data_7NZU
# 
_entry.id   7NZU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.384 
_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   7NZU         pdb_00007nzu 10.2210/pdb7nzu/pdb 
WWPDB D_1292114759 ?            ?                   
# 
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 2022-04-13 
2 'Structure model' 1 1 2024-01-31 
# 
_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' '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' pdbx_initial_refinement_model 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7NZU 
_pdbx_database_status.recvd_initial_deposition_date   2021-03-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_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' 7NZR unspecified 
PDB 'PDB entry for the same citation' 7NZS unspecified 
PDB 'PDB entry for the same citation' 7NZT unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 0000-0001-5080-9367 
'Manakova, E.' 2 0000-0002-6027-2265 
'Grazulis, S.' 3 0000-0002-7928-5218 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of chimeric carbonic anhydrase VA' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Smirnov, A.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0001-5080-9367 
# 
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'                                                           29377.160 1   4.2.1.1 
'N62T, H64Y, A65L, N67Q, I91K, F130Y, L203T' ? ? 
2 non-polymer syn 'ZINC ION'                                                                       65.409    1   ?       ? ? ? 
3 non-polymer syn '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 424.415   1   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                             78.133    1   ?       ? ? ? 
5 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                           195.237   1   ?       ? ? ? 
6 non-polymer syn BICINE                                                                           163.172   1   ?       ? ? ? 
7 water       nat water                                                                            18.015    291 ?       ? ? ? 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNTGYLFQVEFDDSQDKAVLK
GGPLDGTYRLKQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLTECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNTGYLFQVEFDDSQDKAVLK
GGPLDGTYRLKQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
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-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' WWO 
4 'DIMETHYL SULFOXIDE'                                                             DMS 
5 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                           MES 
6 BICINE                                                                           BCN 
7 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  THR n 
1 63  GLY n 
1 64  TYR n 
1 65  LEU 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  LYS 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 VAL 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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                          ? 'C3 H7 N O2'          
89.093  
ARG 'L-peptide linking' y ARGININE                                                                         ? 'C6 H15 N4 O2 1'      
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                       ? 'C4 H8 N2 O3'         
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                  ? 'C4 H7 N O4'          
133.103 
BCN non-polymer         . BICINE                                                                           ? 'C6 H13 N O4'         
163.172 
CYS 'L-peptide linking' y CYSTEINE                                                                         ? 'C3 H7 N O2 S'        
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                             ? 'C2 H6 O S'           
78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                                        ? 'C5 H10 N2 O3'        
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                  ? 'C5 H9 N O4'          
147.129 
GLY 'peptide linking'   y GLYCINE                                                                          ? 'C2 H5 N O2'          
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                        ? 'C6 H10 N3 O2 1'      
156.162 
HOH non-polymer         . WATER                                                                            ? 'H2 O'                
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                       ? 'C6 H13 N O2'         
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                          ? 'C6 H13 N O2'         
131.173 
LYS 'L-peptide linking' y LYSINE                                                                           ? 'C6 H15 N2 O2 1'      
147.195 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                           ? 'C6 H13 N O4 S'       
195.237 
MET 'L-peptide linking' y METHIONINE                                                                       ? 'C5 H11 N O2 S'       
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                    ? 'C9 H11 N O2'         
165.189 
PRO 'L-peptide linking' y PROLINE                                                                          ? 'C5 H9 N O2'          
115.130 
SER 'L-peptide linking' y SERINE                                                                           ? 'C3 H7 N O3'          
105.093 
THR 'L-peptide linking' y THREONINE                                                                        ? 'C4 H9 N O3'          
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                       ? 'C11 H12 N2 O2'       
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                         ? 'C9 H11 N O3'         
181.189 
VAL 'L-peptide linking' y VALINE                                                                           ? 'C5 H11 N O2'         
117.146 
WWO non-polymer         . '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 'C15 H15 F3 N2 O5 S2' 
424.415 
ZN  non-polymer         . 'ZINC ION'                                                                       ? 'Zn 2'                
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   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  THR 62  62  62  THR THR A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  LEU 65  65  65  LEU LEU 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  LYS 91  91  91  LYS LYS 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 126 126 126 LYS LYS A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TRP 191 191 191 TRP TRP A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 CYS 205 205 205 CYS CYS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 TRP 244 244 244 TRP TRP A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 GLN 254 254 254 GLN GLN A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 WWO 1   302 1   WWO WWO A . 
