
ATOM   174  N  N   A PRO A 1 21  ? 30.588  5.677   22.012  0.50 9.33   ? 21  PRO A N   1 
ATOM   175  N  N   B PRO A 1 21  ? 30.569  5.856   21.866  0.50 9.83   ? 21  PRO A N   1 
ATOM   176  C  CA  A PRO A 1 21  ? 30.818  5.100   23.344  0.50 9.52   ? 21  PRO A CA  1 
ATOM   177  C  CA  B PRO A 1 21  ? 30.838  5.445   23.234  0.50 9.73   ? 21  PRO A CA  1 
ATOM   178  C  C   A PRO A 1 21  ? 29.595  4.976   24.239  0.50 9.71   ? 21  PRO A C   1 
ATOM   179  C  C   B PRO A 1 21  ? 29.582  5.340   24.059  0.50 8.55   ? 21  PRO A C   1 
ATOM   180  O  O   A PRO A 1 21  ? 29.636  4.151   25.159  0.50 8.90   ? 21  PRO A O   1 
ATOM   181  O  O   B PRO A 1 21  ? 29.581  4.637   25.090  0.50 7.95   ? 21  PRO A O   1 
ATOM   182  C  CB  A PRO A 1 21  ? 31.872  6.080   23.954  0.50 10.74  ? 21  PRO A CB  1 
ATOM   183  C  CB  B PRO A 1 21  ? 31.807  6.536   23.778  0.50 12.09  ? 21  PRO A CB  1 
ATOM   184  C  CG  A PRO A 1 21  ? 31.703  7.371   23.130  0.50 12.17  ? 21  PRO A CG  1 
ATOM   185  C  CG  B PRO A 1 21  ? 32.542  6.906   22.527  0.50 15.45  ? 21  PRO A CG  1 
ATOM   186  C  CD  A PRO A 1 21  ? 31.513  6.808   21.775  0.50 11.06  ? 21  PRO A CD  1 
ATOM   187  C  CD  B PRO A 1 21  ? 31.449  6.988   21.454  0.50 11.68  ? 21  PRO A CD  1 
ATOM   188  N  N   A ILE A 1 22  ? 28.540  5.769   23.915  0.50 8.23   ? 22  ILE A N   1 
ATOM   189  N  N   B ILE A 1 22  ? 28.506  5.966   23.618  0.50 8.16   ? 22  ILE A N   1 
ATOM   190  C  CA  A ILE A 1 22  ? 27.250  5.682   24.617  0.50 8.54   ? 22  ILE A CA  1 
ATOM   191  C  CA  B ILE A 1 22  ? 27.254  5.843   24.354  0.50 8.76   ? 22  ILE A CA  1 
ATOM   192  C  C   A ILE A 1 22  ? 26.680  4.291   24.438  0.50 7.76   ? 22  ILE A C   1 
ATOM   193  C  C   B ILE A 1 22  ? 26.670  4.403   24.311  0.50 7.78   ? 22  ILE A C   1 
ATOM   194  O  O   A ILE A 1 22  ? 25.788  3.912   25.168  0.50 8.13   ? 22  ILE A O   1 
ATOM   195  O  O   B ILE A 1 22  ? 25.745  4.101   25.041  0.50 8.21   ? 22  ILE A O   1 
ATOM   196  C  CB  A ILE A 1 22  ? 26.251  6.742   24.098  0.50 8.39   ? 22  ILE A CB  1 
ATOM   197  C  CB  B ILE A 1 22  ? 26.268  6.921   23.888  0.50 9.28   ? 22  ILE A CB  1 
ATOM   198  C  CG1 A ILE A 1 22  ? 25.188  7.111   25.141  0.50 8.47   ? 22  ILE A CG1 1 
ATOM   199  C  CG1 B ILE A 1 22  ? 25.169  7.172   24.925  0.50 11.77  ? 22  ILE A CG1 1 
ATOM   200  C  CG2 A ILE A 1 22  ? 25.612  6.348   22.779  0.50 8.23   ? 22  ILE A CG2 1 
ATOM   201  C  CG2 B ILE A 1 22  ? 25.658  6.558   22.531  0.50 10.62  ? 22  ILE A CG2 1 
ATOM   202  C  CD1 A ILE A 1 22  ? 24.278  8.222   24.639  0.50 9.79   ? 22  ILE A CD1 1 
ATOM   203  C  CD1 B ILE A 1 22  ? 25.616  7.741   26.226  0.50 16.25  ? 22  ILE A CD1 1 
ATOM   204  N  N   . ALA A 1 23  ? 27.227  3.504   23.508  1.00 8.34   ? 23  ALA A N   1 
ATOM   205  C  CA  . ALA A 1 23  ? 26.826  2.109   23.403  1.00 8.34   ? 23  ALA A CA  1 
ATOM   206  C  C   . ALA A 1 23  ? 26.913  1.394   24.744  1.00 8.96   ? 23  ALA A C   1 
ATOM   207  O  O   . ALA A 1 23  ? 26.197  0.398   24.930  1.00 9.19   ? 23  ALA A O   1 
ATOM   208  C  CB  . ALA A 1 23  ? 27.670  1.370   22.408  1.00 9.02   ? 23  ALA A CB  1 
ATOM   209  N  N   . LYS A 1 24  ? 27.806  1.846   25.626  1.00 8.82   ? 24  LYS A N   1 
ATOM   210  C  CA  . LYS A 1 24  ? 27.979  1.313   26.941  1.00 9.71   ? 24  LYS A CA  1 
ATOM   211  C  C   . LYS A 1 24  ? 27.326  2.173   28.031  1.00 10.46  ? 24  LYS A C   1 
ATOM   212  O  O   . LYS A 1 24  ? 27.696  2.097   29.196  1.00 11.66  ? 24  LYS A O   1 
ATOM   213  C  CB  . LYS A 1 24  ? 29.468  1.043   27.265  1.00 11.30  ? 24  LYS A CB  1 
ATOM   214  C  CG  . LYS A 1 24  ? 30.094  0.024   26.346  1.00 12.71  ? 24  LYS A CG  1 
ATOM   215  C  CD  . LYS A 1 24  ? 31.568  -0.162  26.768  1.00 16.65  ? 24  LYS A CD  1 
ATOM   216  C  CE  . LYS A 1 24  ? 32.375  -1.011  25.884  1.00 17.43  ? 24  LYS A CE  1 
ATOM   217  N  NZ  . LYS A 1 24  ? 31.900  -2.357  26.045  1.00 21.81  ? 24  LYS A NZ  1 
ATOM   218  N  N   . GLY A 1 25  ? 26.353  2.972   27.633  1.00 9.88   ? 25  GLY A N   1 
ATOM   219  C  CA  . GLY A 1 25  ? 25.694  3.941   28.522  1.00 10.57  ? 25  GLY A CA  1 
ATOM   220  C  C   . GLY A 1 25  ? 24.728  3.292   29.532  1.00 9.80   ? 25  GLY A C   1 
ATOM   221  O  O   . GLY A 1 25  ? 24.595  2.097   29.619  1.00 10.38  ? 25  GLY A O   1 
ATOM   222  N  N   . GLU A 1 26  ? 24.082  4.209   30.244  1.00 10.07  ? 26  GLU A N   1 
ATOM   223  C  CA  . GLU A 1 26  ? 23.231  3.884   31.324  1.00 10.14  ? 26  GLU A CA  1 
ATOM   224  C  C   . GLU A 1 26  ? 21.794  3.567   30.934  1.00 9.98   ? 26  GLU A C   1 
ATOM   225  O  O   . GLU A 1 26  ? 21.031  3.083   31.790  1.00 10.91  ? 26  GLU A O   1 
ATOM   226  C  CB  . GLU A 1 26  ? 23.258  4.973   32.421  1.00 12.76  ? 26  GLU A CB  1 
ATOM   227  C  CG  . GLU A 1 26  ? 24.650  5.118   33.020  1.00 15.53  ? 26  GLU A CG  1 
ATOM   228  C  CD  . GLU A 1 26  ? 25.228  3.838   33.643  1.00 20.51  ? 26  GLU A CD  1 
ATOM   229  O  OE1 . GLU A 1 26  ? 24.526  3.254   34.502  1.00 23.59  ? 26  GLU A OE1 1 
ATOM   230  O  OE2 . GLU A 1 26  ? 26.365  3.446   33.299  1.00 27.44  ? 26  GLU A OE2 1 
ATOM   231  N  N   . ARG A 1 27  ? 21.404  3.855   29.717  1.00 8.14   ? 27  ARG A N   1 
ATOM   232  C  CA  . ARG A 1 27  ? 20.005  3.617   29.321  1.00 7.37   ? 27  ARG A CA  1 
ATOM   233  C  C   . ARG A 1 27  ? 19.936  3.164   27.875  1.00 6.75   ? 27  ARG A C   1 
ATOM   234  O  O   . ARG A 1 27  ? 19.238  3.735   27.046  1.00 6.98   ? 27  ARG A O   1 
ATOM   235  C  CB  . ARG A 1 27  ? 19.084  4.819   29.612  1.00 8.36   ? 27  ARG A CB  1 
ATOM   236  C  CG  . ARG A 1 27  ? 19.489  6.124   29.030  1.00 9.54   ? 27  ARG A CG  1 
ATOM   237  C  CD  . ARG A 1 27  ? 18.568  7.287   29.208  1.00 10.09  ? 27  ARG A CD  1 
ATOM   238  N  NE  . ARG A 1 27  ? 17.444  7.211   28.280  1.00 8.79   ? 27  ARG A NE  1 
ATOM   239  C  CZ  . ARG A 1 27  ? 16.460  8.103   28.216  1.00 8.74   ? 27  ARG A CZ  1 
ATOM   240  N  NH1 . ARG A 1 27  ? 16.454  9.149   29.031  1.00 12.12  ? 27  ARG A NH1 1 
ATOM   241  N  NH2 . ARG A 1 27  ? 15.480  7.949   27.336  1.00 10.01  ? 27  ARG A NH2 1 
ATOM   242  N  N   . GLN A 1 28  ? 20.679  2.082   27.590  1.00 6.63   ? 28  GLN A N   1 
ATOM   243  C  CA  . GLN A 1 28  ? 20.705  1.547   26.240  1.00 6.21   ? 28  GLN A CA  1 
ATOM   244  C  C   . GLN A 1 28  ? 19.574  0.563   25.991  1.00 6.13   ? 28  GLN A C   1 
ATOM   245  O  O   . GLN A 1 28  ? 19.072  -0.115  26.880  1.00 6.96   ? 28  GLN A O   1 
ATOM   246  C  CB  . GLN A 1 28  ? 22.077  0.875   25.985  1.00 7.01   ? 28  GLN A CB  1 
ATOM   247  C  CG  . GLN A 1 28  ? 23.187  1.928   25.879  1.00 7.37   ? 28  GLN A CG  1 
ATOM   248  C  CD  . GLN A 1 28  ? 23.076  2.686   24.582  1.00 6.70   ? 28  GLN A CD  1 
ATOM   249  O  OE1 . GLN A 1 28  ? 23.250  2.115   23.486  1.00 7.20   ? 28  GLN A OE1 1 
ATOM   250  N  NE2 . GLN A 1 28  ? 22.718  3.959   24.674  1.00 7.20   ? 28  GLN A NE2 1 
ATOM   251  N  N   . SER A 1 29  ? 19.206  0.445   24.719  1.00 5.87   ? 29  SER A N   1 
ATOM   252  C  CA  . SER A 1 29  ? 18.158  -0.416  24.230  1.00 5.65   ? 29  SER A CA  1 
ATOM   253  C  C   . SER A 1 29  ? 18.669  -1.308  23.137  1.00 5.56   ? 29  SER A C   1 
ATOM   254  O  O   . SER A 1 29  ? 19.639  -0.964  22.437  1.00 6.01   ? 29  SER A O   1 
ATOM   255  C  CB  . SER A 1 29  ? 17.002  0.430   23.694  1.00 5.73   ? 29  SER A CB  1 
ATOM   256  O  OG  . SER A 1 29  ? 16.401  1.169   24.752  1.00 5.99   ? 29  SER A OG  1 
ATOM   257  N  N   . PRO A 1 30  ? 18.022  -2.452  22.886  1.00 5.47   ? 30  PRO A N   1 
ATOM   258  C  CA  . PRO A 1 30  ? 16.862  -2.983  23.605  1.00 5.55   ? 30  PRO A CA  1 
ATOM   259  C  C   . PRO A 1 30  ? 17.295  -3.627  24.908  1.00 5.49   ? 30  PRO A C   1 
ATOM   260  O  O   . PRO A 1 30  ? 18.471  -3.688  25.245  1.00 6.18   ? 30  PRO A O   1 
ATOM   261  C  CB  . PRO A 1 30  ? 16.326  -4.004  22.597  1.00 5.69   ? 30  PRO A CB  1 
ATOM   262  C  CG  . PRO A 1 30  ? 17.607  -4.589  22.020  1.00 5.89   ? 30  PRO A CG  1 
ATOM   263  C  CD  . PRO A 1 30  ? 18.508  -3.386  21.852  1.00 6.06   ? 30  PRO A CD  1 
ATOM   264  N  N   . VAL A 1 31  ? 16.292  -4.178  25.604  1.00 6.07   ? 31  VAL A N   1 
ATOM   265  C  CA  . VAL A 1 31  ? 16.465  -4.929  26.830  1.00 6.20   ? 31  VAL A CA  1 
ATOM   266  C  C   . VAL A 1 31  ? 15.594  -6.152  26.769  1.00 6.23   ? 31  VAL A C   1 
ATOM   267  O  O   . VAL A 1 31  ? 14.615  -6.209  26.010  1.00 6.75   ? 31  VAL A O   1 
ATOM   268  C  CB  . VAL A 1 31  ? 16.134  -4.087  28.079  1.00 6.86   ? 31  VAL A CB  1 
ATOM   269  C  CG1 . VAL A 1 31  ? 17.100  -2.900  28.193  1.00 7.66   ? 31  VAL A CG1 1 
ATOM   270  C  CG2 . VAL A 1 31  ? 14.691  -3.659  28.130  1.00 7.64   ? 31  VAL A CG2 1 
ATOM   271  N  N   . ASP A 1 32  ? 15.909  -7.135  27.619  1.00 6.39   ? 32  ASP A N   1 
ATOM   272  C  CA  . ASP A 1 32  ? 14.977  -8.213  27.916  1.00 6.78   ? 32  ASP A CA  1 
ATOM   273  C  C   . ASP A 1 32  ? 13.932  -7.676  28.888  1.00 6.75   ? 32  ASP A C   1 
ATOM   274  O  O   . ASP A 1 32  ? 14.257  -7.032  29.890  1.00 8.76   ? 32  ASP A O   1 
ATOM   275  C  CB  . ASP A 1 32  ? 15.707  -9.373  28.535  1.00 7.96   ? 32  ASP A CB  1 
ATOM   276  C  CG  . ASP A 1 32  ? 14.771  -10.567 28.808  1.00 8.53   ? 32  ASP A CG  1 
ATOM   277  O  OD1 . ASP A 1 32  ? 14.103  -11.015 27.868  1.00 8.10   ? 32  ASP A OD1 1 
ATOM   278  O  OD2 . ASP A 1 32  ? 14.720  -10.990 29.994  1.00 10.91  ? 32  ASP A OD2 1 
ATOM   279  N  N   . ILE A 1 33  ? 12.683  -7.981  28.591  1.00 6.51   ? 33  ILE A N   1 
ATOM   280  C  CA  . ILE A 1 33  ? 11.551  -7.648  29.436  1.00 6.92   ? 33  ILE A CA  1 
ATOM   281  C  C   . ILE A 1 33  ? 11.251  -8.870  30.290  1.00 7.29   ? 33  ILE A C   1 
ATOM   282  O  O   . ILE A 1 33  ? 10.718  -9.866  29.789  1.00 8.11   ? 33  ILE A O   1 
ATOM   283  C  CB  . ILE A 1 33  ? 10.366  -7.215  28.619  1.00 7.62   ? 33  ILE A CB  1 
ATOM   284  C  CG1 . ILE A 1 33  ? 10.704  -5.990  27.775  1.00 8.12   ? 33  ILE A CG1 1 
ATOM   285  C  CG2 . ILE A 1 33  ? 9.148   -6.940  29.531  1.00 9.26   ? 33  ILE A CG2 1 
ATOM   286  C  CD1 . ILE A 1 33  ? 9.697   -5.690  26.674  1.00 9.94   ? 33  ILE A CD1 1 
ATOM   287  N  N   A ASP A 1 34  ? 11.769  -8.791  31.523  0.50 8.20   ? 34  ASP A N   1 
ATOM   288  N  N   B ASP A 1 34  ? 11.526  -8.838  31.584  0.50 7.21   ? 34  ASP A N   1 
ATOM   289  C  CA  A ASP A 1 34  ? 11.504  -9.788  32.525  0.50 8.40   ? 34  ASP A CA  1 
ATOM   290  C  CA  B ASP A 1 34  ? 11.218  -9.952  32.502  0.50 8.66   ? 34  ASP A CA  1 
ATOM   291  C  C   A ASP A 1 34  ? 10.011  -9.550  33.018  0.50 10.03  ? 34  ASP A C   1 
ATOM   292  C  C   B ASP A 1 34  ? 9.812   -9.647  33.002  0.50 8.41   ? 34  ASP A C   1 
ATOM   293  O  O   A ASP A 1 34  ? 9.808   -8.630  33.795  0.50 9.65   ? 34  ASP A O   1 
ATOM   294  O  O   B ASP A 1 34  ? 9.583   -8.744  33.808  0.50 9.14   ? 34  ASP A O   1 
ATOM   295  C  CB  A ASP A 1 34  ? 12.518  -9.873  33.670  0.50 10.12  ? 34  ASP A CB  1 
ATOM   296  C  CB  B ASP A 1 34  ? 12.262  -9.828  33.582  0.50 10.60  ? 34  ASP A CB  1 
ATOM   297  C  CG  A ASP A 1 34  ? 12.308  -11.187 34.423  0.50 12.37  ? 34  ASP A CG  1 
ATOM   298  C  CG  B ASP A 1 34  ? 12.046  -10.806 34.761  0.50 11.39  ? 34  ASP A CG  1 
ATOM   299  O  OD1 A ASP A 1 34  ? 11.627  -11.082 35.417  0.50 13.17  ? 34  ASP A OD1 1 
ATOM   300  O  OD1 B ASP A 1 34  ? 10.919  -11.168 34.952  0.50 12.65  ? 34  ASP A OD1 1 
ATOM   301  O  OD2 A ASP A 1 34  ? 12.639  -12.293 33.942  0.50 15.21  ? 34  ASP A OD2 1 
ATOM   302  O  OD2 B ASP A 1 34  ? 12.955  -11.151 35.529  0.50 17.49  ? 34  ASP A OD2 1 
ATOM   303  N  N   . THR A 1 35  ? 8.968   -10.363 32.531  1.00 10.04  ? 35  THR A N   1 
ATOM   304  C  CA  . THR A 1 35  ? 7.543   -10.120 32.759  1.00 11.55  ? 35  THR A CA  1 
ATOM   305  C  C   . THR A 1 35  ? 7.132   -10.256 34.187  1.00 10.31  ? 35  THR A C   1 
ATOM   306  O  O   . THR A 1 35  ? 6.227   -9.583  34.627  1.00 13.22  ? 35  THR A O   1 
ATOM   307  C  CB  . THR A 1 35  ? 6.642   -11.019 31.896  1.00 12.77  ? 35  THR A CB  1 
ATOM   308  O  OG1 . THR A 1 35  ? 6.771   -12.366 32.354  1.00 13.05  ? 35  THR A OG1 1 
ATOM   309  C  CG2 . THR A 1 35  ? 6.993   -10.868 30.454  1.00 14.49  ? 35  THR A CG2 1 
ATOM   310  N  N   . HIS A 1 36  ? 7.838   -11.108 34.923  1.00 10.63  ? 36  HIS A N   1 
ATOM   311  C  CA  . HIS A 1 36  ? 7.542   -11.309 36.312  1.00 11.02  ? 36  HIS A CA  1 
ATOM   312  C  C   . HIS A 1 36  ? 8.049   -10.180 37.167  1.00 11.50  ? 36  HIS A C   1 
ATOM   313  O  O   . HIS A 1 36  ? 7.451   -9.896  38.218  1.00 13.33  ? 36  HIS A O   1 
ATOM   314  C  CB  . HIS A 1 36  ? 8.041   -12.717 36.749  1.00 14.13  ? 36  HIS A CB  1 
ATOM   315  C  CG  . HIS A 1 36  ? 7.108   -13.844 36.249  1.00 14.11  ? 36  HIS A CG  1 
ATOM   316  N  ND1 . HIS A 1 36  ? 5.744   -13.922 36.610  1.00 16.40  ? 36  HIS A ND1 1 
ATOM   317  C  CD2 . HIS A 1 36  ? 7.303   -14.806 35.289  1.00 14.66  ? 36  HIS A CD2 1 
ATOM   318  C  CE1 . HIS A 1 36  ? 5.198   -14.926 35.959  1.00 16.20  ? 36  HIS A CE1 1 
ATOM   319  N  NE2 . HIS A 1 36  ? 6.147   -15.482 35.178  1.00 17.27  ? 36  HIS A NE2 1 
ATOM   320  N  N   . THR A 1 37  ? 9.103   -9.463  36.717  1.00 12.99  ? 37  THR A N   1 
ATOM   321  C  CA  . THR A 1 37  ? 9.682   -8.385  37.489  1.00 12.68  ? 37  THR A CA  1 
ATOM   322  C  C   . THR A 1 37  ? 9.083   -7.024  37.117  1.00 12.60  ? 37  THR A C   1 
ATOM   323  O  O   . THR A 1 37  ? 9.070   -6.109  37.951  1.00 17.45  ? 37  THR A O   1 
ATOM   324  C  CB  . THR A 1 37  ? 11.208  -8.301  37.303  1.00 15.25  ? 37  THR A CB  1 
ATOM   325  O  OG1 . THR A 1 37  ? 11.788  -9.524  37.793  1.00 21.32  ? 37  THR A OG1 1 
ATOM   326  C  CG2 . THR A 1 37  ? 11.881  -7.213  37.983  1.00 16.40  ? 37  THR A CG2 1 
ATOM   327  N  N   . ALA A 1 38  ? 8.571   -6.862  35.924  1.00 10.94  ? 38  ALA A N   1 
ATOM   328  C  CA  . ALA A 1 38  ? 7.933   -5.593  35.506  1.00 10.95  ? 38  ALA A CA  1 
ATOM   329  C  C   . ALA A 1 38  ? 6.707   -5.410  36.364  1.00 13.05  ? 38  ALA A C   1 
ATOM   330  O  O   . ALA A 1 38  ? 5.900   -6.329  36.622  1.00 20.13  ? 38  ALA A O   1 
ATOM   331  C  CB  . ALA A 1 38  ? 7.542   -5.718  34.093  1.00 11.49  ? 38  ALA A CB  1 
ATOM   332  N  N   A LYS A 1 39  ? 6.626   -4.203  36.931  0.50 14.50  ? 39  LYS A N   1 
ATOM   333  N  N   B LYS A 1 39  ? 6.529   -4.301  36.971  0.50 12.52  ? 39  LYS A N   1 
ATOM   334  C  CA  A LYS A 1 39  ? 5.527   -3.928  37.920  0.50 15.92  ? 39  LYS A CA  1 
ATOM   335  C  CA  B LYS A 1 39  ? 5.416   -4.203  37.908  0.50 11.59  ? 39  LYS A CA  1 
ATOM   336  C  C   A LYS A 1 39  ? 4.396   -3.154  37.340  0.50 12.19  ? 39  LYS A C   1 
ATOM   337  C  C   B LYS A 1 39  ? 4.368   -3.332  37.294  0.50 12.76  ? 39  LYS A C   1 
ATOM   338  O  O   A LYS A 1 39  ? 4.607   -2.131  36.689  0.50 9.32   ? 39  LYS A O   1 
ATOM   339  O  O   B LYS A 1 39  ? 4.685   -2.389  36.573  0.50 12.23  ? 39  LYS A O   1 
ATOM   340  C  CB  A LYS A 1 39  ? 6.000   -3.201  39.170  0.50 15.33  ? 39  LYS A CB  1 
ATOM   341  C  CB  B LYS A 1 39  ? 5.875   -3.526  39.194  0.50 11.29  ? 39  LYS A CB  1 
ATOM   342  C  CG  A LYS A 1 39  ? 4.968   -3.195  40.303  0.50 15.00  ? 39  LYS A CG  1 
ATOM   343  C  CG  B LYS A 1 39  ? 4.880   -3.583  40.330  0.50 12.17  ? 39  LYS A CG  1 
ATOM   344  C  CD  A LYS A 1 39  ? 5.430   -2.316  41.467  0.50 20.72  ? 39  LYS A CD  1 
ATOM   345  C  CD  B LYS A 1 39  ? 5.379   -2.730  41.444  0.50 12.29  ? 39  LYS A CD  1 
ATOM   346  C  CE  A LYS A 1 39  ? 4.414   -2.196  42.611  0.50 23.60  ? 39  LYS A CE  1 
ATOM   347  C  CE  B LYS A 1 39  ? 4.488   -2.787  42.696  0.50 12.46  ? 39  LYS A CE  1 
ATOM   348  N  NZ  A LYS A 1 39  ? 3.610   -3.454  42.827  0.50 22.97  ? 39  LYS A NZ  1 
ATOM   349  N  NZ  B LYS A 1 39  ? 4.806   -1.745  43.716  0.50 17.29  ? 39  LYS A NZ  1 
ATOM   350  N  N   . TYR A 1 40  ? 3.141   -3.656  37.528  1.00 14.96  ? 40  TYR A N   1 
ATOM   351  C  CA  . TYR A 1 40  ? 2.030   -2.920  37.120  1.00 13.12  ? 40  TYR A CA  1 
ATOM   352  C  C   . TYR A 1 40  ? 2.090   -1.584  37.762  1.00 11.49  ? 40  TYR A C   1 
ATOM   353  O  O   . TYR A 1 40  ? 2.298   -1.411  39.028  1.00 14.58  ? 40  TYR A O   1 
ATOM   354  C  CB  . TYR A 1 40  ? 0.780   -3.636  37.535  1.00 16.93  ? 40  TYR A CB  1 
ATOM   355  C  CG  . TYR A 1 40  ? -0.490  -2.846  37.386  1.00 17.10  ? 40  TYR A CG  1 
ATOM   356  C  CD1 . TYR A 1 40  ? -0.852  -2.309  36.173  1.00 16.58  ? 40  TYR A CD1 1 
ATOM   357  C  CD2 . TYR A 1 40  ? -1.330  -2.644  38.508  1.00 20.58  ? 40  TYR A CD2 1 
ATOM   358  C  CE1 . TYR A 1 40  ? -2.020  -1.565  36.028  1.00 20.68  ? 40  TYR A CE1 1 
ATOM   359  C  CE2 . TYR A 1 40  ? -2.465  -1.875  38.357  1.00 28.39  ? 40  TYR A CE2 1 
ATOM   360  C  CZ  . TYR A 1 40  ? -2.858  -1.345  37.168  1.00 27.36  ? 40  TYR A CZ  1 
ATOM   361  O  OH  . TYR A 1 40  ? -3.984  -0.574  37.052  1.00 69.65  ? 40  TYR A OH  1 
ATOM   362  N  N   . ASP A 1 41  ? 1.897   -0.539  37.008  1.00 11.98  ? 41  ASP A N   1 
ATOM   363  C  CA  . ASP A 1 41  ? 1.888   0.818   37.489  1.00 12.33  ? 41  ASP A CA  1 
ATOM   364  C  C   . ASP A 1 41  ? 0.495   1.397   37.281  1.00 14.11  ? 41  ASP A C   1 
ATOM   365  O  O   . ASP A 1 41  ? 0.144   1.770   36.167  1.00 14.22  ? 41  ASP A O   1 
ATOM   366  C  CB  . ASP A 1 41  ? 2.934   1.650   36.834  1.00 13.83  ? 41  ASP A CB  1 
ATOM   367  C  CG  . ASP A 1 41  ? 3.065   3.002   37.358  1.00 16.71  ? 41  ASP A CG  1 
ATOM   368  O  OD1 . ASP A 1 41  ? 2.148   3.475   38.154  1.00 17.94  ? 41  ASP A OD1 1 
ATOM   369  O  OD2 . ASP A 1 41  ? 4.030   3.719   36.955  1.00 19.53  ? 41  ASP A OD2 1 
ATOM   370  N  N   . PRO A 1 42  ? -0.339  1.478   38.332  1.00 16.42  ? 42  PRO A N   1 
ATOM   371  C  CA  . PRO A 1 42  ? -1.701  1.960   38.157  1.00 20.97  ? 42  PRO A CA  1 
ATOM   372  C  C   . PRO A 1 42  ? -1.707  3.440   37.815  1.00 18.25  ? 42  PRO A C   1 
ATOM   373  O  O   . PRO A 1 42  ? -2.781  3.973   37.456  1.00 26.96  ? 42  PRO A O   1 
ATOM   374  C  CB  . PRO A 1 42  ? -2.366  1.709   39.542  1.00 24.92  ? 42  PRO A CB  1 
ATOM   375  C  CG  . PRO A 1 42  ? -1.160  1.726   40.471  1.00 25.39  ? 42  PRO A CG  1 
ATOM   376  C  CD  . PRO A 1 42  ? -0.061  1.092   39.727  1.00 18.45  ? 42  PRO A CD  1 
ATOM   377  N  N   . SER A 1 43  ? -0.596  4.123   38.017  1.00 20.33  ? 43  SER A N   1 
ATOM   378  C  CA  . SER A 1 43  ? -0.575  5.541   37.580  1.00 24.42  ? 43  SER A CA  1 
ATOM   379  C  C   . SER A 1 43  ? -0.409  5.737   36.044  1.00 22.14  ? 43  SER A C   1 
ATOM   380  O  O   . SER A 1 43  ? -0.625  6.842   35.536  1.00 28.99  ? 43  SER A O   1 
ATOM   381  C  CB  . SER A 1 43  ? 0.586   6.326   38.188  1.00 24.10  ? 43  SER A CB  1 
ATOM   382  O  OG  . SER A 1 43  ? 1.861   6.004   37.687  1.00 25.78  ? 43  SER A OG  1 
ATOM   383  N  N   . LEU A 1 44  ? -0.037  4.707   35.284  1.00 21.52  ? 44  LEU A N   1 
ATOM   384  C  CA  . LEU A 1 44  ? 0.093   4.831   33.835  1.00 20.23  ? 44  LEU A CA  1 
ATOM   385  C  C   . LEU A 1 44  ? -1.265  5.009   33.198  1.00 24.08  ? 44  LEU A C   1 
ATOM   386  O  O   . LEU A 1 44  ? -2.267  4.537   33.643  1.00 24.38  ? 44  LEU A O   1 
ATOM   387  C  CB  . LEU A 1 44  ? 0.754   3.591   33.242  1.00 17.17  ? 44  LEU A CB  1 
ATOM   388  C  CG  . LEU A 1 44  ? 2.234   3.533   33.417  1.00 14.14  ? 44  LEU A CG  1 
ATOM   389  C  CD1 . LEU A 1 44  ? 2.640   2.153   33.021  1.00 16.18  ? 44  LEU A CD1 1 
ATOM   390  C  CD2 . LEU A 1 44  ? 3.005   4.569   32.682  1.00 15.09  ? 44  LEU A CD2 1 
ATOM   391  N  N   . LYS A 1 45  ? -1.275  5.694   32.085  1.00 17.57  ? 45  LYS A N   1 
ATOM   392  C  CA  . LYS A 1 45  ? -2.478  5.916   31.321  1.00 23.93  ? 45  LYS A CA  1 
ATOM   393  C  C   . LYS A 1 45  ? -2.564  4.957   30.140  1.00 19.41  ? 45  LYS A C   1 
ATOM   394  O  O   . LYS A 1 45  ? -1.546  4.352   29.646  1.00 26.13  ? 45  LYS A O   1 
ATOM   395  C  CB  . LYS A 1 45  ? -2.539  7.357   30.822  1.00 22.01  ? 45  LYS A CB  1 
ATOM   396  C  CG  . LYS A 1 45  ? -2.710  8.379   31.931  1.00 30.09  ? 45  LYS A CG  1 
ATOM   397  C  CD  . LYS A 1 45  ? -2.243  9.755   31.478  1.00 33.97  ? 45  LYS A CD  1 
ATOM   398  C  CE  . LYS A 1 45  ? -1.710  10.561  32.649  1.00 34.15  ? 45  LYS A CE  1 
ATOM   399  N  NZ  . LYS A 1 45  ? -2.801  10.949  33.589  1.00 55.48  ? 45  LYS A NZ  1 
ATOM   400  N  N   A PRO A 1 46  ? -3.814  4.815   29.700  0.50 18.95  ? 46  PRO A N   1 
ATOM   401  N  N   B PRO A 1 46  ? -3.772  4.826   29.603  0.50 18.98  ? 46  PRO A N   1 
ATOM   402  C  CA  A PRO A 1 46  ? -4.182  4.083   28.490  0.50 15.53  ? 46  PRO A CA  1 
ATOM   403  C  CA  B PRO A 1 46  ? -3.972  4.043   28.377  0.50 18.61  ? 46  PRO A CA  1 
ATOM   404  C  C   A PRO A 1 46  ? -3.735  4.877   27.278  0.50 16.24  ? 46  PRO A C   1 
ATOM   405  C  C   B PRO A 1 46  ? -3.375  4.762   27.166  0.50 10.94  ? 46  PRO A C   1 
ATOM   406  O  O   A PRO A 1 46  ? -4.258  5.950   26.974  0.50 17.20  ? 46  PRO A O   1 
ATOM   407  O  O   B PRO A 1 46  ? -3.645  5.948   26.972  0.50 16.10  ? 46  PRO A O   1 
ATOM   408  C  CB  A PRO A 1 46  ? -5.708  4.043   28.561  0.50 17.43  ? 46  PRO A CB  1 
ATOM   409  C  CB  B PRO A 1 46  ? -5.495  3.978   28.255  0.50 21.30  ? 46  PRO A CB  1 
ATOM   410  C  CG  A PRO A 1 46  ? -6.012  4.098   30.019  0.50 19.47  ? 46  PRO A CG  1 
ATOM   411  C  CG  B PRO A 1 46  ? -5.975  5.215   28.936  0.50 19.47  ? 46  PRO A CG  1 
ATOM   412  C  CD  A PRO A 1 46  ? -4.951  4.974   30.623  0.50 14.26  ? 46  PRO A CD  1 
ATOM   413  C  CD  B PRO A 1 46  ? -5.020  5.454   30.072  0.50 22.91  ? 46  PRO A CD  1 
ATOM   414  N  N   A LEU A 1 47  ? -2.745  4.324   26.601  0.50 14.58  ? 47  LEU A N   1 
ATOM   415  N  N   B LEU A 1 47  ? -2.576  4.058   26.368  0.50 17.27  ? 47  LEU A N   1 
ATOM   416  C  CA  A LEU A 1 47  ? -2.043  4.968   25.520  0.50 13.89  ? 47  LEU A CA  1 
ATOM   417  C  CA  B LEU A 1 47  ? -1.918  4.665   25.212  0.50 15.44  ? 47  LEU A CA  1 
ATOM   418  C  C   A LEU A 1 47  ? -3.068  5.483   24.538  0.50 15.53  ? 47  LEU A C   1 
ATOM   419  C  C   B LEU A 1 47  ? -2.950  5.342   24.298  0.50 19.03  ? 47  LEU A C   1 
ATOM   420  O  O   A LEU A 1 47  ? -4.120  4.878   24.331  0.50 16.95  ? 47  LEU A O   1 
ATOM   421  O  O   B LEU A 1 47  ? -3.935  4.710   23.911  0.50 32.90  ? 47  LEU A O   1 
ATOM   422  C  CB  A LEU A 1 47  ? -1.155  3.939   24.819  0.50 18.08  ? 47  LEU A CB  1 
ATOM   423  C  CB  B LEU A 1 47  ? -1.146  3.610   24.416  0.50 18.81  ? 47  LEU A CB  1 
ATOM   424  C  CG  A LEU A 1 47  ? 0.103   4.389   24.077  0.50 17.41  ? 47  LEU A CG  1 
ATOM   425  C  CG  B LEU A 1 47  ? 0.017   4.126   23.563  0.50 19.89  ? 47  LEU A CG  1 
ATOM   426  C  CD1 A LEU A 1 47  ? 1.041   5.119   25.025  0.50 18.68  ? 47  LEU A CD1 1 
ATOM   427  C  CD1 B LEU A 1 47  ? 0.950   4.976   24.414  0.50 17.40  ? 47  LEU A CD1 1 
ATOM   428  C  CD2 A LEU A 1 47  ? 0.795   3.180   23.463  0.50 17.82  ? 47  LEU A CD2 1 
ATOM   429  C  CD2 B LEU A 1 47  ? 0.772   2.981   22.903  0.50 13.73  ? 47  LEU A CD2 1 
ATOM   430  N  N   . SER A 1 48  ? -2.746  6.615   23.936  1.00 11.18  ? 48  SER A N   1 
ATOM   431  C  CA  . SER A 1 48  ? -3.556  7.199   22.902  1.00 10.40  ? 48  SER A CA  1 
ATOM   432  C  C   . SER A 1 48  ? -2.731  7.153   21.598  1.00 10.21  ? 48  SER A C   1 
ATOM   433  O  O   . SER A 1 48  ? -1.734  7.859   21.442  1.00 11.10  ? 48  SER A O   1 
ATOM   434  C  CB  . SER A 1 48  ? -3.919  8.632   23.271  1.00 12.64  ? 48  SER A CB  1 
ATOM   435  O  OG  . SER A 1 48  ? -4.559  9.304   22.201  1.00 15.27  ? 48  SER A OG  1 
ATOM   436  N  N   . VAL A 1 49  ? -3.200  6.325   20.668  1.00 11.02  ? 49  VAL A N   1 
ATOM   437  C  CA  . VAL A 1 49  ? -2.585  6.186   19.389  1.00 11.45  ? 49  VAL A CA  1 
ATOM   438  C  C   . VAL A 1 49  ? -3.560  6.710   18.374  1.00 12.13  ? 49  VAL A C   1 
ATOM   439  O  O   . VAL A 1 49  ? -4.576  6.058   18.176  1.00 15.37  ? 49  VAL A O   1 
ATOM   440  C  CB  . VAL A 1 49  ? -2.246  4.661   19.119  1.00 15.07  ? 49  VAL A CB  1 
ATOM   441  C  CG1 . VAL A 1 49  ? -1.409  4.578   17.822  1.00 18.10  ? 49  VAL A CG1 1 
ATOM   442  C  CG2 . VAL A 1 49  ? -1.406  4.025   20.232  1.00 16.82  ? 49  VAL A CG2 1 
ATOM   443  N  N   A SER A 1 50  ? -3.346  7.896   17.804  0.50 11.70  ? 50  SER A N   1 
ATOM   444  N  N   B SER A 1 50  ? -3.263  7.885   17.802  0.50 12.31  ? 50  SER A N   1 
ATOM   445  C  CA  A SER A 1 50  ? -4.303  8.547   16.934  0.50 13.06  ? 50  SER A CA  1 
ATOM   446  C  CA  B SER A 1 50  ? -4.206  8.557   16.946  0.50 13.31  ? 50  SER A CA  1 
ATOM   447  C  C   A SER A 1 50  ? -3.704  8.672   15.570  0.50 11.83  ? 50  SER A C   1 
ATOM   448  C  C   B SER A 1 50  ? -3.618  8.668   15.573  0.50 12.31  ? 50  SER A C   1 
ATOM   449  O  O   A SER A 1 50  ? -3.017  9.674   15.246  0.50 13.32  ? 50  SER A O   1 
ATOM   450  O  O   B SER A 1 50  ? -2.917  9.667   15.241  0.50 13.50  ? 50  SER A O   1 
ATOM   451  C  CB  A SER A 1 50  ? -4.702  9.912   17.468  0.50 14.32  ? 50  SER A CB  1 
ATOM   452  C  CB  B SER A 1 50  ? -4.583  9.930   17.499  0.50 15.57  ? 50  SER A CB  1 
ATOM   453  O  OG  A SER A 1 50  ? -5.343  9.704   18.689  0.50 12.86  ? 50  SER A OG  1 
ATOM   454  O  OG  B SER A 1 50  ? -5.465  10.594  16.634  0.50 21.30  ? 50  SER A OG  1 
ATOM   455  N  N   . TYR A 1 51  ? -3.909  7.661   14.740  1.00 11.24  ? 51  TYR A N   1 
ATOM   456  C  CA  . TYR A 1 51  ? -3.303  7.587   13.402  1.00 10.92  ? 51  TYR A CA  1 
ATOM   457  C  C   . TYR A 1 51  ? -4.223  7.872   12.251  1.00 12.25  ? 51  TYR A C   1 
ATOM   458  O  O   . TYR A 1 51  ? -3.818  7.731   11.088  1.00 13.90  ? 51  TYR A O   1 
ATOM   459  C  CB  . TYR A 1 51  ? -2.610  6.236   13.212  1.00 11.28  ? 51  TYR A CB  1 
ATOM   460  C  CG  . TYR A 1 51  ? -1.347  5.944   14.004  1.00 9.66   ? 51  TYR A CG  1 
ATOM   461  C  CD1 . TYR A 1 51  ? -0.655  6.933   14.700  1.00 10.12  ? 51  TYR A CD1 1 
ATOM   462  C  CD2 . TYR A 1 51  ? -0.826  4.659   14.010  1.00 9.27   ? 51  TYR A CD2 1 
ATOM   463  C  CE1 . TYR A 1 51  ? 0.509   6.629   15.397  1.00 9.51   ? 51  TYR A CE1 1 
ATOM   464  C  CE2 . TYR A 1 51  ? 0.328   4.349   14.693  1.00 8.72   ? 51  TYR A CE2 1 
ATOM   465  C  CZ  . TYR A 1 51  ? 0.994   5.331   15.387  1.00 8.02   ? 51  TYR A CZ  1 
ATOM   466  O  OH  . TYR A 1 51  ? 2.146   4.991   16.061  1.00 8.73   ? 51  TYR A OH  1 
ATOM   467  N  N   . ASP A 1 52  ? -5.478  8.289   12.539  1.00 14.81  ? 52  ASP A N   1 
ATOM   468  C  CA  . ASP A 1 52  ? -6.419  8.538   11.449  1.00 17.27  ? 52  ASP A CA  1 
ATOM   469  C  C   . ASP A 1 52  ? -5.975  9.478   10.386  1.00 16.76  ? 52  ASP A C   1 
ATOM   470  O  O   . ASP A 1 52  ? -6.344  9.332   9.207   1.00 23.18  ? 52  ASP A O   1 
ATOM   471  C  CB  . ASP A 1 52  ? -7.769  8.989   12.047  1.00 18.99  ? 52  ASP A CB  1 
ATOM   472  C  CG  . ASP A 1 52  ? -7.638  10.121  13.082  1.00 24.55  ? 52  ASP A CG  1 
ATOM   473  O  OD1 . ASP A 1 52  ? -6.934  9.953   14.167  1.00 30.46  ? 52  ASP A OD1 1 
ATOM   474  O  OD2 . ASP A 1 52  ? -8.236  11.207  12.841  1.00 41.27  ? 52  ASP A OD2 1 
ATOM   475  N  N   . GLN A 1 53  ? -5.249  10.499  10.797  1.00 16.94  ? 53  GLN A N   1 
ATOM   476  C  CA  . GLN A 1 53  ? -4.780  11.419  9.747   1.00 17.99  ? 53  GLN A CA  1 
ATOM   477  C  C   . GLN A 1 53  ? -3.370  11.223  9.208   1.00 16.26  ? 53  GLN A C   1 
ATOM   478  O  O   . GLN A 1 53  ? -2.819  12.109  8.552   1.00 16.79  ? 53  GLN A O   1 
ATOM   479  C  CB  . GLN A 1 53  ? -5.023  12.835  10.220  1.00 24.75  ? 53  GLN A CB  1 
ATOM   480  C  CG  . GLN A 1 53  ? -6.507  13.144  10.454  1.00 28.67  ? 53  GLN A CG  1 
ATOM   481  C  CD  . GLN A 1 53  ? -7.277  13.166  9.145   1.00 35.43  ? 53  GLN A CD  1 
ATOM   482  O  OE1 . GLN A 1 53  ? -7.009  14.008  8.272   1.00 57.71  ? 53  GLN A OE1 1 
ATOM   483  N  NE2 . GLN A 1 53  ? -8.178  12.205  8.960   1.00 48.12  ? 53  GLN A NE2 1 
ATOM   484  N  N   . ALA A 1 54  ? -2.772  10.084  9.517   1.00 14.19  ? 54  ALA A N   1 
ATOM   485  C  CA  . ALA A 1 54  ? -1.422  9.853   9.050   1.00 12.56  ? 54  ALA A CA  1 
ATOM   486  C  C   . ALA A 1 54  ? -1.278  9.942   7.513   1.00 13.19  ? 54  ALA A C   1 
ATOM   487  O  O   . ALA A 1 54  ? -2.123  9.427   6.843   1.00 18.35  ? 54  ALA A O   1 
ATOM   488  C  CB  . ALA A 1 54  ? -0.930  8.511   9.560   1.00 13.08  ? 54  ALA A CB  1 
ATOM   489  N  N   . THR A 1 55  ? -0.209  10.598  7.076   1.00 11.71  ? 55  THR A N   1 
ATOM   490  C  CA  . THR A 1 55  ? 0.109   10.787  5.681   1.00 13.77  ? 55  THR A CA  1 
ATOM   491  C  C   . THR A 1 55  ? 1.446   10.201  5.393   1.00 9.71   ? 55  THR A C   1 
ATOM   492  O  O   . THR A 1 55  ? 2.484   10.832  5.614   1.00 10.10  ? 55  THR A O   1 
ATOM   493  C  CB  . THR A 1 55  ? 0.194   12.285  5.331   1.00 20.41  ? 55  THR A CB  1 
ATOM   494  O  OG1 . THR A 1 55  ? -1.027  12.942  5.697   1.00 28.93  ? 55  THR A OG1 1 
ATOM   495  C  CG2 . THR A 1 55  ? 0.459   12.481  3.842   1.00 24.74  ? 55  THR A CG2 1 
ATOM   496  N  N   . SER A 1 56  ? 1.453   8.972   4.886   1.00 9.50   ? 56  SER A N   1 
ATOM   497  C  CA  . SER A 1 56  ? 2.709   8.355   4.473   1.00 8.99   ? 56  SER A CA  1 
ATOM   498  C  C   . SER A 1 56  ? 3.221   9.017   3.182   1.00 9.32   ? 56  SER A C   1 
ATOM   499  O  O   . SER A 1 56  ? 2.446   9.510   2.372   1.00 10.90  ? 56  SER A O   1 
ATOM   500  C  CB  . SER A 1 56  ? 2.601   6.834   4.301   1.00 9.36   ? 56  SER A CB  1 
ATOM   501  O  OG  . SER A 1 56  ? 1.722   6.533   3.231   1.00 10.68  ? 56  SER A OG  1 
ATOM   502  N  N   . LEU A 1 57  ? 4.512   9.035   3.022   1.00 8.73   ? 57  LEU A N   1 
ATOM   503  C  CA  . LEU A 1 57  ? 5.125   9.674   1.860   1.00 10.34  ? 57  LEU A CA  1 
ATOM   504  C  C   . LEU A 1 57  ? 5.887   8.703   0.955   1.00 9.05   ? 57  LEU A C   1 
ATOM   505  O  O   . LEU A 1 57  ? 5.752   8.691   -0.256  1.00 10.36  ? 57  LEU A O   1 
ATOM   506  C  CB  . LEU A 1 57  ? 5.991   10.816  2.256   1.00 13.15  ? 57  LEU A CB  1 
ATOM   507  C  CG  . LEU A 1 57  ? 5.185   12.036  2.776   1.00 15.46  ? 57  LEU A CG  1 
ATOM   508  C  CD1 . LEU A 1 57  ? 6.239   13.116  3.306   1.00 20.13  ? 57  LEU A CD1 1 
ATOM   509  C  CD2 . LEU A 1 57  ? 4.106   12.579  1.760   1.00 22.22  ? 57  LEU A CD2 1 
ATOM   510  N  N   A ARG A 1 58  ? 6.795   7.941   1.585   0.50 8.55   ? 58  ARG A N   1 
ATOM   511  N  N   B ARG A 1 58  ? 6.820   7.929   1.535   0.50 8.85   ? 58  ARG A N   1 
ATOM   512  C  CA  A ARG A 1 58  ? 7.867   7.311   0.865   0.50 8.69   ? 58  ARG A CA  1 
ATOM   513  C  CA  B ARG A 1 58  ? 7.717   7.098   0.741   0.50 9.68   ? 58  ARG A CA  1 
ATOM   514  C  C   A ARG A 1 58  ? 8.333   6.084   1.646   0.50 7.70   ? 58  ARG A C   1 
ATOM   515  C  C   B ARG A 1 58  ? 8.356   6.045   1.617   0.50 7.98   ? 58  ARG A C   1 
ATOM   516  O  O   A ARG A 1 58  ? 8.124   6.050   2.875   0.50 7.19   ? 58  ARG A O   1 
ATOM   517  O  O   B ARG A 1 58  ? 8.331   6.066   2.824   0.50 8.42   ? 58  ARG A O   1 
ATOM   518  C  CB  A ARG A 1 58  ? 8.985   8.367   0.731   0.50 9.20   ? 58  ARG A CB  1 
ATOM   519  C  CB  B ARG A 1 58  ? 8.830   7.976   0.133   0.50 9.01   ? 58  ARG A CB  1 
ATOM   520  C  CG  A ARG A 1 58  ? 10.096  7.968   -0.174  0.50 11.68  ? 58  ARG A CG  1 
ATOM   521  C  CG  B ARG A 1 58  ? 9.754   8.552   1.199   0.50 10.38  ? 58  ARG A CG  1 
ATOM   522  C  CD  A ARG A 1 58  ? 11.059  9.105   -0.406  0.50 13.36  ? 58  ARG A CD  1 
ATOM   523  C  CD  B ARG A 1 58  ? 10.897  9.127   0.507   0.50 12.27  ? 58  ARG A CD  1 
ATOM   524  N  NE  A ARG A 1 58  ? 11.859  9.284   0.798   0.50 12.38  ? 58  ARG A NE  1 
ATOM   525  N  NE  B ARG A 1 58  ? 11.900  9.479   1.511   0.50 14.57  ? 58  ARG A NE  1 
ATOM   526  C  CZ  A ARG A 1 58  ? 13.146  9.607   0.803   0.50 11.29  ? 58  ARG A CZ  1 
ATOM   527  C  CZ  B ARG A 1 58  ? 13.183  9.723   1.269   0.50 13.23  ? 58  ARG A CZ  1 
ATOM   528  N  NH1 A ARG A 1 58  ? 13.781  9.805   -0.341  0.50 13.41  ? 58  ARG A NH1 1 
ATOM   529  N  NH1 B ARG A 1 58  ? 13.667  9.661   0.036   0.50 14.66  ? 58  ARG A NH1 1 
ATOM   530  N  NH2 A ARG A 1 58  ? 13.793  9.738   1.949   0.50 10.89  ? 58  ARG A NH2 1 
ATOM   531  N  NH2 B ARG A 1 58  ? 13.983  10.040  2.276   0.50 14.95  ? 58  ARG A NH2 1 
ATOM   532  N  N   . ILE A 1 59  ? 8.961   5.131   0.943   1.00 7.65   ? 59  ILE A N   1 
ATOM   533  C  CA  . ILE A 1 59  ? 9.676   4.046   1.555   1.00 7.78   ? 59  ILE A CA  1 
ATOM   534  C  C   . ILE A 1 59  ? 11.116  4.091   1.024   1.00 7.76   ? 59  ILE A C   1 
ATOM   535  O  O   . ILE A 1 59  ? 11.310  4.285   -0.180  1.00 9.63   ? 59  ILE A O   1 
ATOM   536  C  CB  . ILE A 1 59  ? 8.954   2.719   1.330   1.00 8.53   ? 59  ILE A CB  1 
ATOM   537  C  CG1 . ILE A 1 59  ? 9.577   1.634   2.226   1.00 8.85   ? 59  ILE A CG1 1 
ATOM   538  C  CG2 . ILE A 1 59  ? 8.875   2.283   -0.117  1.00 9.66   ? 59  ILE A CG2 1 
ATOM   539  C  CD1 . ILE A 1 59  ? 8.752   0.346   2.184   1.00 10.12  ? 59  ILE A CD1 1 
ATOM   540  N  N   . LEU A 1 60  ? 12.101  3.903   1.901   1.00 8.08   ? 60  LEU A N   1 
ATOM   541  C  CA  . LEU A 1 60  ? 13.499  4.121   1.597   1.00 9.05   ? 60  LEU A CA  1 
ATOM   542  C  C   . LEU A 1 60  ? 14.306  2.957   2.160   1.00 7.85   ? 60  LEU A C   1 
ATOM   543  O  O   . LEU A 1 60  ? 14.174  2.642   3.343   1.00 8.44   ? 60  LEU A O   1 
ATOM   544  C  CB  . LEU A 1 60  ? 14.010  5.487   2.321   1.00 10.76  ? 60  LEU A CB  1 
ATOM   545  C  CG  . LEU A 1 60  ? 15.481  5.742   2.237   1.00 10.90  ? 60  LEU A CG  1 
ATOM   546  C  CD1 . LEU A 1 60  ? 15.963  5.931   0.795   1.00 13.29  ? 60  LEU A CD1 1 
ATOM   547  C  CD2 . LEU A 1 60  ? 15.769  6.937   3.078   1.00 13.25  ? 60  LEU A CD2 1 
ATOM   548  N  N   . ASN A 1 61  ? 15.177  2.367   1.354   1.00 7.81   ? 61  ASN A N   1 
ATOM   549  C  CA  . ASN A 1 61  ? 16.176  1.434   1.834   1.00 7.70   ? 61  ASN A CA  1 
ATOM   550  C  C   . ASN A 1 61  ? 17.361  2.226   2.384   1.00 7.81   ? 61  ASN A C   1 
ATOM   551  O  O   . ASN A 1 61  ? 18.064  2.875   1.624   1.00 8.97   ? 61  ASN A O   1 
ATOM   552  C  CB  . ASN A 1 61  ? 16.579  0.469   0.734   1.00 8.32   ? 61  ASN A CB  1 
ATOM   553  C  CG  . ASN A 1 61  ? 17.553  -0.579  1.183   1.00 8.04   ? 61  ASN A CG  1 
ATOM   554  O  OD1 . ASN A 1 61  ? 18.376  -0.322  2.092   1.00 8.81   ? 61  ASN A OD1 1 
ATOM   555  N  ND2 . ASN A 1 61  ? 17.513  -1.748  0.567   1.00 9.05   ? 61  ASN A ND2 1 
ATOM   556  N  N   . VAL A 1 62  ? 17.517  2.242   3.709   1.00 7.94   ? 62  VAL A N   1 
ATOM   557  C  CA  . VAL A 1 62  ? 18.551  3.007   4.390   1.00 8.69   ? 62  VAL A CA  1 
ATOM   558  C  C   . VAL A 1 62  ? 19.809  2.207   4.590   1.00 9.66   ? 62  VAL A C   1 
ATOM   559  O  O   . VAL A 1 62  ? 20.735  2.647   5.305   1.00 12.27  ? 62  VAL A O   1 
ATOM   560  C  CB  . VAL A 1 62  ? 18.031  3.615   5.715   1.00 9.34   ? 62  VAL A CB  1 
ATOM   561  C  CG1 . VAL A 1 62  ? 16.914  4.590   5.449   1.00 12.12  ? 62  VAL A CG1 1 
ATOM   562  C  CG2 . VAL A 1 62  ? 17.612  2.538   6.707   1.00 10.54  ? 62  VAL A CG2 1 
ATOM   563  N  N   . GLY A 1 63  ? 19.898  1.004   4.014   1.00 9.22   ? 63  GLY A N   1 
ATOM   564  C  CA  . GLY A 1 63  ? 21.097  0.184   4.094   1.00 10.46  ? 63  GLY A CA  1 
ATOM   565  C  C   . GLY A 1 63  ? 20.940  -0.845  5.155   1.00 11.21  ? 63  GLY A C   1 
ATOM   566  O  O   . GLY A 1 63  ? 21.024  -2.019  4.895   1.00 21.82  ? 63  GLY A O   1 
ATOM   567  N  N   . HIS A 1 64  ? 20.534  -0.502  6.338   1.00 11.86  ? 64  HIS A N   1 
ATOM   568  C  CA  . HIS A 1 64  ? 20.389  -1.462  7.441   1.00 13.29  ? 64  HIS A CA  1 
ATOM   569  C  C   . HIS A 1 64  ? 18.950  -1.845  7.712   1.00 10.71  ? 64  HIS A C   1 
ATOM   570  O  O   . HIS A 1 64  ? 18.717  -2.690  8.530   1.00 14.69  ? 64  HIS A O   1 
ATOM   571  C  CB  . HIS A 1 64  ? 21.057  -0.937  8.628   1.00 18.60  ? 64  HIS A CB  1 
ATOM   572  C  CG  . HIS A 1 64  ? 20.519  0.340   8.957   1.00 17.59  ? 64  HIS A CG  1 
ATOM   573  N  ND1 . HIS A 1 64  ? 21.016  1.514   8.537   1.00 17.56  ? 64  HIS A ND1 1 
ATOM   574  C  CD2 . HIS A 1 64  ? 19.447  0.618   9.804   1.00 17.61  ? 64  HIS A CD2 1 
ATOM   575  C  CE1 . HIS A 1 64  ? 20.314  2.503   9.059   1.00 17.36  ? 64  HIS A CE1 1 
ATOM   576  N  NE2 . HIS A 1 64  ? 19.324  1.971   9.833   1.00 20.35  ? 64  HIS A NE2 1 
ATOM   577  N  N   . ALA A 1 65  ? 18.000  -1.216  7.015   1.00 9.09   ? 65  ALA A N   1 
ATOM   578  C  CA  . ALA A 1 65  ? 16.574  -1.451  7.163   1.00 9.04   ? 65  ALA A CA  1 
ATOM   579  C  C   . ALA A 1 65  ? 15.878  -0.728  6.030   1.00 7.49   ? 65  ALA A C   1 
ATOM   580  O  O   . ALA A 1 65  ? 16.536  -0.117  5.168   1.00 9.10   ? 65  ALA A O   1 
ATOM   581  C  CB  . ALA A 1 65  ? 16.103  -0.930  8.526   1.00 11.23  ? 65  ALA A CB  1 
ATOM   582  N  N   . PHE A 1 66  ? 14.576  -0.753  6.023   1.00 7.60   ? 66  PHE A N   1 
ATOM   583  C  CA  . PHE A 1 66  ? 13.782  0.194   5.225   1.00 7.51   ? 66  PHE A CA  1 
ATOM   584  C  C   . PHE A 1 66  ? 12.965  1.046   6.161   1.00 7.26   ? 66  PHE A C   1 
ATOM   585  O  O   . PHE A 1 66  ? 12.488  0.621   7.193   1.00 7.91   ? 66  PHE A O   1 
ATOM   586  C  CB  . PHE A 1 66  ? 12.933  -0.503  4.167   1.00 8.75   ? 66  PHE A CB  1 
ATOM   587  C  CG  . PHE A 1 66  ? 11.867  -1.433  4.710   1.00 8.21   ? 66  PHE A CG  1 
ATOM   588  C  CD1 . PHE A 1 66  ? 10.624  -0.926  5.054   1.00 9.13   ? 66  PHE A CD1 1 
ATOM   589  C  CD2 . PHE A 1 66  ? 12.124  -2.777  4.856   1.00 8.11   ? 66  PHE A CD2 1 
ATOM   590  C  CE1 . PHE A 1 66  ? 9.647   -1.784  5.586   1.00 9.41   ? 66  PHE A CE1 1 
ATOM   591  C  CE2 . PHE A 1 66  ? 11.150  -3.640  5.372   1.00 9.35   ? 66  PHE A CE2 1 
ATOM   592  C  CZ  . PHE A 1 66  ? 9.915   -3.120  5.735   1.00 9.04   ? 66  PHE A CZ  1 
ATOM   593  N  N   . HIS A 1 67  ? 12.783  2.317   5.771   1.00 6.95   ? 67  HIS A N   1 
ATOM   594  C  CA  . HIS A 1 67  ? 12.000  3.261   6.518   1.00 7.27   ? 67  HIS A CA  1 
ATOM   595  C  C   . HIS A 1 67  ? 10.782  3.656   5.716   1.00 7.04   ? 67  HIS A C   1 
ATOM   596  O  O   . HIS A 1 67  ? 10.927  4.058   4.552   1.00 8.19   ? 67  HIS A O   1 
ATOM   597  C  CB  . HIS A 1 67  ? 12.818  4.532   6.843   1.00 8.01   ? 67  HIS A CB  1 
ATOM   598  C  CG  . HIS A 1 67  ? 13.872  4.332   7.875   1.00 8.49   ? 67  HIS A CG  1 
ATOM   599  N  ND1 . HIS A 1 67  ? 14.678  5.379   8.302   1.00 10.57  ? 67  HIS A ND1 1 
ATOM   600  C  CD2 . HIS A 1 67  ? 14.258  3.203   8.584   1.00 8.94   ? 67  HIS A CD2 1 
ATOM   601  C  CE1 . HIS A 1 67  ? 15.474  4.817   9.278   1.00 10.82  ? 67  HIS A CE1 1 
ATOM   602  N  NE2 . HIS A 1 67  ? 15.266  3.543   9.429   1.00 10.76  ? 67  HIS A NE2 1 
ATOM   603  N  N   . VAL A 1 68  ? 9.602   3.606   6.319   1.00 6.57   ? 68  VAL A N   1 
ATOM   604  C  CA  . VAL A 1 68  ? 8.411   4.214   5.774   1.00 7.15   ? 68  VAL A CA  1 
ATOM   605  C  C   . VAL A 1 68  ? 8.285   5.545   6.443   1.00 6.90   ? 68  VAL A C   1 
ATOM   606  O  O   . VAL A 1 68  ? 8.128   5.617   7.677   1.00 7.45   ? 68  VAL A O   1 
ATOM   607  C  CB  . VAL A 1 68  ? 7.152   3.346   5.947   1.00 7.39   ? 68  VAL A CB  1 
ATOM   608  C  CG1 . VAL A 1 68  ? 5.941   4.145   5.495   1.00 8.94   ? 68  VAL A CG1 1 
ATOM   609  C  CG2 . VAL A 1 68  ? 7.279   2.064   5.172   1.00 8.82   ? 68  VAL A CG2 1 
ATOM   610  N  N   . GLU A 1 69  ? 8.331   6.619   5.670   1.00 7.29   ? 69  GLU A N   1 
ATOM   611  C  CA  . GLU A 1 69  ? 8.346   7.982   6.179   1.00 7.35   ? 69  GLU A CA  1 
ATOM   612  C  C   . GLU A 1 69  ? 6.990   8.631   6.029   1.00 7.40   ? 69  GLU A C   1 
ATOM   613  O  O   . GLU A 1 69  ? 6.282   8.380   5.040   1.00 9.11   ? 69  GLU A O   1 
ATOM   614  C  CB  . GLU A 1 69  ? 9.389   8.815   5.472   1.00 9.41   ? 69  GLU A CB  1 
ATOM   615  C  CG  . GLU A 1 69  ? 10.809  8.261   5.658   1.00 11.75  ? 69  GLU A CG  1 
ATOM   616  C  CD  . GLU A 1 69  ? 11.882  9.114   5.048   1.00 14.08  ? 69  GLU A CD  1 
ATOM   617  O  OE1 . GLU A 1 69  ? 11.556  9.752   4.006   1.00 20.43  ? 69  GLU A OE1 1 
ATOM   618  O  OE2 . GLU A 1 69  ? 13.088  9.053   5.498   1.00 16.75  ? 69  GLU A OE2 1 
ATOM   619  N  N   . PHE A 1 70  ? 6.654   9.509   6.978   1.00 7.87   ? 70  PHE A N   1 
ATOM   620  C  CA  . PHE A 1 70  ? 5.405   10.228  7.007   1.00 8.06   ? 70  PHE A CA  1 
ATOM   621  C  C   . PHE A 1 70  ? 5.660   11.730  6.983   1.00 8.65   ? 70  PHE A C   1 
ATOM   622  O  O   . PHE A 1 70  ? 6.699   12.212  7.388   1.00 10.22  ? 70  PHE A O   1 
ATOM   623  C  CB  . PHE A 1 70  ? 4.613   9.907   8.297   1.00 8.40   ? 70  PHE A CB  1 
ATOM   624  C  CG  . PHE A 1 70  ? 4.084   8.490   8.342   1.00 7.55   ? 70  PHE A CG  1 
ATOM   625  C  CD1 . PHE A 1 70  ? 4.940   7.406   8.592   1.00 8.60   ? 70  PHE A CD1 1 
ATOM   626  C  CD2 . PHE A 1 70  ? 2.794   8.230   8.043   1.00 8.19   ? 70  PHE A CD2 1 
ATOM   627  C  CE1 . PHE A 1 70  ? 4.470   6.138   8.524   1.00 9.59   ? 70  PHE A CE1 1 
ATOM   628  C  CE2 . PHE A 1 70  ? 2.294   6.935   7.984   1.00 8.85   ? 70  PHE A CE2 1 
ATOM   629  C  CZ  . PHE A 1 70  ? 3.165   5.878   8.234   1.00 9.62   ? 70  PHE A CZ  1 
ATOM   630  N  N   A ASP A 1 71  ? 4.551   12.511  6.784   0.50 9.20   ? 71  ASP A N   1 
ATOM   631  N  N   B ASP A 1 71  ? 4.778   12.434  6.281   0.50 8.40   ? 71  ASP A N   1 
ATOM   632  C  CA  A ASP A 1 71  ? 4.538   13.974  6.911   0.50 10.25  ? 71  ASP A CA  1 
ATOM   633  C  CA  B ASP A 1 71  ? 4.827   13.896  6.303   0.50 10.50  ? 71  ASP A CA  1 
ATOM   634  C  C   A ASP A 1 71  ? 4.475   14.315  8.305   0.50 10.02  ? 71  ASP A C   1 
ATOM   635  C  C   B ASP A 1 71  ? 4.543   14.321  7.824   0.50 11.50  ? 71  ASP A C   1 
ATOM   636  O  O   A ASP A 1 71  ? 3.492   14.148  8.973   0.50 11.59  ? 71  ASP A O   1 
ATOM   637  O  O   B ASP A 1 71  ? 3.387   14.058  8.240   0.50 13.14  ? 71  ASP A O   1 
ATOM   638  C  CB  A ASP A 1 71  ? 3.398   14.561  6.136   0.50 11.09  ? 71  ASP A CB  1 
ATOM   639  C  CB  B ASP A 1 71  ? 3.776   14.418  5.298   0.50 11.82  ? 71  ASP A CB  1 
ATOM   640  C  CG  A ASP A 1 71  ? 3.270   16.140  6.298   0.50 11.22  ? 71  ASP A CG  1 
ATOM   641  C  CG  B ASP A 1 71  ? 3.774   15.869  5.179   0.50 14.25  ? 71  ASP A CG  1 
ATOM   642  O  OD1 A ASP A 1 71  ? 4.183   16.762  6.858   0.50 13.15  ? 71  ASP A OD1 1 
ATOM   643  O  OD1 B ASP A 1 71  ? 4.044   16.530  6.165   0.50 14.64  ? 71  ASP A OD1 1 
ATOM   644  O  OD2 A ASP A 1 71  ? 2.261   16.637  5.920   0.50 16.35  ? 71  ASP A OD2 1 
ATOM   645  O  OD2 B ASP A 1 71  ? 3.441   16.319  4.061   0.50 21.36  ? 71  ASP A OD2 1 
ATOM   646  N  N   . ASP A 1 72  ? 5.533   14.900  8.635   1.00 12.24  ? 72  ASP A N   1 
ATOM   647  C  CA  . ASP A 1 72  ? 5.499   15.326  10.011  1.00 12.44  ? 72  ASP A CA  1 
ATOM   648  C  C   . ASP A 1 72  ? 5.519   16.868  10.090  1.00 14.14  ? 72  ASP A C   1 
ATOM   649  O  O   . ASP A 1 72  ? 5.943   17.407  11.130  1.00 17.48  ? 72  ASP A O   1 
ATOM   650  C  CB  . ASP A 1 72  ? 6.629   14.734  10.798  1.00 12.85  ? 72  ASP A CB  1 
ATOM   651  C  CG  . ASP A 1 72  ? 8.001   15.184  10.406  1.00 13.70  ? 72  ASP A CG  1 
ATOM   652  O  OD1 . ASP A 1 72  ? 8.145   15.890  9.370   1.00 15.72  ? 72  ASP A OD1 1 
ATOM   653  O  OD2 . ASP A 1 72  ? 8.972   14.866  11.171  1.00 13.62  ? 72  ASP A OD2 1 
ATOM   654  N  N   . SER A 1 73  ? 5.044   17.543  9.057   1.00 15.33  ? 73  SER A N   1 
ATOM   655  C  CA  . SER A 1 73  ? 4.973   19.021  9.046   1.00 17.04  ? 73  SER A CA  1 
ATOM   656  C  C   . SER A 1 73  ? 3.716   19.646  9.720   1.00 17.03  ? 73  SER A C   1 
ATOM   657  O  O   . SER A 1 73  ? 3.704   20.840  9.875   1.00 18.10  ? 73  SER A O   1 
ATOM   658  C  CB  . SER A 1 73  ? 5.028   19.512  7.598   1.00 16.62  ? 73  SER A CB  1 
ATOM   659  O  OG  . SER A 1 73  ? 3.825   19.207  6.910   1.00 19.18  ? 73  SER A OG  1 
ATOM   660  N  N   . GLN A 1 74  ? 2.758   18.824  10.121  1.00 19.48  ? 74  GLN A N   1 
ATOM   661  C  CA  . GLN A 1 74  ? 1.612   19.422  10.823  1.00 24.41  ? 74  GLN A CA  1 
ATOM   662  C  C   . GLN A 1 74  ? 1.044   18.407  11.700  1.00 17.55  ? 74  GLN A C   1 
ATOM   663  O  O   . GLN A 1 74  ? 1.351   17.149  11.592  1.00 15.93  ? 74  GLN A O   1 
ATOM   664  C  CB  . GLN A 1 74  ? 0.526   19.997  9.893   1.00 30.90  ? 74  GLN A CB  1 
ATOM   665  C  CG  . GLN A 1 74  ? 0.419   19.470  8.486   1.00 31.58  ? 74  GLN A CG  1 
ATOM   666  C  CD  . GLN A 1 74  ? -0.677  20.159  7.683   1.00 24.25  ? 74  GLN A CD  1 
ATOM   667  O  OE1 . GLN A 1 74  ? -1.608  20.763  8.233   1.00 54.66  ? 74  GLN A OE1 1 
ATOM   668  N  NE2 . GLN A 1 74  ? -0.572  20.004  6.315   1.00 34.57  ? 74  GLN A NE2 1 
ATOM   669  N  N   A ASP A 1 75  ? 0.231   18.754  12.673  0.50 27.35  ? 75  ASP A N   1 
ATOM   670  N  N   B ASP A 1 75  ? 0.041   18.856  12.452  0.50 12.69  ? 75  ASP A N   1 
ATOM   671  C  CA  A ASP A 1 75  ? 0.051   17.754  13.778  0.50 26.85  ? 75  ASP A CA  1 
ATOM   672  C  CA  B ASP A 1 75  ? -0.454  18.109  13.574  0.50 12.78  ? 75  ASP A CA  1 
ATOM   673  C  C   A ASP A 1 75  ? -1.111  16.940  13.397  0.50 30.26  ? 75  ASP A C   1 
ATOM   674  C  C   B ASP A 1 75  ? -1.301  17.008  13.072  0.50 16.68  ? 75  ASP A C   1 
ATOM   675  O  O   A ASP A 1 75  ? -2.263  17.321  13.541  0.50 51.46  ? 75  ASP A O   1 
ATOM   676  O  O   B ASP A 1 75  ? -2.476  17.226  12.879  0.50 20.13  ? 75  ASP A O   1 
ATOM   677  C  CB  A ASP A 1 75  ? -0.250  18.469  15.113  0.50 30.99  ? 75  ASP A CB  1 
ATOM   678  C  CB  B ASP A 1 75  ? -1.241  19.104  14.461  0.50 16.17  ? 75  ASP A CB  1 
ATOM   679  C  CG  A ASP A 1 75  ? 0.534   17.911  16.320  0.50 22.43  ? 75  ASP A CG  1 
ATOM   680  C  CG  B ASP A 1 75  ? -1.748  18.505  15.771  0.50 16.78  ? 75  ASP A CG  1 
ATOM   681  O  OD1 A ASP A 1 75  ? 1.286   16.916  16.191  0.50 15.24  ? 75  ASP A OD1 1 
ATOM   682  O  OD1 B ASP A 1 75  ? -1.431  17.339  16.086  0.50 16.47  ? 75  ASP A OD1 1 
ATOM   683  O  OD2 A ASP A 1 75  ? 0.385   18.510  17.418  0.50 21.79  ? 75  ASP A OD2 1 
ATOM   684  O  OD2 B ASP A 1 75  ? -2.482  19.228  16.488  0.50 26.58  ? 75  ASP A OD2 1 
ATOM   685  N  N   . LYS A 1 76  ? -0.747  15.773  12.932  1.00 15.99  ? 76  LYS A N   1 
ATOM   686  C  CA  . LYS A 1 76  ? -1.482  14.662  12.308  1.00 19.35  ? 76  LYS A CA  1 
ATOM   687  C  C   . LYS A 1 76  ? -1.628  13.469  13.167  1.00 25.26  ? 76  LYS A C   1 
ATOM   688  O  O   . LYS A 1 76  ? -2.545  13.378  13.976  1.00 28.27  ? 76  LYS A O   1 
ATOM   689  C  CB  . LYS A 1 76  ? -1.048  14.332  10.868  1.00 19.45  ? 76  LYS A CB  1 
ATOM   690  C  CG  . LYS A 1 76  ? -1.263  15.410  9.803   1.00 28.76  ? 76  LYS A CG  1 
ATOM   691  C  CD  . LYS A 1 76  ? -0.583  15.200  8.446   1.00 31.66  ? 76  LYS A CD  1 
ATOM   692  C  CE  . LYS A 1 76  ? -1.033  16.212  7.374   1.00 25.72  ? 76  LYS A CE  1 
ATOM   693  N  NZ  . LYS A 1 76  ? -0.434  15.998  6.028   1.00 29.05  ? 76  LYS A NZ  1 
ATOM   694  N  N   . ALA A 1 77  ? -0.771  12.545  12.982  1.00 21.48  ? 77  ALA A N   1 
ATOM   695  C  CA  . ALA A 1 77  ? -0.730  11.239  13.650  1.00 13.23  ? 77  ALA A CA  1 
ATOM   696  C  C   . ALA A 1 77  ? 0.055   11.451  14.923  1.00 11.94  ? 77  ALA A C   1 
ATOM   697  O  O   . ALA A 1 77  ? 1.249   11.911  14.807  1.00 15.42  ? 77  ALA A O   1 
ATOM   698  C  CB  . ALA A 1 77  ? -0.039  10.304  12.681  1.00 16.40  ? 77  ALA A CB  1 
ATOM   699  N  N   A VAL A 1 78  ? -0.481  11.091  16.035  0.50 11.69  ? 78  VAL A N   1 
ATOM   700  N  N   B VAL A 1 78  ? -0.601  11.349  16.089  0.50 9.97   ? 78  VAL A N   1 
ATOM   701  C  CA  A VAL A 1 78  ? 0.288   11.370  17.144  0.50 11.75  ? 78  VAL A CA  1 
ATOM   702  C  CA  B VAL A 1 78  ? -0.099  11.659  17.475  0.50 8.70   ? 78  VAL A CA  1 
ATOM   703  C  C   A VAL A 1 78  ? 0.063   10.231  18.096  0.50 9.32   ? 78  VAL A C   1 
ATOM   704  C  C   B VAL A 1 78  ? -0.154  10.467  18.425  0.50 8.23   ? 78  VAL A C   1 
ATOM   705  O  O   A VAL A 1 78  ? -0.927  9.489   18.039  0.50 9.45   ? 78  VAL A O   1 
ATOM   706  O  O   B VAL A 1 78  ? -1.197  9.808   18.557  0.50 8.22   ? 78  VAL A O   1 
ATOM   707  C  CB  A VAL A 1 78  ? -0.124  12.712  17.796  0.50 11.30  ? 78  VAL A CB  1 
ATOM   708  C  CB  B VAL A 1 78  ? -0.938  12.772  18.138  0.50 9.14   ? 78  VAL A CB  1 
ATOM   709  C  CG1 A VAL A 1 78  ? 0.207   13.924  16.913  0.50 14.05  ? 78  VAL A CG1 1 
ATOM   710  C  CG1 B VAL A 1 78  ? -0.534  12.964  19.564  0.50 10.75  ? 78  VAL A CG1 1 
ATOM   711  C  CG2 A VAL A 1 78  ? -1.611  12.704  18.197  0.50 14.48  ? 78  VAL A CG2 1 
ATOM   712  C  CG2 B VAL A 1 78  ? -0.692  14.069  17.383  0.50 12.53  ? 78  VAL A CG2 1 
ATOM   713  N  N   . LEU A 1 79  ? 0.972   10.195  19.065  1.00 9.14   ? 79  LEU A N   1 
ATOM   714  C  CA  . LEU A 1 79  ? 1.044   9.285   20.214  1.00 8.95   ? 79  LEU A CA  1 
ATOM   715  C  C   . LEU A 1 79  ? 1.078   10.142  21.468  1.00 9.10   ? 79  LEU A C   1 
ATOM   716  O  O   . LEU A 1 79  ? 1.924   11.068  21.578  1.00 9.87   ? 79  LEU A O   1 
ATOM   717  C  CB  . LEU A 1 79  ? 2.278   8.425   20.099  1.00 9.42   ? 79  LEU A CB  1 
ATOM   718  C  CG  . LEU A 1 79  ? 2.489   7.383   21.177  1.00 10.02  ? 79  LEU A CG  1 
ATOM   719  C  CD1 . LEU A 1 79  ? 1.442   6.306   21.087  1.00 13.47  ? 79  LEU A CD1 1 
ATOM   720  C  CD2 . LEU A 1 79  ? 3.847   6.746   21.062  1.00 10.48  ? 79  LEU A CD2 1 
ATOM   721  N  N   . LYS A 1 80  ? 0.227   9.839   22.438  1.00 9.25   ? 80  LYS A N   1 
ATOM   722  C  CA  . LYS A 1 80  ? 0.223   10.569  23.693  1.00 10.27  ? 80  LYS A CA  1 
ATOM   723  C  C   . LYS A 1 80  ? -0.263  9.596   24.776  1.00 9.56   ? 80  LYS A C   1 
ATOM   724  O  O   . LYS A 1 80  ? -0.604  8.454   24.522  1.00 10.36  ? 80  LYS A O   1 
ATOM   725  C  CB  . LYS A 1 80  ? -0.578  11.826  23.630  1.00 12.79  ? 80  LYS A CB  1 
ATOM   726  C  CG  . LYS A 1 80  ? -1.944  11.682  23.433  1.00 15.01  ? 80  LYS A CG  1 
ATOM   727  C  CD  . LYS A 1 80  ? -2.647  13.025  23.222  1.00 19.00  ? 80  LYS A CD  1 
ATOM   728  C  CE  . LYS A 1 80  ? -2.648  13.978  24.386  1.00 42.12  ? 80  LYS A CE  1 
ATOM   729  N  NZ  . LYS A 1 80  ? -3.735  14.954  24.130  1.00 58.82  ? 80  LYS A NZ  1 
ATOM   730  N  N   . GLY A 1 81  ? -0.296  10.089  25.997  1.00 11.24  ? 81  GLY A N   1 
ATOM   731  C  CA  . GLY A 1 81  ? -0.819  9.269   27.063  1.00 12.17  ? 81  GLY A CA  1 
ATOM   732  C  C   . GLY A 1 81  ? 0.244   8.230   27.469  1.00 12.63  ? 81  GLY A C   1 
ATOM   733  O  O   . GLY A 1 81  ? 1.421   8.354   27.206  1.00 11.14  ? 81  GLY A O   1 
ATOM   734  N  N   . GLY A 1 82  ? -0.203  7.224   28.221  1.00 18.03  ? 82  GLY A N   1 
ATOM   735  C  CA  . GLY A 1 82  ? 0.782   6.290   28.883  1.00 16.71  ? 82  GLY A CA  1 
ATOM   736  C  C   . GLY A 1 82  ? 1.749   6.991   29.752  1.00 15.06  ? 82  GLY A C   1 
ATOM   737  O  O   . GLY A 1 82  ? 1.411   7.769   30.654  1.00 18.45  ? 82  GLY A O   1 
ATOM   738  N  N   . PRO A 1 83  ? 2.999   6.625   29.462  1.00 14.25  ? 83  PRO A N   1 
ATOM   739  C  CA  . PRO A 1 83  ? 4.006   7.226   30.255  1.00 15.15  ? 83  PRO A CA  1 
ATOM   740  C  C   . PRO A 1 83  ? 4.290   8.603   29.772  1.00 13.35  ? 83  PRO A C   1 
ATOM   741  O  O   . PRO A 1 83  ? 5.010   9.225   30.464  1.00 16.97  ? 83  PRO A O   1 
ATOM   742  C  CB  . PRO A 1 83  ? 5.179   6.293   30.039  1.00 14.24  ? 83  PRO A CB  1 
ATOM   743  C  CG  . PRO A 1 83  ? 5.044   5.873   28.593  1.00 12.05  ? 83  PRO A CG  1 
ATOM   744  C  CD  . PRO A 1 83  ? 3.551   5.725   28.420  1.00 13.43  ? 83  PRO A CD  1 
ATOM   745  N  N   . LEU A 1 84  ? 3.773   9.050   28.658  1.00 11.17  ? 84  LEU A N   1 
ATOM   746  C  CA  . LEU A 1 84  ? 4.265   10.254  28.028  1.00 10.43  ? 84  LEU A CA  1 
ATOM   747  C  C   . LEU A 1 84  ? 3.628   11.505  28.611  1.00 12.40  ? 84  LEU A C   1 
ATOM   748  O  O   . LEU A 1 84  ? 2.449   11.565  28.883  1.00 14.82  ? 84  LEU A O   1 
ATOM   749  C  CB  . LEU A 1 84  ? 3.958   10.215  26.541  1.00 9.94   ? 84  LEU A CB  1 
ATOM   750  C  CG  . LEU A 1 84  ? 4.528   8.958   25.844  1.00 9.71   ? 84  LEU A CG  1 
ATOM   751  C  CD1 . LEU A 1 84  ? 4.002   8.934   24.408  1.00 10.65  ? 84  LEU A CD1 1 
ATOM   752  C  CD2 . LEU A 1 84  ? 6.046   8.942   25.878  1.00 9.84   ? 84  LEU A CD2 1 
ATOM   753  N  N   . ASP A 1 85  ? 4.418   12.572  28.648  1.00 13.14  ? 85  ASP A N   1 
ATOM   754  C  CA  . ASP A 1 85  ? 3.955   13.919  28.969  1.00 15.94  ? 85  ASP A CA  1 
ATOM   755  C  C   . ASP A 1 85  ? 3.960   14.619  27.576  1.00 16.41  ? 85  ASP A C   1 
ATOM   756  O  O   . ASP A 1 85  ? 4.981   14.585  26.815  1.00 18.43  ? 85  ASP A O   1 
ATOM   757  C  CB  . ASP A 1 85  ? 4.975   14.641  29.960  1.00 17.58  ? 85  ASP A CB  1 
ATOM   758  C  CG  . ASP A 1 85  ? 4.860   14.133  31.377  1.00 19.82  ? 85  ASP A CG  1 
ATOM   759  O  OD1 . ASP A 1 85  ? 3.776   13.562  31.691  1.00 22.87  ? 85  ASP A OD1 1 
ATOM   760  O  OD2 . ASP A 1 85  ? 5.806   14.309  32.230  1.00 24.74  ? 85  ASP A OD2 1 
ATOM   761  N  N   . GLY A 1 86  ? 2.901   15.333  27.205  1.00 18.07  ? 86  GLY A N   1 
ATOM   762  C  CA  . GLY A 1 86  ? 2.858   15.939  25.918  1.00 17.94  ? 86  GLY A CA  1 
ATOM   763  C  C   . GLY A 1 86  ? 2.537   15.027  24.725  1.00 15.51  ? 86  GLY A C   1 
ATOM   764  O  O   . GLY A 1 86  ? 2.077   13.914  24.839  1.00 23.04  ? 86  GLY A O   1 
ATOM   765  N  N   A THR A 1 87  ? 2.748   15.582  23.515  0.50 12.51  ? 87  THR A N   1 
ATOM   766  N  N   B THR A 1 87  ? 2.916   15.504  23.573  0.50 11.81  ? 87  THR A N   1 
ATOM   767  C  CA  A THR A 1 87  ? 2.331   15.017  22.167  0.50 12.32  ? 87  THR A CA  1 
ATOM   768  C  CA  B THR A 1 87  ? 2.440   14.843  22.407  0.50 10.82  ? 87  THR A CA  1 
ATOM   769  C  C   A THR A 1 87  ? 3.506   14.656  21.287  0.50 9.09   ? 87  THR A C   1 
ATOM   770  C  C   B THR A 1 87  ? 3.614   14.574  21.520  0.50 8.67   ? 87  THR A C   1 
ATOM   771  O  O   A THR A 1 87  ? 4.388   15.483  21.029  0.50 8.67   ? 87  THR A O   1 
ATOM   772  O  O   B THR A 1 87  ? 4.585   15.407  21.481  0.50 8.35   ? 87  THR A O   1 
ATOM   773  C  CB  A THR A 1 87  ? 1.566   16.084  21.369  0.50 13.96  ? 87  THR A CB  1 
ATOM   774  C  CB  B THR A 1 87  ? 1.359   15.722  21.740  0.50 11.02  ? 87  THR A CB  1 
ATOM   775  O  OG1 A THR A 1 87  ? 0.418   16.498  22.087  0.50 19.24  ? 87  THR A OG1 1 
ATOM   776  O  OG1 B THR A 1 87  ? 1.917   17.018  21.467  0.50 10.37  ? 87  THR A OG1 1 
ATOM   777  C  CG2 A THR A 1 87  ? 1.141   15.606  20.032  0.50 17.98  ? 87  THR A CG2 1 
ATOM   778  C  CG2 B THR A 1 87  ? 0.206   15.872  22.665  0.50 14.40  ? 87  THR A CG2 1 
ATOM   779  N  N   . TYR A 1 88  ? 3.542   13.421  20.838  1.00 8.52   ? 88  TYR A N   1 
ATOM   780  C  CA  . TYR A 1 88  ? 4.612   12.944  19.996  1.00 8.12   ? 88  TYR A CA  1 
ATOM   781  C  C   . TYR A 1 88  ? 4.067   12.662  18.610  1.00 7.86   ? 88  TYR A C   1 
ATOM   782  O  O   . TYR A 1 88  ? 3.069   11.946  18.452  1.00 11.12  ? 88  TYR A O   1 
ATOM   783  C  CB  . TYR A 1 88  ? 5.263   11.703  20.606  1.00 8.29   ? 88  TYR A CB  1 
ATOM   784  C  CG  . TYR A 1 88  ? 6.034   11.936  21.878  1.00 7.89   ? 88  TYR A CG  1 
ATOM   785  C  CD1 . TYR A 1 88  ? 5.427   12.283  23.086  1.00 8.76   ? 88  TYR A CD1 1 
ATOM   786  C  CD2 . TYR A 1 88  ? 7.411   11.748  21.873  1.00 6.97   ? 88  TYR A CD2 1 
ATOM   787  C  CE1 . TYR A 1 88  ? 6.192   12.460  24.229  1.00 8.84   ? 88  TYR A CE1 1 
ATOM   788  C  CE2 . TYR A 1 88  ? 8.152   11.861  23.027  1.00 7.29   ? 88  TYR A CE2 1 
ATOM   789  C  CZ  . TYR A 1 88  ? 7.538   12.204  24.198  1.00 7.29   ? 88  TYR A CZ  1 
ATOM   790  O  OH  . TYR A 1 88  ? 8.244   12.272  25.369  1.00 8.11   ? 88  TYR A OH  1 
ATOM   791  N  N   . ARG A 1 89  ? 4.743   13.149  17.587  1.00 7.24   ? 89  ARG A N   1 
ATOM   792  C  CA  . ARG A 1 89  ? 4.262   13.083  16.227  1.00 7.61   ? 89  ARG A CA  1 
ATOM   793  C  C   . ARG A 1 89  ? 4.904   11.925  15.490  1.00 6.91   ? 89  ARG A C   1 
ATOM   794  O  O   . ARG A 1 89  ? 6.138   11.823  15.437  1.00 7.25   ? 89  ARG A O   1 
ATOM   795  C  CB  . ARG A 1 89  ? 4.635   14.388  15.547  1.00 9.36   ? 89  ARG A CB  1 
ATOM   796  C  CG  . ARG A 1 89  ? 4.072   14.539  14.175  1.00 10.97  ? 89  ARG A CG  1 
ATOM   797  C  CD  . ARG A 1 89  ? 4.309   15.908  13.548  1.00 12.51  ? 89  ARG A CD  1 
ATOM   798  N  NE  . ARG A 1 89  ? 3.578   16.889  14.375  1.00 13.48  ? 89  ARG A NE  1 
ATOM   799  C  CZ  . ARG A 1 89  ? 3.632   18.200  14.159  1.00 12.41  ? 89  ARG A CZ  1 
ATOM   800  N  NH1 . ARG A 1 89  ? 4.445   18.685  13.240  1.00 14.67  ? 89  ARG A NH1 1 
ATOM   801  N  NH2 . ARG A 1 89  ? 3.008   19.034  14.974  1.00 15.82  ? 89  ARG A NH2 1 
ATOM   802  N  N   . LEU A 1 90  ? 4.070   11.064  14.903  1.00 7.41   ? 90  LEU A N   1 
ATOM   803  C  CA  . LEU A 1 90  ? 4.593   9.968   14.078  1.00 7.36   ? 90  LEU A CA  1 
ATOM   804  C  C   . LEU A 1 90  ? 5.312   10.528  12.882  1.00 7.49   ? 90  LEU A C   1 
ATOM   805  O  O   . LEU A 1 90  ? 4.804   11.385  12.158  1.00 8.37   ? 90  LEU A O   1 
ATOM   806  C  CB  . LEU A 1 90  ? 3.416   9.122   13.573  1.00 8.33   ? 90  LEU A CB  1 
ATOM   807  C  CG  . LEU A 1 90  ? 3.784   7.982   12.597  1.00 8.62   ? 90  LEU A CG  1 
ATOM   808  C  CD1 . LEU A 1 90  ? 4.599   6.886   13.332  1.00 9.25   ? 90  LEU A CD1 1 
ATOM   809  C  CD2 . LEU A 1 90  ? 2.538   7.424   11.995  1.00 9.95   ? 90  LEU A CD2 1 
ATOM   810  N  N   . PHE A 1 91  ? 6.503   9.974   12.610  1.00 6.97   ? 91  PHE A N   1 
ATOM   811  C  CA  . PHE A 1 91  ? 7.270   10.367  11.423  1.00 7.39   ? 91  PHE A CA  1 
ATOM   812  C  C   . PHE A 1 91  ? 7.801   9.212   10.610  1.00 6.70   ? 91  PHE A C   1 
ATOM   813  O  O   . PHE A 1 91  ? 8.149   9.452   9.439   1.00 7.32   ? 91  PHE A O   1 
ATOM   814  C  CB  . PHE A 1 91  ? 8.363   11.388  11.752  1.00 7.92   ? 91  PHE A CB  1 
ATOM   815  C  CG  . PHE A 1 91  ? 9.483   10.815  12.550  1.00 7.09   ? 91  PHE A CG  1 
ATOM   816  C  CD1 . PHE A 1 91  ? 10.653  10.424  11.926  1.00 7.40   ? 91  PHE A CD1 1 
ATOM   817  C  CD2 . PHE A 1 91  ? 9.386   10.668  13.922  1.00 7.07   ? 91  PHE A CD2 1 
ATOM   818  C  CE1 . PHE A 1 91  ? 11.692  9.878   12.657  1.00 7.41   ? 91  PHE A CE1 1 
ATOM   819  C  CE2 . PHE A 1 91  ? 10.407  10.140  14.658  1.00 7.27   ? 91  PHE A CE2 1 
ATOM   820  C  CZ  . PHE A 1 91  ? 11.580  9.730   14.031  1.00 7.07   ? 91  PHE A CZ  1 
ATOM   821  N  N   . GLN A 1 92  ? 7.902   8.013   11.158  1.00 6.62   ? 92  GLN A N   1 
ATOM   822  C  CA  . GLN A 1 92  ? 8.535   6.914   10.422  1.00 6.59   ? 92  GLN A CA  1 
ATOM   823  C  C   . GLN A 1 92  ? 8.202   5.604   11.109  1.00 6.35   ? 92  GLN A C   1 
ATOM   824  O  O   . GLN A 1 92  ? 8.050   5.607   12.346  1.00 6.92   ? 92  GLN A O   1 
ATOM   825  C  CB  . GLN A 1 92  ? 10.040  7.196   10.425  1.00 8.03   ? 92  GLN A CB  1 
ATOM   826  C  CG  . GLN A 1 92  ? 10.939  6.166   9.778   1.00 7.78   ? 92  GLN A CG  1 
