data_6QL3
# 
_entry.id   6QL3 
# 
_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   6QL3         pdb_00006ql3 10.2210/pdb6ql3/pdb 
WWPDB D_1292100370 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2019-09-25 
2 'Structure model' 1 1 2024-01-24 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' '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                        6QL3 
_pdbx_database_status.recvd_initial_deposition_date   2019-01-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'PDB entry for the same citation' 6QL1 unspecified 
PDB 'PDB entry for the same citation' 6QL2 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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Rep' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2045-2322 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            9 
_citation.language                  ? 
_citation.page_first                12710 
_citation.page_last                 12710 
_citation.title                     
'Engineered Carbonic Anhydrase VI-Mimic Enzyme Switched the Structure and Affinities of Inhibitors.' 
_citation.year                      2019 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41598-019-49094-0 
_citation.pdbx_database_id_PubMed   31481705 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kazokaite, J.'   1 ?                   
primary 'Kairys, V.'      2 ?                   
primary 'Smirnoviene, J.' 3 ?                   
primary 'Smirnov, A.'     4 ?                   
primary 'Manakova, E.'    5 ?                   
primary 'Tolvanen, M.'    6 ?                   
primary 'Parkkila, S.'    7 ?                   
primary 'Matulis, D.'     8 0000-0002-6178-6276 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                               29366.055 1   4.2.1.1 
'A65T, N67Q, F130Y, V134Q, L203T' 'human carbonic anhydrase II'                                                        ? 
2 non-polymer syn 'ZINC ION'                                                                           65.409    1   ?       ? 
'3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 
3 non-polymer syn '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 444.489   1   ?       ? Zn 
? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                 78.133    2   ?       ? 
'Dimethyl sulfoxide'                                                                 ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                              106.120   2   ?       ? 
'polyethylene glycol'                                                                ? 
6 non-polymer syn 'MALONIC ACID'                                                                       104.061   1   ?       ? 
ethane-1,2-diol                                                                      ? 
7 non-polymer syn 1,2-ETHANEDIOL                                                                       62.068    1   ?       ? 
Malonate                                                                             ? 
8 non-polymer syn 'BENZOIC ACID'                                                                       122.121   2   ?       ? 
'BENZOIC ACID'                                                                       ? 
9 water       nat water                                                                                18.015    275 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHTFQVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAQQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLTECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHTFQVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAQQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLTECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                           ZN  
3 '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' V14 
4 'DIMETHYL SULFOXIDE'                                                                 DMS 
5 'DI(HYDROXYETHYL)ETHER'                                                              PEG 
6 'MALONIC ACID'                                                                       MLA 
7 1,2-ETHANEDIOL                                                                       EDO 
8 'BENZOIC ACID'                                                                       BEZ 
9 water                                                                                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  THR n 
1 66  PHE n 
1 67  GLN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 TYR n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 GLN n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 THR n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                              ? 'C3 H7 N O2' 
89.093  
ARG 'L-peptide linking' y ARGININE                                                                             ? 'C6 H15 N4 O2 1' 
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                           ? 'C4 H8 N2 O3' 
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                      ? 'C4 H7 N O4' 
133.103 
BEZ non-polymer         . 'BENZOIC ACID'                                                                       ? 'C7 H6 O2' 
122.121 
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 
MLA non-polymer         . 'MALONIC ACID'                                                                       
'DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID; METHANEDICARBOXYLIC ACID' 'C3 H4 O4'            104.061 
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 
V14 non-polymer         . '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 
'C16 H23 F3 N2 O5 S2' 444.489 
VAL 'L-peptide linking' y VALINE                                                                               ? 'C5 H11 N O2' 
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                           ? 'Zn 2' 65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 TYR 130 131 131 TYR TYR A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 GLN 134 135 135 GLN GLN A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 THR 203 204 204 THR THR A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 V14 1   302 1   V14 V14 A . 
D 4 DMS 1   303 1   DMS DMS A . 
E 5 PEG 1   304 2   PEG PEG A . 
F 5 PEG 1   305 4   PEG PEG A . 
G 6 MLA 1   306 5   MLA DXX A . 
H 7 EDO 1   307 6   EDO EDO A . 
I 8 BEZ 1   308 7   BEZ BEZ A . 
J 4 DMS 1   309 8   DMS DMS A . 
K 8 BEZ 1   310 3   BEZ BEZ A . 
L 9 HOH 1   401 171 HOH HOH A . 
L 9 HOH 2   402 214 HOH HOH A . 
L 9 HOH 3   403 266 HOH HOH A . 
L 9 HOH 4   404 96  HOH HOH A . 
L 9 HOH 5   405 268 HOH HOH A . 
L 9 HOH 6   406 219 HOH HOH A . 
L 9 HOH 7   407 140 HOH HOH A . 
L 9 HOH 8   408 227 HOH HOH A . 
L 9 HOH 9   409 100 HOH HOH A . 
L 9 HOH 10  410 161 HOH HOH A . 
L 9 HOH 11  411 249 HOH HOH A . 
L 9 HOH 12  412 61  HOH HOH A . 
L 9 HOH 13  413 110 HOH HOH A . 
L 9 HOH 14  414 131 HOH HOH A . 
L 9 HOH 15  415 216 HOH HOH A . 
L 9 HOH 16  416 169 HOH HOH A . 
L 9 HOH 17  417 267 HOH HOH A . 
L 9 HOH 18  418 262 HOH HOH A . 
L 9 HOH 19  419 199 HOH HOH A . 
L 9 HOH 20  420 56  HOH HOH A . 
L 9 HOH 21  421 89  HOH HOH A . 
L 9 HOH 22  422 18  HOH HOH A . 
L 9 HOH 23  423 162 HOH HOH A . 
L 9 HOH 24  424 167 HOH HOH A . 
L 9 HOH 25  425 119 HOH HOH A . 
L 9 HOH 26  426 274 HOH HOH A . 
L 9 HOH 27  427 108 HOH HOH A . 
L 9 HOH 28  428 200 HOH HOH A . 
L 9 HOH 29  429 186 HOH HOH A . 
L 9 HOH 30  430 95  HOH HOH A . 
L 9 HOH 31  431 67  HOH HOH A . 
L 9 HOH 32  432 22  HOH HOH A . 
L 9 HOH 33  433 65  HOH HOH A . 
L 9 HOH 34  434 117 HOH HOH A . 
L 9 HOH 35  435 54  HOH HOH A . 
L 9 HOH 36  436 25  HOH HOH A . 
L 9 HOH 37  437 180 HOH HOH A . 
L 9 HOH 38  438 149 HOH HOH A . 
L 9 HOH 39  439 2   HOH HOH A . 
L 9 HOH 40  440 71  HOH HOH A . 
L 9 HOH 41  441 113 HOH HOH A . 
L 9 HOH 42  442 176 HOH HOH A . 
L 9 HOH 43  443 259 HOH HOH A . 
L 9 HOH 44  444 212 HOH HOH A . 
L 9 HOH 45  445 123 HOH HOH A . 
L 9 HOH 46  446 178 HOH HOH A . 
L 9 HOH 47  447 28  HOH HOH A . 
L 9 HOH 48  448 81  HOH HOH A . 
L 9 HOH 49  449 272 HOH HOH A . 
L 9 HOH 50  450 150 HOH HOH A . 
L 9 HOH 51  451 173 HOH HOH A . 
L 9 HOH 52  452 53  HOH HOH A . 
L 9 HOH 53  453 74  HOH HOH A . 
L 9 HOH 54  454 137 HOH HOH A . 
L 9 HOH 55  455 32  HOH HOH A . 
L 9 HOH 56  456 94  HOH HOH A . 
L 9 HOH 57  457 49  HOH HOH A . 
L 9 HOH 58  458 12  HOH HOH A . 
L 9 HOH 59  459 77  HOH HOH A . 
L 9 HOH 60  460 38  HOH HOH A . 
L 9 HOH 61  461 6   HOH HOH A . 
L 9 HOH 62  462 92  HOH HOH A . 
L 9 HOH 63  463 175 HOH HOH A . 
L 9 HOH 64  464 64  HOH HOH A . 
L 9 HOH 65  465 17  HOH HOH A . 
L 9 HOH 66  466 55  HOH HOH A . 
L 9 HOH 67  467 87  HOH HOH A . 
L 9 HOH 68  468 63  HOH HOH A . 
L 9 HOH 69  469 194 HOH HOH A . 
L 9 HOH 70  470 37  HOH HOH A . 
L 9 HOH 71  471 163 HOH HOH A . 
L 9 HOH 72  472 99  HOH HOH A . 
L 9 HOH 73  473 7   HOH HOH A . 
L 9 HOH 74  474 42  HOH HOH A . 
L 9 HOH 75  475 156 HOH HOH A . 
L 9 HOH 76  476 153 HOH HOH A . 
L 9 HOH 77  477 76  HOH HOH A . 
L 9 HOH 78  478 31  HOH HOH A . 
L 9 HOH 79  479 111 HOH HOH A . 
L 9 HOH 80  480 13  HOH HOH A . 
L 9 HOH 81  481 202 HOH HOH A . 
L 9 HOH 82  482 72  HOH HOH A . 
L 9 HOH 83  483 181 HOH HOH A . 
L 9 HOH 84  484 11  HOH HOH A . 
L 9 HOH 85  485 80  HOH HOH A . 
L 9 HOH 86  486 20  HOH HOH A . 
L 9 HOH 87  487 185 HOH HOH A . 
L 9 HOH 88  488 107 HOH HOH A . 
L 9 HOH 89  489 16  HOH HOH A . 
L 9 HOH 90  490 62  HOH HOH A . 
L 9 HOH 91  491 193 HOH HOH A . 
L 9 HOH 92  492 46  HOH HOH A . 
L 9 HOH 93  493 1   HOH HOH A . 
L 9 HOH 94  494 160 HOH HOH A . 
L 9 HOH 95  495 203 HOH HOH A . 
L 9 HOH 96  496 60  HOH HOH A . 
L 9 HOH 97  497 187 HOH HOH A . 
L 9 HOH 98  498 124 HOH HOH A . 
L 9 HOH 99  499 90  HOH HOH A . 
L 9 HOH 100 500 24  HOH HOH A . 
L 9 HOH 101 501 139 HOH HOH A . 
L 9 HOH 102 502 205 HOH HOH A . 
L 9 HOH 103 503 58  HOH HOH A . 
L 9 HOH 104 504 254 HOH HOH A . 
L 9 HOH 105 505 128 HOH HOH A . 
L 9 HOH 106 506 250 HOH HOH A . 
L 9 HOH 107 507 44  HOH HOH A . 
L 9 HOH 108 508 109 HOH HOH A . 
L 9 HOH 109 509 168 HOH HOH A . 
L 9 HOH 110 510 5   HOH HOH A . 
L 9 HOH 111 511 8   HOH HOH A . 
L 9 HOH 112 512 179 HOH HOH A . 
L 9 HOH 113 513 204 HOH HOH A . 
L 9 HOH 114 514 122 HOH HOH A . 
L 9 HOH 115 515 147 HOH HOH A . 
L 9 HOH 116 516 218 HOH HOH A . 
L 9 HOH 117 517 52  HOH HOH A . 
L 9 HOH 118 518 10  HOH HOH A . 
L 9 HOH 119 519 226 HOH HOH A . 
L 9 HOH 120 520 4   HOH HOH A . 
L 9 HOH 121 521 265 HOH HOH A . 
L 9 HOH 122 522 263 HOH HOH A . 
L 9 HOH 123 523 190 HOH HOH A . 
L 9 HOH 124 524 70  HOH HOH A . 
L 9 HOH 125 525 29  HOH HOH A . 
L 9 HOH 126 526 132 HOH HOH A . 
L 9 HOH 127 527 136 HOH HOH A . 
L 9 HOH 128 528 85  HOH HOH A . 
L 9 HOH 129 529 41  HOH HOH A . 
L 9 HOH 130 530 27  HOH HOH A . 
L 9 HOH 131 531 192 HOH HOH A . 
L 9 HOH 132 532 69  HOH HOH A . 
L 9 HOH 133 533 98  HOH HOH A . 
L 9 HOH 134 534 86  HOH HOH A . 
L 9 HOH 135 535 105 HOH HOH A . 
L 9 HOH 136 536 245 HOH HOH A . 
L 9 HOH 137 537 45  HOH HOH A . 
L 9 HOH 138 538 34  HOH HOH A . 
L 9 HOH 139 539 50  HOH HOH A . 
L 9 HOH 140 540 88  HOH HOH A . 
L 9 HOH 141 541 182 HOH HOH A . 
L 9 HOH 142 542 243 HOH HOH A . 
L 9 HOH 143 543 114 HOH HOH A . 
L 9 HOH 144 544 51  HOH HOH A . 
L 9 HOH 145 545 79  HOH HOH A . 
L 9 HOH 146 546 234 HOH HOH A . 
L 9 HOH 147 547 26  HOH HOH A . 
L 9 HOH 148 548 101 HOH HOH A . 
L 9 HOH 149 549 264 HOH HOH A . 
L 9 HOH 150 550 170 HOH HOH A . 
L 9 HOH 151 551 84  HOH HOH A . 
L 9 HOH 152 552 30  HOH HOH A . 
L 9 HOH 153 553 177 HOH HOH A . 
L 9 HOH 154 554 36  HOH HOH A . 
L 9 HOH 155 555 125 HOH HOH A . 
L 9 HOH 156 556 196 HOH HOH A . 
L 9 HOH 157 557 39  HOH HOH A . 
L 9 HOH 158 558 15  HOH HOH A . 
L 9 HOH 159 559 126 HOH HOH A . 
L 9 HOH 160 560 148 HOH HOH A . 
L 9 HOH 161 561 14  HOH HOH A . 
L 9 HOH 162 562 48  HOH HOH A . 
L 9 HOH 163 563 68  HOH HOH A . 
L 9 HOH 164 564 145 HOH HOH A . 
L 9 HOH 165 565 201 HOH HOH A . 
L 9 HOH 166 566 73  HOH HOH A . 
L 9 HOH 167 567 3   HOH HOH A . 
L 9 HOH 168 568 19  HOH HOH A . 
L 9 HOH 169 569 121 HOH HOH A . 
L 9 HOH 170 570 195 HOH HOH A . 
L 9 HOH 171 571 21  HOH HOH A . 
L 9 HOH 172 572 43  HOH HOH A . 
L 9 HOH 173 573 116 HOH HOH A . 
L 9 HOH 174 574 82  HOH HOH A . 
L 9 HOH 175 575 83  HOH HOH A . 
L 9 HOH 176 576 78  HOH HOH A . 
L 9 HOH 177 577 57  HOH HOH A . 
L 9 HOH 178 578 206 HOH HOH A . 
L 9 HOH 179 579 97  HOH HOH A . 
L 9 HOH 180 580 9   HOH HOH A . 
L 9 HOH 181 581 118 HOH HOH A . 
L 9 HOH 182 582 143 HOH HOH A . 
L 9 HOH 183 583 23  HOH HOH A . 
L 9 HOH 184 584 135 HOH HOH A . 
L 9 HOH 185 585 208 HOH HOH A . 
L 9 HOH 186 586 188 HOH HOH A . 
L 9 HOH 187 587 269 HOH HOH A . 
L 9 HOH 188 588 155 HOH HOH A . 
L 9 HOH 189 589 165 HOH HOH A . 
L 9 HOH 190 590 127 HOH HOH A . 
L 9 HOH 191 591 228 HOH HOH A . 
L 9 HOH 192 592 141 HOH HOH A . 
L 9 HOH 193 593 133 HOH HOH A . 
L 9 HOH 194 594 59  HOH HOH A . 
L 9 HOH 195 595 224 HOH HOH A . 
L 9 HOH 196 596 103 HOH HOH A . 
L 9 HOH 197 597 271 HOH HOH A . 
L 9 HOH 198 598 33  HOH HOH A . 
L 9 HOH 199 599 75  HOH HOH A . 
L 9 HOH 200 600 198 HOH HOH A . 
L 9 HOH 201 601 183 HOH HOH A . 
L 9 HOH 202 602 106 HOH HOH A . 
L 9 HOH 203 603 154 HOH HOH A . 
L 9 HOH 204 604 152 HOH HOH A . 
L 9 HOH 205 605 174 HOH HOH A . 
L 9 HOH 206 606 47  HOH HOH A . 
L 9 HOH 207 607 248 HOH HOH A . 
L 9 HOH 208 608 166 HOH HOH A . 
L 9 HOH 209 609 207 HOH HOH A . 
L 9 HOH 210 610 197 HOH HOH A . 
L 9 HOH 211 611 164 HOH HOH A . 
L 9 HOH 212 612 211 HOH HOH A . 
L 9 HOH 213 613 172 HOH HOH A . 
L 9 HOH 214 614 273 HOH HOH A . 
L 9 HOH 215 615 40  HOH HOH A . 
L 9 HOH 216 616 120 HOH HOH A . 
L 9 HOH 217 617 270 HOH HOH A . 
L 9 HOH 218 618 146 HOH HOH A . 
L 9 HOH 219 619 221 HOH HOH A . 
L 9 HOH 220 620 191 HOH HOH A . 
L 9 HOH 221 621 222 HOH HOH A . 
L 9 HOH 222 622 184 HOH HOH A . 
L 9 HOH 223 623 66  HOH HOH A . 
L 9 HOH 224 624 189 HOH HOH A . 
L 9 HOH 225 625 251 HOH HOH A . 
L 9 HOH 226 626 233 HOH HOH A . 
L 9 HOH 227 627 261 HOH HOH A . 
L 9 HOH 228 628 129 HOH HOH A . 
L 9 HOH 229 629 247 HOH HOH A . 
L 9 HOH 230 630 210 HOH HOH A . 
L 9 HOH 231 631 229 HOH HOH A . 
L 9 HOH 232 632 258 HOH HOH A . 
L 9 HOH 233 633 91  HOH HOH A . 
L 9 HOH 234 634 223 HOH HOH A . 
L 9 HOH 235 635 151 HOH HOH A . 
L 9 HOH 236 636 236 HOH HOH A . 
L 9 HOH 237 637 138 HOH HOH A . 
L 9 HOH 238 638 237 HOH HOH A . 
L 9 HOH 239 639 209 HOH HOH A . 
L 9 HOH 240 640 275 HOH HOH A . 
L 9 HOH 241 641 253 HOH HOH A . 
L 9 HOH 242 642 134 HOH HOH A . 
L 9 HOH 243 643 215 HOH HOH A . 
L 9 HOH 244 644 225 HOH HOH A . 
L 9 HOH 245 645 220 HOH HOH A . 
L 9 HOH 246 646 260 HOH HOH A . 
L 9 HOH 247 647 235 HOH HOH A . 
L 9 HOH 248 648 242 HOH HOH A . 
L 9 HOH 249 649 246 HOH HOH A . 
L 9 HOH 250 650 115 HOH HOH A . 
L 9 HOH 251 651 35  HOH HOH A . 
L 9 HOH 252 652 130 HOH HOH A . 
L 9 HOH 253 653 239 HOH HOH A . 
L 9 HOH 254 654 255 HOH HOH A . 
L 9 HOH 255 655 112 HOH HOH A . 
L 9 HOH 256 656 244 HOH HOH A . 
L 9 HOH 257 657 217 HOH HOH A . 
L 9 HOH 258 658 93  HOH HOH A . 
L 9 HOH 259 659 213 HOH HOH A . 
L 9 HOH 260 660 144 HOH HOH A . 
L 9 HOH 261 661 104 HOH HOH A . 
L 9 HOH 262 662 257 HOH HOH A . 
L 9 HOH 263 663 157 HOH HOH A . 
L 9 HOH 264 664 241 HOH HOH A . 
L 9 HOH 265 665 142 HOH HOH A . 
L 9 HOH 266 666 231 HOH HOH A . 
L 9 HOH 267 667 230 HOH HOH A . 
L 9 HOH 268 668 102 HOH HOH A . 
L 9 HOH 269 669 232 HOH HOH A . 
L 9 HOH 270 670 158 HOH HOH A . 
L 9 HOH 271 671 159 HOH HOH A . 
L 9 HOH 272 672 238 HOH HOH A . 
L 9 HOH 273 673 240 HOH HOH A . 
L 9 HOH 274 674 256 HOH HOH A . 
L 9 HOH 275 675 252 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
3  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
4  1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
5  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
6  1 Y 1 A LYS 133 ? CD  ? A LYS 132 CD  
7  1 Y 1 A LYS 133 ? CE  ? A LYS 132 CE  
8  1 Y 1 A LYS 133 ? NZ  ? A LYS 132 NZ  
9  1 Y 1 A LYS 159 ? CD  ? A LYS 158 CD  
10 1 Y 1 A LYS 159 ? CE  ? A LYS 158 CE  
11 1 Y 1 A LYS 159 ? NZ  ? A LYS 158 NZ  
12 1 Y 1 A LYS 170 ? NZ  ? A LYS 169 NZ  
13 1 Y 1 A LYS 172 ? CE  ? A LYS 171 CE  
14 1 Y 1 A LYS 172 ? NZ  ? A LYS 171 NZ  
15 1 Y 1 A LEU 224 ? CD1 ? A LEU 223 CD1 
16 1 Y 1 A LYS 228 ? NZ  ? A LYS 227 NZ  
17 1 Y 1 A LYS 257 ? CD  ? A LYS 256 CD  
18 1 Y 1 A LYS 257 ? CE  ? A LYS 256 CE  
19 1 Y 1 A LYS 257 ? NZ  ? A LYS 256 NZ  
20 1 Y 1 A LYS 261 ? CG  ? A LYS 260 CG  
21 1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
22 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
23 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? .    1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.10 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .    3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .    4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .    5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .    6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.170 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6QL3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.209 
_cell.length_a_esd                 ? 
_cell.length_b                     41.373 
_cell.length_b_esd                 ? 
_cell.length_c                     71.846 
_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                         6QL3 
_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                   6QL3 
_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            2.07 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.62 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer was 0.1M sodium BICINE (pH 9), 0.2M ammonium sulfate and 2M sodium malonate (pH 7)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-21 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.975522 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.975522 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6QL3 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.350 
_reflns.d_resolution_low                 69.659 
_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                       52382 
_reflns.number_obs                       52382 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             98.800 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.800 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.088 
_reflns.pdbx_netI_over_av_sigmaI         4.870 
_reflns.pdbx_netI_over_sigmaI            10.800 
_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                  0.102 
_reflns.pdbx_Rpim_I_all                  0.039 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         353839 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.350 1.420  ? 1.8  ? ? ? ? ? 99.000 ? ? ? ? 0.338 ? ? ? ? ? ? ? ? 6.700 0.338 ? ? ? 0.391 0.151 ? 1  1 ? ? 
1.420 1.510  ? 2.2  ? ? ? ? ? 98.500 ? ? ? ? 0.264 ? ? ? ? ? ? ? ? 6.700 0.264 ? ? ? 0.305 0.118 ? 2  1 ? ? 
1.510 1.610  ? 2.6  ? ? ? ? ? 98.300 ? ? ? ? 0.205 ? ? ? ? ? ? ? ? 6.700 0.205 ? ? ? 0.238 0.092 ? 3  1 ? ? 
1.610 1.740  ? 3.2  ? ? ? ? ? 98.300 ? ? ? ? 0.161 ? ? ? ? ? ? ? ? 6.700 0.161 ? ? ? 0.189 0.073 ? 4  1 ? ? 
1.740 1.910  ? 4.3  ? ? ? ? ? 99.200 ? ? ? ? 0.120 ? ? ? ? ? ? ? ? 6.800 0.120 ? ? ? 0.141 0.054 ? 5  1 ? ? 
1.910 2.130  ? 5.7  ? ? ? ? ? 99.300 ? ? ? ? 0.092 ? ? ? ? ? ? ? ? 6.900 0.092 ? ? ? 0.110 0.043 ? 6  1 ? ? 
2.130 2.460  ? 5.9  ? ? ? ? ? 99.400 ? ? ? ? 0.082 ? ? ? ? ? ? ? ? 6.900 0.082 ? ? ? 0.096 0.036 ? 7  1 ? ? 
2.460 3.020  ? 7.2  ? ? ? ? ? 99.600 ? ? ? ? 0.072 ? ? ? ? ? ? ? ? 6.900 0.072 ? ? ? 0.083 0.031 ? 8  1 ? ? 
3.020 4.270  ? 9.8  ? ? ? ? ? 98.500 ? ? ? ? 0.058 ? ? ? ? ? ? ? ? 6.800 0.058 ? ? ? 0.066 0.025 ? 9  1 ? ? 
4.270 69.659 ? 10.0 ? ? ? ? ? 98.300 ? ? ? ? 0.052 ? ? ? ? ? ? ? ? 6.700 0.052 ? ? ? 0.059 0.023 ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            0.8500 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.2900 
_refine.aniso_B[2][2]                            -0.6000 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            -0.0800 
_refine.B_iso_max                                90.280 
_refine.B_iso_mean                               15.1520 
_refine.B_iso_min                                3.180 
_refine.correlation_coeff_Fo_to_Fc               0.9800 
_refine.correlation_coeff_Fo_to_Fc_free          0.9680 
_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                                 6QL3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.3500 
_refine.ls_d_res_low                             39.8300 
_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                     52284 
_refine.ls_number_reflns_R_free                  5161 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.5400 
_refine.ls_percent_reflns_R_free                 9.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1202 
_refine.ls_R_factor_R_free                       0.1558 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1163 
_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                       0.0520 
_refine.pdbx_overall_ESU_R_Free                  0.0500 
_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             0.0517 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2031 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         80 
_refine_hist.number_atoms_solvent             275 
_refine_hist.number_atoms_total               2386 
_refine_hist.d_res_high                       1.3500 
_refine_hist.d_res_low                        39.8300 
# 
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' ? 0.033  0.012  2275 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.195  1.656  3098 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.817  5.000  280  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.612 23.889 108  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.259 15.000 358  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 27.622 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.127  0.200  274  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.020  1793 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 1.913  1.004  1092 ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.505  1.506  1381 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 3.915  1.439  1183 ? r_scbond_it            ? ? 
'X-RAY DIFFRACTION' ? 7.018  3.000  2275 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 31.122 5.000  152  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 15.647 5.000  2330 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.3500 
_refine_ls_shell.d_res_low                        1.3850 
_refine_ls_shell.number_reflns_all                3851 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             394 
_refine_ls_shell.number_reflns_R_work             3457 
_refine_ls_shell.percent_reflns_obs               98.4700 
_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                  0.1940 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1400 
_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                     6QL3 
_struct.title                        
;Crystal structure of chimeric carbonic anhydrase VI with 3-(cyclooctylamino)-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        6QL3 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 6 ? 
H N N 7 ? 
I N N 8 ? 
J N N 4 ? 
K N N 8 ? 
L N N 9 ? 
# 
_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              6QL3 
_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 6QL3 THR A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6QL3 GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6QL3 TYR A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 3 
1 6QL3 GLN A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 4 
1 6QL3 THR A 203 ? UNP P00918 LEU 203 'engineered mutation' 204 5 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1920  ? 
1 MORE         11    ? 
1 'SSA (A^2)'  11200 ? 
# 
_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 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? GLN A 134 ? ASP A 130 GLN A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.011 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V14 . N10 ? ? A ZN  301 A V14 302 1_555 ? ? ? ? ? ? ? 1.890 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.9 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 111.7 ? 
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_555 100.2 ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C V14 .   ? A V14 302 ? 1_555 118.0 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C V14 .   ? A V14 302 ? 1_555 115.6 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C V14 .   ? A V14 302 ? 1_555 106.1 ? 
# 
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 -4.40 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 11.17 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O 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 VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A V14 302 ? 15 'binding site for residue V14 A 302' 
AC3 Software A DMS 303 ? 4  'binding site for residue DMS A 303' 
AC4 Software A PEG 304 ? 7  'binding site for residue PEG A 304' 
AC5 Software A PEG 305 ? 3  'binding site for residue PEG A 305' 
AC6 Software A MLA 306 ? 6  'binding site for residue MLA A 306' 
AC7 Software A EDO 307 ? 6  'binding site for residue EDO A 307' 
AC8 Software A BEZ 308 ? 8  'binding site for residue BEZ A 308' 
AC9 Software A DMS 309 ? 3  'binding site for residue DMS A 309' 
AD1 Software A BEZ 310 ? 5  'binding site for residue BEZ 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  V14 C .   ? V14 A 302 . ? 1_555 ? 
5  AC2 15 ASN A 62  ? ASN A 62  . ? 1_555 ? 
6  AC2 15 THR A 65  ? THR A 65  . ? 1_555 ? 
7  AC2 15 GLN A 67  ? GLN A 67  . ? 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 VAL A 121 ? VAL A 121 . ? 1_555 ? 
13 AC2 15 GLN A 134 ? GLN A 135 . ? 1_555 ? 
14 AC2 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
15 AC2 15 THR A 198 ? THR A 199 . ? 1_555 ? 
16 AC2 15 THR A 199 ? THR A 200 . ? 1_555 ? 
17 AC2 15 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
18 AC2 15 MLA G .   ? MLA A 306 . ? 1_555 ? 
19 AC2 15 EDO H .   ? EDO A 307 . ? 1_555 ? 
20 AC3 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
21 AC3 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
22 AC3 4  HOH L .   ? HOH A 418 . ? 1_555 ? 
23 AC3 4  HOH L .   ? HOH A 546 . ? 1_555 ? 
24 AC4 7  HIS A 17  ? HIS A 17  . ? 1_555 ? 
25 AC4 7  PRO A 21  ? PRO A 21  . ? 1_555 ? 
26 AC4 7  PRO A 46  ? PRO A 46  . ? 1_655 ? 
27 AC4 7  LEU A 47  ? LEU A 47  . ? 1_655 ? 
28 AC4 7  HOH L .   ? HOH A 412 . ? 1_555 ? 
29 AC4 7  HOH L .   ? HOH A 445 . ? 1_655 ? 
30 AC4 7  HOH L .   ? HOH A 507 . ? 1_655 ? 
31 AC5 3  LEU A 60  ? LEU A 60  . ? 1_555 ? 
32 AC5 3  LYS A 169 ? LYS A 170 . ? 1_555 ? 
33 AC5 3  GLY A 170 ? GLY A 171 . ? 1_555 ? 
34 AC6 6  ASN A 62  ? ASN A 62  . ? 1_555 ? 
35 AC6 6  GLN A 67  ? GLN A 67  . ? 1_555 ? 
36 AC6 6  V14 C .   ? V14 A 302 . ? 1_555 ? 
37 AC6 6  EDO H .   ? EDO A 307 . ? 1_555 ? 
38 AC6 6  HOH L .   ? HOH A 403 . ? 1_555 ? 
39 AC6 6  HOH L .   ? HOH A 413 . ? 1_555 ? 
40 AC7 6  GLN A 67  ? GLN A 67  . ? 1_555 ? 
41 AC7 6  ILE A 91  ? ILE A 91  . ? 1_555 ? 
42 AC7 6  GLN A 92  ? GLN A 92  . ? 1_555 ? 
43 AC7 6  V14 C .   ? V14 A 302 . ? 1_555 ? 
44 AC7 6  MLA G .   ? MLA A 306 . ? 1_555 ? 
45 AC7 6  HOH L .   ? HOH A 405 . ? 1_555 ? 
46 AC8 8  GLY A 6   ? GLY A 6   . ? 1_555 ? 
47 AC8 8  TYR A 7   ? TYR A 7   . ? 1_555 ? 
48 AC8 8  GLY A 8   ? GLY A 8   . ? 1_555 ? 
49 AC8 8  ASN A 11  ? ASN A 11  . ? 1_555 ? 
50 AC8 8  PHE A 230 ? PHE A 231 . ? 1_555 ? 
51 AC8 8  GLU A 238 ? GLU A 239 . ? 1_555 ? 
52 AC8 8  HOH L .   ? HOH A 492 . ? 1_555 ? 
53 AC8 8  HOH L .   ? HOH A 553 . ? 1_555 ? 
54 AC9 3  LEU A 100 ? LEU A 100 . ? 1_555 ? 
55 AC9 3  ASP A 101 ? ASP A 101 . ? 1_555 ? 
56 AC9 3  HOH L .   ? HOH A 663 . ? 1_545 ? 
57 AD1 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
58 AD1 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
59 AD1 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
60 AD1 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
61 AD1 5  HOH L .   ? HOH A 494 . ? 1_555 ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    214 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   A 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.82 
# 
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 10  ? ? CD2 A HIS 10  ? ? 1.424 1.354 0.070 0.009 N 
2 1 CG A LEU 224 ? B CD2 A LEU 224 ? ? 2.913 1.514 1.399 0.037 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              224 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              224 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CD2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              224 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                71.22 
_pdbx_validate_rmsd_angle.angle_target_value         111.00 
_pdbx_validate_rmsd_angle.angle_deviation            -39.78 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.70 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -140.35 19.55   
2 1 ARG A 27  ? ? -141.09 54.04   
3 1 LYS A 111 ? ? 71.90   -3.94   
4 1 PHE A 176 ? ? -152.21 65.25   
5 1 ASN A 244 ? ? -97.95  52.63   
6 1 LYS A 252 ? ? 53.16   -136.36 
7 1 ASN A 253 ? ? -90.38  54.68   
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BEZ C    C  N N 74  
BEZ O1   O  N N 75  
BEZ O2   O  N N 76  
BEZ C1   C  Y N 77  
BEZ C2   C  Y N 78  
BEZ C3   C  Y N 79  
BEZ C4   C  Y N 80  
BEZ C5   C  Y N 81  
BEZ C6   C  Y N 82  
BEZ HO2  H  N N 83  
BEZ H2   H  N N 84  
BEZ H3   H  N N 85  
BEZ H4   H  N N 86  
BEZ H5   H  N N 87  
BEZ H6   H  N N 88  
CYS N    N  N N 89  
CYS CA   C  N R 90  
CYS C    C  N N 91  
CYS O    O  N N 92  
CYS CB   C  N N 93  
CYS SG   S  N N 94  
CYS OXT  O  N N 95  
CYS H    H  N N 96  
CYS H2   H  N N 97  
CYS HA   H  N N 98  
CYS HB2  H  N N 99  
CYS HB3  H  N N 100 
CYS HG   H  N N 101 
CYS HXT  H  N N 102 
DMS S    S  N N 103 
DMS O    O  N N 104 
DMS C1   C  N N 105 
DMS C2   C  N N 106 
DMS H11  H  N N 107 
DMS H12  H  N N 108 
DMS H13  H  N N 109 
DMS H21  H  N N 110 
DMS H22  H  N N 111 
DMS H23  H  N N 112 
EDO C1   C  N N 113 
EDO O1   O  N N 114 
EDO C2   C  N N 115 
EDO O2   O  N N 116 
EDO H11  H  N N 117 
EDO H12  H  N N 118 
EDO HO1  H  N N 119 
EDO H21  H  N N 120 
EDO H22  H  N N 121 
EDO HO2  H  N N 122 
GLN N    N  N N 123 
GLN CA   C  N S 124 
GLN C    C  N N 125 
GLN O    O  N N 126 
GLN CB   C  N N 127 
GLN CG   C  N N 128 
GLN CD   C  N N 129 
GLN OE1  O  N N 130 
GLN NE2  N  N N 131 
GLN OXT  O  N N 132 
GLN H    H  N N 133 
GLN H2   H  N N 134 
GLN HA   H  N N 135 
GLN HB2  H  N N 136 
GLN HB3  H  N N 137 
GLN HG2  H  N N 138 
GLN HG3  H  N N 139 
GLN HE21 H  N N 140 
GLN HE22 H  N N 141 
GLN HXT  H  N N 142 
GLU N    N  N N 143 
GLU CA   C  N S 144 
GLU C    C  N N 145 
GLU O    O  N N 146 
GLU CB   C  N N 147 
GLU CG   C  N N 148 
GLU CD   C  N N 149 
GLU OE1  O  N N 150 
GLU OE2  O  N N 151 
GLU OXT  O  N N 152 
GLU H    H  N N 153 
GLU H2   H  N N 154 
GLU HA   H  N N 155 
GLU HB2  H  N N 156 
GLU HB3  H  N N 157 
GLU HG2  H  N N 158 
GLU HG3  H  N N 159 
GLU HE2  H  N N 160 
GLU HXT  H  N N 161 
GLY N    N  N N 162 
GLY CA   C  N N 163 
GLY C    C  N N 164 
GLY O    O  N N 165 
GLY OXT  O  N N 166 
GLY H    H  N N 167 
GLY H2   H  N N 168 
GLY HA2  H  N N 169 
GLY HA3  H  N N 170 
GLY HXT  H  N N 171 
HIS N    N  N N 172 
HIS CA   C  N S 173 
HIS C    C  N N 174 
HIS O    O  N N 175 
HIS CB   C  N N 176 
HIS CG   C  Y N 177 
HIS ND1  N  Y N 178 
HIS CD2  C  Y N 179 
HIS CE1  C  Y N 180 
HIS NE2  N  Y N 181 
HIS OXT  O  N N 182 
HIS H    H  N N 183 
HIS H2   H  N N 184 
HIS HA   H  N N 185 
HIS HB2  H  N N 186 
HIS HB3  H  N N 187 
HIS HD1  H  N N 188 
HIS HD2  H  N N 189 
HIS HE1  H  N N 190 
HIS HE2  H  N N 191 
HIS HXT  H  N N 192 
HOH O    O  N N 193 
HOH H1   H  N N 194 
HOH H2   H  N N 195 
ILE N    N  N N 196 
ILE CA   C  N S 197 
ILE C    C  N N 198 
ILE O    O  N N 199 
ILE CB   C  N S 200 
ILE CG1  C  N N 201 
ILE CG2  C  N N 202 
ILE CD1  C  N N 203 
ILE OXT  O  N N 204 
ILE H    H  N N 205 
ILE H2   H  N N 206 
ILE HA   H  N N 207 
ILE HB   H  N N 208 
ILE HG12 H  N N 209 
ILE HG13 H  N N 210 
ILE HG21 H  N N 211 
ILE HG22 H  N N 212 
ILE HG23 H  N N 213 
ILE HD11 H  N N 214 
ILE HD12 H  N N 215 
ILE HD13 H  N N 216 
ILE HXT  H  N N 217 
LEU N    N  N N 218 
LEU CA   C  N S 219 
LEU C    C  N N 220 
LEU O    O  N N 221 
LEU CB   C  N N 222 
LEU CG   C  N N 223 
LEU CD1  C  N N 224 
LEU CD2  C  N N 225 
LEU OXT  O  N N 226 
LEU H    H  N N 227 
LEU H2   H  N N 228 
LEU HA   H  N N 229 
LEU HB2  H  N N 230 
LEU HB3  H  N N 231 
LEU HG   H  N N 232 
LEU HD11 H  N N 233 
LEU HD12 H  N N 234 
LEU HD13 H  N N 235 
LEU HD21 H  N N 236 
LEU HD22 H  N N 237 
LEU HD23 H  N N 238 
LEU HXT  H  N N 239 
LYS N    N  N N 240 
LYS CA   C  N S 241 
LYS C    C  N N 242 
LYS O    O  N N 243 
LYS CB   C  N N 244 
LYS CG   C  N N 245 
LYS CD   C  N N 246 
LYS CE   C  N N 247 
LYS NZ   N  N N 248 
LYS OXT  O  N N 249 
LYS H    H  N N 250 
LYS H2   H  N N 251 
LYS HA   H  N N 252 
LYS HB2  H  N N 253 
LYS HB3  H  N N 254 
LYS HG2  H  N N 255 
LYS HG3  H  N N 256 
LYS HD2  H  N N 257 
LYS HD3  H  N N 258 
LYS HE2  H  N N 259 
LYS HE3  H  N N 260 
LYS HZ1  H  N N 261 
LYS HZ2  H  N N 262 
LYS HZ3  H  N N 263 
LYS HXT  H  N N 264 
MET N    N  N N 265 
MET CA   C  N S 266 
MET C    C  N N 267 
MET O    O  N N 268 
MET CB   C  N N 269 
MET CG   C  N N 270 
MET SD   S  N N 271 
MET CE   C  N N 272 
MET OXT  O  N N 273 
MET H    H  N N 274 
MET H2   H  N N 275 
MET HA   H  N N 276 
MET HB2  H  N N 277 
MET HB3  H  N N 278 
MET HG2  H  N N 279 
MET HG3  H  N N 280 
MET HE1  H  N N 281 
MET HE2  H  N N 282 
MET HE3  H  N N 283 
MET HXT  H  N N 284 
MLA C1   C  N N 285 
MLA O1A  O  N N 286 
MLA O1B  O  N N 287 
MLA C2   C  N N 288 
MLA C3   C  N N 289 
MLA O3A  O  N N 290 
MLA O3B  O  N N 291 
MLA H1A  H  N N 292 
MLA HC21 H  N N 293 
MLA HC22 H  N N 294 
MLA H3B  H  N N 295 
PEG C1   C  N N 296 
PEG O1   O  N N 297 
PEG C2   C  N N 298 
PEG O2   O  N N 299 
PEG C3   C  N N 300 
PEG C4   C  N N 301 
PEG O4   O  N N 302 
PEG H11  H  N N 303 
PEG H12  H  N N 304 
PEG HO1  H  N N 305 
PEG H21  H  N N 306 
PEG H22  H  N N 307 
PEG H31  H  N N 308 
PEG H32  H  N N 309 
PEG H41  H  N N 310 
PEG H42  H  N N 311 
PEG HO4  H  N N 312 
PHE N    N  N N 313 
PHE CA   C  N S 314 
PHE C    C  N N 315 
PHE O    O  N N 316 
PHE CB   C  N N 317 
PHE CG   C  Y N 318 
PHE CD1  C  Y N 319 
PHE CD2  C  Y N 320 
PHE CE1  C  Y N 321 
PHE CE2  C  Y N 322 
PHE CZ   C  Y N 323 
PHE OXT  O  N N 324 
PHE H    H  N N 325 
PHE H2   H  N N 326 
PHE HA   H  N N 327 
PHE HB2  H  N N 328 
PHE HB3  H  N N 329 
PHE HD1  H  N N 330 
PHE HD2  H  N N 331 
PHE HE1  H  N N 332 
PHE HE2  H  N N 333 
PHE HZ   H  N N 334 
PHE HXT  H  N N 335 
PRO N    N  N N 336 
PRO CA   C  N S 337 
PRO C    C  N N 338 
PRO O    O  N N 339 
PRO CB   C  N N 340 
PRO CG   C  N N 341 
PRO CD   C  N N 342 
PRO OXT  O  N N 343 
PRO H    H  N N 344 
PRO HA   H  N N 345 
PRO HB2  H  N N 346 
PRO HB3  H  N N 347 
PRO HG2  H  N N 348 
PRO HG3  H  N N 349 
PRO HD2  H  N N 350 
PRO HD3  H  N N 351 
PRO HXT  H  N N 352 
SER N    N  N N 353 
SER CA   C  N S 354 
SER C    C  N N 355 
SER O    O  N N 356 
SER CB   C  N N 357 
SER OG   O  N N 358 
SER OXT  O  N N 359 
SER H    H  N N 360 
SER H2   H  N N 361 
SER HA   H  N N 362 
SER HB2  H  N N 363 
SER HB3  H  N N 364 
SER HG   H  N N 365 
SER HXT  H  N N 366 
THR N    N  N N 367 
THR CA   C  N S 368 
THR C    C  N N 369 
THR O    O  N N 370 
THR CB   C  N R 371 
THR OG1  O  N N 372 
THR CG2  C  N N 373 
THR OXT  O  N N 374 
THR H    H  N N 375 
THR H2   H  N N 376 
THR HA   H  N N 377 
THR HB   H  N N 378 
THR HG1  H  N N 379 
THR HG21 H  N N 380 
THR HG22 H  N N 381 
THR HG23 H  N N 382 
THR HXT  H  N N 383 
TRP N    N  N N 384 
TRP CA   C  N S 385 
TRP C    C  N N 386 
TRP O    O  N N 387 
TRP CB   C  N N 388 
TRP CG   C  Y N 389 
TRP CD1  C  Y N 390 
TRP CD2  C  Y N 391 
TRP NE1  N  Y N 392 
TRP CE2  C  Y N 393 
TRP CE3  C  Y N 394 
TRP CZ2  C  Y N 395 
TRP CZ3  C  Y N 396 
TRP CH2  C  Y N 397 
TRP OXT  O  N N 398 
TRP H    H  N N 399 
TRP H2   H  N N 400 
TRP HA   H  N N 401 
TRP HB2  H  N N 402 
TRP HB3  H  N N 403 
TRP HD1  H  N N 404 
TRP HE1  H  N N 405 
TRP HE3  H  N N 406 
TRP HZ2  H  N N 407 
TRP HZ3  H  N N 408 
TRP HH2  H  N N 409 
TRP HXT  H  N N 410 
TYR N    N  N N 411 
TYR CA   C  N S 412 
TYR C    C  N N 413 
TYR O    O  N N 414 
TYR CB   C  N N 415 
TYR CG   C  Y N 416 
TYR CD1  C  Y N 417 
TYR CD2  C  Y N 418 
TYR CE1  C  Y N 419 
TYR CE2  C  Y N 420 
TYR CZ   C  Y N 421 
TYR OH   O  N N 422 
TYR OXT  O  N N 423 
TYR H    H  N N 424 
TYR H2   H  N N 425 
TYR HA   H  N N 426 
TYR HB2  H  N N 427 
TYR HB3  H  N N 428 
TYR HD1  H  N N 429 
TYR HD2  H  N N 430 
TYR HE1  H  N N 431 
TYR HE2  H  N N 432 
TYR HH   H  N N 433 
TYR HXT  H  N N 434 
V14 F20  F  N N 435 
V14 C5   C  Y N 436 
V14 C4   C  Y N 437 
V14 S7   S  N N 438 
V14 O9   O  N N 439 
V14 N10  N  N N 440 
V14 O8   O  N N 441 
V14 C3   C  Y N 442 
V14 F12  F  N N 443 
V14 C2   C  Y N 444 
V14 F13  F  N N 445 
V14 C6   C  Y N 446 
V14 C1   C  Y N 447 
V14 S11  S  N N 448 
V14 O16  O  N N 449 
V14 O17  O  N N 450 
V14 C15  C  N N 451 
V14 C18  C  N N 452 
V14 O21  O  N N 453 
V14 N19  N  N N 454 
V14 C14  C  N N 455 
V14 C28  C  N N 456 
V14 C27  C  N N 457 
V14 C26  C  N N 458 
V14 C25  C  N N 459 
V14 C24  C  N N 460 
V14 C23  C  N N 461 
V14 C22  C  N N 462 
V14 H1   H  N N 463 
V14 H2   H  N N 464 
V14 H3   H  N N 465 
V14 H4   H  N N 466 
V14 H5   H  N N 467 
V14 H6   H  N N 468 
V14 H7   H  N N 469 
V14 H8   H  N N 470 
V14 H9   H  N N 471 
V14 H10  H  N N 472 
V14 H11  H  N N 473 
V14 H12  H  N N 474 
V14 H13  H  N N 475 
V14 H14  H  N N 476 
V14 H15  H  N N 477 
V14 H16  H  N N 478 
V14 H17  H  N N 479 
V14 H18  H  N N 480 
V14 H19  H  N N 481 
V14 H20  H  N N 482 
V14 H21  H  N N 483 
V14 H22  H  N N 484 
V14 H23  H  N N 485 
VAL N    N  N N 486 
VAL CA   C  N S 487 
VAL C    C  N N 488 
VAL O    O  N N 489 
VAL CB   C  N N 490 
VAL CG1  C  N N 491 
VAL CG2  C  N N 492 
VAL OXT  O  N N 493 
VAL H    H  N N 494 
VAL H2   H  N N 495 
VAL HA   H  N N 496 
VAL HB   H  N N 497 
VAL HG11 H  N N 498 
VAL HG12 H  N N 499 
VAL HG13 H  N N 500 
VAL HG21 H  N N 501 
VAL HG22 H  N N 502 
VAL HG23 H  N N 503 
VAL HXT  H  N N 504 
ZN  ZN   ZN N N 505 
# 
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  
BEZ C   O1   doub N N 70  
BEZ C   O2   sing N N 71  
BEZ C   C1   sing N N 72  
BEZ O2  HO2  sing N N 73  
BEZ C1  C2   doub Y N 74  
BEZ C1  C6   sing Y N 75  
BEZ C2  C3   sing Y N 76  
BEZ C2  H2   sing N N 77  
BEZ C3  C4   doub Y N 78  
BEZ C3  H3   sing N N 79  
BEZ C4  C5   sing Y N 80  
BEZ C4  H4   sing N N 81  
BEZ C5  C6   doub Y N 82  
BEZ C5  H5   sing N N 83  
BEZ C6  H6   sing N N 84  
CYS N   CA   sing N N 85  
CYS N   H    sing N N 86  
CYS N   H2   sing N N 87  
CYS CA  C    sing N N 88  
CYS CA  CB   sing N N 89  
CYS CA  HA   sing N N 90  
CYS C   O    doub N N 91  
CYS C   OXT  sing N N 92  
CYS CB  SG   sing N N 93  
CYS CB  HB2  sing N N 94  
CYS CB  HB3  sing N N 95  
CYS SG  HG   sing N N 96  
CYS OXT HXT  sing N N 97  
DMS S   O    doub N N 98  
DMS S   C1   sing N N 99  
DMS S   C2   sing N N 100 
DMS C1  H11  sing N N 101 
DMS C1  H12  sing N N 102 
DMS C1  H13  sing N N 103 
DMS C2  H21  sing N N 104 
DMS C2  H22  sing N N 105 
DMS C2  H23  sing N N 106 
EDO C1  O1   sing N N 107 
EDO C1  C2   sing N N 108 
EDO C1  H11  sing N N 109 
EDO C1  H12  sing N N 110 
EDO O1  HO1  sing N N 111 
EDO C2  O2   sing N N 112 
EDO C2  H21  sing N N 113 
EDO C2  H22  sing N N 114 
EDO O2  HO2  sing N N 115 
GLN N   CA   sing N N 116 
GLN N   H    sing N N 117 
GLN N   H2   sing N N 118 
GLN CA  C    sing N N 119 
GLN CA  CB   sing N N 120 
GLN CA  HA   sing N N 121 
GLN C   O    doub N N 122 
GLN C   OXT  sing N N 123 
GLN CB  CG   sing N N 124 
GLN CB  HB2  sing N N 125 
GLN CB  HB3  sing N N 126 
GLN CG  CD   sing N N 127 
GLN CG  HG2  sing N N 128 
GLN CG  HG3  sing N N 129 
GLN CD  OE1  doub N N 130 
GLN CD  NE2  sing N N 131 
GLN NE2 HE21 sing N N 132 
GLN NE2 HE22 sing N N 133 
GLN OXT HXT  sing N N 134 
GLU N   CA   sing N N 135 
GLU N   H    sing N N 136 
GLU N   H2   sing N N 137 
GLU CA  C    sing N N 138 
GLU CA  CB   sing N N 139 
GLU CA  HA   sing N N 140 
GLU C   O    doub N N 141 
GLU C   OXT  sing N N 142 
GLU CB  CG   sing N N 143 
GLU CB  HB2  sing N N 144 
GLU CB  HB3  sing N N 145 
GLU CG  CD   sing N N 146 
GLU CG  HG2  sing N N 147 
GLU CG  HG3  sing N N 148 
GLU CD  OE1  doub N N 149 
GLU CD  OE2  sing N N 150 
GLU OE2 HE2  sing N N 151 
GLU OXT HXT  sing N N 152 
GLY N   CA   sing N N 153 
GLY N   H    sing N N 154 
GLY N   H2   sing N N 155 
GLY CA  C    sing N N 156 
GLY CA  HA2  sing N N 157 
GLY CA  HA3  sing N N 158 
GLY C   O    doub N N 159 
GLY C   OXT  sing N N 160 
GLY OXT HXT  sing N N 161 
HIS N   CA   sing N N 162 
HIS N   H    sing N N 163 
HIS N   H2   sing N N 164 
HIS CA  C    sing N N 165 
HIS CA  CB   sing N N 166 
HIS CA  HA   sing N N 167 
HIS C   O    doub N N 168 
HIS C   OXT  sing N N 169 
HIS CB  CG   sing N N 170 
HIS CB  HB2  sing N N 171 
HIS CB  HB3  sing N N 172 
HIS CG  ND1  sing Y N 173 
HIS CG  CD2  doub Y N 174 
HIS ND1 CE1  doub Y N 175 
HIS ND1 HD1  sing N N 176 
HIS CD2 NE2  sing Y N 177 
HIS CD2 HD2  sing N N 178 
HIS CE1 NE2  sing Y N 179 
HIS CE1 HE1  sing N N 180 
HIS NE2 HE2  sing N N 181 
HIS OXT HXT  sing N N 182 
HOH O   H1   sing N N 183 
HOH O   H2   sing N N 184 
ILE N   CA   sing N N 185 
ILE N   H    sing N N 186 
ILE N   H2   sing N N 187 
ILE CA  C    sing N N 188 
ILE CA  CB   sing N N 189 
ILE CA  HA   sing N N 190 
ILE C   O    doub N N 191 
ILE C   OXT  sing N N 192 
ILE CB  CG1  sing N N 193 
ILE CB  CG2  sing N N 194 
ILE CB  HB   sing N N 195 
ILE CG1 CD1  sing N N 196 
ILE CG1 HG12 sing N N 197 
ILE CG1 HG13 sing N N 198 
ILE CG2 HG21 sing N N 199 
ILE CG2 HG22 sing N N 200 
ILE CG2 HG23 sing N N 201 
ILE CD1 HD11 sing N N 202 
ILE CD1 HD12 sing N N 203 
ILE CD1 HD13 sing N N 204 
ILE OXT HXT  sing N N 205 
LEU N   CA   sing N N 206 
LEU N   H    sing N N 207 
LEU N   H2   sing N N 208 
LEU CA  C    sing N N 209 
LEU CA  CB   sing N N 210 
LEU CA  HA   sing N N 211 
LEU C   O    doub N N 212 
LEU C   OXT  sing N N 213 
LEU CB  CG   sing N N 214 
LEU CB  HB2  sing N N 215 
LEU CB  HB3  sing N N 216 
LEU CG  CD1  sing N N 217 
LEU CG  CD2  sing N N 218 
LEU CG  HG   sing N N 219 
LEU CD1 HD11 sing N N 220 
LEU CD1 HD12 sing N N 221 
LEU CD1 HD13 sing N N 222 
LEU CD2 HD21 sing N N 223 
LEU CD2 HD22 sing N N 224 
LEU CD2 HD23 sing N N 225 
LEU OXT HXT  sing N N 226 
LYS N   CA   sing N N 227 
LYS N   H    sing N N 228 
LYS N   H2   sing N N 229 
LYS CA  C    sing N N 230 
LYS CA  CB   sing N N 231 
LYS CA  HA   sing N N 232 
LYS C   O    doub N N 233 
LYS C   OXT  sing N N 234 
LYS CB  CG   sing N N 235 
LYS CB  HB2  sing N N 236 
LYS CB  HB3  sing N N 237 
LYS CG  CD   sing N N 238 
LYS CG  HG2  sing N N 239 
LYS CG  HG3  sing N N 240 
LYS CD  CE   sing N N 241 
LYS CD  HD2  sing N N 242 
LYS CD  HD3  sing N N 243 
LYS CE  NZ   sing N N 244 
LYS CE  HE2  sing N N 245 
LYS CE  HE3  sing N N 246 
LYS NZ  HZ1  sing N N 247 
LYS NZ  HZ2  sing N N 248 
LYS NZ  HZ3  sing N N 249 
LYS OXT HXT  sing N N 250 
MET N   CA   sing N N 251 
MET N   H    sing N N 252 
MET N   H2   sing N N 253 
MET CA  C    sing N N 254 
MET CA  CB   sing N N 255 
MET CA  HA   sing N N 256 
MET C   O    doub N N 257 
MET C   OXT  sing N N 258 
MET CB  CG   sing N N 259 
MET CB  HB2  sing N N 260 
MET CB  HB3  sing N N 261 
MET CG  SD   sing N N 262 
MET CG  HG2  sing N N 263 
MET CG  HG3  sing N N 264 
MET SD  CE   sing N N 265 
MET CE  HE1  sing N N 266 
MET CE  HE2  sing N N 267 
MET CE  HE3  sing N N 268 
MET OXT HXT  sing N N 269 
MLA C1  O1A  sing N N 270 
MLA C1  O1B  doub N N 271 
MLA C1  C2   sing N N 272 
MLA O1A H1A  sing N N 273 
MLA C2  C3   sing N N 274 
MLA C2  HC21 sing N N 275 
MLA C2  HC22 sing N N 276 
MLA C3  O3A  doub N N 277 
MLA C3  O3B  sing N N 278 
MLA O3B H3B  sing N N 279 
PEG C1  O1   sing N N 280 
PEG C1  C2   sing N N 281 
PEG C1  H11  sing N N 282 
PEG C1  H12  sing N N 283 
PEG O1  HO1  sing N N 284 
PEG C2  O2   sing N N 285 
PEG C2  H21  sing N N 286 
PEG C2  H22  sing N N 287 
PEG O2  C3   sing N N 288 
PEG C3  C4   sing N N 289 
PEG C3  H31  sing N N 290 
PEG C3  H32  sing N N 291 
PEG C4  O4   sing N N 292 
PEG C4  H41  sing N N 293 
PEG C4  H42  sing N N 294 
PEG O4  HO4  sing N N 295 
PHE N   CA   sing N N 296 
PHE N   H    sing N N 297 
PHE N   H2   sing N N 298 
PHE CA  C    sing N N 299 
PHE CA  CB   sing N N 300 
PHE CA  HA   sing N N 301 
PHE C   O    doub N N 302 
PHE C   OXT  sing N N 303 
PHE CB  CG   sing N N 304 
PHE CB  HB2  sing N N 305 
PHE CB  HB3  sing N N 306 
PHE CG  CD1  doub Y N 307 
PHE CG  CD2  sing Y N 308 
PHE CD1 CE1  sing Y N 309 
PHE CD1 HD1  sing N N 310 
PHE CD2 CE2  doub Y N 311 
PHE CD2 HD2  sing N N 312 
PHE CE1 CZ   doub Y N 313 
PHE CE1 HE1  sing N N 314 
PHE CE2 CZ   sing Y N 315 
PHE CE2 HE2  sing N N 316 
PHE CZ  HZ   sing N N 317 
PHE OXT HXT  sing N N 318 
PRO N   CA   sing N N 319 
PRO N   CD   sing N N 320 
PRO N   H    sing N N 321 
PRO CA  C    sing N N 322 
PRO CA  CB   sing N N 323 
PRO CA  HA   sing N N 324 
PRO C   O    doub N N 325 
PRO C   OXT  sing N N 326 
PRO CB  CG   sing N N 327 
PRO CB  HB2  sing N N 328 
PRO CB  HB3  sing N N 329 
PRO CG  CD   sing N N 330 
PRO CG  HG2  sing N N 331 
PRO CG  HG3  sing N N 332 
PRO CD  HD2  sing N N 333 
PRO CD  HD3  sing N N 334 
PRO OXT HXT  sing N N 335 
SER N   CA   sing N N 336 
SER N   H    sing N N 337 
SER N   H2   sing N N 338 
SER CA  C    sing N N 339 
SER CA  CB   sing N N 340 
SER CA  HA   sing N N 341 
SER C   O    doub N N 342 
SER C   OXT  sing N N 343 
SER CB  OG   sing N N 344 
SER CB  HB2  sing N N 345 
SER CB  HB3  sing N N 346 
SER OG  HG   sing N N 347 
SER OXT HXT  sing N N 348 
THR N   CA   sing N N 349 
THR N   H    sing N N 350 
THR N   H2   sing N N 351 
THR CA  C    sing N N 352 
THR CA  CB   sing N N 353 
THR CA  HA   sing N N 354 
THR C   O    doub N N 355 
THR C   OXT  sing N N 356 
THR CB  OG1  sing N N 357 
THR CB  CG2  sing N N 358 
THR CB  HB   sing N N 359 
THR OG1 HG1  sing N N 360 
THR CG2 HG21 sing N N 361 
THR CG2 HG22 sing N N 362 
THR CG2 HG23 sing N N 363 
THR OXT HXT  sing N N 364 
TRP N   CA   sing N N 365 
TRP N   H    sing N N 366 
TRP N   H2   sing N N 367 
TRP CA  C    sing N N 368 
TRP CA  CB   sing N N 369 
TRP CA  HA   sing N N 370 
TRP C   O    doub N N 371 
TRP C   OXT  sing N N 372 
TRP CB  CG   sing N N 373 
TRP CB  HB2  sing N N 374 
TRP CB  HB3  sing N N 375 
TRP CG  CD1  doub Y N 376 
TRP CG  CD2  sing Y N 377 
TRP CD1 NE1  sing Y N 378 
TRP CD1 HD1  sing N N 379 
TRP CD2 CE2  doub Y N 380 
TRP CD2 CE3  sing Y N 381 
TRP NE1 CE2  sing Y N 382 
TRP NE1 HE1  sing N N 383 
TRP CE2 CZ2  sing Y N 384 
TRP CE3 CZ3  doub Y N 385 
TRP CE3 HE3  sing N N 386 
TRP CZ2 CH2  doub Y N 387 
TRP CZ2 HZ2  sing N N 388 
TRP CZ3 CH2  sing Y N 389 
TRP CZ3 HZ3  sing N N 390 
TRP CH2 HH2  sing N N 391 
TRP OXT HXT  sing N N 392 
TYR N   CA   sing N N 393 
TYR N   H    sing N N 394 
TYR N   H2   sing N N 395 
TYR CA  C    sing N N 396 
TYR CA  CB   sing N N 397 
TYR CA  HA   sing N N 398 
TYR C   O    doub N N 399 
TYR C   OXT  sing N N 400 
TYR CB  CG   sing N N 401 
TYR CB  HB2  sing N N 402 
TYR CB  HB3  sing N N 403 
TYR CG  CD1  doub Y N 404 
TYR CG  CD2  sing Y N 405 
TYR CD1 CE1  sing Y N 406 
TYR CD1 HD1  sing N N 407 
TYR CD2 CE2  doub Y N 408 
TYR CD2 HD2  sing N N 409 
TYR CE1 CZ   doub Y N 410 
TYR CE1 HE1  sing N N 411 
TYR CE2 CZ   sing Y N 412 
TYR CE2 HE2  sing N N 413 
TYR CZ  OH   sing N N 414 
TYR OH  HH   sing N N 415 
TYR OXT HXT  sing N N 416 
V14 C18 O21  sing N N 417 
V14 C18 C15  sing N N 418 
V14 C15 S11  sing N N 419 
V14 O17 S11  doub N N 420 
V14 C22 C23  sing N N 421 
V14 C22 C14  sing N N 422 
V14 C23 C24  sing N N 423 
V14 N19 C14  sing N N 424 
V14 N19 C6   sing N N 425 
V14 C24 C25  sing N N 426 
V14 S11 C1   sing N N 427 
V14 S11 O16  doub N N 428 
V14 C14 C28  sing N N 429 
V14 C6  C1   doub Y N 430 
V14 C6  C5   sing Y N 431 
V14 C1  C2   sing Y N 432 
V14 F20 C5   sing N N 433 
V14 C25 C26  sing N N 434 
V14 C5  C4   doub Y N 435 
V14 C26 C27  sing N N 436 
V14 C28 C27  sing N N 437 
V14 C2  F13  sing N N 438 
V14 C2  C3   doub Y N 439 
V14 C4  C3   sing Y N 440 
V14 C4  S7   sing N N 441 
V14 C3  F12  sing N N 442 
V14 N10 S7   sing N N 443 
V14 S7  O9   doub N N 444 
V14 S7  O8   doub N N 445 
V14 N10 H1   sing N N 446 
V14 N10 H2   sing N N 447 
V14 C15 H3   sing N N 448 
V14 C15 H4   sing N N 449 
V14 C18 H5   sing N N 450 
V14 C18 H6   sing N N 451 
V14 O21 H7   sing N N 452 
V14 N19 H8   sing N N 453 
V14 C14 H9   sing N N 454 
V14 C28 H10  sing N N 455 
V14 C28 H11  sing N N 456 
V14 C27 H12  sing N N 457 
V14 C27 H13  sing N N 458 
V14 C26 H14  sing N N 459 
V14 C26 H15  sing N N 460 
V14 C25 H16  sing N N 461 
V14 C25 H17  sing N N 462 
V14 C24 H18  sing N N 463 
V14 C24 H19  sing N N 464 
V14 C23 H20  sing N N 465 
V14 C23 H21  sing N N 466 
V14 C22 H22  sing N N 467 
V14 C22 H23  sing N N 468 
VAL N   CA   sing N N 469 
VAL N   H    sing N N 470 
VAL N   H2   sing N N 471 
VAL CA  C    sing N N 472 
VAL CA  CB   sing N N 473 
VAL CA  HA   sing N N 474 
VAL C   O    doub N N 475 
VAL C   OXT  sing N N 476 
VAL CB  CG1  sing N N 477 
VAL CB  CG2  sing N N 478 
VAL CB  HB   sing N N 479 
VAL CG1 HG11 sing N N 480 
VAL CG1 HG12 sing N N 481 
VAL CG1 HG13 sing N N 482 
VAL CG2 HG21 sing N N 483 
VAL CG2 HG22 sing N N 484 
VAL CG2 HG23 sing N N 485 
VAL OXT HXT  sing N N 486 
# 
_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                    6QL3 
_atom_sites.fract_transf_matrix[1][1]   0.023692 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005983 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024170 
_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]   0.014356 
_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 4   ? 30.036 2.291   7.408   1.00 39.03 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 30.984 2.008   8.539   1.00 36.73 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.365 0.927   9.421   1.00 23.77 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.559 -0.277  9.265   1.00 23.32 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 31.100 3.317   9.363   1.00 40.58 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 30.027 4.310   9.011   1.00 58.28 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 29.700 5.363   9.849   1.00 77.69 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 29.214 4.416   7.916   1.00 69.20 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 28.719 6.075   9.287   1.00 81.95 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 28.398 5.509   8.094   1.00 77.43 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.509 1.380   10.322  1.00 18.73 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 28.749 0.437   11.146  1.00 13.56 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 27.740 -0.406  10.350  1.00 12.86 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.160 0.043   9.361   1.00 14.92 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.126 1.136   12.359  1.00 12.62 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 26.919 1.938   12.026  1.00 10.94 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 26.884 3.252   11.719  1.00 13.03 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.570 1.461   11.995  1.00 10.10 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.611 3.669   11.461  1.00 13.97 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.775 2.581   11.646  1.00 11.77 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 24.965 0.215   12.250  1.00 10.39 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.404 2.474   11.537  1.00 12.70 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.577 0.117   12.143  1.00 11.18 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 22.822 1.242   11.779  1.00 11.68 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.504 -1.614  10.885  1.00 11.00 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.477 -2.462  10.305  1.00 11.11 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.137 -3.590  11.261  1.00 9.51  ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.176 -3.374  12.484  1.00 9.93  ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 25.806 -4.761  10.697  1.00 10.26 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.352 -5.891  11.508  1.00 10.98 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.240 -7.120  11.272  1.00 14.66 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 25.856 -8.211  11.682  1.00 23.30 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 23.875 -6.213  11.250  1.00 11.00 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.028 -5.113  11.819  1.00 8.52  ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.637 -5.133  13.167  1.00 9.05  ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.523 -4.116  10.986  1.00 9.06  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 21.776 -4.155  13.651  1.00 8.64  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 21.660 -3.162  11.472  1.00 8.93  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.294 -3.187  12.803  1.00 7.89  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.451 -2.218  13.224  1.00 10.20 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.376 -6.980  10.569  1.00 14.91 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 28.295 -8.084  10.253  1.00 19.02 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.229 -8.398  11.412  1.00 18.39 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.365 -7.631  12.372  1.00 23.52 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 30.082 -9.420  11.198  1.00 23.98 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 31.090 -9.853  12.157  1.00 28.17 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 32.101 -8.728  12.379  1.00 24.41 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 32.589 -8.524  13.491  1.00 23.48 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 31.856 -11.043 11.564  1.00 36.03 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 32.873 -11.707 12.475  1.00 45.37 ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? 32.369 -7.949  11.321  1.00 19.47 ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? 33.450 -6.991  11.425  1.00 20.33 ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? 32.978 -5.607  11.793  1.00 19.13 ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? 33.751 -4.779  12.260  1.00 20.71 ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? 34.326 -7.034  10.159  1.00 22.25 ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? 34.945 -8.436  9.865   1.00 31.54 ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? 35.931 -8.972  10.685  1.00 42.89 ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? 34.555 -9.400  8.892   1.00 45.06 ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? 36.130 -10.213 10.271  1.00 45.93 ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? 35.443 -10.498 9.103   1.00 40.11 ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? 31.637 -5.377  11.706  1.00 15.00 ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? 31.170 -4.010  11.953  1.00 15.47 ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? 29.857 -3.981  12.763  1.00 12.74 ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? 29.252 -2.904  12.856  1.00 11.69 ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? 30.959 -3.238  10.645  1.00 14.54 ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? 29.853 -3.807  9.771   1.00 14.04 ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? 29.254 -4.824  10.090  1.00 16.05 ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? 29.529 -3.152  8.667   1.00 17.18 ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? 29.567 -5.099  13.452  1.00 12.80 ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? 28.269 -5.292  14.093  1.00 12.77 ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? 28.272 -4.734  15.509  1.00 9.87  ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? 29.184 -4.007  15.949  1.00 9.72  ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? 27.213 -5.042  16.264  1.00 8.27  ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? 26.979 -4.450  17.564  1.00 8.78  ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? 28.134 -4.506  18.544  1.00 9.35  ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? 28.279 -3.592  19.351  1.00 9.87  ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? 25.777 -5.259  18.059  1.00 11.25 ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? 24.970 -5.543  16.812  1.00 10.44 ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? 26.034 -5.755  15.745  1.00 8.50  ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? 28.992 -5.545  18.498  1.00 11.04 ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? 30.122 -5.655  19.426  1.00 13.50 ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? 31.175 -4.581  19.128  1.00 9.45  ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? 32.080 -4.360  19.959  1.00 12.98 ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? 30.782 -7.043  19.332  1.00 18.97 ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? 29.877 -8.163  19.794  1.00 24.99 ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? 29.663 -8.370  21.291  1.00 39.52 ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? 30.269 -9.331  21.860  1.00 54.90 ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? 28.836 -7.619  21.882  1.00 50.26 ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? 31.133 -4.000  17.912  1.00 9.53  ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? 32.135 -3.024  17.525  1.00 10.21 ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? 31.707 -1.573  17.743  1.00 9.14  ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? 32.509 -0.622  17.676  1.00 10.69 ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? 32.471 -3.173  16.050  1.00 11.50 ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? 33.202 -4.434  15.746  1.00 11.24 ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? 34.604 -4.468  15.803  1.00 16.31 ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? 32.761 -5.650  15.372  1.00 15.52 ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? 34.971 -5.703  15.502  1.00 20.96 ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? 33.875 -6.453  15.213  1.00 20.84 ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? 30.370 -1.344  17.917  1.00 8.86  ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? 29.855 0.002   17.813  1.00 9.16  ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? 30.437 0.939   18.864  1.00 8.78  ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? 30.523 2.140   18.606  1.00 9.02  ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? 28.298 -0.026  17.949  1.00 8.61  ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? 27.629 -0.699  16.790  1.00 6.93  ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? 28.119 -1.120  15.580  1.00 7.89  ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? 26.233 -1.041  16.765  1.00 8.00  ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? 27.152 -1.690  14.807  1.00 7.60  ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? 25.975 -1.644  15.525  1.00 7.97  ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? 25.173 -0.855  17.682  1.00 9.23  ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? 24.704 -2.116  15.157  1.00 7.56  ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? 23.925 -1.335  17.328  1.00 7.12  ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? 23.682 -1.868  16.061  1.00 7.45  ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? 30.800 0.420   20.034  1.00 9.08  ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? 31.302 1.271   21.097  1.00 9.18  ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? 32.561 2.053   20.711  1.00 11.26 ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? 32.811 3.080   21.292  1.00 10.27 ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? 31.535 0.472   22.391  1.00 9.35  ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? 32.766 -0.378  22.295  1.00 11.30 ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? 33.979 0.036   22.780  1.00 13.51 ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? 33.006 -1.527  21.626  1.00 11.25 ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? 34.879 -0.880  22.523  1.00 13.15 ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? 34.324 -1.851  21.827  1.00 13.08 ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? 33.310 1.568   19.708  1.00 12.45 ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? 34.556 2.272   19.397  1.00 12.47 ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? 34.248 3.623   18.745  1.00 11.93 ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? 35.004 4.561   18.892  1.00 18.48 ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? 35.423 1.422   18.470  1.00 13.77 ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? 35.923 0.143   19.144  1.00 13.25 ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? 36.714 -0.758  18.209  1.00 13.36 ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? 35.711 -1.698  17.556  1.00 10.64 ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? 36.429 -2.475  16.499  1.00 13.37 ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 19  ? 33.180 3.727   17.939  1.00 12.24 ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 19  ? 32.786 4.999   17.320  1.00 12.06 ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 19  ? 31.712 5.710   18.134  1.00 12.33 ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 19  ? 31.586 6.910   18.011  1.00 14.59 ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 19  ? 32.263 4.865   15.878  1.00 16.04 ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 19  ? 33.348 4.727   14.799  1.00 27.36 ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 19  ? 34.399 5.422   14.907  1.00 31.70 ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 19  ? 33.124 3.924   13.906  1.00 47.48 ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 20  ? 31.007 4.970   18.998  1.00 10.59 ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 20  ? 29.852 5.491   19.718  1.00 13.46 ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 20  ? 29.949 4.976   21.135  1.00 11.76 ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 20  ? 29.302 3.982   21.506  1.00 10.13 ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 20  ? 28.514 5.030   19.089  1.00 12.63 ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 20  ? 28.418 5.433   17.643  1.00 14.44 ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 20  ? 28.122 6.737   17.295  1.00 15.45 ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 20  ? 28.786 4.479   16.646  1.00 15.51 ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 20  ? 28.143 7.106   15.957  1.00 15.59 ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 20  ? 28.817 4.870   15.297  1.00 15.31 ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 20  ? 28.465 6.185   14.973  1.00 14.93 ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 21  ? 30.812 5.592   21.976  1.00 11.91 ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 21  ? 31.057 5.066   23.323  1.00 12.32 ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 21  ? 29.828 4.977   24.233  1.00 9.98  ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 21  ? 29.866 4.181   25.167  1.00 11.57 ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 21  ? 32.162 5.957   23.919  1.00 17.40 ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 21  ? 32.277 7.092   22.965  1.00 22.99 ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 21  ? 31.708 6.711   21.617  1.00 14.82 ? 21  PRO A CD  1 