D 4 DMS 1   303 1   DMS DMS A . 
E 5 MES 1   304 2   MES MES A . 
F 6 BCN 1   305 3   BCN BCN A . 
G 7 HOH 1   401 258 HOH HOH A . 
G 7 HOH 2   402 187 HOH HOH A . 
G 7 HOH 3   403 50  HOH HOH A . 
G 7 HOH 4   404 217 HOH HOH A . 
G 7 HOH 5   405 259 HOH HOH A . 
G 7 HOH 6   406 273 HOH HOH A . 
G 7 HOH 7   407 233 HOH HOH A . 
G 7 HOH 8   408 237 HOH HOH A . 
G 7 HOH 9   409 141 HOH HOH A . 
G 7 HOH 10  410 241 HOH HOH A . 
G 7 HOH 11  411 53  HOH HOH A . 
G 7 HOH 12  412 247 HOH HOH A . 
G 7 HOH 13  413 276 HOH HOH A . 
G 7 HOH 14  414 144 HOH HOH A . 
G 7 HOH 15  415 286 HOH HOH A . 
G 7 HOH 16  416 214 HOH HOH A . 
G 7 HOH 17  417 112 HOH HOH A . 
G 7 HOH 18  418 267 HOH HOH A . 
G 7 HOH 19  419 164 HOH HOH A . 
G 7 HOH 20  420 45  HOH HOH A . 
G 7 HOH 21  421 97  HOH HOH A . 
G 7 HOH 22  422 135 HOH HOH A . 
G 7 HOH 23  423 260 HOH HOH A . 
G 7 HOH 24  424 137 HOH HOH A . 
G 7 HOH 25  425 122 HOH HOH A . 
G 7 HOH 26  426 185 HOH HOH A . 
G 7 HOH 27  427 143 HOH HOH A . 
G 7 HOH 28  428 210 HOH HOH A . 
G 7 HOH 29  429 274 HOH HOH A . 
G 7 HOH 30  430 128 HOH HOH A . 
G 7 HOH 31  431 249 HOH HOH A . 
G 7 HOH 32  432 179 HOH HOH A . 
G 7 HOH 33  433 25  HOH HOH A . 
G 7 HOH 34  434 2   HOH HOH A . 
G 7 HOH 35  435 225 HOH HOH A . 
G 7 HOH 36  436 246 HOH HOH A . 
G 7 HOH 37  437 176 HOH HOH A . 
G 7 HOH 38  438 256 HOH HOH A . 
G 7 HOH 39  439 248 HOH HOH A . 
G 7 HOH 40  440 148 HOH HOH A . 
G 7 HOH 41  441 130 HOH HOH A . 
G 7 HOH 42  442 231 HOH HOH A . 
G 7 HOH 43  443 189 HOH HOH A . 
G 7 HOH 44  444 30  HOH HOH A . 
G 7 HOH 45  445 209 HOH HOH A . 
G 7 HOH 46  446 100 HOH HOH A . 
G 7 HOH 47  447 16  HOH HOH A . 
G 7 HOH 48  448 111 HOH HOH A . 
G 7 HOH 49  449 114 HOH HOH A . 
G 7 HOH 50  450 18  HOH HOH A . 
G 7 HOH 51  451 75  HOH HOH A . 
G 7 HOH 52  452 65  HOH HOH A . 
G 7 HOH 53  453 39  HOH HOH A . 
G 7 HOH 54  454 10  HOH HOH A . 
G 7 HOH 55  455 266 HOH HOH A . 
G 7 HOH 56  456 46  HOH HOH A . 
G 7 HOH 57  457 3   HOH HOH A . 
G 7 HOH 58  458 54  HOH HOH A . 
G 7 HOH 59  459 31  HOH HOH A . 
G 7 HOH 60  460 153 HOH HOH A . 
G 7 HOH 61  461 211 HOH HOH A . 
G 7 HOH 62  462 56  HOH HOH A . 
G 7 HOH 63  463 83  HOH HOH A . 
G 7 HOH 64  464 113 HOH HOH A . 
G 7 HOH 65  465 47  HOH HOH A . 
G 7 HOH 66  466 171 HOH HOH A . 
G 7 HOH 67  467 49  HOH HOH A . 
G 7 HOH 68  468 292 HOH HOH A . 