ATOM   827  C  CD  . GLN A 1 92  ? 11.654  5.349   10.858  1.00 7.67   ? 92  GLN A CD  1 
ATOM   828  O  OE1 . GLN A 1 92  ? 11.047  4.406   11.382  1.00 8.09   ? 92  GLN A OE1 1 
ATOM   829  N  NE2 . GLN A 1 92  ? 12.875  5.665   11.150  1.00 9.04   ? 92  GLN A NE2 1 
ATOM   830  N  N   . PHE A 1 93  ? 8.132   4.522   10.364  1.00 5.89   ? 93  PHE A N   1 
ATOM   831  C  CA  . PHE A 1 93  ? 8.248   3.214   10.973  1.00 6.01   ? 93  PHE A CA  1 
ATOM   832  C  C   . PHE A 1 93  ? 9.230   2.375   10.180  1.00 5.63   ? 93  PHE A C   1 
ATOM   833  O  O   . PHE A 1 93  ? 9.539   2.611   9.018   1.00 6.01   ? 93  PHE A O   1 
ATOM   834  C  CB  . PHE A 1 93  ? 6.903   2.503   11.168  1.00 6.44   ? 93  PHE A CB  1 
ATOM   835  C  CG  . PHE A 1 93  ? 6.196   2.037   9.940   1.00 6.16   ? 93  PHE A CG  1 
ATOM   836  C  CD1 . PHE A 1 93  ? 6.590   0.865   9.255   1.00 6.92   ? 93  PHE A CD1 1 
ATOM   837  C  CD2 . PHE A 1 93  ? 5.091   2.717   9.460   1.00 6.84   ? 93  PHE A CD2 1 
ATOM   838  C  CE1 . PHE A 1 93  ? 5.921   0.450   8.129   1.00 7.21   ? 93  PHE A CE1 1 
ATOM   839  C  CE2 . PHE A 1 93  ? 4.410   2.268   8.329   1.00 7.29   ? 93  PHE A CE2 1 
ATOM   840  C  CZ  . PHE A 1 93  ? 4.829   1.139   7.669   1.00 7.47   ? 93  PHE A CZ  1 
ATOM   841  N  N   . HIS A 1 94  ? 9.698   1.303   10.850  1.00 5.69   ? 94  HIS A N   1 
ATOM   842  C  CA  . HIS A 1 94  ? 10.633  0.368   10.275  1.00 5.74   ? 94  HIS A CA  1 
ATOM   843  C  C   . HIS A 1 94  ? 10.558  -0.917  11.082  1.00 5.40   ? 94  HIS A C   1 
ATOM   844  O  O   . HIS A 1 94  ? 9.862   -0.991  12.105  1.00 5.91   ? 94  HIS A O   1 
ATOM   845  C  CB  . HIS A 1 94  ? 12.055  0.914   10.261  1.00 5.86   ? 94  HIS A CB  1 
ATOM   846  C  CG  . HIS A 1 94  ? 12.586  1.149   11.649  1.00 5.74   ? 94  HIS A CG  1 
ATOM   847  N  ND1 . HIS A 1 94  ? 12.350  2.288   12.374  1.00 5.91   ? 94  HIS A ND1 1 
ATOM   848  C  CD2 . HIS A 1 94  ? 13.273  0.322   12.494  1.00 5.93   ? 94  HIS A CD2 1 
ATOM   849  C  CE1 . HIS A 1 94  ? 12.878  2.138   13.571  1.00 5.79   ? 94  HIS A CE1 1 
ATOM   850  N  NE2 . HIS A 1 94  ? 13.444  0.953   13.704  1.00 5.47   ? 94  HIS A NE2 1 
ATOM   851  N  N   . PHE A 1 95  ? 11.311  -1.937  10.648  1.00 5.61   ? 95  PHE A N   1 
ATOM   852  C  CA  . PHE A 1 95  ? 11.347  -3.214  11.303  1.00 5.59   ? 95  PHE A CA  1 
ATOM   853  C  C   . PHE A 1 95  ? 12.804  -3.651  11.522  1.00 5.67   ? 95  PHE A C   1 
ATOM   854  O  O   . PHE A 1 95  ? 13.725  -3.168  10.881  1.00 6.41   ? 95  PHE A O   1 
ATOM   855  C  CB  . PHE A 1 95  ? 10.632  -4.298  10.464  1.00 6.16   ? 95  PHE A CB  1 
ATOM   856  C  CG  . PHE A 1 95  ? 9.212   -4.006  10.111  1.00 5.95   ? 95  PHE A CG  1 
ATOM   857  C  CD1 . PHE A 1 95  ? 8.901   -3.145  9.065   1.00 6.82   ? 95  PHE A CD1 1 
ATOM   858  C  CD2 . PHE A 1 95  ? 8.157   -4.652  10.768  1.00 6.48   ? 95  PHE A CD2 1 
ATOM   859  C  CE1 . PHE A 1 95  ? 7.583   -2.930  8.713   1.00 7.90   ? 95  PHE A CE1 1 
ATOM   860  C  CE2 . PHE A 1 95  ? 6.846   -4.424  10.413  1.00 7.26   ? 95  PHE A CE2 1 
ATOM   861  C  CZ  . PHE A 1 95  ? 6.557   -3.544  9.369   1.00 7.27   ? 95  PHE A CZ  1 
ATOM   862  N  N   . HIS A 1 96  ? 12.912  -4.653  12.404  1.00 5.42   ? 96  HIS A N   1 
ATOM   863  C  CA  . HIS A 1 96  ? 14.101  -5.469  12.569  1.00 5.57   ? 96  HIS A CA  1 
ATOM   864  C  C   . HIS A 1 96  ? 13.660  -6.914  12.424  1.00 5.55   ? 96  HIS A C   1 
ATOM   865  O  O   . HIS A 1 96  ? 12.572  -7.259  12.882  1.00 5.97   ? 96  HIS A O   1 
ATOM   866  C  CB  . HIS A 1 96  ? 14.740  -5.267  13.985  1.00 6.11   ? 96  HIS A CB  1 
ATOM   867  C  CG  . HIS A 1 96  ? 15.036  -3.838  14.238  1.00 6.06   ? 96  HIS A CG  1 
ATOM   868  N  ND1 . HIS A 1 96  ? 16.251  -3.273  14.091  1.00 6.53   ? 96  HIS A ND1 1 
ATOM   869  C  CD2 . HIS A 1 96  ? 14.234  -2.798  14.646  1.00 5.73   ? 96  HIS A CD2 1 
ATOM   870  C  CE1 . HIS A 1 96  ? 16.183  -1.968  14.383  1.00 6.56   ? 96  HIS A CE1 1 
ATOM   871  N  NE2 . HIS A 1 96  ? 14.966  -1.644  14.721  1.00 5.63   ? 96  HIS A NE2 1 
ATOM   872  N  N   . TRP A 1 97  ? 14.494  -7.740  11.796  1.00 5.84   ? 97  TRP A N   1 
ATOM   873  C  CA  . TRP A 1 97  ? 14.111  -9.116  11.575  1.00 5.84   ? 97  TRP A CA  1 
ATOM   874  C  C   . TRP A 1 97  ? 15.325  -10.008 11.438  1.00 6.17   ? 97  TRP A C   1 
ATOM   875  O  O   . TRP A 1 97  ? 16.468  -9.558  11.371  1.00 6.41   ? 97  TRP A O   1 
ATOM   876  C  CB  . TRP A 1 97  ? 13.216  -9.238  10.309  1.00 6.41   ? 97  TRP A CB  1 
ATOM   877  C  CG  . TRP A 1 97  ? 13.874  -8.807  9.056   1.00 6.23   ? 97  TRP A CG  1 
ATOM   878  C  CD1 . TRP A 1 97  ? 14.589  -9.614  8.192   1.00 7.18   ? 97  TRP A CD1 1 
ATOM   879  C  CD2 . TRP A 1 97  ? 13.927  -7.482  8.514   1.00 6.30   ? 97  TRP A CD2 1 
ATOM   880  N  NE1 . TRP A 1 97  ? 15.041  -8.866  7.152   1.00 7.42   ? 97  TRP A NE1 1 
ATOM   881  C  CE2 . TRP A 1 97  ? 14.677  -7.546  7.321   1.00 6.60   ? 97  TRP A CE2 1 
ATOM   882  C  CE3 . TRP A 1 97  ? 13.438  -6.253  8.918   1.00 6.37   ? 97  TRP A CE3 1 
ATOM   883  C  CZ2 . TRP A 1 97  ? 14.891  -6.448  6.501   1.00 7.01   ? 97  TRP A CZ2 1 
ATOM   884  C  CZ3 . TRP A 1 97  ? 13.652  -5.134  8.131   1.00 6.63   ? 97  TRP A CZ3 1 
ATOM   885  C  CH2 . TRP A 1 97  ? 14.370  -5.242  6.937   1.00 6.92   ? 97  TRP A CH2 1 
ATOM   886  N  N   . GLY A 1 98  ? 15.048  -11.308 11.444  1.00 6.55   ? 98  GLY A N   1 
ATOM   887  C  CA  . GLY A 1 98  ? 16.072  -12.312 11.467  1.00 7.11   ? 98  GLY A CA  1 
ATOM   888  C  C   . GLY A 1 98  ? 16.310  -13.003 10.145  1.00 7.15   ? 98  GLY A C   1 
ATOM   889  O  O   . GLY A 1 98  ? 15.577  -12.823 9.182   1.00 7.96   ? 98  GLY A O   1 
ATOM   890  N  N   . SER A 1 99  ? 17.352  -13.857 10.151  1.00 8.10   ? 99  SER A N   1 
ATOM   891  C  CA  . SER A 1 99  ? 17.565  -14.796 9.051   1.00 8.50   ? 99  SER A CA  1 
ATOM   892  C  C   . SER A 1 99  ? 16.679  -16.038 9.183   1.00 9.13   ? 99  SER A C   1 
ATOM   893  O  O   . SER A 1 99  ? 16.578  -16.800 8.217   1.00 11.97  ? 99  SER A O   1 
ATOM   894  C  CB  . SER A 1 99  ? 19.033  -15.160 9.003   1.00 9.79   ? 99  SER A CB  1 
ATOM   895  O  OG  . SER A 1 99  ? 19.476  -15.657 10.243  1.00 10.41  ? 99  SER A OG  1 
ATOM   896  N  N   . LEU A 1 100 ? 16.075  -16.238 10.348  1.00 8.84   ? 100 LEU A N   1 
ATOM   897  C  CA  . LEU A 1 100 ? 15.319  -17.435 10.764  1.00 10.39  ? 100 LEU A CA  1 
ATOM   898  C  C   . LEU A 1 100 ? 14.159  -16.931 11.549  1.00 9.38   ? 100 LEU A C   1 
ATOM   899  O  O   . LEU A 1 100 ? 14.270  -15.916 12.230  1.00 9.31   ? 100 LEU A O   1 
ATOM   900  C  CB  . LEU A 1 100 ? 16.174  -18.345 11.686  1.00 12.35  ? 100 LEU A CB  1 
ATOM   901  C  CG  . LEU A 1 100 ? 17.402  -18.852 11.033  1.00 14.05  ? 100 LEU A CG  1 
ATOM   902  C  CD1 . LEU A 1 100 ? 18.350  -19.490 12.059  1.00 18.87  ? 100 LEU A CD1 1 
ATOM   903  C  CD2 . LEU A 1 100 ? 17.098  -19.832 9.941   1.00 17.44  ? 100 LEU A CD2 1 
ATOM   904  N  N   . ASP A 1 101 ? 13.059  -17.679 11.544  1.00 9.81   ? 101 ASP A N   1 
ATOM   905  C  CA  . ASP A 1 101 ? 11.872  -17.261 12.254  1.00 9.30   ? 101 ASP A CA  1 
ATOM   906  C  C   . ASP A 1 101 ? 12.117  -17.138 13.776  1.00 9.70   ? 101 ASP A C   1 
ATOM   907  O  O   . ASP A 1 101 ? 11.416  -16.400 14.443  1.00 11.78  ? 101 ASP A O   1 
ATOM   908  C  CB  . ASP A 1 101 ? 10.690  -18.167 12.039  1.00 10.89  ? 101 ASP A CB  1 
ATOM   909  C  CG  . ASP A 1 101 ? 10.180  -18.216 10.621  1.00 11.78  ? 101 ASP A CG  1 
ATOM   910  O  OD1 . ASP A 1 101 ? 10.497  -17.343 9.796   1.00 11.44  ? 101 ASP A OD1 1 
ATOM   911  O  OD2 . ASP A 1 101 ? 9.399   -19.120 10.365  1.00 16.46  ? 101 ASP A OD2 1 
ATOM   912  N  N   . GLY A 1 102 ? 13.079  -17.879 14.305  1.00 11.04  ? 102 GLY A N   1 
ATOM   913  C  CA  . GLY A 1 102 ? 13.368  -17.878 15.710  1.00 12.66  ? 102 GLY A CA  1 
ATOM   914  C  C   . GLY A 1 102 ? 14.174  -16.720 16.268  1.00 10.46  ? 102 GLY A C   1 
ATOM   915  O  O   . GLY A 1 102 ? 14.500  -16.713 17.465  1.00 11.84  ? 102 GLY A O   1 
ATOM   916  N  N   A GLN A 1 103 ? 14.481  -15.726 15.446  0.50 8.30   ? 103 GLN A N   1 
ATOM   917  N  N   B GLN A 1 103 ? 14.453  -15.717 15.442  0.50 9.70   ? 103 GLN A N   1 
ATOM   918  C  CA  A GLN A 1 103 ? 15.235  -14.567 15.941  0.50 6.67   ? 103 GLN A CA  1 
ATOM   919  C  CA  B GLN A 1 103 ? 15.182  -14.530 15.904  0.50 9.87   ? 103 GLN A CA  1 
ATOM   920  C  C   A GLN A 1 103 ? 14.864  -13.390 15.047  0.50 7.01   ? 103 GLN A C   1 
ATOM   921  C  C   B GLN A 1 103 ? 14.769  -13.370 15.029  0.50 7.69   ? 103 GLN A C   1 
ATOM   922  O  O   A GLN A 1 103 ? 14.360  -13.579 13.957  0.50 7.75   ? 103 GLN A O   1 
ATOM   923  O  O   B GLN A 1 103 ? 14.184  -13.544 13.931  0.50 7.63   ? 103 GLN A O   1 
ATOM   924  C  CB  A GLN A 1 103 ? 16.701  -14.841 15.950  0.50 6.17   ? 103 GLN A CB  1 
ATOM   925  C  CB  B GLN A 1 103 ? 16.670  -14.659 15.834  0.50 13.05  ? 103 GLN A CB  1 
ATOM   926  C  CG  A GLN A 1 103 ? 17.246  -14.996 14.488  0.50 5.50   ? 103 GLN A CG  1 
ATOM   927  C  CG  B GLN A 1 103 ? 17.253  -15.802 16.494  0.50 20.57  ? 103 GLN A CG  1 
ATOM   928  C  CD  A GLN A 1 103 ? 18.560  -15.706 14.486  0.50 6.70   ? 103 GLN A CD  1 
ATOM   929  C  CD  B GLN A 1 103 ? 18.440  -16.310 15.705  0.50 25.10  ? 103 GLN A CD  1 
ATOM   930  O  OE1 A GLN A 1 103 ? 18.756  -16.716 15.219  0.50 10.84  ? 103 GLN A OE1 1 
ATOM   931  O  OE1 B GLN A 1 103 ? 18.304  -16.937 14.686  0.50 16.61  ? 103 GLN A OE1 1 
ATOM   932  N  NE2 A GLN A 1 103 ? 19.529  -15.169 13.787  0.50 6.91   ? 103 GLN A NE2 1 
ATOM   933  N  NE2 B GLN A 1 103 ? 19.573  -16.011 16.151  0.50 19.97  ? 103 GLN A NE2 1 
ATOM   934  N  N   . GLY A 1 104 ? 15.120  -12.185 15.527  1.00 6.66   ? 104 GLY A N   1 
ATOM   935  C  CA  . GLY A 1 104 ? 14.845  -10.979 14.737  1.00 6.74   ? 104 GLY A CA  1 
ATOM   936  C  C   . GLY A 1 104 ? 14.397  -9.808  15.603  1.00 5.95   ? 104 GLY A C   1 
ATOM   937  O  O   . GLY A 1 104 ? 14.671  -8.678  15.247  1.00 6.76   ? 104 GLY A O   1 
ATOM   938  N  N   . SER A 1 105 ? 13.703  -10.076 16.707  1.00 6.04   ? 105 SER A N   1 
ATOM   939  C  CA  . SER A 1 105 ? 13.302  -8.970  17.554  1.00 6.01   ? 105 SER A CA  1 
ATOM   940  C  C   . SER A 1 105 ? 14.523  -8.429  18.310  1.00 5.76   ? 105 SER A C   1 
ATOM   941  O  O   . SER A 1 105 ? 15.539  -9.092  18.509  1.00 6.58   ? 105 SER A O   1 
ATOM   942  C  CB  . SER A 1 105 ? 12.192  -9.333  18.497  1.00 6.16   ? 105 SER A CB  1 
ATOM   943  O  OG  . SER A 1 105 ? 12.538  -10.312 19.472  1.00 6.51   ? 105 SER A OG  1 
ATOM   944  N  N   . GLU A 1 106 ? 14.383  -7.179  18.719  1.00 5.52   ? 106 GLU A N   1 
ATOM   945  C  CA  . GLU A 1 106 ? 15.369  -6.490  19.523  1.00 5.72   ? 106 GLU A CA  1 
ATOM   946  C  C   . GLU A 1 106 ? 15.060  -6.678  21.000  1.00 5.49   ? 106 GLU A C   1 
ATOM   947  O  O   . GLU A 1 106 ? 15.842  -7.238  21.762  1.00 6.22   ? 106 GLU A O   1 
ATOM   948  C  CB  . GLU A 1 106 ? 15.438  -5.012  19.107  1.00 5.78   ? 106 GLU A CB  1 
ATOM   949  C  CG  . GLU A 1 106 ? 15.771  -4.866  17.636  1.00 6.65   ? 106 GLU A CG  1 
ATOM   950  C  CD  . GLU A 1 106 ? 16.560  -3.598  17.380  1.00 5.34   ? 106 GLU A CD  1 
ATOM   951  O  OE1 . GLU A 1 106 ? 15.976  -2.498  17.557  1.00 5.80   ? 106 GLU A OE1 1 
ATOM   952  O  OE2 . GLU A 1 106 ? 17.749  -3.711  17.022  1.00 6.81   ? 106 GLU A OE2 1 
ATOM   953  N  N   . HIS A 1 107 ? 13.877  -6.191  21.439  1.00 5.49   ? 107 HIS A N   1 
ATOM   954  C  CA  . HIS A 1 107 ? 13.427  -6.590  22.734  1.00 5.80   ? 107 HIS A CA  1 
ATOM   955  C  C   . HIS A 1 107 ? 13.110  -8.098  22.740  1.00 5.78   ? 107 HIS A C   1 
ATOM   956  O  O   . HIS A 1 107 ? 12.777  -8.692  21.712  1.00 5.96   ? 107 HIS A O   1 
ATOM   957  C  CB  . HIS A 1 107 ? 12.157  -5.795  23.121  1.00 5.72   ? 107 HIS A CB  1 
ATOM   958  C  CG  . HIS A 1 107 ? 12.469  -4.337  23.251  1.00 5.41   ? 107 HIS A CG  1 
ATOM   959  N  ND1 . HIS A 1 107 ? 12.401  -3.452  22.212  1.00 5.34   ? 107 HIS A ND1 1 
ATOM   960  C  CD2 . HIS A 1 107 ? 12.970  -3.614  24.310  1.00 5.74   ? 107 HIS A CD2 1 
ATOM   961  C  CE1 . HIS A 1 107 ? 12.830  -2.253  22.655  1.00 5.95   ? 107 HIS A CE1 1 
ATOM   962  N  NE2 . HIS A 1 107 ? 13.187  -2.320  23.922  1.00 5.74   ? 107 HIS A NE2 1 
ATOM   963  N  N   . THR A 1 108 ? 13.244  -8.668  23.929  1.00 6.15   ? 108 THR A N   1 
ATOM   964  C  CA  . THR A 1 108 ? 12.867  -10.046 24.188  1.00 6.51   ? 108 THR A CA  1 
ATOM   965  C  C   . THR A 1 108 ? 11.910  -10.040 25.398  1.00 6.47   ? 108 THR A C   1 
ATOM   966  O  O   . THR A 1 108 ? 11.899  -9.080  26.157  1.00 6.81   ? 108 THR A O   1 
ATOM   967  C  CB  . THR A 1 108 ? 14.093  -10.930 24.384  1.00 7.06   ? 108 THR A CB  1 
ATOM   968  O  OG1 . THR A 1 108 ? 14.926  -10.452 25.442  1.00 7.42   ? 108 THR A OG1 1 
ATOM   969  C  CG2 . THR A 1 108 ? 14.889  -11.022 23.109  1.00 7.57   ? 108 THR A CG2 1 
ATOM   970  N  N   . VAL A 1 109 ? 11.149  -11.116 25.518  1.00 7.17   ? 109 VAL A N   1 
ATOM   971  C  CA  . VAL A 1 109 ? 10.153  -11.234 26.580  1.00 7.27   ? 109 VAL A CA  1 
ATOM   972  C  C   . VAL A 1 109 ? 10.482  -12.492 27.348  1.00 7.59   ? 109 VAL A C   1 
ATOM   973  O  O   . VAL A 1 109 ? 10.310  -13.607 26.809  1.00 8.00   ? 109 VAL A O   1 
ATOM   974  C  CB  . VAL A 1 109 ? 8.711   -11.224 26.035  1.00 8.12   ? 109 VAL A CB  1 
ATOM   975  C  CG1 . VAL A 1 109 ? 7.727   -11.365 27.129  1.00 9.38   ? 109 VAL A CG1 1 
ATOM   976  C  CG2 . VAL A 1 109 ? 8.441   -9.969  25.211  1.00 8.82   ? 109 VAL A CG2 1 
ATOM   977  N  N   . ASP A 1 110 ? 10.988  -12.378 28.565  1.00 8.11   ? 110 ASP A N   1 
ATOM   978  C  CA  . ASP A 1 110 ? 11.490  -13.572 29.279  1.00 9.60   ? 110 ASP A CA  1 
ATOM   979  C  C   . ASP A 1 110 ? 12.420  -14.383 28.381  1.00 9.42   ? 110 ASP A C   1 
ATOM   980  O  O   . ASP A 1 110 ? 12.358  -15.624 28.351  1.00 10.55  ? 110 ASP A O   1 
ATOM   981  C  CB  . ASP A 1 110 ? 10.292  -14.416 29.773  1.00 10.95  ? 110 ASP A CB  1 
ATOM   982  C  CG  . ASP A 1 110 ? 9.501   -13.637 30.788  1.00 11.53  ? 110 ASP A CG  1 
ATOM   983  O  OD1 . ASP A 1 110 ? 10.030  -12.752 31.495  1.00 12.17  ? 110 ASP A OD1 1 
ATOM   984  O  OD2 . ASP A 1 110 ? 8.301   -13.928 30.898  1.00 13.76  ? 110 ASP A OD2 1 
ATOM   985  N  N   . LYS A 1 111 ? 13.302  -13.659 27.682  1.00 8.46   ? 111 LYS A N   1 
ATOM   986  C  CA  . LYS A 1 111 ? 14.312  -14.204 26.783  1.00 9.08   ? 111 LYS A CA  1 
ATOM   987  C  C   . LYS A 1 111 ? 13.741  -14.696 25.448  1.00 8.53   ? 111 LYS A C   1 
ATOM   988  O  O   . LYS A 1 111 ? 14.530  -15.057 24.568  1.00 10.53  ? 111 LYS A O   1 
ATOM   989  C  CB  . LYS A 1 111 ? 15.260  -15.229 27.422  1.00 11.56  ? 111 LYS A CB  1 
ATOM   990  C  CG  . LYS A 1 111 ? 15.984  -14.649 28.661  1.00 14.80  ? 111 LYS A CG  1 
ATOM   991  C  CD  . LYS A 1 111 ? 16.901  -13.475 28.377  1.00 16.90  ? 111 LYS A CD  1 
ATOM   992  C  CE  . LYS A 1 111 ? 17.592  -12.775 29.585  1.00 18.64  ? 111 LYS A CE  1 
ATOM   993  N  NZ  . LYS A 1 111 ? 18.837  -13.568 29.824  1.00 18.71  ? 111 LYS A NZ  1 
ATOM   994  N  N   . LYS A 1 112 ? 12.434  -14.700 25.262  1.00 8.46   ? 112 LYS A N   1 
ATOM   995  C  CA  . LYS A 1 112 ? 11.869  -15.084 23.984  1.00 8.73   ? 112 LYS A CA  1 
ATOM   996  C  C   . LYS A 1 112 ? 12.195  -14.049 22.919  1.00 7.72   ? 112 LYS A C   1 
ATOM   997  O  O   . LYS A 1 112 ? 11.945  -12.866 23.121  1.00 7.57   ? 112 LYS A O   1 
ATOM   998  C  CB  . LYS A 1 112 ? 10.315  -15.159 24.073  1.00 9.86   ? 112 LYS A CB  1 
ATOM   999  C  CG  . LYS A 1 112 ? 9.646   -15.554 22.770  1.00 10.82  ? 112 LYS A CG  1 
ATOM   1000 C  CD  . LYS A 1 112 ? 8.101   -15.476 22.849  1.00 12.38  ? 112 LYS A CD  1 
ATOM   1001 C  CE  . LYS A 1 112 ? 7.509   -15.740 21.523  1.00 12.62  ? 112 LYS A CE  1 
ATOM   1002 N  NZ  . LYS A 1 112 ? 7.658   -17.099 21.093  1.00 12.93  ? 112 LYS A NZ  1 
ATOM   1003 N  N   A LYS A 1 113 ? 12.544  -14.573 21.765  0.50 6.98   ? 113 LYS A N   1 
ATOM   1004 N  N   B LYS A 1 113 ? 12.925  -14.423 21.849  0.50 7.37   ? 113 LYS A N   1 
ATOM   1005 C  CA  A LYS A 1 113 ? 12.777  -13.809 20.599  0.50 6.82   ? 113 LYS A CA  1 
ATOM   1006 C  CA  B LYS A 1 113 ? 13.113  -13.617 20.615  0.50 7.95   ? 113 LYS A CA  1 
ATOM   1007 C  C   A LYS A 1 113 ? 11.617  -13.990 19.696  0.50 6.91   ? 113 LYS A C   1 
ATOM   1008 C  C   B LYS A 1 113 ? 11.947  -13.915 19.595  0.50 7.06   ? 113 LYS A C   1 
ATOM   1009 O  O   A LYS A 1 113 ? 11.172  -15.121 19.433  0.50 7.94   ? 113 LYS A O   1 
ATOM   1010 O  O   B LYS A 1 113 ? 11.664  -15.088 19.256  0.50 7.94   ? 113 LYS A O   1 
ATOM   1011 C  CB  A LYS A 1 113 ? 14.067  -14.237 19.906  0.50 7.19   ? 113 LYS A CB  1 
ATOM   1012 C  CB  B LYS A 1 113 ? 14.410  -14.015 19.941  0.50 8.25   ? 113 LYS A CB  1 
ATOM   1013 C  CG  A LYS A 1 113 ? 15.315  -13.875 20.667  0.50 8.14   ? 113 LYS A CG  1 
ATOM   1014 C  CG  B LYS A 1 113 ? 15.676  -13.657 20.681  0.50 9.62   ? 113 LYS A CG  1 
ATOM   1015 C  CD  A LYS A 1 113 ? 16.665  -14.389 20.163  0.50 9.82   ? 113 LYS A CD  1 
ATOM   1016 C  CD  B LYS A 1 113 ? 16.755  -14.367 19.925  0.50 11.07  ? 113 LYS A CD  1 
ATOM   1017 C  CE  A LYS A 1 113 ? 17.831  -13.730 20.912  0.50 11.76  ? 113 LYS A CE  1 
ATOM   1018 C  CE  B LYS A 1 113 ? 18.077  -13.926 20.476  0.50 10.32  ? 113 LYS A CE  1 
ATOM   1019 N  NZ  A LYS A 1 113 ? 19.068  -14.462 20.720  0.50 16.19  ? 113 LYS A NZ  1 
ATOM   1020 N  NZ  B LYS A 1 113 ? 18.387  -14.564 21.749  0.50 10.62  ? 113 LYS A NZ  1 
ATOM   1021 N  N   . TYR A 1 114 ? 11.223  -12.875 19.111  1.00 7.03   ? 114 TYR A N   1 
ATOM   1022 C  CA  . TYR A 1 114 ? 10.237  -12.937 18.062  1.00 7.22   ? 114 TYR A CA  1 
ATOM   1023 C  C   . TYR A 1 114 ? 10.918  -12.889 16.688  1.00 6.77   ? 114 TYR A C   1 
ATOM   1024 O  O   . TYR A 1 114 ? 12.096  -12.574 16.566  1.00 7.21   ? 114 TYR A O   1 
ATOM   1025 C  CB  . TYR A 1 114 ? 9.183   -11.832 18.229  1.00 6.70   ? 114 TYR A CB  1 
ATOM   1026 C  CG  . TYR A 1 114 ? 8.256   -12.067 19.379  1.00 6.95   ? 114 TYR A CG  1 
ATOM   1027 C  CD1 . TYR A 1 114 ? 8.534   -11.645 20.666  1.00 8.97   ? 114 TYR A CD1 1 
ATOM   1028 C  CD2 . TYR A 1 114 ? 7.023   -12.698 19.150  1.00 7.97   ? 114 TYR A CD2 1 
ATOM   1029 C  CE1 . TYR A 1 114 ? 7.601   -11.826 21.697  1.00 10.47  ? 114 TYR A CE1 1 
ATOM   1030 C  CE2 . TYR A 1 114 ? 6.088   -12.878 20.141  1.00 10.25  ? 114 TYR A CE2 1 
ATOM   1031 C  CZ  . TYR A 1 114 ? 6.389   -12.407 21.444  1.00 11.23  ? 114 TYR A CZ  1 
ATOM   1032 O  OH  . TYR A 1 114 ? 5.582   -12.508 22.546  1.00 16.28  ? 114 TYR A OH  1 
ATOM   1033 N  N   . ALA A 1 115 ? 10.150  -13.205 15.653  1.00 7.17   ? 115 ALA A N   1 
ATOM   1034 C  CA  . ALA A 1 115 ? 10.662  -13.199 14.288  1.00 7.01   ? 115 ALA A CA  1 
ATOM   1035 C  C   . ALA A 1 115 ? 11.047  -11.812 13.803  1.00 6.75   ? 115 ALA A C   1 
ATOM   1036 O  O   . ALA A 1 115 ? 11.908  -11.660 12.916  1.00 7.07   ? 115 ALA A O   1 
ATOM   1037 C  CB  . ALA A 1 115 ? 9.635   -13.821 13.356  1.00 8.40   ? 115 ALA A CB  1 
ATOM   1038 N  N   . ALA A 1 116 ? 10.373  -10.784 14.335  1.00 6.74   ? 116 ALA A N   1 
ATOM   1039 C  CA  . ALA A 1 116 ? 10.653  -9.429  13.885  1.00 6.04   ? 116 ALA A CA  1 
ATOM   1040 C  C   . ALA A 1 116 ? 10.060  -8.488  14.936  1.00 5.57   ? 116 ALA A C   1 
ATOM   1041 O  O   . ALA A 1 116 ? 9.322   -8.900  15.828  1.00 6.24   ? 116 ALA A O   1 
ATOM   1042 C  CB  . ALA A 1 116 ? 10.132  -9.172  12.489  1.00 6.87   ? 116 ALA A CB  1 
ATOM   1043 N  N   . GLU A 1 117 ? 10.383  -7.207  14.760  1.00 5.68   ? 117 GLU A N   1 
ATOM   1044 C  CA  . GLU A 1 117 ? 9.862   -6.169  15.678  1.00 5.51   ? 117 GLU A CA  1 
ATOM   1045 C  C   . GLU A 1 117 ? 9.660   -4.922  14.814  1.00 5.35   ? 117 GLU A C   1 
ATOM   1046 O  O   . GLU A 1 117 ? 10.578  -4.493  14.102  1.00 6.15   ? 117 GLU A O   1 
ATOM   1047 C  CB  . GLU A 1 117 ? 10.842  -5.934  16.827  1.00 5.80   ? 117 GLU A CB  1 
ATOM   1048 C  CG  . GLU A 1 117 ? 10.297  -5.021  17.889  1.00 5.67   ? 117 GLU A CG  1 
ATOM   1049 C  CD  . GLU A 1 117 ? 11.243  -4.936  19.107  1.00 5.28   ? 117 GLU A CD  1 
ATOM   1050 O  OE1 . GLU A 1 117 ? 11.938  -5.930  19.381  1.00 6.10   ? 117 GLU A OE1 1 
ATOM   1051 O  OE2 . GLU A 1 117 ? 11.253  -3.861  19.762  1.00 6.16   ? 117 GLU A OE2 1 
ATOM   1052 N  N   . LEU A 1 118 ? 8.467   -4.360  14.924  1.00 5.48   ? 118 LEU A N   1 
ATOM   1053 C  CA  . LEU A 1 118 ? 8.072   -3.118  14.277  1.00 4.92   ? 118 LEU A CA  1 
ATOM   1054 C  C   . LEU A 1 118 ? 8.295   -1.980  15.269  1.00 4.94   ? 118 LEU A C   1 
ATOM   1055 O  O   . LEU A 1 118 ? 7.875   -2.055  16.413  1.00 5.30   ? 118 LEU A O   1 
ATOM   1056 C  CB  . LEU A 1 118 ? 6.582   -3.230  13.930  1.00 5.85   ? 118 LEU A CB  1 
ATOM   1057 C  CG  . LEU A 1 118 ? 5.820   -1.948  13.568  1.00 6.40   ? 118 LEU A CG  1 
ATOM   1058 C  CD1 . LEU A 1 118 ? 6.380   -1.224  12.377  1.00 6.66   ? 118 LEU A CD1 1 
ATOM   1059 C  CD2 . LEU A 1 118 ? 4.391   -2.319  13.318  1.00 7.32   ? 118 LEU A CD2 1 
ATOM   1060 N  N   . HIS A 1 119 ? 8.917   -0.895  14.777  1.00 5.01   ? 119 HIS A N   1 
ATOM   1061 C  CA  . HIS A 1 119 ? 9.143   0.327   15.530  1.00 5.14   ? 119 HIS A CA  1 
ATOM   1062 C  C   . HIS A 1 119 ? 8.476   1.484   14.836  1.00 5.00   ? 119 HIS A C   1 
ATOM   1063 O  O   . HIS A 1 119 ? 8.840   1.798   13.680  1.00 5.92   ? 119 HIS A O   1 
ATOM   1064 C  CB  . HIS A 1 119 ? 10.642  0.596   15.623  1.00 5.41   ? 119 HIS A CB  1 
ATOM   1065 C  CG  . HIS A 1 119 ? 11.356  -0.384  16.523  1.00 5.09   ? 119 HIS A CG  1 
ATOM   1066 N  ND1 . HIS A 1 119 ? 12.719  -0.575  16.514  1.00 5.12   ? 119 HIS A ND1 1 
ATOM   1067 C  CD2 . HIS A 1 119 ? 10.814  -1.202  17.469  1.00 5.51   ? 119 HIS A CD2 1 
ATOM   1068 C  CE1 . HIS A 1 119 ? 12.968  -1.493  17.439  1.00 5.12   ? 119 HIS A CE1 1 
ATOM   1069 N  NE2 . HIS A 1 119 ? 11.847  -1.863  18.039  1.00 5.64   ? 119 HIS A NE2 1 
ATOM   1070 N  N   . LEU A 1 120 ? 7.520   2.111   15.509  1.00 5.07   ? 120 LEU A N   1 
ATOM   1071 C  CA  . LEU A 1 120 ? 6.882   3.325   15.058  1.00 5.53   ? 120 LEU A CA  1 
ATOM   1072 C  C   . LEU A 1 120 ? 7.468   4.482   15.849  1.00 5.12   ? 120 LEU A C   1 
ATOM   1073 O  O   . LEU A 1 120 ? 7.340   4.498   17.067  1.00 5.36   ? 120 LEU A O   1 
ATOM   1074 C  CB  . LEU A 1 120 ? 5.363   3.256   15.201  1.00 5.77   ? 120 LEU A CB  1 
ATOM   1075 C  CG  . LEU A 1 120 ? 4.670   2.178   14.374  1.00 6.37   ? 120 LEU A CG  1 
ATOM   1076 C  CD1 . LEU A 1 120 ? 3.932   1.211   15.266  1.00 9.75   ? 120 LEU A CD1 1 
ATOM   1077 C  CD2 . LEU A 1 120 ? 3.794   2.805   13.340  1.00 8.11   ? 120 LEU A CD2 1 
ATOM   1078 N  N   . ALA A 1 121 ? 8.170   5.379   15.177  1.00 5.64   ? 121 ALA A N   1 
ATOM   1079 C  CA  . ALA A 1 121 ? 8.932   6.434   15.828  1.00 5.67   ? 121 ALA A CA  1 
ATOM   1080 C  C   . ALA A 1 121 ? 8.175   7.767   15.787  1.00 5.66   ? 121 ALA A C   1 
ATOM   1081 O  O   . ALA A 1 121 ? 7.601   8.133   14.769  1.00 6.32   ? 121 ALA A O   1 
ATOM   1082 C  CB  . ALA A 1 121 ? 10.303  6.566   15.178  1.00 6.69   ? 121 ALA A CB  1 
ATOM   1083 N  N   . HIS A 1 122 ? 8.262   8.479   16.911  1.00 5.82   ? 122 HIS A N   1 
ATOM   1084 C  CA  . HIS A 1 122 ? 7.525   9.736   17.104  1.00 5.96   ? 122 HIS A CA  1 
ATOM   1085 C  C   . HIS A 1 122 ? 8.398   10.715  17.818  1.00 6.06   ? 122 HIS A C   1 
ATOM   1086 O  O   . HIS A 1 122 ? 9.110   10.324  18.758  1.00 7.22   ? 122 HIS A O   1 
ATOM   1087 C  CB  . HIS A 1 122 ? 6.280   9.485   17.984  1.00 6.47   ? 122 HIS A CB  1 
ATOM   1088 C  CG  . HIS A 1 122 ? 5.421   8.315   17.640  1.00 6.23   ? 122 HIS A CG  1 
ATOM   1089 N  ND1 . HIS A 1 122 ? 5.821   7.026   17.876  1.00 6.56   ? 122 HIS A ND1 1 
ATOM   1090 C  CD2 . HIS A 1 122 ? 4.186   8.211   17.069  1.00 6.94   ? 122 HIS A CD2 1 
ATOM   1091 C  CE1 . HIS A 1 122 ? 4.823   6.216   17.478  1.00 6.49   ? 122 HIS A CE1 1 
ATOM   1092 N  NE2 . HIS A 1 122 ? 3.814   6.896   16.987  1.00 7.00   ? 122 HIS A NE2 1 
ATOM   1093 N  N   . TRP A 1 123 ? 8.363   11.999  17.454  1.00 6.48   ? 123 TRP A N   1 
ATOM   1094 C  CA  . TRP A 1 123 ? 9.141   13.014  18.139  1.00 6.90   ? 123 TRP A CA  1 
ATOM   1095 C  C   . TRP A 1 123 ? 8.257   13.945  18.941  1.00 6.73   ? 123 TRP A C   1 
ATOM   1096 O  O   . TRP A 1 123 ? 7.126   14.282  18.554  1.00 6.98   ? 123 TRP A O   1 
ATOM   1097 C  CB  . TRP A 1 123 ? 10.077  13.771  17.173  1.00 8.10   ? 123 TRP A CB  1 
ATOM   1098 C  CG  . TRP A 1 123 ? 9.467   14.474  16.034  1.00 8.09   ? 123 TRP A CG  1 
ATOM   1099 C  CD1 . TRP A 1 123 ? 9.351   13.969  14.783  1.00 8.85   ? 123 TRP A CD1 1 
ATOM   1100 C  CD2 . TRP A 1 123 ? 8.977   15.822  15.979  1.00 8.60   ? 123 TRP A CD2 1 
ATOM   1101 N  NE1 . TRP A 1 123 ? 8.785   14.872  13.940  1.00 9.83   ? 123 TRP A NE1 1 
ATOM   1102 C  CE2 . TRP A 1 123 ? 8.523   16.030  14.633  1.00 9.74   ? 123 TRP A CE2 1 
ATOM   1103 C  CE3 . TRP A 1 123 ? 8.908   16.894  16.885  1.00 10.93  ? 123 TRP A CE3 1 
ATOM   1104 C  CZ2 . TRP A 1 123 ? 8.000   17.221  14.195  1.00 11.33  ? 123 TRP A CZ2 1 
ATOM   1105 C  CZ3 . TRP A 1 123 ? 8.346   18.097  16.408  1.00 12.69  ? 123 TRP A CZ3 1 
ATOM   1106 C  CH2 . TRP A 1 123 ? 7.945   18.245  15.104  1.00 13.35  ? 123 TRP A CH2 1 
ATOM   1107 N  N   . ASN A 1 124 ? 8.812   14.397  20.059  1.00 6.86   ? 124 ASN A N   1 
ATOM   1108 C  CA  . ASN A 1 124 ? 8.071   15.234  21.021  1.00 7.52   ? 124 ASN A CA  1 
ATOM   1109 C  C   . ASN A 1 124 ? 7.942   16.647  20.435  1.00 7.51   ? 124 ASN A C   1 
ATOM   1110 O  O   . ASN A 1 124 ? 8.959   17.329  20.222  1.00 7.96   ? 124 ASN A O   1 
ATOM   1111 C  CB  . ASN A 1 124 ? 8.877   15.263  22.304  1.00 7.75   ? 124 ASN A CB  1 
ATOM   1112 C  CG  . ASN A 1 124 ? 8.162   15.890  23.439  1.00 8.40   ? 124 ASN A CG  1 
ATOM   1113 O  OD1 . ASN A 1 124 ? 7.312   16.784  23.230  1.00 9.34   ? 124 ASN A OD1 1 
ATOM   1114 N  ND2 . ASN A 1 124 ? 8.484   15.480  24.649  1.00 9.54   ? 124 ASN A ND2 1 
ATOM   1115 N  N   . THR A 1 125 ? 6.711   17.033  20.139  1.00 8.09   ? 125 THR A N   1 
ATOM   1116 C  CA  . THR A 1 125 ? 6.450   18.312  19.487  1.00 9.46   ? 125 THR A CA  1 
ATOM   1117 C  C   . THR A 1 125 ? 6.855   19.495  20.361  1.00 8.83   ? 125 THR A C   1 
ATOM   1118 O  O   . THR A 1 125 ? 7.156   20.576  19.856  1.00 10.16  ? 125 THR A O   1 
ATOM   1119 C  CB  . THR A 1 125 ? 4.969   18.457  19.089  1.00 12.04  ? 125 THR A CB  1 
ATOM   1120 O  OG1 . THR A 1 125 ? 4.145   18.366  20.258  1.00 15.33  ? 125 THR A OG1 1 
ATOM   1121 C  CG2 . THR A 1 125 ? 4.572   17.365  18.106  1.00 13.08  ? 125 THR A CG2 1 
ATOM   1122 N  N   A LYS A 1 126 ? 7.407   19.113  21.569  0.50 6.88   ? 127 LYS A N   1 
ATOM   1123 N  N   B LYS A 1 126 ? 7.456   19.402  21.758  0.50 7.27   ? 127 LYS A N   1 
ATOM   1124 C  CA  A LYS A 1 126 ? 7.640   20.413  22.185  0.50 7.16   ? 127 LYS A CA  1 
ATOM   1125 C  CA  B LYS A 1 126 ? 7.961   20.545  22.512  0.50 8.13   ? 127 LYS A CA  1 
ATOM   1126 C  C   A LYS A 1 126 ? 9.013   20.974  21.796  0.50 7.54   ? 127 LYS A C   1 
ATOM   1127 C  C   B LYS A 1 126 ? 9.311   20.961  21.995  0.50 8.44   ? 127 LYS A C   1 
ATOM   1128 O  O   A LYS A 1 126 ? 9.312   22.148  22.056  0.50 8.75   ? 127 LYS A O   1 
ATOM   1129 O  O   B LYS A 1 126 ? 9.831   22.028  22.358  0.50 8.27   ? 127 LYS A O   1 
ATOM   1130 C  CB  A LYS A 1 126 ? 7.507   20.316  23.712  0.50 8.60   ? 127 LYS A CB  1 
ATOM   1131 C  CB  B LYS A 1 126 ? 7.977   20.229  23.997  0.50 8.45   ? 127 LYS A CB  1 
ATOM   1132 C  CG  A LYS A 1 126 ? 8.625   19.571  24.334  0.50 8.81   ? 127 LYS A CG  1 
ATOM   1133 C  CG  B LYS A 1 126 ? 9.100   19.327  24.426  0.50 9.24   ? 127 LYS A CG  1 
ATOM   1134 C  CD  A LYS A 1 126 ? 8.260   19.184  25.735  0.50 13.41  ? 127 LYS A CD  1 
ATOM   1135 C  CD  B LYS A 1 126 ? 8.885   18.949  25.879  0.50 10.32  ? 127 LYS A CD  1 
ATOM   1136 C  CE  A LYS A 1 126 ? 9.408   18.524  26.482  0.50 14.81  ? 127 LYS A CE  1 
ATOM   1137 C  CE  B LYS A 1 126 ? 9.156   20.162  26.721  0.50 13.55  ? 127 LYS A CE  1 
ATOM   1138 N  NZ  A LYS A 1 126 ? 8.950   17.974  27.782  0.50 17.58  ? 127 LYS A NZ  1 
ATOM   1139 N  NZ  B LYS A 1 126 ? 8.909   19.624  28.078  0.50 15.89  ? 127 LYS A NZ  1 
ATOM   1140 N  N   . TYR A 1 127 ? 9.883   20.117  21.150  1.00 8.49   ? 128 TYR A N   1 
ATOM   1141 C  CA  . TYR A 1 127 ? 11.194  20.414  20.664  1.00 8.85   ? 128 TYR A CA  1 
ATOM   1142 C  C   . TYR A 1 127 ? 11.188  20.900  19.204  1.00 8.97   ? 128 TYR A C   1 
ATOM   1143 O  O   . TYR A 1 127 ? 12.274  21.158  18.681  1.00 10.02  ? 128 TYR A O   1 
ATOM   1144 C  CB  . TYR A 1 127 ? 12.159  19.270  20.911  1.00 8.95   ? 128 TYR A CB  1 
ATOM   1145 C  CG  . TYR A 1 127 ? 12.252  18.912  22.353  1.00 8.35   ? 128 TYR A CG  1 
ATOM   1146 C  CD1 . TYR A 1 127 ? 12.683  19.834  23.308  1.00 9.59   ? 128 TYR A CD1 1 
ATOM   1147 C  CD2 . TYR A 1 127 ? 11.912  17.630  22.799  1.00 8.48   ? 128 TYR A CD2 1 
ATOM   1148 C  CE1 . TYR A 1 127 ? 12.731  19.515  24.644  1.00 9.71   ? 128 TYR A CE1 1 
ATOM   1149 C  CE2 . TYR A 1 127 ? 11.981  17.287  24.120  1.00 9.04   ? 128 TYR A CE2 1 
ATOM   1150 C  CZ  . TYR A 1 127 ? 12.355  18.245  25.047  1.00 9.74   ? 128 TYR A CZ  1 
ATOM   1151 O  OH  . TYR A 1 127 ? 12.474  17.962  26.396  1.00 11.38  ? 128 TYR A OH  1 
ATOM   1152 N  N   . GLY A 1 128 ? 10.044  21.004  18.573  1.00 9.00   ? 129 GLY A N   1 
ATOM   1153 C  CA  . GLY A 1 128 ? 9.960   21.721  17.288  1.00 9.75   ? 129 GLY A CA  1 
ATOM   1154 C  C   . GLY A 1 128 ? 10.346  20.928  16.062  1.00 10.09  ? 129 GLY A C   1 
ATOM   1155 O  O   . GLY A 1 128 ? 9.704   21.095  15.029  1.00 12.29  ? 129 GLY A O   1 
ATOM   1156 N  N   A ASP A 1 129 ? 11.610  20.299  16.110  0.50 9.46   ? 130 ASP A N   1 
ATOM   1157 N  N   B ASP A 1 129 ? 11.164  19.949  16.131  0.50 7.77   ? 130 ASP A N   1 
ATOM   1158 C  CA  A ASP A 1 129 ? 12.071  19.397  15.010  0.50 9.14   ? 130 ASP A CA  1 
ATOM   1159 C  CA  B ASP A 1 129 ? 11.432  19.097  15.007  0.50 7.94   ? 130 ASP A CA  1 
ATOM   1160 C  C   A ASP A 1 129 ? 12.409  18.006  15.519  0.50 11.60  ? 130 ASP A C   1 
ATOM   1161 C  C   B ASP A 1 129 ? 12.456  17.995  15.551  0.50 10.83  ? 130 ASP A C   1 
ATOM   1162 O  O   A ASP A 1 129 ? 12.518  17.819  16.684  0.50 7.54   ? 130 ASP A O   1 
ATOM   1163 O  O   B ASP A 1 129 ? 13.203  18.023  16.695  0.50 7.74   ? 130 ASP A O   1 
ATOM   1164 C  CB  A ASP A 1 129 ? 12.988  20.053  13.957  0.50 8.68   ? 130 ASP A CB  1 
ATOM   1165 C  CB  B ASP A 1 129 ? 12.105  19.809  13.836  0.50 9.09   ? 130 ASP A CB  1 
ATOM   1166 C  CG  A ASP A 1 129 ? 14.386  20.417  14.469  0.50 8.75   ? 130 ASP A CG  1 
ATOM   1167 C  CG  B ASP A 1 129 ? 13.531  20.221  14.114  0.50 8.35   ? 130 ASP A CG  1 
ATOM   1168 O  OD1 A ASP A 1 129 ? 15.182  19.509  14.712  0.50 10.79  ? 130 ASP A OD1 1 
ATOM   1169 O  OD1 B ASP A 1 129 ? 14.027  19.932  15.217  0.50 10.64  ? 130 ASP A OD1 1 
ATOM   1170 O  OD2 A ASP A 1 129 ? 14.717  21.608  14.575  0.50 12.85  ? 130 ASP A OD2 1 
ATOM   1171 O  OD2 B ASP A 1 129 ? 14.104  20.873  13.221  0.50 11.81  ? 130 ASP A OD2 1 
ATOM   1172 N  N   . LEU A 1 130 ? 12.544  17.025  14.650  1.00 9.89   ? 131 LEU A N   1 
ATOM   1173 C  CA  . LEU A 1 130 ? 13.127  15.742  14.981  1.00 9.13   ? 131 LEU A CA  1 
ATOM   1174 C  C   . LEU A 1 130 ? 14.584  15.883  15.441  1.00 8.78   ? 131 LEU A C   1 
ATOM   1175 O  O   . LEU A 1 130 ? 15.002  15.216  16.406  1.00 9.61   ? 131 LEU A O   1 
ATOM   1176 C  CB  . LEU A 1 130 ? 13.053  14.856  13.787  1.00 8.72   ? 131 LEU A CB  1 
ATOM   1177 C  CG  . LEU A 1 130 ? 13.804  13.520  13.866  1.00 8.41   ? 131 LEU A CG  1 
ATOM   1178 C  CD1 . LEU A 1 130 ? 13.288  12.672  15.038  1.00 9.47   ? 131 LEU A CD1 1 
ATOM   1179 C  CD2 . LEU A 1 130 ? 13.612  12.805  12.532  1.00 10.45  ? 131 LEU A CD2 1 
ATOM   1180 N  N   . GLY A 1 131 ? 15.398  16.666  14.742  1.00 10.54  ? 132 GLY A N   1 
ATOM   1181 C  CA  . GLY A 1 131 ? 16.792  16.766  15.075  1.00 12.39  ? 132 GLY A CA  1 
ATOM   1182 C  C   . GLY A 1 131 ? 17.003  17.328  16.459  1.00 10.98  ? 132 GLY A C   1 
ATOM   1183 O  O   . GLY A 1 131 ? 17.891  16.878  17.193  1.00 12.44  ? 132 GLY A O   1 
ATOM   1184 N  N   A LYS A 1 132 ? 16.210  18.355  16.815  0.50 10.70  ? 133 LYS A N   1 
ATOM   1185 N  N   B LYS A 1 132 ? 16.270  18.346  16.873  0.50 10.67  ? 133 LYS A N   1 
ATOM   1186 C  CA  A LYS A 1 132 ? 16.267  18.895  18.165  0.50 9.59   ? 133 LYS A CA  1 
ATOM   1187 C  CA  B LYS A 1 132 ? 16.449  18.826  18.209  0.50 11.26  ? 133 LYS A CA  1 
ATOM   1188 C  C   A LYS A 1 132 ? 15.848  17.834  19.221  0.50 9.07   ? 133 LYS A C   1 
ATOM   1189 C  C   B LYS A 1 132 ? 15.779  17.892  19.215  0.50 9.66   ? 133 LYS A C   1 
ATOM   1190 O  O   A LYS A 1 132 ? 16.577  17.540  20.285  0.50 8.67   ? 133 LYS A O   1 
ATOM   1191 O  O   B LYS A 1 132 ? 16.187  17.832  20.309  0.50 9.22   ? 133 LYS A O   1 
ATOM   1192 C  CB  A LYS A 1 132 ? 15.485  20.207  18.264  0.50 10.60  ? 133 LYS A CB  1 
ATOM   1193 C  CB  B LYS A 1 132 ? 15.746  20.147  18.358  0.50 10.67  ? 133 LYS A CB  1 
ATOM   1194 C  CG  A LYS A 1 132 ? 16.297  21.351  17.542  0.50 10.67  ? 133 LYS A CG  1 
ATOM   1195 C  CG  B LYS A 1 132 ? 15.868  20.719  19.732  0.50 13.52  ? 133 LYS A CG  1 
ATOM   1196 C  CD  A LYS A 1 132 ? 17.556  21.733  18.331  0.50 14.19  ? 133 LYS A CD  1 
ATOM   1197 C  CD  B LYS A 1 132 ? 17.257  21.219  19.919  0.50 20.54  ? 133 LYS A CD  1 
ATOM   1198 C  CE  A LYS A 1 132 ? 18.124  23.112  18.005  0.50 16.04  ? 133 LYS A CE  1 
ATOM   1199 C  CE  B LYS A 1 132 ? 17.312  22.699  19.473  0.50 21.40  ? 133 LYS A CE  1 
ATOM   1200 N  NZ  A LYS A 1 132 ? 19.387  23.437  18.734  0.50 19.35  ? 133 LYS A NZ  1 
ATOM   1201 N  NZ  B LYS A 1 132 ? 18.749  23.127  19.545  0.50 19.23  ? 133 LYS A NZ  1 
ATOM   1202 N  N   . ALA A 1 133 ? 14.698  17.192  18.885  1.00 8.54   ? 134 ALA A N   1 
ATOM   1203 C  CA  . ALA A 1 133 ? 14.160  16.185  19.797  1.00 8.36   ? 134 ALA A CA  1 
ATOM   1204 C  C   . ALA A 1 133 ? 15.158  15.107  20.109  1.00 7.97   ? 134 ALA A C   1 
ATOM   1205 O  O   . ALA A 1 133 ? 15.235  14.628  21.235  1.00 8.49   ? 134 ALA A O   1 
ATOM   1206 C  CB  . ALA A 1 133 ? 12.883  15.619  19.205  1.00 8.19   ? 134 ALA A CB  1 
ATOM   1207 N  N   . ALA A 1 134 ? 15.925  14.691  19.105  1.00 8.51   ? 135 ALA A N   1 
ATOM   1208 C  CA  . ALA A 1 134 ? 16.861  13.566  19.294  1.00 9.24   ? 135 ALA A CA  1 
ATOM   1209 C  C   . ALA A 1 134 ? 17.972  13.909  20.276  1.00 8.94   ? 135 ALA A C   1 
ATOM   1210 O  O   . ALA A 1 134 ? 18.665  12.977  20.693  1.00 9.79   ? 135 ALA A O   1 
ATOM   1211 C  CB  . ALA A 1 134 ? 17.416  13.159  17.958  1.00 11.67  ? 135 ALA A CB  1 
ATOM   1212 N  N   . GLN A 1 135 ? 18.164  15.172  20.612  1.00 9.59   ? 136 GLN A N   1 
ATOM   1213 C  CA  . GLN A 1 135 ? 19.162  15.608  21.585  1.00 10.25  ? 136 GLN A CA  1 
ATOM   1214 C  C   . GLN A 1 135 ? 18.589  15.704  22.982  1.00 9.46   ? 136 GLN A C   1 
ATOM   1215 O  O   . GLN A 1 135 ? 19.300  16.172  23.907  1.00 11.58  ? 136 GLN A O   1 
ATOM   1216 C  CB  . GLN A 1 135 ? 19.724  16.949  21.145  1.00 12.56  ? 136 GLN A CB  1 
ATOM   1217 C  CG  . GLN A 1 135 ? 20.489  16.783  19.815  1.00 15.05  ? 136 GLN A CG  1 
ATOM   1218 C  CD  . GLN A 1 135 ? 21.640  15.662  19.916  1.00 30.56  ? 136 GLN A CD  1 
ATOM   1219 O  OE1 . GLN A 1 135 ? 22.443  15.608  20.907  1.00 39.87  ? 136 GLN A OE1 1 
ATOM   1220 N  NE2 . GLN A 1 135 ? 21.745  14.787  18.886  1.00 39.11  ? 136 GLN A NE2 1 
ATOM   1221 N  N   . GLN A 1 136 ? 17.383  15.238  23.220  1.00 8.70   ? 137 GLN A N   1 
ATOM   1222 C  CA  . GLN A 1 136 ? 16.720  15.368  24.530  1.00 9.08   ? 137 GLN A CA  1 
ATOM   1223 C  C   . GLN A 1 136 ? 16.401  13.999  25.074  1.00 8.30   ? 137 GLN A C   1 
ATOM   1224 O  O   . GLN A 1 136 ? 16.010  13.102  24.341  1.00 8.27   ? 137 GLN A O   1 
ATOM   1225 C  CB  . GLN A 1 136 ? 15.408  16.151  24.409  1.00 9.02   ? 137 GLN A CB  1 
ATOM   1226 C  CG  . GLN A 1 136 ? 15.509  17.431  23.579  1.00 10.26  ? 137 GLN A CG  1 
ATOM   1227 C  CD  . GLN A 1 136 ? 16.529  18.332  23.930  1.00 12.41  ? 137 GLN A CD  1 
ATOM   1228 O  OE1 . GLN A 1 136 ? 16.825  18.534  25.100  1.00 12.74  ? 137 GLN A OE1 1 
ATOM   1229 N  NE2 . GLN A 1 136 ? 17.147  18.923  22.907  1.00 13.50  ? 137 GLN A NE2 1 
ATOM   1230 N  N   A PRO A 1 137 ? 16.397  13.825  26.423  0.50 7.84   ? 138 PRO A N   1 
ATOM   1231 N  N   B PRO A 1 137 ? 16.523  13.848  26.418  0.50 8.83   ? 138 PRO A N   1 
ATOM   1232 C  CA  A PRO A 1 137 ? 16.158  12.498  26.960  0.50 8.71   ? 138 PRO A CA  1 
ATOM   1233 C  CA  B PRO A 1 137 ? 16.183  12.596  27.040  0.50 8.99   ? 138 PRO A CA  1 
ATOM   1234 C  C   A PRO A 1 137 ? 14.744  12.059  26.888  0.50 9.06   ? 138 PRO A C   1 
ATOM   1235 C  C   B PRO A 1 137 ? 14.787  12.068  26.754  0.50 8.21   ? 138 PRO A C   1 
ATOM   1236 O  O   A PRO A 1 137 ? 14.485  10.894  27.082  0.50 10.38  ? 138 PRO A O   1 
ATOM   1237 O  O   B PRO A 1 137 ? 14.581  10.848  26.678  0.50 9.56   ? 138 PRO A O   1 
ATOM   1238 C  CB  A PRO A 1 137 ? 16.602  12.608  28.435  0.50 9.95   ? 138 PRO A CB  1 
ATOM   1239 C  CB  B PRO A 1 137 ? 16.330  12.899  28.527  0.50 9.80   ? 138 PRO A CB  1 
ATOM   1240 C  CG  A PRO A 1 137 ? 16.407  14.042  28.715  0.50 11.21  ? 138 PRO A CG  1 
ATOM   1241 C  CG  B PRO A 1 137 ? 17.472  13.854  28.530  0.50 10.21  ? 138 PRO A CG  1 
ATOM   1242 C  CD  A PRO A 1 137 ? 16.832  14.776  27.478  0.50 9.28   ? 138 PRO A CD  1 
ATOM   1243 C  CD  B PRO A 1 137 ? 17.237  14.749  27.359  0.50 9.29   ? 138 PRO A CD  1 
ATOM   1244 N  N   . ASP A 1 138 ? 13.817  12.990  26.585  1.00 8.32   ? 139 ASP A N   1 
ATOM   1245 C  CA  . ASP A 1 138 ? 12.447  12.706  26.341  1.00 8.27   ? 139 ASP A CA  1 
ATOM   1246 C  C   . ASP A 1 138 ? 12.038  13.178  24.927  1.00 7.38   ? 139 ASP A C   1 
ATOM   1247 O  O   . ASP A 1 138 ? 10.903  13.596  24.718  1.00 8.06   ? 139 ASP A O   1 
ATOM   1248 C  CB  . ASP A 1 138 ? 11.498  13.311  27.382  1.00 9.14   ? 139 ASP A CB  1 
ATOM   1249 C  CG  . ASP A 1 138 ? 11.572  14.800  27.463  1.00 9.35   ? 139 ASP A CG  1 
ATOM   1250 O  OD1 . ASP A 1 138 ? 12.512  15.406  26.884  1.00 9.84   ? 139 ASP A OD1 1 
ATOM   1251 O  OD2 . ASP A 1 138 ? 10.713  15.393  28.165  1.00 11.16  ? 139 ASP A OD2 1 
ATOM   1252 N  N   . GLY A 1 139 ? 12.961  13.097  23.980  1.00 6.94   ? 140 GLY A N   1 
ATOM   1253 C  CA  . GLY A 1 139 ? 12.668  13.621  22.640  1.00 7.47   ? 140 GLY A CA  1 
ATOM   1254 C  C   . GLY A 1 139 ? 11.863  12.686  21.754  1.00 6.32   ? 140 GLY A C   1 
ATOM   1255 O  O   . GLY A 1 139 ? 11.169  13.161  20.859  1.00 6.96   ? 140 GLY A O   1 
ATOM   1256 N  N   . LEU A 1 140 ? 12.062  11.362  21.925  1.00 6.11   ? 141 LEU A N   1 
ATOM   1257 C  CA  . LEU A 1 140 ? 11.440  10.383  21.045  1.00 6.14   ? 141 LEU A CA  1 
ATOM   1258 C  C   . LEU A 1 140 ? 10.583  9.443   21.859  1.00 5.58   ? 141 LEU A C   1 
ATOM   1259 O  O   . LEU A 1 140 ? 10.932  9.112   22.997  1.00 6.14   ? 141 LEU A O   1 
ATOM   1260 C  CB  . LEU A 1 140 ? 12.521  9.566   20.293  1.00 7.09   ? 141 LEU A CB  1 
ATOM   1261 C  CG  . LEU A 1 140 ? 13.145  10.144  19.037  1.00 9.31   ? 141 LEU A CG  1 
ATOM   1262 C  CD1 . LEU A 1 140 ? 12.282  9.904   17.875  1.00 11.56  ? 141 LEU A CD1 1 
ATOM   1263 C  CD2 . LEU A 1 140 ? 13.717  11.497  19.168  1.00 9.08   ? 141 LEU A CD2 1 
ATOM   1264 N  N   . ALA A 1 141 ? 9.548   8.931   21.229  1.00 5.74   ? 142 ALA A N   1 
ATOM   1265 C  CA  . ALA A 1 141 ? 8.798   7.792   21.780  1.00 6.08   ? 142 ALA A CA  1 
ATOM   1266 C  C   . ALA A 1 141 ? 8.710   6.779   20.659  1.00 5.49   ? 142 ALA A C   1 
ATOM   1267 O  O   . ALA A 1 141 ? 8.295   7.131   19.524  1.00 6.13   ? 142 ALA A O   1 
ATOM   1268 C  CB  . ALA A 1 141 ? 7.404   8.193   22.228  1.00 7.34   ? 142 ALA A CB  1 
ATOM   1269 N  N   . VAL A 1 142 ? 9.137   5.553   20.920  1.00 5.49   ? 143 VAL A N   1 
ATOM   1270 C  CA  . VAL A 1 142 ? 9.073   4.494   19.918  1.00 5.40   ? 143 VAL A CA  1 
ATOM   1271 C  C   . VAL A 1 142 ? 8.120   3.445   20.456  1.00 5.50   ? 143 VAL A C   1 
ATOM   1272 O  O   . VAL A 1 142 ? 8.272   2.949   21.574  1.00 5.85   ? 143 VAL A O   1 
ATOM   1273 C  CB  . VAL A 1 142 ? 10.431  3.920   19.551  1.00 6.04   ? 143 VAL A CB  1 
ATOM   1274 C  CG1 . VAL A 1 142 ? 10.255  2.878   18.454  1.00 6.47   ? 143 VAL A CG1 1 
ATOM   1275 C  CG2 . VAL A 1 142 ? 11.366  5.043   19.074  1.00 7.05   ? 143 VAL A CG2 1 
ATOM   1276 N  N   . LEU A 1 143 ? 7.105   3.151   19.651  1.00 5.42   ? 144 LEU A N   1 
ATOM   1277 C  CA  . LEU A 1 143 ? 6.142   2.094   19.892  1.00 5.73   ? 144 LEU A CA  1 
ATOM   1278 C  C   . LEU A 1 143 ? 6.640   0.834   19.214  1.00 5.56   ? 144 LEU A C   1 
ATOM   1279 O  O   . LEU A 1 143 ? 6.799   0.811   18.004  1.00 6.39   ? 144 LEU A O   1 
ATOM   1280 C  CB  . LEU A 1 143 ? 4.785   2.541   19.357  1.00 7.06   ? 144 LEU A CB  1 
ATOM   1281 C  CG  . LEU A 1 143 ? 3.618   1.604   19.538  1.00 7.77   ? 144 LEU A CG  1 
ATOM   1282 C  CD1 . LEU A 1 143 ? 3.370   1.325   20.992  1.00 10.12  ? 144 LEU A CD1 1 
ATOM   1283 C  CD2 . LEU A 1 143 ? 2.363   2.168   18.881  1.00 9.58   ? 144 LEU A CD2 1 
ATOM   1284 N  N   . GLY A 1 144 ? 6.932   -0.183  20.036  1.00 5.38   ? 145 GLY A N   1 
ATOM   1285 C  CA  . GLY A 1 144 ? 7.447   -1.440  19.529  1.00 5.72   ? 145 GLY A CA  1 
ATOM   1286 C  C   . GLY A 1 144 ? 6.383   -2.531  19.565  1.00 5.24   ? 145 GLY A C   1 
ATOM   1287 O  O   . GLY A 1 144 ? 5.649   -2.656  20.540  1.00 6.20   ? 145 GLY A O   1 
ATOM   1288 N  N   . ILE A 1 145 ? 6.328   -3.288  18.466  1.00 5.36   ? 146 ILE A N   1 
ATOM   1289 C  CA  . ILE A 1 145 ? 5.326   -4.325  18.286  1.00 5.41   ? 146 ILE A CA  1 
ATOM   1290 C  C   . ILE A 1 145 ? 6.030   -5.558  17.784  1.00 5.06   ? 146 ILE A C   1 
ATOM   1291 O  O   . ILE A 1 145 ? 6.751   -5.513  16.791  1.00 5.91   ? 146 ILE A O   1 
ATOM   1292 C  CB  . ILE A 1 145 ? 4.218   -3.863  17.294  1.00 5.98   ? 146 ILE A CB  1 
ATOM   1293 C  CG1 . ILE A 1 145 ? 3.558   -2.595  17.841  1.00 7.90   ? 146 ILE A CG1 1 
ATOM   1294 C  CG2 . ILE A 1 145 ? 3.222   -4.973  17.096  1.00 7.97   ? 146 ILE A CG2 1 
ATOM   1295 C  CD1 . ILE A 1 145 ? 2.549   -1.967  16.955  1.00 7.69   ? 146 ILE A CD1 1 
ATOM   1296 N  N   . PHE A 1 146 ? 5.847   -6.669  18.469  1.00 5.60   ? 147 PHE A N   1 
ATOM   1297 C  CA  . PHE A 1 146 ? 6.458   -7.933  18.064  1.00 5.69   ? 147 PHE A CA  1 
ATOM   1298 C  C   . PHE A 1 146 ? 5.685   -8.546  16.909  1.00 5.93   ? 147 PHE A C   1 
ATOM   1299 O  O   . PHE A 1 146 ? 4.460   -8.447  16.842  1.00 6.64   ? 147 PHE A O   1 
ATOM   1300 C  CB  . PHE A 1 146 ? 6.457   -8.894  19.249  1.00 6.25   ? 147 PHE A CB  1 
ATOM   1301 C  CG  . PHE A 1 146 ? 7.327   -8.416  20.377  1.00 5.70   ? 147 PHE A CG  1 
ATOM   1302 C  CD1 . PHE A 1 146 ? 8.680   -8.223  20.203  1.00 6.23   ? 147 PHE A CD1 1 
ATOM   1303 C  CD2 . PHE A 1 146 ? 6.765   -8.166  21.626  1.00 6.50   ? 147 PHE A CD2 1 
ATOM   1304 C  CE1 . PHE A 1 146 ? 9.502   -7.830  21.252  1.00 6.67   ? 147 PHE A CE1 1 
ATOM   1305 C  CE2 . PHE A 1 146 ? 7.573   -7.745  22.683  1.00 6.89   ? 147 PHE A CE2 1 
ATOM   1306 C  CZ  . PHE A 1 146 ? 8.936   -7.601  22.496  1.00 6.87   ? 147 PHE A CZ  1 
ATOM   1307 N  N   . LEU A 1 147 ? 6.430   -9.266  16.052  1.00 6.11   ? 148 LEU A N   1 
ATOM   1308 C  CA  . LEU A 1 147 ? 5.857   -10.050 14.955  1.00 6.41   ? 148 LEU A CA  1 
ATOM   1309 C  C   . LEU A 1 147 ? 6.191   -11.502 15.184  1.00 6.01   ? 148 LEU A C   1 
ATOM   1310 O  O   . LEU A 1 147 ? 7.357   -11.854 15.361  1.00 7.19   ? 148 LEU A O   1 
ATOM   1311 C  CB  . LEU A 1 147 ? 6.435   -9.620  13.616  1.00 6.56   ? 148 LEU A CB  1 
ATOM   1312 C  CG  . LEU A 1 147 ? 5.873   -8.377  12.939  1.00 7.04   ? 148 LEU A CG  1 
ATOM   1313 C  CD1 . LEU A 1 147 ? 6.037   -7.122  13.797  1.00 8.52   ? 148 LEU A CD1 1 
ATOM   1314 C  CD2 . LEU A 1 147 ? 6.513   -8.158  11.585  1.00 7.78   ? 148 LEU A CD2 1 
ATOM   1315 N  N   . LYS A 1 148 ? 5.162   -12.354 15.160  1.00 6.90   ? 149 LYS A N   1 
ATOM   1316 C  CA  . LYS A 1 148 ? 5.331   -13.804 15.121  1.00 8.11   ? 149 LYS A CA  1 
ATOM   1317 C  C   . LYS A 1 148 ? 4.877   -14.299 13.781  1.00 7.84   ? 149 LYS A C   1 
ATOM   1318 O  O   . LYS A 1 148 ? 4.023   -13.697 13.133  1.00 9.27   ? 149 LYS A O   1 
ATOM   1319 C  CB  . LYS A 1 148 ? 4.585   -14.469 16.261  1.00 9.67   ? 149 LYS A CB  1 
ATOM   1320 C  CG  . LYS A 1 148 ? 3.081   -14.337 16.224  1.00 11.50  ? 149 LYS A CG  1 
ATOM   1321 C  CD  . LYS A 1 148 ? 2.432   -15.116 17.373  1.00 17.08  ? 149 LYS A CD  1 
ATOM   1322 C  CE  . LYS A 1 148 ? 0.987   -15.165 17.196  1.00 23.77  ? 149 LYS A CE  1 
ATOM   1323 N  NZ  . LYS A 1 148 ? 0.524   -16.202 18.174  1.00 138.77 ? 149 LYS A NZ  1 
ATOM   1324 N  N   . VAL A 1 149 ? 5.398   -15.462 13.361  1.00 8.59   ? 150 VAL A N   1 
ATOM   1325 C  CA  . VAL A 1 149 ? 5.029   -16.053 12.098  1.00 8.63   ? 150 VAL A CA  1 
ATOM   1326 C  C   . VAL A 1 149 ? 3.816   -16.981 12.267  1.00 9.40   ? 150 VAL A C   1 
ATOM   1327 O  O   . VAL A 1 149 ? 3.866   -17.952 13.052  1.00 10.46  ? 150 VAL A O   1 
ATOM   1328 C  CB  . VAL A 1 149 ? 6.224   -16.801 11.470  1.00 9.97   ? 150 VAL A CB  1 
ATOM   1329 C  CG1 . VAL A 1 149 ? 5.844   -17.583 10.252  1.00 11.28  ? 150 VAL A CG1 1 
ATOM   1330 C  CG2 . VAL A 1 149 ? 7.313   -15.786 11.141  1.00 10.96  ? 150 VAL A CG2 1 
ATOM   1331 N  N   . GLY A 1 150 ? 2.759   -16.693 11.562  1.00 9.83   ? 151 GLY A N   1 
ATOM   1332 C  CA  . GLY A 1 150 ? 1.545   -17.522 11.593  1.00 10.87  ? 151 GLY A CA  1 
ATOM   1333 C  C   . GLY A 1 150 ? 0.663   -17.060 10.449  1.00 9.65   ? 151 GLY A C   1 
ATOM   1334 O  O   . GLY A 1 150 ? 1.064   -17.151 9.282   1.00 10.70  ? 151 GLY A O   1 
ATOM   1335 N  N   A SER A 1 151 ? -0.518  -16.530 10.754  0.50 10.05  ? 152 SER A N   1 
ATOM   1336 N  N   B SER A 1 151 ? -0.509  -16.543 10.836  0.50 9.91   ? 152 SER A N   1 
ATOM   1337 C  CA  A SER A 1 151 ? -1.364  -16.044 9.659   0.50 10.80  ? 152 SER A CA  1 
ATOM   1338 C  CA  B SER A 1 151 ? -1.406  -15.934 9.863   0.50 9.41   ? 152 SER A CA  1 
ATOM   1339 C  C   A SER A 1 151 ? -0.842  -14.694 9.219   0.50 10.08  ? 152 SER A C   1 
ATOM   1340 C  C   B SER A 1 151 ? -0.721  -14.730 9.185   0.50 8.73   ? 152 SER A C   1 
ATOM   1341 O  O   A SER A 1 151 ? -0.263  -13.896 10.005  0.50 8.81   ? 152 SER A O   1 
ATOM   1342 O  O   B SER A 1 151 ? 0.122   -14.049 9.785   0.50 7.92   ? 152 SER A O   1 
ATOM   1343 C  CB  A SER A 1 151 ? -2.786  -15.840 10.129  0.50 11.51  ? 152 SER A CB  1 
ATOM   1344 C  CB  B SER A 1 151 ? -2.694  -15.545 10.522  0.50 11.44  ? 152 SER A CB  1 
ATOM   1345 O  OG  A SER A 1 151 ? -2.780  -14.825 11.152  0.50 16.83  ? 152 SER A OG  1 
ATOM   1346 O  OG  B SER A 1 151 ? -3.355  -16.706 10.885  0.50 15.00  ? 152 SER A OG  1 
ATOM   1347 N  N   . ALA A 1 152 ? -1.126  -14.374 7.957   1.00 10.01  ? 153 ALA A N   1 
ATOM   1348 C  CA  . ALA A 1 152 ? -0.701  -13.135 7.334   1.00 9.24   ? 153 ALA A CA  1 
ATOM   1349 C  C   . ALA A 1 152 ? -1.338  -11.950 8.034   1.00 8.88   ? 153 ALA A C   1 
ATOM   1350 O  O   . ALA A 1 152 ? -2.458  -12.020 8.528   1.00 10.76  ? 153 ALA A O   1 
ATOM   1351 C  CB  . ALA A 1 152 ? -1.061  -13.135 5.873   1.00 11.03  ? 153 ALA A CB  1 
ATOM   1352 N  N   . LYS A 1 153 ? -0.627  -10.818 7.965   1.00 9.15   ? 154 LYS A N   1 
ATOM   1353 C  CA  . LYS A 1 153 ? -1.182  -9.543  8.418   1.00 9.39   ? 154 LYS A CA  1 
ATOM   1354 C  C   . LYS A 1 153 ? -1.629  -8.764  7.175   1.00 9.19   ? 154 LYS A C   1 
ATOM   1355 O  O   . LYS A 1 153 ? -0.762  -8.326  6.394   1.00 8.94   ? 154 LYS A O   1 
ATOM   1356 C  CB  . LYS A 1 153 ? -0.152  -8.737  9.204   1.00 10.04  ? 154 LYS A CB  1 
ATOM   1357 C  CG  . LYS A 1 153 ? -0.757  -7.515  9.932   1.00 10.73  ? 154 LYS A CG  1 
ATOM   1358 C  CD  . LYS A 1 153 ? -1.656  -7.885  11.088  1.00 13.17  ? 154 LYS A CD  1 
ATOM   1359 C  CE  . LYS A 1 153 ? -1.912  -6.693  11.991  1.00 16.58  ? 154 LYS A CE  1 
ATOM   1360 N  NZ  . LYS A 1 153 ? -2.967  -7.051  12.919  1.00 22.84  ? 154 LYS A NZ  1 
ATOM   1361 N  N   A PRO A 1 154 ? -2.903  -8.697  6.779   0.50 9.46   ? 155 PRO A N   1 
ATOM   1362 N  N   B PRO A 1 154 ? -2.952  -8.594  6.990   0.50 8.60   ? 155 PRO A N   1 
ATOM   1363 C  CA  A PRO A 1 154 ? -3.365  -7.933  5.571   0.50 9.98   ? 155 PRO A CA  1 
ATOM   1364 C  CA  B PRO A 1 154 ? -3.262  -8.131  5.644   0.50 10.32  ? 155 PRO A CA  1 
ATOM   1365 C  C   A PRO A 1 154 ? -2.784  -6.542  5.457   0.50 11.40  ? 155 PRO A C   1 
ATOM   1366 C  C   B PRO A 1 154 ? -2.725  -6.713  5.428   0.50 9.09   ? 155 PRO A C   1 
ATOM   1367 O  O   A PRO A 1 154 ? -2.372  -6.055  4.459   0.50 10.81  ? 155 PRO A O   1 
ATOM   1368 O  O   B PRO A 1 154 ? -2.293  -6.431  4.276   0.50 10.20  ? 155 PRO A O   1 
ATOM   1369 C  CB  A PRO A 1 154 ? -4.876  -7.933  5.798   0.50 10.14  ? 155 PRO A CB  1 
ATOM   1370 C  CB  B PRO A 1 154 ? -4.784  -8.291  5.525   0.50 10.72  ? 155 PRO A CB  1 
ATOM   1371 C  CG  A PRO A 1 154 ? -5.080  -9.354  6.392   0.50 10.36  ? 155 PRO A CG  1 
ATOM   1372 C  CG  B PRO A 1 154 ? -5.253  -9.000  6.822   0.50 14.15  ? 155 PRO A CG  1 
ATOM   1373 C  CD  A PRO A 1 154 ? -4.041  -9.344  7.480   0.50 10.85  ? 155 PRO A CD  1 
ATOM   1374 C  CD  B PRO A 1 154 ? -4.132  -9.033  7.800   0.50 8.84   ? 155 PRO A CD  1 
ATOM   1375 N  N   . GLY A 1 155 ? -2.723  -5.861  6.537   1.00 10.09  ? 156 GLY A N   1 
ATOM   1376 C  CA  . GLY A 1 155 ? -2.249  -4.481  6.504   1.00 11.05  ? 156 GLY A CA  1 
ATOM   1377 C  C   . GLY A 1 155 ? -0.761  -4.338  6.265   1.00 10.07  ? 156 GLY A C   1 
ATOM   1378 O  O   . GLY A 1 155 ? -0.316  -3.216  6.079   1.00 13.19  ? 156 GLY A O   1 
ATOM   1379 N  N   . LEU A 1 156 ? -0.016  -5.421  6.331   1.00 9.12   ? 157 LEU A N   1 
ATOM   1380 C  CA  . LEU A 1 156 ? 1.404   -5.402  5.974   1.00 8.83   ? 157 LEU A CA  1 
ATOM   1381 C  C   . LEU A 1 156 ? 1.675   -5.611  4.509   1.00 8.41   ? 157 LEU A C   1 
ATOM   1382 O  O   . LEU A 1 156 ? 2.759   -5.326  4.038   1.00 8.46   ? 157 LEU A O   1 
ATOM   1383 C  CB  . LEU A 1 156 ? 2.135   -6.454  6.825   1.00 8.46   ? 157 LEU A CB  1 
ATOM   1384 C  CG  . LEU A 1 156 ? 3.645   -6.540  6.683   1.00 8.93   ? 157 LEU A CG  1 
ATOM   1385 C  CD1 . LEU A 1 156 ? 4.347   -5.271  7.073   1.00 9.98   ? 157 LEU A CD1 1 
ATOM   1386 C  CD2 . LEU A 1 156 ? 4.176   -7.724  7.506   1.00 10.14  ? 157 LEU A CD2 1 
ATOM   1387 N  N   . GLN A 1 157 ? 0.701   -6.191  3.775   1.00 9.04   ? 158 GLN A N   1 
ATOM   1388 C  CA  . GLN A 1 157 ? 1.070   -6.687  2.418   1.00 9.49   ? 158 GLN A CA  1 
ATOM   1389 C  C   . GLN A 1 157 ? 1.502   -5.564  1.521   1.00 9.51   ? 158 GLN A C   1 
ATOM   1390 O  O   . GLN A 1 157 ? 2.386   -5.775  0.684   1.00 9.66   ? 158 GLN A O   1 
ATOM   1391 C  CB  . GLN A 1 157 ? -0.060  -7.525  1.865   1.00 11.07  ? 158 GLN A CB  1 
ATOM   1392 C  CG  . GLN A 1 157 ? 0.355   -8.262  0.612   1.00 10.69  ? 158 GLN A CG  1 
ATOM   1393 C  CD  . GLN A 1 157 ? 1.455   -9.238  0.809   1.00 10.33  ? 158 GLN A CD  1 
ATOM   1394 O  OE1 . GLN A 1 157 ? 1.595   -9.834  1.911   1.00 10.46  ? 158 GLN A OE1 1 
ATOM   1395 N  NE2 . GLN A 1 157 ? 2.298   -9.464  -0.202  1.00 12.46  ? 158 GLN A NE2 1 
ATOM   1396 N  N   . LYS A 1 158 ? 0.913   -4.356  1.598   1.00 9.75   ? 159 LYS A N   1 
ATOM   1397 C  CA  . LYS A 1 158 ? 1.379   -3.280  0.730   1.00 9.85   ? 159 LYS A CA  1 
ATOM   1398 C  C   . LYS A 1 158 ? 2.845   -2.922  0.928   1.00 9.41   ? 159 LYS A C   1 
ATOM   1399 O  O   . LYS A 1 158 ? 3.545   -2.577  0.005   1.00 10.59  ? 159 LYS A O   1 
ATOM   1400 C  CB  . LYS A 1 158 ? 0.502   -2.055  0.933   1.00 11.94  ? 159 LYS A CB  1 
ATOM   1401 C  CG  . LYS A 1 158 ? -0.807  -2.161  0.118   1.00 15.88  ? 159 LYS A CG  1 
ATOM   1402 C  CD  . LYS A 1 158 ? -1.601  -0.928  0.101   1.00 22.83  ? 159 LYS A CD  1 
ATOM   1403 C  CE  . LYS A 1 158 ? -3.072  -1.215  -0.320  1.00 27.84  ? 159 LYS A CE  1 
ATOM   1404 N  NZ  . LYS A 1 158 ? -4.034  -0.042  -0.395  1.00 25.59  ? 159 LYS A NZ  1 
ATOM   1405 N  N   . VAL A 1 159 ? 3.311   -3.057  2.196   1.00 8.81   ? 160 VAL A N   1 
ATOM   1406 C  CA  . VAL A 1 159 ? 4.751   -2.874  2.470   1.00 8.56   ? 160 VAL A CA  1 
ATOM   1407 C  C   . VAL A 1 159 ? 5.550   -3.974  1.799   1.00 8.76   ? 160 VAL A C   1 
ATOM   1408 O  O   . VAL A 1 159 ? 6.506   -3.697  1.077   1.00 9.83   ? 160 VAL A O   1 
ATOM   1409 C  CB  . VAL A 1 159 ? 4.999   -2.838  3.982   1.00 8.66   ? 160 VAL A CB  1 
ATOM   1410 C  CG1 . VAL A 1 159 ? 6.499   -2.838  4.264   1.00 10.22  ? 160 VAL A CG1 1 
ATOM   1411 C  CG2 . VAL A 1 159 ? 4.312   -1.688  4.622   1.00 10.61  ? 160 VAL A CG2 1 
ATOM   1412 N  N   . VAL A 1 160 ? 5.149   -5.236  2.011   1.00 8.91   ? 161 VAL A N   1 
ATOM   1413 C  CA  . VAL A 1 160 ? 5.876   -6.332  1.399   1.00 10.06  ? 161 VAL A CA  1 
ATOM   1414 C  C   . VAL A 1 160 ? 5.963   -6.200  -0.098  1.00 10.41  ? 161 VAL A C   1 
ATOM   1415 O  O   . VAL A 1 160 ? 6.997   -6.468  -0.658  1.00 11.58  ? 161 VAL A O   1 
ATOM   1416 C  CB  . VAL A 1 160 ? 5.063   -7.701  1.778   1.00 11.80  ? 161 VAL A CB  1 
ATOM   1417 C  CG1 . VAL A 1 160 ? 5.571   -8.823  0.965   1.00 13.53  ? 161 VAL A CG1 1 
ATOM   1418 C  CG2 . VAL A 1 160 ? 5.205   -7.938  3.248   1.00 12.21  ? 161 VAL A CG2 1 
ATOM   1419 N  N   . ASP A 1 161 ? 4.869   -5.826  -0.735  1.00 11.01  ? 162 ASP A N   1 
ATOM   1420 C  CA  . ASP A 1 161 ? 4.900   -5.796  -2.185  1.00 13.20  ? 162 ASP A CA  1 
ATOM   1421 C  C   . ASP A 1 161 ? 5.741   -4.748  -2.809  1.00 13.73  ? 162 ASP A C   1 
ATOM   1422 O  O   . ASP A 1 161 ? 6.132   -4.894  -3.907  1.00 19.62  ? 162 ASP A O   1 
ATOM   1423 C  CB  . ASP A 1 161 ? 3.555   -5.739  -2.668  1.00 17.45  ? 162 ASP A CB  1 
ATOM   1424 C  CG  . ASP A 1 161 ? 2.881   -7.109  -2.612  1.00 16.30  ? 162 ASP A CG  1 
ATOM   1425 O  OD1 . ASP A 1 161 ? 3.617   -8.116  -2.708  1.00 19.10  ? 162 ASP A OD1 1 
ATOM   1426 O  OD2 . ASP A 1 161 ? 1.644   -7.188  -2.447  1.00 18.42  ? 162 ASP A OD2 1 
ATOM   1427 N  N   . VAL A 1 162 ? 6.044   -3.650  -2.105  1.00 11.03  ? 163 VAL A N   1 
ATOM   1428 C  CA  . VAL A 1 162 ? 6.884   -2.581  -2.661  1.00 11.18  ? 163 VAL A CA  1 
ATOM   1429 C  C   . VAL A 1 162 ? 8.342   -2.884  -2.494  1.00 10.38  ? 163 VAL A C   1 
ATOM   1430 O  O   . VAL A 1 162 ? 9.198   -2.181  -3.055  1.00 11.65  ? 163 VAL A O   1 
ATOM   1431 C  CB  . VAL A 1 162 ? 6.489   -1.210  -2.059  1.00 12.26  ? 163 VAL A CB  1 
ATOM   1432 C  CG1 . VAL A 1 162 ? 7.002   -0.987  -0.669  1.00 11.86  ? 163 VAL A CG1 1 
ATOM   1433 C  CG2 . VAL A 1 162 ? 6.866   -0.058  -2.933  1.00 15.11  ? 163 VAL A CG2 1 
ATOM   1434 N  N   . LEU A 1 163 ? 8.721   -3.878  -1.679  1.00 10.10  ? 164 LEU A N   1 
ATOM   1435 C  CA  . LEU A 1 163 ? 10.141  -4.073  -1.359  1.00 10.36  ? 164 LEU A CA  1 
ATOM   1436 C  C   . LEU A 1 163 ? 10.962  -4.392  -2.555  1.00 10.96  ? 164 LEU A C   1 
ATOM   1437 O  O   . LEU A 1 163 ? 12.139  -4.051  -2.594  1.00 12.04  ? 164 LEU A O   1 
ATOM   1438 C  CB  . LEU A 1 163 ? 10.284  -5.140  -0.292  1.00 10.85  ? 164 LEU A CB  1 
ATOM   1439 C  CG  . LEU A 1 163 ? 9.632   -4.806  1.064   1.00 10.53  ? 164 LEU A CG  1 
ATOM   1440 C  CD1 . LEU A 1 163 ? 9.902   -5.928  2.082   1.00 12.51  ? 164 LEU A CD1 1 
ATOM   1441 C  CD2 . LEU A 1 163 ? 10.060  -3.470  1.635   1.00 11.03  ? 164 LEU A CD2 1 
ATOM   1442 N  N   . ASP A 1 164 ? 10.412  -5.085  -3.562  1.00 14.04  ? 165 ASP A N   1 
ATOM   1443 C  CA  . ASP A 1 164 ? 11.224  -5.393  -4.756  1.00 17.26  ? 165 ASP A CA  1 
ATOM   1444 C  C   . ASP A 1 164 ? 11.651  -4.110  -5.438  1.00 17.15  ? 165 ASP A C   1 
ATOM   1445 O  O   . ASP A 1 164 ? 12.554  -4.215  -6.268  1.00 20.49  ? 165 ASP A O   1 
ATOM   1446 C  CB  . ASP A 1 164 ? 10.484  -6.364  -5.716  1.00 23.87  ? 165 ASP A CB  1 
ATOM   1447 C  CG  . ASP A 1 164 ? 9.507   -5.631  -6.545  1.00 33.03  ? 165 ASP A CG  1 
ATOM   1448 O  OD1 . ASP A 1 164 ? 8.566   -5.088  -5.896  1.00 30.00  ? 165 ASP A OD1 1 
ATOM   1449 O  OD2 . ASP A 1 164 ? 9.705   -5.514  -7.809  1.00 47.22  ? 165 ASP A OD2 1 
ATOM   1450 N  N   . SER A 1 165 ? 11.056  -2.950  -5.178  1.00 13.29  ? 166 SER A N   1 
ATOM   1451 C  CA  . SER A 1 165 ? 11.373  -1.710  -5.835  1.00 13.45  ? 166 SER A CA  1 
ATOM   1452 C  C   . SER A 1 165 ? 12.464  -0.939  -5.117  1.00 11.18  ? 166 SER A C   1 
ATOM   1453 O  O   . SER A 1 165 ? 13.021  0.033   -5.644  1.00 12.76  ? 166 SER A O   1 
ATOM   1454 C  CB  . SER A 1 165 ? 10.112  -0.865  -6.080  1.00 15.96  ? 166 SER A CB  1 
ATOM   1455 O  OG  . SER A 1 165 ? 9.605   -0.302  -4.886  1.00 15.24  ? 166 SER A OG  1 
ATOM   1456 N  N   . ILE A 1 166 ? 12.765  -1.387  -3.890  1.00 9.87   ? 167 ILE A N   1 
ATOM   1457 C  CA  . ILE A 1 166 ? 13.766  -0.731  -3.092  1.00 9.78   ? 167 ILE A CA  1 
ATOM   1458 C  C   . ILE A 1 166 ? 14.789  -1.764  -2.571  1.00 9.22   ? 167 ILE A C   1 
ATOM   1459 O  O   . ILE A 1 166 ? 15.210  -1.723  -1.411  1.00 9.19   ? 167 ILE A O   1 
ATOM   1460 C  CB  . ILE A 1 166 ? 13.180  0.092   -1.921  1.00 9.73   ? 167 ILE A CB  1 
ATOM   1461 C  CG1 . ILE A 1 166 ? 12.333  -0.776  -0.972  1.00 9.36   ? 167 ILE A CG1 1 
ATOM   1462 C  CG2 . ILE A 1 166 ? 12.388  1.309   -2.447  1.00 11.01  ? 167 ILE A CG2 1 
ATOM   1463 C  CD1 . ILE A 1 166 ? 12.359  -0.226  0.430   1.00 10.67  ? 167 ILE A CD1 1 
ATOM   1464 N  N   . LYS A 1 167 ? 15.234  -2.622  -3.477  1.00 10.59  ? 168 LYS A N   1 
ATOM   1465 C  CA  . LYS A 1 167 ? 16.002  -3.791  -3.010  1.00 10.10  ? 168 LYS A CA  1 
ATOM   1466 C  C   . LYS A 1 167 ? 17.298  -3.384  -2.334  1.00 9.45   ? 168 LYS A C   1 
ATOM   1467 O  O   . LYS A 1 167 ? 17.754  -4.036  -1.397  1.00 9.89   ? 168 LYS A O   1 
ATOM   1468 C  CB  . LYS A 1 167 ? 16.303  -4.738  -4.172  1.00 11.95  ? 168 LYS A CB  1 
ATOM   1469 C  CG  . LYS A 1 167 ? 17.053  -5.979  -3.771  1.00 13.68  ? 168 LYS A CG  1 
ATOM   1470 C  CD  . LYS A 1 167 ? 17.121  -6.921  -4.987  1.00 19.61  ? 168 LYS A CD  1 
ATOM   1471 C  CE  . LYS A 1 167 ? 17.818  -8.224  -4.700  1.00 22.77  ? 168 LYS A CE  1 
ATOM   1472 N  NZ  . LYS A 1 167 ? 18.136  -8.953  -5.971  1.00 46.21  ? 168 LYS A NZ  1 
ATOM   1473 N  N   . THR A 1 168 ? 17.960  -2.360  -2.873  1.00 9.51   ? 169 THR A N   1 
ATOM   1474 C  CA  . THR A 1 168 ? 19.309  -1.972  -2.478  1.00 10.13  ? 169 THR A CA  1 
ATOM   1475 C  C   . THR A 1 168 ? 19.331  -0.606  -1.812  1.00 9.07   ? 169 THR A C   1 
ATOM   1476 O  O   . THR A 1 168 ? 18.464  0.256   -1.980  1.00 9.74   ? 169 THR A O   1 
ATOM   1477 C  CB  . THR A 1 168 ? 20.237  -1.995  -3.716  1.00 10.58  ? 169 THR A CB  1 
ATOM   1478 O  OG1 . THR A 1 168 ? 19.650  -1.247  -4.763  1.00 11.86  ? 169 THR A OG1 1 
ATOM   1479 C  CG2 . THR A 1 168 ? 20.451  -3.418  -4.174  1.00 12.39  ? 169 THR A CG2 1 
ATOM   1480 N  N   . LYS A 1 169 ? 20.395  -0.425  -1.013  1.00 10.32  ? 170 LYS A N   1 