ATOM   158  N  N   . ILE A 1 22  ? 28.771 5.753   23.916  1.00 10.10 ? 22  ILE A N   1 
ATOM   159  C  CA  . ILE A 1 22  ? 27.514 5.620   24.663  1.00 9.91  ? 22  ILE A CA  1 
ATOM   160  C  C   . ILE A 1 22  ? 26.939 4.202   24.530  1.00 8.89  ? 22  ILE A C   1 
ATOM   161  O  O   . ILE A 1 22  ? 26.052 3.833   25.305  1.00 9.75  ? 22  ILE A O   1 
ATOM   162  C  CB  . ILE A 1 22  ? 26.526 6.731   24.228  1.00 9.49  ? 22  ILE A CB  1 
ATOM   163  C  CG1 . ILE A 1 22  ? 25.425 6.993   25.266  1.00 13.38 ? 22  ILE A CG1 1 
ATOM   164  C  CG2 . ILE A 1 22  ? 25.916 6.384   22.866  1.00 10.85 ? 22  ILE A CG2 1 
ATOM   165  C  CD1 . ILE A 1 22  ? 25.896 7.502   26.596  1.00 15.90 ? 22  ILE A CD1 1 
ATOM   166  N  N   . ALA A 1 23  ? 27.448 3.363   23.624  1.00 8.13  ? 23  ALA A N   1 
ATOM   167  C  CA  . ALA A 1 23  ? 27.026 1.971   23.526  1.00 7.91  ? 23  ALA A CA  1 
ATOM   168  C  C   . ALA A 1 23  ? 27.116 1.259   24.868  1.00 8.74  ? 23  ALA A C   1 
ATOM   169  O  O   . ALA A 1 23  ? 26.440 0.260   25.069  1.00 10.16 ? 23  ALA A O   1 
ATOM   170  C  CB  . ALA A 1 23  ? 27.869 1.212   22.476  1.00 9.68  ? 23  ALA A CB  1 
ATOM   171  N  N   . LYS A 1 24  ? 28.053 1.699   25.741  1.00 10.01 ? 24  LYS A N   1 
ATOM   172  C  CA  . LYS A 1 24  ? 28.263 1.073   27.055  1.00 11.15 ? 24  LYS A CA  1 
ATOM   173  C  C   . LYS A 1 24  ? 27.649 1.946   28.147  1.00 11.39 ? 24  LYS A C   1 
ATOM   174  O  O   . LYS A 1 24  ? 28.023 1.862   29.315  1.00 14.39 ? 24  LYS A O   1 
ATOM   175  C  CB  . LYS A 1 24  ? 29.769 0.859   27.318  1.00 14.61 ? 24  LYS A CB  1 
ATOM   176  C  CG  . LYS A 1 24  ? 30.382 -0.103  26.294  1.00 17.59 ? 24  LYS A CG  1 
ATOM   177  C  CD  . LYS A 1 24  ? 31.887 -0.273  26.638  1.00 26.42 ? 24  LYS A CD  1 
ATOM   178  C  CE  . LYS A 1 24  ? 32.601 -1.257  25.734  1.00 28.59 ? 24  LYS A CE  1 
ATOM   179  N  NZ  . LYS A 1 24  ? 32.276 -2.640  26.137  1.00 36.54 ? 24  LYS A NZ  1 
ATOM   180  N  N   . GLY A 1 25  ? 26.634 2.756   27.753  1.00 10.72 ? 25  GLY A N   1 
ATOM   181  C  CA  . GLY A 1 25  ? 25.986 3.679   28.684  1.00 11.58 ? 25  GLY A CA  1 
ATOM   182  C  C   . GLY A 1 25  ? 25.029 3.036   29.689  1.00 11.87 ? 25  GLY A C   1 
ATOM   183  O  O   . GLY A 1 25  ? 24.843 1.824   29.717  1.00 12.19 ? 25  GLY A O   1 
ATOM   184  N  N   . GLU A 1 26  ? 24.339 3.882   30.469  1.00 11.90 ? 26  GLU A N   1 
ATOM   185  C  CA  . GLU A 1 26  ? 23.516 3.452   31.572  1.00 13.63 ? 26  GLU A CA  1 
ATOM   186  C  C   . GLU A 1 26  ? 22.086 3.201   31.119  1.00 10.94 ? 26  GLU A C   1 
ATOM   187  O  O   . GLU A 1 26  ? 21.286 2.701   31.927  1.00 12.68 ? 26  GLU A O   1 
ATOM   188  C  CB  . GLU A 1 26  ? 23.540 4.535   32.669  1.00 20.16 ? 26  GLU A CB  1 
ATOM   189  C  CG  . GLU A 1 26  ? 24.941 4.895   33.150  1.00 25.38 ? 26  GLU A CG  1 
ATOM   190  C  CD  . GLU A 1 26  ? 25.660 3.694   33.741  1.00 35.79 ? 26  GLU A CD  1 
ATOM   191  O  OE1 . GLU A 1 26  ? 25.019 2.981   34.551  1.00 42.33 ? 26  GLU A OE1 1 
ATOM   192  O  OE2 . GLU A 1 26  ? 26.860 3.477   33.406  1.00 46.12 ? 26  GLU A OE2 1 
ATOM   193  N  N   . ARG A 1 27  ? 21.691 3.589   29.889  1.00 7.99  ? 27  ARG A N   1 
ATOM   194  C  CA  . ARG A 1 27  ? 20.288 3.441   29.507  1.00 7.23  ? 27  ARG A CA  1 
ATOM   195  C  C   . ARG A 1 27  ? 20.203 2.995   28.052  1.00 5.90  ? 27  ARG A C   1 
ATOM   196  O  O   . ARG A 1 27  ? 19.474 3.556   27.220  1.00 6.72  ? 27  ARG A O   1 
ATOM   197  C  CB  . ARG A 1 27  ? 19.440 4.686   29.784  1.00 11.06 ? 27  ARG A CB  1 
ATOM   198  C  CG  . ARG A 1 27  ? 19.785 6.032   29.185  1.00 16.31 ? 27  ARG A CG  1 
ATOM   199  C  CD  . ARG A 1 27  ? 18.799 7.181   29.463  1.00 19.51 ? 27  ARG A CD  1 
ATOM   200  N  NE  . ARG A 1 27  ? 17.625 7.118   28.603  1.00 15.97 ? 27  ARG A NE  1 
ATOM   201  C  CZ  . ARG A 1 27  ? 16.766 8.115   28.428  1.00 12.76 ? 27  ARG A CZ  1 
ATOM   202  N  NH1 . ARG A 1 27  ? 16.948 9.264   29.056  1.00 12.54 ? 27  ARG A NH1 1 
ATOM   203  N  NH2 . ARG A 1 27  ? 15.729 7.960   27.625  1.00 15.34 ? 27  ARG A NH2 1 
ATOM   204  N  N   . GLN A 1 28  ? 20.895 1.902   27.747  1.00 6.15  ? 28  GLN A N   1 
ATOM   205  C  CA  . GLN A 1 28  ? 20.921 1.397   26.384  1.00 6.17  ? 28  GLN A CA  1 
ATOM   206  C  C   . GLN A 1 28  ? 19.785 0.401   26.104  1.00 4.91  ? 28  GLN A C   1 
ATOM   207  O  O   . GLN A 1 28  ? 19.260 -0.244  27.030  1.00 6.37  ? 28  GLN A O   1 
ATOM   208  C  CB  . GLN A 1 28  ? 22.293 0.693   26.112  1.00 7.31  ? 28  GLN A CB  1 
ATOM   209  C  CG  . GLN A 1 28  ? 23.426 1.736   26.091  1.00 5.87  ? 28  GLN A CG  1 
ATOM   210  C  CD  . GLN A 1 28  ? 23.325 2.535   24.809  1.00 6.70  ? 28  GLN A CD  1 
ATOM   211  O  OE1 . GLN A 1 28  ? 23.498 2.025   23.683  1.00 6.20  ? 28  GLN A OE1 1 
ATOM   212  N  NE2 . GLN A 1 28  ? 22.967 3.809   24.878  1.00 7.89  ? 28  GLN A NE2 1 
ATOM   213  N  N   . SER A 1 29  ? 19.386 0.365   24.838  1.00 5.13  ? 29  SER A N   1 
ATOM   214  C  CA  . SER A 1 29  ? 18.301 -0.510  24.376  1.00 4.58  ? 29  SER A CA  1 
ATOM   215  C  C   . SER A 1 29  ? 18.809 -1.388  23.272  1.00 5.05  ? 29  SER A C   1 
ATOM   216  O  O   . SER A 1 29  ? 19.784 -1.029  22.576  1.00 5.37  ? 29  SER A O   1 
ATOM   217  C  CB  . SER A 1 29  ? 17.165 0.379   23.793  1.00 4.77  ? 29  SER A CB  1 
ATOM   218  O  OG  . SER A 1 29  ? 16.575 1.117   24.880  1.00 5.54  ? 29  SER A OG  1 
ATOM   219  N  N   . PRO A 1 30  ? 18.163 -2.509  22.945  1.00 4.86  ? 30  PRO A N   1 
ATOM   220  C  CA  . PRO A 1 30  ? 16.990 -3.037  23.658  1.00 5.06  ? 30  PRO A CA  1 
ATOM   221  C  C   . PRO A 1 30  ? 17.395 -3.716  24.944  1.00 5.18  ? 30  PRO A C   1 
ATOM   222  O  O   . PRO A 1 30  ? 18.566 -3.759  25.290  1.00 5.42  ? 30  PRO A O   1 
ATOM   223  C  CB  . PRO A 1 30  ? 16.470 -4.048  22.640  1.00 6.05  ? 30  PRO A CB  1 
ATOM   224  C  CG  . PRO A 1 30  ? 17.777 -4.642  22.057  1.00 5.42  ? 30  PRO A CG  1 
ATOM   225  C  CD  . PRO A 1 30  ? 18.657 -3.422  21.896  1.00 4.61  ? 30  PRO A CD  1 
ATOM   226  N  N   . VAL A 1 31  ? 16.400 -4.270  25.649  1.00 4.72  ? 31  VAL A N   1 
ATOM   227  C  CA  . VAL A 1 31  ? 16.573 -5.018  26.853  1.00 4.76  ? 31  VAL A CA  1 
ATOM   228  C  C   . VAL A 1 31  ? 15.705 -6.252  26.785  1.00 5.26  ? 31  VAL A C   1 
ATOM   229  O  O   . VAL A 1 31  ? 14.737 -6.333  26.042  1.00 6.35  ? 31  VAL A O   1 
ATOM   230  C  CB  . VAL A 1 31  ? 16.250 -4.192  28.120  1.00 4.72  ? 31  VAL A CB  1 
ATOM   231  C  CG1 . VAL A 1 31  ? 17.191 -2.999  28.219  1.00 6.43  ? 31  VAL A CG1 1 
ATOM   232  C  CG2 . VAL A 1 31  ? 14.784 -3.744  28.179  1.00 6.78  ? 31  VAL A CG2 1 
ATOM   233  N  N   . ASP A 1 32  ? 16.044 -7.202  27.650  1.00 5.73  ? 32  ASP A N   1 
ATOM   234  C  CA  . ASP A 1 32  ? 15.135 -8.299  27.965  1.00 6.21  ? 32  ASP A CA  1 
ATOM   235  C  C   . ASP A 1 32  ? 14.047 -7.786  28.919  1.00 6.70  ? 32  ASP A C   1 
ATOM   236  O  O   . ASP A 1 32  ? 14.359 -7.155  29.911  1.00 8.92  ? 32  ASP A O   1 
ATOM   237  C  CB  . ASP A 1 32  ? 15.864 -9.498  28.569  1.00 8.54  ? 32  ASP A CB  1 
ATOM   238  C  CG  . ASP A 1 32  ? 14.888 -10.645 28.857  1.00 9.81  ? 32  ASP A CG  1 
ATOM   239  O  OD1 . ASP A 1 32  ? 14.207 -11.113 27.918  1.00 8.98  ? 32  ASP A OD1 1 
ATOM   240  O  OD2 . ASP A 1 32  ? 14.843 -11.086 30.040  1.00 13.25 ? 32  ASP A OD2 1 
ATOM   241  N  N   . ILE A 1 33  ? 12.787 -8.094  28.601  1.00 6.79  ? 33  ILE A N   1 
ATOM   242  C  CA  . ILE A 1 33  ? 11.667 -7.747  29.461  1.00 6.55  ? 33  ILE A CA  1 
ATOM   243  C  C   . ILE A 1 33  ? 11.357 -8.986  30.285  1.00 7.58  ? 33  ILE A C   1 
ATOM   244  O  O   . ILE A 1 33  ? 10.789 -9.961  29.788  1.00 9.18  ? 33  ILE A O   1 
ATOM   245  C  CB  . ILE A 1 33  ? 10.472 -7.275  28.623  1.00 6.70  ? 33  ILE A CB  1 
ATOM   246  C  CG1 . ILE A 1 33  ? 10.850 -6.033  27.812  1.00 8.37  ? 33  ILE A CG1 1 
ATOM   247  C  CG2 . ILE A 1 33  ? 9.306  -7.010  29.573  1.00 9.34  ? 33  ILE A CG2 1 
ATOM   248  C  CD1 . ILE A 1 33  ? 9.852  -5.754  26.656  1.00 10.31 ? 33  ILE A CD1 1 
ATOM   249  N  N   . ASP A 1 34  ? 11.793 -8.932  31.541  1.00 8.55  ? 34  ASP A N   1 
ATOM   250  C  CA  . ASP A 1 34  ? 11.488 -9.995  32.499  1.00 9.44  ? 34  ASP A CA  1 
ATOM   251  C  C   . ASP A 1 34  ? 10.069 -9.754  33.038  1.00 10.57 ? 34  ASP A C   1 
ATOM   252  O  O   . ASP A 1 34  ? 9.845  -8.814  33.796  1.00 12.93 ? 34  ASP A O   1 
ATOM   253  C  CB  . ASP A 1 34  ? 12.572 -10.073 33.593  1.00 12.38 ? 34  ASP A CB  1 
ATOM   254  C  CG  . ASP A 1 34  ? 12.283 -11.012 34.788  1.00 16.80 ? 34  ASP A CG  1 
ATOM   255  O  OD1 . ASP A 1 34  ? 11.173 -11.547 34.917  1.00 18.91 ? 34  ASP A OD1 1 
ATOM   256  O  OD2 . ASP A 1 34  ? 13.146 -11.110 35.655  1.00 30.88 ? 34  ASP A OD2 1 
ATOM   257  N  N   . THR A 1 35  ? 9.099  -10.567 32.623  1.00 13.05 ? 35  THR A N   1 
ATOM   258  C  CA  . THR A 1 35  ? 7.707  -10.253 32.864  1.00 14.31 ? 35  THR A CA  1 
ATOM   259  C  C   . THR A 1 35  ? 7.381  -10.349 34.339  1.00 13.58 ? 35  THR A C   1 
ATOM   260  O  O   . THR A 1 35  ? 6.490  -9.658  34.796  1.00 18.28 ? 35  THR A O   1 
ATOM   261  C  CB  . THR A 1 35  ? 6.785  -11.095 31.984  1.00 16.30 ? 35  THR A CB  1 
ATOM   262  O  OG1 . THR A 1 35  ? 6.905  -12.445 32.420  1.00 17.63 ? 35  THR A OG1 1 
ATOM   263  C  CG2 . THR A 1 35  ? 6.976  -10.934 30.490  1.00 19.72 ? 35  THR A CG2 1 
ATOM   264  N  N   . HIS A 1 36  ? 8.170  -11.139 35.066  1.00 15.44 ? 36  HIS A N   1 
ATOM   265  C  CA  . HIS A 1 36  ? 7.963  -11.394 36.476  1.00 19.26 ? 36  HIS A CA  1 
ATOM   266  C  C   . HIS A 1 36  ? 8.591  -10.309 37.327  1.00 23.48 ? 36  HIS A C   1 
ATOM   267  O  O   . HIS A 1 36  ? 8.230  -10.206 38.495  1.00 40.34 ? 36  HIS A O   1 
ATOM   268  C  CB  . HIS A 1 36  ? 8.570  -12.750 36.851  1.00 19.52 ? 36  HIS A CB  1 
ATOM   269  C  CG  . HIS A 1 36  ? 7.833  -13.840 36.146  1.00 29.99 ? 36  HIS A CG  1 
ATOM   270  N  ND1 . HIS A 1 36  ? 8.442  -14.635 35.099  1.00 30.71 ? 36  HIS A ND1 1 
ATOM   271  C  CD2 . HIS A 1 36  ? 6.539  -14.233 36.244  1.00 28.58 ? 36  HIS A CD2 1 
ATOM   272  C  CE1 . HIS A 1 36  ? 7.552  -15.481 34.633  1.00 41.48 ? 36  HIS A CE1 1 
ATOM   273  N  NE2 . HIS A 1 36  ? 6.382  -15.255 35.297  1.00 33.59 ? 36  HIS A NE2 1 
ATOM   274  N  N   . THR A 1 37  ? 9.470  -9.480  36.762  1.00 17.65 ? 37  THR A N   1 
ATOM   275  C  CA  . THR A 1 37  ? 10.097 -8.401  37.517  1.00 18.58 ? 37  THR A CA  1 
ATOM   276  C  C   . THR A 1 37  ? 9.555  -7.036  37.093  1.00 15.78 ? 37  THR A C   1 
ATOM   277  O  O   . THR A 1 37  ? 9.676  -6.060  37.826  1.00 20.97 ? 37  THR A O   1 
ATOM   278  C  CB  . THR A 1 37  ? 11.616 -8.462  37.301  1.00 26.55 ? 37  THR A CB  1 
ATOM   279  O  OG1 . THR A 1 37  ? 11.996 -9.608  38.071  1.00 33.20 ? 37  THR A OG1 1 
ATOM   280  C  CG2 . THR A 1 37  ? 12.340 -7.233  37.822  1.00 28.14 ? 37  THR A CG2 1 
ATOM   281  N  N   . ALA A 1 38  ? 8.840  -6.941  35.975  1.00 13.28 ? 38  ALA A N   1 
ATOM   282  C  CA  . ALA A 1 38  ? 8.213  -5.672  35.583  1.00 14.10 ? 38  ALA A CA  1 
ATOM   283  C  C   . ALA A 1 38  ? 7.169  -5.329  36.626  1.00 14.90 ? 38  ALA A C   1 
ATOM   284  O  O   . ALA A 1 38  ? 6.495  -6.196  37.187  1.00 20.54 ? 38  ALA A O   1 
ATOM   285  C  CB  . ALA A 1 38  ? 7.632  -5.768  34.201  1.00 12.66 ? 38  ALA A CB  1 
ATOM   286  N  N   A LYS A 1 39  ? 6.999  -4.027  36.870  0.50 14.79 ? 39  LYS A N   1 
ATOM   287  N  N   B LYS A 1 39  ? 7.061  -4.070  36.995  0.50 15.06 ? 39  LYS A N   1 
ATOM   288  C  CA  A LYS A 1 39  ? 6.116  -3.466  37.903  0.50 15.27 ? 39  LYS A CA  1 
ATOM   289  C  CA  B LYS A 1 39  ? 5.970  -3.870  37.939  0.50 15.97 ? 39  LYS A CA  1 
ATOM   290  C  C   A LYS A 1 39  ? 4.809  -2.996  37.246  0.50 12.91 ? 39  LYS A C   1 
ATOM   291  C  C   B LYS A 1 39  ? 4.838  -3.086  37.307  0.50 13.34 ? 39  LYS A C   1 
ATOM   292  O  O   A LYS A 1 39  ? 4.838  -2.091  36.404  0.50 12.87 ? 39  LYS A O   1 
ATOM   293  O  O   B LYS A 1 39  ? 5.027  -2.063  36.638  0.50 14.47 ? 39  LYS A O   1 
ATOM   294  C  CB  A LYS A 1 39  ? 6.896  -2.297  38.530  0.50 13.09 ? 39  LYS A CB  1 
ATOM   295  C  CB  B LYS A 1 39  ? 6.386  -3.224  39.250  0.50 16.44 ? 39  LYS A CB  1 
ATOM   296  C  CG  A LYS A 1 39  ? 6.300  -1.503  39.695  0.50 16.36 ? 39  LYS A CG  1 
ATOM   297  C  CG  B LYS A 1 39  ? 5.240  -3.117  40.271  0.50 18.15 ? 39  LYS A CG  1 
ATOM   298  C  CD  A LYS A 1 39  ? 6.173  -2.226  41.012  0.50 17.90 ? 39  LYS A CD  1 
ATOM   299  C  CD  B LYS A 1 39  ? 5.704  -2.337  41.450  0.50 20.44 ? 39  LYS A CD  1 
ATOM   300  C  CE  A LYS A 1 39  ? 5.441  -1.388  42.040  0.50 20.24 ? 39  LYS A CE  1 
ATOM   301  C  CE  B LYS A 1 39  ? 4.540  -2.052  42.372  0.50 23.09 ? 39  LYS A CE  1 
ATOM   302  N  NZ  A LYS A 1 39  ? 4.825  -2.283  43.050  0.50 23.31 ? 39  LYS A NZ  1 
ATOM   303  N  NZ  B LYS A 1 39  ? 5.038  -1.434  43.625  0.50 25.10 ? 39  LYS A NZ  1 
ATOM   304  N  N   . TYR A 1 40  ? 3.652  -3.569  37.620  1.00 15.71 ? 40  TYR A N   1 
ATOM   305  C  CA  . TYR A 1 40  ? 2.419  -2.942  37.180  1.00 15.14 ? 40  TYR A CA  1 
ATOM   306  C  C   . TYR A 1 40  ? 2.350  -1.571  37.851  1.00 14.88 ? 40  TYR A C   1 
ATOM   307  O  O   . TYR A 1 40  ? 2.497  -1.461  39.093  1.00 18.42 ? 40  TYR A O   1 
ATOM   308  C  CB  . TYR A 1 40  ? 1.213  -3.788  37.595  1.00 16.47 ? 40  TYR A CB  1 
ATOM   309  C  CG  . TYR A 1 40  ? -0.090 -3.062  37.462  1.00 18.90 ? 40  TYR A CG  1 
ATOM   310  C  CD1 . TYR A 1 40  ? -0.557 -2.600  36.236  1.00 19.22 ? 40  TYR A CD1 1 
ATOM   311  C  CD2 . TYR A 1 40  ? -0.903 -2.891  38.583  1.00 26.93 ? 40  TYR A CD2 1 
ATOM   312  C  CE1 . TYR A 1 40  ? -1.792 -1.974  36.142  1.00 26.03 ? 40  TYR A CE1 1 
ATOM   313  C  CE2 . TYR A 1 40  ? -2.148 -2.254  38.503  1.00 28.51 ? 40  TYR A CE2 1 
ATOM   314  C  CZ  . TYR A 1 40  ? -2.587 -1.787  37.272  1.00 35.76 ? 40  TYR A CZ  1 
ATOM   315  O  OH  . TYR A 1 40  ? -3.761 -1.121  37.095  1.00 41.39 ? 40  TYR A OH  1 
ATOM   316  N  N   . ASP A 1 41  ? 2.124  -0.552  37.039  1.00 13.66 ? 41  ASP A N   1 
ATOM   317  C  CA  . ASP A 1 41  ? 1.959  0.804   37.546  1.00 16.08 ? 41  ASP A CA  1 
ATOM   318  C  C   . ASP A 1 41  ? 0.528  1.247   37.281  1.00 20.65 ? 41  ASP A C   1 
ATOM   319  O  O   . ASP A 1 41  ? 0.241  1.607   36.127  1.00 20.69 ? 41  ASP A O   1 
ATOM   320  C  CB  . ASP A 1 41  ? 2.930  1.751   36.822  1.00 19.56 ? 41  ASP A CB  1 
ATOM   321  C  CG  . ASP A 1 41  ? 2.943  3.154   37.408  1.00 28.17 ? 41  ASP A CG  1 
ATOM   322  O  OD1 . ASP A 1 41  ? 1.974  3.501   38.098  1.00 31.07 ? 41  ASP A OD1 1 
ATOM   323  O  OD2 . ASP A 1 41  ? 3.919  3.886   37.162  1.00 36.42 ? 41  ASP A OD2 1 
ATOM   324  N  N   . PRO A 1 42  ? -0.379 1.280   38.318  1.00 29.35 ? 42  PRO A N   1 
ATOM   325  C  CA  . PRO A 1 42  ? -1.789 1.613   38.082  1.00 36.63 ? 42  PRO A CA  1 
ATOM   326  C  C   . PRO A 1 42  ? -1.930 3.044   37.586  1.00 35.83 ? 42  PRO A C   1 
ATOM   327  O  O   . PRO A 1 42  ? -3.023 3.393   37.026  1.00 35.90 ? 42  PRO A O   1 
ATOM   328  C  CB  . PRO A 1 42  ? -2.423 1.423   39.475  1.00 54.16 ? 42  PRO A CB  1 
ATOM   329  C  CG  . PRO A 1 42  ? -1.276 1.723   40.419  1.00 54.72 ? 42  PRO A CG  1 
ATOM   330  C  CD  . PRO A 1 42  ? -0.135 0.948   39.747  1.00 40.39 ? 42  PRO A CD  1 
ATOM   331  N  N   . SER A 1 43  ? -0.855 3.873   37.827  1.00 28.11 ? 43  SER A N   1 
ATOM   332  C  CA  . SER A 1 43  ? -0.989 5.284   37.408  1.00 32.89 ? 43  SER A CA  1 
ATOM   333  C  C   . SER A 1 43  ? -0.634 5.509   35.921  1.00 34.47 ? 43  SER A C   1 
ATOM   334  O  O   . SER A 1 43  ? -0.824 6.610   35.394  1.00 35.03 ? 43  SER A O   1 
ATOM   335  C  CB  . SER A 1 43  ? -0.218 6.194   38.328  1.00 42.99 ? 43  SER A CB  1 
ATOM   336  O  OG  . SER A 1 43  ? 1.178  6.078   38.089  1.00 43.90 ? 43  SER A OG  1 
ATOM   337  N  N   . LEU A 1 44  ? -0.131 4.474   35.216  1.00 25.35 ? 44  LEU A N   1 
ATOM   338  C  CA  . LEU A 1 44  ? 0.110  4.609   33.773  1.00 19.28 ? 44  LEU A CA  1 
ATOM   339  C  C   . LEU A 1 44  ? -1.219 4.735   33.046  1.00 18.68 ? 44  LEU A C   1 
ATOM   340  O  O   . LEU A 1 44  ? -2.177 4.039   33.349  1.00 25.22 ? 44  LEU A O   1 
ATOM   341  C  CB  . LEU A 1 44  ? 0.835  3.376   33.254  1.00 16.14 ? 44  LEU A CB  1 
ATOM   342  C  CG  . LEU A 1 44  ? 2.327  3.373   33.469  1.00 13.33 ? 44  LEU A CG  1 
ATOM   343  C  CD1 . LEU A 1 44  ? 2.806  2.010   33.013  1.00 13.21 ? 44  LEU A CD1 1 
ATOM   344  C  CD2 . LEU A 1 44  ? 3.056  4.494   32.737  1.00 15.10 ? 44  LEU A CD2 1 
ATOM   345  N  N   . LYS A 1 45  ? -1.250 5.655   32.102  1.00 19.79 ? 45  LYS A N   1 
ATOM   346  C  CA  . LYS A 1 45  ? -2.458 5.903   31.338  1.00 18.01 ? 45  LYS A CA  1 
ATOM   347  C  C   . LYS A 1 45  ? -2.521 5.002   30.110  1.00 16.50 ? 45  LYS A C   1 
ATOM   348  O  O   . LYS A 1 45  ? -1.517 4.475   29.686  1.00 14.81 ? 45  LYS A O   1 
ATOM   349  C  CB  . LYS A 1 45  ? -2.443 7.339   30.872  1.00 17.77 ? 45  LYS A CB  1 
ATOM   350  C  CG  . LYS A 1 45  ? -2.451 8.405   31.951  1.00 24.05 ? 45  LYS A CG  1 
ATOM   351  C  CD  . LYS A 1 45  ? -2.611 9.723   31.219  1.00 37.31 ? 45  LYS A CD  1 
ATOM   352  C  CE  . LYS A 1 45  ? -3.292 10.797  32.041  1.00 52.29 ? 45  LYS A CE  1 
ATOM   353  N  NZ  . LYS A 1 45  ? -2.656 10.912  33.372  1.00 60.13 ? 45  LYS A NZ  1 
ATOM   354  N  N   . PRO A 1 46  ? -3.719 4.785   29.510  1.00 15.00 ? 46  PRO A N   1 
ATOM   355  C  CA  . PRO A 1 46  ? -3.804 4.074   28.232  1.00 13.58 ? 46  PRO A CA  1 
ATOM   356  C  C   . PRO A 1 46  ? -3.044 4.883   27.223  1.00 13.35 ? 46  PRO A C   1 
ATOM   357  O  O   . PRO A 1 46  ? -2.948 6.094   27.337  1.00 14.47 ? 46  PRO A O   1 
ATOM   358  C  CB  . PRO A 1 46  ? -5.315 4.116   27.864  1.00 18.22 ? 46  PRO A CB  1 
ATOM   359  C  CG  . PRO A 1 46  ? -6.005 4.377   29.188  1.00 24.26 ? 46  PRO A CG  1 
ATOM   360  C  CD  . PRO A 1 46  ? -5.044 5.211   30.016  1.00 21.63 ? 46  PRO A CD  1 
ATOM   361  N  N   . LEU A 1 47  ? -2.452 4.149   26.302  1.00 11.76 ? 47  LEU A N   1 
ATOM   362  C  CA  . LEU A 1 47  ? -1.800 4.807   25.212  1.00 10.93 ? 47  LEU A CA  1 
ATOM   363  C  C   . LEU A 1 47  ? -2.835 5.406   24.284  1.00 12.43 ? 47  LEU A C   1 
ATOM   364  O  O   . LEU A 1 47  ? -3.881 4.788   24.102  1.00 16.77 ? 47  LEU A O   1 
ATOM   365  C  CB  . LEU A 1 47  ? -1.031 3.703   24.477  1.00 16.18 ? 47  LEU A CB  1 
ATOM   366  C  CG  . LEU A 1 47  ? 0.138  4.058   23.612  1.00 22.18 ? 47  LEU A CG  1 
ATOM   367  C  CD1 . LEU A 1 47  ? 1.180  4.823   24.447  1.00 24.61 ? 47  LEU A CD1 1 
ATOM   368  C  CD2 . LEU A 1 47  ? 0.702  2.742   23.087  1.00 21.50 ? 47  LEU A CD2 1 
ATOM   369  N  N   . SER A 1 48  ? -2.547 6.574   23.740  1.00 10.05 ? 48  SER A N   1 
ATOM   370  C  CA  . SER A 1 48  ? -3.400 7.217   22.759  1.00 9.13  ? 48  SER A CA  1 
ATOM   371  C  C   . SER A 1 48  ? -2.634 7.209   21.439  1.00 10.04 ? 48  SER A C   1 
ATOM   372  O  O   . SER A 1 48  ? -1.633 7.922   21.259  1.00 10.96 ? 48  SER A O   1 
ATOM   373  C  CB  . SER A 1 48  ? -3.710 8.651   23.155  1.00 13.67 ? 48  SER A CB  1 
ATOM   374  O  OG  . SER A 1 48  ? -4.400 9.312   22.108  1.00 18.28 ? 48  SER A OG  1 
ATOM   375  N  N   . VAL A 1 49  ? -3.080 6.388   20.522  1.00 12.10 ? 49  VAL A N   1 
ATOM   376  C  CA  . VAL A 1 49  ? -2.494 6.317   19.204  1.00 13.68 ? 49  VAL A CA  1 
ATOM   377  C  C   . VAL A 1 49  ? -3.459 6.964   18.215  1.00 15.99 ? 49  VAL A C   1 
ATOM   378  O  O   . VAL A 1 49  ? -4.581 6.468   17.995  1.00 20.35 ? 49  VAL A O   1 
ATOM   379  C  CB  . VAL A 1 49  ? -2.240 4.852   18.816  1.00 14.74 ? 49  VAL A CB  1 
ATOM   380  C  CG1 . VAL A 1 49  ? -1.564 4.759   17.449  1.00 21.34 ? 49  VAL A CG1 1 
ATOM   381  C  CG2 . VAL A 1 49  ? -1.392 4.147   19.879  1.00 16.33 ? 49  VAL A CG2 1 
ATOM   382  N  N   . SER A 1 50  ? -3.067 8.099   17.654  1.00 13.64 ? 50  SER A N   1 
ATOM   383  C  CA  . SER A 1 50  ? -3.997 8.854   16.836  1.00 14.37 ? 50  SER A CA  1 
ATOM   384  C  C   . SER A 1 50  ? -3.386 8.926   15.448  1.00 13.66 ? 50  SER A C   1 
ATOM   385  O  O   . SER A 1 50  ? -2.672 9.855   15.175  1.00 14.11 ? 50  SER A O   1 
ATOM   386  C  CB  . SER A 1 50  ? -4.263 10.255  17.377  1.00 21.41 ? 50  SER A CB  1 
ATOM   387  O  OG  . SER A 1 50  ? -4.952 10.123  18.601  1.00 25.81 ? 50  SER A OG  1 
ATOM   388  N  N   . TYR A 1 51  ? -3.667 7.942   14.614  1.00 12.09 ? 51  TYR A N   1 
ATOM   389  C  CA  . TYR A 1 51  ? -3.077 7.778   13.313  1.00 12.30 ? 51  TYR A CA  1 
ATOM   390  C  C   . TYR A 1 51  ? -4.056 8.023   12.178  1.00 15.31 ? 51  TYR A C   1 
ATOM   391  O  O   . TYR A 1 51  ? -3.690 7.829   11.017  1.00 16.10 ? 51  TYR A O   1 
ATOM   392  C  CB  . TYR A 1 51  ? -2.426 6.406   13.202  1.00 14.29 ? 51  TYR A CB  1 
ATOM   393  C  CG  . TYR A 1 51  ? -1.144 6.126   13.974  1.00 10.49 ? 51  TYR A CG  1 
ATOM   394  C  CD1 . TYR A 1 51  ? -0.481 7.137   14.649  1.00 11.64 ? 51  TYR A CD1 1 
ATOM   395  C  CD2 . TYR A 1 51  ? -0.603 4.852   14.025  1.00 9.60  ? 51  TYR A CD2 1 
ATOM   396  C  CE1 . TYR A 1 51  ? 0.686  6.891   15.353  1.00 9.28  ? 51  TYR A CE1 1 
ATOM   397  C  CE2 . TYR A 1 51  ? 0.561  4.588   14.725  1.00 8.99  ? 51  TYR A CE2 1 
ATOM   398  C  CZ  . TYR A 1 51  ? 1.209  5.612   15.392  1.00 8.42  ? 51  TYR A CZ  1 
ATOM   399  O  OH  . TYR A 1 51  ? 2.359  5.361   16.084  1.00 10.12 ? 51  TYR A OH  1 
ATOM   400  N  N   . ASP A 1 52  ? -5.292 8.489   12.476  1.00 21.93 ? 52  ASP A N   1 
ATOM   401  C  CA  . ASP A 1 52  ? -6.309 8.676   11.441  1.00 19.97 ? 52  ASP A CA  1 
ATOM   402  C  C   . ASP A 1 52  ? -5.871 9.621   10.315  1.00 17.28 ? 52  ASP A C   1 
ATOM   403  O  O   . ASP A 1 52  ? -6.307 9.435   9.181   1.00 23.84 ? 52  ASP A O   1 
ATOM   404  C  CB  . ASP A 1 52  ? -7.668 9.015   12.072  1.00 24.63 ? 52  ASP A CB  1 
ATOM   405  C  CG  . ASP A 1 52  ? -7.569 10.078  13.149  1.00 34.72 ? 52  ASP A CG  1 
ATOM   406  O  OD1 . ASP A 1 52  ? -6.857 9.822   14.211  1.00 45.32 ? 52  ASP A OD1 1 
ATOM   407  O  OD2 . ASP A 1 52  ? -8.204 11.155  12.934  1.00 55.77 ? 52  ASP A OD2 1 
ATOM   408  N  N   . GLN A 1 53  ? -5.075 10.646  10.623  1.00 19.47 ? 53  GLN A N   1 
ATOM   409  C  CA  . GLN A 1 53  ? -4.700 11.636  9.613   1.00 25.93 ? 53  GLN A CA  1 
ATOM   410  C  C   . GLN A 1 53  ? -3.303 11.383  9.039   1.00 18.49 ? 53  GLN A C   1 
ATOM   411  O  O   . GLN A 1 53  ? -2.688 12.267  8.440   1.00 18.97 ? 53  GLN A O   1 
ATOM   412  C  CB  . GLN A 1 53  ? -4.778 13.039  10.224  1.00 29.37 ? 53  GLN A CB  1 
ATOM   413  C  CG  . GLN A 1 53  ? -6.218 13.477  10.480  1.00 39.98 ? 53  GLN A CG  1 
ATOM   414  C  CD  . GLN A 1 53  ? -6.886 13.590  9.129   1.00 47.35 ? 53  GLN A CD  1 
ATOM   415  O  OE1 . GLN A 1 53  ? -6.551 14.459  8.308   1.00 45.75 ? 53  GLN A OE1 1 
ATOM   416  N  NE2 . GLN A 1 53  ? -7.779 12.645  8.859   1.00 45.98 ? 53  GLN A NE2 1 
ATOM   417  N  N   . ALA A 1 54  ? -2.748 10.187  9.257   1.00 13.56 ? 54  ALA A N   1 
ATOM   418  C  CA  . ALA A 1 54  ? -1.362 9.946   8.885   1.00 11.58 ? 54  ALA A CA  1 
ATOM   419  C  C   . ALA A 1 54  ? -1.155 10.101  7.386   1.00 13.21 ? 54  ALA A C   1 
ATOM   420  O  O   . ALA A 1 54  ? -1.971 9.660   6.562   1.00 17.15 ? 54  ALA A O   1 
ATOM   421  C  CB  . ALA A 1 54  ? -0.902 8.582   9.323   1.00 13.91 ? 54  ALA A CB  1 
ATOM   422  N  N   . THR A 1 55  ? -0.062 10.776  7.045   1.00 10.71 ? 55  THR A N   1 
ATOM   423  C  CA  . THR A 1 55  ? 0.358  10.967  5.653   1.00 11.06 ? 55  THR A CA  1 
ATOM   424  C  C   . THR A 1 55  ? 1.686  10.282  5.399   1.00 8.99  ? 55  THR A C   1 
ATOM   425  O  O   . THR A 1 55  ? 2.713  10.884  5.636   1.00 10.72 ? 55  THR A O   1 
ATOM   426  C  CB  . THR A 1 55  ? 0.474  12.456  5.291   1.00 14.91 ? 55  THR A CB  1 
ATOM   427  O  OG1 . THR A 1 55  ? -0.821 13.034  5.459   1.00 21.44 ? 55  THR A OG1 1 
ATOM   428  C  CG2 . THR A 1 55  ? 0.863  12.625  3.836   1.00 18.73 ? 55  THR A CG2 1 
ATOM   429  N  N   . SER A 1 56  ? 1.646  9.058   4.903   1.00 9.86  ? 56  SER A N   1 
ATOM   430  C  CA  . SER A 1 56  ? 2.877  8.415   4.500   1.00 9.85  ? 56  SER A CA  1 
ATOM   431  C  C   . SER A 1 56  ? 3.373  9.036   3.198   1.00 11.75 ? 56  SER A C   1 
ATOM   432  O  O   . SER A 1 56  ? 2.593  9.514   2.364   1.00 12.19 ? 56  SER A O   1 
ATOM   433  C  CB  . SER A 1 56  ? 2.735  6.921   4.341   1.00 11.38 ? 56  SER A CB  1 
ATOM   434  O  OG  . SER A 1 56  ? 1.894  6.582   3.234   1.00 12.24 ? 56  SER A OG  1 
ATOM   435  N  N   . LEU A 1 57  ? 4.688  9.050   3.014   1.00 9.82  ? 57  LEU A N   1 
ATOM   436  C  CA  . LEU A 1 57  ? 5.237  9.678   1.806   1.00 11.01 ? 57  LEU A CA  1 
ATOM   437  C  C   . LEU A 1 57  ? 6.079  8.737   0.958   1.00 10.89 ? 57  LEU A C   1 
ATOM   438  O  O   . LEU A 1 57  ? 5.988  8.750   -0.275  1.00 11.43 ? 57  LEU A O   1 
ATOM   439  C  CB  . LEU A 1 57  ? 6.079  10.883  2.233   1.00 13.34 ? 57  LEU A CB  1 
ATOM   440  C  CG  . LEU A 1 57  ? 5.299  12.065  2.855   1.00 16.36 ? 57  LEU A CG  1 
ATOM   441  C  CD1 . LEU A 1 57  ? 6.294  13.133  3.304   1.00 23.68 ? 57  LEU A CD1 1 
ATOM   442  C  CD2 . LEU A 1 57  ? 4.283  12.671  1.861   1.00 21.48 ? 57  LEU A CD2 1 
ATOM   443  N  N   . ARG A 1 58  ? 6.952  7.962   1.585   1.00 9.61  ? 58  ARG A N   1 
ATOM   444  C  CA  . ARG A 1 58  ? 8.044  7.321   0.863   1.00 9.21  ? 58  ARG A CA  1 
ATOM   445  C  C   . ARG A 1 58  ? 8.499  6.128   1.670   1.00 8.68  ? 58  ARG A C   1 
ATOM   446  O  O   . ARG A 1 58  ? 8.381  6.120   2.877   1.00 9.58  ? 58  ARG A O   1 
ATOM   447  C  CB  . ARG A 1 58  ? 9.216  8.294   0.714   1.00 11.97 ? 58  ARG A CB  1 
ATOM   448  C  CG  . ARG A 1 58  ? 10.256 7.867   -0.302  1.00 15.95 ? 58  ARG A CG  1 
ATOM   449  C  CD  . ARG A 1 58  ? 11.236 9.022   -0.466  1.00 17.38 ? 58  ARG A CD  1 
ATOM   450  N  NE  . ARG A 1 58  ? 12.035 9.078   0.740   1.00 15.94 ? 58  ARG A NE  1 
ATOM   451  C  CZ  . ARG A 1 58  ? 13.342 9.281   0.757   1.00 13.65 ? 58  ARG A CZ  1 
ATOM   452  N  NH1 . ARG A 1 58  ? 13.991 9.584   -0.356  1.00 16.73 ? 58  ARG A NH1 1 
ATOM   453  N  NH2 . ARG A 1 58  ? 13.980 9.214   1.901   1.00 15.47 ? 58  ARG A NH2 1 
ATOM   454  N  N   . ILE A 1 59  ? 9.066  5.141   0.980   1.00 7.55  ? 59  ILE A N   1 
ATOM   455  C  CA  . ILE A 1 59  ? 9.728  4.005   1.585   1.00 7.14  ? 59  ILE A CA  1 
ATOM   456  C  C   . ILE A 1 59  ? 11.166 3.991   1.064   1.00 7.23  ? 59  ILE A C   1 
ATOM   457  O  O   . ILE A 1 59  ? 11.431 4.235   -0.145  1.00 9.33  ? 59  ILE A O   1 
ATOM   458  C  CB  . ILE A 1 59  ? 8.963  2.693   1.332   1.00 6.84  ? 59  ILE A CB  1 
ATOM   459  C  CG1 . ILE A 1 59  ? 9.510  1.541   2.184   1.00 8.04  ? 59  ILE A CG1 1 
ATOM   460  C  CG2 . ILE A 1 59  ? 8.906  2.353   -0.147  1.00 10.73 ? 59  ILE A CG2 1 
ATOM   461  C  CD1 . ILE A 1 59  ? 8.627  0.293   2.154   1.00 9.73  ? 59  ILE A CD1 1 
ATOM   462  N  N   . LEU A 1 60  ? 12.117 3.699   1.950   1.00 7.11  ? 60  LEU A N   1 
ATOM   463  C  CA  . LEU A 1 60  ? 13.549 3.835   1.650   1.00 6.42  ? 60  LEU A CA  1 
ATOM   464  C  C   . LEU A 1 60  ? 14.324 2.656   2.235   1.00 6.80  ? 60  LEU A C   1 
ATOM   465  O  O   . LEU A 1 60  ? 14.133 2.344   3.398   1.00 7.66  ? 60  LEU A O   1 
ATOM   466  C  CB  . LEU A 1 60  ? 14.099 5.166   2.259   1.00 9.02  ? 60  LEU A CB  1 
ATOM   467  C  CG  . LEU A 1 60  ? 15.632 5.324   2.256   1.00 9.85  ? 60  LEU A CG  1 
ATOM   468  C  CD1 . LEU A 1 60  ? 16.138 5.582   0.825   1.00 11.77 ? 60  LEU A CD1 1 
ATOM   469  C  CD2 . LEU A 1 60  ? 16.055 6.465   3.222   1.00 11.50 ? 60  LEU A CD2 1 
ATOM   470  N  N   . ASN A 1 61  ? 15.215 2.051   1.428   1.00 7.24  ? 61  ASN A N   1 
ATOM   471  C  CA  . ASN A 1 61  ? 16.183 1.102   1.951   1.00 6.23  ? 61  ASN A CA  1 
ATOM   472  C  C   . ASN A 1 61  ? 17.396 1.934   2.399   1.00 7.02  ? 61  ASN A C   1 
ATOM   473  O  O   . ASN A 1 61  ? 18.056 2.537   1.528   1.00 7.68  ? 61  ASN A O   1 
ATOM   474  C  CB  . ASN A 1 61  ? 16.564 0.093   0.861   1.00 7.49  ? 61  ASN A CB  1 
ATOM   475  C  CG  . ASN A 1 61  ? 17.628 -0.889  1.311   1.00 6.54  ? 61  ASN A CG  1 
ATOM   476  O  OD1 . ASN A 1 61  ? 18.452 -0.557  2.210   1.00 8.19  ? 61  ASN A OD1 1 
ATOM   477  N  ND2 . ASN A 1 61  ? 17.625 -2.086  0.727   1.00 7.32  ? 61  ASN A ND2 1 
ATOM   478  N  N   . ASN A 1 62  ? 17.691 2.028   3.698   1.00 6.83  ? 62  ASN A N   1 
ATOM   479  C  CA  . ASN A 1 62  ? 18.738 2.943   4.169   1.00 7.03  ? 62  ASN A CA  1 
ATOM   480  C  C   . ASN A 1 62  ? 20.054 2.175   4.366   1.00 8.53  ? 62  ASN A C   1 
ATOM   481  O  O   . ASN A 1 62  ? 21.049 2.771   4.849   1.00 11.32 ? 62  ASN A O   1 
ATOM   482  C  CB  . ASN A 1 62  ? 18.307 3.689   5.436   1.00 8.78  ? 62  ASN A CB  1 
ATOM   483  C  CG  . ASN A 1 62  ? 17.982 2.747   6.570   1.00 7.90  ? 62  ASN A CG  1 
ATOM   484  O  OD1 . ASN A 1 62  ? 18.622 1.735   6.767   1.00 7.41  ? 62  ASN A OD1 1 
ATOM   485  N  ND2 . ASN A 1 62  ? 16.926 3.049   7.313   1.00 11.62 ? 62  ASN A ND2 1 
ATOM   486  N  N   . GLY A 1 63  ? 20.128 0.912   3.945   1.00 6.91  ? 63  GLY A N   1 
ATOM   487  C  CA  . GLY A 1 63  ? 21.335 0.117   4.072   1.00 7.66  ? 63  GLY A CA  1 
ATOM   488  C  C   . GLY A 1 63  ? 21.437 -0.673  5.367   1.00 6.92  ? 63  GLY A C   1 
ATOM   489  O  O   . GLY A 1 63  ? 22.339 -1.505  5.516   1.00 10.14 ? 63  GLY A O   1 
ATOM   490  N  N   . HIS A 1 64  ? 20.523 -0.428  6.302   1.00 7.49  ? 64  HIS A N   1 
ATOM   491  C  CA  . HIS A 1 64  ? 20.479 -1.101  7.593   1.00 7.75  ? 64  HIS A CA  1 
ATOM   492  C  C   . HIS A 1 64  ? 19.139 -1.801  7.771   1.00 6.62  ? 64  HIS A C   1 
ATOM   493  O  O   . HIS A 1 64  ? 19.082 -2.896  8.311   1.00 8.13  ? 64  HIS A O   1 
ATOM   494  C  CB  . HIS A 1 64  ? 20.748 -0.120  8.762   1.00 9.19  ? 64  HIS A CB  1 
ATOM   495  C  CG  . HIS A 1 64  ? 21.959 0.724   8.571   1.00 11.33 ? 64  HIS A CG  1 
ATOM   496  N  ND1 . HIS A 1 64  ? 23.250 0.149   8.602   1.00 13.10 ? 64  HIS A ND1 1 
ATOM   497  C  CD2 . HIS A 1 64  ? 22.102 2.020   8.259   1.00 11.55 ? 64  HIS A CD2 1 
ATOM   498  C  CE1 . HIS A 1 64  ? 24.161 1.092   8.418   1.00 15.65 ? 64  HIS A CE1 1 
ATOM   499  N  NE2 . HIS A 1 64  ? 23.480 2.254   8.202   1.00 16.11 ? 64  HIS A NE2 1 
ATOM   500  N  N   . THR A 1 65  ? 18.085 -1.079  7.401   1.00 6.54  ? 65  THR A N   1 
ATOM   501  C  CA  . THR A 1 65  ? 16.712 -1.570  7.423   1.00 6.88  ? 65  THR A CA  1 
ATOM   502  C  C   . THR A 1 65  ? 15.997 -0.804  6.295   1.00 5.87  ? 65  THR A C   1 
ATOM   503  O  O   . THR A 1 65  ? 16.614 -0.152  5.465   1.00 6.97  ? 65  THR A O   1 
ATOM   504  C  CB  . THR A 1 65  ? 16.094 -1.392  8.814   1.00 6.27  ? 65  THR A CB  1 
ATOM   505  O  OG1 . THR A 1 65  ? 14.806 -1.959  8.765   1.00 8.93  ? 65  THR A OG1 1 
ATOM   506  C  CG2 . THR A 1 65  ? 16.011 0.062   9.208   1.00 7.55  ? 65  THR A CG2 1 
ATOM   507  N  N   . PHE A 1 66  ? 14.684 -0.993  6.189   1.00 6.30  ? 66  PHE A N   1 
ATOM   508  C  CA  . PHE A 1 66  ? 13.868 -0.112  5.378   1.00 6.30  ? 66  PHE A CA  1 
ATOM   509  C  C   . PHE A 1 66  ? 12.964 0.694   6.304   1.00 5.16  ? 66  PHE A C   1 
ATOM   510  O  O   . PHE A 1 66  ? 12.587 0.271   7.395   1.00 6.54  ? 66  PHE A O   1 
ATOM   511  C  CB  . PHE A 1 66  ? 13.094 -0.862  4.288   1.00 7.37  ? 66  PHE A CB  1 
ATOM   512  C  CG  . PHE A 1 66  ? 11.982 -1.704  4.828   1.00 7.09  ? 66  PHE A CG  1 
ATOM   513  C  CD1 . PHE A 1 66  ? 10.708 -1.169  4.943   1.00 8.45  ? 66  PHE A CD1 1 
ATOM   514  C  CD2 . PHE A 1 66  ? 12.205 -3.048  5.168   1.00 8.72  ? 66  PHE A CD2 1 
ATOM   515  C  CE1 . PHE A 1 66  ? 9.684  -1.975  5.420   1.00 9.59  ? 66  PHE A CE1 1 
ATOM   516  C  CE2 . PHE A 1 66  ? 11.157 -3.831  5.647   1.00 8.46  ? 66  PHE A CE2 1 
ATOM   517  C  CZ  . PHE A 1 66  ? 9.881  -3.293  5.749   1.00 9.02  ? 66  PHE A CZ  1 
ATOM   518  N  N   . GLN A 1 67  ? 12.611 1.886   5.830   1.00 6.87  ? 67  GLN A N   1 
ATOM   519  C  CA  . GLN A 1 67  ? 11.807 2.787   6.626   1.00 6.76  ? 67  GLN A CA  1 
ATOM   520  C  C   . GLN A 1 67  ? 10.700 3.398   5.770   1.00 5.65  ? 67  GLN A C   1 
ATOM   521  O  O   . GLN A 1 67  ? 10.912 3.754   4.605   1.00 7.51  ? 67  GLN A O   1 
ATOM   522  C  CB  . GLN A 1 67  ? 12.717 3.903   7.195   1.00 8.24  ? 67  GLN A CB  1 
ATOM   523  C  CG  . GLN A 1 67  ? 13.419 4.776   6.137   1.00 9.39  ? 67  GLN A CG  1 
ATOM   524  C  CD  . GLN A 1 67  ? 14.278 5.839   6.761   1.00 9.77  ? 67  GLN A CD  1 
ATOM   525  O  OE1 . GLN A 1 67  ? 14.110 7.055   6.553   1.00 17.91 ? 67  GLN A OE1 1 
ATOM   526  N  NE2 . GLN A 1 67  ? 15.272 5.372   7.467   1.00 9.91  ? 67  GLN A NE2 1 
ATOM   527  N  N   . VAL A 1 68  ? 9.516  3.508   6.383   1.00 6.27  ? 68  VAL A N   1 
ATOM   528  C  CA  . VAL A 1 68  ? 8.407  4.249   5.770   1.00 6.97  ? 68  VAL A CA  1 
ATOM   529  C  C   . VAL A 1 68  ? 8.327  5.589   6.484   1.00 7.61  ? 68  VAL A C   1 
ATOM   530  O  O   . VAL A 1 68  ? 8.206  5.625   7.720   1.00 7.26  ? 68  VAL A O   1 
ATOM   531  C  CB  . VAL A 1 68  ? 7.100  3.441   5.890   1.00 8.64  ? 68  VAL A CB  1 
ATOM   532  C  CG1 . VAL A 1 68  ? 5.900  4.303   5.452   1.00 9.11  ? 68  VAL A CG1 1 
ATOM   533  C  CG2 . VAL A 1 68  ? 7.190  2.168   5.080   1.00 9.02  ? 68  VAL A CG2 1 
ATOM   534  N  N   . GLU A 1 69  ? 8.340  6.662   5.686   1.00 8.41  ? 69  GLU A N   1 
ATOM   535  C  CA  . GLU A 1 69  ? 8.435  7.995   6.269   1.00 8.01  ? 69  GLU A CA  1 
ATOM   536  C  C   . GLU A 1 69  ? 7.069  8.683   6.140   1.00 8.67  ? 69  GLU A C   1 
ATOM   537  O  O   . GLU A 1 69  ? 6.319  8.437   5.158   1.00 10.53 ? 69  GLU A O   1 
ATOM   538  C  CB  . GLU A 1 69  ? 9.420  8.842   5.461   1.00 11.04 ? 69  GLU A CB  1 
ATOM   539  C  CG  . GLU A 1 69  ? 10.773 8.173   5.447   1.00 13.30 ? 69  GLU A CG  1 
ATOM   540  C  CD  . GLU A 1 69  ? 11.669 8.662   4.338   1.00 14.48 ? 69  GLU A CD  1 
ATOM   541  O  OE1 . GLU A 1 69  ? 11.129 9.314   3.386   1.00 16.77 ? 69  GLU A OE1 1 
ATOM   542  O  OE2 . GLU A 1 69  ? 12.856 8.356   4.386   1.00 16.07 ? 69  GLU A OE2 1 
ATOM   543  N  N   . PHE A 1 70  ? 6.826  9.612   7.079   1.00 7.33  ? 70  PHE A N   1 
ATOM   544  C  CA  . PHE A 1 70  ? 5.563  10.341  7.161   1.00 6.82  ? 70  PHE A CA  1 
ATOM   545  C  C   . PHE A 1 70  ? 5.818  11.843  7.131   1.00 8.59  ? 70  PHE A C   1 
ATOM   546  O  O   . PHE A 1 70  ? 6.877  12.337  7.520   1.00 11.46 ? 70  PHE A O   1 
ATOM   547  C  CB  . PHE A 1 70  ? 4.861  9.962   8.470   1.00 7.30  ? 70  PHE A CB  1 
ATOM   548  C  CG  . PHE A 1 70  ? 4.316  8.553   8.403   1.00 7.25  ? 70  PHE A CG  1 
ATOM   549  C  CD1 . PHE A 1 70  ? 5.171  7.478   8.625   1.00 7.86  ? 70  PHE A CD1 1 
ATOM   550  C  CD2 . PHE A 1 70  ? 2.995  8.305   8.112   1.00 7.67  ? 70  PHE A CD2 1 
ATOM   551  C  CE1 . PHE A 1 70  ? 4.719  6.164   8.534   1.00 9.19  ? 70  PHE A CE1 1 
ATOM   552  C  CE2 . PHE A 1 70  ? 2.508  7.000   8.026   1.00 9.27  ? 70  PHE A CE2 1 
ATOM   553  C  CZ  . PHE A 1 70  ? 3.406  5.924   8.204   1.00 8.39  ? 70  PHE A CZ  1 
ATOM   554  N  N   . ASP A 1 71  ? 4.805  12.592  6.711   1.00 10.90 ? 71  ASP A N   1 
ATOM   555  C  CA  . ASP A 1 71  ? 4.818  14.038  6.892   1.00 11.45 ? 71  ASP A CA  1 
ATOM   556  C  C   . ASP A 1 71  ? 4.634  14.383  8.381   1.00 10.14 ? 71  ASP A C   1 
ATOM   557  O  O   . ASP A 1 71  ? 3.589  14.146  8.969   1.00 14.83 ? 71  ASP A O   1 
ATOM   558  C  CB  . ASP A 1 71  ? 3.653  14.668  6.112   1.00 14.49 ? 71  ASP A CB  1 
ATOM   559  C  CG  . ASP A 1 71  ? 3.459  16.163  6.359   1.00 17.30 ? 71  ASP A CG  1 
ATOM   560  O  OD1 . ASP A 1 71  ? 4.379  16.811  6.935   1.00 17.53 ? 71  ASP A OD1 1 
ATOM   561  O  OD2 . ASP A 1 71  ? 2.430  16.715  5.906   1.00 27.27 ? 71  ASP A OD2 1 
ATOM   562  N  N   . ASP A 1 72  ? 5.641  14.980  9.023   1.00 11.34 ? 72  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 72  ? 5.584  15.298  10.446  1.00 11.75 ? 72  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 72  ? 5.598  16.827  10.642  1.00 14.09 ? 72  ASP A C   1 
ATOM   565  O  O   . ASP A 1 72  ? 6.032  17.325  11.700  1.00 15.82 ? 72  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 72  ? 6.797  14.674  11.158  1.00 13.55 ? 72  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 72  ? 8.145  15.290  10.738  1.00 14.72 ? 72  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 72  ? 8.243  15.910  9.624   1.00 16.57 ? 72  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 72  ? 9.113  15.157  11.509  1.00 14.95 ? 72  ASP A OD2 1 
ATOM   570  N  N   . SER A 1 73  ? 5.097  17.577  9.651   1.00 15.66 ? 73  SER A N   1 
ATOM   571  C  CA  . SER A 1 73  ? 5.144  19.036  9.737   1.00 15.14 ? 73  SER A CA  1 
ATOM   572  C  C   . SER A 1 73  ? 3.834  19.618  10.326  1.00 16.59 ? 73  SER A C   1 
ATOM   573  O  O   . SER A 1 73  ? 3.691  20.851  10.443  1.00 19.28 ? 73  SER A O   1 
ATOM   574  C  CB  . SER A 1 73  ? 5.448  19.649  8.362   1.00 18.77 ? 73  SER A CB  1 
ATOM   575  O  OG  . SER A 1 73  ? 4.336  19.461  7.479   1.00 17.42 ? 73  SER A OG  1 
ATOM   576  N  N   . GLN A 1 74  ? 2.942  18.729  10.733  1.00 16.33 ? 74  GLN A N   1 
ATOM   577  C  CA  . GLN A 1 74  ? 1.737  19.109  11.442  1.00 16.77 ? 74  GLN A CA  1 
ATOM   578  C  C   . GLN A 1 74  ? 1.391  17.915  12.313  1.00 14.81 ? 74  GLN A C   1 
ATOM   579  O  O   . GLN A 1 74  ? 1.959  16.868  12.059  1.00 16.72 ? 74  GLN A O   1 
ATOM   580  C  CB  . GLN A 1 74  ? 0.529  19.339  10.529  1.00 21.09 ? 74  GLN A CB  1 
ATOM   581  C  CG  . GLN A 1 74  ? 0.695  20.457  9.556   1.00 22.97 ? 74  GLN A CG  1 
ATOM   582  C  CD  . GLN A 1 74  ? -0.654 20.620  8.909   1.00 22.83 ? 74  GLN A CD  1 
ATOM   583  O  OE1 . GLN A 1 74  ? -1.589 21.170  9.507   1.00 35.81 ? 74  GLN A OE1 1 
ATOM   584  N  NE2 . GLN A 1 74  ? -0.759 20.100  7.706   1.00 23.75 ? 74  GLN A NE2 1 
ATOM   585  N  N   . ASP A 1 75  ? 0.518  18.087  13.326  1.00 19.84 ? 75  ASP A N   1 
ATOM   586  C  CA  . ASP A 1 75  ? 0.097  16.986  14.184  1.00 19.80 ? 75  ASP A CA  1 
ATOM   587  C  C   . ASP A 1 75  ? -0.951 16.232  13.388  1.00 21.71 ? 75  ASP A C   1 
ATOM   588  O  O   . ASP A 1 75  ? -2.071 16.715  13.276  1.00 37.32 ? 75  ASP A O   1 
ATOM   589  C  CB  . ASP A 1 75  ? -0.582 17.469  15.478  1.00 23.89 ? 75  ASP A CB  1 
ATOM   590  C  CG  . ASP A 1 75  ? 0.379  18.084  16.502  1.00 26.73 ? 75  ASP A CG  1 
ATOM   591  O  OD1 . ASP A 1 75  ? 1.585  17.897  16.365  1.00 36.17 ? 75  ASP A OD1 1 
ATOM   592  O  OD2 . ASP A 1 75  ? -0.104 18.755  17.463  1.00 39.18 ? 75  ASP A OD2 1 
ATOM   593  N  N   . LYS A 1 76  ? -0.532 15.193  12.692  1.00 15.25 ? 76  LYS A N   1 
ATOM   594  C  CA  . LYS A 1 76  ? -1.348 14.305  11.881  1.00 17.92 ? 76  LYS A CA  1 
ATOM   595  C  C   . LYS A 1 76  ? -1.384 12.888  12.458  1.00 24.01 ? 76  LYS A C   1 
ATOM   596  O  O   . LYS A 1 76  ? -2.422 12.276  12.589  1.00 63.14 ? 76  LYS A O   1 
ATOM   597  C  CB  . LYS A 1 76  ? -0.678 14.216  10.514  1.00 19.53 ? 76  LYS A CB  1 
ATOM   598  C  CG  . LYS A 1 76  ? -0.767 15.471  9.664   1.00 23.03 ? 76  LYS A CG  1 
ATOM   599  C  CD  . LYS A 1 76  ? -0.192 15.285  8.258   1.00 21.11 ? 76  LYS A CD  1 
ATOM   600  C  CE  . LYS A 1 76  ? -0.836 16.252  7.278   1.00 24.13 ? 76  LYS A CE  1 
ATOM   601  N  NZ  . LYS A 1 76  ? -0.360 15.977  5.904   1.00 22.62 ? 76  LYS A NZ  1 
ATOM   602  N  N   . ALA A 1 77  ? -0.236 12.350  12.742  1.00 15.20 ? 77  ALA A N   1 
ATOM   603  C  CA  . ALA A 1 77  ? -0.168 11.018  13.329  1.00 13.05 ? 77  ALA A CA  1 
ATOM   604  C  C   . ALA A 1 77  ? 0.597  11.158  14.633  1.00 11.56 ? 77  ALA A C   1 
ATOM   605  O  O   . ALA A 1 77  ? 1.795  11.470  14.568  1.00 13.59 ? 77  ALA A O   1 
ATOM   606  C  CB  . ALA A 1 77  ? 0.568  10.089  12.383  1.00 16.53 ? 77  ALA A CB  1 
ATOM   607  N  N   . VAL A 1 78  ? -0.047 11.035  15.783  1.00 9.46  ? 78  VAL A N   1 
ATOM   608  C  CA  . VAL A 1 78  ? 0.635  11.337  17.032  1.00 10.04 ? 78  VAL A CA  1 
ATOM   609  C  C   . VAL A 1 78  ? 0.378  10.247  18.060  1.00 8.99  ? 78  VAL A C   1 
ATOM   610  O  O   . VAL A 1 78  ? -0.635 9.540   18.057  1.00 11.94 ? 78  VAL A O   1 
ATOM   611  C  CB  . VAL A 1 78  ? 0.242  12.700  17.628  1.00 12.37 ? 78  VAL A CB  1 
ATOM   612  C  CG1 . VAL A 1 78  ? 0.505  13.862  16.673  1.00 14.25 ? 78  VAL A CG1 1 
ATOM   613  C  CG2 . VAL A 1 78  ? -1.205 12.675  18.018  1.00 17.51 ? 78  VAL A CG2 1 
ATOM   614  N  N   . LEU A 1 79  ? 1.332  10.144  18.981  1.00 8.38  ? 79  LEU A N   1 
ATOM   615  C  CA  . LEU A 1 79  ? 1.293  9.266   20.125  1.00 8.95  ? 79  LEU A CA  1 
ATOM   616  C  C   . LEU A 1 79  ? 1.259  10.168  21.348  1.00 8.98  ? 79  LEU A C   1 
ATOM   617  O  O   . LEU A 1 79  ? 2.051  11.111  21.438  1.00 10.46 ? 79  LEU A O   1 
ATOM   618  C  CB  . LEU A 1 79  ? 2.538  8.361   20.048  1.00 11.29 ? 79  LEU A CB  1 
ATOM   619  C  CG  . LEU A 1 79  ? 2.641  7.321   21.140  1.00 12.30 ? 79  LEU A CG  1 
ATOM   620  C  CD1 . LEU A 1 79  ? 1.564  6.269   20.969  1.00 15.65 ? 79  LEU A CD1 1 
ATOM   621  C  CD2 . LEU A 1 79  ? 4.009  6.650   21.002  1.00 12.80 ? 79  LEU A CD2 1 
ATOM   622  N  N   A LYS A 1 80  ? 0.339  9.868   22.261  0.50 10.81 ? 80  LYS A N   1 
ATOM   623  N  N   B LYS A 1 80  ? 0.409  9.864   22.310  0.50 10.85 ? 80  LYS A N   1 
ATOM   624  C  CA  A LYS A 1 80  ? 0.097  10.636  23.482  0.50 10.98 ? 80  LYS A CA  1 
ATOM   625  C  CA  B LYS A 1 80  ? 0.455  10.567  23.586  0.50 11.21 ? 80  LYS A CA  1 
ATOM   626  C  C   A LYS A 1 80  ? -0.244 9.648   24.598  0.50 10.94 ? 80  LYS A C   1 
ATOM   627  C  C   B LYS A 1 80  ? -0.149 9.631   24.623  0.50 10.67 ? 80  LYS A C   1 
ATOM   628  O  O   A LYS A 1 80  ? -0.488 8.462   24.320  0.50 12.13 ? 80  LYS A O   1 
ATOM   629  O  O   B LYS A 1 80  ? -0.471 8.467   24.314  0.50 12.36 ? 80  LYS A O   1 
ATOM   630  C  CB  A LYS A 1 80  ? -1.067 11.631  23.307  0.50 13.67 ? 80  LYS A CB  1 
ATOM   631  C  CB  B LYS A 1 80  ? -0.315 11.902  23.548  0.50 15.16 ? 80  LYS A CB  1 
ATOM   632  C  CG  A LYS A 1 80  ? -0.841 12.699  22.237  0.50 16.00 ? 80  LYS A CG  1 
ATOM   633  C  CG  B LYS A 1 80  ? -1.755 11.756  23.089  0.50 16.54 ? 80  LYS A CG  1 
ATOM   634  C  CD  A LYS A 1 80  ? -2.035 13.637  22.069  0.50 19.79 ? 80  LYS A CD  1 
ATOM   635  C  CD  B LYS A 1 80  ? -2.550 13.045  22.929  0.50 24.94 ? 80  LYS A CD  1 
ATOM   636  N  N   . GLY A 1 81  ? -0.246 10.153  25.842  1.00 12.48 ? 81  GLY A N   1 
ATOM   637  C  CA  . GLY A 1 81  ? -0.745 9.332   26.928  1.00 12.73 ? 81  GLY A CA  1 
ATOM   638  C  C   . GLY A 1 81  ? 0.284  8.273   27.265  1.00 11.74 ? 81  GLY A C   1 
ATOM   639  O  O   . GLY A 1 81  ? 1.493  8.486   27.088  1.00 11.83 ? 81  GLY A O   1 
ATOM   640  N  N   . GLY A 1 82  ? -0.181 7.159   27.811  1.00 13.03 ? 82  GLY A N   1 
ATOM   641  C  CA  . GLY A 1 82  ? 0.765  6.173   28.273  1.00 18.06 ? 82  GLY A CA  1 
ATOM   642  C  C   . GLY A 1 82  ? 1.668  6.836   29.311  1.00 16.63 ? 82  GLY A C   1 
ATOM   643  O  O   . GLY A 1 82  ? 1.205  7.599   30.165  1.00 21.98 ? 82  GLY A O   1 
ATOM   644  N  N   . PRO A 1 83  ? 2.998  6.624   29.213  1.00 13.95 ? 83  PRO A N   1 
ATOM   645  C  CA  . PRO A 1 83  ? 3.947  7.187   30.169  1.00 14.31 ? 83  PRO A CA  1 
ATOM   646  C  C   . PRO A 1 83  ? 4.363  8.573   29.705  1.00 15.43 ? 83  PRO A C   1 
ATOM   647  O  O   . PRO A 1 83  ? 5.169  9.211   30.371  1.00 20.41 ? 83  PRO A O   1 
ATOM   648  C  CB  . PRO A 1 83  ? 5.151  6.224   30.038  1.00 16.45 ? 83  PRO A CB  1 
ATOM   649  C  CG  . PRO A 1 83  ? 5.151  5.919   28.565  1.00 13.02 ? 83  PRO A CG  1 
ATOM   650  C  CD  . PRO A 1 83  ? 3.681  5.754   28.222  1.00 14.39 ? 83  PRO A CD  1 
ATOM   651  N  N   . LEU A 1 84  ? 3.799  9.048   28.584  1.00 10.86 ? 84  LEU A N   1 
ATOM   652  C  CA  . LEU A 1 84  ? 4.329  10.269  27.938  1.00 10.36 ? 84  LEU A CA  1 
ATOM   653  C  C   . LEU A 1 84  ? 3.708  11.550  28.478  1.00 14.92 ? 84  LEU A C   1 
ATOM   654  O  O   . LEU A 1 84  ? 2.520  11.562  28.804  1.00 18.72 ? 84  LEU A O   1 
ATOM   655  C  CB  . LEU A 1 84  ? 4.118  10.231  26.421  1.00 9.70  ? 84  LEU A CB  1 
ATOM   656  C  CG  . LEU A 1 84  ? 4.665  8.975   25.739  1.00 9.94  ? 84  LEU A CG  1 
ATOM   657  C  CD1 . LEU A 1 84  ? 4.199  8.911   24.286  1.00 11.60 ? 84  LEU A CD1 1 
ATOM   658  C  CD2 . LEU A 1 84  ? 6.203  8.927   25.749  1.00 11.32 ? 84  LEU A CD2 1 
ATOM   659  N  N   . ASP A 1 85  ? 4.512  12.626  28.546  1.00 16.91 ? 85  ASP A N   1 
ATOM   660  C  CA  . ASP A 1 85  ? 3.948  13.960  28.758  1.00 21.71 ? 85  ASP A CA  1 
ATOM   661  C  C   . ASP A 1 85  ? 3.939  14.626  27.385  1.00 22.05 ? 85  ASP A C   1 
ATOM   662  O  O   . ASP A 1 85  ? 4.955  14.638  26.679  1.00 28.81 ? 85  ASP A O   1 
ATOM   663  C  CB  . ASP A 1 85  ? 4.823  14.735  29.746  1.00 31.19 ? 85  ASP A CB  1 
ATOM   664  C  CG  . ASP A 1 85  ? 4.886  14.111  31.130  1.00 38.28 ? 85  ASP A CG  1 
ATOM   665  O  OD1 . ASP A 1 85  ? 3.899  13.434  31.528  1.00 47.88 ? 85  ASP A OD1 1 
ATOM   666  O  OD2 . ASP A 1 85  ? 5.923  14.334  31.826  1.00 57.41 ? 85  ASP A OD2 1 
ATOM   667  N  N   . GLY A 1 86  ? 2.878  15.308  27.001  1.00 31.21 ? 86  GLY A N   1 
ATOM   668  C  CA  . GLY A 1 86  ? 2.979  15.961  25.701  1.00 29.52 ? 86  GLY A CA  1 
ATOM   669  C  C   . GLY A 1 86  ? 2.846  14.990  24.505  1.00 20.45 ? 86  GLY A C   1 
ATOM   670  O  O   . GLY A 1 86  ? 2.426  13.839  24.629  1.00 24.78 ? 86  GLY A O   1 
ATOM   671  N  N   . THR A 1 87  ? 3.058  15.514  23.311  1.00 14.75 ? 87  THR A N   1 
ATOM   672  C  CA  . THR A 1 87  ? 2.539  14.961  22.075  1.00 14.14 ? 87  THR A CA  1 
ATOM   673  C  C   . THR A 1 87  ? 3.787  14.618  21.249  1.00 10.29 ? 87  THR A C   1 
ATOM   674  O  O   . THR A 1 87  ? 4.752  15.383  21.151  1.00 10.80 ? 87  THR A O   1 
ATOM   675  C  CB  . THR A 1 87  ? 1.768  16.042  21.288  1.00 20.06 ? 87  THR A CB  1 
ATOM   676  O  OG1 . THR A 1 87  ? 0.605  16.321  22.055  1.00 25.35 ? 87  THR A OG1 1 
ATOM   677  C  CG2 . THR A 1 87  ? 1.397  15.593  19.888  1.00 19.45 ? 87  THR A CG2 1 
ATOM   678  N  N   . TYR A 1 88  ? 3.786  13.416  20.738  1.00 8.46  ? 88  TYR A N   1 
ATOM   679  C  CA  . TYR A 1 88  ? 4.899  12.922  19.952  1.00 7.23  ? 88  TYR A CA  1 
ATOM   680  C  C   . TYR A 1 88  ? 4.445  12.597  18.527  1.00 6.81  ? 88  TYR A C   1 
ATOM   681  O  O   . TYR A 1 88  ? 3.490  11.825  18.336  1.00 9.62  ? 88  TYR A O   1 
ATOM   682  C  CB  . TYR A 1 88  ? 5.507  11.685  20.579  1.00 8.25  ? 88  TYR A CB  1 
ATOM   683  C  CG  . TYR A 1 88  ? 6.271  11.893  21.867  1.00 6.38  ? 88  TYR A CG  1 
ATOM   684  C  CD1 . TYR A 1 88  ? 5.652  12.298  23.057  1.00 7.47  ? 88  TYR A CD1 1 
ATOM   685  C  CD2 . TYR A 1 88  ? 7.656  11.679  21.876  1.00 7.05  ? 88  TYR A CD2 1 
ATOM   686  C  CE1 . TYR A 1 88  ? 6.407  12.477  24.220  1.00 9.20  ? 88  TYR A CE1 1 
ATOM   687  C  CE2 . TYR A 1 88  ? 8.399  11.840  23.021  1.00 6.16  ? 88  TYR A CE2 1 
ATOM   688  C  CZ  . TYR A 1 88  ? 7.792  12.213  24.198  1.00 6.28  ? 88  TYR A CZ  1 
ATOM   689  O  OH  . TYR A 1 88  ? 8.471  12.370  25.355  1.00 8.91  ? 88  TYR A OH  1 
ATOM   690  N  N   . ARG A 1 89  ? 5.088  13.191  17.526  1.00 6.28  ? 89  ARG A N   1 
ATOM   691  C  CA  . ARG A 1 89  ? 4.669  13.030  16.140  1.00 6.37  ? 89  ARG A CA  1 
ATOM   692  C  C   . ARG A 1 89  ? 5.398  11.884  15.455  1.00 5.11  ? 89  ARG A C   1 
ATOM   693  O  O   . ARG A 1 89  ? 6.620  11.745  15.602  1.00 5.97  ? 89  ARG A O   1 
ATOM   694  C  CB  . ARG A 1 89  ? 5.028  14.291  15.336  1.00 9.14  ? 89  ARG A CB  1 
ATOM   695  C  CG  . ARG A 1 89  ? 4.107  15.465  15.498  1.00 14.73 ? 89  ARG A CG  1 
ATOM   696  C  CD  . ARG A 1 89  ? 4.201  16.371  14.291  1.00 17.98 ? 89  ARG A CD  1 
ATOM   697  N  NE  . ARG A 1 89  ? 3.559  17.564  14.790  1.00 19.86 ? 89  ARG A NE  1 
ATOM   698  C  CZ  . ARG A 1 89  ? 3.915  18.811  14.537  1.00 20.57 ? 89  ARG A CZ  1 
ATOM   699  N  NH1 . ARG A 1 89  ? 4.922  19.103  13.726  1.00 17.42 ? 89  ARG A NH1 1 
ATOM   700  N  NH2 . ARG A 1 89  ? 3.224  19.769  15.108  1.00 24.54 ? 89  ARG A NH2 1 
ATOM   701  N  N   . LEU A 1 90  ? 4.644  11.055  14.740  1.00 6.10  ? 90  LEU A N   1 
ATOM   702  C  CA  . LEU A 1 90  ? 5.240  9.958   13.990  1.00 6.34  ? 90  LEU A CA  1 
ATOM   703  C  C   . LEU A 1 90  ? 6.056  10.500  12.824  1.00 6.41  ? 90  LEU A C   1 
ATOM   704  O  O   . LEU A 1 90  ? 5.568  11.235  11.980  1.00 9.28  ? 90  LEU A O   1 
ATOM   705  C  CB  . LEU A 1 90  ? 4.129  9.092   13.413  1.00 6.46  ? 90  LEU A CB  1 
ATOM   706  C  CG  . LEU A 1 90  ? 4.526  7.903   12.543  1.00 7.00  ? 90  LEU A CG  1 
ATOM   707  C  CD1 . LEU A 1 90  ? 5.310  6.891   13.373  1.00 7.89  ? 90  LEU A CD1 1 
ATOM   708  C  CD2 . LEU A 1 90  ? 3.274  7.248   11.935  1.00 8.98  ? 90  LEU A CD2 1 
ATOM   709  N  N   . ILE A 1 91  ? 7.317  10.073  12.744  1.00 6.76  ? 91  ILE A N   1 
ATOM   710  C  CA  . ILE A 1 91  ? 8.186  10.448  11.628  1.00 6.43  ? 91  ILE A CA  1 
ATOM   711  C  C   . ILE A 1 91  ? 8.431  9.250   10.696  1.00 5.08  ? 91  ILE A C   1 
ATOM   712  O  O   . ILE A 1 91  ? 8.483  9.414   9.469   1.00 6.11  ? 91  ILE A O   1 
ATOM   713  C  CB  . ILE A 1 91  ? 9.507  11.125  12.091  1.00 7.59  ? 91  ILE A CB  1 
ATOM   714  C  CG1 . ILE A 1 91  ? 10.461 11.393  10.910  1.00 9.75  ? 91  ILE A CG1 1 
ATOM   715  C  CG2 . ILE A 1 91  ? 10.289 10.325  13.113  1.00 8.44  ? 91  ILE A CG2 1 
ATOM   716  C  CD1 . ILE A 1 91  ? 9.955  12.346  9.790   1.00 14.33 ? 91  ILE A CD1 1 
ATOM   717  N  N   . GLN A 1 92  ? 8.635  8.048   11.265  1.00 5.46  ? 92  GLN A N   1 
ATOM   718  C  CA  . GLN A 1 92  ? 8.874  6.896   10.376  1.00 5.83  ? 92  GLN A CA  1 
ATOM   719  C  C   . GLN A 1 92  ? 8.605  5.621   11.148  1.00 5.58  ? 92  GLN A C   1 
ATOM   720  O  O   . GLN A 1 92  ? 8.572  5.649   12.365  1.00 5.70  ? 92  GLN A O   1 
ATOM   721  C  CB  . GLN A 1 92  ? 10.337 6.849   9.839   1.00 6.16  ? 92  GLN A CB  1 
ATOM   722  C  CG  . GLN A 1 92  ? 11.373 6.867   10.990  1.00 8.31  ? 92  GLN A CG  1 
ATOM   723  C  CD  . GLN A 1 92  ? 12.289 5.688   10.841  1.00 8.34  ? 92  GLN A CD  1 
ATOM   724  O  OE1 . GLN A 1 92  ? 11.878 4.563   11.185  1.00 13.46 ? 92  GLN A OE1 1 
ATOM   725  N  NE2 . GLN A 1 92  ? 13.407 5.955   10.190  1.00 14.34 ? 92  GLN A NE2 1 
ATOM   726  N  N   . PHE A 1 93  ? 8.415  4.507   10.420  1.00 4.57  ? 93  PHE A N   1 
ATOM   727  C  CA  . PHE A 1 93  ? 8.561  3.217   11.059  1.00 4.01  ? 93  PHE A CA  1 
ATOM   728  C  C   . PHE A 1 93  ? 9.541  2.379   10.253  1.00 3.36  ? 93  PHE A C   1 
ATOM   729  O  O   . PHE A 1 93  ? 9.784  2.595   9.056   1.00 5.53  ? 93  PHE A O   1 
ATOM   730  C  CB  . PHE A 1 93  ? 7.221  2.468   11.219  1.00 5.39  ? 93  PHE A CB  1 
ATOM   731  C  CG  . PHE A 1 93  ? 6.451  2.053   10.004  1.00 4.26  ? 93  PHE A CG  1 
ATOM   732  C  CD1 . PHE A 1 93  ? 6.839  0.957   9.244   1.00 5.74  ? 93  PHE A CD1 1 
ATOM   733  C  CD2 . PHE A 1 93  ? 5.328  2.775   9.572   1.00 5.52  ? 93  PHE A CD2 1 
ATOM   734  C  CE1 . PHE A 1 93  ? 6.169  0.523   8.116   1.00 6.14  ? 93  PHE A CE1 1 
ATOM   735  C  CE2 . PHE A 1 93  ? 4.616  2.320   8.449   1.00 6.87  ? 93  PHE A CE2 1 
ATOM   736  C  CZ  . PHE A 1 93  ? 5.018  1.206   7.728   1.00 7.07  ? 93  PHE A CZ  1 
ATOM   737  N  N   . HIS A 1 94  ? 10.119 1.383   10.939  1.00 4.32  ? 94  HIS A N   1 
ATOM   738  C  CA  . HIS A 1 94  ? 11.057 0.445   10.337  1.00 3.95  ? 94  HIS A CA  1 
ATOM   739  C  C   . HIS A 1 94  ? 10.954 -0.867  11.069  1.00 3.47  ? 94  HIS A C   1 
ATOM   740  O  O   . HIS A 1 94  ? 10.238 -0.958  12.063  1.00 4.02  ? 94  HIS A O   1 
ATOM   741  C  CB  . HIS A 1 94  ? 12.483 1.017   10.371  1.00 4.80  ? 94  HIS A CB  1 
ATOM   742  C  CG  . HIS A 1 94  ? 12.986 1.186   11.759  1.00 4.27  ? 94  HIS A CG  1 
ATOM   743  N  ND1 . HIS A 1 94  ? 12.783 2.377   12.463  1.00 4.31  ? 94  HIS A ND1 1 
ATOM   744  C  CD2 . HIS A 1 94  ? 13.582 0.318   12.619  1.00 4.93  ? 94  HIS A CD2 1 
ATOM   745  C  CE1 . HIS A 1 94  ? 13.239 2.220   13.702  1.00 4.49  ? 94  HIS A CE1 1 
ATOM   746  N  NE2 . HIS A 1 94  ? 13.703 0.956   13.840  1.00 4.47  ? 94  HIS A NE2 1 
ATOM   747  N  N   . PHE A 1 95  ? 11.682 -1.885  10.599  1.00 4.29  ? 95  PHE A N   1 
ATOM   748  C  CA  . PHE A 1 95  ? 11.654 -3.206  11.206  1.00 3.80  ? 95  PHE A CA  1 
ATOM   749  C  C   . PHE A 1 95  ? 13.083 -3.666  11.493  1.00 3.77  ? 95  PHE A C   1 
ATOM   750  O  O   . PHE A 1 95  ? 14.057 -3.198  10.909  1.00 5.32  ? 95  PHE A O   1 
ATOM   751  C  CB  . PHE A 1 95  ? 10.953 -4.212  10.296  1.00 5.22  ? 95  PHE A CB  1 
ATOM   752  C  CG  . PHE A 1 95  ? 9.492  -3.930  10.009  1.00 5.35  ? 95  PHE A CG  1 
ATOM   753  C  CD1 . PHE A 1 95  ? 9.122  -2.990  9.048   1.00 7.01  ? 95  PHE A CD1 1 
ATOM   754  C  CD2 . PHE A 1 95  ? 8.472  -4.636  10.637  1.00 6.67  ? 95  PHE A CD2 1 
ATOM   755  C  CE1 . PHE A 1 95  ? 7.805  -2.782  8.684   1.00 7.58  ? 95  PHE A CE1 1 
ATOM   756  C  CE2 . PHE A 1 95  ? 7.149  -4.415  10.306  1.00 7.03  ? 95  PHE A CE2 1 
ATOM   757  C  CZ  . PHE A 1 95  ? 6.814  -3.462  9.343   1.00 8.12  ? 95  PHE A CZ  1 
ATOM   758  N  N   . HIS A 1 96  ? 13.157 -4.676  12.338  1.00 3.85  ? 96  HIS A N   1 
ATOM   759  C  CA  . HIS A 1 96  ? 14.348 -5.509  12.516  1.00 3.51  ? 96  HIS A CA  1 
ATOM   760  C  C   . HIS A 1 96  ? 13.902 -6.948  12.376  1.00 4.26  ? 96  HIS A C   1 
ATOM   761  O  O   . HIS A 1 96  ? 12.807 -7.292  12.879  1.00 4.91  ? 96  HIS A O   1 
ATOM   762  C  CB  . HIS A 1 96  ? 14.978 -5.277  13.924  1.00 3.97  ? 96  HIS A CB  1 
ATOM   763  C  CG  . HIS A 1 96  ? 15.288 -3.852  14.242  1.00 3.86  ? 96  HIS A CG  1 
ATOM   764  N  ND1 . HIS A 1 96  ? 16.526 -3.252  13.958  1.00 4.96  ? 96  HIS A ND1 1 
ATOM   765  C  CD2 . HIS A 1 96  ? 14.465 -2.858  14.671  1.00 4.09  ? 96  HIS A CD2 1 
ATOM   766  C  CE1 . HIS A 1 96  ? 16.453 -1.962  14.326  1.00 5.16  ? 96  HIS A CE1 1 
ATOM   767  N  NE2 . HIS A 1 96  ? 15.183 -1.690  14.757  1.00 3.76  ? 96  HIS A NE2 1 
ATOM   768  N  N   . TRP A 1 97  ? 14.686 -7.822  11.758  1.00 4.35  ? 97  TRP A N   1 
ATOM   769  C  CA  . TRP A 1 97  ? 14.254 -9.192  11.575  1.00 4.00  ? 97  TRP A CA  1 
ATOM   770  C  C   . TRP A 1 97  ? 15.457 -10.119 11.453  1.00 3.79  ? 97  TRP A C   1 
ATOM   771  O  O   . TRP A 1 97  ? 16.637 -9.695  11.396  1.00 4.75  ? 97  TRP A O   1 
ATOM   772  C  CB  . TRP A 1 97  ? 13.365 -9.332  10.341  1.00 4.42  ? 97  TRP A CB  1 
ATOM   773  C  CG  . TRP A 1 97  ? 14.018 -8.953  9.048   1.00 4.00  ? 97  TRP A CG  1 
ATOM   774  C  CD1 . TRP A 1 97  ? 14.763 -9.750  8.230   1.00 5.13  ? 97  TRP A CD1 1 
ATOM   775  C  CD2 . TRP A 1 97  ? 14.107 -7.632  8.457   1.00 4.56  ? 97  TRP A CD2 1 
ATOM   776  N  NE1 . TRP A 1 97  ? 15.221 -9.048  7.136   1.00 5.60  ? 97  TRP A NE1 1 
ATOM   777  C  CE2 . TRP A 1 97  ? 14.836 -7.723  7.245   1.00 4.90  ? 97  TRP A CE2 1 
ATOM   778  C  CE3 . TRP A 1 97  ? 13.590 -6.370  8.828   1.00 4.57  ? 97  TRP A CE3 1 
ATOM   779  C  CZ2 . TRP A 1 97  ? 15.080 -6.629  6.420   1.00 6.33  ? 97  TRP A CZ2 1 
ATOM   780  C  CZ3 . TRP A 1 97  ? 13.825 -5.296  8.011   1.00 5.36  ? 97  TRP A CZ3 1 
ATOM   781  C  CH2 . TRP A 1 97  ? 14.598 -5.408  6.846   1.00 6.41  ? 97  TRP A CH2 1 
ATOM   782  N  N   . GLY A 1 98  ? 15.162 -11.419 11.465  1.00 4.60  ? 98  GLY A N   1 
ATOM   783  C  CA  . GLY A 1 98  ? 16.198 -12.419 11.552  1.00 6.20  ? 98  GLY A CA  1 
ATOM   784  C  C   . GLY A 1 98  ? 16.419 -13.143 10.228  1.00 6.18  ? 98  GLY A C   1 
ATOM   785  O  O   . GLY A 1 98  ? 15.707 -12.970 9.227   1.00 7.71  ? 98  GLY A O   1 
ATOM   786  N  N   . SER A 1 99  ? 17.421 -14.046 10.260  1.00 7.89  ? 99  SER A N   1 
ATOM   787  C  CA  . SER A 1 99  ? 17.644 -14.982 9.143   1.00 8.68  ? 99  SER A CA  1 
ATOM   788  C  C   . SER A 1 99  ? 16.766 -16.233 9.268   1.00 8.97  ? 99  SER A C   1 
ATOM   789  O  O   . SER A 1 99  ? 16.604 -16.937 8.285   1.00 12.06 ? 99  SER A O   1 
ATOM   790  C  CB  . SER A 1 99  ? 19.082 -15.392 9.065   1.00 9.54  ? 99  SER A CB  1 
ATOM   791  O  OG  . SER A 1 99  ? 19.511 -15.855 10.339  1.00 10.22 ? 99  SER A OG  1 
ATOM   792  N  N   . LEU A 1 100 ? 16.184 -16.483 10.481  1.00 8.59  ? 100 LEU A N   1 
ATOM   793  C  CA  . LEU A 1 100 ? 15.386 -17.641 10.874  1.00 10.03 ? 100 LEU A CA  1 
ATOM   794  C  C   . LEU A 1 100 ? 14.204 -17.099 11.689  1.00 10.17 ? 100 LEU A C   1 
ATOM   795  O  O   . LEU A 1 100 ? 14.332 -16.051 12.335  1.00 10.32 ? 100 LEU A O   1 
ATOM   796  C  CB  . LEU A 1 100 ? 16.201 -18.584 11.787  1.00 13.66 ? 100 LEU A CB  1 
ATOM   797  C  CG  . LEU A 1 100 ? 17.482 -19.098 11.127  1.00 15.24 ? 100 LEU A CG  1 
ATOM   798  C  CD1 . LEU A 1 100 ? 18.424 -19.690 12.163  1.00 25.68 ? 100 LEU A CD1 1 
ATOM   799  C  CD2 . LEU A 1 100 ? 17.077 -20.131 10.088  1.00 18.37 ? 100 LEU A CD2 1 