G 7 HOH 69  469 79  HOH HOH A . 
G 7 HOH 70  470 98  HOH HOH A . 
G 7 HOH 71  471 7   HOH HOH A . 
G 7 HOH 72  472 21  HOH HOH A . 
G 7 HOH 73  473 80  HOH HOH A . 
G 7 HOH 74  474 24  HOH HOH A . 
G 7 HOH 75  475 26  HOH HOH A . 
G 7 HOH 76  476 149 HOH HOH A . 
G 7 HOH 77  477 13  HOH HOH A . 
G 7 HOH 78  478 38  HOH HOH A . 
G 7 HOH 79  479 62  HOH HOH A . 
G 7 HOH 80  480 263 HOH HOH A . 
G 7 HOH 81  481 125 HOH HOH A . 
G 7 HOH 82  482 33  HOH HOH A . 
G 7 HOH 83  483 74  HOH HOH A . 
G 7 HOH 84  484 58  HOH HOH A . 
G 7 HOH 85  485 14  HOH HOH A . 
G 7 HOH 86  486 55  HOH HOH A . 
G 7 HOH 87  487 1   HOH HOH A . 
G 7 HOH 88  488 106 HOH HOH A . 
G 7 HOH 89  489 19  HOH HOH A . 
G 7 HOH 90  490 23  HOH HOH A . 
G 7 HOH 91  491 6   HOH HOH A . 
G 7 HOH 92  492 59  HOH HOH A . 
G 7 HOH 93  493 86  HOH HOH A . 
G 7 HOH 94  494 93  HOH HOH A . 
G 7 HOH 95  495 9   HOH HOH A . 
G 7 HOH 96  496 151 HOH HOH A . 
G 7 HOH 97  497 29  HOH HOH A . 
G 7 HOH 98  498 182 HOH HOH A . 
G 7 HOH 99  499 37  HOH HOH A . 
G 7 HOH 100 500 156 HOH HOH A . 
G 7 HOH 101 501 92  HOH HOH A . 
G 7 HOH 102 502 284 HOH HOH A . 
G 7 HOH 103 503 96  HOH HOH A . 
G 7 HOH 104 504 101 HOH HOH A . 
G 7 HOH 105 505 51  HOH HOH A . 
G 7 HOH 106 506 202 HOH HOH A . 
G 7 HOH 107 507 133 HOH HOH A . 
G 7 HOH 108 508 104 HOH HOH A . 
G 7 HOH 109 509 66  HOH HOH A . 
G 7 HOH 110 510 44  HOH HOH A . 
G 7 HOH 111 511 177 HOH HOH A . 
G 7 HOH 112 512 20  HOH HOH A . 
G 7 HOH 113 513 4   HOH HOH A . 
G 7 HOH 114 514 131 HOH HOH A . 
G 7 HOH 115 515 67  HOH HOH A . 
G 7 HOH 116 516 129 HOH HOH A . 
G 7 HOH 117 517 28  HOH HOH A . 
G 7 HOH 118 518 5   HOH HOH A . 
G 7 HOH 119 519 158 HOH HOH A . 
G 7 HOH 120 520 201 HOH HOH A . 
G 7 HOH 121 521 195 HOH HOH A . 
G 7 HOH 122 522 194 HOH HOH A . 
G 7 HOH 123 523 12  HOH HOH A . 
G 7 HOH 124 524 43  HOH HOH A . 
G 7 HOH 125 525 52  HOH HOH A . 
G 7 HOH 126 526 17  HOH HOH A . 
G 7 HOH 127 527 78  HOH HOH A . 
G 7 HOH 128 528 220 HOH HOH A . 
G 7 HOH 129 529 69  HOH HOH A . 
G 7 HOH 130 530 15  HOH HOH A . 
G 7 HOH 131 531 84  HOH HOH A . 
G 7 HOH 132 532 22  HOH HOH A . 
G 7 HOH 133 533 174 HOH HOH A . 
G 7 HOH 134 534 279 HOH HOH A . 
G 7 HOH 135 535 219 HOH HOH A . 
G 7 HOH 136 536 94  HOH HOH A . 
G 7 HOH 137 537 68  HOH HOH A . 
G 7 HOH 138 538 41  HOH HOH A . 
G 7 HOH 139 539 145 HOH HOH A . 
G 7 HOH 140 540 108 HOH HOH A . 