ATOM   1481 C  CA  . LYS A 1 169 ? 20.652  0.745   -0.271  1.00 10.53  ? 170 LYS A CA  1 
ATOM   1482 C  C   . LYS A 1 169 ? 20.540  2.005   -1.098  1.00 10.33  ? 170 LYS A C   1 
ATOM   1483 O  O   . LYS A 1 169 ? 21.193  2.106   -2.136  1.00 12.27  ? 170 LYS A O   1 
ATOM   1484 C  CB  . LYS A 1 169 ? 22.017  0.697   0.385   1.00 11.59  ? 170 LYS A CB  1 
ATOM   1485 C  CG  . LYS A 1 169 ? 22.369  1.897   1.257   1.00 14.26  ? 170 LYS A CG  1 
ATOM   1486 C  CD  . LYS A 1 169 ? 23.673  1.731   1.963   1.00 16.75  ? 170 LYS A CD  1 
ATOM   1487 C  CE  . LYS A 1 169 ? 24.745  1.336   0.963   1.00 24.99  ? 170 LYS A CE  1 
ATOM   1488 N  NZ  . LYS A 1 169 ? 25.895  0.657   1.616   1.00 41.11  ? 170 LYS A NZ  1 
ATOM   1489 N  N   . GLY A 1 170 ? 19.749  2.970   -0.682  1.00 10.23  ? 171 GLY A N   1 
ATOM   1490 C  CA  . GLY A 1 170 ? 19.632  4.267   -1.330  1.00 12.04  ? 171 GLY A CA  1 
ATOM   1491 C  C   . GLY A 1 170 ? 18.448  4.357   -2.282  1.00 12.10  ? 171 GLY A C   1 
ATOM   1492 O  O   . GLY A 1 170 ? 18.143  5.433   -2.776  1.00 13.57  ? 171 GLY A O   1 
ATOM   1493 N  N   A LYS A 1 171 ? 17.798  3.228   -2.572  0.50 10.56  ? 172 LYS A N   1 
ATOM   1494 N  N   B LYS A 1 171 ? 17.802  3.221   -2.568  0.50 10.66  ? 172 LYS A N   1 
ATOM   1495 C  CA  A LYS A 1 171 ? 16.567  3.256   -3.368  0.50 10.64  ? 172 LYS A CA  1 
ATOM   1496 C  CA  B LYS A 1 171 ? 16.566  3.239   -3.362  0.50 10.75  ? 172 LYS A CA  1 
ATOM   1497 C  C   A LYS A 1 171 ? 15.391  3.711   -2.524  0.50 10.03  ? 172 LYS A C   1 
ATOM   1498 C  C   B LYS A 1 171 ? 15.388  3.706   -2.522  0.50 10.12  ? 172 LYS A C   1 
ATOM   1499 O  O   A LYS A 1 171 ? 15.249  3.272   -1.388  0.50 9.56   ? 172 LYS A O   1 
ATOM   1500 O  O   B LYS A 1 171 ? 15.242  3.271   -1.382  0.50 9.58   ? 172 LYS A O   1 
ATOM   1501 C  CB  A LYS A 1 171 ? 16.301  1.913   -4.023  0.50 11.05  ? 172 LYS A CB  1 
ATOM   1502 C  CB  B LYS A 1 171 ? 16.276  1.892   -4.030  0.50 11.10  ? 172 LYS A CB  1 
ATOM   1503 C  CG  A LYS A 1 171 ? 17.449  1.488   -4.975  0.50 14.56  ? 172 LYS A CG  1 
ATOM   1504 C  CG  B LYS A 1 171 ? 17.239  1.573   -5.190  0.50 14.15  ? 172 LYS A CG  1 
ATOM   1505 C  CD  A LYS A 1 171 ? 16.939  0.329   -5.828  0.50 18.13  ? 172 LYS A CD  1 
ATOM   1506 C  CD  B LYS A 1 171 ? 16.765  0.452   -6.133  0.50 21.16  ? 172 LYS A CD  1 
ATOM   1507 C  CE  A LYS A 1 171 ? 17.576  0.195   -7.214  0.50 18.00  ? 172 LYS A CE  1 
ATOM   1508 C  CE  B LYS A 1 171 ? 15.548  0.821   -6.977  0.50 18.67  ? 172 LYS A CE  1 
ATOM   1509 N  NZ  A LYS A 1 171 ? 17.243  1.316   -8.078  0.50 24.32  ? 172 LYS A NZ  1 
ATOM   1510 N  NZ  B LYS A 1 171 ? 14.959  -0.207  -7.927  0.50 24.99  ? 172 LYS A NZ  1 
ATOM   1511 N  N   . SER A 1 172 ? 14.515  4.493   -3.130  1.00 11.60  ? 173 SER A N   1 
ATOM   1512 C  CA  . SER A 1 172 ? 13.292  4.929   -2.537  1.00 11.30  ? 173 SER A CA  1 
ATOM   1513 C  C   . SER A 1 172 ? 12.146  4.722   -3.538  1.00 10.83  ? 173 SER A C   1 
ATOM   1514 O  O   . SER A 1 172 ? 12.363  4.689   -4.753  1.00 13.10  ? 173 SER A O   1 
ATOM   1515 C  CB  . SER A 1 172 ? 13.316  6.356   -2.021  1.00 12.84  ? 173 SER A CB  1 
ATOM   1516 O  OG  . SER A 1 172 ? 13.513  7.239   -3.114  1.00 15.05  ? 173 SER A OG  1 
ATOM   1517 N  N   . ALA A 1 173 ? 10.928  4.682   -2.988  1.00 10.96  ? 174 ALA A N   1 
ATOM   1518 C  CA  . ALA A 1 173 ? 9.713   4.573   -3.802  1.00 12.00  ? 174 ALA A CA  1 
ATOM   1519 C  C   . ALA A 1 173 ? 8.626   5.412   -3.178  1.00 11.08  ? 174 ALA A C   1 
ATOM   1520 O  O   . ALA A 1 173 ? 8.522   5.482   -1.945  1.00 10.05  ? 174 ALA A O   1 
ATOM   1521 C  CB  . ALA A 1 173 ? 9.227   3.167   -4.047  1.00 13.09  ? 174 ALA A CB  1 
ATOM   1522 N  N   . ASP A 1 174 ? 7.716   5.960   -3.954  1.00 12.55  ? 175 ASP A N   1 
ATOM   1523 C  CA  . ASP A 1 174 ? 6.582   6.638   -3.387  1.00 13.01  ? 175 ASP A CA  1 
ATOM   1524 C  C   . ASP A 1 174 ? 5.813   5.600   -2.584  1.00 12.31  ? 175 ASP A C   1 
ATOM   1525 O  O   . ASP A 1 174 ? 5.709   4.422   -2.939  1.00 15.89  ? 175 ASP A O   1 
ATOM   1526 C  CB  . ASP A 1 174 ? 5.722   7.234   -4.506  1.00 18.28  ? 175 ASP A CB  1 
ATOM   1527 C  CG  . ASP A 1 174 ? 6.475   8.334   -5.318  1.00 23.36  ? 175 ASP A CG  1 
ATOM   1528 O  OD1 . ASP A 1 174 ? 7.165   9.245   -4.719  1.00 36.71  ? 175 ASP A OD1 1 
ATOM   1529 O  OD2 . ASP A 1 174 ? 6.389   8.362   -6.561  1.00 33.50  ? 175 ASP A OD2 1 
ATOM   1530 N  N   . PHE A 1 175 ? 5.229   6.057   -1.478  1.00 10.62  ? 176 PHE A N   1 
ATOM   1531 C  CA  . PHE A 1 175 ? 4.482   5.162   -0.608  1.00 11.48  ? 176 PHE A CA  1 
ATOM   1532 C  C   . PHE A 1 175 ? 3.397   5.915   0.119   1.00 9.59   ? 176 PHE A C   1 
ATOM   1533 O  O   . PHE A 1 175 ? 3.422   6.077   1.306   1.00 13.96  ? 176 PHE A O   1 
ATOM   1534 C  CB  . PHE A 1 175 ? 5.414   4.389   0.348   1.00 12.22  ? 176 PHE A CB  1 
ATOM   1535 C  CG  . PHE A 1 175 ? 4.785   3.112   0.858   1.00 11.06  ? 176 PHE A CG  1 
ATOM   1536 C  CD1 . PHE A 1 175 ? 4.559   2.046   0.013   1.00 13.66  ? 176 PHE A CD1 1 
ATOM   1537 C  CD2 . PHE A 1 175 ? 4.477   2.962   2.194   1.00 11.53  ? 176 PHE A CD2 1 
ATOM   1538 C  CE1 . PHE A 1 175 ? 4.045   0.875   0.493   1.00 14.47  ? 176 PHE A CE1 1 
ATOM   1539 C  CE2 . PHE A 1 175 ? 3.965   1.766   2.692   1.00 10.92  ? 176 PHE A CE2 1 
ATOM   1540 C  CZ  . PHE A 1 175 ? 3.682   0.739   1.825   1.00 12.18  ? 176 PHE A CZ  1 
ATOM   1541 N  N   . THR A 1 176 ? 2.487   6.493   -0.637  1.00 10.02  ? 177 THR A N   1 
ATOM   1542 C  CA  . THR A 1 176 ? 1.412   7.323   -0.131  1.00 8.93   ? 177 THR A CA  1 
ATOM   1543 C  C   . THR A 1 176 ? 0.227   6.485   0.265   1.00 8.46   ? 177 THR A C   1 
ATOM   1544 O  O   . THR A 1 176 ? 0.013   5.347   -0.204  1.00 9.60   ? 177 THR A O   1 
ATOM   1545 C  CB  . THR A 1 176 ? 1.041   8.371   -1.201  1.00 9.79   ? 177 THR A CB  1 
ATOM   1546 O  OG1 . THR A 1 176 ? 0.636   7.758   -2.414  1.00 15.97  ? 177 THR A OG1 1 
ATOM   1547 C  CG2 . THR A 1 176 ? 2.155   9.416   -1.322  1.00 17.33  ? 177 THR A CG2 1 
ATOM   1548 N  N   . ASN A 1 177 ? -0.596  7.073   1.117   1.00 8.29   ? 178 ASN A N   1 
ATOM   1549 C  CA  . ASN A 1 177 ? -1.859  6.503   1.508   1.00 9.43   ? 178 ASN A CA  1 
ATOM   1550 C  C   . ASN A 1 177 ? -1.772  5.164   2.221   1.00 9.27   ? 178 ASN A C   1 
ATOM   1551 O  O   . ASN A 1 177 ? -2.705  4.377   2.182   1.00 14.15  ? 178 ASN A O   1 
ATOM   1552 C  CB  . ASN A 1 177 ? -2.843  6.438   0.340   1.00 10.23  ? 178 ASN A CB  1 
ATOM   1553 C  CG  . ASN A 1 177 ? -3.037  7.802   -0.272  1.00 10.27  ? 178 ASN A CG  1 
ATOM   1554 O  OD1 . ASN A 1 177 ? -3.654  8.681   0.364   1.00 12.64  ? 178 ASN A OD1 1 
ATOM   1555 N  ND2 . ASN A 1 177 ? -2.450  8.047   -1.384  1.00 10.58  ? 178 ASN A ND2 1 
ATOM   1556 N  N   . PHE A 1 178 ? -0.658  4.898   2.909   1.00 8.29   ? 179 PHE A N   1 
ATOM   1557 C  CA  . PHE A 1 178 ? -0.568  3.705   3.702   1.00 8.93   ? 179 PHE A CA  1 
ATOM   1558 C  C   . PHE A 1 178 ? -1.038  3.997   5.124   1.00 8.82   ? 179 PHE A C   1 
ATOM   1559 O  O   . PHE A 1 178 ? -0.590  4.978   5.731   1.00 9.89   ? 179 PHE A O   1 
ATOM   1560 C  CB  . PHE A 1 178 ? 0.894   3.222   3.751   1.00 9.47   ? 179 PHE A CB  1 
ATOM   1561 C  CG  . PHE A 1 178 ? 1.038   1.966   4.591   1.00 8.87   ? 179 PHE A CG  1 
ATOM   1562 C  CD1 . PHE A 1 178 ? 0.678   0.733   4.103   1.00 10.30  ? 179 PHE A CD1 1 
ATOM   1563 C  CD2 . PHE A 1 178 ? 1.439   2.055   5.908   1.00 8.75   ? 179 PHE A CD2 1 
ATOM   1564 C  CE1 . PHE A 1 178 ? 0.696   -0.391  4.869   1.00 10.80  ? 179 PHE A CE1 1 
ATOM   1565 C  CE2 . PHE A 1 178 ? 1.477   0.940   6.719   1.00 8.75   ? 179 PHE A CE2 1 
ATOM   1566 C  CZ  . PHE A 1 178 ? 1.109   -0.277  6.202   1.00 9.90   ? 179 PHE A CZ  1 
ATOM   1567 N  N   . ASP A 1 179 ? -1.886  3.139   5.643   1.00 9.03   ? 180 ASP A N   1 
ATOM   1568 C  CA  . ASP A 1 179 ? -2.506  3.377   6.941   1.00 8.90   ? 180 ASP A CA  1 
ATOM   1569 C  C   . ASP A 1 179 ? -1.853  2.472   7.994   1.00 7.99   ? 180 ASP A C   1 
ATOM   1570 O  O   . ASP A 1 179 ? -2.062  1.254   8.033   1.00 9.02   ? 180 ASP A O   1 
ATOM   1571 C  CB  . ASP A 1 179 ? -3.992  3.039   6.864   1.00 11.29  ? 180 ASP A CB  1 
ATOM   1572 C  CG  . ASP A 1 179 ? -4.745  3.435   8.078   1.00 11.52  ? 180 ASP A CG  1 
ATOM   1573 O  OD1 . ASP A 1 179 ? -4.152  3.608   9.159   1.00 11.04  ? 180 ASP A OD1 1 
ATOM   1574 O  OD2 . ASP A 1 179 ? -5.988  3.504   7.968   1.00 19.38  ? 180 ASP A OD2 1 
ATOM   1575 N  N   . PRO A 1 180 ? -1.032  3.056   8.876   1.00 7.96   ? 181 PRO A N   1 
ATOM   1576 C  CA  . PRO A 1 180 ? -0.323  2.207   9.872   1.00 8.49   ? 181 PRO A CA  1 
ATOM   1577 C  C   . PRO A 1 180 ? -1.246  1.614   10.904  1.00 8.23   ? 181 PRO A C   1 
ATOM   1578 O  O   . PRO A 1 180 ? -0.786  0.714   11.651  1.00 8.64   ? 181 PRO A O   1 
ATOM   1579 C  CB  . PRO A 1 180 ? 0.695   3.183   10.476  1.00 9.32   ? 181 PRO A CB  1 
ATOM   1580 C  CG  . PRO A 1 180 ? 0.004   4.553   10.357  1.00 9.46   ? 181 PRO A CG  1 
ATOM   1581 C  CD  . PRO A 1 180 ? -0.700  4.482   9.011   1.00 9.28   ? 181 PRO A CD  1 
ATOM   1582 N  N   . ARG A 1 181 ? -2.502  2.014   10.974  1.00 8.46   ? 182 ARG A N   1 
ATOM   1583 C  CA  . ARG A 1 181 ? -3.431  1.325   11.893  1.00 8.98   ? 182 ARG A CA  1 
ATOM   1584 C  C   . ARG A 1 181 ? -3.573  -0.127  11.571  1.00 9.37   ? 182 ARG A C   1 
ATOM   1585 O  O   . ARG A 1 181 ? -3.890  -0.925  12.477  1.00 9.91   ? 182 ARG A O   1 
ATOM   1586 C  CB  . ARG A 1 181 ? -4.783  1.987   11.864  1.00 9.95   ? 182 ARG A CB  1 
ATOM   1587 C  CG  . ARG A 1 181 ? -4.734  3.404   12.392  1.00 10.41  ? 182 ARG A CG  1 
ATOM   1588 C  CD  . ARG A 1 181 ? -6.048  4.105   12.359  1.00 12.69  ? 182 ARG A CD  1 
ATOM   1589 N  NE  . ARG A 1 181 ? -6.443  4.375   11.003  1.00 12.44  ? 182 ARG A NE  1 
ATOM   1590 C  CZ  . ARG A 1 181 ? -7.479  5.105   10.669  1.00 15.14  ? 182 ARG A CZ  1 
ATOM   1591 N  NH1 . ARG A 1 181 ? -8.277  5.580   11.624  1.00 18.30  ? 182 ARG A NH1 1 
ATOM   1592 N  NH2 . ARG A 1 181 ? -7.719  5.334   9.370   1.00 18.75  ? 182 ARG A NH2 1 
ATOM   1593 N  N   . GLY A 1 182 ? -3.324  -0.541  10.323  1.00 9.00   ? 183 GLY A N   1 
ATOM   1594 C  CA  . GLY A 1 182 ? -3.397  -1.928  9.950   1.00 9.99   ? 183 GLY A CA  1 
ATOM   1595 C  C   . GLY A 1 182 ? -2.259  -2.781  10.442  1.00 9.49   ? 183 GLY A C   1 
ATOM   1596 O  O   . GLY A 1 182 ? -2.244  -3.988  10.147  1.00 11.54  ? 183 GLY A O   1 
ATOM   1597 N  N   . LEU A 1 183 ? -1.310  -2.194  11.161  1.00 9.07   ? 184 LEU A N   1 
ATOM   1598 C  CA  . LEU A 1 183 ? -0.176  -2.926  11.718  1.00 9.06   ? 184 LEU A CA  1 
ATOM   1599 C  C   . LEU A 1 183 ? -0.318  -3.173  13.222  1.00 8.65   ? 184 LEU A C   1 
ATOM   1600 O  O   . LEU A 1 183 ? 0.589   -3.756  13.838  1.00 10.82  ? 184 LEU A O   1 
ATOM   1601 C  CB  . LEU A 1 183 ? 1.143   -2.217  11.442  1.00 9.03   ? 184 LEU A CB  1 
ATOM   1602 C  CG  . LEU A 1 183 ? 1.440   -2.056  9.952   1.00 10.06  ? 184 LEU A CG  1 
ATOM   1603 C  CD1 . LEU A 1 183 ? 2.705   -1.191  9.841   1.00 12.70  ? 184 LEU A CD1 1 
ATOM   1604 C  CD2 . LEU A 1 183 ? 1.567   -3.394  9.235   1.00 12.55  ? 184 LEU A CD2 1 
ATOM   1605 N  N   . LEU A 1 184 ? -1.379  -2.685  13.848  1.00 9.67   ? 185 LEU A N   1 
ATOM   1606 C  CA  . LEU A 1 184 ? -1.506  -2.731  15.281  1.00 9.61   ? 185 LEU A CA  1 
ATOM   1607 C  C   . LEU A 1 184 ? -2.300  -3.954  15.775  1.00 11.13  ? 185 LEU A C   1 
ATOM   1608 O  O   . LEU A 1 184 ? -3.309  -4.302  15.199  1.00 16.66  ? 185 LEU A O   1 
ATOM   1609 C  CB  . LEU A 1 184 ? -2.242  -1.461  15.784  1.00 10.56  ? 185 LEU A CB  1 
ATOM   1610 C  CG  . LEU A 1 184 ? -1.688  -0.065  15.364  1.00 9.75   ? 185 LEU A CG  1 
ATOM   1611 C  CD1 . LEU A 1 184 ? -2.513  1.054   15.837  1.00 11.85  ? 185 LEU A CD1 1 
ATOM   1612 C  CD2 . LEU A 1 184 ? -0.218  0.007   15.723  1.00 13.61  ? 185 LEU A CD2 1 
ATOM   1613 N  N   . PRO A 1 185 ? -1.896  -4.535  16.914  1.00 8.81   ? 186 PRO A N   1 
ATOM   1614 C  CA  . PRO A 1 185 ? -2.675  -5.621  17.489  1.00 9.27   ? 186 PRO A CA  1 
ATOM   1615 C  C   . PRO A 1 185 ? -3.932  -5.031  18.169  1.00 9.23   ? 186 PRO A C   1 
ATOM   1616 O  O   . PRO A 1 185 ? -4.131  -3.811  18.269  1.00 10.31  ? 186 PRO A O   1 
ATOM   1617 C  CB  . PRO A 1 185 ? -1.705  -6.192  18.530  1.00 9.13   ? 186 PRO A CB  1 
ATOM   1618 C  CG  . PRO A 1 185 ? -0.970  -4.983  19.006  1.00 8.92   ? 186 PRO A CG  1 
ATOM   1619 C  CD  . PRO A 1 185 ? -0.764  -4.137  17.751  1.00 8.14   ? 186 PRO A CD  1 
ATOM   1620 N  N   A GLU A 1 186 ? -4.756  -6.008  18.507  0.50 8.93   ? 187 GLU A N   1 
ATOM   1621 N  N   B GLU A 1 186 ? -4.822  -5.834  18.820  0.50 8.00   ? 187 GLU A N   1 
ATOM   1622 C  CA  A GLU A 1 186 ? -5.960  -5.665  19.167  0.50 9.77   ? 187 GLU A CA  1 
ATOM   1623 C  CA  B GLU A 1 186 ? -6.072  -5.353  19.490  0.50 7.21   ? 187 GLU A CA  1 
ATOM   1624 C  C   A GLU A 1 186 ? -5.722  -4.796  20.471  0.50 8.77   ? 187 GLU A C   1 
ATOM   1625 C  C   B GLU A 1 186 ? -5.784  -4.599  20.730  0.50 8.74   ? 187 GLU A C   1 
ATOM   1626 O  O   A GLU A 1 186 ? -6.245  -3.665  20.552  0.50 9.57   ? 187 GLU A O   1 
ATOM   1627 O  O   B GLU A 1 186 ? -6.341  -3.536  21.051  0.50 8.90   ? 187 GLU A O   1 
ATOM   1628 C  CB  A GLU A 1 186 ? -6.757  -6.910  19.362  0.50 12.43  ? 187 GLU A CB  1 
ATOM   1629 C  CB  B GLU A 1 186 ? -6.911  -6.555  19.853  0.50 7.26   ? 187 GLU A CB  1 
ATOM   1630 C  CG  A GLU A 1 186 ? -7.950  -6.664  20.219  0.50 21.33  ? 187 GLU A CG  1 
ATOM   1631 C  CG  B GLU A 1 186 ? -7.489  -7.356  18.619  0.50 8.61   ? 187 GLU A CG  1 
ATOM   1632 C  CD  A GLU A 1 186 ? -8.433  -7.926  20.899  0.50 21.86  ? 187 GLU A CD  1 
ATOM   1633 C  CD  B GLU A 1 186 ? -8.223  -8.665  19.023  0.50 10.87  ? 187 GLU A CD  1 
ATOM   1634 O  OE1 A GLU A 1 186 ? -8.460  -8.936  20.131  0.50 22.23  ? 187 GLU A OE1 1 
ATOM   1635 O  OE1 B GLU A 1 186 ? -8.235  -8.987  20.227  0.50 12.85  ? 187 GLU A OE1 1 
ATOM   1636 O  OE2 A GLU A 1 186 ? -8.737  -7.884  22.155  0.50 24.31  ? 187 GLU A OE2 1 
ATOM   1637 O  OE2 B GLU A 1 186 ? -8.805  -9.315  18.173  0.50 13.78  ? 187 GLU A OE2 1 
ATOM   1638 N  N   . SER A 1 187 ? -4.901  -5.247  21.472  1.00 9.12   ? 188 SER A N   1 
ATOM   1639 C  CA  . SER A 1 187 ? -4.672  -4.653  22.751  1.00 9.43   ? 188 SER A CA  1 
ATOM   1640 C  C   . SER A 1 187 ? -3.540  -3.642  22.725  1.00 8.82   ? 188 SER A C   1 
ATOM   1641 O  O   . SER A 1 187 ? -2.506  -3.891  22.055  1.00 9.90   ? 188 SER A O   1 
ATOM   1642 C  CB  . SER A 1 187 ? -4.273  -5.743  23.740  1.00 10.55  ? 188 SER A CB  1 
ATOM   1643 O  OG  . SER A 1 187 ? -4.030  -5.175  25.046  1.00 10.97  ? 188 SER A OG  1 
ATOM   1644 N  N   . LEU A 1 188 ? -3.681  -2.560  23.488  1.00 9.50   ? 189 LEU A N   1 
ATOM   1645 C  CA  . LEU A 1 188 ? -2.641  -1.608  23.736  1.00 9.50   ? 189 LEU A CA  1 
ATOM   1646 C  C   . LEU A 1 188 ? -1.965  -1.828  25.095  1.00 9.42   ? 189 LEU A C   1 
ATOM   1647 O  O   . LEU A 1 188 ? -1.235  -0.928  25.533  1.00 11.40  ? 189 LEU A O   1 
ATOM   1648 C  CB  . LEU A 1 188 ? -3.105  -0.165  23.611  1.00 12.21  ? 189 LEU A CB  1 
ATOM   1649 C  CG  . LEU A 1 188 ? -3.555  0.237   22.230  1.00 12.45  ? 189 LEU A CG  1 
ATOM   1650 C  CD1 . LEU A 1 188 ? -4.099  1.696   22.317  1.00 17.24  ? 189 LEU A CD1 1 
ATOM   1651 C  CD2 . LEU A 1 188 ? -2.445  0.096   21.202  1.00 12.96  ? 189 LEU A CD2 1 
ATOM   1652 N  N   . ASP A 1 189 ? -2.108  -3.011  25.703  1.00 9.25   ? 190 ASP A N   1 
ATOM   1653 C  CA  . ASP A 1 189 ? -1.340  -3.252  26.916  1.00 9.39   ? 190 ASP A CA  1 
ATOM   1654 C  C   . ASP A 1 189 ? 0.152   -3.189  26.561  1.00 7.68   ? 190 ASP A C   1 
ATOM   1655 O  O   . ASP A 1 189 ? 0.574   -3.692  25.511  1.00 7.87   ? 190 ASP A O   1 
ATOM   1656 C  CB  . ASP A 1 189 ? -1.634  -4.682  27.446  1.00 12.35  ? 190 ASP A CB  1 
ATOM   1657 C  CG  . ASP A 1 189 ? -3.005  -4.869  28.105  1.00 15.05  ? 190 ASP A CG  1 
ATOM   1658 O  OD1 . ASP A 1 189 ? -3.623  -3.889  28.433  1.00 18.99  ? 190 ASP A OD1 1 
ATOM   1659 O  OD2 . ASP A 1 189 ? -3.384  -5.993  28.318  1.00 23.03  ? 190 ASP A OD2 1 
ATOM   1660 N  N   . TYR A 1 190 ? 0.941   -2.594  27.476  1.00 7.99   ? 191 TYR A N   1 
ATOM   1661 C  CA  . TYR A 1 190 ? 2.343   -2.335  27.128  1.00 7.22   ? 191 TYR A CA  1 
ATOM   1662 C  C   . TYR A 1 190 ? 3.251   -2.389  28.338  1.00 6.71   ? 191 TYR A C   1 
ATOM   1663 O  O   . TYR A 1 190 ? 2.788   -2.266  29.514  1.00 7.41   ? 191 TYR A O   1 
ATOM   1664 C  CB  . TYR A 1 190 ? 2.489   -0.951  26.426  1.00 7.85   ? 191 TYR A CB  1 
ATOM   1665 C  CG  . TYR A 1 190 ? 2.137   0.211   27.287  1.00 7.81   ? 191 TYR A CG  1 
ATOM   1666 C  CD1 . TYR A 1 190 ? 3.073   0.805   28.146  1.00 8.70   ? 191 TYR A CD1 1 
ATOM   1667 C  CD2 . TYR A 1 190 ? 0.874   0.787   27.253  1.00 8.54   ? 191 TYR A CD2 1 
ATOM   1668 C  CE1 . TYR A 1 190 ? 2.716   1.868   28.976  1.00 9.00   ? 191 TYR A CE1 1 
ATOM   1669 C  CE2 . TYR A 1 190 ? 0.485   1.838   28.063  1.00 9.02   ? 191 TYR A CE2 1 
ATOM   1670 C  CZ  . TYR A 1 190 ? 1.415   2.384   28.940  1.00 9.38   ? 191 TYR A CZ  1 
ATOM   1671 O  OH  . TYR A 1 190 ? 1.115   3.394   29.798  1.00 10.59  ? 191 TYR A OH  1 
ATOM   1672 N  N   . TRP A 1 191 ? 4.533   -2.514  28.052  1.00 6.24   ? 192 TRP A N   1 
ATOM   1673 C  CA  . TRP A 1 191 ? 5.614   -2.247  28.974  1.00 6.37   ? 192 TRP A CA  1 
ATOM   1674 C  C   . TRP A 1 191 ? 6.328   -0.959  28.547  1.00 6.32   ? 192 TRP A C   1 
ATOM   1675 O  O   . TRP A 1 191 ? 6.385   -0.652  27.355  1.00 7.42   ? 192 TRP A O   1 
ATOM   1676 C  CB  . TRP A 1 191 ? 6.621   -3.385  28.960  1.00 6.92   ? 192 TRP A CB  1 
ATOM   1677 C  CG  . TRP A 1 191 ? 6.068   -4.715  29.379  1.00 6.77   ? 192 TRP A CG  1 
ATOM   1678 C  CD1 . TRP A 1 191 ? 5.829   -5.143  30.667  1.00 8.01   ? 192 TRP A CD1 1 
ATOM   1679 C  CD2 . TRP A 1 191 ? 5.799   -5.831  28.535  1.00 7.00   ? 192 TRP A CD2 1 
ATOM   1680 N  NE1 . TRP A 1 191 ? 5.384   -6.419  30.670  1.00 8.26   ? 192 TRP A NE1 1 
ATOM   1681 C  CE2 . TRP A 1 191 ? 5.351   -6.867  29.385  1.00 8.05   ? 192 TRP A CE2 1 
ATOM   1682 C  CE3 . TRP A 1 191 ? 5.882   -6.045  27.173  1.00 7.61   ? 192 TRP A CE3 1 
ATOM   1683 C  CZ2 . TRP A 1 191 ? 5.011   -8.134  28.863  1.00 9.61   ? 192 TRP A CZ2 1 
ATOM   1684 C  CZ3 . TRP A 1 191 ? 5.620   -7.271  26.662  1.00 8.86   ? 192 TRP A CZ3 1 
ATOM   1685 C  CH2 . TRP A 1 191 ? 5.188   -8.312  27.490  1.00 9.98   ? 192 TRP A CH2 1 
ATOM   1686 N  N   . THR A 1 192 ? 6.895   -0.242  29.495  1.00 6.01   ? 193 THR A N   1 
ATOM   1687 C  CA  . THR A 1 192 ? 7.606   0.981   29.161  1.00 6.02   ? 193 THR A CA  1 
ATOM   1688 C  C   . THR A 1 192 ? 8.841   1.139   30.023  1.00 5.87   ? 193 THR A C   1 
ATOM   1689 O  O   . THR A 1 192 ? 8.871   0.761   31.200  1.00 6.60   ? 193 THR A O   1 
ATOM   1690 C  CB  . THR A 1 192 ? 6.682   2.198   29.262  1.00 6.20   ? 193 THR A CB  1 
ATOM   1691 O  OG1 . THR A 1 192 ? 7.358   3.372   28.846  1.00 6.61   ? 193 THR A OG1 1 
ATOM   1692 C  CG2 . THR A 1 192 ? 6.141   2.417   30.690  1.00 7.58   ? 193 THR A CG2 1 
ATOM   1693 N  N   . TYR A 1 193 ? 9.881   1.740   29.441  1.00 5.99   ? 194 TYR A N   1 
ATOM   1694 C  CA  . TYR A 1 193 ? 11.102  2.044   30.157  1.00 6.04   ? 194 TYR A CA  1 
ATOM   1695 C  C   . TYR A 1 193 ? 11.859  3.113   29.365  1.00 5.85   ? 194 TYR A C   1 
ATOM   1696 O  O   . TYR A 1 193 ? 11.653  3.271   28.158  1.00 6.16   ? 194 TYR A O   1 
ATOM   1697 C  CB  . TYR A 1 193 ? 11.962  0.749   30.351  1.00 6.55   ? 194 TYR A CB  1 
ATOM   1698 C  CG  . TYR A 1 193 ? 12.627  0.279   29.085  1.00 6.07   ? 194 TYR A CG  1 
ATOM   1699 C  CD1 . TYR A 1 193 ? 11.938  -0.456  28.113  1.00 6.00   ? 194 TYR A CD1 1 
ATOM   1700 C  CD2 . TYR A 1 193 ? 13.946  0.607   28.838  1.00 6.41   ? 194 TYR A CD2 1 
ATOM   1701 C  CE1 . TYR A 1 193 ? 12.549  -0.804  26.916  1.00 5.72   ? 194 TYR A CE1 1 
ATOM   1702 C  CE2 . TYR A 1 193 ? 14.573  0.267   27.635  1.00 6.24   ? 194 TYR A CE2 1 
ATOM   1703 C  CZ  . TYR A 1 193 ? 13.859  -0.426  26.677  1.00 5.75   ? 194 TYR A CZ  1 
ATOM   1704 O  OH  . TYR A 1 193 ? 14.522  -0.718  25.506  1.00 6.02   ? 194 TYR A OH  1 
ATOM   1705 N  N   . PRO A 1 194 ? 12.793  3.792   30.036  1.00 6.44   ? 195 PRO A N   1 
ATOM   1706 C  CA  . PRO A 1 194 ? 13.627  4.802   29.344  1.00 6.41   ? 195 PRO A CA  1 
ATOM   1707 C  C   . PRO A 1 194 ? 14.825  4.123   28.676  1.00 6.09   ? 195 PRO A C   1 
ATOM   1708 O  O   . PRO A 1 194 ? 15.549  3.363   29.316  1.00 6.59   ? 195 PRO A O   1 
ATOM   1709 C  CB  . PRO A 1 194 ? 14.122  5.713   30.487  1.00 7.67   ? 195 PRO A CB  1 
ATOM   1710 C  CG  . PRO A 1 194 ? 14.142  4.804   31.679  1.00 8.35   ? 195 PRO A CG  1 
ATOM   1711 C  CD  . PRO A 1 194 ? 12.979  3.829   31.500  1.00 7.97   ? 195 PRO A CD  1 
ATOM   1712 N  N   . GLY A 1 195 ? 15.046  4.446   27.405  1.00 5.98   ? 196 GLY A N   1 
ATOM   1713 C  CA  . GLY A 1 195 ? 16.132  3.795   26.670  1.00 6.13   ? 196 GLY A CA  1 
ATOM   1714 C  C   . GLY A 1 195 ? 16.695  4.666   25.582  1.00 5.88   ? 196 GLY A C   1 
ATOM   1715 O  O   . GLY A 1 195 ? 16.829  5.903   25.725  1.00 6.23   ? 196 GLY A O   1 
ATOM   1716 N  N   . SER A 1 196 ? 17.093  3.997   24.503  1.00 5.75   ? 197 SER A N   1 
ATOM   1717 C  CA  . SER A 1 196 ? 17.920  4.613   23.507  1.00 5.91   ? 197 SER A CA  1 
ATOM   1718 C  C   . SER A 1 196 ? 17.493  4.179   22.105  1.00 5.55   ? 197 SER A C   1 
ATOM   1719 O  O   . SER A 1 196 ? 16.723  3.217   21.933  1.00 5.60   ? 197 SER A O   1 
ATOM   1720 C  CB  . SER A 1 196 ? 19.403  4.224   23.672  1.00 6.41   ? 197 SER A CB  1 
ATOM   1721 O  OG  . SER A 1 196 ? 19.668  2.893   23.268  1.00 6.01   ? 197 SER A OG  1 
ATOM   1722 N  N   . LEU A 1 197 ? 18.043  4.844   21.098  1.00 5.60   ? 198 LEU A N   1 
ATOM   1723 C  CA  . LEU A 1 197 ? 18.072  4.284   19.770  1.00 5.85   ? 198 LEU A CA  1 
ATOM   1724 C  C   . LEU A 1 197 ? 18.840  2.963   19.829  1.00 5.33   ? 198 LEU A C   1 
ATOM   1725 O  O   . LEU A 1 197 ? 19.854  2.845   20.526  1.00 5.90   ? 198 LEU A O   1 
ATOM   1726 C  CB  . LEU A 1 197 ? 18.755  5.257   18.809  1.00 6.41   ? 198 LEU A CB  1 
ATOM   1727 C  CG  . LEU A 1 197 ? 18.127  6.630   18.727  1.00 7.02   ? 198 LEU A CG  1 
ATOM   1728 C  CD1 . LEU A 1 197 ? 18.913  7.482   17.714  1.00 8.64   ? 198 LEU A CD1 1 
ATOM   1729 C  CD2 . LEU A 1 197 ? 16.662  6.580   18.326  1.00 7.09   ? 198 LEU A CD2 1 
ATOM   1730 N  N   . THR A 1 198 ? 18.371  1.958   19.071  1.00 5.48   ? 199 THR A N   1 
ATOM   1731 C  CA  . THR A 1 198 ? 18.965  0.626   19.111  1.00 5.52   ? 199 THR A CA  1 
ATOM   1732 C  C   . THR A 1 198 ? 20.095  0.398   18.125  1.00 6.14   ? 199 THR A C   1 
ATOM   1733 O  O   . THR A 1 198 ? 20.629  -0.727  18.076  1.00 6.24   ? 199 THR A O   1 
ATOM   1734 C  CB  . THR A 1 198 ? 17.924  -0.458  18.942  1.00 5.55   ? 199 THR A CB  1 
ATOM   1735 O  OG1 . THR A 1 198 ? 17.422  -0.322  17.604  1.00 5.44   ? 199 THR A OG1 1 
ATOM   1736 C  CG2 . THR A 1 198 ? 16.807  -0.392  19.969  1.00 6.23   ? 199 THR A CG2 1 
ATOM   1737 N  N   . HIS A 1 199 ? 20.442  1.396   17.344  1.00 6.07   ? 200 HIS A N   1 
ATOM   1738 C  CA  . HIS A 1 199 ? 21.612  1.307   16.476  1.00 6.82   ? 200 HIS A CA  1 
ATOM   1739 C  C   . HIS A 1 199 ? 22.198  2.693   16.409  1.00 6.55   ? 200 HIS A C   1 
ATOM   1740 O  O   . HIS A 1 199 ? 21.605  3.667   16.879  1.00 6.66   ? 200 HIS A O   1 
ATOM   1741 C  CB  . HIS A 1 199 ? 21.320  0.673   15.106  1.00 7.14   ? 200 HIS A CB  1 
ATOM   1742 C  CG  . HIS A 1 199 ? 20.141  1.218   14.420  1.00 7.57   ? 200 HIS A CG  1 
ATOM   1743 N  ND1 . HIS A 1 199 ? 18.828  0.734   14.719  1.00 11.35  ? 200 HIS A ND1 1 
ATOM   1744 C  CD2 . HIS A 1 199 ? 19.945  2.179   13.453  1.00 10.81  ? 200 HIS A CD2 1 
ATOM   1745 C  CE1 . HIS A 1 199 ? 17.935  1.360   13.968  1.00 10.55  ? 200 HIS A CE1 1 
ATOM   1746 N  NE2 . HIS A 1 199 ? 18.570  2.229   13.105  1.00 11.30  ? 200 HIS A NE2 1 
ATOM   1747 N  N   . PRO A 1 200 ? 23.421  2.833   15.864  1.00 7.09   ? 201 PRO A N   1 
ATOM   1748 C  CA  . PRO A 1 200 ? 24.079  4.131   15.831  1.00 7.55   ? 201 PRO A CA  1 
ATOM   1749 C  C   . PRO A 1 200 ? 23.168  5.168   15.216  1.00 7.68   ? 201 PRO A C   1 
ATOM   1750 O  O   . PRO A 1 200 ? 22.511  4.930   14.205  1.00 8.50   ? 201 PRO A O   1 
ATOM   1751 C  CB  . PRO A 1 200 ? 25.325  3.854   15.019  1.00 8.95   ? 201 PRO A CB  1 
ATOM   1752 C  CG  . PRO A 1 200 ? 25.693  2.455   15.434  1.00 9.11   ? 201 PRO A CG  1 
ATOM   1753 C  CD  . PRO A 1 200 ? 24.345  1.738   15.398  1.00 7.96   ? 201 PRO A CD  1 
ATOM   1754 N  N   . PRO A 1 201 ? 23.106  6.342   15.841  1.00 8.10   ? 202 PRO A N   1 
ATOM   1755 C  CA  . PRO A 1 201 ? 24.052  6.867   16.841  1.00 8.12   ? 202 PRO A CA  1 
ATOM   1756 C  C   . PRO A 1 201 ? 23.725  6.557   18.294  1.00 7.61   ? 202 PRO A C   1 
ATOM   1757 O  O   . PRO A 1 201 ? 24.370  7.079   19.185  1.00 8.73   ? 202 PRO A O   1 
ATOM   1758 C  CB  . PRO A 1 201 ? 24.043  8.380   16.558  1.00 9.86   ? 202 PRO A CB  1 
ATOM   1759 C  CG  . PRO A 1 201 ? 22.616  8.633   16.165  1.00 10.84  ? 202 PRO A CG  1 
ATOM   1760 C  CD  . PRO A 1 201 ? 22.283  7.446   15.274  1.00 9.39   ? 202 PRO A CD  1 
ATOM   1761 N  N   . LEU A 1 202 ? 22.719  5.702   18.584  1.00 7.06   ? 203 LEU A N   1 
ATOM   1762 C  CA  . LEU A 1 202 ? 22.512  5.135   19.917  1.00 6.83   ? 203 LEU A CA  1 
ATOM   1763 C  C   . LEU A 1 202 ? 22.094  6.177   20.934  1.00 6.58   ? 203 LEU A C   1 
ATOM   1764 O  O   . LEU A 1 202 ? 22.211  5.942   22.146  1.00 7.36   ? 203 LEU A O   1 
ATOM   1765 C  CB  . LEU A 1 202 ? 23.730  4.325   20.392  1.00 7.07   ? 203 LEU A CB  1 
ATOM   1766 C  CG  . LEU A 1 202 ? 24.054  3.097   19.548  1.00 7.07   ? 203 LEU A CG  1 
ATOM   1767 C  CD1 . LEU A 1 202 ? 25.423  2.544   19.959  1.00 9.79   ? 203 LEU A CD1 1 
ATOM   1768 C  CD2 . LEU A 1 202 ? 23.031  1.991   19.734  1.00 7.62   ? 203 LEU A CD2 1 
ATOM   1769 N  N   . TYR A 1 203 ? 21.527  7.291   20.488  1.00 7.13   ? 204 TYR A N   1 
ATOM   1770 C  CA  . TYR A 1 203 ? 21.210  8.375   21.403  1.00 7.47   ? 204 TYR A CA  1 
ATOM   1771 C  C   . TYR A 1 203 ? 20.232  7.898   22.476  1.00 6.73   ? 204 TYR A C   1 
ATOM   1772 O  O   . TYR A 1 203 ? 19.274  7.168   22.229  1.00 6.66   ? 204 TYR A O   1 
ATOM   1773 C  CB  . TYR A 1 203 ? 20.495  9.504   20.640  1.00 8.31   ? 204 TYR A CB  1 
ATOM   1774 C  CG  . TYR A 1 203 ? 21.302  10.239  19.604  1.00 9.31   ? 204 TYR A CG  1 
ATOM   1775 C  CD1 . TYR A 1 203 ? 22.702  10.381  19.692  1.00 10.89  ? 204 TYR A CD1 1 
ATOM   1776 C  CD2 . TYR A 1 203 ? 20.634  10.834  18.566  1.00 12.57  ? 204 TYR A CD2 1 
ATOM   1777 C  CE1 . TYR A 1 203 ? 23.371  11.158  18.772  1.00 13.49  ? 204 TYR A CE1 1 
ATOM   1778 C  CE2 . TYR A 1 203 ? 21.348  11.528  17.593  1.00 15.71  ? 204 TYR A CE2 1 
ATOM   1779 C  CZ  . TYR A 1 203 ? 22.698  11.712  17.715  1.00 14.65  ? 204 TYR A CZ  1 
ATOM   1780 O  OH  . TYR A 1 203 ? 23.357  12.438  16.759  1.00 21.32  ? 204 TYR A OH  1 
ATOM   1781 N  N   . GLU A 1 204 ? 20.450  8.407   23.692  1.00 6.95   ? 205 GLU A N   1 
ATOM   1782 C  CA  . GLU A 1 204 ? 19.629  8.086   24.845  1.00 7.32   ? 205 GLU A CA  1 
ATOM   1783 C  C   . GLU A 1 204 ? 18.467  9.058   24.965  1.00 7.21   ? 205 GLU A C   1 
ATOM   1784 O  O   . GLU A 1 204 ? 18.348  9.842   25.897  1.00 8.66   ? 205 GLU A O   1 
ATOM   1785 C  CB  . GLU A 1 204 ? 20.507  7.995   26.093  1.00 7.93   ? 205 GLU A CB  1 
ATOM   1786 C  CG  . GLU A 1 204 ? 21.352  6.741   26.021  1.00 7.80   ? 205 GLU A CG  1 
ATOM   1787 C  CD  . GLU A 1 204 ? 22.252  6.490   27.193  1.00 8.28   ? 205 GLU A CD  1 
ATOM   1788 O  OE1 . GLU A 1 204 ? 22.592  7.434   27.943  1.00 9.80   ? 205 GLU A OE1 1 
ATOM   1789 O  OE2 . GLU A 1 204 ? 22.641  5.290   27.391  1.00 8.53   ? 205 GLU A OE2 1 
ATOM   1790 N  N   . CYS A 1 205 ? 17.580  8.977   23.984  1.00 6.69   ? 206 CYS A N   1 
ATOM   1791 C  CA  . CYS A 1 205 ? 16.528  9.969   23.752  1.00 6.80   ? 206 CYS A CA  1 
ATOM   1792 C  C   . CYS A 1 205 ? 15.143  9.342   23.691  1.00 6.27   ? 206 CYS A C   1 
ATOM   1793 O  O   . CYS A 1 205 ? 14.209  10.049  23.316  1.00 7.17   ? 206 CYS A O   1 
ATOM   1794 C  CB  . CYS A 1 205 ? 16.798  10.790  22.507  1.00 7.98   ? 206 CYS A CB  1 
ATOM   1795 S  SG  . CYS A 1 205 ? 16.823  9.798   20.972  1.00 7.50   ? 206 CYS A SG  1 
ATOM   1796 N  N   . VAL A 1 206 ? 14.978  8.053   24.000  1.00 6.02   ? 207 VAL A N   1 
ATOM   1797 C  CA  . VAL A 1 206 ? 13.767  7.346   23.681  1.00 5.95   ? 207 VAL A CA  1 
ATOM   1798 C  C   . VAL A 1 206 ? 13.015  6.885   24.923  1.00 5.83   ? 207 VAL A C   1 
ATOM   1799 O  O   . VAL A 1 206 ? 13.601  6.210   25.775  1.00 7.13   ? 207 VAL A O   1 
ATOM   1800 C  CB  . VAL A 1 206 ? 14.048  6.073   22.810  1.00 6.56   ? 207 VAL A CB  1 
ATOM   1801 C  CG1 . VAL A 1 206 ? 12.755  5.350   22.512  1.00 6.39   ? 207 VAL A CG1 1 
ATOM   1802 C  CG2 . VAL A 1 206 ? 14.778  6.437   21.530  1.00 6.88   ? 207 VAL A CG2 1 
ATOM   1803 N  N   . THR A 1 207 ? 11.710  7.178   24.987  1.00 5.68   ? 208 THR A N   1 
ATOM   1804 C  CA  . THR A 1 207 ? 10.795  6.452   25.866  1.00 6.09   ? 208 THR A CA  1 
ATOM   1805 C  C   . THR A 1 207 ? 10.260  5.274   25.049  1.00 5.39   ? 208 THR A C   1 
ATOM   1806 O  O   . THR A 1 207 ? 9.598   5.481   24.018  1.00 5.85   ? 208 THR A O   1 
ATOM   1807 C  CB  . THR A 1 207 ? 9.644   7.311   26.335  1.00 6.67   ? 208 THR A CB  1 
ATOM   1808 O  OG1 . THR A 1 207 ? 10.125  8.443   27.034  1.00 7.39   ? 208 THR A OG1 1 
ATOM   1809 C  CG2 . THR A 1 207 ? 8.714   6.480   27.223  1.00 7.83   ? 208 THR A CG2 1 
ATOM   1810 N  N   . TRP A 1 208 ? 10.583  4.053   25.469  1.00 5.50   ? 209 TRP A N   1 
ATOM   1811 C  CA  . TRP A 1 208 ? 10.115  2.865   24.816  1.00 5.18   ? 209 TRP A CA  1 
ATOM   1812 C  C   . TRP A 1 208 ? 8.757   2.448   25.352  1.00 5.17   ? 209 TRP A C   1 
ATOM   1813 O  O   . TRP A 1 208 ? 8.547   2.405   26.568  1.00 5.55   ? 209 TRP A O   1 
ATOM   1814 C  CB  . TRP A 1 208 ? 11.111  1.711   25.025  1.00 5.23   ? 209 TRP A CB  1 
ATOM   1815 C  CG  . TRP A 1 208 ? 12.237  1.828   24.028  1.00 5.39   ? 209 TRP A CG  1 
ATOM   1816 C  CD1 . TRP A 1 208 ? 13.461  2.380   24.201  1.00 5.96   ? 209 TRP A CD1 1 
ATOM   1817 C  CD2 . TRP A 1 208 ? 12.155  1.410   22.676  1.00 5.30   ? 209 TRP A CD2 1 
ATOM   1818 N  NE1 . TRP A 1 208 ? 14.148  2.376   23.035  1.00 6.31   ? 209 TRP A NE1 1 
ATOM   1819 C  CE2 . TRP A 1 208 ? 13.382  1.779   22.054  1.00 5.71   ? 209 TRP A CE2 1 
ATOM   1820 C  CE3 . TRP A 1 208 ? 11.185  0.785   21.917  1.00 5.65   ? 209 TRP A CE3 1 
ATOM   1821 C  CZ2 . TRP A 1 208 ? 13.637  1.553   20.699  1.00 6.21   ? 209 TRP A CZ2 1 
ATOM   1822 C  CZ3 . TRP A 1 208 ? 11.429  0.530   20.566  1.00 6.45   ? 209 TRP A CZ3 1 
ATOM   1823 C  CH2 . TRP A 1 208 ? 12.642  0.919   19.989  1.00 6.71   ? 209 TRP A CH2 1 
ATOM   1824 N  N   . ILE A 1 209 ? 7.857   2.111   24.434  1.00 5.27   ? 210 ILE A N   1 
ATOM   1825 C  CA  . ILE A 1 209 ? 6.542   1.585   24.744  1.00 5.50   ? 210 ILE A CA  1 
ATOM   1826 C  C   . ILE A 1 209 ? 6.412   0.331   23.905  1.00 5.24   ? 210 ILE A C   1 
ATOM   1827 O  O   . ILE A 1 209 ? 6.322   0.420   22.685  1.00 6.17   ? 210 ILE A O   1 
ATOM   1828 C  CB  . ILE A 1 209 ? 5.446   2.618   24.435  1.00 6.12   ? 210 ILE A CB  1 
ATOM   1829 C  CG1 . ILE A 1 209 ? 5.667   3.880   25.247  1.00 7.64   ? 210 ILE A CG1 1 
ATOM   1830 C  CG2 . ILE A 1 209 ? 4.076   1.999   24.675  1.00 7.13   ? 210 ILE A CG2 1 
ATOM   1831 C  CD1 . ILE A 1 209 ? 4.850   5.077   24.788  1.00 9.48   ? 210 ILE A CD1 1 
ATOM   1832 N  N   . VAL A 1 210 ? 6.467   -0.848  24.537  1.00 5.33   ? 211 VAL A N   1 
ATOM   1833 C  CA  . VAL A 1 210 ? 6.498   -2.136  23.850  1.00 5.47   ? 211 VAL A CA  1 
ATOM   1834 C  C   . VAL A 1 210 ? 5.188   -2.828  24.112  1.00 5.42   ? 211 VAL A C   1 
ATOM   1835 O  O   . VAL A 1 210 ? 4.862   -3.122  25.274  1.00 6.21   ? 211 VAL A O   1 
ATOM   1836 C  CB  . VAL A 1 210 ? 7.711   -2.965  24.274  1.00 6.04   ? 211 VAL A CB  1 
ATOM   1837 C  CG1 . VAL A 1 210 ? 7.687   -4.315  23.578  1.00 7.17   ? 211 VAL A CG1 1 
ATOM   1838 C  CG2 . VAL A 1 210 ? 9.006   -2.226  23.998  1.00 7.19   ? 211 VAL A CG2 1 
ATOM   1839 N  N   . LEU A 1 211 ? 4.411   -3.087  23.067  1.00 6.02   ? 212 LEU A N   1 
ATOM   1840 C  CA  . LEU A 1 211 ? 3.127   -3.751  23.266  1.00 6.21   ? 212 LEU A CA  1 
ATOM   1841 C  C   . LEU A 1 211 ? 3.315   -5.220  23.605  1.00 6.30   ? 212 LEU A C   1 
ATOM   1842 O  O   . LEU A 1 211 ? 4.184   -5.915  23.069  1.00 7.09   ? 212 LEU A O   1 
ATOM   1843 C  CB  . LEU A 1 211 ? 2.263   -3.628  21.994  1.00 6.80   ? 212 LEU A CB  1 
ATOM   1844 C  CG  . LEU A 1 211 ? 1.904   -2.207  21.603  1.00 7.37   ? 212 LEU A CG  1 
ATOM   1845 C  CD1 . LEU A 1 211 ? 0.860   -2.243  20.452  1.00 9.18   ? 212 LEU A CD1 1 
ATOM   1846 C  CD2 . LEU A 1 211 ? 1.402   -1.381  22.727  1.00 8.28   ? 212 LEU A CD2 1 
ATOM   1847 N  N   . LYS A 1 212 ? 2.461   -5.708  24.514  1.00 7.00   ? 213 LYS A N   1 
ATOM   1848 C  CA  . LYS A 1 212 ? 2.510   -7.099  24.907  1.00 8.15   ? 213 LYS A CA  1 
ATOM   1849 C  C   . LYS A 1 212 ? 2.024   -8.044  23.824  1.00 7.25   ? 213 LYS A C   1 
ATOM   1850 O  O   . LYS A 1 212 ? 2.555   -9.152  23.667  1.00 9.22   ? 213 LYS A O   1 
ATOM   1851 C  CB  . LYS A 1 212 ? 1.736   -7.331  26.163  1.00 9.64   ? 213 LYS A CB  1 
ATOM   1852 C  CG  . LYS A 1 212 ? 1.622   -8.807  26.592  1.00 12.00  ? 213 LYS A CG  1 
ATOM   1853 C  CD  . LYS A 1 212 ? 1.031   -8.976  27.931  1.00 18.34  ? 213 LYS A CD  1 
ATOM   1854 C  CE  . LYS A 1 212 ? 0.593   -10.344 28.286  1.00 25.71  ? 213 LYS A CE  1 
ATOM   1855 N  NZ  . LYS A 1 212 ? -0.094  -10.331 29.620  1.00 43.26  ? 213 LYS A NZ  1 
ATOM   1856 N  N   A GLU A 1 213 ? 0.962   -7.614  23.097  0.50 6.73   ? 214 GLU A N   1 
ATOM   1857 N  N   B GLU A 1 213 ? 0.964   -7.699  23.063  0.50 6.92   ? 214 GLU A N   1 
ATOM   1858 C  CA  A GLU A 1 213 ? 0.315   -8.456  22.112  0.50 6.36   ? 214 GLU A CA  1 
ATOM   1859 C  CA  B GLU A 1 213 ? 0.414   -8.640  22.107  0.50 7.67   ? 214 GLU A CA  1 
ATOM   1860 C  C   A GLU A 1 213 ? 1.101   -8.451  20.756  0.50 6.80   ? 214 GLU A C   1 
ATOM   1861 C  C   B GLU A 1 213 ? 1.156   -8.447  20.847  0.50 7.63   ? 214 GLU A C   1 
ATOM   1862 O  O   A GLU A 1 213 ? 1.187   -7.439  20.071  0.50 6.01   ? 214 GLU A O   1 
ATOM   1863 O  O   B GLU A 1 213 ? 1.187   -7.311  20.347  0.50 6.65   ? 214 GLU A O   1 
ATOM   1864 C  CB  A GLU A 1 213 ? -1.156  -7.996  21.937  0.50 7.05   ? 214 GLU A CB  1 
ATOM   1865 C  CB  B GLU A 1 213 ? -1.032  -8.324  21.824  0.50 7.72   ? 214 GLU A CB  1 
ATOM   1866 C  CG  A GLU A 1 213 ? -1.928  -8.935  20.988  0.50 6.75   ? 214 GLU A CG  1 
ATOM   1867 C  CG  B GLU A 1 213 ? -1.679  -9.336  20.890  0.50 10.64  ? 214 GLU A CG  1 
ATOM   1868 C  CD  A GLU A 1 213 ? -3.389  -8.465  20.741  0.50 7.89   ? 214 GLU A CD  1 
ATOM   1869 C  CD  B GLU A 1 213 ? -3.186  -9.101  20.723  0.50 10.74  ? 214 GLU A CD  1 
ATOM   1870 O  OE1 A GLU A 1 213 ? -3.888  -8.521  19.575  0.50 10.08  ? 214 GLU A OE1 1 
ATOM   1871 O  OE1 B GLU A 1 213 ? -3.763  -8.055  21.133  0.50 9.44   ? 214 GLU A OE1 1 
ATOM   1872 O  OE2 A GLU A 1 213 ? -3.962  -7.929  21.706  0.50 8.74   ? 214 GLU A OE2 1 
ATOM   1873 O  OE2 B GLU A 1 213 ? -3.832  -9.984  20.135  0.50 14.99  ? 214 GLU A OE2 1 
ATOM   1874 N  N   A PRO A 1 214 ? 1.629   -9.585  20.308  0.50 6.77   ? 215 PRO A N   1 
ATOM   1875 N  N   B PRO A 1 214 ? 1.720   -9.532  20.313  0.50 7.56   ? 215 PRO A N   1 
ATOM   1876 C  CA  A PRO A 1 214 ? 2.238   -9.497  18.975  0.50 6.85   ? 215 PRO A CA  1 
ATOM   1877 C  CA  B PRO A 1 214 ? 2.365   -9.547  18.981  0.50 8.19   ? 215 PRO A CA  1 
ATOM   1878 C  C   A PRO A 1 214 ? 1.209   -9.389  17.918  0.50 6.86   ? 215 PRO A C   1 
ATOM   1879 C  C   B PRO A 1 214 ? 1.339   -9.555  17.876  0.50 7.74   ? 215 PRO A C   1 
ATOM   1880 O  O   A PRO A 1 214 ? -0.001  -9.686  18.152  0.50 7.37   ? 215 PRO A O   1 
ATOM   1881 O  O   B PRO A 1 214 ? 0.237   -10.053 18.034  0.50 8.67   ? 215 PRO A O   1 
ATOM   1882 C  CB  A PRO A 1 214 ? 2.960   -10.842 18.858  0.50 7.35   ? 215 PRO A CB  1 
ATOM   1883 C  CB  B PRO A 1 214 ? 3.149   -10.882 19.016  0.50 9.32   ? 215 PRO A CB  1 
ATOM   1884 C  CG  A PRO A 1 214 ? 2.195   -11.765 19.677  0.50 8.55   ? 215 PRO A CG  1 
ATOM   1885 C  CG  B PRO A 1 214 ? 3.126   -11.353 20.462  0.50 10.98  ? 215 PRO A CG  1 
ATOM   1886 C  CD  A PRO A 1 214 ? 1.570   -11.010 20.809  0.50 8.04   ? 215 PRO A CD  1 
ATOM   1887 C  CD  B PRO A 1 214 ? 1.902   -10.825 21.082  0.50 8.22   ? 215 PRO A CD  1 
ATOM   1888 N  N   . ILE A 1 215 ? 1.668   -9.055  16.717  1.00 7.38   ? 216 ILE A N   1 
ATOM   1889 C  CA  . ILE A 1 215 ? 0.928   -9.302  15.508  1.00 7.42   ? 216 ILE A CA  1 
ATOM   1890 C  C   . ILE A 1 215 ? 1.449   -10.563 14.845  1.00 7.22   ? 216 ILE A C   1 
ATOM   1891 O  O   . ILE A 1 215 ? 2.616   -10.904 14.989  1.00 8.54   ? 216 ILE A O   1 
ATOM   1892 C  CB  . ILE A 1 215 ? 0.895   -8.113  14.541  1.00 8.04   ? 216 ILE A CB  1 
ATOM   1893 C  CG1 . ILE A 1 215 ? 2.279   -7.733  14.046  1.00 7.91   ? 216 ILE A CG1 1 
ATOM   1894 C  CG2 . ILE A 1 215 ? 0.176   -6.917  15.252  1.00 8.73   ? 216 ILE A CG2 1 
ATOM   1895 C  CD1 . ILE A 1 215 ? 2.256   -6.790  12.860  1.00 9.71   ? 216 ILE A CD1 1 
ATOM   1896 N  N   A SER A 1 216 ? 0.566   -11.167 14.042  0.50 8.49   ? 217 SER A N   1 
ATOM   1897 N  N   B SER A 1 216 ? 0.601   -11.318 14.172  0.50 7.86   ? 217 SER A N   1 
ATOM   1898 C  CA  A SER A 1 216 ? 0.883   -12.335 13.228  0.50 7.90   ? 217 SER A CA  1 
ATOM   1899 C  CA  B SER A 1 216 ? 1.145   -12.383 13.355  0.50 8.59   ? 217 SER A CA  1 
ATOM   1900 C  C   A SER A 1 216 ? 1.164   -11.886 11.799  0.50 7.79   ? 217 SER A C   1 
ATOM   1901 C  C   B SER A 1 216 ? 1.191   -11.921 11.918  0.50 8.03   ? 217 SER A C   1 
ATOM   1902 O  O   A SER A 1 216 ? 0.409   -11.122 11.188  0.50 8.08   ? 217 SER A O   1 
ATOM   1903 O  O   B SER A 1 216 ? 0.278   -11.201 11.452  0.50 8.77   ? 217 SER A O   1 
ATOM   1904 C  CB  A SER A 1 216 ? -0.229  -13.386 13.259  0.50 7.20   ? 217 SER A CB  1 
ATOM   1905 C  CB  B SER A 1 216 ? 0.260   -13.592 13.449  0.50 12.80  ? 217 SER A CB  1 
ATOM   1906 O  OG  A SER A 1 216 ? -0.172  -14.117 14.468  0.50 9.89   ? 217 SER A OG  1 
ATOM   1907 O  OG  B SER A 1 216 ? -0.973  -13.270 12.916  0.50 17.78  ? 217 SER A OG  1 
ATOM   1908 N  N   . VAL A 1 217 ? 2.283   -12.351 11.266  1.00 8.05   ? 218 VAL A N   1 
ATOM   1909 C  CA  . VAL A 1 217 ? 2.598   -12.177 9.857   1.00 7.78   ? 218 VAL A CA  1 
ATOM   1910 C  C   . VAL A 1 217 ? 2.844   -13.544 9.247   1.00 8.20   ? 218 VAL A C   1 
ATOM   1911 O  O   . VAL A 1 217 ? 3.216   -14.478 9.978   1.00 8.55   ? 218 VAL A O   1 
ATOM   1912 C  CB  . VAL A 1 217 ? 3.774   -11.224 9.660   1.00 8.73   ? 218 VAL A CB  1 
ATOM   1913 C  CG1 . VAL A 1 217 ? 3.506   -9.891  10.343  1.00 9.83   ? 218 VAL A CG1 1 
ATOM   1914 C  CG2 . VAL A 1 217 ? 5.077   -11.828 10.167  1.00 10.34  ? 218 VAL A CG2 1 
ATOM   1915 N  N   . SER A 1 218 ? 2.734   -13.678 7.941   1.00 8.32   ? 219 SER A N   1 
ATOM   1916 C  CA  . SER A 1 218 ? 2.990   -15.014 7.385   1.00 9.01   ? 219 SER A CA  1 
ATOM   1917 C  C   . SER A 1 218 ? 4.426   -15.252 7.156   1.00 8.94   ? 219 SER A C   1 
ATOM   1918 O  O   . SER A 1 218 ? 5.264   -14.322 7.009   1.00 9.26   ? 219 SER A O   1 
ATOM   1919 C  CB  . SER A 1 218 ? 2.175   -15.210 6.108   1.00 9.41   ? 219 SER A CB  1 
ATOM   1920 O  OG  . SER A 1 218 ? 2.668   -14.331 5.136   1.00 9.85   ? 219 SER A OG  1 
ATOM   1921 N  N   A SER A 1 219 ? 4.857   -16.530 6.868   0.50 8.07   ? 220 SER A N   1 
ATOM   1922 N  N   B SER A 1 219 ? 4.701   -16.560 7.129   0.50 9.37   ? 220 SER A N   1 
ATOM   1923 C  CA  A SER A 1 219 ? 6.275   -16.873 6.538   0.50 8.42   ? 220 SER A CA  1 
ATOM   1924 C  CA  B SER A 1 219 ? 6.022   -16.902 6.763   0.50 10.12  ? 220 SER A CA  1 
ATOM   1925 C  C   A SER A 1 219 ? 6.661   -16.196 5.261   0.50 9.08   ? 220 SER A C   1 
ATOM   1926 C  C   B SER A 1 219 ? 6.497   -16.171 5.469   0.50 9.76   ? 220 SER A C   1 
ATOM   1927 O  O   A SER A 1 219 ? 7.798   -15.778 5.051   0.50 9.76   ? 220 SER A O   1 
ATOM   1928 O  O   B SER A 1 219 ? 7.623   -15.705 5.454   0.50 9.72   ? 220 SER A O   1 
ATOM   1929 C  CB  A SER A 1 219 ? 6.423   -18.383 6.428   0.50 10.57  ? 220 SER A CB  1 
ATOM   1930 C  CB  B SER A 1 219 ? 6.205   -18.410 6.719   0.50 10.81  ? 220 SER A CB  1 
ATOM   1931 O  OG  A SER A 1 219 ? 5.383   -19.001 5.630   0.50 10.70  ? 220 SER A OG  1 
ATOM   1932 O  OG  B SER A 1 219 ? 7.510   -18.798 6.230   0.50 11.79  ? 220 SER A OG  1 
ATOM   1933 N  N   . GLU A 1 220 ? 5.639   -16.111 4.405   1.00 9.99   ? 221 GLU A N   1 
ATOM   1934 C  CA  . GLU A 1 220 ? 5.986   -15.499 3.122   1.00 10.48  ? 221 GLU A CA  1 
ATOM   1935 C  C   . GLU A 1 220 ? 6.217   -13.998 3.238   1.00 10.47  ? 221 GLU A C   1 
ATOM   1936 O  O   . GLU A 1 220 ? 7.061   -13.442 2.516   1.00 11.86  ? 221 GLU A O   1 
ATOM   1937 C  CB  . GLU A 1 220 ? 4.864   -15.704 2.139   1.00 13.45  ? 221 GLU A CB  1 
ATOM   1938 C  CG  . GLU A 1 220 ? 4.668   -17.212 1.740   1.00 16.63  ? 221 GLU A CG  1 
ATOM   1939 C  CD  . GLU A 1 220 ? 3.768   -17.997 2.712   1.00 17.20  ? 221 GLU A CD  1 
ATOM   1940 O  OE1 . GLU A 1 220 ? 3.239   -17.474 3.664   1.00 15.70  ? 221 GLU A OE1 1 
ATOM   1941 O  OE2 . GLU A 1 220 ? 3.610   -19.220 2.462   1.00 28.01  ? 221 GLU A OE2 1 
ATOM   1942 N  N   . GLN A 1 221 ? 5.483   -13.337 4.124   1.00 9.21   ? 222 GLN A N   1 
ATOM   1943 C  CA  . GLN A 1 221 ? 5.725   -11.916 4.344   1.00 9.37   ? 222 GLN A CA  1 
ATOM   1944 C  C   . GLN A 1 221 ? 7.123   -11.686 4.862   1.00 9.26   ? 222 GLN A C   1 
ATOM   1945 O  O   . GLN A 1 221 ? 7.856   -10.812 4.346   1.00 10.10  ? 222 GLN A O   1 
ATOM   1946 C  CB  . GLN A 1 221 ? 4.657   -11.333 5.252   1.00 8.62   ? 222 GLN A CB  1 
ATOM   1947 C  CG  . GLN A 1 221 ? 3.301   -11.246 4.559   1.00 9.09   ? 222 GLN A CG  1 
ATOM   1948 C  CD  . GLN A 1 221 ? 2.181   -10.702 5.408   1.00 8.22   ? 222 GLN A CD  1 
ATOM   1949 O  OE1 . GLN A 1 221 ? 2.053   -11.057 6.585   1.00 8.51   ? 222 GLN A OE1 1 
ATOM   1950 N  NE2 . GLN A 1 221 ? 1.350   -9.844  4.819   1.00 9.52   ? 222 GLN A NE2 1 
ATOM   1951 N  N   . VAL A 1 222 ? 7.559   -12.411 5.913   1.00 9.41   ? 223 VAL A N   1 
ATOM   1952 C  CA  . VAL A 1 222 ? 8.871   -12.174 6.478   1.00 10.28  ? 223 VAL A CA  1 
ATOM   1953 C  C   . VAL A 1 222 ? 9.946   -12.625 5.491   1.00 10.69  ? 223 VAL A C   1 
ATOM   1954 O  O   . VAL A 1 222 ? 11.021  -12.001 5.425   1.00 10.67  ? 223 VAL A O   1 
ATOM   1955 C  CB  . VAL A 1 222 ? 9.032   -12.693 7.906   1.00 10.94  ? 223 VAL A CB  1 
ATOM   1956 C  CG1 . VAL A 1 222 ? 8.893   -14.153 8.056   1.00 14.31  ? 223 VAL A CG1 1 
ATOM   1957 C  CG2 . VAL A 1 222 ? 10.300  -12.151 8.555   1.00 12.41  ? 223 VAL A CG2 1 
ATOM   1958 N  N   A LEU A 1 223 ? 9.685   -13.658 4.785   0.50 10.33  ? 224 LEU A N   1 
ATOM   1959 N  N   B LEU A 1 223 ? 9.717   -13.716 4.668   0.50 10.94  ? 224 LEU A N   1 
ATOM   1960 C  CA  A LEU A 1 223 ? 10.642  -14.064 3.799   0.50 12.19  ? 224 LEU A CA  1 
ATOM   1961 C  CA  B LEU A 1 223 ? 10.661  -14.141 3.664   0.50 13.33  ? 224 LEU A CA  1 
ATOM   1962 C  C   A LEU A 1 223 ? 10.962  -12.978 2.782   0.50 11.74  ? 224 LEU A C   1 
ATOM   1963 C  C   B LEU A 1 223 ? 10.964  -13.005 2.723   0.50 11.61  ? 224 LEU A C   1 
ATOM   1964 O  O   A LEU A 1 223 ? 12.117  -12.866 2.338   0.50 13.13  ? 224 LEU A O   1 
ATOM   1965 O  O   B LEU A 1 223 ? 12.119  -12.861 2.305   0.50 13.18  ? 224 LEU A O   1 
ATOM   1966 C  CB  A LEU A 1 223 ? 10.104  -15.340 3.086   0.50 12.64  ? 224 LEU A CB  1 
ATOM   1967 C  CB  B LEU A 1 223 ? 10.068  -15.336 2.903   0.50 17.24  ? 224 LEU A CB  1 
ATOM   1968 C  CG  A LEU A 1 223 ? 10.368  -16.694 3.780   0.50 13.29  ? 224 LEU A CG  1 
ATOM   1969 C  CG  B LEU A 1 223 ? 10.473  -15.743 1.495   0.50 24.34  ? 224 LEU A CG  1 
ATOM   1970 C  CD1 A LEU A 1 223 ? 9.423   -17.772 3.281   0.50 20.14  ? 224 LEU A CD1 1 
ATOM   1971 C  CD1 B LEU A 1 223 ? 11.895  -15.526 1.103   0.50 23.24  ? 224 LEU A CD1 1 
ATOM   1972 C  CD2 A LEU A 1 223 ? 11.807  -17.141 3.742   0.50 16.48  ? 224 LEU A CD2 1 
ATOM   1973 C  CD2 B LEU A 1 223 ? 10.093  -17.211 1.463   0.50 20.57  ? 224 LEU A CD2 1 
ATOM   1974 N  N   . LYS A 1 224 ? 9.998   -12.156 2.403   1.00 11.11  ? 225 LYS A N   1 
ATOM   1975 C  CA  . LYS A 1 224 ? 10.238  -11.079 1.501   1.00 10.98  ? 225 LYS A CA  1 
ATOM   1976 C  C   . LYS A 1 224 ? 11.084  -9.981  2.128   1.00 10.01  ? 225 LYS A C   1 
ATOM   1977 O  O   . LYS A 1 224 ? 11.883  -9.356  1.444   1.00 10.58  ? 225 LYS A O   1 
ATOM   1978 C  CB  . LYS A 1 224 ? 8.931   -10.608 0.872   1.00 13.06  ? 225 LYS A CB  1 
ATOM   1979 C  CG  . LYS A 1 224 ? 8.377   -11.723 -0.098  1.00 15.78  ? 225 LYS A CG  1 
ATOM   1980 C  CD  . LYS A 1 224 ? 7.106   -11.414 -0.788  1.00 16.51  ? 225 LYS A CD  1 
ATOM   1981 C  CE  . LYS A 1 224 ? 6.735   -12.399 -1.884  1.00 20.62  ? 225 LYS A CE  1 
ATOM   1982 N  NZ  . LYS A 1 224 ? 5.374   -12.059 -2.489  1.00 18.51  ? 225 LYS A NZ  1 
ATOM   1983 N  N   . PHE A 1 225 ? 10.983  -9.768  3.442   1.00 9.24   ? 226 PHE A N   1 
ATOM   1984 C  CA  . PHE A 1 225 ? 11.851  -8.810  4.088   1.00 9.34   ? 226 PHE A CA  1 
ATOM   1985 C  C   . PHE A 1 225 ? 13.315  -9.310  3.900   1.00 8.99   ? 226 PHE A C   1 
ATOM   1986 O  O   . PHE A 1 225 ? 14.235  -8.505  3.708   1.00 9.60   ? 226 PHE A O   1 
ATOM   1987 C  CB  . PHE A 1 225 ? 11.674  -8.776  5.612   1.00 9.39   ? 226 PHE A CB  1 
ATOM   1988 C  CG  . PHE A 1 225 ? 10.460  -8.054  6.141   1.00 8.70   ? 226 PHE A CG  1 
ATOM   1989 C  CD1 . PHE A 1 225 ? 9.436   -7.587  5.339   1.00 13.36  ? 226 PHE A CD1 1 
ATOM   1990 C  CD2 . PHE A 1 225 ? 10.364  -7.876  7.512   1.00 12.16  ? 226 PHE A CD2 1 
ATOM   1991 C  CE1 . PHE A 1 225 ? 8.344   -6.943  5.907   1.00 14.10  ? 226 PHE A CE1 1 
ATOM   1992 C  CE2 . PHE A 1 225 ? 9.285   -7.238  8.086   1.00 13.61  ? 226 PHE A CE2 1 
ATOM   1993 C  CZ  . PHE A 1 225 ? 8.270   -6.770  7.282   1.00 12.55  ? 226 PHE A CZ  1 
ATOM   1994 N  N   . ARG A 1 226 ? 13.545  -10.624 3.949   1.00 9.12   ? 227 ARG A N   1 
ATOM   1995 C  CA  . ARG A 1 226 ? 14.874  -11.190 3.919   1.00 9.48   ? 227 ARG A CA  1 
ATOM   1996 C  C   . ARG A 1 226 ? 15.485  -11.179 2.521   1.00 10.31  ? 227 ARG A C   1 
ATOM   1997 O  O   . ARG A 1 226 ? 16.648  -11.555 2.359   1.00 11.96  ? 227 ARG A O   1 
ATOM   1998 C  CB  . ARG A 1 226 ? 14.826  -12.607 4.443   1.00 9.76   ? 227 ARG A CB  1 
ATOM   1999 C  CG  . ARG A 1 226 ? 14.365  -12.769 5.873   1.00 9.65   ? 227 ARG A CG  1 
ATOM   2000 C  CD  . ARG A 1 226 ? 14.409  -14.227 6.302   1.00 10.72  ? 227 ARG A CD  1 
ATOM   2001 N  NE  . ARG A 1 226 ? 13.846  -14.402 7.621   1.00 9.95   ? 227 ARG A NE  1 
ATOM   2002 C  CZ  . ARG A 1 226 ? 12.887  -15.275 7.930   1.00 10.46  ? 227 ARG A CZ  1 
ATOM   2003 N  NH1 . ARG A 1 226 ? 12.444  -16.131 6.992   1.00 12.91  ? 227 ARG A NH1 1 
ATOM   2004 N  NH2 . ARG A 1 226 ? 12.335  -15.262 9.116   1.00 11.70  ? 227 ARG A NH2 1 
ATOM   2005 N  N   . LYS A 1 227 ? 14.724  -10.754 1.482   1.00 9.61   ? 228 LYS A N   1 
ATOM   2006 C  CA  . LYS A 1 227 ? 15.248  -10.580 0.160   1.00 10.25  ? 228 LYS A CA  1 
ATOM   2007 C  C   . LYS A 1 227 ? 15.842  -9.232  -0.098  1.00 9.91   ? 228 LYS A C   1 
ATOM   2008 O  O   . LYS A 1 227 ? 16.474  -9.005  -1.159  1.00 10.97  ? 228 LYS A O   1 
ATOM   2009 C  CB  . LYS A 1 227 ? 14.160  -10.900 -0.883  1.00 12.89  ? 228 LYS A CB  1 
ATOM   2010 C  CG  . LYS A 1 227 ? 13.693  -12.330 -0.853  1.00 17.59  ? 228 LYS A CG  1 
ATOM   2011 C  CD  . LYS A 1 227 ? 12.613  -12.546 -1.906  1.00 30.99  ? 228 LYS A CD  1 
ATOM   2012 C  CE  . LYS A 1 227 ? 12.692  -13.976 -2.448  1.00 47.71  ? 228 LYS A CE  1 
ATOM   2013 N  NZ  . LYS A 1 227 ? 12.362  -13.941 -3.889  1.00 69.72  ? 228 LYS A NZ  1 
ATOM   2014 N  N   . LEU A 1 228 ? 15.642  -8.286  0.791   1.00 8.94   ? 229 LEU A N   1 
ATOM   2015 C  CA  . LEU A 1 228 ? 16.264  -6.989  0.694   1.00 8.89   ? 229 LEU A CA  1 
ATOM   2016 C  C   . LEU A 1 228 ? 17.780  -7.144  0.793   1.00 8.67   ? 229 LEU A C   1 
ATOM   2017 O  O   . LEU A 1 228 ? 18.318  -8.173  1.213   1.00 9.00   ? 229 LEU A O   1 
ATOM   2018 C  CB  . LEU A 1 228 ? 15.717  -6.094  1.764   1.00 8.95   ? 229 LEU A CB  1 
ATOM   2019 C  CG  . LEU A 1 228 ? 14.302  -5.589  1.580   1.00 8.93   ? 229 LEU A CG  1 
ATOM   2020 C  CD1 . LEU A 1 228 ? 13.790  -4.995  2.856   1.00 10.61  ? 229 LEU A CD1 1 
ATOM   2021 C  CD2 . LEU A 1 228 ? 14.256  -4.577  0.458   1.00 12.56  ? 229 LEU A CD2 1 
ATOM   2022 N  N   . ASN A 1 229 ? 18.494  -6.072  0.424   1.00 9.20   ? 230 ASN A N   1 
ATOM   2023 C  CA  . ASN A 1 229 ? 19.947  -6.066  0.406   1.00 9.83   ? 230 ASN A CA  1 
ATOM   2024 C  C   . ASN A 1 229 ? 20.473  -4.903  1.279   1.00 9.42   ? 230 ASN A C   1 
ATOM   2025 O  O   . ASN A 1 229 ? 19.985  -3.772  1.183   1.00 10.39  ? 230 ASN A O   1 
ATOM   2026 C  CB  . ASN A 1 229 ? 20.526  -5.823  -0.992  1.00 10.65  ? 230 ASN A CB  1 
ATOM   2027 C  CG  . ASN A 1 229 ? 20.411  -6.965  -1.908  1.00 13.05  ? 230 ASN A CG  1 
ATOM   2028 O  OD1 . ASN A 1 229 ? 20.850  -6.777  -3.061  1.00 16.02  ? 230 ASN A OD1 1 
ATOM   2029 N  ND2 . ASN A 1 229 ? 19.834  -8.126  -1.542  1.00 13.88  ? 230 ASN A ND2 1 
ATOM   2030 N  N   . PHE A 1 230 ? 21.517  -5.213  2.064   1.00 9.59   ? 231 PHE A N   1 
ATOM   2031 C  CA  . PHE A 1 230 ? 22.235  -4.191  2.778   1.00 9.94   ? 231 PHE A CA  1 
ATOM   2032 C  C   . PHE A 1 230 ? 23.036  -3.291  1.855   1.00 10.68  ? 231 PHE A C   1 
ATOM   2033 O  O   . PHE A 1 230 ? 23.306  -2.125  2.162   1.00 12.52  ? 231 PHE A O   1 
ATOM   2034 C  CB  . PHE A 1 230 ? 23.280  -4.825  3.756   1.00 10.00  ? 231 PHE A CB  1 
ATOM   2035 C  CG  . PHE A 1 230 ? 22.755  -5.465  5.029   1.00 9.83   ? 231 PHE A CG  1 
ATOM   2036 C  CD1 . PHE A 1 230 ? 21.997  -4.745  5.944   1.00 11.49  ? 231 PHE A CD1 1 
ATOM   2037 C  CD2 . PHE A 1 230 ? 23.081  -6.761  5.314   1.00 10.63  ? 231 PHE A CD2 1 
ATOM   2038 C  CE1 . PHE A 1 230 ? 21.616  -5.303  7.153   1.00 11.88  ? 231 PHE A CE1 1 
ATOM   2039 C  CE2 . PHE A 1 230 ? 22.719  -7.307  6.541   1.00 11.08  ? 231 PHE A CE2 1 
ATOM   2040 C  CZ  . PHE A 1 230 ? 21.958  -6.600  7.469   1.00 10.65  ? 231 PHE A CZ  1 
ATOM   2041 N  N   . ASN A 1 231 ? 23.536  -3.848  0.769   1.00 10.80  ? 232 ASN A N   1 
ATOM   2042 C  CA  . ASN A 1 231 ? 24.416  -3.149  -0.179  1.00 12.19  ? 232 ASN A CA  1 
ATOM   2043 C  C   . ASN A 1 231 ? 23.663  -2.267  -1.108  1.00 11.54  ? 232 ASN A C   1 
ATOM   2044 O  O   . ASN A 1 231 ? 22.466  -2.431  -1.344  1.00 11.49  ? 232 ASN A O   1 
ATOM   2045 C  CB  . ASN A 1 231 ? 25.206  -4.239  -0.965  1.00 13.54  ? 232 ASN A CB  1 
ATOM   2046 C  CG  . ASN A 1 231 ? 24.204  -5.188  -1.658  1.00 12.52  ? 232 ASN A CG  1 
ATOM   2047 O  OD1 . ASN A 1 231 ? 23.642  -6.048  -0.989  1.00 13.58  ? 232 ASN A OD1 1 
ATOM   2048 N  ND2 . ASN A 1 231 ? 23.910  -4.998  -2.971  1.00 15.74  ? 232 ASN A ND2 1 
ATOM   2049 N  N   . GLY A 1 232 ? 24.416  -1.372  -1.733  1.00 12.23  ? 233 GLY A N   1 
ATOM   2050 C  CA  . GLY A 1 232 ? 23.907  -0.595  -2.854  1.00 13.12  ? 233 GLY A CA  1 
ATOM   2051 C  C   . GLY A 1 232 ? 23.924  -1.343  -4.164  1.00 12.42  ? 233 GLY A C   1 
ATOM   2052 O  O   . GLY A 1 232 ? 24.603  -2.333  -4.295  1.00 14.17  ? 233 GLY A O   1 
ATOM   2053 N  N   . GLU A 1 233 ? 23.166  -0.837  -5.149  1.00 13.20  ? 234 GLU A N   1 
ATOM   2054 C  CA  . GLU A 1 233 ? 23.123  -1.436  -6.467  1.00 14.13  ? 234 GLU A CA  1 
ATOM   2055 C  C   . GLU A 1 233 ? 24.587  -1.373  -7.004  1.00 13.66  ? 234 GLU A C   1 
ATOM   2056 O  O   . GLU A 1 233 ? 25.326  -0.395  -6.868  1.00 14.27  ? 234 GLU A O   1 
ATOM   2057 C  CB  . GLU A 1 233 ? 22.225  -0.626  -7.391  1.00 13.30  ? 234 GLU A CB  1 
ATOM   2058 C  CG  . GLU A 1 233 ? 21.974  -1.274  -8.746  1.00 14.50  ? 234 GLU A CG  1 
ATOM   2059 C  CD  . GLU A 1 233 ? 21.134  -0.374  -9.638  1.00 20.03  ? 234 GLU A CD  1 
ATOM   2060 O  OE1 . GLU A 1 233 ? 20.839  0.773   -9.232  1.00 20.29  ? 234 GLU A OE1 1 
ATOM   2061 O  OE2 . GLU A 1 233 ? 20.760  -0.811  -10.738 1.00 24.08  ? 234 GLU A OE2 1 
ATOM   2062 N  N   . GLY A 1 234 ? 24.993  -2.445  -7.595  1.00 15.60  ? 235 GLY A N   1 
ATOM   2063 C  CA  . GLY A 1 234 ? 26.332  -2.492  -8.199  1.00 17.05  ? 235 GLY A CA  1 
ATOM   2064 C  C   . GLY A 1 234 ? 27.422  -2.975  -7.258  1.00 15.91  ? 235 GLY A C   1 
ATOM   2065 O  O   . GLY A 1 234 ? 28.522  -3.247  -7.712  1.00 21.42  ? 235 GLY A O   1 
ATOM   2066 N  N   . GLU A 1 235 ? 27.094  -3.165  -5.988  1.00 15.26  ? 236 GLU A N   1 
ATOM   2067 C  CA  . GLU A 1 235 ? 27.989  -3.705  -4.981  1.00 16.09  ? 236 GLU A CA  1 
ATOM   2068 C  C   . GLU A 1 235 ? 27.688  -5.182  -4.705  1.00 15.70  ? 236 GLU A C   1 
ATOM   2069 O  O   . GLU A 1 235 ? 26.569  -5.626  -5.066  1.00 17.81  ? 236 GLU A O   1 
ATOM   2070 C  CB  . GLU A 1 235 ? 27.836  -3.017  -3.656  1.00 17.28  ? 236 GLU A CB  1 
ATOM   2071 C  CG  . GLU A 1 235 ? 28.090  -1.546  -3.817  1.00 19.45  ? 236 GLU A CG  1 
ATOM   2072 C  CD  . GLU A 1 235 ? 27.910  -0.760  -2.566  1.00 23.53  ? 236 GLU A CD  1 
ATOM   2073 O  OE1 . GLU A 1 235 ? 27.290  -1.318  -1.615  1.00 24.62  ? 236 GLU A OE1 1 
ATOM   2074 O  OE2 . GLU A 1 235 ? 28.453  0.375   -2.499  1.00 56.45  ? 236 GLU A OE2 1 
ATOM   2075 N  N   . PRO A 1 236 ? 28.581  -5.908  -4.102  1.00 17.51  ? 237 PRO A N   1 
ATOM   2076 C  CA  . PRO A 1 236 ? 28.306  -7.328  -3.785  1.00 16.28  ? 237 PRO A CA  1 
ATOM   2077 C  C   . PRO A 1 236 ? 27.025  -7.466  -2.905  1.00 13.87  ? 237 PRO A C   1 
ATOM   2078 O  O   . PRO A 1 236 ? 26.851  -6.741  -1.974  1.00 15.22  ? 237 PRO A O   1 
ATOM   2079 C  CB  . PRO A 1 236 ? 29.549  -7.757  -3.017  1.00 20.17  ? 237 PRO A CB  1 
ATOM   2080 C  CG  . PRO A 1 236 ? 30.623  -6.942  -3.729  1.00 26.74  ? 237 PRO A CG  1 
ATOM   2081 C  CD  . PRO A 1 236 ? 29.988  -5.554  -3.807  1.00 22.00  ? 237 PRO A CD  1 
ATOM   2082 N  N   . GLU A 1 237 ? 26.261  -8.479  -3.276  1.00 14.04  ? 238 GLU A N   1 
ATOM   2083 C  CA  . GLU A 1 237 ? 24.945  -8.652  -2.550  1.00 13.62  ? 238 GLU A CA  1 
ATOM   2084 C  C   . GLU A 1 237 ? 25.128  -9.231  -1.170  1.00 13.04  ? 238 GLU A C   1 
ATOM   2085 O  O   . GLU A 1 237 ? 25.791  -10.263 -1.003  1.00 13.75  ? 238 GLU A O   1 
ATOM   2086 C  CB  . GLU A 1 237 ? 24.004  -9.523  -3.371  1.00 16.10  ? 238 GLU A CB  1 
ATOM   2087 C  CG  . GLU A 1 237 ? 22.652  -9.696  -2.677  1.00 19.72  ? 238 GLU A CG  1 
ATOM   2088 C  CD  . GLU A 1 237 ? 21.565  -10.552 -3.383  1.00 22.07  ? 238 GLU A CD  1 
ATOM   2089 O  OE1 . GLU A 1 237 ? 21.930  -11.561 -3.970  1.00 40.46  ? 238 GLU A OE1 1 
ATOM   2090 O  OE2 . GLU A 1 237 ? 20.323  -10.263 -3.324  1.00 19.16  ? 238 GLU A OE2 1 
ATOM   2091 N  N   . GLU A 1 238 ? 24.525  -8.589  -0.206  1.00 12.05  ? 239 GLU A N   1 
ATOM   2092 C  CA  . GLU A 1 238 ? 24.496  -9.024  1.151   1.00 12.39  ? 239 GLU A CA  1 
ATOM   2093 C  C   . GLU A 1 238 ? 23.031  -8.974  1.615   1.00 10.40  ? 239 GLU A C   1 
ATOM   2094 O  O   . GLU A 1 238 ? 22.472  -7.885  1.665   1.00 12.12  ? 239 GLU A O   1 
ATOM   2095 C  CB  . GLU A 1 238 ? 25.281  -8.034  2.009   1.00 15.94  ? 239 GLU A CB  1 
ATOM   2096 C  CG  . GLU A 1 238 ? 26.744  -7.898  1.701   1.00 19.22  ? 239 GLU A CG  1 
ATOM   2097 C  CD  . GLU A 1 238 ? 27.362  -6.885  2.655   1.00 33.18  ? 239 GLU A CD  1 
ATOM   2098 O  OE1 . GLU A 1 238 ? 27.635  -7.136  3.886   1.00 42.21  ? 239 GLU A OE1 1 
ATOM   2099 O  OE2 . GLU A 1 238 ? 27.612  -5.759  2.166   1.00 40.13  ? 239 GLU A OE2 1 
ATOM   2100 N  N   . LEU A 1 239 ? 22.440  -10.111 1.894   1.00 10.01  ? 240 LEU A N   1 
ATOM   2101 C  CA  . LEU A 1 239 ? 21.040  -10.085 2.258   1.00 9.30   ? 240 LEU A CA  1 
ATOM   2102 C  C   . LEU A 1 239 ? 20.834  -9.324  3.569   1.00 8.89   ? 240 LEU A C   1 
ATOM   2103 O  O   . LEU A 1 239 ? 21.571  -9.504  4.565   1.00 9.49   ? 240 LEU A O   1 
ATOM   2104 C  CB  . LEU A 1 239 ? 20.502  -11.492 2.394   1.00 10.75  ? 240 LEU A CB  1 
ATOM   2105 C  CG  . LEU A 1 239 ? 20.498  -12.312 1.090   1.00 13.25  ? 240 LEU A CG  1 
ATOM   2106 C  CD1 . LEU A 1 239 ? 20.034  -13.735 1.370   1.00 18.67  ? 240 LEU A CD1 1 
ATOM   2107 C  CD2 . LEU A 1 239 ? 19.594  -11.699 0.097   1.00 14.45  ? 240 LEU A CD2 1 
ATOM   2108 N  N   . MET A 1 240 ? 19.758  -8.539  3.580   1.00 8.75   ? 241 MET A N   1 
ATOM   2109 C  CA  . MET A 1 240 ? 19.408  -7.743  4.754   1.00 8.30   ? 241 MET A CA  1 
ATOM   2110 C  C   . MET A 1 240 ? 18.608  -8.639  5.715   1.00 7.62   ? 241 MET A C   1 
ATOM   2111 O  O   . MET A 1 240 ? 17.414  -8.793  5.606   1.00 8.21   ? 241 MET A O   1 
ATOM   2112 C  CB  . MET A 1 240 ? 18.549  -6.583  4.312   1.00 9.21   ? 241 MET A CB  1 
ATOM   2113 C  CG  . MET A 1 240 ? 18.254  -5.588  5.445   1.00 8.87   ? 241 MET A CG  1 
ATOM   2114 S  SD  . MET A 1 240 ? 17.153  -4.250  5.003   1.00 9.10   ? 241 MET A SD  1 
ATOM   2115 C  CE  . MET A 1 240 ? 18.180  -3.335  3.874   1.00 13.47  ? 241 MET A CE  1 
ATOM   2116 N  N   . VAL A 1 241 ? 19.352  -9.262  6.617   1.00 7.61   ? 242 VAL A N   1 
ATOM   2117 C  CA  . VAL A 1 241 ? 18.822  -10.140 7.653   1.00 7.13   ? 242 VAL A CA  1 
ATOM   2118 C  C   . VAL A 1 241 ? 19.616  -9.882  8.920   1.00 6.82   ? 242 VAL A C   1 
ATOM   2119 O  O   . VAL A 1 241 ? 20.781  -9.473  8.914   1.00 7.49   ? 242 VAL A O   1 
ATOM   2120 C  CB  . VAL A 1 241 ? 18.933  -11.648 7.279   1.00 8.00   ? 242 VAL A CB  1 
ATOM   2121 C  CG1 . VAL A 1 241 ? 18.054  -11.945 6.087   1.00 9.87   ? 242 VAL A CG1 1 
ATOM   2122 C  CG2 . VAL A 1 241 ? 20.387  -12.058 7.034   1.00 9.17   ? 242 VAL A CG2 1 
ATOM   2123 N  N   . ASP A 1 242 ? 18.990  -10.208 10.077  1.00 6.53   ? 243 ASP A N   1 
ATOM   2124 C  CA  . ASP A 1 242 ? 19.662  -10.089 11.361  1.00 6.85   ? 243 ASP A CA  1 
ATOM   2125 C  C   . ASP A 1 242 ? 20.133  -8.676  11.631  1.00 6.39   ? 243 ASP A C   1 
ATOM   2126 O  O   . ASP A 1 242 ? 21.242  -8.457  12.125  1.00 8.15   ? 243 ASP A O   1 
ATOM   2127 C  CB  . ASP A 1 242 ? 20.720  -11.153 11.574  1.00 7.60   ? 243 ASP A CB  1 
ATOM   2128 C  CG  . ASP A 1 242 ? 20.140  -12.531 11.661  1.00 7.56   ? 243 ASP A CG  1 
ATOM   2129 O  OD1 . ASP A 1 242 ? 19.106  -12.719 12.313  1.00 7.63   ? 243 ASP A OD1 1 
ATOM   2130 O  OD2 . ASP A 1 242 ? 20.751  -13.473 11.036  1.00 9.72   ? 243 ASP A OD2 1 
ATOM   2131 N  N   . ASN A 1 243 ? 19.227  -7.729  11.394  1.00 6.15   ? 244 ASN A N   1 
ATOM   2132 C  CA  . ASN A 1 243 ? 19.512  -6.314  11.642  1.00 6.11   ? 244 ASN A CA  1 
ATOM   2133 C  C   . ASN A 1 243 ? 18.965  -5.873  12.994  1.00 6.14   ? 244 ASN A C   1 