ATOM   800  N  N   . ASP A 1 101 ? 13.102 -17.850 11.718  1.00 11.56 ? 101 ASP A N   1 
ATOM   801  C  CA  . ASP A 1 101 ? 11.891 -17.347 12.378  1.00 10.70 ? 101 ASP A CA  1 
ATOM   802  C  C   . ASP A 1 101 ? 12.090 -17.242 13.905  1.00 12.46 ? 101 ASP A C   1 
ATOM   803  O  O   . ASP A 1 101 ? 11.334 -16.516 14.544  1.00 14.71 ? 101 ASP A O   1 
ATOM   804  C  CB  . ASP A 1 101 ? 10.687 -18.238 12.039  1.00 12.49 ? 101 ASP A CB  1 
ATOM   805  C  CG  . ASP A 1 101 ? 10.229 -18.221 10.581  1.00 15.45 ? 101 ASP A CG  1 
ATOM   806  O  OD1 . ASP A 1 101 ? 10.640 -17.340 9.794   1.00 15.93 ? 101 ASP A OD1 1 
ATOM   807  O  OD2 . ASP A 1 101 ? 9.468  -19.136 10.215  1.00 21.60 ? 101 ASP A OD2 1 
ATOM   808  N  N   . GLY A 1 102 ? 13.082 -17.933 14.507  1.00 13.00 ? 102 GLY A N   1 
ATOM   809  C  CA  . GLY A 1 102 ? 13.294 -17.892 15.953  1.00 13.76 ? 102 GLY A CA  1 
ATOM   810  C  C   . GLY A 1 102 ? 14.184 -16.743 16.445  1.00 11.36 ? 102 GLY A C   1 
ATOM   811  O  O   . GLY A 1 102 ? 14.584 -16.754 17.618  1.00 13.46 ? 102 GLY A O   1 
ATOM   812  N  N   . GLN A 1 103 ? 14.539 -15.780 15.572  1.00 8.32  ? 103 GLN A N   1 
ATOM   813  C  CA  . GLN A 1 103 ? 15.303 -14.621 15.990  1.00 7.82  ? 103 GLN A CA  1 
ATOM   814  C  C   . GLN A 1 103 ? 14.961 -13.462 15.073  1.00 6.22  ? 103 GLN A C   1 
ATOM   815  O  O   . GLN A 1 103 ? 14.386 -13.653 14.000  1.00 7.23  ? 103 GLN A O   1 
ATOM   816  C  CB  . GLN A 1 103 ? 16.816 -14.897 15.939  1.00 8.63  ? 103 GLN A CB  1 
ATOM   817  C  CG  . GLN A 1 103 ? 17.318 -15.141 14.516  1.00 8.77  ? 103 GLN A CG  1 
ATOM   818  C  CD  . GLN A 1 103 ? 18.629 -15.865 14.518  1.00 11.81 ? 103 GLN A CD  1 
ATOM   819  O  OE1 . GLN A 1 103 ? 18.669 -16.997 15.007  1.00 15.90 ? 103 GLN A OE1 1 
ATOM   820  N  NE2 . GLN A 1 103 ? 19.623 -15.248 13.892  1.00 11.13 ? 103 GLN A NE2 1 
ATOM   821  N  N   . GLY A 1 104 ? 15.294 -12.230 15.553  1.00 5.94  ? 104 GLY A N   1 
ATOM   822  C  CA  . GLY A 1 104 ? 15.003 -11.063 14.727  1.00 5.41  ? 104 GLY A CA  1 
ATOM   823  C  C   . GLY A 1 104 ? 14.566 -9.870  15.562  1.00 4.89  ? 104 GLY A C   1 
ATOM   824  O  O   . GLY A 1 104 ? 14.815 -8.727  15.223  1.00 5.61  ? 104 GLY A O   1 
ATOM   825  N  N   . SER A 1 105 ? 13.829 -10.135 16.669  1.00 4.82  ? 105 SER A N   1 
ATOM   826  C  CA  . SER A 1 105 ? 13.441 -9.021  17.525  1.00 5.63  ? 105 SER A CA  1 
ATOM   827  C  C   . SER A 1 105 ? 14.637 -8.462  18.310  1.00 4.63  ? 105 SER A C   1 
ATOM   828  O  O   . SER A 1 105 ? 15.655 -9.127  18.517  1.00 6.32  ? 105 SER A O   1 
ATOM   829  C  CB  . SER A 1 105 ? 12.287 -9.364  18.508  1.00 5.95  ? 105 SER A CB  1 
ATOM   830  O  OG  . SER A 1 105 ? 12.671 -10.338 19.436  1.00 5.75  ? 105 SER A OG  1 
ATOM   831  N  N   . GLU A 1 106 ? 14.506 -7.207  18.702  1.00 4.21  ? 106 GLU A N   1 
ATOM   832  C  CA  . GLU A 1 106 ? 15.514 -6.523  19.506  1.00 4.66  ? 106 GLU A CA  1 
ATOM   833  C  C   . GLU A 1 106 ? 15.194 -6.720  20.977  1.00 4.02  ? 106 GLU A C   1 
ATOM   834  O  O   . GLU A 1 106 ? 15.986 -7.289  21.755  1.00 5.47  ? 106 GLU A O   1 
ATOM   835  C  CB  . GLU A 1 106 ? 15.579 -5.061  19.102  1.00 5.23  ? 106 GLU A CB  1 
ATOM   836  C  CG  . GLU A 1 106 ? 16.023 -4.887  17.663  1.00 6.06  ? 106 GLU A CG  1 
ATOM   837  C  CD  . GLU A 1 106 ? 16.725 -3.599  17.452  1.00 6.12  ? 106 GLU A CD  1 
ATOM   838  O  OE1 . GLU A 1 106 ? 16.136 -2.536  17.706  1.00 6.59  ? 106 GLU A OE1 1 
ATOM   839  O  OE2 . GLU A 1 106 ? 17.880 -3.663  16.936  1.00 7.78  ? 106 GLU A OE2 1 
ATOM   840  N  N   . HIS A 1 107 ? 14.022 -6.298  21.408  1.00 4.49  ? 107 HIS A N   1 
ATOM   841  C  CA  . HIS A 1 107 ? 13.551 -6.659  22.744  1.00 4.81  ? 107 HIS A CA  1 
ATOM   842  C  C   . HIS A 1 107 ? 13.265 -8.166  22.761  1.00 4.97  ? 107 HIS A C   1 
ATOM   843  O  O   . HIS A 1 107 ? 12.940 -8.776  21.731  1.00 4.87  ? 107 HIS A O   1 
ATOM   844  C  CB  . HIS A 1 107 ? 12.296 -5.872  23.115  1.00 4.88  ? 107 HIS A CB  1 
ATOM   845  C  CG  . HIS A 1 107 ? 12.620 -4.435  23.295  1.00 4.55  ? 107 HIS A CG  1 
ATOM   846  N  ND1 . HIS A 1 107 ? 12.532 -3.533  22.258  1.00 4.97  ? 107 HIS A ND1 1 
ATOM   847  C  CD2 . HIS A 1 107 ? 13.100 -3.744  24.362  1.00 5.01  ? 107 HIS A CD2 1 
ATOM   848  C  CE1 . HIS A 1 107 ? 12.976 -2.330  22.694  1.00 5.72  ? 107 HIS A CE1 1 
ATOM   849  N  NE2 . HIS A 1 107 ? 13.328 -2.437  24.001  1.00 5.74  ? 107 HIS A NE2 1 
ATOM   850  N  N   . THR A 1 108 ? 13.367 -8.711  23.965  1.00 5.64  ? 108 THR A N   1 
ATOM   851  C  CA  . THR A 1 108 ? 12.987 -10.122 24.175  1.00 5.38  ? 108 THR A CA  1 
ATOM   852  C  C   . THR A 1 108 ? 12.029 -10.118 25.366  1.00 5.76  ? 108 THR A C   1 
ATOM   853  O  O   . THR A 1 108 ? 12.024 -9.158  26.146  1.00 6.37  ? 108 THR A O   1 
ATOM   854  C  CB  . THR A 1 108 ? 14.209 -11.025 24.367  1.00 7.06  ? 108 THR A CB  1 
ATOM   855  O  OG1 . THR A 1 108 ? 15.009 -10.557 25.454  1.00 7.14  ? 108 THR A OG1 1 
ATOM   856  C  CG2 . THR A 1 108 ? 15.061 -11.074 23.110  1.00 7.46  ? 108 THR A CG2 1 
ATOM   857  N  N   . VAL A 1 109 ? 11.247 -11.185 25.516  1.00 7.29  ? 109 VAL A N   1 
ATOM   858  C  CA  . VAL A 1 109 ? 10.265 -11.279 26.604  1.00 9.07  ? 109 VAL A CA  1 
ATOM   859  C  C   . VAL A 1 109 ? 10.597 -12.578 27.323  1.00 9.31  ? 109 VAL A C   1 
ATOM   860  O  O   . VAL A 1 109 ? 10.443 -13.662 26.734  1.00 10.18 ? 109 VAL A O   1 
ATOM   861  C  CB  . VAL A 1 109 ? 8.826  -11.272 26.041  1.00 10.21 ? 109 VAL A CB  1 
ATOM   862  C  CG1 . VAL A 1 109 ? 7.849  -11.400 27.180  1.00 11.91 ? 109 VAL A CG1 1 
ATOM   863  C  CG2 . VAL A 1 109 ? 8.551  -9.981  25.320  1.00 10.30 ? 109 VAL A CG2 1 
ATOM   864  N  N   . ASP A 1 110 ? 11.057 -12.492 28.583  1.00 8.84  ? 110 ASP A N   1 
ATOM   865  C  CA  . ASP A 1 110 ? 11.499 -13.713 29.261  1.00 10.31 ? 110 ASP A CA  1 
ATOM   866  C  C   . ASP A 1 110 ? 12.455 -14.524 28.381  1.00 10.21 ? 110 ASP A C   1 
ATOM   867  O  O   . ASP A 1 110 ? 12.399 -15.755 28.334  1.00 11.57 ? 110 ASP A O   1 
ATOM   868  C  CB  . ASP A 1 110 ? 10.269 -14.521 29.682  1.00 13.20 ? 110 ASP A CB  1 
ATOM   869  C  CG  . ASP A 1 110 ? 9.414  -13.775 30.692  1.00 13.75 ? 110 ASP A CG  1 
ATOM   870  O  OD1 . ASP A 1 110 ? 9.987  -12.953 31.452  1.00 15.33 ? 110 ASP A OD1 1 
ATOM   871  O  OD2 . ASP A 1 110 ? 8.162  -14.025 30.734  1.00 21.05 ? 110 ASP A OD2 1 
ATOM   872  N  N   . LYS A 1 111 ? 13.381 -13.804 27.718  1.00 8.66  ? 111 LYS A N   1 
ATOM   873  C  CA  . LYS A 1 111 ? 14.455 -14.281 26.832  1.00 9.07  ? 111 LYS A CA  1 
ATOM   874  C  C   . LYS A 1 111 ? 13.911 -14.790 25.490  1.00 11.18 ? 111 LYS A C   1 
ATOM   875  O  O   . LYS A 1 111 ? 14.694 -15.193 24.635  1.00 12.47 ? 111 LYS A O   1 
ATOM   876  C  CB  . LYS A 1 111 ? 15.366 -15.329 27.507  1.00 12.79 ? 111 LYS A CB  1 
ATOM   877  C  CG  . LYS A 1 111 ? 15.985 -14.851 28.830  1.00 16.64 ? 111 LYS A CG  1 
ATOM   878  C  CD  . LYS A 1 111 ? 16.945 -13.710 28.584  1.00 23.08 ? 111 LYS A CD  1 
ATOM   879  C  CE  . LYS A 1 111 ? 17.618 -13.237 29.855  1.00 28.13 ? 111 LYS A CE  1 
ATOM   880  N  NZ  . LYS A 1 111 ? 19.029 -13.623 29.795  1.00 37.35 ? 111 LYS A NZ  1 
ATOM   881  N  N   . LYS A 1 112 ? 12.598 -14.830 25.293  1.00 9.16  ? 112 LYS A N   1 
ATOM   882  C  CA  . LYS A 1 112 ? 12.044 -15.238 23.995  1.00 10.55 ? 112 LYS A CA  1 
ATOM   883  C  C   . LYS A 1 112 ? 12.266 -14.170 22.938  1.00 8.65  ? 112 LYS A C   1 
ATOM   884  O  O   . LYS A 1 112 ? 12.001 -12.986 23.170  1.00 8.03  ? 112 LYS A O   1 
ATOM   885  C  CB  . LYS A 1 112 ? 10.529 -15.438 24.091  1.00 13.82 ? 112 LYS A CB  1 
ATOM   886  C  CG  . LYS A 1 112 ? 9.815  -15.816 22.805  1.00 18.94 ? 112 LYS A CG  1 
ATOM   887  C  CD  . LYS A 1 112 ? 8.290  -15.859 22.879  1.00 23.52 ? 112 LYS A CD  1 
ATOM   888  C  CE  . LYS A 1 112 ? 7.725  -15.995 21.475  1.00 28.27 ? 112 LYS A CE  1 
ATOM   889  N  NZ  . LYS A 1 112 ? 8.103  -17.264 20.822  1.00 32.08 ? 112 LYS A NZ  1 
ATOM   890  N  N   A LYS A 1 113 ? 12.846 -14.606 21.816  0.50 8.67  ? 113 LYS A N   1 
ATOM   891  N  N   B LYS A 1 113 ? 12.768 -14.605 21.783  0.50 9.44  ? 113 LYS A N   1 
ATOM   892  C  CA  A LYS A 1 113 ? 12.969 -13.807 20.603  0.50 7.82  ? 113 LYS A CA  1 
ATOM   893  C  CA  B LYS A 1 113 ? 12.976 -13.730 20.638  0.50 8.85  ? 113 LYS A CA  1 
ATOM   894  C  C   A LYS A 1 113 ? 11.756 -14.022 19.710  0.50 6.01  ? 113 LYS A C   1 
ATOM   895  C  C   B LYS A 1 113 ? 11.939 -14.014 19.563  0.50 7.53  ? 113 LYS A C   1 
ATOM   896  O  O   A LYS A 1 113 ? 11.207 -15.118 19.600  0.50 6.79  ? 113 LYS A O   1 
ATOM   897  O  O   B LYS A 1 113 ? 11.744 -15.168 19.171  0.50 9.69  ? 113 LYS A O   1 
ATOM   898  C  CB  A LYS A 1 113 ? 14.229 -14.186 19.810  0.50 8.43  ? 113 LYS A CB  1 
ATOM   899  C  CB  B LYS A 1 113 ? 14.326 -14.041 19.991  0.50 9.62  ? 113 LYS A CB  1 
ATOM   900  C  CG  A LYS A 1 113 ? 15.541 -13.945 20.549  0.50 9.49  ? 113 LYS A CG  1 
ATOM   901  C  CG  B LYS A 1 113 ? 15.536 -13.598 20.800  0.50 8.71  ? 113 LYS A CG  1 
ATOM   902  C  CD  A LYS A 1 113 ? 16.799 -14.472 19.842  0.50 10.64 ? 113 LYS A CD  1 
ATOM   903  C  CD  B LYS A 1 113 ? 16.808 -14.269 20.284  0.50 9.61  ? 113 LYS A CD  1 
ATOM   904  C  CE  A LYS A 1 113 ? 18.068 -13.909 20.466  0.50 12.61 ? 113 LYS A CE  1 
ATOM   905  C  CE  B LYS A 1 113 ? 18.055 -13.791 21.005  0.50 11.05 ? 113 LYS A CE  1 
ATOM   906  N  NZ  A LYS A 1 113 ? 18.433 -14.647 21.696  0.50 15.65 ? 113 LYS A NZ  1 
ATOM   907  N  NZ  B LYS A 1 113 ? 19.251 -14.553 20.566  0.50 13.60 ? 113 LYS A NZ  1 
ATOM   908  N  N   . TYR A 1 114 ? 11.306 -12.932 19.093  1.00 5.85  ? 114 TYR A N   1 
ATOM   909  C  CA  . TYR A 1 114 ? 10.326 -12.999 17.999  1.00 6.00  ? 114 TYR A CA  1 
ATOM   910  C  C   . TYR A 1 114 ? 11.009 -12.925 16.650  1.00 5.20  ? 114 TYR A C   1 
ATOM   911  O  O   . TYR A 1 114 ? 12.205 -12.632 16.543  1.00 5.58  ? 114 TYR A O   1 
ATOM   912  C  CB  . TYR A 1 114 ? 9.324  -11.856 18.171  1.00 6.44  ? 114 TYR A CB  1 
ATOM   913  C  CG  . TYR A 1 114 ? 8.394  -12.108 19.329  1.00 6.73  ? 114 TYR A CG  1 
ATOM   914  C  CD1 . TYR A 1 114 ? 8.700  -11.721 20.619  1.00 9.29  ? 114 TYR A CD1 1 
ATOM   915  C  CD2 . TYR A 1 114 ? 7.193  -12.775 19.098  1.00 8.15  ? 114 TYR A CD2 1 
ATOM   916  C  CE1 . TYR A 1 114 ? 7.795  -11.919 21.670  1.00 10.87 ? 114 TYR A CE1 1 
ATOM   917  C  CE2 . TYR A 1 114 ? 6.276  -12.983 20.135  1.00 10.00 ? 114 TYR A CE2 1 
ATOM   918  C  CZ  . TYR A 1 114 ? 6.584  -12.523 21.402  1.00 12.90 ? 114 TYR A CZ  1 
ATOM   919  O  OH  . TYR A 1 114 ? 5.743  -12.804 22.449  1.00 19.97 ? 114 TYR A OH  1 
ATOM   920  N  N   . ALA A 1 115 ? 10.250 -13.215 15.591  1.00 6.32  ? 115 ALA A N   1 
ATOM   921  C  CA  . ALA A 1 115 ? 10.800 -13.257 14.238  1.00 6.01  ? 115 ALA A CA  1 
ATOM   922  C  C   . ALA A 1 115 ? 11.219 -11.870 13.788  1.00 5.79  ? 115 ALA A C   1 
ATOM   923  O  O   . ALA A 1 115 ? 12.066 -11.681 12.895  1.00 5.97  ? 115 ALA A O   1 
ATOM   924  C  CB  . ALA A 1 115 ? 9.777  -13.839 13.288  1.00 7.76  ? 115 ALA A CB  1 
ATOM   925  N  N   . ALA A 1 116 ? 10.576 -10.816 14.316  1.00 4.79  ? 116 ALA A N   1 
ATOM   926  C  CA  . ALA A 1 116 ? 10.858 -9.456  13.866  1.00 5.16  ? 116 ALA A CA  1 
ATOM   927  C  C   . ALA A 1 116 ? 10.280 -8.488  14.889  1.00 4.14  ? 116 ALA A C   1 
ATOM   928  O  O   . ALA A 1 116 ? 9.523  -8.899  15.781  1.00 4.68  ? 116 ALA A O   1 
ATOM   929  C  CB  . ALA A 1 116 ? 10.334 -9.165  12.446  1.00 5.98  ? 116 ALA A CB  1 
ATOM   930  N  N   . GLU A 1 117 ? 10.606 -7.208  14.737  1.00 3.89  ? 117 GLU A N   1 
ATOM   931  C  CA  . GLU A 1 117 ? 10.056 -6.169  15.599  1.00 3.75  ? 117 GLU A CA  1 
ATOM   932  C  C   . GLU A 1 117 ? 9.858  -4.931  14.743  1.00 4.41  ? 117 GLU A C   1 
ATOM   933  O  O   . GLU A 1 117 ? 10.750 -4.548  13.989  1.00 6.09  ? 117 GLU A O   1 
ATOM   934  C  CB  . GLU A 1 117 ? 11.003 -5.960  16.755  1.00 5.40  ? 117 GLU A CB  1 
ATOM   935  C  CG  . GLU A 1 117 ? 10.452 -5.064  17.894  1.00 6.00  ? 117 GLU A CG  1 
ATOM   936  C  CD  . GLU A 1 117 ? 11.376 -4.999  19.116  1.00 4.75  ? 117 GLU A CD  1 
ATOM   937  O  OE1 . GLU A 1 117 ? 12.066 -6.008  19.405  1.00 6.33  ? 117 GLU A OE1 1 
ATOM   938  O  OE2 . GLU A 1 117 ? 11.352 -3.959  19.829  1.00 6.96  ? 117 GLU A OE2 1 
ATOM   939  N  N   . LEU A 1 118 ? 8.697  -4.338  14.853  1.00 3.91  ? 118 LEU A N   1 
ATOM   940  C  CA  . LEU A 1 118 ? 8.312  -3.094  14.200  1.00 3.90  ? 118 LEU A CA  1 
ATOM   941  C  C   . LEU A 1 118 ? 8.511  -1.973  15.224  1.00 3.18  ? 118 LEU A C   1 
ATOM   942  O  O   . LEU A 1 118 ? 8.065  -2.036  16.360  1.00 4.30  ? 118 LEU A O   1 
ATOM   943  C  CB  . LEU A 1 118 ? 6.807  -3.207  13.826  1.00 5.09  ? 118 LEU A CB  1 
ATOM   944  C  CG  . LEU A 1 118 ? 6.057  -1.906  13.510  1.00 4.59  ? 118 LEU A CG  1 
ATOM   945  C  CD1 . LEU A 1 118 ? 6.649  -1.221  12.284  1.00 6.60  ? 118 LEU A CD1 1 
ATOM   946  C  CD2 . LEU A 1 118 ? 4.586  -2.250  13.271  1.00 7.54  ? 118 LEU A CD2 1 
ATOM   947  N  N   . HIS A 1 119 ? 9.140  -0.883  14.753  1.00 3.53  ? 119 HIS A N   1 
ATOM   948  C  CA  . HIS A 1 119 ? 9.401  0.296   15.557  1.00 4.01  ? 119 HIS A CA  1 
ATOM   949  C  C   . HIS A 1 119 ? 8.789  1.498   14.846  1.00 3.43  ? 119 HIS A C   1 
ATOM   950  O  O   . HIS A 1 119 ? 9.162  1.854   13.714  1.00 4.62  ? 119 HIS A O   1 
ATOM   951  C  CB  . HIS A 1 119 ? 10.928 0.517   15.664  1.00 4.99  ? 119 HIS A CB  1 
ATOM   952  C  CG  . HIS A 1 119 ? 11.499 -0.490  16.606  1.00 4.39  ? 119 HIS A CG  1 
ATOM   953  N  ND1 . HIS A 1 119 ? 12.895 -0.736  16.572  1.00 5.18  ? 119 HIS A ND1 1 
ATOM   954  C  CD2 . HIS A 1 119 ? 10.949 -1.257  17.571  1.00 4.18  ? 119 HIS A CD2 1 
ATOM   955  C  CE1 . HIS A 1 119 ? 13.142 -1.664  17.492  1.00 5.05  ? 119 HIS A CE1 1 
ATOM   956  N  NE2 . HIS A 1 119 ? 11.961 -2.021  18.128  1.00 4.86  ? 119 HIS A NE2 1 
ATOM   957  N  N   . LEU A 1 120 ? 7.819  2.134   15.541  1.00 3.84  ? 120 LEU A N   1 
ATOM   958  C  CA  . LEU A 1 120 ? 7.212  3.381   15.108  1.00 4.14  ? 120 LEU A CA  1 
ATOM   959  C  C   . LEU A 1 120 ? 7.854  4.523   15.874  1.00 3.63  ? 120 LEU A C   1 
ATOM   960  O  O   . LEU A 1 120 ? 7.709  4.555   17.088  1.00 4.05  ? 120 LEU A O   1 
ATOM   961  C  CB  . LEU A 1 120 ? 5.683  3.317   15.295  1.00 4.64  ? 120 LEU A CB  1 
ATOM   962  C  CG  . LEU A 1 120 ? 5.005  2.240   14.414  1.00 5.78  ? 120 LEU A CG  1 
ATOM   963  C  CD1 . LEU A 1 120 ? 4.232  1.256   15.281  1.00 9.55  ? 120 LEU A CD1 1 
ATOM   964  C  CD2 . LEU A 1 120 ? 4.086  2.904   13.367  1.00 8.60  ? 120 LEU A CD2 1 
ATOM   965  N  N   . VAL A 1 121 ? 8.587  5.368   15.160  1.00 4.26  ? 121 VAL A N   1 
ATOM   966  C  CA  . VAL A 1 121 ? 9.438  6.368   15.823  1.00 4.09  ? 121 VAL A CA  1 
ATOM   967  C  C   . VAL A 1 121 ? 8.729  7.731   15.830  1.00 4.47  ? 121 VAL A C   1 
ATOM   968  O  O   . VAL A 1 121 ? 8.267  8.188   14.776  1.00 5.41  ? 121 VAL A O   1 
ATOM   969  C  CB  . VAL A 1 121 ? 10.795 6.473   15.085  1.00 4.89  ? 121 VAL A CB  1 
ATOM   970  C  CG1 . VAL A 1 121 ? 11.692 7.484   15.790  1.00 6.72  ? 121 VAL A CG1 1 
ATOM   971  C  CG2 . VAL A 1 121 ? 11.469 5.105   14.947  1.00 5.92  ? 121 VAL A CG2 1 
ATOM   972  N  N   . HIS A 1 122 ? 8.671  8.332   17.028  1.00 4.26  ? 122 HIS A N   1 
ATOM   973  C  CA  . HIS A 1 122 ? 7.962  9.603   17.204  1.00 4.65  ? 122 HIS A CA  1 
ATOM   974  C  C   . HIS A 1 122 ? 8.864  10.588  17.934  1.00 4.65  ? 122 HIS A C   1 
ATOM   975  O  O   . HIS A 1 122 ? 9.675  10.175  18.777  1.00 5.88  ? 122 HIS A O   1 
ATOM   976  C  CB  . HIS A 1 122 ? 6.670  9.442   18.057  1.00 5.09  ? 122 HIS A CB  1 
ATOM   977  C  CG  . HIS A 1 122 ? 5.785  8.315   17.643  1.00 5.06  ? 122 HIS A CG  1 
ATOM   978  N  ND1 . HIS A 1 122 ? 6.114  7.004   17.855  1.00 5.24  ? 122 HIS A ND1 1 
ATOM   979  C  CD2 . HIS A 1 122 ? 4.568  8.315   17.059  1.00 5.32  ? 122 HIS A CD2 1 
ATOM   980  C  CE1 . HIS A 1 122 ? 5.097  6.213   17.437  1.00 6.05  ? 122 HIS A CE1 1 
ATOM   981  N  NE2 . HIS A 1 122 ? 4.131  7.024   16.907  1.00 6.14  ? 122 HIS A NE2 1 
ATOM   982  N  N   . TRP A 1 123 ? 8.682  11.896  17.676  1.00 4.87  ? 123 TRP A N   1 
ATOM   983  C  CA  . TRP A 1 123 ? 9.511  12.880  18.380  1.00 5.45  ? 123 TRP A CA  1 
ATOM   984  C  C   . TRP A 1 123 ? 8.587  13.848  19.111  1.00 5.11  ? 123 TRP A C   1 
ATOM   985  O  O   . TRP A 1 123 ? 7.468  14.211  18.663  1.00 6.06  ? 123 TRP A O   1 
ATOM   986  C  CB  . TRP A 1 123 ? 10.445 13.609  17.388  1.00 6.55  ? 123 TRP A CB  1 
ATOM   987  C  CG  . TRP A 1 123 ? 9.774  14.285  16.239  1.00 6.05  ? 123 TRP A CG  1 
ATOM   988  C  CD1 . TRP A 1 123 ? 9.499  13.723  15.027  1.00 6.93  ? 123 TRP A CD1 1 
ATOM   989  C  CD2 . TRP A 1 123 ? 9.349  15.666  16.149  1.00 6.18  ? 123 TRP A CD2 1 
ATOM   990  N  NE1 . TRP A 1 123 ? 8.907  14.635  14.187  1.00 8.22  ? 123 TRP A NE1 1 
ATOM   991  C  CE2 . TRP A 1 123 ? 8.829  15.851  14.838  1.00 7.80  ? 123 TRP A CE2 1 
ATOM   992  C  CE3 . TRP A 1 123 ? 9.410  16.774  17.026  1.00 7.65  ? 123 TRP A CE3 1 
ATOM   993  C  CZ2 . TRP A 1 123 ? 8.309  17.070  14.389  1.00 9.49  ? 123 TRP A CZ2 1 
ATOM   994  C  CZ3 . TRP A 1 123 ? 8.879  17.974  16.583  1.00 9.56  ? 123 TRP A CZ3 1 
ATOM   995  C  CH2 . TRP A 1 123 ? 8.345  18.131  15.286  1.00 9.31  ? 123 TRP A CH2 1 
ATOM   996  N  N   . ASN A 1 124 ? 9.123  14.381  20.220  1.00 5.46  ? 124 ASN A N   1 
ATOM   997  C  CA  . ASN A 1 124 ? 8.360  15.226  21.124  1.00 6.28  ? 124 ASN A CA  1 
ATOM   998  C  C   . ASN A 1 124 ? 8.222  16.610  20.511  1.00 7.30  ? 124 ASN A C   1 
ATOM   999  O  O   . ASN A 1 124 ? 9.240  17.303  20.313  1.00 6.46  ? 124 ASN A O   1 
ATOM   1000 C  CB  . ASN A 1 124 ? 9.147  15.284  22.435  1.00 8.45  ? 124 ASN A CB  1 
ATOM   1001 C  CG  . ASN A 1 124 ? 8.357  15.907  23.549  1.00 10.56 ? 124 ASN A CG  1 
ATOM   1002 O  OD1 . ASN A 1 124 ? 7.553  16.841  23.324  1.00 10.95 ? 124 ASN A OD1 1 
ATOM   1003 N  ND2 . ASN A 1 124 ? 8.612  15.423  24.760  1.00 13.78 ? 124 ASN A ND2 1 
ATOM   1004 N  N   . THR A 1 125 ? 6.985  17.085  20.260  1.00 7.71  ? 125 THR A N   1 
ATOM   1005 C  CA  . THR A 1 125 ? 6.791  18.321  19.496  1.00 9.94  ? 125 THR A CA  1 
ATOM   1006 C  C   . THR A 1 125 ? 7.293  19.545  20.288  1.00 10.22 ? 125 THR A C   1 
ATOM   1007 O  O   . THR A 1 125 ? 7.504  20.592  19.683  1.00 11.72 ? 125 THR A O   1 
ATOM   1008 C  CB  . THR A 1 125 ? 5.312  18.500  19.156  1.00 13.76 ? 125 THR A CB  1 
ATOM   1009 O  OG1 . THR A 1 125 ? 4.582  18.553  20.384  1.00 15.94 ? 125 THR A OG1 1 
ATOM   1010 C  CG2 . THR A 1 125 ? 4.834  17.364  18.284  1.00 17.66 ? 125 THR A CG2 1 
ATOM   1011 N  N   . LYS A 1 126 ? 7.563  19.444  21.644  1.00 9.20  ? 127 LYS A N   1 
ATOM   1012 C  CA  . LYS A 1 126 ? 8.099  20.605  22.357  1.00 12.58 ? 127 LYS A CA  1 
ATOM   1013 C  C   . LYS A 1 126 ? 9.502  20.937  21.866  1.00 10.84 ? 127 LYS A C   1 
ATOM   1014 O  O   . LYS A 1 126 ? 9.960  22.030  22.148  1.00 13.86 ? 127 LYS A O   1 
ATOM   1015 C  CB  . LYS A 1 126 ? 7.964  20.384  23.852  1.00 15.70 ? 127 LYS A CB  1 
ATOM   1016 C  CG  . LYS A 1 126 ? 9.032  19.526  24.460  1.00 16.53 ? 127 LYS A CG  1 
ATOM   1017 C  CD  . LYS A 1 126 ? 8.571  19.192  25.886  1.00 20.73 ? 127 LYS A CD  1 
ATOM   1018 C  CE  . LYS A 1 126 ? 9.756  18.739  26.693  1.00 30.02 ? 127 LYS A CE  1 
ATOM   1019 N  NZ  . LYS A 1 126 ? 9.437  18.591  28.126  1.00 42.68 ? 127 LYS A NZ  1 
ATOM   1020 N  N   . TYR A 1 127 ? 10.165 20.030  21.140  1.00 7.88  ? 128 TYR A N   1 
ATOM   1021 C  CA  . TYR A 1 127 ? 11.529 20.289  20.690  1.00 7.62  ? 128 TYR A CA  1 
ATOM   1022 C  C   . TYR A 1 127 ? 11.575 20.697  19.227  1.00 8.39  ? 128 TYR A C   1 
ATOM   1023 O  O   . TYR A 1 127 ? 12.665 20.894  18.659  1.00 9.97  ? 128 TYR A O   1 
ATOM   1024 C  CB  . TYR A 1 127 ? 12.450 19.097  20.967  1.00 8.38  ? 128 TYR A CB  1 
ATOM   1025 C  CG  . TYR A 1 127 ? 12.522 18.779  22.430  1.00 9.89  ? 128 TYR A CG  1 
ATOM   1026 C  CD1 . TYR A 1 127 ? 12.915 19.764  23.337  1.00 12.06 ? 128 TYR A CD1 1 
ATOM   1027 C  CD2 . TYR A 1 127 ? 12.182 17.523  22.912  1.00 9.52  ? 128 TYR A CD2 1 
ATOM   1028 C  CE1 . TYR A 1 127 ? 12.955 19.494  24.697  1.00 15.00 ? 128 TYR A CE1 1 
ATOM   1029 C  CE2 . TYR A 1 127 ? 12.272 17.223  24.269  1.00 11.31 ? 128 TYR A CE2 1 
ATOM   1030 C  CZ  . TYR A 1 127 ? 12.686 18.226  25.147  1.00 13.61 ? 128 TYR A CZ  1 
ATOM   1031 O  OH  . TYR A 1 127 ? 12.740 17.963  26.482  1.00 17.29 ? 128 TYR A OH  1 
ATOM   1032 N  N   . GLY A 1 128 ? 10.412 20.849  18.589  1.00 8.85  ? 129 GLY A N   1 
ATOM   1033 C  CA  . GLY A 1 128 ? 10.333 21.550  17.295  1.00 9.36  ? 129 GLY A CA  1 
ATOM   1034 C  C   . GLY A 1 128 ? 10.732 20.752  16.046  1.00 8.52  ? 129 GLY A C   1 
ATOM   1035 O  O   . GLY A 1 128 ? 10.125 20.924  14.997  1.00 9.28  ? 129 GLY A O   1 
ATOM   1036 N  N   . ASP A 1 129 ? 11.785 19.902  16.131  1.00 7.98  ? 130 ASP A N   1 
ATOM   1037 C  CA  . ASP A 1 129 ? 12.119 19.006  15.035  1.00 8.28  ? 130 ASP A CA  1 
ATOM   1038 C  C   . ASP A 1 129 ? 12.813 17.767  15.613  1.00 7.34  ? 130 ASP A C   1 
ATOM   1039 O  O   . ASP A 1 129 ? 13.275 17.768  16.757  1.00 8.20  ? 130 ASP A O   1 
ATOM   1040 C  CB  . ASP A 1 129 ? 12.989 19.722  13.961  1.00 10.40 ? 130 ASP A CB  1 
ATOM   1041 C  CG  . ASP A 1 129 ? 14.394 20.121  14.409  1.00 12.63 ? 130 ASP A CG  1 
ATOM   1042 O  OD1 . ASP A 1 129 ? 15.250 19.260  14.577  1.00 16.81 ? 130 ASP A OD1 1 
ATOM   1043 O  OD2 . ASP A 1 129 ? 14.665 21.324  14.503  1.00 18.05 ? 130 ASP A OD2 1 
ATOM   1044 N  N   . TYR A 1 130 ? 12.882 16.723  14.796  1.00 7.70  ? 131 TYR A N   1 
ATOM   1045 C  CA  . TYR A 1 130 ? 13.421 15.483  15.335  1.00 8.04  ? 131 TYR A CA  1 
ATOM   1046 C  C   . TYR A 1 130 ? 14.904 15.584  15.620  1.00 7.94  ? 131 TYR A C   1 
ATOM   1047 O  O   . TYR A 1 130 ? 15.397 14.823  16.474  1.00 9.07  ? 131 TYR A O   1 
ATOM   1048 C  CB  . TYR A 1 130 ? 13.137 14.244  14.480  1.00 8.88  ? 131 TYR A CB  1 
ATOM   1049 C  CG  . TYR A 1 130 ? 13.703 14.285  13.097  1.00 11.19 ? 131 TYR A CG  1 
ATOM   1050 C  CD1 . TYR A 1 130 ? 15.031 13.942  12.845  1.00 14.41 ? 131 TYR A CD1 1 
ATOM   1051 C  CD2 . TYR A 1 130 ? 12.876 14.555  12.002  1.00 14.32 ? 131 TYR A CD2 1 
ATOM   1052 C  CE1 . TYR A 1 130 ? 15.548 13.937  11.547  1.00 19.96 ? 131 TYR A CE1 1 
ATOM   1053 C  CE2 . TYR A 1 130 ? 13.384 14.588  10.706  1.00 22.61 ? 131 TYR A CE2 1 
ATOM   1054 C  CZ  . TYR A 1 130 ? 14.721 14.282  10.484  1.00 21.15 ? 131 TYR A CZ  1 
ATOM   1055 O  OH  . TYR A 1 130 ? 15.201 14.249  9.221   1.00 29.46 ? 131 TYR A OH  1 
ATOM   1056 N  N   . GLY A 1 131 ? 15.627 16.476  14.888  1.00 8.70  ? 132 GLY A N   1 
ATOM   1057 C  CA  . GLY A 1 131 ? 17.051 16.563  15.154  1.00 10.59 ? 132 GLY A CA  1 
ATOM   1058 C  C   . GLY A 1 131 ? 17.312 17.153  16.546  1.00 8.70  ? 132 GLY A C   1 
ATOM   1059 O  O   . GLY A 1 131 ? 18.201 16.721  17.290  1.00 12.24 ? 132 GLY A O   1 
ATOM   1060 N  N   A LYS A 1 132 ? 16.503 18.153  16.915  0.50 9.69  ? 133 LYS A N   1 
ATOM   1061 N  N   B LYS A 1 132 ? 16.516 18.149  16.938  0.50 9.43  ? 133 LYS A N   1 
ATOM   1062 C  CA  A LYS A 1 132 ? 16.600 18.763  18.230  0.50 8.05  ? 133 LYS A CA  1 
ATOM   1063 C  CA  B LYS A 1 132 ? 16.713 18.695  18.268  0.50 8.35  ? 133 LYS A CA  1 
ATOM   1064 C  C   A LYS A 1 132 ? 16.153 17.780  19.306  0.50 7.64  ? 133 LYS A C   1 
ATOM   1065 C  C   B LYS A 1 132 ? 16.177 17.734  19.328  0.50 7.78  ? 133 LYS A C   1 
ATOM   1066 O  O   A LYS A 1 132 ? 16.745 17.689  20.378  0.50 10.26 ? 133 LYS A O   1 
ATOM   1067 O  O   B LYS A 1 132 ? 16.727 17.611  20.418  0.50 10.05 ? 133 LYS A O   1 
ATOM   1068 C  CB  A LYS A 1 132 ? 15.770 20.053  18.312  0.50 10.12 ? 133 LYS A CB  1 
ATOM   1069 C  CB  B LYS A 1 132 ? 16.088 20.085  18.436  0.50 8.79  ? 133 LYS A CB  1 
ATOM   1070 C  CG  A LYS A 1 132 ? 16.481 21.293  17.794  0.50 12.05 ? 133 LYS A CG  1 
ATOM   1071 C  CG  B LYS A 1 132 ? 16.108 20.572  19.873  0.50 11.50 ? 133 LYS A CG  1 
ATOM   1072 N  N   . ALA A 1 133 ? 15.082 17.040  18.998  1.00 6.54  ? 134 ALA A N   1 
ATOM   1073 C  CA  . ALA A 1 133 ? 14.515 16.085  19.943  1.00 6.89  ? 134 ALA A CA  1 
ATOM   1074 C  C   . ALA A 1 133 ? 15.509 14.988  20.313  1.00 7.77  ? 134 ALA A C   1 
ATOM   1075 O  O   . ALA A 1 133 ? 15.560 14.548  21.461  1.00 7.24  ? 134 ALA A O   1 
ATOM   1076 C  CB  . ALA A 1 133 ? 13.236 15.477  19.364  1.00 7.81  ? 134 ALA A CB  1 
ATOM   1077 N  N   . GLN A 1 134 ? 16.331 14.575  19.353  1.00 8.75  ? 135 GLN A N   1 
ATOM   1078 C  CA  . GLN A 1 134 ? 17.301 13.487  19.650  1.00 11.75 ? 135 GLN A CA  1 
ATOM   1079 C  C   . GLN A 1 134 ? 18.337 13.916  20.690  1.00 11.52 ? 135 GLN A C   1 
ATOM   1080 O  O   . GLN A 1 134 ? 19.033 13.039  21.223  1.00 21.18 ? 135 GLN A O   1 
ATOM   1081 C  CB  . GLN A 1 134 ? 18.153 13.214  18.428  1.00 19.76 ? 135 GLN A CB  1 
ATOM   1082 C  CG  . GLN A 1 134 ? 17.563 12.207  17.474  1.00 23.79 ? 135 GLN A CG  1 
ATOM   1083 C  CD  . GLN A 1 134 ? 18.546 12.331  16.352  1.00 27.95 ? 135 GLN A CD  1 
ATOM   1084 O  OE1 . GLN A 1 134 ? 19.680 11.919  16.464  1.00 25.35 ? 135 GLN A OE1 1 
ATOM   1085 N  NE2 . GLN A 1 134 ? 18.176 13.065  15.336  1.00 21.89 ? 135 GLN A NE2 1 
ATOM   1086 N  N   . GLN A 1 135 ? 18.490 15.213  20.917  1.00 13.57 ? 136 GLN A N   1 
ATOM   1087 C  CA  . GLN A 1 135 ? 19.456 15.689  21.885  1.00 17.99 ? 136 GLN A CA  1 
ATOM   1088 C  C   . GLN A 1 135 ? 18.898 15.777  23.298  1.00 14.29 ? 136 GLN A C   1 
ATOM   1089 O  O   . GLN A 1 135 ? 19.552 16.332  24.191  1.00 18.98 ? 136 GLN A O   1 
ATOM   1090 C  CB  . GLN A 1 135 ? 20.005 17.049  21.409  1.00 24.28 ? 136 GLN A CB  1 
ATOM   1091 C  CG  . GLN A 1 135 ? 20.530 17.036  19.971  1.00 32.04 ? 136 GLN A CG  1 
ATOM   1092 C  CD  . GLN A 1 135 ? 20.760 18.458  19.428  1.00 48.32 ? 136 GLN A CD  1 
ATOM   1093 O  OE1 . GLN A 1 135 ? 21.103 19.379  20.195  1.00 61.48 ? 136 GLN A OE1 1 
ATOM   1094 N  NE2 . GLN A 1 135 ? 20.557 18.652  18.077  1.00 38.50 ? 136 GLN A NE2 1 
ATOM   1095 N  N   . GLN A 1 136 ? 17.671 15.254  23.499  1.00 10.70 ? 137 GLN A N   1 
ATOM   1096 C  CA  . GLN A 1 136 ? 16.994 15.431  24.773  1.00 8.96  ? 137 GLN A CA  1 
ATOM   1097 C  C   . GLN A 1 136 ? 16.689 14.083  25.403  1.00 8.69  ? 137 GLN A C   1 
ATOM   1098 O  O   . GLN A 1 136 ? 16.345 13.149  24.671  1.00 8.38  ? 137 GLN A O   1 
ATOM   1099 C  CB  . GLN A 1 136 ? 15.692 16.215  24.644  1.00 10.87 ? 137 GLN A CB  1 
ATOM   1100 C  CG  . GLN A 1 136 ? 15.743 17.415  23.701  1.00 13.93 ? 137 GLN A CG  1 
ATOM   1101 C  CD  . GLN A 1 136 ? 16.836 18.385  24.075  1.00 15.90 ? 137 GLN A CD  1 
ATOM   1102 O  OE1 . GLN A 1 136 ? 17.067 18.617  25.260  1.00 18.62 ? 137 GLN A OE1 1 
ATOM   1103 N  NE2 . GLN A 1 136 ? 17.472 18.990  23.061  1.00 22.07 ? 137 GLN A NE2 1 
ATOM   1104 N  N   . PRO A 1 137 ? 16.678 13.984  26.753  1.00 8.82  ? 138 PRO A N   1 
ATOM   1105 C  CA  . PRO A 1 137 ? 16.464 12.681  27.361  1.00 10.60 ? 138 PRO A CA  1 
ATOM   1106 C  C   . PRO A 1 137 ? 15.064 12.128  27.162  1.00 9.86  ? 138 PRO A C   1 
ATOM   1107 O  O   . PRO A 1 137 ? 14.898 10.904  27.211  1.00 13.70 ? 138 PRO A O   1 
ATOM   1108 C  CB  . PRO A 1 137 ? 16.653 12.922  28.876  1.00 16.37 ? 138 PRO A CB  1 
ATOM   1109 C  CG  . PRO A 1 137 ? 16.701 14.419  29.031  1.00 21.96 ? 138 PRO A CG  1 
ATOM   1110 C  CD  . PRO A 1 137 ? 17.115 15.027  27.695  1.00 13.95 ? 138 PRO A CD  1 
ATOM   1111 N  N   . ASP A 1 138 ? 14.117 13.036  26.828  1.00 8.24  ? 139 ASP A N   1 
ATOM   1112 C  CA  . ASP A 1 138 ? 12.711 12.672  26.580  1.00 11.28 ? 139 ASP A CA  1 
ATOM   1113 C  C   . ASP A 1 138 ? 12.341 13.083  25.158  1.00 7.88  ? 139 ASP A C   1 
ATOM   1114 O  O   . ASP A 1 138 ? 11.220 13.499  24.893  1.00 11.03 ? 139 ASP A O   1 
ATOM   1115 C  CB  . ASP A 1 138 ? 11.740 13.332  27.581  1.00 13.82 ? 139 ASP A CB  1 
ATOM   1116 C  CG  . ASP A 1 138 ? 11.843 14.845  27.594  1.00 15.66 ? 139 ASP A CG  1 
ATOM   1117 O  OD1 . ASP A 1 138 ? 12.790 15.407  27.011  1.00 14.93 ? 139 ASP A OD1 1 
ATOM   1118 O  OD2 . ASP A 1 138 ? 11.012 15.461  28.285  1.00 17.58 ? 139 ASP A OD2 1 
ATOM   1119 N  N   . GLY A 1 139 ? 13.275 13.004  24.221  1.00 5.98  ? 140 GLY A N   1 
ATOM   1120 C  CA  . GLY A 1 139 ? 13.022 13.542  22.927  1.00 6.09  ? 140 GLY A CA  1 
ATOM   1121 C  C   . GLY A 1 139 ? 12.177 12.644  22.018  1.00 4.90  ? 140 GLY A C   1 
ATOM   1122 O  O   . GLY A 1 139 ? 11.502 13.171  21.116  1.00 5.62  ? 140 GLY A O   1 
ATOM   1123 N  N   . LEU A 1 140 ? 12.370 11.338  22.099  1.00 4.92  ? 141 LEU A N   1 
ATOM   1124 C  CA  . LEU A 1 140 ? 11.735 10.397  21.185  1.00 4.92  ? 141 LEU A CA  1 
ATOM   1125 C  C   . LEU A 1 140 ? 10.902 9.425   21.985  1.00 4.81  ? 141 LEU A C   1 
ATOM   1126 O  O   . LEU A 1 140 ? 11.199 9.129   23.154  1.00 5.36  ? 141 LEU A O   1 
ATOM   1127 C  CB  . LEU A 1 140 ? 12.764 9.594   20.359  1.00 5.80  ? 141 LEU A CB  1 
ATOM   1128 C  CG  . LEU A 1 140 ? 13.724 10.403  19.508  1.00 7.83  ? 141 LEU A CG  1 
ATOM   1129 C  CD1 . LEU A 1 140 ? 14.656 9.472   18.743  1.00 10.14 ? 141 LEU A CD1 1 
ATOM   1130 C  CD2 . LEU A 1 140 ? 13.057 11.364  18.557  1.00 9.69  ? 141 LEU A CD2 1 
ATOM   1131 N  N   . ALA A 1 141 ? 9.890  8.881   21.315  1.00 4.81  ? 142 ALA A N   1 
ATOM   1132 C  CA  . ALA A 1 141 ? 9.130  7.755   21.849  1.00 4.77  ? 142 ALA A CA  1 
ATOM   1133 C  C   . ALA A 1 141 ? 9.021  6.735   20.728  1.00 3.33  ? 142 ALA A C   1 
ATOM   1134 O  O   . ALA A 1 141 ? 8.621  7.104   19.617  1.00 5.14  ? 142 ALA A O   1 
ATOM   1135 C  CB  . ALA A 1 141 ? 7.725  8.144   22.319  1.00 6.36  ? 142 ALA A CB  1 
ATOM   1136 N  N   . VAL A 1 142 ? 9.466  5.498   21.019  1.00 4.39  ? 143 VAL A N   1 
ATOM   1137 C  CA  . VAL A 1 142 ? 9.376  4.473   20.006  1.00 4.73  ? 143 VAL A CA  1 
ATOM   1138 C  C   . VAL A 1 142 ? 8.385  3.444   20.506  1.00 4.34  ? 143 VAL A C   1 
ATOM   1139 O  O   . VAL A 1 142 ? 8.521  2.921   21.601  1.00 4.72  ? 143 VAL A O   1 
ATOM   1140 C  CB  . VAL A 1 142 ? 10.742 3.841   19.668  1.00 4.30  ? 143 VAL A CB  1 
ATOM   1141 C  CG1 . VAL A 1 142 ? 10.562 2.834   18.548  1.00 4.80  ? 143 VAL A CG1 1 
ATOM   1142 C  CG2 . VAL A 1 142 ? 11.743 4.941   19.244  1.00 6.08  ? 143 VAL A CG2 1 
ATOM   1143 N  N   . LEU A 1 143 ? 7.384  3.196   19.661  1.00 3.90  ? 144 LEU A N   1 
ATOM   1144 C  CA  . LEU A 1 143 ? 6.397  2.155   19.916  1.00 4.49  ? 144 LEU A CA  1 
ATOM   1145 C  C   . LEU A 1 143 ? 6.898  0.876   19.241  1.00 3.98  ? 144 LEU A C   1 
ATOM   1146 O  O   . LEU A 1 143 ? 7.039  0.848   18.010  1.00 5.53  ? 144 LEU A O   1 
ATOM   1147 C  CB  . LEU A 1 143 ? 5.046  2.622   19.362  1.00 6.25  ? 144 LEU A CB  1 
ATOM   1148 C  CG  . LEU A 1 143 ? 3.902  1.626   19.486  1.00 6.47  ? 144 LEU A CG  1 
ATOM   1149 C  CD1 . LEU A 1 143 ? 3.638  1.356   20.954  1.00 7.97  ? 144 LEU A CD1 1 
ATOM   1150 C  CD2 . LEU A 1 143 ? 2.646  2.229   18.846  1.00 8.53  ? 144 LEU A CD2 1 
ATOM   1151 N  N   . GLY A 1 144 ? 7.151  -0.161  20.010  1.00 3.98  ? 145 GLY A N   1 
ATOM   1152 C  CA  . GLY A 1 144 ? 7.661  -1.425  19.511  1.00 4.35  ? 145 GLY A CA  1 
ATOM   1153 C  C   . GLY A 1 144 ? 6.598  -2.523  19.525  1.00 3.80  ? 145 GLY A C   1 
ATOM   1154 O  O   . GLY A 1 144 ? 5.863  -2.636  20.527  1.00 5.39  ? 145 GLY A O   1 
ATOM   1155 N  N   . ILE A 1 145 ? 6.531  -3.288  18.447  1.00 3.98  ? 146 ILE A N   1 
ATOM   1156 C  CA  . ILE A 1 145 ? 5.493  -4.308  18.260  1.00 4.21  ? 146 ILE A CA  1 
ATOM   1157 C  C   . ILE A 1 145 ? 6.222  -5.559  17.764  1.00 4.07  ? 146 ILE A C   1 
ATOM   1158 O  O   . ILE A 1 145 ? 6.943  -5.525  16.755  1.00 5.02  ? 146 ILE A O   1 
ATOM   1159 C  CB  . ILE A 1 145 ? 4.414  -3.853  17.262  1.00 4.68  ? 146 ILE A CB  1 
ATOM   1160 C  CG1 . ILE A 1 145 ? 3.786  -2.536  17.743  1.00 6.81  ? 146 ILE A CG1 1 
ATOM   1161 C  CG2 . ILE A 1 145 ? 3.388  -4.941  17.043  1.00 6.87  ? 146 ILE A CG2 1 
ATOM   1162 C  CD1 . ILE A 1 145 ? 2.757  -1.892  16.795  1.00 7.26  ? 146 ILE A CD1 1 
ATOM   1163 N  N   . PHE A 1 146 ? 6.034  -6.676  18.456  1.00 4.07  ? 147 PHE A N   1 
ATOM   1164 C  CA  . PHE A 1 146 ? 6.653  -7.933  18.057  1.00 4.37  ? 147 PHE A CA  1 
ATOM   1165 C  C   . PHE A 1 146 ? 5.896  -8.572  16.891  1.00 4.63  ? 147 PHE A C   1 
ATOM   1166 O  O   . PHE A 1 146 ? 4.660  -8.420  16.796  1.00 6.13  ? 147 PHE A O   1 
ATOM   1167 C  CB  . PHE A 1 146 ? 6.653  -8.924  19.208  1.00 4.84  ? 147 PHE A CB  1 
ATOM   1168 C  CG  . PHE A 1 146 ? 7.489  -8.459  20.359  1.00 3.60  ? 147 PHE A CG  1 
ATOM   1169 C  CD1 . PHE A 1 146 ? 8.879  -8.294  20.188  1.00 5.00  ? 147 PHE A CD1 1 
ATOM   1170 C  CD2 . PHE A 1 146 ? 6.927  -8.182  21.592  1.00 4.80  ? 147 PHE A CD2 1 
ATOM   1171 C  CE1 . PHE A 1 146 ? 9.676  -7.929  21.292  1.00 5.12  ? 147 PHE A CE1 1 
ATOM   1172 C  CE2 . PHE A 1 146 ? 7.705  -7.800  22.665  1.00 5.24  ? 147 PHE A CE2 1 
ATOM   1173 C  CZ  . PHE A 1 146 ? 9.084  -7.686  22.519  1.00 5.84  ? 147 PHE A CZ  1 
ATOM   1174 N  N   . LEU A 1 147 ? 6.622  -9.240  15.990  1.00 4.51  ? 148 LEU A N   1 
ATOM   1175 C  CA  . LEU A 1 147 ? 6.022  -10.004 14.909  1.00 4.43  ? 148 LEU A CA  1 
ATOM   1176 C  C   . LEU A 1 147 ? 6.333  -11.485 15.148  1.00 4.62  ? 148 LEU A C   1 
ATOM   1177 O  O   . LEU A 1 147 ? 7.498  -11.849 15.301  1.00 5.82  ? 148 LEU A O   1 
ATOM   1178 C  CB  . LEU A 1 147 ? 6.602  -9.648  13.533  1.00 5.64  ? 148 LEU A CB  1 
ATOM   1179 C  CG  . LEU A 1 147 ? 6.070  -8.377  12.909  1.00 5.51  ? 148 LEU A CG  1 
ATOM   1180 C  CD1 . LEU A 1 147 ? 6.264  -7.106  13.773  1.00 7.36  ? 148 LEU A CD1 1 
ATOM   1181 C  CD2 . LEU A 1 147 ? 6.707  -8.158  11.517  1.00 6.83  ? 148 LEU A CD2 1 
ATOM   1182 N  N   . LYS A 1 148 ? 5.289  -12.329 15.155  1.00 6.35  ? 149 LYS A N   1 
ATOM   1183 C  CA  . LYS A 1 148 ? 5.464  -13.764 15.141  1.00 7.52  ? 149 LYS A CA  1 
ATOM   1184 C  C   . LYS A 1 148 ? 4.971  -14.304 13.806  1.00 7.05  ? 149 LYS A C   1 
ATOM   1185 O  O   . LYS A 1 148 ? 4.112  -13.715 13.181  1.00 10.37 ? 149 LYS A O   1 
ATOM   1186 C  CB  . LYS A 1 148 ? 4.739  -14.444 16.299  1.00 11.43 ? 149 LYS A CB  1 
ATOM   1187 C  CG  . LYS A 1 148 ? 3.219  -14.277 16.304  1.00 12.66 ? 149 LYS A CG  1 
ATOM   1188 C  CD  . LYS A 1 148 ? 2.634  -15.024 17.530  1.00 18.34 ? 149 LYS A CD  1 
ATOM   1189 C  CE  . LYS A 1 148 ? 1.155  -15.348 17.356  1.00 27.83 ? 149 LYS A CE  1 
ATOM   1190 N  NZ  . LYS A 1 148 ? 0.533  -15.728 18.657  1.00 37.17 ? 149 LYS A NZ  1 
ATOM   1191 N  N   . VAL A 1 149 ? 5.549  -15.409 13.371  1.00 9.10  ? 150 VAL A N   1 
ATOM   1192 C  CA  . VAL A 1 149 ? 5.139  -16.055 12.129  1.00 9.34  ? 150 VAL A CA  1 
ATOM   1193 C  C   . VAL A 1 149 ? 3.916  -16.955 12.340  1.00 10.09 ? 150 VAL A C   1 
ATOM   1194 O  O   . VAL A 1 149 ? 3.954  -17.892 13.142  1.00 11.59 ? 150 VAL A O   1 
ATOM   1195 C  CB  . VAL A 1 149 ? 6.355  -16.780 11.504  1.00 9.20  ? 150 VAL A CB  1 
ATOM   1196 C  CG1 . VAL A 1 149 ? 5.906  -17.563 10.262  1.00 11.25 ? 150 VAL A CG1 1 
ATOM   1197 C  CG2 . VAL A 1 149 ? 7.421  -15.781 11.126  1.00 11.92 ? 150 VAL A CG2 1 
ATOM   1198 N  N   . GLY A 1 150 ? 2.861  -16.682 11.585  1.00 10.24 ? 151 GLY A N   1 
ATOM   1199 C  CA  . GLY A 1 150 ? 1.666  -17.515 11.617  1.00 9.92  ? 151 GLY A CA  1 
ATOM   1200 C  C   . GLY A 1 150 ? 0.793  -17.084 10.439  1.00 9.24  ? 151 GLY A C   1 
ATOM   1201 O  O   . GLY A 1 150 ? 1.179  -17.203 9.278   1.00 10.57 ? 151 GLY A O   1 
ATOM   1202 N  N   A SER A 1 151 ? -0.356 -16.508 10.781  0.50 10.38 ? 152 SER A N   1 
ATOM   1203 N  N   B SER A 1 151 ? -0.423 -16.630 10.738  0.50 9.63  ? 152 SER A N   1 
ATOM   1204 C  CA  A SER A 1 151 ? -1.281 -15.942 9.796   0.50 10.35 ? 152 SER A CA  1 
ATOM   1205 C  CA  B SER A 1 151 ? -1.293 -16.072 9.697   0.50 10.37 ? 152 SER A CA  1 
ATOM   1206 C  C   A SER A 1 151 ? -0.733 -14.655 9.182   0.50 9.41  ? 152 SER A C   1 
ATOM   1207 C  C   B SER A 1 151 ? -0.680 -14.784 9.135   0.50 9.25  ? 152 SER A C   1 
ATOM   1208 O  O   A SER A 1 151 ? -0.088 -13.864 9.867   0.50 8.94  ? 152 SER A O   1 
ATOM   1209 O  O   B SER A 1 151 ? 0.116  -14.137 9.808   0.50 9.71  ? 152 SER A O   1 
ATOM   1210 C  CB  A SER A 1 151 ? -2.613 -15.654 10.442  0.50 12.50 ? 152 SER A CB  1 
ATOM   1211 C  CB  B SER A 1 151 ? -2.698 -15.818 10.245  0.50 13.38 ? 152 SER A CB  1 
ATOM   1212 O  OG  A SER A 1 151 ? -3.247 -16.865 10.764  0.50 14.76 ? 152 SER A OG  1 
ATOM   1213 O  OG  B SER A 1 151 ? -2.692 -14.719 11.160  0.50 15.70 ? 152 SER A OG  1 
ATOM   1214 N  N   . ALA A 1 152 ? -1.051 -14.395 7.911   1.00 9.70  ? 153 ALA A N   1 
ATOM   1215 C  CA  . ALA A 1 152 ? -0.617 -13.136 7.295   1.00 10.15 ? 153 ALA A CA  1 
ATOM   1216 C  C   . ALA A 1 152 ? -1.222 -11.929 8.014   1.00 9.77  ? 153 ALA A C   1 
ATOM   1217 O  O   . ALA A 1 152 ? -2.330 -11.989 8.581   1.00 11.69 ? 153 ALA A O   1 
ATOM   1218 C  CB  . ALA A 1 152 ? -0.997 -13.040 5.820   1.00 12.46 ? 153 ALA A CB  1 
ATOM   1219 N  N   . LYS A 1 153 ? -0.553 -10.792 7.932   1.00 9.69  ? 154 LYS A N   1 
ATOM   1220 C  CA  . LYS A 1 153 ? -1.064 -9.523  8.429   1.00 8.92  ? 154 LYS A CA  1 
ATOM   1221 C  C   . LYS A 1 153 ? -1.477 -8.721  7.203   1.00 9.11  ? 154 LYS A C   1 
ATOM   1222 O  O   . LYS A 1 153 ? -0.638 -8.282  6.389   1.00 9.33  ? 154 LYS A O   1 
ATOM   1223 C  CB  . LYS A 1 153 ? 0.008  -8.753  9.215   1.00 8.91  ? 154 LYS A CB  1 
ATOM   1224 C  CG  . LYS A 1 153 ? -0.442 -7.488  9.926   1.00 11.01 ? 154 LYS A CG  1 
ATOM   1225 C  CD  . LYS A 1 153 ? -1.336 -7.871  11.102  1.00 11.82 ? 154 LYS A CD  1 
ATOM   1226 C  CE  . LYS A 1 153 ? -1.511 -6.685  12.001  1.00 13.23 ? 154 LYS A CE  1 
ATOM   1227 N  NZ  . LYS A 1 153 ? -2.456 -7.082  13.034  1.00 15.69 ? 154 LYS A NZ  1 
ATOM   1228 N  N   . PRO A 1 154 ? -2.791 -8.595  6.914   1.00 10.30 ? 155 PRO A N   1 
ATOM   1229 C  CA  . PRO A 1 154 ? -3.230 -7.985  5.640   1.00 12.53 ? 155 PRO A CA  1 
ATOM   1230 C  C   . PRO A 1 154 ? -2.679 -6.564  5.524   1.00 9.95  ? 155 PRO A C   1 
ATOM   1231 O  O   . PRO A 1 154 ? -2.257 -6.171  4.444   1.00 13.05 ? 155 PRO A O   1 
ATOM   1232 C  CB  . PRO A 1 154 ? -4.754 -7.998  5.729   1.00 15.81 ? 155 PRO A CB  1 
ATOM   1233 C  CG  . PRO A 1 154 ? -5.041 -9.123  6.729   1.00 19.78 ? 155 PRO A CG  1 
ATOM   1234 C  CD  . PRO A 1 154 ? -3.901 -9.180  7.709   1.00 12.78 ? 155 PRO A CD  1 
ATOM   1235 N  N   . GLY A 1 155 ? -2.583 -5.833  6.640   1.00 9.72  ? 156 GLY A N   1 
ATOM   1236 C  CA  . GLY A 1 155 ? -2.146 -4.442  6.633   1.00 11.50 ? 156 GLY A CA  1 
ATOM   1237 C  C   . GLY A 1 155 ? -0.663 -4.255  6.350   1.00 10.67 ? 156 GLY A C   1 
ATOM   1238 O  O   . GLY A 1 155 ? -0.205 -3.143  6.111   1.00 15.25 ? 156 GLY A O   1 
ATOM   1239 N  N   . LEU A 1 156 ? 0.077  -5.363  6.391   1.00 9.06  ? 157 LEU A N   1 
ATOM   1240 C  CA  . LEU A 1 156 ? 1.491  -5.326  6.041   1.00 8.74  ? 157 LEU A CA  1 
ATOM   1241 C  C   . LEU A 1 156 ? 1.702  -5.580  4.564   1.00 8.92  ? 157 LEU A C   1 
ATOM   1242 O  O   . LEU A 1 156 ? 2.807  -5.304  4.063   1.00 9.66  ? 157 LEU A O   1 
ATOM   1243 C  CB  . LEU A 1 156 ? 2.237  -6.369  6.891   1.00 9.04  ? 157 LEU A CB  1 
ATOM   1244 C  CG  . LEU A 1 156 ? 3.754  -6.502  6.692   1.00 9.71  ? 157 LEU A CG  1 
ATOM   1245 C  CD1 . LEU A 1 156 ? 4.511  -5.203  7.046   1.00 10.32 ? 157 LEU A CD1 1 
ATOM   1246 C  CD2 . LEU A 1 156 ? 4.302  -7.633  7.552   1.00 11.75 ? 157 LEU A CD2 1 
ATOM   1247 N  N   . GLN A 1 157 ? 0.721  -6.124  3.831   1.00 8.84  ? 158 GLN A N   1 
ATOM   1248 C  CA  . GLN A 1 157 ? 1.024  -6.613  2.494   1.00 10.29 ? 158 GLN A CA  1 
ATOM   1249 C  C   . GLN A 1 157 ? 1.475  -5.483  1.561   1.00 10.42 ? 158 GLN A C   1 
ATOM   1250 O  O   . GLN A 1 157 ? 2.312  -5.750  0.695   1.00 11.31 ? 158 GLN A O   1 
ATOM   1251 C  CB  . GLN A 1 157 ? -0.112 -7.436  1.911   1.00 12.22 ? 158 GLN A CB  1 
ATOM   1252 C  CG  . GLN A 1 157 ? 0.277  -8.189  0.634   1.00 14.14 ? 158 GLN A CG  1 
ATOM   1253 C  CD  . GLN A 1 157 ? 1.403  -9.181  0.832   1.00 12.83 ? 158 GLN A CD  1 
ATOM   1254 O  OE1 . GLN A 1 157 ? 1.570  -9.738  1.909   1.00 12.74 ? 158 GLN A OE1 1 
ATOM   1255 N  NE2 . GLN A 1 157 ? 2.217  -9.420  -0.195  1.00 14.40 ? 158 GLN A NE2 1 
ATOM   1256 N  N   A LYS A 1 158 ? 0.906  -4.262  1.680   0.50 10.88 ? 159 LYS A N   1 
ATOM   1257 N  N   B LYS A 1 158 ? 0.917  -4.264  1.673   0.50 10.41 ? 159 LYS A N   1 
ATOM   1258 C  CA  A LYS A 1 158 ? 1.279  -3.138  0.818   0.50 10.80 ? 159 LYS A CA  1 
ATOM   1259 C  CA  B LYS A 1 158 ? 1.312  -3.185  0.769   0.50 9.97  ? 159 LYS A CA  1 
ATOM   1260 C  C   A LYS A 1 158 ? 2.780  -2.857  0.956   0.50 9.58  ? 159 LYS A C   1 
ATOM   1261 C  C   B LYS A 1 158 ? 2.799  -2.858  0.950   0.50 9.17  ? 159 LYS A C   1 
ATOM   1262 O  O   A LYS A 1 158 ? 3.444  -2.488  -0.013  0.50 12.37 ? 159 LYS A O   1 
ATOM   1263 O  O   B LYS A 1 158 ? 3.474  -2.466  -0.001  0.50 11.89 ? 159 LYS A O   1 
ATOM   1264 C  CB  A LYS A 1 158 ? 0.468  -1.878  1.162   0.50 15.11 ? 159 LYS A CB  1 
ATOM   1265 C  CB  B LYS A 1 158 ? 0.409  -1.963  0.961   0.50 12.69 ? 159 LYS A CB  1 
ATOM   1266 C  CG  A LYS A 1 158 ? 0.676  -0.686  0.227   0.50 20.23 ? 159 LYS A CG  1 
ATOM   1267 C  CG  B LYS A 1 158 ? -0.925 -2.081  0.242   0.50 13.10 ? 159 LYS A CG  1 
ATOM   1268 N  N   . VAL A 1 159 ? 3.304  -3.035  2.175   1.00 8.95  ? 160 VAL A N   1 
ATOM   1269 C  CA  . VAL A 1 159 ? 4.715  -2.830  2.454   1.00 7.53  ? 160 VAL A CA  1 
ATOM   1270 C  C   . VAL A 1 159 ? 5.516  -3.952  1.784   1.00 9.63  ? 160 VAL A C   1 
ATOM   1271 O  O   . VAL A 1 159 ? 6.456  -3.690  1.034   1.00 10.30 ? 160 VAL A O   1 
ATOM   1272 C  CB  . VAL A 1 159 ? 4.996  -2.793  3.940   1.00 9.15  ? 160 VAL A CB  1 
ATOM   1273 C  CG1 . VAL A 1 159 ? 6.510  -2.837  4.201   1.00 11.24 ? 160 VAL A CG1 1 
ATOM   1274 C  CG2 . VAL A 1 159 ? 4.303  -1.619  4.617   1.00 11.34 ? 160 VAL A CG2 1 
ATOM   1275 N  N   . VAL A 1 160 ? 5.128  -5.202  2.027   1.00 9.69  ? 161 VAL A N   1 
ATOM   1276 C  CA  . VAL A 1 160 ? 5.844  -6.333  1.454   1.00 13.36 ? 161 VAL A CA  1 
ATOM   1277 C  C   . VAL A 1 160 ? 5.898  -6.218  -0.068  1.00 11.06 ? 161 VAL A C   1 
ATOM   1278 O  O   . VAL A 1 160 ? 6.934  -6.488  -0.690  1.00 12.93 ? 161 VAL A O   1 
ATOM   1279 C  CB  . VAL A 1 160 ? 5.183  -7.680  1.922   1.00 17.15 ? 161 VAL A CB  1 
ATOM   1280 C  CG1 . VAL A 1 160 ? 5.529  -8.960  1.123   1.00 18.95 ? 161 VAL A CG1 1 
ATOM   1281 C  CG2 . VAL A 1 160 ? 5.462  -7.849  3.413   1.00 20.39 ? 161 VAL A CG2 1 
ATOM   1282 N  N   . ASP A 1 161 ? 4.781  -5.790  -0.690  1.00 11.27 ? 162 ASP A N   1 
ATOM   1283 C  CA  . ASP A 1 161 ? 4.745  -5.841  -2.138  1.00 14.76 ? 162 ASP A CA  1 
ATOM   1284 C  C   . ASP A 1 161 ? 5.633  -4.806  -2.824  1.00 15.35 ? 162 ASP A C   1 
ATOM   1285 O  O   . ASP A 1 161 ? 5.857  -4.954  -4.046  1.00 19.71 ? 162 ASP A O   1 
ATOM   1286 C  CB  . ASP A 1 161 ? 3.314  -5.737  -2.570  1.00 19.50 ? 162 ASP A CB  1 
ATOM   1287 C  CG  . ASP A 1 161 ? 2.727  -7.146  -2.571  1.00 28.43 ? 162 ASP A CG  1 
ATOM   1288 O  OD1 . ASP A 1 161 ? 3.533  -8.149  -2.607  1.00 33.93 ? 162 ASP A OD1 1 
ATOM   1289 O  OD2 . ASP A 1 161 ? 1.508  -7.246  -2.475  1.00 31.61 ? 162 ASP A OD2 1 
ATOM   1290 N  N   . VAL A 1 162 ? 6.058  -3.727  -2.120  1.00 12.85 ? 163 VAL A N   1 
ATOM   1291 C  CA  . VAL A 1 162 ? 6.884  -2.724  -2.778  1.00 13.58 ? 163 VAL A CA  1 
ATOM   1292 C  C   . VAL A 1 162 ? 8.375  -3.009  -2.566  1.00 12.02 ? 163 VAL A C   1 
ATOM   1293 O  O   . VAL A 1 162 ? 9.211  -2.311  -3.121  1.00 13.44 ? 163 VAL A O   1 
ATOM   1294 C  CB  . VAL A 1 162 ? 6.535  -1.322  -2.223  1.00 14.74 ? 163 VAL A CB  1 
ATOM   1295 C  CG1 . VAL A 1 162 ? 7.118  -1.043  -0.836  1.00 14.50 ? 163 VAL A CG1 1 
ATOM   1296 C  CG2 . VAL A 1 162 ? 6.871  -0.171  -3.174  1.00 20.82 ? 163 VAL A CG2 1 
ATOM   1297 N  N   . LEU A 1 163 ? 8.753  -3.971  -1.701  1.00 11.78 ? 164 LEU A N   1 
ATOM   1298 C  CA  . LEU A 1 163 ? 10.146 -4.186  -1.314  1.00 10.21 ? 164 LEU A CA  1 
ATOM   1299 C  C   . LEU A 1 163 ? 11.037 -4.525  -2.506  1.00 12.02 ? 164 LEU A C   1 
ATOM   1300 O  O   . LEU A 1 163 ? 12.188 -4.084  -2.529  1.00 11.59 ? 164 LEU A O   1 
ATOM   1301 C  CB  . LEU A 1 163 ? 10.296 -5.235  -0.218  1.00 10.19 ? 164 LEU A CB  1 
ATOM   1302 C  CG  . LEU A 1 163 ? 9.606  -4.845  1.105   1.00 9.60  ? 164 LEU A CG  1 
ATOM   1303 C  CD1 . LEU A 1 163 ? 9.854  -5.966  2.129   1.00 11.14 ? 164 LEU A CD1 1 
ATOM   1304 C  CD2 . LEU A 1 163 ? 10.144 -3.535  1.639   1.00 11.10 ? 164 LEU A CD2 1 
ATOM   1305 N  N   . ASP A 1 164 ? 10.493 -5.188  -3.534  1.00 14.65 ? 165 ASP A N   1 
ATOM   1306 C  CA  . ASP A 1 164 ? 11.348 -5.466  -4.697  1.00 15.84 ? 165 ASP A CA  1 
ATOM   1307 C  C   . ASP A 1 164 ? 11.785 -4.176  -5.408  1.00 15.97 ? 165 ASP A C   1 
ATOM   1308 O  O   . ASP A 1 164 ? 12.807 -4.174  -6.084  1.00 23.73 ? 165 ASP A O   1 
ATOM   1309 C  CB  . ASP A 1 164 ? 10.657 -6.402  -5.693  1.00 25.32 ? 165 ASP A CB  1 
ATOM   1310 C  CG  . ASP A 1 164 ? 9.607  -5.659  -6.511  1.00 33.45 ? 165 ASP A CG  1 
ATOM   1311 O  OD1 . ASP A 1 164 ? 8.632  -5.144  -5.886  1.00 31.46 ? 165 ASP A OD1 1 
ATOM   1312 O  OD2 . ASP A 1 164 ? 9.774  -5.562  -7.765  1.00 46.51 ? 165 ASP A OD2 1 
ATOM   1313 N  N   . SER A 1 165 ? 11.079 -3.063  -5.201  1.00 14.01 ? 166 SER A N   1 
ATOM   1314 C  CA  . SER A 1 165 ? 11.486 -1.834  -5.865  1.00 15.88 ? 166 SER A CA  1 
ATOM   1315 C  C   . SER A 1 165 ? 12.529 -1.062  -5.049  1.00 11.94 ? 166 SER A C   1 
ATOM   1316 O  O   . SER A 1 165 ? 13.063 -0.075  -5.554  1.00 14.86 ? 166 SER A O   1 
ATOM   1317 C  CB  . SER A 1 165 ? 10.266 -0.991  -6.215  1.00 23.49 ? 166 SER A CB  1 
ATOM   1318 O  OG  . SER A 1 165 ? 9.788  -0.420  -5.021  1.00 22.21 ? 166 SER A OG  1 
ATOM   1319 N  N   . ILE A 1 166 ? 12.838 -1.521  -3.826  1.00 10.64 ? 167 ILE A N   1 
ATOM   1320 C  CA  . ILE A 1 166 ? 13.850 -0.882  -2.996  1.00 9.46  ? 167 ILE A CA  1 
ATOM   1321 C  C   . ILE A 1 166 ? 14.851 -1.929  -2.487  1.00 7.57  ? 167 ILE A C   1 
ATOM   1322 O  O   . ILE A 1 166 ? 15.263 -1.899  -1.319  1.00 9.52  ? 167 ILE A O   1 
ATOM   1323 C  CB  . ILE A 1 166 ? 13.250 -0.042  -1.850  1.00 9.61  ? 167 ILE A CB  1 
ATOM   1324 C  CG1 . ILE A 1 166 ? 12.425 -0.903  -0.920  1.00 9.79  ? 167 ILE A CG1 1 
ATOM   1325 C  CG2 . ILE A 1 166 ? 12.461 1.161   -2.391  1.00 11.35 ? 167 ILE A CG2 1 
ATOM   1326 C  CD1 . ILE A 1 166 ? 12.370 -0.318  0.473   1.00 10.98 ? 167 ILE A CD1 1 
ATOM   1327 N  N   . LYS A 1 167 ? 15.264 -2.813  -3.400  1.00 9.24  ? 168 LYS A N   1 
ATOM   1328 C  CA  . LYS A 1 167 ? 16.067 -3.953  -2.988  1.00 8.04  ? 168 LYS A CA  1 
ATOM   1329 C  C   . LYS A 1 167 ? 17.383 -3.530  -2.324  1.00 7.86  ? 168 LYS A C   1 
ATOM   1330 O  O   . LYS A 1 167 ? 17.846 -4.219  -1.390  1.00 9.00  ? 168 LYS A O   1 
ATOM   1331 C  CB  . LYS A 1 167 ? 16.390 -4.842  -4.215  1.00 10.66 ? 168 LYS A CB  1 
ATOM   1332 C  CG  . LYS A 1 167 ? 17.110 -6.128  -3.818  1.00 12.99 ? 168 LYS A CG  1 
ATOM   1333 C  CD  . LYS A 1 167 ? 17.337 -7.025  -5.033  1.00 17.98 ? 168 LYS A CD  1 
ATOM   1334 C  CE  . LYS A 1 167 ? 18.215 -8.204  -4.658  1.00 22.45 ? 168 LYS A CE  1 
ATOM   1335 N  NZ  . LYS A 1 167 ? 18.307 -9.200  -5.758  1.00 35.05 ? 168 LYS A NZ  1 
ATOM   1336 N  N   . THR A 1 168 ? 18.039 -2.481  -2.858  1.00 9.06  ? 169 THR A N   1 
ATOM   1337 C  CA  . THR A 1 168 ? 19.385 -2.135  -2.477  1.00 8.76  ? 169 THR A CA  1 
ATOM   1338 C  C   . THR A 1 168 ? 19.436 -0.779  -1.784  1.00 8.11  ? 169 THR A C   1 
ATOM   1339 O  O   . THR A 1 168 ? 18.527 0.083   -1.868  1.00 8.63  ? 169 THR A O   1 
ATOM   1340 C  CB  . THR A 1 168 ? 20.339 -2.174  -3.681  1.00 9.77  ? 169 THR A CB  1 
ATOM   1341 O  OG1 . THR A 1 168 ? 19.742 -1.403  -4.723  1.00 11.61 ? 169 THR A OG1 1 
ATOM   1342 C  CG2 . THR A 1 168 ? 20.507 -3.621  -4.117  1.00 12.59 ? 169 THR A CG2 1 
ATOM   1343 N  N   A LYS A 1 169 ? 20.489 -0.627  -0.992  0.50 8.68  ? 170 LYS A N   1 
ATOM   1344 N  N   B LYS A 1 169 ? 20.536 -0.588  -1.069  0.50 9.44  ? 170 LYS A N   1 
ATOM   1345 C  CA  A LYS A 1 169 ? 20.738 0.584   -0.226  0.50 8.75  ? 170 LYS A CA  1 
ATOM   1346 C  CA  B LYS A 1 169 ? 20.769 0.584   -0.240  0.50 9.35  ? 170 LYS A CA  1 
ATOM   1347 C  C   A LYS A 1 169 ? 20.610 1.844   -1.081  0.50 8.47  ? 170 LYS A C   1 
ATOM   1348 C  C   B LYS A 1 169 ? 20.700 1.889   -1.033  0.50 9.19  ? 170 LYS A C   1 
ATOM   1349 O  O   A LYS A 1 169 ? 21.158 1.907   -2.196  0.50 9.70  ? 170 LYS A O   1 
ATOM   1350 O  O   B LYS A 1 169 ? 21.390 2.026   -2.060  0.50 11.93 ? 170 LYS A O   1 
ATOM   1351 C  CB  A LYS A 1 169 ? 22.156 0.520   0.345   0.50 9.43  ? 170 LYS A CB  1 
ATOM   1352 C  CB  B LYS A 1 169 ? 22.165 0.475   0.372   0.50 10.15 ? 170 LYS A CB  1 
ATOM   1353 C  CG  A LYS A 1 169 ? 22.577 1.737   1.178   0.50 10.58 ? 170 LYS A CG  1 
ATOM   1354 C  CG  B LYS A 1 169 ? 22.646 1.743   1.082   0.50 11.49 ? 170 LYS A CG  1 
ATOM   1355 C  CD  A LYS A 1 169 ? 23.890 1.496   1.899   0.50 13.19 ? 170 LYS A CD  1 
ATOM   1356 C  CD  B LYS A 1 169 ? 24.018 1.573   1.699   0.50 14.96 ? 170 LYS A CD  1 
ATOM   1357 C  CE  A LYS A 1 169 ? 24.297 2.577   2.884   0.50 19.68 ? 170 LYS A CE  1 
ATOM   1358 C  CE  B LYS A 1 169 ? 25.061 1.085   0.714   0.50 18.58 ? 170 LYS A CE  1 
ATOM   1359 N  N   . GLY A 1 170 ? 19.869 2.833   -0.563  1.00 8.71  ? 171 GLY A N   1 
ATOM   1360 C  CA  . GLY A 1 170 ? 19.689 4.128   -1.219  1.00 11.04 ? 171 GLY A CA  1 
ATOM   1361 C  C   . GLY A 1 170 ? 18.497 4.189   -2.179  1.00 10.78 ? 171 GLY A C   1 
ATOM   1362 O  O   . GLY A 1 170 ? 18.178 5.294   -2.653  1.00 14.00 ? 171 GLY A O   1 
ATOM   1363 N  N   . LYS A 1 171 ? 17.860 3.039   -2.461  1.00 9.27  ? 172 LYS A N   1 
ATOM   1364 C  CA  . LYS A 1 171 ? 16.657 3.056   -3.281  1.00 11.19 ? 172 LYS A CA  1 
ATOM   1365 C  C   . LYS A 1 171 ? 15.446 3.497   -2.460  1.00 8.29  ? 172 LYS A C   1 
ATOM   1366 O  O   . LYS A 1 171 ? 15.267 3.055   -1.325  1.00 9.44  ? 172 LYS A O   1 
ATOM   1367 C  CB  . LYS A 1 171 ? 16.467 1.699   -3.921  1.00 10.93 ? 172 LYS A CB  1 
ATOM   1368 C  CG  . LYS A 1 171 ? 17.500 1.365   -4.986  1.00 14.31 ? 172 LYS A CG  1 
ATOM   1369 C  CD  . LYS A 1 171 ? 17.046 0.273   -5.895  1.00 24.03 ? 172 LYS A CD  1 
ATOM   1370 N  N   . SER A 1 172 ? 14.638 4.368   -3.056  1.00 11.27 ? 173 SER A N   1 
ATOM   1371 C  CA  . SER A 1 172 ? 13.372 4.748   -2.462  1.00 11.89 ? 173 SER A CA  1 
ATOM   1372 C  C   . SER A 1 172 ? 12.237 4.610   -3.477  1.00 11.31 ? 173 SER A C   1 
ATOM   1373 O  O   . SER A 1 172 ? 12.435 4.607   -4.709  1.00 14.74 ? 173 SER A O   1 
ATOM   1374 C  CB  . SER A 1 172 ? 13.449 6.170   -1.937  1.00 12.46 ? 173 SER A CB  1 
ATOM   1375 O  OG  . SER A 1 172 ? 13.621 7.104   -2.996  1.00 16.12 ? 173 SER A OG  1 
ATOM   1376 N  N   . ALA A 1 173 ? 11.025 4.607   -2.942  1.00 12.82 ? 174 ALA A N   1 
ATOM   1377 C  CA  . ALA A 1 173 ? 9.848  4.604   -3.794  1.00 13.69 ? 174 ALA A CA  1 
ATOM   1378 C  C   . ALA A 1 173 ? 8.742  5.443   -3.144  1.00 10.95 ? 174 ALA A C   1 
ATOM   1379 O  O   . ALA A 1 173 ? 8.637  5.498   -1.911  1.00 9.59  ? 174 ALA A O   1 
ATOM   1380 C  CB  . ALA A 1 173 ? 9.374  3.196   -4.054  1.00 16.46 ? 174 ALA A CB  1 
ATOM   1381 N  N   . ASP A 1 174 ? 7.858  5.995   -3.982  1.00 14.57 ? 175 ASP A N   1 
ATOM   1382 C  CA  . ASP A 1 174 ? 6.716  6.675   -3.428  1.00 15.71 ? 175 ASP A CA  1 
ATOM   1383 C  C   . ASP A 1 174 ? 5.918  5.654   -2.622  1.00 14.00 ? 175 ASP A C   1 
ATOM   1384 O  O   . ASP A 1 174 ? 5.782  4.483   -2.981  1.00 17.54 ? 175 ASP A O   1 
ATOM   1385 C  CB  . ASP A 1 174 ? 5.857  7.291   -4.556  1.00 20.23 ? 175 ASP A CB  1 
ATOM   1386 C  CG  . ASP A 1 174 ? 6.531  8.379   -5.409  1.00 34.45 ? 175 ASP A CG  1 
ATOM   1387 O  OD1 . ASP A 1 174 ? 7.302  9.233   -4.844  1.00 41.04 ? 175 ASP A OD1 1 
ATOM   1388 O  OD2 . ASP A 1 174 ? 6.292  8.381   -6.645  1.00 45.84 ? 175 ASP A OD2 1 
ATOM   1389 N  N   . PHE A 1 175 ? 5.354  6.133   -1.515  1.00 12.40 ? 176 PHE A N   1 
ATOM   1390 C  CA  . PHE A 1 175 ? 4.602  5.234   -0.647  1.00 11.24 ? 176 PHE A CA  1 
ATOM   1391 C  C   . PHE A 1 175 ? 3.551  6.039   0.079   1.00 10.72 ? 176 PHE A C   1 
ATOM   1392 O  O   . PHE A 1 175 ? 3.553  6.191   1.291   1.00 14.64 ? 176 PHE A O   1 
ATOM   1393 C  CB  . PHE A 1 175 ? 5.556  4.465   0.269   1.00 11.27 ? 176 PHE A CB  1 
ATOM   1394 C  CG  . PHE A 1 175 ? 4.962  3.184   0.811   1.00 11.06 ? 176 PHE A CG  1 
ATOM   1395 C  CD1 . PHE A 1 175 ? 4.720  2.098   -0.027  1.00 10.19 ? 176 PHE A CD1 1 
ATOM   1396 C  CD2 . PHE A 1 175 ? 4.577  3.064   2.152   1.00 11.28 ? 176 PHE A CD2 1 
ATOM   1397 C  CE1 . PHE A 1 175 ? 4.174  0.921   0.466   1.00 11.91 ? 176 PHE A CE1 1 
ATOM   1398 C  CE2 . PHE A 1 175 ? 4.016  1.887   2.664   1.00 11.60 ? 176 PHE A CE2 1 
ATOM   1399 C  CZ  . PHE A 1 175 ? 3.819  0.828   1.803   1.00 11.30 ? 176 PHE A CZ  1 
ATOM   1400 N  N   . THR A 1 176 ? 2.625  6.556   -0.680  1.00 12.33 ? 177 THR A N   1 
ATOM   1401 C  CA  . THR A 1 176 ? 1.555  7.391   -0.159  1.00 11.28 ? 177 THR A CA  1 
ATOM   1402 C  C   . THR A 1 176 ? 0.351  6.553   0.230   1.00 9.05  ? 177 THR A C   1 
ATOM   1403 O  O   . THR A 1 176 ? 0.173  5.413   -0.201  1.00 11.18 ? 177 THR A O   1 
ATOM   1404 C  CB  . THR A 1 176 ? 1.165  8.458   -1.197  1.00 11.81 ? 177 THR A CB  1 
ATOM   1405 O  OG1 . THR A 1 176 ? 0.804  7.817   -2.417  1.00 17.63 ? 177 THR A OG1 1 
ATOM   1406 C  CG2 . THR A 1 176 ? 2.293  9.448   -1.398  1.00 17.88 ? 177 THR A CG2 1 
ATOM   1407 N  N   . ASN A 1 177 ? -0.449 7.113   1.136   1.00 9.76  ? 178 ASN A N   1 
ATOM   1408 C  CA  . ASN A 1 177 ? -1.742 6.544   1.491   1.00 10.80 ? 178 ASN A CA  1 
ATOM   1409 C  C   . ASN A 1 177 ? -1.612 5.213   2.212   1.00 10.25 ? 178 ASN A C   1 
ATOM   1410 O  O   . ASN A 1 177 ? -2.545 4.401   2.175   1.00 15.82 ? 178 ASN A O   1 
ATOM   1411 C  CB  . ASN A 1 177 ? -2.705 6.444   0.298   1.00 11.29 ? 178 ASN A CB  1 
ATOM   1412 C  CG  . ASN A 1 177 ? -2.898 7.821   -0.293  1.00 12.57 ? 178 ASN A CG  1 
ATOM   1413 O  OD1 . ASN A 1 177 ? -3.557 8.681   0.302   1.00 15.74 ? 178 ASN A OD1 1 
ATOM   1414 N  ND2 . ASN A 1 177 ? -2.288 8.079   -1.451  1.00 13.20 ? 178 ASN A ND2 1 
ATOM   1415 N  N   . PHE A 1 178 ? -0.519 4.999   2.929   1.00 9.18  ? 179 PHE A N   1 
ATOM   1416 C  CA  . PHE A 1 178 ? -0.395 3.815   3.746   1.00 9.71  ? 179 PHE A CA  1 
ATOM   1417 C  C   . PHE A 1 178 ? -0.912 4.081   5.151   1.00 9.46  ? 179 PHE A C   1 
ATOM   1418 O  O   . PHE A 1 178 ? -0.543 5.069   5.770   1.00 11.17 ? 179 PHE A O   1 
ATOM   1419 C  CB  . PHE A 1 178 ? 1.050  3.351   3.811   1.00 10.23 ? 179 PHE A CB  1 
ATOM   1420 C  CG  . PHE A 1 178 ? 1.192  2.102   4.655   1.00 10.05 ? 179 PHE A CG  1 
ATOM   1421 C  CD1 . PHE A 1 178 ? 0.794  0.859   4.156   1.00 10.34 ? 179 PHE A CD1 1 
ATOM   1422 C  CD2 . PHE A 1 178 ? 1.564  2.191   5.994   1.00 9.35  ? 179 PHE A CD2 1 
ATOM   1423 C  CE1 . PHE A 1 178 ? 0.814  -0.258  4.975   1.00 11.40 ? 179 PHE A CE1 1 
ATOM   1424 C  CE2 . PHE A 1 178 ? 1.622  1.030   6.783   1.00 8.81  ? 179 PHE A CE2 1 
ATOM   1425 C  CZ  . PHE A 1 178 ? 1.256  -0.199  6.282   1.00 9.69  ? 179 PHE A CZ  1 
ATOM   1426 N  N   . ASP A 1 179 ? -1.760 3.185   5.658   1.00 9.88  ? 180 ASP A N   1 
ATOM   1427 C  CA  . ASP A 1 179 ? -2.368 3.403   6.973   1.00 8.99  ? 180 ASP A CA  1 
ATOM   1428 C  C   . ASP A 1 179 ? -1.649 2.574   8.019   1.00 9.24  ? 180 ASP A C   1 
ATOM   1429 O  O   . ASP A 1 179 ? -1.833 1.376   8.088   1.00 10.28 ? 180 ASP A O   1 
ATOM   1430 C  CB  . ASP A 1 179 ? -3.846 3.067   6.894   1.00 12.60 ? 180 ASP A CB  1 
ATOM   1431 C  CG  . ASP A 1 179 ? -4.643 3.468   8.117   1.00 16.08 ? 180 ASP A CG  1 
ATOM   1432 O  OD1 . ASP A 1 179 ? -4.034 3.712   9.148   1.00 12.33 ? 180 ASP A OD1 1 
ATOM   1433 O  OD2 . ASP A 1 179 ? -5.884 3.517   7.980   1.00 25.15 ? 180 ASP A OD2 1 
ATOM   1434 N  N   . PRO A 1 180 ? -0.871 3.182   8.922   1.00 9.00  ? 181 PRO A N   1 
ATOM   1435 C  CA  . PRO A 1 180 ? -0.156 2.350   9.886   1.00 9.06  ? 181 PRO A CA  1 
ATOM   1436 C  C   . PRO A 1 180 ? -1.041 1.717   10.966  1.00 8.24  ? 181 PRO A C   1 
ATOM   1437 O  O   . PRO A 1 180 ? -0.574 0.837   11.698  1.00 8.93  ? 181 PRO A O   1 
ATOM   1438 C  CB  . PRO A 1 180 ? 0.832  3.358   10.485  1.00 10.28 ? 181 PRO A CB  1 
ATOM   1439 C  CG  . PRO A 1 180 ? 0.173  4.713   10.360  1.00 9.92  ? 181 PRO A CG  1 
ATOM   1440 C  CD  . PRO A 1 180 ? -0.578 4.626   9.047   1.00 10.70 ? 181 PRO A CD  1 
ATOM   1441 N  N   . ARG A 1 181 ? -2.318 2.129   11.013  1.00 8.85  ? 182 ARG A N   1 
ATOM   1442 C  CA  . ARG A 1 181 ? -3.232 1.480   11.961  1.00 9.49  ? 182 ARG A CA  1 
ATOM   1443 C  C   . ARG A 1 181 ? -3.338 -0.007  11.622  1.00 8.27  ? 182 ARG A C   1 
ATOM   1444 O  O   . ARG A 1 181 ? -3.699 -0.801  12.505  1.00 10.53 ? 182 ARG A O   1 
ATOM   1445 C  CB  . ARG A 1 181 ? -4.614 2.127   11.937  1.00 10.40 ? 182 ARG A CB  1 
ATOM   1446 C  CG  . ARG A 1 181 ? -4.542 3.563   12.430  1.00 12.78 ? 182 ARG A CG  1 
ATOM   1447 C  CD  . ARG A 1 181 ? -5.921 4.178   12.452  1.00 14.11 ? 182 ARG A CD  1 
ATOM   1448 N  NE  . ARG A 1 181 ? -6.298 4.411   11.076  1.00 14.35 ? 182 ARG A NE  1 
ATOM   1449 C  CZ  . ARG A 1 181 ? -7.389 5.106   10.699  1.00 18.88 ? 182 ARG A CZ  1 
ATOM   1450 N  NH1 . ARG A 1 181 ? -8.219 5.550   11.634  1.00 27.31 ? 182 ARG A NH1 1 
ATOM   1451 N  NH2 . ARG A 1 181 ? -7.696 5.252   9.416   1.00 21.17 ? 182 ARG A NH2 1 
ATOM   1452 N  N   . GLY A 1 182 ? -3.135 -0.387  10.350  1.00 9.35  ? 183 GLY A N   1 
ATOM   1453 C  CA  . GLY A 1 182 ? -3.215 -1.777  9.957   1.00 9.21  ? 183 GLY A CA  1 
ATOM   1454 C  C   . GLY A 1 182 ? -2.072 -2.651  10.457  1.00 9.22  ? 183 GLY A C   1 
ATOM   1455 O  O   . GLY A 1 182 ? -2.086 -3.852  10.181  1.00 12.64 ? 183 GLY A O   1 
ATOM   1456 N  N   . LEU A 1 183 ? -1.082 -2.069  11.188  1.00 8.76  ? 184 LEU A N   1 
ATOM   1457 C  CA  . LEU A 1 183 ? 0.046  -2.846  11.697  1.00 8.81  ? 184 LEU A CA  1 
ATOM   1458 C  C   . LEU A 1 183 ? -0.113 -3.102  13.203  1.00 8.22  ? 184 LEU A C   1 
ATOM   1459 O  O   . LEU A 1 183 ? 0.785  -3.697  13.803  1.00 10.54 ? 184 LEU A O   1 
ATOM   1460 C  CB  . LEU A 1 183 ? 1.345  -2.058  11.451  1.00 9.17  ? 184 LEU A CB  1 
ATOM   1461 C  CG  . LEU A 1 183 ? 1.712  -1.923  9.964   1.00 10.18 ? 184 LEU A CG  1 
ATOM   1462 C  CD1 . LEU A 1 183 ? 2.966  -1.120  9.778   1.00 12.11 ? 184 LEU A CD1 1 
ATOM   1463 C  CD2 . LEU A 1 183 ? 1.830  -3.259  9.282   1.00 14.48 ? 184 LEU A CD2 1 
ATOM   1464 N  N   . LEU A 1 184 ? -1.203 -2.648  13.839  1.00 8.51  ? 185 LEU A N   1 
ATOM   1465 C  CA  . LEU A 1 184 ? -1.314 -2.719  15.300  1.00 8.82  ? 185 LEU A CA  1 
ATOM   1466 C  C   . LEU A 1 184 ? -2.031 -3.998  15.703  1.00 9.86  ? 185 LEU A C   1 
ATOM   1467 O  O   . LEU A 1 184 ? -2.928 -4.448  15.007  1.00 15.65 ? 185 LEU A O   1 
ATOM   1468 C  CB  . LEU A 1 184 ? -2.125 -1.509  15.812  1.00 9.35  ? 185 LEU A CB  1 
ATOM   1469 C  CG  . LEU A 1 184 ? -1.556 -0.115  15.438  1.00 10.78 ? 185 LEU A CG  1 
ATOM   1470 C  CD1 . LEU A 1 184 ? -2.469 0.985   15.987  1.00 14.10 ? 185 LEU A CD1 1 
ATOM   1471 C  CD2 . LEU A 1 184 ? -0.134 0.049   15.940  1.00 14.00 ? 185 LEU A CD2 1 
ATOM   1472 N  N   . PRO A 1 185 ? -1.695 -4.567  16.879  1.00 7.85  ? 186 PRO A N   1 
ATOM   1473 C  CA  . PRO A 1 185 ? -2.487 -5.670  17.429  1.00 8.51  ? 186 PRO A CA  1 
ATOM   1474 C  C   . PRO A 1 185 ? -3.753 -5.115  18.051  1.00 9.03  ? 186 PRO A C   1 
ATOM   1475 O  O   . PRO A 1 185 ? -3.963 -3.908  18.101  1.00 10.02 ? 186 PRO A O   1 
ATOM   1476 C  CB  . PRO A 1 185 ? -1.543 -6.229  18.495  1.00 7.95  ? 186 PRO A CB  1 
ATOM   1477 C  CG  . PRO A 1 185 ? -0.846 -4.979  18.978  1.00 6.94  ? 186 PRO A CG  1 
ATOM   1478 C  CD  . PRO A 1 185 ? -0.599 -4.078  17.740  1.00 6.56  ? 186 PRO A CD  1 
ATOM   1479 N  N   A GLU A 1 186 ? -4.578 -6.053  18.542  0.50 11.61 ? 187 GLU A N   1 
ATOM   1480 N  N   B GLU A 1 186 ? -4.617 -6.004  18.577  0.50 10.72 ? 187 GLU A N   1 
ATOM   1481 C  CA  A GLU A 1 186 ? -5.868 -5.725  19.140  0.50 13.33 ? 187 GLU A CA  1 
ATOM   1482 C  CA  B GLU A 1 186 ? -5.899 -5.562  19.138  0.50 11.48 ? 187 GLU A CA  1 
ATOM   1483 C  C   A GLU A 1 186 ? -5.642 -4.830  20.366  0.50 11.50 ? 187 GLU A C   1 
ATOM   1484 C  C   B GLU A 1 186 ? -5.670 -4.798  20.443  0.50 9.46  ? 187 GLU A C   1 
ATOM   1485 O  O   A GLU A 1 186 ? -6.193 -3.722  20.431  0.50 15.84 ? 187 GLU A O   1 