G 7 HOH 141 541 255 HOH HOH A . 
G 7 HOH 142 542 72  HOH HOH A . 
G 7 HOH 143 543 221 HOH HOH A . 
G 7 HOH 144 544 34  HOH HOH A . 
G 7 HOH 145 545 121 HOH HOH A . 
G 7 HOH 146 546 181 HOH HOH A . 
G 7 HOH 147 547 175 HOH HOH A . 
G 7 HOH 148 548 123 HOH HOH A . 
G 7 HOH 149 549 132 HOH HOH A . 
G 7 HOH 150 550 288 HOH HOH A . 
G 7 HOH 151 551 95  HOH HOH A . 
G 7 HOH 152 552 102 HOH HOH A . 
G 7 HOH 153 553 271 HOH HOH A . 
G 7 HOH 154 554 160 HOH HOH A . 
G 7 HOH 155 555 159 HOH HOH A . 
G 7 HOH 156 556 36  HOH HOH A . 
G 7 HOH 157 557 291 HOH HOH A . 
G 7 HOH 158 558 70  HOH HOH A . 
G 7 HOH 159 559 136 HOH HOH A . 
G 7 HOH 160 560 77  HOH HOH A . 
G 7 HOH 161 561 117 HOH HOH A . 
G 7 HOH 162 562 88  HOH HOH A . 
G 7 HOH 163 563 277 HOH HOH A . 
G 7 HOH 164 564 87  HOH HOH A . 
G 7 HOH 165 565 180 HOH HOH A . 
G 7 HOH 166 566 223 HOH HOH A . 
G 7 HOH 167 567 8   HOH HOH A . 
G 7 HOH 168 568 163 HOH HOH A . 
G 7 HOH 169 569 90  HOH HOH A . 
G 7 HOH 170 570 126 HOH HOH A . 
G 7 HOH 171 571 110 HOH HOH A . 
G 7 HOH 172 572 48  HOH HOH A . 
G 7 HOH 173 573 147 HOH HOH A . 
G 7 HOH 174 574 109 HOH HOH A . 
G 7 HOH 175 575 27  HOH HOH A . 
G 7 HOH 176 576 40  HOH HOH A . 
G 7 HOH 177 577 60  HOH HOH A . 
G 7 HOH 178 578 134 HOH HOH A . 
G 7 HOH 179 579 105 HOH HOH A . 
G 7 HOH 180 580 11  HOH HOH A . 
G 7 HOH 181 581 150 HOH HOH A . 
G 7 HOH 182 582 234 HOH HOH A . 
G 7 HOH 183 583 146 HOH HOH A . 
G 7 HOH 184 584 71  HOH HOH A . 
G 7 HOH 185 585 99  HOH HOH A . 
G 7 HOH 186 586 262 HOH HOH A . 
G 7 HOH 187 587 166 HOH HOH A . 
G 7 HOH 188 588 252 HOH HOH A . 
G 7 HOH 189 589 103 HOH HOH A . 
G 7 HOH 190 590 191 HOH HOH A . 
G 7 HOH 191 591 115 HOH HOH A . 
G 7 HOH 192 592 63  HOH HOH A . 
G 7 HOH 193 593 193 HOH HOH A . 
G 7 HOH 194 594 89  HOH HOH A . 
G 7 HOH 195 595 290 HOH HOH A . 
G 7 HOH 196 596 192 HOH HOH A . 
G 7 HOH 197 597 85  HOH HOH A . 
G 7 HOH 198 598 127 HOH HOH A . 
G 7 HOH 199 599 287 HOH HOH A . 
G 7 HOH 200 600 118 HOH HOH A . 
G 7 HOH 201 601 216 HOH HOH A . 
G 7 HOH 202 602 73  HOH HOH A . 
G 7 HOH 203 603 224 HOH HOH A . 
G 7 HOH 204 604 264 HOH HOH A . 
G 7 HOH 205 605 278 HOH HOH A . 
G 7 HOH 206 606 157 HOH HOH A . 
G 7 HOH 207 607 183 HOH HOH A . 
G 7 HOH 208 608 81  HOH HOH A . 
G 7 HOH 209 609 120 HOH HOH A . 
G 7 HOH 210 610 215 HOH HOH A . 
G 7 HOH 211 611 207 HOH HOH A . 
G 7 HOH 212 612 213 HOH HOH A . 