ATOM   2134 O  O   . ASN A 1 243 ? 18.357  -4.803  13.131  1.00 7.17   ? 244 ASN A O   1 
ATOM   2135 C  CB  . ASN A 1 243 ? 18.965  -5.457  10.493  1.00 6.58   ? 244 ASN A CB  1 
ATOM   2136 C  CG  . ASN A 1 243 ? 17.485  -5.594  10.325  1.00 6.61   ? 244 ASN A CG  1 
ATOM   2137 O  OD1 . ASN A 1 243 ? 16.843  -6.461  10.897  1.00 7.50   ? 244 ASN A OD1 1 
ATOM   2138 N  ND2 . ASN A 1 243 ? 16.903  -4.691  9.537   1.00 9.45   ? 244 ASN A ND2 1 
ATOM   2139 N  N   . TRP A 1 244 ? 19.219  -6.703  14.021  1.00 6.41   ? 245 TRP A N   1 
ATOM   2140 C  CA  . TRP A 1 244 ? 18.787  -6.461  15.384  1.00 6.17   ? 245 TRP A CA  1 
ATOM   2141 C  C   . TRP A 1 244 ? 20.009  -6.389  16.286  1.00 6.45   ? 245 TRP A C   1 
ATOM   2142 O  O   . TRP A 1 244 ? 20.989  -7.121  16.134  1.00 7.45   ? 245 TRP A O   1 
ATOM   2143 C  CB  . TRP A 1 244 ? 17.814  -7.568  15.862  1.00 6.49   ? 245 TRP A CB  1 
ATOM   2144 C  CG  . TRP A 1 244 ? 18.286  -8.964  15.656  1.00 6.59   ? 245 TRP A CG  1 
ATOM   2145 C  CD1 . TRP A 1 244 ? 18.184  -9.667  14.507  1.00 6.64   ? 245 TRP A CD1 1 
ATOM   2146 C  CD2 . TRP A 1 244 ? 18.890  -9.845  16.623  1.00 6.35   ? 245 TRP A CD2 1 
ATOM   2147 N  NE1 . TRP A 1 244 ? 18.665  -10.944 14.654  1.00 7.05   ? 245 TRP A NE1 1 
ATOM   2148 C  CE2 . TRP A 1 244 ? 19.115  -11.068 15.965  1.00 7.20   ? 245 TRP A CE2 1 
ATOM   2149 C  CE3 . TRP A 1 244 ? 19.184  -9.728  17.976  1.00 7.97   ? 245 TRP A CE3 1 
ATOM   2150 C  CZ2 . TRP A 1 244 ? 19.667  -12.168 16.615  1.00 8.09   ? 245 TRP A CZ2 1 
ATOM   2151 C  CZ3 . TRP A 1 244 ? 19.720  -10.843 18.629  1.00 8.21   ? 245 TRP A CZ3 1 
ATOM   2152 C  CH2 . TRP A 1 244 ? 19.953  -12.018 17.956  1.00 8.88   ? 245 TRP A CH2 1 
ATOM   2153 N  N   . ARG A 1 245 ? 19.909  -5.506  17.288  1.00 6.21   ? 246 ARG A N   1 
ATOM   2154 C  CA  . ARG A 1 245 ? 20.881  -5.446  18.381  1.00 5.93   ? 246 ARG A CA  1 
ATOM   2155 C  C   . ARG A 1 245 ? 20.363  -6.370  19.497  1.00 6.27   ? 246 ARG A C   1 
ATOM   2156 O  O   . ARG A 1 245 ? 19.203  -6.346  19.836  1.00 6.75   ? 246 ARG A O   1 
ATOM   2157 C  CB  . ARG A 1 245 ? 20.974  -4.019  18.905  1.00 6.38   ? 246 ARG A CB  1 
ATOM   2158 C  CG  . ARG A 1 245 ? 22.108  -3.823  19.905  1.00 6.60   ? 246 ARG A CG  1 
ATOM   2159 C  CD  . ARG A 1 245 ? 22.013  -2.490  20.601  1.00 6.60   ? 246 ARG A CD  1 
ATOM   2160 N  NE  . ARG A 1 245 ? 23.251  -2.134  21.250  1.00 6.80   ? 246 ARG A NE  1 
ATOM   2161 C  CZ  . ARG A 1 245 ? 23.429  -1.061  22.020  1.00 6.80   ? 246 ARG A CZ  1 
ATOM   2162 N  NH1 . ARG A 1 245 ? 22.420  -0.293  22.388  1.00 7.23   ? 246 ARG A NH1 1 
ATOM   2163 N  NH2 . ARG A 1 245 ? 24.671  -0.761  22.442  1.00 8.52   ? 246 ARG A NH2 1 
ATOM   2164 N  N   . PRO A 1 246 ? 21.246  -7.154  20.104  1.00 7.12   ? 247 PRO A N   1 
ATOM   2165 C  CA  . PRO A 1 246 ? 20.818  -7.988  21.223  1.00 7.52   ? 247 PRO A CA  1 
ATOM   2166 C  C   . PRO A 1 246 ? 20.480  -7.117  22.432  1.00 7.47   ? 247 PRO A C   1 
ATOM   2167 O  O   . PRO A 1 246 ? 20.836  -5.925  22.556  1.00 7.45   ? 247 PRO A O   1 
ATOM   2168 C  CB  . PRO A 1 246 ? 22.045  -8.847  21.533  1.00 10.49  ? 247 PRO A CB  1 
ATOM   2169 C  CG  . PRO A 1 246 ? 22.862  -8.811  20.289  1.00 13.22  ? 247 PRO A CG  1 
ATOM   2170 C  CD  . PRO A 1 246 ? 22.655  -7.434  19.719  1.00 8.80   ? 247 PRO A CD  1 
ATOM   2171 N  N   . ALA A 1 247 ? 19.791  -7.761  23.377  1.00 7.97   ? 248 ALA A N   1 
ATOM   2172 C  CA  . ALA A 1 247 ? 19.444  -7.098  24.649  1.00 8.14   ? 248 ALA A CA  1 
ATOM   2173 C  C   . ALA A 1 247 ? 20.707  -6.599  25.372  1.00 7.78   ? 248 ALA A C   1 
ATOM   2174 O  O   . ALA A 1 247 ? 21.737  -7.283  25.428  1.00 8.91   ? 248 ALA A O   1 
ATOM   2175 C  CB  . ALA A 1 247 ? 18.663  -8.077  25.535  1.00 9.24   ? 248 ALA A CB  1 
ATOM   2176 N  N   . GLN A 1 248 ? 20.554  -5.419  25.941  1.00 7.30   ? 249 GLN A N   1 
ATOM   2177 C  CA  . GLN A 1 248 ? 21.600  -4.708  26.653  1.00 7.69   ? 249 GLN A CA  1 
ATOM   2178 C  C   . GLN A 1 248 ? 21.329  -4.712  28.136  1.00 8.32   ? 249 GLN A C   1 
ATOM   2179 O  O   . GLN A 1 248 ? 20.181  -4.903  28.567  1.00 8.79   ? 249 GLN A O   1 
ATOM   2180 C  CB  . GLN A 1 248 ? 21.684  -3.281  26.121  1.00 8.26   ? 249 GLN A CB  1 
ATOM   2181 C  CG  . GLN A 1 248 ? 21.979  -3.219  24.640  1.00 8.82   ? 249 GLN A CG  1 
ATOM   2182 C  CD  . GLN A 1 248 ? 23.328  -3.895  24.327  1.00 8.62   ? 249 GLN A CD  1 
ATOM   2183 O  OE1 . GLN A 1 248 ? 24.376  -3.516  24.862  1.00 11.06  ? 249 GLN A OE1 1 
ATOM   2184 N  NE2 . GLN A 1 248 ? 23.309  -4.868  23.435  1.00 9.68   ? 249 GLN A NE2 1 
ATOM   2185 N  N   . PRO A 1 249 ? 22.344  -4.361  28.961  1.00 10.14  ? 250 PRO A N   1 
ATOM   2186 C  CA  . PRO A 1 249 ? 22.162  -4.414  30.390  1.00 11.10  ? 250 PRO A CA  1 
ATOM   2187 C  C   . PRO A 1 249 ? 21.053  -3.389  30.838  1.00 9.07   ? 250 PRO A C   1 
ATOM   2188 O  O   . PRO A 1 249 ? 21.060  -2.240  30.442  1.00 9.72   ? 250 PRO A O   1 
ATOM   2189 C  CB  . PRO A 1 249 ? 23.557  -4.009  30.919  1.00 14.88  ? 250 PRO A CB  1 
ATOM   2190 C  CG  . PRO A 1 249 ? 24.499  -4.407  29.884  1.00 15.37  ? 250 PRO A CG  1 
ATOM   2191 C  CD  . PRO A 1 249 ? 23.766  -4.112  28.573  1.00 12.56  ? 250 PRO A CD  1 
ATOM   2192 N  N   . LEU A 1 250 ? 20.195  -3.897  31.735  1.00 9.51   ? 251 LEU A N   1 
ATOM   2193 C  CA  . LEU A 1 250 ? 19.147  -3.024  32.233  1.00 9.15   ? 251 LEU A CA  1 
ATOM   2194 C  C   . LEU A 1 250 ? 19.669  -1.923  33.121  1.00 8.77   ? 251 LEU A C   1 
ATOM   2195 O  O   . LEU A 1 250 ? 19.086  -0.826  33.196  1.00 9.57   ? 251 LEU A O   1 
ATOM   2196 C  CB  . LEU A 1 250 ? 18.090  -3.856  32.993  1.00 10.33  ? 251 LEU A CB  1 
ATOM   2197 C  CG  . LEU A 1 250 ? 16.791  -3.145  33.390  1.00 10.45  ? 251 LEU A CG  1 
ATOM   2198 C  CD1 . LEU A 1 250 ? 16.035  -2.595  32.163  1.00 10.57  ? 251 LEU A CD1 1 
ATOM   2199 C  CD2 . LEU A 1 250 ? 15.905  -4.119  34.170  1.00 14.02  ? 251 LEU A CD2 1 
ATOM   2200 N  N   . LYS A 1 251 ? 20.743  -2.168  33.862  1.00 10.12  ? 252 LYS A N   1 
ATOM   2201 C  CA  . LYS A 1 251 ? 21.364  -1.132  34.696  1.00 10.96  ? 252 LYS A CA  1 
ATOM   2202 C  C   . LYS A 1 251 ? 20.331  -0.551  35.677  1.00 10.84  ? 252 LYS A C   1 
ATOM   2203 O  O   . LYS A 1 251 ? 19.526  -1.372  36.190  1.00 13.24  ? 252 LYS A O   1 
ATOM   2204 C  CB  . LYS A 1 251 ? 22.133  -0.149  33.915  1.00 12.59  ? 252 LYS A CB  1 
ATOM   2205 C  CG  . LYS A 1 251 ? 23.267  -0.804  33.135  1.00 14.28  ? 252 LYS A CG  1 
ATOM   2206 C  CD  . LYS A 1 251 ? 24.229  0.156   32.519  1.00 15.68  ? 252 LYS A CD  1 
ATOM   2207 C  CE  . LYS A 1 251 ? 25.402  -0.529  31.898  1.00 22.56  ? 252 LYS A CE  1 
ATOM   2208 N  NZ  . LYS A 1 251 ? 26.257  0.362   31.061  1.00 20.37  ? 252 LYS A NZ  1 
ATOM   2209 N  N   . ASN A 1 252 ? 20.362  0.700   35.963  1.00 10.75  ? 253 ASN A N   1 
ATOM   2210 C  CA  . ASN A 1 252 ? 19.467  1.285   36.938  1.00 17.57  ? 253 ASN A CA  1 
ATOM   2211 C  C   . ASN A 1 252 ? 18.129  1.606   36.301  1.00 15.20  ? 253 ASN A C   1 
ATOM   2212 O  O   . ASN A 1 252 ? 17.740  2.773   36.241  1.00 17.32  ? 253 ASN A O   1 
ATOM   2213 C  CB  . ASN A 1 252 ? 20.093  2.561   37.511  1.00 20.73  ? 253 ASN A CB  1 
ATOM   2214 C  CG  . ASN A 1 252 ? 19.431  3.018   38.796  1.00 20.63  ? 253 ASN A CG  1 
ATOM   2215 O  OD1 . ASN A 1 252 ? 18.955  2.204   39.586  1.00 29.89  ? 253 ASN A OD1 1 
ATOM   2216 N  ND2 . ASN A 1 252 ? 19.405  4.330   39.015  1.00 25.92  ? 253 ASN A ND2 1 
ATOM   2217 N  N   . ARG A 1 253 ? 17.416  0.593   35.810  1.00 11.95  ? 254 ARG A N   1 
ATOM   2218 C  CA  . ARG A 1 253 ? 16.084  0.897   35.283  1.00 9.37   ? 254 ARG A CA  1 
ATOM   2219 C  C   . ARG A 1 253 ? 15.026  -0.058  35.739  1.00 9.70   ? 254 ARG A C   1 
ATOM   2220 O  O   . ARG A 1 253 ? 15.350  -1.178  36.105  1.00 15.04  ? 254 ARG A O   1 
ATOM   2221 C  CB  . ARG A 1 253 ? 16.129  0.944   33.759  1.00 8.33   ? 254 ARG A CB  1 
ATOM   2222 C  CG  . ARG A 1 253 ? 17.022  2.048   33.233  1.00 8.42   ? 254 ARG A CG  1 
ATOM   2223 C  CD  . ARG A 1 253 ? 17.125  2.049   31.712  1.00 7.75   ? 254 ARG A CD  1 
ATOM   2224 N  NE  . ARG A 1 253 ? 17.938  0.911   31.277  1.00 7.37   ? 254 ARG A NE  1 
ATOM   2225 C  CZ  . ARG A 1 253 ? 18.173  0.650   30.011  1.00 6.55   ? 254 ARG A CZ  1 
ATOM   2226 N  NH1 . ARG A 1 253 ? 17.576  1.320   29.037  1.00 6.53   ? 254 ARG A NH1 1 
ATOM   2227 N  NH2 . ARG A 1 253 ? 19.010  -0.350  29.696  1.00 6.96   ? 254 ARG A NH2 1 
ATOM   2228 N  N   . GLN A 1 254 ? 13.797  0.420   35.766  1.00 9.55   ? 255 GLN A N   1 
ATOM   2229 C  CA  . GLN A 1 254 ? 12.631  -0.353  36.012  1.00 10.37  ? 255 GLN A CA  1 
ATOM   2230 C  C   . GLN A 1 254 ? 11.765  -0.354  34.784  1.00 9.53   ? 255 GLN A C   1 
ATOM   2231 O  O   . GLN A 1 254 ? 11.566  0.686   34.133  1.00 13.56  ? 255 GLN A O   1 
ATOM   2232 C  CB  . GLN A 1 254 ? 11.814  0.092   37.222  1.00 12.16  ? 255 GLN A CB  1 
ATOM   2233 C  CG  . GLN A 1 254 ? 12.551  -0.088  38.478  1.00 13.85  ? 255 GLN A CG  1 
ATOM   2234 C  CD  . GLN A 1 254 ? 11.617  0.057   39.605  1.00 15.78  ? 255 GLN A CD  1 
ATOM   2235 O  OE1 . GLN A 1 254 ? 10.794  1.025   39.651  1.00 20.31  ? 255 GLN A OE1 1 
ATOM   2236 N  NE2 . GLN A 1 254 ? 11.702  -0.930  40.557  1.00 17.91  ? 255 GLN A NE2 1 
ATOM   2237 N  N   . ILE A 1 255 ? 11.243  -1.523  34.440  1.00 8.25   ? 256 ILE A N   1 
ATOM   2238 C  CA  . ILE A 1 255 ? 10.258  -1.676  33.377  1.00 7.72   ? 256 ILE A CA  1 
ATOM   2239 C  C   . ILE A 1 255 ? 8.888   -1.673  34.027  1.00 7.89   ? 256 ILE A C   1 
ATOM   2240 O  O   . ILE A 1 255 ? 8.662   -2.453  34.957  1.00 9.69   ? 256 ILE A O   1 
ATOM   2241 C  CB  . ILE A 1 255 ? 10.506  -2.916  32.557  1.00 8.51   ? 256 ILE A CB  1 
ATOM   2242 C  CG1 . ILE A 1 255 ? 11.955  -2.890  31.992  1.00 8.92   ? 256 ILE A CG1 1 
ATOM   2243 C  CG2 . ILE A 1 255 ? 9.450   -3.014  31.453  1.00 10.05  ? 256 ILE A CG2 1 
ATOM   2244 C  CD1 . ILE A 1 255 ? 12.296  -4.108  31.182  1.00 10.61  ? 256 ILE A CD1 1 
ATOM   2245 N  N   A LYS A 1 256 ? 7.966   -0.892  33.511  0.50 7.31   ? 257 LYS A N   1 
ATOM   2246 N  N   B LYS A 1 256 ? 8.022   -0.740  33.624  0.50 7.79   ? 257 LYS A N   1 
ATOM   2247 C  CA  A LYS A 1 256 ? 6.669   -0.714  34.102  0.50 8.02   ? 257 LYS A CA  1 
ATOM   2248 C  CA  B LYS A 1 256 ? 6.663   -0.683  34.135  0.50 8.27   ? 257 LYS A CA  1 
ATOM   2249 C  C   A LYS A 1 256 ? 5.605   -1.207  33.167  0.50 7.44   ? 257 LYS A C   1 
ATOM   2250 C  C   B LYS A 1 256 ? 5.731   -1.390  33.167  0.50 7.04   ? 257 LYS A C   1 
ATOM   2251 O  O   A LYS A 1 256 ? 5.631   -0.956  31.957  0.50 7.17   ? 257 LYS A O   1 
ATOM   2252 O  O   B LYS A 1 256 ? 5.933   -1.401  31.944  0.50 6.74   ? 257 LYS A O   1 
ATOM   2253 C  CB  A LYS A 1 256 ? 6.460   0.769   34.390  0.50 8.70   ? 257 LYS A CB  1 
ATOM   2254 C  CB  B LYS A 1 256 ? 6.177   0.778   34.359  0.50 9.51   ? 257 LYS A CB  1 
ATOM   2255 C  CG  A LYS A 1 256 ? 7.461   1.227   35.434  0.50 11.29  ? 257 LYS A CG  1 
ATOM   2256 C  CG  B LYS A 1 256 ? 7.103   1.601   35.255  0.50 11.81  ? 257 LYS A CG  1 
ATOM   2257 C  CD  A LYS A 1 256 ? 7.255   2.651   35.803  0.50 14.60  ? 257 LYS A CD  1 
ATOM   2258 C  CD  B LYS A 1 256 ? 7.542   0.962   36.572  0.50 18.24  ? 257 LYS A CD  1 
ATOM   2259 C  CE  A LYS A 1 256 ? 8.472   3.076   36.645  0.50 19.03  ? 257 LYS A CE  1 
ATOM   2260 C  CE  B LYS A 1 256 ? 8.418   2.000   37.329  0.50 23.97  ? 257 LYS A CE  1 
ATOM   2261 N  NZ  A LYS A 1 256 ? 8.422   4.499   37.097  0.50 17.78  ? 257 LYS A NZ  1 
ATOM   2262 N  NZ  B LYS A 1 256 ? 8.798   1.744   38.748  0.50 26.80  ? 257 LYS A NZ  1 
ATOM   2263 N  N   . ALA A 1 257 ? 4.651   -1.977  33.710  1.00 8.77   ? 258 ALA A N   1 
ATOM   2264 C  CA  . ALA A 1 257 ? 3.569   -2.564  32.957  1.00 8.47   ? 258 ALA A CA  1 
ATOM   2265 C  C   . ALA A 1 257 ? 2.305   -1.723  33.096  1.00 8.50   ? 258 ALA A C   1 
ATOM   2266 O  O   . ALA A 1 257 ? 1.978   -1.251  34.170  1.00 9.96   ? 258 ALA A O   1 
ATOM   2267 C  CB  . ALA A 1 257 ? 3.310   -4.014  33.401  1.00 10.67  ? 258 ALA A CB  1 
ATOM   2268 N  N   . SER A 1 258 ? 1.574   -1.599  31.991  1.00 8.32   ? 259 SER A N   1 
ATOM   2269 C  CA  . SER A 1 258 ? 0.331   -0.861  31.991  1.00 9.49   ? 259 SER A CA  1 
ATOM   2270 C  C   . SER A 1 258 ? -0.848  -1.717  32.467  1.00 10.48  ? 259 SER A C   1 
ATOM   2271 O  O   . SER A 1 258 ? -1.958  -1.148  32.540  1.00 13.77  ? 259 SER A O   1 
ATOM   2272 C  CB  . SER A 1 258 ? 0.034   -0.354  30.585  1.00 9.63   ? 259 SER A CB  1 
ATOM   2273 O  OG  . SER A 1 258 ? -0.426  -1.401  29.763  1.00 9.11   ? 259 SER A OG  1 
ATOM   2274 N  N   . PHE A 1 259 ? -0.626  -2.998  32.692  1.00 11.09  ? 260 PHE A N   1 
ATOM   2275 C  CA  . PHE A 1 259 ? -1.708  -3.970  32.879  1.00 13.18  ? 260 PHE A CA  1 
ATOM   2276 C  C   . PHE A 1 259 ? -1.289  -4.854  34.034  1.00 18.78  ? 260 PHE A C   1 
ATOM   2277 O  O   . PHE A 1 259 ? -0.125  -5.070  34.334  1.00 19.31  ? 260 PHE A O   1 
ATOM   2278 C  CB  . PHE A 1 259 ? -1.869  -4.790  31.583  1.00 13.18  ? 260 PHE A CB  1 
ATOM   2279 C  CG  . PHE A 1 259 ? -0.596  -5.544  31.206  1.00 12.07  ? 260 PHE A CG  1 
ATOM   2280 C  CD1 . PHE A 1 259 ? 0.388   -4.918  30.503  1.00 10.38  ? 260 PHE A CD1 1 
ATOM   2281 C  CD2 . PHE A 1 259 ? -0.394  -6.849  31.661  1.00 15.05  ? 260 PHE A CD2 1 
ATOM   2282 C  CE1 . PHE A 1 259 ? 1.558   -5.558  30.210  1.00 11.45  ? 260 PHE A CE1 1 
ATOM   2283 C  CE2 . PHE A 1 259 ? 0.771   -7.497  31.395  1.00 20.64  ? 260 PHE A CE2 1 
ATOM   2284 C  CZ  . PHE A 1 259 ? 1.740   -6.868  30.649  1.00 16.25  ? 260 PHE A CZ  1 
ATOM   2285 N  N   . LYS A 1 260 ? -2.380  -5.313  34.663  1.00 27.24  ? 261 LYS A N   1 
ATOM   2286 C  CA  . LYS A 1 260 ? -2.649  -6.551  35.431  1.00 46.60  ? 261 LYS A CA  1 
ATOM   2287 C  C   . LYS A 1 260 ? -2.458  -6.672  36.935  1.00 61.26  ? 261 LYS A C   1 
ATOM   2288 O  O   . LYS A 1 260 ? -3.225  -6.003  37.656  1.00 54.36  ? 261 LYS A O   1 
ATOM   2289 C  CB  . LYS A 1 260 ? -2.532  -7.890  34.625  1.00 71.03  ? 261 LYS A CB  1 
ATOM   2290 C  CG  . LYS A 1 260 ? -3.513  -7.910  33.420  1.00 77.93  ? 261 LYS A CG  1 
ATOM   2291 C  CD  . LYS A 1 260 ? -3.782  -9.321  32.873  1.00 70.12  ? 261 LYS A CD  1 
ATOM   2292 C  CE  . LYS A 1 260 ? -2.787  -9.709  31.756  1.00 55.12  ? 261 LYS A CE  1 
ATOM   2293 N  NZ  . LYS A 1 260 ? -1.524  -10.326 32.288  1.00 40.12  ? 261 LYS A NZ  1 
ATOM   2294 O  OXT . LYS A 1 260 ? -1.613  -7.418  37.430  1.00 84.32  ? 261 LYS A OXT 1 
HETATM 2295 ZN ZN  . ZN  B 2 .   ? 14.191  0.098   15.337  1.00 5.13   ? 301 ZN  A ZN  1 
HETATM 2296 F  F27 . WWO C 3 .   ? 13.883  4.806   14.796  1.00 7.13   ? 302 WWO A F27 1 
HETATM 2297 C  C5  . WWO C 3 .   ? 15.210  4.775   14.856  1.00 6.39   ? 302 WWO A C5  1 
HETATM 2298 C  C4  . WWO C 3 .   ? 15.871  3.878   15.691  1.00 6.11   ? 302 WWO A C4  1 
HETATM 2299 S  S7  . WWO C 3 .   ? 15.043  2.670   16.769  1.00 5.74   ? 302 WWO A S7  1 
HETATM 2300 O  O9  . WWO C 3 .   ? 13.647  2.875   16.586  1.00 6.07   ? 302 WWO A O9  1 
HETATM 2301 N  N10 . WWO C 3 .   ? 15.471  1.273   16.217  1.00 5.74   ? 302 WWO A N10 1 
HETATM 2302 O  O8  . WWO C 3 .   ? 15.616  2.952   18.063  1.00 6.42   ? 302 WWO A O8  1 
HETATM 2303 C  C3  . WWO C 3 .   ? 17.255  3.925   15.700  1.00 6.36   ? 302 WWO A C3  1 
HETATM 2304 F  F12 . WWO C 3 .   ? 17.947  3.071   16.438  1.00 6.99   ? 302 WWO A F12 1 
HETATM 2305 C  C2  . WWO C 3 .   ? 17.944  4.834   14.930  1.00 7.12   ? 302 WWO A C2  1 
HETATM 2306 F  F13 . WWO C 3 .   ? 19.270  4.847   15.066  1.00 8.30   ? 302 WWO A F13 1 
HETATM 2307 C  C6  . WWO C 3 .   ? 15.899  5.680   13.999  1.00 7.09   ? 302 WWO A C6  1 
HETATM 2308 C  C1  . WWO C 3 .   ? 17.280  5.689   14.048  1.00 7.62   ? 302 WWO A C1  1 
HETATM 2309 S  S11 . WWO C 3 .   ? 18.309  6.797   13.102  1.00 9.34   ? 302 WWO A S11 1 
HETATM 2310 O  O22 . WWO C 3 .   ? 19.030  7.642   14.071  1.00 12.02  ? 302 WWO A O22 1 
HETATM 2311 O  O23 . WWO C 3 .   ? 17.509  7.404   12.078  1.00 11.16  ? 302 WWO A O23 1 
HETATM 2312 C  C21 . WWO C 3 .   ? 19.505  5.843   12.359  1.00 10.65  ? 302 WWO A C21 1 
HETATM 2313 C  C24 . WWO C 3 .   ? 18.877  5.094   11.174  1.00 13.99  ? 302 WWO A C24 1 
HETATM 2314 O  O25 . WWO C 3 .   ? 17.743  4.268   11.450  1.00 14.44  ? 302 WWO A O25 1 
HETATM 2315 N  N26 . WWO C 3 .   ? 15.108  6.453   13.124  1.00 8.01   ? 302 WWO A N26 1 
HETATM 2316 C  C14 . WWO C 3 .   ? 14.263  7.471   13.740  1.00 8.15   ? 302 WWO A C14 1 
HETATM 2317 C  C15 . WWO C 3 .   ? 15.055  8.652   14.240  1.00 8.55   ? 302 WWO A C15 1 
HETATM 2318 C  C20 . WWO C 3 .   ? 15.367  8.782   15.614  1.00 10.02  ? 302 WWO A C20 1 
HETATM 2319 C  C19 . WWO C 3 .   ? 16.141  9.805   16.078  1.00 11.63  ? 302 WWO A C19 1 
HETATM 2320 C  C18 . WWO C 3 .   ? 16.636  10.750  15.152  1.00 11.38  ? 302 WWO A C18 1 
HETATM 2321 C  C17 . WWO C 3 .   ? 16.355  10.631  13.827  1.00 11.14  ? 302 WWO A C17 1 
HETATM 2322 C  C16 . WWO C 3 .   ? 15.562  9.596   13.353  1.00 9.34   ? 302 WWO A C16 1 
HETATM 2323 F  F27 A WWO D 3 .   ? 14.440  11.923  9.509   0.50 66.14  ? 303 WWO A F27 1 
HETATM 2324 F  F27 B WWO D 3 .   ? 14.335  11.820  9.802   0.50 16.54  ? 303 WWO A F27 1 
HETATM 2325 C  C5  A WWO D 3 .   ? 15.562  11.147  9.488   0.50 49.77  ? 303 WWO A C5  1 
HETATM 2326 C  C5  B WWO D 3 .   ? 15.477  11.067  9.729   0.50 14.56  ? 303 WWO A C5  1 
HETATM 2327 C  C4  A WWO D 3 .   ? 15.437  9.741   9.335   0.50 35.21  ? 303 WWO A C4  1 
HETATM 2328 C  C4  B WWO D 3 .   ? 15.373  9.759   9.345   0.50 15.97  ? 303 WWO A C4  1 
HETATM 2329 S  S7  A WWO D 3 .   ? 13.830  8.894   9.209   0.50 15.30  ? 303 WWO A S7  1 
HETATM 2330 S  S7  B WWO D 3 .   ? 13.798  8.888   9.159   0.50 17.64  ? 303 WWO A S7  1 
HETATM 2331 O  O9  A WWO D 3 .   ? 12.769  9.836   8.925   0.50 17.09  ? 303 WWO A O9  1 
HETATM 2332 O  O9  B WWO D 3 .   ? 12.687  9.863   8.864   0.50 22.94  ? 303 WWO A O9  1 
HETATM 2333 N  N10 A WWO D 3 .   ? 13.820  7.928   7.913   0.50 12.23  ? 303 WWO A N10 1 
HETATM 2334 N  N10 B WWO D 3 .   ? 13.818  8.019   7.649   0.50 22.95  ? 303 WWO A N10 1 
HETATM 2335 O  O8  A WWO D 3 .   ? 13.921  8.167   10.410  0.50 11.24  ? 303 WWO A O8  1 
HETATM 2336 O  O8  B WWO D 3 .   ? 13.935  8.233   10.371  0.50 15.70  ? 303 WWO A O8  1 
HETATM 2337 C  C3  A WWO D 3 .   ? 16.596  8.950   9.309   0.50 44.63  ? 303 WWO A C3  1 
HETATM 2338 C  C3  B WWO D 3 .   ? 16.516  8.988   9.348   0.50 12.88  ? 303 WWO A C3  1 
HETATM 2339 F  F12 A WWO D 3 .   ? 16.557  7.597   9.160   0.50 55.17  ? 303 WWO A F12 1 
HETATM 2340 F  F12 B WWO D 3 .   ? 16.585  7.730   9.012   0.50 14.45  ? 303 WWO A F12 1 
HETATM 2341 C  C2  A WWO D 3 .   ? 17.844  9.542   9.410   0.50 64.73  ? 303 WWO A C2  1 
HETATM 2342 C  C2  B WWO D 3 .   ? 17.706  9.636   9.578   0.50 16.32  ? 303 WWO A C2  1 
HETATM 2343 F  F13 A WWO D 3 .   ? 18.943  8.733   9.366   0.50 87.51  ? 303 WWO A F13 1 
HETATM 2344 F  F13 B WWO D 3 .   ? 18.843  8.936   9.475   0.50 19.65  ? 303 WWO A F13 1 
HETATM 2345 C  C6  A WWO D 3 .   ? 16.839  11.773  9.592   0.50 55.44  ? 303 WWO A C6  1 
HETATM 2346 C  C6  B WWO D 3 .   ? 16.684  11.700  10.002  0.50 16.14  ? 303 WWO A C6  1 
HETATM 2347 C  C1  A WWO D 3 .   ? 17.982  10.935  9.555   0.50 68.43  ? 303 WWO A C1  1 
HETATM 2348 C  C1  B WWO D 3 .   ? 17.862  10.981  9.877   0.50 17.84  ? 303 WWO A C1  1 
HETATM 2349 S  S11 A WWO D 3 .   ? 19.653  11.612  9.677   0.50 100.74 ? 303 WWO A S11 1 
HETATM 2350 S  S11 B WWO D 3 .   ? 19.566  11.515  10.148  0.50 33.87  ? 303 WWO A S11 1 
HETATM 2351 O  O22 A WWO D 3 .   ? 19.930  11.890  11.178  0.50 151.12 ? 303 WWO A O22 1 
HETATM 2352 O  O22 B WWO D 3 .   ? 19.568  13.066  10.328  0.50 42.88  ? 303 WWO A O22 1 
HETATM 2353 O  O23 A WWO D 3 .   ? 19.567  13.078  9.153   0.50 135.33 ? 303 WWO A O23 1 
HETATM 2354 O  O23 B WWO D 3 .   ? 20.448  11.320  8.881   0.50 44.93  ? 303 WWO A O23 1 
HETATM 2355 C  C21 A WWO D 3 .   ? 21.159  10.816  9.015   0.50 51.74  ? 303 WWO A C21 1 
HETATM 2356 C  C21 B WWO D 3 .   ? 20.686  10.887  11.472  0.50 33.48  ? 303 WWO A C21 1 
HETATM 2357 C  C24 A WWO D 3 .   ? 20.874  10.391  7.584   0.50 41.69  ? 303 WWO A C24 1 
HETATM 2358 C  C24 B WWO D 3 .   ? 19.940  10.056  12.503  0.50 23.37  ? 303 WWO A C24 1 
HETATM 2359 O  O25 A WWO D 3 .   ? 21.089  9.003   7.452   0.50 54.75  ? 303 WWO A O25 1 
HETATM 2360 O  O25 B WWO D 3 .   ? 20.116  10.449  13.830  0.50 25.60  ? 303 WWO A O25 1 
HETATM 2361 N  N26 A WWO D 3 .   ? 16.997  13.205  9.752   0.50 57.55  ? 303 WWO A N26 1 
HETATM 2362 N  N26 B WWO D 3 .   ? 16.693  13.027  10.343  0.50 19.79  ? 303 WWO A N26 1 
HETATM 2363 C  C14 A WWO D 3 .   ? 15.881  14.123  9.974   0.50 37.47  ? 303 WWO A C14 1 
HETATM 2364 C  C14 B WWO D 3 .   ? 15.879  14.138  9.874   0.50 29.00  ? 303 WWO A C14 1 
HETATM 2365 C  C15 A WWO D 3 .   ? 16.033  15.449  10.700  0.50 35.33  ? 303 WWO A C15 1 
HETATM 2366 C  C15 B WWO D 3 .   ? 15.977  15.456  10.616  0.50 22.30  ? 303 WWO A C15 1 
HETATM 2367 C  C20 A WWO D 3 .   ? 14.837  16.168  10.993  0.50 32.70  ? 303 WWO A C20 1 
HETATM 2368 C  C20 B WWO D 3 .   ? 14.800  16.129  11.058  0.50 20.53  ? 303 WWO A C20 1 
HETATM 2369 C  C19 A WWO D 3 .   ? 14.814  17.439  11.643  0.50 23.81  ? 303 WWO A C19 1 
HETATM 2370 C  C19 B WWO D 3 .   ? 14.816  17.436  11.685  0.50 17.77  ? 303 WWO A C19 1 
HETATM 2371 C  C18 A WWO D 3 .   ? 16.049  18.036  12.022  0.50 28.93  ? 303 WWO A C18 1 
HETATM 2372 C  C18 B WWO D 3 .   ? 16.059  18.094  11.975  0.50 22.48  ? 303 WWO A C18 1 
HETATM 2373 C  C17 A WWO D 3 .   ? 17.266  17.334  11.712  0.50 37.44  ? 303 WWO A C17 1 
HETATM 2374 C  C17 B WWO D 3 .   ? 17.260  17.434  11.452  0.50 22.48  ? 303 WWO A C17 1 
HETATM 2375 C  C16 A WWO D 3 .   ? 17.258  16.056  11.068  0.50 43.16  ? 303 WWO A C16 1 
HETATM 2376 C  C16 B WWO D 3 .   ? 17.192  16.141  10.843  0.50 20.81  ? 303 WWO A C16 1 
HETATM 2377 S  S   . DMS E 4 .   ? 22.256  -9.869  15.013  1.00 17.08  ? 304 DMS A S   1 
HETATM 2378 O  O   . DMS E 4 .   ? 22.833  -11.241 14.548  1.00 24.33  ? 304 DMS A O   1 
HETATM 2379 C  C1  . DMS E 4 .   ? 22.566  -9.797  16.631  1.00 17.45  ? 304 DMS A C1  1 
HETATM 2380 C  C2  . DMS E 4 .   ? 23.395  -8.704  14.622  1.00 18.30  ? 304 DMS A C2  1 
HETATM 2381 N  N1  . BCN F 5 .   ? 0.443   -12.855 23.391  1.00 24.65  ? 305 BCN A N1  1 
HETATM 2382 C  C1  . BCN F 5 .   ? 1.354   -12.247 24.391  1.00 26.02  ? 305 BCN A C1  1 
HETATM 2383 C  C2  . BCN F 5 .   ? 1.008   -13.221 25.490  1.00 32.91  ? 305 BCN A C2  1 
HETATM 2384 O  O21 . BCN F 5 .   ? 0.048   -14.085 25.412  1.00 40.52  ? 305 BCN A O21 1 
HETATM 2385 O  O22 . BCN F 5 .   ? 1.645   -13.150 26.501  1.00 28.94  ? 305 BCN A O22 1 
HETATM 2386 C  C3  . BCN F 5 .   ? -0.740  -12.117 22.980  1.00 20.63  ? 305 BCN A C3  1 
HETATM 2387 C  C4  . BCN F 5 .   ? -2.194  -12.654 23.209  1.00 38.97  ? 305 BCN A C4  1 
HETATM 2388 O  O4  . BCN F 5 .   ? -3.020  -12.712 22.012  1.00 46.39  ? 305 BCN A O4  1 
HETATM 2389 C  C5  . BCN F 5 .   ? 0.961   -13.794 22.425  1.00 16.54  ? 305 BCN A C5  1 
HETATM 2390 C  C6  . BCN F 5 .   ? 0.041   -14.822 21.727  1.00 46.49  ? 305 BCN A C6  1 
HETATM 2391 O  O6  . BCN F 5 .   ? 0.080   -14.530 20.316  1.00 47.28  ? 305 BCN A O6  1 
HETATM 2392 C  C1  . PEG G 6 .   ? 35.507  4.854   23.957  1.00 18.18  ? 306 PEG A C1  1 
HETATM 2393 O  O1  . PEG G 6 .   ? 34.721  4.151   22.974  1.00 19.38  ? 306 PEG A O1  1 
HETATM 2394 C  C2  . PEG G 6 .   ? 35.308  6.396   24.227  1.00 19.09  ? 306 PEG A C2  1 
HETATM 2395 O  O2  . PEG G 6 .   ? 35.083  7.055   25.573  1.00 25.31  ? 306 PEG A O2  1 
HETATM 2396 C  C3  . PEG G 6 .   ? 33.944  7.185   26.491  1.00 31.24  ? 306 PEG A C3  1 
HETATM 2397 C  C4  . PEG G 6 .   ? 33.361  5.886   27.181  1.00 26.85  ? 306 PEG A C4  1 
HETATM 2398 O  O4  . PEG G 6 .   ? 33.332  6.273   28.539  1.00 65.63  ? 306 PEG A O4  1 
HETATM 2399 C  C1  . EDO H 7 .   ? 8.501   8.967   31.039  1.00 16.90  ? 307 EDO A C1  1 
HETATM 2400 O  O1  . EDO H 7 .   ? 8.226   9.319   32.428  1.00 45.00  ? 307 EDO A O1  1 
HETATM 2401 C  C2  . EDO H 7 .   ? 8.006   10.082  30.057  1.00 10.88  ? 307 EDO A C2  1 
HETATM 2402 O  O2  . EDO H 7 .   ? 8.233   9.638   28.734  1.00 18.84  ? 307 EDO A O2  1 
HETATM 2403 C  C1  . EDO I 7 .   ? -2.975  -0.208  28.879  1.00 21.34  ? 308 EDO A C1  1 
HETATM 2404 O  O1  . EDO I 7 .   ? -3.107  -1.584  29.483  1.00 19.02  ? 308 EDO A O1  1 
HETATM 2405 C  C2  . EDO I 7 .   ? -3.224  0.057   27.358  1.00 21.59  ? 308 EDO A C2  1 
HETATM 2406 O  O2  . EDO I 7 .   ? -3.011  1.203   26.649  1.00 17.09  ? 308 EDO A O2  1 
HETATM 2407 N  N1  . BCN J 5 .   ? 18.653  -15.932 5.385   1.00 33.03  ? 309 BCN A N1  1 
HETATM 2408 C  C1  . BCN J 5 .   ? 17.948  -15.627 4.077   1.00 34.48  ? 309 BCN A C1  1 
HETATM 2409 C  C2  . BCN J 5 .   ? 16.730  -16.476 3.715   1.00 35.19  ? 309 BCN A C2  1 
HETATM 2410 O  O21 . BCN J 5 .   ? 15.600  -15.938 3.458   1.00 35.56  ? 309 BCN A O21 1 
HETATM 2411 O  O22 . BCN J 5 .   ? 16.838  -17.754 3.635   1.00 58.78  ? 309 BCN A O22 1 
HETATM 2412 C  C3  . BCN J 5 .   ? 18.552  -17.262 6.194   1.00 22.49  ? 309 BCN A C3  1 
HETATM 2413 C  C4  . BCN J 5 .   ? 17.481  -18.429 6.336   1.00 23.89  ? 309 BCN A C4  1 
HETATM 2414 O  O4  . BCN J 5 .   ? 16.916  -19.247 5.239   1.00 31.82  ? 309 BCN A O4  1 
HETATM 2415 C  C5  . BCN J 5 .   ? 20.133  -15.440 5.166   1.00 25.36  ? 309 BCN A C5  1 
HETATM 2416 C  C6  . BCN J 5 .   ? 21.180  -16.048 6.273   1.00 29.70  ? 309 BCN A C6  1 
HETATM 2417 O  O6  . BCN J 5 .   ? 22.408  -15.572 7.088   1.00 22.88  ? 309 BCN A O6  1 
HETATM 2418 N  N1  . BCN K 5 .   ? 12.716  -19.676 7.900   1.00 20.56  ? 310 BCN A N1  1 
HETATM 2419 C  C1  . BCN K 5 .   ? 14.018  -19.673 7.114   1.00 22.94  ? 310 BCN A C1  1 
HETATM 2420 C  C2  . BCN K 5 .   ? 13.937  -18.715 5.868   1.00 44.37  ? 310 BCN A C2  1 
HETATM 2421 O  O21 . BCN K 5 .   ? 13.229  -19.273 4.934   1.00 46.68  ? 310 BCN A O21 1 
HETATM 2422 O  O22 . BCN K 5 .   ? 14.542  -17.514 5.782   1.00 31.97  ? 310 BCN A O22 1 
HETATM 2423 C  C3  . BCN K 5 .   ? 13.032  -19.600 9.224   1.00 17.63  ? 310 BCN A C3  1 
HETATM 2424 C  C4  . BCN K 5 .   ? 13.089  -20.283 10.452  1.00 18.11  ? 310 BCN A C4  1 
HETATM 2425 O  O4  . BCN K 5 .   ? 13.693  -21.729 10.616  1.00 28.11  ? 310 BCN A O4  1 
HETATM 2426 C  C5  . BCN K 5 .   ? 11.508  -20.291 7.207   1.00 28.71  ? 310 BCN A C5  1 
HETATM 2427 C  C6  . BCN K 5 .   ? 11.591  -21.693 6.534   1.00 35.65  ? 310 BCN A C6  1 
HETATM 2428 O  O6  . BCN K 5 .   ? 10.962  -22.828 7.273   1.00 24.65  ? 310 BCN A O6  1 
HETATM 2429 O  O   . HOH L 8 .   ? -4.597  -8.748  17.821  1.00 23.26  ? 401 HOH A O   1 
HETATM 2430 O  O   . HOH L 8 .   ? 19.984  -15.664 17.989  1.00 32.20  ? 402 HOH A O   1 
HETATM 2431 O  O   . HOH L 8 .   ? -6.996  8.007   15.095  1.00 19.93  ? 403 HOH A O   1 
HETATM 2432 O  O   . HOH L 8 .   ? -4.949  7.995   27.064  1.00 25.06  ? 404 HOH A O   1 
HETATM 2433 O  O   . HOH L 8 .   ? 32.996  8.536   18.275  1.00 80.10  ? 405 HOH A O   1 
HETATM 2434 O  O   . HOH L 8 .   ? 16.689  0.585   37.856  1.00 26.88  ? 406 HOH A O   1 
HETATM 2435 O  O   . HOH L 8 .   ? 8.130   -0.379  39.318  1.00 31.51  ? 407 HOH A O   1 
HETATM 2436 O  O   . HOH L 8 .   ? 6.312   8.050   32.775  1.00 28.12  ? 408 HOH A O   1 
HETATM 2437 O  O   . HOH L 8 .   ? 3.962   19.699  22.205  1.00 21.68  ? 409 HOH A O   1 
HETATM 2438 O  O   . HOH L 8 .   ? 27.792  4.045   31.429  1.00 32.96  ? 410 HOH A O   1 
HETATM 2439 O  O   . HOH L 8 .   ? 6.737   -6.662  -5.481  1.00 33.33  ? 411 HOH A O   1 
HETATM 2440 O  O   . HOH L 8 .   ? 10.832  17.758  29.376  1.00 18.64  ? 412 HOH A O   1 
HETATM 2441 O  O   . HOH L 8 .   ? 0.204   -5.220  -1.921  1.00 27.36  ? 413 HOH A O   1 
HETATM 2442 O  O   . HOH L 8 .   ? 15.927  4.155   37.308  1.00 23.07  ? 414 HOH A O   1 
HETATM 2443 O  O   . HOH L 8 .   ? 4.667   7.161   -8.007  1.00 23.53  ? 415 HOH A O   1 
HETATM 2444 O  O   . HOH L 8 .   ? 10.424  -3.984  38.350  1.00 19.78  ? 416 HOH A O   1 
HETATM 2445 O  O   . HOH L 8 .   ? 34.296  2.258   24.652  1.00 16.44  ? 417 HOH A O   1 
HETATM 2446 O  O   . HOH L 8 .   ? 17.995  1.684   41.910  1.00 34.85  ? 418 HOH A O   1 
HETATM 2447 O  O   . HOH L 8 .   ? 9.832   -13.325 34.053  1.00 18.64  ? 419 HOH A O   1 
HETATM 2448 O  O   . HOH L 8 .   ? 31.446  -8.935  16.271  1.00 15.41  ? 420 HOH A O   1 
HETATM 2449 O  O   . HOH L 8 .   ? 8.668   14.219  29.228  1.00 19.45  ? 421 HOH A O   1 
HETATM 2450 O  O   . HOH L 8 .   ? 29.481  -3.256  -10.117 1.00 23.99  ? 422 HOH A O   1 
HETATM 2451 O  O   . HOH L 8 .   ? 3.863   -12.309 37.370  1.00 22.69  ? 423 HOH A O   1 
HETATM 2452 O  O   . HOH L 8 .   ? 25.194  -0.534  28.862  1.00 21.52  ? 424 HOH A O   1 
HETATM 2453 O  O   . HOH L 8 .   ? 3.855   -20.938 4.407   1.00 27.99  ? 425 HOH A O   1 
HETATM 2454 O  O   . HOH L 8 .   ? 0.550   10.286  30.135  1.00 22.21  ? 426 HOH A O   1 
HETATM 2455 O  O   . HOH L 8 .   ? 22.680  10.047  27.992  1.00 23.34  ? 427 HOH A O   1 
HETATM 2456 O  O   . HOH L 8 .   ? -2.271  2.140   34.693  1.00 25.48  ? 428 HOH A O   1 
HETATM 2457 O  O   . HOH L 8 .   ? 13.602  9.954   29.361  1.00 15.15  ? 429 HOH A O   1 
HETATM 2458 O  O   . HOH L 8 .   ? -3.230  10.498  20.282  1.00 15.46  ? 430 HOH A O   1 
HETATM 2459 O  O   . HOH L 8 .   ? -1.894  -13.184 16.212  1.00 28.94  ? 431 HOH A O   1 
HETATM 2460 O  O   . HOH L 8 .   ? -9.845  -10.784 21.375  1.00 34.81  ? 432 HOH A O   1 
HETATM 2461 O  O   . HOH L 8 .   ? 7.231   16.063  27.254  1.00 20.03  ? 433 HOH A O   1 
HETATM 2462 O  O   . HOH L 8 .   ? -6.371  -8.983  22.450  1.00 27.76  ? 434 HOH A O   1 
HETATM 2463 O  O   . HOH L 8 .   ? 25.521  1.142   35.704  1.00 41.36  ? 435 HOH A O   1 
HETATM 2464 O  O   . HOH L 8 .   ? -4.660  1.000   35.058  1.00 26.50  ? 436 HOH A O   1 
HETATM 2465 O  O   . HOH L 8 .   ? -3.985  -9.116  24.055  1.00 25.35  ? 437 HOH A O   1 
HETATM 2466 O  O   . HOH L 8 .   ? 22.477  4.093   35.929  1.00 41.57  ? 438 HOH A O   1 
HETATM 2467 O  O   . HOH L 8 .   ? 19.548  -2.143  15.893  1.00 7.89   ? 439 HOH A O   1 
HETATM 2468 O  O   . HOH L 8 .   ? 20.915  -12.481 31.047  1.00 28.26  ? 440 HOH A O   1 
HETATM 2469 O  O   . HOH L 8 .   ? 12.399  -1.904  7.976   1.00 6.90   ? 441 HOH A O   1 
HETATM 2470 O  O   . HOH L 8 .   ? -1.749  -4.155  2.721   1.00 15.02  ? 442 HOH A O   1 
HETATM 2471 O  O   . HOH L 8 .   ? 11.923  7.741   28.849  1.00 13.02  ? 443 HOH A O   1 
HETATM 2472 O  O   . HOH L 8 .   ? 25.133  -1.508  26.436  1.00 17.19  ? 444 HOH A O   1 
HETATM 2473 O  O   . HOH L 8 .   ? -6.392  -5.663  26.152  1.00 28.63  ? 445 HOH A O   1 
HETATM 2474 O  O   . HOH L 8 .   ? 8.815   -2.338  37.604  1.00 29.24  ? 446 HOH A O   1 
HETATM 2475 O  O   . HOH L 8 .   ? 21.538  5.127   5.819   1.00 27.74  ? 447 HOH A O   1 
HETATM 2476 O  O   . HOH L 8 .   ? 4.093   -12.113 26.385  1.00 17.09  ? 448 HOH A O   1 
HETATM 2477 O  O   . HOH L 8 .   ? 20.864  3.002   34.448  1.00 23.77  ? 449 HOH A O   1 
HETATM 2478 O  O   . HOH L 8 .   ? 24.475  6.972   29.774  1.00 13.21  ? 450 HOH A O   1 
HETATM 2479 O  O   . HOH L 8 .   ? -0.888  -12.381 18.691  1.00 25.33  ? 451 HOH A O   1 
HETATM 2480 O  O   . HOH L 8 .   ? 8.014   -20.406 8.480   1.00 18.90  ? 452 HOH A O   1 
HETATM 2481 O  O   . HOH L 8 .   ? 2.592   -1.678  45.213  1.00 29.13  ? 453 HOH A O   1 
HETATM 2482 O  O   . HOH L 8 .   ? 28.630  -5.488  -0.414  1.00 24.61  ? 454 HOH A O   1 
HETATM 2483 O  O   . HOH L 8 .   ? 23.496  2.071   7.691   1.00 30.79  ? 455 HOH A O   1 
HETATM 2484 O  O   . HOH L 8 .   ? 7.103   -19.220 3.585   1.00 32.11  ? 456 HOH A O   1 
HETATM 2485 O  O   . HOH L 8 .   ? 19.571  -11.219 -5.957  1.00 32.52  ? 457 HOH A O   1 
HETATM 2486 O  O   . HOH L 8 .   ? 16.914  22.469  15.851  1.00 24.94  ? 458 HOH A O   1 
HETATM 2487 O  O   . HOH L 8 .   ? 32.031  3.273   25.997  1.00 18.10  ? 459 HOH A O   1 
HETATM 2488 O  O   . HOH L 8 .   ? 20.583  -18.685 15.185  1.00 29.37  ? 460 HOH A O   1 
HETATM 2489 O  O   . HOH L 8 .   ? 16.607  -14.106 1.516   1.00 25.01  ? 461 HOH A O   1 
HETATM 2490 O  O   . HOH L 8 .   ? 13.899  -14.916 1.646   1.00 18.44  ? 462 HOH A O   1 
HETATM 2491 O  O   . HOH L 8 .   ? 10.385  10.550  25.383  1.00 8.28   ? 463 HOH A O   1 
HETATM 2492 O  O   . HOH L 8 .   ? 13.856  -13.011 31.549  1.00 19.34  ? 464 HOH A O   1 
HETATM 2493 O  O   . HOH L 8 .   ? 2.060   15.318  1.976   1.00 34.91  ? 465 HOH A O   1 
HETATM 2494 O  O   . HOH L 8 .   ? 12.417  -13.627 36.446  1.00 19.25  ? 466 HOH A O   1 
HETATM 2495 O  O   . HOH L 8 .   ? 11.255  3.553   38.840  1.00 22.38  ? 467 HOH A O   1 
HETATM 2496 O  O   . HOH L 8 .   ? 5.095   -8.347  38.217  1.00 28.21  ? 468 HOH A O   1 
HETATM 2497 O  O   . HOH L 8 .   ? 21.049  1.056   -4.665  1.00 12.69  ? 469 HOH A O   1 
HETATM 2498 O  O   . HOH L 8 .   ? 5.576   2.596   -4.920  1.00 29.25  ? 470 HOH A O   1 
HETATM 2499 O  O   . HOH L 8 .   ? 10.250  22.859  24.892  1.00 15.98  ? 471 HOH A O   1 
HETATM 2500 O  O   . HOH L 8 .   ? 12.963  -13.566 11.317  1.00 8.41   ? 472 HOH A O   1 
HETATM 2501 O  O   . HOH L 8 .   ? -5.345  4.742   21.132  1.00 15.63  ? 473 HOH A O   1 
HETATM 2502 O  O   . HOH L 8 .   ? 5.799   -9.389  -3.678  1.00 38.95  ? 474 HOH A O   1 
HETATM 2503 O  O   . HOH L 8 .   ? 22.863  -13.716 9.356   1.00 15.78  ? 475 HOH A O   1 
HETATM 2504 O  O   . HOH L 8 .   ? 0.816   12.615  26.857  1.00 14.77  ? 476 HOH A O   1 
HETATM 2505 O  O   . HOH L 8 .   ? 3.039   -18.592 8.109   1.00 12.11  ? 477 HOH A O   1 
HETATM 2506 O  O   . HOH L 8 .   ? 18.478  -17.268 21.559  1.00 28.26  ? 478 HOH A O   1 
HETATM 2507 O  O   . HOH L 8 .   ? 23.408  -11.359 5.301   1.00 14.74  ? 479 HOH A O   1 
HETATM 2508 O  O   . HOH L 8 .   ? -1.143  -16.503 13.616  1.00 16.38  ? 480 HOH A O   1 
HETATM 2509 O  O   . HOH L 8 .   ? 14.763  -2.643  -6.385  1.00 18.70  ? 481 HOH A O   1 
HETATM 2510 O  O   . HOH L 8 .   ? 10.196  -17.567 20.096  1.00 12.94  ? 482 HOH A O   1 
HETATM 2511 O  O   . HOH L 8 .   ? 8.424   14.956  31.873  1.00 19.58  ? 483 HOH A O   1 
HETATM 2512 O  O   . HOH L 8 .   ? 19.811  11.053  27.847  1.00 24.07  ? 484 HOH A O   1 
HETATM 2513 O  O   . HOH L 8 .   ? -2.433  -11.389 11.288  1.00 15.45  ? 485 HOH A O   1 
HETATM 2514 O  O   . HOH L 8 .   ? -0.233  9.680   1.909   1.00 11.84  ? 486 HOH A O   1 
HETATM 2515 O  O   . HOH L 8 .   ? 2.378   -19.587 14.656  1.00 16.38  ? 487 HOH A O   1 
HETATM 2516 O  O   . HOH L 8 .   ? -2.528  -9.200  17.228  1.00 18.16  ? 488 HOH A O   1 
HETATM 2517 O  O   . HOH L 8 .   ? 18.384  -6.888  29.121  1.00 9.78   ? 489 HOH A O   1 
HETATM 2518 O  O   . HOH L 8 .   ? 19.481  6.633   -4.837  1.00 19.64  ? 490 HOH A O   1 
HETATM 2519 O  O   . HOH L 8 .   ? 4.821   -10.487 24.425  1.00 11.92  ? 491 HOH A O   1 
HETATM 2520 O  O   . HOH L 8 .   ? 16.183  -10.184 32.163  1.00 17.13  ? 492 HOH A O   1 
HETATM 2521 O  O   . HOH L 8 .   ? 1.140   -2.459  41.277  1.00 26.45  ? 493 HOH A O   1 
HETATM 2522 O  O   . HOH L 8 .   ? -9.350  -5.241  22.532  1.00 25.60  ? 494 HOH A O   1 
HETATM 2523 O  O   . HOH L 8 .   ? 29.632  -1.859  21.184  1.00 11.07  ? 495 HOH A O   1 
HETATM 2524 O  O   . HOH L 8 .   ? 1.921   -19.098 5.436   1.00 20.37  ? 496 HOH A O   1 
HETATM 2525 O  O   . HOH L 8 .   ? 36.338  -0.487  14.554  1.00 14.75  ? 497 HOH A O   1 
HETATM 2526 O  O   . HOH L 8 .   ? 17.409  -10.928 -2.877  1.00 20.85  ? 498 HOH A O   1 
HETATM 2527 O  O   . HOH L 8 .   ? -4.746  9.959   6.233   1.00 33.87  ? 499 HOH A O   1 
HETATM 2528 O  O   . HOH L 8 .   ? 7.281   12.211  27.940  1.00 13.23  ? 500 HOH A O   1 
HETATM 2529 O  O   . HOH L 8 .   ? -2.813  1.773   1.274   1.00 26.13  ? 501 HOH A O   1 
HETATM 2530 O  O   . HOH L 8 .   ? 10.563  -16.419 17.062  1.00 10.96  ? 502 HOH A O   1 
HETATM 2531 O  O   . HOH L 8 .   ? 3.875   -6.583  20.412  1.00 7.21   ? 503 HOH A O   1 
HETATM 2532 O  O   . HOH L 8 .   ? -3.581  -8.406  15.241  1.00 35.25  ? 504 HOH A O   1 
HETATM 2533 O  O   . HOH L 8 .   ? 9.930   -17.513 7.102   1.00 22.51  ? 505 HOH A O   1 
HETATM 2534 O  O   . HOH L 8 .   ? 21.356  9.273   29.586  1.00 22.47  ? 506 HOH A O   1 
HETATM 2535 O  O   . HOH L 8 .   ? 14.027  23.111  19.531  1.00 12.41  ? 507 HOH A O   1 
HETATM 2536 O  O   . HOH L 8 .   ? 16.358  -11.684 18.036  1.00 7.83   ? 508 HOH A O   1 
HETATM 2537 O  O   . HOH L 8 .   ? 26.108  8.956   20.221  1.00 12.52  ? 509 HOH A O   1 
HETATM 2538 O  O   . HOH L 8 .   ? 6.243   -16.849 18.736  1.00 12.02  ? 510 HOH A O   1 
HETATM 2539 O  O   . HOH L 8 .   ? -6.222  -3.435  27.616  1.00 30.06  ? 511 HOH A O   1 
HETATM 2540 O  O   . HOH L 8 .   ? -0.677  -5.315  23.657  1.00 9.67   ? 512 HOH A O   1 
HETATM 2541 O  O   . HOH L 8 .   ? 17.384  -9.367  20.903  1.00 8.20   ? 513 HOH A O   1 
HETATM 2542 O  O   . HOH L 8 .   ? 16.653  -6.522  31.175  1.00 16.46  ? 514 HOH A O   1 
HETATM 2543 O  O   . HOH L 8 .   ? 4.497   -13.943 32.496  1.00 30.18  ? 515 HOH A O   1 
HETATM 2544 O  O   . HOH L 8 .   ? 2.717   -1.891  -2.551  1.00 21.16  ? 516 HOH A O   1 
HETATM 2545 O  O   . HOH L 8 .   ? 17.106  -14.057 24.332  1.00 11.60  ? 517 HOH A O   1 
HETATM 2546 O  O   . HOH L 8 .   ? 17.510  -11.444 25.185  1.00 9.46   ? 518 HOH A O   1 
HETATM 2547 O  O   . HOH L 8 .   ? 22.810  6.007   11.657  1.00 28.71  ? 519 HOH A O   1 
HETATM 2548 O  O   . HOH L 8 .   ? -1.061  7.562   4.809   1.00 12.29  ? 520 HOH A O   1 
HETATM 2549 O  O   . HOH L 8 .   ? 20.318  12.500  22.882  1.00 18.04  ? 521 HOH A O   1 
HETATM 2550 O  O   . HOH L 8 .   ? 20.000  15.250  16.382  1.00 24.86  ? 522 HOH A O   1 
HETATM 2551 O  O   . HOH L 8 .   ? -0.664  17.486  3.682   1.00 29.66  ? 523 HOH A O   1 
HETATM 2552 O  O   . HOH L 8 .   ? 12.210  2.568   -6.557  1.00 22.52  ? 524 HOH A O   1 
HETATM 2553 O  O   . HOH L 8 .   ? 14.358  -3.449  37.386  1.00 12.73  ? 525 HOH A O   1 
HETATM 2554 O  O   . HOH L 8 .   ? 30.018  9.436   18.363  1.00 32.30  ? 526 HOH A O   1 
HETATM 2555 O  O   . HOH L 8 .   ? 24.231  -7.187  26.678  1.00 35.98  ? 527 HOH A O   1 
HETATM 2556 O  O   . HOH L 8 .   ? 7.490   0.999   -6.162  1.00 25.53  ? 528 HOH A O   1 
HETATM 2557 O  O   . HOH L 8 .   ? -5.256  5.076   15.652  1.00 14.57  ? 529 HOH A O   1 
HETATM 2558 O  O   . HOH L 8 .   ? 22.145  -10.024 25.084  1.00 23.39  ? 530 HOH A O   1 
HETATM 2559 O  O   . HOH L 8 .   ? 5.346   10.767  -2.079  1.00 21.99  ? 531 HOH A O   1 
HETATM 2560 O  O   . HOH L 8 .   ? 6.529   -14.750 28.901  1.00 20.39  ? 532 HOH A O   1 
HETATM 2561 O  O   . HOH L 8 .   ? -2.203  -1.277  6.856   1.00 16.71  ? 533 HOH A O   1 
HETATM 2562 O  O   . HOH L 8 .   ? -3.969  -5.913  9.083   1.00 12.95  ? 534 HOH A O   1 
HETATM 2563 O  O   . HOH L 8 .   ? 1.721   -5.170  41.680  1.00 41.21  ? 535 HOH A O   1 
HETATM 2564 O  O   . HOH L 8 .   ? 7.086   22.054  15.274  1.00 14.29  ? 536 HOH A O   1 
HETATM 2565 O  O   . HOH L 8 .   ? 4.756   17.778  23.798  1.00 14.22  ? 537 HOH A O   1 
HETATM 2566 O  O   . HOH L 8 .   ? -3.736  6.518   8.562   1.00 29.96  ? 538 HOH A O   1 
HETATM 2567 O  O   . HOH L 8 .   ? 17.824  14.023  12.707  1.00 32.34  ? 539 HOH A O   1 
HETATM 2568 O  O   . HOH L 8 .   ? 32.836  1.688   16.074  1.00 17.58  ? 540 HOH A O   1 
HETATM 2569 O  O   . HOH L 8 .   ? 7.568   -16.674 14.662  1.00 12.13  ? 541 HOH A O   1 
HETATM 2570 O  O   . HOH L 8 .   ? 2.415   12.693  11.471  1.00 16.54  ? 542 HOH A O   1 
HETATM 2571 O  O   . HOH L 8 .   ? 15.298  18.918  27.428  1.00 22.27  ? 543 HOH A O   1 
HETATM 2572 O  O   . HOH L 8 .   ? -1.261  5.778   -3.042  1.00 21.46  ? 544 HOH A O   1 
HETATM 2573 O  O   . HOH L 8 .   ? 26.744  -10.282 -5.381  1.00 19.79  ? 545 HOH A O   1 
HETATM 2574 O  O   . HOH L 8 .   ? 27.929  -1.545  29.843  1.00 30.28  ? 546 HOH A O   1 
HETATM 2575 O  O   . HOH L 8 .   ? 19.103  -2.653  -7.142  1.00 21.53  ? 547 HOH A O   1 
HETATM 2576 O  O   . HOH L 8 .   ? 4.370   16.598  33.042  1.00 23.11  ? 548 HOH A O   1 
HETATM 2577 O  O   . HOH L 8 .   ? 7.891   -15.055 26.648  1.00 13.55  ? 549 HOH A O   1 
HETATM 2578 O  O   . HOH L 8 .   ? 14.043  -6.499  -7.011  1.00 32.80  ? 550 HOH A O   1 
HETATM 2579 O  O   . HOH L 8 .   ? -4.513  11.429  13.363  1.00 34.02  ? 551 HOH A O   1 
HETATM 2580 O  O   . HOH L 8 .   ? 18.427  -1.618  11.560  1.00 13.78  ? 552 HOH A O   1 
HETATM 2581 O  O   . HOH L 8 .   ? 22.513  -4.317  34.360  1.00 24.24  ? 553 HOH A O   1 
HETATM 2582 O  O   . HOH L 8 .   ? 23.534  -9.493  9.564   1.00 16.05  ? 554 HOH A O   1 
HETATM 2583 O  O   . HOH L 8 .   ? 0.724   15.542  29.001  1.00 44.11  ? 555 HOH A O   1 
HETATM 2584 O  O   . HOH L 8 .   ? 4.528   -8.092  32.924  1.00 14.22  ? 556 HOH A O   1 
HETATM 2585 O  O   . HOH L 8 .   ? 28.380  7.954   21.606  1.00 12.28  ? 557 HOH A O   1 
HETATM 2586 O  O   . HOH L 8 .   ? 11.740  -8.241  -1.159  1.00 23.22  ? 558 HOH A O   1 
HETATM 2587 O  O   . HOH L 8 .   ? 25.952  -3.119  21.193  1.00 11.11  ? 559 HOH A O   1 
HETATM 2588 O  O   . HOH L 8 .   ? 3.544   -14.409 22.010  1.00 17.74  ? 560 HOH A O   1 
HETATM 2589 O  O   . HOH L 8 .   ? 34.890  7.685   19.429  1.00 25.84  ? 561 HOH A O   1 
HETATM 2590 O  O   . HOH L 8 .   ? 28.960  5.216   27.800  1.00 26.64  ? 562 HOH A O   1 
HETATM 2591 O  O   . HOH L 8 .   ? 2.622   -10.652 -3.511  1.00 18.75  ? 563 HOH A O   1 
HETATM 2592 O  O   . HOH L 8 .   ? 13.493  -6.811  32.619  1.00 13.30  ? 564 HOH A O   1 
HETATM 2593 O  O   . HOH L 8 .   ? 8.152   -7.042  -3.194  1.00 25.01  ? 565 HOH A O   1 
HETATM 2594 O  O   . HOH L 8 .   ? 23.313  -4.742  -7.448  1.00 43.73  ? 566 HOH A O   1 
HETATM 2595 O  O   . HOH L 8 .   ? 30.968  2.157   14.284  1.00 29.63  ? 567 HOH A O   1 
HETATM 2596 O  O   . HOH L 8 .   ? 20.675  3.141   -10.811 1.00 22.18  ? 568 HOH A O   1 
HETATM 2597 O  O   . HOH L 8 .   ? -3.616  -16.425 13.710  1.00 36.85  ? 569 HOH A O   1 
HETATM 2598 O  O   . HOH L 8 .   ? 24.555  -0.044  8.823   1.00 18.83  ? 570 HOH A O   1 
HETATM 2599 O  O   . HOH L 8 .   ? -0.777  21.556  12.027  1.00 25.14  ? 571 HOH A O   1 
HETATM 2600 O  O   . HOH L 8 .   ? 14.342  16.675  28.668  1.00 22.24  ? 572 HOH A O   1 
HETATM 2601 O  O   . HOH L 8 .   ? 23.891  2.999   -1.871  1.00 25.14  ? 573 HOH A O   1 
HETATM 2602 O  O   . HOH L 8 .   ? 2.092   5.301   -3.203  1.00 67.93  ? 574 HOH A O   1 
HETATM 2603 O  O   . HOH L 8 .   ? 1.643   11.899  8.923   1.00 10.77  ? 575 HOH A O   1 
HETATM 2604 O  O   . HOH L 8 .   ? 5.580   21.310  13.141  1.00 12.07  ? 576 HOH A O   1 
HETATM 2605 O  O   . HOH L 8 .   ? 16.279  1.514   11.175  1.00 14.24  ? 577 HOH A O   1 
HETATM 2606 O  O   . HOH L 8 .   ? 24.265  -1.371  4.753   1.00 24.12  ? 578 HOH A O   1 
HETATM 2607 O  O   . HOH L 8 .   ? 29.181  -7.435  16.656  1.00 18.63  ? 579 HOH A O   1 
HETATM 2608 O  O   . HOH L 8 .   ? 3.950   -9.714  36.380  1.00 25.82  ? 580 HOH A O   1 
HETATM 2609 O  O   . HOH L 8 .   ? -5.052  -4.471  12.908  1.00 20.87  ? 581 HOH A O   1 
HETATM 2610 O  O   . HOH L 8 .   ? 10.145  11.119  8.187   1.00 29.30  ? 582 HOH A O   1 
HETATM 2611 O  O   . HOH L 8 .   ? -5.860  -1.966  25.287  1.00 16.75  ? 583 HOH A O   1 
HETATM 2612 O  O   . HOH L 8 .   ? 20.617  -12.522 22.195  1.00 15.88  ? 584 HOH A O   1 
HETATM 2613 O  O   . HOH L 8 .   ? 9.898   2.945   33.436  1.00 19.06  ? 585 HOH A O   1 
HETATM 2614 O  O   . HOH L 8 .   ? 9.038   4.594   30.861  1.00 14.15  ? 586 HOH A O   1 
HETATM 2615 O  O   . HOH L 8 .   ? 25.350  6.278   10.822  1.00 42.32  ? 587 HOH A O   1 
HETATM 2616 O  O   . HOH L 8 .   ? 34.010  -1.672  13.496  1.00 31.34  ? 588 HOH A O   1 
HETATM 2617 O  O   . HOH L 8 .   ? 25.846  -5.772  22.362  1.00 26.20  ? 589 HOH A O   1 
HETATM 2618 O  O   . HOH L 8 .   ? 22.122  0.413   29.471  1.00 12.46  ? 590 HOH A O   1 
HETATM 2619 O  O   . HOH L 8 .   ? -2.087  -9.992  14.010  1.00 19.02  ? 591 HOH A O   1 
HETATM 2620 O  O   . HOH L 8 .   ? 7.526   -14.850 0.016   1.00 34.46  ? 592 HOH A O   1 
HETATM 2621 O  O   . HOH L 8 .   ? 11.824  -3.888  36.027  1.00 14.21  ? 593 HOH A O   1 
HETATM 2622 O  O   . HOH L 8 .   ? 22.317  10.642  23.585  1.00 14.38  ? 594 HOH A O   1 
HETATM 2623 O  O   . HOH L 8 .   ? 2.819   -6.086  39.106  1.00 28.35  ? 595 HOH A O   1 
HETATM 2624 O  O   . HOH L 8 .   ? 9.690   19.847  12.389  1.00 20.33  ? 596 HOH A O   1 
HETATM 2625 O  O   . HOH L 8 .   ? 19.677  5.306   1.780   1.00 24.90  ? 597 HOH A O   1 
HETATM 2626 O  O   . HOH L 8 .   ? 20.323  -6.686  32.598  1.00 21.40  ? 598 HOH A O   1 
HETATM 2627 O  O   . HOH L 8 .   ? 15.809  -1.226  11.538  1.00 11.96  ? 599 HOH A O   1 
HETATM 2628 O  O   . HOH L 8 .   ? 4.153   0.607   40.050  1.00 31.80  ? 600 HOH A O   1 
HETATM 2629 O  O   . HOH L 8 .   ? -4.992  -4.512  33.615  1.00 39.82  ? 601 HOH A O   1 
HETATM 2630 O  O   . HOH L 8 .   ? 13.919  3.253   35.025  1.00 21.01  ? 602 HOH A O   1 
HETATM 2631 O  O   . HOH L 8 .   ? 15.339  5.191   -5.855  1.00 68.63  ? 603 HOH A O   1 
HETATM 2632 O  O   . HOH L 8 .   ? 35.890  -8.381  14.624  1.00 21.72  ? 604 HOH A O   1 
HETATM 2633 O  O   . HOH L 8 .   ? -1.918  17.559  18.970  1.00 39.72  ? 605 HOH A O   1 
HETATM 2634 O  O   . HOH L 8 .   ? 7.056   16.592  6.291   1.00 34.50  ? 606 HOH A O   1 
HETATM 2635 O  O   . HOH L 8 .   ? 18.229  -16.209 30.949  1.00 24.47  ? 607 HOH A O   1 
HETATM 2636 O  O   . HOH L 8 .   ? 12.211  -18.047 26.700  1.00 23.01  ? 608 HOH A O   1 
HETATM 2637 O  O   . HOH L 8 .   ? 25.185  -4.784  8.076   1.00 22.98  ? 609 HOH A O   1 
HETATM 2638 O  O   . HOH L 8 .   ? 5.823   22.087  17.719  1.00 12.80  ? 610 HOH A O   1 
HETATM 2639 O  O   . HOH L 8 .   ? -2.495  1.712   32.134  1.00 25.60  ? 611 HOH A O   1 
HETATM 2640 O  O   . HOH L 8 .   ? 8.117   5.351   -6.802  1.00 21.88  ? 612 HOH A O   1 
HETATM 2641 O  O   . HOH L 8 .   ? 17.304  -2.636  37.752  1.00 30.81  ? 613 HOH A O   1 
HETATM 2642 O  O   . HOH L 8 .   ? 18.822  -10.499 22.897  1.00 8.71   ? 614 HOH A O   1 
HETATM 2643 O  O   . HOH L 8 .   ? -0.166  -17.841 6.690   1.00 20.68  ? 615 HOH A O   1 
HETATM 2644 O  O   . HOH L 8 .   ? 3.410   7.265   -3.464  1.00 22.99  ? 616 HOH A O   1 
HETATM 2645 O  O   . HOH L 8 .   ? -3.712  -7.640  1.984   1.00 19.52  ? 617 HOH A O   1 
HETATM 2646 O  O   . HOH L 8 .   ? 31.070  -0.680  14.099  1.00 19.78  ? 618 HOH A O   1 
HETATM 2647 O  O   . HOH L 8 .   ? -5.363  -5.613  30.493  1.00 27.37  ? 619 HOH A O   1 
HETATM 2648 O  O   . HOH L 8 .   ? 24.064  -12.577 1.531   1.00 20.46  ? 620 HOH A O   1 
HETATM 2649 O  O   . HOH L 8 .   ? 8.654   18.628  11.028  1.00 27.89  ? 621 HOH A O   1 
HETATM 2650 O  O   . HOH L 8 .   ? 12.673  -17.546 21.717  1.00 12.78  ? 622 HOH A O   1 
HETATM 2651 O  O   . HOH L 8 .   ? 26.097  11.450  16.141  1.00 41.27  ? 623 HOH A O   1 
HETATM 2652 O  O   . HOH L 8 .   ? 18.172  -13.123 32.695  1.00 29.17  ? 624 HOH A O   1 
HETATM 2653 O  O   . HOH L 8 .   ? 15.666  -11.702 34.356  1.00 30.93  ? 625 HOH A O   1 
HETATM 2654 O  O   . HOH L 8 .   ? 11.027  17.201  12.060  1.00 17.80  ? 626 HOH A O   1 
HETATM 2655 O  O   . HOH L 8 .   ? 19.239  13.206  14.672  1.00 25.49  ? 627 HOH A O   1 
HETATM 2656 O  O   . HOH L 8 .   ? 12.491  10.972  -2.808  1.00 34.20  ? 628 HOH A O   1 
HETATM 2657 O  O   . HOH L 8 .   ? 13.578  -6.700  -2.294  1.00 24.97  ? 629 HOH A O   1 
HETATM 2658 O  O   . HOH L 8 .   ? 11.387  -6.082  34.234  1.00 16.64  ? 630 HOH A O   1 
HETATM 2659 O  O   . HOH L 8 .   ? 31.337  -4.241  -8.310  1.00 37.62  ? 631 HOH A O   1 
HETATM 2660 O  O   . HOH L 8 .   ? 8.106   20.933  12.406  1.00 19.62  ? 632 HOH A O   1 
HETATM 2661 O  O   . HOH L 8 .   ? 31.414  -7.394  8.907   1.00 34.74  ? 633 HOH A O   1 
HETATM 2662 O  O   . HOH L 8 .   ? 0.236   2.253   0.094   1.00 37.28  ? 634 HOH A O   1 
HETATM 2663 O  O   . HOH L 8 .   ? 19.353  13.012  25.368  1.00 20.47  ? 635 HOH A O   1 
HETATM 2664 O  O   . HOH L 8 .   ? 10.586  8.056   -3.911  1.00 38.02  ? 636 HOH A O   1 
HETATM 2665 O  O   . HOH L 8 .   ? -7.088  -10.155 15.671  1.00 33.19  ? 637 HOH A O   1 
HETATM 2666 O  O   . HOH L 8 .   ? 20.764  -13.666 27.330  1.00 39.06  ? 638 HOH A O   1 
HETATM 2667 O  O   . HOH L 8 .   ? 31.160  8.611   15.310  1.00 37.67  ? 639 HOH A O   1 
HETATM 2668 O  O   . HOH L 8 .   ? 2.095   -17.987 20.290  1.00 45.93  ? 640 HOH A O   1 
HETATM 2669 O  O   . HOH L 8 .   ? 30.403  3.870   12.063  1.00 32.00  ? 641 HOH A O   1 
HETATM 2670 O  O   . HOH L 8 .   ? 21.208  2.781   -6.769  1.00 23.48  ? 642 HOH A O   1 
HETATM 2671 O  O   . HOH L 8 .   ? 29.634  -2.591  23.793  1.00 20.47  ? 643 HOH A O   1 
HETATM 2672 O  O   . HOH L 8 .   ? -4.664  13.696  17.015  1.00 34.10  ? 644 HOH A O   1 
HETATM 2673 O  O   . HOH L 8 .   ? -5.941  -14.022 10.794  1.00 38.49  ? 645 HOH A O   1 
HETATM 2674 O  O   . HOH L 8 .   ? -4.477  6.439   4.090   1.00 31.34  ? 646 HOH A O   1 
HETATM 2675 O  O   . HOH L 8 .   ? 25.529  -7.913  8.292   1.00 35.23  ? 647 HOH A O   1 
HETATM 2676 O  O   . HOH L 8 .   ? 3.080   -6.993  34.977  1.00 33.48  ? 648 HOH A O   1 
HETATM 2677 O  O   . HOH L 8 .   ? 8.039   -15.400 17.009  1.00 10.45  ? 649 HOH A O   1 
HETATM 2678 O  O   . HOH L 8 .   ? 23.325  -12.762 -1.126  1.00 30.67  ? 650 HOH A O   1 
HETATM 2679 O  O   . HOH L 8 .   ? -1.406  -10.476 25.014  1.00 28.69  ? 651 HOH A O   1 
HETATM 2680 O  O   . HOH L 8 .   ? 4.344   -13.173 28.613  1.00 30.12  ? 652 HOH A O   1 
HETATM 2681 O  O   . HOH L 8 .   ? 24.939  13.216  21.078  1.00 42.65  ? 653 HOH A O   1 
HETATM 2682 O  O   . HOH L 8 .   ? -1.724  -7.746  25.393  1.00 16.85  ? 654 HOH A O   1 
HETATM 2683 O  O   . HOH L 8 .   ? 4.031   -2.406  -5.132  1.00 31.94  ? 655 HOH A O   1 
HETATM 2684 O  O   . HOH L 8 .   ? 15.867  22.701  21.508  1.00 20.98  ? 656 HOH A O   1 
HETATM 2685 O  O   . HOH L 8 .   ? 2.879   -10.091 31.484  1.00 21.64  ? 657 HOH A O   1 
HETATM 2686 O  O   . HOH L 8 .   ? 35.673  2.158   15.138  1.00 15.85  ? 658 HOH A O   1 
HETATM 2687 O  O   . HOH L 8 .   ? 29.132  8.577   25.966  1.00 37.84  ? 659 HOH A O   1 
HETATM 2688 O  O   . HOH L 8 .   ? -4.437  12.979  19.642  1.00 24.61  ? 660 HOH A O   1 
HETATM 2689 O  O   . HOH L 8 .   ? 19.453  -11.202 27.155  1.00 22.66  ? 661 HOH A O   1 
HETATM 2690 O  O   . HOH L 8 .   ? 21.150  -0.781  39.388  1.00 43.35  ? 662 HOH A O   1 
HETATM 2691 O  O   . HOH L 8 .   ? 10.397  6.893   30.792  1.00 16.88  ? 663 HOH A O   1 
HETATM 2692 O  O   . HOH L 8 .   ? 18.993  20.412  15.560  1.00 32.91  ? 664 HOH A O   1 
HETATM 2693 O  O   . HOH L 8 .   ? 30.289  -7.819  0.751   1.00 35.72  ? 665 HOH A O   1 
HETATM 2694 O  O   . HOH L 8 .   ? -3.814  11.190  26.496  1.00 44.06  ? 666 HOH A O   1 
HETATM 2695 O  O   . HOH L 8 .   ? 17.764  8.777   5.770   1.00 39.06  ? 667 HOH A O   1 
HETATM 2696 O  O   . HOH L 8 .   ? 3.134   21.870  17.435  1.00 18.08  ? 668 HOH A O   1 
HETATM 2697 O  O   . HOH L 8 .   ? 35.223  8.301   22.022  1.00 24.86  ? 669 HOH A O   1 
HETATM 2698 O  O   . HOH L 8 .   ? 23.384  -1.087  37.353  1.00 39.73  ? 670 HOH A O   1 
HETATM 2699 O  O   . HOH L 8 .   ? 23.819  -11.563 8.048   1.00 22.68  ? 671 HOH A O   1 
HETATM 2700 O  O   . HOH L 8 .   ? 26.545  -11.531 2.503   1.00 21.82  ? 672 HOH A O   1 
HETATM 2701 O  O   . HOH L 8 .   ? 23.793  -2.354  7.490   1.00 22.92  ? 673 HOH A O   1 
HETATM 2702 O  O   . HOH L 8 .   ? -6.014  -4.717  4.967   1.00 28.61  ? 674 HOH A O   1 
HETATM 2703 O  O   . HOH L 8 .   ? -3.408  15.397  20.331  1.00 31.85  ? 675 HOH A O   1 
HETATM 2704 O  O   . HOH L 8 .   ? 24.251  1.130   5.692   1.00 32.98  ? 676 HOH A O   1 
HETATM 2705 O  O   . HOH L 8 .   ? 31.120  -1.061  -9.532  1.00 32.76  ? 677 HOH A O   1 
HETATM 2706 O  O   . HOH L 8 .   ? 16.574  -3.719  -7.910  1.00 33.30  ? 678 HOH A O   1 
HETATM 2707 O  O   . HOH L 8 .   ? 29.209  9.790   23.377  1.00 39.78  ? 679 HOH A O   1 
HETATM 2708 O  O   . HOH L 8 .   ? 4.352   -15.878 24.076  1.00 25.02  ? 680 HOH A O   1 
HETATM 2709 O  O   . HOH L 8 .   ? 3.991   -16.142 20.169  1.00 20.40  ? 681 HOH A O   1 
HETATM 2710 O  O   . HOH L 8 .   ? 21.378  -13.948 24.205  1.00 39.87  ? 682 HOH A O   1 
HETATM 2711 O  O   . HOH L 8 .   ? 1.024   -0.501  43.088  1.00 34.77  ? 683 HOH A O   1 
HETATM 2712 O  O   . HOH L 8 .   ? 19.708  -11.411 32.997  1.00 23.35  ? 684 HOH A O   1 
HETATM 2713 O  O   . HOH L 8 .   ? 27.315  -3.366  27.487  1.00 42.45  ? 685 HOH A O   1 
HETATM 2714 O  O   . HOH L 8 .   ? 18.926  -15.656 25.501  1.00 25.07  ? 686 HOH A O   1 
HETATM 2715 O  O   . HOH L 8 .   ? -11.189 7.758   13.184  1.00 40.19  ? 687 HOH A O   1 
HETATM 2716 O  O   . HOH L 8 .   ? 3.145   -12.417 30.692  1.00 27.67  ? 688 HOH A O   1 
HETATM 2717 O  O   . HOH L 8 .   ? 5.428   -14.525 25.989  1.00 30.29  ? 689 HOH A O   1 
HETATM 2718 O  O   . HOH L 8 .   ? 4.675   18.824  26.349  1.00 31.55  ? 690 HOH A O   1 
HETATM 2719 O  O   . HOH L 8 .   ? 5.682   -16.052 -2.126  1.00 48.61  ? 691 HOH A O   1 
HETATM 2720 O  O   . HOH L 8 .   ? 7.157   5.482   33.123  1.00 23.68  ? 692 HOH A O   1 
HETATM 2721 O  O   . HOH L 8 .   ? 16.098  -7.816  33.420  1.00 21.68  ? 693 HOH A O   1 
HETATM 2722 O  O   . HOH L 8 .   ? 36.254  0.701   26.151  1.00 20.19  ? 694 HOH A O   1 
HETATM 2723 O  O   . HOH L 8 .   ? -8.075  -3.775  24.727  1.00 20.19  ? 695 HOH A O   1 
HETATM 2724 O  O   . HOH L 8 .   ? 11.720  4.964   34.707  1.00 19.40  ? 696 HOH A O   1 
HETATM 2725 O  O   . HOH L 8 .   ? -3.151  -5.182  0.419   1.00 26.17  ? 697 HOH A O   1 
HETATM 2726 O  O   . HOH L 8 .   ? 18.731  -9.826  31.637  1.00 29.19  ? 698 HOH A O   1 
HETATM 2727 O  O   . HOH L 8 .   ? 9.295   2.788   -7.676  1.00 31.73  ? 699 HOH A O   1 
HETATM 2728 O  O   . HOH L 8 .   ? 26.790  -9.144  16.918  1.00 42.53  ? 700 HOH A O   1 
HETATM 2729 O  O   . HOH L 8 .   ? -6.718  -5.149  7.648   1.00 30.02  ? 701 HOH A O   1 
HETATM 2730 O  O   . HOH L 8 .   ? 22.357  -8.036  31.017  1.00 52.30  ? 702 HOH A O   1 
HETATM 2731 O  O   . HOH L 8 .   ? 4.253   21.645  23.373  1.00 29.62  ? 703 HOH A O   1 
HETATM 2732 O  O   . HOH L 8 .   ? 16.352  -6.037  -8.471  1.00 46.74  ? 704 HOH A O   1 
HETATM 2733 O  O   . HOH L 8 .   ? 9.401   13.299  34.243  1.00 32.92  ? 705 HOH A O   1 
HETATM 2734 O  O   . HOH L 8 .   ? 24.976  -10.003 23.514  1.00 39.72  ? 706 HOH A O   1 
HETATM 2735 O  O   . HOH L 8 .   ? 22.842  -12.411 20.626  1.00 27.27  ? 707 HOH A O   1 
HETATM 2736 O  O   . HOH L 8 .   ? 23.372  10.944  30.307  1.00 36.11  ? 708 HOH A O   1 
HETATM 2737 O  O   . HOH L 8 .   ? -0.175  -18.911 14.483  1.00 26.26  ? 709 HOH A O   1 
HETATM 2738 O  O   . HOH L 8 .   ? 22.384  5.144   2.062   1.00 33.21  ? 710 HOH A O   1 
HETATM 2739 O  O   . HOH L 8 .   ? 7.853   23.723  25.893  1.00 21.29  ? 711 HOH A O   1 
HETATM 2740 O  O   . HOH L 8 .   ? 19.713  -9.251  29.024  1.00 14.90  ? 712 HOH A O   1 
HETATM 2741 O  O   . HOH L 8 .   ? 14.661  -19.126 26.296  1.00 28.81  ? 713 HOH A O   1 
HETATM 2742 O  O   . HOH L 8 .   ? 13.662  -8.169  -4.586  1.00 38.56  ? 714 HOH A O   1 
HETATM 2743 O  O   . HOH L 8 .   ? 30.027  -11.201 16.316  1.00 33.91  ? 715 HOH A O   1 
HETATM 2744 O  O   . HOH L 8 .   ? 27.358  10.369  18.276  1.00 23.52  ? 716 HOH A O   1 
HETATM 2745 O  O   . HOH L 8 .   ? 22.921  11.581  26.057  1.00 23.89  ? 717 HOH A O   1 
HETATM 2746 O  O   . HOH L 8 .   ? 27.079  7.513   28.943  1.00 72.32  ? 718 HOH A O   1 
HETATM 2747 O  O   . HOH L 8 .   ? 2.455   4.483   -6.328  1.00 55.35  ? 719 HOH A O   1 
HETATM 2748 O  O   . HOH L 8 .   ? 24.320  4.914   -0.012  1.00 32.52  ? 720 HOH A O   1 
HETATM 2749 O  O   . HOH L 8 .   ? 24.944  10.601  22.261  1.00 19.20  ? 721 HOH A O   1 
HETATM 2750 O  O   . HOH L 8 .   ? 19.203  -15.027 34.301  1.00 29.33  ? 722 HOH A O   1 
HETATM 2751 O  O   . HOH L 8 .   ? 20.502  -5.161  -7.511  1.00 35.02  ? 723 HOH A O   1 
HETATM 2752 O  O   . HOH L 8 .   ? 8.501   15.714  4.509   1.00 40.04  ? 724 HOH A O   1 
HETATM 2753 O  O   . HOH L 8 .   ? 18.307  -7.472  34.637  1.00 25.76  ? 725 HOH A O   1 
HETATM 2754 O  O   . HOH L 8 .   ? 34.915  0.851   28.597  1.00 36.93  ? 726 HOH A O   1 
HETATM 2755 O  O   . HOH L 8 .   ? 27.051  10.971  24.178  1.00 31.47  ? 727 HOH A O   1 
HETATM 2756 O  O   . HOH L 8 .   ? 20.670  -12.982 34.703  1.00 49.90  ? 728 HOH A O   1 
HETATM 2757 O  O   . HOH L 8 .   ? 0.628   -12.184 37.521  1.00 33.39  ? 729 HOH A O   1 
HETATM 2758 O  O   . HOH L 8 .   ? 33.204  -8.000  -5.828  1.00 25.08  ? 730 HOH A O   1 
HETATM 2759 O  O   . HOH L 8 .   ? 32.799  -9.340  -3.379  1.00 16.95  ? 731 HOH A O   1 
HETATM 2760 O  O   . HOH L 8 .   ? 18.421  -10.365 34.752  1.00 36.89  ? 732 HOH A O   1 
HETATM 2761 O  O   . HOH L 8 .   ? 32.765  -8.019  -0.937  1.00 24.04  ? 733 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 3   ? 0.3783 0.4343 0.1861 -0.0844 0.0653  -0.0299 3   HIS A N   
2    C  CA  . HIS A 3   ? 0.2266 0.2955 0.3420 0.0388  0.0152  -0.0439 3   HIS A CA  
3    C  C   . HIS A 3   ? 0.2273 0.4578 0.2840 0.0186  0.0166  -0.0024 3   HIS A C   
4    O  O   . HIS A 3   ? 0.5199 0.5073 0.3161 -0.0406 -0.0992 -0.0760 3   HIS A O   
5    C  CB  . HIS A 3   ? 0.2648 0.3398 0.3201 -0.0231 -0.0113 0.0124  3   HIS A CB  
6    C  CG  . HIS A 3   ? 0.1644 0.4352 0.2585 0.0351  -0.0476 0.0230  3   HIS A CG  
7    N  ND1 . HIS A 3   ? 0.2745 0.5317 0.2737 -0.0674 0.0215  -0.0230 3   HIS A ND1 
8    C  CD2 . HIS A 3   ? 0.1524 0.3709 0.2946 -0.0794 -0.0227 -0.0727 3   HIS A CD2 
9    C  CE1 . HIS A 3   ? 0.2106 0.3643 0.3639 0.0225  0.0724  0.0275  3   HIS A CE1 
10   N  NE2 . HIS A 3   ? 0.1997 0.3971 0.4052 -0.0059 0.0753  0.0159  3   HIS A NE2 
11   N  N   . HIS A 4   ? 0.1729 0.6621 0.4111 -0.0260 0.0707  0.1074  4   HIS A N   
12   C  CA  . HIS A 4   ? 0.1904 0.5242 0.4029 -0.0436 0.1704  0.1374  4   HIS A CA  
13   C  C   . HIS A 4   ? 0.1655 0.2700 0.3488 -0.0288 0.1098  0.0104  4   HIS A C   
14   O  O   . HIS A 4   ? 0.2134 0.2640 0.2662 -0.0111 0.1002  0.0153  4   HIS A O   
15   C  CB  . HIS A 4   ? 0.4133 2.0692 1.2881 0.2574  -0.0231 0.8047  4   HIS A CB  
16   C  CG  . HIS A 4   ? 0.5820 1.9314 0.9391 0.1650  -0.0456 1.1092  4   HIS A CG  
17   N  ND1 . HIS A 4   ? 0.5572 1.6937 1.1258 0.3039  -0.0361 0.9149  4   HIS A ND1 
18   C  CD2 . HIS A 4   ? 0.4826 1.8233 1.8135 0.1155  -0.0154 0.6434  4   HIS A CD2 
19   C  CE1 . HIS A 4   ? 0.1142 2.3608 2.0280 0.0746  -0.4028 0.2966  4   HIS A CE1 
20   N  NE2 . HIS A 4   ? 1.3753 1.1260 1.4009 -0.2373 0.3463  0.1562  4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.1293 0.3183 0.2399 -0.0035 0.0693  0.0414  5   TRP A N   
22   C  CA  . TRP A 5   ? 0.1207 0.2407 0.1802 -0.0240 0.0403  0.0024  5   TRP A CA  
23   C  C   . TRP A 5   ? 0.1206 0.2157 0.1462 0.0208  0.0164  0.0151  5   TRP A C   
24   O  O   . TRP A 5   ? 0.1618 0.2138 0.1712 0.0080  0.0373  0.0249  5   TRP A O   