ATOM   1486 O  O   B GLU A 1 186 ? -6.290 -3.784  20.709  0.50 12.05 ? 187 GLU A O   1 
ATOM   1487 C  CB  A GLU A 1 186 ? -6.601 -7.019  19.508  0.50 17.47 ? 187 GLU A CB  1 
ATOM   1488 C  CB  B GLU A 1 186 ? -6.775 -6.753  19.535  0.50 13.56 ? 187 GLU A CB  1 
ATOM   1489 C  CG  A GLU A 1 186 ? -7.732 -6.806  20.487  0.50 20.81 ? 187 GLU A CG  1 
ATOM   1490 C  CG  B GLU A 1 186 ? -7.465 -7.434  18.379  0.50 16.28 ? 187 GLU A CG  1 
ATOM   1491 C  CD  A GLU A 1 186 ? -8.444 -8.124  20.819  0.50 21.13 ? 187 GLU A CD  1 
ATOM   1492 C  CD  B GLU A 1 186 ? -8.192 -8.705  18.808  0.50 17.65 ? 187 GLU A CD  1 
ATOM   1493 O  OE1 A GLU A 1 186 ? -8.278 -9.060  19.963  0.50 25.30 ? 187 GLU A OE1 1 
ATOM   1494 O  OE1 B GLU A 1 186 ? -8.026 -9.159  19.964  0.50 27.74 ? 187 GLU A OE1 1 
ATOM   1495 O  OE2 A GLU A 1 186 ? -9.072 -8.179  21.923  0.50 25.85 ? 187 GLU A OE2 1 
ATOM   1496 O  OE2 B GLU A 1 186 ? -8.889 -9.247  17.958  0.50 20.47 ? 187 GLU A OE2 1 
ATOM   1497 N  N   . SER A 1 187 ? -4.757 -5.304  21.292  1.00 9.81  ? 188 SER A N   1 
ATOM   1498 C  CA  . SER A 1 187 ? -4.571 -4.674  22.593  1.00 9.99  ? 188 SER A CA  1 
ATOM   1499 C  C   . SER A 1 187 ? -3.442 -3.663  22.520  1.00 9.44  ? 188 SER A C   1 
ATOM   1500 O  O   . SER A 1 187 ? -2.422 -3.886  21.847  1.00 10.85 ? 188 SER A O   1 
ATOM   1501 C  CB  . SER A 1 187 ? -4.137 -5.728  23.592  1.00 11.47 ? 188 SER A CB  1 
ATOM   1502 O  OG  . SER A 1 187 ? -3.891 -5.183  24.886  1.00 12.96 ? 188 SER A OG  1 
ATOM   1503 N  N   . LEU A 1 188 ? -3.571 -2.577  23.283  1.00 9.93  ? 189 LEU A N   1 
ATOM   1504 C  CA  . LEU A 1 188 ? -2.501 -1.598  23.488  1.00 9.15  ? 189 LEU A CA  1 
ATOM   1505 C  C   . LEU A 1 188 ? -1.884 -1.688  24.886  1.00 7.73  ? 189 LEU A C   1 
ATOM   1506 O  O   . LEU A 1 188 ? -1.230 -0.750  25.325  1.00 10.00 ? 189 LEU A O   1 
ATOM   1507 C  CB  . LEU A 1 188 ? -2.996 -0.169  23.213  1.00 10.64 ? 189 LEU A CB  1 
ATOM   1508 C  CG  . LEU A 1 188 ? -3.423 0.199   21.792  1.00 11.69 ? 189 LEU A CG  1 
ATOM   1509 C  CD1 . LEU A 1 188 ? -3.977 1.617   21.672  1.00 15.92 ? 189 LEU A CD1 1 
ATOM   1510 C  CD2 . LEU A 1 188 ? -2.343 -0.087  20.793  1.00 14.49 ? 189 LEU A CD2 1 
ATOM   1511 N  N   . ASP A 1 189 ? -2.032 -2.824  25.578  1.00 8.91  ? 190 ASP A N   1 
ATOM   1512 C  CA  . ASP A 1 189 ? -1.274 -3.073  26.817  1.00 10.57 ? 190 ASP A CA  1 
ATOM   1513 C  C   . ASP A 1 189 ? 0.243  -3.075  26.540  1.00 8.41  ? 190 ASP A C   1 
ATOM   1514 O  O   . ASP A 1 189 ? 0.654  -3.550  25.466  1.00 7.09  ? 190 ASP A O   1 
ATOM   1515 C  CB  . ASP A 1 189 ? -1.700 -4.422  27.422  1.00 11.88 ? 190 ASP A CB  1 
ATOM   1516 C  CG  . ASP A 1 189 ? -3.095 -4.485  28.074  1.00 17.69 ? 190 ASP A CG  1 
ATOM   1517 O  OD1 . ASP A 1 189 ? -3.661 -3.425  28.238  1.00 23.11 ? 190 ASP A OD1 1 
ATOM   1518 O  OD2 . ASP A 1 189 ? -3.544 -5.622  28.328  1.00 28.78 ? 190 ASP A OD2 1 
ATOM   1519 N  N   . TYR A 1 190 ? 1.009  -2.472  27.466  1.00 7.98  ? 191 TYR A N   1 
ATOM   1520 C  CA  . TYR A 1 190 ? 2.418  -2.227  27.073  1.00 6.29  ? 191 TYR A CA  1 
ATOM   1521 C  C   . TYR A 1 190 ? 3.307  -2.293  28.329  1.00 6.57  ? 191 TYR A C   1 
ATOM   1522 O  O   . TYR A 1 190 ? 2.873  -2.170  29.481  1.00 7.78  ? 191 TYR A O   1 
ATOM   1523 C  CB  . TYR A 1 190 ? 2.521  -0.850  26.407  1.00 6.70  ? 191 TYR A CB  1 
ATOM   1524 C  CG  . TYR A 1 190 ? 2.175  0.304   27.315  1.00 6.42  ? 191 TYR A CG  1 
ATOM   1525 C  CD1 . TYR A 1 190 ? 3.086  0.895   28.200  1.00 7.04  ? 191 TYR A CD1 1 
ATOM   1526 C  CD2 . TYR A 1 190 ? 0.872  0.815   27.300  1.00 8.25  ? 191 TYR A CD2 1 
ATOM   1527 C  CE1 . TYR A 1 190 ? 2.722  1.931   29.035  1.00 7.64  ? 191 TYR A CE1 1 
ATOM   1528 C  CE2 . TYR A 1 190 ? 0.527  1.894   28.060  1.00 8.60  ? 191 TYR A CE2 1 
ATOM   1529 C  CZ  . TYR A 1 190 ? 1.438  2.460   28.923  1.00 8.21  ? 191 TYR A CZ  1 
ATOM   1530 O  OH  . TYR A 1 190 ? 1.083  3.471   29.776  1.00 9.86  ? 191 TYR A OH  1 
ATOM   1531 N  N   . TRP A 1 191 ? 4.612  -2.458  28.012  1.00 5.20  ? 192 TRP A N   1 
ATOM   1532 C  CA  . TRP A 1 191 ? 5.684  -2.189  28.967  1.00 5.62  ? 192 TRP A CA  1 
ATOM   1533 C  C   . TRP A 1 191 ? 6.388  -0.891  28.544  1.00 5.34  ? 192 TRP A C   1 
ATOM   1534 O  O   . TRP A 1 191 ? 6.387  -0.549  27.374  1.00 6.52  ? 192 TRP A O   1 
ATOM   1535 C  CB  . TRP A 1 191 ? 6.733  -3.343  28.920  1.00 6.39  ? 192 TRP A CB  1 
ATOM   1536 C  CG  . TRP A 1 191 ? 6.222  -4.688  29.344  1.00 5.81  ? 192 TRP A CG  1 
ATOM   1537 C  CD1 . TRP A 1 191 ? 6.013  -5.126  30.625  1.00 7.86  ? 192 TRP A CD1 1 
ATOM   1538 C  CD2 . TRP A 1 191 ? 5.953  -5.802  28.471  1.00 6.08  ? 192 TRP A CD2 1 
ATOM   1539 N  NE1 . TRP A 1 191 ? 5.589  -6.442  30.595  1.00 8.27  ? 192 TRP A NE1 1 
ATOM   1540 C  CE2 . TRP A 1 191 ? 5.527  -6.882  29.275  1.00 6.92  ? 192 TRP A CE2 1 
ATOM   1541 C  CE3 . TRP A 1 191 ? 6.007  -5.973  27.084  1.00 7.25  ? 192 TRP A CE3 1 
ATOM   1542 C  CZ2 . TRP A 1 191 ? 5.224  -8.137  28.734  1.00 9.41  ? 192 TRP A CZ2 1 
ATOM   1543 C  CZ3 . TRP A 1 191 ? 5.710  -7.206  26.538  1.00 8.69  ? 192 TRP A CZ3 1 
ATOM   1544 C  CH2 . TRP A 1 191 ? 5.356  -8.280  27.371  1.00 9.85  ? 192 TRP A CH2 1 
ATOM   1545 N  N   . THR A 1 192 ? 6.996  -0.207  29.525  1.00 5.47  ? 193 THR A N   1 
ATOM   1546 C  CA  . THR A 1 192 ? 7.736  1.000   29.174  1.00 5.42  ? 193 THR A CA  1 
ATOM   1547 C  C   . THR A 1 192 ? 8.958  1.132   30.059  1.00 5.70  ? 193 THR A C   1 
ATOM   1548 O  O   . THR A 1 192 ? 8.979  0.690   31.199  1.00 6.34  ? 193 THR A O   1 
ATOM   1549 C  CB  . THR A 1 192 ? 6.798  2.221   29.287  1.00 6.27  ? 193 THR A CB  1 
ATOM   1550 O  OG1 . THR A 1 192 ? 7.527  3.380   28.845  1.00 7.10  ? 193 THR A OG1 1 
ATOM   1551 C  CG2 . THR A 1 192 ? 6.250  2.436   30.698  1.00 7.58  ? 193 THR A CG2 1 
ATOM   1552 N  N   . TYR A 1 193 ? 10.009 1.710   29.461  1.00 5.32  ? 194 TYR A N   1 
ATOM   1553 C  CA  . TYR A 1 193 ? 11.242 1.977   30.208  1.00 6.30  ? 194 TYR A CA  1 
ATOM   1554 C  C   . TYR A 1 193 ? 12.031 3.022   29.445  1.00 5.32  ? 194 TYR A C   1 
ATOM   1555 O  O   . TYR A 1 193 ? 11.803 3.233   28.257  1.00 5.28  ? 194 TYR A O   1 
ATOM   1556 C  CB  . TYR A 1 193 ? 12.071 0.697   30.421  1.00 5.67  ? 194 TYR A CB  1 
ATOM   1557 C  CG  . TYR A 1 193 ? 12.755 0.240   29.149  1.00 4.93  ? 194 TYR A CG  1 
ATOM   1558 C  CD1 . TYR A 1 193 ? 12.079 -0.502  28.184  1.00 4.68  ? 194 TYR A CD1 1 
ATOM   1559 C  CD2 . TYR A 1 193 ? 14.084 0.567   28.905  1.00 5.46  ? 194 TYR A CD2 1 
ATOM   1560 C  CE1 . TYR A 1 193 ? 12.670 -0.895  26.982  1.00 4.56  ? 194 TYR A CE1 1 
ATOM   1561 C  CE2 . TYR A 1 193 ? 14.696 0.181   27.725  1.00 4.70  ? 194 TYR A CE2 1 
ATOM   1562 C  CZ  . TYR A 1 193 ? 13.992 -0.508  26.757  1.00 4.05  ? 194 TYR A CZ  1 
ATOM   1563 O  OH  . TYR A 1 193 ? 14.648 -0.818  25.593  1.00 4.76  ? 194 TYR A OH  1 
ATOM   1564 N  N   . PRO A 1 194 ? 12.959 3.742   30.117  1.00 6.39  ? 195 PRO A N   1 
ATOM   1565 C  CA  . PRO A 1 194 ? 13.788 4.730   29.423  1.00 6.85  ? 195 PRO A CA  1 
ATOM   1566 C  C   . PRO A 1 194 ? 15.017 4.083   28.804  1.00 5.23  ? 195 PRO A C   1 
ATOM   1567 O  O   . PRO A 1 194 ? 15.708 3.293   29.473  1.00 6.29  ? 195 PRO A O   1 
ATOM   1568 C  CB  . PRO A 1 194 ? 14.239 5.628   30.606  1.00 6.97  ? 195 PRO A CB  1 
ATOM   1569 C  CG  . PRO A 1 194 ? 14.281 4.719   31.813  1.00 8.25  ? 195 PRO A CG  1 
ATOM   1570 C  CD  . PRO A 1 194 ? 13.137 3.736   31.573  1.00 7.61  ? 195 PRO A CD  1 
ATOM   1571 N  N   . GLY A 1 195 ? 15.238 4.385   27.520  1.00 6.06  ? 196 GLY A N   1 
ATOM   1572 C  CA  . GLY A 1 195 ? 16.381 3.762   26.844  1.00 7.07  ? 196 GLY A CA  1 
ATOM   1573 C  C   . GLY A 1 195 ? 16.930 4.634   25.751  1.00 4.98  ? 196 GLY A C   1 
ATOM   1574 O  O   . GLY A 1 195 ? 17.058 5.831   25.911  1.00 4.95  ? 196 GLY A O   1 
ATOM   1575 N  N   . SER A 1 196 ? 17.312 3.934   24.692  1.00 4.90  ? 197 SER A N   1 
ATOM   1576 C  CA  . SER A 1 196 ? 18.186 4.580   23.672  1.00 5.38  ? 197 SER A CA  1 
ATOM   1577 C  C   . SER A 1 196 ? 17.739 4.191   22.272  1.00 4.51  ? 197 SER A C   1 
ATOM   1578 O  O   . SER A 1 196 ? 16.965 3.244   22.096  1.00 5.29  ? 197 SER A O   1 
ATOM   1579 C  CB  . SER A 1 196 ? 19.659 4.158   23.859  1.00 6.63  ? 197 SER A CB  1 
ATOM   1580 O  OG  . SER A 1 196 ? 19.875 2.818   23.390  1.00 6.17  ? 197 SER A OG  1 
ATOM   1581 N  N   . LEU A 1 197 ? 18.286 4.858   21.244  1.00 4.94  ? 198 LEU A N   1 
ATOM   1582 C  CA  . LEU A 1 197 ? 18.281 4.300   19.903  1.00 4.86  ? 198 LEU A CA  1 
ATOM   1583 C  C   . LEU A 1 197 ? 19.000 2.974   19.929  1.00 4.97  ? 198 LEU A C   1 
ATOM   1584 O  O   . LEU A 1 197 ? 19.991 2.809   20.660  1.00 6.78  ? 198 LEU A O   1 
ATOM   1585 C  CB  . LEU A 1 197 ? 18.987 5.266   18.931  1.00 7.04  ? 198 LEU A CB  1 
ATOM   1586 C  CG  . LEU A 1 197 ? 18.345 6.647   18.819  1.00 6.59  ? 198 LEU A CG  1 
ATOM   1587 C  CD1 . LEU A 1 197 ? 19.231 7.494   17.947  1.00 9.27  ? 198 LEU A CD1 1 
ATOM   1588 C  CD2 . LEU A 1 197 ? 16.944 6.531   18.220  1.00 7.98  ? 198 LEU A CD2 1 
ATOM   1589 N  N   . THR A 1 198 ? 18.563 2.029   19.091  1.00 5.42  ? 199 THR A N   1 
ATOM   1590 C  CA  . THR A 1 198 ? 19.231 0.728   19.018  1.00 5.14  ? 199 THR A CA  1 
ATOM   1591 C  C   . THR A 1 198 ? 20.227 0.640   17.849  1.00 4.92  ? 199 THR A C   1 
ATOM   1592 O  O   . THR A 1 198 ? 20.818 -0.419  17.677  1.00 6.50  ? 199 THR A O   1 
ATOM   1593 C  CB  . THR A 1 198 ? 18.242 -0.452  18.974  1.00 4.64  ? 199 THR A CB  1 
ATOM   1594 O  OG1 . THR A 1 198 ? 17.642 -0.390  17.658  1.00 4.92  ? 199 THR A OG1 1 
ATOM   1595 C  CG2 . THR A 1 198 ? 17.212 -0.396  20.081  1.00 5.69  ? 199 THR A CG2 1 
ATOM   1596 N  N   . THR A 1 199 ? 20.367 1.736   17.084  1.00 6.20  ? 200 THR A N   1 
ATOM   1597 C  CA  . THR A 1 199 ? 21.418 1.838   16.089  1.00 6.07  ? 200 THR A CA  1 
ATOM   1598 C  C   . THR A 1 199 ? 22.257 3.036   16.447  1.00 7.50  ? 200 THR A C   1 
ATOM   1599 O  O   . THR A 1 199 ? 21.771 3.985   17.061  1.00 7.09  ? 200 THR A O   1 
ATOM   1600 C  CB  . THR A 1 199 ? 20.819 2.096   14.694  1.00 7.55  ? 200 THR A CB  1 
ATOM   1601 O  OG1 . THR A 1 199 ? 19.908 3.203   14.739  1.00 12.68 ? 200 THR A OG1 1 
ATOM   1602 C  CG2 . THR A 1 199 ? 20.070 0.871   14.230  1.00 8.01  ? 200 THR A CG2 1 
ATOM   1603 N  N   . PRO A 1 200 ? 23.525 3.089   15.966  1.00 7.65  ? 201 PRO A N   1 
ATOM   1604 C  CA  . PRO A 1 200 ? 24.300 4.338   16.093  1.00 8.23  ? 201 PRO A CA  1 
ATOM   1605 C  C   . PRO A 1 200 ? 23.414 5.483   15.611  1.00 8.37  ? 201 PRO A C   1 
ATOM   1606 O  O   . PRO A 1 200 ? 22.696 5.354   14.578  1.00 9.53  ? 201 PRO A O   1 
ATOM   1607 C  CB  . PRO A 1 200 ? 25.462 4.035   15.112  1.00 9.54  ? 201 PRO A CB  1 
ATOM   1608 C  CG  . PRO A 1 200 ? 25.673 2.548   15.335  1.00 8.83  ? 201 PRO A CG  1 
ATOM   1609 C  CD  . PRO A 1 200 ? 24.274 1.966   15.351  1.00 8.28  ? 201 PRO A CD  1 
ATOM   1610 N  N   . PRO A 1 201 ? 23.449 6.641   16.292  1.00 8.51  ? 202 PRO A N   1 
ATOM   1611 C  CA  . PRO A 1 201 ? 24.428 6.999   17.326  1.00 9.21  ? 202 PRO A CA  1 
ATOM   1612 C  C   . PRO A 1 201 ? 24.085 6.546   18.751  1.00 7.39  ? 202 PRO A C   1 
ATOM   1613 O  O   . PRO A 1 201 ? 24.826 6.851   19.666  1.00 8.51  ? 202 PRO A O   1 
ATOM   1614 C  CB  . PRO A 1 201 ? 24.416 8.532   17.306  1.00 11.50 ? 202 PRO A CB  1 
ATOM   1615 C  CG  . PRO A 1 201 ? 23.022 8.875   16.848  1.00 12.78 ? 202 PRO A CG  1 
ATOM   1616 C  CD  . PRO A 1 201 ? 22.653 7.796   15.859  1.00 9.83  ? 202 PRO A CD  1 
ATOM   1617 N  N   . LEU A 1 202 ? 23.051 5.700   18.932  1.00 6.76  ? 203 LEU A N   1 
ATOM   1618 C  CA  . LEU A 1 202 ? 22.777 5.045   20.219  1.00 5.39  ? 203 LEU A CA  1 
ATOM   1619 C  C   . LEU A 1 202 ? 22.421 6.031   21.335  1.00 7.10  ? 203 LEU A C   1 
ATOM   1620 O  O   . LEU A 1 202 ? 22.484 5.732   22.500  1.00 7.59  ? 203 LEU A O   1 
ATOM   1621 C  CB  . LEU A 1 202 ? 23.939 4.115   20.662  1.00 7.07  ? 203 LEU A CB  1 
ATOM   1622 C  CG  . LEU A 1 202 ? 24.259 2.995   19.668  1.00 6.76  ? 203 LEU A CG  1 
ATOM   1623 C  CD1 . LEU A 1 202 ? 25.599 2.329   20.045  1.00 9.86  ? 203 LEU A CD1 1 
ATOM   1624 C  CD2 . LEU A 1 202 ? 23.168 1.954   19.522  1.00 7.18  ? 203 LEU A CD2 1 
ATOM   1625 N  N   . THR A 1 203 ? 21.916 7.194   20.910  1.00 7.67  ? 204 THR A N   1 
ATOM   1626 C  CA  . THR A 1 203 ? 21.646 8.287   21.835  1.00 7.94  ? 204 THR A CA  1 
ATOM   1627 C  C   . THR A 1 203 ? 20.562 7.874   22.842  1.00 6.60  ? 204 THR A C   1 
ATOM   1628 O  O   . THR A 1 203 ? 19.573 7.196   22.488  1.00 6.91  ? 204 THR A O   1 
ATOM   1629 C  CB  . THR A 1 203 ? 21.108 9.496   21.064  1.00 10.07 ? 204 THR A CB  1 
ATOM   1630 O  OG1 . THR A 1 203 ? 22.052 9.689   20.015  1.00 13.13 ? 204 THR A OG1 1 
ATOM   1631 C  CG2 . THR A 1 203 ? 21.055 10.762  21.874  1.00 13.23 ? 204 THR A CG2 1 
ATOM   1632 N  N   . GLU A 1 204 ? 20.745 8.293   24.091  1.00 7.49  ? 205 GLU A N   1 
ATOM   1633 C  CA  . GLU A 1 204 ? 19.845 7.951   25.185  1.00 6.65  ? 205 GLU A CA  1 
ATOM   1634 C  C   . GLU A 1 204 ? 18.698 8.947   25.284  1.00 8.20  ? 205 GLU A C   1 
ATOM   1635 O  O   . GLU A 1 204 ? 18.547 9.682   26.262  1.00 11.83 ? 205 GLU A O   1 
ATOM   1636 C  CB  . GLU A 1 204 ? 20.651 7.750   26.482  1.00 9.04  ? 205 GLU A CB  1 
ATOM   1637 C  CG  . GLU A 1 204 ? 21.642 6.603   26.357  1.00 9.21  ? 205 GLU A CG  1 
ATOM   1638 C  CD  . GLU A 1 204 ? 22.447 6.269   27.604  1.00 10.49 ? 205 GLU A CD  1 
ATOM   1639 O  OE1 . GLU A 1 204 ? 22.720 7.183   28.426  1.00 15.02 ? 205 GLU A OE1 1 
ATOM   1640 O  OE2 . GLU A 1 204 ? 22.892 5.086   27.701  1.00 9.95  ? 205 GLU A OE2 1 
ATOM   1641 N  N   . CYS A 1 205 ? 17.860 8.935   24.251  1.00 5.73  ? 206 CYS A N   1 
ATOM   1642 C  CA  . CYS A 1 205 ? 16.809 9.948   24.132  1.00 6.92  ? 206 CYS A CA  1 
ATOM   1643 C  C   . CYS A 1 205 ? 15.416 9.323   23.968  1.00 5.53  ? 206 CYS A C   1 
ATOM   1644 O  O   . CYS A 1 205 ? 14.510 10.025  23.536  1.00 7.37  ? 206 CYS A O   1 
ATOM   1645 C  CB  . CYS A 1 205 ? 17.052 10.816  22.902  1.00 7.28  ? 206 CYS A CB  1 
ATOM   1646 S  SG  . CYS A 1 205 ? 17.233 9.896   21.347  1.00 9.06  ? 206 CYS A SG  1 
ATOM   1647 N  N   . VAL A 1 206 ? 15.266 8.029   24.238  1.00 5.57  ? 207 VAL A N   1 
ATOM   1648 C  CA  . VAL A 1 206 ? 14.037 7.310   23.854  1.00 4.54  ? 207 VAL A CA  1 
ATOM   1649 C  C   . VAL A 1 206 ? 13.269 6.831   25.072  1.00 5.32  ? 207 VAL A C   1 
ATOM   1650 O  O   . VAL A 1 206 ? 13.815 6.161   25.944  1.00 6.42  ? 207 VAL A O   1 
ATOM   1651 C  CB  . VAL A 1 206 ? 14.340 6.085   22.979  1.00 5.03  ? 207 VAL A CB  1 
ATOM   1652 C  CG1 . VAL A 1 206 ? 13.032 5.316   22.629  1.00 6.40  ? 207 VAL A CG1 1 
ATOM   1653 C  CG2 . VAL A 1 206 ? 15.118 6.471   21.708  1.00 6.46  ? 207 VAL A CG2 1 
ATOM   1654 N  N   . THR A 1 207 ? 11.961 7.192   25.112  1.00 5.24  ? 208 THR A N   1 
ATOM   1655 C  CA  . THR A 1 207 ? 11.027 6.459   25.961  1.00 5.04  ? 208 THR A CA  1 
ATOM   1656 C  C   . THR A 1 207 ? 10.475 5.281   25.145  1.00 4.45  ? 208 THR A C   1 
ATOM   1657 O  O   . THR A 1 207 ? 9.833  5.465   24.105  1.00 5.55  ? 208 THR A O   1 
ATOM   1658 C  CB  . THR A 1 207 ? 9.833  7.314   26.404  1.00 6.94  ? 208 THR A CB  1 
ATOM   1659 O  OG1 . THR A 1 207 ? 10.365 8.418   27.151  1.00 8.41  ? 208 THR A OG1 1 
ATOM   1660 C  CG2 . THR A 1 207 ? 8.836  6.530   27.237  1.00 7.74  ? 208 THR A CG2 1 
ATOM   1661 N  N   . TRP A 1 208 ? 10.783 4.046   25.571  1.00 5.16  ? 209 TRP A N   1 
ATOM   1662 C  CA  . TRP A 1 208 ? 10.310 2.863   24.872  1.00 4.27  ? 209 TRP A CA  1 
ATOM   1663 C  C   . TRP A 1 208 ? 8.950  2.432   25.384  1.00 5.07  ? 209 TRP A C   1 
ATOM   1664 O  O   . TRP A 1 208 ? 8.726  2.376   26.575  1.00 4.56  ? 209 TRP A O   1 
ATOM   1665 C  CB  . TRP A 1 208 ? 11.319 1.682   25.092  1.00 5.28  ? 209 TRP A CB  1 
ATOM   1666 C  CG  . TRP A 1 208 ? 12.471 1.780   24.133  1.00 4.63  ? 209 TRP A CG  1 
ATOM   1667 C  CD1 . TRP A 1 208 ? 13.691 2.397   24.356  1.00 5.66  ? 209 TRP A CD1 1 
ATOM   1668 C  CD2 . TRP A 1 208 ? 12.417 1.393   22.762  1.00 4.95  ? 209 TRP A CD2 1 
ATOM   1669 N  NE1 . TRP A 1 208 ? 14.374 2.371   23.165  1.00 5.75  ? 209 TRP A NE1 1 
ATOM   1670 C  CE2 . TRP A 1 208 ? 13.661 1.742   22.186  1.00 4.98  ? 209 TRP A CE2 1 
ATOM   1671 C  CE3 . TRP A 1 208 ? 11.455 0.721   21.964  1.00 4.15  ? 209 TRP A CE3 1 
ATOM   1672 C  CZ2 . TRP A 1 208 ? 13.954 1.487   20.866  1.00 4.61  ? 209 TRP A CZ2 1 
ATOM   1673 C  CZ3 . TRP A 1 208 ? 11.760 0.447   20.651  1.00 5.66  ? 209 TRP A CZ3 1 
ATOM   1674 C  CH2 . TRP A 1 208 ? 13.003 0.830   20.109  1.00 5.00  ? 209 TRP A CH2 1 
ATOM   1675 N  N   . ILE A 1 209 ? 8.084  2.097   24.420  1.00 4.35  ? 210 ILE A N   1 
ATOM   1676 C  CA  . ILE A 1 209 ? 6.736  1.581   24.798  1.00 4.56  ? 210 ILE A CA  1 
ATOM   1677 C  C   . ILE A 1 209 ? 6.624  0.331   23.926  1.00 4.28  ? 210 ILE A C   1 
ATOM   1678 O  O   . ILE A 1 209 ? 6.593  0.414   22.690  1.00 5.38  ? 210 ILE A O   1 
ATOM   1679 C  CB  . ILE A 1 209 ? 5.671  2.611   24.409  1.00 5.50  ? 210 ILE A CB  1 
ATOM   1680 C  CG1 . ILE A 1 209 ? 5.858  3.869   25.242  1.00 6.86  ? 210 ILE A CG1 1 
ATOM   1681 C  CG2 . ILE A 1 209 ? 4.255  1.998   24.673  1.00 7.28  ? 210 ILE A CG2 1 
ATOM   1682 C  CD1 . ILE A 1 209 ? 4.996  5.051   24.715  1.00 8.55  ? 210 ILE A CD1 1 
ATOM   1683 N  N   . VAL A 1 210 ? 6.624  -0.834  24.583  1.00 4.47  ? 211 VAL A N   1 
ATOM   1684 C  CA  . VAL A 1 210 ? 6.650  -2.119  23.848  1.00 4.07  ? 211 VAL A CA  1 
ATOM   1685 C  C   . VAL A 1 210 ? 5.301  -2.808  24.125  1.00 4.78  ? 211 VAL A C   1 
ATOM   1686 O  O   . VAL A 1 210 ? 4.949  -3.069  25.264  1.00 4.92  ? 211 VAL A O   1 
ATOM   1687 C  CB  . VAL A 1 210 ? 7.808  -3.019  24.315  1.00 4.31  ? 211 VAL A CB  1 
ATOM   1688 C  CG1 . VAL A 1 210 ? 7.760  -4.359  23.585  1.00 5.69  ? 211 VAL A CG1 1 
ATOM   1689 C  CG2 . VAL A 1 210 ? 9.134  -2.275  24.046  1.00 6.27  ? 211 VAL A CG2 1 
ATOM   1690 N  N   . LEU A 1 211 ? 4.582  -3.083  23.042  1.00 5.33  ? 212 LEU A N   1 
ATOM   1691 C  CA  . LEU A 1 211 ? 3.259  -3.720  23.209  1.00 5.35  ? 212 LEU A CA  1 
ATOM   1692 C  C   . LEU A 1 211 ? 3.395  -5.182  23.609  1.00 5.35  ? 212 LEU A C   1 
ATOM   1693 O  O   . LEU A 1 211 ? 4.244  -5.924  23.093  1.00 6.06  ? 212 LEU A O   1 
ATOM   1694 C  CB  . LEU A 1 211 ? 2.447  -3.591  21.905  1.00 5.22  ? 212 LEU A CB  1 
ATOM   1695 C  CG  . LEU A 1 211 ? 2.070  -2.196  21.482  1.00 6.12  ? 212 LEU A CG  1 
ATOM   1696 C  CD1 . LEU A 1 211 ? 1.077  -2.193  20.294  1.00 8.06  ? 212 LEU A CD1 1 
ATOM   1697 C  CD2 . LEU A 1 211 ? 1.580  -1.340  22.636  1.00 8.28  ? 212 LEU A CD2 1 
ATOM   1698 N  N   . LYS A 1 212 ? 2.520  -5.618  24.533  1.00 6.08  ? 213 LYS A N   1 
ATOM   1699 C  CA  . LYS A 1 212 ? 2.533  -7.019  24.974  1.00 8.28  ? 213 LYS A CA  1 
ATOM   1700 C  C   . LYS A 1 212 ? 2.083  -7.996  23.893  1.00 7.18  ? 213 LYS A C   1 
ATOM   1701 O  O   . LYS A 1 212 ? 2.584  -9.117  23.812  1.00 10.02 ? 213 LYS A O   1 
ATOM   1702 C  CB  . LYS A 1 212 ? 1.645  -7.110  26.228  1.00 13.99 ? 213 LYS A CB  1 
ATOM   1703 C  CG  . LYS A 1 212 ? 1.184  -8.487  26.684  1.00 21.70 ? 213 LYS A CG  1 
ATOM   1704 C  CD  . LYS A 1 212 ? 0.040  -8.332  27.725  1.00 30.53 ? 213 LYS A CD  1 
ATOM   1705 C  CE  . LYS A 1 212 ? -1.408 -8.336  27.243  1.00 39.79 ? 213 LYS A CE  1 
ATOM   1706 N  NZ  . LYS A 1 212 ? -1.644 -7.912  25.827  1.00 36.10 ? 213 LYS A NZ  1 
ATOM   1707 N  N   A GLU A 1 213 ? 1.112  -7.583  23.072  0.50 6.27  ? 214 GLU A N   1 
ATOM   1708 N  N   B GLU A 1 213 ? 1.124  -7.578  23.071  0.50 6.17  ? 214 GLU A N   1 
ATOM   1709 C  CA  A GLU A 1 213 ? 0.477  -8.467  22.096  0.50 6.91  ? 214 GLU A CA  1 
ATOM   1710 C  CA  B GLU A 1 213 ? 0.539  -8.516  22.123  0.50 6.40  ? 214 GLU A CA  1 
ATOM   1711 C  C   A GLU A 1 213 ? 1.260  -8.415  20.789  0.50 5.67  ? 214 GLU A C   1 
ATOM   1712 C  C   B GLU A 1 213 ? 1.280  -8.419  20.792  0.50 5.72  ? 214 GLU A C   1 
ATOM   1713 O  O   A GLU A 1 213 ? 1.383  -7.348  20.210  0.50 6.34  ? 214 GLU A O   1 
ATOM   1714 O  O   B GLU A 1 213 ? 1.352  -7.359  20.187  0.50 6.33  ? 214 GLU A O   1 
ATOM   1715 C  CB  A GLU A 1 213 ? -0.916 -7.930  21.739  0.50 8.50  ? 214 GLU A CB  1 
ATOM   1716 C  CB  B GLU A 1 213 ? -0.965 -8.284  21.941  0.50 7.69  ? 214 GLU A CB  1 
ATOM   1717 C  CG  A GLU A 1 213 ? -1.778 -8.906  20.957  0.50 11.87 ? 214 GLU A CG  1 
ATOM   1718 C  CG  B GLU A 1 213 ? -1.573 -9.258  20.958  0.50 9.48  ? 214 GLU A CG  1 
ATOM   1719 C  CD  A GLU A 1 213 ? -3.185 -8.385  20.647  0.50 15.64 ? 214 GLU A CD  1 
ATOM   1720 C  CD  B GLU A 1 213 ? -3.078 -9.135  20.744  0.50 11.46 ? 214 GLU A CD  1 
ATOM   1721 O  OE1 A GLU A 1 213 ? -3.689 -8.652  19.522  0.50 18.32 ? 214 GLU A OE1 1 
ATOM   1722 O  OE1 B GLU A 1 213 ? -3.687 -8.096  21.175  0.50 10.56 ? 214 GLU A OE1 1 
ATOM   1723 O  OE2 A GLU A 1 213 ? -3.762 -7.690  21.516  0.50 19.69 ? 214 GLU A OE2 1 
ATOM   1724 O  OE2 B GLU A 1 213 ? -3.645 -10.062 20.118  0.50 17.61 ? 214 GLU A OE2 1 
ATOM   1725 N  N   A PRO A 1 214 ? 1.814  -9.535  20.277  0.50 5.84  ? 215 PRO A N   1 
ATOM   1726 N  N   B PRO A 1 214 ? 1.944  -9.509  20.360  0.50 5.94  ? 215 PRO A N   1 
ATOM   1727 C  CA  A PRO A 1 214 ? 2.494  -9.453  18.995  0.50 6.10  ? 215 PRO A CA  1 
ATOM   1728 C  CA  B PRO A 1 214 ? 2.524  -9.525  19.018  0.50 6.59  ? 215 PRO A CA  1 
ATOM   1729 C  C   A PRO A 1 214 ? 1.419  -9.376  17.921  0.50 6.44  ? 215 PRO A C   1 
ATOM   1730 C  C   B PRO A 1 214 ? 1.491  -9.580  17.886  0.50 7.25  ? 215 PRO A C   1 
ATOM   1731 O  O   A PRO A 1 214 ? 0.242  -9.649  18.180  0.50 6.77  ? 215 PRO A O   1 
ATOM   1732 O  O   B PRO A 1 214 ? 0.385  -10.103 18.052  0.50 8.16  ? 215 PRO A O   1 
ATOM   1733 C  CB  A PRO A 1 214 ? 3.177  -10.823 18.851  0.50 6.43  ? 215 PRO A CB  1 
ATOM   1734 C  CB  B PRO A 1 214 ? 3.331  -10.833 19.021  0.50 8.01  ? 215 PRO A CB  1 
ATOM   1735 C  CG  A PRO A 1 214 ? 2.356  -11.760 19.720  0.50 7.60  ? 215 PRO A CG  1 
ATOM   1736 C  CG  B PRO A 1 214 ? 3.443  -11.235 20.486  0.50 9.46  ? 215 PRO A CG  1 
ATOM   1737 C  CD  A PRO A 1 214 ? 1.712  -10.914 20.801  0.50 7.52  ? 215 PRO A CD  1 
ATOM   1738 C  CD  B PRO A 1 214 ? 2.179  -10.749 21.138  0.50 6.63  ? 215 PRO A CD  1 
ATOM   1739 N  N   . ILE A 1 215 ? 1.875  -9.063  16.704  1.00 6.47  ? 216 ILE A N   1 
ATOM   1740 C  CA  . ILE A 1 215 ? 1.077  -9.281  15.503  1.00 6.98  ? 216 ILE A CA  1 
ATOM   1741 C  C   . ILE A 1 215 ? 1.591  -10.536 14.828  1.00 6.81  ? 216 ILE A C   1 
ATOM   1742 O  O   . ILE A 1 215 ? 2.775  -10.905 15.001  1.00 7.82  ? 216 ILE A O   1 
ATOM   1743 C  CB  . ILE A 1 215 ? 1.081  -8.066  14.547  1.00 6.79  ? 216 ILE A CB  1 
ATOM   1744 C  CG1 . ILE A 1 215 ? 2.501  -7.707  14.060  1.00 7.40  ? 216 ILE A CG1 1 
ATOM   1745 C  CG2 . ILE A 1 215 ? 0.424  -6.850  15.250  1.00 9.24  ? 216 ILE A CG2 1 
ATOM   1746 C  CD1 . ILE A 1 215 ? 2.512  -6.718  12.878  1.00 8.85  ? 216 ILE A CD1 1 
ATOM   1747 N  N   A SER A 1 216 ? 0.701  -11.146 14.049  0.50 8.24  ? 217 SER A N   1 
ATOM   1748 N  N   B SER A 1 216 ? 0.719  -11.285 14.149  0.50 8.30  ? 217 SER A N   1 
ATOM   1749 C  CA  A SER A 1 216 ? 1.014  -12.311 13.241  0.50 7.50  ? 217 SER A CA  1 
ATOM   1750 C  CA  B SER A 1 216 ? 1.218  -12.390 13.335  0.50 8.62  ? 217 SER A CA  1 
ATOM   1751 C  C   A SER A 1 216 ? 1.302  -11.839 11.830  0.50 7.61  ? 217 SER A C   1 
ATOM   1752 C  C   B SER A 1 216 ? 1.302  -11.935 11.894  0.50 7.59  ? 217 SER A C   1 
ATOM   1753 O  O   A SER A 1 216 ? 0.541  -11.048 11.272  0.50 9.04  ? 217 SER A O   1 
ATOM   1754 O  O   B SER A 1 216 ? 0.369  -11.335 11.368  0.50 8.81  ? 217 SER A O   1 
ATOM   1755 C  CB  A SER A 1 216 ? -0.122 -13.305 13.281  0.50 8.92  ? 217 SER A CB  1 
ATOM   1756 C  CB  B SER A 1 216 ? 0.371  -13.641 13.401  0.50 12.12 ? 217 SER A CB  1 
ATOM   1757 O  OG  A SER A 1 216 ? -0.098 -13.999 14.518  0.50 13.18 ? 217 SER A OG  1 
ATOM   1758 O  OG  B SER A 1 216 ? -0.968 -13.326 13.098  0.50 15.87 ? 217 SER A OG  1 
ATOM   1759 N  N   . VAL A 1 217 ? 2.391  -12.363 11.263  1.00 7.26  ? 218 VAL A N   1 
ATOM   1760 C  CA  . VAL A 1 217 ? 2.684  -12.209 9.843   1.00 7.39  ? 218 VAL A CA  1 
ATOM   1761 C  C   . VAL A 1 217 ? 2.929  -13.565 9.241   1.00 7.98  ? 218 VAL A C   1 
ATOM   1762 O  O   . VAL A 1 217 ? 3.292  -14.500 9.964   1.00 7.69  ? 218 VAL A O   1 
ATOM   1763 C  CB  . VAL A 1 217 ? 3.881  -11.277 9.643   1.00 8.73  ? 218 VAL A CB  1 
ATOM   1764 C  CG1 . VAL A 1 217 ? 3.594  -9.943  10.318  1.00 9.12  ? 218 VAL A CG1 1 
ATOM   1765 C  CG2 . VAL A 1 217 ? 5.182  -11.879 10.196  1.00 10.99 ? 218 VAL A CG2 1 
ATOM   1766 N  N   . SER A 1 218 ? 2.835  -13.683 7.931   1.00 8.45  ? 219 SER A N   1 
ATOM   1767 C  CA  . SER A 1 218 ? 2.993  -15.027 7.381   1.00 9.03  ? 219 SER A CA  1 
ATOM   1768 C  C   . SER A 1 218 ? 4.464  -15.302 7.109   1.00 8.65  ? 219 SER A C   1 
ATOM   1769 O  O   . SER A 1 218 ? 5.299  -14.394 6.993   1.00 7.90  ? 219 SER A O   1 
ATOM   1770 C  CB  . SER A 1 218 ? 2.234  -15.241 6.101   1.00 9.41  ? 219 SER A CB  1 
ATOM   1771 O  OG  . SER A 1 218 ? 2.700  -14.325 5.127   1.00 11.37 ? 219 SER A OG  1 
ATOM   1772 N  N   . SER A 1 219 ? 4.795  -16.585 6.926   1.00 9.46  ? 220 SER A N   1 
ATOM   1773 C  CA  . SER A 1 219 ? 6.159  -16.936 6.576   1.00 10.06 ? 220 SER A CA  1 
ATOM   1774 C  C   . SER A 1 219 ? 6.556  -16.263 5.259   1.00 10.69 ? 220 SER A C   1 
ATOM   1775 O  O   . SER A 1 219 ? 7.700  -15.800 5.129   1.00 12.82 ? 220 SER A O   1 
ATOM   1776 C  CB  . SER A 1 219 ? 6.328  -18.446 6.530   1.00 14.65 ? 220 SER A CB  1 
ATOM   1777 O  OG  . SER A 1 219 ? 5.401  -19.071 5.650   1.00 16.39 ? 220 SER A OG  1 
ATOM   1778 N  N   . GLU A 1 220 ? 5.614  -16.120 4.311   1.00 9.49  ? 221 GLU A N   1 
ATOM   1779 C  CA  . GLU A 1 220 ? 5.968  -15.531 3.033   1.00 11.40 ? 221 GLU A CA  1 
ATOM   1780 C  C   . GLU A 1 220 ? 6.228  -14.031 3.201   1.00 10.65 ? 221 GLU A C   1 
ATOM   1781 O  O   . GLU A 1 220 ? 7.077  -13.453 2.508   1.00 11.48 ? 221 GLU A O   1 
ATOM   1782 C  CB  . GLU A 1 220 ? 4.832  -15.693 2.023   1.00 13.97 ? 221 GLU A CB  1 
ATOM   1783 C  CG  . GLU A 1 220 ? 4.553  -17.122 1.598   1.00 19.56 ? 221 GLU A CG  1 
ATOM   1784 C  CD  . GLU A 1 220 ? 3.635  -17.931 2.487   1.00 21.51 ? 221 GLU A CD  1 
ATOM   1785 O  OE1 . GLU A 1 220 ? 3.165  -17.443 3.534   1.00 17.88 ? 221 GLU A OE1 1 
ATOM   1786 O  OE2 . GLU A 1 220 ? 3.370  -19.060 2.128   1.00 29.56 ? 221 GLU A OE2 1 
ATOM   1787 N  N   . GLN A 1 221 ? 5.503  -13.366 4.120   1.00 9.21  ? 222 GLN A N   1 
ATOM   1788 C  CA  . GLN A 1 221 ? 5.757  -11.937 4.299   1.00 7.96  ? 222 GLN A CA  1 
ATOM   1789 C  C   . GLN A 1 221 ? 7.171  -11.703 4.843   1.00 7.87  ? 222 GLN A C   1 
ATOM   1790 O  O   . GLN A 1 221 ? 7.920  -10.830 4.357   1.00 9.83  ? 222 GLN A O   1 
ATOM   1791 C  CB  . GLN A 1 221 ? 4.737  -11.327 5.243   1.00 8.04  ? 222 GLN A CB  1 
ATOM   1792 C  CG  . GLN A 1 221 ? 3.393  -11.160 4.546   1.00 8.02  ? 222 GLN A CG  1 
ATOM   1793 C  CD  . GLN A 1 221 ? 2.266  -10.672 5.431   1.00 7.39  ? 222 GLN A CD  1 
ATOM   1794 O  OE1 . GLN A 1 221 ? 2.127  -11.065 6.600   1.00 7.91  ? 222 GLN A OE1 1 
ATOM   1795 N  NE2 . GLN A 1 221 ? 1.441  -9.796  4.849   1.00 7.91  ? 222 GLN A NE2 1 
ATOM   1796 N  N   . VAL A 1 222 ? 7.581  -12.488 5.858   1.00 8.05  ? 223 VAL A N   1 
ATOM   1797 C  CA  . VAL A 1 222 ? 8.911  -12.272 6.442   1.00 9.59  ? 223 VAL A CA  1 
ATOM   1798 C  C   . VAL A 1 222 ? 9.982  -12.739 5.429   1.00 9.45  ? 223 VAL A C   1 
ATOM   1799 O  O   . VAL A 1 222 ? 11.053 -12.153 5.380   1.00 10.25 ? 223 VAL A O   1 
ATOM   1800 C  CB  . VAL A 1 222 ? 9.057  -12.823 7.874   1.00 14.26 ? 223 VAL A CB  1 
ATOM   1801 C  CG1 . VAL A 1 222 ? 8.984  -14.318 7.907   1.00 18.26 ? 223 VAL A CG1 1 
ATOM   1802 C  CG2 . VAL A 1 222 ? 10.405 -12.412 8.493   1.00 16.26 ? 223 VAL A CG2 1 
ATOM   1803 N  N   A LEU A 1 223 ? 9.700  -13.715 4.548   0.50 8.50  ? 224 LEU A N   1 
ATOM   1804 N  N   B LEU A 1 223 ? 9.656  -13.766 4.626   0.50 10.43 ? 224 LEU A N   1 
ATOM   1805 C  CA  A LEU A 1 223 ? 10.688 -14.144 3.557   0.50 10.15 ? 224 LEU A CA  1 
ATOM   1806 C  CA  B LEU A 1 223 ? 10.540 -14.204 3.558   0.50 12.23 ? 224 LEU A CA  1 
ATOM   1807 C  C   A LEU A 1 223 ? 10.974 -13.019 2.573   0.50 9.98  ? 224 LEU A C   1 
ATOM   1808 C  C   B LEU A 1 223 ? 10.960 -13.001 2.724   0.50 9.96  ? 224 LEU A C   1 
ATOM   1809 O  O   A LEU A 1 223 ? 12.057 -12.935 1.992   0.50 11.22 ? 224 LEU A O   1 
ATOM   1810 O  O   B LEU A 1 223 ? 12.148 -12.833 2.441   0.50 10.92 ? 224 LEU A O   1 
ATOM   1811 C  CB  A LEU A 1 223 ? 10.168 -15.364 2.784   0.50 12.23 ? 224 LEU A CB  1 
ATOM   1812 C  CB  B LEU A 1 223 ? 9.836  -15.258 2.689   0.50 16.67 ? 224 LEU A CB  1 
ATOM   1813 C  CG  A LEU A 1 223 ? 10.291 -16.696 3.502   0.50 12.52 ? 224 LEU A CG  1 
ATOM   1814 C  CG  B LEU A 1 223 ? 10.595 -15.611 1.414   0.50 20.54 ? 224 LEU A CG  1 
ATOM   1815 C  CD2 . LEU A 1 223 ? 11.726 -17.127 3.629   1.00 16.35 ? 224 LEU A CD2 1 
ATOM   1816 N  N   . LYS A 1 224 ? 9.988  -12.151 2.366   1.00 10.09 ? 225 LYS A N   1 
ATOM   1817 C  CA  . LYS A 1 224 ? 10.238 -11.032 1.473   1.00 10.67 ? 225 LYS A CA  1 
ATOM   1818 C  C   . LYS A 1 224 ? 11.134 -9.981  2.148   1.00 8.55  ? 225 LYS A C   1 
ATOM   1819 O  O   . LYS A 1 224 ? 11.953 -9.370  1.475   1.00 9.87  ? 225 LYS A O   1 
ATOM   1820 C  CB  . LYS A 1 224 ? 8.895  -10.504 0.908   1.00 12.93 ? 225 LYS A CB  1 
ATOM   1821 C  CG  . LYS A 1 224 ? 8.271  -11.481 -0.110  1.00 19.42 ? 225 LYS A CG  1 
ATOM   1822 C  CD  . LYS A 1 224 ? 6.950  -11.173 -0.810  1.00 25.63 ? 225 LYS A CD  1 
ATOM   1823 C  CE  . LYS A 1 224 ? 6.649  -12.025 -2.044  1.00 43.56 ? 225 LYS A CE  1 
ATOM   1824 N  NZ  . LYS A 1 224 ? 5.187  -12.172 -2.356  1.00 37.72 ? 225 LYS A NZ  1 
ATOM   1825 N  N   . PHE A 1 225 ? 11.027 -9.772  3.467   1.00 7.65  ? 226 PHE A N   1 
ATOM   1826 C  CA  . PHE A 1 225 ? 11.970 -8.889  4.126   1.00 6.32  ? 226 PHE A CA  1 
ATOM   1827 C  C   . PHE A 1 225 ? 13.404 -9.394  3.900   1.00 7.17  ? 226 PHE A C   1 
ATOM   1828 O  O   . PHE A 1 225 ? 14.342 -8.610  3.713   1.00 7.87  ? 226 PHE A O   1 
ATOM   1829 C  CB  . PHE A 1 225 ? 11.783 -8.909  5.646   1.00 6.90  ? 226 PHE A CB  1 
ATOM   1830 C  CG  . PHE A 1 225 ? 10.600 -8.155  6.231   1.00 8.03  ? 226 PHE A CG  1 
ATOM   1831 C  CD1 . PHE A 1 225 ? 9.562  -7.657  5.458   1.00 11.09 ? 226 PHE A CD1 1 
ATOM   1832 C  CD2 . PHE A 1 225 ? 10.488 -8.003  7.631   1.00 10.87 ? 226 PHE A CD2 1 
ATOM   1833 C  CE1 . PHE A 1 225 ? 8.513  -6.965  6.060   1.00 13.37 ? 226 PHE A CE1 1 
ATOM   1834 C  CE2 . PHE A 1 225 ? 9.478  -7.276  8.210   1.00 12.34 ? 226 PHE A CE2 1 
ATOM   1835 C  CZ  . PHE A 1 225 ? 8.480  -6.781  7.418   1.00 11.27 ? 226 PHE A CZ  1 
ATOM   1836 N  N   . ARG A 1 226 ? 13.586 -10.732 3.992   1.00 6.79  ? 227 ARG A N   1 
ATOM   1837 C  CA  . ARG A 1 226 ? 14.940 -11.310 3.871   1.00 7.06  ? 227 ARG A CA  1 
ATOM   1838 C  C   . ARG A 1 226 ? 15.497 -11.297 2.456   1.00 7.97  ? 227 ARG A C   1 
ATOM   1839 O  O   . ARG A 1 226 ? 16.665 -11.694 2.272   1.00 10.35 ? 227 ARG A O   1 
ATOM   1840 C  CB  . ARG A 1 226 ? 14.876 -12.754 4.391   1.00 9.08  ? 227 ARG A CB  1 
ATOM   1841 C  CG  . ARG A 1 226 ? 14.430 -12.883 5.856   1.00 7.96  ? 227 ARG A CG  1 
ATOM   1842 C  CD  . ARG A 1 226 ? 14.506 -14.340 6.256   1.00 9.54  ? 227 ARG A CD  1 
ATOM   1843 N  NE  . ARG A 1 226 ? 13.955 -14.511 7.626   1.00 8.66  ? 227 ARG A NE  1 
ATOM   1844 C  CZ  . ARG A 1 226 ? 13.021 -15.391 7.984   1.00 9.52  ? 227 ARG A CZ  1 
ATOM   1845 N  NH1 . ARG A 1 226 ? 12.528 -16.268 7.109   1.00 15.39 ? 227 ARG A NH1 1 
ATOM   1846 N  NH2 . ARG A 1 226 ? 12.562 -15.370 9.231   1.00 11.63 ? 227 ARG A NH2 1 
ATOM   1847 N  N   A LYS A 1 227 ? 14.712 -10.801 1.486   0.50 9.00  ? 228 LYS A N   1 
ATOM   1848 N  N   B LYS A 1 227 ? 14.749 -10.822 1.442   0.50 7.79  ? 228 LYS A N   1 
ATOM   1849 C  CA  A LYS A 1 227 ? 15.187 -10.652 0.120   0.50 9.92  ? 228 LYS A CA  1 
ATOM   1850 C  CA  B LYS A 1 227 ? 15.327 -10.690 0.107   0.50 9.10  ? 228 LYS A CA  1 
ATOM   1851 C  C   A LYS A 1 227 ? 15.952 -9.338  -0.051  0.50 8.74  ? 228 LYS A C   1 
ATOM   1852 C  C   B LYS A 1 227 ? 15.842 -9.266  -0.157  0.50 7.89  ? 228 LYS A C   1 
ATOM   1853 O  O   A LYS A 1 227 ? 16.771 -9.222  -0.971  0.50 10.81 ? 228 LYS A O   1 
ATOM   1854 O  O   B LYS A 1 227 ? 16.370 -8.989  -1.242  0.50 7.22  ? 228 LYS A O   1 
ATOM   1855 C  CB  A LYS A 1 227 ? 13.976 -10.763 -0.809  0.50 11.86 ? 228 LYS A CB  1 
ATOM   1856 C  CB  B LYS A 1 227 ? 14.272 -11.123 -0.917  0.50 9.59  ? 228 LYS A CB  1 
ATOM   1857 C  CG  A LYS A 1 227 ? 13.405 -12.174 -0.928  0.50 14.00 ? 228 LYS A CG  1 
ATOM   1858 C  CG  B LYS A 1 227 ? 13.949 -12.615 -0.935  0.50 13.21 ? 228 LYS A CG  1 
ATOM   1859 C  CD  A LYS A 1 227 ? 12.453 -12.334 -2.111  0.50 17.79 ? 228 LYS A CD  1 
ATOM   1860 C  CD  B LYS A 1 227 ? 12.786 -13.011 -1.843  0.50 19.00 ? 228 LYS A CD  1 
ATOM   1861 C  CE  A LYS A 1 227 ? 13.218 -12.532 -3.402  0.50 23.76 ? 228 LYS A CE  1 
ATOM   1862 C  CE  B LYS A 1 227 ? 12.984 -14.314 -2.596  0.50 27.61 ? 228 LYS A CE  1 
ATOM   1863 N  N   . LEU A 1 228 ? 15.659 -8.343  0.809   1.00 7.79  ? 229 LEU A N   1 
ATOM   1864 C  CA  . LEU A 1 228 ? 16.327 -7.068  0.726   1.00 7.37  ? 229 LEU A CA  1 
ATOM   1865 C  C   . LEU A 1 228 ? 17.837 -7.250  0.850   1.00 6.80  ? 229 LEU A C   1 
ATOM   1866 O  O   . LEU A 1 228 ? 18.338 -8.289  1.282   1.00 7.83  ? 229 LEU A O   1 
ATOM   1867 C  CB  . LEU A 1 228 ? 15.831 -6.162  1.847   1.00 8.26  ? 229 LEU A CB  1 
ATOM   1868 C  CG  . LEU A 1 228 ? 14.380 -5.699  1.696   1.00 8.80  ? 229 LEU A CG  1 
ATOM   1869 C  CD1 . LEU A 1 228 ? 13.891 -5.070  2.994   1.00 8.96  ? 229 LEU A CD1 1 
ATOM   1870 C  CD2 . LEU A 1 228 ? 14.272 -4.708  0.535   1.00 10.16 ? 229 LEU A CD2 1 
ATOM   1871 N  N   . ASN A 1 229 ? 18.574 -6.201  0.495   1.00 8.40  ? 230 ASN A N   1 
ATOM   1872 C  CA  . ASN A 1 229 ? 20.047 -6.222  0.509   1.00 7.88  ? 230 ASN A CA  1 
ATOM   1873 C  C   . ASN A 1 229 ? 20.573 -5.091  1.369   1.00 6.69  ? 230 ASN A C   1 
ATOM   1874 O  O   . ASN A 1 229 ? 20.070 -3.974  1.291   1.00 8.55  ? 230 ASN A O   1 
ATOM   1875 C  CB  . ASN A 1 229 ? 20.619 -5.998  -0.904  1.00 9.77  ? 230 ASN A CB  1 
ATOM   1876 C  CG  . ASN A 1 229 ? 20.489 -7.129  -1.881  1.00 11.03 ? 230 ASN A CG  1 
ATOM   1877 O  OD1 . ASN A 1 229 ? 20.967 -6.997  -3.022  1.00 15.66 ? 230 ASN A OD1 1 
ATOM   1878 N  ND2 . ASN A 1 229 ? 19.893 -8.257  -1.526  1.00 13.24 ? 230 ASN A ND2 1 
ATOM   1879 N  N   . PHE A 1 230 ? 21.656 -5.357  2.121   1.00 7.33  ? 231 PHE A N   1 
ATOM   1880 C  CA  . PHE A 1 230 ? 22.346 -4.269  2.804   1.00 6.75  ? 231 PHE A CA  1 
ATOM   1881 C  C   . PHE A 1 230 ? 23.156 -3.419  1.824   1.00 8.08  ? 231 PHE A C   1 
ATOM   1882 O  O   . PHE A 1 230 ? 23.391 -2.211  2.056   1.00 10.37 ? 231 PHE A O   1 
ATOM   1883 C  CB  . PHE A 1 230 ? 23.339 -4.867  3.790   1.00 7.83  ? 231 PHE A CB  1 
ATOM   1884 C  CG  . PHE A 1 230 ? 22.810 -5.487  5.055   1.00 8.14  ? 231 PHE A CG  1 
ATOM   1885 C  CD1 . PHE A 1 230 ? 22.064 -4.708  5.951   1.00 8.24  ? 231 PHE A CD1 1 
ATOM   1886 C  CD2 . PHE A 1 230 ? 23.076 -6.810  5.396   1.00 8.59  ? 231 PHE A CD2 1 
ATOM   1887 C  CE1 . PHE A 1 230 ? 21.631 -5.208  7.187   1.00 8.49  ? 231 PHE A CE1 1 
ATOM   1888 C  CE2 . PHE A 1 230 ? 22.629 -7.347  6.603   1.00 9.11  ? 231 PHE A CE2 1 
ATOM   1889 C  CZ  . PHE A 1 230 ? 21.944 -6.535  7.501   1.00 7.81  ? 231 PHE A CZ  1 
ATOM   1890 N  N   . ASN A 1 231 ? 23.670 -4.052  0.759   1.00 8.86  ? 232 ASN A N   1 
ATOM   1891 C  CA  . ASN A 1 231 ? 24.553 -3.417  -0.199  1.00 8.92  ? 232 ASN A CA  1 
ATOM   1892 C  C   . ASN A 1 231 ? 23.778 -2.504  -1.142  1.00 10.46 ? 232 ASN A C   1 
ATOM   1893 O  O   . ASN A 1 231 ? 22.568 -2.615  -1.335  1.00 10.81 ? 232 ASN A O   1 
ATOM   1894 C  CB  . ASN A 1 231 ? 25.258 -4.475  -1.054  1.00 10.89 ? 232 ASN A CB  1 
ATOM   1895 C  CG  . ASN A 1 231 ? 24.239 -5.425  -1.673  1.00 10.22 ? 232 ASN A CG  1 
ATOM   1896 O  OD1 . ASN A 1 231 ? 23.718 -6.304  -0.972  1.00 11.16 ? 232 ASN A OD1 1 
ATOM   1897 N  ND2 . ASN A 1 231 ? 23.933 -5.256  -2.963  1.00 12.91 ? 232 ASN A ND2 1 
ATOM   1898 N  N   . GLY A 1 232 ? 24.548 -1.612  -1.809  1.00 10.36 ? 233 GLY A N   1 
ATOM   1899 C  CA  . GLY A 1 232 ? 23.981 -0.832  -2.913  1.00 11.71 ? 233 GLY A CA  1 
ATOM   1900 C  C   . GLY A 1 232 ? 23.946 -1.646  -4.195  1.00 10.07 ? 233 GLY A C   1 
ATOM   1901 O  O   . GLY A 1 232 ? 24.625 -2.670  -4.316  1.00 12.29 ? 233 GLY A O   1 
ATOM   1902 N  N   . GLU A 1 233 ? 23.244 -1.124  -5.212  1.00 11.49 ? 234 GLU A N   1 
ATOM   1903 C  CA  . GLU A 1 233 ? 23.185 -1.694  -6.557  1.00 11.64 ? 234 GLU A CA  1 
ATOM   1904 C  C   . GLU A 1 233 ? 24.596 -1.787  -7.121  1.00 12.75 ? 234 GLU A C   1 
ATOM   1905 O  O   . GLU A 1 233 ? 25.403 -0.889  -6.961  1.00 12.97 ? 234 GLU A O   1 
ATOM   1906 C  CB  . GLU A 1 233 ? 22.300 -0.786  -7.440  1.00 15.77 ? 234 GLU A CB  1 
ATOM   1907 C  CG  . GLU A 1 233 ? 21.988 -1.345  -8.822  1.00 16.13 ? 234 GLU A CG  1 
ATOM   1908 C  CD  . GLU A 1 233 ? 21.139 -0.418  -9.685  1.00 24.95 ? 234 GLU A CD  1 
ATOM   1909 O  OE1 . GLU A 1 233 ? 20.853 0.755   -9.226  1.00 25.01 ? 234 GLU A OE1 1 
ATOM   1910 O  OE2 . GLU A 1 233 ? 20.752 -0.863  -10.815 1.00 27.21 ? 234 GLU A OE2 1 
ATOM   1911 N  N   . GLY A 1 234 ? 24.891 -2.893  -7.789  1.00 14.16 ? 235 GLY A N   1 
ATOM   1912 C  CA  . GLY A 1 234 ? 26.164 -3.047  -8.476  1.00 14.50 ? 235 GLY A CA  1 
ATOM   1913 C  C   . GLY A 1 234 ? 27.272 -3.435  -7.504  1.00 13.30 ? 235 GLY A C   1 
ATOM   1914 O  O   . GLY A 1 234 ? 28.440 -3.453  -7.893  1.00 17.26 ? 235 GLY A O   1 
ATOM   1915 N  N   . GLU A 1 235 ? 26.912 -3.765  -6.261  1.00 15.40 ? 236 GLU A N   1 
ATOM   1916 C  CA  . GLU A 1 235 ? 27.858 -4.224  -5.242  1.00 15.59 ? 236 GLU A CA  1 
ATOM   1917 C  C   . GLU A 1 235 ? 27.570 -5.672  -4.883  1.00 17.64 ? 236 GLU A C   1 
ATOM   1918 O  O   . GLU A 1 235 ? 26.486 -6.167  -5.160  1.00 18.00 ? 236 GLU A O   1 
ATOM   1919 C  CB  . GLU A 1 235 ? 27.747 -3.439  -3.934  1.00 17.55 ? 236 GLU A CB  1 
ATOM   1920 C  CG  . GLU A 1 235 ? 28.166 -1.986  -4.033  1.00 17.90 ? 236 GLU A CG  1 
ATOM   1921 C  CD  . GLU A 1 235 ? 27.981 -1.134  -2.764  1.00 33.69 ? 236 GLU A CD  1 
ATOM   1922 O  OE1 . GLU A 1 235 ? 27.305 -1.559  -1.762  1.00 28.26 ? 236 GLU A OE1 1 
ATOM   1923 O  OE2 . GLU A 1 235 ? 28.539 -0.036  -2.740  1.00 41.92 ? 236 GLU A OE2 1 
ATOM   1924 N  N   . PRO A 1 236 ? 28.510 -6.405  -4.248  1.00 16.83 ? 237 PRO A N   1 
ATOM   1925 C  CA  . PRO A 1 236 ? 28.263 -7.811  -3.921  1.00 18.61 ? 237 PRO A CA  1 
ATOM   1926 C  C   . PRO A 1 236 ? 27.014 -7.917  -3.021  1.00 15.57 ? 237 PRO A C   1 
ATOM   1927 O  O   . PRO A 1 236 ? 26.784 -7.115  -2.110  1.00 14.77 ? 237 PRO A O   1 
ATOM   1928 C  CB  . PRO A 1 236 ? 29.501 -8.155  -3.083  1.00 19.50 ? 237 PRO A CB  1 
ATOM   1929 C  CG  . PRO A 1 236 ? 30.599 -7.251  -3.681  1.00 22.97 ? 237 PRO A CG  1 
ATOM   1930 C  CD  . PRO A 1 236 ? 29.871 -5.933  -3.893  1.00 22.79 ? 237 PRO A CD  1 
ATOM   1931 N  N   . GLU A 1 237 ? 26.187 -8.928  -3.308  1.00 14.20 ? 238 GLU A N   1 
ATOM   1932 C  CA  . GLU A 1 237 ? 24.901 -9.100  -2.638  1.00 14.94 ? 238 GLU A CA  1 
ATOM   1933 C  C   . GLU A 1 237 ? 25.137 -9.601  -1.217  1.00 11.48 ? 238 GLU A C   1 
ATOM   1934 O  O   . GLU A 1 237 ? 25.628 -10.702 -1.018  1.00 12.26 ? 238 GLU A O   1 
ATOM   1935 C  CB  . GLU A 1 237 ? 23.946 -10.052 -3.389  1.00 17.17 ? 238 GLU A CB  1 
ATOM   1936 C  CG  . GLU A 1 237 ? 22.558 -10.094 -2.711  1.00 17.90 ? 238 GLU A CG  1 
ATOM   1937 C  CD  . GLU A 1 237 ? 21.450 -10.740 -3.554  1.00 24.33 ? 238 GLU A CD  1 
ATOM   1938 O  OE1 . GLU A 1 237 ? 21.804 -11.345 -4.630  1.00 34.34 ? 238 GLU A OE1 1 
ATOM   1939 O  OE2 . GLU A 1 237 ? 20.247 -10.508 -3.257  1.00 20.98 ? 238 GLU A OE2 1 
ATOM   1940 N  N   . GLU A 1 238 ? 24.615 -8.861  -0.239  1.00 11.40 ? 239 GLU A N   1 
ATOM   1941 C  CA  . GLU A 1 238 ? 24.594 -9.275  1.157   1.00 11.65 ? 239 GLU A CA  1 
ATOM   1942 C  C   . GLU A 1 238 ? 23.166 -9.153  1.645   1.00 9.25  ? 239 GLU A C   1 
ATOM   1943 O  O   . GLU A 1 238 ? 22.647 -8.037  1.722   1.00 11.19 ? 239 GLU A O   1 
ATOM   1944 C  CB  . GLU A 1 238 ? 25.492 -8.352  1.982   1.00 15.15 ? 239 GLU A CB  1 
ATOM   1945 C  CG  . GLU A 1 238 ? 25.704 -8.912  3.368   1.00 22.45 ? 239 GLU A CG  1 
ATOM   1946 C  CD  . GLU A 1 238 ? 26.521 -10.204 3.478   1.00 30.42 ? 239 GLU A CD  1 
ATOM   1947 O  OE1 . GLU A 1 238 ? 27.632 -10.279 2.863   1.00 40.00 ? 239 GLU A OE1 1 
ATOM   1948 O  OE2 . GLU A 1 238 ? 26.072 -11.118 4.209   1.00 30.08 ? 239 GLU A OE2 1 
ATOM   1949 N  N   . LEU A 1 239 ? 22.492 -10.283 1.909   1.00 8.86  ? 240 LEU A N   1 
ATOM   1950 C  CA  . LEU A 1 239 ? 21.094 -10.212 2.275   1.00 8.41  ? 240 LEU A CA  1 
ATOM   1951 C  C   . LEU A 1 239 ? 20.934 -9.448  3.581   1.00 7.20  ? 240 LEU A C   1 
ATOM   1952 O  O   . LEU A 1 239 ? 21.664 -9.648  4.560   1.00 8.44  ? 240 LEU A O   1 
ATOM   1953 C  CB  . LEU A 1 239 ? 20.552 -11.640 2.463   1.00 10.68 ? 240 LEU A CB  1 
ATOM   1954 C  CG  . LEU A 1 239 ? 20.484 -12.483 1.202   1.00 10.09 ? 240 LEU A CG  1 
ATOM   1955 C  CD1 . LEU A 1 239 ? 19.919 -13.864 1.534   1.00 15.83 ? 240 LEU A CD1 1 
ATOM   1956 C  CD2 . LEU A 1 239 ? 19.636 -11.809 0.103   1.00 12.77 ? 240 LEU A CD2 1 
ATOM   1957 N  N   . MET A 1 240 ? 19.900 -8.601  3.606   1.00 7.05  ? 241 MET A N   1 
ATOM   1958 C  CA  . MET A 1 240 ? 19.576 -7.817  4.798   1.00 7.03  ? 241 MET A CA  1 
ATOM   1959 C  C   . MET A 1 240 ? 18.766 -8.746  5.722   1.00 7.10  ? 241 MET A C   1 
ATOM   1960 O  O   . MET A 1 240 ? 17.546 -8.950  5.591   1.00 7.30  ? 241 MET A O   1 
ATOM   1961 C  CB  . MET A 1 240 ? 18.737 -6.620  4.370   1.00 8.20  ? 241 MET A CB  1 
ATOM   1962 C  CG  . MET A 1 240 ? 18.365 -5.677  5.572   1.00 6.86  ? 241 MET A CG  1 
ATOM   1963 S  SD  . MET A 1 240 ? 17.425 -4.284  5.074   1.00 8.45  ? 241 MET A SD  1 
ATOM   1964 C  CE  . MET A 1 240 ? 18.708 -3.234  4.383   1.00 9.74  ? 241 MET A CE  1 
ATOM   1965 N  N   . VAL A 1 241 ? 19.509 -9.396  6.651   1.00 6.97  ? 242 VAL A N   1 
ATOM   1966 C  CA  . VAL A 1 241 ? 18.939 -10.281 7.659   1.00 5.68  ? 242 VAL A CA  1 
ATOM   1967 C  C   . VAL A 1 241 ? 19.730 -10.066 8.942   1.00 5.33  ? 242 VAL A C   1 
ATOM   1968 O  O   . VAL A 1 241 ? 20.910 -9.647  8.892   1.00 7.10  ? 242 VAL A O   1 
ATOM   1969 C  CB  . VAL A 1 241 ? 19.030 -11.781 7.292   1.00 6.97  ? 242 VAL A CB  1 
ATOM   1970 C  CG1 . VAL A 1 241 ? 18.081 -12.122 6.093   1.00 8.93  ? 242 VAL A CG1 1 
ATOM   1971 C  CG2 . VAL A 1 241 ? 20.502 -12.252 7.032   1.00 9.58  ? 242 VAL A CG2 1 
ATOM   1972 N  N   . ASP A 1 242 ? 19.103 -10.359 10.083  1.00 5.85  ? 243 ASP A N   1 
ATOM   1973 C  CA  . ASP A 1 242 ? 19.795 -10.233 11.360  1.00 5.12  ? 243 ASP A CA  1 
ATOM   1974 C  C   . ASP A 1 242 ? 20.269 -8.817  11.602  1.00 5.42  ? 243 ASP A C   1 
ATOM   1975 O  O   . ASP A 1 242 ? 21.372 -8.574  12.090  1.00 7.80  ? 243 ASP A O   1 
ATOM   1976 C  CB  . ASP A 1 242 ? 20.873 -11.284 11.605  1.00 6.20  ? 243 ASP A CB  1 
ATOM   1977 C  CG  . ASP A 1 242 ? 20.290 -12.679 11.704  1.00 7.44  ? 243 ASP A CG  1 
ATOM   1978 O  OD1 . ASP A 1 242 ? 19.238 -12.835 12.363  1.00 6.96  ? 243 ASP A OD1 1 
ATOM   1979 O  OD2 . ASP A 1 242 ? 20.869 -13.628 11.127  1.00 9.45  ? 243 ASP A OD2 1 
ATOM   1980 N  N   . ASN A 1 243 ? 19.381 -7.852  11.341  1.00 4.62  ? 244 ASN A N   1 
ATOM   1981 C  CA  . ASN A 1 243 ? 19.681 -6.438  11.554  1.00 5.07  ? 244 ASN A CA  1 
ATOM   1982 C  C   . ASN A 1 243 ? 19.095 -6.031  12.900  1.00 5.56  ? 244 ASN A C   1 
ATOM   1983 O  O   . ASN A 1 243 ? 18.394 -5.007  12.970  1.00 6.20  ? 244 ASN A O   1 
ATOM   1984 C  CB  . ASN A 1 243 ? 19.161 -5.593  10.390  1.00 6.26  ? 244 ASN A CB  1 
ATOM   1985 C  CG  . ASN A 1 243 ? 17.683 -5.765  10.119  1.00 5.98  ? 244 ASN A CG  1 
ATOM   1986 O  OD1 . ASN A 1 243 ? 17.011 -6.634  10.675  1.00 7.88  ? 244 ASN A OD1 1 
ATOM   1987 N  ND2 . ASN A 1 243 ? 17.181 -4.918  9.239   1.00 6.73  ? 244 ASN A ND2 1 
ATOM   1988 N  N   . TRP A 1 244 ? 19.422 -6.767  13.945  1.00 5.36  ? 245 TRP A N   1 
ATOM   1989 C  CA  . TRP A 1 244 ? 18.934 -6.491  15.293  1.00 5.14  ? 245 TRP A CA  1 
ATOM   1990 C  C   . TRP A 1 244 ? 20.131 -6.364  16.247  1.00 4.67  ? 245 TRP A C   1 
ATOM   1991 O  O   . TRP A 1 244 ? 21.150 -7.075  16.123  1.00 6.00  ? 245 TRP A O   1 
ATOM   1992 C  CB  . TRP A 1 244 ? 17.958 -7.565  15.777  1.00 4.59  ? 245 TRP A CB  1 
ATOM   1993 C  CG  . TRP A 1 244 ? 18.418 -8.988  15.620  1.00 4.92  ? 245 TRP A CG  1 
ATOM   1994 C  CD1 . TRP A 1 244 ? 18.307 -9.717  14.458  1.00 5.32  ? 245 TRP A CD1 1 
ATOM   1995 C  CD2 . TRP A 1 244 ? 19.028 -9.861  16.597  1.00 5.22  ? 245 TRP A CD2 1 
ATOM   1996 N  NE1 . TRP A 1 244 ? 18.810 -10.998 14.650  1.00 5.24  ? 245 TRP A NE1 1 
ATOM   1997 C  CE2 . TRP A 1 244 ? 19.243 -11.123 15.966  1.00 5.36  ? 245 TRP A CE2 1 
ATOM   1998 C  CE3 . TRP A 1 244 ? 19.277 -9.709  17.985  1.00 6.08  ? 245 TRP A CE3 1 
ATOM   1999 C  CZ2 . TRP A 1 244 ? 19.782 -12.206 16.688  1.00 7.60  ? 245 TRP A CZ2 1 
ATOM   2000 C  CZ3 . TRP A 1 244 ? 19.814 -10.788 18.669  1.00 7.71  ? 245 TRP A CZ3 1 
ATOM   2001 C  CH2 . TRP A 1 244 ? 20.048 -12.020 18.029  1.00 8.56  ? 245 TRP A CH2 1 
ATOM   2002 N  N   . ARG A 1 245 ? 20.010 -5.468  17.194  1.00 4.88  ? 246 ARG A N   1 
ATOM   2003 C  CA  . ARG A 1 245 ? 20.979 -5.371  18.279  1.00 4.74  ? 246 ARG A CA  1 
ATOM   2004 C  C   . ARG A 1 245 ? 20.508 -6.296  19.403  1.00 5.16  ? 246 ARG A C   1 
ATOM   2005 O  O   . ARG A 1 245 ? 19.313 -6.280  19.747  1.00 6.57  ? 246 ARG A O   1 
ATOM   2006 C  CB  . ARG A 1 245 ? 21.046 -3.930  18.791  1.00 5.27  ? 246 ARG A CB  1 
ATOM   2007 C  CG  . ARG A 1 245 ? 22.165 -3.701  19.834  1.00 6.22  ? 246 ARG A CG  1 
ATOM   2008 C  CD  . ARG A 1 245 ? 22.082 -2.330  20.463  1.00 7.76  ? 246 ARG A CD  1 
ATOM   2009 N  NE  . ARG A 1 245 ? 23.338 -1.927  21.080  1.00 6.65  ? 246 ARG A NE  1 
ATOM   2010 C  CZ  . ARG A 1 245 ? 23.458 -0.953  21.975  1.00 6.21  ? 246 ARG A CZ  1 
ATOM   2011 N  NH1 . ARG A 1 245 ? 22.392 -0.274  22.362  1.00 6.54  ? 246 ARG A NH1 1 
ATOM   2012 N  NH2 . ARG A 1 245 ? 24.644 -0.660  22.478  1.00 8.97  ? 246 ARG A NH2 1 
ATOM   2013 N  N   . PRO A 1 246 ? 21.404 -7.099  20.036  1.00 5.78  ? 247 PRO A N   1 
ATOM   2014 C  CA  . PRO A 1 246 ? 20.990 -7.907  21.191  1.00 7.07  ? 247 PRO A CA  1 
ATOM   2015 C  C   . PRO A 1 246 ? 20.648 -7.078  22.428  1.00 6.57  ? 247 PRO A C   1 
ATOM   2016 O  O   . PRO A 1 246 ? 20.978 -5.891  22.562  1.00 6.57  ? 247 PRO A O   1 
ATOM   2017 C  CB  . PRO A 1 246 ? 22.167 -8.826  21.486  1.00 10.20 ? 247 PRO A CB  1 
ATOM   2018 C  CG  . PRO A 1 246 ? 23.120 -8.640  20.328  1.00 13.46 ? 247 PRO A CG  1 
ATOM   2019 C  CD  . PRO A 1 246 ? 22.825 -7.296  19.683  1.00 6.97  ? 247 PRO A CD  1 
ATOM   2020 N  N   . ALA A 1 247 ? 19.984 -7.770  23.365  1.00 6.75  ? 248 ALA A N   1 
ATOM   2021 C  CA  . ALA A 1 247 ? 19.605 -7.145  24.625  1.00 6.88  ? 248 ALA A CA  1 
ATOM   2022 C  C   . ALA A 1 247 ? 20.856 -6.602  25.340  1.00 6.70  ? 248 ALA A C   1 
ATOM   2023 O  O   . ALA A 1 247 ? 21.904 -7.310  25.420  1.00 8.66  ? 248 ALA A O   1 
ATOM   2024 C  CB  . ALA A 1 247 ? 18.833 -8.150  25.477  1.00 9.83  ? 248 ALA A CB  1 
ATOM   2025 N  N   . GLN A 1 248 ? 20.706 -5.439  25.972  1.00 6.48  ? 249 GLN A N   1 
ATOM   2026 C  CA  . GLN A 1 248 ? 21.763 -4.733  26.683  1.00 5.77  ? 249 GLN A CA  1 
ATOM   2027 C  C   . GLN A 1 248 ? 21.448 -4.773  28.162  1.00 6.70  ? 249 GLN A C   1 
ATOM   2028 O  O   . GLN A 1 248 ? 20.299 -5.001  28.590  1.00 8.29  ? 249 GLN A O   1 
ATOM   2029 C  CB  . GLN A 1 248 ? 21.771 -3.286  26.189  1.00 6.94  ? 249 GLN A CB  1 
ATOM   2030 C  CG  . GLN A 1 248 ? 22.088 -3.212  24.696  1.00 8.04  ? 249 GLN A CG  1 
ATOM   2031 C  CD  . GLN A 1 248 ? 23.423 -3.856  24.354  1.00 7.93  ? 249 GLN A CD  1 
ATOM   2032 O  OE1 . GLN A 1 248 ? 24.480 -3.544  24.919  1.00 11.75 ? 249 GLN A OE1 1 
ATOM   2033 N  NE2 . GLN A 1 248 ? 23.413 -4.770  23.383  1.00 9.37  ? 249 GLN A NE2 1 
ATOM   2034 N  N   . PRO A 1 249 ? 22.437 -4.485  29.026  1.00 8.80  ? 250 PRO A N   1 
ATOM   2035 C  CA  . PRO A 1 249 ? 22.193 -4.585  30.464  1.00 10.33 ? 250 PRO A CA  1 
ATOM   2036 C  C   . PRO A 1 249 ? 21.153 -3.564  30.929  1.00 8.90  ? 250 PRO A C   1 
ATOM   2037 O  O   . PRO A 1 249 ? 21.178 -2.384  30.554  1.00 9.84  ? 250 PRO A O   1 
ATOM   2038 C  CB  . PRO A 1 249 ? 23.595 -4.215  31.069  1.00 15.36 ? 250 PRO A CB  1 
ATOM   2039 C  CG  . PRO A 1 249 ? 24.567 -4.576  29.988  1.00 16.03 ? 250 PRO A CG  1 
ATOM   2040 C  CD  . PRO A 1 249 ? 23.855 -4.192  28.696  1.00 13.17 ? 250 PRO A CD  1 
ATOM   2041 N  N   . LEU A 1 250 ? 20.232 -4.010  31.800  1.00 10.05 ? 251 LEU A N   1 
ATOM   2042 C  CA  . LEU A 1 250 ? 19.183 -3.134  32.287  1.00 8.59  ? 251 LEU A CA  1 
ATOM   2043 C  C   . LEU A 1 250 ? 19.737 -2.070  33.237  1.00 9.11  ? 251 LEU A C   1 
ATOM   2044 O  O   . LEU A 1 250 ? 19.235 -0.948  33.317  1.00 10.49 ? 251 LEU A O   1 
ATOM   2045 C  CB  . LEU A 1 250 ? 18.159 -4.025  33.018  1.00 11.94 ? 251 LEU A CB  1 
ATOM   2046 C  CG  . LEU A 1 250 ? 16.849 -3.336  33.418  1.00 13.14 ? 251 LEU A CG  1 
ATOM   2047 C  CD1 . LEU A 1 250 ? 16.116 -2.752  32.195  1.00 11.06 ? 251 LEU A CD1 1 
ATOM   2048 C  CD2 . LEU A 1 250 ? 15.975 -4.307  34.172  1.00 15.98 ? 251 LEU A CD2 1 
ATOM   2049 N  N   . LYS A 1 251 ? 20.802 -2.389  33.953  1.00 10.16 ? 252 LYS A N   1 
ATOM   2050 C  CA  . LYS A 1 251 ? 21.430 -1.441  34.881  1.00 11.78 ? 252 LYS A CA  1 
ATOM   2051 C  C   . LYS A 1 251 ? 20.406 -0.869  35.862  1.00 13.27 ? 252 LYS A C   1 
ATOM   2052 O  O   . LYS A 1 251 ? 19.637 -1.662  36.397  1.00 17.20 ? 252 LYS A O   1 
ATOM   2053 C  CB  . LYS A 1 251 ? 22.245 -0.384  34.138  1.00 14.24 ? 252 LYS A CB  1 
ATOM   2054 C  CG  . LYS A 1 251 ? 23.433 -1.038  33.449  1.00 16.88 ? 252 LYS A CG  1 
ATOM   2055 C  CD  . LYS A 1 251 ? 24.309 -0.121  32.639  1.00 22.13 ? 252 LYS A CD  1 
ATOM   2056 C  CE  . LYS A 1 251 ? 25.651 -0.763  32.374  1.00 23.34 ? 252 LYS A CE  1 
ATOM   2057 N  NZ  . LYS A 1 251 ? 26.502 0.104   31.532  1.00 27.06 ? 252 LYS A NZ  1 
ATOM   2058 N  N   . ASN A 1 252 ? 20.413 0.445   36.140  1.00 12.06 ? 253 ASN A N   1 
ATOM   2059 C  CA  . ASN A 1 252 ? 19.555 0.956   37.203  1.00 20.09 ? 253 ASN A CA  1 
ATOM   2060 C  C   . ASN A 1 252 ? 18.200 1.351   36.619  1.00 24.14 ? 253 ASN A C   1 
ATOM   2061 O  O   . ASN A 1 252 ? 17.862 2.537   36.794  1.00 38.27 ? 253 ASN A O   1 
ATOM   2062 C  CB  . ASN A 1 252 ? 20.246 2.127   37.921  1.00 26.46 ? 253 ASN A CB  1 
ATOM   2063 C  CG  . ASN A 1 252 ? 19.557 2.551   39.210  1.00 31.90 ? 253 ASN A CG  1 
ATOM   2064 O  OD1 . ASN A 1 252 ? 19.389 1.746   40.124  1.00 57.31 ? 253 ASN A OD1 1 
ATOM   2065 N  ND2 . ASN A 1 252 ? 19.230 3.833   39.328  1.00 42.54 ? 253 ASN A ND2 1 
ATOM   2066 N  N   . ARG A 1 253 ? 17.516 0.401   35.905  1.00 12.66 ? 254 ARG A N   1 
ATOM   2067 C  CA  . ARG A 1 253 ? 16.198 0.710   35.377  1.00 10.06 ? 254 ARG A CA  1 
ATOM   2068 C  C   . ARG A 1 253 ? 15.155 -0.280  35.832  1.00 10.44 ? 254 ARG A C   1 
ATOM   2069 O  O   . ARG A 1 253 ? 15.459 -1.439  36.046  1.00 16.30 ? 254 ARG A O   1 
ATOM   2070 C  CB  . ARG A 1 253 ? 16.285 0.761   33.847  1.00 8.17  ? 254 ARG A CB  1 
ATOM   2071 C  CG  . ARG A 1 253 ? 17.118 1.960   33.393  1.00 8.64  ? 254 ARG A CG  1 
ATOM   2072 C  CD  . ARG A 1 253 ? 17.244 1.927   31.881  1.00 7.67  ? 254 ARG A CD  1 
ATOM   2073 N  NE  . ARG A 1 253 ? 18.077 0.830   31.398  1.00 6.73  ? 254 ARG A NE  1 
ATOM   2074 C  CZ  . ARG A 1 253 ? 18.313 0.578   30.112  1.00 5.65  ? 254 ARG A CZ  1 
ATOM   2075 N  NH1 . ARG A 1 253 ? 17.727 1.255   29.128  1.00 6.57  ? 254 ARG A NH1 1 
ATOM   2076 N  NH2 . ARG A 1 253 ? 19.171 -0.408  29.792  1.00 5.57  ? 254 ARG A NH2 1 
ATOM   2077 N  N   . GLN A 1 254 ? 13.932 0.229   35.933  1.00 10.88 ? 255 GLN A N   1 
ATOM   2078 C  CA  . GLN A 1 254 ? 12.768 -0.617  36.190  1.00 12.27 ? 255 GLN A CA  1 
ATOM   2079 C  C   . GLN A 1 254 ? 11.842 -0.537  34.977  1.00 9.75  ? 255 GLN A C   1 
ATOM   2080 O  O   . GLN A 1 254 ? 11.575 0.546   34.430  1.00 17.29 ? 255 GLN A O   1 
ATOM   2081 C  CB  . GLN A 1 254 ? 12.031 -0.077  37.419  1.00 16.88 ? 255 GLN A CB  1 
ATOM   2082 C  CG  . GLN A 1 254 ? 12.636 -0.555  38.720  1.00 31.39 ? 255 GLN A CG  1 
ATOM   2083 C  CD  . GLN A 1 254 ? 11.690 -0.549  39.911  1.00 47.36 ? 255 GLN A CD  1 
ATOM   2084 O  OE1 . GLN A 1 254 ? 12.116 -0.253  41.038  1.00 58.31 ? 255 GLN A OE1 1 
ATOM   2085 N  NE2 . GLN A 1 254 ? 10.413 -0.907  39.687  1.00 39.90 ? 255 GLN A NE2 1 
ATOM   2086 N  N   . ILE A 1 255 ? 11.446 -1.688  34.479  1.00 9.27  ? 256 ILE A N   1 
ATOM   2087 C  CA  . ILE A 1 255 ? 10.420 -1.761  33.448  1.00 8.29  ? 256 ILE A CA  1 
ATOM   2088 C  C   . ILE A 1 255 ? 9.057  -1.735  34.124  1.00 8.51  ? 256 ILE A C   1 
ATOM   2089 O  O   . ILE A 1 255 ? 8.788  -2.465  35.069  1.00 9.86  ? 256 ILE A O   1 
ATOM   2090 C  CB  . ILE A 1 255 ? 10.625 -3.021  32.605  1.00 8.68  ? 256 ILE A CB  1 
ATOM   2091 C  CG1 . ILE A 1 255 ? 12.066 -3.031  32.018  1.00 9.96  ? 256 ILE A CG1 1 
ATOM   2092 C  CG2 . ILE A 1 255 ? 9.558  -3.040  31.486  1.00 10.07 ? 256 ILE A CG2 1 
ATOM   2093 C  CD1 . ILE A 1 255 ? 12.371 -4.251  31.162  1.00 11.19 ? 256 ILE A CD1 1 
ATOM   2094 N  N   . LYS A 1 256 ? 8.189  -0.853  33.611  1.00 6.95  ? 257 LYS A N   1 
ATOM   2095 C  CA  . LYS A 1 256 ? 6.833  -0.714  34.148  1.00 7.72  ? 257 LYS A CA  1 
ATOM   2096 C  C   . LYS A 1 256 ? 5.842  -1.349  33.165  1.00 6.61  ? 257 LYS A C   1 
ATOM   2097 O  O   . LYS A 1 256 ? 6.028  -1.234  31.961  1.00 9.47  ? 257 LYS A O   1 
ATOM   2098 C  CB  . LYS A 1 256 ? 6.510  0.774   34.426  1.00 9.55  ? 257 LYS A CB  1 
ATOM   2099 C  CG  . LYS A 1 256 ? 7.438  1.492   35.445  1.00 19.06 ? 257 LYS A CG  1 
ATOM   2100 N  N   . ALA A 1 257 ? 4.811  -1.969  33.698  1.00 8.59  ? 258 ALA A N   1 
ATOM   2101 C  CA  . ALA A 1 257 ? 3.731  -2.577  32.920  1.00 8.95  ? 258 ALA A CA  1 
ATOM   2102 C  C   . ALA A 1 257 ? 2.437  -1.796  33.100  1.00 8.21  ? 258 ALA A C   1 
ATOM   2103 O  O   . ALA A 1 257 ? 2.090  -1.404  34.227  1.00 10.67 ? 258 ALA A O   1 
ATOM   2104 C  CB  . ALA A 1 257 ? 3.528  -4.023  33.297  1.00 11.27 ? 258 ALA A CB  1 
ATOM   2105 N  N   . SER A 1 258 ? 1.701  -1.612  32.002  1.00 8.17  ? 259 SER A N   1 
ATOM   2106 C  CA  . SER A 1 258 ? 0.393  -0.953  32.082  1.00 9.49  ? 259 SER A CA  1 
ATOM   2107 C  C   . SER A 1 258 ? -0.744 -1.897  32.443  1.00 9.86  ? 259 SER A C   1 
ATOM   2108 O  O   . SER A 1 258 ? -1.877 -1.393  32.576  1.00 16.46 ? 259 SER A O   1 
ATOM   2109 C  CB  . SER A 1 258 ? 0.060  -0.346  30.734  1.00 11.01 ? 259 SER A CB  1 
ATOM   2110 O  OG  . SER A 1 258 ? -0.349 -1.352  29.795  1.00 9.72  ? 259 SER A OG  1 
ATOM   2111 N  N   . PHE A 1 259 ? -0.419 -3.171  32.738  1.00 11.55 ? 260 PHE A N   1 
ATOM   2112 C  CA  . PHE A 1 259 ? -1.399 -4.252  32.914  1.00 13.60 ? 260 PHE A CA  1 
ATOM   2113 C  C   . PHE A 1 259 ? -0.859 -5.190  33.992  1.00 19.34 ? 260 PHE A C   1 
ATOM   2114 O  O   . PHE A 1 259 ? 0.355  -5.228  34.246  1.00 18.66 ? 260 PHE A O   1 
ATOM   2115 C  CB  . PHE A 1 259 ? -1.637 -4.968  31.568  1.00 13.83 ? 260 PHE A CB  1 
ATOM   2116 C  CG  . PHE A 1 259 ? -0.390 -5.656  31.065  1.00 12.78 ? 260 PHE A CG  1 
ATOM   2117 C  CD1 . PHE A 1 259 ? 0.587  -4.951  30.365  1.00 10.61 ? 260 PHE A CD1 1 
ATOM   2118 C  CD2 . PHE A 1 259 ? -0.155 -7.006  31.369  1.00 17.15 ? 260 PHE A CD2 1 
ATOM   2119 C  CE1 . PHE A 1 259 ? 1.746  -5.581  29.944  1.00 12.80 ? 260 PHE A CE1 1 
ATOM   2120 C  CE2 . PHE A 1 259 ? 1.024  -7.623  30.953  1.00 18.34 ? 260 PHE A CE2 1 
ATOM   2121 C  CZ  . PHE A 1 259 ? 1.982  -6.911  30.231  1.00 14.67 ? 260 PHE A CZ  1 
ATOM   2122 N  N   . LYS A 1 260 ? -1.800 -5.961  34.557  1.00 27.01 ? 261 LYS A N   1 
ATOM   2123 C  CA  . LYS A 1 260 ? -1.700 -7.060  35.514  1.00 41.70 ? 261 LYS A CA  1 
ATOM   2124 C  C   . LYS A 1 260 ? -2.294 -6.646  36.877  1.00 45.26 ? 261 LYS A C   1 
ATOM   2125 O  O   . LYS A 1 260 ? -1.625 -6.508  37.885  1.00 64.78 ? 261 LYS A O   1 
ATOM   2126 C  CB  . LYS A 1 260 ? -0.315 -7.724  35.617  1.00 56.85 ? 261 LYS A CB  1 
ATOM   2127 O  OXT . LYS A 1 260 ? -3.484 -6.413  37.035  1.00 51.23 ? 261 LYS A OXT 1 
HETATM 2128 ZN ZN  . ZN  B 2 .   ? 14.384 0.010   15.479  1.00 4.69  ? 301 ZN  A ZN  1 
HETATM 2129 F  F20 . V14 C 3 .   ? 15.019 5.321   15.693  1.00 11.69 ? 302 V14 A F20 1 
HETATM 2130 C  C5  . V14 C 3 .   ? 15.642 4.487   14.802  1.00 11.21 ? 302 V14 A C5  1 
HETATM 2131 C  C4  . V14 C 3 .   ? 15.990 3.178   15.197  1.00 8.21  ? 302 V14 A C4  1 
HETATM 2132 S  S7  . V14 C 3 .   ? 15.345 2.606   16.783  1.00 6.92  ? 302 V14 A S7  1 
HETATM 2133 O  O9  . V14 C 3 .   ? 13.946 3.025   16.712  1.00 6.59  ? 302 V14 A O9  1 
HETATM 2134 N  N10 . V14 C 3 .   ? 15.477 0.982   16.676  1.00 7.60  ? 302 V14 A N10 1 
HETATM 2135 O  O8  . V14 C 3 .   ? 16.192 3.145   17.803  1.00 7.02  ? 302 V14 A O8  1 
HETATM 2136 C  C3  . V14 C 3 .   ? 16.590 2.380   14.228  1.00 9.24  ? 302 V14 A C3  1 
HETATM 2137 F  F12 . V14 C 3 .   ? 16.950 1.115   14.459  1.00 11.81 ? 302 V14 A F12 1 
HETATM 2138 C  C2  . V14 C 3 .   ? 16.804 2.847   12.993  1.00 11.13 ? 302 V14 A C2  1 
HETATM 2139 F  F13 . V14 C 3 .   ? 17.339 1.964   12.121  1.00 15.43 ? 302 V14 A F13 1 
HETATM 2140 C  C6  . V14 C 3 .   ? 15.854 4.983   13.517  1.00 11.51 ? 302 V14 A C6  1 
HETATM 2141 C  C1  . V14 C 3 .   ? 16.487 4.135   12.572  1.00 10.79 ? 302 V14 A C1  1 
HETATM 2142 S  S11 . V14 C 3 .   ? 16.786 4.425   10.854  1.00 16.15 ? 302 V14 A S11 1 
HETATM 2143 O  O16 . V14 C 3 .   ? 16.430 5.890   10.627  1.00 18.89 ? 302 V14 A O16 1 
HETATM 2144 O  O17 . V14 C 3 .   ? 15.844 3.462   10.046  1.00 19.95 ? 302 V14 A O17 1 
HETATM 2145 C  C15 . V14 C 3 .   ? 18.420 3.926   10.465  1.00 18.22 ? 302 V14 A C15 1 
HETATM 2146 C  C18 . V14 C 3 .   ? 19.625 4.333   11.243  1.00 25.98 ? 302 V14 A C18 1 
HETATM 2147 O  O21 . V14 C 3 .   ? 19.357 5.572   11.733  1.00 35.75 ? 302 V14 A O21 1 
HETATM 2148 N  N19 . V14 C 3 .   ? 15.408 6.326   13.218  1.00 13.94 ? 302 V14 A N19 1 
HETATM 2149 C  C14 . V14 C 3 .   ? 15.465 7.508   14.100  1.00 16.16 ? 302 V14 A C14 1 
HETATM 2150 C  C28 . V14 C 3 .   ? 16.966 7.606   14.638  1.00 20.82 ? 302 V14 A C28 1 
HETATM 2151 C  C27 . V14 C 3 .   ? 17.926 8.335   13.753  1.00 30.89 ? 302 V14 A C27 1 
HETATM 2152 C  C26 . V14 C 3 .   ? 18.043 9.862   13.876  1.00 29.30 ? 302 V14 A C26 1 
HETATM 2153 C  C25 . V14 C 3 .   ? 16.824 10.771  13.756  1.00 37.19 ? 302 V14 A C25 1 
HETATM 2154 C  C24 . V14 C 3 .   ? 15.763 10.639  14.852  1.00 29.88 ? 302 V14 A C24 1 
HETATM 2155 C  C23 . V14 C 3 .   ? 14.472 9.977   14.287  1.00 21.82 ? 302 V14 A C23 1 
HETATM 2156 C  C22 . V14 C 3 .   ? 14.798 8.692   13.392  1.00 20.35 ? 302 V14 A C22 1 
HETATM 2157 S  S   . DMS D 4 .   ? 22.438 -9.961  14.988  1.00 14.59 ? 303 DMS A S   1 
HETATM 2158 O  O   . DMS D 4 .   ? 23.197 -11.218 14.643  1.00 22.84 ? 303 DMS A O   1 
HETATM 2159 C  C1  . DMS D 4 .   ? 23.562 -8.656  14.577  1.00 15.15 ? 303 DMS A C1  1 
HETATM 2160 C  C2  . DMS D 4 .   ? 22.659 -9.842  16.718  1.00 13.20 ? 303 DMS A C2  1 
HETATM 2161 C  C1  . PEG E 5 .   ? 33.790 7.457   27.084  1.00 56.45 ? 304 PEG A C1  1 
HETATM 2162 O  O1  . PEG E 5 .   ? 33.488 6.036   27.404  1.00 45.29 ? 304 PEG A O1  1 
HETATM 2163 C  C2  . PEG E 5 .   ? 34.281 7.639   25.654  1.00 59.19 ? 304 PEG A C2  1 
HETATM 2164 O  O2  . PEG E 5 .   ? 35.381 6.765   25.368  1.00 40.07 ? 304 PEG A O2  1 
HETATM 2165 C  C3  . PEG E 5 .   ? 35.443 6.275   24.008  1.00 34.08 ? 304 PEG A C3  1 
HETATM 2166 C  C4  . PEG E 5 .   ? 35.797 4.765   23.931  1.00 25.03 ? 304 PEG A C4  1 
HETATM 2167 O  O4  . PEG E 5 .   ? 35.067 3.987   22.924  1.00 25.31 ? 304 PEG A O4  1 
HETATM 2168 C  C1  . PEG F 5 .   ? 21.312 6.110   2.527   1.00 46.28 ? 305 PEG A C1  1 
HETATM 2169 O  O1  . PEG F 5 .   ? 22.253 5.174   2.004   1.00 36.84 ? 305 PEG A O1  1 
HETATM 2170 C  C2  . PEG F 5 .   ? 19.977 6.099   1.801   1.00 37.01 ? 305 PEG A C2  1 