G 7 HOH 213 613 270 HOH HOH A . 
G 7 HOH 214 614 167 HOH HOH A . 
G 7 HOH 215 615 244 HOH HOH A . 
G 7 HOH 216 616 76  HOH HOH A . 
G 7 HOH 217 617 57  HOH HOH A . 
G 7 HOH 218 618 64  HOH HOH A . 
G 7 HOH 219 619 61  HOH HOH A . 
G 7 HOH 220 620 227 HOH HOH A . 
G 7 HOH 221 621 162 HOH HOH A . 
G 7 HOH 222 622 275 HOH HOH A . 
G 7 HOH 223 623 294 HOH HOH A . 
G 7 HOH 224 624 236 HOH HOH A . 
G 7 HOH 225 625 184 HOH HOH A . 
G 7 HOH 226 626 280 HOH HOH A . 
G 7 HOH 227 627 142 HOH HOH A . 
G 7 HOH 228 628 107 HOH HOH A . 
G 7 HOH 229 629 116 HOH HOH A . 
G 7 HOH 230 630 173 HOH HOH A . 
G 7 HOH 231 631 281 HOH HOH A . 
G 7 HOH 232 632 139 HOH HOH A . 
G 7 HOH 233 633 32  HOH HOH A . 
G 7 HOH 234 634 230 HOH HOH A . 
G 7 HOH 235 635 119 HOH HOH A . 
G 7 HOH 236 636 42  HOH HOH A . 
G 7 HOH 237 637 200 HOH HOH A . 
G 7 HOH 238 638 265 HOH HOH A . 
G 7 HOH 239 639 243 HOH HOH A . 
G 7 HOH 240 640 91  HOH HOH A . 
G 7 HOH 241 641 250 HOH HOH A . 
G 7 HOH 242 642 124 HOH HOH A . 
G 7 HOH 243 643 208 HOH HOH A . 
G 7 HOH 244 644 238 HOH HOH A . 
G 7 HOH 245 645 253 HOH HOH A . 
G 7 HOH 246 646 169 HOH HOH A . 
G 7 HOH 247 647 155 HOH HOH A . 
G 7 HOH 248 648 186 HOH HOH A . 
G 7 HOH 249 649 240 HOH HOH A . 
G 7 HOH 250 650 165 HOH HOH A . 
G 7 HOH 251 651 198 HOH HOH A . 
G 7 HOH 252 652 168 HOH HOH A . 
G 7 HOH 253 653 254 HOH HOH A . 
G 7 HOH 254 654 261 HOH HOH A . 
G 7 HOH 255 655 269 HOH HOH A . 
G 7 HOH 256 656 188 HOH HOH A . 
G 7 HOH 257 657 138 HOH HOH A . 
G 7 HOH 258 658 205 HOH HOH A . 
G 7 HOH 259 659 285 HOH HOH A . 
G 7 HOH 260 660 152 HOH HOH A . 
G 7 HOH 261 661 190 HOH HOH A . 
G 7 HOH 262 662 178 HOH HOH A . 
G 7 HOH 263 663 268 HOH HOH A . 
G 7 HOH 264 664 222 HOH HOH A . 
G 7 HOH 265 665 196 HOH HOH A . 
G 7 HOH 266 666 289 HOH HOH A . 
G 7 HOH 267 667 212 HOH HOH A . 
G 7 HOH 268 668 232 HOH HOH A . 
G 7 HOH 269 669 35  HOH HOH A . 
G 7 HOH 270 670 235 HOH HOH A . 
G 7 HOH 271 671 283 HOH HOH A . 
G 7 HOH 272 672 257 HOH HOH A . 
G 7 HOH 273 673 170 HOH HOH A . 
G 7 HOH 274 674 272 HOH HOH A . 
G 7 HOH 275 675 154 HOH HOH A . 
G 7 HOH 276 676 229 HOH HOH A . 
G 7 HOH 277 677 199 HOH HOH A . 
G 7 HOH 278 678 161 HOH HOH A . 
G 7 HOH 279 679 251 HOH HOH A . 
G 7 HOH 280 680 226 HOH HOH A . 
G 7 HOH 281 681 218 HOH HOH A . 
G 7 HOH 282 682 172 HOH HOH A . 
G 7 HOH 283 683 293 HOH HOH A . 
G 7 HOH 284 684 239 HOH HOH A . 