25   C  CB  . TRP A 5   ? 0.1002 0.1821 0.1762 0.0024  0.0250  -0.0015 5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1209 0.1571 0.1387 0.0000  0.0204  0.0171  5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.1436 0.1946 0.1596 -0.0046 0.0222  0.0405  5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.1080 0.1553 0.1185 -0.0019 0.0175  -0.0041 5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.1729 0.1784 0.1536 0.0113  0.0335  0.0421  5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.1371 0.1692 0.1128 0.0076  0.0164  0.0234  5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.1049 0.1564 0.1256 -0.0080 0.0193  -0.0194 5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.1377 0.2273 0.1094 0.0377  -0.0086 -0.0131 5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.1150 0.1800 0.1116 -0.0003 0.0007  -0.0353 5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.1059 0.2166 0.1081 0.0131  -0.0015 -0.0200 5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.1371 0.1803 0.1517 0.0276  0.0230  -0.0013 6   GLY A N   
36   C  CA  . GLY A 6   ? 0.1518 0.1961 0.1333 0.0157  0.0237  -0.0013 6   GLY A CA  
37   C  C   . GLY A 6   ? 0.1136 0.1817 0.1252 0.0263  0.0195  -0.0269 6   GLY A C   
38   O  O   . GLY A 6   ? 0.1102 0.1896 0.1405 0.0231  0.0197  -0.0089 6   GLY A O   
39   N  N   . TYR A 7   ? 0.1291 0.1764 0.1667 0.0136  0.0491  -0.0315 7   TYR A N   
40   C  CA  . TYR A 7   ? 0.1306 0.1780 0.2228 0.0359  0.0390  -0.0340 7   TYR A CA  
41   C  C   . TYR A 7   ? 0.1553 0.1785 0.2506 0.0291  0.0272  -0.0201 7   TYR A C   
42   O  O   . TYR A 7   ? 0.1737 0.2202 0.3276 0.0263  0.0542  -0.0138 7   TYR A O   
43   C  CB  . TYR A 7   ? 0.1479 0.1771 0.1933 0.0113  0.0269  -0.0626 7   TYR A CB  
44   C  CG  . TYR A 7   ? 0.1025 0.1492 0.1307 -0.0052 0.0146  -0.0443 7   TYR A CG  
45   C  CD1 . TYR A 7   ? 0.1004 0.1372 0.1269 0.0000  0.0007  -0.0181 7   TYR A CD1 
46   C  CD2 . TYR A 7   ? 0.1024 0.1724 0.1127 -0.0162 0.0164  -0.0247 7   TYR A CD2 
47   C  CE1 . TYR A 7   ? 0.0920 0.1092 0.1076 -0.0100 0.0049  -0.0043 7   TYR A CE1 
48   C  CE2 . TYR A 7   ? 0.1150 0.1456 0.1058 -0.0187 0.0100  0.0041  7   TYR A CE2 
49   C  CZ  . TYR A 7   ? 0.0955 0.1111 0.0875 -0.0074 0.0015  -0.0071 7   TYR A CZ  
50   O  OH  . TYR A 7   ? 0.1167 0.0940 0.1007 -0.0077 0.0086  0.0093  7   TYR A OH  
51   N  N   . GLY A 8   ? 0.1776 0.2367 0.2491 0.0797  0.0725  -0.0131 8   GLY A N   
52   C  CA  . GLY A 8   ? 0.2056 0.2818 0.2874 0.0631  0.0685  -0.0560 8   GLY A CA  
53   C  C   . GLY A 8   ? 0.2439 0.1749 0.2380 0.0734  0.0803  -0.0253 8   GLY A C   
54   O  O   . GLY A 8   ? 0.1731 0.2047 0.2196 0.0204  0.0631  -0.0315 8   GLY A O   
55   N  N   . LYS A 9   ? 0.2170 0.2151 0.2317 0.0648  0.0206  -0.0439 9   LYS A N   
56   C  CA  . LYS A 9   ? 0.2728 0.1635 0.2206 0.0355  -0.0401 -0.0068 9   LYS A CA  
57   C  C   . LYS A 9   ? 0.1898 0.1633 0.2186 0.0566  0.0658  0.0153  9   LYS A C   
58   O  O   . LYS A 9   ? 0.1823 0.2052 0.2119 -0.0080 0.0573  0.0060  9   LYS A O   
59   C  CB  . LYS A 9   ? 0.2032 0.2788 0.3343 0.0597  -0.0450 -0.0108 9   LYS A CB  
60   C  CG  . LYS A 9   ? 0.2748 0.3014 0.4399 0.0873  -0.1057 -0.0450 9   LYS A CG  
61   C  CD  . LYS A 9   ? 0.3738 0.2940 0.5401 0.0868  0.0386  0.0760  9   LYS A CD  
62   C  CE  . LYS A 9   ? 0.3844 0.5099 0.6344 0.0970  0.0401  0.2561  9   LYS A CE  
63   N  NZ  . LYS A 9   ? 0.8379 0.8368 0.6574 -0.4144 0.0901  0.3116  9   LYS A NZ  
64   N  N   A HIS A 10  ? 0.1157 0.1699 0.2637 0.0537  0.0789  0.0456  10  HIS A N   
65   N  N   B HIS A 10  ? 0.0784 0.1667 0.1951 0.0085  0.0105  -0.0218 10  HIS A N   
66   C  CA  A HIS A 10  ? 0.1244 0.1560 0.1643 0.0229  0.0027  0.0172  10  HIS A CA  
67   C  CA  B HIS A 10  ? 0.0614 0.1983 0.1229 -0.0164 0.0074  -0.0065 10  HIS A CA  
68   C  C   A HIS A 10  ? 0.1758 0.2017 0.1855 0.0974  0.0584  0.0205  10  HIS A C   
69   C  C   B HIS A 10  ? 0.1089 0.1676 0.1226 0.0015  0.0351  -0.0176 10  HIS A C   
70   O  O   A HIS A 10  ? 0.1413 0.2203 0.1877 0.0274  0.0125  -0.0289 10  HIS A O   
71   O  O   B HIS A 10  ? 0.1014 0.1693 0.1676 0.0111  0.0096  -0.0071 10  HIS A O   
72   C  CB  A HIS A 10  ? 0.1078 0.1890 0.1513 0.0423  0.0076  -0.0421 10  HIS A CB  
73   C  CB  B HIS A 10  ? 0.0718 0.1621 0.1199 0.0057  0.0137  0.0082  10  HIS A CB  
74   C  CG  A HIS A 10  ? 0.1484 0.1350 0.1638 -0.0242 0.0340  -0.0087 10  HIS A CG  
75   C  CG  B HIS A 10  ? 0.0701 0.1550 0.1508 -0.0094 0.0073  -0.0007 10  HIS A CG  
76   N  ND1 A HIS A 10  ? 0.1604 0.1597 0.2029 -0.0005 0.0249  -0.0057 10  HIS A ND1 
77   N  ND1 B HIS A 10  ? 0.1110 0.1431 0.1543 -0.0031 -0.0052 -0.0031 10  HIS A ND1 
78   C  CD2 A HIS A 10  ? 0.2037 0.1492 0.2535 -0.0221 0.0223  -0.0759 10  HIS A CD2 
79   C  CD2 B HIS A 10  ? 0.1377 0.1711 0.1341 -0.0031 0.0210  -0.0282 10  HIS A CD2 
80   C  CE1 A HIS A 10  ? 0.1491 0.2263 0.2567 0.0092  0.0610  -0.0551 10  HIS A CE1 
81   C  CE1 B HIS A 10  ? 0.1105 0.1198 0.2195 0.0104  0.0184  -0.0092 10  HIS A CE1 
82   N  NE2 A HIS A 10  ? 0.2111 0.1847 0.3316 0.0102  0.0021  -0.1203 10  HIS A NE2 
83   N  NE2 B HIS A 10  ? 0.1416 0.1181 0.2217 -0.0263 0.0263  -0.0276 10  HIS A NE2 
84   N  N   . ASN A 11  ? 0.1395 0.2232 0.1967 0.0738  0.0684  0.0417  11  ASN A N   
85   C  CA  . ASN A 11  ? 0.1407 0.2034 0.1676 0.0489  0.0560  0.0294  11  ASN A CA  
86   C  C   . ASN A 11  ? 0.1261 0.1835 0.1477 0.0384  0.0346  0.0154  11  ASN A C   
87   O  O   . ASN A 11  ? 0.1316 0.1792 0.1583 0.0361  0.0419  0.0043  11  ASN A O   
88   C  CB  . ASN A 11  ? 0.1615 0.2217 0.1703 0.0702  0.0392  0.0147  11  ASN A CB  
89   C  CG  . ASN A 11  ? 0.1924 0.2518 0.1446 0.0672  0.0776  -0.0120 11  ASN A CG  
90   O  OD1 . ASN A 11  ? 0.1807 0.2682 0.1993 0.0241  0.0416  0.0049  11  ASN A OD1 
91   N  ND2 . ASN A 11  ? 0.2657 0.3348 0.1777 0.0538  0.0694  0.0344  11  ASN A ND2 
92   N  N   . GLY A 12  ? 0.1128 0.2038 0.1562 0.0226  0.0318  0.0046  12  GLY A N   
93   C  CA  . GLY A 12  ? 0.1225 0.2001 0.1350 0.0274  0.0350  -0.0037 12  GLY A CA  
94   C  C   . GLY A 12  ? 0.0931 0.1661 0.1308 0.0222  0.0220  0.0132  12  GLY A C   
95   O  O   . GLY A 12  ? 0.0779 0.1583 0.1600 0.0043  0.0111  0.0137  12  GLY A O   
96   N  N   . PRO A 13  ? 0.0926 0.1335 0.1376 0.0041  0.0129  -0.0031 13  PRO A N   
97   C  CA  . PRO A 13  ? 0.0905 0.1218 0.1457 0.0085  0.0193  0.0000  13  PRO A CA  
98   C  C   . PRO A 13  ? 0.0911 0.1441 0.1310 0.0010  0.0154  0.0003  13  PRO A C   
99   O  O   . PRO A 13  ? 0.0936 0.1679 0.1506 -0.0054 0.0111  -0.0174 13  PRO A O   
100  C  CB  . PRO A 13  ? 0.0989 0.1257 0.1429 -0.0013 0.0186  -0.0073 13  PRO A CB  
101  C  CG  . PRO A 13  ? 0.1079 0.1544 0.1467 -0.0151 0.0147  -0.0046 13  PRO A CG  
102  C  CD  . PRO A 13  ? 0.1226 0.1527 0.1571 0.0062  0.0281  -0.0141 13  PRO A CD  
103  N  N   . GLU A 14  ? 0.1213 0.1277 0.1633 0.0195  0.0144  0.0185  14  GLU A N   
104  C  CA  . GLU A 14  ? 0.1122 0.1482 0.2099 0.0148  -0.0187 0.0366  14  GLU A CA  
105  C  C   . GLU A 14  ? 0.1005 0.1257 0.1837 0.0250  0.0102  0.0100  14  GLU A C   
106  O  O   . GLU A 14  ? 0.1096 0.1661 0.1765 0.0233  -0.0183 0.0211  14  GLU A O   
107  C  CB  . GLU A 14  ? 0.1806 0.1400 0.3244 0.0120  -0.0860 0.0505  14  GLU A CB  
108  C  CG  . GLU A 14  ? 0.2730 0.2100 0.3149 -0.0351 -0.0917 0.0430  14  GLU A CG  
109  C  CD  . GLU A 14  ? 0.4304 0.4697 0.4135 -0.2133 -0.0706 0.1585  14  GLU A CD  
110  O  OE1 . GLU A 14  ? 0.6272 0.4796 0.3145 -0.1914 0.0507  0.1298  14  GLU A OE1 
111  O  OE2 . GLU A 14  ? 0.5067 0.4977 0.7192 -0.3260 -0.0194 0.1635  14  GLU A OE2 
112  N  N   . HIS A 15  ? 0.1013 0.1244 0.1567 0.0275  -0.0021 0.0070  15  HIS A N   
113  C  CA  . HIS A 15  ? 0.0800 0.1261 0.1533 0.0124  0.0060  0.0085  15  HIS A CA  
114  C  C   . HIS A 15  ? 0.0679 0.1345 0.1397 0.0108  0.0091  0.0057  15  HIS A C   
115  O  O   . HIS A 15  ? 0.0608 0.1580 0.1568 0.0156  0.0104  0.0132  15  HIS A O   
116  C  CB  . HIS A 15  ? 0.0921 0.1665 0.1530 0.0333  0.0119  0.0154  15  HIS A CB  
117  C  CG  . HIS A 15  ? 0.1032 0.1336 0.1689 0.0348  0.0054  0.0035  15  HIS A CG  
118  N  ND1 . HIS A 15  ? 0.0931 0.1658 0.1909 0.0219  0.0149  -0.0103 15  HIS A ND1 
119  C  CD2 . HIS A 15  ? 0.1101 0.1449 0.1923 0.0275  0.0026  0.0146  15  HIS A CD2 
120  C  CE1 . HIS A 15  ? 0.1250 0.1456 0.2044 0.0342  0.0100  0.0015  15  HIS A CE1 
121  N  NE2 . HIS A 15  ? 0.1451 0.1620 0.1934 0.0307  0.0135  -0.0176 15  HIS A NE2 
122  N  N   . TRP A 16  ? 0.0662 0.1301 0.1406 0.0147  0.0086  0.0066  16  TRP A N   
123  C  CA  . TRP A 16  ? 0.0582 0.1165 0.1406 0.0065  -0.0026 0.0023  16  TRP A CA  
124  C  C   . TRP A 16  ? 0.0510 0.1254 0.1269 0.0076  0.0026  0.0007  16  TRP A C   
125  O  O   . TRP A 16  ? 0.0681 0.1253 0.1358 0.0049  -0.0054 0.0071  16  TRP A O   
126  C  CB  . TRP A 16  ? 0.0620 0.1298 0.1271 0.0046  0.0017  -0.0040 16  TRP A CB  
127  C  CG  . TRP A 16  ? 0.0646 0.1042 0.1191 0.0035  0.0068  0.0077  16  TRP A CG  
128  C  CD1 . TRP A 16  ? 0.0707 0.1474 0.1229 0.0133  0.0148  0.0020  16  TRP A CD1 
129  C  CD2 . TRP A 16  ? 0.0593 0.1011 0.1246 0.0081  0.0054  0.0052  16  TRP A CD2 
130  N  NE1 . TRP A 16  ? 0.0726 0.1479 0.1180 0.0088  0.0071  -0.0023 16  TRP A NE1 
131  C  CE2 . TRP A 16  ? 0.0796 0.1099 0.1099 0.0137  0.0143  -0.0007 16  TRP A CE2 
132  C  CE3 . TRP A 16  ? 0.0599 0.1048 0.1152 0.0073  0.0083  0.0046  16  TRP A CE3 
133  C  CZ2 . TRP A 16  ? 0.0758 0.1049 0.1204 -0.0017 0.0104  -0.0031 16  TRP A CZ2 
134  C  CZ3 . TRP A 16  ? 0.0734 0.1033 0.1208 -0.0017 0.0119  0.0076  16  TRP A CZ3 
135  C  CH2 . TRP A 16  ? 0.0750 0.1067 0.1162 0.0031  -0.0015 0.0077  16  TRP A CH2 
136  N  N   . HIS A 17  ? 0.0636 0.1312 0.1286 0.0060  0.0037  0.0049  17  HIS A N   
137  C  CA  . HIS A 17  ? 0.0639 0.1429 0.1231 -0.0035 0.0001  -0.0028 17  HIS A CA  
138  C  C   . HIS A 17  ? 0.0647 0.1407 0.1492 0.0019  -0.0107 0.0055  17  HIS A C   
139  O  O   . HIS A 17  ? 0.0619 0.1615 0.1697 -0.0108 0.0006  0.0066  17  HIS A O   
140  C  CB  . HIS A 17  ? 0.0750 0.1647 0.1250 0.0099  0.0001  0.0031  17  HIS A CB  
141  C  CG  . HIS A 17  ? 0.0882 0.1685 0.1383 0.0155  0.0023  0.0318  17  HIS A CG  
142  N  ND1 . HIS A 17  ? 0.0776 0.2029 0.1644 0.0149  -0.0203 0.0304  17  HIS A ND1 
143  C  CD2 . HIS A 17  ? 0.0999 0.1759 0.1618 0.0315  0.0006  0.0491  17  HIS A CD2 
144  C  CE1 . HIS A 17  ? 0.0946 0.1982 0.1772 0.0359  -0.0031 0.0458  17  HIS A CE1 
145  N  NE2 . HIS A 17  ? 0.1048 0.1912 0.1518 0.0339  0.0088  0.0425  17  HIS A NE2 
146  N  N   . LYS A 18  ? 0.0511 0.1492 0.1482 0.0049  -0.0008 0.0184  18  LYS A N   
147  C  CA  . LYS A 18  ? 0.0564 0.1679 0.1578 -0.0024 0.0027  0.0109  18  LYS A CA  
148  C  C   . LYS A 18  ? 0.0628 0.1641 0.1787 -0.0149 0.0000  0.0270  18  LYS A C   
149  O  O   . LYS A 18  ? 0.1128 0.1929 0.2795 -0.0507 -0.0522 0.0803  18  LYS A O   
150  C  CB  . LYS A 18  ? 0.0672 0.1793 0.1722 0.0187  0.0189  0.0463  18  LYS A CB  
151  C  CG  . LYS A 18  ? 0.0762 0.2241 0.1591 0.0339  0.0065  0.0485  18  LYS A CG  
152  C  CD  . LYS A 18  ? 0.0646 0.2142 0.1738 0.0147  -0.0003 0.0562  18  LYS A CD  
153  C  CE  . LYS A 18  ? 0.0812 0.1648 0.1655 0.0326  0.0209  0.0472  18  LYS A CE  
154  N  NZ  . LYS A 18  ? 0.0799 0.1836 0.1668 0.0383  0.0114  0.0546  18  LYS A NZ  
155  N  N   . ASP A 19  ? 0.0685 0.1782 0.1510 0.0052  0.0003  0.0215  19  ASP A N   
156  C  CA  . ASP A 19  ? 0.0848 0.1709 0.1701 0.0024  -0.0035 0.0342  19  ASP A CA  
157  C  C   . ASP A 19  ? 0.0711 0.1436 0.1914 -0.0120 0.0013  0.0292  19  ASP A C   
158  O  O   . ASP A 19  ? 0.1155 0.1317 0.2307 -0.0152 0.0260  0.0423  19  ASP A O   
159  C  CB  . ASP A 19  ? 0.1000 0.2020 0.1604 0.0287  0.0162  0.0383  19  ASP A CB  
160  C  CG  . ASP A 19  ? 0.1359 0.3070 0.2099 0.0118  0.0401  -0.0174 19  ASP A CG  
161  O  OD1 . ASP A 19  ? 0.1234 0.3028 0.2569 0.0216  0.0597  0.0851  19  ASP A OD1 
162  O  OD2 . ASP A 19  ? 0.2240 0.5473 0.4304 -0.0516 0.1303  -0.2021 19  ASP A OD2 
163  N  N   . PHE A 20  ? 0.0670 0.1401 0.1527 -0.0138 -0.0001 0.0087  20  PHE A N   
164  C  CA  . PHE A 20  ? 0.0658 0.1351 0.1645 -0.0030 0.0012  0.0087  20  PHE A CA  
165  C  C   . PHE A 20  ? 0.0668 0.1319 0.1580 -0.0035 -0.0052 0.0003  20  PHE A C   
166  O  O   . PHE A 20  ? 0.0815 0.1225 0.1413 -0.0085 0.0041  0.0003  20  PHE A O   
167  C  CB  . PHE A 20  ? 0.0680 0.1464 0.1521 -0.0144 -0.0013 0.0137  20  PHE A CB  
168  C  CG  . PHE A 20  ? 0.0628 0.1685 0.1625 -0.0252 -0.0054 0.0337  20  PHE A CG  
169  C  CD1 . PHE A 20  ? 0.0926 0.1832 0.2159 -0.0230 -0.0088 0.0700  20  PHE A CD1 
170  C  CD2 . PHE A 20  ? 0.0650 0.2182 0.1559 -0.0263 0.0013  0.0100  20  PHE A CD2 
171  C  CE1 . PHE A 20  ? 0.1040 0.2214 0.2247 -0.0436 -0.0159 0.0659  20  PHE A CE1 
172  C  CE2 . PHE A 20  ? 0.0776 0.2396 0.1685 -0.0408 -0.0062 0.0218  20  PHE A CE2 
173  C  CZ  . PHE A 20  ? 0.1084 0.2533 0.1964 -0.0562 -0.0228 0.0878  20  PHE A CZ  
174  N  N   A PRO A 21  ? 0.0617 0.1274 0.1652 -0.0109 -0.0189 0.0116  21  PRO A N   
175  N  N   B PRO A 21  ? 0.0937 0.1321 0.1474 -0.0176 -0.0129 0.0055  21  PRO A N   
176  C  CA  A PRO A 21  ? 0.0723 0.1350 0.1544 -0.0241 -0.0203 0.0133  21  PRO A CA  
177  C  CA  B PRO A 21  ? 0.0780 0.1291 0.1624 -0.0024 -0.0078 0.0252  21  PRO A CA  
178  C  C   A PRO A 21  ? 0.0876 0.1235 0.1577 -0.0227 -0.0103 0.0113  21  PRO A C   
179  C  C   B PRO A 21  ? 0.0719 0.1055 0.1474 -0.0031 -0.0157 0.0110  21  PRO A C   
180  O  O   A PRO A 21  ? 0.0750 0.1037 0.1591 -0.0137 -0.0260 -0.0003 21  PRO A O   
181  O  O   B PRO A 21  ? 0.0645 0.1058 0.1315 0.0034  -0.0156 0.0024  21  PRO A O   
182  C  CB  A PRO A 21  ? 0.0579 0.1825 0.1677 -0.0540 -0.0287 0.0505  21  PRO A CB  
183  C  CB  B PRO A 21  ? 0.1196 0.1469 0.1924 -0.0260 -0.0379 0.0318  21  PRO A CB  
184  C  CG  A PRO A 21  ? 0.0926 0.1495 0.2199 -0.0595 -0.0410 -0.0041 21  PRO A CG  
185  C  CG  B PRO A 21  ? 0.1571 0.2551 0.1747 -0.0768 -0.0445 0.0449  21  PRO A CG  
186  C  CD  A PRO A 21  ? 0.0702 0.1556 0.1943 -0.0307 -0.0208 0.0269  21  PRO A CD  
187  C  CD  B PRO A 21  ? 0.1080 0.1659 0.1699 -0.0604 -0.0111 0.0057  21  PRO A CD  
188  N  N   A ILE A 22  ? 0.0680 0.1263 0.1181 -0.0248 -0.0082 0.0082  22  ILE A N   
189  N  N   B ILE A 22  ? 0.0777 0.1174 0.1146 -0.0087 -0.0212 -0.0049 22  ILE A N   
190  C  CA  A ILE A 22  ? 0.0487 0.1186 0.1571 -0.0046 -0.0121 0.0024  22  ILE A CA  
191  C  CA  B ILE A 22  ? 0.1094 0.1277 0.0957 -0.0115 -0.0092 -0.0252 22  ILE A CA  
192  C  C   A ILE A 22  ? 0.0610 0.1104 0.1234 -0.0043 -0.0074 -0.0089 22  ILE A C   
193  C  C   B ILE A 22  ? 0.0780 0.1163 0.1013 -0.0138 -0.0162 -0.0071 22  ILE A C   
194  O  O   A ILE A 22  ? 0.0585 0.1095 0.1406 -0.0032 -0.0136 0.0034  22  ILE A O   
195  O  O   B ILE A 22  ? 0.0890 0.1129 0.1097 -0.0081 -0.0073 -0.0049 22  ILE A O   
196  C  CB  A ILE A 22  ? 0.0648 0.1168 0.1370 -0.0220 -0.0142 -0.0027 22  ILE A CB  
197  C  CB  B ILE A 22  ? 0.1328 0.1136 0.1060 -0.0052 -0.0111 -0.0230 22  ILE A CB  
198  C  CG1 A ILE A 22  ? 0.0756 0.1016 0.1442 -0.0151 -0.0027 -0.0212 22  ILE A CG1 
199  C  CG1 B ILE A 22  ? 0.1507 0.1337 0.1626 0.0027  0.0074  -0.0291 22  ILE A CG1 
200  C  CG2 A ILE A 22  ? 0.0564 0.1283 0.1279 0.0017  -0.0078 0.0252  22  ILE A CG2 
201  C  CG2 B ILE A 22  ? 0.1550 0.1287 0.1198 -0.0496 -0.0251 -0.0055 22  ILE A CG2 
202  C  CD1 A ILE A 22  ? 0.0932 0.1014 0.1771 -0.0071 -0.0060 0.0049  22  ILE A CD1 
203  C  CD1 B ILE A 22  ? 0.1876 0.2229 0.2070 0.0425  0.0161  -0.0694 22  ILE A CD1 
204  N  N   . ALA A 23  ? 0.0680 0.1255 0.1234 -0.0057 -0.0083 -0.0135 23  ALA A N   
205  C  CA  . ALA A 23  ? 0.0743 0.1155 0.1270 -0.0006 -0.0060 -0.0152 23  ALA A CA  
206  C  C   . ALA A 23  ? 0.0573 0.1398 0.1432 -0.0013 -0.0077 -0.0212 23  ALA A C   
207  O  O   . ALA A 23  ? 0.0807 0.1306 0.1377 -0.0063 -0.0026 -0.0081 23  ALA A O   
208  C  CB  . ALA A 23  ? 0.0670 0.1365 0.1391 -0.0074 -0.0038 -0.0161 23  ALA A CB  
209  N  N   . LYS A 24  ? 0.0891 0.1269 0.1191 0.0043  -0.0154 -0.0087 24  LYS A N   
210  C  CA  . LYS A 24  ? 0.0865 0.1500 0.1322 0.0097  -0.0108 -0.0065 24  LYS A CA  
211  C  C   . LYS A 24  ? 0.0992 0.1652 0.1326 -0.0017 -0.0253 -0.0222 24  LYS A C   
212  O  O   . LYS A 24  ? 0.1145 0.2011 0.1272 0.0086  -0.0164 -0.0133 24  LYS A O   
213  C  CB  . LYS A 24  ? 0.1053 0.1764 0.1475 0.0154  -0.0329 0.0000  24  LYS A CB  
214  C  CG  . LYS A 24  ? 0.1171 0.1993 0.1662 0.0303  -0.0155 0.0114  24  LYS A CG  
215  C  CD  . LYS A 24  ? 0.1175 0.2660 0.2488 0.0643  0.0038  0.0364  24  LYS A CD  
216  C  CE  . LYS A 24  ? 0.1859 0.2524 0.2240 0.0529  0.0350  0.0732  24  LYS A CE  
217  N  NZ  . LYS A 24  ? 0.2124 0.2689 0.3474 -0.0068 0.0741  -0.0684 24  LYS A NZ  
218  N  N   . GLY A 25  ? 0.0847 0.1615 0.1290 0.0020  -0.0120 -0.0193 25  GLY A N   
219  C  CA  . GLY A 25  ? 0.0991 0.1595 0.1430 -0.0137 -0.0113 -0.0247 25  GLY A CA  
220  C  C   . GLY A 25  ? 0.0854 0.1653 0.1213 -0.0162 -0.0198 -0.0294 25  GLY A C   
221  O  O   . GLY A 25  ? 0.1106 0.1623 0.1212 0.0006  -0.0186 -0.0129 25  GLY A O   
222  N  N   . GLU A 26  ? 0.0873 0.1828 0.1121 -0.0005 -0.0168 -0.0302 26  GLU A N   
223  C  CA  . GLU A 26  ? 0.1164 0.1703 0.0983 -0.0082 -0.0236 -0.0281 26  GLU A CA  
224  C  C   . GLU A 26  ? 0.1114 0.1659 0.1018 -0.0026 -0.0044 -0.0318 26  GLU A C   
225  O  O   . GLU A 26  ? 0.1395 0.1882 0.0865 -0.0125 -0.0218 -0.0136 26  GLU A O   
226  C  CB  . GLU A 26  ? 0.1246 0.2217 0.1384 -0.0118 -0.0300 -0.0733 26  GLU A CB  
227  C  CG  . GLU A 26  ? 0.1518 0.2802 0.1580 -0.0344 -0.0579 -0.0753 26  GLU A CG  
228  C  CD  . GLU A 26  ? 0.2010 0.4104 0.1678 0.0005  -0.1103 -0.0577 26  GLU A CD  
229  O  OE1 . GLU A 26  ? 0.3097 0.3384 0.2480 0.0251  -0.0502 -0.0505 26  GLU A OE1 
230  O  OE2 . GLU A 26  ? 0.2093 0.4643 0.3689 0.0671  -0.0920 0.0193  26  GLU A OE2 
231  N  N   . ARG A 27  ? 0.0964 0.1274 0.0854 0.0000  -0.0252 -0.0249 27  ARG A N   
232  C  CA  . ARG A 27  ? 0.0887 0.1011 0.0899 0.0032  -0.0052 -0.0153 27  ARG A CA  
233  C  C   . ARG A 27  ? 0.0860 0.0901 0.0803 -0.0083 0.0015  -0.0166 27  ARG A C   
234  O  O   . ARG A 27  ? 0.0787 0.1055 0.0808 0.0048  -0.0110 -0.0183 27  ARG A O   
235  C  CB  . ARG A 27  ? 0.1066 0.1255 0.0856 0.0019  -0.0076 -0.0225 27  ARG A CB  
236  C  CG  . ARG A 27  ? 0.1322 0.1095 0.1207 0.0051  -0.0187 -0.0076 27  ARG A CG  
237  C  CD  . ARG A 27  ? 0.1586 0.1150 0.1097 -0.0043 -0.0220 -0.0092 27  ARG A CD  
238  N  NE  . ARG A 27  ? 0.1313 0.1078 0.0946 0.0000  0.0035  -0.0086 27  ARG A NE  
239  C  CZ  . ARG A 27  ? 0.1275 0.1190 0.0855 0.0137  0.0142  -0.0006 27  ARG A CZ  
240  N  NH1 . ARG A 27  ? 0.1701 0.1451 0.1453 0.0242  -0.0041 -0.0652 27  ARG A NH1 
241  N  NH2 . ARG A 27  ? 0.1181 0.1273 0.1345 0.0031  0.0085  -0.0333 27  ARG A NH2 
242  N  N   . GLN A 28  ? 0.0732 0.1014 0.0773 -0.0037 -0.0074 -0.0153 28  GLN A N   
243  C  CA  . GLN A 28  ? 0.0668 0.0918 0.0772 -0.0080 -0.0006 -0.0212 28  GLN A CA  
244  C  C   . GLN A 28  ? 0.0664 0.0900 0.0761 0.0046  0.0052  -0.0054 28  GLN A C   
245  O  O   . GLN A 28  ? 0.0892 0.1011 0.0740 -0.0085 -0.0165 -0.0062 28  GLN A O   
246  C  CB  . GLN A 28  ? 0.0645 0.1067 0.0948 0.0031  -0.0080 -0.0051 28  GLN A CB  
247  C  CG  . GLN A 28  ? 0.0678 0.1140 0.0980 0.0006  -0.0103 -0.0100 28  GLN A CG  
248  C  CD  . GLN A 28  ? 0.0617 0.0969 0.0958 0.0000  -0.0105 -0.0153 28  GLN A CD  
249  O  OE1 . GLN A 28  ? 0.0734 0.1041 0.0960 -0.0091 -0.0027 -0.0131 28  GLN A OE1 
250  N  NE2 . GLN A 28  ? 0.0712 0.0936 0.1084 -0.0077 0.0013  -0.0138 28  GLN A NE2 
251  N  N   . SER A 29  ? 0.0671 0.0848 0.0709 0.0020  -0.0041 -0.0062 29  SER A N   
252  C  CA  . SER A 29  ? 0.0675 0.0750 0.0719 0.0021  -0.0017 -0.0037 29  SER A CA  
253  C  C   . SER A 29  ? 0.0599 0.0777 0.0735 0.0037  -0.0074 0.0000  29  SER A C   
254  O  O   . SER A 29  ? 0.0640 0.0811 0.0831 0.0027  -0.0013 -0.0062 29  SER A O   
255  C  CB  . SER A 29  ? 0.0671 0.0715 0.0791 0.0055  -0.0031 -0.0065 29  SER A CB  
256  O  OG  . SER A 29  ? 0.0703 0.0729 0.0841 0.0052  0.0020  -0.0089 29  SER A OG  
257  N  N   . PRO A 30  ? 0.0666 0.0707 0.0701 0.0003  -0.0063 -0.0038 30  PRO A N   
258  C  CA  . PRO A 30  ? 0.0678 0.0706 0.0723 0.0043  0.0046  -0.0003 30  PRO A CA  
259  C  C   . PRO A 30  ? 0.0671 0.0668 0.0743 0.0038  -0.0003 -0.0081 30  PRO A C   
260  O  O   . PRO A 30  ? 0.0732 0.0856 0.0758 0.0038  -0.0063 0.0000  30  PRO A O   
261  C  CB  . PRO A 30  ? 0.0644 0.0786 0.0729 0.0027  -0.0012 -0.0077 30  PRO A CB  
262  C  CG  . PRO A 30  ? 0.0703 0.0754 0.0777 0.0000  -0.0027 -0.0046 30  PRO A CG  
263  C  CD  . PRO A 30  ? 0.0755 0.0804 0.0741 0.0076  0.0028  -0.0082 30  PRO A CD  
264  N  N   . VAL A 31  ? 0.0784 0.0847 0.0674 0.0126  0.0000  0.0074  31  VAL A N   
265  C  CA  . VAL A 31  ? 0.0817 0.0764 0.0773 0.0083  0.0081  0.0085  31  VAL A CA  
266  C  C   . VAL A 31  ? 0.0796 0.0833 0.0735 0.0175  0.0012  0.0024  31  VAL A C   
267  O  O   . VAL A 31  ? 0.0838 0.0841 0.0882 0.0049  -0.0003 0.0143  31  VAL A O   
268  C  CB  . VAL A 31  ? 0.0952 0.0902 0.0750 0.0030  -0.0060 0.0031  31  VAL A CB  
269  C  CG1 . VAL A 31  ? 0.1036 0.1040 0.0830 -0.0099 0.0034  -0.0104 31  VAL A CG1 
270  C  CG2 . VAL A 31  ? 0.1046 0.0873 0.0980 0.0141  0.0167  0.0048  31  VAL A CG2 
271  N  N   . ASP A 32  ? 0.0875 0.0820 0.0732 0.0104  0.0038  0.0048  32  ASP A N   
272  C  CA  . ASP A 32  ? 0.0946 0.0786 0.0840 0.0057  0.0065  0.0164  32  ASP A CA  
273  C  C   . ASP A 32  ? 0.1032 0.0844 0.0688 0.0098  0.0043  0.0065  32  ASP A C   
274  O  O   . ASP A 32  ? 0.1178 0.1324 0.0823 0.0040  0.0057  -0.0148 32  ASP A O   
275  C  CB  . ASP A 32  ? 0.1139 0.0907 0.0975 0.0127  -0.0046 0.0160  32  ASP A CB  
276  C  CG  . ASP A 32  ? 0.1333 0.0900 0.1005 0.0163  -0.0040 0.0353  32  ASP A CG  
277  O  OD1 . ASP A 32  ? 0.1235 0.0849 0.0991 0.0105  -0.0019 0.0199  32  ASP A OD1 
278  O  OD2 . ASP A 32  ? 0.1943 0.1186 0.1014 -0.0218 -0.0140 0.0318  32  ASP A OD2 
279  N  N   . ILE A 33  ? 0.0965 0.0768 0.0738 0.0093  0.0040  0.0142  33  ILE A N   
280  C  CA  . ILE A 33  ? 0.1016 0.0821 0.0790 0.0131  0.0140  0.0155  33  ILE A CA  
281  C  C   . ILE A 33  ? 0.1081 0.0829 0.0856 0.0183  0.0098  0.0126  33  ILE A C   
282  O  O   . ILE A 33  ? 0.1263 0.0892 0.0926 0.0035  0.0147  0.0186  33  ILE A O   
283  C  CB  . ILE A 33  ? 0.1000 0.0900 0.0992 0.0110  0.0115  0.0231  33  ILE A CB  
284  C  CG1 . ILE A 33  ? 0.1081 0.1022 0.0981 0.0080  -0.0031 0.0186  33  ILE A CG1 
285  C  CG2 . ILE A 33  ? 0.1186 0.1199 0.1130 0.0205  0.0240  0.0118  33  ILE A CG2 
286  C  CD1 . ILE A 33  ? 0.1060 0.1314 0.1402 0.0127  -0.0113 0.0296  33  ILE A CD1 
287  N  N   A ASP A 34  ? 0.1131 0.1183 0.0798 0.0252  0.0136  0.0311  34  ASP A N   
288  N  N   B ASP A 34  ? 0.1085 0.0887 0.0766 -0.0013 0.0362  0.0142  34  ASP A N   
289  C  CA  A ASP A 34  ? 0.1251 0.1077 0.0864 -0.0068 0.0241  0.0088  34  ASP A CA  
290  C  CA  B ASP A 34  ? 0.1412 0.1008 0.0870 0.0154  0.0093  0.0463  34  ASP A CA  
291  C  C   A ASP A 34  ? 0.1653 0.1154 0.1002 0.0379  0.0309  0.0252  34  ASP A C   
292  C  C   B ASP A 34  ? 0.1326 0.0974 0.0894 0.0266  0.0119  0.0493  34  ASP A C   
293  O  O   A ASP A 34  ? 0.1269 0.1393 0.1005 -0.0017 0.0089  0.0030  34  ASP A O   
294  O  O   B ASP A 34  ? 0.1377 0.1269 0.0823 0.0074  0.0217  0.0197  34  ASP A O   
295  C  CB  A ASP A 34  ? 0.1562 0.1316 0.0964 0.0175  0.0175  0.0231  34  ASP A CB  
296  C  CB  B ASP A 34  ? 0.1691 0.1231 0.1105 0.0443  0.0052  0.0353  34  ASP A CB  
297  C  CG  A ASP A 34  ? 0.2140 0.1335 0.1222 0.0155  0.0307  0.0368  34  ASP A CG  
298  C  CG  B ASP A 34  ? 0.1553 0.1809 0.0964 0.0763  0.0288  0.0498  34  ASP A CG  
299  O  OD1 A ASP A 34  ? 0.2228 0.1455 0.1319 0.0208  0.0421  0.0232  34  ASP A OD1 
300  O  OD1 B ASP A 34  ? 0.1625 0.2031 0.1148 0.0320  0.0027  0.0736  34  ASP A OD1 
301  O  OD2 A ASP A 34  ? 0.2815 0.1423 0.1541 0.0675  0.0436  0.0667  34  ASP A OD2 
302  O  OD2 B ASP A 34  ? 0.2605 0.2439 0.1601 -0.0524 -0.0610 0.1298  34  ASP A OD2 
303  N  N   . THR A 35  ? 0.1521 0.1307 0.0983 0.0253  0.0210  0.0542  35  THR A N   
304  C  CA  . THR A 35  ? 0.1538 0.1684 0.1164 0.0432  0.0340  0.0573  35  THR A CA  
305  C  C   . THR A 35  ? 0.1588 0.1296 0.1032 0.0408  0.0277  0.0280  35  THR A C   
306  O  O   . THR A 35  ? 0.2020 0.1671 0.1328 0.0640  0.0436  0.0441  35  THR A O   
307  C  CB  . THR A 35  ? 0.1604 0.1877 0.1370 0.0311  0.0195  0.0405  35  THR A CB  
308  O  OG1 . THR A 35  ? 0.1746 0.1886 0.1326 0.0082  0.0331  0.0454  35  THR A OG1 
309  C  CG2 . THR A 35  ? 0.1834 0.2263 0.1410 0.0491  0.0205  0.0427  35  THR A CG2 
310  N  N   . HIS A 36  ? 0.1694 0.1263 0.1081 0.0276  0.0247  0.0362  36  HIS A N   
311  C  CA  . HIS A 36  ? 0.1918 0.1319 0.0947 0.0197  0.0333  0.0388  36  HIS A CA  
312  C  C   . HIS A 36  ? 0.1797 0.1796 0.0777 0.0178  0.0147  0.0410  36  HIS A C   
313  O  O   . HIS A 36  ? 0.1641 0.2314 0.1105 0.0087  0.0065  0.0237  36  HIS A O   
314  C  CB  . HIS A 36  ? 0.2515 0.1712 0.1138 0.0271  -0.0005 0.0754  36  HIS A CB  
315  C  CG  . HIS A 36  ? 0.2657 0.1345 0.1358 0.0230  -0.0362 0.0161  36  HIS A CG  
316  N  ND1 . HIS A 36  ? 0.2493 0.2010 0.1729 -0.0421 -0.0529 0.0373  36  HIS A ND1 
317  C  CD2 . HIS A 36  ? 0.2149 0.1743 0.1678 -0.0168 -0.0439 0.0485  36  HIS A CD2 
318  C  CE1 . HIS A 36  ? 0.2475 0.1899 0.1779 -0.0041 -0.0267 0.0165  36  HIS A CE1 
319  N  NE2 . HIS A 36  ? 0.2687 0.1965 0.1911 0.0115  -0.0496 0.0296  36  HIS A NE2 
320  N  N   . THR A 37  ? 0.2407 0.1208 0.1321 0.0388  0.0555  0.0326  37  THR A N   
321  C  CA  . THR A 37  ? 0.1920 0.1661 0.1236 0.0381  0.0091  0.0527  37  THR A CA  
322  C  C   . THR A 37  ? 0.2069 0.1368 0.1349 0.0458  0.0201  0.0024  37  THR A C   
323  O  O   . THR A 37  ? 0.3203 0.1779 0.1648 0.0760  -0.0688 -0.0027 37  THR A O   
324  C  CB  . THR A 37  ? 0.2432 0.1324 0.2039 -0.0035 -0.0710 0.0522  37  THR A CB  
325  O  OG1 . THR A 37  ? 0.3307 0.1893 0.2901 0.0856  0.0278  0.0980  37  THR A OG1 
326  C  CG2 . THR A 37  ? 0.2152 0.2250 0.1826 0.0390  -0.0419 0.0295  37  THR A CG2 
327  N  N   . ALA A 38  ? 0.1898 0.1327 0.0927 0.0384  0.0218  0.0293  38  ALA A N   
328  C  CA  . ALA A 38  ? 0.1836 0.1368 0.0953 0.0516  0.0228  0.0222  38  ALA A CA  
329  C  C   . ALA A 38  ? 0.1978 0.1412 0.1567 -0.0048 0.0395  0.0164  38  ALA A C   
330  O  O   . ALA A 38  ? 0.2630 0.2161 0.2858 0.0038  0.1202  -0.0015 38  ALA A O   
331  C  CB  . ALA A 38  ? 0.1781 0.1344 0.1237 0.0331  -0.0049 0.0208  38  ALA A CB  
332  N  N   A LYS A 39  ? 0.2169 0.2342 0.0997 0.1150  0.0118  -0.0046 39  LYS A N   
333  N  N   B LYS A 39  ? 0.1884 0.1582 0.1289 -0.0212 0.0087  0.0065  39  LYS A N   
334  C  CA  A LYS A 39  ? 0.2487 0.2673 0.0887 0.1428  0.0234  0.0021  39  LYS A CA  
335  C  CA  B LYS A 39  ? 0.1503 0.1692 0.1207 -0.0480 -0.0057 0.0147  39  LYS A CA  
336  C  C   A LYS A 39  ? 0.1880 0.2073 0.0675 0.0522  -0.0105 0.0229  39  LYS A C   
337  C  C   B LYS A 39  ? 0.1624 0.1858 0.1365 0.0071  -0.0082 0.0046  39  LYS A C   
338  O  O   A LYS A 39  ? 0.1207 0.1653 0.0680 0.0597  -0.0127 0.0012  39  LYS A O   
339  O  O   B LYS A 39  ? 0.1359 0.2032 0.1255 0.0031  0.0178  -0.0077 39  LYS A O   
340  C  CB  A LYS A 39  ? 0.1639 0.2951 0.1234 0.0891  -0.0201 -0.0041 39  LYS A CB  
341  C  CB  B LYS A 39  ? 0.1600 0.1541 0.1146 -0.0046 -0.0133 0.0074  39  LYS A CB  
342  C  CG  A LYS A 39  ? 0.2515 0.1934 0.1250 0.0326  0.0218  -0.0092 39  LYS A CG  
343  C  CG  B LYS A 39  ? 0.1393 0.1960 0.1270 0.0579  -0.0318 0.0063  39  LYS A CG  
344  C  CD  A LYS A 39  ? 0.2601 0.3574 0.1695 0.0015  -0.0870 0.0013  39  LYS A CD  
345  C  CD  B LYS A 39  ? 0.1661 0.1641 0.1367 0.0841  -0.0239 0.0102  39  LYS A CD  
346  C  CE  A LYS A 39  ? 0.3607 0.3014 0.2344 -0.0194 -0.0038 -0.0754 39  LYS A CE  
347  C  CE  B LYS A 39  ? 0.1668 0.1721 0.1343 0.0368  -0.0068 0.0164  39  LYS A CE  
348  N  NZ  A LYS A 39  ? 0.3820 0.2021 0.2885 0.0612  0.0706  -0.0370 39  LYS A NZ  
349  N  NZ  B LYS A 39  ? 0.2295 0.3255 0.1018 0.1198  -0.0425 -0.0555 39  LYS A NZ  
350  N  N   . TYR A 40  ? 0.1819 0.2933 0.0929 -0.0093 0.0105  0.0031  40  TYR A N   
351  C  CA  . TYR A 40  ? 0.1800 0.2188 0.0996 0.0038  0.0458  0.0043  40  TYR A CA  
352  C  C   . TYR A 40  ? 0.1171 0.1957 0.1236 0.0214  0.0219  0.0256  40  TYR A C   
353  O  O   . TYR A 40  ? 0.1831 0.2825 0.0882 0.0597  0.0070  -0.0062 40  TYR A O   
354  C  CB  . TYR A 40  ? 0.1781 0.3402 0.1247 -0.0375 0.0177  0.0478  40  TYR A CB  
355  C  CG  . TYR A 40  ? 0.1859 0.3345 0.1293 -0.0364 0.0311  0.0283  40  TYR A CG  
356  C  CD1 . TYR A 40  ? 0.1834 0.3276 0.1186 -0.0724 0.0108  -0.0129 40  TYR A CD1 
357  C  CD2 . TYR A 40  ? 0.2014 0.4444 0.1360 -0.0216 0.0291  0.0038  40  TYR A CD2 
358  C  CE1 . TYR A 40  ? 0.1517 0.4663 0.1676 -0.0456 0.0258  -0.0137 40  TYR A CE1 
359  C  CE2 . TYR A 40  ? 0.1869 0.6818 0.2099 0.0483  0.0366  0.0046  40  TYR A CE2 
360  C  CZ  . TYR A 40  ? 0.2535 0.6345 0.1517 0.0093  0.0172  -0.0154 40  TYR A CZ  
361  O  OH  . TYR A 40  ? 0.3350 1.3610 0.9502 0.0535  0.0131  0.1797  40  TYR A OH  
362  N  N   . ASP A 41  ? 0.1509 0.1896 0.1147 0.0120  0.0273  -0.0141 41  ASP A N   
363  C  CA  . ASP A 41  ? 0.1580 0.1782 0.1322 -0.0046 -0.0220 0.0034  41  ASP A CA  
364  C  C   . ASP A 41  ? 0.1913 0.2445 0.1002 0.0379  0.0175  -0.0031 41  ASP A C   
365  O  O   . ASP A 41  ? 0.1606 0.2565 0.1230 0.0252  0.0019  -0.0250 41  ASP A O   
366  C  CB  . ASP A 41  ? 0.1567 0.1831 0.1858 -0.0199 -0.0474 -0.0109 41  ASP A CB  
367  C  CG  . ASP A 41  ? 0.1851 0.2066 0.2430 -0.0218 -0.0511 -0.0649 41  ASP A CG  
368  O  OD1 . ASP A 41  ? 0.2718 0.2065 0.2032 0.0377  -0.0498 -0.0782 41  ASP A OD1 
369  O  OD2 . ASP A 41  ? 0.2400 0.1946 0.3075 -0.0439 -0.1092 -0.0140 41  ASP A OD2 
370  N  N   . PRO A 42  ? 0.1977 0.2881 0.1378 0.0533  0.0238  -0.0026 42  PRO A N   
371  C  CA  . PRO A 42  ? 0.2001 0.3790 0.2176 0.0846  0.0445  0.0255  42  PRO A CA  
372  C  C   . PRO A 42  ? 0.1859 0.3228 0.1847 0.0829  0.0188  -0.0173 42  PRO A C   
373  O  O   . PRO A 42  ? 0.2802 0.4605 0.2836 0.1683  0.0209  -0.0174 42  PRO A O   
374  C  CB  . PRO A 42  ? 0.2648 0.4720 0.2099 0.1379  0.0854  -0.0159 42  PRO A CB  
375  C  CG  . PRO A 42  ? 0.3021 0.4916 0.1708 0.0694  0.0423  -0.0340 42  PRO A CG  
376  C  CD  . PRO A 42  ? 0.2624 0.3300 0.1087 0.0822  0.0359  0.0052  42  PRO A CD  
377  N  N   . SER A 43  ? 0.2256 0.3341 0.2125 0.0887  0.0003  -0.0694 43  SER A N   
378  C  CA  . SER A 43  ? 0.4079 0.2696 0.2502 0.0307  -0.0137 -0.0988 43  SER A CA  
379  C  C   . SER A 43  ? 0.2651 0.3140 0.2617 0.1343  -0.0197 0.0105  43  SER A C   
380  O  O   . SER A 43  ? 0.4135 0.3337 0.3542 0.1766  -0.1075 -0.0087 43  SER A O   
381  C  CB  . SER A 43  ? 0.3822 0.2953 0.2380 0.0456  -0.0388 -0.0710 43  SER A CB  
382  O  OG  . SER A 43  ? 0.4408 0.1823 0.3564 0.0702  -0.0956 -0.0615 43  SER A OG  
383  N  N   . LEU A 44  ? 0.2745 0.3619 0.1810 0.0961  -0.0239 -0.0087 44  LEU A N   
384  C  CA  . LEU A 44  ? 0.2322 0.3661 0.1701 -0.0193 -0.0575 0.0476  44  LEU A CA  
385  C  C   . LEU A 44  ? 0.1715 0.4539 0.2892 -0.0307 -0.0258 0.1622  44  LEU A C   
386  O  O   . LEU A 44  ? 0.1872 0.5266 0.2124 -0.0174 0.0051  0.0926  44  LEU A O   
387  C  CB  . LEU A 44  ? 0.1882 0.3413 0.1225 -0.0344 -0.0173 0.0092  44  LEU A CB  
388  C  CG  . LEU A 44  ? 0.1658 0.2328 0.1385 -0.0397 -0.0109 0.0140  44  LEU A CG  
389  C  CD1 . LEU A 44  ? 0.2617 0.2371 0.1158 -0.0625 0.0040  -0.0263 44  LEU A CD1 
390  C  CD2 . LEU A 44  ? 0.2178 0.1944 0.1609 0.0080  -0.0252 0.0065  44  LEU A CD2 
391  N  N   . LYS A 45  ? 0.2433 0.2252 0.1988 0.0007  -0.0226 0.0041  45  LYS A N   
392  C  CA  . LYS A 45  ? 0.3010 0.1732 0.4347 0.0416  -0.1914 -0.0709 45  LYS A CA  
393  C  C   . LYS A 45  ? 0.2296 0.3811 0.1265 0.1534  0.0190  0.0066  45  LYS A C   
394  O  O   . LYS A 45  ? 0.1497 0.5339 0.3093 -0.0658 0.0724  -0.2149 45  LYS A O   
395  C  CB  . LYS A 45  ? 0.3476 0.2888 0.1997 0.2145  0.0397  0.0167  45  LYS A CB  
396  C  CG  . LYS A 45  ? 0.2906 0.5939 0.2585 -0.0449 -0.0857 -0.0878 45  LYS A CG  
397  C  CD  . LYS A 45  ? 0.3684 0.5939 0.3282 -0.0208 0.1206  -0.1278 45  LYS A CD  
398  C  CE  . LYS A 45  ? 0.4128 0.5497 0.3350 0.0505  0.0756  -0.1058 45  LYS A CE  
399  N  NZ  . LYS A 45  ? 0.4918 0.9915 0.6245 0.1959  0.2480  -0.0816 45  LYS A NZ  
400  N  N   A PRO A 46  ? 0.1165 0.3592 0.2439 -0.0658 0.0826  -0.0912 46  PRO A N   
401  N  N   B PRO A 46  ? 0.2790 0.2520 0.1902 0.0386  -0.0527 0.0996  46  PRO A N   
402  C  CA  A PRO A 46  ? 0.1757 0.1517 0.2624 0.0408  -0.0054 -0.0098 46  PRO A CA  
403  C  CA  B PRO A 46  ? 0.1788 0.3562 0.1720 -0.0383 0.0040  0.0960  46  PRO A CA  
404  C  C   A PRO A 46  ? 0.1877 0.2540 0.1752 -0.0038 -0.0344 -0.0076 46  PRO A C   
405  C  C   B PRO A 46  ? 0.0811 0.2317 0.1025 0.0406  0.0476  0.0166  46  PRO A C   
406  O  O   A PRO A 46  ? 0.0768 0.2969 0.2795 -0.0015 -0.0610 0.0791  46  PRO A O   
407  O  O   B PRO A 46  ? 0.1772 0.2322 0.2022 -0.0593 -0.0027 0.0091  46  PRO A O   
408  C  CB  A PRO A 46  ? 0.1655 0.2899 0.2066 -0.0588 0.0027  0.0116  46  PRO A CB  
409  C  CB  B PRO A 46  ? 0.1754 0.4251 0.2085 -0.0060 0.0165  0.0962  46  PRO A CB  
410  C  CG  A PRO A 46  ? 0.1246 0.3576 0.2572 -0.0621 0.0734  -0.0272 46  PRO A CG  
411  C  CG  B PRO A 46  ? 0.1216 0.4277 0.1904 0.0790  0.0878  0.0967  46  PRO A CG  
412  C  CD  A PRO A 46  ? 0.1111 0.1733 0.2574 0.0584  0.0006  0.0373  46  PRO A CD  
413  C  CD  B PRO A 46  ? 0.0983 0.3551 0.4167 0.1368  0.1289  0.2493  46  PRO A CD  
414  N  N   A LEU A 47  ? 0.0867 0.2401 0.2270 -0.0500 -0.0230 0.1287  47  LEU A N   
415  N  N   B LEU A 47  ? 0.1650 0.2387 0.2522 0.0926  0.0225  -0.0094 47  LEU A N   
416  C  CA  A LEU A 47  ? 0.0602 0.2556 0.2117 -0.0562 -0.0318 0.1553  47  LEU A CA  
417  C  CA  B LEU A 47  ? 0.1129 0.2680 0.2055 0.0274  0.0988  -0.0826 47  LEU A CA  
418  C  C   A LEU A 47  ? 0.0496 0.2752 0.2653 -0.0346 -0.0465 0.1792  47  LEU A C   
419  C  C   B LEU A 47  ? 0.1626 0.2294 0.3307 -0.0989 -0.0137 0.0876  47  LEU A C   
420  O  O   A LEU A 47  ? 0.0563 0.2698 0.3177 -0.0772 -0.0929 0.2229  47  LEU A O   
421  O  O   B LEU A 47  ? 0.1775 0.4237 0.6486 -0.1776 -0.0522 0.1058  47  LEU A O   
422  C  CB  A LEU A 47  ? 0.0940 0.2111 0.3817 -0.0340 -0.0665 0.1345  47  LEU A CB  
423  C  CB  B LEU A 47  ? 0.2230 0.3336 0.1581 0.1952  0.0742  0.0122  47  LEU A CB  
424  C  CG  A LEU A 47  ? 0.0700 0.1596 0.4318 -0.0302 -0.0454 0.1618  47  LEU A CG  
425  C  CG  B LEU A 47  ? 0.1992 0.2931 0.2635 -0.0456 0.0698  -0.0997 47  LEU A CG  
426  C  CD1 A LEU A 47  ? 0.0829 0.2475 0.3794 -0.0571 -0.0109 0.0816  47  LEU A CD1 
427  C  CD1 B LEU A 47  ? 0.1146 0.1600 0.3865 -0.0078 -0.0768 0.0529  47  LEU A CD1 
428  C  CD2 A LEU A 47  ? 0.0979 0.1727 0.4061 -0.0200 -0.0737 0.1387  47  LEU A CD2 
429  C  CD2 B LEU A 47  ? 0.0919 0.2206 0.2090 0.0001  0.0297  0.0099  47  LEU A CD2 
430  N  N   . SER A 48  ? 0.0952 0.1757 0.1536 -0.0194 -0.0017 0.0480  48  SER A N   
431  C  CA  . SER A 48  ? 0.0887 0.1568 0.1497 0.0031  0.0021  0.0286  48  SER A CA  
432  C  C   . SER A 48  ? 0.0882 0.1495 0.1500 -0.0019 0.0133  0.0331  48  SER A C   
433  O  O   . SER A 48  ? 0.0948 0.1694 0.1573 -0.0286 0.0243  0.0111  48  SER A O   
434  C  CB  . SER A 48  ? 0.1272 0.1863 0.1667 0.0311  0.0065  0.0297  48  SER A CB  
435  O  OG  . SER A 48  ? 0.1403 0.2255 0.2143 0.0372  0.0149  0.0643  48  SER A OG  
436  N  N   . VAL A 49  ? 0.1208 0.1459 0.1519 -0.0287 0.0152  0.0108  49  VAL A N   
437  C  CA  . VAL A 49  ? 0.1308 0.1536 0.1506 -0.0383 0.0210  -0.0024 49  VAL A CA  
438  C  C   . VAL A 49  ? 0.1238 0.1777 0.1591 -0.0678 0.0175  -0.0165 49  VAL A C   
439  O  O   . VAL A 49  ? 0.1747 0.2475 0.1614 -0.1079 -0.0074 0.0172  49  VAL A O   
440  C  CB  . VAL A 49  ? 0.1923 0.1649 0.2154 -0.0608 0.0790  -0.0165 49  VAL A CB  
441  C  CG1 . VAL A 49  ? 0.2658 0.1939 0.2280 -0.0263 0.0781  -0.0219 49  VAL A CG1 
442  C  CG2 . VAL A 49  ? 0.1577 0.1720 0.3093 -0.0138 0.0593  0.0253  49  VAL A CG2 
443  N  N   A SER A 50  ? 0.0981 0.1732 0.1729 -0.0425 0.0175  -0.0097 50  SER A N   
444  N  N   B SER A 50  ? 0.1172 0.1728 0.1776 -0.0346 0.0159  -0.0100 50  SER A N   
445  C  CA  A SER A 50  ? 0.0932 0.2027 0.2002 -0.0006 0.0133  -0.0299 50  SER A CA  
446  C  CA  B SER A 50  ? 0.0997 0.1987 0.2070 -0.0051 0.0156  -0.0283 50  SER A CA  
447  C  C   A SER A 50  ? 0.0840 0.1715 0.1937 -0.0177 -0.0006 -0.0131 50  SER A C   
448  C  C   B SER A 50  ? 0.0978 0.1738 0.1960 -0.0054 -0.0052 -0.0071 50  SER A C   
449  O  O   A SER A 50  ? 0.1660 0.1497 0.1903 -0.0381 0.0120  0.0054  50  SER A O   
450  O  O   B SER A 50  ? 0.1673 0.1542 0.1915 -0.0318 0.0049  0.0060  50  SER A O   
451  C  CB  A SER A 50  ? 0.1316 0.2140 0.1984 0.0215  0.0185  -0.0049 50  SER A CB  
452  C  CB  B SER A 50  ? 0.1559 0.2210 0.2144 0.0200  0.0423  -0.0109 50  SER A CB  
453  O  OG  A SER A 50  ? 0.1192 0.1771 0.1922 -0.0051 0.0174  -0.0252 50  SER A OG  
454  O  OG  B SER A 50  ? 0.2071 0.2806 0.3215 0.0217  0.0032  -0.0190 50  SER A OG  
455  N  N   . TYR A 51  ? 0.0923 0.1530 0.1814 -0.0074 -0.0120 0.0015  51  TYR A N   
456  C  CA  . TYR A 51  ? 0.0917 0.1519 0.1712 0.0019  0.0041  0.0063  51  TYR A CA  
457  C  C   . TYR A 51  ? 0.1090 0.1806 0.1756 -0.0133 -0.0068 0.0308  51  TYR A C   
458  O  O   . TYR A 51  ? 0.1149 0.2305 0.1826 0.0201  -0.0166 0.0401  51  TYR A O   
459  C  CB  . TYR A 51  ? 0.1106 0.1585 0.1594 -0.0071 -0.0217 -0.0070 51  TYR A CB  
460  C  CG  . TYR A 51  ? 0.0923 0.1291 0.1454 -0.0146 -0.0044 0.0093  51  TYR A CG  
461  C  CD1 . TYR A 51  ? 0.0934 0.1176 0.1735 -0.0063 -0.0078 -0.0063 51  TYR A CD1 
462  C  CD2 . TYR A 51  ? 0.0992 0.1264 0.1263 -0.0020 0.0092  -0.0041 51  TYR A CD2 
463  C  CE1 . TYR A 51  ? 0.0930 0.1141 0.1541 -0.0052 -0.0116 -0.0111 51  TYR A CE1 
464  C  CE2 . TYR A 51  ? 0.0917 0.1208 0.1187 -0.0131 -0.0049 0.0001  51  TYR A CE2 
465  C  CZ  . TYR A 51  ? 0.0805 0.1122 0.1120 -0.0068 -0.0038 0.0017  51  TYR A CZ  
466  O  OH  . TYR A 51  ? 0.0850 0.1018 0.1447 -0.0110 -0.0114 0.0003  51  TYR A OH  
467  N  N   . ASP A 52  ? 0.0895 0.2426 0.2305 -0.0055 -0.0184 0.0505  52  ASP A N   
468  C  CA  . ASP A 52  ? 0.1060 0.3102 0.2398 0.0063  -0.0340 0.0926  52  ASP A CA  
469  C  C   . ASP A 52  ? 0.1625 0.2302 0.2439 0.0568  -0.0211 0.0568  52  ASP A C   
470  O  O   . ASP A 52  ? 0.2915 0.3278 0.2612 0.0821  -0.0467 0.0573  52  ASP A O   
471  C  CB  . ASP A 52  ? 0.1186 0.3359 0.2669 0.0454  -0.0175 0.0648  52  ASP A CB  
472  C  CG  . ASP A 52  ? 0.2673 0.3181 0.3470 0.0763  -0.0013 0.0427  52  ASP A CG  
473  O  OD1 . ASP A 52  ? 0.2693 0.5040 0.3840 -0.0017 0.0192  0.0026  52  ASP A OD1 
474  O  OD2 . ASP A 52  ? 0.4740 0.3334 0.7605 0.0738  -0.0017 0.2242  52  ASP A OD2 
475  N  N   . GLN A 53  ? 0.1163 0.1808 0.3463 0.0331  0.0500  0.0665  53  GLN A N   
476  C  CA  . GLN A 53  ? 0.1568 0.2041 0.3224 0.0526  0.0458  0.0811  53  GLN A CA  
477  C  C   . GLN A 53  ? 0.1271 0.2043 0.2865 0.0115  0.0255  0.0412  53  GLN A C   
478  O  O   . GLN A 53  ? 0.1680 0.1886 0.2811 0.0196  0.0076  0.0498  53  GLN A O   
479  C  CB  . GLN A 53  ? 0.2294 0.2178 0.4930 0.0812  0.1058  0.0384  53  GLN A CB  
480  C  CG  . GLN A 53  ? 0.2725 0.3066 0.5101 0.1108  0.1817  0.0747  53  GLN A CG  
481  C  CD  . GLN A 53  ? 0.3740 0.5418 0.4300 0.1578  0.1195  0.2770  53  GLN A CD  
482  O  OE1 . GLN A 53  ? 0.7774 0.6324 0.7828 0.0315  0.0769  0.4568  53  GLN A OE1 
483  N  NE2 . GLN A 53  ? 0.4722 0.4246 0.9312 0.0939  0.0538  0.2127  53  GLN A NE2 
484  N  N   . ALA A 54  ? 0.1162 0.1620 0.2610 0.0094  0.0254  -0.0063 54  ALA A N   
485  C  CA  . ALA A 54  ? 0.1146 0.1561 0.2065 -0.0030 0.0089  -0.0372 54  ALA A CA  
486  C  C   . ALA A 54  ? 0.1049 0.2157 0.1802 0.0212  -0.0200 -0.0467 54  ALA A C   
487  O  O   . ALA A 54  ? 0.1208 0.3172 0.2592 -0.0335 -0.0187 -0.1000 54  ALA A O   
488  C  CB  . ALA A 54  ? 0.1228 0.1563 0.2177 0.0154  0.0026  -0.0236 54  ALA A CB  
489  N  N   . THR A 55  ? 0.0979 0.1810 0.1659 0.0315  -0.0228 0.0108  55  THR A N   
490  C  CA  . THR A 55  ? 0.1655 0.1891 0.1685 0.0843  -0.0489 0.0318  55  THR A CA  
491  C  C   . THR A 55  ? 0.1245 0.1162 0.1280 0.0144  -0.0342 0.0326  55  THR A C   
492  O  O   . THR A 55  ? 0.1333 0.1069 0.1433 0.0076  -0.0231 0.0266  55  THR A O   
493  C  CB  . THR A 55  ? 0.2673 0.2667 0.2412 0.1275  -0.0230 0.0798  55  THR A CB  
494  O  OG1 . THR A 55  ? 0.2682 0.2137 0.6171 0.0807  -0.1702 -0.0271 55  THR A OG1 
495  C  CG2 . THR A 55  ? 0.4648 0.2459 0.2291 0.2104  0.0136  0.1345  55  THR A CG2 
496  N  N   . SER A 56  ? 0.1168 0.1178 0.1262 0.0120  -0.0353 0.0286  56  SER A N   
497  C  CA  . SER A 56  ? 0.1181 0.1020 0.1210 -0.0043 -0.0308 0.0211  56  SER A CA  
498  C  C   . SER A 56  ? 0.1251 0.1102 0.1185 0.0177  -0.0394 0.0244  56  SER A C   
499  O  O   . SER A 56  ? 0.1394 0.1407 0.1339 0.0168  -0.0368 0.0394  56  SER A O   
500  C  CB  . SER A 56  ? 0.1307 0.1193 0.1054 -0.0071 -0.0469 0.0154  56  SER A CB  
501  O  OG  . SER A 56  ? 0.1481 0.1287 0.1289 -0.0299 -0.0522 0.0296  56  SER A OG  
502  N  N   . LEU A 57  ? 0.1297 0.0947 0.1071 0.0198  -0.0185 0.0166  57  LEU A N   
503  C  CA  . LEU A 57  ? 0.1483 0.1057 0.1388 0.0206  -0.0147 0.0364  57  LEU A CA  
504  C  C   . LEU A 57  ? 0.1208 0.0964 0.1263 0.0107  -0.0133 0.0275  57  LEU A C   
505  O  O   . LEU A 57  ? 0.1513 0.1412 0.1008 0.0270  -0.0188 0.0285  57  LEU A O   
506  C  CB  . LEU A 57  ? 0.2301 0.0997 0.1699 -0.0247 0.0263  0.0320  57  LEU A CB  
507  C  CG  . LEU A 57  ? 0.2653 0.1393 0.1828 -0.0133 -0.0245 0.0196  57  LEU A CG  
508  C  CD1 . LEU A 57  ? 0.3289 0.1432 0.2926 -0.0608 0.0317  0.0063  57  LEU A CD1 
509  C  CD2 . LEU A 57  ? 0.3461 0.1970 0.3012 0.0905  -0.0683 0.0586  57  LEU A CD2 
510  N  N   A ARG A 58  ? 0.1236 0.0769 0.1240 0.0155  -0.0085 0.0261  58  ARG A N   
511  N  N   B ARG A 58  ? 0.1187 0.1137 0.1035 0.0203  -0.0164 0.0201  58  ARG A N   
512  C  CA  A ARG A 58  ? 0.1118 0.1099 0.1081 0.0126  -0.0174 0.0357  58  ARG A CA  
513  C  CA  B ARG A 58  ? 0.1360 0.1185 0.1131 0.0186  0.0187  0.0386  58  ARG A CA  
514  C  C   A ARG A 58  ? 0.1167 0.0984 0.0772 -0.0035 -0.0093 0.0219  58  ARG A C   
515  C  C   B ARG A 58  ? 0.1180 0.1095 0.0755 -0.0071 -0.0083 0.0091  58  ARG A C   
516  O  O   A ARG A 58  ? 0.1084 0.0789 0.0856 0.0017  -0.0062 0.0198  58  ARG A O   
517  O  O   B ARG A 58  ? 0.1213 0.1155 0.0830 0.0093  -0.0071 0.0140  58  ARG A O   
518  C  CB  A ARG A 58  ? 0.1468 0.1058 0.0966 -0.0222 -0.0366 0.0041  58  ARG A CB  
519  C  CB  B ARG A 58  ? 0.1288 0.1121 0.1014 0.0043  -0.0003 0.0109  58  ARG A CB  
520  C  CG  A ARG A 58  ? 0.1527 0.1551 0.1360 -0.0177 -0.0054 0.0482  58  ARG A CG  
521  C  CG  B ARG A 58  ? 0.0993 0.1475 0.1474 -0.0118 -0.0190 0.0381  58  ARG A CG  
522  C  CD  A ARG A 58  ? 0.1701 0.1744 0.1632 -0.0304 0.0193  0.0549  58  ARG A CD  
523  C  CD  B ARG A 58  ? 0.1618 0.1550 0.1492 -0.0458 0.0060  0.0193  58  ARG A CD  
524  N  NE  A ARG A 58  ? 0.1453 0.1521 0.1727 -0.0553 0.0215  0.0355  58  ARG A NE  
525  N  NE  B ARG A 58  ? 0.1729 0.1762 0.2045 -0.0364 -0.0153 0.0221  58  ARG A NE  
526  C  CZ  A ARG A 58  ? 0.1465 0.1192 0.1632 -0.0216 0.0373  0.0266  58  ARG A CZ  
527  C  CZ  B ARG A 58  ? 0.1666 0.1322 0.2038 -0.0450 -0.0007 0.0403  58  ARG A CZ  
528  N  NH1 A ARG A 58  ? 0.1932 0.1381 0.1779 -0.0800 0.0662  0.0271  58  ARG A NH1 
529  N  NH1 B ARG A 58  ? 0.2219 0.1427 0.1923 -0.0121 0.0030  0.0185  58  ARG A NH1 
530  N  NH2 A ARG A 58  ? 0.1353 0.1419 0.1366 -0.0326 0.0436  0.0399  58  ARG A NH2 
531  N  NH2 B ARG A 58  ? 0.1856 0.1747 0.2074 -0.0070 0.0060  0.0107  58  ARG A NH2 
532  N  N   . ILE A 59  ? 0.1104 0.0999 0.0800 0.0049  -0.0071 0.0237  59  ILE A N   
533  C  CA  . ILE A 59  ? 0.1076 0.1079 0.0797 0.0024  -0.0132 0.0285  59  ILE A CA  
534  C  C   . ILE A 59  ? 0.1116 0.1067 0.0762 0.0110  -0.0013 0.0175  59  ILE A C   
535  O  O   . ILE A 59  ? 0.1298 0.1590 0.0768 0.0164  0.0089  0.0351  59  ILE A O   
536  C  CB  . ILE A 59  ? 0.1206 0.1154 0.0882 -0.0015 -0.0148 0.0203  59  ILE A CB  
537  C  CG1 . ILE A 59  ? 0.1519 0.1044 0.0797 0.0020  -0.0031 0.0263  59  ILE A CG1 
538  C  CG2 . ILE A 59  ? 0.1592 0.1265 0.0810 0.0129  -0.0176 0.0175  59  ILE A CG2 
539  C  CD1 . ILE A 59  ? 0.1912 0.1014 0.0917 -0.0089 -0.0192 0.0135  59  ILE A CD1 
540  N  N   . LEU A 60  ? 0.0997 0.1195 0.0874 0.0198  0.0038  0.0313  60  LEU A N   
541  C  CA  . LEU A 60  ? 0.0978 0.1394 0.1067 0.0219  0.0035  0.0511  60  LEU A CA  
542  C  C   . LEU A 60  ? 0.1046 0.1033 0.0900 0.0000  0.0199  0.0331  60  LEU A C   
543  O  O   . LEU A 60  ? 0.1078 0.1211 0.0917 0.0138  0.0136  0.0329  60  LEU A O   
544  C  CB  . LEU A 60  ? 0.1230 0.0938 0.1918 -0.0010 -0.0015 0.0423  60  LEU A CB  
545  C  CG  . LEU A 60  ? 0.1453 0.1310 0.1378 -0.0020 -0.0037 0.0164  60  LEU A CG  
546  C  CD1 . LEU A 60  ? 0.1547 0.1758 0.1741 -0.0115 0.0184  0.0584  60  LEU A CD1 
547  C  CD2 . LEU A 60  ? 0.1793 0.1058 0.2182 -0.0070 -0.0049 0.0124  60  LEU A CD2 
548  N  N   . ASN A 61  ? 0.1004 0.1092 0.0870 0.0024  0.0031  0.0240  61  ASN A N   
549  C  CA  . ASN A 61  ? 0.0964 0.1081 0.0876 0.0000  0.0054  0.0193  61  ASN A CA  
550  C  C   . ASN A 61  ? 0.0979 0.1057 0.0932 -0.0035 0.0122  0.0233  61  ASN A C   
551  O  O   . ASN A 61  ? 0.1128 0.1206 0.1076 -0.0140 0.0113  0.0296  61  ASN A O   
552  C  CB  . ASN A 61  ? 0.1101 0.1181 0.0879 0.0057  0.0076  0.0156  61  ASN A CB  
553  C  CG  . ASN A 61  ? 0.1088 0.1099 0.0864 -0.0120 0.0122  0.0125  61  ASN A CG  
554  O  OD1 . ASN A 61  ? 0.1181 0.1062 0.1102 0.0074  0.0065  0.0163  61  ASN A OD1 
555  N  ND2 . ASN A 61  ? 0.1375 0.1070 0.0990 0.0027  0.0210  0.0044  61  ASN A ND2 
556  N  N   . VAL A 62  ? 0.0934 0.1097 0.0986 -0.0096 0.0055  0.0176  62  VAL A N   
557  C  CA  . VAL A 62  ? 0.1026 0.1116 0.1156 -0.0109 0.0000  0.0227  62  VAL A CA  
558  C  C   . VAL A 62  ? 0.1171 0.1358 0.1141 -0.0164 0.0000  0.0148  62  VAL A C   
559  O  O   . VAL A 62  ? 0.1280 0.1836 0.1544 -0.0082 -0.0198 -0.0172 62  VAL A O   
560  C  CB  . VAL A 62  ? 0.1299 0.1142 0.1103 -0.0144 -0.0035 -0.0019 62  VAL A CB  
561  C  CG1 . VAL A 62  ? 0.1484 0.1532 0.1587 0.0197  -0.0060 -0.0062 62  VAL A CG1 
562  C  CG2 . VAL A 62  ? 0.1552 0.1386 0.1066 -0.0153 0.0060  0.0000  62  VAL A CG2 
563  N  N   . GLY A 63  ? 0.1130 0.1372 0.0997 0.0044  0.0000  0.0230  63  GLY A N   
564  C  CA  . GLY A 63  ? 0.1193 0.1650 0.1130 0.0073  0.0024  0.0208  63  GLY A CA  
565  C  C   . GLY A 63  ? 0.1424 0.1335 0.1498 0.0217  0.0013  0.0113  63  GLY A C   
566  O  O   . GLY A 63  ? 0.4611 0.1862 0.1815 0.1140  0.0074  0.0192  63  GLY A O   
567  N  N   . HIS A 64  ? 0.1379 0.1641 0.1483 0.0006  0.0136  0.0560  64  HIS A N   
568  C  CA  . HIS A 64  ? 0.1033 0.2298 0.1719 0.0034  -0.0060 0.1041  64  HIS A CA  
569  C  C   . HIS A 64  ? 0.1182 0.1404 0.1480 -0.0043 -0.0074 0.0604  64  HIS A C   
570  O  O   . HIS A 64  ? 0.1333 0.2154 0.2093 -0.0164 -0.0225 0.1284  64  HIS A O   
571  C  CB  . HIS A 64  ? 0.1309 0.3657 0.2100 -0.0278 -0.0441 0.1455  64  HIS A CB  
572  C  CG  . HIS A 64  ? 0.1636 0.3898 0.1147 -0.1184 -0.0392 0.0680  64  HIS A CG  
573  N  ND1 . HIS A 64  ? 0.2143 0.3084 0.1441 -0.0573 -0.0287 0.0000  64  HIS A ND1 
574  C  CD2 . HIS A 64  ? 0.1865 0.3777 0.1049 -0.0939 -0.0397 0.0529  64  HIS A CD2 
575  C  CE1 . HIS A 64  ? 0.2515 0.2565 0.1513 -0.1230 0.0060  -0.0199 64  HIS A CE1 
576  N  NE2 . HIS A 64  ? 0.2166 0.4230 0.1336 -0.0821 0.0173  -0.0582 64  HIS A NE2 
577  N  N   . ALA A 65  ? 0.1123 0.1150 0.1177 0.0031  -0.0102 0.0320  65  ALA A N   
578  C  CA  . ALA A 65  ? 0.1217 0.1228 0.0986 -0.0048 -0.0028 0.0256  65  ALA A CA  
579  C  C   . ALA A 65  ? 0.1186 0.0902 0.0755 -0.0013 0.0017  0.0120  65  ALA A C   
580  O  O   . ALA A 65  ? 0.1181 0.1193 0.1083 -0.0049 0.0038  0.0243  65  ALA A O   
581  C  CB  . ALA A 65  ? 0.1293 0.2026 0.0946 -0.0115 -0.0255 0.0192  65  ALA A CB  
582  N  N   . PHE A 66  ? 0.1111 0.0967 0.0805 0.0121  -0.0043 0.0194  66  PHE A N   
583  C  CA  . PHE A 66  ? 0.1185 0.0953 0.0712 0.0124  0.0000  0.0155  66  PHE A CA  
584  C  C   . PHE A 66  ? 0.1094 0.1001 0.0659 -0.0007 0.0019  0.0148  66  PHE A C   
585  O  O   . PHE A 66  ? 0.1395 0.0893 0.0716 0.0055  0.0096  0.0119  66  PHE A O   
586  C  CB  . PHE A 66  ? 0.1380 0.1055 0.0886 0.0097  -0.0098 0.0024  66  PHE A CB  
587  C  CG  . PHE A 66  ? 0.1304 0.1178 0.0636 0.0013  -0.0103 -0.0021 66  PHE A CG  
588  C  CD1 . PHE A 66  ? 0.1167 0.1396 0.0904 0.0073  -0.0303 0.0020  66  PHE A CD1 
589  C  CD2 . PHE A 66  ? 0.1262 0.1023 0.0795 0.0089  -0.0071 -0.0051 66  PHE A CD2 
590  C  CE1 . PHE A 66  ? 0.1337 0.1315 0.0922 0.0051  -0.0335 -0.0023 66  PHE A CE1 
591  C  CE2 . PHE A 66  ? 0.1504 0.1233 0.0815 -0.0017 -0.0217 -0.0204 66  PHE A CE2 
592  C  CZ  . PHE A 66  ? 0.1273 0.1269 0.0890 -0.0052 -0.0196 -0.0080 66  PHE A CZ  
593  N  N   . HIS A 67  ? 0.0960 0.0858 0.0820 0.0049  0.0007  0.0136  67  HIS A N   
594  C  CA  . HIS A 67  ? 0.1058 0.0874 0.0826 0.0088  -0.0001 0.0137  67  HIS A CA  
595  C  C   . HIS A 67  ? 0.1087 0.0820 0.0763 0.0052  -0.0063 0.0120  67  HIS A C   
596  O  O   . HIS A 67  ? 0.1098 0.1263 0.0746 0.0092  0.0013  0.0342  67  HIS A O   
597  C  CB  . HIS A 67  ? 0.1097 0.1009 0.0934 -0.0105 0.0001  0.0028  67  HIS A CB  
598  C  CG  . HIS A 67  ? 0.1049 0.1196 0.0976 -0.0130 0.0113  -0.0046 67  HIS A CG  
599  N  ND1 . HIS A 67  ? 0.1401 0.1277 0.1340 -0.0115 0.0051  -0.0088 67  HIS A ND1 
600  C  CD2 . HIS A 67  ? 0.1035 0.1556 0.0803 0.0077  -0.0044 0.0048  67  HIS A CD2 
601  C  CE1 . HIS A 67  ? 0.1120 0.1928 0.1062 0.0043  -0.0109 0.0012  67  HIS A CE1 
602  N  NE2 . HIS A 67  ? 0.1139 0.1881 0.1067 -0.0121 -0.0082 0.0010  67  HIS A NE2 
603  N  N   . VAL A 68  ? 0.1023 0.0715 0.0758 0.0111  -0.0034 0.0124  68  VAL A N   
604  C  CA  . VAL A 68  ? 0.1051 0.0948 0.0716 0.0142  -0.0104 0.0130  68  VAL A CA  
605  C  C   . VAL A 68  ? 0.1023 0.0812 0.0786 0.0052  -0.0038 0.0186  68  VAL A C   
606  O  O   . VAL A 68  ? 0.1279 0.0799 0.0750 0.0102  -0.0041 0.0148  68  VAL A O   
607  C  CB  . VAL A 68  ? 0.1040 0.0885 0.0879 0.0013  -0.0109 0.0078  68  VAL A CB  
608  C  CG1 . VAL A 68  ? 0.1121 0.1257 0.1016 -0.0008 -0.0167 0.0041  68  VAL A CG1 
609  C  CG2 . VAL A 68  ? 0.1246 0.1142 0.0960 -0.0156 0.0006  -0.0010 68  VAL A CG2 
610  N  N   . GLU A 69  ? 0.1138 0.0794 0.0834 0.0071  -0.0049 0.0194  69  GLU A N   
611  C  CA  . GLU A 69  ? 0.1115 0.0850 0.0825 0.0027  0.0012  0.0194  69  GLU A CA  
612  C  C   . GLU A 69  ? 0.1140 0.0927 0.0741 0.0041  -0.0077 0.0287  69  GLU A C   
613  O  O   . GLU A 69  ? 0.1352 0.0991 0.1115 0.0131  -0.0307 0.0142  69  GLU A O   
614  C  CB  . GLU A 69  ? 0.1361 0.0912 0.1299 0.0071  0.0157  0.0283  69  GLU A CB  
615  C  CG  . GLU A 69  ? 0.1297 0.1296 0.1872 0.0000  0.0297  0.0610  69  GLU A CG  
616  C  CD  . GLU A 69  ? 0.1473 0.1504 0.2372 0.0230  0.0753  0.0644  69  GLU A CD  
617  O  OE1 . GLU A 69  ? 0.2791 0.2342 0.2630 0.0513  0.1263  0.1386  69  GLU A OE1 
618  O  OE2 . GLU A 69  ? 0.1359 0.2229 0.2777 0.0000  0.0485  0.0830  69  GLU A OE2 
619  N  N   . PHE A 70  ? 0.1034 0.0945 0.1007 0.0041  -0.0080 0.0216  70  PHE A N   
620  C  CA  . PHE A 70  ? 0.1055 0.0884 0.1120 0.0185  -0.0116 0.0135  70  PHE A CA  
621  C  C   . PHE A 70  ? 0.1199 0.0881 0.1203 0.0178  -0.0116 0.0178  70  PHE A C   
622  O  O   . PHE A 70  ? 0.1228 0.0949 0.1703 0.0081  -0.0121 0.0174  70  PHE A O   
623  C  CB  . PHE A 70  ? 0.1236 0.0919 0.1034 0.0141  -0.0044 0.0111  70  PHE A CB  
624  C  CG  . PHE A 70  ? 0.1041 0.0970 0.0856 0.0166  -0.0035 0.0164  70  PHE A CG  
625  C  CD1 . PHE A 70  ? 0.1134 0.0908 0.1222 0.0219  0.0088  0.0331  70  PHE A CD1 
626  C  CD2 . PHE A 70  ? 0.1108 0.0971 0.1028 0.0110  -0.0049 0.0311  70  PHE A CD2 
627  C  CE1 . PHE A 70  ? 0.1358 0.0896 0.1389 0.0304  0.0204  0.0295  70  PHE A CE1 
628  C  CE2 . PHE A 70  ? 0.1155 0.1097 0.1110 -0.0041 -0.0003 0.0210  70  PHE A CE2 
629  C  CZ  . PHE A 70  ? 0.1453 0.0883 0.1319 0.0088  0.0254  0.0144  70  PHE A CZ  
630  N  N   A ASP A 71  ? 0.1259 0.0875 0.1361 0.0148  -0.0032 0.0430  71  ASP A N   
631  N  N   B ASP A 71  ? 0.1209 0.0904 0.1075 0.0248  -0.0003 0.0198  71  ASP A N   
632  C  CA  A ASP A 71  ? 0.1448 0.0910 0.1533 0.0288  -0.0131 0.0500  71  ASP A CA  
633  C  CA  B ASP A 71  ? 0.1641 0.0898 0.1450 0.0030  0.0005  0.0502  71  ASP A CA  
634  C  C   A ASP A 71  ? 0.1377 0.0799 0.1631 0.0131  -0.0151 0.0146  71  ASP A C   
635  C  C   B ASP A 71  ? 0.1744 0.0722 0.1902 0.0114  0.0350  0.0432  71  ASP A C   
636  O  O   A ASP A 71  ? 0.1542 0.1376 0.1485 -0.0127 -0.0179 0.0170  71  ASP A O   
637  O  O   B ASP A 71  ? 0.1931 0.1101 0.1961 -0.0104 0.0254  -0.0126 71  ASP A O   
638  C  CB  A ASP A 71  ? 0.1613 0.1031 0.1571 0.0579  -0.0034 0.0423  71  ASP A CB  
639  C  CB  B ASP A 71  ? 0.1747 0.1297 0.1448 0.0320  0.0057  0.0734  71  ASP A CB  
640  C  CG  A ASP A 71  ? 0.1440 0.0952 0.1870 0.0132  -0.0174 0.0434  71  ASP A CG  
641  C  CG  B ASP A 71  ? 0.2403 0.1293 0.1714 0.0601  -0.0621 0.0096  71  ASP A CG  
642  O  OD1 A ASP A 71  ? 0.2143 0.0833 0.2018 0.0298  -0.0282 0.0335  71  ASP A OD1 
643  O  OD1 B ASP A 71  ? 0.2910 0.0875 0.1776 0.0237  -0.0456 0.0297  71  ASP A OD1 
644  O  OD2 A ASP A 71  ? 0.1852 0.1210 0.3149 0.0467  -0.0715 0.0299  71  ASP A OD2 
645  O  OD2 B ASP A 71  ? 0.4410 0.1424 0.2280 0.0762  -0.0852 0.0533  71  ASP A OD2 
646  N  N   . ASP A 72  ? 0.1650 0.0945 0.2053 0.0242  0.0071  0.0118  72  ASP A N   
647  C  CA  . ASP A 72  ? 0.1736 0.0870 0.2117 0.0219  0.0252  0.0142  72  ASP A CA  
648  C  C   . ASP A 72  ? 0.2001 0.0883 0.2486 -0.0120 0.0430  0.0020  72  ASP A C   
649  O  O   . ASP A 72  ? 0.3039 0.1106 0.2496 -0.0038 0.0733  -0.0161 72  ASP A O   
650  C  CB  . ASP A 72  ? 0.2138 0.0993 0.1747 0.0234  0.0313  -0.0065 72  ASP A CB  
651  C  CG  . ASP A 72  ? 0.2099 0.1714 0.1389 0.0265  0.0203  0.0197  72  ASP A CG  
652  O  OD1 . ASP A 72  ? 0.1893 0.2240 0.1840 0.0105  -0.0013 0.0496  72  ASP A OD1 
653  O  OD2 . ASP A 72  ? 0.2162 0.1689 0.1322 0.0057  0.0031  0.0076  72  ASP A OD2 
654  N  N   . SER A 73  ? 0.1959 0.0869 0.2992 0.0194  0.0472  0.0505  73  SER A N   
655  C  CA  . SER A 73  ? 0.2455 0.0995 0.3023 0.0096  0.0872  0.0384  73  SER A CA  
656  C  C   . SER A 73  ? 0.2423 0.0949 0.3097 0.0115  0.0741  -0.0073 73  SER A C   
657  O  O   . SER A 73  ? 0.2980 0.0929 0.2969 0.0452  0.0373  0.0114  73  SER A O   
658  C  CB  . SER A 73  ? 0.2964 0.0893 0.2457 -0.0054 0.0784  0.0335  73  SER A CB  
659  O  OG  . SER A 73  ? 0.3064 0.1385 0.2838 0.0381  0.0274  0.0509  73  SER A OG  
660  N  N   . GLN A 74  ? 0.2642 0.1063 0.3695 0.0078  0.1030  0.0166  74  GLN A N   
661  C  CA  . GLN A 74  ? 0.3077 0.1673 0.4523 0.0658  0.1569  0.0218  74  GLN A CA  
662  C  C   . GLN A 74  ? 0.1791 0.1680 0.3197 0.0397  -0.0076 -0.0035 74  GLN A C   
663  O  O   . GLN A 74  ? 0.1875 0.1922 0.2254 -0.0283 -0.0270 0.0308  74  GLN A O   
664  C  CB  . GLN A 74  ? 0.2585 0.4939 0.4216 0.1465  -0.0038 -0.1048 74  GLN A CB  
665  C  CG  . GLN A 74  ? 0.2269 0.3084 0.6643 0.0671  -0.1413 -0.2336 74  GLN A CG  
666  C  CD  . GLN A 74  ? 0.3134 0.2436 0.3643 0.0478  0.0621  0.0425  74  GLN A CD  
667  O  OE1 . GLN A 74  ? 0.4779 0.7192 0.8794 0.2383  0.1735  -0.0147 74  GLN A OE1 
668  N  NE2 . GLN A 74  ? 0.4801 0.4672 0.3659 0.0059  -0.0362 -0.1836 74  GLN A NE2 
669  N  N   A ASP A 75  ? 0.1758 0.5106 0.3526 -0.1189 0.0855  -0.1048 75  ASP A N   
670  N  N   B ASP A 75  ? 0.1656 0.1243 0.1921 0.0288  -0.0428 0.0265  75  ASP A N   
671  C  CA  A ASP A 75  ? 0.3874 0.3422 0.2903 0.0100  -0.0939 -0.1372 75  ASP A CA  
672  C  CA  B ASP A 75  ? 0.1763 0.0782 0.2308 -0.0196 -0.0368 0.0425  75  ASP A CA  
673  C  C   A ASP A 75  ? 0.4104 0.2380 0.5012 -0.0088 -0.0390 -0.0737 75  ASP A C   
674  C  C   B ASP A 75  ? 0.1595 0.1297 0.3445 -0.0458 -0.0463 0.0239  75  ASP A C   
675  O  O   A ASP A 75  ? 0.5504 0.4598 0.9451 0.1937  -0.0533 0.1564  75  ASP A O   
676  O  O   B ASP A 75  ? 0.1872 0.1385 0.4388 -0.0348 -0.0628 -0.0595 75  ASP A O   
677  C  CB  A ASP A 75  ? 0.3907 0.5360 0.2508 0.0423  0.0252  -0.0645 75  ASP A CB  
678  C  CB  B ASP A 75  ? 0.2278 0.1385 0.2479 -0.0030 0.0524  0.0544  75  ASP A CB  
679  C  CG  A ASP A 75  ? 0.2260 0.3700 0.2561 0.0340  0.1315  -0.0247 75  ASP A CG  
680  C  CG  B ASP A 75  ? 0.2455 0.1887 0.2031 0.0003  0.0518  0.0331  75  ASP A CG  
681  O  OD1 A ASP A 75  ? 0.2148 0.2642 0.1000 -0.0175 0.0074  0.0161  75  ASP A OD1 
682  O  OD1 B ASP A 75  ? 0.1532 0.2169 0.2558 -0.0390 0.0174  0.0640  75  ASP A OD1 
683  O  OD2 A ASP A 75  ? 0.3190 0.3276 0.1810 0.1115  0.0153  -0.0043 75  ASP A OD2 
684  O  OD2 B ASP A 75  ? 0.4004 0.3508 0.2585 0.1107  0.0832  -0.0500 75  ASP A OD2 
685  N  N   . LYS A 76  ? 0.1722 0.1563 0.2786 -0.0344 -0.0436 0.0671  76  LYS A N   
686  C  CA  . LYS A 76  ? 0.2031 0.1353 0.3966 -0.0008 -0.0076 0.0328  76  LYS A CA  
687  C  C   . LYS A 76  ? 0.3082 0.1852 0.4661 0.0068  -0.0200 0.1044  76  LYS A C   
688  O  O   . LYS A 76  ? 0.2791 0.3242 0.4708 -0.0162 0.0476  0.1474  76  LYS A O   
689  C  CB  . LYS A 76  ? 0.2684 0.1203 0.3503 -0.0361 -0.1238 0.0524  76  LYS A CB  
690  C  CG  . LYS A 76  ? 0.5605 0.1969 0.3352 0.0219  -0.2651 0.0533  76  LYS A CG  
691  C  CD  . LYS A 76  ? 0.7415 0.1469 0.3143 -0.0966 -0.1568 0.0308  76  LYS A CD  
692  C  CE  . LYS A 76  ? 0.4336 0.2569 0.2867 -0.0219 0.0038  0.0408  76  LYS A CE  
693  N  NZ  . LYS A 76  ? 0.4365 0.3165 0.3504 0.0986  -0.0024 0.1464  76  LYS A NZ  
694  N  N   . ALA A 77  ? 0.3003 0.2037 0.3120 0.0507  -0.1801 0.0399  77  ALA A N   
695  C  CA  . ALA A 77  ? 0.1268 0.1978 0.1780 -0.0024 -0.0214 0.0344  77  ALA A CA  
696  C  C   . ALA A 77  ? 0.0829 0.1677 0.2029 0.0043  -0.0403 0.0194  77  ALA A C   
697  O  O   . ALA A 77  ? 0.1421 0.2362 0.2072 -0.0237 -0.0076 0.0373  77  ALA A O   
698  C  CB  . ALA A 77  ? 0.1952 0.2152 0.2125 0.0264  -0.0551 -0.0037 77  ALA A CB  
699  N  N   A VAL A 78  ? 0.1138 0.1286 0.2014 -0.0057 -0.0132 0.0328  78  VAL A N   
700  N  N   B VAL A 78  ? 0.1237 0.1080 0.1467 -0.0077 -0.0410 0.0417  78  VAL A N   
701  C  CA  A VAL A 78  ? 0.1664 0.1324 0.1475 0.0388  -0.0125 0.0183  78  VAL A CA  
702  C  CA  B VAL A 78  ? 0.1036 0.0898 0.1368 -0.0168 -0.0163 0.0255  78  VAL A CA  
703  C  C   A VAL A 78  ? 0.0972 0.1112 0.1456 0.0054  -0.0160 -0.0113 78  VAL A C   
704  C  C   B VAL A 78  ? 0.0896 0.0936 0.1291 -0.0020 0.0193  0.0159  78  VAL A C   
705  O  O   A VAL A 78  ? 0.1268 0.1168 0.1151 -0.0080 -0.0184 0.0017  78  VAL A O   
706  O  O   B VAL A 78  ? 0.0952 0.1067 0.1102 -0.0038 0.0167  0.0027  78  VAL A O   
707  C  CB  A VAL A 78  ? 0.1404 0.1242 0.1645 0.0001  -0.0149 0.0093  78  VAL A CB  
708  C  CB  B VAL A 78  ? 0.0732 0.1254 0.1483 0.0066  -0.0001 0.0351  78  VAL A CB  
709  C  CG1 A VAL A 78  ? 0.1562 0.1402 0.2373 0.0348  0.0137  0.0630  78  VAL A CG1 