HETATM 2171 O  O2  . PEG F 5 .   ? 19.434 7.421   1.702   1.00 53.67 ? 305 PEG A O2  1 
HETATM 2172 C  C3  . PEG F 5 .   ? 19.490 7.978   0.390   1.00 51.26 ? 305 PEG A C3  1 
HETATM 2173 C  C4  . PEG F 5 .   ? 18.119 8.095   -0.193  1.00 31.27 ? 305 PEG A C4  1 
HETATM 2174 O  O4  . PEG F 5 .   ? 18.092 7.905   -1.617  1.00 23.55 ? 305 PEG A O4  1 
HETATM 2175 C  C1  . MLA G 6 .   ? 17.513 7.157   7.615   1.00 38.05 ? 306 MLA A C1  1 
HETATM 2176 O  O1A . MLA G 6 .   ? 16.770 7.182   8.637   1.00 28.84 ? 306 MLA A O1A 1 
HETATM 2177 O  O1B . MLA G 6 .   ? 18.413 6.333   7.473   1.00 40.91 ? 306 MLA A O1B 1 
HETATM 2178 C  C2  . MLA G 6 .   ? 17.265 8.184   6.472   1.00 42.32 ? 306 MLA A C2  1 
HETATM 2179 C  C3  . MLA G 6 .   ? 17.301 9.722   6.859   1.00 75.43 ? 306 MLA A C3  1 
HETATM 2180 O  O3A . MLA G 6 .   ? 18.514 10.255  6.874   1.00 84.50 ? 306 MLA A O3A 1 
HETATM 2181 O  O3B . MLA G 6 .   ? 16.293 10.380  7.258   1.00 90.28 ? 306 MLA A O3B 1 
HETATM 2182 C  C1  . EDO H 7 .   ? 14.271 9.653   9.827   1.00 30.59 ? 307 EDO A C1  1 
HETATM 2183 O  O1  . EDO H 7 .   ? 14.834 8.394   9.491   1.00 37.68 ? 307 EDO A O1  1 
HETATM 2184 C  C2  . EDO H 7 .   ? 13.016 9.837   9.073   1.00 37.40 ? 307 EDO A C2  1 
HETATM 2185 O  O2  . EDO H 7 .   ? 13.224 10.306  7.764   1.00 47.86 ? 307 EDO A O2  1 
HETATM 2186 C  C   . BEZ I 8 .   ? 26.495 -4.987  7.140   1.00 29.76 ? 308 BEZ A C   1 
HETATM 2187 O  O1  . BEZ I 8 .   ? 27.266 -4.067  6.659   1.00 29.09 ? 308 BEZ A O1  1 
HETATM 2188 O  O2  . BEZ I 8 .   ? 25.450 -4.749  7.887   1.00 18.07 ? 308 BEZ A O2  1 
HETATM 2189 C  C1  . BEZ I 8 .   ? 26.880 -6.448  6.872   1.00 35.72 ? 308 BEZ A C1  1 
HETATM 2190 C  C2  . BEZ I 8 .   ? 28.090 -6.756  6.245   1.00 41.58 ? 308 BEZ A C2  1 
HETATM 2191 C  C3  . BEZ I 8 .   ? 28.449 -8.079  6.020   1.00 42.29 ? 308 BEZ A C3  1 
HETATM 2192 C  C4  . BEZ I 8 .   ? 27.607 -9.104  6.421   1.00 48.78 ? 308 BEZ A C4  1 
HETATM 2193 C  C5  . BEZ I 8 .   ? 26.400 -8.812  7.049   1.00 40.97 ? 308 BEZ A C5  1 
HETATM 2194 C  C6  . BEZ I 8 .   ? 26.035 -7.489  7.277   1.00 30.67 ? 308 BEZ A C6  1 
HETATM 2195 S  S   . DMS J 4 .   ? 12.760 -19.737 8.690   1.00 33.02 ? 309 DMS A S   1 
HETATM 2196 O  O   . DMS J 4 .   ? 13.076 -20.284 10.188  1.00 24.51 ? 309 DMS A O   1 
HETATM 2197 C  C1  . DMS J 4 .   ? 11.694 -21.026 8.001   1.00 36.47 ? 309 DMS A C1  1 
HETATM 2198 C  C2  . DMS J 4 .   ? 14.223 -20.108 7.676   1.00 30.83 ? 309 DMS A C2  1 
HETATM 2199 C  C   . BEZ K 8 .   ? 10.321 -9.971  -3.615  1.00 28.80 ? 310 BEZ A C   1 
HETATM 2200 O  O1  . BEZ K 8 .   ? 10.547 -10.863 -4.510  1.00 40.83 ? 310 BEZ A O1  1 
HETATM 2201 O  O2  . BEZ K 8 .   ? 9.190  -9.735  -3.078  1.00 32.89 ? 310 BEZ A O2  1 
HETATM 2202 C  C1  . BEZ K 8 .   ? 11.471 -9.137  -3.186  1.00 27.75 ? 310 BEZ A C1  1 
HETATM 2203 C  C2  . BEZ K 8 .   ? 11.475 -8.504  -1.928  1.00 22.92 ? 310 BEZ A C2  1 
HETATM 2204 C  C3  . BEZ K 8 .   ? 12.579 -7.740  -1.560  1.00 23.66 ? 310 BEZ A C3  1 
HETATM 2205 C  C4  . BEZ K 8 .   ? 13.650 -7.573  -2.434  1.00 25.98 ? 310 BEZ A C4  1 
HETATM 2206 C  C5  . BEZ K 8 .   ? 13.669 -8.223  -3.666  1.00 22.46 ? 310 BEZ A C5  1 
HETATM 2207 C  C6  . BEZ K 8 .   ? 12.576 -9.009  -4.043  1.00 27.81 ? 310 BEZ A C6  1 
HETATM 2208 O  O   . HOH L 9 .   ? -4.420 -8.732  17.858  1.00 26.77 ? 401 HOH A O   1 
HETATM 2209 O  O   . HOH L 9 .   ? 9.872  -13.353 33.996  1.00 30.53 ? 402 HOH A O   1 
HETATM 2210 O  O   . HOH L 9 .   ? 20.236 5.105   7.928   1.00 52.21 ? 403 HOH A O   1 
HETATM 2211 O  O   . HOH L 9 .   ? 21.111 11.544  18.233  1.00 39.49 ? 404 HOH A O   1 
HETATM 2212 O  O   . HOH L 9 .   ? 11.700 11.706  6.693   1.00 44.43 ? 405 HOH A O   1 
HETATM 2213 O  O   . HOH L 9 .   ? 3.271  21.095  6.192   1.00 11.69 ? 406 HOH A O   1 
HETATM 2214 O  O   . HOH L 9 .   ? 4.600  7.266   -7.909  1.00 32.01 ? 407 HOH A O   1 
HETATM 2215 O  O   . HOH L 9 .   ? 6.890  -6.779  -5.225  1.00 25.15 ? 408 HOH A O   1 
HETATM 2216 O  O   . HOH L 9 .   ? 6.691  -16.744 18.865  1.00 38.87 ? 409 HOH A O   1 
HETATM 2217 O  O   . HOH L 9 .   ? 6.679  -14.821 28.913  1.00 30.79 ? 410 HOH A O   1 
HETATM 2218 O  O   . HOH L 9 .   ? 21.606 -7.063  -5.430  1.00 39.43 ? 411 HOH A O   1 
HETATM 2219 O  O   . HOH L 9 .   ? 34.594 2.123   24.520  1.00 18.80 ? 412 HOH A O   1 
HETATM 2220 O  O   . HOH L 9 .   ? 15.071 9.864   5.119   1.00 29.62 ? 413 HOH A O   1 
HETATM 2221 O  O   . HOH L 9 .   ? -4.628 11.481  13.547  1.00 36.18 ? 414 HOH A O   1 
HETATM 2222 O  O   . HOH L 9 .   ? 10.490 -3.657  38.030  1.00 47.81 ? 415 HOH A O   1 
HETATM 2223 O  O   . HOH L 9 .   ? 15.400 18.610  27.186  1.00 40.40 ? 416 HOH A O   1 
HETATM 2224 O  O   . HOH L 9 .   ? 0.604  7.812   32.634  1.00 36.98 ? 417 HOH A O   1 
HETATM 2225 O  O   . HOH L 9 .   ? 22.619 -13.680 14.269  1.00 41.54 ? 418 HOH A O   1 
HETATM 2226 O  O   . HOH L 9 .   ? 10.473 2.859   34.366  1.00 43.37 ? 419 HOH A O   1 
HETATM 2227 O  O   . HOH L 9 .   ? 14.923 -2.745  -6.397  1.00 25.46 ? 420 HOH A O   1 
HETATM 2228 O  O   . HOH L 9 .   ? -2.157 -11.832 11.231  1.00 59.44 ? 421 HOH A O   1 
HETATM 2229 O  O   . HOH L 9 .   ? 24.607 6.746   30.146  1.00 20.08 ? 422 HOH A O   1 
HETATM 2230 O  O   . HOH L 9 .   ? 5.790  -8.682  37.379  1.00 25.60 ? 423 HOH A O   1 
HETATM 2231 O  O   . HOH L 9 .   ? 22.727 -13.763 -4.774  1.00 41.86 ? 424 HOH A O   1 
HETATM 2232 O  O   . HOH L 9 .   ? 1.406  -2.193  41.331  1.00 47.04 ? 425 HOH A O   1 
HETATM 2233 O  O   . HOH L 9 .   ? 20.587 15.977  16.566  1.00 34.53 ? 426 HOH A O   1 
HETATM 2234 O  O   . HOH L 9 .   ? -0.701 -12.400 18.618  1.00 42.34 ? 427 HOH A O   1 
HETATM 2235 O  O   . HOH L 9 .   ? -3.923 -9.090  23.709  1.00 38.99 ? 428 HOH A O   1 
HETATM 2236 O  O   . HOH L 9 .   ? 0.527  10.349  29.967  1.00 28.36 ? 429 HOH A O   1 
HETATM 2237 O  O   . HOH L 9 .   ? 32.658 1.385   16.017  1.00 26.43 ? 430 HOH A O   1 
HETATM 2238 O  O   . HOH L 9 .   ? 25.472 -1.749  26.537  1.00 19.29 ? 431 HOH A O   1 
HETATM 2239 O  O   . HOH L 9 .   ? 10.629 10.487  25.572  1.00 11.62 ? 432 HOH A O   1 
HETATM 2240 O  O   . HOH L 9 .   ? 23.226 9.703   27.931  1.00 23.79 ? 433 HOH A O   1 
HETATM 2241 O  O   . HOH L 9 .   ? 4.503  -13.203 33.137  1.00 40.88 ? 434 HOH A O   1 
HETATM 2242 O  O   . HOH L 9 .   ? 14.248 -18.312 19.701  1.00 25.74 ? 435 HOH A O   1 
HETATM 2243 O  O   . HOH L 9 .   ? 7.630  -20.593 11.400  1.00 19.82 ? 436 HOH A O   1 
HETATM 2244 O  O   . HOH L 9 .   ? 4.708  16.110  33.339  1.00 34.34 ? 437 HOH A O   1 
HETATM 2245 O  O   . HOH L 9 .   ? -6.171 -5.627  26.121  1.00 40.96 ? 438 HOH A O   1 
HETATM 2246 O  O   . HOH L 9 .   ? 19.781 -2.241  15.792  1.00 8.85  ? 439 HOH A O   1 
HETATM 2247 O  O   . HOH L 9 .   ? 19.772 10.548  28.429  1.00 44.30 ? 440 HOH A O   1 
HETATM 2248 O  O   . HOH L 9 .   ? 25.615 1.198   -5.352  1.00 33.02 ? 441 HOH A O   1 
HETATM 2249 O  O   . HOH L 9 .   ? 28.880 -3.216  -0.434  1.00 38.92 ? 442 HOH A O   1 
HETATM 2250 O  O   . HOH L 9 .   ? -0.425 21.380  17.435  1.00 37.94 ? 443 HOH A O   1 
HETATM 2251 O  O   . HOH L 9 .   ? 32.384 -5.326  22.403  1.00 27.22 ? 444 HOH A O   1 
HETATM 2252 O  O   . HOH L 9 .   ? -4.768 8.008   26.973  1.00 25.92 ? 445 HOH A O   1 
HETATM 2253 O  O   . HOH L 9 .   ? 18.587 -1.441  11.475  1.00 36.55 ? 446 HOH A O   1 
HETATM 2254 O  O   . HOH L 9 .   ? 1.755  -19.025 5.162   1.00 22.99 ? 447 HOH A O   1 
HETATM 2255 O  O   . HOH L 9 .   ? 18.977 -2.692  -6.936  1.00 31.73 ? 448 HOH A O   1 
HETATM 2256 O  O   . HOH L 9 .   ? 33.896 8.006   15.375  1.00 41.60 ? 449 HOH A O   1 
HETATM 2257 O  O   . HOH L 9 .   ? 10.618 -17.700 20.025  1.00 30.04 ? 450 HOH A O   1 
HETATM 2258 O  O   . HOH L 9 .   ? 2.562  -10.475 -3.502  1.00 37.60 ? 451 HOH A O   1 
HETATM 2259 O  O   . HOH L 9 .   ? 17.370 -10.993 -2.887  1.00 25.21 ? 452 HOH A O   1 
HETATM 2260 O  O   . HOH L 9 .   ? -2.921 10.610  20.281  1.00 23.18 ? 453 HOH A O   1 
HETATM 2261 O  O   . HOH L 9 .   ? 8.904  14.306  29.475  1.00 37.34 ? 454 HOH A O   1 
HETATM 2262 O  O   . HOH L 9 .   ? 3.246  12.442  11.392  1.00 16.87 ? 455 HOH A O   1 
HETATM 2263 O  O   . HOH L 9 .   ? 20.898 2.798   34.580  1.00 26.29 ? 456 HOH A O   1 
HETATM 2264 O  O   . HOH L 9 .   ? 5.898  21.544  13.180  1.00 19.32 ? 457 HOH A O   1 
HETATM 2265 O  O   . HOH L 9 .   ? 21.214 0.877   -4.677  1.00 12.08 ? 458 HOH A O   1 
HETATM 2266 O  O   . HOH L 9 .   ? 22.901 -13.873 9.382   1.00 17.74 ? 459 HOH A O   1 
HETATM 2267 O  O   . HOH L 9 .   ? 16.296 -10.172 32.119  1.00 26.45 ? 460 HOH A O   1 
HETATM 2268 O  O   . HOH L 9 .   ? 13.085 -13.649 11.359  1.00 8.22  ? 461 HOH A O   1 
HETATM 2269 O  O   . HOH L 9 .   ? -4.691 -3.430  13.238  1.00 25.63 ? 462 HOH A O   1 
HETATM 2270 O  O   . HOH L 9 .   ? 36.414 -4.800  11.813  1.00 29.34 ? 463 HOH A O   1 
HETATM 2271 O  O   . HOH L 9 .   ? 10.459 -16.391 17.134  1.00 21.57 ? 464 HOH A O   1 
HETATM 2272 O  O   . HOH L 9 .   ? 17.564 -9.313  20.902  1.00 8.74  ? 465 HOH A O   1 
HETATM 2273 O  O   . HOH L 9 .   ? 6.352  21.747  17.525  1.00 26.12 ? 466 HOH A O   1 
HETATM 2274 O  O   . HOH L 9 .   ? 9.209  11.217  3.226   1.00 19.67 ? 467 HOH A O   1 
HETATM 2275 O  O   . HOH L 9 .   ? 14.096 -13.134 31.655  1.00 21.12 ? 468 HOH A O   1 
HETATM 2276 O  O   . HOH L 9 .   ? -6.731 8.248   21.213  1.00 39.54 ? 469 HOH A O   1 
HETATM 2277 O  O   . HOH L 9 .   ? 23.553 -11.456 5.297   1.00 14.80 ? 470 HOH A O   1 
HETATM 2278 O  O   . HOH L 9 .   ? 2.100  19.428  18.902  1.00 34.75 ? 471 HOH A O   1 
HETATM 2279 O  O   . HOH L 9 .   ? 2.242  -19.078 14.893  1.00 31.30 ? 472 HOH A O   1 
HETATM 2280 O  O   . HOH L 9 .   ? 16.472 -11.689 18.097  1.00 7.61  ? 473 HOH A O   1 
HETATM 2281 O  O   . HOH L 9 .   ? 26.580 8.837   20.297  1.00 15.62 ? 474 HOH A O   1 
HETATM 2282 O  O   . HOH L 9 .   ? 20.899 2.811   -11.012 1.00 32.47 ? 475 HOH A O   1 
HETATM 2283 O  O   . HOH L 9 .   ? -5.168 -5.639  30.518  1.00 34.80 ? 476 HOH A O   1 
HETATM 2284 O  O   . HOH L 9 .   ? 22.949 9.722   24.822  1.00 31.45 ? 477 HOH A O   1 
HETATM 2285 O  O   . HOH L 9 .   ? -0.097 9.787   1.969   1.00 15.11 ? 478 HOH A O   1 
HETATM 2286 O  O   . HOH L 9 .   ? 17.003 22.211  15.606  1.00 25.47 ? 479 HOH A O   1 
HETATM 2287 O  O   . HOH L 9 .   ? 18.523 -7.001  29.158  1.00 9.40  ? 480 HOH A O   1 
HETATM 2288 O  O   . HOH L 9 .   ? 23.210 -4.936  -8.483  1.00 34.85 ? 481 HOH A O   1 
HETATM 2289 O  O   . HOH L 9 .   ? 28.583 -5.816  -0.510  1.00 24.93 ? 482 HOH A O   1 
HETATM 2290 O  O   . HOH L 9 .   ? -4.685 9.884   6.297   1.00 46.61 ? 483 HOH A O   1 
HETATM 2291 O  O   . HOH L 9 .   ? 3.128  -18.738 8.124   1.00 11.68 ? 484 HOH A O   1 
HETATM 2292 O  O   . HOH L 9 .   ? 7.629  22.052  15.013  1.00 16.83 ? 485 HOH A O   1 
HETATM 2293 O  O   . HOH L 9 .   ? 29.713 -2.026  21.085  1.00 13.04 ? 486 HOH A O   1 
HETATM 2294 O  O   . HOH L 9 .   ? -4.675 -7.115  11.421  1.00 24.91 ? 487 HOH A O   1 
HETATM 2295 O  O   . HOH L 9 .   ? 9.069  12.660  5.902   1.00 25.62 ? 488 HOH A O   1 
HETATM 2296 O  O   . HOH L 9 .   ? 7.356  12.356  27.873  1.00 17.89 ? 489 HOH A O   1 
HETATM 2297 O  O   . HOH L 9 .   ? 22.400 -10.001 25.108  1.00 21.91 ? 490 HOH A O   1 
HETATM 2298 O  O   . HOH L 9 .   ? 24.573 -7.070  26.059  1.00 32.50 ? 491 HOH A O   1 
HETATM 2299 O  O   . HOH L 9 .   ? 23.852 -2.436  7.861   1.00 16.03 ? 492 HOH A O   1 
HETATM 2300 O  O   . HOH L 9 .   ? 4.050  -6.527  20.408  1.00 7.08  ? 493 HOH A O   1 
HETATM 2301 O  O   . HOH L 9 .   ? 8.247  -7.138  -3.102  1.00 21.34 ? 494 HOH A O   1 
HETATM 2302 O  O   . HOH L 9 .   ? 8.973  18.561  9.312   1.00 31.40 ? 495 HOH A O   1 
HETATM 2303 O  O   . HOH L 9 .   ? 16.799 -6.907  31.193  1.00 19.70 ? 496 HOH A O   1 
HETATM 2304 O  O   . HOH L 9 .   ? 7.087  -2.914  -6.435  1.00 42.70 ? 497 HOH A O   1 
HETATM 2305 O  O   . HOH L 9 .   ? 6.585  16.852  5.262   1.00 59.93 ? 498 HOH A O   1 
HETATM 2306 O  O   . HOH L 9 .   ? 2.429  -1.841  -2.507  1.00 26.46 ? 499 HOH A O   1 
HETATM 2307 O  O   . HOH L 9 .   ? -1.697 -3.929  2.917   1.00 22.26 ? 500 HOH A O   1 
HETATM 2308 O  O   . HOH L 9 .   ? 3.645  -14.515 21.861  1.00 31.29 ? 501 HOH A O   1 
HETATM 2309 O  O   . HOH L 9 .   ? 17.969 -17.345 22.129  1.00 41.64 ? 502 HOH A O   1 
HETATM 2310 O  O   . HOH L 9 .   ? 12.450 2.526   -6.540  1.00 31.01 ? 503 HOH A O   1 
HETATM 2311 O  O   . HOH L 9 .   ? 29.607 -10.842 8.861   1.00 39.90 ? 504 HOH A O   1 
HETATM 2312 O  O   . HOH L 9 .   ? 13.882 -14.978 1.529   1.00 19.51 ? 505 HOH A O   1 
HETATM 2313 O  O   . HOH L 9 .   ? 5.522  2.391   -4.793  1.00 42.16 ? 506 HOH A O   1 
HETATM 2314 O  O   . HOH L 9 .   ? -5.331 4.799   20.891  1.00 28.05 ? 507 HOH A O   1 
HETATM 2315 O  O   . HOH L 9 .   ? -5.317 5.625   15.450  1.00 25.62 ? 508 HOH A O   1 
HETATM 2316 O  O   . HOH L 9 .   ? -0.112 20.751  13.818  1.00 33.42 ? 509 HOH A O   1 
HETATM 2317 O  O   . HOH L 9 .   ? -0.884 7.653   4.799   1.00 13.67 ? 510 HOH A O   1 
HETATM 2318 O  O   . HOH L 9 .   ? -0.514 -5.157  23.517  1.00 9.18  ? 511 HOH A O   1 
HETATM 2319 O  O   . HOH L 9 .   ? 25.861 -1.277  2.942   1.00 35.01 ? 512 HOH A O   1 
HETATM 2320 O  O   . HOH L 9 .   ? 30.976 2.159   14.083  1.00 43.67 ? 513 HOH A O   1 
HETATM 2321 O  O   . HOH L 9 .   ? 12.776 -13.687 36.650  1.00 29.39 ? 514 HOH A O   1 
HETATM 2322 O  O   . HOH L 9 .   ? -2.975 -0.669  29.157  1.00 31.42 ? 515 HOH A O   1 
HETATM 2323 O  O   . HOH L 9 .   ? 1.575  19.360  6.139   1.00 24.68 ? 516 HOH A O   1 
HETATM 2324 O  O   . HOH L 9 .   ? 36.512 -0.536  14.493  1.00 24.03 ? 517 HOH A O   1 
HETATM 2325 O  O   . HOH L 9 .   ? 17.644 -11.450 25.227  1.00 10.54 ? 518 HOH A O   1 
HETATM 2326 O  O   . HOH L 9 .   ? -0.217 -5.155  -1.794  1.00 46.58 ? 519 HOH A O   1 
HETATM 2327 O  O   . HOH L 9 .   ? 17.275 -14.120 24.476  1.00 13.96 ? 520 HOH A O   1 
HETATM 2328 O  O   . HOH L 9 .   ? 21.083 10.749  14.337  1.00 44.79 ? 521 HOH A O   1 
HETATM 2329 O  O   . HOH L 9 .   ? 20.904 -18.657 14.644  1.00 39.65 ? 522 HOH A O   1 
HETATM 2330 O  O   . HOH L 9 .   ? 24.408 4.904   8.181   1.00 42.50 ? 523 HOH A O   1 
HETATM 2331 O  O   . HOH L 9 .   ? 13.652 -6.976  32.623  1.00 15.58 ? 524 HOH A O   1 
HETATM 2332 O  O   . HOH L 9 .   ? 4.898  17.744  23.518  1.00 22.60 ? 525 HOH A O   1 
HETATM 2333 O  O   . HOH L 9 .   ? 14.097 -6.352  -7.322  1.00 38.23 ? 526 HOH A O   1 
HETATM 2334 O  O   . HOH L 9 .   ? 19.339 6.470   -4.938  1.00 27.56 ? 527 HOH A O   1 
HETATM 2335 O  O   . HOH L 9 .   ? 25.592 -0.798  28.995  1.00 25.01 ? 528 HOH A O   1 
HETATM 2336 O  O   . HOH L 9 .   ? 0.831  12.649  26.629  1.00 17.19 ? 529 HOH A O   1 
HETATM 2337 O  O   . HOH L 9 .   ? -2.108 -1.126  6.809   1.00 19.30 ? 530 HOH A O   1 
HETATM 2338 O  O   . HOH L 9 .   ? 3.757  -5.525  39.654  1.00 37.97 ? 531 HOH A O   1 
HETATM 2339 O  O   . HOH L 9 .   ? 4.980  -10.500 24.387  1.00 17.12 ? 532 HOH A O   1 
HETATM 2340 O  O   . HOH L 9 .   ? -1.992 1.420   34.403  1.00 31.39 ? 533 HOH A O   1 
HETATM 2341 O  O   . HOH L 9 .   ? 7.964  -15.021 26.623  1.00 22.63 ? 534 HOH A O   1 
HETATM 2342 O  O   . HOH L 9 .   ? 16.443 -14.137 0.860   1.00 28.58 ? 535 HOH A O   1 
HETATM 2343 O  O   . HOH L 9 .   ? -2.950 -15.921 6.464   1.00 40.49 ? 536 HOH A O   1 
HETATM 2344 O  O   . HOH L 9 .   ? 24.044 3.014   -2.154  1.00 34.18 ? 537 HOH A O   1 
HETATM 2345 O  O   . HOH L 9 .   ? -3.846 -5.852  9.205   1.00 16.40 ? 538 HOH A O   1 
HETATM 2346 O  O   . HOH L 9 .   ? 15.541 17.797  12.161  1.00 19.47 ? 539 HOH A O   1 
HETATM 2347 O  O   . HOH L 9 .   ? 5.495  10.939  -2.018  1.00 27.63 ? 540 HOH A O   1 
HETATM 2348 O  O   . HOH L 9 .   ? 12.265 -13.499 33.161  1.00 52.41 ? 541 HOH A O   1 
HETATM 2349 O  O   . HOH L 9 .   ? -1.565 21.999  12.228  1.00 40.57 ? 542 HOH A O   1 
HETATM 2350 O  O   . HOH L 9 .   ? 14.423 -3.734  37.374  1.00 25.67 ? 543 HOH A O   1 
HETATM 2351 O  O   . HOH L 9 .   ? 7.325  16.074  27.341  1.00 34.93 ? 544 HOH A O   1 
HETATM 2352 O  O   . HOH L 9 .   ? 24.544 10.557  21.092  1.00 26.30 ? 545 HOH A O   1 
HETATM 2353 O  O   . HOH L 9 .   ? 24.505 -11.688 12.154  1.00 36.98 ? 546 HOH A O   1 
HETATM 2354 O  O   . HOH L 9 .   ? -2.899 1.213   26.545  1.00 13.25 ? 547 HOH A O   1 
HETATM 2355 O  O   . HOH L 9 .   ? 12.887 -17.414 30.606  1.00 33.45 ? 548 HOH A O   1 
HETATM 2356 O  O   . HOH L 9 .   ? 24.925 6.370   10.833  1.00 39.98 ? 549 HOH A O   1 
HETATM 2357 O  O   . HOH L 9 .   ? 30.580 3.911   12.147  1.00 42.09 ? 550 HOH A O   1 
HETATM 2358 O  O   . HOH L 9 .   ? 29.157 -7.536  16.454  1.00 24.71 ? 551 HOH A O   1 
HETATM 2359 O  O   . HOH L 9 .   ? 9.224  4.695   30.741  1.00 18.19 ? 552 HOH A O   1 
HETATM 2360 O  O   . HOH L 9 .   ? 26.780 -1.244  6.780   1.00 27.17 ? 553 HOH A O   1 
HETATM 2361 O  O   . HOH L 9 .   ? 9.883  19.697  12.415  1.00 13.68 ? 554 HOH A O   1 
HETATM 2362 O  O   . HOH L 9 .   ? 14.649 -18.029 24.153  1.00 38.62 ? 555 HOH A O   1 
HETATM 2363 O  O   . HOH L 9 .   ? -7.449 1.337   6.942   1.00 52.13 ? 556 HOH A O   1 
HETATM 2364 O  O   . HOH L 9 .   ? 23.667 -9.539  9.722   1.00 19.75 ? 557 HOH A O   1 
HETATM 2365 O  O   . HOH L 9 .   ? 25.996 -3.087  21.040  1.00 11.35 ? 558 HOH A O   1 
HETATM 2366 O  O   . HOH L 9 .   ? 8.236  5.500   -6.801  1.00 23.96 ? 559 HOH A O   1 
HETATM 2367 O  O   . HOH L 9 .   ? -2.315 -9.332  16.870  1.00 38.24 ? 560 HOH A O   1 
HETATM 2368 O  O   . HOH L 9 .   ? 1.748  11.918  9.009   1.00 12.42 ? 561 HOH A O   1 
HETATM 2369 O  O   . HOH L 9 .   ? -2.818 1.076   3.986   1.00 20.72 ? 562 HOH A O   1 
HETATM 2370 O  O   . HOH L 9 .   ? -1.170 -16.549 13.657  1.00 23.46 ? 563 HOH A O   1 
HETATM 2371 O  O   . HOH L 9 .   ? 22.311 -4.800  34.555  1.00 27.01 ? 564 HOH A O   1 
HETATM 2372 O  O   . HOH L 9 .   ? 26.892 3.040   8.405   1.00 37.78 ? 565 HOH A O   1 
HETATM 2373 O  O   . HOH L 9 .   ? 11.969 -4.191  35.870  1.00 17.31 ? 566 HOH A O   1 
HETATM 2374 O  O   . HOH L 9 .   ? 22.362 0.123   29.526  1.00 11.99 ? 567 HOH A O   1 
HETATM 2375 O  O   . HOH L 9 .   ? -1.190 5.774   -3.009  1.00 23.50 ? 568 HOH A O   1 
HETATM 2376 O  O   . HOH L 9 .   ? 31.455 -8.976  16.140  1.00 24.68 ? 569 HOH A O   1 
HETATM 2377 O  O   . HOH L 9 .   ? 7.464  0.983   -6.088  1.00 35.27 ? 570 HOH A O   1 
HETATM 2378 O  O   . HOH L 9 .   ? 4.769  -8.031  32.901  1.00 18.95 ? 571 HOH A O   1 
HETATM 2379 O  O   . HOH L 9 .   ? -1.928 -9.759  14.071  1.00 16.97 ? 572 HOH A O   1 
HETATM 2380 O  O   . HOH L 9 .   ? 2.253  14.139  13.067  1.00 19.40 ? 573 HOH A O   1 
HETATM 2381 O  O   . HOH L 9 .   ? 20.475 -6.815  32.602  1.00 23.54 ? 574 HOH A O   1 
HETATM 2382 O  O   . HOH L 9 .   ? 7.757  -16.605 14.880  1.00 19.58 ? 575 HOH A O   1 
HETATM 2383 O  O   . HOH L 9 .   ? -5.723 -2.054  25.205  1.00 18.75 ? 576 HOH A O   1 
HETATM 2384 O  O   . HOH L 9 .   ? 9.814  -17.467 6.981   1.00 30.58 ? 577 HOH A O   1 
HETATM 2385 O  O   . HOH L 9 .   ? 32.209 -1.968  7.517   1.00 41.22 ? 578 HOH A O   1 
HETATM 2386 O  O   . HOH L 9 .   ? 32.470 3.118   26.037  1.00 24.44 ? 579 HOH A O   1 
HETATM 2387 O  O   . HOH L 9 .   ? 18.978 -10.502 22.892  1.00 8.89  ? 580 HOH A O   1 
HETATM 2388 O  O   . HOH L 9 .   ? 29.500 5.026   27.972  1.00 36.99 ? 581 HOH A O   1 
HETATM 2389 O  O   . HOH L 9 .   ? 35.255 7.502   18.805  1.00 41.06 ? 582 HOH A O   1 
HETATM 2390 O  O   . HOH L 9 .   ? 11.129 17.180  12.260  1.00 14.00 ? 583 HOH A O   1 
HETATM 2391 O  O   . HOH L 9 .   ? 31.336 -7.187  8.636   1.00 34.15 ? 584 HOH A O   1 
HETATM 2392 O  O   . HOH L 9 .   ? -6.220 -9.267  22.328  1.00 53.19 ? 585 HOH A O   1 
HETATM 2393 O  O   . HOH L 9 .   ? 26.043 -5.645  22.296  1.00 33.53 ? 586 HOH A O   1 
HETATM 2394 O  O   . HOH L 9 .   ? 3.911  -9.925  36.271  1.00 36.66 ? 587 HOH A O   1 
HETATM 2395 O  O   . HOH L 9 .   ? -0.038 -17.753 6.606   1.00 28.65 ? 588 HOH A O   1 
HETATM 2396 O  O   . HOH L 9 .   ? 34.400 -4.007  24.540  1.00 35.18 ? 589 HOH A O   1 
HETATM 2397 O  O   . HOH L 9 .   ? 13.808 3.080   35.044  1.00 25.64 ? 590 HOH A O   1 
HETATM 2398 O  O   . HOH L 9 .   ? -3.130 1.619   1.234   1.00 38.11 ? 591 HOH A O   1 
HETATM 2399 O  O   . HOH L 9 .   ? 2.613  -7.153  34.766  1.00 36.52 ? 592 HOH A O   1 
HETATM 2400 O  O   . HOH L 9 .   ? 15.580 5.508   -5.696  1.00 31.56 ? 593 HOH A O   1 
HETATM 2401 O  O   . HOH L 9 .   ? 12.715 -17.635 21.735  1.00 19.76 ? 594 HOH A O   1 
HETATM 2402 O  O   . HOH L 9 .   ? 19.934 -15.929 17.953  1.00 40.94 ? 595 HOH A O   1 
HETATM 2403 O  O   . HOH L 9 .   ? 20.850 -12.511 22.140  1.00 23.30 ? 596 HOH A O   1 
HETATM 2404 O  O   . HOH L 9 .   ? 22.552 4.067   35.987  1.00 44.45 ? 597 HOH A O   1 
HETATM 2405 O  O   . HOH L 9 .   ? 28.736 8.077   21.932  1.00 14.95 ? 598 HOH A O   1 
HETATM 2406 O  O   . HOH L 9 .   ? 2.725  5.813   -3.695  1.00 41.17 ? 599 HOH A O   1 
HETATM 2407 O  O   . HOH L 9 .   ? 7.222  -14.622 -0.316  1.00 42.74 ? 600 HOH A O   1 
HETATM 2408 O  O   . HOH L 9 .   ? 13.928 2.989   37.268  1.00 38.39 ? 601 HOH A O   1 
HETATM 2409 O  O   . HOH L 9 .   ? 3.688  -21.272 4.238   1.00 35.94 ? 602 HOH A O   1 
HETATM 2410 O  O   . HOH L 9 .   ? 10.843 7.884   -4.069  1.00 44.55 ? 603 HOH A O   1 
HETATM 2411 O  O   . HOH L 9 .   ? 25.061 -0.132  4.953   1.00 51.24 ? 604 HOH A O   1 
HETATM 2412 O  O   . HOH L 9 .   ? 8.388  -16.811 32.100  1.00 38.03 ? 605 HOH A O   1 
HETATM 2413 O  O   . HOH L 9 .   ? 11.580 -6.238  34.069  1.00 21.74 ? 606 HOH A O   1 
HETATM 2414 O  O   . HOH L 9 .   ? 15.868 -11.103 -5.324  1.00 36.64 ? 607 HOH A O   1 
HETATM 2415 O  O   . HOH L 9 .   ? 8.320  9.851   29.056  1.00 29.89 ? 608 HOH A O   1 
HETATM 2416 O  O   . HOH L 9 .   ? -3.160 1.658   31.495  1.00 38.34 ? 609 HOH A O   1 
HETATM 2417 O  O   . HOH L 9 .   ? 12.992 -18.276 26.496  1.00 48.25 ? 610 HOH A O   1 
HETATM 2418 O  O   . HOH L 9 .   ? -3.781 6.685   8.036   1.00 47.46 ? 611 HOH A O   1 
HETATM 2419 O  O   . HOH L 9 .   ? 31.356 -0.605  13.552  1.00 28.78 ? 612 HOH A O   1 
HETATM 2420 O  O   . HOH L 9 .   ? -3.698 -7.669  1.978   1.00 27.10 ? 613 HOH A O   1 
HETATM 2421 O  O   . HOH L 9 .   ? 31.510 8.719   15.310  1.00 38.16 ? 614 HOH A O   1 
HETATM 2422 O  O   . HOH L 9 .   ? 21.422 2.640   -6.614  1.00 24.51 ? 615 HOH A O   1 
HETATM 2423 O  O   . HOH L 9 .   ? -4.705 -4.673  33.677  1.00 35.69 ? 616 HOH A O   1 
HETATM 2424 O  O   . HOH L 9 .   ? -4.340 13.116  19.904  1.00 49.08 ? 617 HOH A O   1 
HETATM 2425 O  O   . HOH L 9 .   ? 29.000 -6.966  -7.488  1.00 42.24 ? 618 HOH A O   1 
HETATM 2426 O  O   . HOH L 9 .   ? 8.177  -15.422 16.980  1.00 21.19 ? 619 HOH A O   1 
HETATM 2427 O  O   . HOH L 9 .   ? 34.197 -1.648  13.400  1.00 32.93 ? 620 HOH A O   1 
HETATM 2428 O  O   . HOH L 9 .   ? 19.469 -11.429 27.272  1.00 29.83 ? 621 HOH A O   1 
HETATM 2429 O  O   . HOH L 9 .   ? 35.752 1.938   15.028  1.00 61.64 ? 622 HOH A O   1 
HETATM 2430 O  O   . HOH L 9 .   ? 29.733 -2.760  23.757  1.00 25.58 ? 623 HOH A O   1 
HETATM 2431 O  O   . HOH L 9 .   ? -5.564 7.089   6.694   1.00 52.90 ? 624 HOH A O   1 
HETATM 2432 O  O   . HOH L 9 .   ? 20.281 12.519  25.167  1.00 35.66 ? 625 HOH A O   1 
HETATM 2433 O  O   . HOH L 9 .   ? 27.468 -9.027  14.974  1.00 38.17 ? 626 HOH A O   1 
HETATM 2434 O  O   . HOH L 9 .   ? 21.834 -8.398  28.856  1.00 40.41 ? 627 HOH A O   1 
HETATM 2435 O  O   . HOH L 9 .   ? -4.185 6.600   4.539   1.00 54.94 ? 628 HOH A O   1 
HETATM 2436 O  O   . HOH L 9 .   ? -2.603 -1.529  3.915   1.00 32.86 ? 629 HOH A O   1 
HETATM 2437 O  O   . HOH L 9 .   ? 32.665 -4.732  7.698   1.00 51.26 ? 630 HOH A O   1 
HETATM 2438 O  O   . HOH L 9 .   ? -6.933 -1.269  10.796  1.00 35.32 ? 631 HOH A O   1 
HETATM 2439 O  O   . HOH L 9 .   ? 33.130 2.538   28.553  1.00 37.28 ? 632 HOH A O   1 
HETATM 2440 O  O   . HOH L 9 .   ? 23.996 -11.633 8.126   1.00 23.25 ? 633 HOH A O   1 
HETATM 2441 O  O   . HOH L 9 .   ? 18.881 -10.267 31.471  1.00 30.94 ? 634 HOH A O   1 
HETATM 2442 O  O   . HOH L 9 .   ? 10.753 6.770   30.674  1.00 31.68 ? 635 HOH A O   1 
HETATM 2443 O  O   . HOH L 9 .   ? 16.112 -8.083  33.206  1.00 33.50 ? 636 HOH A O   1 
HETATM 2444 O  O   . HOH L 9 .   ? 15.890 -0.407  40.200  1.00 44.97 ? 637 HOH A O   1 
HETATM 2445 O  O   . HOH L 9 .   ? 15.150 -7.812  35.261  1.00 50.50 ? 638 HOH A O   1 
HETATM 2446 O  O   . HOH L 9 .   ? 24.208 -3.905  -11.519 1.00 33.64 ? 639 HOH A O   1 
HETATM 2447 O  O   . HOH L 9 .   ? -8.434 1.240   9.957   1.00 42.49 ? 640 HOH A O   1 
HETATM 2448 O  O   . HOH L 9 .   ? 29.382 -0.707  4.883   1.00 42.81 ? 641 HOH A O   1 
HETATM 2449 O  O   . HOH L 9 .   ? 19.035 -15.825 25.466  1.00 33.53 ? 642 HOH A O   1 
HETATM 2450 O  O   . HOH L 9 .   ? 4.250  -12.543 37.346  1.00 29.88 ? 643 HOH A O   1 
HETATM 2451 O  O   . HOH L 9 .   ? 4.245  -16.224 20.337  1.00 43.26 ? 644 HOH A O   1 
HETATM 2452 O  O   . HOH L 9 .   ? 5.101  18.670  26.811  1.00 47.89 ? 645 HOH A O   1 
HETATM 2453 O  O   . HOH L 9 .   ? -1.016 -11.301 23.633  1.00 54.08 ? 646 HOH A O   1 
HETATM 2454 O  O   . HOH L 9 .   ? 24.156 -15.963 10.449  1.00 42.80 ? 647 HOH A O   1 
HETATM 2455 O  O   . HOH L 9 .   ? 8.320  11.892  -1.500  1.00 41.27 ? 648 HOH A O   1 
HETATM 2456 O  O   . HOH L 9 .   ? -2.791 -5.228  0.106   1.00 42.04 ? 649 HOH A O   1 
HETATM 2457 O  O   . HOH L 9 .   ? 4.151  -12.101 26.325  1.00 31.79 ? 650 HOH A O   1 
HETATM 2458 O  O   . HOH L 9 .   ? 19.824 -9.495  29.106  1.00 18.39 ? 651 HOH A O   1 
HETATM 2459 O  O   . HOH L 9 .   ? 22.743 -8.168  31.224  1.00 39.24 ? 652 HOH A O   1 
HETATM 2460 O  O   . HOH L 9 .   ? 3.152  -10.425 31.734  1.00 37.41 ? 653 HOH A O   1 
HETATM 2461 O  O   . HOH L 9 .   ? 26.162 -8.866  17.981  1.00 37.21 ? 654 HOH A O   1 
HETATM 2462 O  O   . HOH L 9 .   ? 23.058 -12.424 20.719  1.00 40.67 ? 655 HOH A O   1 
HETATM 2463 O  O   . HOH L 9 .   ? 12.684 -15.756 34.771  1.00 35.24 ? 656 HOH A O   1 
HETATM 2464 O  O   . HOH L 9 .   ? 8.719  15.372  4.900   1.00 36.54 ? 657 HOH A O   1 
HETATM 2465 O  O   . HOH L 9 .   ? 1.122  -13.720 22.592  1.00 62.45 ? 658 HOH A O   1 
HETATM 2466 O  O   . HOH L 9 .   ? 27.355 7.101   29.678  1.00 41.18 ? 659 HOH A O   1 
HETATM 2467 O  O   . HOH L 9 .   ? 21.138 -5.326  -7.372  1.00 42.21 ? 660 HOH A O   1 
HETATM 2468 O  O   . HOH L 9 .   ? 9.259  12.658  0.775   1.00 25.81 ? 661 HOH A O   1 
HETATM 2469 O  O   . HOH L 9 .   ? 25.114 -9.996  23.665  1.00 39.14 ? 662 HOH A O   1 
HETATM 2470 O  O   . HOH L 9 .   ? 13.265 18.222  10.521  1.00 22.10 ? 663 HOH A O   1 
HETATM 2471 O  O   . HOH L 9 .   ? -5.612 0.587   26.018  1.00 20.35 ? 664 HOH A O   1 
HETATM 2472 O  O   . HOH L 9 .   ? 17.114 -13.723 -2.045  1.00 34.54 ? 665 HOH A O   1 
HETATM 2473 O  O   . HOH L 9 .   ? 24.974 10.915  23.441  1.00 38.04 ? 666 HOH A O   1 
HETATM 2474 O  O   . HOH L 9 .   ? 27.680 10.323  18.215  1.00 33.48 ? 667 HOH A O   1 
HETATM 2475 O  O   . HOH L 9 .   ? 19.703 5.013   -7.164  1.00 26.56 ? 668 HOH A O   1 
HETATM 2476 O  O   . HOH L 9 .   ? 18.043 -7.539  34.200  1.00 43.91 ? 669 HOH A O   1 
HETATM 2477 O  O   . HOH L 9 .   ? 3.518  -19.609 17.633  1.00 30.20 ? 670 HOH A O   1 
HETATM 2478 O  O   . HOH L 9 .   ? 7.946  -17.842 26.103  1.00 32.25 ? 671 HOH A O   1 
HETATM 2479 O  O   . HOH L 9 .   ? 16.018 -6.096  37.690  1.00 66.60 ? 672 HOH A O   1 
HETATM 2480 O  O   . HOH L 9 .   ? -6.866 0.444   28.389  1.00 33.33 ? 673 HOH A O   1 
HETATM 2481 O  O   . HOH L 9 .   ? 25.202 -11.271 21.700  1.00 40.77 ? 674 HOH A O   1 
HETATM 2482 O  O   . HOH L 9 .   ? 33.580 -3.007  4.626   1.00 44.25 ? 675 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS A 4   ? 0.3342 0.6315 0.5173 -0.0280 0.0973  0.2325  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.4656 0.4444 0.4855 -0.1395 0.0381  0.1965  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.1929 0.3406 0.3694 0.0653  0.1439  0.0846  4   HIS A C   
4    O  O   . HIS A 4   ? 0.1951 0.3420 0.3489 0.0127  0.1168  0.0564  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.3726 0.5359 0.6330 -0.0296 0.2985  0.0731  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.5604 0.6574 0.9965 -0.0488 0.0423  0.3887  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 1.0853 0.9219 0.9446 -0.0870 -0.0594 0.2178  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.8467 1.0689 0.7136 -0.2468 0.0880  0.2192  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 1.3606 0.6786 1.0747 -0.1153 -0.1784 0.2602  4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 0.5489 1.1936 1.1995 -0.2664 -0.5024 0.1949  4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.1494 0.2537 0.3082 -0.0520 0.1140  0.0124  5   TRP A N   
12   C  CA  . TRP A 5   ? 0.0982 0.1923 0.2246 -0.0210 0.0772  -0.0100 5   TRP A CA  
13   C  C   . TRP A 5   ? 0.0539 0.1879 0.2467 -0.0012 0.0820  0.0011  5   TRP A C   
14   O  O   . TRP A 5   ? 0.1092 0.2101 0.2475 0.0055  0.0877  0.0196  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.0641 0.1646 0.2505 0.0105  0.0664  -0.0111 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.0770 0.1344 0.2041 -0.0047 0.0525  0.0015  5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.1092 0.1619 0.2239 0.0086  0.0679  0.0486  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.0607 0.1746 0.1486 0.0130  0.0431  -0.0220 5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.1143 0.2059 0.2105 0.0395  0.0805  0.0526  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1160 0.2036 0.1275 0.0254  0.0498  0.0290  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.0476 0.2116 0.1357 -0.0468 0.0435  -0.0523 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.1172 0.2302 0.1351 0.0135  0.0179  0.0178  5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.0417 0.2314 0.1515 0.0020  0.0321  -0.0190 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.0721 0.2285 0.1432 -0.0095 0.0359  -0.0272 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.0294 0.1565 0.2319 -0.0006 0.0709  -0.0359 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.0646 0.1639 0.1936 -0.0270 0.0637  -0.0161 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.0425 0.1534 0.1655 0.0058  0.0493  -0.0225 6   GLY A C   
28   O  O   . GLY A 6   ? 0.0151 0.1894 0.1727 -0.0029 0.0348  -0.0449 6   GLY A O   
29   N  N   . TYR A 7   ? 0.0601 0.1605 0.1692 -0.0093 0.0753  -0.0309 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.0352 0.1459 0.2362 0.0065  0.0796  -0.0197 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.0655 0.1592 0.3323 0.0427  0.0873  0.0011  7   TYR A C   
32   O  O   . TYR A 7   ? 0.1512 0.1703 0.5636 0.0238  0.1582  0.0490  7   TYR A O   
33   C  CB  . TYR A 7   ? 0.0366 0.1989 0.1822 -0.0031 0.0684  -0.0603 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.0256 0.1486 0.1495 -0.0068 0.0317  -0.0277 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.0200 0.1655 0.1584 -0.0232 0.0431  -0.0303 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.0730 0.1305 0.1405 -0.0152 0.0265  -0.0278 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.0431 0.1025 0.1826 -0.0215 0.0157  -0.0167 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.0776 0.1405 0.1210 -0.0279 0.0494  -0.0212 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.0575 0.1186 0.1237 -0.0326 0.0471  -0.0299 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.1016 0.1328 0.1531 0.0089  0.0182  -0.0370 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.0549 0.1881 0.3237 0.0131  0.0776  -0.0737 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.1430 0.2026 0.3772 0.0528  0.1133  -0.0762 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.1377 0.1583 0.4026 0.0206  0.0991  0.0245  8   GLY A C   
44   O  O   . GLY A 8   ? 0.1663 0.3103 0.4171 0.0203  0.1734  -0.0357 8   GLY A O   
45   N  N   . LYS A 9   ? 0.1515 0.1632 0.5965 0.0136  0.1542  -0.0190 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.1901 0.2562 0.6240 0.0219  0.0779  -0.0398 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.1743 0.2687 0.4846 0.0099  0.0939  0.0789  9   LYS A C   
48   O  O   . LYS A 9   ? 0.1899 0.2737 0.4284 0.0438  0.1264  0.0551  9   LYS A O   
49   C  CB  . LYS A 9   ? 0.2712 0.2122 0.8855 0.0669  0.1644  0.0125  9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.5955 0.3808 0.7476 0.1324  0.0681  -0.0370 9   LYS A CG  
51   N  N   . HIS A 10  ? 0.1441 0.1684 0.4271 0.0542  0.1782  -0.0030 10  HIS A N   
52   C  CA  . HIS A 10  ? 0.1113 0.2827 0.3783 0.0104  0.1204  0.0243  10  HIS A CA  
53   C  C   . HIS A 10  ? 0.0898 0.2827 0.3545 0.0707  0.0274  0.0453  10  HIS A C   
54   O  O   . HIS A 10  ? 0.0917 0.2727 0.4221 0.0348  0.1344  -0.0373 10  HIS A O   
55   C  CB  . HIS A 10  ? 0.1355 0.2713 0.4383 -0.0046 0.2035  0.0250  10  HIS A CB  
56   C  CG  . HIS A 10  ? 0.2605 0.3043 0.6332 0.0376  0.3677  0.0687  10  HIS A CG  
57   N  ND1 . HIS A 10  ? 0.5748 0.4471 0.6075 0.0575  0.0930  0.0410  10  HIS A ND1 
58   C  CD2 . HIS A 10  ? 0.5129 0.3463 0.8528 0.1319  0.2965  -0.0537 10  HIS A CD2 
59   C  CE1 . HIS A 10  ? 0.4379 0.5195 0.7875 0.3251  0.3277  -0.0333 10  HIS A CE1 
60   N  NE2 . HIS A 10  ? 0.3077 0.3831 0.8332 0.1528  0.3922  -0.1085 10  HIS A NE2 
61   N  N   . ASN A 11  ? 0.0725 0.2089 0.2882 0.0265  0.0878  0.0370  11  ASN A N   
62   C  CA  . ASN A 11  ? 0.1099 0.2001 0.2777 -0.0095 0.1235  0.0120  11  ASN A CA  
63   C  C   . ASN A 11  ? 0.0770 0.1790 0.2278 0.0071  0.0690  -0.0308 11  ASN A C   
64   O  O   . ASN A 11  ? 0.0488 0.1901 0.2053 -0.0002 0.0697  0.0099  11  ASN A O   
65   C  CB  . ASN A 11  ? 0.0506 0.2399 0.2616 -0.0059 0.1036  -0.0051 11  ASN A CB  
66   C  CG  . ASN A 11  ? 0.1108 0.2170 0.2055 0.0024  0.1078  -0.0147 11  ASN A CG  
67   O  OD1 . ASN A 11  ? 0.0964 0.2672 0.2461 -0.0413 0.0933  0.0037  11  ASN A OD1 
68   N  ND2 . ASN A 11  ? 0.1401 0.2917 0.2209 0.0113  0.1005  0.0301  11  ASN A ND2 
69   N  N   . GLY A 12  ? 0.0540 0.2312 0.2009 -0.0013 0.0946  -0.0157 12  GLY A N   
70   C  CA  . GLY A 12  ? 0.0454 0.2661 0.1736 0.0217  0.0793  0.0209  12  GLY A CA  
71   C  C   . GLY A 12  ? 0.0153 0.1653 0.1941 0.0017  0.0410  0.0095  12  GLY A C   
72   O  O   . GLY A 12  ? 0.0116 0.1705 0.1872 0.0094  0.0276  0.0113  12  GLY A O   
73   N  N   . PRO A 13  ? 0.0161 0.1317 0.1665 -0.0045 0.0394  -0.0085 13  PRO A N   
74   C  CA  . PRO A 13  ? 0.0267 0.1463 0.1603 0.0105  0.0469  0.0046  13  PRO A CA  
75   C  C   . PRO A 13  ? 0.0325 0.1497 0.1729 -0.0018 0.0361  -0.0071 13  PRO A C   
76   O  O   . PRO A 13  ? 0.0270 0.1614 0.1863 0.0029  0.0387  -0.0174 13  PRO A O   
77   C  CB  . PRO A 13  ? 0.0490 0.1851 0.1930 -0.0336 0.0535  -0.0274 13  PRO A CB  
78   C  CG  . PRO A 13  ? 0.0502 0.1779 0.1685 -0.0076 0.0727  -0.0314 13  PRO A CG  
79   C  CD  . PRO A 13  ? 0.0212 0.1668 0.1348 -0.0151 0.0416  -0.0262 13  PRO A CD  
80   N  N   . GLU A 14  ? 0.0407 0.1438 0.2350 0.0009  0.0256  0.0355  14  GLU A N   
81   C  CA  . GLU A 14  ? 0.0815 0.1738 0.2575 0.0193  -0.0036 0.0467  14  GLU A CA  
82   C  C   . GLU A 14  ? 0.0311 0.1472 0.1806 0.0495  0.0089  0.0129  14  GLU A C   
83   O  O   . GLU A 14  ? 0.0610 0.2097 0.2224 0.0416  -0.0190 0.0111  14  GLU A O   
84   C  CB  . GLU A 14  ? 0.1371 0.1761 0.4075 0.0370  -0.0912 0.0743  14  GLU A CB  
85   C  CG  . GLU A 14  ? 0.2605 0.2770 0.4119 -0.0266 0.0010  0.0539  14  GLU A CG  
86   C  CD  . GLU A 14  ? 0.5406 0.5137 0.4472 0.1316  0.1486  0.0708  14  GLU A CD  
87   O  OE1 . GLU A 14  ? 0.8862 0.4436 0.7559 -0.0140 0.1306  0.2904  14  GLU A OE1 
88   O  OE2 . GLU A 14  ? 0.9326 0.4713 0.5057 0.1515  0.3162  -0.0153 14  GLU A OE2 
89   N  N   . HIS A 15  ? 0.0341 0.1254 0.2025 0.0183  0.0196  0.0217  15  HIS A N   
90   C  CA  . HIS A 15  ? 0.0379 0.1346 0.2152 0.0073  0.0356  -0.0024 15  HIS A CA  
91   C  C   . HIS A 15  ? 0.0097 0.1417 0.1959 0.0160  0.0141  -0.0209 15  HIS A C   
92   O  O   . HIS A 15  ? 0.0126 0.1449 0.2485 0.0165  0.0309  -0.0095 15  HIS A O   
93   C  CB  . HIS A 15  ? 0.0384 0.1779 0.2206 0.0373  0.0609  0.0155  15  HIS A CB  
94   C  CG  . HIS A 15  ? 0.0673 0.1840 0.1757 0.0469  0.0405  -0.0026 15  HIS A CG  
95   N  ND1 . HIS A 15  ? 0.0635 0.2824 0.2735 0.0670  0.0155  -0.0478 15  HIS A ND1 
96   C  CD2 . HIS A 15  ? 0.1022 0.1700 0.3175 0.0674  0.0367  -0.0307 15  HIS A CD2 
97   C  CE1 . HIS A 15  ? 0.1901 0.2927 0.3136 0.0986  -0.0177 -0.1026 15  HIS A CE1 
98   N  NE2 . HIS A 15  ? 0.1466 0.2477 0.3973 0.1175  0.0680  -0.0915 15  HIS A NE2 
99   N  N   . TRP A 16  ? 0.0093 0.1460 0.1813 0.0167  0.0145  0.0114  16  TRP A N   
100  C  CA  . TRP A 16  ? 0.0079 0.1471 0.1929 0.0096  0.0136  0.0046  16  TRP A CA  
101  C  C   . TRP A 16  ? 0.0168 0.1329 0.1837 0.0076  0.0415  -0.0087 16  TRP A C   
102  O  O   . TRP A 16  ? 0.0064 0.1426 0.1937 0.0034  0.0003  -0.0026 16  TRP A O   
103  C  CB  . TRP A 16  ? 0.0068 0.1556 0.1645 -0.0043 0.0077  -0.0161 16  TRP A CB  
104  C  CG  . TRP A 16  ? 0.0094 0.1113 0.1423 0.0029  0.0181  -0.0039 16  TRP A CG  
105  C  CD1 . TRP A 16  ? 0.0332 0.1391 0.1274 -0.0086 0.0279  -0.0010 16  TRP A CD1 
106  C  CD2 . TRP A 16  ? 0.0139 0.1217 0.1684 0.0090  0.0345  0.0210  16  TRP A CD2 
107  N  NE1 . TRP A 16  ? 0.0177 0.1303 0.1407 0.0093  0.0368  -0.0117 16  TRP A NE1 
108  C  CE2 . TRP A 16  ? 0.0133 0.1172 0.1723 0.0027  0.0339  0.0194  16  TRP A CE2 
109  C  CE3 . TRP A 16  ? 0.0128 0.1047 0.2331 -0.0011 0.0381  0.0098  16  TRP A CE3 
110  C  CZ2 . TRP A 16  ? 0.0141 0.1186 0.1547 0.0004  0.0339  0.0069  16  TRP A CZ2 
111  C  CZ3 . TRP A 16  ? 0.0064 0.1152 0.1488 -0.0006 0.0034  -0.0252 16  TRP A CZ3 
112  C  CH2 . TRP A 16  ? 0.0258 0.1289 0.1282 0.0086  0.0351  -0.0069 16  TRP A CH2 
113  N  N   . HIS A 17  ? 0.0125 0.1729 0.1595 0.0009  0.0304  -0.0167 17  HIS A N   
114  C  CA  . HIS A 17  ? 0.0179 0.1779 0.1527 -0.0120 0.0128  0.0086  17  HIS A CA  
115  C  C   . HIS A 17  ? 0.0100 0.1930 0.2247 -0.0261 0.0003  -0.0146 17  HIS A C   
116  O  O   . HIS A 17  ? 0.0067 0.1571 0.2260 0.0074  0.0053  0.0130  17  HIS A O   
117  C  CB  . HIS A 17  ? 0.0120 0.1857 0.1574 0.0266  0.0143  0.0124  17  HIS A CB  
118  C  CG  . HIS A 17  ? 0.0232 0.1998 0.2065 0.0398  -0.0125 -0.0102 17  HIS A CG  
119  N  ND1 . HIS A 17  ? 0.0194 0.2366 0.2575 0.0116  -0.0033 0.0095  17  HIS A ND1 
120  C  CD2 . HIS A 17  ? 0.0346 0.1642 0.2285 0.0597  0.0100  0.0348  17  HIS A CD2 
121  C  CE1 . HIS A 17  ? 0.0186 0.2490 0.2321 0.0345  0.0221  0.0498  17  HIS A CE1 
122  N  NE2 . HIS A 17  ? 0.0295 0.2301 0.2372 0.0516  -0.0009 0.0564  17  HIS A NE2 
123  N  N   . LYS A 18  ? 0.0084 0.1939 0.2705 -0.0015 0.0232  0.0140  18  LYS A N   
124  C  CA  . LYS A 18  ? 0.0155 0.2188 0.2393 -0.0165 0.0411  0.0198  18  LYS A CA  
125  C  C   . LYS A 18  ? 0.0132 0.2012 0.2386 -0.0358 0.0017  -0.0044 18  LYS A C   
126  O  O   . LYS A 18  ? 0.0558 0.2077 0.4386 -0.0670 -0.0368 0.0507  18  LYS A O   
127  C  CB  . LYS A 18  ? 0.0105 0.2245 0.2883 0.0217  0.0266  0.0279  18  LYS A CB  
128  C  CG  . LYS A 18  ? 0.0091 0.2328 0.2615 0.0225  0.0127  0.0113  18  LYS A CG  
129  C  CD  . LYS A 18  ? 0.0187 0.2595 0.2294 0.0253  0.0082  -0.0079 18  LYS A CD  
130  C  CE  . LYS A 18  ? 0.0299 0.1954 0.1788 0.0436  0.0120  -0.0016 18  LYS A CE  
131  N  NZ  . LYS A 18  ? 0.0390 0.2388 0.2303 0.0756  0.0548  0.0403  18  LYS A NZ  
132  N  N   . ASP A 19  ? 0.0080 0.2080 0.2489 -0.0089 0.0037  0.0425  19  ASP A N   
133  C  CA  . ASP A 19  ? 0.0434 0.1585 0.2561 -0.0115 0.0299  0.0046  19  ASP A CA  
134  C  C   . ASP A 19  ? 0.0145 0.1784 0.2755 -0.0072 0.0284  0.0435  19  ASP A C   
135  O  O   . ASP A 19  ? 0.0410 0.1800 0.3331 -0.0238 0.0617  0.0533  19  ASP A O   
136  C  CB  . ASP A 19  ? 0.0348 0.3140 0.2605 0.0365  0.0016  -0.0055 19  ASP A CB  
137  C  CG  . ASP A 19  ? 0.1226 0.5811 0.3358 0.0124  0.0875  -0.0757 19  ASP A CG  
138  O  OD1 . ASP A 19  ? 0.2288 0.5837 0.3917 -0.0782 0.1197  -0.0318 19  ASP A OD1 
139  O  OD2 . ASP A 19  ? 0.3814 0.8507 0.5719 -0.0709 0.2020  -0.2999 19  ASP A OD2 
140  N  N   . PHE A 20  ? 0.0251 0.1531 0.2240 -0.0129 0.0287  0.0182  20  PHE A N   
141  C  CA  . PHE A 20  ? 0.0065 0.2350 0.2699 0.0006  -0.0074 0.0061  20  PHE A CA  
142  C  C   . PHE A 20  ? 0.0070 0.1715 0.2682 -0.0059 0.0116  -0.0205 20  PHE A C   
143  O  O   . PHE A 20  ? 0.0069 0.1636 0.2142 -0.0016 0.0111  -0.0038 20  PHE A O   
144  C  CB  . PHE A 20  ? 0.0123 0.2193 0.2482 -0.0356 -0.0038 0.0453  20  PHE A CB  
145  C  CG  . PHE A 20  ? 0.0239 0.2673 0.2573 -0.0564 0.0247  0.0521  20  PHE A CG  
146  C  CD1 . PHE A 20  ? 0.0495 0.2623 0.2752 -0.0531 0.0164  0.0769  20  PHE A CD1 
147  C  CD2 . PHE A 20  ? 0.0366 0.2802 0.2723 -0.0847 0.0118  0.0663  20  PHE A CD2 
148  C  CE1 . PHE A 20  ? 0.0621 0.2766 0.2534 -0.0368 0.0261  0.0351  20  PHE A CE1 
149  C  CE2 . PHE A 20  ? 0.0187 0.2964 0.2665 -0.0356 0.0400  0.0414  20  PHE A CE2 
150  C  CZ  . PHE A 20  ? 0.0323 0.2769 0.2579 -0.0625 0.0267  0.0612  20  PHE A CZ  
151  N  N   . PRO A 21  ? 0.0238 0.1898 0.2388 -0.0463 0.0426  -0.0248 21  PRO A N   
152  C  CA  . PRO A 21  ? 0.0267 0.2233 0.2178 -0.0664 0.0081  -0.0335 21  PRO A CA  
153  C  C   . PRO A 21  ? 0.0091 0.1802 0.1897 -0.0050 0.0036  -0.0171 21  PRO A C   
154  O  O   . PRO A 21  ? 0.0220 0.1932 0.2244 -0.0370 -0.0331 0.0150  21  PRO A O   
155  C  CB  . PRO A 21  ? 0.0436 0.2993 0.3182 -0.0923 -0.0500 -0.0012 21  PRO A CB  
156  C  CG  . PRO A 21  ? 0.2281 0.3004 0.3448 -0.1399 -0.0847 0.0052  21  PRO A CG  
157  C  CD  . PRO A 21  ? 0.0376 0.2226 0.3028 -0.0752 0.0389  -0.0004 21  PRO A CD  
158  N  N   . ILE A 22  ? 0.0101 0.1405 0.2330 -0.0218 -0.0036 -0.0282 22  ILE A N   
159  C  CA  . ILE A 22  ? 0.0095 0.1452 0.2216 -0.0207 -0.0002 -0.0310 22  ILE A CA  
160  C  C   . ILE A 22  ? 0.0095 0.1444 0.1837 -0.0166 -0.0092 -0.0388 22  ILE A C   
161  O  O   . ILE A 22  ? 0.0074 0.1563 0.2065 -0.0110 0.0088  -0.0134 22  ILE A O   
162  C  CB  . ILE A 22  ? 0.0132 0.1481 0.1991 -0.0115 -0.0083 -0.0367 22  ILE A CB  
163  C  CG1 . ILE A 22  ? 0.0809 0.2147 0.2129 -0.0386 0.0402  -0.0780 22  ILE A CG1 
164  C  CG2 . ILE A 22  ? 0.0538 0.1785 0.1797 -0.0283 -0.0264 -0.0067 22  ILE A CG2 
165  C  CD1 . ILE A 22  ? 0.1034 0.2715 0.2291 -0.0344 -0.0075 -0.0680 22  ILE A CD1 
166  N  N   . ALA A 23  ? 0.0087 0.1333 0.1670 -0.0116 -0.0125 -0.0212 23  ALA A N   
167  C  CA  . ALA A 23  ? 0.0098 0.1333 0.1571 -0.0063 0.0141  -0.0132 23  ALA A CA  
168  C  C   . ALA A 23  ? 0.0226 0.1451 0.1641 0.0006  0.0016  0.0041  23  ALA A C   
169  O  O   . ALA A 23  ? 0.0411 0.1445 0.2004 -0.0015 0.0286  -0.0074 23  ALA A O   
170  C  CB  . ALA A 23  ? 0.0105 0.1476 0.2095 0.0100  0.0246  -0.0224 23  ALA A CB  
171  N  N   . LYS A 24  ? 0.0257 0.1847 0.1696 0.0267  -0.0044 -0.0303 24  LYS A N   
172  C  CA  . LYS A 24  ? 0.0337 0.2180 0.1720 0.0226  -0.0107 -0.0116 24  LYS A CA  
173  C  C   . LYS A 24  ? 0.0704 0.2001 0.1621 0.0125  -0.0084 -0.0111 24  LYS A C   
174  O  O   . LYS A 24  ? 0.0445 0.3097 0.1926 0.0223  -0.0239 -0.0325 24  LYS A O   
175  C  CB  . LYS A 24  ? 0.0497 0.3046 0.2009 0.0580  -0.0189 0.0132  24  LYS A CB  
176  C  CG  . LYS A 24  ? 0.1231 0.3466 0.1987 0.0731  0.0193  0.0106  24  LYS A CG  
177  C  CD  . LYS A 24  ? 0.1097 0.4672 0.4270 0.0454  -0.0337 -0.0192 24  LYS A CD  
178  C  CE  . LYS A 24  ? 0.2903 0.3934 0.4024 0.0187  0.0807  0.0115  24  LYS A CE  
179  N  NZ  . LYS A 24  ? 0.5341 0.3426 0.5116 0.1073  0.2024  0.0421  24  LYS A NZ  
180  N  N   . GLY A 25  ? 0.0373 0.1966 0.1734 0.0153  0.0288  -0.0141 25  GLY A N   
181  C  CA  . GLY A 25  ? 0.0211 0.2371 0.1815 -0.0034 0.0100  -0.0584 25  GLY A CA  
182  C  C   . GLY A 25  ? 0.0485 0.2724 0.1300 -0.0136 -0.0244 -0.0479 25  GLY A C   
183  O  O   . GLY A 25  ? 0.0319 0.2740 0.1573 0.0029  0.0055  -0.0315 25  GLY A O   
184  N  N   . GLU A 26  ? 0.0251 0.3060 0.1210 -0.0086 -0.0328 -0.0482 26  GLU A N   
185  C  CA  . GLU A 26  ? 0.0513 0.3450 0.1214 0.0033  -0.0133 -0.0436 26  GLU A CA  
186  C  C   . GLU A 26  ? 0.0442 0.2691 0.1023 0.0217  -0.0034 -0.0442 26  GLU A C   
187  O  O   . GLU A 26  ? 0.0874 0.2820 0.1122 0.0040  0.0002  -0.0158 26  GLU A O   
188  C  CB  . GLU A 26  ? 0.1044 0.4860 0.1754 0.0114  -0.0206 -0.1398 26  GLU A CB  
189  C  CG  . GLU A 26  ? 0.1286 0.5723 0.2633 -0.0947 -0.0146 -0.0681 26  GLU A CG  
190  C  CD  . GLU A 26  ? 0.3183 0.6549 0.3863 -0.0773 -0.1670 0.0114  26  GLU A CD  
191  O  OE1 . GLU A 26  ? 0.3772 0.7497 0.4816 -0.1398 -0.1450 0.0450  26  GLU A OE1 
192  O  OE2 . GLU A 26  ? 0.3007 0.7316 0.7199 0.0663  -0.1879 0.1204  26  GLU A OE2 
193  N  N   . ARG A 27  ? 0.0172 0.1562 0.1301 -0.0069 -0.0243 -0.0396 27  ARG A N   
194  C  CA  . ARG A 27  ? 0.0098 0.1549 0.1099 0.0177  -0.0151 -0.0305 27  ARG A CA  
195  C  C   . ARG A 27  ? 0.0070 0.1226 0.0945 -0.0008 0.0077  -0.0099 27  ARG A C   
196  O  O   . ARG A 27  ? 0.0075 0.1214 0.1262 0.0104  -0.0065 -0.0178 27  ARG A O   
197  C  CB  . ARG A 27  ? 0.0734 0.1717 0.1750 0.0520  -0.0405 -0.0450 27  ARG A CB  
198  C  CG  . ARG A 27  ? 0.1350 0.2485 0.2362 0.0329  0.0133  -0.0237 27  ARG A CG  
199  C  CD  . ARG A 27  ? 0.1540 0.2893 0.2978 0.0827  0.0060  0.0116  27  ARG A CD  
200  N  NE  . ARG A 27  ? 0.1779 0.1950 0.2337 0.0428  0.0401  -0.0204 27  ARG A NE  
201  C  CZ  . ARG A 27  ? 0.1736 0.1535 0.1577 0.0394  0.0590  -0.0275 27  ARG A CZ  
202  N  NH1 . ARG A 27  ? 0.0445 0.2030 0.2288 0.0062  0.0257  -0.1172 27  ARG A NH1 
203  N  NH2 . ARG A 27  ? 0.1605 0.2091 0.2132 -0.0529 0.0469  -0.0586 27  ARG A NH2 
204  N  N   . GLN A 28  ? 0.0069 0.1265 0.1003 -0.0061 0.0065  -0.0357 28  GLN A N   
205  C  CA  . GLN A 28  ? 0.0068 0.1215 0.1061 0.0075  -0.0055 -0.0541 28  GLN A CA  
206  C  C   . GLN A 28  ? 0.0064 0.0872 0.0930 0.0028  -0.0011 -0.0232 28  GLN A C   
207  O  O   . GLN A 28  ? 0.0224 0.1368 0.0829 -0.0059 0.0051  -0.0167 28  GLN A O   
208  C  CB  . GLN A 28  ? 0.0069 0.1233 0.1475 0.0034  0.0065  -0.0405 28  GLN A CB  
209  C  CG  . GLN A 28  ? 0.0104 0.1102 0.1022 -0.0096 -0.0027 -0.0304 28  GLN A CG  
210  C  CD  . GLN A 28  ? 0.0066 0.1366 0.1112 -0.0012 -0.0054 -0.0163 28  GLN A CD  
211  O  OE1 . GLN A 28  ? 0.0080 0.1036 0.1237 -0.0124 -0.0012 -0.0215 28  GLN A OE1 
212  N  NE2 . GLN A 28  ? 0.0064 0.1312 0.1621 0.0001  -0.0045 -0.0143 28  GLN A NE2 
213  N  N   . SER A 29  ? 0.0069 0.0915 0.0964 0.0071  -0.0009 -0.0330 29  SER A N   
214  C  CA  . SER A 29  ? 0.0072 0.0745 0.0921 0.0077  -0.0035 -0.0167 29  SER A CA  
215  C  C   . SER A 29  ? 0.0109 0.0894 0.0916 0.0047  0.0185  -0.0083 29  SER A C   
216  O  O   . SER A 29  ? 0.0108 0.0942 0.0991 0.0036  0.0195  -0.0089 29  SER A O   
217  C  CB  . SER A 29  ? 0.0093 0.0905 0.0814 0.0153  0.0029  -0.0051 29  SER A CB  
218  O  OG  . SER A 29  ? 0.0098 0.0896 0.1112 0.0070  0.0153  -0.0191 29  SER A OG  
219  N  N   . PRO A 30  ? 0.0135 0.0777 0.0935 0.0092  0.0219  -0.0066 30  PRO A N   
220  C  CA  . PRO A 30  ? 0.0217 0.0973 0.0732 -0.0084 0.0226  0.0047  30  PRO A CA  
221  C  C   . PRO A 30  ? 0.0073 0.0936 0.0960 0.0024  0.0093  0.0086  30  PRO A C   
222  O  O   . PRO A 30  ? 0.0080 0.1105 0.0875 0.0125  -0.0014 0.0183  30  PRO A O   
223  C  CB  . PRO A 30  ? 0.0098 0.1181 0.1021 0.0154  0.0078  -0.0230 30  PRO A CB  
224  C  CG  . PRO A 30  ? 0.0087 0.0800 0.1172 -0.0023 0.0161  -0.0294 30  PRO A CG  
225  C  CD  . PRO A 30  ? 0.0272 0.0634 0.0844 -0.0032 0.0063  -0.0219 30  PRO A CD  
226  N  N   . VAL A 31  ? 0.0092 0.0855 0.0846 0.0128  0.0119  0.0276  31  VAL A N   
227  C  CA  . VAL A 31  ? 0.0276 0.0782 0.0749 0.0001  0.0140  0.0167  31  VAL A CA  
228  C  C   . VAL A 31  ? 0.0088 0.0882 0.1030 0.0051  0.0146  0.0049  31  VAL A C   
229  O  O   . VAL A 31  ? 0.0069 0.1155 0.1189 0.0060  0.0065  0.0292  31  VAL A O   
230  C  CB  . VAL A 31  ? 0.0068 0.0801 0.0922 -0.0045 0.0050  -0.0097 31  VAL A CB  
231  C  CG1 . VAL A 31  ? 0.0344 0.0989 0.1109 -0.0314 0.0131  -0.0184 31  VAL A CG1 
232  C  CG2 . VAL A 31  ? 0.0155 0.1287 0.1132 0.0189  0.0233  -0.0157 31  VAL A CG2 
233  N  N   . ASP A 32  ? 0.0200 0.0982 0.0991 0.0061  0.0072  0.0113  32  ASP A N   
234  C  CA  . ASP A 32  ? 0.0470 0.0838 0.1050 0.0122  0.0337  0.0233  32  ASP A CA  
235  C  C   . ASP A 32  ? 0.0380 0.1201 0.0964 0.0099  0.0234  0.0074  32  ASP A C   
236  O  O   . ASP A 32  ? 0.0443 0.1725 0.1221 0.0033  0.0328  -0.0190 32  ASP A O   
237  C  CB  . ASP A 32  ? 0.0801 0.1091 0.1353 0.0228  0.0214  0.0526  32  ASP A CB  
238  C  CG  . ASP A 32  ? 0.1239 0.1049 0.1438 -0.0049 0.0015  0.0225  32  ASP A CG  
239  O  OD1 . ASP A 32  ? 0.0758 0.1272 0.1380 0.0068  0.0048  0.0238  32  ASP A OD1 
240  O  OD2 . ASP A 32  ? 0.2086 0.1450 0.1497 -0.0064 0.0019  0.0357  32  ASP A OD2 
241  N  N   . ILE A 33  ? 0.0432 0.1346 0.0803 0.0070  0.0242  0.0210  33  ILE A N   
242  C  CA  . ILE A 33  ? 0.0525 0.1098 0.0863 0.0215  0.0331  0.0440  33  ILE A CA  
243  C  C   . ILE A 33  ? 0.1073 0.0958 0.0849 0.0114  0.0324  0.0285  33  ILE A C   
244  O  O   . ILE A 33  ? 0.1115 0.0989 0.1384 -0.0063 0.0212  0.0249  33  ILE A O   
245  C  CB  . ILE A 33  ? 0.0425 0.1275 0.0845 0.0219  0.0380  0.0368  33  ILE A CB  
246  C  CG1 . ILE A 33  ? 0.0840 0.1143 0.1197 0.0433  0.0158  0.0589  33  ILE A CG1 
247  C  CG2 . ILE A 33  ? 0.0507 0.1710 0.1329 0.0275  0.0558  0.0087  33  ILE A CG2 
248  C  CD1 . ILE A 33  ? 0.0715 0.1695 0.1509 0.0231  0.0021  0.0919  33  ILE A CD1 
249  N  N   . ASP A 34  ? 0.0915 0.1537 0.0795 0.0212  0.0232  0.0475  34  ASP A N   
250  C  CA  . ASP A 34  ? 0.0895 0.1614 0.1077 0.0164  0.0228  0.0647  34  ASP A CA  
251  C  C   . ASP A 34  ? 0.1243 0.1314 0.1459 0.0357  0.0582  0.0690  34  ASP A C   
252  O  O   . ASP A 34  ? 0.1585 0.1520 0.1804 0.0504  0.0556  0.0299  34  ASP A O   
253  C  CB  . ASP A 34  ? 0.1365 0.2126 0.1210 0.0453  -0.0012 0.0375  34  ASP A CB  
254  C  CG  . ASP A 34  ? 0.1620 0.2469 0.2295 0.0693  0.0328  0.1098  34  ASP A CG  
255  O  OD1 . ASP A 34  ? 0.1879 0.3031 0.2274 0.0827  0.0954  0.1262  34  ASP A OD1 
256  O  OD2 . ASP A 34  ? 0.3093 0.4357 0.4282 0.0406  -0.1005 0.2537  34  ASP A OD2 
257  N  N   . THR A 35  ? 0.0876 0.2138 0.1943 0.0254  0.0362  0.0805  35  THR A N   
258  C  CA  . THR A 35  ? 0.1158 0.2485 0.1796 0.0812  0.0509  0.0784  35  THR A CA  
259  C  C   . THR A 35  ? 0.1577 0.1857 0.1724 0.0632  0.0613  0.0221  35  THR A C   
260  O  O   . THR A 35  ? 0.1993 0.2368 0.2583 0.0919  0.0986  0.0106  35  THR A O   
261  C  CB  . THR A 35  ? 0.1265 0.2936 0.1993 0.0305  0.0256  0.0958  35  THR A CB  
262  O  OG1 . THR A 35  ? 0.1578 0.2654 0.2468 0.0026  0.0523  0.0779  35  THR A OG1 
263  C  CG2 . THR A 35  ? 0.1718 0.3704 0.2068 0.0526  0.0431  0.1271  35  THR A CG2 
264  N  N   . HIS A 36  ? 0.2055 0.1875 0.1937 0.0773  0.1201  0.0785  36  HIS A N   
265  C  CA  . HIS A 36  ? 0.3272 0.2115 0.1932 0.1036  0.1514  0.0966  36  HIS A CA  
266  C  C   . HIS A 36  ? 0.4623 0.2113 0.2184 0.0822  0.1987  0.0436  36  HIS A C   
267  O  O   . HIS A 36  ? 0.9175 0.3730 0.2420 -0.0441 0.3185  -0.0551 36  HIS A O   
268  C  CB  . HIS A 36  ? 0.3754 0.2265 0.1395 0.1050  0.1026  0.1326  36  HIS A CB  
269  C  CG  . HIS A 36  ? 0.5966 0.2900 0.2529 0.1339  -0.0134 0.0562  36  HIS A CG  
270  N  ND1 . HIS A 36  ? 0.6334 0.2828 0.2505 0.2089  -0.0158 0.0961  36  HIS A ND1 
271  C  CD2 . HIS A 36  ? 0.6588 0.2149 0.2122 -0.0075 -0.1039 0.1018  36  HIS A CD2 
272  C  CE1 . HIS A 36  ? 0.8031 0.3772 0.3955 0.0677  -0.0337 -0.0197 36  HIS A CE1 
273  N  NE2 . HIS A 36  ? 0.7977 0.2150 0.2634 0.0836  -0.0248 0.0152  36  HIS A NE2 
274  N  N   . THR A 37  ? 0.2626 0.2016 0.2063 0.1268  0.0652  0.0600  37  THR A N   
275  C  CA  . THR A 37  ? 0.3272 0.2314 0.1472 0.0961  0.0723  0.0686  37  THR A CA  
276  C  C   . THR A 37  ? 0.2583 0.2344 0.1068 0.0958  0.0370  0.0388  37  THR A C   
277  O  O   . THR A 37  ? 0.3485 0.2717 0.1764 0.0765  -0.0236 0.0068  37  THR A O   
278  C  CB  . THR A 37  ? 0.2697 0.2488 0.4900 0.1366  -0.1386 0.0298  37  THR A CB  
279  O  OG1 . THR A 37  ? 0.4644 0.3477 0.4493 0.1337  0.0452  0.1362  37  THR A OG1 
280  C  CG2 . THR A 37  ? 0.3818 0.3667 0.3208 0.0323  -0.1321 0.0873  37  THR A CG2 
281  N  N   . ALA A 38  ? 0.1991 0.1975 0.1080 0.0908  0.0571  0.0559  38  ALA A N   
282  C  CA  . ALA A 38  ? 0.1976 0.2195 0.1188 0.1360  0.0535  0.0326  38  ALA A CA  
283  C  C   . ALA A 38  ? 0.1890 0.1958 0.1814 0.0782  0.1032  0.0537  38  ALA A C   
284  O  O   . ALA A 38  ? 0.2716 0.2399 0.2687 0.0485  0.1613  0.0465  38  ALA A O   
285  C  CB  . ALA A 38  ? 0.1091 0.1897 0.1822 0.0560  0.0312  0.0141  38  ALA A CB  
286  N  N   A LYS A 39  ? 0.1971 0.2222 0.1427 0.1237  0.0328  0.0053  39  LYS A N   
287  N  N   B LYS A 39  ? 0.1896 0.2291 0.1534 0.1447  0.0247  0.0019  39  LYS A N   
288  C  CA  A LYS A 39  ? 0.1608 0.2716 0.1477 0.1345  0.0172  0.0008  39  LYS A CA  
289  C  CA  B LYS A 39  ? 0.1876 0.2934 0.1258 0.1315  0.0188  0.0502  39  LYS A CA  
290  C  C   A LYS A 39  ? 0.1315 0.2835 0.0754 0.1129  0.0435  -0.0079 39  LYS A C   
291  C  C   B LYS A 39  ? 0.1458 0.2564 0.1045 0.1170  0.0412  0.0223  39  LYS A C   
292  O  O   A LYS A 39  ? 0.1436 0.2809 0.0644 0.0680  0.0312  -0.0040 39  LYS A O   
293  O  O   B LYS A 39  ? 0.1254 0.3047 0.1195 0.0841  0.0373  0.0736  39  LYS A O   
294  C  CB  A LYS A 39  ? 0.1770 0.2606 0.0594 0.1168  0.0001  0.0444  39  LYS A CB  
295  C  CB  B LYS A 39  ? 0.2504 0.2749 0.0991 0.1341  0.0207  0.0594  39  LYS A CB  
296  C  CG  A LYS A 39  ? 0.2167 0.3037 0.1012 0.1181  0.0105  0.0049  39  LYS A CG  
297  C  CG  B LYS A 39  ? 0.1810 0.4001 0.1084 0.2061  -0.0219 0.0409  39  LYS A CG  
298  C  CD  A LYS A 39  ? 0.2464 0.3312 0.1027 0.0482  -0.0075 0.0035  39  LYS A CD  
299  C  CD  B LYS A 39  ? 0.2027 0.3845 0.1894 0.1685  0.0048  -0.0126 39  LYS A CD  
300  C  CE  A LYS A 39  ? 0.2512 0.3740 0.1438 0.0741  -0.0021 -0.0187 39  LYS A CE  
301  C  CE  B LYS A 39  ? 0.2673 0.4569 0.1531 0.1776  0.0075  -0.1118 39  LYS A CE  
302  N  NZ  A LYS A 39  ? 0.2533 0.4286 0.2036 0.1476  0.0491  0.0423  39  LYS A NZ  
303  N  NZ  B LYS A 39  ? 0.2461 0.4322 0.2751 0.1251  -0.0530 -0.1671 39  LYS A NZ  
304  N  N   . TYR A 40  ? 0.1944 0.2681 0.1343 0.0623  0.0522  0.0228  40  TYR A N   
305  C  CA  . TYR A 40  ? 0.1427 0.2674 0.1652 0.0433  0.0873  0.0034  40  TYR A CA  
306  C  C   . TYR A 40  ? 0.1587 0.2688 0.1377 0.0623  0.0672  0.0269  40  TYR A C   
307  O  O   . TYR A 40  ? 0.2055 0.3644 0.1297 0.1179  0.0487  0.0051  40  TYR A O   
308  C  CB  . TYR A 40  ? 0.1705 0.3342 0.1208 0.0119  0.0710  0.0447  40  TYR A CB  
309  C  CG  . TYR A 40  ? 0.1283 0.4284 0.1613 0.0018  0.0659  0.0709  40  TYR A CG  
310  C  CD1 . TYR A 40  ? 0.1872 0.3556 0.1875 -0.0381 0.0412  0.0806  40  TYR A CD1 
311  C  CD2 . TYR A 40  ? 0.2263 0.5716 0.2252 0.0644  0.1383  0.0658  40  TYR A CD2 
312  C  CE1 . TYR A 40  ? 0.2080 0.5565 0.2245 0.0258  0.0540  0.0446  40  TYR A CE1 
313  C  CE2 . TYR A 40  ? 0.1892 0.5940 0.3000 0.0350  0.1042  0.0095  40  TYR A CE2 
314  C  CZ  . TYR A 40  ? 0.3419 0.8158 0.2009 -0.0216 0.0910  -0.0282 40  TYR A CZ  
315  O  OH  . TYR A 40  ? 0.3140 0.7353 0.5235 0.0957  -0.0148 0.0339  40  TYR A OH  
316  N  N   . ASP A 41  ? 0.1111 0.2575 0.1502 0.0768  0.0572  0.0176  41  ASP A N   
317  C  CA  . ASP A 41  ? 0.1933 0.2478 0.1696 0.1205  -0.0095 0.0220  41  ASP A CA  
318  C  C   . ASP A 41  ? 0.1951 0.3826 0.2069 0.1379  -0.0011 0.0195  41  ASP A C   
319  O  O   . ASP A 41  ? 0.2432 0.3614 0.1815 0.1683  0.0309  0.0032  41  ASP A O   
320  C  CB  . ASP A 41  ? 0.3053 0.1799 0.2579 0.0697  0.0128  -0.0070 41  ASP A CB  
321  C  CG  . ASP A 41  ? 0.4753 0.2215 0.3733 0.0273  -0.0059 -0.0710 41  ASP A CG  
322  O  OD1 . ASP A 41  ? 0.4927 0.3388 0.3491 0.1542  -0.0996 -0.0897 41  ASP A OD1 
323  O  OD2 . ASP A 41  ? 0.5103 0.3459 0.5274 -0.0763 -0.1314 -0.0100 41  ASP A OD2 
324  N  N   . PRO A 42  ? 0.3529 0.5826 0.1793 0.3209  0.0668  0.0077  42  PRO A N   
325  C  CA  . PRO A 42  ? 0.3765 0.6900 0.3251 0.2942  0.0079  0.0675  42  PRO A CA  
326  C  C   . PRO A 42  ? 0.5050 0.6571 0.1993 0.1709  0.1245  0.0435  42  PRO A C   
327  O  O   . PRO A 42  ? 0.4102 0.6860 0.2676 0.2118  0.1397  0.1093  42  PRO A O   
328  C  CB  . PRO A 42  ? 0.6077 1.0026 0.4476 0.2051  0.2070  0.0679  42  PRO A CB  
329  C  CG  . PRO A 42  ? 0.7239 1.0526 0.3025 0.3692  0.3447  -0.0659 42  PRO A CG  
330  C  CD  . PRO A 42  ? 0.5310 0.8063 0.1971 0.2231  0.0966  0.1266  42  PRO A CD  
331  N  N   . SER A 43  ? 0.4990 0.4371 0.1321 0.2539  0.0990  -0.0099 43  SER A N   
332  C  CA  . SER A 43  ? 0.6651 0.3970 0.1872 0.2365  -0.0148 -0.0379 43  SER A CA  
333  C  C   . SER A 43  ? 0.6740 0.4541 0.1814 0.2985  -0.0018 -0.0659 43  SER A C   
334  O  O   . SER A 43  ? 0.5993 0.4327 0.2989 0.3015  -0.0326 -0.0675 43  SER A O   
335  C  CB  . SER A 43  ? 0.8261 0.4385 0.3689 0.1888  -0.0359 -0.1181 43  SER A CB  
336  O  OG  . SER A 43  ? 0.8953 0.4253 0.3470 0.1995  -0.0531 -0.0666 43  SER A OG  
337  N  N   . LEU A 44  ? 0.3802 0.4296 0.1534 0.2237  0.0023  -0.0477 44  LEU A N   
338  C  CA  . LEU A 44  ? 0.1998 0.3703 0.1626 0.1585  -0.0073 0.0044  44  LEU A CA  
339  C  C   . LEU A 44  ? 0.1312 0.3578 0.2205 0.0964  0.0427  0.0504  44  LEU A C   
340  O  O   . LEU A 44  ? 0.1689 0.5274 0.2615 0.0439  0.0485  0.1414  44  LEU A O   
341  C  CB  . LEU A 44  ? 0.1076 0.3374 0.1682 0.0899  0.0172  0.0208  44  LEU A CB  
342  C  CG  . LEU A 44  ? 0.1036 0.1987 0.2041 0.0406  0.0103  0.0194  44  LEU A CG  
343  C  CD1 . LEU A 44  ? 0.0982 0.2299 0.1738 0.0363  0.0529  -0.0027 44  LEU A CD1 
344  C  CD2 . LEU A 44  ? 0.1742 0.1847 0.2150 0.0051  -0.0140 0.0111  44  LEU A CD2 
345  N  N   . LYS A 45  ? 0.2054 0.3310 0.2156 0.1018  -0.0006 0.0528  45  LYS A N   
346  C  CA  . LYS A 45  ? 0.1779 0.2684 0.2379 0.0646  0.0033  -0.0073 45  LYS A CA  
347  C  C   . LYS A 45  ? 0.0935 0.2770 0.2564 0.0885  0.0174  -0.0080 45  LYS A C   
348  O  O   . LYS A 45  ? 0.0469 0.2751 0.2407 0.0309  0.0258  -0.0167 45  LYS A O   
349  C  CB  . LYS A 45  ? 0.1854 0.2672 0.2224 0.1203  0.0323  -0.0099 45  LYS A CB  
350  C  CG  . LYS A 45  ? 0.2490 0.3944 0.2702 0.0612  -0.0148 -0.1018 45  LYS A CG  
351  C  CD  . LYS A 45  ? 0.5456 0.4142 0.4577 0.0400  0.0500  -0.0359 45  LYS A CD  
352  C  CE  . LYS A 45  ? 0.9078 0.5646 0.5143 0.0583  -0.0164 -0.2552 45  LYS A CE  
353  N  NZ  . LYS A 45  ? 0.8590 0.7899 0.6357 -0.2014 -0.1491 -0.2962 45  LYS A NZ  
354  N  N   . PRO A 46  ? 0.0743 0.2795 0.2161 -0.0095 0.0613  -0.0001 46  PRO A N   
355  C  CA  . PRO A 46  ? 0.0763 0.2712 0.1685 0.0000  0.0279  0.0397  46  PRO A CA  
356  C  C   . PRO A 46  ? 0.0527 0.2399 0.2147 0.0034  0.0589  0.0258  46  PRO A C   
357  O  O   . PRO A 46  ? 0.0493 0.2665 0.2339 -0.0403 0.0185  0.0309  46  PRO A O   
358  C  CB  . PRO A 46  ? 0.0575 0.3661 0.2684 -0.0193 0.0302  -0.0042 46  PRO A CB  
359  C  CG  . PRO A 46  ? 0.1840 0.4296 0.3079 0.0083  0.0800  -0.0853 46  PRO A CG  
360  C  CD  . PRO A 46  ? 0.1666 0.3542 0.3008 0.0836  0.0903  -0.1368 46  PRO A CD  
361  N  N   . LEU A 47  ? 0.0362 0.1982 0.2123 -0.0074 0.0120  0.0325  47  LEU A N   
362  C  CA  . LEU A 47  ? 0.0171 0.1674 0.2308 -0.0300 0.0286  0.0268  47  LEU A CA  
363  C  C   . LEU A 47  ? 0.0478 0.1681 0.2565 -0.0385 0.0006  0.0535  47  LEU A C   
364  O  O   . LEU A 47  ? 0.0835 0.2425 0.3110 -0.0956 -0.0250 0.1035  47  LEU A O   
365  C  CB  . LEU A 47  ? 0.1693 0.1825 0.2630 0.0006  0.0308  -0.0061 47  LEU A CB  
366  C  CG  . LEU A 47  ? 0.1224 0.3186 0.4019 -0.0430 0.0350  -0.1324 47  LEU A CG  
367  C  CD1 . LEU A 47  ? 0.0967 0.3412 0.4970 -0.0392 0.0237  -0.1872 47  LEU A CD1 
368  C  CD2 . LEU A 47  ? 0.0849 0.3455 0.3865 0.0091  -0.0245 -0.1725 47  LEU A CD2 
369  N  N   . SER A 48  ? 0.0252 0.1700 0.1865 -0.0019 0.0228  0.0416  48  SER A N   
370  C  CA  . SER A 48  ? 0.0232 0.1583 0.1655 -0.0290 0.0234  0.0295  48  SER A CA  
371  C  C   . SER A 48  ? 0.0276 0.1639 0.1899 -0.0400 0.0454  -0.0017 48  SER A C   
372  O  O   . SER A 48  ? 0.0461 0.1885 0.1817 -0.0727 0.0411  -0.0108 48  SER A O   
373  C  CB  . SER A 48  ? 0.1050 0.1452 0.2691 -0.0129 0.0009  0.0429  48  SER A CB  
374  O  OG  . SER A 48  ? 0.1314 0.2774 0.2856 0.0263  0.0048  0.0505  48  SER A OG  
375  N  N   . VAL A 49  ? 0.0677 0.2158 0.1763 -0.0586 0.0332  -0.0084 49  VAL A N   
376  C  CA  . VAL A 49  ? 0.0910 0.2415 0.1872 -0.1081 0.0517  -0.0521 49  VAL A CA  
377  C  C   . VAL A 49  ? 0.0989 0.3222 0.1861 -0.1160 0.0380  -0.0051 49  VAL A C   
378  O  O   . VAL A 49  ? 0.1423 0.3808 0.2499 -0.1680 -0.0133 0.0691  49  VAL A O   
379  C  CB  . VAL A 49  ? 0.1222 0.2385 0.1993 -0.0809 0.0640  -0.0264 49  VAL A CB  
380  C  CG1 . VAL A 49  ? 0.2457 0.3644 0.2005 -0.1477 0.1021  -0.0304 49  VAL A CG1 
381  C  CG2 . VAL A 49  ? 0.0900 0.2327 0.2978 -0.0395 0.0571  0.0186  49  VAL A CG2 
382  N  N   . SER A 50  ? 0.0571 0.2770 0.1840 -0.0566 0.0230  -0.0192 50  SER A N   
383  C  CA  . SER A 50  ? 0.0163 0.2952 0.2346 -0.0495 0.0212  -0.0166 50  SER A CA  
384  C  C   . SER A 50  ? 0.0127 0.2995 0.2068 -0.0425 -0.0030 -0.0174 50  SER A C   
385  O  O   . SER A 50  ? 0.0482 0.2479 0.2398 -0.0342 0.0065  0.0212  50  SER A O   
386  C  CB  . SER A 50  ? 0.1736 0.2907 0.3489 -0.0489 0.1084  -0.0121 50  SER A CB  
387  O  OG  . SER A 50  ? 0.2368 0.4327 0.3111 -0.0590 0.0696  -0.0604 50  SER A OG  
388  N  N   . TYR A 51  ? 0.0227 0.2379 0.1987 -0.0291 0.0082  -0.0038 51  TYR A N   
389  C  CA  . TYR A 51  ? 0.0738 0.2285 0.1650 -0.0511 0.0051  0.0212  51  TYR A CA  
390  C  C   . TYR A 51  ? 0.1076 0.2784 0.1955 -0.0201 -0.0117 0.0252  51  TYR A C   
391  O  O   . TYR A 51  ? 0.1093 0.2870 0.2151 -0.0005 -0.0168 0.0358  51  TYR A O   
392  C  CB  . TYR A 51  ? 0.0795 0.2824 0.1808 -0.0021 -0.0529 -0.0137 51  TYR A CB  
393  C  CG  . TYR A 51  ? 0.0392 0.1874 0.1718 -0.0219 -0.0133 0.0171  51  TYR A CG  
394  C  CD1 . TYR A 51  ? 0.0313 0.1914 0.2194 -0.0185 -0.0022 -0.0047 51  TYR A CD1 
395  C  CD2 . TYR A 51  ? 0.0355 0.1808 0.1483 -0.0233 0.0127  -0.0182 51  TYR A CD2 
396  C  CE1 . TYR A 51  ? 0.0249 0.1728 0.1548 -0.0239 0.0301  0.0233  51  TYR A CE1 
397  C  CE2 . TYR A 51  ? 0.0279 0.1804 0.1329 -0.0329 0.0143  -0.0289 51  TYR A CE2 
398  C  CZ  . TYR A 51  ? 0.0203 0.1631 0.1366 -0.0355 0.0310  -0.0156 51  TYR A CZ  
399  O  OH  . TYR A 51  ? 0.0434 0.1574 0.1835 -0.0232 -0.0004 -0.0136 51  TYR A OH  
400  N  N   . ASP A 52  ? 0.0519 0.4483 0.3330 -0.0474 0.0110  0.0554  52  ASP A N   
401  C  CA  . ASP A 52  ? 0.1414 0.3388 0.2782 0.0291  0.0386  0.0968  52  ASP A CA  
402  C  C   . ASP A 52  ? 0.0644 0.2820 0.3100 0.0034  0.0131  0.0804  52  ASP A C   
403  O  O   . ASP A 52  ? 0.2239 0.3830 0.2986 0.0778  -0.0221 0.1070  52  ASP A O   
404  C  CB  . ASP A 52  ? 0.0680 0.4943 0.3735 0.0067  0.0287  0.0895  52  ASP A CB  
405  C  CG  . ASP A 52  ? 0.2025 0.4656 0.6511 -0.0274 0.0577  0.0158  52  ASP A CG  
406  O  OD1 . ASP A 52  ? 0.3493 0.6997 0.6730 0.1046  0.1242  0.1411  52  ASP A OD1 
407  O  OD2 . ASP A 52  ? 0.3866 0.6454 1.0869 0.1284  0.0526  0.2597  52  ASP A OD2 
408  N  N   . GLN A 53  ? 0.0594 0.3049 0.3753 0.0080  0.0073  0.0350  53  GLN A N   
409  C  CA  . GLN A 53  ? 0.1596 0.3441 0.4816 -0.0249 0.0902  0.0735  53  GLN A CA  
410  C  C   . GLN A 53  ? 0.1602 0.1930 0.3493 0.0228  0.0248  -0.0024 53  GLN A C   
411  O  O   . GLN A 53  ? 0.1395 0.2228 0.3585 0.0205  -0.0156 0.0143  53  GLN A O   
412  C  CB  . GLN A 53  ? 0.2199 0.3833 0.5128 0.1169  0.0502  0.0258  53  GLN A CB  
413  C  CG  . GLN A 53  ? 0.2095 0.5734 0.7359 0.1078  0.1118  0.0741  53  GLN A CG  
414  C  CD  . GLN A 53  ? 0.4748 0.6017 0.7225 0.0815  0.0683  0.2192  53  GLN A CD  
415  O  OE1 . GLN A 53  ? 0.3112 0.7276 0.6993 -0.0272 -0.1957 0.2137  53  GLN A OE1 
416  N  NE2 . GLN A 53  ? 0.3388 0.5189 0.8894 0.2137  0.1023  0.3209  53  GLN A NE2 
417  N  N   . ALA A 54  ? 0.0682 0.1728 0.2741 -0.0145 0.0245  -0.0011 54  ALA A N   
418  C  CA  . ALA A 54  ? 0.0750 0.1680 0.1969 0.0122  0.0130  -0.0075 54  ALA A CA  
419  C  C   . ALA A 54  ? 0.1359 0.1667 0.1991 -0.0270 -0.0068 0.0190  54  ALA A C   
420  O  O   . ALA A 54  ? 0.1090 0.2843 0.2580 -0.0283 -0.0240 -0.0392 54  ALA A O   
421  C  CB  . ALA A 54  ? 0.1081 0.1948 0.2256 0.0201  0.0197  0.0279  54  ALA A CB  
422  N  N   . THR A 55  ? 0.0894 0.1484 0.1689 0.0143  0.0116  0.0254  55  THR A N   
423  C  CA  . THR A 55  ? 0.0933 0.1630 0.1639 0.0362  -0.0184 0.0377  55  THR A CA  
424  C  C   . THR A 55  ? 0.0876 0.1254 0.1283 0.0223  -0.0434 0.0445  55  THR A C   
425  O  O   . THR A 55  ? 0.0935 0.1418 0.1720 0.0079  -0.0361 0.0318  55  THR A O   
426  C  CB  . THR A 55  ? 0.1294 0.1883 0.2489 0.0456  -0.0190 0.0933  55  THR A CB  
427  O  OG1 . THR A 55  ? 0.1440 0.2145 0.4562 0.0656  -0.0598 0.0337  55  THR A OG1 
428  C  CG2 . THR A 55  ? 0.2903 0.1907 0.2307 0.0942  -0.0182 0.0779  55  THR A CG2 
429  N  N   . SER A 56  ? 0.1040 0.1163 0.1544 0.0221  -0.0272 0.0379  56  SER A N   
430  C  CA  . SER A 56  ? 0.0942 0.1409 0.1391 0.0198  -0.0353 0.0252  56  SER A CA  
431  C  C   . SER A 56  ? 0.1393 0.1617 0.1452 0.0276  -0.0278 0.0402  56  SER A C   
432  O  O   . SER A 56  ? 0.1298 0.1763 0.1570 0.0175  -0.0319 0.0504  56  SER A O   
433  C  CB  . SER A 56  ? 0.1685 0.1351 0.1286 0.0127  -0.0384 0.0074  56  SER A CB  
434  O  OG  . SER A 56  ? 0.1120 0.1883 0.1646 -0.0236 -0.0434 0.0562  56  SER A OG  
435  N  N   . LEU A 57  ? 0.1373 0.1077 0.1278 0.0504  -0.0072 0.0435  57  LEU A N   
436  C  CA  . LEU A 57  ? 0.1416 0.1165 0.1602 0.0373  0.0131  0.0486  57  LEU A CA  
437  C  C   . LEU A 57  ? 0.1544 0.1347 0.1244 0.0412  -0.0129 0.0392  57  LEU A C   
438  O  O   . LEU A 57  ? 0.1567 0.1613 0.1164 0.0292  -0.0208 0.0160  57  LEU A O   
439  C  CB  . LEU A 57  ? 0.2077 0.1113 0.1876 0.0035  0.0405  0.0336  57  LEU A CB  
440  C  CG  . LEU A 57  ? 0.2559 0.1303 0.2353 0.0445  0.0710  0.0589  57  LEU A CG  
441  C  CD1 . LEU A 57  ? 0.4412 0.0906 0.3679 -0.0442 0.1005  0.0383  57  LEU A CD1 
442  C  CD2 . LEU A 57  ? 0.2748 0.1953 0.3462 0.0873  0.0590  0.1107  57  LEU A CD2 
443  N  N   . ARG A 58  ? 0.1179 0.1332 0.1141 0.0373  -0.0055 0.0233  58  ARG A N   
444  C  CA  . ARG A 58  ? 0.0763 0.1341 0.1395 0.0353  -0.0129 0.0315  58  ARG A CA  
445  C  C   . ARG A 58  ? 0.1111 0.1271 0.0914 0.0271  -0.0131 0.0089  58  ARG A C   
446  O  O   . ARG A 58  ? 0.1448 0.1294 0.0894 0.0211  0.0212  0.0147  58  ARG A O   
447  C  CB  . ARG A 58  ? 0.1091 0.1527 0.1930 0.0262  0.0099  0.0226  58  ARG A CB  
448  C  CG  . ARG A 58  ? 0.1307 0.2405 0.2346 -0.0037 0.0539  0.0294  58  ARG A CG  
449  C  CD  . ARG A 58  ? 0.1384 0.3126 0.2093 -0.0438 0.0469  0.0343  58  ARG A CD  
450  N  NE  . ARG A 58  ? 0.1376 0.2123 0.2555 -0.0536 0.0314  0.0639  58  ARG A NE  
451  C  CZ  . ARG A 58  ? 0.1192 0.1856 0.2140 -0.0401 0.0576  0.0627  58  ARG A CZ  
452  N  NH1 . ARG A 58  ? 0.2059 0.2208 0.2090 -0.0976 0.0871  0.0046  58  ARG A NH1 
453  N  NH2 . ARG A 58  ? 0.1073 0.2285 0.2519 -0.0478 0.0516  0.0517  58  ARG A NH2 
454  N  N   . ILE A 59  ? 0.0955 0.0969 0.0944 -0.0005 0.0138  0.0113  59  ILE A N   
455  C  CA  . ILE A 59  ? 0.0666 0.0948 0.1099 0.0098  0.0078  -0.0002 59  ILE A CA  
456  C  C   . ILE A 59  ? 0.0707 0.1276 0.0761 -0.0067 0.0074  0.0203  59  ILE A C   
457  O  O   . ILE A 59  ? 0.1197 0.1659 0.0689 0.0133  0.0058  0.0165  59  ILE A O   
458  C  CB  . ILE A 59  ? 0.0849 0.0946 0.0801 0.0020  0.0089  0.0132  59  ILE A CB  
459  C  CG1 . ILE A 59  ? 0.1050 0.0854 0.1150 -0.0002 -0.0084 0.0228  59  ILE A CG1 
460  C  CG2 . ILE A 59  ? 0.1419 0.1774 0.0885 0.0304  -0.0419 -0.0031 59  ILE A CG2 
461  C  CD1 . ILE A 59  ? 0.1269 0.1135 0.1293 -0.0244 -0.0179 0.0303  59  ILE A CD1 
462  N  N   . LEU A 60  ? 0.0560 0.1371 0.0770 0.0054  0.0157  0.0152  60  LEU A N   
463  C  CA  . LEU A 60  ? 0.0516 0.1138 0.0786 0.0031  0.0068  0.0118  60  LEU A CA  
464  C  C   . LEU A 60  ? 0.0688 0.1102 0.0794 0.0055  0.0179  0.0115  60  LEU A C   
465  O  O   . LEU A 60  ? 0.0745 0.1376 0.0790 0.0060  0.0298  0.0127  60  LEU A O   
466  C  CB  . LEU A 60  ? 0.0763 0.1039 0.1624 -0.0158 0.0148  0.0113  60  LEU A CB  
467  C  CG  . LEU A 60  ? 0.0820 0.1553 0.1368 -0.0291 0.0290  -0.0218 60  LEU A CG  
468  C  CD1 . LEU A 60  ? 0.1483 0.1685 0.1301 -0.0466 0.0229  -0.0105 60  LEU A CD1 
469  C  CD2 . LEU A 60  ? 0.1488 0.1143 0.1738 -0.0420 0.0033  -0.0075 60  LEU A CD2 
470  N  N   . ASN A 61  ? 0.0801 0.0903 0.1047 0.0030  0.0339  0.0095  61  ASN A N   
471  C  CA  . ASN A 61  ? 0.0568 0.0971 0.0829 -0.0034 0.0250  -0.0082 61  ASN A CA  
472  C  C   . ASN A 61  ? 0.0704 0.1199 0.0763 -0.0243 0.0357  -0.0053 61  ASN A C   
473  O  O   . ASN A 61  ? 0.0754 0.1226 0.0937 -0.0188 0.0335  0.0171  61  ASN A O   
474  C  CB  . ASN A 61  ? 0.0919 0.0842 0.1081 0.0001  0.0374  -0.0117 61  ASN A CB  
475  C  CG  . ASN A 61  ? 0.0855 0.0824 0.0804 -0.0107 0.0324  -0.0038 61  ASN A CG  
476  O  OD1 . ASN A 61  ? 0.0939 0.1235 0.0937 -0.0136 0.0366  -0.0089 61  ASN A OD1 
477  N  ND2 . ASN A 61  ? 0.0957 0.1040 0.0784 -0.0262 0.0471  -0.0238 61  ASN A ND2 
478  N  N   . ASN A 62  ? 0.0750 0.0998 0.0845 -0.0179 0.0272  -0.0178 62  ASN A N   
479  C  CA  . ASN A 62  ? 0.0876 0.0795 0.0998 -0.0178 0.0150  -0.0036 62  ASN A CA  
480  C  C   . ASN A 62  ? 0.0856 0.1011 0.1373 -0.0122 0.0463  0.0114  62  ASN A C   
481  O  O   . ASN A 62  ? 0.1195 0.1470 0.1635 -0.0493 0.0431  -0.0105 62  ASN A O   
482  C  CB  . ASN A 62  ? 0.1315 0.1122 0.0899 -0.0397 0.0023  -0.0175 62  ASN A CB  
483  C  CG  . ASN A 62  ? 0.1108 0.0950 0.0943 0.0156  0.0318  -0.0146 62  ASN A CG  
484  O  OD1 . ASN A 62  ? 0.0718 0.1005 0.1092 0.0058  0.0417  0.0012  62  ASN A OD1 
485  N  ND2 . ASN A 62  ? 0.1172 0.1919 0.1323 0.0240  0.0485  -0.0277 62  ASN A ND2 
486  N  N   . GLY A 63  ? 0.0584 0.1016 0.1025 -0.0053 0.0369  0.0268  63  GLY A N   
487  C  CA  . GLY A 63  ? 0.0567 0.1293 0.1050 0.0069  0.0373  0.0217  63  GLY A CA  
488  C  C   . GLY A 63  ? 0.0519 0.1102 0.1009 -0.0222 0.0244  0.0088  63  GLY A C   
489  O  O   . GLY A 63  ? 0.0657 0.1714 0.1481 0.0157  0.0554  0.0205  63  GLY A O   
490  N  N   . HIS A 64  ? 0.0484 0.1257 0.1106 -0.0280 0.0387  0.0353  64  HIS A N   
491  C  CA  . HIS A 64  ? 0.0653 0.1172 0.1118 -0.0332 0.0372  0.0354  64  HIS A CA  
492  C  C   . HIS A 64  ? 0.0418 0.1194 0.0905 -0.0179 0.0118  0.0362  64  HIS A C   
493  O  O   . HIS A 64  ? 0.0339 0.1247 0.1502 -0.0136 0.0137  0.0478  64  HIS A O   
494  C  CB  . HIS A 64  ? 0.0804 0.1576 0.1109 -0.0482 0.0074  0.0243  64  HIS A CB  
495  C  CG  . HIS A 64  ? 0.1034 0.1542 0.1729 -0.0614 0.0185  0.0024  64  HIS A CG  
496  N  ND1 . HIS A 64  ? 0.0854 0.2579 0.1544 -0.0456 0.0186  -0.0195 64  HIS A ND1 
497  C  CD2 . HIS A 64  ? 0.1300 0.1513 0.1574 -0.0838 -0.0068 -0.0021 64  HIS A CD2 
498  C  CE1 . HIS A 64  ? 0.0727 0.2770 0.2450 -0.0526 0.0378  -0.0157 64  HIS A CE1 
499  N  NE2 . HIS A 64  ? 0.1304 0.2522 0.2295 -0.0836 0.0350  -0.0091 64  HIS A NE2 
500  N  N   . THR A 65  ? 0.0400 0.1048 0.1034 0.0001  0.0335  0.0156  65  THR A N   
501  C  CA  . THR A 65  ? 0.0375 0.1341 0.0895 -0.0017 0.0239  0.0399  65  THR A CA  
502  C  C   . THR A 65  ? 0.0346 0.1072 0.0811 0.0100  0.0292  0.0278  65  THR A C   
503  O  O   . THR A 65  ? 0.0479 0.1233 0.0934 -0.0060 0.0478  0.0151  65  THR A O   
504  C  CB  . THR A 65  ? 0.0277 0.1079 0.1025 -0.0141 0.0318  0.0205  65  THR A CB  
505  O  OG1 . THR A 65  ? 0.0434 0.1917 0.1041 -0.0488 0.0069  0.0610  65  THR A OG1 
506  C  CG2 . THR A 65  ? 0.0627 0.1057 0.1183 -0.0156 0.0084  0.0043  65  THR A CG2 
507  N  N   . PHE A 66  ? 0.0366 0.1204 0.0824 0.0163  -0.0031 0.0129  66  PHE A N   
508  C  CA  . PHE A 66  ? 0.0515 0.1239 0.0637 0.0210  0.0064  0.0107  66  PHE A CA  
509  C  C   . PHE A 66  ? 0.0269 0.1190 0.0499 0.0114  0.0034  0.0178  66  PHE A C   
510  O  O   . PHE A 66  ? 0.0657 0.1247 0.0578 0.0034  0.0223  0.0151  66  PHE A O   
511  C  CB  . PHE A 66  ? 0.0883 0.1084 0.0831 -0.0126 0.0219  -0.0013 66  PHE A CB  
512  C  CG  . PHE A 66  ? 0.0977 0.0982 0.0732 -0.0177 0.0111  0.0012  66  PHE A CG  
513  C  CD1 . PHE A 66  ? 0.0898 0.1257 0.1056 -0.0162 -0.0099 -0.0063 66  PHE A CD1 
514  C  CD2 . PHE A 66  ? 0.1416 0.0978 0.0917 -0.0222 -0.0025 0.0114  66  PHE A CD2 
515  C  CE1 . PHE A 66  ? 0.0930 0.1253 0.1461 -0.0258 -0.0100 -0.0068 66  PHE A CE1 
516  C  CE2 . PHE A 66  ? 0.1025 0.0996 0.1190 -0.0018 -0.0051 -0.0053 66  PHE A CE2 
517  C  CZ  . PHE A 66  ? 0.0788 0.1337 0.1301 -0.0183 0.0022  0.0038  66  PHE A CZ  
518  N  N   . GLN A 67  ? 0.0261 0.1237 0.1111 0.0298  0.0256  0.0239  67  GLN A N   
519  C  CA  . GLN A 67  ? 0.0241 0.1132 0.1194 0.0305  0.0005  0.0093  67  GLN A CA  
520  C  C   . GLN A 67  ? 0.0461 0.1272 0.0413 0.0158  0.0042  0.0092  67  GLN A C   
521  O  O   . GLN A 67  ? 0.0662 0.1714 0.0475 0.0106  0.0176  0.0168  67  GLN A O   
522  C  CB  . GLN A 67  ? 0.0725 0.1233 0.1172 -0.0088 0.0042  0.0190  67  GLN A CB  
523  C  CG  . GLN A 67  ? 0.0883 0.1432 0.1251 -0.0262 -0.0047 0.0184  67  GLN A CG  
524  C  CD  . GLN A 67  ? 0.0686 0.1504 0.1522 -0.0070 -0.0097 -0.0098 67  GLN A CD  
525  O  OE1 . GLN A 67  ? 0.2070 0.1537 0.3197 -0.0020 -0.0241 -0.0329 67  GLN A OE1 
526  N  NE2 . GLN A 67  ? 0.0937 0.1142 0.1685 -0.0151 -0.0400 -0.0135 67  GLN A NE2 
527  N  N   . VAL A 68  ? 0.0366 0.1058 0.0959 0.0215  0.0104  0.0168  68  VAL A N   
528  C  CA  . VAL A 68  ? 0.0761 0.1186 0.0702 0.0302  -0.0111 0.0154  68  VAL A CA  
529  C  C   . VAL A 68  ? 0.0815 0.1090 0.0986 0.0217  0.0278  0.0272  68  VAL A C   
530  O  O   . VAL A 68  ? 0.0718 0.1109 0.0928 0.0256  0.0194  0.0445  68  VAL A O   
531  C  CB  . VAL A 68  ? 0.0619 0.1359 0.1305 0.0350  0.0022  0.0095  68  VAL A CB  
532  C  CG1 . VAL A 68  ? 0.0820 0.1366 0.1272 0.0392  -0.0044 0.0215  68  VAL A CG1 
533  C  CG2 . VAL A 68  ? 0.1023 0.1549 0.0854 0.0392  0.0139  0.0030  68  VAL A CG2 
534  N  N   . GLU A 69  ? 0.0914 0.1108 0.1174 0.0333  0.0026  0.0381  69  GLU A N   
535  C  CA  . GLU A 69  ? 0.0876 0.0807 0.1358 0.0108  0.0179  0.0532  69  GLU A CA  
536  C  C   . GLU A 69  ? 0.1208 0.0935 0.1152 0.0430  0.0081  0.0337  69  GLU A C   
537  O  O   . GLU A 69  ? 0.1380 0.1280 0.1341 0.0421  -0.0085 0.0219  69  GLU A O   
538  C  CB  . GLU A 69  ? 0.1142 0.1110 0.1941 0.0166  0.0722  0.0512  69  GLU A CB  
539  C  CG  . GLU A 69  ? 0.0653 0.2173 0.2227 -0.0100 0.0266  -0.0037 69  GLU A CG  
540  C  CD  . GLU A 69  ? 0.1181 0.2077 0.2241 0.0148  0.0293  0.0493  69  GLU A CD  
541  O  OE1 . GLU A 69  ? 0.1506 0.2494 0.2371 -0.0153 0.0372  0.0861  69  GLU A OE1 
542  O  OE2 . GLU A 69  ? 0.1056 0.2176 0.2873 0.0005  0.0827  0.0599  69  GLU A OE2 
543  N  N   . PHE A 70  ? 0.0530 0.0971 0.1283 0.0279  0.0212  0.0201  70  PHE A N   
544  C  CA  . PHE A 70  ? 0.0501 0.0876 0.1214 0.0270  0.0043  0.0420  70  PHE A CA  
545  C  C   . PHE A 70  ? 0.1064 0.0863 0.1336 0.0280  0.0031  0.0164  70  PHE A C   
546  O  O   . PHE A 70  ? 0.1050 0.1343 0.1958 0.0106  -0.0002 0.0335  70  PHE A O   
547  C  CB  . PHE A 70  ? 0.0675 0.1076 0.1022 0.0097  0.0091  0.0210  70  PHE A CB  
548  C  CG  . PHE A 70  ? 0.0498 0.1161 0.1092 0.0121  -0.0059 0.0254  70  PHE A CG  
549  C  CD1 . PHE A 70  ? 0.0907 0.1040 0.1040 0.0247  0.0159  0.0312  70  PHE A CD1 
550  C  CD2 . PHE A 70  ? 0.0575 0.1384 0.0953 -0.0081 -0.0032 0.0149  70  PHE A CD2 
551  C  CE1 . PHE A 70  ? 0.0836 0.1272 0.1383 -0.0020 0.0092  0.0237  70  PHE A CE1 
552  C  CE2 . PHE A 70  ? 0.0883 0.1319 0.1319 0.0055  0.0250  0.0449  70  PHE A CE2 
553  C  CZ  . PHE A 70  ? 0.0703 0.1452 0.1032 0.0156  0.0278  0.0161  70  PHE A CZ  
554  N  N   . ASP A 71  ? 0.1310 0.1179 0.1650 0.0389  -0.0100 0.0557  71  ASP A N   
555  C  CA  . ASP A 71  ? 0.1276 0.1091 0.1984 0.0194  0.0011  0.0630  71  ASP A CA  
556  C  C   . ASP A 71  ? 0.0961 0.0908 0.1984 0.0089  -0.0127 0.0175  71  ASP A C   
557  O  O   . ASP A 71  ? 0.1427 0.1621 0.2584 -0.0316 0.0146  0.0272  71  ASP A O   
558  C  CB  . ASP A 71  ? 0.1660 0.1210 0.2633 0.0145  -0.0521 0.0758  71  ASP A CB  
559  C  CG  . ASP A 71  ? 0.1847 0.1179 0.3549 0.0044  -0.0651 0.0427  71  ASP A CG  
560  O  OD1 . ASP A 71  ? 0.1619 0.1461 0.3579 0.0194  -0.0510 0.0581  71  ASP A OD1 
561  O  OD2 . ASP A 71  ? 0.2934 0.2149 0.5277 0.0457  -0.1976 0.0121  71  ASP A OD2 
562  N  N   . ASP A 72  ? 0.1077 0.1138 0.2091 0.0041  -0.0321 0.0251  72  ASP A N   
563  C  CA  . ASP A 72  ? 0.1364 0.1009 0.2090 0.0103  -0.0183 0.0299  72  ASP A CA  
564  C  C   . ASP A 72  ? 0.1365 0.1067 0.2922 0.0130  -0.0559 0.0047  72  ASP A C   
565  O  O   . ASP A 72  ? 0.1689 0.1432 0.2888 -0.0249 -0.0619 0.0275  72  ASP A O   
566  C  CB  . ASP A 72  ? 0.1229 0.1466 0.2451 0.0088  -0.0184 0.0423  72  ASP A CB  
567  C  CG  . ASP A 72  ? 0.1176 0.2330 0.2088 0.0178  0.0071  0.0719  72  ASP A CG  
568  O  OD1 . ASP A 72  ? 0.1537 0.2452 0.2305 -0.0027 0.0041  0.0943  72  ASP A OD1 
569  O  OD2 . ASP A 72  ? 0.1174 0.2405 0.2101 0.0034  0.0051  0.0609  72  ASP A OD2 
570  N  N   . SER A 73  ? 0.1517 0.1135 0.3298 -0.0010 -0.0305 0.0594  73  SER A N   
571  C  CA  . SER A 73  ? 0.1377 0.1207 0.3165 0.0269  -0.0744 0.0454  73  SER A CA  
572  C  C   . SER A 73  ? 0.1129 0.1353 0.3819 0.0033  -0.0722 0.0032  73  SER A C   
573  O  O   . SER A 73  ? 0.2044 0.1146 0.4134 -0.0237 -0.0894 0.0553  73  SER A O   
574  C  CB  . SER A 73  ? 0.1887 0.1887 0.3355 0.0058  -0.0527 0.0927  73  SER A CB  
575  O  OG  . SER A 73  ? 0.2245 0.1426 0.2947 0.0435  -0.0502 0.0539  73  SER A OG  
576  N  N   . GLN A 74  ? 0.1395 0.1511 0.3298 0.0110  -0.0566 0.0027  74  GLN A N   
577  C  CA  . GLN A 74  ? 0.1793 0.1666 0.2911 0.0584  -0.0433 -0.0135 74  GLN A CA  
578  C  C   . GLN A 74  ? 0.1452 0.1639 0.2533 0.0222  -0.0766 -0.0195 74  GLN A C   
579  O  O   . GLN A 74  ? 0.1544 0.1537 0.3269 0.0147  -0.0600 -0.0093 74  GLN A O   
580  C  CB  . GLN A 74  ? 0.2152 0.2388 0.3470 0.0858  -0.0769 0.0402  74  GLN A CB  
581  C  CG  . GLN A 74  ? 0.2432 0.2612 0.3682 -0.0012 -0.1312 0.0300  74  GLN A CG  
582  C  CD  . GLN A 74  ? 0.1815 0.3467 0.3392 -0.0785 -0.0807 0.0805  74  GLN A CD  
583  O  OE1 . GLN A 74  ? 0.2999 0.6185 0.4422 0.0027  0.0550  0.2140  74  GLN A OE1 
584  N  NE2 . GLN A 74  ? 0.2778 0.3006 0.3240 0.0010  -0.0685 0.0629  74  GLN A NE2 
585  N  N   . ASP A 75  ? 0.2005 0.2557 0.2974 0.0212  -0.0343 -0.0343 75  ASP A N   
586  C  CA  . ASP A 75  ? 0.2158 0.2118 0.3245 0.0076  -0.0586 -0.0546 75  ASP A CA  
587  C  C   . ASP A 75  ? 0.2009 0.2454 0.3783 0.0856  -0.1317 -0.0824 75  ASP A C   
588  O  O   . ASP A 75  ? 0.1966 0.4861 0.7350 0.1300  -0.1341 -0.0489 75  ASP A O   
589  C  CB  . ASP A 75  ? 0.3509 0.2505 0.3061 0.1472  -0.0427 -0.0085 75  ASP A CB  
590  C  CG  . ASP A 75  ? 0.4119 0.3157 0.2879 -0.0615 0.0966  -0.0537 75  ASP A CG  
591  O  OD1 . ASP A 75  ? 0.3705 0.5914 0.4121 -0.0194 -0.1359 -0.1868 75  ASP A OD1 
592  O  OD2 . ASP A 75  ? 0.5804 0.5386 0.3694 0.0687  0.1244  -0.1332 75  ASP A OD2 
593  N  N   . LYS A 76  ? 0.1251 0.1673 0.2870 0.0266  -0.0417 -0.0005 76  LYS A N   
594  C  CA  . LYS A 76  ? 0.1965 0.2292 0.2551 -0.0026 -0.0979 0.0135  76  LYS A CA  
595  C  C   . LYS A 76  ? 0.2461 0.3219 0.3439 0.2064  0.0130  0.1465  76  LYS A C   
596  O  O   . LYS A 76  ? 0.2934 0.5396 1.5661 -0.3336 0.0019  0.1463  76  LYS A O   
597  C  CB  . LYS A 76  ? 0.2855 0.2069 0.2496 -0.0223 -0.1067 0.0264  76  LYS A CB  
598  C  CG  . LYS A 76  ? 0.3919 0.2464 0.2366 0.0115  -0.0842 0.0465  76  LYS A CG  
599  C  CD  . LYS A 76  ? 0.3345 0.2052 0.2623 0.0053  -0.0264 0.0546  76  LYS A CD  
600  C  CE  . LYS A 76  ? 0.3683 0.2533 0.2949 0.0902  -0.0277 0.0363  76  LYS A CE  
601  N  NZ  . LYS A 76  ? 0.2161 0.2922 0.3510 0.0316  0.0671  0.0450  76  LYS A NZ  
602  N  N   . ALA A 77  ? 0.1231 0.1933 0.2609 0.0370  -0.0289 0.0334  77  ALA A N   
603  C  CA  . ALA A 77  ? 0.1113 0.1824 0.2019 0.0051  0.0006  -0.0038 77  ALA A CA  
604  C  C   . ALA A 77  ? 0.0370 0.1904 0.2119 -0.0217 0.0073  -0.0054 77  ALA A C   
605  O  O   . ALA A 77  ? 0.0314 0.2515 0.2332 -0.0170 0.0145  -0.0097 77  ALA A O   
606  C  CB  . ALA A 77  ? 0.1653 0.2710 0.1914 0.0666  -0.0159 -0.0319 77  ALA A CB  
607  N  N   . VAL A 78  ? 0.0417 0.1287 0.1890 -0.0035 -0.0131 0.0189  78  VAL A N   
608  C  CA  . VAL A 78  ? 0.0525 0.1366 0.1921 -0.0165 -0.0083 0.0190  78  VAL A CA  
609  C  C   . VAL A 78  ? 0.0282 0.1463 0.1671 -0.0282 0.0107  0.0040  78  VAL A C   
610  O  O   . VAL A 78  ? 0.0525 0.1706 0.2303 -0.0538 -0.0499 0.0380  78  VAL A O   
611  C  CB  . VAL A 78  ? 0.1146 0.1556 0.1998 0.0036  0.0241  0.0141  78  VAL A CB  
612  C  CG1 . VAL A 78  ? 0.1477 0.1477 0.2460 0.0165  0.0259  0.0303  78  VAL A CG1 
613  C  CG2 . VAL A 78  ? 0.1240 0.2497 0.2916 0.0173  0.0572  -0.0376 78  VAL A CG2 
614  N  N   . LEU A 79  ? 0.0278 0.1382 0.1522 -0.0048 0.0190  0.0105  79  LEU A N   
615  C  CA  . LEU A 79  ? 0.0392 0.1204 0.1803 -0.0152 0.0253  0.0066  79  LEU A CA  
616  C  C   . LEU A 79  ? 0.0655 0.1057 0.1699 -0.0368 0.0343  0.0176  79  LEU A C   
617  O  O   . LEU A 79  ? 0.0826 0.1264 0.1883 -0.0565 0.0392  -0.0132 79  LEU A O   
618  C  CB  . LEU A 79  ? 0.0073 0.1813 0.2404 -0.0108 0.0055  0.0403  79  LEU A CB  
619  C  CG  . LEU A 79  ? 0.0648 0.1912 0.2112 -0.0122 0.0034  0.0251  79  LEU A CG  
620  C  CD1 . LEU A 79  ? 0.0895 0.1634 0.3417 -0.0236 0.0589  0.0587  79  LEU A CD1 
621  C  CD2 . LEU A 79  ? 0.0729 0.1923 0.2212 0.0038  0.0294  0.0445  79  LEU A CD2 
622  N  N   A LYS A 80  ? 0.0572 0.1824 0.1711 -0.0298 0.0487  -0.0173 80  LYS A N   
623  N  N   B LYS A 80  ? 0.0419 0.1738 0.1965 -0.0454 0.0491  -0.0085 80  LYS A N   
624  C  CA  A LYS A 80  ? 0.0946 0.1377 0.1847 -0.0110 0.0532  -0.0114 80  LYS A CA  
625  C  CA  B LYS A 80  ? 0.0916 0.1581 0.1761 -0.0236 0.0350  0.0129  80  LYS A CA  
626  C  C   A LYS A 80  ? 0.0479 0.1800 0.1875 -0.0043 0.0595  -0.0076 80  LYS A C   
627  C  C   B LYS A 80  ? 0.0538 0.1752 0.1766 -0.0016 0.0472  0.0013  80  LYS A C   
628  O  O   A LYS A 80  ? 0.0803 0.1649 0.2156 -0.0430 0.0414  0.0012  80  LYS A O   
629  O  O   B LYS A 80  ? 0.0792 0.1689 0.2216 -0.0457 0.0406  0.0027  80  LYS A O   
630  C  CB  A LYS A 80  ? 0.1013 0.2041 0.2138 0.0282  0.0660  -0.0322 80  LYS A CB  
631  C  CB  B LYS A 80  ? 0.1262 0.1660 0.2837 -0.0068 0.0304  0.0315  80  LYS A CB  
632  C  CG  A LYS A 80  ? 0.1899 0.1919 0.2259 0.0121  0.0593  -0.0443 80  LYS A CG  
633  C  CG  B LYS A 80  ? 0.0607 0.2515 0.3161 0.0149  0.1199  0.0539  80  LYS A CG  
634  C  CD  A LYS A 80  ? 0.1393 0.2503 0.3621 0.0080  0.0536  -0.0596 80  LYS A CD  
635  C  CD  B LYS A 80  ? 0.1851 0.3011 0.4611 0.0957  0.1216  0.0333  80  LYS A CD  
636  N  N   . GLY A 81  ? 0.1011 0.1975 0.1757 -0.0042 0.0875  0.0201  81  GLY A N   
637  C  CA  . GLY A 81  ? 0.0838 0.2098 0.1897 0.0125  0.0856  0.0407  81  GLY A CA  
638  C  C   . GLY A 81  ? 0.0686 0.1524 0.2249 -0.0182 0.0895  0.0318  81  GLY A C   
639  O  O   . GLY A 81  ? 0.0669 0.1892 0.1935 -0.0372 0.0663  0.0071  81  GLY A O   
640  N  N   . GLY A 82  ? 0.0757 0.1531 0.2661 -0.0298 0.0686  0.0413  82  GLY A N   
641  C  CA  . GLY A 82  ? 0.1606 0.1770 0.3485 0.0080  0.0670  0.0774  82  GLY A CA  
642  C  C   . GLY A 82  ? 0.1098 0.2289 0.2932 0.0658  0.1057  0.0399  82  GLY A C   
643  O  O   . GLY A 82  ? 0.2041 0.3334 0.2972 0.1297  0.1326  0.0307  82  GLY A O   
644  N  N   . PRO A 83  ? 0.0943 0.1732 0.2625 0.0357  0.0853  0.0232  83  PRO A N   
645  C  CA  . PRO A 83  ? 0.1707 0.1811 0.1918 0.0739  0.0556  -0.0044 83  PRO A CA  
646  C  C   . PRO A 83  ? 0.1470 0.1881 0.2511 0.0536  0.0241  -0.0187 83  PRO A C   
647  O  O   . PRO A 83  ? 0.1865 0.3222 0.2669 0.0440  -0.0334 -0.0270 83  PRO A O   
648  C  CB  . PRO A 83  ? 0.1869 0.2274 0.2107 0.1061  0.0300  0.0386  83  PRO A CB  
649  C  CG  . PRO A 83  ? 0.0906 0.1799 0.2242 0.0878  0.0320  0.0046  83  PRO A CG  
650  C  CD  . PRO A 83  ? 0.0731 0.2115 0.2623 0.0515  0.0829  0.0177  83  PRO A CD  
651  N  N   . LEU A 84  ? 0.1018 0.1075 0.2032 0.0374  0.0565  -0.0316 84  LEU A N   
652  C  CA  . LEU A 84  ? 0.1030 0.1073 0.1835 0.0274  0.0488  -0.0434 84  LEU A CA  
653  C  C   . LEU A 84  ? 0.1160 0.1301 0.3208 0.0441  0.0455  -0.0840 84  LEU A C   
654  O  O   . LEU A 84  ? 0.1517 0.2168 0.3427 0.0723  0.0992  -0.1035 84  LEU A O   
655  C  CB  . LEU A 84  ? 0.0498 0.1353 0.1835 0.0321  0.0367  -0.0255 84  LEU A CB  
656  C  CG  . LEU A 84  ? 0.0490 0.1206 0.2080 0.0318  0.0497  -0.0120 84  LEU A CG  
657  C  CD1 . LEU A 84  ? 0.0763 0.1732 0.1912 0.0124  0.0483  -0.0011 84  LEU A CD1 
658  C  CD2 . LEU A 84  ? 0.0496 0.1423 0.2382 0.0031  0.0872  -0.0241 84  LEU A CD2 
659  N  N   . ASP A 85  ? 0.1606 0.1458 0.3359 0.0219  0.0541  -0.1017 85  ASP A N   
660  C  CA  . ASP A 85  ? 0.2174 0.1059 0.5015 -0.0239 0.0904  -0.0968 85  ASP A CA  
661  C  C   . ASP A 85  ? 0.1637 0.1669 0.5073 -0.0785 0.1137  -0.0649 85  ASP A C   
662  O  O   . ASP A 85  ? 0.2496 0.3550 0.4900 -0.0322 0.1694  -0.1479 85  ASP A O   
663  C  CB  . ASP A 85  ? 0.3953 0.3017 0.4878 -0.0419 0.0576  -0.1763 85  ASP A CB  
664  C  CG  . ASP A 85  ? 0.5391 0.2658 0.6494 0.0061  -0.0185 -0.1470 85  ASP A CG  
665  O  OD1 . ASP A 85  ? 0.5732 0.5256 0.7205 -0.0999 0.1437  -0.3115 85  ASP A OD1 
666  O  OD2 . ASP A 85  ? 0.4462 0.6319 1.1032 -0.0851 -0.0624 -0.2439 85  ASP A OD2 
667  N  N   . GLY A 86  ? 0.2672 0.3923 0.5264 0.0234  0.1092  0.0046  86  GLY A N   
668  C  CA  . GLY A 86  ? 0.4461 0.2814 0.3940 -0.1504 0.0888  -0.1230 86  GLY A CA  
669  C  C   . GLY A 86  ? 0.2964 0.1890 0.2913 -0.0969 0.1251  -0.0385 86  GLY A C   
670  O  O   . GLY A 86  ? 0.4299 0.2130 0.2985 -0.1609 0.1631  -0.0599 86  GLY A O   
671  N  N   . THR A 87  ? 0.1235 0.1972 0.2396 -0.0207 0.1038  -0.0653 87  THR A N   
672  C  CA  . THR A 87  ? 0.1138 0.1979 0.2255 -0.0153 0.1133  -0.0197 87  THR A CA  
673  C  C   . THR A 87  ? 0.0507 0.1147 0.2253 -0.0234 0.0664  -0.0152 87  THR A C   
674  O  O   . THR A 87  ? 0.0745 0.0836 0.2521 -0.0208 0.0908  -0.0227 87  THR A O   
675  C  CB  . THR A 87  ? 0.1526 0.2979 0.3114 0.0851  0.0354  -0.0523 87  THR A CB  
676  O  OG1 . THR A 87  ? 0.1754 0.3610 0.4264 0.0595  0.0998  -0.1197 87  THR A OG1 
677  C  CG2 . THR A 87  ? 0.1267 0.2853 0.3270 0.0779  0.0143  -0.0163 87  THR A CG2 
678  N  N   . TYR A 88  ? 0.0213 0.1185 0.1817 0.0013  0.0507  -0.0156 88  TYR A N   
679  C  CA  . TYR A 88  ? 0.0172 0.0946 0.1627 -0.0022 0.0410  -0.0244 88  TYR A CA  
680  C  C   . TYR A 88  ? 0.0091 0.0939 0.1558 -0.0089 0.0164  0.0018  88  TYR A C   
681  O  O   . TYR A 88  ? 0.0415 0.1465 0.1774 -0.0588 0.0172  0.0076  88  TYR A O   
682  C  CB  . TYR A 88  ? 0.0493 0.0905 0.1735 -0.0047 0.0204  -0.0186 88  TYR A CB  
683  C  CG  . TYR A 88  ? 0.0292 0.0732 0.1398 0.0073  0.0387  -0.0228 88  TYR A CG  
684  C  CD1 . TYR A 88  ? 0.0387 0.0987 0.1465 -0.0050 0.0501  -0.0328 88  TYR A CD1 
685  C  CD2 . TYR A 88  ? 0.0337 0.0779 0.1560 0.0238  0.0230  -0.0069 88  TYR A CD2 
686  C  CE1 . TYR A 88  ? 0.0303 0.1656 0.1535 -0.0206 0.0593  -0.0459 88  TYR A CE1 
687  C  CE2 . TYR A 88  ? 0.0410 0.0838 0.1093 0.0067  0.0585  -0.0035 88  TYR A CE2 
688  C  CZ  . TYR A 88  ? 0.0329 0.0807 0.1249 -0.0005 0.0518  -0.0367 88  TYR A CZ  
689  O  OH  . TYR A 88  ? 0.0689 0.1420 0.1276 -0.0129 0.0469  -0.0390 88  TYR A OH  
690  N  N   . ARG A 89  ? 0.0236 0.0900 0.1249 0.0141  0.0276  -0.0099 89  ARG A N   
691  C  CA  . ARG A 89  ? 0.0366 0.0594 0.1459 -0.0046 0.0069  -0.0039 89  ARG A CA  
692  C  C   . ARG A 89  ? 0.0147 0.0617 0.1177 0.0001  0.0004  0.0079  89  ARG A C   
693  O  O   . ARG A 89  ? 0.0148 0.0788 0.1330 0.0031  0.0010  0.0026  89  ARG A O   
694  C  CB  . ARG A 89  ? 0.0700 0.0531 0.2240 -0.0173 0.0055  0.0151  89  ARG A CB  
695  C  CG  . ARG A 89  ? 0.1032 0.1405 0.3158 0.0500  -0.0348 0.0454  89  ARG A CG  
696  C  CD  . ARG A 89  ? 0.1246 0.0908 0.4677 -0.0019 -0.0785 0.1404  89  ARG A CD  
697  N  NE  . ARG A 89  ? 0.1941 0.2147 0.3456 0.0130  -0.1278 0.0774  89  ARG A NE  
698  C  CZ  . ARG A 89  ? 0.2534 0.1824 0.3456 0.0447  -0.0888 0.0662  89  ARG A CZ  
699  N  NH1 . ARG A 89  ? 0.2544 0.1678 0.2397 0.0339  -0.0732 0.0149  89  ARG A NH1 
700  N  NH2 . ARG A 89  ? 0.1991 0.2655 0.4676 0.0089  -0.0856 -0.0369 89  ARG A NH2 
701  N  N   . LEU A 90  ? 0.0330 0.0788 0.1197 0.0002  0.0048  -0.0150 90  LEU A N   
702  C  CA  . LEU A 90  ? 0.0513 0.0732 0.1164 -0.0062 0.0142  -0.0130 90  LEU A CA  
703  C  C   . LEU A 90  ? 0.0381 0.0840 0.1214 0.0067  -0.0017 0.0165  90  LEU A C   
704  O  O   . LEU A 90  ? 0.0660 0.1501 0.1365 0.0326  0.0079  0.0440  90  LEU A O   
705  C  CB  . LEU A 90  ? 0.0416 0.0897 0.1141 -0.0009 0.0004  -0.0079 90  LEU A CB  
706  C  CG  . LEU A 90  ? 0.0788 0.0794 0.1075 -0.0010 -0.0099 -0.0043 90  LEU A CG  
707  C  CD1 . LEU A 90  ? 0.0837 0.1136 0.1025 0.0053  -0.0076 0.0069  90  LEU A CD1 
708  C  CD2 . LEU A 90  ? 0.0759 0.1502 0.1150 -0.0127 -0.0183 0.0034  90  LEU A CD2 
709  N  N   . ILE A 91  ? 0.0480 0.0926 0.1160 0.0218  0.0290  0.0210  91  ILE A N   
710  C  CA  . ILE A 91  ? 0.0752 0.0715 0.0973 0.0121  0.0223  0.0151  91  ILE A CA  
711  C  C   . ILE A 91  ? 0.0401 0.0562 0.0968 0.0025  0.0122  0.0199  91  ILE A C   
712  O  O   . ILE A 91  ? 0.0705 0.0710 0.0906 0.0088  -0.0029 0.0149  91  ILE A O   
713  C  CB  . ILE A 91  ? 0.0876 0.0700 0.1307 0.0070  0.0216  0.0051  91  ILE A CB  
714  C  CG1 . ILE A 91  ? 0.1032 0.1366 0.1307 -0.0538 0.0198  0.0127  91  ILE A CG1 
715  C  CG2 . ILE A 91  ? 0.0903 0.1089 0.1214 0.0008  0.0083  0.0068  91  ILE A CG2 
716  C  CD1 . ILE A 91  ? 0.1965 0.1703 0.1777 -0.0119 -0.0236 0.0151  91  ILE A CD1 
717  N  N   . GLN A 92  ? 0.0433 0.0562 0.1080 0.0110  0.0060  0.0201  92  GLN A N   
718  C  CA  . GLN A 92  ? 0.0513 0.0588 0.1113 0.0035  0.0309  0.0244  92  GLN A CA  
719  C  C   . GLN A 92  ? 0.0633 0.0716 0.0772 -0.0032 -0.0025 0.0284  92  GLN A C   
720  O  O   . GLN A 92  ? 0.0632 0.0745 0.0786 0.0182  0.0194  0.0163  92  GLN A O   
721  C  CB  . GLN A 92  ? 0.0348 0.0914 0.1076 -0.0012 0.0076  0.0192  92  GLN A CB  
722  C  CG  . GLN A 92  ? 0.0575 0.1238 0.1344 0.0231  -0.0167 0.0337  92  GLN A CG  
723  C  CD  . GLN A 92  ? 0.1104 0.0930 0.1132 0.0042  0.0027  0.0159  92  GLN A CD  
724  O  OE1 . GLN A 92  ? 0.2198 0.0743 0.2174 0.0006  -0.0763 0.0379  92  GLN A OE1 
725  N  NE2 . GLN A 92  ? 0.0436 0.2906 0.2105 0.0263  0.0168  -0.1230 92  GLN A NE2 
726  N  N   . PHE A 93  ? 0.0269 0.0479 0.0987 0.0077  0.0013  0.0257  93  PHE A N   
727  C  CA  . PHE A 93  ? 0.0178 0.0363 0.0982 0.0049  0.0094  0.0152  93  PHE A CA  
728  C  C   . PHE A 93  ? 0.0097 0.0485 0.0693 -0.0067 0.0092  0.0142  93  PHE A C   
729  O  O   . PHE A 93  ? 0.0528 0.0961 0.0613 0.0065  0.0041  0.0149  93  PHE A O   
730  C  CB  . PHE A 93  ? 0.0299 0.0863 0.0885 -0.0225 -0.0036 0.0142  93  PHE A CB  
731  C  CG  . PHE A 93  ? 0.0071 0.0666 0.0881 -0.0057 0.0036  0.0073  93  PHE A CG  
732  C  CD1 . PHE A 93  ? 0.0480 0.0863 0.0838 -0.0078 0.0018  -0.0142 93  PHE A CD1 
733  C  CD2 . PHE A 93  ? 0.0265 0.1021 0.0811 0.0054  -0.0097 0.0273  93  PHE A CD2 
734  C  CE1 . PHE A 93  ? 0.0218 0.1086 0.1028 -0.0124 -0.0084 -0.0170 93  PHE A CE1 
735  C  CE2 . PHE A 93  ? 0.0493 0.1129 0.0988 -0.0205 -0.0026 0.0033  93  PHE A CE2 
736  C  CZ  . PHE A 93  ? 0.0549 0.1221 0.0917 -0.0013 -0.0156 0.0106  93  PHE A CZ  
737  N  N   . HIS A 94  ? 0.0172 0.0513 0.0955 0.0102  -0.0054 0.0069  94  HIS A N   
738  C  CA  . HIS A 94  ? 0.0072 0.0540 0.0888 -0.0031 0.0052  0.0027  94  HIS A CA  
739  C  C   . HIS A 94  ? 0.0081 0.0639 0.0598 0.0010  0.0060  0.0018  94  HIS A C   
740  O  O   . HIS A 94  ? 0.0191 0.0700 0.0635 0.0026  0.0109  0.0159  94  HIS A O   
741  C  CB  . HIS A 94  ? 0.0174 0.0794 0.0853 -0.0212 -0.0086 -0.0148 94  HIS A CB  
742  C  CG  . HIS A 94  ? 0.0100 0.0813 0.0709 -0.0122 0.0118  -0.0088 94  HIS A CG  
743  N  ND1 . HIS A 94  ? 0.0097 0.0817 0.0725 -0.0118 0.0111  -0.0078 94  HIS A ND1 
744  C  CD2 . HIS A 94  ? 0.0137 0.1034 0.0702 -0.0159 0.0170  0.0033  94  HIS A CD2 
745  C  CE1 . HIS A 94  ? 0.0071 0.0819 0.0814 -0.0042 0.0068  -0.0032 94  HIS A CE1 
746  N  NE2 . HIS A 94  ? 0.0065 0.0827 0.0803 0.0003  -0.0040 0.0022  94  HIS A NE2 
747  N  N   . PHE A 95  ? 0.0118 0.0702 0.0809 0.0152  0.0044  0.0075  95  PHE A N   
748  C  CA  . PHE A 95  ? 0.0102 0.0584 0.0757 0.0030  0.0027  -0.0076 95  PHE A CA  
749  C  C   . PHE A 95  ? 0.0075 0.0698 0.0659 -0.0024 0.0083  -0.0045 95  PHE A C   
750  O  O   . PHE A 95  ? 0.0359 0.0851 0.0810 -0.0019 0.0313  0.0225  95  PHE A O   
751  C  CB  . PHE A 95  ? 0.0238 0.0741 0.1005 -0.0002 -0.0110 -0.0196 95  PHE A CB  
752  C  CG  . PHE A 95  ? 0.0270 0.0797 0.0964 -0.0047 -0.0215 -0.0089 95  PHE A CG  
753  C  CD1 . PHE A 95  ? 0.0562 0.1034 0.1068 0.0251  -0.0181 -0.0030 95  PHE A CD1 
754  C  CD2 . PHE A 95  ? 0.0270 0.1057 0.1206 -0.0250 -0.0095 -0.0328 95  PHE A CD2 
755  C  CE1 . PHE A 95  ? 0.0527 0.1347 0.1005 0.0280  -0.0144 -0.0215 95  PHE A CE1 
756  C  CE2 . PHE A 95  ? 0.0398 0.1065 0.1208 -0.0111 -0.0212 -0.0350 95  PHE A CE2 
757  C  CZ  . PHE A 95  ? 0.0646 0.1304 0.1134 0.0263  0.0047  -0.0237 95  PHE A CZ  
758  N  N   . HIS A 96  ? 0.0104 0.0722 0.0635 0.0127  0.0018  -0.0008 96  HIS A N   
759  C  CA  . HIS A 96  ? 0.0151 0.0540 0.0643 0.0126  0.0080  -0.0071 96  HIS A CA  
760  C  C   . HIS A 96  ? 0.0137 0.0699 0.0783 -0.0086 0.0208  0.0013  96  HIS A C   
761  O  O   . HIS A 96  ? 0.0147 0.0751 0.0968 -0.0046 0.0269  -0.0001 96  HIS A O   
762  C  CB  . HIS A 96  ? 0.0245 0.0558 0.0703 0.0055  0.0033  0.0031  96  HIS A CB  
763  C  CG  . HIS A 96  ? 0.0086 0.0529 0.0851 0.0061  0.0109  0.0011  96  HIS A CG  
764  N  ND1 . HIS A 96  ? 0.0110 0.0621 0.1154 -0.0082 0.0144  -0.0163 96  HIS A ND1 
765  C  CD2 . HIS A 96  ? 0.0072 0.0493 0.0989 0.0045  0.0052  -0.0085 96  HIS A CD2 
766  C  CE1 . HIS A 96  ? 0.0259 0.0811 0.0890 0.0013  0.0296  -0.0509 96  HIS A CE1 
767  N  NE2 . HIS A 96  ? 0.0111 0.0529 0.0788 -0.0006 0.0186  -0.0106 96  HIS A NE2 
768  N  N   . TRP A 97  ? 0.0278 0.0576 0.0797 -0.0065 0.0167  -0.0046 97  TRP A N   
769  C  CA  . TRP A 97  ? 0.0203 0.0555 0.0761 0.0058  0.0133  -0.0173 97  TRP A CA  
770  C  C   . TRP A 97  ? 0.0148 0.0521 0.0768 0.0013  0.0187  -0.0069 97  TRP A C   
771  O  O   . TRP A 97  ? 0.0154 0.0662 0.0988 -0.0005 0.0272  0.0027  97  TRP A O   
772  C  CB  . TRP A 97  ? 0.0475 0.0748 0.0455 0.0031  0.0247  -0.0095 97  TRP A CB  
773  C  CG  . TRP A 97  ? 0.0363 0.0653 0.0503 -0.0141 0.0234  -0.0158 97  TRP A CG  
774  C  CD1 . TRP A 97  ? 0.0425 0.0991 0.0533 -0.0201 0.0385  -0.0259 97  TRP A CD1 
775  C  CD2 . TRP A 97  ? 0.0354 0.0687 0.0689 -0.0121 0.0273  -0.0103 97  TRP A CD2 
776  N  NE1 . TRP A 97  ? 0.0757 0.0773 0.0597 -0.0025 0.0297  -0.0087 97  TRP A NE1 
777  C  CE2 . TRP A 97  ? 0.0326 0.0792 0.0741 -0.0076 0.0309  -0.0095 97  TRP A CE2 
778  C  CE3 . TRP A 97  ? 0.0357 0.0677 0.0700 -0.0089 0.0208  -0.0102 97  TRP A CE3 
779  C  CZ2 . TRP A 97  ? 0.0621 0.0836 0.0948 -0.0030 0.0187  0.0057  97  TRP A CZ2 
780  C  CZ3 . TRP A 97  ? 0.0361 0.0818 0.0858 -0.0027 0.0290  0.0069  97  TRP A CZ3 
781  C  CH2 . TRP A 97  ? 0.0673 0.0876 0.0886 -0.0124 0.0414  0.0022  97  TRP A CH2 
782  N  N   . GLY A 98  ? 0.0447 0.0477 0.0822 0.0030  0.0167  -0.0043 98  GLY A N   
783  C  CA  . GLY A 98  ? 0.0600 0.0581 0.1174 0.0179  0.0250  -0.0189 98  GLY A CA  
784  C  C   . GLY A 98  ? 0.0628 0.0685 0.1034 0.0015  0.0373  -0.0103 98  GLY A C   
785  O  O   . GLY A 98  ? 0.0917 0.0865 0.1147 0.0076  0.0325  -0.0215 98  GLY A O   
786  N  N   . SER A 99  ? 0.0709 0.1081 0.1208 0.0239  0.0573  -0.0174 99  SER A N   
787  C  CA  . SER A 99  ? 0.0894 0.0978 0.1426 0.0229  0.0491  -0.0330 99  SER A CA  
788  C  C   . SER A 99  ? 0.1167 0.0845 0.1395 0.0201  0.0276  -0.0249 99  SER A C   
789  O  O   . SER A 99  ? 0.1520 0.1405 0.1656 -0.0201 0.0313  -0.0435 99  SER A O   
790  C  CB  . SER A 99  ? 0.1086 0.1344 0.1190 0.0533  0.0373  -0.0696 99  SER A CB  
791  O  OG  . SER A 99  ? 0.1077 0.1108 0.1700 0.0071  0.0378  -0.0094 99  SER A OG  
792  N  N   . LEU A 100 ? 0.0727 0.0903 0.1632 -0.0094 0.0310  -0.0111 100 LEU A N   
793  C  CA  . LEU A 100 ? 0.0793 0.0704 0.2314 -0.0071 0.0445  -0.0257 100 LEU A CA  
794  C  C   . LEU A 100 ? 0.1117 0.0809 0.1940 0.0020  0.0542  -0.0122 100 LEU A C   
795  O  O   . LEU A 100 ? 0.1215 0.0943 0.1761 -0.0003 0.0460  -0.0230 100 LEU A O   
796  C  CB  . LEU A 100 ? 0.1217 0.1501 0.2471 0.0449  0.0234  -0.0117 100 LEU A CB  
797  C  CG  . LEU A 100 ? 0.1864 0.1588 0.2336 0.0615  0.0633  -0.0167 100 LEU A CG  
798  C  CD1 . LEU A 100 ? 0.2748 0.3707 0.3299 0.1865  0.0690  0.0222  100 LEU A CD1 
799  C  CD2 . LEU A 100 ? 0.2417 0.2246 0.2316 -0.0107 0.0442  -0.0380 100 LEU A CD2 
800  N  N   . ASP A 101 ? 0.0804 0.1142 0.2447 0.0122  0.0394  -0.0088 101 ASP A N   
801  C  CA  . ASP A 101 ? 0.1037 0.0774 0.2253 -0.0036 0.0675  0.0044  101 ASP A CA  
802  C  C   . ASP A 101 ? 0.1667 0.1002 0.2064 -0.0116 0.0871  0.0201  101 ASP A C   
803  O  O   . ASP A 101 ? 0.2173 0.1056 0.2361 0.0326  0.0700  0.0201  101 ASP A O   
804  C  CB  . ASP A 101 ? 0.0973 0.1154 0.2618 -0.0218 0.0655  0.0356  101 ASP A CB  
805  C  CG  . ASP A 101 ? 0.1720 0.1025 0.3126 -0.0478 0.0688  -0.0496 101 ASP A CG  
806  O  OD1 . ASP A 101 ? 0.1650 0.1418 0.2982 -0.0543 0.0505  -0.0239 101 ASP A OD1 
807  O  OD2 . ASP A 101 ? 0.2989 0.2020 0.3194 -0.1737 0.0798  -0.0410 101 ASP A OD2 
808  N  N   . GLY A 102 ? 0.1826 0.1077 0.2037 -0.0516 0.0278  0.0182  102 GLY A N   
809  C  CA  . GLY A 102 ? 0.2004 0.1018 0.2208 -0.0258 0.0413  0.0241  102 GLY A CA  
810  C  C   . GLY A 102 ? 0.1384 0.1147 0.1782 -0.0159 0.0529  0.0337  102 GLY A C   
811  O  O   . GLY A 102 ? 0.2039 0.1283 0.1792 -0.0207 0.0471  0.0211  102 GLY A O   
812  N  N   . GLN A 103 ? 0.0959 0.0788 0.1414 -0.0083 0.0617  -0.0048 103 GLN A N   
813  C  CA  . GLN A 103 ? 0.0952 0.0795 0.1224 0.0009  0.0351  0.0006  103 GLN A CA  
814  C  C   . GLN A 103 ? 0.0591 0.0833 0.0937 0.0015  0.0421  -0.0091 103 GLN A C   
815  O  O   . GLN A 103 ? 0.0655 0.0944 0.1147 0.0017  0.0218  -0.0154 103 GLN A O   
816  C  CB  . GLN A 103 ? 0.1077 0.1025 0.1174 0.0269  0.0463  -0.0178 103 GLN A CB  
817  C  CG  . GLN A 103 ? 0.0881 0.1282 0.1170 0.0461  0.0533  0.0130  103 GLN A CG  
818  C  CD  . GLN A 103 ? 0.1095 0.1486 0.1905 0.0722  0.0792  0.0686  103 GLN A CD  
819  O  OE1 . GLN A 103 ? 0.1799 0.1598 0.2645 0.0656  0.0651  0.0864  103 GLN A OE1 
820  N  NE2 . GLN A 103 ? 0.0838 0.1455 0.1932 0.0314  0.0518  0.0277  103 GLN A NE2 
821  N  N   . GLY A 104 ? 0.0497 0.0741 0.1018 0.0046  0.0387  0.0011  104 GLY A N   
822  C  CA  . GLY A 104 ? 0.0415 0.0662 0.0980 -0.0009 0.0286  -0.0013 104 GLY A CA  
823  C  C   . GLY A 104 ? 0.0312 0.0715 0.0829 -0.0044 0.0252  -0.0001 104 GLY A C   
824  O  O   . GLY A 104 ? 0.0323 0.0847 0.0960 -0.0111 0.0231  0.0036  104 GLY A O   
825  N  N   . SER A 105 ? 0.0221 0.0794 0.0815 0.0067  0.0233  0.0059  105 SER A N   
826  C  CA  . SER A 105 ? 0.0181 0.0777 0.1179 -0.0031 0.0206  -0.0149 105 SER A CA  
827  C  C   . SER A 105 ? 0.0401 0.0466 0.0891 -0.0012 0.0065  0.0103  105 SER A C   
828  O  O   . SER A 105 ? 0.0340 0.0840 0.1219 0.0085  0.0013  -0.0042 105 SER A O   
829  C  CB  . SER A 105 ? 0.0191 0.0892 0.1174 0.0039  0.0156  0.0147  105 SER A CB  
830  O  OG  . SER A 105 ? 0.0294 0.0660 0.1229 -0.0046 0.0190  0.0059  105 SER A OG  
831  N  N   . GLU A 106 ? 0.0224 0.0560 0.0813 -0.0116 0.0111  -0.0033 106 GLU A N   
832  C  CA  . GLU A 106 ? 0.0357 0.0697 0.0715 -0.0198 0.0126  -0.0115 106 GLU A CA  
833  C  C   . GLU A 106 ? 0.0155 0.0534 0.0838 0.0000  0.0265  0.0040  106 GLU A C   
834  O  O   . GLU A 106 ? 0.0293 0.0874 0.0912 -0.0004 0.0030  0.0073  106 GLU A O   
835  C  CB  . GLU A 106 ? 0.0533 0.0754 0.0698 -0.0077 0.0254  -0.0100 106 GLU A CB  
836  C  CG  . GLU A 106 ? 0.0820 0.0732 0.0749 -0.0019 0.0428  -0.0189 106 GLU A CG  
837  C  CD  . GLU A 106 ? 0.0314 0.0982 0.1028 -0.0064 0.0374  -0.0156 106 GLU A CD  
838  O  OE1 . GLU A 106 ? 0.0128 0.1021 0.1353 0.0065  0.0178  -0.0108 106 GLU A OE1 
839  O  OE2 . GLU A 106 ? 0.0172 0.1438 0.1344 0.0244  0.0261  0.0052  106 GLU A OE2 
840  N  N   . HIS A 107 ? 0.0205 0.0734 0.0765 0.0000  0.0306  -0.0094 107 HIS A N   
841  C  CA  . HIS A 107 ? 0.0206 0.0820 0.0798 -0.0042 0.0324  -0.0136 107 HIS A CA  
842  C  C   . HIS A 107 ? 0.0238 0.0782 0.0867 0.0013  0.0010  0.0001  107 HIS A C   
843  O  O   . HIS A 107 ? 0.0251 0.0754 0.0844 -0.0111 0.0077  0.0129  107 HIS A O   
844  C  CB  . HIS A 107 ? 0.0215 0.0828 0.0812 0.0095  0.0176  -0.0137 107 HIS A CB  
845  C  CG  . HIS A 107 ? 0.0227 0.0818 0.0682 0.0037  0.0315  -0.0039 107 HIS A CG  
846  N  ND1 . HIS A 107 ? 0.0247 0.0770 0.0869 0.0116  0.0102  0.0040  107 HIS A ND1 
847  C  CD2 . HIS A 107 ? 0.0154 0.0800 0.0950 0.0112  0.0223  -0.0170 107 HIS A CD2 
848  C  CE1 . HIS A 107 ? 0.0442 0.0795 0.0937 0.0060  0.0070  0.0003  107 HIS A CE1 
849  N  NE2 . HIS A 107 ? 0.0321 0.0856 0.1003 0.0149  0.0104  0.0089  107 HIS A NE2 
850  N  N   . THR A 108 ? 0.0484 0.0714 0.0946 -0.0118 0.0162  0.0102  108 THR A N   
851  C  CA  . THR A 108 ? 0.0491 0.0693 0.0860 0.0044  0.0190  0.0334  108 THR A CA  
852  C  C   . THR A 108 ? 0.0431 0.0966 0.0791 0.0036  0.0086  0.0185  108 THR A C   
853  O  O   . THR A 108 ? 0.0450 0.1073 0.0895 -0.0036 0.0178  0.0084  108 THR A O   
854  C  CB  . THR A 108 ? 0.0633 0.1195 0.0853 0.0297  -0.0016 0.0069  108 THR A CB  
855  O  OG1 . THR A 108 ? 0.0529 0.1093 0.1089 0.0036  0.0003  0.0087  108 THR A OG1 
856  C  CG2 . THR A 108 ? 0.0651 0.1272 0.0908 0.0124  0.0089  -0.0034 108 THR A CG2 
857  N  N   . VAL A 109 ? 0.0675 0.1047 0.1049 -0.0162 0.0170  0.0300  109 VAL A N   
858  C  CA  . VAL A 109 ? 0.0576 0.1602 0.1269 -0.0064 0.0190  0.0447  109 VAL A CA  
859  C  C   . VAL A 109 ? 0.0973 0.1250 0.1316 -0.0244 0.0212  0.0179  109 VAL A C   
860  O  O   . VAL A 109 ? 0.1014 0.1343 0.1509 -0.0362 0.0055  0.0087  109 VAL A O   
861  C  CB  . VAL A 109 ? 0.0560 0.1659 0.1660 -0.0011 0.0119  0.0724  109 VAL A CB  
862  C  CG1 . VAL A 109 ? 0.0879 0.1677 0.1969 -0.0044 0.0401  0.0753  109 VAL A CG1 
863  C  CG2 . VAL A 109 ? 0.0907 0.1369 0.1637 0.0158  0.0190  0.0473  109 VAL A CG2 
864  N  N   . ASP A 110 ? 0.0844 0.1264 0.1249 -0.0060 0.0253  0.0352  110 ASP A N   
865  C  CA  . ASP A 110 ? 0.1298 0.1077 0.1540 0.0023  0.0472  0.0325  110 ASP A CA  
866  C  C   . ASP A 110 ? 0.1315 0.1261 0.1303 0.0130  0.0369  0.0282  110 ASP A C   
867  O  O   . ASP A 110 ? 0.1666 0.1197 0.1533 0.0052  0.0171  0.0495  110 ASP A O   
868  C  CB  . ASP A 110 ? 0.1574 0.1594 0.1849 -0.0157 0.0846  0.0532  110 ASP A CB  
869  C  CG  . ASP A 110 ? 0.2151 0.1443 0.1631 0.0236  0.0682  0.0693  110 ASP A CG  
870  O  OD1 . ASP A 110 ? 0.2091 0.1757 0.1973 0.0147  0.0746  0.0433  110 ASP A OD1 
871  O  OD2 . ASP A 110 ? 0.2328 0.2665 0.3003 -0.0512 0.1129  0.0861  110 ASP A OD2 
872  N  N   . LYS A 111 ? 0.0876 0.1341 0.1073 0.0206  0.0157  0.0236  111 LYS A N   
873  C  CA  . LYS A 111 ? 0.0953 0.1262 0.1231 0.0390  0.0097  -0.0022 111 LYS A CA  
874  C  C   . LYS A 111 ? 0.1379 0.1624 0.1246 -0.0084 0.0073  0.0118  111 LYS A C   
875  O  O   . LYS A 111 ? 0.1466 0.1544 0.1725 0.0043  0.0245  -0.0114 111 LYS A O   
876  C  CB  . LYS A 111 ? 0.1721 0.1657 0.1480 0.0728  -0.0053 0.0205  111 LYS A CB  
877  C  CG  . LYS A 111 ? 0.2583 0.1912 0.1826 0.0719  -0.0532 0.0118  111 LYS A CG  
878  C  CD  . LYS A 111 ? 0.2529 0.2921 0.3316 0.0351  -0.0710 -0.0541 111 LYS A CD  
879  C  CE  . LYS A 111 ? 0.3172 0.4896 0.2619 0.1380  -0.0681 -0.0551 111 LYS A CE  
880  N  NZ  . LYS A 111 ? 0.3424 0.5917 0.4849 0.1698  -0.1720 0.0297  111 LYS A NZ  
881  N  N   . LYS A 112 ? 0.1235 0.1014 0.1228 0.0194  0.0223  0.0109  112 LYS A N   
882  C  CA  . LYS A 112 ? 0.1515 0.1377 0.1113 -0.0078 0.0345  0.0100  112 LYS A CA  
883  C  C   . LYS A 112 ? 0.0930 0.1063 0.1290 0.0269  0.0122  0.0127  112 LYS A C   
884  O  O   . LYS A 112 ? 0.0854 0.1014 0.1181 0.0044  0.0305  -0.0068 112 LYS A O   
885  C  CB  . LYS A 112 ? 0.1653 0.2034 0.1562 -0.0613 0.0274  0.0479  112 LYS A CB  
886  C  CG  . LYS A 112 ? 0.1973 0.3105 0.2119 -0.1318 0.0296  -0.0526 112 LYS A CG  
887  C  CD  . LYS A 112 ? 0.1935 0.3615 0.3384 -0.0888 -0.0474 0.0133  112 LYS A CD  
888  C  CE  . LYS A 112 ? 0.3488 0.3923 0.3327 0.0435  -0.0663 -0.0425 112 LYS A CE  
889  N  NZ  . LYS A 112 ? 0.4798 0.2379 0.5013 0.0103  -0.0983 0.0606  112 LYS A NZ  
890  N  N   A LYS A 113 ? 0.1079 0.0872 0.1343 0.0409  0.0122  0.0069  113 LYS A N   
891  N  N   B LYS A 113 ? 0.1195 0.1111 0.1282 0.0422  0.0188  0.0148  113 LYS A N   
892  C  CA  A LYS A 113 ? 0.0702 0.0943 0.1328 0.0201  0.0055  0.0061  113 LYS A CA  
893  C  CA  B LYS A 113 ? 0.0831 0.1311 0.1220 0.0377  0.0212  0.0159  113 LYS A CA  
894  C  C   A LYS A 113 ? 0.0354 0.0534 0.1393 0.0054  0.0300  0.0062  113 LYS A C   
895  C  C   B LYS A 113 ? 0.0634 0.0740 0.1486 0.0283  0.0245  0.0107  113 LYS A C   
896  O  O   A LYS A 113 ? 0.0824 0.0613 0.1143 -0.0192 0.0341  0.0217  113 LYS A O   
897  O  O   B LYS A 113 ? 0.1523 0.0775 0.1384 -0.0004 0.0397  0.0159  113 LYS A O   
898  C  CB  A LYS A 113 ? 0.0594 0.1000 0.1606 0.0128  -0.0019 -0.0353 113 LYS A CB  
899  C  CB  B LYS A 113 ? 0.0858 0.1420 0.1379 0.0410  0.0230  -0.0071 113 LYS A CB  
900  C  CG  A LYS A 113 ? 0.0664 0.1251 0.1688 0.0179  -0.0156 -0.0132 113 LYS A CG  
901  C  CG  B LYS A 113 ? 0.0749 0.1741 0.0820 0.0399  0.0516  -0.0197 113 LYS A CG  
902  C  CD  A LYS A 113 ? 0.1002 0.1558 0.1483 0.0265  -0.0021 -0.0348 113 LYS A CD  
903  C  CD  B LYS A 113 ? 0.0443 0.1998 0.1208 0.0478  0.0245  -0.0122 113 LYS A CD  
904  C  CE  A LYS A 113 ? 0.1097 0.2138 0.1558 0.0283  -0.0299 -0.0205 113 LYS A CE  
905  C  CE  B LYS A 113 ? 0.1091 0.1646 0.1459 0.0120  -0.0066 -0.0253 113 LYS A CE  
906  N  NZ  A LYS A 113 ? 0.1377 0.2579 0.1990 0.0623  0.0151  0.0391  113 LYS A NZ  
907  N  NZ  B LYS A 113 ? 0.1397 0.1655 0.2117 0.0293  0.0276  -0.0046 113 LYS A NZ  
908  N  N   . TYR A 114 ? 0.0337 0.0706 0.1177 0.0151  0.0221  0.0073  114 TYR A N   
909  C  CA  . TYR A 114 ? 0.0458 0.0833 0.0986 0.0178  0.0308  0.0036  114 TYR A CA  
910  C  C   . TYR A 114 ? 0.0312 0.0593 0.1068 -0.0141 0.0378  -0.0062 114 TYR A C   
911  O  O   . TYR A 114 ? 0.0308 0.0673 0.1140 -0.0137 0.0361  0.0063  114 TYR A O   
912  C  CB  . TYR A 114 ? 0.0436 0.0636 0.1375 0.0128  0.0356  0.0340  114 TYR A CB  
913  C  CG  . TYR A 114 ? 0.0217 0.1021 0.1318 -0.0070 0.0197  0.0164  114 TYR A CG  
914  C  CD1 . TYR A 114 ? 0.1224 0.1082 0.1222 0.0370  0.0278  0.0181  114 TYR A CD1 
915  C  CD2 . TYR A 114 ? 0.0204 0.1025 0.1865 -0.0072 0.0473  0.0195  114 TYR A CD2 
916  C  CE1 . TYR A 114 ? 0.1100 0.1613 0.1419 0.0198  0.0312  0.0120  114 TYR A CE1 
917  C  CE2 . TYR A 114 ? 0.0419 0.1560 0.1817 -0.0041 0.0688  0.0067  114 TYR A CE2 
918  C  CZ  . TYR A 114 ? 0.1164 0.2071 0.1668 -0.0104 0.0784  0.0233  114 TYR A CZ  
919  O  OH  . TYR A 114 ? 0.1832 0.3603 0.2152 0.0310  0.1426  0.0531  114 TYR A OH  
920  N  N   . ALA A 115 ? 0.0662 0.0686 0.1052 -0.0177 0.0230  -0.0268 115 ALA A N   
921  C  CA  . ALA A 115 ? 0.0607 0.0593 0.1082 -0.0119 0.0167  -0.0201 115 ALA A CA  
922  C  C   . ALA A 115 ? 0.0536 0.0628 0.1036 -0.0051 0.0362  -0.0099 115 ALA A C   
923  O  O   . ALA A 115 ? 0.0398 0.0820 0.1049 -0.0079 0.0303  -0.0044 115 ALA A O   
924  C  CB  . ALA A 115 ? 0.0660 0.0919 0.1369 -0.0069 -0.0018 -0.0372 115 ALA A CB  
925  N  N   . ALA A 116 ? 0.0393 0.0496 0.0930 -0.0143 0.0129  -0.0143 116 ALA A N   
926  C  CA  . ALA A 116 ? 0.0578 0.0511 0.0872 -0.0043 0.0217  -0.0087 116 ALA A CA  
927  C  C   . ALA A 116 ? 0.0134 0.0560 0.0878 -0.0089 0.0221  -0.0065 116 ALA A C   
928  O  O   . ALA A 116 ? 0.0179 0.0761 0.0835 -0.0193 0.0150  0.0024  116 ALA A O   
929  C  CB  . ALA A 116 ? 0.0385 0.1032 0.0854 -0.0011 0.0243  0.0058  116 ALA A CB  
930  N  N   . GLU A 117 ? 0.0130 0.0488 0.0858 -0.0015 0.0196  -0.0142 117 GLU A N   
931  C  CA  . GLU A 117 ? 0.0137 0.0464 0.0822 0.0003  0.0187  -0.0109 117 GLU A CA  
932  C  C   . GLU A 117 ? 0.0128 0.0668 0.0876 0.0043  0.0228  0.0046  117 GLU A C   
933  O  O   . GLU A 117 ? 0.0276 0.0804 0.1233 -0.0012 0.0390  0.0268  117 GLU A O   
934  C  CB  . GLU A 117 ? 0.0215 0.0876 0.0960 -0.0068 0.0100  -0.0307 117 GLU A CB  
935  C  CG  . GLU A 117 ? 0.0563 0.1020 0.0695 0.0097  0.0017  -0.0190 117 GLU A CG  
936  C  CD  . GLU A 117 ? 0.0417 0.0664 0.0722 -0.0132 0.0074  0.0139  117 GLU A CD  
937  O  OE1 . GLU A 117 ? 0.0197 0.1037 0.1170 0.0065  0.0089  0.0107  117 GLU A OE1 
938  O  OE2 . GLU A 117 ? 0.0712 0.1039 0.0892 0.0024  -0.0168 -0.0173 117 GLU A OE2 
939  N  N   . LEU A 118 ? 0.0135 0.0601 0.0750 0.0087  0.0081  -0.0030 118 LEU A N   
940  C  CA  . LEU A 118 ? 0.0064 0.0544 0.0873 0.0007  0.0027  -0.0040 118 LEU A CA  
941  C  C   . LEU A 118 ? 0.0075 0.0584 0.0548 0.0045  0.0065  0.0048  118 LEU A C   
942  O  O   . LEU A 118 ? 0.0303 0.0713 0.0617 -0.0032 0.0173  0.0077  118 LEU A O   
943  C  CB  . LEU A 118 ? 0.0073 0.0790 0.1071 0.0084  0.0022  0.0075  118 LEU A CB  
944  C  CG  . LEU A 118 ? 0.0089 0.0719 0.0935 -0.0047 -0.0078 0.0260  118 LEU A CG  
945  C  CD1 . LEU A 118 ? 0.0502 0.1095 0.0910 -0.0113 -0.0015 0.0307  118 LEU A CD1 
946  C  CD2 . LEU A 118 ? 0.0164 0.1465 0.1233 -0.0198 -0.0242 0.0170  118 LEU A CD2 
947  N  N   . HIS A 119 ? 0.0103 0.0529 0.0709 0.0074  0.0066  0.0098  119 HIS A N   
948  C  CA  . HIS A 119 ? 0.0063 0.0645 0.0814 -0.0003 -0.0002 0.0072  119 HIS A CA  
949  C  C   . HIS A 119 ? 0.0074 0.0573 0.0657 -0.0034 0.0068  0.0039  119 HIS A C   
950  O  O   . HIS A 119 ? 0.0190 0.0891 0.0673 0.0105  0.0168  0.0027  119 HIS A O   
951  C  CB  . HIS A 119 ? 0.0082 0.0872 0.0940 0.0093  0.0087  0.0033  119 HIS A CB  
952  C  CG  . HIS A 119 ? 0.0091 0.0808 0.0770 0.0003  0.0141  0.0007  119 HIS A CG  
953  N  ND1 . HIS A 119 ? 0.0100 0.0986 0.0882 -0.0105 0.0160  -0.0183 119 HIS A ND1 
954  C  CD2 . HIS A 119 ? 0.0094 0.0867 0.0628 -0.0098 -0.0111 0.0074  119 HIS A CD2 
955  C  CE1 . HIS A 119 ? 0.0269 0.0847 0.0802 0.0060  0.0178  -0.0307 119 HIS A CE1 
956  N  NE2 . HIS A 119 ? 0.0127 0.0939 0.0779 0.0091  -0.0036 0.0041  119 HIS A NE2 
957  N  N   . LEU A 120 ? 0.0077 0.0532 0.0849 0.0007  0.0102  -0.0028 120 LEU A N   
958  C  CA  . LEU A 120 ? 0.0078 0.0574 0.0922 0.0014  0.0111  -0.0019 120 LEU A CA  
959  C  C   . LEU A 120 ? 0.0130 0.0417 0.0833 0.0106  0.0108  0.0035  120 LEU A C   
960  O  O   . LEU A 120 ? 0.0064 0.0704 0.0771 0.0025  0.0016  -0.0028 120 LEU A O   
961  C  CB  . LEU A 120 ? 0.0072 0.0661 0.1028 0.0063  0.0041  -0.0054 120 LEU A CB  
962  C  CG  . LEU A 120 ? 0.0132 0.0978 0.1086 -0.0239 -0.0100 0.0083  120 LEU A CG  
963  C  CD1 . LEU A 120 ? 0.1231 0.0991 0.1404 -0.0666 -0.0022 0.0209  120 LEU A CD1 
964  C  CD2 . LEU A 120 ? 0.0635 0.1319 0.1315 0.0259  -0.0381 -0.0119 120 LEU A CD2 
965  N  N   . VAL A 121 ? 0.0066 0.0525 0.1028 0.0005  0.0057  0.0096  121 VAL A N   
966  C  CA  . VAL A 121 ? 0.0153 0.0553 0.0847 0.0018  0.0253  -0.0133 121 VAL A CA  
967  C  C   . VAL A 121 ? 0.0247 0.0573 0.0876 0.0047  0.0103  0.0027  121 VAL A C   
968  O  O   . VAL A 121 ? 0.0302 0.0892 0.0860 -0.0001 0.0055  0.0089  121 VAL A O   
969  C  CB  . VAL A 121 ? 0.0095 0.0729 0.1035 0.0057  0.0162  0.0013  121 VAL A CB  
970  C  CG1 . VAL A 121 ? 0.0091 0.1133 0.1330 -0.0161 0.0089  -0.0150 121 VAL A CG1 
971  C  CG2 . VAL A 121 ? 0.0203 0.0862 0.1185 0.0260  0.0238  -0.0030 121 VAL A CG2 
972  N  N   . HIS A 122 ? 0.0089 0.0532 0.0996 0.0002  0.0150  -0.0141 122 HIS A N   
973  C  CA  . HIS A 122 ? 0.0129 0.0497 0.1140 -0.0047 0.0264  -0.0138 122 HIS A CA  
974  C  C   . HIS A 122 ? 0.0138 0.0688 0.0941 -0.0136 0.0202  -0.0018 122 HIS A C   
975  O  O   . HIS A 122 ? 0.0337 0.0619 0.1276 -0.0110 -0.0059 0.0126  122 HIS A O   
976  C  CB  . HIS A 122 ? 0.0127 0.0706 0.1102 -0.0063 0.0247  -0.0040 122 HIS A CB  
977  C  CG  . HIS A 122 ? 0.0127 0.0756 0.1040 -0.0043 0.0126  -0.0121 122 HIS A CG  
978  N  ND1 . HIS A 122 ? 0.0132 0.0684 0.1176 -0.0050 0.0275  -0.0124 122 HIS A ND1 
979  C  CD2 . HIS A 122 ? 0.0104 0.0958 0.0960 -0.0078 0.0187  -0.0208 122 HIS A CD2 
980  C  CE1 . HIS A 122 ? 0.0096 0.0782 0.1421 -0.0018 0.0210  -0.0139 122 HIS A CE1 
981  N  NE2 . HIS A 122 ? 0.0108 0.0931 0.1293 -0.0093 0.0204  0.0021  122 HIS A NE2 
982  N  N   . TRP A 123 ? 0.0199 0.0559 0.1094 -0.0101 0.0371  -0.0210 123 TRP A N   
983  C  CA  . TRP A 123 ? 0.0151 0.0628 0.1289 -0.0115 0.0315  -0.0218 123 TRP A CA  
984  C  C   . TRP A 123 ? 0.0100 0.0641 0.1201 -0.0053 0.0205  -0.0184 123 TRP A C   
985  O  O   . TRP A 123 ? 0.0129 0.0924 0.1247 0.0013  0.0150  0.0027  123 TRP A O   
986  C  CB  . TRP A 123 ? 0.0116 0.1216 0.1155 -0.0204 0.0119  0.0081  123 TRP A CB  
987  C  CG  . TRP A 123 ? 0.0145 0.0897 0.1256 -0.0086 0.0011  -0.0082 123 TRP A CG  
988  C  CD1 . TRP A 123 ? 0.0571 0.0926 0.1135 -0.0391 -0.0318 0.0184  123 TRP A CD1 
989  C  CD2 . TRP A 123 ? 0.0287 0.0865 0.1196 -0.0118 0.0203  0.0063  123 TRP A CD2 
990  N  NE1 . TRP A 123 ? 0.0745 0.0886 0.1493 -0.0226 -0.0511 0.0097  123 TRP A NE1 
991  C  CE2 . TRP A 123 ? 0.0612 0.0953 0.1395 -0.0174 -0.0113 0.0082  123 TRP A CE2 
992  C  CE3 . TRP A 123 ? 0.0661 0.0807 0.1437 -0.0062 0.0167  0.0015  123 TRP A CE3 
993  C  CZ2 . TRP A 123 ? 0.1016 0.0979 0.1610 -0.0069 0.0234  0.0234  123 TRP A CZ2 
994  C  CZ3 . TRP A 123 ? 0.1140 0.0754 0.1736 -0.0203 0.0216  0.0269  123 TRP A CZ3 
995  C  CH2 . TRP A 123 ? 0.0810 0.0987 0.1739 -0.0077 0.0188  0.0165  123 TRP A CH2 
996  N  N   . ASN A 124 ? 0.0242 0.0813 0.1018 -0.0186 0.0405  -0.0278 124 ASN A N   
997  C  CA  . ASN A 124 ? 0.0406 0.0873 0.1109 -0.0071 0.0412  -0.0337 124 ASN A CA  
998  C  C   . ASN A 124 ? 0.0311 0.0926 0.1535 -0.0162 0.0273  -0.0166 124 ASN A C   
999  O  O   . ASN A 124 ? 0.0229 0.0883 0.1344 -0.0081 0.0296  -0.0168 124 ASN A O   
1000 C  CB  . ASN A 124 ? 0.1099 0.1156 0.0955 -0.0237 0.0347  -0.0073 124 ASN A CB  
1001 C  CG  . ASN A 124 ? 0.1481 0.1099 0.1430 -0.0357 0.0681  -0.0229 124 ASN A CG  
1002 O  OD1 . ASN A 124 ? 0.1261 0.1150 0.1749 -0.0218 0.0710  -0.0399 124 ASN A OD1 
1003 N  ND2 . ASN A 124 ? 0.2552 0.1328 0.1355 -0.0364 0.0610  -0.0200 124 ASN A ND2 
1004 N  N   . THR A 125 ? 0.0461 0.0752 0.1714 -0.0021 0.0193  -0.0196 125 THR A N   
1005 C  CA  . THR A 125 ? 0.0569 0.0743 0.2463 0.0190  0.0072  -0.0013 125 THR A CA  
1006 C  C   . THR A 125 ? 0.0513 0.0644 0.2727 0.0311  0.0319  -0.0113 125 THR A C   
1007 O  O   . THR A 125 ? 0.0600 0.0923 0.2928 0.0167  0.0419  0.0053  125 THR A O   
1008 C  CB  . THR A 125 ? 0.0714 0.1566 0.2949 0.0200  -0.0303 -0.0104 125 THR A CB  
1009 O  OG1 . THR A 125 ? 0.0822 0.1432 0.3802 0.0083  0.0252  -0.0054 125 THR A OG1 
1010 C  CG2 . THR A 125 ? 0.1662 0.1364 0.3683 -0.0445 -0.0851 0.0150  125 THR A CG2 
1011 N  N   . LYS A 126 ? 0.0706 0.0942 0.1846 0.0010  0.0614  -0.0344 127 LYS A N   
1012 C  CA  . LYS A 126 ? 0.1426 0.1129 0.2222 -0.0302 0.0817  -0.0555 127 LYS A CA  
1013 C  C   . LYS A 126 ? 0.1330 0.0937 0.1851 -0.0121 0.0694  -0.0484 127 LYS A C   
1014 O  O   . LYS A 126 ? 0.1808 0.0950 0.2507 -0.0216 0.0964  -0.0838 127 LYS A O   
1015 C  CB  . LYS A 126 ? 0.2328 0.1235 0.2403 -0.0322 0.0705  -0.0364 127 LYS A CB  
1016 C  CG  . LYS A 126 ? 0.2460 0.1890 0.1928 -0.0119 0.0701  -0.0660 127 LYS A CG  
1017 C  CD  . LYS A 126 ? 0.3165 0.2769 0.1942 -0.1055 0.0873  -0.0562 127 LYS A CD  
1018 C  CE  . LYS A 126 ? 0.3744 0.5031 0.2630 0.0092  0.0934  0.0264  127 LYS A CE  
1019 N  NZ  . LYS A 126 ? 0.6969 0.6275 0.2971 0.0153  0.2039  0.1169  127 LYS A NZ  
1020 N  N   . TYR A 127 ? 0.0688 0.0846 0.1459 -0.0044 0.0451  -0.0186 128 TYR A N   
1021 C  CA  . TYR A 127 ? 0.0538 0.1029 0.1329 -0.0113 0.0162  -0.0204 128 TYR A CA  
1022 C  C   . TYR A 127 ? 0.0706 0.0986 0.1495 -0.0061 0.0375  -0.0031 128 TYR A C   
1023 O  O   . TYR A 127 ? 0.0682 0.1473 0.1632 -0.0256 0.0352  0.0021  128 TYR A O   
1024 C  CB  . TYR A 127 ? 0.0724 0.1152 0.1308 0.0068  0.0175  -0.0279 128 TYR A CB  
1025 C  CG  . TYR A 127 ? 0.1229 0.1253 0.1275 -0.0032 -0.0017 -0.0389 128 TYR A CG  
1026 C  CD1 . TYR A 127 ? 0.1502 0.1369 0.1710 -0.0035 -0.0416 -0.0518 128 TYR A CD1 
1027 C  CD2 . TYR A 127 ? 0.0621 0.1316 0.1680 0.0059  -0.0054 -0.0347 128 TYR A CD2 
1028 C  CE1 . TYR A 127 ? 0.2565 0.1437 0.1696 0.0068  -0.0173 -0.0409 128 TYR A CE1 
1029 C  CE2 . TYR A 127 ? 0.1244 0.1624 0.1430 0.0150  0.0103  -0.0348 128 TYR A CE2 
1030 C  CZ  . TYR A 127 ? 0.2258 0.1588 0.1326 0.0047  0.0155  -0.0310 128 TYR A CZ  
1031 O  OH  . TYR A 127 ? 0.3202 0.2030 0.1337 0.0624  0.0376  -0.0383 128 TYR A OH  
1032 N  N   . GLY A 128 ? 0.0775 0.1044 0.1544 0.0150  0.0193  0.0019  129 GLY A N   
1033 C  CA  . GLY A 128 ? 0.0883 0.1081 0.1591 0.0109  0.0170  0.0027  129 GLY A CA  
1034 C  C   . GLY A 128 ? 0.0910 0.0829 0.1497 0.0009  0.0120  0.0192  129 GLY A C   
1035 O  O   . GLY A 128 ? 0.0754 0.1179 0.1591 0.0162  0.0081  0.0317  129 GLY A O   
1036 N  N   . ASP A 129 ? 0.0716 0.0968 0.1347 0.0020  0.0201  0.0011  130 ASP A N   
1037 C  CA  . ASP A 129 ? 0.0894 0.1020 0.1231 0.0201  0.0223  0.0079  130 ASP A CA  
1038 C  C   . ASP A 129 ? 0.0595 0.1007 0.1186 0.0096  0.0152  -0.0023 130 ASP A C   
1039 O  O   . ASP A 129 ? 0.0558 0.1274 0.1282 0.0186  0.0092  -0.0071 130 ASP A O   
1040 C  CB  . ASP A 129 ? 0.0998 0.1517 0.1437 0.0225  0.0273  0.0488  130 ASP A CB  
1041 C  CG  . ASP A 129 ? 0.1172 0.1466 0.2159 0.0359  0.0055  -0.0519 130 ASP A CG  
1042 O  OD1 . ASP A 129 ? 0.1635 0.1448 0.3301 0.0247  -0.0034 0.0604  130 ASP A OD1 
1043 O  OD2 . ASP A 129 ? 0.1667 0.1648 0.3542 0.0156  0.0253  0.0607  130 ASP A OD2 
1044 N  N   . TYR A 130 ? 0.0675 0.0977 0.1272 0.0149  0.0328  -0.0087 131 TYR A N   
1045 C  CA  . TYR A 130 ? 0.0653 0.0949 0.1452 -0.0129 0.0049  0.0050  131 TYR A CA  
1046 C  C   . TYR A 130 ? 0.0538 0.1189 0.1289 0.0006  0.0280  0.0362  131 TYR A C   
1047 O  O   . TYR A 130 ? 0.0949 0.1107 0.1391 -0.0192 0.0137  0.0568  131 TYR A O   
1048 C  CB  . TYR A 130 ? 0.1160 0.0996 0.1217 -0.0147 0.0330  -0.0038 131 TYR A CB  
1049 C  CG  . TYR A 130 ? 0.1657 0.1384 0.1208 0.0370  0.0403  -0.0144 131 TYR A CG  
1050 C  CD1 . TYR A 130 ? 0.1711 0.1459 0.2303 -0.0119 0.1109  -0.0392 131 TYR A CD1 
1051 C  CD2 . TYR A 130 ? 0.2546 0.1714 0.1181 0.0738  0.0256  -0.0330 131 TYR A CD2 
1052 C  CE1 . TYR A 130 ? 0.3358 0.1747 0.2477 -0.0324 0.1713  -0.0750 131 TYR A CE1 
1053 C  CE2 . TYR A 130 ? 0.4753 0.2174 0.1662 0.1425  0.1214  0.0000  131 TYR A CE2 
1054 C  CZ  . TYR A 130 ? 0.4117 0.1584 0.2336 0.0480  0.2207  0.0188  131 TYR A CZ  
1055 O  OH  . TYR A 130 ? 0.6342 0.2464 0.2386 0.0143  0.2685  -0.0252 131 TYR A OH  
1056 N  N   . GLY A 131 ? 0.0540 0.1405 0.1359 -0.0116 0.0440  0.0268  132 GLY A N   
1057 C  CA  . GLY A 131 ? 0.0542 0.1678 0.1800 -0.0165 0.0358  0.0148  132 GLY A CA  
1058 C  C   . GLY A 131 ? 0.0345 0.1192 0.1767 -0.0177 0.0370  0.0379  132 GLY A C   
1059 O  O   . GLY A 131 ? 0.0785 0.1477 0.2386 0.0129  -0.0067 0.0249  132 GLY A O   
1060 N  N   A LYS A 132 ? 0.0549 0.1120 0.2011 -0.0340 0.0450  0.0010  133 LYS A N   
1061 N  N   B LYS A 132 ? 0.0522 0.1183 0.1876 -0.0368 0.0480  -0.0015 133 LYS A N   
1062 C  CA  A LYS A 132 ? 0.0409 0.0770 0.1876 -0.0210 0.0168  0.0118  133 LYS A CA  
1063 C  CA  B LYS A 132 ? 0.0497 0.0964 0.1710 -0.0304 0.0231  0.0135  133 LYS A CA  
1064 C  C   A LYS A 132 ? 0.0357 0.0844 0.1703 -0.0303 -0.0132 0.0122  133 LYS A C   
1065 C  C   B LYS A 132 ? 0.0363 0.0960 0.1634 -0.0388 -0.0039 0.0151  133 LYS A C   
1066 O  O   A LYS A 132 ? 0.0865 0.1350 0.1681 -0.0244 -0.0256 0.0335  133 LYS A O   
1067 O  O   B LYS A 132 ? 0.0687 0.1412 0.1720 -0.0411 -0.0207 0.0372  133 LYS A O   
1068 C  CB  A LYS A 132 ? 0.0803 0.0891 0.2151 0.0050  -0.0242 -0.0027 133 LYS A CB  
1069 C  CB  B LYS A 132 ? 0.0604 0.1039 0.1695 -0.0185 0.0027  0.0010  133 LYS A CB  
1070 C  CG  A LYS A 132 ? 0.1416 0.1041 0.2120 0.0013  -0.0194 0.0305  133 LYS A CG  
1071 C  CG  B LYS A 132 ? 0.1355 0.1043 0.1973 0.0137  0.0541  -0.0429 133 LYS A CG  
1072 N  N   . ALA A 133 ? 0.0310 0.0836 0.1340 -0.0301 0.0100  -0.0036 134 ALA A N   
1073 C  CA  . ALA A 133 ? 0.0337 0.1075 0.1204 -0.0207 0.0134  0.0058  134 ALA A CA  
1074 C  C   . ALA A 133 ? 0.0508 0.1138 0.1307 -0.0052 0.0326  0.0239  134 ALA A C   
1075 O  O   . ALA A 133 ? 0.0258 0.1189 0.1301 -0.0066 0.0129  0.0077  134 ALA A O   
1076 C  CB  . ALA A 133 ? 0.0432 0.1068 0.1466 -0.0345 0.0138  -0.0089 134 ALA A CB  
1077 N  N   . GLN A 134 ? 0.0732 0.1083 0.1511 0.0272  0.0444  0.0309  135 GLN A N   
1078 C  CA  . GLN A 134 ? 0.1122 0.1815 0.1527 0.0719  0.0440  0.0754  135 GLN A CA  
1079 C  C   . GLN A 134 ? 0.0477 0.2081 0.1817 0.0548  0.0825  0.1219  135 GLN A C   