710  C  CG1 B VAL A 78  ? 0.1000 0.1501 0.1581 0.0125  0.0082  0.0188  78  VAL A CG1 
711  C  CG2 A VAL A 78  ? 0.1316 0.1815 0.2369 0.0588  0.0146  -0.0322 78  VAL A CG2 
712  C  CG2 B VAL A 78  ? 0.1787 0.1107 0.1867 0.0184  0.0049  0.0265  78  VAL A CG2 
713  N  N   . LEU A 79  ? 0.0999 0.1181 0.1290 -0.0046 0.0013  0.0174  79  LEU A N   
714  C  CA  . LEU A 79  ? 0.0914 0.1112 0.1372 -0.0081 0.0024  0.0013  79  LEU A CA  
715  C  C   . LEU A 79  ? 0.0919 0.1137 0.1400 0.0017  0.0041  0.0082  79  LEU A C   
716  O  O   . LEU A 79  ? 0.1154 0.1199 0.1396 -0.0119 0.0115  0.0046  79  LEU A O   
717  C  CB  . LEU A 79  ? 0.1020 0.1120 0.1438 -0.0008 0.0076  0.0131  79  LEU A CB  
718  C  CG  . LEU A 79  ? 0.1203 0.1251 0.1351 0.0143  0.0165  0.0161  79  LEU A CG  
719  C  CD1 . LEU A 79  ? 0.1101 0.1322 0.2694 0.0038  0.0395  0.0493  79  LEU A CD1 
720  C  CD2 . LEU A 79  ? 0.1164 0.1476 0.1339 0.0162  0.0077  0.0055  79  LEU A CD2 
721  N  N   . LYS A 80  ? 0.1049 0.1152 0.1314 -0.0065 0.0230  0.0085  80  LYS A N   
722  C  CA  . LYS A 80  ? 0.1187 0.1137 0.1578 -0.0005 0.0184  0.0176  80  LYS A CA  
723  C  C   . LYS A 80  ? 0.1058 0.1112 0.1459 0.0115  0.0333  0.0126  80  LYS A C   
724  O  O   . LYS A 80  ? 0.1058 0.1256 0.1620 -0.0017 0.0055  0.0309  80  LYS A O   
725  C  CB  . LYS A 80  ? 0.1877 0.1446 0.1537 0.0399  0.0304  0.0114  80  LYS A CB  
726  C  CG  . LYS A 80  ? 0.1898 0.1472 0.2333 0.0066  0.0276  0.0458  80  LYS A CG  
727  C  CD  . LYS A 80  ? 0.1617 0.2093 0.3506 0.0848  -0.0071 -0.0015 80  LYS A CD  
728  C  CE  . LYS A 80  ? 0.5608 0.3907 0.6485 0.1914  -0.0922 -0.1767 80  LYS A CE  
729  N  NZ  . LYS A 80  ? 0.7325 0.6054 0.8970 0.4320  0.2184  -0.0450 80  LYS A NZ  
730  N  N   . GLY A 81  ? 0.1509 0.1289 0.1471 0.0255  0.0493  0.0219  81  GLY A N   
731  C  CA  . GLY A 81  ? 0.1489 0.1386 0.1747 0.0333  0.0509  0.0386  81  GLY A CA  
732  C  C   . GLY A 81  ? 0.1437 0.1351 0.2010 0.0233  0.0518  0.0305  81  GLY A C   
733  O  O   . GLY A 81  ? 0.1155 0.1314 0.1761 0.0065  0.0333  0.0034  81  GLY A O   
734  N  N   . GLY A 82  ? 0.1420 0.1720 0.3709 0.0549  0.1028  0.1119  82  GLY A N   
735  C  CA  . GLY A 82  ? 0.2050 0.1503 0.2793 0.0500  0.0507  0.0878  82  GLY A CA  
736  C  C   . GLY A 82  ? 0.1732 0.1865 0.2124 0.0640  0.0533  0.0648  82  GLY A C   
737  O  O   . GLY A 82  ? 0.2293 0.2475 0.2240 0.1212  0.1098  0.0529  82  GLY A O   
738  N  N   . PRO A 83  ? 0.1658 0.1393 0.2362 0.0625  0.0872  0.0707  83  PRO A N   
739  C  CA  . PRO A 83  ? 0.2047 0.1651 0.2056 0.0750  0.0397  0.0592  83  PRO A CA  
740  C  C   . PRO A 83  ? 0.1767 0.1772 0.1533 0.0390  0.0187  -0.0057 83  PRO A C   
741  O  O   . PRO A 83  ? 0.2412 0.2257 0.1777 0.0615  -0.0126 0.0266  83  PRO A O   
742  C  CB  . PRO A 83  ? 0.1967 0.1485 0.1956 0.0615  0.0155  0.0401  83  PRO A CB  
743  C  CG  . PRO A 83  ? 0.1335 0.1501 0.1738 0.0322  0.0439  0.0318  83  PRO A CG  
744  C  CD  . PRO A 83  ? 0.1483 0.1162 0.2457 0.0263  0.0606  0.0243  83  PRO A CD  
745  N  N   . LEU A 84  ? 0.1551 0.1244 0.1447 0.0434  0.0357  0.0176  84  LEU A N   
746  C  CA  . LEU A 84  ? 0.1307 0.1142 0.1511 0.0373  0.0241  -0.0098 84  LEU A CA  
747  C  C   . LEU A 84  ? 0.1685 0.1120 0.1905 0.0443  0.0109  -0.0234 84  LEU A C   
748  O  O   . LEU A 84  ? 0.1729 0.1758 0.2143 0.0639  0.0192  -0.0373 84  LEU A O   
749  C  CB  . LEU A 84  ? 0.1269 0.0938 0.1570 0.0285  0.0234  -0.0092 84  LEU A CB  
750  C  CG  . LEU A 84  ? 0.1217 0.0928 0.1542 0.0179  0.0331  0.0044  84  LEU A CG  
751  C  CD1 . LEU A 84  ? 0.1463 0.1154 0.1428 0.0196  0.0227  -0.0111 84  LEU A CD1 
752  C  CD2 . LEU A 84  ? 0.1146 0.0979 0.1613 0.0132  0.0303  -0.0017 84  LEU A CD2 
753  N  N   . ASP A 85  ? 0.2019 0.1150 0.1821 0.0527  -0.0015 -0.0320 85  ASP A N   
754  C  CA  . ASP A 85  ? 0.3116 0.1204 0.1733 0.0478  -0.0140 -0.0375 85  ASP A CA  
755  C  C   . ASP A 85  ? 0.2615 0.1086 0.2533 0.0489  0.0089  -0.0097 85  ASP A C   
756  O  O   . ASP A 85  ? 0.2502 0.2345 0.2152 0.0500  0.0328  -0.0494 85  ASP A O   
757  C  CB  . ASP A 85  ? 0.3199 0.1256 0.2222 0.0251  0.0443  -0.0200 85  ASP A CB  
758  C  CG  . ASP A 85  ? 0.2117 0.2971 0.2441 0.0080  0.0592  0.0043  85  ASP A CG  
759  O  OD1 . ASP A 85  ? 0.2703 0.3878 0.2108 -0.0377 0.0381  0.0416  85  ASP A OD1 
760  O  OD2 . ASP A 85  ? 0.3064 0.3772 0.2561 -0.0992 -0.0195 0.0006  85  ASP A OD2 
761  N  N   . GLY A 86  ? 0.2450 0.2342 0.2071 0.0379  -0.0100 0.0300  86  GLY A N   
762  C  CA  . GLY A 86  ? 0.2621 0.2384 0.1809 -0.0122 0.0098  0.0456  86  GLY A CA  
763  C  C   . GLY A 86  ? 0.2019 0.2132 0.1740 -0.0304 -0.0109 0.0322  86  GLY A C   
764  O  O   . GLY A 86  ? 0.3059 0.3170 0.2524 -0.1500 -0.0195 0.0794  86  GLY A O   
765  N  N   A THR A 87  ? 0.1641 0.1332 0.1780 0.0335  0.0093  -0.0125 87  THR A N   
766  N  N   B THR A 87  ? 0.1395 0.1386 0.1706 0.0048  0.0546  -0.0133 87  THR A N   
767  C  CA  A THR A 87  ? 0.1457 0.1438 0.1783 0.0445  -0.0082 -0.0355 87  THR A CA  
768  C  CA  B THR A 87  ? 0.1058 0.1160 0.1890 0.0168  0.0288  -0.0028 87  THR A CA  
769  C  C   A THR A 87  ? 0.1253 0.0838 0.1362 0.0076  -0.0086 0.0043  87  THR A C   
770  C  C   B THR A 87  ? 0.1122 0.0952 0.1216 0.0115  0.0142  0.0027  87  THR A C   
771  O  O   A THR A 87  ? 0.1242 0.0907 0.1145 0.0126  -0.0057 -0.0092 87  THR A O   
772  O  O   B THR A 87  ? 0.1268 0.0800 0.1102 0.0082  -0.0074 0.0168  87  THR A O   
773  C  CB  A THR A 87  ? 0.1511 0.1497 0.2296 0.0710  -0.0065 -0.0157 87  THR A CB  
774  C  CB  B THR A 87  ? 0.1143 0.1193 0.1850 0.0057  0.0092  0.0038  87  THR A CB  
775  O  OG1 A THR A 87  ? 0.2144 0.2421 0.2745 0.1498  0.0021  -0.0777 87  THR A OG1 
776  O  OG1 B THR A 87  ? 0.1243 0.1081 0.1614 0.0231  0.0071  0.0098  87  THR A OG1 
777  C  CG2 A THR A 87  ? 0.1914 0.2448 0.2468 0.1108  -0.0410 -0.0684 87  THR A CG2 
778  C  CG2 B THR A 87  ? 0.1252 0.1625 0.2594 0.0181  0.0485  0.0406  87  THR A CG2 
779  N  N   . TYR A 88  ? 0.0986 0.0878 0.1374 0.0163  0.0094  0.0049  88  TYR A N   
780  C  CA  . TYR A 88  ? 0.0881 0.0893 0.1309 0.0093  0.0179  0.0153  88  TYR A CA  
781  C  C   . TYR A 88  ? 0.0883 0.0946 0.1155 0.0038  -0.0041 0.0082  88  TYR A C   
782  O  O   . TYR A 88  ? 0.1157 0.1732 0.1333 -0.0441 -0.0131 0.0285  88  TYR A O   
783  C  CB  . TYR A 88  ? 0.1120 0.0870 0.1158 0.0087  -0.0057 -0.0098 88  TYR A CB  
784  C  CG  . TYR A 88  ? 0.1049 0.0688 0.1260 0.0092  0.0124  0.0048  88  TYR A CG  
785  C  CD1 . TYR A 88  ? 0.1228 0.0970 0.1129 0.0183  0.0097  0.0054  88  TYR A CD1 
786  C  CD2 . TYR A 88  ? 0.0974 0.0668 0.1005 0.0157  0.0093  0.0015  88  TYR A CD2 
787  C  CE1 . TYR A 88  ? 0.1186 0.0962 0.1207 0.0153  0.0234  0.0055  88  TYR A CE1 
788  C  CE2 . TYR A 88  ? 0.1028 0.0653 0.1085 0.0055  0.0170  0.0000  88  TYR A CE2 
789  C  CZ  . TYR A 88  ? 0.1050 0.0692 0.1025 0.0062  0.0060  -0.0062 88  TYR A CZ  
790  O  OH  . TYR A 88  ? 0.1141 0.0872 0.1068 0.0059  0.0098  -0.0071 88  TYR A OH  
791  N  N   . ARG A 89  ? 0.0940 0.0650 0.1159 0.0165  0.0040  0.0013  89  ARG A N   
792  C  CA  . ARG A 89  ? 0.1000 0.0741 0.1150 0.0115  0.0000  0.0127  89  ARG A CA  
793  C  C   . ARG A 89  ? 0.0935 0.0700 0.0988 0.0028  -0.0104 0.0104  89  ARG A C   
794  O  O   . ARG A 89  ? 0.0955 0.0771 0.1027 0.0038  -0.0017 0.0037  89  ARG A O   
795  C  CB  . ARG A 89  ? 0.1427 0.0635 0.1493 0.0019  -0.0037 0.0204  89  ARG A CB  
796  C  CG  . ARG A 89  ? 0.2173 0.0825 0.1166 0.0054  -0.0092 0.0096  89  ARG A CG  
797  C  CD  . ARG A 89  ? 0.2423 0.0860 0.1468 0.0247  0.0228  0.0099  89  ARG A CD  
798  N  NE  . ARG A 89  ? 0.2473 0.0973 0.1675 0.0006  0.0164  0.0366  89  ARG A NE  
799  C  CZ  . ARG A 89  ? 0.2102 0.1146 0.1466 0.0200  0.0210  0.0115  89  ARG A CZ  
800  N  NH1 . ARG A 89  ? 0.2517 0.1010 0.2046 0.0186  0.0575  0.0337  89  ARG A NH1 
801  N  NH2 . ARG A 89  ? 0.2845 0.1293 0.1872 0.0650  0.0454  0.0273  89  ARG A NH2 
802  N  N   . LEU A 90  ? 0.1076 0.0662 0.1077 0.0038  -0.0086 0.0147  90  LEU A N   
803  C  CA  . LEU A 90  ? 0.1034 0.0744 0.1017 -0.0048 -0.0124 0.0074  90  LEU A CA  
804  C  C   . LEU A 90  ? 0.0995 0.0790 0.1058 0.0137  -0.0152 0.0074  90  LEU A C   
805  O  O   . LEU A 90  ? 0.1093 0.0951 0.1137 0.0259  -0.0052 0.0253  90  LEU A O   
806  C  CB  . LEU A 90  ? 0.1035 0.0913 0.1215 -0.0020 -0.0141 0.0144  90  LEU A CB  
807  C  CG  . LEU A 90  ? 0.1187 0.0874 0.1213 -0.0066 -0.0148 -0.0148 90  LEU A CG  
808  C  CD1 . LEU A 90  ? 0.1412 0.0781 0.1322 -0.0057 -0.0130 0.0000  90  LEU A CD1 
809  C  CD2 . LEU A 90  ? 0.1340 0.1200 0.1239 -0.0152 -0.0296 -0.0131 90  LEU A CD2 
810  N  N   . PHE A 91  ? 0.1097 0.0636 0.0912 0.0037  -0.0074 0.0068  91  PHE A N   
811  C  CA  . PHE A 91  ? 0.1167 0.0619 0.1020 0.0000  -0.0094 0.0126  91  PHE A CA  
812  C  C   . PHE A 91  ? 0.0908 0.0629 0.1007 0.0000  -0.0152 0.0087  91  PHE A C   
813  O  O   . PHE A 91  ? 0.1125 0.0749 0.0905 0.0044  -0.0010 0.0237  91  PHE A O   
814  C  CB  . PHE A 91  ? 0.1216 0.0664 0.1129 -0.0049 0.0000  0.0126  91  PHE A CB  
815  C  CG  . PHE A 91  ? 0.0986 0.0617 0.1090 -0.0041 -0.0059 -0.0020 91  PHE A CG  
816  C  CD1 . PHE A 91  ? 0.1042 0.0659 0.1110 -0.0066 0.0023  0.0062  91  PHE A CD1 
817  C  CD2 . PHE A 91  ? 0.1026 0.0610 0.1048 -0.0024 0.0028  -0.0015 91  PHE A CD2 
818  C  CE1 . PHE A 91  ? 0.1058 0.0732 0.1025 -0.0131 0.0038  -0.0065 91  PHE A CE1 
819  C  CE2 . PHE A 91  ? 0.1072 0.0681 0.1007 -0.0152 0.0082  -0.0052 91  PHE A CE2 
820  C  CZ  . PHE A 91  ? 0.0952 0.0682 0.1049 -0.0119 0.0023  -0.0046 91  PHE A CZ  
821  N  N   . GLN A 92  ? 0.1099 0.0570 0.0844 0.0035  -0.0017 0.0131  92  GLN A N   
822  C  CA  . GLN A 92  ? 0.1032 0.0654 0.0816 0.0060  -0.0020 0.0168  92  GLN A CA  
823  C  C   . GLN A 92  ? 0.0964 0.0698 0.0747 0.0120  -0.0051 0.0126  92  GLN A C   
824  O  O   . GLN A 92  ? 0.1254 0.0625 0.0750 0.0120  -0.0044 0.0071  92  GLN A O   
825  C  CB  . GLN A 92  ? 0.0996 0.0891 0.1160 0.0109  -0.0098 0.0178  92  GLN A CB  
826  C  CG  . GLN A 92  ? 0.1149 0.0896 0.0908 0.0000  -0.0068 0.0035  92  GLN A CG  
827  C  CD  . GLN A 92  ? 0.0975 0.0876 0.1061 0.0000  -0.0193 0.0021  92  GLN A CD  
828  O  OE1 . GLN A 92  ? 0.1133 0.0738 0.1201 0.0006  -0.0318 0.0185  92  GLN A OE1 
829  N  NE2 . GLN A 92  ? 0.1031 0.1288 0.1116 -0.0010 -0.0100 0.0044  92  GLN A NE2 
830  N  N   . PHE A 93  ? 0.0894 0.0586 0.0754 0.0017  -0.0068 0.0076  93  PHE A N   
831  C  CA  . PHE A 93  ? 0.0935 0.0571 0.0778 0.0030  -0.0054 0.0077  93  PHE A CA  
832  C  C   . PHE A 93  ? 0.0789 0.0689 0.0657 -0.0010 -0.0126 0.0127  93  PHE A C   
833  O  O   . PHE A 93  ? 0.0932 0.0658 0.0692 0.0057  -0.0013 0.0088  93  PHE A O   
834  C  CB  . PHE A 93  ? 0.0891 0.0756 0.0798 0.0063  -0.0073 0.0107  93  PHE A CB  
835  C  CG  . PHE A 93  ? 0.0829 0.0690 0.0820 0.0026  -0.0038 0.0083  93  PHE A CG  
836  C  CD1 . PHE A 93  ? 0.0963 0.0785 0.0879 0.0043  -0.0137 0.0012  93  PHE A CD1 
837  C  CD2 . PHE A 93  ? 0.0893 0.0793 0.0909 0.0051  -0.0052 0.0104  93  PHE A CD2 
838  C  CE1 . PHE A 93  ? 0.0987 0.0798 0.0952 -0.0015 -0.0120 -0.0015 93  PHE A CE1 
839  C  CE2 . PHE A 93  ? 0.0944 0.0886 0.0937 0.0060  -0.0236 0.0077  93  PHE A CE2 
840  C  CZ  . PHE A 93  ? 0.0961 0.0882 0.0995 0.0048  -0.0231 0.0034  93  PHE A CZ  
841  N  N   . HIS A 94  ? 0.0819 0.0653 0.0689 0.0073  -0.0026 0.0070  94  HIS A N   
842  C  CA  . HIS A 94  ? 0.0840 0.0715 0.0625 0.0015  -0.0051 0.0062  94  HIS A CA  
843  C  C   . HIS A 94  ? 0.0823 0.0621 0.0606 0.0043  -0.0041 0.0020  94  HIS A C   
844  O  O   . HIS A 94  ? 0.0962 0.0637 0.0643 0.0060  0.0038  0.0052  94  HIS A O   
845  C  CB  . HIS A 94  ? 0.0881 0.0688 0.0655 -0.0026 -0.0035 0.0138  94  HIS A CB  
846  C  CG  . HIS A 94  ? 0.0785 0.0645 0.0750 -0.0040 -0.0010 0.0060  94  HIS A CG  
847  N  ND1 . HIS A 94  ? 0.0879 0.0631 0.0734 -0.0027 -0.0097 0.0041  94  HIS A ND1 
848  C  CD2 . HIS A 94  ? 0.0806 0.0758 0.0687 -0.0020 -0.0041 0.0024  94  HIS A CD2 
849  C  CE1 . HIS A 94  ? 0.0819 0.0615 0.0766 -0.0023 -0.0032 0.0032  94  HIS A CE1 
850  N  NE2 . HIS A 94  ? 0.0742 0.0597 0.0737 -0.0048 -0.0017 0.0074  94  HIS A NE2 
851  N  N   . PHE A 95  ? 0.0802 0.0623 0.0706 -0.0052 -0.0089 0.0041  95  PHE A N   
852  C  CA  . PHE A 95  ? 0.0800 0.0608 0.0715 0.0032  -0.0043 0.0052  95  PHE A CA  
853  C  C   . PHE A 95  ? 0.0863 0.0666 0.0625 -0.0008 -0.0035 -0.0038 95  PHE A C   
854  O  O   . PHE A 95  ? 0.0879 0.0769 0.0785 0.0006  0.0038  0.0154  95  PHE A O   
855  C  CB  . PHE A 95  ? 0.0847 0.0738 0.0754 0.0027  -0.0043 -0.0013 95  PHE A CB  
856  C  CG  . PHE A 95  ? 0.0875 0.0694 0.0689 -0.0017 -0.0093 -0.0046 95  PHE A CG  
857  C  CD1 . PHE A 95  ? 0.1046 0.0803 0.0740 0.0066  -0.0094 0.0006  95  PHE A CD1 
858  C  CD2 . PHE A 95  ? 0.0791 0.0813 0.0855 -0.0082 -0.0040 -0.0119 95  PHE A CD2 
859  C  CE1 . PHE A 95  ? 0.1128 0.0974 0.0898 0.0098  -0.0265 -0.0068 95  PHE A CE1 
860  C  CE2 . PHE A 95  ? 0.0902 0.0846 0.1007 -0.0012 -0.0017 -0.0162 95  PHE A CE2 
861  C  CZ  . PHE A 95  ? 0.0930 0.0911 0.0918 0.0074  -0.0175 -0.0159 95  PHE A CZ  
862  N  N   . HIS A 96  ? 0.0806 0.0627 0.0624 0.0015  -0.0046 0.0000  96  HIS A N   
863  C  CA  . HIS A 96  ? 0.0772 0.0617 0.0725 0.0055  0.0013  -0.0049 96  HIS A CA  
864  C  C   . HIS A 96  ? 0.0758 0.0674 0.0674 0.0087  -0.0027 -0.0005 96  HIS A C   
865  O  O   . HIS A 96  ? 0.0812 0.0662 0.0795 0.0024  0.0043  -0.0031 96  HIS A O   
866  C  CB  . HIS A 96  ? 0.0807 0.0728 0.0784 0.0102  -0.0044 -0.0062 96  HIS A CB  
867  C  CG  . HIS A 96  ? 0.0822 0.0759 0.0720 0.0054  -0.0099 0.0012  96  HIS A CG  
868  N  ND1 . HIS A 96  ? 0.0752 0.0688 0.1037 0.0060  -0.0063 -0.0038 96  HIS A ND1 
869  C  CD2 . HIS A 96  ? 0.0840 0.0590 0.0747 0.0032  -0.0082 -0.0013 96  HIS A CD2 
870  C  CE1 . HIS A 96  ? 0.0820 0.0685 0.0986 0.0000  -0.0001 -0.0057 96  HIS A CE1 
871  N  NE2 . HIS A 96  ? 0.0734 0.0688 0.0717 -0.0024 0.0015  0.0012  96  HIS A NE2 
872  N  N   . TRP A 97  ? 0.0892 0.0646 0.0680 0.0052  0.0031  -0.0015 97  TRP A N   
873  C  CA  . TRP A 97  ? 0.0843 0.0582 0.0791 0.0065  0.0062  -0.0049 97  TRP A CA  
874  C  C   . TRP A 97  ? 0.1000 0.0649 0.0691 0.0040  0.0083  0.0000  97  TRP A C   
875  O  O   . TRP A 97  ? 0.0870 0.0707 0.0855 0.0074  0.0137  0.0013  97  TRP A O   
876  C  CB  . TRP A 97  ? 0.0975 0.0784 0.0673 -0.0046 -0.0054 -0.0019 97  TRP A CB  
877  C  CG  . TRP A 97  ? 0.0900 0.0726 0.0738 0.0020  -0.0035 -0.0105 97  TRP A CG  
878  C  CD1 . TRP A 97  ? 0.1133 0.0847 0.0744 0.0057  0.0065  -0.0044 97  TRP A CD1 
879  C  CD2 . TRP A 97  ? 0.0890 0.0814 0.0687 -0.0013 -0.0010 -0.0006 97  TRP A CD2 
880  N  NE1 . TRP A 97  ? 0.1162 0.0834 0.0823 0.0049  0.0130  -0.0017 97  TRP A NE1 
881  C  CE2 . TRP A 97  ? 0.1019 0.0746 0.0741 0.0037  0.0077  -0.0041 97  TRP A CE2 
882  C  CE3 . TRP A 97  ? 0.0988 0.0712 0.0716 0.0023  -0.0031 0.0000  97  TRP A CE3 
883  C  CZ2 . TRP A 97  ? 0.1023 0.0887 0.0752 0.0003  0.0027  0.0044  97  TRP A CZ2 
884  C  CZ3 . TRP A 97  ? 0.0947 0.0840 0.0729 0.0098  0.0000  -0.0048 97  TRP A CZ3 
885  C  CH2 . TRP A 97  ? 0.1067 0.0770 0.0789 -0.0008 -0.0017 0.0027  97  TRP A CH2 
886  N  N   . GLY A 98  ? 0.1105 0.0684 0.0698 0.0031  0.0085  -0.0074 98  GLY A N   
887  C  CA  . GLY A 98  ? 0.1185 0.0699 0.0816 0.0228  0.0073  -0.0051 98  GLY A CA  
888  C  C   . GLY A 98  ? 0.1171 0.0680 0.0863 0.0010  0.0059  0.0000  98  GLY A C   
889  O  O   . GLY A 98  ? 0.1374 0.0749 0.0900 0.0076  0.0031  -0.0098 98  GLY A O   
890  N  N   . SER A 99  ? 0.1372 0.0689 0.1013 0.0120  0.0229  -0.0127 99  SER A N   
891  C  CA  . SER A 99  ? 0.1318 0.0780 0.1128 0.0102  0.0132  -0.0243 99  SER A CA  
892  C  C   . SER A 99  ? 0.1330 0.0842 0.1297 0.0228  0.0071  -0.0296 99  SER A C   
893  O  O   . SER A 99  ? 0.1909 0.1068 0.1570 0.0089  -0.0082 -0.0588 99  SER A O   
894  C  CB  . SER A 99  ? 0.1428 0.0949 0.1342 0.0287  0.0266  -0.0263 99  SER A CB  
895  O  OG  . SER A 99  ? 0.1367 0.0873 0.1714 0.0250  0.0296  -0.0046 99  SER A OG  
896  N  N   . LEU A 100 ? 0.1268 0.0712 0.1378 0.0104  0.0130  -0.0208 100 LEU A N   
897  C  CA  . LEU A 100 ? 0.1448 0.0767 0.1731 0.0108  0.0215  -0.0233 100 LEU A CA  
898  C  C   . LEU A 100 ? 0.1435 0.0636 0.1492 0.0012  0.0132  -0.0230 100 LEU A C   
899  O  O   . LEU A 100 ? 0.1494 0.0687 0.1356 0.0031  0.0096  -0.0186 100 LEU A O   
900  C  CB  . LEU A 100 ? 0.1787 0.1079 0.1824 0.0270  0.0244  -0.0046 100 LEU A CB  
901  C  CG  . LEU A 100 ? 0.2070 0.1171 0.2097 0.0430  0.0223  -0.0274 100 LEU A CG  
902  C  CD1 . LEU A 100 ? 0.2025 0.2418 0.2727 0.1026  -0.0208 -0.0392 100 LEU A CD1 
903  C  CD2 . LEU A 100 ? 0.2486 0.1507 0.2632 0.0238  0.0822  -0.0599 100 LEU A CD2 
904  N  N   . ASP A 101 ? 0.1291 0.0791 0.1644 0.0065  0.0140  -0.0267 101 ASP A N   
905  C  CA  . ASP A 101 ? 0.1486 0.0653 0.1394 0.0074  0.0234  -0.0102 101 ASP A CA  
906  C  C   . ASP A 101 ? 0.1648 0.0653 0.1384 -0.0006 0.0219  0.0017  101 ASP A C   
907  O  O   . ASP A 101 ? 0.2210 0.0808 0.1457 0.0234  0.0392  0.0093  101 ASP A O   
908  C  CB  . ASP A 101 ? 0.1661 0.0997 0.1475 -0.0020 0.0156  0.0041  101 ASP A CB  
909  C  CG  . ASP A 101 ? 0.1553 0.1045 0.1876 -0.0304 0.0412  -0.0092 101 ASP A CG  
910  O  OD1 . ASP A 101 ? 0.1570 0.1279 0.1495 -0.0243 0.0085  -0.0254 101 ASP A OD1 
911  O  OD2 . ASP A 101 ? 0.2275 0.1791 0.2186 -0.0989 0.0274  -0.0214 101 ASP A OD2 
912  N  N   . GLY A 102 ? 0.1828 0.0732 0.1632 -0.0214 -0.0151 0.0230  102 GLY A N   
913  C  CA  . GLY A 102 ? 0.2013 0.1005 0.1792 -0.0432 -0.0163 0.0410  102 GLY A CA  
914  C  C   . GLY A 102 ? 0.1764 0.0852 0.1358 -0.0046 0.0163  0.0214  102 GLY A C   
915  O  O   . GLY A 102 ? 0.2054 0.1101 0.1342 -0.0151 0.0110  0.0260  102 GLY A O   
916  N  N   A GLN A 103 ? 0.1404 0.0719 0.1031 -0.0071 0.0181  0.0054  103 GLN A N   
917  N  N   B GLN A 103 ? 0.1755 0.0711 0.1216 -0.0088 0.0217  0.0113  103 GLN A N   
918  C  CA  A GLN A 103 ? 0.1058 0.0611 0.0864 0.0073  0.0149  0.0000  103 GLN A CA  
919  C  CA  B GLN A 103 ? 0.1837 0.0674 0.1235 -0.0155 0.0188  0.0048  103 GLN A CA  
920  C  C   A GLN A 103 ? 0.1113 0.0666 0.0882 0.0015  0.0154  0.0046  103 GLN A C   
921  C  C   B GLN A 103 ? 0.1198 0.0775 0.0946 0.0054  0.0241  -0.0124 103 GLN A C   
922  O  O   A GLN A 103 ? 0.1208 0.0793 0.0943 -0.0089 0.0074  -0.0028 103 GLN A O   
923  O  O   B GLN A 103 ? 0.1313 0.0668 0.0917 0.0000  0.0216  -0.0097 103 GLN A O   
924  C  CB  A GLN A 103 ? 0.1077 0.0478 0.0786 0.0183  0.0073  -0.0057 103 GLN A CB  
925  C  CB  B GLN A 103 ? 0.2272 0.1045 0.1640 -0.0258 0.0348  0.0474  103 GLN A CB  
926  C  CG  A GLN A 103 ? 0.1006 0.0355 0.0726 0.0263  0.0234  0.0142  103 GLN A CG  
927  C  CG  B GLN A 103 ? 0.3314 0.1899 0.2601 -0.0324 0.0233  0.0544  103 GLN A CG  
928  C  CD  A GLN A 103 ? 0.1114 0.0502 0.0928 0.0329  0.0309  0.0195  103 GLN A CD  
929  C  CD  B GLN A 103 ? 0.3944 0.2928 0.2664 0.0996  -0.0509 -0.0507 103 GLN A CD  
930  O  OE1 A GLN A 103 ? 0.1694 0.1030 0.1395 0.0674  0.0447  0.0604  103 GLN A OE1 
931  O  OE1 B GLN A 103 ? 0.2364 0.1500 0.2444 0.0149  -0.0143 -0.0241 103 GLN A OE1 
932  N  NE2 A GLN A 103 ? 0.1000 0.0640 0.0983 0.0383  0.0195  0.0260  103 GLN A NE2 
933  N  NE2 B GLN A 103 ? 0.2310 0.1902 0.3375 0.0432  0.1110  0.0575  103 GLN A NE2 
934  N  N   . GLY A 104 ? 0.0947 0.0694 0.0888 0.0054  0.0152  0.0000  104 GLY A N   
935  C  CA  . GLY A 104 ? 0.1084 0.0691 0.0784 0.0043  0.0098  -0.0027 104 GLY A CA  
936  C  C   . GLY A 104 ? 0.0829 0.0608 0.0823 -0.0013 0.0003  0.0017  104 GLY A C   
937  O  O   . GLY A 104 ? 0.0964 0.0714 0.0888 0.0000  0.0059  0.0030  104 GLY A O   
938  N  N   . SER A 105 ? 0.0884 0.0688 0.0723 -0.0006 0.0043  -0.0032 105 SER A N   
939  C  CA  . SER A 105 ? 0.0861 0.0652 0.0769 0.0003  0.0030  -0.0062 105 SER A CA  
940  C  C   . SER A 105 ? 0.0812 0.0662 0.0715 0.0020  0.0049  0.0040  105 SER A C   
941  O  O   . SER A 105 ? 0.0896 0.0678 0.0925 0.0087  -0.0031 -0.0055 105 SER A O   
942  C  CB  . SER A 105 ? 0.0887 0.0650 0.0802 0.0012  0.0035  0.0008  105 SER A CB  
943  O  OG  . SER A 105 ? 0.0981 0.0650 0.0839 0.0024  0.0023  0.0043  105 SER A OG  
944  N  N   . GLU A 106 ? 0.0812 0.0590 0.0692 -0.0003 -0.0035 0.0019  106 GLU A N   
945  C  CA  . GLU A 106 ? 0.0812 0.0653 0.0709 0.0055  0.0000  0.0041  106 GLU A CA  
946  C  C   . GLU A 106 ? 0.0723 0.0572 0.0790 0.0040  -0.0073 0.0034  106 GLU A C   
947  O  O   . GLU A 106 ? 0.0829 0.0732 0.0802 0.0097  -0.0023 0.0046  106 GLU A O   
948  C  CB  . GLU A 106 ? 0.0829 0.0673 0.0692 0.0019  0.0013  0.0019  106 GLU A CB  
949  C  CG  . GLU A 106 ? 0.1133 0.0656 0.0733 -0.0043 0.0059  -0.0027 106 GLU A CG  
950  C  CD  . GLU A 106 ? 0.0683 0.0688 0.0656 0.0054  0.0001  0.0026  106 GLU A CD  
951  O  OE1 . GLU A 106 ? 0.0675 0.0705 0.0820 -0.0003 0.0012  0.0021  106 GLU A OE1 
952  O  OE2 . GLU A 106 ? 0.0736 0.0822 0.1026 0.0065  0.0000  -0.0043 106 GLU A OE2 
953  N  N   . HIS A 107 ? 0.0752 0.0631 0.0701 0.0001  0.0035  0.0063  107 HIS A N   
954  C  CA  . HIS A 107 ? 0.0835 0.0665 0.0701 0.0066  -0.0001 0.0020  107 HIS A CA  
955  C  C   . HIS A 107 ? 0.0794 0.0666 0.0734 0.0104  0.0008  0.0104  107 HIS A C   
956  O  O   . HIS A 107 ? 0.0895 0.0604 0.0761 0.0063  -0.0049 0.0041  107 HIS A O   
957  C  CB  . HIS A 107 ? 0.0854 0.0646 0.0671 0.0035  0.0070  0.0015  107 HIS A CB  
958  C  CG  . HIS A 107 ? 0.0689 0.0724 0.0639 0.0103  0.0005  -0.0013 107 HIS A CG  
959  N  ND1 . HIS A 107 ? 0.0790 0.0620 0.0617 0.0051  -0.0020 0.0041  107 HIS A ND1 
960  C  CD2 . HIS A 107 ? 0.0723 0.0697 0.0760 0.0135  -0.0027 -0.0044 107 HIS A CD2 
961  C  CE1 . HIS A 107 ? 0.0797 0.0718 0.0743 0.0032  -0.0070 -0.0032 107 HIS A CE1 
962  N  NE2 . HIS A 107 ? 0.0793 0.0673 0.0715 0.0071  -0.0008 -0.0032 107 HIS A NE2 
963  N  N   . THR A 108 ? 0.0946 0.0602 0.0787 0.0093  0.0052  0.0071  108 THR A N   
964  C  CA  . THR A 108 ? 0.1040 0.0610 0.0820 0.0087  0.0023  0.0152  108 THR A CA  
965  C  C   . THR A 108 ? 0.0971 0.0671 0.0813 0.0113  -0.0005 0.0076  108 THR A C   
966  O  O   . THR A 108 ? 0.1036 0.0689 0.0861 0.0081  0.0046  0.0097  108 THR A O   
967  C  CB  . THR A 108 ? 0.1102 0.0688 0.0891 0.0028  -0.0027 0.0085  108 THR A CB  
968  O  OG1 . THR A 108 ? 0.1124 0.0780 0.0914 0.0116  -0.0048 0.0110  108 THR A OG1 
969  C  CG2 . THR A 108 ? 0.1140 0.0797 0.0937 0.0155  0.0094  0.0000  108 THR A CG2 
970  N  N   . VAL A 109 ? 0.1122 0.0673 0.0928 -0.0012 0.0063  0.0148  109 VAL A N   
971  C  CA  . VAL A 109 ? 0.1064 0.0797 0.0899 0.0055  0.0057  0.0174  109 VAL A CA  
972  C  C   . VAL A 109 ? 0.1165 0.0687 0.1028 -0.0030 0.0142  0.0148  109 VAL A C   
973  O  O   . VAL A 109 ? 0.1254 0.0729 0.1054 0.0024  0.0041  0.0148  109 VAL A O   
974  C  CB  . VAL A 109 ? 0.1190 0.0873 0.1019 -0.0031 0.0034  0.0241  109 VAL A CB  
975  C  CG1 . VAL A 109 ? 0.1280 0.1028 0.1254 0.0023  0.0189  0.0245  109 VAL A CG1 
976  C  CG2 . VAL A 109 ? 0.1169 0.1000 0.1181 -0.0060 -0.0071 0.0294  109 VAL A CG2 
977  N  N   . ASP A 110 ? 0.1350 0.0795 0.0935 0.0017  0.0035  0.0265  110 ASP A N   
978  C  CA  . ASP A 110 ? 0.1638 0.0885 0.1124 0.0179  0.0116  0.0317  110 ASP A CA  
979  C  C   . ASP A 110 ? 0.1685 0.0832 0.1061 0.0270  0.0088  0.0277  110 ASP A C   
980  O  O   . ASP A 110 ? 0.2014 0.0715 0.1278 0.0219  0.0081  0.0315  110 ASP A O   
981  C  CB  . ASP A 110 ? 0.1896 0.0960 0.1305 0.0186  0.0461  0.0417  110 ASP A CB  
982  C  CG  . ASP A 110 ? 0.1894 0.1286 0.1199 0.0103  0.0403  0.0496  110 ASP A CG  
983  O  OD1 . ASP A 110 ? 0.1962 0.1218 0.1442 0.0233  0.0425  0.0362  110 ASP A OD1 
984  O  OD2 . ASP A 110 ? 0.1794 0.1785 0.1649 0.0211  0.0438  0.0294  110 ASP A OD2 
985  N  N   . LYS A 111 ? 0.1286 0.0882 0.1046 0.0208  0.0015  0.0214  111 LYS A N   
986  C  CA  . LYS A 111 ? 0.1377 0.1014 0.1058 0.0294  0.0093  0.0091  111 LYS A CA  
987  C  C   . LYS A 111 ? 0.1495 0.0679 0.1064 0.0182  0.0038  0.0146  111 LYS A C   
988  O  O   . LYS A 111 ? 0.1547 0.1260 0.1192 0.0310  0.0178  0.0099  111 LYS A O   
989  C  CB  . LYS A 111 ? 0.1902 0.1200 0.1289 0.0535  -0.0068 0.0344  111 LYS A CB  
990  C  CG  . LYS A 111 ? 0.2428 0.1731 0.1463 0.0869  -0.0370 0.0465  111 LYS A CG  
991  C  CD  . LYS A 111 ? 0.2199 0.2246 0.1974 0.0692  -0.0733 -0.0348 111 LYS A CD  
992  C  CE  . LYS A 111 ? 0.2802 0.2067 0.2213 0.0384  -0.0797 0.0174  111 LYS A CE  
993  N  NZ  . LYS A 111 ? 0.2667 0.2477 0.1962 0.0291  -0.0307 0.0346  111 LYS A NZ  
994  N  N   . LYS A 112 ? 0.1467 0.0697 0.1046 0.0143  -0.0015 0.0195  112 LYS A N   
995  C  CA  . LYS A 112 ? 0.1547 0.0683 0.1084 0.0153  0.0037  0.0063  112 LYS A CA  
996  C  C   . LYS A 112 ? 0.1274 0.0671 0.0987 0.0055  -0.0065 0.0076  112 LYS A C   
997  O  O   . LYS A 112 ? 0.1254 0.0607 0.1014 0.0120  0.0048  0.0060  112 LYS A O   
998  C  CB  . LYS A 112 ? 0.1591 0.0917 0.1235 -0.0166 -0.0040 0.0060  112 LYS A CB  
999  C  CG  . LYS A 112 ? 0.1613 0.1061 0.1436 -0.0115 -0.0062 -0.0190 112 LYS A CG  
1000 C  CD  . LYS A 112 ? 0.1685 0.1720 0.1298 -0.0240 -0.0215 0.0138  112 LYS A CD  
1001 C  CE  . LYS A 112 ? 0.1844 0.1248 0.1701 0.0013  -0.0207 -0.0049 112 LYS A CE  
1002 N  NZ  . LYS A 112 ? 0.1949 0.1221 0.1741 -0.0007 -0.0315 0.0179  112 LYS A NZ  
1003 N  N   A LYS A 113 ? 0.1039 0.0675 0.0936 0.0028  -0.0166 0.0041  113 LYS A N   
1004 N  N   B LYS A 113 ? 0.1127 0.0711 0.0962 0.0126  0.0000  0.0063  113 LYS A N   
1005 C  CA  A LYS A 113 ? 0.0956 0.0471 0.1160 0.0070  0.0093  0.0027  113 LYS A CA  
1006 C  CA  B LYS A 113 ? 0.1110 0.1007 0.0901 -0.0010 -0.0076 0.0154  113 LYS A CA  
1007 C  C   A LYS A 113 ? 0.0948 0.0601 0.1076 -0.0065 0.0170  0.0110  113 LYS A C   
1008 C  C   B LYS A 113 ? 0.1017 0.0678 0.0987 0.0085  0.0109  0.0043  113 LYS A C   
1009 O  O   A LYS A 113 ? 0.1049 0.0610 0.1356 -0.0066 0.0083  0.0172  113 LYS A O   
1010 O  O   B LYS A 113 ? 0.1074 0.0735 0.1204 0.0175  0.0164  0.0027  113 LYS A O   
1011 C  CB  A LYS A 113 ? 0.0870 0.0847 0.1014 0.0049  -0.0104 0.0062  113 LYS A CB  
1012 C  CB  B LYS A 113 ? 0.1081 0.0678 0.1372 0.0017  0.0038  -0.0129 113 LYS A CB  
1013 C  CG  A LYS A 113 ? 0.1022 0.0986 0.1084 -0.0281 0.0116  -0.0020 113 LYS A CG  
1014 C  CG  B LYS A 113 ? 0.1048 0.1483 0.1124 0.0199  -0.0035 0.0195  113 LYS A CG  
1015 C  CD  A LYS A 113 ? 0.1158 0.1401 0.1171 0.0166  0.0127  0.0094  113 LYS A CD  
1016 C  CD  B LYS A 113 ? 0.1337 0.1095 0.1772 0.0364  -0.0003 -0.0111 113 LYS A CD  
1017 C  CE  A LYS A 113 ? 0.1377 0.1615 0.1474 0.0107  0.0077  0.0074  113 LYS A CE  
1018 C  CE  B LYS A 113 ? 0.1004 0.1439 0.1480 0.0419  0.0299  -0.0155 113 LYS A CE  
1019 N  NZ  A LYS A 113 ? 0.1589 0.1812 0.2746 0.0344  0.0588  0.0083  113 LYS A NZ  
1020 N  NZ  B LYS A 113 ? 0.1108 0.1571 0.1356 0.0320  0.0087  -0.0201 113 LYS A NZ  
1021 N  N   . TYR A 114 ? 0.0995 0.0636 0.1039 0.0063  0.0038  0.0024  114 TYR A N   
1022 C  CA  . TYR A 114 ? 0.1120 0.0638 0.0983 -0.0046 0.0001  0.0062  114 TYR A CA  
1023 C  C   . TYR A 114 ? 0.0996 0.0505 0.1069 -0.0013 0.0001  -0.0059 114 TYR A C   
1024 O  O   . TYR A 114 ? 0.0975 0.0717 0.1043 0.0065  0.0068  -0.0097 114 TYR A O   
1025 C  CB  . TYR A 114 ? 0.0918 0.0648 0.0978 0.0046  0.0035  0.0104  114 TYR A CB  
1026 C  CG  . TYR A 114 ? 0.1102 0.0554 0.0981 0.0081  -0.0038 0.0027  114 TYR A CG  
1027 C  CD1 . TYR A 114 ? 0.1421 0.0864 0.1124 0.0114  -0.0068 0.0046  114 TYR A CD1 
1028 C  CD2 . TYR A 114 ? 0.1108 0.0703 0.1215 -0.0008 0.0127  0.0068  114 TYR A CD2 
1029 C  CE1 . TYR A 114 ? 0.1924 0.1072 0.0981 0.0441  0.0194  0.0085  114 TYR A CE1 
1030 C  CE2 . TYR A 114 ? 0.1335 0.0982 0.1577 -0.0082 0.0342  -0.0010 114 TYR A CE2 
1031 C  CZ  . TYR A 114 ? 0.1518 0.1298 0.1451 0.0087  0.0573  0.0296  114 TYR A CZ  
1032 O  OH  . TYR A 114 ? 0.2632 0.1767 0.1784 0.0188  0.1114  0.0125  114 TYR A OH  
1033 N  N   . ALA A 115 ? 0.1067 0.0608 0.1046 -0.0089 -0.0015 -0.0027 115 ALA A N   
1034 C  CA  . ALA A 115 ? 0.1063 0.0620 0.0979 -0.0089 0.0012  -0.0083 115 ALA A CA  
1035 C  C   . ALA A 115 ? 0.0988 0.0643 0.0932 -0.0001 -0.0020 -0.0100 115 ALA A C   
1036 O  O   . ALA A 115 ? 0.1058 0.0614 0.1015 0.0000  0.0105  -0.0097 115 ALA A O   
1037 C  CB  . ALA A 115 ? 0.1160 0.0908 0.1120 -0.0098 -0.0076 -0.0131 115 ALA A CB  
1038 N  N   . ALA A 116 ? 0.1032 0.0564 0.0961 0.0000  0.0111  -0.0021 116 ALA A N   
1039 C  CA  . ALA A 116 ? 0.0957 0.0572 0.0766 0.0001  0.0085  -0.0034 116 ALA A CA  
1040 C  C   . ALA A 116 ? 0.0828 0.0575 0.0711 0.0023  -0.0059 -0.0012 116 ALA A C   
1041 O  O   . ALA A 116 ? 0.0926 0.0636 0.0806 -0.0023 0.0116  0.0010  116 ALA A O   
1042 C  CB  . ALA A 116 ? 0.1064 0.0699 0.0843 -0.0076 0.0049  -0.0046 116 ALA A CB  
1043 N  N   . GLU A 117 ? 0.0920 0.0531 0.0707 0.0034  0.0020  -0.0034 117 GLU A N   
1044 C  CA  . GLU A 117 ? 0.0807 0.0554 0.0732 0.0037  -0.0012 -0.0010 117 GLU A CA  
1045 C  C   . GLU A 117 ? 0.0794 0.0634 0.0604 -0.0020 0.0043  0.0008  117 GLU A C   
1046 O  O   . GLU A 117 ? 0.0846 0.0687 0.0803 0.0132  0.0066  0.0132  117 GLU A O   
1047 C  CB  . GLU A 117 ? 0.0873 0.0680 0.0649 0.0060  -0.0102 0.0024  117 GLU A CB  
1048 C  CG  . GLU A 117 ? 0.0838 0.0649 0.0665 -0.0001 -0.0085 -0.0030 117 GLU A CG  
1049 C  CD  . GLU A 117 ? 0.0759 0.0585 0.0661 0.0020  0.0021  0.0062  117 GLU A CD  
1050 O  OE1 . GLU A 117 ? 0.0840 0.0734 0.0741 0.0076  -0.0044 0.0037  117 GLU A OE1 
1051 O  OE2 . GLU A 117 ? 0.0984 0.0634 0.0722 0.0000  -0.0120 0.0062  117 GLU A OE2 
1052 N  N   . LEU A 118 ? 0.0770 0.0616 0.0696 0.0010  -0.0046 0.0010  118 LEU A N   
1053 C  CA  . LEU A 118 ? 0.0760 0.0529 0.0579 -0.0008 -0.0035 0.0046  118 LEU A CA  
1054 C  C   . LEU A 118 ? 0.0700 0.0566 0.0608 0.0003  0.0006  0.0098  118 LEU A C   
1055 O  O   . LEU A 118 ? 0.0794 0.0582 0.0637 -0.0041 -0.0028 0.0026  118 LEU A O   
1056 C  CB  . LEU A 118 ? 0.0769 0.0731 0.0719 0.0019  -0.0038 0.0049  118 LEU A CB  
1057 C  CG  . LEU A 118 ? 0.0856 0.0768 0.0806 0.0068  -0.0119 0.0068  118 LEU A CG  
1058 C  CD1 . LEU A 118 ? 0.1015 0.0708 0.0805 -0.0006 -0.0171 0.0164  118 LEU A CD1 
1059 C  CD2 . LEU A 118 ? 0.0828 0.0919 0.1034 0.0052  -0.0126 0.0082  118 LEU A CD2 
1060 N  N   . HIS A 119 ? 0.0725 0.0549 0.0627 0.0017  -0.0035 0.0000  119 HIS A N   
1061 C  CA  . HIS A 119 ? 0.0718 0.0582 0.0653 0.0001  -0.0097 0.0032  119 HIS A CA  
1062 C  C   . HIS A 119 ? 0.0682 0.0554 0.0662 -0.0049 -0.0074 0.0055  119 HIS A C   
1063 O  O   . HIS A 119 ? 0.0905 0.0647 0.0693 0.0109  -0.0026 0.0126  119 HIS A O   
1064 C  CB  . HIS A 119 ? 0.0768 0.0560 0.0727 -0.0008 -0.0105 0.0035  119 HIS A CB  
1065 C  CG  . HIS A 119 ? 0.0688 0.0619 0.0626 0.0005  -0.0041 0.0001  119 HIS A CG  
1066 N  ND1 . HIS A 119 ? 0.0698 0.0564 0.0681 0.0000  -0.0105 -0.0023 119 HIS A ND1 
1067 C  CD2 . HIS A 119 ? 0.0787 0.0615 0.0691 0.0076  -0.0147 0.0027  119 HIS A CD2 
1068 C  CE1 . HIS A 119 ? 0.0659 0.0597 0.0688 -0.0052 0.0000  -0.0020 119 HIS A CE1 
1069 N  NE2 . HIS A 119 ? 0.0709 0.0705 0.0726 0.0026  -0.0041 0.0049  119 HIS A NE2 
1070 N  N   . LEU A 120 ? 0.0719 0.0548 0.0659 0.0048  -0.0035 0.0051  120 LEU A N   
1071 C  CA  . LEU A 120 ? 0.0710 0.0599 0.0790 0.0010  -0.0068 0.0035  120 LEU A CA  
1072 C  C   . LEU A 120 ? 0.0673 0.0576 0.0693 0.0124  -0.0049 0.0111  120 LEU A C   
1073 O  O   . LEU A 120 ? 0.0702 0.0568 0.0763 0.0059  -0.0032 0.0046  120 LEU A O   
1074 C  CB  . LEU A 120 ? 0.0723 0.0711 0.0755 0.0040  -0.0082 -0.0024 120 LEU A CB  
1075 C  CG  . LEU A 120 ? 0.0838 0.0777 0.0804 -0.0049 -0.0078 -0.0020 120 LEU A CG  
1076 C  CD1 . LEU A 120 ? 0.1723 0.0934 0.1045 -0.0412 -0.0060 -0.0023 120 LEU A CD1 
1077 C  CD2 . LEU A 120 ? 0.0918 0.1201 0.0960 0.0121  -0.0186 -0.0098 120 LEU A CD2 
1078 N  N   . ALA A 121 ? 0.0826 0.0589 0.0725 0.0001  -0.0049 0.0054  121 ALA A N   
1079 C  CA  . ALA A 121 ? 0.0834 0.0553 0.0764 -0.0031 -0.0003 0.0028  121 ALA A CA  
1080 C  C   . ALA A 121 ? 0.0778 0.0566 0.0804 0.0017  -0.0043 0.0073  121 ALA A C   
1081 O  O   . ALA A 121 ? 0.0904 0.0648 0.0848 0.0071  -0.0094 0.0077  121 ALA A O   
1082 C  CB  . ALA A 121 ? 0.0847 0.0687 0.1006 0.0026  0.0012  -0.0017 121 ALA A CB  
1083 N  N   . HIS A 122 ? 0.0842 0.0607 0.0761 0.0015  -0.0026 0.0060  122 HIS A N   
1084 C  CA  . HIS A 122 ? 0.0881 0.0532 0.0848 0.0000  -0.0049 0.0041  122 HIS A CA  
1085 C  C   . HIS A 122 ? 0.0923 0.0584 0.0794 0.0027  0.0013  0.0020  122 HIS A C   
1086 O  O   . HIS A 122 ? 0.1133 0.0659 0.0948 -0.0131 -0.0108 0.0040  122 HIS A O   
1087 C  CB  . HIS A 122 ? 0.0916 0.0595 0.0945 0.0108  0.0055  -0.0010 122 HIS A CB  
1088 C  CG  . HIS A 122 ? 0.0847 0.0639 0.0881 0.0076  0.0017  0.0120  122 HIS A CG  
1089 N  ND1 . HIS A 122 ? 0.0837 0.0662 0.0991 -0.0007 0.0013  0.0027  122 HIS A ND1 
1090 C  CD2 . HIS A 122 ? 0.0817 0.0819 0.0998 -0.0005 0.0037  0.0017  122 HIS A CD2 
1091 C  CE1 . HIS A 122 ? 0.0743 0.0759 0.0962 0.0100  0.0017  0.0027  122 HIS A CE1 
1092 N  NE2 . HIS A 122 ? 0.0803 0.0823 0.1032 0.0000  -0.0051 0.0057  122 HIS A NE2 
1093 N  N   . TRP A 123 ? 0.0951 0.0580 0.0932 0.0021  0.0006  -0.0052 123 TRP A N   
1094 C  CA  . TRP A 123 ? 0.0976 0.0566 0.1077 -0.0037 0.0026  -0.0098 123 TRP A CA  
1095 C  C   . TRP A 123 ? 0.0944 0.0586 0.1026 -0.0063 0.0005  0.0007  123 TRP A C   
1096 O  O   . TRP A 123 ? 0.0911 0.0640 0.1097 0.0013  -0.0017 -0.0063 123 TRP A O   
1097 C  CB  . TRP A 123 ? 0.1034 0.0918 0.1124 -0.0181 0.0133  -0.0142 123 TRP A CB  
1098 C  CG  . TRP A 123 ? 0.1333 0.0701 0.1037 -0.0208 0.0225  -0.0035 123 TRP A CG  
1099 C  CD1 . TRP A 123 ? 0.1445 0.0751 0.1165 -0.0121 0.0182  -0.0043 123 TRP A CD1 
1100 C  CD2 . TRP A 123 ? 0.1404 0.0628 0.1234 -0.0241 0.0237  -0.0052 123 TRP A CD2 
1101 N  NE1 . TRP A 123 ? 0.1876 0.0625 0.1234 -0.0232 0.0141  0.0017  123 TRP A NE1 
1102 C  CE2 . TRP A 123 ? 0.1801 0.0708 0.1187 -0.0153 0.0178  0.0087  123 TRP A CE2 
1103 C  CE3 . TRP A 123 ? 0.2215 0.0540 0.1395 -0.0355 0.0419  -0.0063 123 TRP A CE3 
1104 C  CZ2 . TRP A 123 ? 0.2284 0.0729 0.1290 -0.0040 0.0227  0.0218  123 TRP A CZ2 
1105 C  CZ3 . TRP A 123 ? 0.2615 0.0737 0.1466 -0.0144 0.0515  -0.0055 123 TRP A CZ3 
1106 C  CH2 . TRP A 123 ? 0.2931 0.0627 0.1511 0.0046  0.0478  0.0154  123 TRP A CH2 
1107 N  N   . ASN A 124 ? 0.1014 0.0601 0.0991 0.0013  0.0017  -0.0020 124 ASN A N   
1108 C  CA  . ASN A 124 ? 0.1208 0.0602 0.1043 0.0126  0.0097  -0.0098 124 ASN A CA  
1109 C  C   . ASN A 124 ? 0.1220 0.0621 0.1008 0.0001  0.0113  -0.0102 124 ASN A C   
1110 O  O   . ASN A 124 ? 0.1331 0.0612 0.1079 0.0003  0.0093  -0.0049 124 ASN A O   
1111 C  CB  . ASN A 124 ? 0.1274 0.0701 0.0969 -0.0005 0.0070  -0.0044 124 ASN A CB  
1112 C  CG  . ASN A 124 ? 0.1568 0.0580 0.1043 0.0030  0.0238  0.0001  124 ASN A CG  
1113 O  OD1 . ASN A 124 ? 0.1606 0.0724 0.1217 0.0115  0.0182  -0.0065 124 ASN A OD1 
1114 N  ND2 . ASN A 124 ? 0.1779 0.0691 0.1152 0.0065  0.0218  -0.0096 124 ASN A ND2 
1115 N  N   . THR A 125 ? 0.1243 0.0619 0.1209 0.0174  0.0024  -0.0104 125 THR A N   
1116 C  CA  . THR A 125 ? 0.1576 0.0627 0.1391 0.0149  -0.0032 0.0060  125 THR A CA  
1117 C  C   . THR A 125 ? 0.1348 0.0585 0.1420 0.0138  0.0000  0.0040  125 THR A C   
1118 O  O   . THR A 125 ? 0.1729 0.0672 0.1458 0.0089  -0.0071 0.0136  125 THR A O   
1119 C  CB  . THR A 125 ? 0.1673 0.0895 0.2006 0.0315  -0.0491 0.0001  125 THR A CB  
1120 O  OG1 . THR A 125 ? 0.1873 0.1234 0.2714 0.0597  0.0154  0.0024  125 THR A OG1 
1121 C  CG2 . THR A 125 ? 0.1957 0.0887 0.2125 -0.0020 -0.0696 0.0000  125 THR A CG2 
1122 N  N   A LYS A 126 ? 0.1134 0.0541 0.0936 -0.0027 -0.0297 -0.0086 127 LYS A N   
1123 N  N   B LYS A 126 ? 0.1108 0.0662 0.0991 0.0211  -0.0127 -0.0074 127 LYS A N   
1124 C  CA  A LYS A 126 ? 0.1103 0.0731 0.0883 0.0096  -0.0263 -0.0196 127 LYS A CA  
1125 C  CA  B LYS A 126 ? 0.1381 0.0531 0.1174 -0.0008 -0.0071 -0.0051 127 LYS A CA  
1126 C  C   A LYS A 126 ? 0.1295 0.0611 0.0956 0.0081  -0.0209 -0.0049 127 LYS A C   
1127 C  C   B LYS A 126 ? 0.1367 0.0675 0.1162 -0.0030 0.0027  -0.0086 127 LYS A C   
1128 O  O   A LYS A 126 ? 0.1172 0.0664 0.1488 -0.0003 -0.0274 -0.0241 127 LYS A O   
1129 O  O   B LYS A 126 ? 0.1215 0.0601 0.1325 0.0065  -0.0103 -0.0098 127 LYS A O   
1130 C  CB  A LYS A 126 ? 0.1323 0.0820 0.1123 0.0120  -0.0262 -0.0397 127 LYS A CB  
1131 C  CB  B LYS A 126 ? 0.1058 0.0991 0.1162 -0.0093 -0.0008 0.0051  127 LYS A CB  
1132 C  CG  A LYS A 126 ? 0.1136 0.1026 0.1184 0.0274  -0.0265 -0.0228 127 LYS A CG  
1133 C  CG  B LYS A 126 ? 0.1423 0.0785 0.1301 0.0032  0.0124  0.0208  127 LYS A CG  
1134 C  CD  A LYS A 126 ? 0.1632 0.2414 0.1046 0.0419  -0.0447 -0.0302 127 LYS A CD  
1135 C  CD  B LYS A 126 ? 0.1509 0.1067 0.1343 0.0164  0.0005  0.0167  127 LYS A CD  
1136 C  CE  A LYS A 126 ? 0.1502 0.2646 0.1477 0.0335  -0.0109 0.0390  127 LYS A CE  
1137 C  CE  B LYS A 126 ? 0.2967 0.1052 0.1128 0.0482  0.0230  0.0003  127 LYS A CE  
1138 N  NZ  A LYS A 126 ? 0.2151 0.2876 0.1650 0.0881  -0.0152 0.0608  127 LYS A NZ  
1139 N  NZ  B LYS A 126 ? 0.2939 0.2081 0.1017 0.0762  0.0449  0.0010  127 LYS A NZ  
1140 N  N   . TYR A 127 ? 0.1435 0.0678 0.1111 -0.0060 0.0087  -0.0054 128 TYR A N   
1141 C  CA  . TYR A 127 ? 0.1504 0.0683 0.1174 -0.0013 0.0091  -0.0140 128 TYR A CA  
1142 C  C   . TYR A 127 ? 0.1641 0.0612 0.1154 -0.0102 0.0263  -0.0100 128 TYR A C   
1143 O  O   . TYR A 127 ? 0.1676 0.0856 0.1274 -0.0102 0.0165  -0.0083 128 TYR A O   
1144 C  CB  . TYR A 127 ? 0.1386 0.0835 0.1180 -0.0137 0.0070  -0.0105 128 TYR A CB  
1145 C  CG  . TYR A 127 ? 0.1246 0.0812 0.1111 0.0044  -0.0077 -0.0111 128 TYR A CG  
1146 C  CD1 . TYR A 127 ? 0.1545 0.0788 0.1307 -0.0019 -0.0007 -0.0162 128 TYR A CD1 
1147 C  CD2 . TYR A 127 ? 0.1274 0.0965 0.0980 -0.0111 0.0040  -0.0115 128 TYR A CD2 
1148 C  CE1 . TYR A 127 ? 0.1711 0.0857 0.1119 -0.0024 -0.0120 -0.0099 128 TYR A CE1 
1149 C  CE2 . TYR A 127 ? 0.1339 0.1046 0.1048 -0.0060 0.0044  -0.0247 128 TYR A CE2 
1150 C  CZ  . TYR A 127 ? 0.1676 0.1138 0.0882 0.0051  0.0046  -0.0093 128 TYR A CZ  
1151 O  OH  . TYR A 127 ? 0.2149 0.1041 0.1130 0.0019  -0.0031 -0.0159 128 TYR A OH  
1152 N  N   . GLY A 128 ? 0.1551 0.0741 0.1124 -0.0046 -0.0110 0.0020  129 GLY A N   
1153 C  CA  . GLY A 128 ? 0.1879 0.0682 0.1143 0.0049  -0.0001 0.0063  129 GLY A CA  
1154 C  C   . GLY A 128 ? 0.2021 0.0759 0.1052 0.0094  0.0005  0.0194  129 GLY A C   
1155 O  O   . GLY A 128 ? 0.2680 0.0831 0.1155 0.0250  0.0040  0.0136  129 GLY A O   
1156 N  N   A ASP A 129 ? 0.1852 0.0577 0.1165 -0.0156 0.0305  -0.0006 130 ASP A N   
1157 N  N   B ASP A 129 ? 0.1542 0.0403 0.1007 -0.0156 -0.0006 0.0131  130 ASP A N   
1158 C  CA  A ASP A 129 ? 0.1615 0.0734 0.1120 -0.0105 0.0098  -0.0037 130 ASP A CA  
1159 C  CA  B ASP A 129 ? 0.1528 0.0421 0.1066 -0.0147 0.0204  0.0054  130 ASP A CA  
1160 C  C   A ASP A 129 ? 0.2493 0.0953 0.0961 0.0270  0.0307  0.0082  130 ASP A C   
1161 C  C   B ASP A 129 ? 0.2396 0.0741 0.0975 0.0322  0.0105  0.0200  130 ASP A C   
1162 O  O   A ASP A 129 ? 0.1066 0.0760 0.1039 -0.0007 0.0185  0.0062  130 ASP A O   
1163 O  O   B ASP A 129 ? 0.1155 0.0581 0.1203 0.0012  0.0166  -0.0006 130 ASP A O   
1164 C  CB  A ASP A 129 ? 0.1332 0.0910 0.1055 -0.0078 -0.0051 0.0098  130 ASP A CB  
1165 C  CB  B ASP A 129 ? 0.1401 0.1054 0.0996 0.0000  0.0044  0.0228  130 ASP A CB  
1166 C  CG  A ASP A 129 ? 0.1342 0.0745 0.1235 0.0085  0.0119  0.0140  130 ASP A CG  
1167 C  CG  B ASP A 129 ? 0.1292 0.0638 0.1242 0.0068  0.0218  0.0034  130 ASP A CG  
1168 O  OD1 A ASP A 129 ? 0.1757 0.1031 0.1309 0.0031  -0.0226 0.0251  130 ASP A OD1 
1169 O  OD1 B ASP A 129 ? 0.1430 0.0963 0.1648 -0.0073 0.0229  0.0070  130 ASP A OD1 
1170 O  OD2 A ASP A 129 ? 0.1799 0.0969 0.2116 -0.0071 -0.0038 0.0505  130 ASP A OD2 
1171 O  OD2 B ASP A 129 ? 0.2016 0.0879 0.1592 0.0087  0.0714  0.0209  130 ASP A OD2 
1172 N  N   . LEU A 130 ? 0.1978 0.0743 0.1035 0.0115  0.0220  0.0083  131 LEU A N   
1173 C  CA  . LEU A 130 ? 0.1587 0.0632 0.1247 -0.0063 0.0221  0.0100  131 LEU A CA  
1174 C  C   . LEU A 130 ? 0.1592 0.0653 0.1088 -0.0120 0.0216  -0.0063 131 LEU A C   
1175 O  O   . LEU A 130 ? 0.1595 0.0957 0.1099 -0.0241 0.0137  -0.0115 131 LEU A O   
1176 C  CB  . LEU A 130 ? 0.1406 0.0749 0.1158 -0.0028 0.0070  -0.0074 131 LEU A CB  
1177 C  CG  . LEU A 130 ? 0.1318 0.0696 0.1181 -0.0038 0.0126  -0.0052 131 LEU A CG  
1178 C  CD1 . LEU A 130 ? 0.1425 0.0653 0.1518 -0.0043 -0.0015 0.0176  131 LEU A CD1 
1179 C  CD2 . LEU A 130 ? 0.1774 0.0841 0.1353 0.0000  -0.0019 0.0008  131 LEU A CD2 
1180 N  N   . GLY A 131 ? 0.1678 0.1169 0.1154 -0.0353 0.0303  -0.0104 132 GLY A N   
1181 C  CA  . GLY A 131 ? 0.1882 0.1435 0.1387 -0.0527 0.0527  -0.0167 132 GLY A CA  
1182 C  C   . GLY A 131 ? 0.1407 0.1340 0.1421 -0.0478 0.0216  -0.0168 132 GLY A C   
1183 O  O   . GLY A 131 ? 0.1440 0.1621 0.1666 -0.0275 0.0286  -0.0447 132 GLY A O   
1184 N  N   A LYS A 132 ? 0.1613 0.1172 0.1280 -0.0487 0.0359  -0.0315 133 LYS A N   
1185 N  N   B LYS A 132 ? 0.1897 0.0976 0.1178 -0.0412 0.0421  0.0020  133 LYS A N   
1186 C  CA  A LYS A 132 ? 0.1403 0.1036 0.1204 -0.0390 0.0163  -0.0027 133 LYS A CA  
1187 C  CA  B LYS A 132 ? 0.2064 0.0824 0.1386 -0.0197 0.0406  0.0024  133 LYS A CA  
1188 C  C   A LYS A 132 ? 0.1398 0.0954 0.1092 -0.0211 0.0205  -0.0070 133 LYS A C   
1189 C  C   B LYS A 132 ? 0.1518 0.0974 0.1175 -0.0320 0.0071  -0.0096 133 LYS A C   
1190 O  O   A LYS A 132 ? 0.1191 0.0916 0.1184 -0.0318 0.0162  -0.0263 133 LYS A O   
1191 O  O   B LYS A 132 ? 0.1186 0.1030 0.1286 -0.0122 0.0057  -0.0245 133 LYS A O   
1192 C  CB  A LYS A 132 ? 0.1527 0.0768 0.1732 -0.0267 -0.0178 0.0048  133 LYS A CB  
1193 C  CB  B LYS A 132 ? 0.1436 0.1039 0.1580 -0.0093 0.0040  -0.0077 133 LYS A CB  
1194 C  CG  A LYS A 132 ? 0.1106 0.0700 0.2247 0.0055  -0.0049 0.0222  133 LYS A CG  
1195 C  CG  B LYS A 132 ? 0.2319 0.1132 0.1684 -0.0335 0.0215  -0.0337 133 LYS A CG  
1196 C  CD  A LYS A 132 ? 0.2044 0.1086 0.2258 -0.0225 -0.0452 0.0658  133 LYS A CD  
1197 C  CD  B LYS A 132 ? 0.2407 0.2291 0.3104 -0.0417 -0.0326 -0.1432 133 LYS A CD  
1198 C  CE  A LYS A 132 ? 0.2002 0.1371 0.2721 -0.0533 0.0107  0.0116  133 LYS A CE  
1199 C  CE  B LYS A 132 ? 0.2498 0.3393 0.2237 0.0417  -0.0215 -0.0035 133 LYS A CE  
1200 N  NZ  A LYS A 132 ? 0.2187 0.2328 0.2834 -0.0807 -0.0015 0.0441  133 LYS A NZ  
1201 N  NZ  B LYS A 132 ? 0.3456 0.1650 0.2198 -0.0641 -0.0178 -0.0430 133 LYS A NZ  
1202 N  N   . ALA A 133 ? 0.1391 0.0830 0.1020 -0.0284 0.0131  -0.0122 134 ALA A N   
1203 C  CA  . ALA A 133 ? 0.1221 0.0976 0.0979 -0.0245 0.0037  0.0008  134 ALA A CA  
1204 C  C   . ALA A 133 ? 0.1225 0.0890 0.0911 -0.0299 0.0054  -0.0085 134 ALA A C   
1205 O  O   . ALA A 133 ? 0.1081 0.1137 0.1006 -0.0204 0.0044  -0.0111 134 ALA A O   
1206 C  CB  . ALA A 133 ? 0.1281 0.0857 0.0970 -0.0337 0.0012  0.0048  134 ALA A CB  
1207 N  N   . ALA A 134 ? 0.1193 0.0914 0.1124 -0.0243 0.0162  -0.0161 135 ALA A N   
1208 C  CA  . ALA A 134 ? 0.1173 0.1059 0.1278 -0.0141 0.0093  -0.0124 135 ALA A CA  
1209 C  C   . ALA A 134 ? 0.1146 0.1092 0.1157 -0.0184 0.0203  -0.0057 135 ALA A C   
1210 O  O   . ALA A 134 ? 0.1208 0.1254 0.1259 -0.0199 0.0098  -0.0151 135 ALA A O   
1211 C  CB  . ALA A 134 ? 0.1583 0.1678 0.1171 0.0143  0.0100  -0.0401 135 ALA A CB  
1212 N  N   . GLN A 135 ? 0.1289 0.1139 0.1215 -0.0373 0.0122  -0.0171 136 GLN A N   
1213 C  CA  . GLN A 135 ? 0.1260 0.1306 0.1327 -0.0434 0.0024  -0.0309 136 GLN A CA  
1214 C  C   . GLN A 135 ? 0.1151 0.1099 0.1343 -0.0208 -0.0097 -0.0183 136 GLN A C   
1215 O  O   . GLN A 135 ? 0.1356 0.1732 0.1308 -0.0397 -0.0038 -0.0271 136 GLN A O   
1216 C  CB  . GLN A 135 ? 0.1583 0.1745 0.1442 -0.0790 0.0136  -0.0270 136 GLN A CB  
1217 C  CG  . GLN A 135 ? 0.2203 0.1929 0.1586 -0.1124 0.0346  -0.0125 136 GLN A CG  
1218 C  CD  . GLN A 135 ? 0.1984 0.5658 0.3968 -0.0057 0.0315  -0.1701 136 GLN A CD  
1219 O  OE1 . GLN A 135 ? 0.2471 0.8116 0.4559 -0.0040 -0.0035 -0.1713 136 GLN A OE1 
1220 N  NE2 . GLN A 135 ? 0.2973 0.6887 0.4997 0.1289  -0.0582 -0.2867 136 GLN A NE2 
1221 N  N   . GLN A 136 ? 0.1163 0.1011 0.1131 -0.0162 -0.0037 -0.0181 137 GLN A N   
1222 C  CA  . GLN A 136 ? 0.1350 0.1162 0.0938 -0.0171 -0.0052 -0.0214 137 GLN A CA  
1223 C  C   . GLN A 136 ? 0.1199 0.0952 0.1000 -0.0057 0.0065  -0.0234 137 GLN A C   
1224 O  O   . GLN A 136 ? 0.1278 0.0996 0.0867 -0.0012 -0.0054 -0.0175 137 GLN A O   
1225 C  CB  . GLN A 136 ? 0.1368 0.0942 0.1115 -0.0032 0.0038  -0.0046 137 GLN A CB  
1226 C  CG  . GLN A 136 ? 0.1493 0.1178 0.1225 -0.0100 -0.0041 -0.0108 137 GLN A CG  
1227 C  CD  . GLN A 136 ? 0.1983 0.1310 0.1421 -0.0267 -0.0078 -0.0242 137 GLN A CD  
1228 O  OE1 . GLN A 136 ? 0.2027 0.1366 0.1448 -0.0201 0.0031  -0.0306 137 GLN A OE1 
1229 N  NE2 . GLN A 136 ? 0.2129 0.1486 0.1510 -0.0518 0.0105  -0.0142 137 GLN A NE2 
1230 N  N   A PRO A 137 ? 0.1075 0.0969 0.0934 0.0024  -0.0096 -0.0193 138 PRO A N   
1231 N  N   B PRO A 137 ? 0.1128 0.1290 0.0935 -0.0099 -0.0076 -0.0375 138 PRO A N   
1232 C  CA  A PRO A 137 ? 0.1486 0.0940 0.0882 0.0054  -0.0052 -0.0019 138 PRO A CA  
1233 C  CA  B PRO A 137 ? 0.1386 0.1264 0.0763 0.0266  -0.0086 0.0021  138 PRO A CA  
1234 C  C   A PRO A 137 ? 0.1324 0.1199 0.0917 0.0023  -0.0107 -0.0176 138 PRO A C   
1235 C  C   B PRO A 137 ? 0.1264 0.1093 0.0760 0.0068  -0.0035 0.0001  138 PRO A C   
1236 O  O   A PRO A 137 ? 0.1587 0.1220 0.1137 0.0097  -0.0109 0.0030  138 PRO A O   
1237 O  O   B PRO A 137 ? 0.1348 0.0916 0.1368 0.0063  0.0209  0.0131  138 PRO A O   
1238 C  CB  A PRO A 137 ? 0.1453 0.1385 0.0940 0.0048  0.0034  -0.0250 138 PRO A CB  
1239 C  CB  B PRO A 137 ? 0.1678 0.1266 0.0777 0.0037  -0.0263 -0.0035 138 PRO A CB  
1240 C  CG  A PRO A 137 ? 0.1697 0.1621 0.0939 0.0085  -0.0244 -0.0397 138 PRO A CG  
1241 C  CG  B PRO A 137 ? 0.1366 0.1660 0.0854 -0.0012 -0.0198 -0.0299 138 PRO A CG  
1242 C  CD  A PRO A 137 ? 0.1123 0.1444 0.0957 -0.0040 -0.0046 -0.0337 138 PRO A CD  
1243 C  CD  B PRO A 137 ? 0.1264 0.1431 0.0833 -0.0174 -0.0034 -0.0273 138 PRO A CD  
1244 N  N   . ASP A 138 ? 0.1255 0.1005 0.0900 0.0027  -0.0019 -0.0076 139 ASP A N   
1245 C  CA  . ASP A 138 ? 0.1184 0.1063 0.0891 0.0000  0.0054  -0.0060 139 ASP A CA  
1246 C  C   . ASP A 138 ? 0.1190 0.0861 0.0750 -0.0073 0.0043  -0.0109 139 ASP A C   
1247 O  O   . ASP A 138 ? 0.1183 0.0863 0.1014 0.0024  0.0078  -0.0027 139 ASP A O   
1248 C  CB  . ASP A 138 ? 0.1404 0.1172 0.0896 -0.0094 0.0094  -0.0003 139 ASP A CB  
1249 C  CG  . ASP A 138 ? 0.1372 0.1236 0.0943 0.0093  0.0027  -0.0129 139 ASP A CG  
1250 O  OD1 . ASP A 138 ? 0.1530 0.1035 0.1171 0.0110  0.0086  -0.0247 139 ASP A OD1 
1251 O  OD2 . ASP A 138 ? 0.1735 0.1395 0.1111 0.0178  0.0251  -0.0280 139 ASP A OD2 
1252 N  N   . GLY A 139 ? 0.1134 0.0691 0.0810 -0.0070 -0.0006 -0.0085 140 GLY A N   
1253 C  CA  . GLY A 139 ? 0.1157 0.0796 0.0883 -0.0100 -0.0087 -0.0076 140 GLY A CA  
1254 C  C   . GLY A 139 ? 0.0945 0.0667 0.0787 -0.0074 0.0071  -0.0055 140 GLY A C   
1255 O  O   . GLY A 139 ? 0.1085 0.0710 0.0847 0.0019  -0.0017 0.0021  140 GLY A O   
1256 N  N   . LEU A 140 ? 0.0838 0.0598 0.0883 -0.0019 0.0076  -0.0065 141 LEU A N   
1257 C  CA  . LEU A 140 ? 0.0876 0.0617 0.0839 -0.0073 -0.0041 -0.0013 141 LEU A CA  
1258 C  C   . LEU A 140 ? 0.0812 0.0619 0.0690 0.0012  0.0010  0.0030  141 LEU A C   
1259 O  O   . LEU A 140 ? 0.0854 0.0636 0.0843 -0.0031 -0.0012 0.0001  141 LEU A O   
1260 C  CB  . LEU A 140 ? 0.1067 0.0781 0.0841 -0.0164 0.0183  -0.0127 141 LEU A CB  
1261 C  CG  . LEU A 140 ? 0.1402 0.1204 0.0930 -0.0306 0.0269  -0.0115 141 LEU A CG  
1262 C  CD1 . LEU A 140 ? 0.1868 0.1394 0.1130 -0.0183 0.0021  -0.0077 141 LEU A CD1 
1263 C  CD2 . LEU A 140 ? 0.1222 0.1066 0.1162 -0.0137 0.0111  -0.0065 141 LEU A CD2 
1264 N  N   . ALA A 141 ? 0.0776 0.0582 0.0821 -0.0027 0.0013  0.0005  142 ALA A N   
1265 C  CA  . ALA A 141 ? 0.0873 0.0555 0.0881 0.0015  0.0010  -0.0006 142 ALA A CA  
1266 C  C   . ALA A 141 ? 0.0688 0.0594 0.0803 -0.0054 -0.0003 0.0076  142 ALA A C   
1267 O  O   . ALA A 141 ? 0.0898 0.0606 0.0823 -0.0003 -0.0059 0.0062  142 ALA A O   
1268 C  CB  . ALA A 141 ? 0.0885 0.0770 0.1130 -0.0034 0.0174  0.0000  142 ALA A CB  
1269 N  N   . VAL A 142 ? 0.0741 0.0550 0.0794 -0.0024 -0.0038 -0.0003 143 VAL A N   
1270 C  CA  . VAL A 142 ? 0.0726 0.0595 0.0726 0.0017  -0.0049 0.0017  143 VAL A CA  
1271 C  C   . VAL A 142 ? 0.0777 0.0629 0.0680 0.0087  -0.0063 0.0027  143 VAL A C   
1272 O  O   . VAL A 142 ? 0.0830 0.0640 0.0749 -0.0052 -0.0083 0.0049  143 VAL A O   
1273 C  CB  . VAL A 142 ? 0.0753 0.0780 0.0759 0.0012  -0.0071 0.0063  143 VAL A CB  
1274 C  CG1 . VAL A 142 ? 0.0866 0.0849 0.0740 0.0140  -0.0038 -0.0057 143 VAL A CG1 
1275 C  CG2 . VAL A 142 ? 0.0846 0.0908 0.0923 -0.0026 0.0000  0.0043  143 VAL A CG2 
1276 N  N   . LEU A 143 ? 0.0731 0.0562 0.0767 0.0003  -0.0035 0.0006  144 LEU A N   
1277 C  CA  . LEU A 143 ? 0.0680 0.0617 0.0881 -0.0035 -0.0074 0.0005  144 LEU A CA  
1278 C  C   . LEU A 143 ? 0.0785 0.0655 0.0672 -0.0046 -0.0038 0.0063  144 LEU A C   
1279 O  O   . LEU A 143 ? 0.1002 0.0723 0.0700 -0.0049 0.0015  0.0051  144 LEU A O   
1280 C  CB  . LEU A 143 ? 0.0822 0.0974 0.0882 0.0086  -0.0020 0.0107  144 LEU A CB  
1281 C  CG  . LEU A 143 ? 0.0800 0.0908 0.1240 -0.0043 -0.0131 0.0104  144 LEU A CG  
1282 C  CD1 . LEU A 143 ? 0.0961 0.1520 0.1360 -0.0247 -0.0038 0.0531  144 LEU A CD1 
1283 C  CD2 . LEU A 143 ? 0.0847 0.1375 0.1415 -0.0015 -0.0135 0.0159  144 LEU A CD2 
1284 N  N   . GLY A 144 ? 0.0769 0.0580 0.0696 -0.0076 -0.0065 0.0003  145 GLY A N   
1285 C  CA  . GLY A 144 ? 0.0835 0.0575 0.0762 -0.0065 -0.0035 -0.0003 145 GLY A CA  
1286 C  C   . GLY A 144 ? 0.0752 0.0599 0.0636 0.0030  -0.0068 0.0060  145 GLY A C   
1287 O  O   . GLY A 144 ? 0.0987 0.0706 0.0661 -0.0127 0.0060  0.0007  145 GLY A O   
1288 N  N   . ILE A 145 ? 0.0778 0.0576 0.0679 -0.0005 0.0017  -0.0013 146 ILE A N   
1289 C  CA  . ILE A 145 ? 0.0753 0.0611 0.0690 -0.0027 -0.0021 -0.0026 146 ILE A CA  
1290 C  C   . ILE A 145 ? 0.0752 0.0553 0.0617 -0.0052 -0.0060 0.0000  146 ILE A C   
1291 O  O   . ILE A 145 ? 0.0832 0.0575 0.0835 -0.0027 0.0098  0.0020  146 ILE A O   
1292 C  CB  . ILE A 145 ? 0.0788 0.0666 0.0815 0.0092  -0.0057 0.0027  146 ILE A CB  
1293 C  CG1 . ILE A 145 ? 0.1157 0.0806 0.1035 0.0281  -0.0206 0.0006  146 ILE A CG1 
1294 C  CG2 . ILE A 145 ? 0.0883 0.0842 0.1299 -0.0038 -0.0295 0.0054  146 ILE A CG2 
1295 C  CD1 . ILE A 145 ? 0.1005 0.0791 0.1122 0.0017  -0.0137 0.0038  146 ILE A CD1 
1296 N  N   . PHE A 146 ? 0.0820 0.0537 0.0769 0.0038  -0.0005 -0.0001 147 PHE A N   
1297 C  CA  . PHE A 146 ? 0.0863 0.0498 0.0800 0.0008  -0.0066 0.0007  147 PHE A CA  
1298 C  C   . PHE A 146 ? 0.0895 0.0533 0.0823 0.0020  0.0020  -0.0010 147 PHE A C   
1299 O  O   . PHE A 146 ? 0.0900 0.0743 0.0878 -0.0007 -0.0041 -0.0071 147 PHE A O   
1300 C  CB  . PHE A 146 ? 0.0907 0.0615 0.0854 -0.0035 -0.0086 0.0006  147 PHE A CB  
1301 C  CG  . PHE A 146 ? 0.0803 0.0538 0.0824 0.0020  -0.0078 0.0073  147 PHE A CG  
1302 C  CD1 . PHE A 146 ? 0.0920 0.0548 0.0896 0.0060  -0.0024 0.0034  147 PHE A CD1 
1303 C  CD2 . PHE A 146 ? 0.1006 0.0575 0.0888 -0.0008 -0.0063 0.0114  147 PHE A CD2 
1304 C  CE1 . PHE A 146 ? 0.0967 0.0679 0.0886 0.0005  -0.0127 -0.0023 147 PHE A CE1 
1305 C  CE2 . PHE A 146 ? 0.1004 0.0797 0.0813 0.0038  -0.0023 0.0049  147 PHE A CE2 
1306 C  CZ  . PHE A 146 ? 0.1006 0.0701 0.0900 -0.0005 -0.0108 0.0137  147 PHE A CZ  
1307 N  N   . LEU A 147 ? 0.0972 0.0566 0.0780 -0.0019 -0.0054 0.0024  148 LEU A N   
1308 C  CA  . LEU A 147 ? 0.1033 0.0597 0.0805 -0.0091 -0.0024 -0.0103 148 LEU A CA  
1309 C  C   . LEU A 147 ? 0.0907 0.0703 0.0673 -0.0015 -0.0055 -0.0023 148 LEU A C   
1310 O  O   . LEU A 147 ? 0.1053 0.0644 0.1032 0.0001  -0.0012 0.0003  148 LEU A O   
1311 C  CB  . LEU A 147 ? 0.1066 0.0639 0.0785 -0.0021 0.0000  -0.0055 148 LEU A CB  
1312 C  CG  . LEU A 147 ? 0.1209 0.0653 0.0812 -0.0046 -0.0094 -0.0046 148 LEU A CG  
1313 C  CD1 . LEU A 147 ? 0.1580 0.0623 0.1032 -0.0076 -0.0225 0.0000  148 LEU A CD1 
1314 C  CD2 . LEU A 147 ? 0.1172 0.0804 0.0978 -0.0089 -0.0097 0.0111  148 LEU A CD2 
1315 N  N   . LYS A 148 ? 0.1043 0.0597 0.0979 -0.0077 -0.0057 0.0020  149 LYS A N   
1316 C  CA  . LYS A 148 ? 0.1324 0.0621 0.1136 -0.0188 -0.0102 0.0065  149 LYS A CA  
1317 C  C   . LYS A 148 ? 0.1142 0.0608 0.1228 -0.0063 -0.0251 -0.0015 149 LYS A C   
1318 O  O   . LYS A 148 ? 0.1489 0.0936 0.1095 0.0125  -0.0326 -0.0144 149 LYS A O   
1319 C  CB  . LYS A 148 ? 0.1624 0.0864 0.1185 -0.0209 -0.0051 0.0185  149 LYS A CB  
1320 C  CG  . LYS A 148 ? 0.1462 0.1281 0.1624 -0.0439 0.0010  0.0232  149 LYS A CG  
1321 C  CD  . LYS A 148 ? 0.2125 0.1888 0.2477 -0.0706 0.0524  0.0447  149 LYS A CD  
1322 C  CE  . LYS A 148 ? 0.2270 0.3443 0.3316 -0.0283 0.0311  0.1280  149 LYS A CE  
1323 N  NZ  . LYS A 148 ? 0.4979 2.2771 2.4972 0.3131  0.6557  2.1342  149 LYS A NZ  
1324 N  N   . VAL A 149 ? 0.1415 0.0597 0.1248 -0.0010 -0.0296 -0.0032 150 VAL A N   
1325 C  CA  . VAL A 149 ? 0.1448 0.0659 0.1168 -0.0032 -0.0211 -0.0035 150 VAL A CA  
1326 C  C   . VAL A 149 ? 0.1620 0.0606 0.1347 0.0034  -0.0063 0.0000  150 VAL A C   
1327 O  O   . VAL A 149 ? 0.1664 0.0759 0.1551 0.0006  -0.0168 0.0137  150 VAL A O   
1328 C  CB  . VAL A 149 ? 0.1412 0.0900 0.1473 0.0068  -0.0218 -0.0089 150 VAL A CB  
1329 C  CG1 . VAL A 149 ? 0.1686 0.1166 0.1431 -0.0059 -0.0286 -0.0234 150 VAL A CG1 
1330 C  CG2 . VAL A 149 ? 0.1436 0.1154 0.1572 -0.0086 -0.0196 -0.0021 150 VAL A CG2 
1331 N  N   . GLY A 150 ? 0.1456 0.0773 0.1504 -0.0121 -0.0331 0.0118  151 GLY A N   
1332 C  CA  . GLY A 150 ? 0.1427 0.0975 0.1726 -0.0294 -0.0364 0.0297  151 GLY A CA  
1333 C  C   . GLY A 150 ? 0.1474 0.0847 0.1344 -0.0294 -0.0231 -0.0086 151 GLY A C   
1334 O  O   . GLY A 150 ? 0.1642 0.1000 0.1422 -0.0248 -0.0188 -0.0151 151 GLY A O   
1335 N  N   A SER A 151 ? 0.1450 0.0956 0.1410 -0.0161 -0.0241 0.0074  152 SER A N   
1336 N  N   B SER A 151 ? 0.1352 0.0964 0.1446 -0.0219 -0.0288 -0.0044 152 SER A N   
1337 C  CA  A SER A 151 ? 0.1543 0.1274 0.1287 -0.0099 -0.0088 0.0273  152 SER A CA  
1338 C  CA  B SER A 151 ? 0.1229 0.0960 0.1386 -0.0452 -0.0335 -0.0277 152 SER A CA  
1339 C  C   A SER A 151 ? 0.1396 0.1132 0.1298 -0.0219 -0.0118 -0.0049 152 SER A C   
1340 C  C   B SER A 151 ? 0.1290 0.0937 0.1086 -0.0130 -0.0256 -0.0181 152 SER A C   
1341 O  O   A SER A 151 ? 0.1120 0.0963 0.1264 -0.0177 0.0057  -0.0082 152 SER A O   
1342 O  O   B SER A 151 ? 0.0952 0.1106 0.0952 -0.0114 -0.0086 -0.0248 152 SER A O   
1343 C  CB  A SER A 151 ? 0.1247 0.1490 0.1635 -0.0586 0.0001  0.0119  152 SER A CB  
1344 C  CB  B SER A 151 ? 0.1324 0.1234 0.1787 -0.0135 -0.0245 -0.0015 152 SER A CB  
1345 O  OG  A SER A 151 ? 0.1986 0.2129 0.2278 -0.0476 0.0249  -0.0185 152 SER A OG  
1346 O  OG  B SER A 151 ? 0.1257 0.2090 0.2349 -0.0478 -0.0062 0.0746  152 SER A OG  
1347 N  N   . ALA A 152 ? 0.1413 0.1018 0.1368 -0.0082 -0.0399 -0.0137 153 ALA A N   
1348 C  CA  . ALA A 152 ? 0.1359 0.0983 0.1165 -0.0140 -0.0284 -0.0017 153 ALA A CA  
1349 C  C   . ALA A 152 ? 0.1166 0.1010 0.1194 -0.0115 -0.0193 -0.0010 153 ALA A C   
1350 O  O   . ALA A 152 ? 0.1270 0.1199 0.1617 -0.0227 -0.0001 -0.0144 153 ALA A O   
1351 C  CB  . ALA A 152 ? 0.1604 0.1392 0.1195 0.0028  -0.0096 0.0010  153 ALA A CB  
1352 N  N   . LYS A 153 ? 0.1193 0.1041 0.1239 -0.0130 -0.0217 0.0035  154 LYS A N   
1353 C  CA  . LYS A 153 ? 0.1326 0.0980 0.1261 -0.0104 -0.0233 0.0059  154 LYS A CA  
1354 C  C   . LYS A 153 ? 0.1024 0.1059 0.1405 -0.0138 -0.0037 -0.0008 154 LYS A C   
1355 O  O   . LYS A 153 ? 0.1042 0.1069 0.1282 -0.0043 -0.0205 0.0020  154 LYS A O   
1356 C  CB  . LYS A 153 ? 0.1429 0.1120 0.1264 -0.0215 -0.0353 0.0052  154 LYS A CB  
1357 C  CG  . LYS A 153 ? 0.1787 0.0894 0.1395 -0.0194 -0.0273 -0.0024 154 LYS A CG  
1358 C  CD  . LYS A 153 ? 0.2280 0.1216 0.1506 -0.0267 0.0087  -0.0149 154 LYS A CD  
1359 C  CE  . LYS A 153 ? 0.3704 0.1403 0.1192 -0.0024 0.0397  -0.0034 154 LYS A CE  
1360 N  NZ  . LYS A 153 ? 0.5065 0.1587 0.2025 -0.0674 0.1297  -0.0273 154 LYS A NZ  
1361 N  N   A PRO A 154 ? 0.1128 0.1164 0.1300 -0.0154 -0.0212 0.0124  155 PRO A N   
1362 N  N   B PRO A 154 ? 0.0922 0.1095 0.1246 -0.0188 -0.0141 -0.0065 155 PRO A N   
1363 C  CA  A PRO A 154 ? 0.1013 0.1541 0.1238 -0.0176 -0.0337 0.0055  155 PRO A CA  
1364 C  CA  B PRO A 154 ? 0.0788 0.1562 0.1571 0.0146  -0.0182 0.0388  155 PRO A CA  
1365 C  C   A PRO A 154 ? 0.1264 0.1605 0.1460 -0.0225 -0.0291 0.0258  155 PRO A C   
1366 C  C   B PRO A 154 ? 0.0740 0.1420 0.1291 0.0148  -0.0204 0.0006  155 PRO A C   
1367 O  O   A PRO A 154 ? 0.1150 0.1490 0.1465 0.0038  -0.0168 0.0485  155 PRO A O   
1368 O  O   B PRO A 154 ? 0.1370 0.1322 0.1181 0.0066  -0.0142 0.0057  155 PRO A O   
1369 C  CB  A PRO A 154 ? 0.1137 0.1377 0.1335 -0.0172 -0.0326 -0.0031 155 PRO A CB  
1370 C  CB  B PRO A 154 ? 0.0884 0.1449 0.1738 -0.0027 -0.0157 -0.0038 155 PRO A CB  
1371 C  CG  A PRO A 154 ? 0.1085 0.1229 0.1618 -0.0197 -0.0035 -0.0445 155 PRO A CG  
1372 C  CG  B PRO A 154 ? 0.0942 0.2806 0.1626 0.0049  -0.0043 0.0274  155 PRO A CG  
1373 C  CD  A PRO A 154 ? 0.1424 0.1310 0.1387 -0.0126 0.0082  -0.0111 155 PRO A CD  
1374 C  CD  B PRO A 154 ? 0.0952 0.1169 0.1235 -0.0032 0.0092  -0.0057 155 PRO A CD  
1375 N  N   . GLY A 155 ? 0.1014 0.1312 0.1504 0.0040  -0.0159 0.0179  156 GLY A N   
1376 C  CA  . GLY A 155 ? 0.1243 0.1103 0.1851 0.0028  0.0093  0.0295  156 GLY A CA  
1377 C  C   . GLY A 155 ? 0.1283 0.1089 0.1451 0.0000  -0.0165 0.0262  156 GLY A C   
1378 O  O   . GLY A 155 ? 0.1396 0.1059 0.2552 -0.0115 0.0108  0.0298  156 GLY A O   
1379 N  N   . LEU A 156 ? 0.1102 0.1088 0.1272 -0.0102 -0.0164 0.0098  157 LEU A N   
1380 C  CA  . LEU A 156 ? 0.1049 0.1105 0.1199 -0.0151 -0.0154 0.0081  157 LEU A CA  
1381 C  C   . LEU A 156 ? 0.1124 0.0954 0.1116 -0.0167 -0.0245 0.0013  157 LEU A C   
1382 O  O   . LEU A 156 ? 0.1113 0.1061 0.1039 -0.0241 -0.0179 0.0000  157 LEU A O   
1383 C  CB  . LEU A 156 ? 0.0970 0.1002 0.1240 -0.0049 -0.0146 0.0010  157 LEU A CB  
1384 C  CG  . LEU A 156 ? 0.1111 0.1094 0.1185 -0.0115 -0.0144 0.0021  157 LEU A CG  
1385 C  CD1 . LEU A 156 ? 0.1242 0.1341 0.1209 -0.0337 -0.0265 -0.0074 157 LEU A CD1 
1386 C  CD2 . LEU A 156 ? 0.1337 0.1196 0.1316 -0.0087 -0.0315 0.0020  157 LEU A CD2 
1387 N  N   . GLN A 157 ? 0.1123 0.1099 0.1208 -0.0200 -0.0243 0.0065  158 GLN A N   
1388 C  CA  . GLN A 157 ? 0.1333 0.1156 0.1115 -0.0408 -0.0278 -0.0083 158 GLN A CA  
1389 C  C   . GLN A 157 ? 0.1235 0.1200 0.1177 -0.0342 -0.0406 -0.0043 158 GLN A C   
1390 O  O   . GLN A 157 ? 0.1308 0.1243 0.1115 -0.0248 -0.0219 -0.0121 158 GLN A O   
1391 C  CB  . GLN A 157 ? 0.1467 0.1252 0.1485 -0.0395 -0.0375 0.0113  158 GLN A CB  
1392 C  CG  . GLN A 157 ? 0.1436 0.1142 0.1483 -0.0236 -0.0419 -0.0096 158 GLN A CG  
1393 C  CD  . GLN A 157 ? 0.1383 0.1195 0.1345 -0.0366 -0.0241 -0.0109 158 GLN A CD  