1080 O  O   . GLN A 134 ? 0.1088 0.3129 0.3829 0.0944  0.0534  0.2249  135 GLN A O   
1081 C  CB  . GLN A 134 ? 0.2590 0.2841 0.2075 0.1628  0.1084  0.0671  135 GLN A CB  
1082 C  CG  . GLN A 134 ? 0.1527 0.4462 0.3046 0.0498  -0.0137 0.0469  135 GLN A CG  
1083 C  CD  . GLN A 134 ? 0.1619 0.6326 0.2673 -0.0289 -0.0357 0.1068  135 GLN A CD  
1084 O  OE1 . GLN A 134 ? 0.1588 0.5527 0.2514 -0.0370 0.0871  -0.1375 135 GLN A OE1 
1085 N  NE2 . GLN A 134 ? 0.3941 0.1784 0.2594 0.0502  -0.0214 -0.0683 135 GLN A NE2 
1086 N  N   . GLN A 135 ? 0.0385 0.2414 0.2356 -0.0149 0.0491  0.1187  136 GLN A N   
1087 C  CA  . GLN A 135 ? 0.0752 0.3617 0.2465 -0.0403 -0.0087 0.1178  136 GLN A CA  
1088 C  C   . GLN A 135 ? 0.0568 0.2303 0.2557 -0.0608 -0.0296 0.0494  136 GLN A C   
1089 O  O   . GLN A 135 ? 0.1106 0.3227 0.2875 -0.1133 -0.0643 0.0451  136 GLN A O   
1090 C  CB  . GLN A 135 ? 0.1553 0.4191 0.3481 -0.1382 -0.0800 0.1591  136 GLN A CB  
1091 C  CG  . GLN A 135 ? 0.3022 0.5873 0.3276 -0.1987 -0.0798 0.2639  136 GLN A CG  
1092 C  CD  . GLN A 135 ? 0.5919 0.6334 0.6108 -0.2532 -0.0297 0.2723  136 GLN A CD  
1093 O  OE1 . GLN A 135 ? 0.7551 0.9471 0.6335 -0.5510 -0.1013 0.2386  136 GLN A OE1 
1094 N  NE2 . GLN A 135 ? 0.2533 0.6583 0.5514 -0.1450 0.0702  0.1564  136 GLN A NE2 
1095 N  N   . GLN A 136 ? 0.0581 0.1764 0.1720 -0.0375 -0.0055 0.0608  137 GLN A N   
1096 C  CA  . GLN A 136 ? 0.0872 0.1244 0.1286 -0.0119 -0.0304 -0.0089 137 GLN A CA  
1097 C  C   . GLN A 136 ? 0.0860 0.1451 0.0989 -0.0027 0.0038  -0.0207 137 GLN A C   
1098 O  O   . GLN A 136 ? 0.0807 0.1468 0.0908 -0.0156 0.0099  -0.0183 137 GLN A O   
1099 C  CB  . GLN A 136 ? 0.1258 0.1195 0.1678 0.0103  -0.0303 0.0051  137 GLN A CB  
1100 C  CG  . GLN A 136 ? 0.1796 0.1481 0.2016 -0.0164 -0.0176 0.0295  137 GLN A CG  
1101 C  CD  . GLN A 136 ? 0.1344 0.2655 0.2043 -0.0471 0.0223  0.0163  137 GLN A CD  
1102 O  OE1 . GLN A 136 ? 0.2420 0.2275 0.2378 -0.0462 -0.0761 -0.0441 137 GLN A OE1 
1103 N  NE2 . GLN A 136 ? 0.2665 0.3315 0.2405 -0.1317 0.0621  0.0122  137 GLN A NE2 
1104 N  N   . PRO A 137 ? 0.0741 0.1689 0.0919 0.0122  0.0017  -0.0403 138 PRO A N   
1105 C  CA  . PRO A 137 ? 0.0960 0.2063 0.1004 0.0263  0.0115  0.0168  138 PRO A CA  
1106 C  C   . PRO A 137 ? 0.0982 0.1743 0.1018 0.0348  0.0276  0.0109  138 PRO A C   
1107 O  O   . PRO A 137 ? 0.1372 0.1771 0.2061 0.0206  0.0436  -0.0104 138 PRO A O   
1108 C  CB  . PRO A 137 ? 0.2674 0.2575 0.0968 0.0182  -0.0181 0.0366  138 PRO A CB  
1109 C  CG  . PRO A 137 ? 0.4106 0.2899 0.1337 -0.0162 -0.0405 -0.0409 138 PRO A CG  
1110 C  CD  . PRO A 137 ? 0.1750 0.2395 0.1154 -0.0203 -0.0196 -0.0748 138 PRO A CD  
1111 N  N   . ASP A 138 ? 0.0639 0.1635 0.0853 0.0185  0.0238  0.0050  139 ASP A N   
1112 C  CA  . ASP A 138 ? 0.0533 0.2652 0.1098 0.0106  0.0483  0.0197  139 ASP A CA  
1113 C  C   . ASP A 138 ? 0.0487 0.1454 0.1054 -0.0085 0.0442  -0.0006 139 ASP A C   
1114 O  O   . ASP A 138 ? 0.0575 0.2061 0.1553 0.0151  0.0399  0.0071  139 ASP A O   
1115 C  CB  . ASP A 138 ? 0.1368 0.2546 0.1335 0.0279  0.0856  0.0173  139 ASP A CB  
1116 C  CG  . ASP A 138 ? 0.1565 0.2575 0.1808 0.0523  0.0640  -0.0155 139 ASP A CG  
1117 O  OD1 . ASP A 138 ? 0.1700 0.1989 0.1983 0.0527  0.0480  -0.0368 139 ASP A OD1 
1118 O  OD2 . ASP A 138 ? 0.1632 0.2662 0.2386 0.0342  0.0841  -0.0520 139 ASP A OD2 
1119 N  N   . GLY A 139 ? 0.0505 0.0939 0.0829 -0.0019 0.0332  -0.0034 140 GLY A N   
1120 C  CA  . GLY A 139 ? 0.0637 0.0883 0.0791 -0.0129 0.0151  -0.0016 140 GLY A CA  
1121 C  C   . GLY A 139 ? 0.0205 0.0675 0.0982 0.0006  0.0293  -0.0102 140 GLY A C   
1122 O  O   . GLY A 139 ? 0.0436 0.0636 0.1061 0.0051  0.0166  -0.0044 140 GLY A O   
1123 N  N   . LEU A 140 ? 0.0118 0.0657 0.1093 -0.0021 0.0233  -0.0234 141 LEU A N   
1124 C  CA  . LEU A 140 ? 0.0156 0.0664 0.1048 -0.0029 0.0288  -0.0316 141 LEU A CA  
1125 C  C   . LEU A 140 ? 0.0072 0.0644 0.1109 0.0051  0.0048  -0.0179 141 LEU A C   
1126 O  O   . LEU A 140 ? 0.0179 0.0786 0.1070 -0.0145 0.0153  -0.0048 141 LEU A O   
1127 C  CB  . LEU A 140 ? 0.0234 0.0817 0.1154 -0.0076 0.0423  -0.0352 141 LEU A CB  
1128 C  CG  . LEU A 140 ? 0.0317 0.1127 0.1531 0.0187  0.0580  0.0065  141 LEU A CG  
1129 C  CD1 . LEU A 140 ? 0.0473 0.1640 0.1740 0.0491  0.0663  0.0027  141 LEU A CD1 
1130 C  CD2 . LEU A 140 ? 0.0682 0.1258 0.1738 0.0223  0.0482  0.0362  141 LEU A CD2 
1131 N  N   . ALA A 141 ? 0.0081 0.0630 0.1116 -0.0069 0.0125  -0.0248 142 ALA A N   
1132 C  CA  . ALA A 141 ? 0.0091 0.0588 0.1133 -0.0049 0.0172  -0.0241 142 ALA A CA  
1133 C  C   . ALA A 141 ? 0.0097 0.0463 0.0704 -0.0055 0.0060  0.0059  142 ALA A C   
1134 O  O   . ALA A 141 ? 0.0454 0.0675 0.0824 0.0023  -0.0066 0.0171  142 ALA A O   
1135 C  CB  . ALA A 141 ? 0.0208 0.0942 0.1265 -0.0038 0.0410  -0.0310 142 ALA A CB  
1136 N  N   . VAL A 142 ? 0.0076 0.0470 0.1122 -0.0001 0.0118  0.0000  143 VAL A N   
1137 C  CA  . VAL A 142 ? 0.0106 0.0535 0.1154 -0.0005 0.0216  -0.0062 143 VAL A CA  
1138 C  C   . VAL A 142 ? 0.0080 0.0694 0.0873 -0.0073 0.0082  -0.0015 143 VAL A C   
1139 O  O   . VAL A 142 ? 0.0136 0.0783 0.0872 0.0035  0.0052  -0.0003 143 VAL A O   
1140 C  CB  . VAL A 142 ? 0.0063 0.0602 0.0967 -0.0004 0.0014  -0.0095 143 VAL A CB  
1141 C  CG1 . VAL A 142 ? 0.0161 0.0900 0.0761 0.0032  0.0108  -0.0182 143 VAL A CG1 
1142 C  CG2 . VAL A 142 ? 0.0177 0.1164 0.0968 -0.0215 0.0223  0.0146  143 VAL A CG2 
1143 N  N   . LEU A 143 ? 0.0085 0.0469 0.0929 -0.0084 0.0085  -0.0119 144 LEU A N   
1144 C  CA  . LEU A 143 ? 0.0096 0.0490 0.1120 -0.0110 0.0088  -0.0077 144 LEU A CA  
1145 C  C   . LEU A 143 ? 0.0153 0.0497 0.0861 -0.0185 0.0111  -0.0053 144 LEU A C   
1146 O  O   . LEU A 143 ? 0.0355 0.0930 0.0817 -0.0109 0.0189  -0.0002 144 LEU A O   
1147 C  CB  . LEU A 143 ? 0.0156 0.0840 0.1377 -0.0102 -0.0077 0.0075  144 LEU A CB  
1148 C  CG  . LEU A 143 ? 0.0077 0.1122 0.1258 -0.0074 0.0081  0.0251  144 LEU A CG  
1149 C  CD1 . LEU A 143 ? 0.0297 0.1494 0.1238 -0.0171 0.0131  0.0225  144 LEU A CD1 
1150 C  CD2 . LEU A 143 ? 0.0072 0.1427 0.1740 -0.0054 -0.0113 0.0206  144 LEU A CD2 
1151 N  N   . GLY A 144 ? 0.0094 0.0425 0.0993 -0.0101 0.0060  -0.0067 145 GLY A N   
1152 C  CA  . GLY A 144 ? 0.0232 0.0467 0.0952 -0.0091 0.0084  -0.0135 145 GLY A CA  
1153 C  C   . GLY A 144 ? 0.0106 0.0521 0.0815 -0.0002 0.0179  -0.0027 145 GLY A C   
1154 O  O   . GLY A 144 ? 0.0267 0.0950 0.0829 -0.0034 0.0320  -0.0036 145 GLY A O   
1155 N  N   . ILE A 145 ? 0.0075 0.0476 0.0962 -0.0069 0.0036  -0.0096 146 ILE A N   
1156 C  CA  . ILE A 145 ? 0.0081 0.0562 0.0956 -0.0094 0.0026  -0.0106 146 ILE A CA  
1157 C  C   . ILE A 145 ? 0.0113 0.0612 0.0820 -0.0033 0.0189  0.0030  146 ILE A C   
1158 O  O   . ILE A 145 ? 0.0234 0.0847 0.0824 -0.0207 0.0294  0.0016  146 ILE A O   
1159 C  CB  . ILE A 145 ? 0.0169 0.0677 0.0934 -0.0042 0.0000  -0.0031 146 ILE A CB  
1160 C  CG1 . ILE A 145 ? 0.0466 0.0885 0.1237 0.0233  -0.0084 -0.0136 146 ILE A CG1 
1161 C  CG2 . ILE A 145 ? 0.0221 0.0865 0.1524 -0.0096 -0.0242 -0.0162 146 ILE A CG2 
1162 C  CD1 . ILE A 145 ? 0.0655 0.1072 0.1032 0.0013  -0.0085 0.0161  146 ILE A CD1 
1163 N  N   . PHE A 146 ? 0.0122 0.0522 0.0903 0.0030  0.0217  0.0000  147 PHE A N   
1164 C  CA  . PHE A 146 ? 0.0133 0.0491 0.1034 0.0000  0.0128  -0.0071 147 PHE A CA  
1165 C  C   . PHE A 146 ? 0.0115 0.0739 0.0906 -0.0010 0.0208  -0.0108 147 PHE A C   
1166 O  O   . PHE A 146 ? 0.0115 0.0931 0.1282 0.0034  0.0221  -0.0322 147 PHE A O   
1167 C  CB  . PHE A 146 ? 0.0310 0.0670 0.0860 -0.0158 0.0097  -0.0073 147 PHE A CB  
1168 C  CG  . PHE A 146 ? 0.0120 0.0445 0.0802 -0.0038 0.0099  0.0085  147 PHE A CG  
1169 C  CD1 . PHE A 146 ? 0.0117 0.0675 0.1106 -0.0117 0.0048  -0.0024 147 PHE A CD1 
1170 C  CD2 . PHE A 146 ? 0.0518 0.0524 0.0781 -0.0171 0.0119  -0.0011 147 PHE A CD2 
1171 C  CE1 . PHE A 146 ? 0.0222 0.0768 0.0955 -0.0047 0.0089  -0.0108 147 PHE A CE1 
1172 C  CE2 . PHE A 146 ? 0.0276 0.0724 0.0989 -0.0314 0.0079  0.0094  147 PHE A CE2 
1173 C  CZ  . PHE A 146 ? 0.0267 0.1023 0.0928 -0.0175 0.0155  0.0070  147 PHE A CZ  
1174 N  N   . LEU A 147 ? 0.0107 0.0846 0.0761 0.0043  0.0080  -0.0217 148 LEU A N   
1175 C  CA  . LEU A 147 ? 0.0225 0.0664 0.0791 -0.0130 0.0089  -0.0121 148 LEU A CA  
1176 C  C   . LEU A 147 ? 0.0209 0.0696 0.0847 -0.0044 0.0179  -0.0201 148 LEU A C   
1177 O  O   . LEU A 147 ? 0.0227 0.0768 0.1214 -0.0008 0.0200  -0.0055 148 LEU A O   
1178 C  CB  . LEU A 147 ? 0.0369 0.0891 0.0882 -0.0003 0.0218  -0.0057 148 LEU A CB  
1179 C  CG  . LEU A 147 ? 0.0316 0.0704 0.1075 -0.0178 0.0016  -0.0118 148 LEU A CG  
1180 C  CD1 . LEU A 147 ? 0.1095 0.0801 0.0901 -0.0204 0.0081  -0.0140 148 LEU A CD1 
1181 C  CD2 . LEU A 147 ? 0.0565 0.0908 0.1120 -0.0264 0.0102  -0.0032 148 LEU A CD2 
1182 N  N   . LYS A 148 ? 0.0553 0.0691 0.1167 -0.0253 0.0100  -0.0089 149 LYS A N   
1183 C  CA  . LYS A 148 ? 0.0775 0.0668 0.1416 -0.0251 -0.0220 -0.0132 149 LYS A CA  
1184 C  C   . LYS A 148 ? 0.0573 0.0765 0.1341 -0.0044 -0.0302 -0.0100 149 LYS A C   
1185 O  O   . LYS A 148 ? 0.1048 0.1462 0.1432 0.0351  -0.0518 -0.0097 149 LYS A O   
1186 C  CB  . LYS A 148 ? 0.0795 0.2142 0.1405 -0.0571 -0.0294 0.0107  149 LYS A CB  
1187 C  CG  . LYS A 148 ? 0.0921 0.1962 0.1925 -0.0226 0.0288  0.0133  149 LYS A CG  
1188 C  CD  . LYS A 148 ? 0.2023 0.2330 0.2615 -0.0323 0.0782  0.0493  149 LYS A CD  
1189 C  CE  . LYS A 148 ? 0.2045 0.5272 0.3255 -0.0629 0.0704  0.0732  149 LYS A CE  
1190 N  NZ  . LYS A 148 ? 0.3930 0.6038 0.4155 -0.1666 0.1361  0.1708  149 LYS A NZ  
1191 N  N   . VAL A 149 ? 0.0951 0.0776 0.1729 0.0055  -0.0261 -0.0223 150 VAL A N   
1192 C  CA  . VAL A 149 ? 0.0846 0.1095 0.1606 -0.0198 -0.0133 -0.0181 150 VAL A CA  
1193 C  C   . VAL A 149 ? 0.0863 0.1222 0.1750 -0.0220 -0.0234 -0.0104 150 VAL A C   
1194 O  O   . VAL A 149 ? 0.1117 0.1497 0.1788 -0.0318 -0.0257 0.0133  150 VAL A O   
1195 C  CB  . VAL A 149 ? 0.0873 0.0883 0.1738 -0.0194 -0.0130 -0.0158 150 VAL A CB  
1196 C  CG1 . VAL A 149 ? 0.1359 0.1286 0.1628 -0.0359 -0.0237 -0.0114 150 VAL A CG1 
1197 C  CG2 . VAL A 149 ? 0.1005 0.1190 0.2332 -0.0461 -0.0076 -0.0298 150 VAL A CG2 
1198 N  N   . GLY A 150 ? 0.0828 0.1233 0.1826 -0.0542 -0.0403 -0.0288 151 GLY A N   
1199 C  CA  . GLY A 150 ? 0.0731 0.1398 0.1641 -0.0487 -0.0260 0.0310  151 GLY A CA  
1200 C  C   . GLY A 150 ? 0.0594 0.1409 0.1508 -0.0332 -0.0355 -0.0223 151 GLY A C   
1201 O  O   . GLY A 150 ? 0.1077 0.1280 0.1657 -0.0346 0.0125  -0.0044 151 GLY A O   
1202 N  N   A SER A 151 ? 0.0630 0.1183 0.2130 -0.0139 -0.0299 0.0121  152 SER A N   
1203 N  N   B SER A 151 ? 0.0661 0.1053 0.1946 -0.0248 -0.0144 0.0146  152 SER A N   
1204 C  CA  A SER A 151 ? 0.0723 0.1179 0.2030 0.0027  -0.0226 0.0068  152 SER A CA  
1205 C  CA  B SER A 151 ? 0.0882 0.1336 0.1723 -0.0225 -0.0201 0.0054  152 SER A CA  
1206 C  C   A SER A 151 ? 0.1276 0.1009 0.1289 -0.0104 -0.0187 -0.0334 152 SER A C   
1207 C  C   B SER A 151 ? 0.1045 0.1083 0.1386 -0.0234 -0.0344 -0.0223 152 SER A C   
1208 O  O   A SER A 151 ? 0.0886 0.1267 0.1240 -0.0041 -0.0320 -0.0271 152 SER A O   
1209 O  O   B SER A 151 ? 0.1034 0.1256 0.1400 -0.0205 -0.0355 -0.0335 152 SER A O   
1210 C  CB  A SER A 151 ? 0.1253 0.1092 0.2404 -0.0122 0.0324  -0.0514 152 SER A CB  
1211 C  CB  B SER A 151 ? 0.0621 0.2077 0.2385 -0.0686 -0.0271 -0.0214 152 SER A CB  
1212 O  OG  A SER A 151 ? 0.0840 0.1610 0.3159 0.0005  0.0148  0.0739  152 SER A OG  
1213 O  OG  B SER A 151 ? 0.1262 0.2938 0.1764 -0.0679 -0.0239 -0.0417 152 SER A OG  
1214 N  N   . ALA A 152 ? 0.1183 0.1120 0.1382 0.0109  -0.0208 -0.0048 153 ALA A N   
1215 C  CA  . ALA A 152 ? 0.1300 0.1262 0.1294 -0.0173 -0.0354 -0.0162 153 ALA A CA  
1216 C  C   . ALA A 152 ? 0.0842 0.1292 0.1578 -0.0248 -0.0151 -0.0210 153 ALA A C   
1217 O  O   . ALA A 152 ? 0.1059 0.1463 0.1917 -0.0283 0.0199  -0.0199 153 ALA A O   
1218 C  CB  . ALA A 152 ? 0.1578 0.1767 0.1387 -0.0243 -0.0719 -0.0291 153 ALA A CB  
1219 N  N   . LYS A 153 ? 0.1146 0.0989 0.1544 -0.0122 -0.0252 -0.0083 154 LYS A N   
1220 C  CA  . LYS A 153 ? 0.0865 0.1181 0.1341 0.0009  -0.0389 -0.0033 154 LYS A CA  
1221 C  C   . LYS A 153 ? 0.0615 0.1444 0.1401 0.0223  -0.0270 0.0042  154 LYS A C   
1222 O  O   . LYS A 153 ? 0.0680 0.1341 0.1523 -0.0075 -0.0162 -0.0091 154 LYS A O   
1223 C  CB  . LYS A 153 ? 0.0939 0.1181 0.1264 -0.0064 -0.0419 0.0091  154 LYS A CB  
1224 C  CG  . LYS A 153 ? 0.1574 0.1249 0.1359 -0.0156 -0.0403 -0.0048 154 LYS A CG  
1225 C  CD  . LYS A 153 ? 0.1829 0.1335 0.1326 -0.0096 -0.0383 0.0154  154 LYS A CD  
1226 C  CE  . LYS A 153 ? 0.1998 0.1709 0.1318 0.0133  0.0036  0.0139  154 LYS A CE  
1227 N  NZ  . LYS A 153 ? 0.1807 0.2321 0.1833 -0.0223 0.0332  -0.0085 154 LYS A NZ  
1228 N  N   . PRO A 154 ? 0.0527 0.1425 0.1962 -0.0183 -0.0282 0.0466  155 PRO A N   
1229 C  CA  . PRO A 154 ? 0.0436 0.1958 0.2367 -0.0297 -0.0641 0.0663  155 PRO A CA  
1230 C  C   . PRO A 154 ? 0.0427 0.1732 0.1620 -0.0091 -0.0311 0.0342  155 PRO A C   
1231 O  O   . PRO A 154 ? 0.0691 0.2666 0.1603 -0.0109 -0.0161 0.0588  155 PRO A O   
1232 C  CB  . PRO A 154 ? 0.0438 0.2208 0.3359 -0.0468 -0.0332 0.0718  155 PRO A CB  
1233 C  CG  . PRO A 154 ? 0.0946 0.3559 0.3010 -0.0592 -0.0566 0.1379  155 PRO A CG  
1234 C  CD  . PRO A 154 ? 0.0835 0.1993 0.2027 -0.0175 -0.0040 0.0713  155 PRO A CD  
1235 N  N   . GLY A 155 ? 0.0400 0.1343 0.1950 -0.0108 -0.0205 0.0058  156 GLY A N   
1236 C  CA  . GLY A 155 ? 0.0693 0.1395 0.2281 -0.0168 -0.0082 0.0168  156 GLY A CA  
1237 C  C   . GLY A 155 ? 0.0617 0.1405 0.2032 0.0116  -0.0278 0.0561  156 GLY A C   
1238 O  O   . GLY A 155 ? 0.1312 0.1389 0.3092 -0.0031 -0.0131 0.0394  156 GLY A O   
1239 N  N   . LEU A 156 ? 0.0493 0.1297 0.1653 0.0095  -0.0089 0.0178  157 LEU A N   
1240 C  CA  . LEU A 156 ? 0.0431 0.1377 0.1513 -0.0286 -0.0319 0.0027  157 LEU A CA  
1241 C  C   . LEU A 156 ? 0.0585 0.1358 0.1445 -0.0370 -0.0331 0.0103  157 LEU A C   
1242 O  O   . LEU A 156 ? 0.0540 0.1483 0.1646 -0.0290 -0.0300 0.0190  157 LEU A O   
1243 C  CB  . LEU A 156 ? 0.0567 0.1257 0.1610 -0.0020 -0.0261 -0.0128 157 LEU A CB  
1244 C  CG  . LEU A 156 ? 0.0505 0.1416 0.1770 -0.0316 -0.0306 -0.0029 157 LEU A CG  
1245 C  CD1 . LEU A 156 ? 0.0615 0.1664 0.1641 -0.0568 -0.0302 0.0016  157 LEU A CD1 
1246 C  CD2 . LEU A 156 ? 0.0976 0.1415 0.2073 -0.0158 -0.0511 -0.0013 157 LEU A CD2 
1247 N  N   . GLN A 157 ? 0.0867 0.1153 0.1339 -0.0271 -0.0395 -0.0100 158 GLN A N   
1248 C  CA  . GLN A 157 ? 0.1118 0.1447 0.1344 -0.0533 -0.0370 -0.0132 158 GLN A CA  
1249 C  C   . GLN A 157 ? 0.1239 0.1368 0.1351 -0.0375 -0.0293 -0.0100 158 GLN A C   
1250 O  O   . GLN A 157 ? 0.1300 0.1664 0.1333 -0.0315 -0.0289 -0.0195 158 GLN A O   
1251 C  CB  . GLN A 157 ? 0.1269 0.1807 0.1567 -0.0770 -0.0480 -0.0099 158 GLN A CB  
1252 C  CG  . GLN A 157 ? 0.1734 0.1840 0.1799 -0.0629 -0.0642 -0.0329 158 GLN A CG  
1253 C  CD  . GLN A 157 ? 0.1602 0.1789 0.1481 -0.0637 0.0074  0.0109  158 GLN A CD  
1254 O  OE1 . GLN A 157 ? 0.1772 0.1571 0.1497 -0.0649 0.0026  0.0043  158 GLN A OE1 
1255 N  NE2 . GLN A 157 ? 0.1829 0.2217 0.1426 -0.0611 -0.0053 -0.0219 158 GLN A NE2 
1256 N  N   A LYS A 158 ? 0.1093 0.1322 0.1718 -0.0424 -0.0653 -0.0048 159 LYS A N   
1257 N  N   B LYS A 158 ? 0.1020 0.1326 0.1609 -0.0436 -0.0559 -0.0049 159 LYS A N   
1258 C  CA  A LYS A 158 ? 0.0978 0.1366 0.1760 -0.0301 -0.0701 -0.0027 159 LYS A CA  
1259 C  CA  B LYS A 158 ? 0.0858 0.1348 0.1581 -0.0259 -0.0504 -0.0073 159 LYS A CA  
1260 C  C   A LYS A 158 ? 0.0882 0.1373 0.1384 -0.0177 -0.0467 0.0044  159 LYS A C   
1261 C  C   B LYS A 158 ? 0.0795 0.1359 0.1330 -0.0192 -0.0389 0.0036  159 LYS A C   
1262 O  O   A LYS A 158 ? 0.1353 0.1781 0.1565 -0.0498 -0.0226 0.0075  159 LYS A O   
1263 O  O   B LYS A 158 ? 0.1307 0.1788 0.1420 -0.0475 -0.0192 0.0070  159 LYS A O   
1264 C  CB  A LYS A 158 ? 0.1756 0.1724 0.2260 0.0373  -0.0989 0.0087  159 LYS A CB  
1265 C  CB  B LYS A 158 ? 0.1441 0.1553 0.1826 0.0149  -0.0542 0.0087  159 LYS A CB  
1266 C  CG  A LYS A 158 ? 0.2673 0.1930 0.3082 0.0317  -0.1265 0.0504  159 LYS A CG  
1267 C  CG  B LYS A 158 ? 0.1285 0.1752 0.1941 0.0257  -0.0461 0.0048  159 LYS A CG  
1268 N  N   . VAL A 159 ? 0.0702 0.1343 0.1355 -0.0272 -0.0455 0.0000  160 VAL A N   
1269 C  CA  . VAL A 159 ? 0.0628 0.1190 0.1043 -0.0078 -0.0368 -0.0071 160 VAL A CA  
1270 C  C   . VAL A 159 ? 0.1056 0.1168 0.1434 -0.0029 0.0010  -0.0026 160 VAL A C   
1271 O  O   . VAL A 159 ? 0.1034 0.1376 0.1504 -0.0102 0.0020  -0.0013 160 VAL A O   
1272 C  CB  . VAL A 159 ? 0.0977 0.1418 0.1082 -0.0093 -0.0412 -0.0089 160 VAL A CB  
1273 C  CG1 . VAL A 159 ? 0.0874 0.1987 0.1409 -0.0544 -0.0237 0.0376  160 VAL A CG1 
1274 C  CG2 . VAL A 159 ? 0.1483 0.1483 0.1340 0.0042  -0.0266 -0.0350 160 VAL A CG2 
1275 N  N   . VAL A 160 ? 0.1285 0.1055 0.1340 -0.0135 -0.0479 -0.0080 161 VAL A N   
1276 C  CA  . VAL A 160 ? 0.2191 0.1222 0.1664 0.0219  -0.0080 0.0091  161 VAL A CA  
1277 C  C   . VAL A 160 ? 0.1596 0.1154 0.1451 -0.0113 -0.0079 -0.0383 161 VAL A C   
1278 O  O   . VAL A 160 ? 0.1863 0.1412 0.1637 -0.0245 0.0192  -0.0181 161 VAL A O   
1279 C  CB  . VAL A 160 ? 0.3574 0.1174 0.1770 0.0075  0.0227  0.0242  161 VAL A CB  
1280 C  CG1 . VAL A 160 ? 0.3028 0.1239 0.2931 -0.0134 -0.0164 0.0034  161 VAL A CG1 
1281 C  CG2 . VAL A 160 ? 0.4332 0.1743 0.1673 0.0505  0.0700  0.0388  161 VAL A CG2 
1282 N  N   . ASP A 161 ? 0.1668 0.1599 0.1013 -0.0462 -0.0187 -0.0229 162 ASP A N   
1283 C  CA  . ASP A 161 ? 0.2235 0.2314 0.1059 -0.0977 -0.0144 0.0053  162 ASP A CA  
1284 C  C   . ASP A 161 ? 0.2431 0.2289 0.1111 -0.1099 -0.0248 0.0087  162 ASP A C   
1285 O  O   . ASP A 161 ? 0.3086 0.3168 0.1233 -0.1063 -0.0241 -0.0189 162 ASP A O   
1286 C  CB  . ASP A 161 ? 0.2404 0.3334 0.1669 -0.1131 -0.0422 -0.0085 162 ASP A CB  
1287 C  CG  . ASP A 161 ? 0.2832 0.3984 0.3984 -0.2132 -0.0557 -0.0342 162 ASP A CG  
1288 O  OD1 . ASP A 161 ? 0.3987 0.5180 0.3725 -0.0968 0.0890  0.0776  162 ASP A OD1 
1289 O  OD2 . ASP A 161 ? 0.2618 0.6282 0.3110 -0.1248 -0.0414 0.0502  162 ASP A OD2 
1290 N  N   . VAL A 162 ? 0.1671 0.1894 0.1317 -0.0647 -0.0149 0.0122  163 VAL A N   
1291 C  CA  . VAL A 162 ? 0.1777 0.1962 0.1420 -0.0741 -0.0372 0.0255  163 VAL A CA  
1292 C  C   . VAL A 162 ? 0.1718 0.1491 0.1357 -0.0447 0.0031  0.0156  163 VAL A C   
1293 O  O   . VAL A 162 ? 0.1810 0.1729 0.1567 -0.0452 0.0290  0.0160  163 VAL A O   
1294 C  CB  . VAL A 162 ? 0.1609 0.1628 0.2361 -0.0262 -0.0383 0.0585  163 VAL A CB  
1295 C  CG1 . VAL A 162 ? 0.1790 0.1474 0.2242 -0.0144 0.0119  -0.0067 163 VAL A CG1 
1296 C  CG2 . VAL A 162 ? 0.2220 0.3212 0.2478 -0.0140 0.0514  0.1258  163 VAL A CG2 
1297 N  N   . LEU A 163 ? 0.1527 0.1488 0.1461 -0.0370 -0.0189 -0.0018 164 LEU A N   
1298 C  CA  . LEU A 163 ? 0.1328 0.1624 0.0926 -0.0302 0.0288  0.0163  164 LEU A CA  
1299 C  C   . LEU A 163 ? 0.2009 0.1542 0.1014 -0.0303 0.0445  -0.0051 164 LEU A C   
1300 O  O   . LEU A 163 ? 0.1501 0.1698 0.1204 -0.0128 0.0433  0.0022  164 LEU A O   
1301 C  CB  . LEU A 163 ? 0.1492 0.1316 0.1065 0.0060  0.0312  0.0042  164 LEU A CB  
1302 C  CG  . LEU A 163 ? 0.1386 0.1380 0.0880 -0.0188 0.0210  0.0094  164 LEU A CG  
1303 C  CD1 . LEU A 163 ? 0.0833 0.1641 0.1756 0.0314  0.0074  0.0581  164 LEU A CD1 
1304 C  CD2 . LEU A 163 ? 0.1041 0.1721 0.1452 -0.0222 0.0368  -0.0347 164 LEU A CD2 
1305 N  N   . ASP A 164 ? 0.2244 0.2034 0.1287 -0.0394 0.0478  -0.0614 165 ASP A N   
1306 C  CA  . ASP A 164 ? 0.2813 0.2120 0.1083 -0.0345 0.0586  -0.0315 165 ASP A CA  
1307 C  C   . ASP A 164 ? 0.2454 0.2643 0.0969 -0.0359 0.0730  0.0006  165 ASP A C   
1308 O  O   . ASP A 164 ? 0.3110 0.3924 0.1980 -0.0222 0.1571  0.0023  165 ASP A O   
1309 C  CB  . ASP A 164 ? 0.3822 0.4221 0.1578 -0.1235 0.0745  -0.1328 165 ASP A CB  
1310 C  CG  . ASP A 164 ? 0.4832 0.5268 0.2611 -0.1456 0.0530  -0.0860 165 ASP A CG  
1311 O  OD1 . ASP A 164 ? 0.4855 0.4577 0.2519 -0.2097 0.0976  -0.0413 165 ASP A OD1 
1312 O  OD2 . ASP A 164 ? 0.6542 0.8543 0.2587 -0.1527 0.1679  -0.1356 165 ASP A OD2 
1313 N  N   . SER A 165 ? 0.1619 0.2465 0.1240 -0.0449 -0.0212 -0.0068 166 SER A N   
1314 C  CA  . SER A 165 ? 0.2045 0.2618 0.1368 -0.0554 -0.0272 -0.0004 166 SER A CA  
1315 C  C   . SER A 165 ? 0.1479 0.2083 0.0974 -0.0262 0.0155  0.0195  166 SER A C   
1316 O  O   . SER A 165 ? 0.2162 0.1966 0.1516 -0.0402 0.0134  0.0333  166 SER A O   
1317 C  CB  . SER A 165 ? 0.3144 0.2922 0.2856 0.0175  0.0776  0.1119  166 SER A CB  
1318 O  OG  . SER A 165 ? 0.2476 0.2795 0.3168 0.0381  -0.0211 0.0923  166 SER A OG  
1319 N  N   . ILE A 166 ? 0.1458 0.1610 0.0973 -0.0046 -0.0117 -0.0013 167 ILE A N   
1320 C  CA  . ILE A 166 ? 0.0892 0.1154 0.1547 -0.0094 0.0268  -0.0132 167 ILE A CA  
1321 C  C   . ILE A 166 ? 0.0648 0.1141 0.1089 -0.0078 0.0386  -0.0204 167 ILE A C   
1322 O  O   . ILE A 166 ? 0.1231 0.1326 0.1058 -0.0159 0.0431  -0.0150 167 ILE A O   
1323 C  CB  . ILE A 166 ? 0.0910 0.1225 0.1515 -0.0121 0.0414  -0.0063 167 ILE A CB  
1324 C  CG1 . ILE A 166 ? 0.1256 0.1524 0.0939 -0.0352 0.0157  -0.0008 167 ILE A CG1 
1325 C  CG2 . ILE A 166 ? 0.0851 0.1544 0.1918 -0.0066 0.0103  0.0006  167 ILE A CG2 
1326 C  CD1 . ILE A 166 ? 0.1613 0.1465 0.1092 -0.0345 0.0167  -0.0100 167 ILE A CD1 
1327 N  N   . LYS A 167 ? 0.1168 0.1251 0.1092 0.0070  0.0450  -0.0163 168 LYS A N   
1328 C  CA  . LYS A 167 ? 0.0633 0.1487 0.0935 0.0181  0.0256  -0.0298 168 LYS A CA  
1329 C  C   . LYS A 167 ? 0.0593 0.1316 0.1079 -0.0168 0.0413  0.0058  168 LYS A C   
1330 O  O   . LYS A 167 ? 0.0948 0.1405 0.1067 -0.0068 0.0174  0.0036  168 LYS A O   
1331 C  CB  . LYS A 167 ? 0.1749 0.1136 0.1163 0.0152  0.0361  -0.0358 168 LYS A CB  
1332 C  CG  . LYS A 167 ? 0.1878 0.1199 0.1858 0.0122  0.0048  -0.0277 168 LYS A CG  
1333 C  CD  . LYS A 167 ? 0.3198 0.1535 0.2095 0.0317  -0.0220 -0.0607 168 LYS A CD  
1334 C  CE  . LYS A 167 ? 0.4586 0.1565 0.2380 0.0581  -0.0093 -0.0485 168 LYS A CE  
1335 N  NZ  . LYS A 167 ? 0.5264 0.4052 0.4002 0.0797  0.0539  -0.2368 168 LYS A NZ  
1336 N  N   . THR A 168 ? 0.0838 0.1315 0.1289 -0.0190 0.0418  0.0125  169 THR A N   
1337 C  CA  . THR A 168 ? 0.0680 0.1311 0.1337 -0.0052 0.0574  -0.0081 169 THR A CA  
1338 C  C   . THR A 168 ? 0.0860 0.1122 0.1099 -0.0072 0.0608  0.0114  169 THR A C   
1339 O  O   . THR A 168 ? 0.0991 0.1054 0.1235 -0.0039 0.0583  0.0136  169 THR A O   
1340 C  CB  . THR A 168 ? 0.1049 0.1377 0.1286 0.0179  0.0659  0.0254  169 THR A CB  
1341 O  OG1 . THR A 168 ? 0.1289 0.1781 0.1341 0.0146  0.0526  0.0320  169 THR A OG1 
1342 C  CG2 . THR A 168 ? 0.1562 0.1650 0.1573 0.0238  0.0854  -0.0316 169 THR A CG2 
1343 N  N   A LYS A 169 ? 0.1122 0.1127 0.1048 -0.0469 0.0479  0.0182  170 LYS A N   
1344 N  N   B LYS A 169 ? 0.1064 0.1509 0.1011 -0.0378 0.0580  0.0042  170 LYS A N   
1345 C  CA  A LYS A 169 ? 0.0817 0.1201 0.1307 -0.0254 0.0221  -0.0011 170 LYS A CA  
1346 C  CA  B LYS A 169 ? 0.0978 0.1497 0.1077 -0.0150 0.0529  -0.0060 170 LYS A CA  
1347 C  C   A LYS A 169 ? 0.0531 0.1348 0.1339 -0.0237 0.0542  0.0116  170 LYS A C   
1348 C  C   B LYS A 169 ? 0.0606 0.1677 0.1210 -0.0124 0.0656  0.0115  170 LYS A C   
1349 O  O   A LYS A 169 ? 0.1101 0.1319 0.1267 -0.0505 0.0618  -0.0042 170 LYS A O   
1350 O  O   B LYS A 169 ? 0.1613 0.1900 0.1018 -0.0788 0.0741  0.0253  170 LYS A O   
1351 C  CB  A LYS A 169 ? 0.0912 0.1531 0.1140 -0.0144 0.0113  0.0033  170 LYS A CB  
1352 C  CB  B LYS A 169 ? 0.0991 0.1869 0.0998 0.0136  0.0567  0.0027  170 LYS A CB  
1353 C  CG  A LYS A 169 ? 0.0912 0.1768 0.1340 -0.0464 0.0152  -0.0060 170 LYS A CG  
1354 C  CG  B LYS A 169 ? 0.1059 0.2002 0.1304 -0.0232 0.0894  -0.0002 170 LYS A CG  
1355 C  CD  A LYS A 169 ? 0.0800 0.2133 0.2077 -0.0653 0.0001  -0.0183 170 LYS A CD  
1356 C  CD  B LYS A 169 ? 0.1222 0.2518 0.1943 -0.0078 0.0632  -0.0514 170 LYS A CD  
1357 C  CE  A LYS A 169 ? 0.1973 0.2931 0.2572 -0.1212 -0.0664 -0.0411 170 LYS A CE  
1358 C  CE  B LYS A 169 ? 0.0955 0.3273 0.2831 0.0353  0.0938  -0.0209 170 LYS A CE  
1359 N  N   . GLY A 170 ? 0.0763 0.1238 0.1307 -0.0173 0.0322  0.0011  171 GLY A N   
1360 C  CA  . GLY A 170 ? 0.0910 0.1225 0.2061 -0.0254 0.0314  0.0255  171 GLY A CA  
1361 C  C   . GLY A 170 ? 0.1161 0.1319 0.1614 0.0002  0.0557  0.0236  171 GLY A C   
1362 O  O   . GLY A 170 ? 0.1904 0.1254 0.2161 -0.0001 0.0397  0.0359  171 GLY A O   
1363 N  N   . LYS A 171 ? 0.0883 0.1344 0.1293 -0.0133 0.0613  0.0280  172 LYS A N   
1364 C  CA  . LYS A 171 ? 0.1152 0.1570 0.1530 0.0102  0.0398  0.0242  172 LYS A CA  
1365 C  C   . LYS A 171 ? 0.0937 0.1170 0.1041 -0.0100 0.0199  0.0331  172 LYS A C   
1366 O  O   . LYS A 171 ? 0.0952 0.1538 0.1095 0.0146  0.0357  0.0401  172 LYS A O   
1367 C  CB  . LYS A 171 ? 0.1093 0.1583 0.1477 -0.0057 0.0356  0.0157  172 LYS A CB  
1368 C  CG  . LYS A 171 ? 0.0939 0.2082 0.2414 -0.0022 0.0581  -0.0649 172 LYS A CG  
1369 C  CD  . LYS A 171 ? 0.2282 0.3517 0.3331 -0.0146 0.0245  -0.1527 172 LYS A CD  
1370 N  N   . SER A 172 ? 0.1318 0.1854 0.1111 0.0449  0.0236  0.0373  173 SER A N   
1371 C  CA  . SER A 172 ? 0.1368 0.1810 0.1340 0.0479  0.0279  0.0206  173 SER A CA  
1372 C  C   . SER A 172 ? 0.1359 0.1965 0.0973 0.0662  0.0511  0.0299  173 SER A C   
1373 O  O   . SER A 172 ? 0.1939 0.2752 0.0908 0.0746  0.0466  0.0346  173 SER A O   
1374 C  CB  . SER A 172 ? 0.1531 0.1903 0.1300 0.0306  0.0072  0.0238  173 SER A CB  
1375 O  OG  . SER A 172 ? 0.2098 0.1969 0.2055 0.0289  0.0100  0.0644  173 SER A OG  
1376 N  N   . ALA A 173 ? 0.1129 0.2461 0.1280 0.0908  0.0309  0.0419  174 ALA A N   
1377 C  CA  . ALA A 173 ? 0.1391 0.2310 0.1498 0.0630  -0.0038 0.0348  174 ALA A CA  
1378 C  C   . ALA A 173 ? 0.1095 0.2063 0.1000 0.0194  -0.0261 -0.0006 174 ALA A C   
1379 O  O   . ALA A 173 ? 0.1021 0.1609 0.1012 0.0370  -0.0080 0.0133  174 ALA A O   
1380 C  CB  . ALA A 173 ? 0.2083 0.2298 0.1872 0.0332  0.0204  0.0842  174 ALA A CB  
1381 N  N   . ASP A 174 ? 0.1644 0.2613 0.1279 0.0666  -0.0111 0.0560  175 ASP A N   
1382 C  CA  . ASP A 174 ? 0.1332 0.3359 0.1276 0.0653  -0.0117 0.0651  175 ASP A CA  
1383 C  C   . ASP A 174 ? 0.1237 0.2400 0.1680 0.0912  0.0071  0.0266  175 ASP A C   
1384 O  O   . ASP A 174 ? 0.1698 0.2658 0.2308 0.0544  0.0029  -0.0364 175 ASP A O   
1385 C  CB  . ASP A 174 ? 0.1587 0.4381 0.1720 0.1337  -0.0136 0.0914  175 ASP A CB  
1386 C  CG  . ASP A 174 ? 0.4360 0.5186 0.3542 -0.0212 -0.1149 0.1613  175 ASP A CG  
1387 O  OD1 . ASP A 174 ? 0.4943 0.6521 0.4130 -0.0324 -0.2073 0.0179  175 ASP A OD1 
1388 O  OD2 . ASP A 174 ? 0.6343 0.7309 0.3765 -0.0211 -0.1835 0.0409  175 ASP A OD2 
1389 N  N   . PHE A 175 ? 0.0854 0.2316 0.1541 0.0274  0.0205  0.0173  176 PHE A N   
1390 C  CA  . PHE A 175 ? 0.0713 0.1912 0.1644 0.0502  -0.0054 0.0372  176 PHE A CA  
1391 C  C   . PHE A 175 ? 0.1007 0.1562 0.1504 0.0257  0.0058  0.0237  176 PHE A C   
1392 O  O   . PHE A 175 ? 0.1559 0.2379 0.1626 0.1014  -0.0633 -0.0252 176 PHE A O   
1393 C  CB  . PHE A 175 ? 0.0989 0.1397 0.1897 0.0241  -0.0254 0.0475  176 PHE A CB  
1394 C  CG  . PHE A 175 ? 0.1039 0.1279 0.1885 0.0050  -0.0328 0.0064  176 PHE A CG  
1395 C  CD1 . PHE A 175 ? 0.0809 0.1441 0.1621 -0.0025 -0.0245 0.0059  176 PHE A CD1 
1396 C  CD2 . PHE A 175 ? 0.0895 0.1551 0.1840 0.0142  -0.0275 0.0295  176 PHE A CD2 
1397 C  CE1 . PHE A 175 ? 0.1725 0.1251 0.1548 0.0157  -0.0009 0.0145  176 PHE A CE1 
1398 C  CE2 . PHE A 175 ? 0.1125 0.1477 0.1803 0.0086  -0.0190 0.0171  176 PHE A CE2 
1399 C  CZ  . PHE A 175 ? 0.1230 0.1599 0.1463 0.0163  -0.0244 0.0306  176 PHE A CZ  
1400 N  N   . THR A 176 ? 0.1420 0.1892 0.1373 0.0337  -0.0219 0.0258  177 THR A N   
1401 C  CA  . THR A 176 ? 0.1065 0.1689 0.1531 0.0212  -0.0076 0.0483  177 THR A CA  
1402 C  C   . THR A 176 ? 0.0964 0.1372 0.1102 0.0190  -0.0368 0.0204  177 THR A C   
1403 O  O   . THR A 176 ? 0.1613 0.1375 0.1261 0.0231  -0.0345 0.0164  177 THR A O   
1404 C  CB  . THR A 176 ? 0.1058 0.1986 0.1445 -0.0093 -0.0303 0.0619  177 THR A CB  
1405 O  OG1 . THR A 176 ? 0.2939 0.2572 0.1186 0.0763  -0.0237 0.0408  177 THR A OG1 
1406 C  CG2 . THR A 176 ? 0.1553 0.2375 0.2864 -0.0388 -0.0114 0.0994  177 THR A CG2 
1407 N  N   . ASN A 177 ? 0.1207 0.1491 0.1009 -0.0039 -0.0134 0.0216  178 ASN A N   
1408 C  CA  . ASN A 177 ? 0.1355 0.1804 0.0942 -0.0280 -0.0315 0.0671  178 ASN A CA  
1409 C  C   . ASN A 177 ? 0.1110 0.1519 0.1265 -0.0030 -0.0357 0.0428  178 ASN A C   
1410 O  O   . ASN A 177 ? 0.1402 0.1754 0.2855 -0.0310 -0.0860 0.0857  178 ASN A O   
1411 C  CB  . ASN A 177 ? 0.1206 0.1463 0.1620 -0.0082 -0.0683 0.0402  178 ASN A CB  
1412 C  CG  . ASN A 177 ? 0.1095 0.1745 0.1936 0.0351  -0.0271 0.0691  178 ASN A CG  
1413 O  OD1 . ASN A 177 ? 0.1402 0.2073 0.2505 0.0392  -0.0033 0.0513  178 ASN A OD1 
1414 N  ND2 . ASN A 177 ? 0.1058 0.2001 0.1955 -0.0182 -0.0389 0.1093  178 ASN A ND2 
1415 N  N   . PHE A 178 ? 0.1084 0.1616 0.0786 -0.0002 -0.0170 0.0529  179 PHE A N   
1416 C  CA  . PHE A 178 ? 0.1128 0.1682 0.0879 -0.0017 -0.0308 0.0550  179 PHE A CA  
1417 C  C   . PHE A 178 ? 0.1321 0.1402 0.0873 -0.0124 -0.0368 0.0414  179 PHE A C   
1418 O  O   . PHE A 178 ? 0.1337 0.1653 0.1254 -0.0498 -0.0206 0.0212  179 PHE A O   
1419 C  CB  . PHE A 178 ? 0.1163 0.1585 0.1140 0.0077  -0.0218 0.0567  179 PHE A CB  
1420 C  CG  . PHE A 178 ? 0.1282 0.1250 0.1285 0.0076  -0.0318 0.0401  179 PHE A CG  
1421 C  CD1 . PHE A 178 ? 0.1146 0.1355 0.1425 -0.0032 -0.0163 0.0347  179 PHE A CD1 
1422 C  CD2 . PHE A 178 ? 0.0842 0.1512 0.1196 0.0159  -0.0044 0.0550  179 PHE A CD2 
1423 C  CE1 . PHE A 178 ? 0.1469 0.1469 0.1393 -0.0024 -0.0400 0.0366  179 PHE A CE1 
1424 C  CE2 . PHE A 178 ? 0.0540 0.1377 0.1427 -0.0122 -0.0134 0.0563  179 PHE A CE2 
1425 C  CZ  . PHE A 178 ? 0.0761 0.1620 0.1301 -0.0217 -0.0129 0.0528  179 PHE A CZ  
1426 N  N   . ASP A 179 ? 0.1127 0.1650 0.0976 -0.0082 -0.0232 0.0482  180 ASP A N   
1427 C  CA  . ASP A 179 ? 0.0686 0.1574 0.1154 -0.0054 -0.0258 0.0411  180 ASP A CA  
1428 C  C   . ASP A 179 ? 0.0630 0.1716 0.1164 0.0013  -0.0175 0.0432  180 ASP A C   
1429 O  O   . ASP A 179 ? 0.0698 0.1702 0.1505 -0.0193 -0.0055 0.0392  180 ASP A O   
1430 C  CB  . ASP A 179 ? 0.0591 0.2303 0.1892 0.0079  -0.0339 0.0375  180 ASP A CB  
1431 C  CG  . ASP A 179 ? 0.0863 0.3225 0.2020 0.0201  -0.0348 0.0158  180 ASP A CG  
1432 O  OD1 . ASP A 179 ? 0.0811 0.2155 0.1718 0.0084  0.0029  0.0277  180 ASP A OD1 
1433 O  OD2 . ASP A 179 ? 0.0858 0.5283 0.3413 0.0142  -0.0537 -0.0544 180 ASP A OD2 
1434 N  N   . PRO A 180 ? 0.0759 0.1436 0.1225 0.0128  -0.0177 0.0189  181 PRO A N   
1435 C  CA  . PRO A 180 ? 0.0727 0.1412 0.1301 -0.0226 -0.0234 0.0431  181 PRO A CA  
1436 C  C   . PRO A 180 ? 0.0562 0.1494 0.1073 -0.0032 -0.0175 0.0211  181 PRO A C   
1437 O  O   . PRO A 180 ? 0.0741 0.1450 0.1201 0.0005  -0.0175 0.0220  181 PRO A O   
1438 C  CB  . PRO A 180 ? 0.0745 0.1423 0.1736 -0.0323 -0.0020 0.0280  181 PRO A CB  
1439 C  CG  . PRO A 180 ? 0.0865 0.1468 0.1437 -0.0162 -0.0239 0.0063  181 PRO A CG  
1440 C  CD  . PRO A 180 ? 0.1061 0.1527 0.1477 -0.0203 -0.0414 0.0219  181 PRO A CD  
1441 N  N   . ARG A 181 ? 0.0524 0.1337 0.1499 -0.0094 -0.0063 0.0318  182 ARG A N   
1442 C  CA  . ARG A 181 ? 0.0389 0.1585 0.1632 0.0093  0.0228  0.0172  182 ARG A CA  
1443 C  C   . ARG A 181 ? 0.0411 0.1570 0.1159 0.0003  -0.0085 0.0222  182 ARG A C   
1444 O  O   . ARG A 181 ? 0.0781 0.1753 0.1466 0.0094  -0.0058 0.0373  182 ARG A O   
1445 C  CB  . ARG A 181 ? 0.0549 0.1646 0.1754 0.0248  0.0150  0.0124  182 ARG A CB  
1446 C  CG  . ARG A 181 ? 0.1163 0.1671 0.2020 0.0326  0.0109  -0.0135 182 ARG A CG  
1447 C  CD  . ARG A 181 ? 0.1170 0.2030 0.2162 0.0479  0.0207  0.0445  182 ARG A CD  
1448 N  NE  . ARG A 181 ? 0.1056 0.1937 0.2458 0.0357  0.0091  0.0820  182 ARG A NE  
1449 C  CZ  . ARG A 181 ? 0.1718 0.2730 0.2724 0.1178  -0.0182 0.0254  182 ARG A CZ  
1450 N  NH1 . ARG A 181 ? 0.1937 0.4160 0.4279 0.1322  0.0978  0.0103  182 ARG A NH1 
1451 N  NH2 . ARG A 181 ? 0.1497 0.3633 0.2910 0.1218  0.0092  0.0697  182 ARG A NH2 
1452 N  N   . GLY A 182 ? 0.0618 0.1401 0.1533 0.0105  -0.0122 -0.0168 183 GLY A N   
1453 C  CA  . GLY A 182 ? 0.0686 0.1240 0.1573 0.0011  -0.0370 0.0108  183 GLY A CA  
1454 C  C   . GLY A 182 ? 0.0558 0.1440 0.1504 0.0109  -0.0210 0.0067  183 GLY A C   
1455 O  O   . GLY A 182 ? 0.1093 0.1535 0.2174 0.0121  -0.0658 -0.0022 183 GLY A O   
1456 N  N   . LEU A 183 ? 0.0476 0.1786 0.1065 0.0050  -0.0141 0.0259  184 LEU A N   
1457 C  CA  . LEU A 183 ? 0.0391 0.1585 0.1372 -0.0002 -0.0052 0.0361  184 LEU A CA  
1458 C  C   . LEU A 183 ? 0.0427 0.1366 0.1328 0.0016  -0.0122 0.0242  184 LEU A C   
1459 O  O   . LEU A 183 ? 0.0662 0.1757 0.1583 0.0350  0.0012  0.0479  184 LEU A O   
1460 C  CB  . LEU A 183 ? 0.0336 0.1800 0.1348 -0.0030 -0.0094 0.0340  184 LEU A CB  
1461 C  CG  . LEU A 183 ? 0.0655 0.1878 0.1333 0.0029  -0.0131 0.0299  184 LEU A CG  
1462 C  CD1 . LEU A 183 ? 0.0651 0.2460 0.1490 -0.0174 -0.0422 0.0968  184 LEU A CD1 
1463 C  CD2 . LEU A 183 ? 0.1714 0.2030 0.1757 0.0324  0.0175  0.0032  184 LEU A CD2 
1464 N  N   . LEU A 184 ? 0.0472 0.1476 0.1285 -0.0018 -0.0040 0.0266  185 LEU A N   
1465 C  CA  . LEU A 184 ? 0.0534 0.1477 0.1337 -0.0171 0.0154  0.0445  185 LEU A CA  
1466 C  C   . LEU A 184 ? 0.0393 0.1547 0.1807 -0.0265 -0.0420 0.0543  185 LEU A C   
1467 O  O   . LEU A 184 ? 0.1294 0.2433 0.2220 -0.0944 -0.1164 0.1041  185 LEU A O   
1468 C  CB  . LEU A 184 ? 0.0443 0.1768 0.1337 -0.0150 0.0070  0.0055  185 LEU A CB  
1469 C  CG  . LEU A 184 ? 0.0337 0.1826 0.1930 -0.0049 0.0016  0.0046  185 LEU A CG  
1470 C  CD1 . LEU A 184 ? 0.1304 0.1966 0.2088 0.0326  0.0548  0.0248  185 LEU A CD1 
1471 C  CD2 . LEU A 184 ? 0.0759 0.2331 0.2229 0.0006  -0.0588 -0.0434 185 LEU A CD2 
1472 N  N   . PRO A 185 ? 0.0097 0.1416 0.1470 -0.0182 -0.0148 0.0267  186 PRO A N   
1473 C  CA  . PRO A 185 ? 0.0190 0.1494 0.1548 -0.0232 -0.0080 0.0386  186 PRO A CA  
1474 C  C   . PRO A 185 ? 0.0400 0.1146 0.1883 -0.0135 -0.0122 0.0168  186 PRO A C   
1475 O  O   . PRO A 185 ? 0.0209 0.1168 0.2429 0.0110  -0.0208 0.0320  186 PRO A O   
1476 C  CB  . PRO A 185 ? 0.0287 0.1499 0.1235 -0.0031 -0.0016 0.0040  186 PRO A CB  
1477 C  CG  . PRO A 185 ? 0.0306 0.1418 0.0912 0.0064  -0.0034 0.0034  186 PRO A CG  
1478 C  CD  . PRO A 185 ? 0.0075 0.1402 0.1016 -0.0093 0.0066  0.0072  186 PRO A CD  
1479 N  N   A GLU A 186 ? 0.0519 0.1691 0.2203 -0.0455 0.0017  0.0275  187 GLU A N   
1480 N  N   B GLU A 186 ? 0.0434 0.1472 0.2166 -0.0313 -0.0044 0.0264  187 GLU A N   
1481 C  CA  A GLU A 186 ? 0.0400 0.2210 0.2454 -0.0318 -0.0067 0.0275  187 GLU A CA  
1482 C  CA  B GLU A 186 ? 0.0273 0.1724 0.2364 -0.0340 -0.0162 0.0086  187 GLU A CA  
1483 C  C   A GLU A 186 ? 0.0719 0.1711 0.1937 -0.0427 0.0155  0.0632  187 GLU A C   
1484 C  C   B GLU A 186 ? 0.0251 0.1333 0.2009 -0.0326 0.0242  0.0281  187 GLU A C   
1485 O  O   A GLU A 186 ? 0.1164 0.1890 0.2964 -0.0019 0.0064  0.0348  187 GLU A O   
1486 O  O   B GLU A 186 ? 0.0437 0.1936 0.2203 0.0286  -0.0205 -0.0131 187 GLU A O   
1487 C  CB  A GLU A 186 ? 0.1016 0.2332 0.3288 -0.0629 -0.0052 0.0237  187 GLU A CB  
1488 C  CB  B GLU A 186 ? 0.0553 0.1861 0.2735 -0.0466 -0.0047 0.0239  187 GLU A CB  
1489 C  CG  A GLU A 186 ? 0.0754 0.2709 0.4442 -0.0479 0.0168  -0.0001 187 GLU A CG  
1490 C  CG  B GLU A 186 ? 0.0833 0.1822 0.3528 -0.0281 -0.0595 -0.0008 187 GLU A CG  
1491 C  CD  A GLU A 186 ? 0.0953 0.2637 0.4437 -0.0218 -0.0318 0.0971  187 GLU A CD  
1492 C  CD  B GLU A 186 ? 0.0392 0.1784 0.4528 -0.0046 -0.0726 0.0358  187 GLU A CD  
1493 O  OE1 A GLU A 186 ? 0.1508 0.3046 0.5057 -0.0603 0.0277  0.0306  187 GLU A OE1 
1494 O  OE1 B GLU A 186 ? 0.3541 0.2353 0.4647 -0.1117 -0.0585 0.0749  187 GLU A OE1 
1495 O  OE2 A GLU A 186 ? 0.1831 0.3453 0.4536 0.0030  0.0171  0.0618  187 GLU A OE2 
1496 O  OE2 B GLU A 186 ? 0.1594 0.2252 0.3930 -0.0402 -0.0504 0.0211  187 GLU A OE2 
1497 N  N   . SER A 187 ? 0.0179 0.1850 0.1696 -0.0419 0.0013  0.0105  188 SER A N   
1498 C  CA  . SER A 187 ? 0.0284 0.1516 0.1994 -0.0361 -0.0074 0.0017  188 SER A CA  
1499 C  C   . SER A 187 ? 0.0189 0.2011 0.1387 -0.0422 0.0226  -0.0071 188 SER A C   
1500 O  O   . SER A 187 ? 0.0137 0.2242 0.1743 -0.0334 0.0233  -0.0239 188 SER A O   
1501 C  CB  . SER A 187 ? 0.0685 0.2030 0.1641 -0.0260 0.0033  0.0250  188 SER A CB  
1502 O  OG  . SER A 187 ? 0.0917 0.1908 0.2100 -0.0439 0.0250  -0.0057 188 SER A OG  
1503 N  N   . LEU A 188 ? 0.0108 0.1805 0.1858 -0.0280 0.0001  -0.0131 189 LEU A N   
1504 C  CA  . LEU A 188 ? 0.0164 0.1635 0.1678 -0.0385 -0.0126 0.0100  189 LEU A CA  
1505 C  C   . LEU A 188 ? 0.0074 0.1400 0.1463 0.0005  0.0052  -0.0244 189 LEU A C   
1506 O  O   . LEU A 188 ? 0.0400 0.1734 0.1664 -0.0274 -0.0135 -0.0262 189 LEU A O   
1507 C  CB  . LEU A 188 ? 0.0529 0.1588 0.1926 -0.0243 -0.0086 0.0126  189 LEU A CB  
1508 C  CG  . LEU A 188 ? 0.0297 0.1951 0.2192 -0.0011 -0.0026 0.0331  189 LEU A CG  
1509 C  CD1 . LEU A 188 ? 0.1344 0.1942 0.2763 0.0162  -0.0569 0.0705  189 LEU A CD1 
1510 C  CD2 . LEU A 188 ? 0.0323 0.2917 0.2263 -0.0348 0.0190  0.0318  189 LEU A CD2 
1511 N  N   . ASP A 189 ? 0.0274 0.1700 0.1409 -0.0040 0.0497  -0.0048 190 ASP A N   
1512 C  CA  . ASP A 189 ? 0.0380 0.2318 0.1319 -0.0120 0.0601  0.0267  190 ASP A CA  
1513 C  C   . ASP A 189 ? 0.0300 0.1491 0.1405 -0.0134 0.0560  -0.0176 190 ASP A C   
1514 O  O   . ASP A 189 ? 0.0142 0.1423 0.1128 -0.0210 0.0244  -0.0158 190 ASP A O   
1515 C  CB  . ASP A 189 ? 0.0621 0.2509 0.1380 -0.0601 0.0190  0.0523  190 ASP A CB  
1516 C  CG  . ASP A 189 ? 0.0661 0.4120 0.1939 -0.0476 0.0528  0.0009  190 ASP A CG  
1517 O  OD1 . ASP A 189 ? 0.1448 0.4128 0.3201 -0.0710 0.1322  -0.0583 190 ASP A OD1 
1518 O  OD2 . ASP A 189 ? 0.2559 0.5004 0.3370 -0.1362 0.0435  0.1452  190 ASP A OD2 
1519 N  N   . TYR A 190 ? 0.0273 0.1382 0.1376 -0.0121 0.0504  0.0062  191 TYR A N   
1520 C  CA  . TYR A 190 ? 0.0199 0.1197 0.0993 -0.0047 0.0342  0.0151  191 TYR A CA  
1521 C  C   . TYR A 190 ? 0.0232 0.1334 0.0930 0.0067  0.0379  0.0016  191 TYR A C   
1522 O  O   . TYR A 190 ? 0.0310 0.1552 0.1095 0.0054  0.0502  -0.0005 191 TYR A O   
1523 C  CB  . TYR A 190 ? 0.0362 0.1040 0.1143 0.0069  0.0484  0.0138  191 TYR A CB  
1524 C  CG  . TYR A 190 ? 0.0251 0.1067 0.1120 -0.0104 0.0222  0.0022  191 TYR A CG  
1525 C  CD1 . TYR A 190 ? 0.0163 0.1140 0.1369 -0.0135 0.0231  -0.0041 191 TYR A CD1 
1526 C  CD2 . TYR A 190 ? 0.0327 0.1499 0.1305 0.0094  0.0341  -0.0091 191 TYR A CD2 
1527 C  CE1 . TYR A 190 ? 0.0403 0.1210 0.1286 0.0005  0.0129  -0.0073 191 TYR A CE1 
1528 C  CE2 . TYR A 190 ? 0.0531 0.1472 0.1265 0.0098  -0.0018 -0.0130 191 TYR A CE2 
1529 C  CZ  . TYR A 190 ? 0.0515 0.1580 0.1023 0.0171  -0.0040 -0.0102 191 TYR A CZ  
1530 O  OH  . TYR A 190 ? 0.0752 0.1481 0.1512 0.0160  0.0095  -0.0260 191 TYR A OH  
1531 N  N   . TRP A 191 ? 0.0101 0.1013 0.0861 -0.0012 0.0173  -0.0086 192 TRP A N   
1532 C  CA  . TRP A 191 ? 0.0103 0.1108 0.0924 -0.0059 0.0182  -0.0086 192 TRP A CA  
1533 C  C   . TRP A 191 ? 0.0191 0.1118 0.0716 -0.0059 0.0240  -0.0034 192 TRP A C   
1534 O  O   . TRP A 191 ? 0.0442 0.1301 0.0734 -0.0110 0.0143  -0.0109 192 TRP A O   
1535 C  CB  . TRP A 191 ? 0.0242 0.1086 0.1097 0.0033  0.0230  0.0004  192 TRP A CB  
1536 C  CG  . TRP A 191 ? 0.0194 0.0965 0.1047 0.0249  0.0236  -0.0030 192 TRP A CG  
1537 C  CD1 . TRP A 191 ? 0.0607 0.1129 0.1251 0.0209  0.0314  0.0205  192 TRP A CD1 
1538 C  CD2 . TRP A 191 ? 0.0209 0.1058 0.1041 0.0161  0.0070  0.0033  192 TRP A CD2 
1539 N  NE1 . TRP A 191 ? 0.0801 0.1124 0.1217 0.0108  0.0350  0.0091  192 TRP A NE1 
1540 C  CE2 . TRP A 191 ? 0.0357 0.1037 0.1235 0.0386  0.0228  0.0164  192 TRP A CE2 
1541 C  CE3 . TRP A 191 ? 0.0205 0.1423 0.1127 0.0250  0.0219  -0.0322 192 TRP A CE3 
1542 C  CZ2 . TRP A 191 ? 0.0694 0.1316 0.1563 0.0125  0.0167  0.0027  192 TRP A CZ2 
1543 C  CZ3 . TRP A 191 ? 0.0440 0.1359 0.1504 0.0050  0.0262  -0.0244 192 TRP A CZ3 
1544 C  CH2 . TRP A 191 ? 0.0612 0.1452 0.1678 0.0030  -0.0069 -0.0153 192 TRP A CH2 
1545 N  N   . THR A 192 ? 0.0078 0.1189 0.0812 -0.0025 0.0101  0.0051  193 THR A N   
1546 C  CA  . THR A 192 ? 0.0086 0.1043 0.0929 0.0063  0.0125  -0.0046 193 THR A CA  
1547 C  C   . THR A 192 ? 0.0179 0.1099 0.0885 -0.0034 0.0063  0.0242  193 THR A C   
1548 O  O   . THR A 192 ? 0.0321 0.1330 0.0757 0.0111  0.0102  0.0055  193 THR A O   
1549 C  CB  . THR A 192 ? 0.0317 0.1201 0.0865 0.0212  0.0431  0.0103  193 THR A CB  
1550 O  OG1 . THR A 192 ? 0.0290 0.1107 0.1301 0.0105  0.0195  0.0080  193 THR A OG1 
1551 C  CG2 . THR A 192 ? 0.0470 0.1627 0.0782 0.0390  0.0421  -0.0026 193 THR A CG2 
1552 N  N   . TYR A 193 ? 0.0080 0.1055 0.0883 -0.0023 0.0119  -0.0139 194 TYR A N   
1553 C  CA  . TYR A 193 ? 0.0100 0.1221 0.1071 0.0202  0.0026  -0.0072 194 TYR A CA  
1554 C  C   . TYR A 193 ? 0.0116 0.1074 0.0829 0.0217  -0.0088 -0.0234 194 TYR A C   
1555 O  O   . TYR A 193 ? 0.0072 0.1037 0.0897 -0.0075 -0.0047 0.0001  194 TYR A O   
1556 C  CB  . TYR A 193 ? 0.0375 0.1012 0.0765 0.0292  0.0168  -0.0130 194 TYR A CB  
1557 C  CG  . TYR A 193 ? 0.0170 0.0941 0.0763 0.0241  0.0077  -0.0194 194 TYR A CG  
1558 C  CD1 . TYR A 193 ? 0.0277 0.0800 0.0700 0.0176  0.0073  -0.0104 194 TYR A CD1 
1559 C  CD2 . TYR A 193 ? 0.0203 0.0980 0.0890 0.0256  0.0150  -0.0269 194 TYR A CD2 
1560 C  CE1 . TYR A 193 ? 0.0107 0.0797 0.0828 0.0059  0.0170  -0.0026 194 TYR A CE1 
1561 C  CE2 . TYR A 193 ? 0.0293 0.0714 0.0777 0.0015  0.0131  -0.0297 194 TYR A CE2 
1562 C  CZ  . TYR A 193 ? 0.0072 0.0724 0.0743 0.0032  0.0061  -0.0128 194 TYR A CZ  
1563 O  OH  . TYR A 193 ? 0.0163 0.0765 0.0881 0.0091  0.0242  -0.0016 194 TYR A OH  
1564 N  N   . PRO A 194 ? 0.0073 0.1529 0.0827 0.0110  -0.0049 -0.0218 195 PRO A N   
1565 C  CA  . PRO A 194 ? 0.0081 0.1210 0.1310 0.0140  -0.0021 -0.0356 195 PRO A CA  
1566 C  C   . PRO A 194 ? 0.0086 0.0709 0.1190 0.0107  -0.0131 -0.0391 195 PRO A C   
1567 O  O   . PRO A 194 ? 0.0137 0.1147 0.1106 0.0245  -0.0017 -0.0122 195 PRO A O   
1568 C  CB  . PRO A 194 ? 0.0177 0.1346 0.1125 -0.0068 0.0039  -0.0295 195 PRO A CB  
1569 C  CG  . PRO A 194 ? 0.0588 0.1984 0.0562 -0.0357 0.0027  -0.0409 195 PRO A CG  
1570 C  CD  . PRO A 194 ? 0.0349 0.1745 0.0795 -0.0128 -0.0032 -0.0495 195 PRO A CD  
1571 N  N   . GLY A 195 ? 0.0063 0.1048 0.1191 0.0010  0.0014  -0.0316 196 GLY A N   
1572 C  CA  . GLY A 195 ? 0.0105 0.1480 0.1099 0.0070  0.0198  -0.0036 196 GLY A CA  
1573 C  C   . GLY A 195 ? 0.0071 0.0941 0.0880 -0.0019 -0.0069 -0.0215 196 GLY A C   
1574 O  O   . GLY A 195 ? 0.0071 0.0872 0.0939 -0.0008 0.0081  -0.0182 196 GLY A O   
1575 N  N   . SER A 196 ? 0.0094 0.1018 0.0750 0.0018  0.0142  -0.0054 197 SER A N   
1576 C  CA  . SER A 196 ? 0.0106 0.1124 0.0814 0.0032  0.0174  -0.0054 197 SER A CA  
1577 C  C   . SER A 196 ? 0.0118 0.0685 0.0908 0.0140  0.0102  -0.0161 197 SER A C   
1578 O  O   . SER A 196 ? 0.0079 0.0867 0.1065 0.0079  0.0070  -0.0159 197 SER A O   
1579 C  CB  . SER A 196 ? 0.0065 0.1110 0.1344 0.0048  -0.0028 -0.0344 197 SER A CB  
1580 O  OG  . SER A 196 ? 0.0063 0.1038 0.1240 0.0009  0.0000  -0.0256 197 SER A OG  
1581 N  N   . LEU A 197 ? 0.0071 0.0917 0.0890 0.0053  0.0052  -0.0141 198 LEU A N   
1582 C  CA  . LEU A 197 ? 0.0087 0.0824 0.0935 -0.0031 0.0144  -0.0134 198 LEU A CA  
1583 C  C   . LEU A 197 ? 0.0084 0.0832 0.0971 -0.0011 0.0136  -0.0055 198 LEU A C   
1584 O  O   . LEU A 197 ? 0.0069 0.1297 0.1208 -0.0021 0.0083  -0.0289 198 LEU A O   
1585 C  CB  . LEU A 197 ? 0.0081 0.1115 0.1479 -0.0025 0.0144  0.0268  198 LEU A CB  
1586 C  CG  . LEU A 197 ? 0.0389 0.0907 0.1207 -0.0146 0.0091  0.0208  198 LEU A CG  
1587 C  CD1 . LEU A 197 ? 0.0804 0.1244 0.1474 -0.0691 0.0049  0.0165  198 LEU A CD1 
1588 C  CD2 . LEU A 197 ? 0.0188 0.1361 0.1483 0.0074  0.0280  0.0234  198 LEU A CD2 
1589 N  N   . THR A 198 ? 0.0077 0.0932 0.1051 -0.0011 0.0118  -0.0148 199 THR A N   
1590 C  CA  . THR A 198 ? 0.0133 0.0827 0.0994 -0.0063 0.0246  -0.0026 199 THR A CA  
1591 C  C   . THR A 198 ? 0.0094 0.0911 0.0865 -0.0078 0.0154  -0.0235 199 THR A C   
1592 O  O   . THR A 198 ? 0.0107 0.1119 0.1243 0.0064  0.0201  -0.0187 199 THR A O   
1593 C  CB  . THR A 198 ? 0.0095 0.0878 0.0788 -0.0061 0.0149  -0.0104 199 THR A CB  
1594 O  OG1 . THR A 198 ? 0.0106 0.1005 0.0757 0.0012  0.0172  0.0051  199 THR A OG1 
1595 C  CG2 . THR A 198 ? 0.0199 0.1044 0.0917 0.0173  0.0280  -0.0106 199 THR A CG2 
1596 N  N   . THR A 199 ? 0.0167 0.1010 0.1180 -0.0094 0.0330  -0.0071 200 THR A N   
1597 C  CA  . THR A 199 ? 0.0207 0.1068 0.1030 -0.0150 0.0362  -0.0167 200 THR A CA  
1598 C  C   . THR A 199 ? 0.0144 0.1279 0.1427 -0.0230 0.0239  -0.0083 200 THR A C   
1599 O  O   . THR A 199 ? 0.0094 0.1100 0.1500 -0.0042 0.0205  0.0000  200 THR A O   
1600 C  CB  . THR A 199 ? 0.0458 0.1235 0.1172 -0.0251 0.0020  -0.0124 200 THR A CB  
1601 O  OG1 . THR A 199 ? 0.1372 0.1574 0.1871 0.0155  -0.0121 -0.0196 200 THR A OG1 
1602 C  CG2 . THR A 199 ? 0.0220 0.1559 0.1265 -0.0432 0.0063  -0.0190 200 THR A CG2 
1603 N  N   . PRO A 200 ? 0.0174 0.1222 0.1509 -0.0243 0.0312  -0.0080 201 PRO A N   
1604 C  CA  . PRO A 200 ? 0.0205 0.1265 0.1656 -0.0252 0.0374  0.0008  201 PRO A CA  
1605 C  C   . PRO A 200 ? 0.0432 0.1222 0.1526 -0.0234 0.0425  0.0023  201 PRO A C   
1606 O  O   . PRO A 200 ? 0.0776 0.1346 0.1499 -0.0179 0.0353  0.0004  201 PRO A O   
1607 C  CB  . PRO A 200 ? 0.0211 0.1481 0.1930 -0.0032 0.0506  -0.0201 201 PRO A CB  
1608 C  CG  . PRO A 200 ? 0.0142 0.1568 0.1644 -0.0307 0.0216  -0.0283 201 PRO A CG  
1609 C  CD  . PRO A 200 ? 0.0149 0.1340 0.1657 -0.0250 0.0279  -0.0206 201 PRO A CD  
1610 N  N   . PRO A 201 ? 0.0159 0.1394 0.1678 -0.0245 0.0289  -0.0028 202 PRO A N   
1611 C  CA  . PRO A 201 ? 0.0534 0.1369 0.1596 -0.0652 0.0316  -0.0074 202 PRO A CA  
1612 C  C   . PRO A 201 ? 0.0125 0.1166 0.1515 -0.0108 0.0266  0.0049  202 PRO A C   
1613 O  O   . PRO A 201 ? 0.0206 0.1264 0.1763 -0.0168 0.0052  -0.0058 202 PRO A O   
1614 C  CB  . PRO A 201 ? 0.1005 0.1364 0.2001 -0.0133 0.0446  0.0029  202 PRO A CB  
1615 C  CG  . PRO A 201 ? 0.1268 0.1111 0.2477 -0.0313 -0.0171 0.0087  202 PRO A CG  
1616 C  CD  . PRO A 201 ? 0.0609 0.1201 0.1926 -0.0111 0.0229  0.0046  202 PRO A CD  
1617 N  N   . LEU A 202 ? 0.0115 0.0856 0.1597 -0.0035 0.0270  0.0130  203 LEU A N   
1618 C  CA  . LEU A 202 ? 0.0070 0.0624 0.1355 -0.0047 0.0068  -0.0075 203 LEU A CA  
1619 C  C   . LEU A 202 ? 0.0099 0.0833 0.1766 -0.0159 0.0144  -0.0351 203 LEU A C   
1620 O  O   . LEU A 202 ? 0.0074 0.1117 0.1692 -0.0074 0.0113  -0.0320 203 LEU A O   
1621 C  CB  . LEU A 202 ? 0.0063 0.0787 0.1836 0.0006  -0.0010 -0.0199 203 LEU A CB  
1622 C  CG  . LEU A 202 ? 0.0068 0.0826 0.1675 0.0049  -0.0061 -0.0214 203 LEU A CG  
1623 C  CD1 . LEU A 202 ? 0.0114 0.1546 0.2084 0.0272  -0.0066 -0.0178 203 LEU A CD1 
1624 C  CD2 . LEU A 202 ? 0.0096 0.1152 0.1479 -0.0187 0.0105  -0.0426 203 LEU A CD2 
1625 N  N   . THR A 203 ? 0.0100 0.0767 0.2046 -0.0024 0.0268  -0.0331 204 THR A N   
1626 C  CA  . THR A 203 ? 0.0130 0.0837 0.2050 -0.0044 0.0293  -0.0298 204 THR A CA  
1627 C  C   . THR A 203 ? 0.0088 0.0794 0.1624 -0.0126 0.0145  -0.0497 204 THR A C   
1628 O  O   . THR A 203 ? 0.0076 0.0915 0.1635 -0.0088 -0.0038 -0.0351 204 THR A O   
1629 C  CB  . THR A 203 ? 0.0790 0.0894 0.2140 0.0067  0.0567  0.0053  204 THR A CB  
1630 O  OG1 . THR A 203 ? 0.0955 0.1199 0.2831 0.0102  0.0988  0.0254  204 THR A OG1 
1631 C  CG2 . THR A 203 ? 0.0891 0.1115 0.3018 0.0111  0.0528  -0.0383 204 THR A CG2 
1632 N  N   . GLU A 204 ? 0.0348 0.1034 0.1463 0.0043  0.0124  -0.0488 205 GLU A N   
1633 C  CA  . GLU A 204 ? 0.0238 0.1129 0.1158 0.0131  -0.0162 -0.0456 205 GLU A CA  
1634 C  C   . GLU A 204 ? 0.0387 0.1240 0.1487 0.0292  -0.0236 -0.0121 205 GLU A C   
1635 O  O   . GLU A 204 ? 0.0687 0.1960 0.1847 0.0544  -0.0584 -0.0526 205 GLU A O   
1636 C  CB  . GLU A 204 ? 0.0267 0.1508 0.1657 0.0396  -0.0529 -0.0636 205 GLU A CB  
1637 C  CG  . GLU A 204 ? 0.0142 0.1594 0.1763 0.0347  -0.0090 -0.0383 205 GLU A CG  
1638 C  CD  . GLU A 204 ? 0.0189 0.1774 0.2020 0.0109  -0.0395 -0.0394 205 GLU A CD  
1639 O  OE1 . GLU A 204 ? 0.1172 0.1790 0.2745 0.0171  -0.0966 -0.0601 205 GLU A OE1 
1640 O  OE2 . GLU A 204 ? 0.0497 0.1535 0.1747 0.0008  -0.0124 -0.0350 205 GLU A OE2 
1641 N  N   . CYS A 205 ? 0.0081 0.0867 0.1229 0.0111  -0.0020 -0.0240 206 CYS A N   
1642 C  CA  . CYS A 205 ? 0.0068 0.1037 0.1524 0.0057  -0.0051 0.0031  206 CYS A CA  
1643 C  C   . CYS A 205 ? 0.0083 0.0739 0.1280 0.0115  -0.0042 -0.0319 206 CYS A C   
1644 O  O   . CYS A 205 ? 0.0102 0.0976 0.1720 0.0131  -0.0167 0.0088  206 CYS A O   
1645 C  CB  . CYS A 205 ? 0.0192 0.1237 0.1335 -0.0164 0.0172  -0.0065 206 CYS A CB  
1646 S  SG  . CYS A 205 ? 0.0588 0.1483 0.1372 0.0092  0.0145  -0.0137 206 CYS A SG  
1647 N  N   . VAL A 206 ? 0.0064 0.0796 0.1257 -0.0023 0.0002  -0.0370 207 VAL A N   
1648 C  CA  . VAL A 206 ? 0.0097 0.0625 0.1004 -0.0069 -0.0091 -0.0153 207 VAL A CA  
1649 C  C   . VAL A 206 ? 0.0080 0.0695 0.1247 0.0098  -0.0031 0.0052  207 VAL A C   
1650 O  O   . VAL A 206 ? 0.0154 0.1002 0.1285 0.0111  -0.0003 0.0115  207 VAL A O   
1651 C  CB  . VAL A 206 ? 0.0089 0.0694 0.1129 -0.0109 0.0118  -0.0205 207 VAL A CB  
1652 C  CG1 . VAL A 206 ? 0.0233 0.0815 0.1382 -0.0167 -0.0245 -0.0298 207 VAL A CG1 
1653 C  CG2 . VAL A 206 ? 0.0176 0.1086 0.1190 -0.0022 0.0262  -0.0031 207 VAL A CG2 
1654 N  N   . THR A 207 ? 0.0071 0.0726 0.1193 -0.0006 0.0096  -0.0144 208 THR A N   
1655 C  CA  . THR A 207 ? 0.0091 0.0738 0.1084 -0.0070 0.0102  -0.0161 208 THR A CA  
1656 C  C   . THR A 207 ? 0.0089 0.0758 0.0842 0.0013  0.0134  -0.0161 208 THR A C   
1657 O  O   . THR A 207 ? 0.0181 0.0901 0.1025 -0.0135 -0.0020 0.0020  208 THR A O   
1658 C  CB  . THR A 207 ? 0.0097 0.1089 0.1452 -0.0075 0.0212  -0.0236 208 THR A CB  
1659 O  OG1 . THR A 207 ? 0.0568 0.1070 0.1555 -0.0012 0.0250  -0.0474 208 THR A OG1 
1660 C  CG2 . THR A 207 ? 0.0308 0.1217 0.1415 0.0064  0.0421  0.0046  208 THR A CG2 
1661 N  N   . TRP A 208 ? 0.0082 0.0680 0.1199 0.0069  0.0089  -0.0164 209 TRP A N   
1662 C  CA  . TRP A 208 ? 0.0086 0.0546 0.0988 0.0034  0.0141  0.0041  209 TRP A CA  
1663 C  C   . TRP A 208 ? 0.0125 0.1028 0.0775 0.0048  0.0206  0.0039  209 TRP A C   
1664 O  O   . TRP A 208 ? 0.0108 0.0882 0.0743 0.0065  0.0158  -0.0055 209 TRP A O   
1665 C  CB  . TRP A 208 ? 0.0103 0.0830 0.1074 0.0165  0.0100  0.0169  209 TRP A CB  
1666 C  CG  . TRP A 208 ? 0.0073 0.0736 0.0951 0.0083  0.0018  0.0085  209 TRP A CG  
1667 C  CD1 . TRP A 208 ? 0.0067 0.0894 0.1187 0.0027  0.0060  0.0090  209 TRP A CD1 
1668 C  CD2 . TRP A 208 ? 0.0093 0.0720 0.1069 0.0112  0.0082  -0.0114 209 TRP A CD2 
1669 N  NE1 . TRP A 208 ? 0.0121 0.0960 0.1102 0.0162  0.0022  -0.0122 209 TRP A NE1 
1670 C  CE2 . TRP A 208 ? 0.0193 0.0869 0.0830 0.0196  0.0224  -0.0095 209 TRP A CE2 
1671 C  CE3 . TRP A 208 ? 0.0208 0.0622 0.0745 0.0176  -0.0015 0.0003  209 TRP A CE3 
1672 C  CZ2 . TRP A 208 ? 0.0238 0.0785 0.0730 0.0293  0.0096  -0.0089 209 TRP A CZ2 
1673 C  CZ3 . TRP A 208 ? 0.0520 0.0790 0.0840 0.0171  0.0208  -0.0002 209 TRP A CZ3 
1674 C  CH2 . TRP A 208 ? 0.0294 0.0900 0.0706 0.0298  0.0033  -0.0069 209 TRP A CH2 
1675 N  N   . ILE A 209 ? 0.0125 0.0762 0.0763 -0.0010 0.0207  -0.0002 210 ILE A N   
1676 C  CA  . ILE A 209 ? 0.0093 0.0652 0.0989 -0.0051 0.0157  -0.0062 210 ILE A CA  
1677 C  C   . ILE A 209 ? 0.0088 0.0797 0.0740 0.0011  0.0127  -0.0039 210 ILE A C   
1678 O  O   . ILE A 209 ? 0.0468 0.0833 0.0745 -0.0044 0.0048  -0.0035 210 ILE A O   
1679 C  CB  . ILE A 209 ? 0.0092 0.0745 0.1253 -0.0057 0.0168  -0.0007 210 ILE A CB  
1680 C  CG1 . ILE A 209 ? 0.0081 0.0956 0.1570 0.0126  -0.0028 -0.0270 210 ILE A CG1 
1681 C  CG2 . ILE A 209 ? 0.0182 0.1233 0.1351 -0.0214 0.0317  0.0013  210 ILE A CG2 
1682 C  CD1 . ILE A 209 ? 0.0108 0.1174 0.1964 0.0218  0.0013  0.0121  210 ILE A CD1 
1683 N  N   . VAL A 210 ? 0.0067 0.0727 0.0904 0.0000  0.0056  0.0039  211 VAL A N   
1684 C  CA  . VAL A 210 ? 0.0076 0.0661 0.0809 -0.0005 0.0096  0.0155  211 VAL A CA  
1685 C  C   . VAL A 210 ? 0.0206 0.0804 0.0807 -0.0051 0.0317  0.0044  211 VAL A C   
1686 O  O   . VAL A 210 ? 0.0170 0.0970 0.0727 -0.0174 0.0172  0.0051  211 VAL A O   
1687 C  CB  . VAL A 210 ? 0.0104 0.0628 0.0903 0.0072  0.0174  0.0099  211 VAL A CB  
1688 C  CG1 . VAL A 210 ? 0.0397 0.0759 0.1005 0.0069  0.0052  -0.0098 211 VAL A CG1 
1689 C  CG2 . VAL A 210 ? 0.0126 0.1054 0.1202 0.0057  0.0267  0.0305  211 VAL A CG2 
1690 N  N   . LEU A 211 ? 0.0136 0.0936 0.0953 -0.0128 0.0232  -0.0108 212 LEU A N   
1691 C  CA  . LEU A 211 ? 0.0134 0.1045 0.0853 -0.0198 0.0147  0.0036  212 LEU A CA  
1692 C  C   . LEU A 211 ? 0.0259 0.0949 0.0824 -0.0258 0.0155  -0.0129 212 LEU A C   
1693 O  O   . LEU A 211 ? 0.0245 0.1018 0.1039 -0.0186 0.0181  -0.0124 212 LEU A O   
1694 C  CB  . LEU A 211 ? 0.0160 0.1037 0.0787 -0.0229 0.0151  0.0095  212 LEU A CB  
1695 C  CG  . LEU A 211 ? 0.0118 0.1190 0.1018 -0.0080 0.0049  0.0104  212 LEU A CG  
1696 C  CD1 . LEU A 211 ? 0.0082 0.1641 0.1337 -0.0129 -0.0125 0.0318  212 LEU A CD1 
1697 C  CD2 . LEU A 211 ? 0.0530 0.1346 0.1269 0.0271  0.0479  0.0103  212 LEU A CD2 
1698 N  N   . LYS A 212 ? 0.0166 0.1169 0.0974 -0.0331 0.0020  0.0109  213 LYS A N   
1699 C  CA  . LYS A 212 ? 0.0991 0.1068 0.1086 -0.0234 -0.0050 0.0066  213 LYS A CA  
1700 C  C   . LYS A 212 ? 0.0591 0.1073 0.1065 -0.0325 0.0013  0.0207  213 LYS A C   
1701 O  O   . LYS A 212 ? 0.0743 0.1170 0.1894 -0.0104 -0.0151 0.0100  213 LYS A O   
1702 C  CB  . LYS A 212 ? 0.2328 0.1923 0.1064 -0.1017 0.0289  0.0219  213 LYS A CB  
1703 C  CG  . LYS A 212 ? 0.3875 0.2039 0.2332 -0.1190 0.0759  0.0359  213 LYS A CG  
1704 C  CD  . LYS A 212 ? 0.4706 0.3657 0.3236 -0.1713 0.1655  0.0717  213 LYS A CD  
1705 C  CE  . LYS A 212 ? 0.4975 0.5754 0.4390 0.0487  0.1729  -0.0113 213 LYS A CE  
1706 N  NZ  . LYS A 212 ? 0.2816 0.5031 0.5870 -0.1359 -0.1304 0.0380  213 LYS A NZ  
1707 N  N   A GLU A 213 ? 0.0233 0.1280 0.0867 -0.0379 0.0150  0.0133  214 GLU A N   
1708 N  N   B GLU A 213 ? 0.0218 0.0960 0.1164 -0.0298 0.0086  0.0086  214 GLU A N   
1709 C  CA  A GLU A 213 ? 0.0285 0.1377 0.0960 -0.0292 0.0195  -0.0033 214 GLU A CA  
1710 C  CA  B GLU A 213 ? 0.0211 0.0973 0.1247 -0.0198 0.0186  -0.0054 214 GLU A CA  
1711 C  C   A GLU A 213 ? 0.0235 0.1027 0.0892 -0.0228 0.0111  0.0118  214 GLU A C   
1712 C  C   B GLU A 213 ? 0.0156 0.0777 0.1240 -0.0142 0.0151  0.0102  214 GLU A C   
1713 O  O   A GLU A 213 ? 0.0274 0.1068 0.1068 -0.0138 0.0068  0.0188  214 GLU A O   
1714 O  O   B GLU A 213 ? 0.0220 0.0847 0.1339 -0.0100 0.0126  0.0164  214 GLU A O   
1715 C  CB  A GLU A 213 ? 0.0222 0.1925 0.1081 -0.0238 0.0227  -0.0071 214 GLU A CB  
1716 C  CB  B GLU A 213 ? 0.0309 0.0946 0.1664 -0.0077 -0.0118 -0.0132 214 GLU A CB  
1717 C  CG  A GLU A 213 ? 0.1093 0.2123 0.1294 -0.0380 0.0025  -0.0331 214 GLU A CG  
1718 C  CG  B GLU A 213 ? 0.0898 0.0880 0.1825 -0.0006 -0.0064 -0.0359 214 GLU A CG  
1719 C  CD  A GLU A 213 ? 0.1402 0.2572 0.1969 -0.0165 -0.0193 0.0060  214 GLU A CD  
1720 C  CD  B GLU A 213 ? 0.0863 0.0998 0.2492 0.0035  0.0137  -0.0188 214 GLU A CD  
1721 O  OE1 A GLU A 213 ? 0.1484 0.3161 0.2316 -0.0450 -0.0601 0.0230  214 GLU A OE1 
1722 O  OE1 B GLU A 213 ? 0.0169 0.0903 0.2940 -0.0297 0.0136  -0.0425 214 GLU A OE1 
1723 O  OE2 A GLU A 213 ? 0.1610 0.3567 0.2303 -0.0163 0.0197  -0.0336 214 GLU A OE2 
1724 O  OE2 B GLU A 213 ? 0.1923 0.1296 0.3473 -0.0575 -0.0249 -0.0139 214 GLU A OE2 
1725 N  N   A PRO A 214 ? 0.0336 0.0982 0.0899 -0.0188 0.0026  0.0100  215 PRO A N   
1726 N  N   B PRO A 214 ? 0.0197 0.0840 0.1217 -0.0076 0.0276  0.0154  215 PRO A N   
1727 C  CA  A PRO A 214 ? 0.0343 0.0995 0.0978 -0.0078 0.0108  -0.0020 215 PRO A CA  
1728 C  CA  B PRO A 214 ? 0.0376 0.0955 0.1171 0.0022  0.0239  -0.0011 215 PRO A CA  
1729 C  C   A PRO A 214 ? 0.0256 0.1147 0.1045 -0.0219 0.0111  -0.0104 215 PRO A C   
1730 C  C   B PRO A 214 ? 0.0414 0.1179 0.1163 -0.0229 0.0242  -0.0107 215 PRO A C   
1731 O  O   A PRO A 214 ? 0.0212 0.0867 0.1492 -0.0103 0.0110  0.0044  215 PRO A O   
1732 O  O   B PRO A 214 ? 0.0434 0.1181 0.1483 -0.0328 -0.0023 -0.0023 215 PRO A O   
1733 C  CB  A PRO A 214 ? 0.0179 0.0842 0.1420 -0.0179 -0.0058 0.0122  215 PRO A CB  
1734 C  CB  B PRO A 214 ? 0.0522 0.0847 0.1671 0.0006  0.0271  0.0100  215 PRO A CB  
1735 C  CG  A PRO A 214 ? 0.0593 0.1016 0.1278 -0.0226 0.0157  0.0071  215 PRO A CG  
1736 C  CG  B PRO A 214 ? 0.0734 0.1258 0.1603 0.0284  0.0467  -0.0074 215 PRO A CG  
1737 C  CD  A PRO A 214 ? 0.0698 0.0953 0.1204 -0.0201 0.0121  0.0105  215 PRO A CD  
1738 C  CD  B PRO A 214 ? 0.0346 0.0716 0.1455 0.0020  0.0244  0.0081  215 PRO A CD  
1739 N  N   . ILE A 215 ? 0.0405 0.1201 0.0849 -0.0049 0.0031  -0.0181 216 ILE A N   
1740 C  CA  . ILE A 215 ? 0.0524 0.1197 0.0930 -0.0054 -0.0079 -0.0177 216 ILE A CA  
1741 C  C   . ILE A 215 ? 0.0451 0.1004 0.1131 -0.0105 0.0044  0.0019  216 ILE A C   
1742 O  O   . ILE A 215 ? 0.0452 0.1163 0.1355 -0.0011 0.0013  -0.0368 216 ILE A O   
1743 C  CB  . ILE A 215 ? 0.0332 0.1201 0.1045 0.0159  0.0126  -0.0067 216 ILE A CB  
1744 C  CG1 . ILE A 215 ? 0.0345 0.1344 0.1120 0.0026  0.0000  0.0211  216 ILE A CG1 
1745 C  CG2 . ILE A 215 ? 0.0592 0.1300 0.1620 0.0352  0.0234  -0.0217 216 ILE A CG2 
1746 C  CD1 . ILE A 215 ? 0.0731 0.1321 0.1312 0.0347  -0.0093 0.0266  216 ILE A CD1 
1747 N  N   A SER A 216 ? 0.0542 0.1147 0.1440 -0.0076 -0.0074 -0.0130 217 SER A N   
1748 N  N   B SER A 216 ? 0.0551 0.1289 0.1312 -0.0249 0.0128  -0.0147 217 SER A N   
1749 C  CA  A SER A 216 ? 0.0445 0.1050 0.1354 -0.0088 -0.0214 -0.0066 217 SER A CA  
1750 C  CA  B SER A 216 ? 0.0933 0.1269 0.1074 -0.0144 0.0136  -0.0012 217 SER A CA  
1751 C  C   A SER A 216 ? 0.0486 0.1030 0.1376 -0.0073 -0.0215 0.0038  217 SER A C   
1752 C  C   B SER A 216 ? 0.0669 0.1154 0.1059 -0.0208 -0.0042 0.0027  217 SER A C   
1753 O  O   A SER A 216 ? 0.0527 0.1300 0.1606 -0.0085 -0.0064 0.0467  217 SER A O   
1754 O  O   B SER A 216 ? 0.0874 0.1434 0.1039 -0.0138 -0.0212 -0.0003 217 SER A O   
1755 C  CB  A SER A 216 ? 0.0597 0.0806 0.1987 -0.0083 -0.0427 -0.0105 217 SER A CB  
1756 C  CB  B SER A 216 ? 0.1201 0.1772 0.1631 -0.0529 0.0194  0.1017  217 SER A CB  
1757 O  OG  A SER A 216 ? 0.1408 0.1721 0.1876 -0.0524 0.0111  -0.0050 217 SER A OG  
1758 O  OG  B SER A 216 ? 0.1243 0.2853 0.1930 -0.0767 -0.0489 0.0049  217 SER A OG  
1759 N  N   . VAL A 217 ? 0.0655 0.1022 0.1082 -0.0089 -0.0214 -0.0176 218 VAL A N   
1760 C  CA  . VAL A 217 ? 0.0644 0.0939 0.1225 -0.0193 -0.0064 -0.0079 218 VAL A CA  
1761 C  C   . VAL A 217 ? 0.0964 0.0829 0.1239 -0.0196 -0.0221 -0.0042 218 VAL A C   
1762 O  O   . VAL A 217 ? 0.0855 0.0907 0.1160 -0.0136 -0.0156 -0.0038 218 VAL A O   
1763 C  CB  . VAL A 217 ? 0.0655 0.0855 0.1806 -0.0226 -0.0264 -0.0168 218 VAL A CB  
1764 C  CG1 . VAL A 217 ? 0.0883 0.0919 0.1664 -0.0330 -0.0025 -0.0160 218 VAL A CG1 
1765 C  CG2 . VAL A 217 ? 0.0542 0.1088 0.2544 -0.0223 -0.0253 -0.0221 218 VAL A CG2 
1766 N  N   . SER A 218 ? 0.0996 0.0966 0.1247 -0.0149 -0.0195 -0.0077 219 SER A N   
1767 C  CA  . SER A 218 ? 0.0791 0.1201 0.1438 -0.0218 -0.0167 -0.0391 219 SER A CA  
1768 C  C   . SER A 218 ? 0.0797 0.0892 0.1596 -0.0244 -0.0050 -0.0217 219 SER A C   
1769 O  O   . SER A 218 ? 0.0714 0.0895 0.1391 -0.0238 -0.0196 0.0095  219 SER A O   
1770 C  CB  . SER A 218 ? 0.1220 0.1213 0.1143 -0.0477 -0.0080 -0.0230 219 SER A CB  
1771 O  OG  . SER A 218 ? 0.1305 0.1300 0.1714 -0.0449 -0.0098 -0.0055 219 SER A OG  
1772 N  N   . SER A 219 ? 0.0876 0.0987 0.1731 0.0160  -0.0111 -0.0226 220 SER A N   
1773 C  CA  . SER A 219 ? 0.0892 0.0951 0.1979 -0.0049 0.0073  -0.0118 220 SER A CA  
1774 C  C   . SER A 219 ? 0.0955 0.1264 0.1843 -0.0196 -0.0060 -0.0130 220 SER A C   
1775 O  O   . SER A 219 ? 0.1098 0.1479 0.2295 -0.0341 0.0201  0.0267  220 SER A O   
1776 C  CB  . SER A 219 ? 0.2192 0.0908 0.2463 -0.0165 0.0244  -0.0347 220 SER A CB  
1777 O  OG  . SER A 219 ? 0.2048 0.1308 0.2870 -0.0062 0.0201  -0.0128 220 SER A OG  
1778 N  N   . GLU A 220 ? 0.1003 0.1120 0.1481 0.0061  0.0155  -0.0183 221 GLU A N   
1779 C  CA  . GLU A 220 ? 0.1418 0.1326 0.1587 -0.0238 -0.0018 0.0002  221 GLU A CA  
1780 C  C   . GLU A 220 ? 0.1208 0.1361 0.1477 -0.0319 0.0130  -0.0111 221 GLU A C   
1781 O  O   . GLU A 220 ? 0.1332 0.1379 0.1649 -0.0137 0.0445  -0.0132 221 GLU A O   