1394 O  OE1 . GLN A 157 ? 0.1543 0.1143 0.1288 -0.0083 -0.0197 -0.0083 158 GLN A OE1 
1395 N  NE2 . GLN A 157 ? 0.1861 0.1553 0.1318 -0.0441 -0.0031 -0.0346 158 GLN A NE2 
1396 N  N   . LYS A 158 ? 0.1292 0.1209 0.1199 -0.0262 -0.0370 0.0113  159 LYS A N   
1397 C  CA  . LYS A 158 ? 0.1255 0.1148 0.1339 -0.0157 -0.0320 0.0120  159 LYS A CA  
1398 C  C   . LYS A 158 ? 0.1335 0.1162 0.1076 -0.0110 -0.0237 0.0088  159 LYS A C   
1399 O  O   . LYS A 158 ? 0.1571 0.1361 0.1087 -0.0313 -0.0159 0.0119  159 LYS A O   
1400 C  CB  . LYS A 158 ? 0.1614 0.1123 0.1797 0.0038  -0.0328 0.0253  159 LYS A CB  
1401 C  CG  . LYS A 158 ? 0.2025 0.2096 0.1914 -0.0021 -0.0350 0.0601  159 LYS A CG  
1402 C  CD  . LYS A 158 ? 0.2192 0.3458 0.3025 0.0780  -0.0483 0.0794  159 LYS A CD  
1403 C  CE  . LYS A 158 ? 0.3300 0.2117 0.5157 -0.0097 -0.1889 0.0658  159 LYS A CE  
1404 N  NZ  . LYS A 158 ? 0.3501 0.3337 0.2883 -0.0071 -0.0917 -0.0115 159 LYS A NZ  
1405 N  N   . VAL A 159 ? 0.1259 0.1032 0.1057 -0.0085 -0.0206 -0.0066 160 VAL A N   
1406 C  CA  . VAL A 159 ? 0.1067 0.1075 0.1111 -0.0137 -0.0166 -0.0109 160 VAL A CA  
1407 C  C   . VAL A 159 ? 0.1181 0.1105 0.1040 -0.0175 -0.0142 -0.0104 160 VAL A C   
1408 O  O   . VAL A 159 ? 0.1296 0.1222 0.1216 -0.0192 -0.0020 -0.0082 160 VAL A O   
1409 C  CB  . VAL A 159 ? 0.1165 0.1076 0.1046 -0.0188 -0.0185 -0.0041 160 VAL A CB  
1410 C  CG1 . VAL A 159 ? 0.1278 0.1392 0.1213 -0.0337 -0.0154 -0.0026 160 VAL A CG1 
1411 C  CG2 . VAL A 159 ? 0.1600 0.1235 0.1192 -0.0040 -0.0115 -0.0215 160 VAL A CG2 
1412 N  N   . VAL A 160 ? 0.1334 0.0988 0.1060 -0.0087 -0.0222 -0.0088 161 VAL A N   
1413 C  CA  . VAL A 160 ? 0.1591 0.1061 0.1169 -0.0054 0.0057  -0.0140 161 VAL A CA  
1414 C  C   . VAL A 160 ? 0.1560 0.1067 0.1330 -0.0215 0.0151  -0.0238 161 VAL A C   
1415 O  O   . VAL A 160 ? 0.1660 0.1393 0.1347 -0.0284 0.0178  -0.0266 161 VAL A O   
1416 C  CB  . VAL A 160 ? 0.1626 0.1306 0.1551 0.0107  0.0065  -0.0179 161 VAL A CB  
1417 C  CG1 . VAL A 160 ? 0.1889 0.1349 0.1903 0.0054  -0.0179 -0.0403 161 VAL A CG1 
1418 C  CG2 . VAL A 160 ? 0.1668 0.1369 0.1601 -0.0082 0.0034  0.0032  161 VAL A CG2 
1419 N  N   . ASP A 161 ? 0.1776 0.1322 0.1084 -0.0388 -0.0259 -0.0165 162 ASP A N   
1420 C  CA  . ASP A 161 ? 0.2076 0.1863 0.1072 -0.0577 -0.0227 -0.0170 162 ASP A CA  
1421 C  C   . ASP A 161 ? 0.2560 0.1823 0.0833 -0.0575 -0.0109 -0.0074 162 ASP A C   
1422 O  O   . ASP A 161 ? 0.3901 0.2342 0.1211 -0.0612 0.0406  -0.0310 162 ASP A O   
1423 C  CB  . ASP A 161 ? 0.2459 0.3034 0.1136 -0.1128 -0.0428 -0.0010 162 ASP A CB  
1424 C  CG  . ASP A 161 ? 0.2098 0.2497 0.1597 -0.0204 -0.0395 -0.0390 162 ASP A CG  
1425 O  OD1 . ASP A 161 ? 0.2870 0.2522 0.1863 -0.0838 -0.0289 -0.0133 162 ASP A OD1 
1426 O  OD2 . ASP A 161 ? 0.2728 0.2357 0.1912 -0.0335 -0.0326 -0.0482 162 ASP A OD2 
1427 N  N   . VAL A 162 ? 0.1509 0.1652 0.1028 -0.0208 -0.0241 -0.0057 163 VAL A N   
1428 C  CA  . VAL A 162 ? 0.1439 0.1678 0.1127 -0.0258 -0.0166 0.0200  163 VAL A CA  
1429 C  C   . VAL A 162 ? 0.1449 0.1513 0.0980 -0.0038 -0.0028 0.0046  163 VAL A C   
1430 O  O   . VAL A 162 ? 0.1572 0.1766 0.1085 -0.0077 -0.0100 0.0154  163 VAL A O   
1431 C  CB  . VAL A 162 ? 0.1592 0.1474 0.1588 -0.0024 -0.0046 0.0111  163 VAL A CB  
1432 C  CG1 . VAL A 162 ? 0.1765 0.1476 0.1263 -0.0174 0.0077  -0.0046 163 VAL A CG1 
1433 C  CG2 . VAL A 162 ? 0.2040 0.1969 0.1729 0.0132  0.0089  0.0281  163 VAL A CG2 
1434 N  N   . LEU A 163 ? 0.1354 0.1483 0.0999 -0.0026 -0.0120 0.0005  164 LEU A N   
1435 C  CA  . LEU A 163 ? 0.1525 0.1462 0.0947 -0.0137 0.0006  0.0046  164 LEU A CA  
1436 C  C   . LEU A 163 ? 0.1620 0.1430 0.1114 0.0024  0.0107  0.0000  164 LEU A C   
1437 O  O   . LEU A 163 ? 0.1658 0.1655 0.1263 0.0038  0.0209  0.0054  164 LEU A O   
1438 C  CB  . LEU A 163 ? 0.1524 0.1385 0.1211 0.0020  0.0051  0.0129  164 LEU A CB  
1439 C  CG  . LEU A 163 ? 0.1465 0.1392 0.1143 0.0071  -0.0074 0.0087  164 LEU A CG  
1440 C  CD1 . LEU A 163 ? 0.1703 0.1509 0.1539 0.0125  -0.0065 0.0427  164 LEU A CD1 
1441 C  CD2 . LEU A 163 ? 0.1630 0.1429 0.1131 -0.0019 -0.0253 -0.0110 164 LEU A CD2 
1442 N  N   . ASP A 164 ? 0.2527 0.1717 0.1088 -0.0131 0.0085  -0.0216 165 ASP A N   
1443 C  CA  . ASP A 164 ? 0.2752 0.2182 0.1622 -0.0119 0.0579  -0.0524 165 ASP A CA  
1444 C  C   . ASP A 164 ? 0.2840 0.2445 0.1227 -0.0114 0.0522  -0.0172 165 ASP A C   
1445 O  O   . ASP A 164 ? 0.2606 0.3301 0.1878 -0.0041 0.0799  -0.0200 165 ASP A O   
1446 C  CB  . ASP A 164 ? 0.4032 0.3151 0.1884 -0.0834 0.0526  -0.1010 165 ASP A CB  
1447 C  CG  . ASP A 164 ? 0.4352 0.5368 0.2827 -0.1604 0.0318  -0.0640 165 ASP A CG  
1448 O  OD1 . ASP A 164 ? 0.4158 0.4621 0.2617 -0.1401 -0.0215 -0.0326 165 ASP A OD1 
1449 O  OD2 . ASP A 164 ? 0.7761 0.7448 0.2732 -0.2040 0.1779  -0.1825 165 ASP A OD2 
1450 N  N   . SER A 165 ? 0.1889 0.2233 0.0926 -0.0122 -0.0153 -0.0023 166 SER A N   
1451 C  CA  . SER A 165 ? 0.1668 0.2328 0.1112 -0.0049 -0.0093 0.0236  166 SER A CA  
1452 C  C   . SER A 165 ? 0.1577 0.1706 0.0961 0.0063  0.0054  0.0115  166 SER A C   
1453 O  O   . SER A 165 ? 0.1682 0.2047 0.1120 -0.0031 -0.0046 0.0511  166 SER A O   
1454 C  CB  . SER A 165 ? 0.1849 0.2940 0.1272 0.0189  -0.0161 0.0370  166 SER A CB  
1455 O  OG  . SER A 165 ? 0.1988 0.2017 0.1782 0.0137  -0.0132 0.0313  166 SER A OG  
1456 N  N   . ILE A 166 ? 0.1308 0.1541 0.0900 0.0000  -0.0035 0.0212  167 ILE A N   
1457 C  CA  . ILE A 166 ? 0.1406 0.1253 0.1057 0.0177  0.0031  0.0102  167 ILE A CA  
1458 C  C   . ILE A 166 ? 0.1261 0.1386 0.0856 -0.0010 0.0121  0.0126  167 ILE A C   
1459 O  O   . ILE A 166 ? 0.1210 0.1353 0.0926 0.0031  0.0099  0.0076  167 ILE A O   
1460 C  CB  . ILE A 166 ? 0.1291 0.1513 0.0891 0.0214  0.0020  0.0081  167 ILE A CB  
1461 C  CG1 . ILE A 166 ? 0.1077 0.1435 0.1041 0.0023  0.0035  -0.0019 167 ILE A CG1 
1462 C  CG2 . ILE A 166 ? 0.1444 0.1457 0.1281 0.0270  0.0031  0.0225  167 ILE A CG2 
1463 C  CD1 . ILE A 166 ? 0.1516 0.1431 0.1105 0.0015  0.0293  -0.0052 167 ILE A CD1 
1464 N  N   . LYS A 167 ? 0.1447 0.1553 0.1022 0.0175  0.0148  0.0086  168 LYS A N   
1465 C  CA  . LYS A 167 ? 0.1467 0.1318 0.1050 0.0135  0.0087  -0.0003 168 LYS A CA  
1466 C  C   . LYS A 167 ? 0.1351 0.1231 0.1005 0.0077  0.0250  0.0065  168 LYS A C   
1467 O  O   . LYS A 167 ? 0.1409 0.1239 0.1107 0.0043  0.0113  0.0170  168 LYS A O   
1468 C  CB  . LYS A 167 ? 0.1557 0.1694 0.1288 0.0023  0.0027  -0.0161 168 LYS A CB  
1469 C  CG  . LYS A 167 ? 0.2117 0.1526 0.1553 0.0208  0.0020  -0.0237 168 LYS A CG  
1470 C  CD  . LYS A 167 ? 0.2987 0.1835 0.2626 0.0370  -0.0427 -0.0797 168 LYS A CD  
1471 C  CE  . LYS A 167 ? 0.3503 0.2565 0.2581 0.0811  -0.0288 -0.0362 168 LYS A CE  
1472 N  NZ  . LYS A 167 ? 0.6355 0.6664 0.4537 0.0236  -0.0074 -0.3815 168 LYS A NZ  
1473 N  N   . THR A 168 ? 0.1222 0.1425 0.0964 0.0130  0.0155  0.0183  169 THR A N   
1474 C  CA  . THR A 168 ? 0.1275 0.1412 0.1159 0.0175  0.0274  0.0176  169 THR A CA  
1475 C  C   . THR A 168 ? 0.1166 0.1236 0.1040 0.0052  0.0252  0.0307  169 THR A C   
1476 O  O   . THR A 168 ? 0.1187 0.1328 0.1182 0.0130  0.0253  0.0329  169 THR A O   
1477 C  CB  . THR A 168 ? 0.1572 0.1454 0.0992 0.0176  0.0298  0.0146  169 THR A CB  
1478 O  OG1 . THR A 168 ? 0.1509 0.1904 0.1094 0.0205  0.0399  0.0340  169 THR A OG1 
1479 C  CG2 . THR A 168 ? 0.1754 0.1641 0.1313 0.0265  0.0496  0.0080  169 THR A CG2 
1480 N  N   . LYS A 169 ? 0.1317 0.1463 0.1138 0.0021  0.0199  0.0103  170 LYS A N   
1481 C  CA  . LYS A 169 ? 0.1190 0.1507 0.1303 0.0020  0.0098  0.0368  170 LYS A CA  
1482 C  C   . LYS A 169 ? 0.1261 0.1394 0.1271 -0.0049 0.0304  0.0361  170 LYS A C   
1483 O  O   . LYS A 169 ? 0.1458 0.1771 0.1432 -0.0066 0.0480  0.0432  170 LYS A O   
1484 C  CB  . LYS A 169 ? 0.1393 0.1647 0.1365 -0.0127 0.0015  0.0384  170 LYS A CB  
1485 C  CG  . LYS A 169 ? 0.1875 0.1983 0.1559 -0.0467 0.0068  0.0329  170 LYS A CG  
1486 C  CD  . LYS A 169 ? 0.1985 0.2658 0.1720 -0.0590 0.0049  0.0283  170 LYS A CD  
1487 C  CE  . LYS A 169 ? 0.2592 0.4332 0.2570 -0.0930 0.0094  0.0274  170 LYS A CE  
1488 N  NZ  . LYS A 169 ? 0.3842 0.6550 0.5228 0.0666  0.0077  -0.0856 170 LYS A NZ  
1489 N  N   . GLY A 170 ? 0.1225 0.1230 0.1429 -0.0132 0.0234  0.0200  171 GLY A N   
1490 C  CA  . GLY A 170 ? 0.1385 0.1451 0.1736 -0.0355 0.0170  0.0438  171 GLY A CA  
1491 C  C   . GLY A 170 ? 0.1533 0.1429 0.1636 -0.0254 0.0406  0.0555  171 GLY A C   
1492 O  O   . GLY A 170 ? 0.1997 0.1234 0.1923 -0.0104 0.0357  0.0518  171 GLY A O   
1493 N  N   A LYS A 171 ? 0.1268 0.1561 0.1184 0.0026  0.0274  0.0452  172 LYS A N   
1494 N  N   B LYS A 171 ? 0.1273 0.1576 0.1199 -0.0001 0.0291  0.0443  172 LYS A N   
1495 C  CA  A LYS A 171 ? 0.1254 0.1546 0.1238 0.0142  0.0295  0.0443  172 LYS A CA  
1496 C  CA  B LYS A 171 ? 0.1293 0.1579 0.1211 0.0054  0.0311  0.0423  172 LYS A CA  
1497 C  C   A LYS A 171 ? 0.1234 0.1454 0.1123 0.0177  0.0220  0.0511  172 LYS A C   
1498 C  C   B LYS A 171 ? 0.1255 0.1462 0.1128 0.0175  0.0219  0.0529  172 LYS A C   
1499 O  O   A LYS A 171 ? 0.1310 0.1402 0.0918 0.0147  0.0186  0.0296  172 LYS A O   
1500 O  O   B LYS A 171 ? 0.1330 0.1386 0.0925 0.0149  0.0187  0.0313  172 LYS A O   
1501 C  CB  A LYS A 171 ? 0.1369 0.1701 0.1128 0.0038  0.0140  0.0326  172 LYS A CB  
1502 C  CB  B LYS A 171 ? 0.1298 0.1729 0.1189 0.0048  0.0091  0.0270  172 LYS A CB  
1503 C  CG  A LYS A 171 ? 0.2457 0.2132 0.0944 0.0502  0.0406  0.0410  172 LYS A CG  
1504 C  CG  B LYS A 171 ? 0.1054 0.2389 0.1932 0.0304  -0.0005 -0.0362 172 LYS A CG  
1505 C  CD  A LYS A 171 ? 0.2039 0.2910 0.1940 0.0929  -0.0087 -0.0100 172 LYS A CD  
1506 C  CD  B LYS A 171 ? 0.3589 0.3614 0.0834 -0.0168 -0.0247 -0.0408 172 LYS A CD  
1507 C  CE  A LYS A 171 ? 0.2138 0.3032 0.1668 0.1316  -0.0035 -0.0273 172 LYS A CE  
1508 C  CE  B LYS A 171 ? 0.2382 0.3116 0.1595 -0.0028 0.0406  0.0447  172 LYS A CE  
1509 N  NZ  A LYS A 171 ? 0.4280 0.1913 0.3045 0.0491  0.1361  0.0304  172 LYS A NZ  
1510 N  NZ  B LYS A 171 ? 0.4384 0.3587 0.1525 -0.1247 0.1193  0.0003  172 LYS A NZ  
1511 N  N   . SER A 172 ? 0.1596 0.1703 0.1108 0.0390  0.0340  0.0621  173 SER A N   
1512 C  CA  . SER A 172 ? 0.1440 0.1770 0.1080 0.0219  0.0216  0.0544  173 SER A CA  
1513 C  C   . SER A 172 ? 0.1588 0.1641 0.0883 0.0454  0.0049  0.0265  173 SER A C   
1514 O  O   . SER A 172 ? 0.1736 0.2344 0.0895 0.0425  0.0168  0.0505  173 SER A O   
1515 C  CB  . SER A 172 ? 0.1816 0.1779 0.1282 0.0201  -0.0109 0.0335  173 SER A CB  
1516 O  OG  . SER A 172 ? 0.2170 0.1772 0.1773 0.0092  -0.0131 0.0531  173 SER A OG  
1517 N  N   . ALA A 173 ? 0.1374 0.1827 0.0961 0.0364  -0.0087 0.0427  174 ALA A N   
1518 C  CA  . ALA A 173 ? 0.1562 0.2082 0.0913 0.0375  0.0015  0.0337  174 ALA A CA  
1519 C  C   . ALA A 173 ? 0.1554 0.1916 0.0735 0.0296  -0.0189 0.0390  174 ALA A C   
1520 O  O   . ALA A 173 ? 0.1397 0.1533 0.0888 0.0245  -0.0104 0.0260  174 ALA A O   
1521 C  CB  . ALA A 173 ? 0.1858 0.2043 0.1070 0.0395  -0.0107 -0.0092 174 ALA A CB  
1522 N  N   . ASP A 174 ? 0.1727 0.2072 0.0967 0.0370  -0.0153 0.0399  175 ASP A N   
1523 C  CA  . ASP A 174 ? 0.1564 0.2105 0.1274 0.0668  -0.0091 0.0533  175 ASP A CA  
1524 C  C   . ASP A 174 ? 0.1288 0.1773 0.1616 0.0234  -0.0351 -0.0206 175 ASP A C   
1525 O  O   . ASP A 174 ? 0.1580 0.2295 0.2161 0.0280  -0.0091 -0.0675 175 ASP A O   
1526 C  CB  . ASP A 174 ? 0.2249 0.3289 0.1407 0.1111  -0.0270 0.0443  175 ASP A CB  
1527 C  CG  . ASP A 174 ? 0.3296 0.3091 0.2487 0.0087  -0.1202 0.0984  175 ASP A CG  
1528 O  OD1 . ASP A 174 ? 0.5769 0.4323 0.3858 -0.1362 -0.2858 0.0927  175 ASP A OD1 
1529 O  OD2 . ASP A 174 ? 0.3379 0.6076 0.3273 0.0838  -0.1402 -0.0299 175 ASP A OD2 
1530 N  N   . PHE A 175 ? 0.1131 0.1605 0.1297 0.0207  -0.0141 0.0055  176 PHE A N   
1531 C  CA  . PHE A 175 ? 0.1175 0.1393 0.1793 0.0148  -0.0236 -0.0001 176 PHE A CA  
1532 C  C   . PHE A 175 ? 0.1112 0.1204 0.1324 0.0073  -0.0265 0.0166  176 PHE A C   
1533 O  O   . PHE A 175 ? 0.1847 0.2047 0.1409 0.0820  -0.0860 -0.0454 176 PHE A O   
1534 C  CB  . PHE A 175 ? 0.1243 0.1141 0.2258 0.0186  -0.0148 0.0187  176 PHE A CB  
1535 C  CG  . PHE A 175 ? 0.1191 0.1128 0.1881 0.0015  -0.0087 -0.0010 176 PHE A CG  
1536 C  CD1 . PHE A 175 ? 0.1911 0.1275 0.2002 -0.0020 0.0480  -0.0108 176 PHE A CD1 
1537 C  CD2 . PHE A 175 ? 0.1342 0.1238 0.1800 0.0115  -0.0449 -0.0115 176 PHE A CD2 
1538 C  CE1 . PHE A 175 ? 0.2390 0.1178 0.1928 -0.0019 0.0377  -0.0043 176 PHE A CE1 
1539 C  CE2 . PHE A 175 ? 0.1196 0.1160 0.1791 -0.0003 -0.0364 0.0176  176 PHE A CE2 
1540 C  CZ  . PHE A 175 ? 0.1388 0.1351 0.1887 0.0007  -0.0017 -0.0066 176 PHE A CZ  
1541 N  N   . THR A 176 ? 0.1347 0.1420 0.1041 0.0287  -0.0074 0.0355  177 THR A N   
1542 C  CA  . THR A 176 ? 0.1099 0.1181 0.1111 0.0076  -0.0037 0.0308  177 THR A CA  
1543 C  C   . THR A 176 ? 0.1189 0.1099 0.0925 0.0003  -0.0197 0.0208  177 THR A C   
1544 O  O   . THR A 176 ? 0.1431 0.1210 0.1004 0.0000  -0.0160 0.0143  177 THR A O   
1545 C  CB  . THR A 176 ? 0.1032 0.1422 0.1262 0.0142  -0.0157 0.0546  177 THR A CB  
1546 O  OG1 . THR A 176 ? 0.3152 0.1985 0.0928 0.1070  -0.0228 0.0357  177 THR A OG1 
1547 C  CG2 . THR A 176 ? 0.1350 0.2107 0.3129 0.0076  0.0085  0.1658  177 THR A CG2 
1548 N  N   . ASN A 177 ? 0.0996 0.1200 0.0951 0.0017  -0.0170 0.0252  178 ASN A N   
1549 C  CA  . ASN A 177 ? 0.1112 0.1371 0.1097 -0.0021 -0.0094 0.0397  178 ASN A CA  
1550 C  C   . ASN A 177 ? 0.1068 0.1363 0.1087 -0.0093 -0.0122 0.0284  178 ASN A C   
1551 O  O   . ASN A 177 ? 0.1322 0.1759 0.2293 -0.0447 -0.0597 0.0945  178 ASN A O   
1552 C  CB  . ASN A 177 ? 0.1198 0.1436 0.1253 -0.0041 -0.0359 0.0493  178 ASN A CB  
1553 C  CG  . ASN A 177 ? 0.1257 0.1407 0.1235 0.0081  -0.0339 0.0179  178 ASN A CG  
1554 O  OD1 . ASN A 177 ? 0.1406 0.1616 0.1780 0.0231  -0.0057 0.0414  178 ASN A OD1 
1555 N  ND2 . ASN A 177 ? 0.1404 0.1483 0.1131 0.0038  -0.0307 0.0281  178 ASN A ND2 
1556 N  N   . PHE A 178 ? 0.1115 0.1196 0.0837 -0.0041 -0.0137 0.0204  179 PHE A N   
1557 C  CA  . PHE A 178 ? 0.1250 0.1199 0.0943 -0.0093 -0.0230 0.0284  179 PHE A CA  
1558 C  C   . PHE A 178 ? 0.1221 0.1242 0.0885 -0.0078 -0.0155 0.0262  179 PHE A C   
1559 O  O   . PHE A 178 ? 0.1581 0.1366 0.0811 -0.0284 -0.0146 0.0118  179 PHE A O   
1560 C  CB  . PHE A 178 ? 0.1385 0.1184 0.1028 0.0118  -0.0070 0.0305  179 PHE A CB  
1561 C  CG  . PHE A 178 ? 0.1220 0.1165 0.0981 -0.0126 -0.0165 0.0251  179 PHE A CG  
1562 C  CD1 . PHE A 178 ? 0.1615 0.1209 0.1087 -0.0035 -0.0119 0.0265  179 PHE A CD1 
1563 C  CD2 . PHE A 178 ? 0.0989 0.1200 0.1133 -0.0109 -0.0124 0.0285  179 PHE A CD2 
1564 C  CE1 . PHE A 178 ? 0.1689 0.1169 0.1242 -0.0027 -0.0086 0.0104  179 PHE A CE1 
1565 C  CE2 . PHE A 178 ? 0.0947 0.1217 0.1159 0.0006  -0.0044 0.0278  179 PHE A CE2 
1566 C  CZ  . PHE A 178 ? 0.1282 0.1284 0.1193 0.0046  -0.0024 0.0406  179 PHE A CZ  
1567 N  N   . ASP A 179 ? 0.1192 0.1238 0.0997 0.0005  -0.0195 0.0271  180 ASP A N   
1568 C  CA  . ASP A 179 ? 0.1049 0.1368 0.0962 -0.0048 -0.0144 0.0241  180 ASP A CA  
1569 C  C   . ASP A 179 ? 0.1104 0.1067 0.0861 -0.0038 0.0000  0.0166  180 ASP A C   
1570 O  O   . ASP A 179 ? 0.1256 0.1124 0.1044 -0.0077 -0.0049 0.0109  180 ASP A O   
1571 C  CB  . ASP A 179 ? 0.1139 0.1888 0.1259 0.0035  -0.0105 0.0335  180 ASP A CB  
1572 C  CG  . ASP A 179 ? 0.1239 0.1597 0.1539 0.0073  0.0051  0.0228  180 ASP A CG  
1573 O  OD1 . ASP A 179 ? 0.1368 0.1506 0.1322 0.0197  0.0031  0.0399  180 ASP A OD1 
1574 O  OD2 . ASP A 179 ? 0.1139 0.4106 0.2117 0.0102  0.0115  -0.0540 180 ASP A OD2 
1575 N  N   . PRO A 180 ? 0.1077 0.1044 0.0900 -0.0030 -0.0126 0.0177  181 PRO A N   
1576 C  CA  . PRO A 180 ? 0.1086 0.1222 0.0914 -0.0034 -0.0086 0.0208  181 PRO A CA  
1577 C  C   . PRO A 180 ? 0.1023 0.1187 0.0913 -0.0080 -0.0109 0.0175  181 PRO A C   
1578 O  O   . PRO A 180 ? 0.1158 0.1141 0.0981 0.0019  -0.0137 0.0255  181 PRO A O   
1579 C  CB  . PRO A 180 ? 0.1028 0.1450 0.1059 -0.0082 -0.0168 0.0271  181 PRO A CB  
1580 C  CG  . PRO A 180 ? 0.1398 0.1253 0.0940 -0.0052 -0.0196 0.0113  181 PRO A CG  
1581 C  CD  . PRO A 180 ? 0.1326 0.1230 0.0969 -0.0140 -0.0152 0.0155  181 PRO A CD  
1582 N  N   . ARG A 181 ? 0.1043 0.1199 0.0972 0.0024  0.0035  0.0253  182 ARG A N   
1583 C  CA  . ARG A 181 ? 0.1152 0.1130 0.1128 0.0030  -0.0017 0.0196  182 ARG A CA  
1584 C  C   . ARG A 181 ? 0.1107 0.1347 0.1106 0.0005  -0.0094 0.0295  182 ARG A C   
1585 O  O   . ARG A 181 ? 0.1336 0.1221 0.1208 -0.0006 0.0076  0.0340  182 ARG A O   
1586 C  CB  . ARG A 181 ? 0.1172 0.1354 0.1253 0.0012  0.0020  0.0251  182 ARG A CB  
1587 C  CG  . ARG A 181 ? 0.1370 0.1377 0.1208 0.0000  0.0303  -0.0055 182 ARG A CG  
1588 C  CD  . ARG A 181 ? 0.1460 0.1712 0.1649 0.0165  0.0351  0.0337  182 ARG A CD  
1589 N  NE  . ARG A 181 ? 0.1422 0.1618 0.1685 0.0232  0.0359  0.0364  182 ARG A NE  
1590 C  CZ  . ARG A 181 ? 0.1576 0.1889 0.2287 0.0535  0.0527  0.0516  182 ARG A CZ  
1591 N  NH1 . ARG A 181 ? 0.1726 0.2633 0.2592 0.0776  0.0502  0.0353  182 ARG A NH1 
1592 N  NH2 . ARG A 181 ? 0.1833 0.2730 0.2560 0.0798  0.0032  0.1032  182 ARG A NH2 
1593 N  N   . GLY A 182 ? 0.1093 0.1304 0.1023 0.0040  -0.0187 0.0119  183 GLY A N   
1594 C  CA  . GLY A 182 ? 0.1454 0.1222 0.1118 -0.0060 -0.0242 0.0214  183 GLY A CA  
1595 C  C   . GLY A 182 ? 0.1297 0.1074 0.1235 -0.0001 -0.0186 0.0088  183 GLY A C   
1596 O  O   . GLY A 182 ? 0.1650 0.1189 0.1545 -0.0168 -0.0232 0.0065  183 GLY A O   
1597 N  N   . LEU A 183 ? 0.1318 0.1145 0.0983 0.0054  -0.0156 0.0162  184 LEU A N   
1598 C  CA  . LEU A 183 ? 0.1316 0.1023 0.1101 0.0107  -0.0161 0.0132  184 LEU A CA  
1599 C  C   . LEU A 183 ? 0.1343 0.0904 0.1036 -0.0115 -0.0171 0.0132  184 LEU A C   
1600 O  O   . LEU A 183 ? 0.1595 0.1255 0.1261 0.0109  -0.0185 0.0452  184 LEU A O   
1601 C  CB  . LEU A 183 ? 0.1255 0.1225 0.0949 0.0192  -0.0038 0.0231  184 LEU A CB  
1602 C  CG  . LEU A 183 ? 0.1381 0.1437 0.1001 0.0228  -0.0125 0.0197  184 LEU A CG  
1603 C  CD1 . LEU A 183 ? 0.1401 0.2196 0.1226 0.0215  -0.0115 0.0636  184 LEU A CD1 
1604 C  CD2 . LEU A 183 ? 0.1969 0.1647 0.1151 0.0322  -0.0034 -0.0140 184 LEU A CD2 
1605 N  N   . LEU A 184 ? 0.1435 0.1217 0.1019 0.0049  -0.0049 0.0223  185 LEU A N   
1606 C  CA  . LEU A 184 ? 0.1337 0.1236 0.1076 -0.0324 -0.0074 0.0362  185 LEU A CA  
1607 C  C   . LEU A 184 ? 0.1588 0.1342 0.1298 -0.0529 -0.0463 0.0427  185 LEU A C   
1608 O  O   . LEU A 184 ? 0.2473 0.2016 0.1838 -0.1247 -0.1137 0.1049  185 LEU A O   
1609 C  CB  . LEU A 184 ? 0.1378 0.1551 0.1084 -0.0280 0.0119  0.0390  185 LEU A CB  
1610 C  CG  . LEU A 184 ? 0.0971 0.1351 0.1379 -0.0065 -0.0108 0.0166  185 LEU A CG  
1611 C  CD1 . LEU A 184 ? 0.1263 0.1631 0.1607 0.0214  -0.0143 0.0181  185 LEU A CD1 
1612 C  CD2 . LEU A 184 ? 0.1158 0.1314 0.2700 0.0028  -0.0577 0.0317  185 LEU A CD2 
1613 N  N   . PRO A 185 ? 0.1023 0.1243 0.1079 -0.0219 -0.0153 0.0309  186 PRO A N   
1614 C  CA  . PRO A 185 ? 0.1198 0.1146 0.1175 -0.0153 -0.0131 0.0408  186 PRO A CA  
1615 C  C   . PRO A 185 ? 0.0879 0.1237 0.1387 -0.0103 -0.0285 0.0392  186 PRO A C   
1616 O  O   . PRO A 185 ? 0.0831 0.1206 0.1879 -0.0097 -0.0276 0.0478  186 PRO A O   
1617 C  CB  . PRO A 185 ? 0.0947 0.1307 0.1213 0.0024  0.0055  0.0240  186 PRO A CB  
1618 C  CG  . PRO A 185 ? 0.0888 0.1370 0.1130 0.0114  -0.0066 0.0181  186 PRO A CG  
1619 C  CD  . PRO A 185 ? 0.0864 0.1155 0.1071 0.0000  -0.0015 0.0167  186 PRO A CD  
1620 N  N   A GLU A 186 ? 0.1044 0.1269 0.1077 -0.0346 -0.0243 0.0074  187 GLU A N   
1621 N  N   B GLU A 186 ? 0.0890 0.1001 0.1148 0.0006  -0.0020 0.0296  187 GLU A N   
1622 C  CA  A GLU A 186 ? 0.0917 0.1490 0.1305 -0.0088 -0.0333 0.0129  187 GLU A CA  
1623 C  CA  B GLU A 186 ? 0.0688 0.0751 0.1298 -0.0026 0.0081  0.0041  187 GLU A CA  
1624 C  C   A GLU A 186 ? 0.0511 0.1591 0.1228 0.0037  -0.0052 0.0043  187 GLU A C   
1625 C  C   B GLU A 186 ? 0.0872 0.0984 0.1465 -0.0071 -0.0086 0.0153  187 GLU A C   
1626 O  O   A GLU A 186 ? 0.0788 0.1737 0.1111 0.0289  -0.0055 -0.0114 187 GLU A O   
1627 O  O   B GLU A 186 ? 0.0893 0.1277 0.1210 0.0114  -0.0080 -0.0074 187 GLU A O   
1628 C  CB  A GLU A 186 ? 0.1421 0.1557 0.1740 -0.0230 -0.0264 -0.0028 187 GLU A CB  
1629 C  CB  B GLU A 186 ? 0.0581 0.1033 0.1145 -0.0280 0.0114  -0.0071 187 GLU A CB  
1630 C  CG  A GLU A 186 ? 0.3057 0.2734 0.2311 0.0384  0.0646  0.0293  187 GLU A CG  
1631 C  CG  B GLU A 186 ? 0.0922 0.0988 0.1360 -0.0335 -0.0309 -0.0027 187 GLU A CG  
1632 C  CD  A GLU A 186 ? 0.2389 0.2574 0.3341 0.0249  -0.0436 0.0516  187 GLU A CD  
1633 C  CD  B GLU A 186 ? 0.1146 0.1066 0.1917 -0.0346 -0.0397 0.0131  187 GLU A CD  
1634 O  OE1 A GLU A 186 ? 0.2046 0.1812 0.4587 -0.0379 -0.0675 0.0527  187 GLU A OE1 
1635 O  OE1 B GLU A 186 ? 0.1121 0.1668 0.2092 -0.0502 -0.0170 0.0211  187 GLU A OE1 
1636 O  OE2 A GLU A 186 ? 0.3125 0.1962 0.4149 0.0515  0.0856  0.1685  187 GLU A OE2 
1637 O  OE2 B GLU A 186 ? 0.1770 0.1168 0.2295 -0.0626 -0.0657 -0.0006 187 GLU A OE2 
1638 N  N   . SER A 187 ? 0.0718 0.1433 0.1313 -0.0137 -0.0189 0.0232  188 SER A N   
1639 C  CA  . SER A 187 ? 0.0717 0.1430 0.1435 -0.0125 -0.0074 0.0203  188 SER A CA  
1640 C  C   . SER A 187 ? 0.0723 0.1284 0.1344 -0.0043 -0.0109 0.0272  188 SER A C   
1641 O  O   . SER A 187 ? 0.0812 0.1547 0.1402 -0.0109 0.0076  -0.0052 188 SER A O   
1642 C  CB  . SER A 187 ? 0.1120 0.1517 0.1369 -0.0303 -0.0185 0.0164  188 SER A CB  
1643 O  OG  . SER A 187 ? 0.1039 0.1720 0.1407 -0.0244 -0.0055 0.0299  188 SER A OG  
1644 N  N   . LEU A 188 ? 0.0762 0.1395 0.1450 -0.0161 -0.0121 0.0063  189 LEU A N   
1645 C  CA  . LEU A 188 ? 0.0791 0.1240 0.1578 -0.0060 -0.0114 0.0104  189 LEU A CA  
1646 C  C   . LEU A 188 ? 0.0917 0.1421 0.1242 -0.0100 0.0099  -0.0087 189 LEU A C   
1647 O  O   . LEU A 188 ? 0.1192 0.1606 0.1530 -0.0286 -0.0092 -0.0137 189 LEU A O   
1648 C  CB  . LEU A 188 ? 0.0900 0.1486 0.2252 0.0005  -0.0094 0.0041  189 LEU A CB  
1649 C  CG  . LEU A 188 ? 0.0892 0.1351 0.2484 0.0071  -0.0140 0.0443  189 LEU A CG  
1650 C  CD1 . LEU A 188 ? 0.1397 0.1425 0.3725 0.0241  -0.0116 0.0581  189 LEU A CD1 
1651 C  CD2 . LEU A 188 ? 0.1010 0.2012 0.1900 -0.0046 -0.0237 0.0401  189 LEU A CD2 
1652 N  N   . ASP A 189 ? 0.0791 0.1574 0.1146 -0.0054 0.0085  -0.0012 190 ASP A N   
1653 C  CA  . ASP A 189 ? 0.0772 0.1677 0.1118 -0.0253 0.0087  -0.0109 190 ASP A CA  
1654 C  C   . ASP A 189 ? 0.0916 0.1087 0.0914 -0.0109 -0.0024 0.0015  190 ASP A C   
1655 O  O   . ASP A 189 ? 0.0786 0.1228 0.0975 -0.0103 0.0017  -0.0021 190 ASP A O   
1656 C  CB  . ASP A 189 ? 0.1218 0.2292 0.1181 -0.0763 0.0076  0.0414  190 ASP A CB  
1657 C  CG  . ASP A 189 ? 0.1524 0.2741 0.1454 -0.0760 0.0066  0.0606  190 ASP A CG  
1658 O  OD1 . ASP A 189 ? 0.1121 0.3968 0.2126 -0.0443 0.0443  -0.0296 190 ASP A OD1 
1659 O  OD2 . ASP A 189 ? 0.2175 0.4332 0.2242 -0.1787 -0.0131 0.1177  190 ASP A OD2 
1660 N  N   . TYR A 190 ? 0.0807 0.1317 0.0908 -0.0087 -0.0003 0.0109  191 TYR A N   
1661 C  CA  . TYR A 190 ? 0.0749 0.1160 0.0831 -0.0065 -0.0037 0.0082  191 TYR A CA  
1662 C  C   . TYR A 190 ? 0.0894 0.0916 0.0738 -0.0035 0.0000  0.0038  191 TYR A C   
1663 O  O   . TYR A 190 ? 0.0843 0.1182 0.0786 -0.0076 0.0041  0.0041  191 TYR A O   
1664 C  CB  . TYR A 190 ? 0.0791 0.1280 0.0910 -0.0122 -0.0070 0.0133  191 TYR A CB  
1665 C  CG  . TYR A 190 ? 0.0922 0.1110 0.0935 -0.0174 -0.0052 0.0237  191 TYR A CG  
1666 C  CD1 . TYR A 190 ? 0.1057 0.1118 0.1128 -0.0176 -0.0052 0.0168  191 TYR A CD1 
1667 C  CD2 . TYR A 190 ? 0.1079 0.1173 0.0989 -0.0015 0.0003  0.0087  191 TYR A CD2 
1668 C  CE1 . TYR A 190 ? 0.1166 0.1118 0.1133 -0.0102 -0.0071 0.0161  191 TYR A CE1 
1669 C  CE2 . TYR A 190 ? 0.1172 0.1128 0.1127 0.0005  -0.0082 0.0167  191 TYR A CE2 
1670 C  CZ  . TYR A 190 ? 0.1333 0.1113 0.1114 -0.0093 0.0000  0.0019  191 TYR A CZ  
1671 O  OH  . TYR A 190 ? 0.1560 0.1186 0.1275 0.0051  -0.0115 0.0000  191 TYR A OH  
1672 N  N   . TRP A 191 ? 0.0717 0.0859 0.0794 -0.0046 0.0000  0.0076  192 TRP A N   
1673 C  CA  . TRP A 191 ? 0.0864 0.0858 0.0698 -0.0103 0.0000  0.0046  192 TRP A CA  
1674 C  C   . TRP A 191 ? 0.0799 0.0918 0.0681 -0.0035 0.0031  0.0024  192 TRP A C   
1675 O  O   . TRP A 191 ? 0.1122 0.1043 0.0653 -0.0220 0.0043  0.0008  192 TRP A O   
1676 C  CB  . TRP A 191 ? 0.0934 0.0921 0.0775 -0.0023 -0.0049 0.0089  192 TRP A CB  
1677 C  CG  . TRP A 191 ? 0.0849 0.0929 0.0790 0.0096  -0.0020 0.0031  192 TRP A CG  
1678 C  CD1 . TRP A 191 ? 0.1177 0.0947 0.0918 0.0032  -0.0035 0.0073  192 TRP A CD1 
1679 C  CD2 . TRP A 191 ? 0.0829 0.0855 0.0974 0.0094  -0.0024 0.0015  192 TRP A CD2 
1680 N  NE1 . TRP A 191 ? 0.1252 0.0916 0.0970 0.0005  -0.0031 0.0153  192 TRP A NE1 
1681 C  CE2 . TRP A 191 ? 0.1101 0.0884 0.1071 0.0071  0.0006  0.0178  192 TRP A CE2 
1682 C  CE3 . TRP A 191 ? 0.0829 0.1085 0.0976 0.0000  -0.0057 0.0041  192 TRP A CE3 
1683 C  CZ2 . TRP A 191 ? 0.1077 0.0953 0.1620 0.0012  -0.0121 0.0065  192 TRP A CZ2 
1684 C  CZ3 . TRP A 191 ? 0.0869 0.1275 0.1220 -0.0021 -0.0013 -0.0192 192 TRP A CZ3 
1685 C  CH2 . TRP A 191 ? 0.1027 0.1230 0.1533 0.0118  -0.0127 -0.0220 192 TRP A CH2 
1686 N  N   . THR A 192 ? 0.0806 0.0859 0.0616 -0.0003 0.0005  0.0078  193 THR A N   
1687 C  CA  . THR A 192 ? 0.0791 0.0838 0.0657 0.0020  0.0035  0.0017  193 THR A CA  
1688 C  C   . THR A 192 ? 0.0762 0.0850 0.0616 0.0071  0.0000  0.0005  193 THR A C   
1689 O  O   . THR A 192 ? 0.0812 0.1017 0.0676 0.0020  0.0000  0.0035  193 THR A O   
1690 C  CB  . THR A 192 ? 0.0815 0.0773 0.0766 0.0057  0.0023  0.0034  193 THR A CB  
1691 O  OG1 . THR A 192 ? 0.0865 0.0786 0.0856 0.0082  0.0060  -0.0035 193 THR A OG1 
1692 C  CG2 . THR A 192 ? 0.0975 0.1104 0.0799 0.0100  0.0146  -0.0059 193 THR A CG2 
1693 N  N   . TYR A 193 ? 0.0699 0.0879 0.0694 0.0054  -0.0057 0.0015  194 TYR A N   
1694 C  CA  . TYR A 193 ? 0.0772 0.0874 0.0645 0.0024  -0.0003 0.0012  194 TYR A CA  
1695 C  C   . TYR A 193 ? 0.0735 0.0816 0.0671 0.0107  -0.0017 -0.0060 194 TYR A C   
1696 O  O   . TYR A 193 ? 0.0804 0.0882 0.0652 0.0054  -0.0030 -0.0037 194 TYR A O   
1697 C  CB  . TYR A 193 ? 0.0840 0.0982 0.0664 0.0178  -0.0043 0.0003  194 TYR A CB  
1698 C  CG  . TYR A 193 ? 0.0872 0.0702 0.0732 0.0017  -0.0105 0.0035  194 TYR A CG  
1699 C  CD1 . TYR A 193 ? 0.0780 0.0760 0.0737 0.0037  -0.0046 0.0068  194 TYR A CD1 
1700 C  CD2 . TYR A 193 ? 0.0802 0.0832 0.0802 0.0049  -0.0148 0.0021  194 TYR A CD2 
1701 C  CE1 . TYR A 193 ? 0.0716 0.0724 0.0731 0.0032  -0.0089 -0.0015 194 TYR A CE1 
1702 C  CE2 . TYR A 193 ? 0.0837 0.0764 0.0768 0.0007  -0.0005 -0.0052 194 TYR A CE2 
1703 C  CZ  . TYR A 193 ? 0.0784 0.0666 0.0732 0.0077  -0.0041 -0.0007 194 TYR A CZ  
1704 O  OH  . TYR A 193 ? 0.0819 0.0743 0.0725 0.0015  0.0024  -0.0038 194 TYR A OH  
1705 N  N   . PRO A 194 ? 0.0798 0.0972 0.0674 0.0038  -0.0003 -0.0104 195 PRO A N   
1706 C  CA  . PRO A 194 ? 0.0796 0.0875 0.0760 0.0020  0.0001  -0.0110 195 PRO A CA  
1707 C  C   . PRO A 194 ? 0.0711 0.0745 0.0856 -0.0006 -0.0153 -0.0155 195 PRO A C   
1708 O  O   . PRO A 194 ? 0.0838 0.0956 0.0709 0.0093  -0.0071 -0.0063 195 PRO A O   
1709 C  CB  . PRO A 194 ? 0.1049 0.0992 0.0870 -0.0037 -0.0051 -0.0277 195 PRO A CB  
1710 C  CG  . PRO A 194 ? 0.1113 0.1275 0.0781 -0.0035 -0.0083 -0.0231 195 PRO A CG  
1711 C  CD  . PRO A 194 ? 0.1006 0.1332 0.0690 -0.0052 -0.0017 -0.0137 195 PRO A CD  
1712 N  N   . GLY A 195 ? 0.0771 0.0825 0.0673 0.0012  0.0017  -0.0041 196 GLY A N   
1713 C  CA  . GLY A 195 ? 0.0743 0.0814 0.0769 0.0034  0.0071  -0.0041 196 GLY A CA  
1714 C  C   . GLY A 195 ? 0.0668 0.0740 0.0825 0.0006  -0.0068 -0.0027 196 GLY A C   
1715 O  O   . GLY A 195 ? 0.0768 0.0753 0.0847 -0.0024 -0.0003 -0.0107 196 GLY A O   
1716 N  N   . SER A 196 ? 0.0648 0.0793 0.0742 -0.0020 0.0030  -0.0096 197 SER A N   
1717 C  CA  . SER A 196 ? 0.0649 0.0799 0.0796 -0.0054 0.0028  -0.0082 197 SER A CA  
1718 C  C   . SER A 196 ? 0.0601 0.0646 0.0860 0.0049  -0.0074 -0.0041 197 SER A C   
1719 O  O   . SER A 196 ? 0.0597 0.0708 0.0821 -0.0040 -0.0010 -0.0055 197 SER A O   
1720 C  CB  . SER A 196 ? 0.0738 0.0814 0.0879 -0.0071 -0.0013 -0.0081 197 SER A CB  
1721 O  OG  . SER A 196 ? 0.0665 0.0754 0.0863 0.0024  -0.0038 -0.0049 197 SER A OG  
1722 N  N   . LEU A 197 ? 0.0664 0.0671 0.0789 -0.0057 0.0081  -0.0024 198 LEU A N   
1723 C  CA  . LEU A 197 ? 0.0666 0.0770 0.0784 -0.0003 0.0013  0.0035  198 LEU A CA  
1724 C  C   . LEU A 197 ? 0.0617 0.0703 0.0702 -0.0015 0.0043  0.0054  198 LEU A C   
1725 O  O   . LEU A 197 ? 0.0594 0.0855 0.0793 0.0006  -0.0006 -0.0031 198 LEU A O   
1726 C  CB  . LEU A 197 ? 0.0762 0.0813 0.0859 -0.0010 0.0059  -0.0035 198 LEU A CB  
1727 C  CG  . LEU A 197 ? 0.0920 0.0734 0.1011 -0.0049 -0.0003 0.0120  198 LEU A CG  
1728 C  CD1 . LEU A 197 ? 0.1046 0.0917 0.1317 -0.0151 -0.0077 0.0283  198 LEU A CD1 
1729 C  CD2 . LEU A 197 ? 0.0839 0.0884 0.0967 0.0086  0.0059  0.0026  198 LEU A CD2 
1730 N  N   . THR A 198 ? 0.0655 0.0645 0.0778 -0.0017 0.0000  -0.0013 199 THR A N   
1731 C  CA  . THR A 198 ? 0.0572 0.0738 0.0785 0.0052  0.0000  -0.0063 199 THR A CA  
1732 C  C   . THR A 198 ? 0.0682 0.0782 0.0865 -0.0044 -0.0121 -0.0030 199 THR A C   
1733 O  O   . THR A 198 ? 0.0663 0.0791 0.0913 0.0027  -0.0003 0.0043  199 THR A O   
1734 C  CB  . THR A 198 ? 0.0615 0.0803 0.0688 -0.0008 -0.0013 -0.0020 199 THR A CB  
1735 O  OG1 . THR A 198 ? 0.0653 0.0698 0.0715 -0.0005 -0.0049 0.0026  199 THR A OG1 
1736 C  CG2 . THR A 198 ? 0.0728 0.0789 0.0847 -0.0052 0.0035  -0.0031 199 THR A CG2 
1737 N  N   . HIS A 199 ? 0.0608 0.0796 0.0899 -0.0044 0.0000  -0.0034 200 HIS A N   
1738 C  CA  . HIS A 199 ? 0.0738 0.0917 0.0936 -0.0146 0.0073  -0.0008 200 HIS A CA  
1739 C  C   . HIS A 199 ? 0.0646 0.0983 0.0857 -0.0051 -0.0008 -0.0051 200 HIS A C   
1740 O  O   . HIS A 199 ? 0.0736 0.0930 0.0861 -0.0080 -0.0003 0.0040  200 HIS A O   
1741 C  CB  . HIS A 199 ? 0.0653 0.1107 0.0948 -0.0003 0.0049  -0.0066 200 HIS A CB  
1742 C  CG  . HIS A 199 ? 0.0945 0.0935 0.0992 0.0035  0.0062  -0.0131 200 HIS A CG  
1743 N  ND1 . HIS A 199 ? 0.1000 0.1225 0.2085 0.0006  -0.0425 -0.0452 200 HIS A ND1 
1744 C  CD2 . HIS A 199 ? 0.1441 0.1377 0.1288 0.0223  0.0028  0.0044  200 HIS A CD2 
1745 C  CE1 . HIS A 199 ? 0.1077 0.1456 0.1475 0.0305  -0.0421 -0.0207 200 HIS A CE1 
1746 N  NE2 . HIS A 199 ? 0.1738 0.1414 0.1138 0.0571  -0.0427 -0.0109 200 HIS A NE2 
1747 N  N   . PRO A 200 ? 0.0694 0.1044 0.0954 -0.0073 0.0015  -0.0019 201 PRO A N   
1748 C  CA  . PRO A 200 ? 0.0672 0.1174 0.1022 -0.0194 -0.0031 -0.0010 201 PRO A CA  
1749 C  C   . PRO A 200 ? 0.0874 0.1077 0.0963 -0.0295 0.0155  0.0076  201 PRO A C   
1750 O  O   . PRO A 200 ? 0.0955 0.1238 0.1035 -0.0212 -0.0040 0.0187  201 PRO A O   
1751 C  CB  . PRO A 200 ? 0.0714 0.1379 0.1307 -0.0245 0.0089  0.0020  201 PRO A CB  
1752 C  CG  . PRO A 200 ? 0.0709 0.1384 0.1368 -0.0127 0.0052  -0.0044 201 PRO A CG  
1753 C  CD  . PRO A 200 ? 0.0544 0.1282 0.1196 -0.0052 0.0098  -0.0173 201 PRO A CD  
1754 N  N   . PRO A 201 ? 0.0794 0.1134 0.1146 -0.0143 0.0038  0.0110  202 PRO A N   
1755 C  CA  . PRO A 201 ? 0.0961 0.1067 0.1054 -0.0167 0.0086  0.0054  202 PRO A CA  
1756 C  C   . PRO A 201 ? 0.0685 0.0997 0.1208 -0.0104 0.0000  -0.0108 202 PRO A C   
1757 O  O   . PRO A 201 ? 0.0910 0.1087 0.1316 -0.0253 0.0063  -0.0049 202 PRO A O   
1758 C  CB  . PRO A 201 ? 0.1155 0.1075 0.1517 -0.0339 0.0096  0.0147  202 PRO A CB  
1759 C  CG  . PRO A 201 ? 0.1256 0.1199 0.1662 -0.0116 0.0092  0.0167  202 PRO A CG  
1760 C  CD  . PRO A 201 ? 0.0998 0.1102 0.1465 -0.0137 -0.0096 0.0194  202 PRO A CD  
1761 N  N   . LEU A 202 ? 0.0732 0.0898 0.1052 -0.0082 0.0065  -0.0021 203 LEU A N   
1762 C  CA  . LEU A 202 ? 0.0659 0.0896 0.1036 -0.0063 0.0006  -0.0049 203 LEU A CA  
1763 C  C   . LEU A 202 ? 0.0690 0.0873 0.0935 -0.0164 0.0012  -0.0034 203 LEU A C   
1764 O  O   . LEU A 202 ? 0.0758 0.0914 0.1124 -0.0041 0.0044  -0.0172 203 LEU A O   
1765 C  CB  . LEU A 202 ? 0.0636 0.0890 0.1157 -0.0008 -0.0020 -0.0096 203 LEU A CB  
1766 C  CG  . LEU A 202 ? 0.0738 0.0952 0.0995 0.0015  0.0080  -0.0136 203 LEU A CG  
1767 C  CD1 . LEU A 202 ? 0.0662 0.1325 0.1729 0.0017  -0.0065 -0.0215 203 LEU A CD1 
1768 C  CD2 . LEU A 202 ? 0.0760 0.0974 0.1157 -0.0032 -0.0023 -0.0070 203 LEU A CD2 
1769 N  N   . TYR A 203 ? 0.0772 0.0813 0.1121 -0.0087 0.0031  -0.0107 204 TYR A N   
1770 C  CA  . TYR A 203 ? 0.0763 0.0926 0.1147 -0.0125 0.0065  -0.0132 204 TYR A CA  
1771 C  C   . TYR A 203 ? 0.0715 0.0793 0.1048 -0.0071 0.0024  -0.0105 204 TYR A C   
1772 O  O   . TYR A 203 ? 0.0751 0.0771 0.1005 -0.0113 -0.0017 -0.0077 204 TYR A O   
1773 C  CB  . TYR A 203 ? 0.0952 0.0812 0.1392 -0.0074 0.0035  0.0049  204 TYR A CB  
1774 C  CG  . TYR A 203 ? 0.1243 0.0898 0.1395 0.0027  0.0239  0.0055  204 TYR A CG  
1775 C  CD1 . TYR A 203 ? 0.1246 0.1113 0.1775 -0.0296 0.0318  0.0038  204 TYR A CD1 
1776 C  CD2 . TYR A 203 ? 0.1473 0.1431 0.1870 0.0198  0.0256  0.0590  204 TYR A CD2 
1777 C  CE1 . TYR A 203 ? 0.1640 0.1363 0.2119 -0.0342 0.0825  0.0230  204 TYR A CE1 
1778 C  CE2 . TYR A 203 ? 0.2150 0.1616 0.2201 0.0120  0.0646  0.0715  204 TYR A CE2 
1779 C  CZ  . TYR A 203 ? 0.1996 0.1299 0.2269 -0.0162 0.0799  0.0445  204 TYR A CZ  
1780 O  OH  . TYR A 203 ? 0.3061 0.1844 0.3192 0.0054  0.1380  0.1190  204 TYR A OH  
1781 N  N   . GLU A 204 ? 0.0749 0.0860 0.1031 -0.0073 0.0037  -0.0116 205 GLU A N   
1782 C  CA  . GLU A 204 ? 0.0877 0.0780 0.1120 -0.0109 -0.0127 -0.0175 205 GLU A CA  
1783 C  C   . GLU A 204 ? 0.0974 0.0834 0.0927 -0.0080 -0.0026 -0.0181 205 GLU A C   
1784 O  O   . GLU A 204 ? 0.1120 0.1169 0.0998 0.0245  -0.0175 -0.0281 205 GLU A O   
1785 C  CB  . GLU A 204 ? 0.0888 0.1069 0.1053 0.0008  -0.0287 -0.0219 205 GLU A CB  
1786 C  CG  . GLU A 204 ? 0.0905 0.0996 0.1061 -0.0032 -0.0148 -0.0143 205 GLU A CG  
1787 C  CD  . GLU A 204 ? 0.0953 0.1084 0.1106 -0.0116 -0.0120 -0.0206 205 GLU A CD  
1788 O  OE1 . GLU A 204 ? 0.1108 0.1219 0.1393 -0.0065 -0.0351 -0.0297 205 GLU A OE1 
1789 O  OE2 . GLU A 204 ? 0.0865 0.1254 0.1120 0.0020  -0.0142 -0.0161 205 GLU A OE2 
1790 N  N   . CYS A 205 ? 0.0822 0.0744 0.0973 -0.0098 -0.0027 -0.0122 206 CYS A N   
1791 C  CA  . CYS A 205 ? 0.0811 0.0771 0.1001 0.0057  -0.0003 -0.0087 206 CYS A CA  
1792 C  C   . CYS A 205 ? 0.0816 0.0733 0.0831 -0.0006 -0.0034 -0.0068 206 CYS A C   
1793 O  O   . CYS A 205 ? 0.0864 0.0722 0.1136 0.0028  -0.0116 -0.0049 206 CYS A O   
1794 C  CB  . CYS A 205 ? 0.1154 0.0830 0.1045 -0.0195 -0.0012 0.0017  206 CYS A CB  
1795 S  SG  . CYS A 205 ? 0.0986 0.0895 0.0965 -0.0063 0.0015  -0.0027 206 CYS A SG  
1796 N  N   . VAL A 206 ? 0.0791 0.0625 0.0869 -0.0019 0.0057  -0.0006 207 VAL A N   
1797 C  CA  . VAL A 206 ? 0.0768 0.0627 0.0866 -0.0089 -0.0019 -0.0015 207 VAL A CA  
1798 C  C   . VAL A 206 ? 0.0793 0.0641 0.0781 0.0034  -0.0051 -0.0023 207 VAL A C   
1799 O  O   . VAL A 206 ? 0.0843 0.0858 0.1005 0.0017  -0.0007 0.0115  207 VAL A O   
1800 C  CB  . VAL A 206 ? 0.0806 0.0747 0.0936 0.0071  0.0017  -0.0065 207 VAL A CB  
1801 C  CG1 . VAL A 206 ? 0.0811 0.0732 0.0883 -0.0041 -0.0093 -0.0060 207 VAL A CG1 
1802 C  CG2 . VAL A 206 ? 0.0846 0.0744 0.1023 -0.0021 0.0120  -0.0077 207 VAL A CG2 
1803 N  N   . THR A 207 ? 0.0659 0.0599 0.0900 0.0032  -0.0043 -0.0015 208 THR A N   
1804 C  CA  . THR A 207 ? 0.0766 0.0716 0.0831 -0.0034 0.0037  0.0017  208 THR A CA  
1805 C  C   . THR A 207 ? 0.0678 0.0692 0.0678 0.0000  0.0015  0.0057  208 THR A C   
1806 O  O   . THR A 207 ? 0.0812 0.0641 0.0769 0.0038  -0.0070 0.0005  208 THR A O   
1807 C  CB  . THR A 207 ? 0.0935 0.0615 0.0984 0.0000  0.0082  -0.0093 208 THR A CB  
1808 O  OG1 . THR A 207 ? 0.1020 0.0749 0.1035 0.0077  0.0049  -0.0122 208 THR A OG1 
1809 C  CG2 . THR A 207 ? 0.0934 0.0997 0.1043 -0.0003 0.0266  0.0005  208 THR A CG2 
1810 N  N   . TRP A 208 ? 0.0700 0.0647 0.0741 0.0034  -0.0041 0.0071  209 TRP A N   
1811 C  CA  . TRP A 208 ? 0.0634 0.0636 0.0697 -0.0008 -0.0044 -0.0006 209 TRP A CA  
1812 C  C   . TRP A 208 ? 0.0696 0.0572 0.0697 0.0059  -0.0038 -0.0015 209 TRP A C   
1813 O  O   . TRP A 208 ? 0.0758 0.0719 0.0629 0.0005  0.0019  0.0000  209 TRP A O   
1814 C  CB  . TRP A 208 ? 0.0702 0.0604 0.0679 0.0057  -0.0020 0.0054  209 TRP A CB  
1815 C  CG  . TRP A 208 ? 0.0592 0.0639 0.0814 0.0063  -0.0076 0.0000  209 TRP A CG  
1816 C  CD1 . TRP A 208 ? 0.0702 0.0727 0.0831 0.0080  0.0020  0.0000  209 TRP A CD1 
1817 C  CD2 . TRP A 208 ? 0.0690 0.0606 0.0715 0.0060  0.0017  0.0008  209 TRP A CD2 
1818 N  NE1 . TRP A 208 ? 0.0691 0.0753 0.0949 0.0027  0.0005  0.0060  209 TRP A NE1 
1819 C  CE2 . TRP A 208 ? 0.0683 0.0649 0.0833 0.0078  -0.0027 0.0052  209 TRP A CE2 
1820 C  CE3 . TRP A 208 ? 0.0812 0.0610 0.0725 0.0054  -0.0035 0.0015  209 TRP A CE3 
1821 C  CZ2 . TRP A 208 ? 0.0850 0.0706 0.0803 0.0201  0.0078  0.0076  209 TRP A CZ2 
1822 C  CZ3 . TRP A 208 ? 0.0904 0.0714 0.0830 0.0119  -0.0043 0.0003  209 TRP A CZ3 
1823 C  CH2 . TRP A 208 ? 0.0989 0.0736 0.0822 0.0242  0.0052  -0.0032 209 TRP A CH2 
1824 N  N   . ILE A 209 ? 0.0638 0.0636 0.0727 0.0027  -0.0023 0.0012  210 ILE A N   
1825 C  CA  . ILE A 209 ? 0.0638 0.0635 0.0814 0.0010  -0.0065 0.0010  210 ILE A CA  
1826 C  C   . ILE A 209 ? 0.0638 0.0679 0.0673 0.0043  -0.0034 0.0059  210 ILE A C   
1827 O  O   . ILE A 209 ? 0.0992 0.0679 0.0671 0.0017  -0.0015 0.0057  210 ILE A O   
1828 C  CB  . ILE A 209 ? 0.0706 0.0673 0.0944 0.0087  0.0023  0.0008  210 ILE A CB  
1829 C  CG1 . ILE A 209 ? 0.0850 0.0835 0.1216 0.0188  -0.0108 -0.0082 210 ILE A CG1 
1830 C  CG2 . ILE A 209 ? 0.0680 0.0971 0.1054 0.0049  0.0013  0.0104  210 ILE A CG2 
1831 C  CD1 . ILE A 209 ? 0.1041 0.0874 0.1685 0.0285  -0.0068 0.0012  210 ILE A CD1 
1832 N  N   . VAL A 210 ? 0.0681 0.0678 0.0663 0.0013  -0.0013 0.0054  211 VAL A N   
1833 C  CA  . VAL A 210 ? 0.0747 0.0647 0.0681 -0.0006 -0.0020 0.0005  211 VAL A CA  
1834 C  C   . VAL A 210 ? 0.0707 0.0675 0.0673 -0.0008 0.0010  0.0031  211 VAL A C   
1835 O  O   . VAL A 210 ? 0.0788 0.0874 0.0696 -0.0135 -0.0006 0.0081  211 VAL A O   
1836 C  CB  . VAL A 210 ? 0.0711 0.0714 0.0869 -0.0020 -0.0010 0.0037  211 VAL A CB  
1837 C  CG1 . VAL A 210 ? 0.0926 0.0770 0.1027 0.0028  -0.0031 0.0028  211 VAL A CG1 
1838 C  CG2 . VAL A 210 ? 0.0702 0.0830 0.1196 0.0017  -0.0024 0.0051  211 VAL A CG2 
1839 N  N   . LEU A 211 ? 0.0724 0.0841 0.0720 -0.0060 0.0026  0.0027  212 LEU A N   
1840 C  CA  . LEU A 211 ? 0.0743 0.0847 0.0768 -0.0093 -0.0057 0.0040  212 LEU A CA  
1841 C  C   . LEU A 211 ? 0.0668 0.0969 0.0753 -0.0068 -0.0087 -0.0003 212 LEU A C   
1842 O  O   . LEU A 211 ? 0.0869 0.0928 0.0894 -0.0013 -0.0006 0.0043  212 LEU A O   
1843 C  CB  . LEU A 211 ? 0.0811 0.0998 0.0775 -0.0076 -0.0074 0.0071  212 LEU A CB  
1844 C  CG  . LEU A 211 ? 0.0768 0.1052 0.0980 -0.0043 -0.0107 0.0140  212 LEU A CG  
1845 C  CD1 . LEU A 211 ? 0.0838 0.1527 0.1121 0.0017  -0.0186 0.0189  212 LEU A CD1 
1846 C  CD2 . LEU A 211 ? 0.0952 0.1098 0.1093 0.0065  0.0059  0.0173  212 LEU A CD2 
1847 N  N   . LYS A 212 ? 0.0863 0.1005 0.0791 -0.0175 -0.0020 0.0146  213 LYS A N   
1848 C  CA  . LYS A 212 ? 0.1096 0.0970 0.1026 -0.0183 -0.0035 0.0225  213 LYS A CA  
1849 C  C   . LYS A 212 ? 0.0961 0.0896 0.0896 -0.0100 -0.0068 0.0242  213 LYS A C   
1850 O  O   . LYS A 212 ? 0.1096 0.0908 0.1497 -0.0015 -0.0383 0.0186  213 LYS A O   
1851 C  CB  . LYS A 212 ? 0.1439 0.1323 0.0899 -0.0533 -0.0017 0.0231  213 LYS A CB  
1852 C  CG  . LYS A 212 ? 0.1660 0.1520 0.1378 -0.0310 -0.0057 0.0348  213 LYS A CG  
1853 C  CD  . LYS A 212 ? 0.2694 0.2594 0.1679 -0.0653 0.0130  0.1189  213 LYS A CD  
1854 C  CE  . LYS A 212 ? 0.4595 0.2804 0.2367 -0.0230 0.1115  0.1030  213 LYS A CE  
1855 N  NZ  . LYS A 212 ? 0.7031 0.6409 0.2994 -0.0103 0.1162  0.0887  213 LYS A NZ  
1856 N  N   A GLU A 213 ? 0.0735 0.1071 0.0749 -0.0129 0.0028  0.0085  214 GLU A N   
1857 N  N   B GLU A 213 ? 0.0873 0.0916 0.0841 -0.0003 -0.0020 0.0083  214 GLU A N   
1858 C  CA  A GLU A 213 ? 0.0776 0.0754 0.0886 -0.0115 -0.0066 0.0176  214 GLU A CA  
1859 C  CA  B GLU A 213 ? 0.0956 0.0894 0.1060 0.0003  -0.0103 -0.0055 214 GLU A CA  
1860 C  C   A GLU A 213 ? 0.0948 0.0776 0.0858 -0.0055 -0.0115 0.0076  214 GLU A C   
1861 C  C   B GLU A 213 ? 0.0976 0.0834 0.1086 -0.0080 -0.0193 0.0074  214 GLU A C   
1862 O  O   A GLU A 213 ? 0.0900 0.0711 0.0670 -0.0071 -0.0026 0.0046  214 GLU A O   
1863 O  O   B GLU A 213 ? 0.0912 0.0727 0.0885 -0.0003 0.0113  0.0017  214 GLU A O   
1864 C  CB  A GLU A 213 ? 0.0671 0.1002 0.1004 -0.0152 -0.0074 -0.0130 214 GLU A CB  
1865 C  CB  B GLU A 213 ? 0.1025 0.0844 0.1063 -0.0097 0.0038  0.0200  214 GLU A CB  
1866 C  CG  A GLU A 213 ? 0.0726 0.0830 0.1007 -0.0076 0.0027  0.0048  214 GLU A CG  
1867 C  CG  B GLU A 213 ? 0.1114 0.1236 0.1688 -0.0097 -0.0277 -0.0160 214 GLU A CG  
1868 C  CD  A GLU A 213 ? 0.0820 0.0961 0.1216 -0.0114 -0.0195 -0.0132 214 GLU A CD  
1869 C  CD  B GLU A 213 ? 0.1113 0.1331 0.1636 -0.0113 -0.0074 -0.0136 214 GLU A CD  
1870 O  OE1 A GLU A 213 ? 0.1119 0.1313 0.1396 -0.0137 -0.0329 0.0260  214 GLU A OE1 
1871 O  OE1 B GLU A 213 ? 0.0961 0.1419 0.1206 -0.0028 -0.0063 -0.0054 214 GLU A OE1 
1872 O  OE2 A GLU A 213 ? 0.0934 0.1310 0.1074 -0.0105 -0.0065 -0.0115 214 GLU A OE2 
1873 O  OE2 B GLU A 213 ? 0.1348 0.1703 0.2644 -0.0373 -0.0020 -0.0434 214 GLU A OE2 
1874 N  N   A PRO A 214 ? 0.0867 0.0732 0.0970 -0.0080 -0.0083 0.0034  215 PRO A N   
1875 N  N   B PRO A 214 ? 0.1072 0.0729 0.1070 -0.0082 -0.0038 0.0113  215 PRO A N   
1876 C  CA  A PRO A 214 ? 0.0891 0.0722 0.0988 -0.0082 -0.0068 -0.0010 215 PRO A CA  
1877 C  CA  B PRO A 214 ? 0.1127 0.1000 0.0981 -0.0010 -0.0066 -0.0006 215 PRO A CA  
1878 C  C   A PRO A 214 ? 0.0795 0.0759 0.1050 -0.0006 -0.0065 -0.0114 215 PRO A C   
1879 C  C   B PRO A 214 ? 0.1093 0.0715 0.1130 -0.0078 -0.0107 0.0007  215 PRO A C   
1880 O  O   A PRO A 214 ? 0.0812 0.0891 0.1095 -0.0091 0.0027  -0.0038 215 PRO A O   
1881 O  O   B PRO A 214 ? 0.1125 0.1015 0.1152 -0.0130 -0.0063 -0.0076 215 PRO A O   
1882 C  CB  A PRO A 214 ? 0.1030 0.0778 0.0981 0.0043  -0.0120 0.0044  215 PRO A CB  
1883 C  CB  B PRO A 214 ? 0.1418 0.0890 0.1234 0.0093  -0.0054 0.0007  215 PRO A CB  
1884 C  CG  A PRO A 214 ? 0.1062 0.0876 0.1307 -0.0109 0.0006  0.0059  215 PRO A CG  
1885 C  CG  B PRO A 214 ? 0.1494 0.1231 0.1445 0.0105  0.0103  0.0421  215 PRO A CG  
1886 C  CD  A PRO A 214 ? 0.1222 0.0771 0.1059 -0.0026 -0.0181 -0.0001 215 PRO A CD  
1887 C  CD  B PRO A 214 ? 0.1076 0.0717 0.1330 -0.0054 0.0070  0.0100  215 PRO A CD  
1888 N  N   . ILE A 215 ? 0.0931 0.1000 0.0870 -0.0065 -0.0041 -0.0068 216 ILE A N   
1889 C  CA  . ILE A 215 ? 0.0919 0.0877 0.1020 -0.0041 -0.0098 -0.0089 216 ILE A CA  
1890 C  C   . ILE A 215 ? 0.0877 0.0904 0.0961 -0.0060 -0.0114 -0.0037 216 ILE A C   
1891 O  O   . ILE A 215 ? 0.0988 0.0877 0.1379 -0.0103 -0.0094 -0.0178 216 ILE A O   
1892 C  CB  . ILE A 215 ? 0.1229 0.0890 0.0935 0.0111  -0.0062 -0.0070 216 ILE A CB  
1893 C  CG1 . ILE A 215 ? 0.1116 0.0970 0.0918 -0.0005 0.0051  0.0038  216 ILE A CG1 
1894 C  CG2 . ILE A 215 ? 0.1093 0.1050 0.1172 0.0043  -0.0007 -0.0124 216 ILE A CG2 
1895 C  CD1 . ILE A 215 ? 0.1409 0.1143 0.1137 -0.0076 0.0008  0.0138  216 ILE A CD1 
1896 N  N   A SER A 216 ? 0.1138 0.0903 0.1182 -0.0197 -0.0234 0.0007  217 SER A N   
1897 N  N   B SER A 216 ? 0.1011 0.0918 0.1053 -0.0080 -0.0125 -0.0054 217 SER A N   
1898 C  CA  A SER A 216 ? 0.1011 0.0955 0.1034 -0.0092 -0.0326 -0.0019 217 SER A CA  
1899 C  CA  B SER A 216 ? 0.1614 0.0513 0.1137 -0.0137 -0.0186 -0.0200 217 SER A CA  
1900 C  C   A SER A 216 ? 0.1173 0.0728 0.1055 -0.0078 -0.0164 -0.0043 217 SER A C   
1901 C  C   B SER A 216 ? 0.1150 0.0758 0.1142 -0.0100 -0.0254 -0.0051 217 SER A C   
1902 O  O   A SER A 216 ? 0.1155 0.0988 0.0923 0.0035  -0.0001 0.0013  217 SER A O   
1903 O  O   B SER A 216 ? 0.1068 0.1034 0.1228 0.0000  -0.0120 0.0122  217 SER A O   
1904 C  CB  A SER A 216 ? 0.0996 0.0715 0.1025 0.0066  -0.0260 -0.0149 217 SER A CB  
1905 C  CB  B SER A 216 ? 0.1634 0.1049 0.2179 -0.0199 -0.0099 0.0313  217 SER A CB  
1906 O  OG  A SER A 216 ? 0.1556 0.1022 0.1176 -0.0425 -0.0175 0.0070  217 SER A OG  
1907 O  OG  B SER A 216 ? 0.1747 0.1955 0.3050 0.0043  -0.0292 0.0048  217 SER A OG  
1908 N  N   . VAL A 217 ? 0.1210 0.0712 0.1136 -0.0082 -0.0157 -0.0154 218 VAL A N   
1909 C  CA  . VAL A 217 ? 0.1137 0.0712 0.1104 0.0000  -0.0103 -0.0015 218 VAL A CA  
1910 C  C   . VAL A 217 ? 0.1207 0.0667 0.1239 -0.0043 -0.0163 -0.0096 218 VAL A C   
1911 O  O   . VAL A 217 ? 0.1336 0.0747 0.1162 -0.0098 -0.0196 -0.0006 218 VAL A O   
1912 C  CB  . VAL A 217 ? 0.1290 0.0688 0.1335 -0.0066 -0.0307 -0.0020 218 VAL A CB  
1913 C  CG1 . VAL A 217 ? 0.1471 0.0768 0.1494 -0.0190 -0.0337 -0.0135 218 VAL A CG1 
1914 C  CG2 . VAL A 217 ? 0.1228 0.0873 0.1826 -0.0082 -0.0168 -0.0154 218 VAL A CG2 
1915 N  N   . SER A 218 ? 0.1251 0.0800 0.1110 -0.0132 -0.0129 -0.0218 219 SER A N   
1916 C  CA  . SER A 218 ? 0.1412 0.0706 0.1304 -0.0178 -0.0091 -0.0147 219 SER A CA  
1917 C  C   . SER A 218 ? 0.1439 0.0775 0.1182 -0.0189 -0.0186 -0.0141 219 SER A C   
1918 O  O   . SER A 218 ? 0.1323 0.0868 0.1325 -0.0052 -0.0211 -0.0089 219 SER A O   
1919 C  CB  . SER A 218 ? 0.1510 0.0902 0.1162 -0.0304 -0.0223 -0.0087 219 SER A CB  
1920 O  OG  . SER A 218 ? 0.1525 0.0986 0.1231 -0.0182 -0.0113 -0.0006 219 SER A OG  
1921 N  N   A SER A 219 ? 0.1244 0.0639 0.1180 -0.0198 -0.0098 0.0046  220 SER A N   
1922 N  N   B SER A 219 ? 0.1447 0.0934 0.1180 0.0302  0.0157  0.0118  220 SER A N   
1923 C  CA  A SER A 219 ? 0.1271 0.0612 0.1316 -0.0024 -0.0131 -0.0092 220 SER A CA  
1924 C  CA  B SER A 219 ? 0.1568 0.0921 0.1357 -0.0007 0.0074  -0.0049 220 SER A CA  
1925 C  C   A SER A 219 ? 0.1248 0.0768 0.1432 0.0080  -0.0143 -0.0021 220 SER A C   
1926 C  C   B SER A 219 ? 0.1341 0.0936 0.1430 -0.0073 -0.0130 -0.0027 220 SER A C   
1927 O  O   A SER A 219 ? 0.1488 0.0930 0.1288 -0.0085 0.0282  0.0104  220 SER A O   
1928 O  O   B SER A 219 ? 0.1136 0.1233 0.1323 0.0010  -0.0043 -0.0152 220 SER A O   
1929 C  CB  A SER A 219 ? 0.1827 0.0709 0.1477 0.0116  0.0012  0.0078  220 SER A CB  
1930 C  CB  B SER A 219 ? 0.1565 0.1120 0.1420 -0.0008 0.0194  -0.0073 220 SER A CB  
1931 O  OG  A SER A 219 ? 0.1773 0.0833 0.1458 0.0166  -0.0012 0.0006  220 SER A OG  
1932 O  OG  B SER A 219 ? 0.1785 0.1074 0.1618 0.0368  -0.0153 -0.0253 220 SER A OG  
1933 N  N   . GLU A 220 ? 0.1523 0.0910 0.1361 0.0006  -0.0121 -0.0043 221 GLU A N   
1934 C  CA  . GLU A 220 ? 0.1551 0.1186 0.1243 0.0120  -0.0110 -0.0142 221 GLU A CA  
1935 C  C   . GLU A 220 ? 0.1641 0.1054 0.1280 0.0170  -0.0175 0.0068  221 GLU A C   
1936 O  O   . GLU A 220 ? 0.1649 0.1337 0.1519 0.0132  0.0219  0.0076  221 GLU A O   
1937 C  CB  . GLU A 220 ? 0.2067 0.1477 0.1564 0.0168  -0.0206 -0.0259 221 GLU A CB  
1938 C  CG  . GLU A 220 ? 0.2741 0.1807 0.1771 0.0023  -0.0472 -0.0414 221 GLU A CG  
1939 C  CD  . GLU A 220 ? 0.3129 0.1500 0.1904 -0.0188 -0.0718 -0.0734 221 GLU A CD  
1940 O  OE1 . GLU A 220 ? 0.2581 0.1347 0.2037 -0.0342 -0.0293 -0.0410 221 GLU A OE1 
1941 O  OE2 . GLU A 220 ? 0.6075 0.1708 0.2858 -0.0553 -0.0340 -0.0816 221 GLU A OE2 
1942 N  N   . GLN A 221 ? 0.1262 0.0974 0.1262 0.0133  -0.0087 -0.0113 222 GLN A N   
1943 C  CA  . GLN A 221 ? 0.1393 0.0890 0.1277 -0.0020 -0.0065 0.0125  222 GLN A CA  
1944 C  C   . GLN A 221 ? 0.1237 0.1102 0.1175 0.0000  -0.0088 0.0073  222 GLN A C   
1945 O  O   . GLN A 221 ? 0.1393 0.1213 0.1230 -0.0092 0.0007  0.0171  222 GLN A O   
1946 C  CB  . GLN A 221 ? 0.1094 0.0976 0.1203 -0.0020 -0.0037 0.0000  222 GLN A CB  
1947 C  CG  . GLN A 221 ? 0.1297 0.0958 0.1196 -0.0048 -0.0103 -0.0051 222 GLN A CG  
1948 C  CD  . GLN A 221 ? 0.1156 0.0930 0.1034 -0.0198 -0.0068 -0.0086 222 GLN A CD  
1949 O  OE1 . GLN A 221 ? 0.1202 0.0851 0.1176 -0.0010 -0.0116 -0.0020 222 GLN A OE1 
1950 N  NE2 . GLN A 221 ? 0.1226 0.0974 0.1413 -0.0012 -0.0276 0.0054  222 GLN A NE2 
1951 N  N   . VAL A 222 ? 0.1327 0.1048 0.1199 0.0032  -0.0146 0.0126  223 VAL A N   
1952 C  CA  . VAL A 222 ? 0.1368 0.1262 0.1273 -0.0166 -0.0183 0.0142  223 VAL A CA  
1953 C  C   . VAL A 222 ? 0.1261 0.1272 0.1527 -0.0065 -0.0197 0.0147  223 VAL A C   
1954 O  O   . VAL A 222 ? 0.1269 0.1281 0.1504 -0.0131 -0.0087 0.0197  223 VAL A O   
1955 C  CB  . VAL A 222 ? 0.1377 0.1343 0.1435 -0.0019 -0.0111 0.0144  223 VAL A CB  
1956 C  CG1 . VAL A 222 ? 0.1842 0.1621 0.1974 -0.0193 -0.0322 0.0401  223 VAL A CG1 
1957 C  CG2 . VAL A 222 ? 0.1803 0.1501 0.1407 -0.0170 -0.0175 0.0264  223 VAL A CG2 
1958 N  N   A LEU A 223 ? 0.1217 0.1243 0.1464 0.0000  -0.0076 0.0086  224 LEU A N   
1959 N  N   B LEU A 223 ? 0.1371 0.1111 0.1671 -0.0052 -0.0108 0.0088  224 LEU A N   
1960 C  CA  A LEU A 223 ? 0.1518 0.1199 0.1912 0.0264  -0.0031 -0.0171 224 LEU A CA  
1961 C  CA  B LEU A 223 ? 0.1649 0.1441 0.1974 -0.0179 0.0148  -0.0060 224 LEU A CA  
1962 C  C   A LEU A 223 ? 0.1342 0.1484 0.1632 0.0097  0.0001  -0.0163 224 LEU A C   
1963 C  C   B LEU A 223 ? 0.1430 0.1416 0.1564 0.0066  -0.0032 -0.0129 224 LEU A C   
1964 O  O   A LEU A 223 ? 0.1328 0.1694 0.1965 0.0071  0.0263  -0.0074 224 LEU A O   
1965 O  O   B LEU A 223 ? 0.1377 0.1720 0.1909 0.0049  0.0219  -0.0052 224 LEU A O   
1966 C  CB  A LEU A 223 ? 0.1596 0.1254 0.1952 0.0197  -0.0020 -0.0166 224 LEU A CB  
1967 C  CB  B LEU A 223 ? 0.2391 0.1676 0.2480 -0.0412 -0.0074 -0.0399 224 LEU A CB  
1968 C  CG  A LEU A 223 ? 0.2004 0.1529 0.1512 -0.0077 0.0465  0.0167  224 LEU A CG  
1969 C  CG  B LEU A 223 ? 0.3377 0.2390 0.3479 0.0307  0.0725  -0.1216 224 LEU A CG  
1970 C  CD1 A LEU A 223 ? 0.3097 0.1483 0.3070 -0.0460 0.0274  -0.1093 224 LEU A CD1 
1971 C  CD1 B LEU A 223 ? 0.4255 0.3012 0.1562 -0.0644 0.0976  0.0176  224 LEU A CD1 
1972 C  CD2 A LEU A 223 ? 0.2180 0.1915 0.2166 0.0604  0.0285  -0.0573 224 LEU A CD2 
1973 C  CD2 B LEU A 223 ? 0.3533 0.2168 0.2113 0.0680  0.0333  -0.1137 224 LEU A CD2 
1974 N  N   . LYS A 224 ? 0.1297 0.1604 0.1321 0.0133  -0.0020 0.0015  225 LYS A N   
1975 C  CA  . LYS A 224 ? 0.1254 0.1673 0.1244 -0.0168 0.0017  0.0059  225 LYS A CA  
1976 C  C   . LYS A 224 ? 0.1284 0.1456 0.1062 0.0119  0.0060  0.0219  225 LYS A C   
1977 O  O   . LYS A 224 ? 0.1322 0.1543 0.1155 -0.0035 0.0038  0.0121  225 LYS A O   
1978 C  CB  . LYS A 224 ? 0.1464 0.2019 0.1477 0.0098  -0.0245 0.0281  225 LYS A CB  
1979 C  CG  . LYS A 224 ? 0.1651 0.2624 0.1717 -0.0467 -0.0412 0.0041  225 LYS A CG  
1980 C  CD  . LYS A 224 ? 0.1939 0.2164 0.2169 -0.0182 -0.0303 -0.0430 225 LYS A CD  
1981 C  CE  . LYS A 224 ? 0.2329 0.3287 0.2216 -0.0038 -0.0467 -0.1057 225 LYS A CE  
1982 N  NZ  . LYS A 224 ? 0.2150 0.2671 0.2211 -0.0333 0.0215  -0.0644 225 LYS A NZ  
1983 N  N   . PHE A 225 ? 0.1138 0.1230 0.1141 0.0136  0.0010  0.0155  226 PHE A N   
1984 C  CA  . PHE A 225 ? 0.1247 0.1186 0.1112 0.0100  0.0219  0.0092  226 PHE A CA  
1985 C  C   . PHE A 225 ? 0.1300 0.1169 0.0944 -0.0081 0.0147  0.0035  226 PHE A C   
1986 O  O   . PHE A 225 ? 0.1378 0.1194 0.1072 0.0041  0.0166  -0.0082 226 PHE A O   
1987 C  CB  . PHE A 225 ? 0.1492 0.1030 0.1046 0.0219  0.0197  0.0131  226 PHE A CB  
1988 C  CG  . PHE A 225 ? 0.1155 0.0829 0.1317 -0.0140 0.0093  -0.0166 226 PHE A CG  
1989 C  CD1 . PHE A 225 ? 0.1745 0.2037 0.1295 0.0766  0.0305  0.0308  226 PHE A CD1 
1990 C  CD2 . PHE A 225 ? 0.1322 0.1853 0.1442 0.0060  0.0005  -0.0524 226 PHE A CD2 
1991 C  CE1 . PHE A 225 ? 0.1402 0.2073 0.1882 0.0665  0.0342  0.0680  226 PHE A CE1 
1992 C  CE2 . PHE A 225 ? 0.1377 0.2079 0.1714 0.0118  -0.0111 -0.0807 226 PHE A CE2 
1993 C  CZ  . PHE A 225 ? 0.1225 0.1510 0.2034 -0.0136 0.0057  -0.0772 226 PHE A CZ  
1994 N  N   . ARG A 226 ? 0.1284 0.1203 0.0974 0.0087  0.0035  -0.0012 227 ARG A N   
1995 C  CA  . ARG A 226 ? 0.1159 0.1298 0.1142 0.0166  0.0115  -0.0015 227 ARG A CA  
1996 C  C   . ARG A 226 ? 0.1372 0.1283 0.1260 0.0154  0.0195  0.0013  227 ARG A C   
1997 O  O   . ARG A 226 ? 0.1430 0.1685 0.1429 0.0225  0.0278  -0.0001 227 ARG A O   
1998 C  CB  . ARG A 226 ? 0.1416 0.1251 0.1039 0.0195  0.0015  0.0040  227 ARG A CB  
1999 C  CG  . ARG A 226 ? 0.1363 0.1190 0.1111 0.0046  -0.0020 0.0034  227 ARG A CG  
2000 C  CD  . ARG A 226 ? 0.1746 0.1221 0.1104 0.0019  0.0017  0.0194  227 ARG A CD  
2001 N  NE  . ARG A 226 ? 0.1444 0.1085 0.1248 -0.0057 -0.0219 0.0125  227 ARG A NE  
2002 C  CZ  . ARG A 226 ? 0.1533 0.1147 0.1291 -0.0168 -0.0060 -0.0065 227 ARG A CZ  
2003 N  NH1 . ARG A 226 ? 0.1852 0.1336 0.1715 -0.0324 -0.0102 -0.0557 227 ARG A NH1 
2004 N  NH2 . ARG A 226 ? 0.1845 0.1076 0.1524 -0.0267 -0.0065 -0.0129 227 ARG A NH2 
2005 N  N   . LYS A 227 ? 0.1468 0.1213 0.0966 -0.0015 0.0197  -0.0052 228 LYS A N   
2006 C  CA  . LYS A 227 ? 0.1559 0.1284 0.1050 -0.0098 0.0205  -0.0167 228 LYS A CA  
2007 C  C   . LYS A 227 ? 0.1471 0.1385 0.0908 -0.0017 0.0124  -0.0159 228 LYS A C   
2008 O  O   . LYS A 227 ? 0.1761 0.1542 0.0865 -0.0027 0.0346  -0.0140 228 LYS A O   
2009 C  CB  . LYS A 227 ? 0.1764 0.1958 0.1173 -0.0421 0.0107  -0.0428 228 LYS A CB  
2010 C  CG  . LYS A 227 ? 0.2423 0.2259 0.2000 -0.0913 0.0469  -0.0789 228 LYS A CG  
2011 C  CD  . LYS A 227 ? 0.3325 0.5623 0.2825 -0.1467 0.0209  -0.2199 228 LYS A CD  
2012 C  CE  . LYS A 227 ? 0.4514 0.7077 0.6535 0.1335  -0.1289 -0.4273 228 LYS A CE  
2013 N  NZ  . LYS A 227 ? 0.8330 1.0735 0.7425 0.1644  -0.0898 -0.3156 228 LYS A NZ  
2014 N  N   . LEU A 228 ? 0.1318 0.1156 0.0918 0.0031  0.0104  -0.0155 229 LEU A N   
2015 C  CA  . LEU A 228 ? 0.1187 0.1367 0.0820 -0.0001 0.0021  -0.0087 229 LEU A CA  
2016 C  C   . LEU A 228 ? 0.1358 0.1110 0.0825 0.0088  0.0204  -0.0031 229 LEU A C   
2017 O  O   . LEU A 228 ? 0.1351 0.1116 0.0951 0.0116  0.0197  -0.0052 229 LEU A O   
2018 C  CB  . LEU A 228 ? 0.1130 0.1324 0.0944 0.0055  0.0105  -0.0115 229 LEU A CB  
2019 C  CG  . LEU A 228 ? 0.1113 0.1413 0.0864 0.0093  0.0118  -0.0049 229 LEU A CG  
2020 C  CD1 . LEU A 228 ? 0.1268 0.1527 0.1235 0.0209  0.0054  -0.0247 229 LEU A CD1 
2021 C  CD2 . LEU A 228 ? 0.1465 0.1893 0.1415 0.0366  0.0348  0.0463  229 LEU A CD2 
2022 N  N   . ASN A 229 ? 0.1196 0.1316 0.0982 0.0055  0.0126  -0.0010 230 ASN A N   
2023 C  CA  . ASN A 229 ? 0.1274 0.1369 0.1090 0.0160  0.0165  -0.0063 230 ASN A CA  
2024 C  C   . ASN A 229 ? 0.1146 0.1341 0.1093 0.0111  0.0331  0.0261  230 ASN A C   
2025 O  O   . ASN A 229 ? 0.1376 0.1316 0.1253 0.0197  0.0240  0.0138  230 ASN A O   
2026 C  CB  . ASN A 229 ? 0.1436 0.1561 0.1050 0.0211  0.0274  0.0087  230 ASN A CB  
2027 C  CG  . ASN A 229 ? 0.1923 0.1951 0.1084 0.0531  0.0278  -0.0175 230 ASN A CG  
2028 O  OD1 . ASN A 229 ? 0.2691 0.2249 0.1146 0.0555  0.0403  -0.0092 230 ASN A OD1 
2029 N  ND2 . ASN A 229 ? 0.1849 0.1932 0.1491 0.0183  0.0267  -0.0253 230 ASN A ND2 
2030 N  N   . PHE A 230 ? 0.1119 0.1388 0.1136 0.0046  0.0119  0.0083  231 PHE A N   
2031 C  CA  . PHE A 230 ? 0.1319 0.1250 0.1206 0.0065  0.0289  0.0216  231 PHE A CA  
2032 C  C   . PHE A 230 ? 0.1448 0.1431 0.1178 0.0031  0.0087  0.0121  231 PHE A C   
2033 O  O   . PHE A 230 ? 0.1704 0.1474 0.1578 -0.0175 0.0120  0.0263  231 PHE A O   
2034 C  CB  . PHE A 230 ? 0.1324 0.1245 0.1228 -0.0015 0.0000  0.0118  231 PHE A CB  
2035 C  CG  . PHE A 230 ? 0.1385 0.1162 0.1187 0.0003  0.0057  0.0111  231 PHE A CG  
2036 C  CD1 . PHE A 230 ? 0.1747 0.1366 0.1253 0.0092  0.0350  0.0170  231 PHE A CD1 
2037 C  CD2 . PHE A 230 ? 0.1561 0.1309 0.1166 0.0089  -0.0019 0.0089  231 PHE A CD2 
2038 C  CE1 . PHE A 230 ? 0.1755 0.1535 0.1222 0.0116  0.0082  0.0254  231 PHE A CE1 
2039 C  CE2 . PHE A 230 ? 0.1675 0.1231 0.1301 0.0010  0.0006  0.0220  231 PHE A CE2 
2040 C  CZ  . PHE A 230 ? 0.1571 0.1368 0.1107 -0.0234 0.0015  0.0098  231 PHE A CZ  
2041 N  N   . ASN A 231 ? 0.1360 0.1563 0.1180 -0.0038 0.0184  0.0175  232 ASN A N   
2042 C  CA  . ASN A 231 ? 0.1281 0.1891 0.1457 0.0063  0.0394  0.0573  232 ASN A CA  
2043 C  C   . ASN A 231 ? 0.1237 0.1960 0.1186 0.0131  0.0395  0.0452  232 ASN A C   
2044 O  O   . ASN A 231 ? 0.1270 0.1715 0.1380 0.0244  0.0181  0.0197  232 ASN A O   
2045 C  CB  . ASN A 231 ? 0.1488 0.1944 0.1712 0.0208  0.0494  0.0489  232 ASN A CB  
2046 C  CG  . ASN A 231 ? 0.1381 0.1842 0.1534 0.0340  0.0434  0.0348  232 ASN A CG  
2047 O  OD1 . ASN A 231 ? 0.1652 0.1938 0.1570 0.0427  0.0427  0.0258  232 ASN A OD1 
2048 N  ND2 . ASN A 231 ? 0.2150 0.2275 0.1555 0.0935  0.0392  0.0294  232 ASN A ND2 
2049 N  N   . GLY A 232 ? 0.1444 0.1706 0.1494 0.0071  0.0274  0.0425  233 GLY A N   
2050 C  CA  . GLY A 232 ? 0.1794 0.1676 0.1513 0.0266  0.0412  0.0494  233 GLY A CA  
2051 C  C   . GLY A 232 ? 0.1362 0.1816 0.1539 0.0249  0.0406  0.0454  233 GLY A C   
2052 O  O   . GLY A 232 ? 0.1870 0.2135 0.1377 0.0480  0.0593  0.0452  233 GLY A O   
2053 N  N   . GLU A 233 ? 0.1689 0.2072 0.1253 0.0432  0.0582  0.0637  234 GLU A N   
2054 C  CA  . GLU A 233 ? 0.2025 0.1859 0.1485 0.0185  0.0571  0.0456  234 GLU A CA  
2055 C  C   . GLU A 233 ? 0.1991 0.1694 0.1507 0.0456  0.0390  0.0372  234 GLU A C   
2056 O  O   . GLU A 233 ? 0.1797 0.2021 0.1604 0.0137  0.0498  0.0296  234 GLU A O   
2057 C  CB  . GLU A 233 ? 0.1483 0.2123 0.1447 0.0197  0.0333  0.0425  234 GLU A CB  
2058 C  CG  . GLU A 233 ? 0.1598 0.2018 0.1890 -0.0214 0.0254  0.0461  234 GLU A CG  
2059 C  CD  . GLU A 233 ? 0.1905 0.3472 0.2231 0.0153  0.0381  0.0280  234 GLU A CD  
2060 O  OE1 . GLU A 233 ? 0.2547 0.2646 0.2515 0.0494  0.0507  0.0986  234 GLU A OE1 
2061 O  OE2 . GLU A 233 ? 0.3404 0.3492 0.2251 -0.0595 -0.0644 0.0388  234 GLU A OE2 
2062 N  N   . GLY A 234 ? 0.2351 0.1918 0.1656 0.0406  0.0544  0.0310  235 GLY A N   
2063 C  CA  . GLY A 234 ? 0.2344 0.2723 0.1411 0.0964  0.0513  0.0160  235 GLY A CA  
2064 C  C   . GLY A 234 ? 0.1923 0.2481 0.1640 0.0401  0.0496  0.0049  235 GLY A C   
2065 O  O   . GLY A 234 ? 0.2493 0.3722 0.1920 0.0878  0.1143  0.0288  235 GLY A O   
2066 N  N   . GLU A 235 ? 0.1815 0.2304 0.1679 0.0425  0.0428  0.0538  236 GLU A N   
2067 C  CA  . GLU A 235 ? 0.1844 0.2157 0.2110 0.0606  0.0201  0.0438  236 GLU A CA  
2068 C  C   . GLU A 235 ? 0.1923 0.2277 0.1763 0.0640  0.0666  0.0303  236 GLU A C   
2069 O  O   . GLU A 235 ? 0.2329 0.2655 0.1782 0.0419  0.0427  0.0588  236 GLU A O   
2070 C  CB  . GLU A 235 ? 0.2159 0.2698 0.1705 0.0295  0.0502  0.0797  236 GLU A CB  
2071 C  CG  . GLU A 235 ? 0.2102 0.3183 0.2101 -0.0080 0.0434  0.0494  236 GLU A CG  
2072 C  CD  . GLU A 235 ? 0.2815 0.3519 0.2605 -0.0750 0.0948  -0.0065 236 GLU A CD  
2073 O  OE1 . GLU A 235 ? 0.2500 0.4228 0.2626 -0.0635 0.0478  0.0586  236 GLU A OE1 
2074 O  OE2 . GLU A 235 ? 0.7005 0.5902 0.8543 -0.0954 -0.0344 0.0373  236 GLU A OE2 
2075 N  N   . PRO A 236 ? 0.1808 0.2797 0.2046 0.0788  0.0723  0.0656  237 PRO A N   
2076 C  CA  . PRO A 236 ? 0.1823 0.2362 0.2000 0.0577  0.0582  0.0644  237 PRO A CA  
2077 C  C   . PRO A 236 ? 0.1959 0.1976 0.1333 0.0458  0.0209  0.0153  237 PRO A C   