1782 C  CB  . GLU A 220 ? 0.1867 0.1650 0.1790 -0.0065 -0.0353 -0.0572 221 GLU A CB  
1783 C  CG  . GLU A 220 ? 0.2461 0.2052 0.2920 -0.0621 -0.0012 -0.1134 221 GLU A CG  
1784 C  CD  . GLU A 220 ? 0.3334 0.2095 0.2740 -0.0702 -0.0047 -0.0868 221 GLU A CD  
1785 O  OE1 . GLU A 220 ? 0.2084 0.1993 0.2715 -0.0725 -0.0323 -0.0447 221 GLU A OE1 
1786 O  OE2 . GLU A 220 ? 0.5085 0.2434 0.3711 -0.1088 0.0375  -0.1315 221 GLU A OE2 
1787 N  N   . GLN A 221 ? 0.1073 0.1037 0.1389 -0.0120 -0.0049 -0.0001 222 GLN A N   
1788 C  CA  . GLN A 221 ? 0.0824 0.1054 0.1147 0.0071  -0.0139 -0.0127 222 GLN A CA  
1789 C  C   . GLN A 221 ? 0.0854 0.0961 0.1177 -0.0227 -0.0103 0.0177  222 GLN A C   
1790 O  O   . GLN A 221 ? 0.0980 0.1268 0.1487 -0.0368 0.0055  0.0350  222 GLN A O   
1791 C  CB  . GLN A 221 ? 0.0573 0.1341 0.1142 -0.0012 -0.0219 -0.0212 222 GLN A CB  
1792 C  CG  . GLN A 221 ? 0.0522 0.1178 0.1346 -0.0117 -0.0232 -0.0081 222 GLN A CG  
1793 C  CD  . GLN A 221 ? 0.0795 0.0939 0.1073 -0.0124 -0.0093 0.0129  222 GLN A CD  
1794 O  OE1 . GLN A 221 ? 0.0900 0.1009 0.1095 -0.0092 -0.0108 0.0067  222 GLN A OE1 
1795 N  NE2 . GLN A 221 ? 0.0669 0.1107 0.1231 -0.0052 -0.0252 0.0031  222 GLN A NE2 
1796 N  N   . VAL A 222 ? 0.0874 0.1025 0.1159 -0.0089 -0.0259 0.0145  223 VAL A N   
1797 C  CA  . VAL A 222 ? 0.0802 0.1407 0.1436 -0.0006 -0.0280 0.0245  223 VAL A CA  
1798 C  C   . VAL A 222 ? 0.0795 0.1079 0.1716 -0.0272 -0.0103 0.0177  223 VAL A C   
1799 O  O   . VAL A 222 ? 0.0847 0.1355 0.1691 -0.0403 0.0077  0.0026  223 VAL A O   
1800 C  CB  . VAL A 222 ? 0.1480 0.2051 0.1887 -0.0359 -0.0819 0.0685  223 VAL A CB  
1801 C  CG1 . VAL A 222 ? 0.1646 0.2023 0.3266 -0.0407 -0.0745 0.0122  223 VAL A CG1 
1802 C  CG2 . VAL A 222 ? 0.1493 0.2803 0.1882 -0.0384 -0.0979 0.0840  223 VAL A CG2 
1803 N  N   A LEU A 223 ? 0.0709 0.1052 0.1466 -0.0141 0.0461  0.0038  224 LEU A N   
1804 N  N   B LEU A 223 ? 0.1233 0.1097 0.1632 0.0219  -0.0018 -0.0089 224 LEU A N   
1805 C  CA  A LEU A 223 ? 0.0874 0.1150 0.1833 -0.0179 0.0677  -0.0100 224 LEU A CA  
1806 C  CA  B LEU A 223 ? 0.1420 0.1229 0.1994 -0.0181 0.0373  -0.0115 224 LEU A CA  
1807 C  C   A LEU A 223 ? 0.0754 0.1249 0.1788 -0.0197 0.0472  -0.0013 224 LEU A C   
1808 C  C   B LEU A 223 ? 0.0589 0.1419 0.1775 -0.0416 -0.0147 -0.0030 224 LEU A C   
1809 O  O   A LEU A 223 ? 0.0697 0.1587 0.1978 0.0412  0.0586  -0.0094 224 LEU A O   
1810 O  O   B LEU A 223 ? 0.0761 0.1729 0.1657 -0.0905 -0.0030 -0.0229 224 LEU A O   
1811 C  CB  A LEU A 223 ? 0.1147 0.1348 0.2148 -0.0394 0.0912  -0.0344 224 LEU A CB  
1812 C  CB  B LEU A 223 ? 0.2326 0.1351 0.2655 -0.0578 0.0245  -0.0263 224 LEU A CB  
1813 C  CG  A LEU A 223 ? 0.1091 0.1804 0.1861 -0.0403 0.0716  -0.0094 224 LEU A CG  
1814 C  CG  B LEU A 223 ? 0.2773 0.1311 0.3719 -0.0348 0.0788  -0.0927 224 LEU A CG  
1815 C  CD2 . LEU A 223 ? 0.1251 0.1551 0.3412 -0.0127 0.0618  0.0086  224 LEU A CD2 
1816 N  N   . LYS A 224 ? 0.0838 0.1272 0.1721 -0.0293 0.0013  -0.0054 225 LYS A N   
1817 C  CA  . LYS A 224 ? 0.1009 0.1479 0.1567 -0.0250 -0.0145 0.0097  225 LYS A CA  
1818 C  C   . LYS A 224 ? 0.0969 0.1296 0.0985 -0.0154 0.0264  -0.0003 225 LYS A C   
1819 O  O   . LYS A 224 ? 0.1212 0.1423 0.1116 -0.0249 0.0439  -0.0038 225 LYS A O   
1820 C  CB  . LYS A 224 ? 0.0951 0.1901 0.2062 -0.0041 0.0057  0.0419  225 LYS A CB  
1821 C  CG  . LYS A 224 ? 0.1817 0.2575 0.2985 -0.1001 -0.0526 0.0516  225 LYS A CG  
1822 C  CD  . LYS A 224 ? 0.1102 0.4950 0.3686 -0.0598 -0.0105 -0.0947 225 LYS A CD  
1823 C  CE  . LYS A 224 ? 0.5553 0.7233 0.3764 -0.0461 -0.1120 -0.1546 225 LYS A CE  
1824 N  NZ  . LYS A 224 ? 0.4590 0.5414 0.4325 -0.1184 0.2487  -0.1175 225 LYS A NZ  
1825 N  N   . PHE A 225 ? 0.1018 0.0885 0.1002 0.0021  0.0069  -0.0162 226 PHE A N   
1826 C  CA  . PHE A 225 ? 0.0664 0.0935 0.0804 0.0047  0.0271  -0.0131 226 PHE A CA  
1827 C  C   . PHE A 225 ? 0.0689 0.0935 0.1102 0.0094  0.0303  0.0106  226 PHE A C   
1828 O  O   . PHE A 225 ? 0.0864 0.1125 0.0998 -0.0106 0.0418  -0.0047 226 PHE A O   
1829 C  CB  . PHE A 225 ? 0.0691 0.1132 0.0797 0.0055  0.0201  -0.0020 226 PHE A CB  
1830 C  CG  . PHE A 225 ? 0.0776 0.1023 0.1251 0.0001  0.0365  -0.0087 226 PHE A CG  
1831 C  CD1 . PHE A 225 ? 0.1156 0.1262 0.1795 0.0453  0.0285  0.0148  226 PHE A CD1 
1832 C  CD2 . PHE A 225 ? 0.0856 0.1832 0.1444 -0.0107 0.0604  -0.0429 226 PHE A CD2 
1833 C  CE1 . PHE A 225 ? 0.1576 0.1650 0.1854 0.0358  0.0785  0.0008  226 PHE A CE1 
1834 C  CE2 . PHE A 225 ? 0.0479 0.2583 0.1624 0.0010  0.0339  -0.0659 226 PHE A CE2 
1835 C  CZ  . PHE A 225 ? 0.0765 0.1569 0.1948 -0.0030 0.0201  -0.0478 226 PHE A CZ  
1836 N  N   . ARG A 226 ? 0.0777 0.0915 0.0888 0.0193  0.0341  -0.0020 227 ARG A N   
1837 C  CA  . ARG A 226 ? 0.0697 0.1057 0.0926 0.0129  0.0312  -0.0044 227 ARG A CA  
1838 C  C   . ARG A 226 ? 0.0653 0.1283 0.1092 -0.0020 0.0502  0.0109  227 ARG A C   
1839 O  O   . ARG A 226 ? 0.0698 0.1742 0.1493 0.0116  0.0491  -0.0146 227 ARG A O   
1840 C  CB  . ARG A 226 ? 0.1267 0.1125 0.1057 0.0179  0.0653  0.0050  227 ARG A CB  
1841 C  CG  . ARG A 226 ? 0.0991 0.0991 0.1044 0.0177  0.0615  0.0051  227 ARG A CG  
1842 C  CD  . ARG A 226 ? 0.1414 0.1066 0.1145 -0.0009 0.0536  0.0185  227 ARG A CD  
1843 N  NE  . ARG A 226 ? 0.1014 0.1161 0.1116 -0.0348 0.0301  0.0212  227 ARG A NE  
1844 C  CZ  . ARG A 226 ? 0.1101 0.1086 0.1430 -0.0487 0.0405  -0.0227 227 ARG A CZ  
1845 N  NH1 . ARG A 226 ? 0.1364 0.1799 0.2683 -0.0754 0.0044  -0.0942 227 ARG A NH1 
1846 N  NH2 . ARG A 226 ? 0.1541 0.1294 0.1581 -0.0611 0.0754  0.0000  227 ARG A NH2 
1847 N  N   A LYS A 227 ? 0.1176 0.1186 0.1056 -0.0143 0.0230  0.0030  228 LYS A N   
1848 N  N   B LYS A 227 ? 0.0779 0.1386 0.0792 0.0116  0.0564  -0.0127 228 LYS A N   
1849 C  CA  A LYS A 227 ? 0.1472 0.1260 0.1037 -0.0436 0.0311  -0.0387 228 LYS A CA  
1850 C  CA  B LYS A 227 ? 0.1154 0.1531 0.0770 -0.0385 0.0619  -0.0366 228 LYS A CA  
1851 C  C   A LYS A 227 ? 0.1207 0.1131 0.0982 -0.0230 0.0242  -0.0287 228 LYS A C   
1852 C  C   B LYS A 227 ? 0.0831 0.1452 0.0713 -0.0172 0.0525  -0.0245 228 LYS A C   
1853 O  O   A LYS A 227 ? 0.1280 0.1817 0.1007 -0.0245 0.0237  -0.0151 228 LYS A O   
1854 O  O   B LYS A 227 ? 0.0763 0.1365 0.0612 -0.0281 0.0321  -0.0166 228 LYS A O   
1855 C  CB  A LYS A 227 ? 0.1678 0.1365 0.1463 -0.0541 0.0013  -0.0548 228 LYS A CB  
1856 C  CB  B LYS A 227 ? 0.1067 0.1814 0.0763 -0.0005 0.0594  -0.0656 228 LYS A CB  
1857 C  CG  A LYS A 227 ? 0.1675 0.1448 0.2198 -0.0577 0.0365  -0.1083 228 LYS A CG  
1858 C  CG  B LYS A 227 ? 0.1516 0.1911 0.1591 -0.0388 0.0531  -0.0478 228 LYS A CG  
1859 C  CD  A LYS A 227 ? 0.1811 0.2465 0.2485 -0.0878 0.0211  -0.0990 228 LYS A CD  
1860 C  CD  B LYS A 227 ? 0.1933 0.2978 0.2308 -0.0164 0.0117  -0.1165 228 LYS A CD  
1861 C  CE  A LYS A 227 ? 0.3001 0.2842 0.3183 -0.0807 0.0958  -0.1761 228 LYS A CE  
1862 C  CE  B LYS A 227 ? 0.3886 0.2755 0.3850 -0.0704 -0.0460 -0.1577 228 LYS A CE  
1863 N  N   . LEU A 228 ? 0.0970 0.1129 0.0862 -0.0192 0.0195  -0.0222 229 LEU A N   
1864 C  CA  . LEU A 228 ? 0.0803 0.1036 0.0961 -0.0124 0.0128  -0.0226 229 LEU A CA  
1865 C  C   . LEU A 228 ? 0.0822 0.0973 0.0786 -0.0077 0.0197  -0.0296 229 LEU A C   
1866 O  O   . LEU A 228 ? 0.0880 0.1007 0.1086 0.0016  0.0354  -0.0103 229 LEU A O   
1867 C  CB  . LEU A 228 ? 0.1031 0.1133 0.0973 0.0097  0.0140  -0.0200 229 LEU A CB  
1868 C  CG  . LEU A 228 ? 0.0944 0.1631 0.0768 0.0099  0.0147  0.0089  229 LEU A CG  
1869 C  CD1 . LEU A 228 ? 0.0895 0.1645 0.0865 -0.0073 0.0135  -0.0131 229 LEU A CD1 
1870 C  CD2 . LEU A 228 ? 0.1330 0.1588 0.0942 0.0140  0.0237  0.0172  229 LEU A CD2 
1871 N  N   . ASN A 229 ? 0.0876 0.1282 0.1034 -0.0316 0.0403  -0.0195 230 ASN A N   
1872 C  CA  . ASN A 229 ? 0.0847 0.1588 0.0556 -0.0142 0.0250  -0.0293 230 ASN A CA  
1873 C  C   . ASN A 229 ? 0.0820 0.1034 0.0686 0.0024  0.0266  -0.0049 230 ASN A C   
1874 O  O   . ASN A 229 ? 0.0679 0.1217 0.1353 0.0127  0.0454  0.0063  230 ASN A O   
1875 C  CB  . ASN A 229 ? 0.1341 0.1724 0.0648 -0.0114 0.0465  -0.0295 230 ASN A CB  
1876 C  CG  . ASN A 229 ? 0.1132 0.1865 0.1194 -0.0141 0.0628  -0.0530 230 ASN A CG  
1877 O  OD1 . ASN A 229 ? 0.2551 0.2120 0.1279 0.0227  0.1094  -0.0458 230 ASN A OD1 
1878 N  ND2 . ASN A 229 ? 0.1734 0.1685 0.1613 -0.0417 0.0406  -0.0538 230 ASN A ND2 
1879 N  N   . PHE A 230 ? 0.0636 0.1465 0.0684 -0.0351 0.0351  -0.0001 231 PHE A N   
1880 C  CA  . PHE A 230 ? 0.0709 0.1092 0.0761 -0.0227 0.0330  0.0111  231 PHE A CA  
1881 C  C   . PHE A 230 ? 0.0637 0.1488 0.0943 -0.0336 0.0510  0.0075  231 PHE A C   
1882 O  O   . PHE A 230 ? 0.1192 0.1465 0.1283 -0.0513 0.0620  -0.0068 231 PHE A O   
1883 C  CB  . PHE A 230 ? 0.0792 0.1289 0.0894 -0.0234 0.0296  0.0238  231 PHE A CB  
1884 C  CG  . PHE A 230 ? 0.0962 0.0926 0.1201 -0.0462 0.0669  0.0018  231 PHE A CG  
1885 C  CD1 . PHE A 230 ? 0.0822 0.1298 0.1009 -0.0277 0.0336  -0.0212 231 PHE A CD1 
1886 C  CD2 . PHE A 230 ? 0.1048 0.1007 0.1206 -0.0201 0.0483  -0.0012 231 PHE A CD2 
1887 C  CE1 . PHE A 230 ? 0.1079 0.1009 0.1138 -0.0315 0.0160  0.0052  231 PHE A CE1 
1888 C  CE2 . PHE A 230 ? 0.1084 0.1375 0.1000 0.0153  0.0357  0.0107  231 PHE A CE2 
1889 C  CZ  . PHE A 230 ? 0.0628 0.1253 0.1086 0.0163  0.0172  0.0062  231 PHE A CZ  
1890 N  N   . ASN A 231 ? 0.0881 0.1483 0.1002 -0.0138 0.0639  0.0146  232 ASN A N   
1891 C  CA  . ASN A 231 ? 0.0858 0.1571 0.0958 -0.0173 0.0596  0.0187  232 ASN A CA  
1892 C  C   . ASN A 231 ? 0.0883 0.2007 0.1083 0.0000  0.0571  0.0138  232 ASN A C   
1893 O  O   . ASN A 231 ? 0.0907 0.1793 0.1405 0.0080  0.0502  -0.0208 232 ASN A O   
1894 C  CB  . ASN A 231 ? 0.0810 0.1908 0.1416 -0.0087 0.0770  -0.0016 232 ASN A CB  
1895 C  CG  . ASN A 231 ? 0.0926 0.1558 0.1398 0.0032  0.0650  0.0081  232 ASN A CG  
1896 O  OD1 . ASN A 231 ? 0.1244 0.1584 0.1412 -0.0183 0.0842  -0.0168 232 ASN A OD1 
1897 N  ND2 . ASN A 231 ? 0.1714 0.1825 0.1366 0.0702  0.0547  0.0035  232 ASN A ND2 
1898 N  N   . GLY A 232 ? 0.1389 0.1405 0.1141 -0.0070 0.0671  -0.0013 233 GLY A N   
1899 C  CA  . GLY A 232 ? 0.1847 0.1258 0.1341 0.0033  0.0601  0.0047  233 GLY A CA  
1900 C  C   . GLY A 232 ? 0.1219 0.1628 0.0978 0.0196  0.0568  0.0163  233 GLY A C   
1901 O  O   . GLY A 232 ? 0.1362 0.1814 0.1494 0.0408  0.0791  0.0099  233 GLY A O   
1902 N  N   . GLU A 233 ? 0.1637 0.1897 0.0833 0.0074  0.0466  0.0264  234 GLU A N   
1903 C  CA  . GLU A 233 ? 0.1416 0.2005 0.0998 -0.0110 0.0317  0.0102  234 GLU A CA  
1904 C  C   . GLU A 233 ? 0.1549 0.1885 0.1409 0.0082  0.0479  -0.0040 234 GLU A C   
1905 O  O   . GLU A 233 ? 0.1588 0.1885 0.1455 0.0032  0.0649  -0.0148 234 GLU A O   
1906 C  CB  . GLU A 233 ? 0.2276 0.2612 0.1101 0.0626  0.0417  0.0257  234 GLU A CB  
1907 C  CG  . GLU A 233 ? 0.2030 0.2929 0.1170 -0.0211 0.0411  0.0318  234 GLU A CG  
1908 C  CD  . GLU A 233 ? 0.3094 0.3657 0.2727 0.0783  -0.0149 0.0221  234 GLU A CD  
1909 O  OE1 . GLU A 233 ? 0.2816 0.3629 0.3057 0.0350  0.1003  0.0269  234 GLU A OE1 
1910 O  OE2 . GLU A 233 ? 0.3161 0.4318 0.2860 -0.0686 0.0232  0.0128  234 GLU A OE2 
1911 N  N   . GLY A 234 ? 0.2059 0.2204 0.1116 0.0287  0.0916  0.0000  235 GLY A N   
1912 C  CA  . GLY A 234 ? 0.1976 0.2191 0.1341 0.0708  0.0775  -0.0216 235 GLY A CA  
1913 C  C   . GLY A 234 ? 0.1789 0.2012 0.1250 0.0908  0.1065  -0.0020 235 GLY A C   
1914 O  O   . GLY A 234 ? 0.1918 0.2947 0.1692 0.0609  0.1379  -0.0049 235 GLY A O   
1915 N  N   . GLU A 235 ? 0.1944 0.2515 0.1391 0.0328  0.1056  0.0212  236 GLU A N   
1916 C  CA  . GLU A 235 ? 0.1617 0.2565 0.1738 0.0478  0.1075  0.0319  236 GLU A CA  
1917 C  C   . GLU A 235 ? 0.1942 0.2842 0.1918 0.0513  0.1439  0.0460  236 GLU A C   
1918 O  O   . GLU A 235 ? 0.1914 0.2381 0.2544 0.0498  0.1185  0.0566  236 GLU A O   
1919 C  CB  . GLU A 235 ? 0.1808 0.2350 0.2508 0.0485  0.0815  -0.0273 236 GLU A CB  
1920 C  CG  . GLU A 235 ? 0.1887 0.2301 0.2613 0.0198  0.0805  0.0391  236 GLU A CG  
1921 C  CD  . GLU A 235 ? 0.5147 0.3811 0.3840 -0.0736 0.1379  -0.0952 236 GLU A CD  
1922 O  OE1 . GLU A 235 ? 0.1280 0.3391 0.6064 -0.0133 0.0948  0.0713  236 GLU A OE1 
1923 O  OE2 . GLU A 235 ? 0.7575 0.3520 0.4832 -0.0988 0.2412  0.0121  236 GLU A OE2 
1924 N  N   . PRO A 236 ? 0.1767 0.2334 0.2292 0.0342  0.1124  0.0564  237 PRO A N   
1925 C  CA  . PRO A 236 ? 0.2227 0.2445 0.2400 0.0296  0.1719  0.0603  237 PRO A CA  
1926 C  C   . PRO A 236 ? 0.1790 0.2120 0.2005 0.0457  0.1197  0.0312  237 PRO A C   
1927 O  O   . PRO A 236 ? 0.1380 0.2372 0.1858 0.0487  0.0895  0.0252  237 PRO A O   
1928 C  CB  . PRO A 236 ? 0.2134 0.2820 0.2454 0.0447  0.1461  0.0222  237 PRO A CB  
1929 C  CG  . PRO A 236 ? 0.1966 0.3712 0.3046 0.0560  0.1092  0.1298  237 PRO A CG  
1930 C  CD  . PRO A 236 ? 0.1796 0.3776 0.3086 0.0793  0.0756  0.0640  237 PRO A CD  
1931 N  N   . GLU A 237 ? 0.1588 0.2068 0.1739 0.0579  0.0923  0.0017  238 GLU A N   
1932 C  CA  . GLU A 237 ? 0.1901 0.2263 0.1512 0.0335  0.1173  -0.0043 238 GLU A CA  
1933 C  C   . GLU A 237 ? 0.1280 0.1359 0.1724 0.0262  0.1164  -0.0078 238 GLU A C   
1934 O  O   . GLU A 237 ? 0.1567 0.1377 0.1713 0.0397  0.0719  -0.0088 238 GLU A O   
1935 C  CB  . GLU A 237 ? 0.2377 0.2363 0.1785 0.0614  0.0878  -0.0464 238 GLU A CB  
1936 C  CG  . GLU A 237 ? 0.2213 0.2471 0.2117 0.0328  0.0719  -0.0842 238 GLU A CG  
1937 C  CD  . GLU A 237 ? 0.3040 0.4296 0.1905 -0.0230 0.0489  -0.0864 238 GLU A CD  
1938 O  OE1 . GLU A 237 ? 0.5456 0.4564 0.3026 0.0343  0.0290  -0.1987 238 GLU A OE1 
1939 O  OE2 . GLU A 237 ? 0.3481 0.2104 0.2386 -0.0574 0.0883  -0.0867 238 GLU A OE2 
1940 N  N   . GLU A 238 ? 0.1116 0.1874 0.1343 -0.0115 0.1103  -0.0259 239 GLU A N   
1941 C  CA  . GLU A 238 ? 0.1210 0.1781 0.1434 -0.0491 0.1028  -0.0238 239 GLU A CA  
1942 C  C   . GLU A 238 ? 0.1118 0.1204 0.1192 0.0027  0.0763  -0.0158 239 GLU A C   
1943 O  O   . GLU A 238 ? 0.1197 0.1256 0.1800 0.0136  0.0750  -0.0031 239 GLU A O   
1944 C  CB  . GLU A 238 ? 0.1305 0.2532 0.1919 -0.0707 0.0343  0.0027  239 GLU A CB  
1945 C  CG  . GLU A 238 ? 0.2590 0.3800 0.2138 0.0405  -0.0078 0.0181  239 GLU A CG  
1946 C  CD  . GLU A 238 ? 0.2798 0.5039 0.3721 0.1101  -0.0105 0.1307  239 GLU A CD  
1947 O  OE1 . GLU A 238 ? 0.1560 0.7325 0.6311 0.0441  0.0132  -0.0675 239 GLU A OE1 
1948 O  OE2 . GLU A 238 ? 0.1897 0.4268 0.5264 0.1472  0.1198  0.0842  239 GLU A OE2 
1949 N  N   . LEU A 239 ? 0.0934 0.1483 0.0948 -0.0092 0.0502  -0.0148 240 LEU A N   
1950 C  CA  . LEU A 239 ? 0.0899 0.1068 0.1226 0.0016  0.0563  -0.0378 240 LEU A CA  
1951 C  C   . LEU A 239 ? 0.0907 0.0885 0.0944 0.0013  0.0619  -0.0058 240 LEU A C   
1952 O  O   . LEU A 239 ? 0.0749 0.1289 0.1168 0.0051  0.0580  0.0036  240 LEU A O   
1953 C  CB  . LEU A 239 ? 0.1179 0.0941 0.1936 0.0144  0.0163  -0.0376 240 LEU A CB  
1954 C  CG  . LEU A 239 ? 0.0691 0.1322 0.1821 0.0012  0.0176  -0.0465 240 LEU A CG  
1955 C  CD1 . LEU A 239 ? 0.1933 0.1240 0.2839 0.0066  0.0161  -0.0071 240 LEU A CD1 
1956 C  CD2 . LEU A 239 ? 0.1741 0.1251 0.1861 0.0198  -0.0081 -0.0614 240 LEU A CD2 
1957 N  N   . MET A 240 ? 0.0739 0.0876 0.1064 -0.0041 0.0641  -0.0041 241 MET A N   
1958 C  CA  . MET A 240 ? 0.0766 0.0876 0.1027 0.0079  0.0601  -0.0023 241 MET A CA  
1959 C  C   . MET A 240 ? 0.0630 0.1171 0.0897 -0.0163 0.0354  -0.0037 241 MET A C   
1960 O  O   . MET A 240 ? 0.0644 0.1314 0.0815 -0.0084 0.0351  -0.0027 241 MET A O   
1961 C  CB  . MET A 240 ? 0.1095 0.1028 0.0991 0.0308  0.0323  -0.0257 241 MET A CB  
1962 C  CG  . MET A 240 ? 0.0637 0.1138 0.0831 0.0074  0.0351  -0.0239 241 MET A CG  
1963 S  SD  . MET A 240 ? 0.0939 0.1113 0.1158 -0.0030 0.0489  -0.0063 241 MET A SD  
1964 C  CE  . MET A 240 ? 0.0795 0.1785 0.1120 -0.0166 0.0497  0.0187  241 MET A CE  
1965 N  N   . VAL A 241 ? 0.0822 0.1031 0.0795 -0.0006 0.0485  0.0144  242 VAL A N   
1966 C  CA  . VAL A 241 ? 0.0817 0.0790 0.0553 -0.0073 0.0366  -0.0096 242 VAL A CA  
1967 C  C   . VAL A 241 ? 0.0461 0.0946 0.0618 0.0055  0.0331  0.0059  242 VAL A C   
1968 O  O   . VAL A 241 ? 0.0472 0.1181 0.1044 -0.0046 0.0407  -0.0105 242 VAL A O   
1969 C  CB  . VAL A 241 ? 0.0582 0.0826 0.1240 -0.0120 0.0337  -0.0232 242 VAL A CB  
1970 C  CG1 . VAL A 241 ? 0.1088 0.1079 0.1225 -0.0182 0.0207  -0.0403 242 VAL A CG1 
1971 C  CG2 . VAL A 241 ? 0.0715 0.1427 0.1498 0.0147  0.0446  -0.0036 242 VAL A CG2 
1972 N  N   . ASP A 242 ? 0.0712 0.0932 0.0576 0.0041  0.0456  -0.0100 243 ASP A N   
1973 C  CA  . ASP A 242 ? 0.0446 0.0694 0.0803 0.0170  0.0381  -0.0052 243 ASP A CA  
1974 C  C   . ASP A 242 ? 0.0311 0.0709 0.1041 0.0072  0.0409  0.0031  243 ASP A C   
1975 O  O   . ASP A 242 ? 0.0398 0.0957 0.1606 0.0051  0.0276  -0.0114 243 ASP A O   
1976 C  CB  . ASP A 242 ? 0.0419 0.0815 0.1118 0.0252  0.0546  0.0062  243 ASP A CB  
1977 C  CG  . ASP A 242 ? 0.0639 0.0906 0.1280 0.0111  0.0385  -0.0018 243 ASP A CG  
1978 O  OD1 . ASP A 242 ? 0.0518 0.0779 0.1348 0.0150  0.0282  0.0044  243 ASP A OD1 
1979 O  OD2 . ASP A 242 ? 0.0867 0.1161 0.1562 0.0078  0.0640  -0.0234 243 ASP A OD2 
1980 N  N   . ASN A 243 ? 0.0201 0.0710 0.0842 0.0030  0.0261  -0.0105 244 ASN A N   
1981 C  CA  . ASN A 243 ? 0.0232 0.0777 0.0917 -0.0102 0.0352  0.0063  244 ASN A CA  
1982 C  C   . ASN A 243 ? 0.0202 0.0906 0.1004 0.0057  0.0358  0.0038  244 ASN A C   
1983 O  O   . ASN A 243 ? 0.0425 0.0994 0.0935 0.0252  0.0390  0.0027  244 ASN A O   
1984 C  CB  . ASN A 243 ? 0.0164 0.1186 0.1025 -0.0085 0.0070  0.0167  244 ASN A CB  
1985 C  CG  . ASN A 243 ? 0.0153 0.1071 0.1050 -0.0032 0.0289  0.0128  244 ASN A CG  
1986 O  OD1 . ASN A 243 ? 0.0216 0.1191 0.1586 -0.0049 0.0460  0.0232  244 ASN A OD1 
1987 N  ND2 . ASN A 243 ? 0.0376 0.1161 0.1016 -0.0161 0.0201  0.0263  244 ASN A ND2 
1988 N  N   . TRP A 244 ? 0.0169 0.1107 0.0761 -0.0094 0.0200  -0.0073 245 TRP A N   
1989 C  CA  . TRP A 244 ? 0.0151 0.0984 0.0818 -0.0183 0.0206  -0.0056 245 TRP A CA  
1990 C  C   . TRP A 244 ? 0.0108 0.0869 0.0798 0.0000  0.0178  -0.0120 245 TRP A C   
1991 O  O   . TRP A 244 ? 0.0177 0.0962 0.1140 0.0109  0.0150  -0.0204 245 TRP A O   
1992 C  CB  . TRP A 244 ? 0.0200 0.0653 0.0890 -0.0065 0.0330  -0.0019 245 TRP A CB  
1993 C  CG  . TRP A 244 ? 0.0168 0.0738 0.0964 0.0077  0.0291  -0.0023 245 TRP A CG  
1994 C  CD1 . TRP A 244 ? 0.0225 0.0750 0.1044 0.0034  0.0389  -0.0102 245 TRP A CD1 
1995 C  CD2 . TRP A 244 ? 0.0247 0.0797 0.0937 0.0015  0.0222  -0.0027 245 TRP A CD2 
1996 N  NE1 . TRP A 244 ? 0.0269 0.0807 0.0914 0.0018  0.0253  0.0074  245 TRP A NE1 
1997 C  CE2 . TRP A 244 ? 0.0231 0.0869 0.0937 0.0100  0.0194  0.0003  245 TRP A CE2 
1998 C  CE3 . TRP A 244 ? 0.0551 0.0867 0.0891 -0.0043 0.0170  0.0196  245 TRP A CE3 
1999 C  CZ2 . TRP A 244 ? 0.0684 0.0961 0.1244 0.0122  0.0067  0.0152  245 TRP A CZ2 
2000 C  CZ3 . TRP A 244 ? 0.0715 0.1018 0.1196 0.0340  0.0330  0.0164  245 TRP A CZ3 
2001 C  CH2 . TRP A 244 ? 0.0741 0.1093 0.1419 0.0461  -0.0084 -0.0058 245 TRP A CH2 
2002 N  N   . ARG A 245 ? 0.0195 0.0977 0.0682 -0.0151 0.0136  -0.0206 246 ARG A N   
2003 C  CA  . ARG A 245 ? 0.0095 0.0959 0.0745 -0.0024 0.0146  -0.0158 246 ARG A CA  
2004 C  C   . ARG A 245 ? 0.0154 0.0840 0.0964 0.0001  0.0153  -0.0035 246 ARG A C   
2005 O  O   . ARG A 245 ? 0.0250 0.1160 0.1084 -0.0025 0.0328  -0.0187 246 ARG A O   
2006 C  CB  . ARG A 245 ? 0.0072 0.1080 0.0849 -0.0077 0.0068  -0.0319 246 ARG A CB  
2007 C  CG  . ARG A 245 ? 0.0085 0.1165 0.1115 -0.0153 0.0062  -0.0342 246 ARG A CG  
2008 C  CD  . ARG A 245 ? 0.0089 0.1423 0.1436 -0.0166 0.0146  -0.0571 246 ARG A CD  
2009 N  NE  . ARG A 245 ? 0.0090 0.1067 0.1369 -0.0159 -0.0010 -0.0191 246 ARG A NE  
2010 C  CZ  . ARG A 245 ? 0.0111 0.1379 0.0871 -0.0244 0.0090  -0.0259 246 ARG A CZ  
2011 N  NH1 . ARG A 245 ? 0.0297 0.1136 0.1049 -0.0215 0.0376  -0.0032 246 ARG A NH1 
2012 N  NH2 . ARG A 245 ? 0.0104 0.1674 0.1628 -0.0243 -0.0049 -0.0207 246 ARG A NH2 
2013 N  N   . PRO A 246 ? 0.0292 0.0905 0.1000 0.0132  0.0186  -0.0095 247 PRO A N   
2014 C  CA  . PRO A 246 ? 0.0515 0.1056 0.1117 0.0313  0.0394  0.0040  247 PRO A CA  
2015 C  C   . PRO A 246 ? 0.0564 0.0883 0.1049 0.0243  0.0277  0.0114  247 PRO A C   
2016 O  O   . PRO A 246 ? 0.0272 0.0937 0.1285 0.0138  0.0070  -0.0001 247 PRO A O   
2017 C  CB  . PRO A 246 ? 0.1018 0.1377 0.1480 0.0763  0.0295  0.0013  247 PRO A CB  
2018 C  CG  . PRO A 246 ? 0.1240 0.1727 0.2148 0.0736  0.0541  0.0719  247 PRO A CG  
2019 C  CD  . PRO A 246 ? 0.0399 0.1354 0.0897 0.0535  0.0223  0.0104  247 PRO A CD  
2020 N  N   . ALA A 247 ? 0.0577 0.1028 0.0959 0.0110  0.0291  0.0072  248 ALA A N   
2021 C  CA  . ALA A 247 ? 0.0428 0.1294 0.0890 0.0019  0.0197  -0.0063 248 ALA A CA  
2022 C  C   . ALA A 247 ? 0.0486 0.1118 0.0939 0.0297  -0.0057 -0.0004 248 ALA A C   
2023 O  O   . ALA A 247 ? 0.0754 0.1272 0.1262 0.0545  -0.0055 -0.0121 248 ALA A O   
2024 C  CB  . ALA A 247 ? 0.1091 0.1700 0.0944 0.0036  0.0442  0.0223  248 ALA A CB  
2025 N  N   . GLN A 248 ? 0.0227 0.1097 0.1136 0.0079  -0.0043 -0.0047 249 GLN A N   
2026 C  CA  . GLN A 248 ? 0.0276 0.0964 0.0951 0.0172  -0.0027 -0.0106 249 GLN A CA  
2027 C  C   . GLN A 248 ? 0.0436 0.1145 0.0964 0.0131  -0.0040 -0.0036 249 GLN A C   
2028 O  O   . GLN A 248 ? 0.0573 0.1420 0.1156 0.0122  0.0172  0.0136  249 GLN A O   
2029 C  CB  . GLN A 248 ? 0.0461 0.1005 0.1168 0.0022  -0.0064 -0.0068 249 GLN A CB  
2030 C  CG  . GLN A 248 ? 0.0636 0.1118 0.1298 0.0000  0.0277  0.0024  249 GLN A CG  
2031 C  CD  . GLN A 248 ? 0.0217 0.1592 0.1203 -0.0249 0.0145  -0.0021 249 GLN A CD  
2032 O  OE1 . GLN A 248 ? 0.0407 0.2202 0.1854 -0.0539 -0.0019 -0.0124 249 GLN A OE1 
2033 N  NE2 . GLN A 248 ? 0.0847 0.1551 0.1161 0.0102  0.0079  0.0003  249 GLN A NE2 
2034 N  N   . PRO A 249 ? 0.0441 0.1757 0.1146 0.0370  -0.0190 -0.0111 250 PRO A N   
2035 C  CA  . PRO A 249 ? 0.0716 0.2118 0.1091 0.0716  -0.0153 0.0081  250 PRO A CA  
2036 C  C   . PRO A 249 ? 0.0709 0.1739 0.0933 0.0518  -0.0094 0.0171  250 PRO A C   
2037 O  O   . PRO A 249 ? 0.0525 0.1790 0.1423 0.0467  -0.0126 0.0064  250 PRO A O   
2038 C  CB  . PRO A 249 ? 0.0964 0.2974 0.1897 0.1235  -0.0784 -0.0763 250 PRO A CB  
2039 C  CG  . PRO A 249 ? 0.1140 0.3317 0.1631 0.0200  -0.0638 -0.0776 250 PRO A CG  
2040 C  CD  . PRO A 249 ? 0.0259 0.2603 0.2142 0.0238  -0.0629 -0.0421 250 PRO A CD  
2041 N  N   . LEU A 250 ? 0.0926 0.1984 0.0907 0.0517  0.0097  0.0055  251 LEU A N   
2042 C  CA  . LEU A 250 ? 0.0917 0.1553 0.0792 0.0281  0.0231  0.0042  251 LEU A CA  
2043 C  C   . LEU A 250 ? 0.0719 0.1857 0.0885 0.0388  -0.0005 -0.0103 251 LEU A C   
2044 O  O   . LEU A 250 ? 0.0582 0.1771 0.1634 0.0337  -0.0179 -0.0119 251 LEU A O   
2045 C  CB  . LEU A 250 ? 0.1303 0.1707 0.1527 0.0211  0.0491  0.0317  251 LEU A CB  
2046 C  CG  . LEU A 250 ? 0.0961 0.2465 0.1566 -0.0024 0.0550  0.0414  251 LEU A CG  
2047 C  CD1 . LEU A 250 ? 0.0779 0.2084 0.1339 0.0144  0.0372  -0.0132 251 LEU A CD1 
2048 C  CD2 . LEU A 250 ? 0.1792 0.2041 0.2237 -0.0513 0.0763  0.0109  251 LEU A CD2 
2049 N  N   . LYS A 251 ? 0.0743 0.2002 0.1115 0.0396  -0.0122 -0.0111 252 LYS A N   
2050 C  CA  . LYS A 251 ? 0.0985 0.2368 0.1122 0.0748  -0.0421 -0.0394 252 LYS A CA  
2051 C  C   . LYS A 251 ? 0.1028 0.2140 0.1875 0.0893  -0.0164 -0.0303 252 LYS A C   
2052 O  O   . LYS A 251 ? 0.1700 0.2971 0.1864 0.0073  0.0153  -0.0199 252 LYS A O   
2053 C  CB  . LYS A 251 ? 0.1307 0.2368 0.1732 0.0570  -0.0357 -0.0363 252 LYS A CB  
2054 C  CG  . LYS A 251 ? 0.1894 0.2436 0.2083 0.0431  0.0337  -0.0633 252 LYS A CG  
2055 C  CD  . LYS A 251 ? 0.2576 0.3481 0.2352 0.0325  0.0595  -0.0535 252 LYS A CD  
2056 C  CE  . LYS A 251 ? 0.2489 0.3132 0.3245 0.0286  0.1095  -0.0159 252 LYS A CE  
2057 N  NZ  . LYS A 251 ? 0.2458 0.3959 0.3862 0.0062  0.1201  0.0285  252 LYS A NZ  
2058 N  N   . ASN A 252 ? 0.1038 0.2229 0.1315 0.0586  -0.0324 -0.0582 253 ASN A N   
2059 C  CA  . ASN A 252 ? 0.1469 0.4192 0.1973 0.0807  -0.0272 -0.1531 253 ASN A CA  
2060 C  C   . ASN A 252 ? 0.1581 0.5607 0.1984 0.0749  -0.0826 -0.1357 253 ASN A C   
2061 O  O   . ASN A 252 ? 0.3869 0.5394 0.5277 0.1124  -0.1148 -0.2091 253 ASN A O   
2062 C  CB  . ASN A 252 ? 0.2651 0.5176 0.2227 0.0255  -0.0763 -0.1995 253 ASN A CB  
2063 C  CG  . ASN A 252 ? 0.3866 0.5929 0.2324 0.2076  -0.0567 -0.1722 253 ASN A CG  
2064 O  OD1 . ASN A 252 ? 0.7791 0.8647 0.5335 0.2721  -0.1366 0.1738  253 ASN A OD1 
2065 N  ND2 . ASN A 252 ? 0.5097 0.5689 0.5378 0.2454  -0.2013 0.0380  253 ASN A ND2 
2066 N  N   . ARG A 253 ? 0.0734 0.3298 0.0776 0.0886  -0.0027 -0.0111 254 ARG A N   
2067 C  CA  . ARG A 253 ? 0.0355 0.2241 0.1226 0.0381  0.0143  -0.0098 254 ARG A CA  
2068 C  C   . ARG A 253 ? 0.0937 0.2068 0.0961 0.0314  0.0392  -0.0037 254 ARG A C   
2069 O  O   . ARG A 253 ? 0.1785 0.2162 0.2248 0.0312  0.0618  0.0254  254 ARG A O   
2070 C  CB  . ARG A 253 ? 0.0428 0.1574 0.1102 0.0113  0.0137  -0.0139 254 ARG A CB  
2071 C  CG  . ARG A 253 ? 0.0741 0.1682 0.0858 -0.0005 0.0211  -0.0231 254 ARG A CG  
2072 C  CD  . ARG A 253 ? 0.0411 0.1652 0.0851 0.0347  0.0134  -0.0124 254 ARG A CD  
2073 N  NE  . ARG A 253 ? 0.0125 0.1527 0.0903 0.0194  0.0129  -0.0060 254 ARG A NE  
2074 C  CZ  . ARG A 253 ? 0.0146 0.1127 0.0874 0.0221  0.0145  -0.0134 254 ARG A CZ  
2075 N  NH1 . ARG A 253 ? 0.0064 0.1441 0.0992 -0.0014 0.0026  0.0079  254 ARG A NH1 
2076 N  NH2 . ARG A 253 ? 0.0083 0.1015 0.1018 0.0127  0.0016  -0.0263 254 ARG A NH2 
2077 N  N   . GLN A 254 ? 0.0499 0.2348 0.1285 -0.0104 0.0040  -0.0478 255 GLN A N   
2078 C  CA  . GLN A 254 ? 0.0867 0.3078 0.0716 -0.0530 0.0048  -0.0227 255 GLN A CA  
2079 C  C   . GLN A 254 ? 0.0784 0.1885 0.1036 -0.0108 -0.0091 -0.0357 255 GLN A C   
2080 O  O   . GLN A 254 ? 0.1743 0.1998 0.2827 0.0081  -0.1031 -0.0259 255 GLN A O   
2081 C  CB  . GLN A 254 ? 0.1506 0.3859 0.1048 -0.0780 0.0375  -0.0743 255 GLN A CB  
2082 C  CG  . GLN A 254 ? 0.3725 0.6213 0.1989 -0.0264 -0.0165 -0.0006 255 GLN A CG  
2083 C  CD  . GLN A 254 ? 0.4548 0.8958 0.4487 -0.0388 0.1610  -0.0355 255 GLN A CD  
2084 O  OE1 . GLN A 254 ? 0.5607 1.1430 0.5120 0.0842  -0.0366 0.0214  255 GLN A OE1 
2085 N  NE2 . GLN A 254 ? 0.4839 0.8225 0.2095 -0.0528 0.1377  -0.0388 255 GLN A NE2 
2086 N  N   . ILE A 255 ? 0.0533 0.1908 0.1082 -0.0243 -0.0065 -0.0337 256 ILE A N   
2087 C  CA  . ILE A 255 ? 0.0499 0.1707 0.0941 0.0059  0.0032  -0.0294 256 ILE A CA  
2088 C  C   . ILE A 255 ? 0.0583 0.1454 0.1197 0.0004  0.0201  0.0201  256 ILE A C   
2089 O  O   . ILE A 255 ? 0.0888 0.1562 0.1294 0.0071  0.0266  0.0379  256 ILE A O   
2090 C  CB  . ILE A 255 ? 0.0402 0.1724 0.1172 0.0146  -0.0095 -0.0386 256 ILE A CB  
2091 C  CG1 . ILE A 255 ? 0.0588 0.1663 0.1533 0.0425  0.0189  -0.0259 256 ILE A CG1 
2092 C  CG2 . ILE A 255 ? 0.0648 0.2058 0.1118 0.0210  -0.0175 -0.0172 256 ILE A CG2 
2093 C  CD1 . ILE A 255 ? 0.0939 0.1632 0.1681 -0.0029 0.0254  -0.0476 256 ILE A CD1 
2094 N  N   . LYS A 256 ? 0.0477 0.1343 0.0819 -0.0018 0.0093  -0.0029 257 LYS A N   
2095 C  CA  . LYS A 256 ? 0.0601 0.1402 0.0932 -0.0131 0.0302  -0.0168 257 LYS A CA  
2096 C  C   . LYS A 256 ? 0.0393 0.1488 0.0628 -0.0049 0.0352  0.0072  257 LYS A C   
2097 O  O   . LYS A 256 ? 0.0833 0.2131 0.0633 -0.0286 0.0363  0.0188  257 LYS A O   
2098 C  CB  . LYS A 256 ? 0.0736 0.1456 0.1437 0.0106  0.0289  -0.0138 257 LYS A CB  
2099 C  CG  . LYS A 256 ? 0.2479 0.1942 0.2820 -0.0386 -0.0204 -0.1050 257 LYS A CG  
2100 N  N   . ALA A 257 ? 0.0506 0.1876 0.0882 -0.0150 0.0502  0.0177  258 ALA A N   
2101 C  CA  . ALA A 257 ? 0.0485 0.1810 0.1104 0.0188  0.0289  0.0066  258 ALA A CA  
2102 C  C   . ALA A 257 ? 0.0806 0.1456 0.0858 0.0302  0.0523  0.0062  258 ALA A C   
2103 O  O   . ALA A 257 ? 0.0905 0.2362 0.0786 0.0337  0.0475  -0.0075 258 ALA A O   
2104 C  CB  . ALA A 257 ? 0.0900 0.1779 0.1603 0.0064  0.0445  0.0035  258 ALA A CB  
2105 N  N   . SER A 258 ? 0.0721 0.1350 0.1032 0.0136  0.0421  0.0113  259 SER A N   
2106 C  CA  . SER A 258 ? 0.0610 0.1646 0.1347 0.0104  0.0397  0.0018  259 SER A CA  
2107 C  C   . SER A 258 ? 0.0436 0.2082 0.1226 0.0111  0.0550  -0.0154 259 SER A C   
2108 O  O   . SER A 258 ? 0.0504 0.3387 0.2362 0.0475  0.0796  -0.0012 259 SER A O   
2109 C  CB  . SER A 258 ? 0.0991 0.1706 0.1486 -0.0081 0.0011  0.0081  259 SER A CB  
2110 O  OG  . SER A 258 ? 0.0572 0.1868 0.1254 -0.0158 0.0438  0.0088  259 SER A OG  
2111 N  N   . PHE A 259 ? 0.0657 0.2109 0.1621 -0.0228 0.0480  -0.0044 260 PHE A N   
2112 C  CA  . PHE A 259 ? 0.0530 0.2551 0.2088 -0.0421 0.0441  0.0003  260 PHE A CA  
2113 C  C   . PHE A 259 ? 0.1508 0.3413 0.2425 -0.0339 0.0737  0.0610  260 PHE A C   
2114 O  O   . PHE A 259 ? 0.1826 0.2910 0.2353 -0.0376 0.0281  0.0761  260 PHE A O   
2115 C  CB  . PHE A 259 ? 0.0824 0.2235 0.2197 -0.0330 0.0622  -0.0071 260 PHE A CB  
2116 C  CG  . PHE A 259 ? 0.0798 0.2178 0.1878 -0.0132 0.0466  0.0431  260 PHE A CG  
2117 C  CD1 . PHE A 259 ? 0.0557 0.1864 0.1612 -0.0232 0.0323  -0.0024 260 PHE A CD1 
2118 C  CD2 . PHE A 259 ? 0.1732 0.2278 0.2508 0.0294  0.0659  0.0331  260 PHE A CD2 
2119 C  CE1 . PHE A 259 ? 0.0833 0.1948 0.2083 -0.0110 0.0333  -0.0365 260 PHE A CE1 
2120 C  CE2 . PHE A 259 ? 0.1221 0.3019 0.2726 -0.0377 0.0965  -0.0204 260 PHE A CE2 
2121 C  CZ  . PHE A 259 ? 0.1220 0.1978 0.2377 -0.0296 0.0482  -0.0141 260 PHE A CZ  
2122 N  N   . LYS A 260 ? 0.2803 0.4710 0.2745 -0.1323 0.1046  0.0948  261 LYS A N   
2123 C  CA  . LYS A 260 ? 0.5759 0.7286 0.2798 -0.0928 0.0230  0.2392  261 LYS A CA  
2124 C  C   . LYS A 260 ? 0.4106 0.9182 0.3906 -0.0747 0.0958  0.2359  261 LYS A C   
2125 O  O   . LYS A 260 ? 0.7160 1.0174 0.7278 0.0810  -0.2610 0.1892  261 LYS A O   
2126 C  CB  . LYS A 260 ? 0.7557 0.8663 0.5382 0.0693  0.0268  0.0717  261 LYS A CB  
2127 O  OXT . LYS A 260 ? 0.3279 0.7275 0.8909 -0.1391 0.0466  0.1526  261 LYS A OXT 
2128 ZN ZN  . ZN  B .   ? 0.0072 0.0785 0.0925 0.0037  0.0072  -0.0073 301 ZN  A ZN  
2129 F  F20 . V14 C .   ? 0.1251 0.1328 0.1863 0.0085  0.0111  -0.0008 302 V14 A F20 
2130 C  C5  . V14 C .   ? 0.1192 0.1390 0.1675 -0.0058 0.0145  -0.0062 302 V14 A C5  
2131 C  C4  . V14 C .   ? 0.0502 0.1332 0.1286 -0.0172 -0.0095 -0.0314 302 V14 A C4  
2132 S  S7  . V14 C .   ? 0.0325 0.1076 0.1229 -0.0031 -0.0154 -0.0245 302 V14 A S7  
2133 O  O9  . V14 C .   ? 0.0308 0.1152 0.1045 -0.0009 -0.0154 -0.0141 302 V14 A O9  
2134 N  N10 . V14 C .   ? 0.0294 0.0867 0.1725 -0.0302 -0.0311 -0.0305 302 V14 A N10 
2135 O  O8  . V14 C .   ? 0.0364 0.0817 0.1486 0.0179  -0.0256 -0.0517 302 V14 A O8  
2136 C  C3  . V14 C .   ? 0.0319 0.1477 0.1713 0.0068  0.0226  -0.0168 302 V14 A C3  
2137 F  F12 . V14 C .   ? 0.0321 0.1476 0.2690 0.0048  0.0544  -0.0122 302 V14 A F12 
2138 C  C2  . V14 C .   ? 0.0777 0.1606 0.1845 0.0092  0.0217  0.0041  302 V14 A C2  
2139 F  F13 . V14 C .   ? 0.1384 0.2478 0.2002 0.0290  0.0442  -0.0245 302 V14 A F13 
2140 C  C6  . V14 C .   ? 0.0867 0.1490 0.2018 0.0128  0.0353  0.0215  302 V14 A C6  
2141 C  C1  . V14 C .   ? 0.0689 0.1749 0.1662 0.0200  0.0440  0.0339  302 V14 A C1  
2142 S  S11 . V14 C .   ? 0.1571 0.2702 0.1861 0.0129  0.0527  0.0347  302 V14 A S11 
2143 O  O16 . V14 C .   ? 0.1840 0.2717 0.2618 0.0719  0.0595  0.1214  302 V14 A O16 
2144 O  O17 . V14 C .   ? 0.3614 0.2262 0.1703 -0.0396 0.0641  -0.0432 302 V14 A O17 
2145 C  C15 . V14 C .   ? 0.1074 0.3588 0.2260 -0.0463 0.0528  0.0679  302 V14 A C15 
2146 C  C18 . V14 C .   ? 0.3219 0.4097 0.2554 -0.1269 -0.0634 -0.0185 302 V14 A C18 
2147 O  O21 . V14 C .   ? 0.4329 0.3740 0.5511 0.0685  0.0959  0.0900  302 V14 A O21 
2148 N  N19 . V14 C .   ? 0.1254 0.1599 0.2441 0.0117  0.0036  0.0508  302 V14 A N19 
2149 C  C14 . V14 C .   ? 0.1358 0.1009 0.3773 -0.0214 -0.0074 0.0375  302 V14 A C14 
2150 C  C28 . V14 C .   ? 0.1262 0.1868 0.4781 -0.0328 -0.0148 0.0739  302 V14 A C28 
2151 C  C27 . V14 C .   ? 0.3909 0.2713 0.5113 -0.1429 -0.0145 0.1807  302 V14 A C27 
2152 C  C26 . V14 C .   ? 0.3054 0.3148 0.4931 -0.0781 -0.1320 0.0232  302 V14 A C26 
2153 C  C25 . V14 C .   ? 0.4683 0.3358 0.6090 0.0474  0.1635  0.1606  302 V14 A C25 
2154 C  C24 . V14 C .   ? 0.3079 0.2644 0.5630 -0.1297 0.1024  0.0458  302 V14 A C24 
2155 C  C23 . V14 C .   ? 0.1506 0.1820 0.4964 0.0572  0.0899  0.0310  302 V14 A C23 
2156 C  C22 . V14 C .   ? 0.2281 0.2120 0.3330 0.0545  0.0161  0.0827  302 V14 A C22 
2157 S  S   . DMS D .   ? 0.1443 0.2196 0.1905 -0.0057 0.0242  -0.0200 303 DMS A S   
2158 O  O   . DMS D .   ? 0.2777 0.2411 0.3489 0.0431  0.0983  -0.1005 303 DMS A O   
2159 C  C1  . DMS D .   ? 0.0871 0.1955 0.2928 -0.0097 0.0408  -0.0522 303 DMS A C1  
2160 C  C2  . DMS D .   ? 0.1351 0.1998 0.1664 0.0495  0.0145  -0.0044 303 DMS A C2  
2161 C  C1  . PEG E .   ? 0.6585 0.6375 0.8487 -0.0632 0.0354  0.0209  304 PEG A C1  
2162 O  O1  . PEG E .   ? 0.3719 0.8116 0.5371 -0.2489 -0.1395 0.2395  304 PEG A O1  
2163 C  C2  . PEG E .   ? 0.6075 0.8422 0.7991 0.0760  0.0351  -0.1106 304 PEG A C2  
2164 O  O2  . PEG E .   ? 0.2519 0.6610 0.6093 -0.0640 -0.1733 0.0641  304 PEG A O2  
2165 C  C3  . PEG E .   ? 0.1935 0.4271 0.6743 -0.1650 0.0233  -0.0059 304 PEG A C3  
2166 C  C4  . PEG E .   ? 0.1253 0.4526 0.3730 -0.0526 -0.0534 0.0085  304 PEG A C4  
2167 O  O4  . PEG E .   ? 0.1782 0.3305 0.4526 0.0585  -0.0491 -0.0389 304 PEG A O4  
2168 C  C1  . PEG F .   ? 0.5669 0.5268 0.6646 0.0469  0.0184  -0.0610 305 PEG A C1  
2169 O  O1  . PEG F .   ? 0.7742 0.2293 0.3960 -0.0089 0.0610  0.0135  305 PEG A O1  
2170 C  C2  . PEG F .   ? 0.3270 0.4550 0.6243 -0.1798 0.1733  -0.2378 305 PEG A C2  
2171 O  O2  . PEG F .   ? 0.7985 0.6185 0.6222 -0.0061 0.2586  -0.0368 305 PEG A O2  
2172 C  C3  . PEG F .   ? 0.6822 0.5932 0.6722 0.0030  -0.1493 0.0528  305 PEG A C3  
2173 C  C4  . PEG F .   ? 0.3529 0.2307 0.6043 -0.0276 0.2230  -0.0466 305 PEG A C4  
2174 O  O4  . PEG F .   ? 0.1833 0.1907 0.5207 -0.0391 0.0986  0.0956  305 PEG A O4  
2175 C  C1  . MLA G .   ? 0.3008 0.6100 0.5349 -0.0595 0.0107  -0.0208 306 MLA A C1  
2176 O  O1A . MLA G .   ? 0.3159 0.4309 0.3488 -0.1289 -0.0917 0.0401  306 MLA A O1A 
2177 O  O1B . MLA G .   ? 0.5039 0.3290 0.7216 -0.1088 0.0212  -0.2312 306 MLA A O1B 
2178 C  C2  . MLA G .   ? 0.3294 0.6330 0.6454 -0.1446 -0.2394 0.0558  306 MLA A C2  
2179 C  C3  . MLA G .   ? 0.8087 0.8020 1.2553 -0.0529 -0.2994 0.0401  306 MLA A C3  
2180 O  O3A . MLA G .   ? 0.7736 1.1781 1.2589 -0.0675 -0.2682 0.2945  306 MLA A O3A 
2181 O  O3B . MLA G .   ? 0.6793 1.2058 1.5453 0.2219  -0.4323 -0.0853 306 MLA A O3B 
2182 C  C1  . EDO H .   ? 0.3869 0.2878 0.4875 0.0348  0.2189  0.0067  307 EDO A C1  
2183 O  O1  . EDO H .   ? 0.4471 0.3259 0.6587 0.0798  0.0020  -0.0863 307 EDO A O1  
2184 C  C2  . EDO H .   ? 0.3789 0.4990 0.5431 0.0118  0.2618  -0.0097 307 EDO A C2  
2185 O  O2  . EDO H .   ? 0.6953 0.4916 0.6317 0.1272  0.2575  0.0514  307 EDO A O2  
2186 C  C   . BEZ I .   ? 0.2310 0.3919 0.5075 -0.0231 0.2007  -0.0238 308 BEZ A C   
2187 O  O1  . BEZ I .   ? 0.4322 0.3215 0.3513 -0.0332 0.0986  0.0844  308 BEZ A O1  
2188 O  O2  . BEZ I .   ? 0.1937 0.2827 0.2102 -0.0019 0.0615  -0.0466 308 BEZ A O2  
2189 C  C1  . BEZ I .   ? 0.3639 0.4051 0.5881 -0.0431 0.0446  -0.1522 308 BEZ A C1  
2190 C  C2  . BEZ I .   ? 0.3710 0.5026 0.7063 -0.0520 0.0705  -0.2393 308 BEZ A C2  
2191 C  C3  . BEZ I .   ? 0.4898 0.5419 0.5750 -0.0541 -0.1544 -0.3065 308 BEZ A C3  
2192 C  C4  . BEZ I .   ? 0.6722 0.4160 0.7654 -0.0118 -0.0577 -0.2979 308 BEZ A C4  
2193 C  C5  . BEZ I .   ? 0.6248 0.3768 0.5550 0.0035  -0.1439 -0.1205 308 BEZ A C5  
2194 C  C6  . BEZ I .   ? 0.2503 0.4060 0.5089 0.0038  -0.1368 -0.1177 308 BEZ A C6  
2195 S  S   . DMS J .   ? 0.3516 0.3557 0.5471 0.0536  0.0546  -0.0754 309 DMS A S   
2196 O  O   . DMS J .   ? 0.4008 0.1962 0.3341 0.0168  -0.1076 -0.1137 309 DMS A O   
2197 C  C1  . DMS J .   ? 0.5730 0.2572 0.5553 0.1245  -0.3225 -0.0845 309 DMS A C1  
2198 C  C2  . DMS J .   ? 0.2885 0.4824 0.4002 0.1418  -0.0061 -0.1402 309 DMS A C2  
2199 C  C   . BEZ K .   ? 0.2735 0.2942 0.5263 -0.0690 0.1128  -0.1252 310 BEZ A C   
2200 O  O1  . BEZ K .   ? 0.5431 0.4529 0.5554 0.0432  0.0545  -0.2276 310 BEZ A O1  
2201 O  O2  . BEZ K .   ? 0.3388 0.4041 0.5068 0.0440  0.1825  -0.0290 310 BEZ A O2  
2202 C  C1  . BEZ K .   ? 0.2710 0.3075 0.4758 -0.1123 0.0904  -0.0521 310 BEZ A C1  
2203 C  C2  . BEZ K .   ? 0.2544 0.2005 0.4156 0.0332  0.0162  0.0288  310 BEZ A C2  
2204 C  C3  . BEZ K .   ? 0.3793 0.2004 0.3191 -0.0218 -0.0106 -0.0269 310 BEZ A C3  
2205 C  C4  . BEZ K .   ? 0.3193 0.3317 0.3360 -0.0137 -0.0002 -0.0125 310 BEZ A C4  
2206 C  C5  . BEZ K .   ? 0.2539 0.2676 0.3316 -0.0375 0.0493  0.0343  310 BEZ A C5  
2207 C  C6  . BEZ K .   ? 0.3309 0.3032 0.4223 -0.0765 0.1139  -0.0353 310 BEZ A C6  
2208 O  O   . HOH L .   ? 0.1495 0.3268 0.5407 -0.0506 0.0009  -0.0347 401 HOH A O   
2209 O  O   . HOH L .   ? 0.3320 0.3036 0.5244 0.0659  -0.0687 -0.0111 402 HOH A O   
2210 O  O   . HOH L .   ? 0.7881 0.3219 0.8735 0.0917  -0.4276 -0.1780 403 HOH A O   
2211 O  O   . HOH L .   ? 0.5716 0.2569 0.6720 -0.0331 0.1254  0.1251  404 HOH A O   
2212 O  O   . HOH L .   ? 0.4340 0.4548 0.7993 0.0543  0.1588  -0.0825 405 HOH A O   
2213 O  O   . HOH L .   ? 0.1565 0.0926 0.1951 0.0108  -0.0394 -0.0075 406 HOH A O   
2214 O  O   . HOH L .   ? 0.2612 0.4115 0.5434 0.1581  -0.1588 -0.0543 407 HOH A O   
2215 O  O   . HOH L .   ? 0.4462 0.3528 0.1563 -0.2184 0.0586  -0.1049 408 HOH A O   
2216 O  O   . HOH L .   ? 0.6620 0.4652 0.3495 0.3250  0.1975  0.1980  409 HOH A O   
2217 O  O   . HOH L .   ? 0.3165 0.5988 0.2546 -0.2385 0.0000  0.1065  410 HOH A O   
2218 O  O   . HOH L .   ? 0.4907 0.7240 0.2835 0.0803  0.2263  0.0000  411 HOH A O   
2219 O  O   . HOH L .   ? 0.0919 0.3345 0.2879 -0.0447 -0.0160 -0.0247 412 HOH A O   
2220 O  O   . HOH L .   ? 0.4875 0.3620 0.2759 -0.2476 0.0908  0.0462  413 HOH A O   
2221 O  O   . HOH L .   ? 0.2979 0.4200 0.6567 -0.0753 -0.0703 -0.0136 414 HOH A O   
2222 O  O   . HOH L .   ? 0.5734 0.8853 0.3577 -0.3154 0.2717  -0.2448 415 HOH A O   
2223 O  O   . HOH L .   ? 0.2755 0.4766 0.7829 -0.0873 -0.1552 0.1402  416 HOH A O   
2224 O  O   . HOH L .   ? 0.6357 0.4670 0.3021 0.0140  0.1280  -0.0540 417 HOH A O   
2225 O  O   . HOH L .   ? 0.3973 0.4752 0.7057 0.1140  -0.1080 -0.1581 418 HOH A O   
2226 O  O   . HOH L .   ? 0.3911 0.2425 1.0141 0.0710  0.1509  0.1342  419 HOH A O   
2227 O  O   . HOH L .   ? 0.3998 0.4406 0.1269 0.0730  0.0293  0.0050  420 HOH A O   
2228 O  O   . HOH L .   ? 0.8513 0.8045 0.6025 -0.0846 -0.1752 0.3309  421 HOH A O   
2229 O  O   . HOH L .   ? 0.1432 0.2758 0.3438 0.0593  -0.0987 -0.0754 422 HOH A O   
2230 O  O   . HOH L .   ? 0.3488 0.2443 0.3796 -0.0115 0.0829  0.0498  423 HOH A O   
2231 O  O   . HOH L .   ? 0.3661 0.4092 0.8151 0.0451  -0.0203 -0.2874 424 HOH A O   
2232 O  O   . HOH L .   ? 0.6057 0.9166 0.2649 -0.3485 0.1098  0.0451  425 HOH A O   
2233 O  O   . HOH L .   ? 0.2368 0.5334 0.5418 0.0055  0.0884  0.0970  426 HOH A O   
2234 O  O   . HOH L .   ? 0.4886 0.4009 0.7191 -0.1878 -0.0719 0.1195  427 HOH A O   
2235 O  O   . HOH L .   ? 0.4569 0.3554 0.6688 -0.0385 0.2857  -0.0064 428 HOH A O   
2236 O  O   . HOH L .   ? 0.3581 0.3761 0.3431 0.1040  0.1766  -0.0085 429 HOH A O   
2237 O  O   . HOH L .   ? 0.2287 0.3177 0.4576 0.0700  0.1092  0.1372  430 HOH A O   
2238 O  O   . HOH L .   ? 0.2619 0.2391 0.2319 -0.0854 -0.0044 -0.0417 431 HOH A O   
2239 O  O   . HOH L .   ? 0.1018 0.1646 0.1747 -0.0381 0.0351  0.0036  432 HOH A O   
2240 O  O   . HOH L .   ? 0.2302 0.2544 0.4192 0.0000  -0.1752 -0.0717 433 HOH A O   
2241 O  O   . HOH L .   ? 0.2569 0.6437 0.6527 -0.0384 0.0418  0.3325  434 HOH A O   
2242 O  O   . HOH L .   ? 0.3937 0.3244 0.2597 -0.2068 -0.0336 0.0472  435 HOH A O   
2243 O  O   . HOH L .   ? 0.2411 0.1993 0.3125 -0.0427 -0.0370 0.0189  436 HOH A O   
2244 O  O   . HOH L .   ? 0.4424 0.5437 0.3187 -0.1107 0.0460  -0.1876 437 HOH A O   
2245 O  O   . HOH L .   ? 0.2615 0.7845 0.5103 -0.1794 0.1306  -0.2086 438 HOH A O   
2246 O  O   . HOH L .   ? 0.0496 0.1531 0.1336 0.0038  0.0119  -0.0148 439 HOH A O   
2247 O  O   . HOH L .   ? 0.6560 0.4995 0.5274 0.1207  -0.1717 -0.4493 440 HOH A O   
2248 O  O   . HOH L .   ? 0.4449 0.3754 0.4343 -0.1140 0.2229  -0.1230 441 HOH A O   
2249 O  O   . HOH L .   ? 0.6551 0.3521 0.4716 0.0223  -0.1848 -0.0983 442 HOH A O   
2250 O  O   . HOH L .   ? 0.4697 0.4529 0.5191 0.1346  -0.0238 -0.0373 443 HOH A O   
2251 O  O   . HOH L .   ? 0.4320 0.3581 0.2440 -0.0632 -0.0383 0.0895  444 HOH A O   
2252 O  O   . HOH L .   ? 0.1283 0.3845 0.4719 0.0747  0.0003  0.0081  445 HOH A O   
2253 O  O   . HOH L .   ? 0.2511 0.6711 0.4663 0.1096  0.1552  -0.0842 446 HOH A O   
2254 O  O   . HOH L .   ? 0.2676 0.2138 0.3922 -0.0337 0.0586  -0.0581 447 HOH A O   
2255 O  O   . HOH L .   ? 0.5368 0.4174 0.2512 -0.2601 -0.1041 -0.0018 448 HOH A O   
2256 O  O   . HOH L .   ? 0.5863 0.3865 0.6075 0.0943  0.1852  -0.0167 449 HOH A O   
2257 O  O   . HOH L .   ? 0.3858 0.2827 0.4726 0.0300  0.0818  -0.1226 450 HOH A O   
2258 O  O   . HOH L .   ? 0.4189 0.7531 0.2566 -0.2990 -0.0979 0.1557  451 HOH A O   
2259 O  O   . HOH L .   ? 0.3768 0.3881 0.1929 -0.0042 0.1628  -0.0952 452 HOH A O   
2260 O  O   . HOH L .   ? 0.2274 0.2824 0.3707 0.0406  -0.0006 -0.0096 453 HOH A O   
2261 O  O   . HOH L .   ? 0.3355 0.4857 0.5976 -0.1344 0.3146  -0.2612 454 HOH A O   
2262 O  O   . HOH L .   ? 0.1243 0.2499 0.2669 0.0417  -0.0188 0.0250  455 HOH A O   
2263 O  O   . HOH L .   ? 0.5668 0.3212 0.1109 0.0089  -0.0006 0.0006  456 HOH A O   
2264 O  O   . HOH L .   ? 0.2679 0.1592 0.3068 -0.0662 -0.0857 0.0587  457 HOH A O   
2265 O  O   . HOH L .   ? 0.1511 0.1849 0.1229 0.0168  0.0796  0.0231  458 HOH A O   
2266 O  O   . HOH L .   ? 0.1560 0.2669 0.2508 0.0738  0.1034  0.0644  459 HOH A O   
2267 O  O   . HOH L .   ? 0.4053 0.4091 0.1903 -0.0541 -0.1280 0.0210  460 HOH A O   
2268 O  O   . HOH L .   ? 0.0644 0.1065 0.1415 -0.0134 0.0345  -0.0203 461 HOH A O   
2269 O  O   . HOH L .   ? 0.2522 0.4835 0.2382 0.0792  -0.0445 0.1184  462 HOH A O   
2270 O  O   . HOH L .   ? 0.1142 0.4512 0.5493 -0.0542 -0.0299 0.0033  463 HOH A O   
2271 O  O   . HOH L .   ? 0.3402 0.1693 0.3100 -0.0735 0.1453  -0.0547 464 HOH A O   
2272 O  O   . HOH L .   ? 0.0544 0.1441 0.1333 0.0201  0.0263  -0.0089 465 HOH A O   
2273 O  O   . HOH L .   ? 0.2651 0.4144 0.3129 -0.1007 0.0290  0.0417  466 HOH A O   
2274 O  O   . HOH L .   ? 0.1764 0.2615 0.3092 -0.0250 0.0129  0.0763  467 HOH A O   
2275 O  O   . HOH L .   ? 0.3662 0.2393 0.1968 -0.0712 0.0141  0.0723  468 HOH A O   
2276 O  O   . HOH L .   ? 0.2988 0.4329 0.7706 0.0203  0.0447  0.0009  469 HOH A O   
2277 O  O   . HOH L .   ? 0.1720 0.2015 0.1887 0.0617  0.0055  -0.0036 470 HOH A O   
2278 O  O   . HOH L .   ? 0.2263 0.6100 0.4839 0.1403  -0.0552 -0.2640 471 HOH A O   
2279 O  O   . HOH L .   ? 0.2792 0.4601 0.4498 -0.0359 -0.0798 0.1879  472 HOH A O   
2280 O  O   . HOH L .   ? 0.0652 0.1124 0.1117 0.0175  0.0089  -0.0166 473 HOH A O   
2281 O  O   . HOH L .   ? 0.0820 0.1878 0.3236 -0.0458 -0.0414 0.0150  474 HOH A O   
2282 O  O   . HOH L .   ? 0.3617 0.3448 0.5273 -0.2006 -0.1745 0.1855  475 HOH A O   
2283 O  O   . HOH L .   ? 0.2849 0.6041 0.4332 0.0087  0.1404  0.1196  476 HOH A O   
2284 O  O   . HOH L .   ? 0.2809 0.3973 0.5168 0.0597  -0.0041 -0.0236 477 HOH A O   
2285 O  O   . HOH L .   ? 0.1745 0.1900 0.2095 0.0631  -0.0646 -0.0012 478 HOH A O   
2286 O  O   . HOH L .   ? 0.3086 0.3363 0.3226 -0.1092 -0.0217 0.1023  479 HOH A O   
2287 O  O   . HOH L .   ? 0.0379 0.1592 0.1599 0.0109  -0.0366 0.0166  480 HOH A O   
2288 O  O   . HOH L .   ? 0.4365 0.2968 0.5908 -0.1863 0.0248  -0.0781 481 HOH A O   
2289 O  O   . HOH L .   ? 0.1838 0.3207 0.4428 0.0593  0.0484  -0.0929 482 HOH A O   
2290 O  O   . HOH L .   ? 0.4138 0.9460 0.4112 -0.0114 -0.0989 0.1577  483 HOH A O   
2291 O  O   . HOH L .   ? 0.1108 0.1312 0.2018 -0.0354 -0.0031 0.0125  484 HOH A O   
2292 O  O   . HOH L .   ? 0.1196 0.1817 0.3381 0.0447  -0.0281 0.0145  485 HOH A O   
2293 O  O   . HOH L .   ? 0.0738 0.1836 0.2380 -0.0040 0.0372  -0.0011 486 HOH A O   
2294 O  O   . HOH L .   ? 0.2452 0.3227 0.3784 0.0447  -0.0498 0.0359  487 HOH A O   
2295 O  O   . HOH L .   ? 0.1897 0.4436 0.3399 -0.0302 0.0836  0.0154  488 HOH A O   
2296 O  O   . HOH L .   ? 0.1412 0.3552 0.1833 -0.0359 0.1151  -0.0847 489 HOH A O   
2297 O  O   . HOH L .   ? 0.3718 0.1588 0.3018 0.1360  -0.0511 -0.0004 490 HOH A O   
2298 O  O   . HOH L .   ? 0.1907 0.4498 0.5942 0.0972  -0.0759 0.0923  491 HOH A O   
2299 O  O   . HOH L .   ? 0.1364 0.2300 0.2425 -0.0054 -0.0220 -0.0102 492 HOH A O   
2300 O  O   . HOH L .   ? 0.0251 0.1058 0.1382 -0.0150 0.0472  -0.0044 493 HOH A O   
2301 O  O   . HOH L .   ? 0.2716 0.3037 0.2356 -0.0890 0.0516  -0.0934 494 HOH A O   
2302 O  O   . HOH L .   ? 0.4156 0.2785 0.4986 -0.0911 -0.1527 0.0751  495 HOH A O   
2303 O  O   . HOH L .   ? 0.1569 0.3556 0.2361 0.0177  0.0252  -0.0541 496 HOH A O   
2304 O  O   . HOH L .   ? 0.4669 0.9274 0.2281 -0.0693 -0.0336 0.0285  497 HOH A O   
2305 O  O   . HOH L .   ? 0.7533 0.3743 1.1492 -0.1423 0.3561  -0.1403 498 HOH A O   
2306 O  O   . HOH L .   ? 0.3827 0.4225 0.2001 -0.0478 -0.0674 0.0990  499 HOH A O   
2307 O  O   . HOH L .   ? 0.2039 0.2956 0.3460 0.0851  0.0942  0.1094  500 HOH A O   
2308 O  O   . HOH L .   ? 0.4113 0.3359 0.4418 -0.0630 0.0978  0.1482  501 HOH A O   
2309 O  O   . HOH L .   ? 0.9096 0.2429 0.4295 -0.0419 -0.1398 -0.0116 502 HOH A O   
2310 O  O   . HOH L .   ? 0.6481 0.2788 0.2509 0.0588  0.0639  0.0547  503 HOH A O   
2311 O  O   . HOH L .   ? 0.4918 0.4178 0.6063 0.1763  0.0474  -0.1420 504 HOH A O   
2312 O  O   . HOH L .   ? 0.1826 0.2242 0.3345 0.0140  0.0174  -0.0407 505 HOH A O   
2313 O  O   . HOH L .   ? 0.2331 0.9696 0.3991 0.0803  -0.0188 -0.1146 506 HOH A O   
2314 O  O   . HOH L .   ? 0.2784 0.4480 0.3394 -0.1923 -0.0716 0.1080  507 HOH A O   
2315 O  O   . HOH L .   ? 0.2115 0.4950 0.2667 -0.1606 0.0379  -0.0168 508 HOH A O   
2316 O  O   . HOH L .   ? 0.5976 0.2720 0.4002 0.1784  0.0025  -0.0243 509 HOH A O   
2317 O  O   . HOH L .   ? 0.1609 0.1937 0.1648 -0.0164 -0.0563 -0.0053 510 HOH A O   
2318 O  O   . HOH L .   ? 0.0205 0.1501 0.1782 -0.0109 0.0216  -0.0425 511 HOH A O   
2319 O  O   . HOH L .   ? 0.3725 0.5019 0.4557 -0.1883 -0.1644 -0.0284 512 HOH A O   
2320 O  O   . HOH L .   ? 0.2667 0.8275 0.5649 0.1509  -0.0796 -0.4256 513 HOH A O   
2321 O  O   . HOH L .   ? 0.2091 0.3007 0.6070 -0.0234 0.0223  0.2043  514 HOH A O   
2322 O  O   . HOH L .   ? 0.1933 0.6697 0.3305 -0.0344 -0.0065 -0.1335 515 HOH A O   
2323 O  O   . HOH L .   ? 0.2212 0.3315 0.3851 0.0011  -0.1043 0.0434  516 HOH A O   
2324 O  O   . HOH L .   ? 0.1808 0.4612 0.2709 0.1421  0.0669  0.1935  517 HOH A O   
2325 O  O   . HOH L .   ? 0.0761 0.1368 0.1875 0.0124  -0.0013 0.0233  518 HOH A O   
2326 O  O   . HOH L .   ? 0.7077 0.4824 0.5798 0.0800  -0.2277 -0.1091 519 HOH A O   
2327 O  O   . HOH L .   ? 0.1630 0.1237 0.2438 0.0148  -0.0021 -0.0241 520 HOH A O   
2328 O  O   . HOH L .   ? 0.5254 0.8294 0.3471 0.2244  -0.0487 0.0678  521 HOH A O   
2329 O  O   . HOH L .   ? 0.3484 0.3848 0.7733 0.0707  0.0493  0.1417  522 HOH A O   
2330 O  O   . HOH L .   ? 0.7799 0.3369 0.4979 -0.2465 0.0929  0.0380  523 HOH A O   
2331 O  O   . HOH L .   ? 0.2181 0.2210 0.1524 -0.0258 0.0105  -0.0052 524 HOH A O   
2332 O  O   . HOH L .   ? 0.2289 0.1781 0.4518 -0.0511 0.2073  -0.0756 525 HOH A O   
2333 O  O   . HOH L .   ? 0.4156 0.5322 0.5047 0.0566  0.0070  -0.2229 526 HOH A O   
2334 O  O   . HOH L .   ? 0.4284 0.3518 0.2667 -0.0515 0.0961  0.1213  527 HOH A O   
2335 O  O   . HOH L .   ? 0.2971 0.2405 0.4124 -0.0790 0.1199  -0.0738 528 HOH A O   
2336 O  O   . HOH L .   ? 0.1858 0.1879 0.2795 -0.0469 0.0978  -0.0563 529 HOH A O   
2337 O  O   . HOH L .   ? 0.1627 0.2029 0.3678 -0.0529 0.0460  -0.0193 530 HOH A O   
2338 O  O   . HOH L .   ? 0.5844 0.5128 0.3453 0.2755  0.2439  0.2278  531 HOH A O   
2339 O  O   . HOH L .   ? 0.1426 0.2601 0.2478 0.0568  -0.0267 -0.0108 532 HOH A O   
2340 O  O   . HOH L .   ? 0.2447 0.6767 0.2712 0.0732  0.0473  0.1753  533 HOH A O   
2341 O  O   . HOH L .   ? 0.2142 0.2655 0.3798 -0.0406 0.0623  -0.0348 534 HOH A O   
2342 O  O   . HOH L .   ? 0.1269 0.2992 0.6597 0.0039  0.0422  -0.1673 535 HOH A O   
2343 O  O   . HOH L .   ? 0.5933 0.4544 0.4904 -0.3116 -0.2154 0.0337  536 HOH A O   
2344 O  O   . HOH L .   ? 0.2461 0.5183 0.5341 -0.1189 0.1070  -0.0414 537 HOH A O   
2345 O  O   . HOH L .   ? 0.1664 0.2011 0.2557 -0.0035 -0.0420 -0.0034 538 HOH A O   
2346 O  O   . HOH L .   ? 0.2503 0.2995 0.1897 0.1034  0.1017  0.0863  539 HOH A O   
2347 O  O   . HOH L .   ? 0.2839 0.3736 0.3922 -0.0263 0.0133  0.1795  540 HOH A O   
2348 O  O   . HOH L .   ? 0.5116 0.8362 0.6434 0.1305  0.2788  0.2746  541 HOH A O   
2349 O  O   . HOH L .   ? 0.7394 0.3374 0.4647 -0.1158 0.1012  0.1263  542 HOH A O   
2350 O  O   . HOH L .   ? 0.1847 0.4777 0.3129 0.0644  0.0460  0.0579  543 HOH A O   
2351 O  O   . HOH L .   ? 0.5969 0.4123 0.3179 -0.1769 0.1879  -0.1480 544 HOH A O   
2352 O  O   . HOH L .   ? 0.1499 0.3032 0.5462 -0.0719 0.1265  -0.0223 545 HOH A O   
2353 O  O   . HOH L .   ? 0.2016 0.7110 0.4924 -0.1160 0.0767  -0.0642 546 HOH A O   
2354 O  O   . HOH L .   ? 0.0824 0.1807 0.2404 -0.0122 0.0291  -0.0289 547 HOH A O   
2355 O  O   . HOH L .   ? 0.5750 0.3352 0.3606 0.1551  0.2312  0.1729  548 HOH A O   
2356 O  O   . HOH L .   ? 0.5498 0.4045 0.5644 0.2380  0.1870  0.2311  549 HOH A O   
2357 O  O   . HOH L .   ? 0.3018 0.5274 0.7697 -0.1301 0.2949  -0.1793 550 HOH A O   
2358 O  O   . HOH L .   ? 0.2173 0.2983 0.4231 0.1039  -0.1055 -0.1405 551 HOH A O   
2359 O  O   . HOH L .   ? 0.2105 0.2227 0.2580 0.0335  -0.0581 -0.0873 552 HOH A O   
2360 O  O   . HOH L .   ? 0.2734 0.3854 0.3732 -0.0161 0.0310  0.0298  553 HOH A O   
2361 O  O   . HOH L .   ? 0.1570 0.1445 0.2180 -0.0110 0.0159  0.0222  554 HOH A O   
2362 O  O   . HOH L .   ? 0.7823 0.2557 0.4293 0.1861  -0.1461 -0.1584 555 HOH A O   
2363 O  O   . HOH L .   ? 0.1632 0.6727 1.1447 0.2397  -0.0583 -0.3346 556 HOH A O   
2364 O  O   . HOH L .   ? 0.0768 0.2431 0.4304 0.0271  0.0370  -0.0465 557 HOH A O   
2365 O  O   . HOH L .   ? 0.0129 0.2511 0.1670 0.0286  0.0170  -0.0462 558 HOH A O   
2366 O  O   . HOH L .   ? 0.3018 0.4239 0.1846 0.1178  -0.0136 0.0228  559 HOH A O   
2367 O  O   . HOH L .   ? 0.2443 0.5850 0.6236 -0.0738 0.0807  0.1171  560 HOH A O   
2368 O  O   . HOH L .   ? 0.0937 0.1603 0.2179 0.0194  -0.0222 0.0055  561 HOH A O   
2369 O  O   . HOH L .   ? 0.2659 0.2893 0.2317 -0.0885 -0.0125 -0.0453 562 HOH A O   
2370 O  O   . HOH L .   ? 0.3798 0.2709 0.2404 -0.0243 0.0460  0.0203  563 HOH A O   
2371 O  O   . HOH L .   ? 0.4676 0.3413 0.2173 0.2665  -0.0564 0.0010  564 HOH A O   
2372 O  O   . HOH L .   ? 0.3086 0.8360 0.2909 -0.0947 0.0471  0.0561  565 HOH A O   
2373 O  O   . HOH L .   ? 0.1610 0.3130 0.1835 0.0207  0.0036  0.0618  566 HOH A O   
2374 O  O   . HOH L .   ? 0.0451 0.2572 0.1531 0.0113  -0.0276 0.0449  567 HOH A O   
2375 O  O   . HOH L .   ? 0.1979 0.5405 0.1544 0.1805  -0.0259 -0.0263 568 HOH A O   
2376 O  O   . HOH L .   ? 0.2496 0.2397 0.4485 0.0151  0.0027  -0.0069 569 HOH A O   
2377 O  O   . HOH L .   ? 0.3649 0.4246 0.5507 -0.0223 0.0741  -0.1146 570 HOH A O   
2378 O  O   . HOH L .   ? 0.2734 0.2192 0.2273 0.0271  0.0961  0.0853  571 HOH A O   
2379 O  O   . HOH L .   ? 0.0924 0.2690 0.2834 0.0536  -0.0652 0.0063  572 HOH A O   
2380 O  O   . HOH L .   ? 0.1474 0.2981 0.2917 0.0033  0.0018  0.0111  573 HOH A O   
2381 O  O   . HOH L .   ? 0.3832 0.2124 0.2989 0.0818  0.0412  0.0884  574 HOH A O   
2382 O  O   . HOH L .   ? 0.1700 0.2133 0.3606 0.0336  -0.0669 0.0673  575 HOH A O   
2383 O  O   . HOH L .   ? 0.1344 0.3132 0.2648 0.0867  0.0577  0.0337  576 HOH A O   
2384 O  O   . HOH L .   ? 0.2295 0.2546 0.6778 -0.0474 0.0339  -0.1496 577 HOH A O   
2385 O  O   . HOH L .   ? 0.3355 0.5195 0.7111 -0.1346 0.0113  0.0855  578 HOH A O   
2386 O  O   . HOH L .   ? 0.0813 0.4207 0.4266 0.0184  -0.0019 0.0735  579 HOH A O   
2387 O  O   . HOH L .   ? 0.0695 0.1138 0.1542 0.0122  0.0117  -0.0143 580 HOH A O   
2388 O  O   . HOH L .   ? 0.2921 0.7930 0.3204 -0.0172 0.0403  0.0998  581 HOH A O   
2389 O  O   . HOH L .   ? 0.2353 0.3944 0.9302 -0.1122 0.1155  -0.1835 582 HOH A O   
2390 O  O   . HOH L .   ? 0.1910 0.1860 0.1551 0.0622  -0.0311 -0.0288 583 HOH A O   
2391 O  O   . HOH L .   ? 0.3621 0.4630 0.4723 -0.0076 0.1897  -0.0781 584 HOH A O   
2392 O  O   . HOH L .   ? 0.3876 0.9627 0.6706 -0.0340 0.0269  0.5223  585 HOH A O   
2393 O  O   . HOH L .   ? 0.2843 0.5605 0.4289 0.1474  0.0915  0.0796  586 HOH A O   
2394 O  O   . HOH L .   ? 0.4071 0.6847 0.3010 0.0987  -0.0073 0.0309  587 HOH A O   
2395 O  O   . HOH L .   ? 0.3265 0.3169 0.4447 0.0179  -0.0214 -0.0264 588 HOH A O   
2396 O  O   . HOH L .   ? 0.4235 0.3341 0.5790 0.0289  0.3278  0.0080  589 HOH A O   
2397 O  O   . HOH L .   ? 0.2393 0.4390 0.2957 0.0788  0.0901  0.0519  590 HOH A O   
2398 O  O   . HOH L .   ? 0.5026 0.4268 0.5184 -0.0236 -0.0726 0.1251  591 HOH A O   
2399 O  O   . HOH L .   ? 0.6793 0.2523 0.4559 0.0444  0.3398  0.0606  592 HOH A O   
2400 O  O   . HOH L .   ? 0.3118 0.5960 0.2913 0.0829  0.1144  0.2312  593 HOH A O   
2401 O  O   . HOH L .   ? 0.3269 0.1596 0.2641 0.0954  0.0292  -0.0585 594 HOH A O   
2402 O  O   . HOH L .   ? 0.7643 0.2685 0.5227 0.1154  -0.2706 -0.1094 595 HOH A O   
2403 O  O   . HOH L .   ? 0.2054 0.2605 0.4194 0.0881  -0.0129 0.0845  596 HOH A O   
2404 O  O   . HOH L .   ? 0.5012 0.8591 0.3286 -0.2947 0.1192  -0.1492 597 HOH A O   
2405 O  O   . HOH L .   ? 0.0530 0.1835 0.3315 -0.0039 0.0013  0.0130  598 HOH A O   
2406 O  O   . HOH L .   ? 0.5711 0.7698 0.2231 0.2155  -0.2942 -0.0054 599 HOH A O   
2407 O  O   . HOH L .   ? 0.5496 0.7783 0.2960 -0.0724 0.1454  -0.1930 600 HOH A O   
2408 O  O   . HOH L .   ? 0.3173 0.5083 0.6329 0.1014  0.0188  -0.1496 601 HOH A O   
2409 O  O   . HOH L .   ? 0.4917 0.3747 0.4992 0.0174  -0.1160 -0.2135 602 HOH A O   
2410 O  O   . HOH L .   ? 0.6623 0.5899 0.4404 0.2830  0.0456  0.2863  603 HOH A O   
2411 O  O   . HOH L .   ? 0.3075 1.2093 0.4300 -0.0500 0.0489  0.3792  604 HOH A O   
2412 O  O   . HOH L .   ? 0.3268 0.3495 0.7684 -0.1363 -0.0070 0.1497  605 HOH A O   
2413 O  O   . HOH L .   ? 0.2763 0.2440 0.3055 0.1004  0.1238  0.0976  606 HOH A O   
2414 O  O   . HOH L .   ? 0.4439 0.4017 0.5466 0.0291  -0.0234 -0.1444 607 HOH A O   
2415 O  O   . HOH L .   ? 0.1610 0.2407 0.7337 -0.0223 -0.0390 0.0578  608 HOH A O   
2416 O  O   . HOH L .   ? 0.6510 0.2974 0.5082 0.0834  0.3888  0.0443  609 HOH A O   
2417 O  O   . HOH L .   ? 0.9266 0.4437 0.4630 -0.0910 -0.0249 0.1007  610 HOH A O   
2418 O  O   . HOH L .   ? 0.4889 0.3567 0.9572 -0.0159 -0.2997 -0.1638 611 HOH A O   
2419 O  O   . HOH L .   ? 0.3159 0.3010 0.4763 -0.0168 -0.0974 -0.0348 612 HOH A O   
2420 O  O   . HOH L .   ? 0.3069 0.3951 0.3274 -0.0332 0.0467  -0.0968 613 HOH A O   
2421 O  O   . HOH L .   ? 0.4320 0.3618 0.6559 -0.0043 0.0396  0.0381  614 HOH A O   
2422 O  O   . HOH L .   ? 0.2935 0.3482 0.2895 0.0303  0.1250  0.1458  615 HOH A O   
2423 O  O   . HOH L .   ? 0.1700 0.5747 0.6114 -0.0716 0.0763  -0.0417 616 HOH A O   
2424 O  O   . HOH L .   ? 0.4996 0.4112 0.9542 0.0406  0.3145  -0.1185 617 HOH A O   
2425 O  O   . HOH L .   ? 0.6470 0.7006 0.2573 0.3840  0.0430  0.0985  618 HOH A O   
2426 O  O   . HOH L .   ? 0.2407 0.1820 0.3822 -0.0266 -0.0757 -0.0418 619 HOH A O   
2427 O  O   . HOH L .   ? 0.2728 0.4684 0.5100 -0.1059 0.0346  0.0286  620 HOH A O   
2428 O  O   . HOH L .   ? 0.3758 0.2982 0.4593 0.0365  -0.2480 0.0892  621 HOH A O   
2429 O  O   . HOH L .   ? 1.0783 0.4724 0.7912 0.4113  0.2411  0.3019  622 HOH A O   
2430 O  O   . HOH L .   ? 0.2958 0.3729 0.3028 0.0440  -0.0239 -0.0791 623 HOH A O   
2431 O  O   . HOH L .   ? 0.8369 0.5890 0.5840 -0.2022 -0.1483 0.2299  624 HOH A O   
2432 O  O   . HOH L .   ? 0.4194 0.3837 0.5518 -0.1567 0.1103  -0.1544 625 HOH A O   
2433 O  O   . HOH L .   ? 0.2312 0.3832 0.8359 -0.0572 -0.0763 -0.1267 626 HOH A O   
2434 O  O   . HOH L .   ? 0.2507 0.8394 0.4451 0.1634  -0.1280 -0.0480 627 HOH A O   
2435 O  O   . HOH L .   ? 0.5120 0.6718 0.9036 0.0049  0.2366  0.0559  628 HOH A O   
2436 O  O   . HOH L .   ? 0.4207 0.2903 0.5374 0.1100  -0.0842 0.0702  629 HOH A O   
2437 O  O   . HOH L .   ? 0.7889 0.5497 0.6091 0.0019  0.2546  0.0009  630 HOH A O   
2438 O  O   . HOH L .   ? 0.0996 0.6034 0.6390 0.0504  -0.0314 -0.0533 631 HOH A O   
2439 O  O   . HOH L .   ? 0.4478 0.5519 0.4169 -0.0817 -0.0607 -0.0021 632 HOH A O   
2440 O  O   . HOH L .   ? 0.2514 0.3168 0.3151 -0.0494 -0.0555 0.0552  633 HOH A O   
2441 O  O   . HOH L .   ? 0.2663 0.5345 0.3747 0.0072  0.0369  -0.0798 634 HOH A O   
2442 O  O   . HOH L .   ? 0.2084 0.5490 0.4462 -0.0151 -0.0417 -0.2214 635 HOH A O   
2443 O  O   . HOH L .   ? 0.3044 0.4092 0.5592 0.0296  0.1694  -0.0930 636 HOH A O   
2444 O  O   . HOH L .   ? 0.5647 0.7228 0.4209 0.1000  0.1548  0.1237  637 HOH A O   
2445 O  O   . HOH L .   ? 0.2713 0.8365 0.8108 0.0186  -0.2526 -0.2982 638 HOH A O   
2446 O  O   . HOH L .   ? 0.2961 0.6632 0.3189 -0.2368 0.1544  -0.1560 639 HOH A O   
2447 O  O   . HOH L .   ? 0.4439 0.5182 0.6522 0.0436  -0.0643 -0.0164 640 HOH A O   
2448 O  O   . HOH L .   ? 0.3639 0.3730 0.8895 -0.0889 -0.1367 0.0462  641 HOH A O   
2449 O  O   . HOH L .   ? 0.2979 0.5406 0.4354 0.1304  -0.0796 -0.0225 642 HOH A O   
2450 O  O   . HOH L .   ? 0.4110 0.4432 0.2810 -0.1030 0.1215  0.0824  643 HOH A O   
2451 O  O   . HOH L .   ? 0.4600 0.5369 0.6466 -0.0752 0.2208  -0.0704 644 HOH A O   
2452 O  O   . HOH L .   ? 0.4561 0.4616 0.9018 -0.0395 0.2810  -0.2220 645 HOH A O   
2453 O  O   . HOH L .   ? 0.5340 0.8214 0.6995 -0.0517 -0.1597 0.3130  646 HOH A O   
2454 O  O   . HOH L .   ? 0.4831 0.4582 0.6848 0.1171  0.1031  -0.1167 647 HOH A O   
2455 O  O   . HOH L .   ? 0.4379 0.5820 0.5480 0.0089  0.0974  0.1808  648 HOH A O   
2456 O  O   . HOH L .   ? 0.5554 0.5025 0.5396 -0.1034 -0.2379 0.0728  649 HOH A O   
2457 O  O   . HOH L .   ? 0.2835 0.4422 0.4821 -0.0331 0.0215  0.1761  650 HOH A O   
2458 O  O   . HOH L .   ? 0.2198 0.2032 0.2759 0.0675  -0.0216 0.0155  651 HOH A O   
2459 O  O   . HOH L .   ? 0.5205 0.2728 0.6973 0.0465  0.1150  -0.1262 652 HOH A O   
2460 O  O   . HOH L .   ? 0.1516 0.3632 0.9066 0.0297  -0.0245 -0.0981 653 HOH A O   
2461 O  O   . HOH L .   ? 0.3766 0.2710 0.7659 0.0232  -0.0763 -0.0638 654 HOH A O   
2462 O  O   . HOH L .   ? 0.4584 0.5327 0.5542 0.3173  0.0380  0.0495  655 HOH A O   
2463 O  O   . HOH L .   ? 0.4066 0.5732 0.3589 -0.0710 0.1439  0.1177  656 HOH A O   
2464 O  O   . HOH L .   ? 0.4961 0.3740 0.5183 -0.1791 0.0928  -0.1120 657 HOH A O   
2465 O  O   . HOH L .   ? 0.6664 0.8795 0.8269 -0.1646 -0.1832 0.2061  658 HOH A O   
2466 O  O   . HOH L .   ? 0.2864 0.5528 0.7253 -0.2376 -0.2282 -0.0521 659 HOH A O   
2467 O  O   . HOH L .   ? 0.9013 0.3090 0.3934 -0.1353 0.2985  -0.0961 660 HOH A O   
2468 O  O   . HOH L .   ? 0.3129 0.3184 0.3489 -0.1259 -0.0011 0.0886  661 HOH A O   
2469 O  O   . HOH L .   ? 0.3000 0.4126 0.7746 0.1163  0.0983  0.0125  662 HOH A O   
2470 O  O   . HOH L .   ? 0.2960 0.4155 0.1282 0.0948  0.0857  0.0019  663 HOH A O   
2471 O  O   . HOH L .   ? 0.1767 0.2276 0.3689 -0.0075 0.0152  -0.0260 664 HOH A O   
2472 O  O   . HOH L .   ? 0.4710 0.4561 0.3852 -0.1496 0.1192  -0.1504 665 HOH A O   
2473 O  O   . HOH L .   ? 0.2824 0.6152 0.5477 -0.1099 -0.0091 -0.1747 666 HOH A O   
2474 O  O   . HOH L .   ? 0.3043 0.2663 0.7014 -0.0951 0.1518  0.1004  667 HOH A O   
2475 O  O   . HOH L .   ? 0.3592 0.2726 0.3772 0.0132  0.1112  0.0564  668 HOH A O   
2476 O  O   . HOH L .   ? 0.4264 0.3536 0.8881 0.0179  0.1685  0.1743  669 HOH A O   
2477 O  O   . HOH L .   ? 0.3201 0.4447 0.3826 0.1224  0.0270  0.1200  670 HOH A O   
2478 O  O   . HOH L .   ? 0.3227 0.2888 0.6136 0.0103  0.1697  0.0504  671 HOH A O   
2479 O  O   . HOH L .   ? 1.3516 0.6279 0.5509 0.3611  0.1590  0.3649  672 HOH A O   
2480 O  O   . HOH L .   ? 0.2475 0.5314 0.4875 -0.1323 0.0506  0.0475  673 HOH A O   
2481 O  O   . HOH L .   ? 0.5694 0.3585 0.6211 0.1393  0.0811  0.1219  674 HOH A O   
2482 O  O   . HOH L .   ? 0.6824 0.4480 0.5507 0.1639  -0.0115 -0.1504 675 HOH A O   
# 