2078 O  O   . PRO A 236 ? 0.1747 0.2293 0.1741 0.0197  0.0412  0.0232  237 PRO A O   
2079 C  CB  . PRO A 236 ? 0.1624 0.3003 0.3036 0.0432  0.0621  0.0966  237 PRO A CB  
2080 C  CG  . PRO A 236 ? 0.1941 0.3966 0.4251 0.1032  0.1142  0.2381  237 PRO A CG  
2081 C  CD  . PRO A 236 ? 0.1579 0.3535 0.3244 0.0833  0.0649  0.1425  237 PRO A CD  
2082 N  N   . GLU A 237 ? 0.1748 0.2138 0.1446 0.0604  0.0308  0.0003  238 GLU A N   
2083 C  CA  . GLU A 237 ? 0.1870 0.2196 0.1106 0.0494  0.0456  -0.0021 238 GLU A CA  
2084 C  C   . GLU A 237 ? 0.1397 0.2035 0.1520 0.0458  0.0364  -0.0028 238 GLU A C   
2085 O  O   . GLU A 237 ? 0.1744 0.2011 0.1468 0.0724  0.0452  0.0100  238 GLU A O   
2086 C  CB  . GLU A 237 ? 0.2124 0.2469 0.1524 0.0646  0.0443  -0.0198 238 GLU A CB  
2087 C  CG  . GLU A 237 ? 0.2233 0.2870 0.2389 0.0340  0.0266  -0.0879 238 GLU A CG  
2088 C  CD  . GLU A 237 ? 0.2725 0.3684 0.1974 0.0549  0.0419  -0.0939 238 GLU A CD  
2089 O  OE1 . GLU A 237 ? 0.3176 0.5368 0.6827 0.0640  -0.0531 -0.3786 238 GLU A OE1 
2090 O  OE2 . GLU A 237 ? 0.2809 0.2482 0.1985 0.0161  0.0646  -0.0355 238 GLU A OE2 
2091 N  N   . GLU A 238 ? 0.1375 0.1905 0.1299 0.0384  0.0458  0.0233  239 GLU A N   
2092 C  CA  . GLU A 238 ? 0.1363 0.1949 0.1395 0.0186  0.0384  0.0089  239 GLU A CA  
2093 C  C   . GLU A 238 ? 0.1288 0.1563 0.1099 0.0329  0.0346  0.0068  239 GLU A C   
2094 O  O   . GLU A 238 ? 0.1469 0.1328 0.1805 0.0221  0.0450  0.0170  239 GLU A O   
2095 C  CB  . GLU A 238 ? 0.1755 0.2727 0.1573 -0.0092 0.0176  0.0129  239 GLU A CB  
2096 C  CG  . GLU A 238 ? 0.2296 0.2294 0.2711 -0.0174 0.0652  -0.0586 239 GLU A CG  
2097 C  CD  . GLU A 238 ? 0.3637 0.4785 0.4181 -0.1501 -0.0794 -0.0738 239 GLU A CD  
2098 O  OE1 . GLU A 238 ? 0.5800 0.6085 0.4149 -0.0909 -0.1234 -0.1902 239 GLU A OE1 
2099 O  OE2 . GLU A 238 ? 0.7174 0.3641 0.4433 -0.1211 -0.0465 -0.0934 239 GLU A OE2 
2100 N  N   . LEU A 239 ? 0.1386 0.1394 0.1023 0.0227  0.0449  0.0065  240 LEU A N   
2101 C  CA  . LEU A 239 ? 0.1169 0.1284 0.1077 0.0124  0.0218  -0.0024 240 LEU A CA  
2102 C  C   . LEU A 239 ? 0.1165 0.1275 0.0935 0.0021  0.0278  0.0175  240 LEU A C   
2103 O  O   . LEU A 239 ? 0.1299 0.1284 0.1018 0.0241  0.0255  0.0092  240 LEU A O   
2104 C  CB  . LEU A 239 ? 0.1357 0.1168 0.1560 0.0113  0.0285  -0.0146 240 LEU A CB  
2105 C  CG  . LEU A 239 ? 0.1658 0.1546 0.1828 0.0344  0.0182  -0.0348 240 LEU A CG  
2106 C  CD1 . LEU A 239 ? 0.2648 0.1290 0.3152 0.0294  -0.0208 -0.0362 240 LEU A CD1 
2107 C  CD2 . LEU A 239 ? 0.2396 0.1631 0.1465 0.0125  0.0133  -0.0449 240 LEU A CD2 
2108 N  N   . MET A 240 ? 0.1248 0.1186 0.0888 0.0278  0.0298  0.0083  241 MET A N   
2109 C  CA  . MET A 240 ? 0.1256 0.1035 0.0858 0.0175  0.0305  0.0017  241 MET A CA  
2110 C  C   . MET A 240 ? 0.1074 0.1068 0.0752 0.0076  0.0137  -0.0065 241 MET A C   
2111 O  O   . MET A 240 ? 0.1086 0.1211 0.0821 0.0074  0.0086  0.0048  241 MET A O   
2112 C  CB  . MET A 240 ? 0.1412 0.1215 0.0870 0.0234  0.0315  0.0124  241 MET A CB  
2113 C  CG  . MET A 240 ? 0.1307 0.1183 0.0881 0.0000  0.0238  -0.0098 241 MET A CG  
2114 S  SD  . MET A 240 ? 0.1375 0.0979 0.1104 0.0059  0.0289  0.0071  241 MET A SD  
2115 C  CE  . MET A 240 ? 0.2441 0.1281 0.1394 0.0060  0.0731  0.0233  241 MET A CE  
2116 N  N   . VAL A 241 ? 0.1124 0.1076 0.0688 0.0030  0.0078  0.0003  242 VAL A N   
2117 C  CA  . VAL A 241 ? 0.1101 0.0840 0.0767 -0.0013 0.0167  0.0035  242 VAL A CA  
2118 C  C   . VAL A 241 ? 0.0951 0.0823 0.0815 0.0115  0.0137  -0.0049 242 VAL A C   
2119 O  O   . VAL A 241 ? 0.1040 0.0979 0.0822 0.0049  0.0156  -0.0015 242 VAL A O   
2120 C  CB  . VAL A 241 ? 0.1196 0.0966 0.0873 -0.0124 0.0093  -0.0175 242 VAL A CB  
2121 C  CG1 . VAL A 241 ? 0.1557 0.1096 0.1096 -0.0010 -0.0110 -0.0168 242 VAL A CG1 
2122 C  CG2 . VAL A 241 ? 0.1422 0.0979 0.1083 0.0220  0.0091  -0.0215 242 VAL A CG2 
2123 N  N   . ASP A 242 ? 0.0954 0.0766 0.0759 0.0074  0.0062  -0.0043 243 ASP A N   
2124 C  CA  . ASP A 242 ? 0.1028 0.0749 0.0825 0.0175  0.0055  -0.0024 243 ASP A CA  
2125 C  C   . ASP A 242 ? 0.0917 0.0776 0.0733 0.0108  0.0006  -0.0001 243 ASP A C   
2126 O  O   . ASP A 242 ? 0.1067 0.0854 0.1173 0.0115  -0.0138 -0.0044 243 ASP A O   
2127 C  CB  . ASP A 242 ? 0.1120 0.0728 0.1040 0.0170  0.0118  0.0031  243 ASP A CB  
2128 C  CG  . ASP A 242 ? 0.1099 0.0788 0.0981 0.0074  0.0065  -0.0096 243 ASP A CG  
2129 O  OD1 . ASP A 242 ? 0.1125 0.0758 0.1014 0.0137  0.0171  0.0054  243 ASP A OD1 
2130 O  OD2 . ASP A 242 ? 0.1386 0.0802 0.1503 0.0127  0.0335  -0.0160 243 ASP A OD2 
2131 N  N   . ASN A 243 ? 0.0892 0.0750 0.0693 0.0073  0.0115  0.0000  244 ASN A N   
2132 C  CA  . ASN A 243 ? 0.0873 0.0691 0.0753 0.0120  0.0096  0.0006  244 ASN A CA  
2133 C  C   . ASN A 243 ? 0.0798 0.0743 0.0790 0.0076  -0.0001 -0.0043 244 ASN A C   
2134 O  O   . ASN A 243 ? 0.1005 0.0816 0.0900 0.0201  0.0074  0.0060  244 ASN A O   
2135 C  CB  . ASN A 243 ? 0.0917 0.0793 0.0789 0.0044  0.0013  0.0054  244 ASN A CB  
2136 C  CG  . ASN A 243 ? 0.0909 0.0762 0.0838 -0.0030 0.0007  0.0052  244 ASN A CG  
2137 O  OD1 . ASN A 243 ? 0.0885 0.0816 0.1146 -0.0003 0.0021  0.0230  244 ASN A OD1 
2138 N  ND2 . ASN A 243 ? 0.1071 0.1237 0.1280 -0.0135 -0.0118 0.0467  244 ASN A ND2 
2139 N  N   . TRP A 244 ? 0.0978 0.0717 0.0740 0.0076  0.0006  -0.0074 245 TRP A N   
2140 C  CA  . TRP A 244 ? 0.0864 0.0793 0.0687 0.0138  0.0000  -0.0080 245 TRP A CA  
2141 C  C   . TRP A 244 ? 0.0890 0.0770 0.0788 0.0118  0.0046  -0.0020 245 TRP A C   
2142 O  O   . TRP A 244 ? 0.0938 0.0983 0.0907 0.0280  -0.0054 -0.0146 245 TRP A O   
2143 C  CB  . TRP A 244 ? 0.0881 0.0734 0.0850 0.0093  -0.0017 -0.0086 245 TRP A CB  
2144 C  CG  . TRP A 244 ? 0.0879 0.0823 0.0799 0.0102  0.0078  -0.0017 245 TRP A CG  
2145 C  CD1 . TRP A 244 ? 0.0952 0.0698 0.0868 0.0006  0.0135  -0.0055 245 TRP A CD1 
2146 C  CD2 . TRP A 244 ? 0.0863 0.0734 0.0815 0.0065  0.0080  -0.0005 245 TRP A CD2 
2147 N  NE1 . TRP A 244 ? 0.1015 0.0759 0.0902 0.0068  0.0082  0.0049  245 TRP A NE1 
2148 C  CE2 . TRP A 244 ? 0.0996 0.0802 0.0937 0.0094  0.0125  0.0060  245 TRP A CE2 
2149 C  CE3 . TRP A 244 ? 0.1190 0.0969 0.0869 0.0131  0.0015  0.0005  245 TRP A CE3 
2150 C  CZ2 . TRP A 244 ? 0.1248 0.0850 0.0974 0.0162  0.0114  0.0065  245 TRP A CZ2 
2151 C  CZ3 . TRP A 244 ? 0.1140 0.1019 0.0960 0.0103  -0.0082 0.0104  245 TRP A CZ3 
2152 C  CH2 . TRP A 244 ? 0.1246 0.0864 0.1263 0.0131  0.0003  0.0104  245 TRP A CH2 
2153 N  N   . ARG A 245 ? 0.0778 0.0817 0.0762 0.0066  0.0041  -0.0142 246 ARG A N   
2154 C  CA  . ARG A 245 ? 0.0662 0.0803 0.0788 0.0074  -0.0010 -0.0076 246 ARG A CA  
2155 C  C   . ARG A 245 ? 0.0846 0.0767 0.0769 0.0120  0.0013  -0.0159 246 ARG A C   
2156 O  O   . ARG A 245 ? 0.0814 0.0877 0.0873 0.0027  0.0035  -0.0063 246 ARG A O   
2157 C  CB  . ARG A 245 ? 0.0734 0.0935 0.0754 -0.0013 0.0013  -0.0109 246 ARG A CB  
2158 C  CG  . ARG A 245 ? 0.0649 0.0964 0.0892 0.0074  -0.0017 -0.0054 246 ARG A CG  
2159 C  CD  . ARG A 245 ? 0.0698 0.1001 0.0807 0.0006  -0.0032 -0.0179 246 ARG A CD  
2160 N  NE  . ARG A 245 ? 0.0680 0.0954 0.0946 -0.0051 0.0001  -0.0131 246 ARG A NE  
2161 C  CZ  . ARG A 245 ? 0.0675 0.1044 0.0861 -0.0097 0.0017  -0.0010 246 ARG A CZ  
2162 N  NH1 . ARG A 245 ? 0.0840 0.0987 0.0918 -0.0030 0.0142  -0.0104 246 ARG A NH1 
2163 N  NH2 . ARG A 245 ? 0.0837 0.1340 0.1060 -0.0185 -0.0003 -0.0122 246 ARG A NH2 
2164 N  N   . PRO A 246 ? 0.0983 0.0838 0.0882 0.0200  0.0008  -0.0043 247 PRO A N   
2165 C  CA  . PRO A 246 ? 0.1077 0.0865 0.0912 0.0149  0.0041  -0.0038 247 PRO A CA  
2166 C  C   . PRO A 246 ? 0.1104 0.0972 0.0759 0.0118  -0.0052 0.0063  247 PRO A C   
2167 O  O   . PRO A 246 ? 0.1032 0.0978 0.0817 0.0111  -0.0046 -0.0010 247 PRO A O   
2168 C  CB  . PRO A 246 ? 0.1536 0.1220 0.1228 0.0575  -0.0065 -0.0066 247 PRO A CB  
2169 C  CG  . PRO A 246 ? 0.1218 0.1649 0.2155 0.0392  0.0221  0.0608  247 PRO A CG  
2170 C  CD  . PRO A 246 ? 0.1092 0.1095 0.1155 0.0263  -0.0080 0.0120  247 PRO A CD  
2171 N  N   . ALA A 247 ? 0.1114 0.1025 0.0885 0.0184  0.0052  0.0083  248 ALA A N   
2172 C  CA  . ALA A 247 ? 0.1088 0.0995 0.1007 0.0176  -0.0020 0.0020  248 ALA A CA  
2173 C  C   . ALA A 247 ? 0.1033 0.1018 0.0903 0.0292  -0.0091 0.0121  248 ALA A C   
2174 O  O   . ALA A 247 ? 0.1152 0.1243 0.0988 0.0434  -0.0071 0.0044  248 ALA A O   
2175 C  CB  . ALA A 247 ? 0.1293 0.1116 0.1099 0.0152  0.0142  0.0094  248 ALA A CB  
2176 N  N   . GLN A 248 ? 0.0860 0.1032 0.0882 0.0126  -0.0034 0.0043  249 GLN A N   
2177 C  CA  . GLN A 248 ? 0.0722 0.1196 0.1000 0.0207  0.0003  0.0013  249 GLN A CA  
2178 C  C   . GLN A 248 ? 0.0988 0.1252 0.0919 0.0355  -0.0093 0.0074  249 GLN A C   
2179 O  O   . GLN A 248 ? 0.1171 0.1173 0.0993 0.0239  0.0035  0.0115  249 GLN A O   
2180 C  CB  . GLN A 248 ? 0.0979 0.1114 0.1045 0.0000  -0.0114 -0.0026 249 GLN A CB  
2181 C  CG  . GLN A 248 ? 0.1237 0.1146 0.0965 0.0081  -0.0093 0.0071  249 GLN A CG  
2182 C  CD  . GLN A 248 ? 0.0984 0.1331 0.0960 0.0038  -0.0003 0.0054  249 GLN A CD  
2183 O  OE1 . GLN A 248 ? 0.1032 0.1828 0.1342 -0.0168 0.0044  -0.0266 249 GLN A OE1 
2184 N  NE2 . GLN A 248 ? 0.1169 0.1387 0.1119 0.0124  0.0035  0.0031  249 GLN A NE2 
2185 N  N   . PRO A 249 ? 0.1040 0.1782 0.1031 0.0458  -0.0172 -0.0005 250 PRO A N   
2186 C  CA  . PRO A 249 ? 0.1362 0.1904 0.0948 0.0694  -0.0286 -0.0063 250 PRO A CA  
2187 C  C   . PRO A 249 ? 0.1137 0.1508 0.0803 0.0234  -0.0148 0.0086  250 PRO A C   
2188 O  O   . PRO A 249 ? 0.1094 0.1480 0.1119 0.0225  -0.0087 0.0186  250 PRO A O   
2189 C  CB  . PRO A 249 ? 0.1400 0.2829 0.1421 0.0882  -0.0480 -0.0414 250 PRO A CB  
2190 C  CG  . PRO A 249 ? 0.1365 0.3052 0.1421 0.0339  -0.0414 -0.0368 250 PRO A CG  
2191 C  CD  . PRO A 249 ? 0.0922 0.2344 0.1506 0.0262  -0.0337 -0.0122 250 PRO A CD  
2192 N  N   . LEU A 250 ? 0.1460 0.1330 0.0822 0.0454  -0.0130 0.0071  251 LEU A N   
2193 C  CA  . LEU A 250 ? 0.1384 0.1184 0.0905 0.0092  -0.0037 0.0015  251 LEU A CA  
2194 C  C   . LEU A 250 ? 0.1186 0.1184 0.0961 0.0245  -0.0068 0.0024  251 LEU A C   
2195 O  O   . LEU A 250 ? 0.1215 0.1233 0.1186 0.0245  -0.0266 -0.0044 251 LEU A O   
2196 C  CB  . LEU A 250 ? 0.1856 0.1078 0.0989 0.0111  0.0035  -0.0003 251 LEU A CB  
2197 C  CG  . LEU A 250 ? 0.1636 0.1343 0.0989 -0.0060 0.0178  0.0013  251 LEU A CG  
2198 C  CD1 . LEU A 250 ? 0.1291 0.1484 0.1239 -0.0137 -0.0035 -0.0041 251 LEU A CD1 
2199 C  CD2 . LEU A 250 ? 0.2221 0.1632 0.1474 -0.0372 0.0538  0.0054  251 LEU A CD2 
2200 N  N   . LYS A 251 ? 0.1334 0.1550 0.0958 0.0353  -0.0230 -0.0037 252 LYS A N   
2201 C  CA  . LYS A 251 ? 0.1449 0.1730 0.0982 0.0410  -0.0242 -0.0133 252 LYS A CA  
2202 C  C   . LYS A 251 ? 0.1208 0.1536 0.1371 0.0125  -0.0155 0.0032  252 LYS A C   
2203 O  O   . LYS A 251 ? 0.1983 0.1793 0.1254 0.0131  0.0114  -0.0160 252 LYS A O   
2204 C  CB  . LYS A 251 ? 0.1297 0.2043 0.1444 0.0094  -0.0199 -0.0350 252 LYS A CB  
2205 C  CG  . LYS A 251 ? 0.1425 0.2169 0.1831 -0.0006 0.0060  -0.0320 252 LYS A CG  
2206 C  CD  . LYS A 251 ? 0.1339 0.2563 0.2054 0.0104  0.0071  0.0054  252 LYS A CD  
2207 C  CE  . LYS A 251 ? 0.1873 0.2707 0.3989 0.0775  0.0549  0.0864  252 LYS A CE  
2208 N  NZ  . LYS A 251 ? 0.1791 0.2989 0.2958 0.0575  0.0239  0.0595  252 LYS A NZ  
2209 N  N   . ASN A 252 ? 0.1517 0.1517 0.1049 0.0136  -0.0254 -0.0265 253 ASN A N   
2210 C  CA  . ASN A 252 ? 0.1835 0.3122 0.1717 0.0549  -0.0467 -0.1014 253 ASN A CA  
2211 C  C   . ASN A 252 ? 0.1973 0.2166 0.1634 0.0155  -0.0373 -0.0425 253 ASN A C   
2212 O  O   . ASN A 252 ? 0.2487 0.2296 0.1793 0.0305  -0.0137 -0.0390 253 ASN A O   
2213 C  CB  . ASN A 252 ? 0.2626 0.3503 0.1746 0.0245  -0.0639 -0.1226 253 ASN A CB  
2214 C  CG  . ASN A 252 ? 0.2705 0.2711 0.2421 -0.0099 0.0410  -0.0533 253 ASN A CG  
2215 O  OD1 . ASN A 252 ? 0.4618 0.4524 0.2211 -0.0146 0.0956  0.0817  253 ASN A OD1 
2216 N  ND2 . ASN A 252 ? 0.3431 0.3097 0.3318 0.0368  0.0161  -0.1567 253 ASN A ND2 
2217 N  N   . ARG A 253 ? 0.1400 0.2423 0.0716 0.0381  0.0062  0.0348  254 ARG A N   
2218 C  CA  . ARG A 253 ? 0.1235 0.1393 0.0932 0.0237  -0.0046 -0.0015 254 ARG A CA  
2219 C  C   . ARG A 253 ? 0.1506 0.1262 0.0917 0.0240  0.0171  -0.0030 254 ARG A C   
2220 O  O   . ARG A 253 ? 0.1915 0.1728 0.2071 0.0623  0.0709  0.0557  254 ARG A O   
2221 C  CB  . ARG A 253 ? 0.1234 0.1160 0.0768 0.0074  0.0065  -0.0089 254 ARG A CB  
2222 C  CG  . ARG A 253 ? 0.1208 0.1102 0.0888 0.0076  -0.0055 -0.0140 254 ARG A CG  
2223 C  CD  . ARG A 253 ? 0.1218 0.0936 0.0788 0.0131  -0.0003 -0.0063 254 ARG A CD  
2224 N  NE  . ARG A 253 ? 0.0992 0.1035 0.0770 0.0116  -0.0081 0.0000  254 ARG A NE  
2225 C  CZ  . ARG A 253 ? 0.0773 0.0883 0.0831 -0.0037 -0.0012 0.0032  254 ARG A CZ  
2226 N  NH1 . ARG A 253 ? 0.0846 0.0908 0.0727 0.0027  -0.0116 0.0062  254 ARG A NH1 
2227 N  NH2 . ARG A 253 ? 0.0812 0.1034 0.0798 0.0078  -0.0077 0.0041  254 ARG A NH2 
2228 N  N   . GLN A 254 ? 0.1175 0.1475 0.0974 0.0083  -0.0136 -0.0135 255 GLN A N   
2229 C  CA  . GLN A 254 ? 0.1322 0.1694 0.0925 -0.0038 -0.0048 -0.0087 255 GLN A CA  
2230 C  C   . GLN A 254 ? 0.1430 0.1162 0.1028 0.0124  -0.0216 0.0013  255 GLN A C   
2231 O  O   . GLN A 254 ? 0.2222 0.1247 0.1683 -0.0085 -0.0604 0.0115  255 GLN A O   
2232 C  CB  . GLN A 254 ? 0.1679 0.1791 0.1147 -0.0098 0.0032  -0.0082 255 GLN A CB  
2233 C  CG  . GLN A 254 ? 0.2164 0.2011 0.1084 -0.0137 0.0153  0.0295  255 GLN A CG  
2234 C  CD  . GLN A 254 ? 0.2790 0.1580 0.1624 0.0253  0.0311  0.0088  255 GLN A CD  
2235 O  OE1 . GLN A 254 ? 0.3271 0.1871 0.2572 0.0216  0.0595  -0.0297 255 GLN A OE1 
2236 N  NE2 . GLN A 254 ? 0.2883 0.2552 0.1369 -0.0403 0.0489  0.0289  255 GLN A NE2 
2237 N  N   . ILE A 255 ? 0.1124 0.1172 0.0835 0.0107  -0.0073 0.0005  256 ILE A N   
2238 C  CA  . ILE A 255 ? 0.0930 0.1156 0.0847 0.0088  -0.0032 0.0102  256 ILE A CA  
2239 C  C   . ILE A 255 ? 0.1014 0.1107 0.0873 0.0012  -0.0013 0.0141  256 ILE A C   
2240 O  O   . ILE A 255 ? 0.1351 0.1256 0.1070 0.0233  0.0121  0.0394  256 ILE A O   
2241 C  CB  . ILE A 255 ? 0.1216 0.1107 0.0909 0.0118  -0.0149 0.0000  256 ILE A CB  
2242 C  CG1 . ILE A 255 ? 0.1045 0.1220 0.1120 0.0175  -0.0043 -0.0043 256 ILE A CG1 
2243 C  CG2 . ILE A 255 ? 0.1325 0.1453 0.1040 0.0089  -0.0131 -0.0065 256 ILE A CG2 
2244 C  CD1 . ILE A 255 ? 0.1422 0.1465 0.1140 0.0028  0.0167  -0.0142 256 ILE A CD1 
2245 N  N   A LYS A 256 ? 0.0869 0.1121 0.0785 -0.0015 -0.0012 0.0190  257 LYS A N   
2246 N  N   B LYS A 256 ? 0.0996 0.1186 0.0776 0.0027  -0.0091 0.0091  257 LYS A N   
2247 C  CA  A LYS A 256 ? 0.1013 0.1306 0.0729 0.0073  0.0019  0.0184  257 LYS A CA  
2248 C  CA  B LYS A 256 ? 0.1035 0.1299 0.0805 0.0028  -0.0038 0.0118  257 LYS A CA  
2249 C  C   A LYS A 256 ? 0.0948 0.1134 0.0743 0.0057  0.0099  0.0038  257 LYS A C   
2250 C  C   B LYS A 256 ? 0.0834 0.1146 0.0690 0.0076  -0.0046 0.0193  257 LYS A C   
2251 O  O   A LYS A 256 ? 0.1048 0.0965 0.0708 0.0161  0.0066  -0.0035 257 LYS A O   
2252 O  O   B LYS A 256 ? 0.0970 0.0905 0.0683 0.0098  0.0031  0.0015  257 LYS A O   
2253 C  CB  A LYS A 256 ? 0.1005 0.1439 0.0861 0.0124  0.0160  -0.0200 257 LYS A CB  
2254 C  CB  B LYS A 256 ? 0.1528 0.1060 0.1024 0.0007  -0.0120 -0.0130 257 LYS A CB  
2255 C  CG  A LYS A 256 ? 0.1969 0.1378 0.0938 0.0287  -0.0397 -0.0049 257 LYS A CG  
2256 C  CG  B LYS A 256 ? 0.1107 0.1639 0.1738 -0.0006 -0.0122 -0.0248 257 LYS A CG  
2257 C  CD  A LYS A 256 ? 0.2176 0.1353 0.2016 -0.0421 0.0103  -0.0450 257 LYS A CD  
2258 C  CD  B LYS A 256 ? 0.3012 0.1896 0.2022 0.0789  -0.0813 -0.0588 257 LYS A CD  
2259 C  CE  A LYS A 256 ? 0.2498 0.1990 0.2739 -0.0052 -0.0434 -0.0697 257 LYS A CE  
2260 C  CE  B LYS A 256 ? 0.2286 0.3499 0.3321 0.0346  -0.1110 -0.0537 257 LYS A CE  
2261 N  NZ  A LYS A 256 ? 0.2261 0.1811 0.2680 -0.0333 0.0340  -0.0361 257 LYS A NZ  
2262 N  NZ  B LYS A 256 ? 0.3382 0.3549 0.3249 -0.0359 -0.0527 0.0812  257 LYS A NZ  
2263 N  N   . ALA A 257 ? 0.1054 0.1453 0.0823 -0.0147 0.0137  0.0120  258 ALA A N   
2264 C  CA  . ALA A 257 ? 0.0957 0.1368 0.0891 -0.0148 0.0034  0.0000  258 ALA A CA  
2265 C  C   . ALA A 257 ? 0.1001 0.1431 0.0796 -0.0055 0.0098  0.0031  258 ALA A C   
2266 O  O   . ALA A 257 ? 0.1121 0.1785 0.0876 0.0000  0.0124  -0.0078 258 ALA A O   
2267 C  CB  . ALA A 257 ? 0.1411 0.1580 0.1060 -0.0244 0.0098  0.0124  258 ALA A CB  
2268 N  N   . SER A 258 ? 0.0966 0.1418 0.0776 -0.0006 0.0121  0.0073  259 SER A N   
2269 C  CA  . SER A 258 ? 0.1024 0.1521 0.1058 -0.0026 0.0057  0.0063  259 SER A CA  
2270 C  C   . SER A 258 ? 0.0970 0.1834 0.1176 -0.0178 0.0355  -0.0057 259 SER A C   
2271 O  O   . SER A 258 ? 0.1040 0.2644 0.1547 0.0043  0.0305  0.0223  259 SER A O   
2272 C  CB  . SER A 258 ? 0.1198 0.1301 0.1157 -0.0113 0.0041  0.0083  259 SER A CB  
2273 O  OG  . SER A 258 ? 0.0979 0.1535 0.0947 -0.0083 0.0021  -0.0021 259 SER A OG  
2274 N  N   . PHE A 259 ? 0.1231 0.1908 0.1074 -0.0399 0.0138  0.0161  260 PHE A N   
2275 C  CA  . PHE A 259 ? 0.1510 0.2050 0.1445 -0.0507 0.0143  0.0441  260 PHE A CA  
2276 C  C   . PHE A 259 ? 0.2635 0.2802 0.1696 -0.1495 -0.0076 0.0865  260 PHE A C   
2277 O  O   . PHE A 259 ? 0.2917 0.2630 0.1787 -0.1093 -0.0513 0.0872  260 PHE A O   
2278 C  CB  . PHE A 259 ? 0.1344 0.1775 0.1887 -0.0417 -0.0065 0.0161  260 PHE A CB  
2279 C  CG  . PHE A 259 ? 0.1362 0.1634 0.1588 -0.0364 -0.0175 0.0452  260 PHE A CG  
2280 C  CD1 . PHE A 259 ? 0.1266 0.1529 0.1147 -0.0309 -0.0189 0.0065  260 PHE A CD1 
2281 C  CD2 . PHE A 259 ? 0.1728 0.1622 0.2366 -0.0142 -0.0030 0.0328  260 PHE A CD2 
2282 C  CE1 . PHE A 259 ? 0.1361 0.1546 0.1442 -0.0275 -0.0227 0.0195  260 PHE A CE1 
2283 C  CE2 . PHE A 259 ? 0.2030 0.1600 0.4210 -0.0258 -0.0038 0.1222  260 PHE A CE2 
2284 C  CZ  . PHE A 259 ? 0.1800 0.1559 0.2813 0.0070  0.0171  0.0120  260 PHE A CZ  
2285 N  N   . LYS A 260 ? 0.3000 0.5406 0.1944 -0.1859 -0.0049 0.1650  261 LYS A N   
2286 C  CA  . LYS A 260 ? 0.6019 0.6394 0.5291 -0.0725 0.0582  0.2709  261 LYS A CA  
2287 C  C   . LYS A 260 ? 0.9090 0.8551 0.5633 -0.0562 0.0137  0.0980  261 LYS A C   
2288 O  O   . LYS A 260 ? 0.8576 0.3362 0.8713 -0.0728 -0.1199 -0.0816 261 LYS A O   
2289 C  CB  . LYS A 260 ? 1.2819 0.5702 0.8464 -0.5285 0.0181  0.1831  261 LYS A CB  
2290 C  CG  . LYS A 260 ? 1.1507 0.9277 0.8824 -0.5558 0.1586  0.0000  261 LYS A CG  
2291 C  CD  . LYS A 260 ? 1.0719 0.9993 0.5932 0.0759  0.1673  -0.2415 261 LYS A CD  
2292 C  CE  . LYS A 260 ? 0.5917 0.7849 0.7178 0.1010  0.1336  0.1572  261 LYS A CE  
2293 N  NZ  . LYS A 260 ? 0.5931 0.5667 0.3646 -0.1331 -0.0138 0.2047  261 LYS A NZ  
2294 O  OXT . LYS A 260 ? 0.4815 1.0966 1.6253 -0.3203 -0.3533 0.2178  261 LYS A OXT 
2295 ZN ZN  . ZN  B .   ? 0.0675 0.0593 0.0681 -0.0005 -0.0054 0.0015  301 ZN  A ZN  
2296 F  F27 . WWO C .   ? 0.0856 0.0684 0.1165 -0.0003 -0.0211 0.0098  302 WWO A F27 
2297 C  C5  . WWO C .   ? 0.0824 0.0652 0.0949 -0.0057 -0.0142 0.0019  302 WWO A C5  
2298 C  C4  . WWO C .   ? 0.0917 0.0614 0.0791 -0.0030 -0.0127 0.0021  302 WWO A C4  
2299 S  S7  . WWO C .   ? 0.0715 0.0644 0.0822 -0.0027 -0.0120 -0.0013 302 WWO A S7  
2300 O  O9  . WWO C .   ? 0.0758 0.0707 0.0840 0.0020  -0.0137 -0.0034 302 WWO A O9  
2301 N  N10 . WWO C .   ? 0.0700 0.0644 0.0835 -0.0052 -0.0173 0.0013  302 WWO A N10 
2302 O  O8  . WWO C .   ? 0.0814 0.0712 0.0912 -0.0052 -0.0055 -0.0043 302 WWO A O8  
2303 C  C3  . WWO C .   ? 0.0789 0.0722 0.0904 0.0043  -0.0081 0.0028  302 WWO A C3  
2304 F  F12 . WWO C .   ? 0.0785 0.0799 0.1070 -0.0035 -0.0098 0.0098  302 WWO A F12 
2305 C  C2  . WWO C .   ? 0.0751 0.0898 0.1053 -0.0059 0.0041  0.0035  302 WWO A C2  
2306 F  F13 . WWO C .   ? 0.0856 0.1104 0.1193 -0.0102 0.0060  0.0177  302 WWO A F13 
2307 C  C6  . WWO C .   ? 0.0983 0.0776 0.0931 0.0000  -0.0109 0.0032  302 WWO A C6  
2308 C  C1  . WWO C .   ? 0.0917 0.0815 0.1160 -0.0030 -0.0017 0.0082  302 WWO A C1  
2309 S  S11 . WWO C .   ? 0.1172 0.1051 0.1324 -0.0043 0.0148  0.0223  302 WWO A S11 
2310 O  O22 . WWO C .   ? 0.1541 0.1312 0.1714 -0.0588 0.0192  -0.0078 302 WWO A O22 
2311 O  O23 . WWO C .   ? 0.1497 0.1237 0.1504 0.0127  0.0264  0.0478  302 WWO A O23 
2312 C  C21 . WWO C .   ? 0.1278 0.1555 0.1212 -0.0132 0.0337  0.0401  302 WWO A C21 
2313 C  C24 . WWO C .   ? 0.1966 0.1617 0.1729 0.0021  0.0344  0.0236  302 WWO A C24 
2314 O  O25 . WWO C .   ? 0.2349 0.1648 0.1490 0.0348  -0.0017 0.0250  302 WWO A O25 
2315 N  N26 . WWO C .   ? 0.1146 0.0811 0.1086 0.0043  -0.0197 0.0111  302 WWO A N26 
2316 C  C14 . WWO C .   ? 0.0989 0.0751 0.1353 0.0038  -0.0142 0.0141  302 WWO A C14 
2317 C  C15 . WWO C .   ? 0.1173 0.0791 0.1281 0.0013  -0.0255 -0.0013 302 WWO A C15 
2318 C  C20 . WWO C .   ? 0.1396 0.0934 0.1475 0.0133  -0.0320 -0.0125 302 WWO A C20 
2319 C  C19 . WWO C .   ? 0.1655 0.1014 0.1749 0.0154  -0.0476 -0.0225 302 WWO A C19 
2320 C  C18 . WWO C .   ? 0.1500 0.0953 0.1869 -0.0161 -0.0236 -0.0114 302 WWO A C18 
2321 C  C17 . WWO C .   ? 0.1476 0.1002 0.1753 -0.0160 -0.0098 -0.0074 302 WWO A C17 
2322 C  C16 . WWO C .   ? 0.1291 0.0767 0.1491 -0.0119 -0.0026 -0.0026 302 WWO A C16 
2323 F  F27 A WWO D .   ? 0.6496 0.8111 1.0522 0.0693  0.0601  -0.1811 303 WWO A F27 
2324 F  F27 B WWO D .   ? 0.2445 0.1592 0.2247 -0.0037 0.0526  -0.0362 303 WWO A F27 
2325 C  C5  A WWO D .   ? 0.5076 0.3916 0.9919 -0.1932 0.0714  -0.2687 303 WWO A C5  
2326 C  C5  B WWO D .   ? 0.2252 0.1745 0.1536 -0.0208 0.0057  0.0071  303 WWO A C5  
2327 C  C4  A WWO D .   ? 0.3515 0.3341 0.6521 -0.1127 -0.0219 -0.0835 303 WWO A C4  
2328 C  C4  B WWO D .   ? 0.2518 0.1840 0.1709 -0.0270 0.0516  0.0152  303 WWO A C4  
2329 S  S7  A WWO D .   ? 0.2675 0.1335 0.1802 -0.0172 0.0375  0.0043  303 WWO A S7  
2330 S  S7  B WWO D .   ? 0.3089 0.1633 0.1977 -0.0471 0.0741  0.0077  303 WWO A S7  
2331 O  O9  A WWO D .   ? 0.2610 0.1190 0.2694 0.0593  0.0348  0.0211  303 WWO A O9  
2332 O  O9  B WWO D .   ? 0.3088 0.3379 0.2248 0.0344  0.0803  0.0571  303 WWO A O9  
2333 N  N10 A WWO D .   ? 0.2008 0.2011 0.0627 -0.0034 0.0086  0.0256  303 WWO A N10 
2334 N  N10 B WWO D .   ? 0.1722 0.1301 0.5694 0.0048  -0.0308 -0.0922 303 WWO A N10 
2335 O  O8  A WWO D .   ? 0.1736 0.1323 0.1209 -0.0003 0.0342  -0.0074 303 WWO A O8  
2336 O  O8  B WWO D .   ? 0.2978 0.1600 0.1384 -0.0397 0.0597  0.0220  303 WWO A O8  
2337 C  C3  A WWO D .   ? 0.3801 0.4844 0.8309 -0.0274 -0.0245 0.0762  303 WWO A C3  
2338 C  C3  B WWO D .   ? 0.2127 0.1092 0.1673 -0.0340 0.0230  0.0244  303 WWO A C3  
2339 F  F12 A WWO D .   ? 0.5868 0.5942 0.9150 -0.0108 -0.1076 -0.0791 303 WWO A F12 
2340 F  F12 B WWO D .   ? 0.1565 0.1864 0.2057 -0.0215 -0.0131 0.0439  303 WWO A F12 
2341 C  C2  A WWO D .   ? 0.5307 0.5902 1.3385 -0.1647 -0.0520 -0.1077 303 WWO A C2  
2342 C  C2  B WWO D .   ? 0.1922 0.1727 0.2549 -0.0234 -0.0339 -0.0434 303 WWO A C2  
2343 F  F13 A WWO D .   ? 0.8213 0.8981 1.6052 0.1030  0.0943  0.2673  303 WWO A F13 
2344 F  F13 B WWO D .   ? 0.1506 0.2104 0.3856 -0.0417 -0.0113 0.0046  303 WWO A F13 
2345 C  C6  A WWO D .   ? 0.3801 0.6032 1.1231 -0.0763 -0.0846 -0.2381 303 WWO A C6  
2346 C  C6  B WWO D .   ? 0.2216 0.1689 0.2226 -0.0313 0.1062  0.0463  303 WWO A C6  
2347 C  C1  A WWO D .   ? 0.7063 0.5726 1.3210 0.0971  0.0478  -0.3310 303 WWO A C1  
2348 C  C1  B WWO D .   ? 0.2163 0.1573 0.3039 -0.0886 0.0454  -0.0275 303 WWO A C1  
2349 S  S11 A WWO D .   ? 0.8471 1.2324 1.7477 -0.1615 0.2084  -0.1225 303 WWO A S11 
2350 S  S11 B WWO D .   ? 0.2949 0.3262 0.6656 -0.1735 0.0105  -0.1265 303 WWO A S11 
2351 O  O22 A WWO D .   ? 1.9512 2.0634 1.7272 -0.1724 0.1398  -0.3116 303 WWO A O22 
2352 O  O22 B WWO D .   ? 0.4659 0.3231 0.8403 -0.0768 0.1720  -0.2969 303 WWO A O22 
2353 O  O23 A WWO D .   ? 2.3375 1.8293 0.9749 -0.3725 0.6328  0.5220  303 WWO A O23 
2354 O  O23 B WWO D .   ? 0.2382 0.6880 0.7809 -0.1247 0.0604  -0.0817 303 WWO A O23 
2355 C  C21 A WWO D .   ? 0.5590 0.8503 0.5564 -0.1216 -0.3449 -0.0454 303 WWO A C21 
2356 C  C21 B WWO D .   ? 0.2472 0.4167 0.6082 -0.0621 0.2058  0.0219  303 WWO A C21 
2357 C  C24 A WWO D .   ? 0.7375 0.3614 0.4851 0.1359  -0.1591 -0.0236 303 WWO A C24 
2358 C  C24 B WWO D .   ? 0.3230 0.1280 0.4366 -0.0526 0.1115  -0.0115 303 WWO A C24 
2359 O  O25 A WWO D .   ? 0.8924 0.2687 0.9189 -0.1163 -0.2894 -0.0900 303 WWO A O25 
2360 O  O25 B WWO D .   ? 0.2039 0.2240 0.5447 -0.0263 -0.0329 -0.0689 303 WWO A O25 
2361 N  N26 A WWO D .   ? 0.6560 0.5151 1.0154 0.1571  0.0071  -0.1511 303 WWO A N26 
2362 N  N26 B WWO D .   ? 0.2630 0.1756 0.3134 -0.1049 0.0093  -0.0153 303 WWO A N26 
2363 C  C14 A WWO D .   ? 0.5681 0.3165 0.5388 0.0454  0.0419  0.0230  303 WWO A C14 
2364 C  C14 B WWO D .   ? 0.4724 0.1764 0.4532 -0.0152 0.0763  0.0671  303 WWO A C14 
2365 C  C15 A WWO D .   ? 0.4923 0.3129 0.5370 0.0291  0.0631  0.0085  303 WWO A C15 
2366 C  C15 B WWO D .   ? 0.3267 0.1680 0.3522 -0.0177 0.0443  0.1216  303 WWO A C15 
2367 C  C20 A WWO D .   ? 0.4708 0.3109 0.4607 0.0233  0.0013  -0.0230 303 WWO A C20 
2368 C  C20 B WWO D .   ? 0.3445 0.1844 0.2509 0.0006  0.0544  0.1097  303 WWO A C20 
2369 C  C19 A WWO D .   ? 0.3181 0.2403 0.3458 -0.0035 -0.0187 0.0549  303 WWO A C19 
2370 C  C19 B WWO D .   ? 0.2904 0.2134 0.1712 -0.0132 0.0236  0.1014  303 WWO A C19 
2371 C  C18 A WWO D .   ? 0.4124 0.3434 0.3434 -0.1062 -0.0274 0.0732  303 WWO A C18 
2372 C  C18 B WWO D .   ? 0.3754 0.2426 0.2360 -0.0627 -0.0141 0.0900  303 WWO A C18 
2373 C  C17 A WWO D .   ? 0.5063 0.4559 0.4602 -0.0024 -0.0878 -0.0087 303 WWO A C17 
2374 C  C17 B WWO D .   ? 0.4228 0.3030 0.1280 -0.0335 0.0280  -0.0063 303 WWO A C17 
2375 C  C16 A WWO D .   ? 0.5856 0.4740 0.5799 0.0130  -0.0350 -0.0533 303 WWO A C16 
2376 C  C16 B WWO D .   ? 0.2314 0.2380 0.3210 0.0653  0.0392  0.0392  303 WWO A C16 
2377 S  S   . DMS E .   ? 0.2016 0.2500 0.1972 -0.0068 0.0130  -0.0405 304 DMS A S   
2378 O  O   . DMS E .   ? 0.2578 0.3285 0.3377 0.0244  0.0438  -0.1298 304 DMS A O   
2379 C  C1  . DMS E .   ? 0.1512 0.2745 0.2372 0.0399  0.0249  -0.0579 304 DMS A C1  
2380 C  C2  . DMS E .   ? 0.1675 0.2795 0.2484 -0.0121 -0.0110 -0.0035 304 DMS A C2  
2381 N  N1  . BCN F .   ? 0.3104 0.3095 0.3163 0.0092  0.0133  -0.0414 305 BCN A N1  
2382 C  C1  . BCN F .   ? 0.3337 0.4383 0.2167 -0.0978 0.0263  -0.0020 305 BCN A C1  
2383 C  C2  . BCN F .   ? 0.1757 0.6370 0.4375 -0.0645 -0.0564 0.1589  305 BCN A C2  
2384 O  O21 . BCN F .   ? 0.4180 0.6754 0.4458 -0.2264 -0.1374 0.2026  305 BCN A O21 
2385 O  O22 . BCN F .   ? 0.2549 0.4208 0.4237 -0.1180 -0.0560 0.1190  305 BCN A O22 
2386 C  C3  . BCN F .   ? 0.2824 0.1978 0.3036 0.0121  0.0524  0.0778  305 BCN A C3  
2387 C  C4  . BCN F .   ? 0.4020 0.5680 0.5105 -0.0956 0.1093  0.1501  305 BCN A C4  
2388 O  O4  . BCN F .   ? 0.5317 0.4870 0.7437 -0.1699 -0.1630 -0.1764 305 BCN A O4  
2389 C  C5  . BCN F .   ? 0.2511 0.1374 0.2396 -0.0122 0.0722  0.0055  305 BCN A C5  
2390 C  C6  . BCN F .   ? 0.8167 0.4733 0.4760 -0.0882 -0.1738 -0.1890 305 BCN A C6  
2391 O  O6  . BCN F .   ? 0.8708 0.4417 0.4837 -0.4205 0.1706  0.0051  305 BCN A O6  
2392 C  C1  . PEG G .   ? 0.1184 0.2608 0.3115 -0.0384 -0.0284 -0.0046 306 PEG A C1  
2393 O  O1  . PEG G .   ? 0.1318 0.3510 0.2533 -0.0357 -0.0208 0.0023  306 PEG A O1  
2394 C  C2  . PEG G .   ? 0.1148 0.2576 0.3528 -0.0328 -0.0252 -0.0289 306 PEG A C2  
2395 O  O2  . PEG G .   ? 0.2588 0.3048 0.3978 -0.0507 -0.0164 0.0177  306 PEG A O2  
2396 C  C3  . PEG G .   ? 0.3745 0.5192 0.2933 -0.1377 -0.0221 -0.0593 306 PEG A C3  
2397 C  C4  . PEG G .   ? 0.2475 0.4469 0.3257 -0.0877 -0.1015 0.0006  306 PEG A C4  
2398 O  O4  . PEG G .   ? 1.0286 0.9994 0.4652 -0.2234 0.1495  -0.1098 306 PEG A O4  
2399 C  C1  . EDO H .   ? 0.2223 0.2134 0.2062 0.0478  0.0410  0.0315  307 EDO A C1  
2400 O  O1  . EDO H .   ? 0.6226 0.6506 0.4363 0.0474  0.0896  -0.0916 307 EDO A O1  
2401 C  C2  . EDO H .   ? 0.1341 0.1463 0.1330 -0.0020 -0.0023 -0.0214 307 EDO A C2  
2402 O  O2  . EDO H .   ? 0.2651 0.2118 0.2389 0.0240  0.0842  -0.0030 307 EDO A O2  
2403 C  C1  . EDO I .   ? 0.2189 0.3443 0.2473 -0.0065 -0.0003 0.0732  308 EDO A C1  
2404 O  O1  . EDO I .   ? 0.1738 0.2998 0.2488 0.0078  0.0228  -0.0233 308 EDO A O1  
2405 C  C2  . EDO I .   ? 0.3461 0.2056 0.2685 0.0241  0.0115  0.0386  308 EDO A C2  
2406 O  O2  . EDO I .   ? 0.2006 0.2257 0.2228 0.0065  -0.0001 -0.0148 308 EDO A O2  
2407 N  N1  . BCN J .   ? 0.3980 0.3644 0.4923 -0.0487 -0.0428 -0.0329 309 BCN A N1  
2408 C  C1  . BCN J .   ? 0.4300 0.4289 0.4510 0.0807  -0.0520 -0.1089 309 BCN A C1  
2409 C  C2  . BCN J .   ? 0.4083 0.4489 0.4796 0.1870  0.0131  -0.1925 309 BCN A C2  
2410 O  O21 . BCN J .   ? 0.3477 0.4986 0.5047 0.1238  0.0241  -0.0646 309 BCN A O21 
2411 O  O22 . BCN J .   ? 0.9413 0.4959 0.7961 0.0480  -0.0785 0.1252  309 BCN A O22 
2412 C  C3  . BCN J .   ? 0.3165 0.2951 0.2428 0.0381  0.0017  -0.0741 309 BCN A C3  
2413 C  C4  . BCN J .   ? 0.4090 0.3327 0.1659 0.0093  0.0982  -0.0608 309 BCN A C4  
2414 O  O4  . BCN J .   ? 0.3959 0.4320 0.3813 0.0485  0.0230  -0.0918 309 BCN A O4  
2415 C  C5  . BCN J .   ? 0.3010 0.2960 0.3662 -0.0734 -0.0007 -0.0960 309 BCN A C5  
2416 C  C6  . BCN J .   ? 0.2648 0.4790 0.3844 0.0339  0.0182  -0.0233 309 BCN A C6  
2417 O  O6  . BCN J .   ? 0.3425 0.2912 0.2354 0.0302  0.0689  -0.0588 309 BCN A O6  
2418 N  N1  . BCN K .   ? 0.2075 0.3005 0.2730 -0.0326 0.0110  -0.0791 310 BCN A N1  
2419 C  C1  . BCN K .   ? 0.2450 0.2809 0.3458 0.0555  0.0850  -0.0458 310 BCN A C1  
2420 C  C2  . BCN K .   ? 0.5971 0.4835 0.6053 -0.0908 0.0040  0.0615  310 BCN A C2  
2421 O  O21 . BCN K .   ? 0.5892 0.5902 0.5939 0.0220  0.0666  -0.1544 310 BCN A O21 
2422 O  O22 . BCN K .   ? 0.3887 0.2491 0.5769 0.1121  0.0566  0.0685  310 BCN A O22 
2423 C  C3  . BCN K .   ? 0.1953 0.1747 0.2998 0.0076  0.0718  -0.0912 310 BCN A C3  
2424 C  C4  . BCN K .   ? 0.2770 0.1836 0.2274 -0.0032 0.0081  -0.1107 310 BCN A C4  
2425 O  O4  . BCN K .   ? 0.3878 0.3849 0.2949 -0.0271 0.0848  -0.0012 310 BCN A O4  
2426 C  C5  . BCN K .   ? 0.3463 0.3422 0.4020 -0.0688 -0.0013 -0.0043 310 BCN A C5  
2427 C  C6  . BCN K .   ? 0.4456 0.4747 0.4341 -0.0910 0.1110  0.0272  310 BCN A C6  
2428 O  O6  . BCN K .   ? 0.3161 0.2725 0.3479 -0.0483 0.0526  -0.0167 310 BCN A O6  
2429 O  O   . HOH L .   ? 0.2667 0.2628 0.3542 -0.0710 -0.0232 -0.0505 401 HOH A O   
2430 O  O   . HOH L .   ? 0.6662 0.1967 0.3601 0.1444  -0.1150 -0.0355 402 HOH A O   
2431 O  O   . HOH L .   ? 0.1851 0.3355 0.2366 -0.0240 -0.0212 0.0353  403 HOH A O   
2432 O  O   . HOH L .   ? 0.2263 0.3323 0.3932 0.0331  -0.0234 -0.0159 404 HOH A O   
2433 O  O   . HOH L .   ? 0.9172 0.5321 1.5938 -0.1196 -0.5113 0.1053  405 HOH A O   
2434 O  O   . HOH L .   ? 0.3343 0.5354 0.1516 0.1943  0.0597  0.0331  406 HOH A O   
2435 O  O   . HOH L .   ? 0.4181 0.5546 0.2245 -0.0839 0.0048  0.0000  407 HOH A O   
2436 O  O   . HOH L .   ? 0.4884 0.2680 0.3118 0.0758  0.0776  -0.0248 408 HOH A O   
2437 O  O   . HOH L .   ? 0.2689 0.2743 0.2804 0.0485  -0.0049 -0.0104 409 HOH A O   
2438 O  O   . HOH L .   ? 0.2939 0.6769 0.2813 0.1193  -0.1103 -0.1378 410 HOH A O   
2439 O  O   . HOH L .   ? 0.5338 0.3310 0.4013 -0.1798 0.1985  -0.0895 411 HOH A O   
2440 O  O   . HOH L .   ? 0.3578 0.1705 0.1800 -0.0465 0.0833  -0.0548 412 HOH A O   
2441 O  O   . HOH L .   ? 0.4271 0.2739 0.3384 -0.0715 -0.1873 -0.0687 413 HOH A O   
2442 O  O   . HOH L .   ? 0.2405 0.2414 0.3944 0.0322  -0.0222 -0.1316 414 HOH A O   
2443 O  O   . HOH L .   ? 0.2098 0.2790 0.4054 0.0942  -0.1124 -0.0634 415 HOH A O   
2444 O  O   . HOH L .   ? 0.3682 0.2004 0.1829 -0.0656 -0.1000 0.0520  416 HOH A O   
2445 O  O   . HOH L .   ? 0.1116 0.2928 0.2202 -0.0298 -0.0203 0.0111  417 HOH A O   
2446 O  O   . HOH L .   ? 0.4880 0.4176 0.4183 0.0584  0.2014  -0.0410 418 HOH A O   
2447 O  O   . HOH L .   ? 0.2642 0.2040 0.2398 0.0274  0.0184  0.0381  419 HOH A O   
2448 O  O   . HOH L .   ? 0.1764 0.1826 0.2264 0.0046  0.0099  -0.0093 420 HOH A O   
2449 O  O   . HOH L .   ? 0.2166 0.3149 0.2076 -0.0571 0.0645  -0.1319 421 HOH A O   
2450 O  O   . HOH L .   ? 0.3206 0.3088 0.2818 0.0584  0.1280  0.0168  422 HOH A O   
2451 O  O   . HOH L .   ? 0.3045 0.3280 0.2294 -0.0313 -0.0405 0.0842  423 HOH A O   
2452 O  O   . HOH L .   ? 0.3695 0.1950 0.2531 -0.0584 0.1152  -0.0631 424 HOH A O   
2453 O  O   . HOH L .   ? 0.5012 0.1837 0.3785 -0.0284 -0.0873 0.1207  425 HOH A O   
2454 O  O   . HOH L .   ? 0.2964 0.3375 0.2098 0.1045  0.0414  0.0159  426 HOH A O   
2455 O  O   . HOH L .   ? 0.4171 0.1850 0.2847 -0.0564 -0.0767 -0.0292 427 HOH A O   
2456 O  O   . HOH L .   ? 0.1860 0.5722 0.2099 0.0195  -0.0159 0.0815  428 HOH A O   
2457 O  O   . HOH L .   ? 0.2178 0.1752 0.1827 -0.0059 0.0137  -0.0105 429 HOH A O   
2458 O  O   . HOH L .   ? 0.1624 0.2275 0.1973 0.0274  0.0324  0.0351  430 HOH A O   
2459 O  O   . HOH L .   ? 0.3558 0.4447 0.2989 -0.1140 0.0896  -0.0877 431 HOH A O   
2460 O  O   . HOH L .   ? 0.3172 0.3705 0.6348 -0.1242 0.0445  0.2097  432 HOH A O   
2461 O  O   . HOH L .   ? 0.4410 0.1782 0.1420 -0.0557 0.1085  -0.0208 433 HOH A O   
2462 O  O   . HOH L .   ? 0.3095 0.3506 0.3946 -0.0557 0.0478  0.1472  434 HOH A O   
2463 O  O   . HOH L .   ? 0.4259 0.5123 0.6330 0.0285  -0.0538 -0.0127 435 HOH A O   
2464 O  O   . HOH L .   ? 0.1852 0.5601 0.2615 0.0828  0.0140  0.0059  436 HOH A O   
2465 O  O   . HOH L .   ? 0.2919 0.3185 0.3524 -0.0339 0.0860  0.0644  437 HOH A O   
2466 O  O   . HOH L .   ? 0.5302 0.8040 0.2453 -0.2639 -0.0361 -0.0987 438 HOH A O   
2467 O  O   . HOH L .   ? 0.0976 0.1043 0.0978 -0.0159 0.0115  -0.0065 439 HOH A O   
2468 O  O   . HOH L .   ? 0.5072 0.2194 0.3472 -0.0266 -0.1682 0.0113  440 HOH A O   
2469 O  O   . HOH L .   ? 0.1089 0.0860 0.0668 -0.0003 0.0043  0.0049  441 HOH A O   
2470 O  O   . HOH L .   ? 0.1659 0.1895 0.2153 0.0216  0.0156  0.0557  442 HOH A O   
2471 O  O   . HOH L .   ? 0.1711 0.1497 0.1738 0.0085  -0.0195 -0.0130 443 HOH A O   
2472 O  O   . HOH L .   ? 0.3348 0.1611 0.1572 -0.0381 -0.0320 -0.0068 444 HOH A O   
2473 O  O   . HOH L .   ? 0.2389 0.5055 0.3434 -0.1061 0.1036  0.0082  445 HOH A O   
2474 O  O   . HOH L .   ? 0.3828 0.6126 0.1155 -0.1394 0.0401  0.0379  446 HOH A O   
2475 O  O   . HOH L .   ? 0.3612 0.2382 0.4542 -0.0876 -0.0120 -0.0496 447 HOH A O   
2476 O  O   . HOH L .   ? 0.2145 0.1669 0.2675 0.0109  0.0132  0.0487  448 HOH A O   
2477 O  O   . HOH L .   ? 0.6075 0.1754 0.1200 0.0287  -0.0509 -0.0131 449 HOH A O   
2478 O  O   . HOH L .   ? 0.1583 0.1494 0.1940 0.0017  -0.0832 -0.0368 450 HOH A O   
2479 O  O   . HOH L .   ? 0.3826 0.2002 0.3795 -0.1377 0.0148  0.0423  451 HOH A O   
2480 O  O   . HOH L .   ? 0.2861 0.1992 0.2328 -0.0533 -0.0377 0.0230  452 HOH A O   
2481 O  O   . HOH L .   ? 0.3601 0.4742 0.2725 0.0278  0.0493  0.0161  453 HOH A O   
2482 O  O   . HOH L .   ? 0.2166 0.3154 0.4029 0.0467  0.0005  0.0461  454 HOH A O   
2483 O  O   . HOH L .   ? 0.3894 0.4970 0.2833 -0.0043 0.0066  0.0483  455 HOH A O   
2484 O  O   . HOH L .   ? 0.3468 0.5480 0.3251 0.0839  0.0000  -0.0646 456 HOH A O   
2485 O  O   . HOH L .   ? 0.3996 0.4291 0.4068 0.0109  -0.0017 -0.0066 457 HOH A O   
2486 O  O   . HOH L .   ? 0.3167 0.2687 0.3621 0.0027  0.0518  0.1303  458 HOH A O   
2487 O  O   . HOH L .   ? 0.1095 0.2879 0.2901 0.0242  0.0142  0.1028  459 HOH A O   
2488 O  O   . HOH L .   ? 0.2935 0.2831 0.5392 0.1230  -0.0098 0.0193  460 HOH A O   
2489 O  O   . HOH L .   ? 0.2468 0.2560 0.4471 0.0410  0.0531  -0.0306 461 HOH A O   
2490 O  O   . HOH L .   ? 0.1924 0.2107 0.2973 -0.0093 0.0198  -0.0421 462 HOH A O   
2491 O  O   . HOH L .   ? 0.1243 0.0842 0.1059 -0.0006 0.0122  -0.0020 463 HOH A O   
2492 O  O   . HOH L .   ? 0.3801 0.1702 0.1845 -0.0608 0.0044  0.0634  464 HOH A O   
2493 O  O   . HOH L .   ? 0.4762 0.4956 0.3546 -0.0637 -0.0529 0.2459  465 HOH A O   
2494 O  O   . HOH L .   ? 0.3237 0.1902 0.2177 -0.0296 -0.0837 0.0522  466 HOH A O   
2495 O  O   . HOH L .   ? 0.5145 0.1596 0.1759 -0.0772 -0.0474 -0.0322 467 HOH A O   
2496 O  O   . HOH L .   ? 0.3224 0.2640 0.4853 -0.0204 -0.1316 0.0997  468 HOH A O   
2497 O  O   . HOH L .   ? 0.1659 0.1797 0.1363 0.0152  0.0476  0.0555  469 HOH A O   
2498 O  O   . HOH L .   ? 0.3953 0.3903 0.3255 0.1525  -0.1586 -0.1473 470 HOH A O   
2499 O  O   . HOH L .   ? 0.2376 0.1748 0.1947 0.0006  -0.0110 -0.0203 471 HOH A O   
2500 O  O   . HOH L .   ? 0.1207 0.0869 0.1120 0.0044  0.0136  -0.0126 472 HOH A O   
2501 O  O   . HOH L .   ? 0.1589 0.1903 0.2444 -0.0608 -0.0284 0.0617  473 HOH A O   
2502 O  O   . HOH L .   ? 0.5026 0.4235 0.5537 -0.1729 0.0741  -0.1405 474 HOH A O   
2503 O  O   . HOH L .   ? 0.1838 0.2423 0.1735 0.0395  0.0364  0.0124  475 HOH A O   
2504 O  O   . HOH L .   ? 0.1787 0.1583 0.2241 0.0188  0.0285  0.0124  476 HOH A O   
2505 O  O   . HOH L .   ? 0.1895 0.1027 0.1679 -0.0412 0.0000  -0.0157 477 HOH A O   
2506 O  O   . HOH L .   ? 0.3617 0.2094 0.5026 0.0469  -0.0663 0.1344  478 HOH A O   
2507 O  O   . HOH L .   ? 0.1842 0.1755 0.2002 0.0425  0.0248  -0.0027 479 HOH A O   
2508 O  O   . HOH L .   ? 0.2475 0.1706 0.2039 -0.0274 0.0057  -0.0098 480 HOH A O   
2509 O  O   . HOH L .   ? 0.2910 0.2872 0.1323 0.0204  0.0103  0.0250  481 HOH A O   
2510 O  O   . HOH L .   ? 0.2269 0.0955 0.1691 -0.0140 -0.0054 0.0024  482 HOH A O   
2511 O  O   . HOH L .   ? 0.2741 0.2527 0.2168 -0.1098 0.0909  -0.1039 483 HOH A O   
2512 O  O   . HOH L .   ? 0.2834 0.2540 0.3770 0.0816  -0.1697 -0.1878 484 HOH A O   
2513 O  O   . HOH L .   ? 0.1884 0.1970 0.2016 0.0046  -0.0230 0.0080  485 HOH A O   
2514 O  O   . HOH L .   ? 0.1554 0.1235 0.1708 0.0211  -0.0582 0.0137  486 HOH A O   
2515 O  O   . HOH L .   ? 0.2162 0.1633 0.2425 -0.0096 -0.0085 0.0868  487 HOH A O   
2516 O  O   . HOH L .   ? 0.1800 0.2748 0.2349 -0.0113 -0.0697 0.0099  488 HOH A O   
2517 O  O   . HOH L .   ? 0.1217 0.1322 0.1174 0.0111  -0.0286 0.0097  489 HOH A O   
2518 O  O   . HOH L .   ? 0.3415 0.2157 0.1890 -0.0320 0.0654  0.0533  490 HOH A O   
2519 O  O   . HOH L .   ? 0.1321 0.1587 0.1620 0.0160  -0.0137 0.0093  491 HOH A O   
2520 O  O   . HOH L .   ? 0.2863 0.2229 0.1414 0.0089  -0.0233 -0.0237 492 HOH A O   
2521 O  O   . HOH L .   ? 0.3691 0.4867 0.1489 0.0020  0.0465  0.0734  493 HOH A O   
2522 O  O   . HOH L .   ? 0.3815 0.3722 0.2188 0.1412  0.0181  0.0663  494 HOH A O   
2523 O  O   . HOH L .   ? 0.1156 0.1590 0.1457 -0.0219 -0.0008 0.0052  495 HOH A O   
2524 O  O   . HOH L .   ? 0.3158 0.1817 0.2761 -0.0665 0.0551  -0.0646 496 HOH A O   
2525 O  O   . HOH L .   ? 0.1788 0.2110 0.1705 0.0348  0.0265  0.0610  497 HOH A O   
2526 O  O   . HOH L .   ? 0.3278 0.2883 0.1758 0.0320  0.0636  -0.0597 498 HOH A O   
2527 O  O   . HOH L .   ? 0.4054 0.4099 0.4715 0.0913  -0.2181 0.0174  499 HOH A O   
2528 O  O   . HOH L .   ? 0.1961 0.1598 0.1464 0.0183  0.0494  -0.0059 500 HOH A O   
2529 O  O   . HOH L .   ? 0.4390 0.2809 0.2727 -0.0024 -0.0568 -0.0335 501 HOH A O   
2530 O  O   . HOH L .   ? 0.1647 0.0917 0.1598 -0.0105 0.0017  0.0021  502 HOH A O   
2531 O  O   . HOH L .   ? 0.0937 0.0898 0.0903 -0.0043 0.0130  -0.0030 503 HOH A O   
2532 O  O   . HOH L .   ? 0.4341 0.6014 0.3037 -0.3499 -0.0166 0.0096  504 HOH A O   
2533 O  O   . HOH L .   ? 0.2496 0.4271 0.1784 -0.1262 0.0282  -0.1160 505 HOH A O   
2534 O  O   . HOH L .   ? 0.2184 0.2305 0.4047 0.0197  -0.0474 -0.1360 506 HOH A O   
2535 O  O   . HOH L .   ? 0.1953 0.1236 0.1525 -0.0151 -0.0020 -0.0088 507 HOH A O   
2536 O  O   . HOH L .   ? 0.1187 0.0799 0.0988 0.0203  -0.0066 -0.0082 508 HOH A O   
2537 O  O   . HOH L .   ? 0.1301 0.1289 0.2166 -0.0320 -0.0381 0.0008  509 HOH A O   
2538 O  O   . HOH L .   ? 0.1844 0.1216 0.1504 0.0034  -0.0094 0.0140  510 HOH A O   
2539 O  O   . HOH L .   ? 0.2178 0.5310 0.3935 0.0443  -0.0882 0.1052  511 HOH A O   
2540 O  O   . HOH L .   ? 0.0804 0.1356 0.1512 0.0041  -0.0161 -0.0297 512 HOH A O   
2541 O  O   . HOH L .   ? 0.1033 0.1094 0.0984 0.0296  -0.0027 -0.0031 513 HOH A O   
2542 O  O   . HOH L .   ? 0.1908 0.2793 0.1552 -0.0265 -0.0080 -0.0631 514 HOH A O   
2543 O  O   . HOH L .   ? 0.2982 0.4882 0.3601 -0.0777 -0.0060 0.2194  515 HOH A O   
2544 O  O   . HOH L .   ? 0.3034 0.3291 0.1712 -0.0469 -0.0851 0.0566  516 HOH A O   
2545 O  O   . HOH L .   ? 0.1580 0.1216 0.1608 0.0392  0.0048  0.0132  517 HOH A O   
2546 O  O   . HOH L .   ? 0.1200 0.1142 0.1248 0.0263  -0.0107 0.0220  518 HOH A O   
2547 O  O   . HOH L .   ? 0.5717 0.3402 0.1789 -0.0277 0.0790  0.0910  519 HOH A O   
2548 O  O   . HOH L .   ? 0.1448 0.1600 0.1621 -0.0052 -0.0370 0.0214  520 HOH A O   
2549 O  O   . HOH L .   ? 0.2685 0.1724 0.2445 0.0182  -0.0773 -0.0315 521 HOH A O   
2550 O  O   . HOH L .   ? 0.2243 0.3370 0.3829 0.0000  0.0798  -0.1555 522 HOH A O   
2551 O  O   . HOH L .   ? 0.4287 0.4083 0.2899 0.0711  -0.1700 0.0000  523 HOH A O   
2552 O  O   . HOH L .   ? 0.4352 0.2443 0.1761 0.0830  0.0234  0.0571  524 HOH A O   
2553 O  O   . HOH L .   ? 0.1699 0.1675 0.1464 0.0274  0.0193  0.0299  525 HOH A O   
2554 O  O   . HOH L .   ? 0.1931 0.2531 0.7810 -0.0088 0.0308  0.0164  526 HOH A O   
2555 O  O   . HOH L .   ? 0.2522 0.3393 0.7753 0.1212  -0.2257 -0.0465 527 HOH A O   
2556 O  O   . HOH L .   ? 0.3323 0.2816 0.3560 0.0604  -0.0359 -0.0790 528 HOH A O   
2557 O  O   . HOH L .   ? 0.1415 0.2247 0.1872 0.0060  0.0038  0.0102  529 HOH A O   
2558 O  O   . HOH L .   ? 0.4456 0.1685 0.2745 0.1337  -0.0976 -0.0255 530 HOH A O   
2559 O  O   . HOH L .   ? 0.2489 0.2899 0.2966 -0.0282 -0.0252 0.1641  531 HOH A O   
2560 O  O   . HOH L .   ? 0.2515 0.3046 0.2186 -0.0811 0.0680  0.0062  532 HOH A O   
2561 O  O   . HOH L .   ? 0.2048 0.1448 0.2852 -0.0098 0.0480  -0.0276 533 HOH A O   
2562 O  O   . HOH L .   ? 0.1759 0.1563 0.1596 -0.0219 0.0142  -0.0005 534 HOH A O   
2563 O  O   . HOH L .   ? 0.7967 0.3616 0.4074 -0.0153 0.1049  0.0670  535 HOH A O   
2564 O  O   . HOH L .   ? 0.2709 0.0962 0.1755 0.0397  -0.0595 -0.0089 536 HOH A O   
2565 O  O   . HOH L .   ? 0.2115 0.1107 0.2178 0.0182  0.0065  -0.0094 537 HOH A O   
2566 O  O   . HOH L .   ? 0.3443 0.2639 0.5297 -0.0131 -0.0170 -0.1661 538 HOH A O   
2567 O  O   . HOH L .   ? 0.4187 0.3910 0.4189 0.0085  0.0065  0.0132  539 HOH A O   
2568 O  O   . HOH L .   ? 0.1676 0.2599 0.2402 0.0073  -0.0178 0.0096  540 HOH A O   
2569 O  O   . HOH L .   ? 0.2152 0.1093 0.1363 0.0300  -0.0060 0.0092  541 HOH A O   
2570 O  O   . HOH L .   ? 0.1722 0.2660 0.1898 0.0859  -0.0586 -0.0410 542 HOH A O   
2571 O  O   . HOH L .   ? 0.2020 0.4255 0.2185 0.0020  0.0289  -0.0593 543 HOH A O   
2572 O  O   . HOH L .   ? 0.2342 0.4557 0.1251 0.1415  -0.0614 -0.0566 544 HOH A O   
2573 O  O   . HOH L .   ? 0.2319 0.3104 0.2093 0.1321  0.0222  -0.0403 545 HOH A O   
2574 O  O   . HOH L .   ? 0.3228 0.3919 0.4359 0.1099  0.0408  0.0186  546 HOH A O   
2575 O  O   . HOH L .   ? 0.2883 0.2982 0.2315 -0.0751 -0.0220 -0.0188 547 HOH A O   
2576 O  O   . HOH L .   ? 0.4144 0.2432 0.2203 -0.0476 0.0639  -0.0535 548 HOH A O   
2577 O  O   . HOH L .   ? 0.1768 0.1286 0.2093 -0.0264 0.0280  -0.0195 549 HOH A O   
2578 O  O   . HOH L .   ? 0.3842 0.4942 0.3677 -0.0450 0.0208  -0.0760 550 HOH A O   
2579 O  O   . HOH L .   ? 0.3075 0.3648 0.6204 0.0135  -0.2189 0.0992  551 HOH A O   
2580 O  O   . HOH L .   ? 0.1080 0.2632 0.1524 0.0010  -0.0081 -0.0205 552 HOH A O   
2581 O  O   . HOH L .   ? 0.4153 0.3237 0.1817 0.2201  -0.0595 0.0166  553 HOH A O   
2582 O  O   . HOH L .   ? 0.1493 0.2198 0.2405 0.0228  0.0068  0.0231  554 HOH A O   
2583 O  O   . HOH L .   ? 0.4827 0.7520 0.4408 0.0754  0.2380  -0.1421 555 HOH A O   
2584 O  O   . HOH L .   ? 0.1902 0.1771 0.1730 0.0287  0.0310  0.0822  556 HOH A O   
2585 O  O   . HOH L .   ? 0.1014 0.1492 0.2158 -0.0071 -0.0041 -0.0124 557 HOH A O   
2586 O  O   . HOH L .   ? 0.4427 0.2421 0.1973 0.1560  0.0535  0.0441  558 HOH A O   
2587 O  O   . HOH L .   ? 0.0859 0.1838 0.1520 0.0263  0.0059  -0.0236 559 HOH A O   
2588 O  O   . HOH L .   ? 0.2445 0.1814 0.2480 0.0148  0.0684  0.0414  560 HOH A O   
2589 O  O   . HOH L .   ? 0.2267 0.2088 0.5461 -0.0537 0.0304  0.0810  561 HOH A O   
2590 O  O   . HOH L .   ? 0.3048 0.4007 0.3064 -0.0793 0.0329  -0.0076 562 HOH A O   
2591 O  O   . HOH L .   ? 0.2489 0.2676 0.1957 -0.0873 -0.0419 -0.0195 563 HOH A O   
2592 O  O   . HOH L .   ? 0.1824 0.1735 0.1494 0.0024  0.0000  -0.0060 564 HOH A O   
2593 O  O   . HOH L .   ? 0.3319 0.3885 0.2296 -0.0656 0.0733  -0.1552 565 HOH A O   
2594 O  O   . HOH L .   ? 0.6741 0.1772 0.8100 -0.0171 0.1385  -0.0114 566 HOH A O   
2595 O  O   . HOH L .   ? 0.3271 0.3928 0.4056 0.1661  -0.1981 -0.1536 567 HOH A O   
2596 O  O   . HOH L .   ? 0.2879 0.2082 0.3465 -0.1057 -0.1341 0.1037  568 HOH A O   
2597 O  O   . HOH L .   ? 0.3233 0.7258 0.3508 -0.0087 -0.0048 0.1544  569 HOH A O   
2598 O  O   . HOH L .   ? 0.2204 0.2669 0.2280 0.0231  -0.0140 -0.0144 570 HOH A O   
2599 O  O   . HOH L .   ? 0.3106 0.1664 0.4783 -0.0219 0.0294  0.0781  571 HOH A O   
2600 O  O   . HOH L .   ? 0.2363 0.2105 0.3982 0.0060  -0.0052 -0.0392 572 HOH A O   
2601 O  O   . HOH L .   ? 0.3019 0.3562 0.2969 -0.0945 0.0856  0.0216  573 HOH A O   
2602 O  O   . HOH L .   ? 1.1840 0.8213 0.5758 -0.1555 -0.2423 -0.1891 574 HOH A O   
2603 O  O   . HOH L .   ? 0.1256 0.1199 0.1635 0.0068  -0.0107 0.0102  575 HOH A O   
2604 O  O   . HOH L .   ? 0.2021 0.0870 0.1693 0.0178  -0.0063 0.0261  576 HOH A O   
2605 O  O   . HOH L .   ? 0.1686 0.2162 0.1562 0.0031  -0.0170 0.0480  577 HOH A O   
2606 O  O   . HOH L .   ? 0.3449 0.2709 0.3007 -0.0013 -0.1172 -0.0240 578 HOH A O   
2607 O  O   . HOH L .   ? 0.1988 0.2155 0.2933 0.0720  -0.0612 -0.0790 579 HOH A O   
2608 O  O   . HOH L .   ? 0.3616 0.3037 0.3156 0.0773  0.1136  0.1050  580 HOH A O   
2609 O  O   . HOH L .   ? 0.2520 0.3231 0.2178 0.0454  -0.0201 -0.0200 581 HOH A O   
2610 O  O   . HOH L .   ? 0.3736 0.5260 0.2136 -0.1891 0.0222  0.0835  582 HOH A O   
2611 O  O   . HOH L .   ? 0.1307 0.2784 0.2273 0.0496  0.0383  0.0342  583 HOH A O   
2612 O  O   . HOH L .   ? 0.1744 0.1722 0.2565 0.0689  -0.0254 -0.0212 584 HOH A O   
2613 O  O   . HOH L .   ? 0.2549 0.2820 0.1871 -0.0120 0.0322  -0.0138 585 HOH A O   
2614 O  O   . HOH L .   ? 0.1634 0.1631 0.2109 0.0173  -0.0511 -0.0856 586 HOH A O   
2615 O  O   . HOH L .   ? 0.5141 0.5382 0.5557 0.2435  0.1908  0.2151  587 HOH A O   
2616 O  O   . HOH L .   ? 0.1618 0.6330 0.3959 -0.0516 -0.0564 -0.0856 588 HOH A O   
2617 O  O   . HOH L .   ? 0.3129 0.4002 0.2822 0.1861  0.1106  0.0538  589 HOH A O   
2618 O  O   . HOH L .   ? 0.1042 0.2371 0.1321 -0.0197 -0.0313 0.0460  590 HOH A O   
2619 O  O   . HOH L .   ? 0.1453 0.3248 0.2526 0.0538  -0.0207 -0.0074 591 HOH A O   
2620 O  O   . HOH L .   ? 0.4902 0.5479 0.2709 0.0406  0.1072  -0.1497 592 HOH A O   
2621 O  O   . HOH L .   ? 0.1957 0.1555 0.1888 0.0048  -0.0059 0.0593  593 HOH A O   
2622 O  O   . HOH L .   ? 0.1870 0.1621 0.1970 -0.0697 -0.0324 -0.0241 594 HOH A O   
2623 O  O   . HOH L .   ? 0.4011 0.2757 0.4002 0.0285  0.1114  0.1212  595 HOH A O   
2624 O  O   . HOH L .   ? 0.3709 0.1675 0.2342 -0.0119 0.0370  0.0076  596 HOH A O   
2625 O  O   . HOH L .   ? 0.3556 0.3768 0.2134 -0.1784 0.0340  -0.0065 597 HOH A O   
2626 O  O   . HOH L .   ? 0.3673 0.1932 0.2524 0.1061  0.0285  0.0747  598 HOH A O   
2627 O  O   . HOH L .   ? 0.1425 0.1782 0.1336 0.0127  0.0040  0.0160  599 HOH A O   
2628 O  O   . HOH L .   ? 0.4788 0.3379 0.3914 -0.0712 -0.2063 0.0718  600 HOH A O   
2629 O  O   . HOH L .   ? 0.2455 0.7059 0.5616 -0.1339 0.0511  -0.0252 601 HOH A O   
2630 O  O   . HOH L .   ? 0.2836 0.2105 0.3039 0.0688  0.0936  0.0661  602 HOH A O   
2631 O  O   . HOH L .   ? 0.7583 1.2178 0.6316 0.0998  0.1497  0.1442  603 HOH A O   
2632 O  O   . HOH L .   ? 0.2108 0.2545 0.3598 0.0820  -0.0718 -0.1014 604 HOH A O   
2633 O  O   . HOH L .   ? 0.2168 0.7226 0.5698 0.0732  0.1071  0.0822  605 HOH A O   
2634 O  O   . HOH L .   ? 0.3860 0.2980 0.6269 -0.0857 0.1265  -0.0839 606 HOH A O   
2635 O  O   . HOH L .   ? 0.2782 0.3050 0.3463 -0.0003 0.0104  0.0873  607 HOH A O   
2636 O  O   . HOH L .   ? 0.4411 0.1410 0.2921 0.0120  -0.0729 -0.0243 608 HOH A O   
2637 O  O   . HOH L .   ? 0.3671 0.3161 0.1899 -0.0094 0.0263  -0.0296 609 HOH A O   
2638 O  O   . HOH L .   ? 0.2010 0.1198 0.1653 -0.0006 -0.0443 0.0063  610 HOH A O   
2639 O  O   . HOH L .   ? 0.3404 0.2957 0.3362 0.0874  0.1715  0.0807  611 HOH A O   
2640 O  O   . HOH L .   ? 0.3244 0.3729 0.1339 0.0597  -0.0283 0.0405  612 HOH A O   
2641 O  O   . HOH L .   ? 0.3034 0.5170 0.3501 0.0826  0.0092  0.2178  613 HOH A O   
2642 O  O   . HOH L .   ? 0.1137 0.0946 0.1224 0.0193  -0.0052 0.0118  614 HOH A O   
2643 O  O   . HOH L .   ? 0.3012 0.2284 0.2558 -0.0206 -0.0476 -0.0357 615 HOH A O   
2644 O  O   . HOH L .   ? 0.3046 0.3743 0.1948 0.1347  -0.0804 0.0205  616 HOH A O   
2645 O  O   . HOH L .   ? 0.2475 0.3086 0.1855 -0.0965 -0.0291 -0.0222 617 HOH A O   
2646 O  O   . HOH L .   ? 0.1940 0.2874 0.2703 -0.0054 0.0066  0.0342  618 HOH A O   
2647 O  O   . HOH L .   ? 0.1918 0.5566 0.2912 -0.0410 0.0643  0.0379  619 HOH A O   
2648 O  O   . HOH L .   ? 0.1879 0.1715 0.4176 0.0566  0.0342  -0.0696 620 HOH A O   
2649 O  O   . HOH L .   ? 0.4941 0.3014 0.2640 0.1000  -0.0395 0.0054  621 HOH A O   
2650 O  O   . HOH L .   ? 0.2376 0.0999 0.1476 0.0276  0.0070  0.0035  622 HOH A O   
2651 O  O   . HOH L .   ? 0.3037 0.5533 0.7109 -0.0832 0.0006  0.3914  623 HOH A O   
2652 O  O   . HOH L .   ? 0.5073 0.2838 0.3172 0.1129  0.0650  0.0904  624 HOH A O   
2653 O  O   . HOH L .   ? 0.4056 0.4859 0.2833 0.1062  -0.0471 0.1576  625 HOH A O   
2654 O  O   . HOH L .   ? 0.3100 0.1950 0.1713 0.0900  0.0146  0.0494  626 HOH A O   
2655 O  O   . HOH L .   ? 0.3213 0.2653 0.3819 -0.0449 -0.0043 -0.0375 627 HOH A O   
2656 O  O   . HOH L .   ? 0.3424 0.5673 0.3896 0.0027  0.0088  0.1926  628 HOH A O   
2657 O  O   . HOH L .   ? 0.3244 0.3984 0.2256 0.0275  0.0017  0.0469  629 HOH A O   
2658 O  O   . HOH L .   ? 0.2750 0.1774 0.1799 0.0366  0.0299  0.0038  630 HOH A O   
2659 O  O   . HOH L .   ? 0.3334 0.3652 0.7307 -0.0706 -0.0734 0.1398  631 HOH A O   
2660 O  O   . HOH L .   ? 0.3138 0.1739 0.2574 -0.0340 0.0425  0.0103  632 HOH A O   
2661 O  O   . HOH L .   ? 0.4727 0.4981 0.3490 0.0425  0.1304  -0.0505 633 HOH A O   
2662 O  O   . HOH L .   ? 0.6661 0.4322 0.3179 -0.1713 -0.1327 0.1142  634 HOH A O   
2663 O  O   . HOH L .   ? 0.1985 0.2815 0.2978 0.0357  0.0324  0.0680  635 HOH A O   
2664 O  O   . HOH L .   ? 0.4316 0.5146 0.4982 0.0247  -0.1247 0.0988  636 HOH A O   
2665 O  O   . HOH L .   ? 0.3551 0.2326 0.6733 0.0254  0.0785  0.0031  637 HOH A O   
2666 O  O   . HOH L .   ? 0.4079 0.5878 0.4881 0.2330  -0.0439 -0.0816 638 HOH A O   
2667 O  O   . HOH L .   ? 0.2389 0.4083 0.7839 -0.0746 -0.0917 -0.0107 639 HOH A O   
2668 O  O   . HOH L .   ? 0.2373 0.7263 0.7814 -0.1838 0.0250  -0.1599 640 HOH A O   
2669 O  O   . HOH L .   ? 0.2524 0.4205 0.5426 -0.0970 0.1220  -0.1762 641 HOH A O   
2670 O  O   . HOH L .   ? 0.4480 0.1956 0.2484 0.0538  0.1569  0.0892  642 HOH A O   
2671 O  O   . HOH L .   ? 0.2761 0.3043 0.1974 -0.0399 -0.0297 -0.0062 643 HOH A O   
2672 O  O   . HOH L .   ? 0.4632 0.3587 0.4735 0.0068  -0.1206 0.0148  644 HOH A O   
2673 O  O   . HOH L .   ? 0.5296 0.5124 0.4203 0.0675  0.0000  -0.0282 645 HOH A O   
2674 O  O   . HOH L .   ? 0.3932 0.5307 0.2666 0.2083  0.0272  0.0997  646 HOH A O   
2675 O  O   . HOH L .   ? 0.3228 0.5699 0.4456 -0.1235 -0.0211 -0.0586 647 HOH A O   
2676 O  O   . HOH L .   ? 0.6858 0.2307 0.3555 0.1032  0.2504  0.0092  648 HOH A O   
2677 O  O   . HOH L .   ? 0.1486 0.0984 0.1498 -0.0024 -0.0081 -0.0082 649 HOH A O   
2678 O  O   . HOH L .   ? 0.3463 0.4460 0.3729 0.1972  0.1174  0.1394  650 HOH A O   
2679 O  O   . HOH L .   ? 0.3971 0.2752 0.4176 -0.0178 0.1140  0.0037  651 HOH A O   
2680 O  O   . HOH L .   ? 0.3377 0.4386 0.3679 0.0107  0.0588  0.1612  652 HOH A O   
2681 O  O   . HOH L .   ? 0.8294 0.2338 0.5572 -0.0533 -0.1044 -0.0452 653 HOH A O   
2682 O  O   . HOH L .   ? 0.1974 0.2569 0.1858 -0.0109 0.0020  0.0197  654 HOH A O   
2683 O  O   . HOH L .   ? 0.3391 0.4736 0.4007 -0.0982 -0.0908 -0.0121 655 HOH A O   
2684 O  O   . HOH L .   ? 0.2978 0.2691 0.2301 -0.0335 -0.0540 0.0196  656 HOH A O   
2685 O  O   . HOH L .   ? 0.2777 0.2448 0.2996 -0.0218 -0.0329 0.0346  657 HOH A O   
2686 O  O   . HOH L .   ? 0.2292 0.1941 0.1790 0.0461  0.0564  0.0476  658 HOH A O   
2687 O  O   . HOH L .   ? 0.5860 0.3459 0.5056 0.0467  -0.1102 -0.1630 659 HOH A O   
2688 O  O   . HOH L .   ? 0.3283 0.2615 0.3452 0.0733  -0.0155 0.0876  660 HOH A O   
2689 O  O   . HOH L .   ? 0.3616 0.1802 0.3188 0.0948  -0.1923 -0.0220 661 HOH A O   
2690 O  O   . HOH L .   ? 0.5263 0.8386 0.2820 0.3370  -0.0326 0.0467  662 HOH A O   
2691 O  O   . HOH L .   ? 0.2348 0.2142 0.1922 -0.0359 -0.0091 -0.0164 663 HOH A O   
2692 O  O   . HOH L .   ? 0.2797 0.2648 0.7056 -0.0015 -0.1001 0.1732  664 HOH A O   
2693 O  O   . HOH L .   ? 0.4453 0.4230 0.4887 0.1049  -0.0250 -0.0725 665 HOH A O   
2694 O  O   . HOH L .   ? 0.3632 0.8895 0.4210 0.2980  0.1492  0.2513  666 HOH A O   
2695 O  O   . HOH L .   ? 0.6514 0.5206 0.3120 -0.2412 0.0215  0.1951  667 HOH A O   
2696 O  O   . HOH L .   ? 0.2515 0.2114 0.2238 -0.0120 -0.0043 0.0239  668 HOH A O   
2697 O  O   . HOH L .   ? 0.1243 0.3984 0.4216 0.0300  -0.0296 0.0852  669 HOH A O   
2698 O  O   . HOH L .   ? 0.4955 0.6893 0.3246 -0.0715 -0.2060 0.0450  670 HOH A O   
2699 O  O   . HOH L .   ? 0.2894 0.3255 0.2466 -0.0612 -0.0028 0.0103  671 HOH A O   
2700 O  O   . HOH L .   ? 0.2899 0.2526 0.2863 0.0313  0.0939  -0.0252 672 HOH A O   
2701 O  O   . HOH L .   ? 0.2797 0.3116 0.2795 0.0062  -0.0573 -0.0425 673 HOH A O   
2702 O  O   . HOH L .   ? 0.2849 0.4548 0.3470 0.0773  0.0860  0.0989  674 HOH A O   
2703 O  O   . HOH L .   ? 0.3386 0.3910 0.4805 0.0851  0.0978  0.0948  675 HOH A O   
2704 O  O   . HOH L .   ? 0.4086 0.3479 0.4964 0.0719  -0.1780 -0.0847 676 HOH A O   
2705 O  O   . HOH L .   ? 0.2685 0.4334 0.5429 0.0109  0.0579  0.0364  677 HOH A O   
2706 O  O   . HOH L .   ? 0.3434 0.7376 0.1841 0.0608  0.0315  -0.0560 678 HOH A O   
2707 O  O   . HOH L .   ? 0.4584 0.4250 0.6276 -0.0548 -0.2018 -0.1732 679 HOH A O   
2708 O  O   . HOH L .   ? 0.2919 0.1878 0.4708 0.0372  -0.0308 0.0247  680 HOH A O   
2709 O  O   . HOH L .   ? 0.2166 0.3061 0.2522 -0.0153 0.0586  -0.0767 681 HOH A O   
2710 O  O   . HOH L .   ? 0.4453 0.4762 0.5934 0.1427  -0.0645 0.2072  682 HOH A O   
2711 O  O   . HOH L .   ? 0.4420 0.6292 0.2497 0.0432  -0.0092 -0.0452 683 HOH A O   
2712 O  O   . HOH L .   ? 0.4519 0.2328 0.2023 0.0617  -0.0089 0.0518  684 HOH A O   
2713 O  O   . HOH L .   ? 0.3181 0.9376 0.3569 0.0671  -0.0317 0.2079  685 HOH A O   
2714 O  O   . HOH L .   ? 0.3262 0.3260 0.3003 0.1748  -0.0754 0.0115  686 HOH A O   
2715 O  O   . HOH L .   ? 0.3673 0.7832 0.3761 -0.2398 -0.0037 0.1483  687 HOH A O   
2716 O  O   . HOH L .   ? 0.3939 0.3492 0.3082 0.0632  -0.0241 0.0071  688 HOH A O   
2717 O  O   . HOH L .   ? 0.2924 0.2468 0.6112 0.0690  -0.0908 0.0141  689 HOH A O   
2718 O  O   . HOH L .   ? 0.2831 0.6136 0.3018 0.0168  0.0200  -0.1967 690 HOH A O   
2719 O  O   . HOH L .   ? 0.3574 0.5896 0.8999 -0.0318 0.2863  -0.0810 691 HOH A O   
2720 O  O   . HOH L .   ? 0.4566 0.2387 0.2041 0.0887  -0.0120 -0.0333 692 HOH A O   
2721 O  O   . HOH L .   ? 0.3495 0.2779 0.1959 -0.0037 -0.0265 -0.0228 693 HOH A O   
2722 O  O   . HOH L .   ? 0.1802 0.3393 0.2475 -0.0175 -0.0222 0.0340  694 HOH A O   
2723 O  O   . HOH L .   ? 0.1893 0.2675 0.3100 0.0285  0.0344  0.0791  695 HOH A O   
2724 O  O   . HOH L .   ? 0.3025 0.2486 0.1859 0.0553  0.0271  -0.0551 696 HOH A O   
2725 O  O   . HOH L .   ? 0.4302 0.3172 0.2468 -0.0265 -0.1297 -0.0272 697 HOH A O   
2726 O  O   . HOH L .   ? 0.4124 0.4830 0.2137 0.0812  0.0165  0.0500  698 HOH A O   
2727 O  O   . HOH L .   ? 0.4747 0.5072 0.2234 0.1993  -0.0239 0.0082  699 HOH A O   
2728 O  O   . HOH L .   ? 0.6200 0.2477 0.7481 -0.0472 -0.2348 0.0088  700 HOH A O   
2729 O  O   . HOH L .   ? 0.3959 0.4715 0.2730 -0.1756 0.0982  0.0212  701 HOH A O   
2730 O  O   . HOH L .   ? 0.6644 0.2556 1.0667 -0.0008 0.0412  0.0900  702 HOH A O   
2731 O  O   . HOH L .   ? 0.2867 0.3885 0.4503 0.0873  -0.0015 -0.0524 703 HOH A O   
2732 O  O   . HOH L .   ? 0.6412 0.5939 0.5407 -0.0337 -0.1863 -0.1647 704 HOH A O   
2733 O  O   . HOH L .   ? 0.4923 0.2549 0.5036 -0.0060 -0.2339 -0.0780 705 HOH A O   
2734 O  O   . HOH L .   ? 0.3616 0.6078 0.5396 0.2427  -0.1134 -0.0722 706 HOH A O   
2735 O  O   . HOH L .   ? 0.2908 0.2662 0.4790 0.0859  0.0960  0.0277  707 HOH A O   
2736 O  O   . HOH L .   ? 0.7177 0.3208 0.3334 0.0124  -0.1712 -0.1194 708 HOH A O   
2737 O  O   . HOH L .   ? 0.3535 0.1920 0.4521 0.0255  0.1410  0.0860  709 HOH A O   
2738 O  O   . HOH L .   ? 0.3556 0.4636 0.4424 -0.1535 0.1023  0.0428  710 HOH A O   
2739 O  O   . HOH L .   ? 0.3452 0.1239 0.3398 -0.0096 0.0988  -0.0068 711 HOH A O   
2740 O  O   . HOH L .   ? 0.2076 0.1691 0.1894 0.0458  -0.0270 0.0177  712 HOH A O   
2741 O  O   . HOH L .   ? 0.4946 0.2193 0.3806 0.0546  -0.0195 -0.0445 713 HOH A O   
2742 O  O   . HOH L .   ? 0.5899 0.4593 0.4158 0.1605  -0.0935 -0.0804 714 HOH A O   
2743 O  O   . HOH L .   ? 0.4068 0.3594 0.5220 -0.1591 0.0218  0.0637  715 HOH A O   
2744 O  O   . HOH L .   ? 0.2084 0.2381 0.4469 -0.0386 0.0599  0.0794  716 HOH A O   
2745 O  O   . HOH L .   ? 0.4632 0.2041 0.2401 -0.0296 -0.0992 -0.0549 717 HOH A O   
2746 O  O   . HOH L .   ? 0.0548 1.0007 1.6923 -0.1439 -0.0123 0.7324  718 HOH A O   
2747 O  O   . HOH L .   ? 0.8895 0.5371 0.6762 0.0768  0.0419  -0.2061 719 HOH A O   
2748 O  O   . HOH L .   ? 0.3522 0.4569 0.4266 -0.0733 0.0438  0.1459  720 HOH A O   
2749 O  O   . HOH L .   ? 0.1775 0.2732 0.2786 -0.0581 0.0320  -0.0794 721 HOH A O   
2750 O  O   . HOH L .   ? 0.4361 0.4153 0.2630 0.1833  -0.0397 0.0394  722 HOH A O   
2751 O  O   . HOH L .   ? 0.4262 0.5439 0.3605 0.0260  0.0882  -0.0962 723 HOH A O   
2752 O  O   . HOH L .   ? 0.3802 0.5023 0.6385 -0.0750 0.0513  -0.2752 724 HOH A O   
2753 O  O   . HOH L .   ? 0.4025 0.2860 0.2901 -0.0219 0.0419  0.0008  725 HOH A O   
2754 O  O   . HOH L .   ? 0.3253 0.7103 0.3673 -0.1164 0.0806  0.0100  726 HOH A O   
2755 O  O   . HOH L .   ? 0.3203 0.3962 0.4790 -0.1120 -0.0998 -0.0878 727 HOH A O   
2756 O  O   . HOH L .   ? 1.0536 0.3558 0.4866 -0.1132 -0.3894 0.1747  728 HOH A O   
2757 O  O   . HOH L .   ? 0.7864 0.2536 0.2286 -0.1307 -0.0328 0.0838  729 HOH A O   
2758 O  O   . HOH L .   ? 0.2430 0.3314 0.3783 0.0847  0.1286  0.1193  730 HOH A O   
2759 O  O   . HOH L .   ? 0.2527 0.1679 0.2231 0.0214  0.0163  -0.0445 731 HOH A O   
2760 O  O   . HOH L .   ? 0.5480 0.4921 0.3614 0.1907  -0.1448 -0.0326 732 HOH A O   
2761 O  O   . HOH L .   ? 0.3761 0.2982 0.2389 0.0649  -0.0346 -0.0926 733 HOH A O   
# 