G 7 HOH 285 685 82  HOH HOH A . 
G 7 HOH 286 686 242 HOH HOH A . 
G 7 HOH 287 687 140 HOH HOH A . 
G 7 HOH 288 688 228 HOH HOH A . 
G 7 HOH 289 689 206 HOH HOH A . 
G 7 HOH 290 690 245 HOH HOH A . 
G 7 HOH 291 691 197 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   ? CG  ? A LYS 9   CG  
2  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
3  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
4  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
5  1 Y 1 A LYS 45  ? CD  ? A LYS 45  CD  
6  1 Y 1 A LYS 45  ? CE  ? A LYS 45  CE  
7  1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
8  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
9  1 Y 1 A LYS 158 ? CG  ? A LYS 158 CG  
10 1 Y 1 A LYS 158 ? CD  ? A LYS 158 CD  
11 1 Y 1 A LYS 158 ? CE  ? A LYS 158 CE  
12 1 Y 1 A LYS 158 ? NZ  ? A LYS 158 NZ  
13 1 Y 1 A LYS 169 ? CE  ? A LYS 169 CE  
14 1 Y 1 A LYS 169 ? NZ  ? A LYS 169 NZ  
15 1 Y 1 A LYS 171 ? CE  ? A LYS 171 CE  
16 1 Y 1 A LYS 171 ? NZ  ? A LYS 171 NZ  
17 1 Y 1 A GLU 238 ? CD  ? A GLU 238 CD  
18 1 Y 1 A GLU 238 ? OE1 ? A GLU 238 OE1 
19 1 Y 1 A GLU 238 ? OE2 ? A GLU 238 OE2 
20 1 Y 1 A LYS 256 ? CE  ? A LYS 256 CE  
21 1 Y 1 A LYS 256 ? NZ  ? A LYS 256 NZ  
22 1 Y 1 A LYS 260 ? CD  ? A LYS 260 CD  
23 1 Y 1 A LYS 260 ? CE  ? A LYS 260 CE  
24 1 Y 1 A LYS 260 ? NZ  ? A LYS 260 NZ  
25 1 N 1 A MES 304 ? S   ? E MES 1   S   
26 1 N 1 A MES 304 ? O1S ? E MES 1   O1S 
27 1 N 1 A MES 304 ? O2S ? E MES 1   O2S 
28 1 N 1 A MES 304 ? O3S ? E MES 1   O3S 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.240 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7NZU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.197 
_cell.length_a_esd                 ? 
_cell.length_b                     41.271 
_cell.length_b_esd                 ? 
_cell.length_c                     71.531 
_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                         7NZU 
_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                   7NZU 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.06 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.15 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_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   0.97630 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97630 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         7NZU 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.240 
_reflns.d_resolution_low                 69.334 
_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                       65883 
_reflns.number_obs                       65883 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             97.300 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.600 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.037 
_reflns.pdbx_netI_over_av_sigmaI         8.400 
_reflns.pdbx_netI_over_sigmaI            25.900 
_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                  0.047 
_reflns.pdbx_Rpim_I_all                  0.018 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         436245 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
1.240 1.310  ? 3.700  48854 ? ? ? 8433 85.900 ? ? ? ? 0.183 ? ? ? ? ? ? ? ? 5.800 0.183 ? ? 8.400  0.230 0.093 ? 1  1 ? ? ? 
1.310 1.390  ? 4.500  61629 ? ? ? 9227 99.100 ? ? ? ? 0.144 ? ? ? ? ? ? ? ? 6.700 0.144 ? ? 11.700 0.173 0.066 ? 2  1 ? ? ? 
1.390 1.480  ? 6.100  56773 ? ? ? 8641 98.800 ? ? ? ? 0.103 ? ? ? ? ? ? ? ? 6.600 0.103 ? ? 15.000 0.127 0.049 ? 3  1 ? ? ? 
1.480 1.600  ? 8.800  55328 ? ? ? 8121 99.300 ? ? ? ? 0.072 ? ? ? ? ? ? ? ? 6.800 0.072 ? ? 20.300 0.091 0.034 ? 4  1 ? ? ? 
1.600 1.750  ? 12.500 49159 ? ? ? 7435 98.900 ? ? ? ? 0.053 ? ? ? ? ? ? ? ? 6.600 0.053 ? ? 25.700 0.069 0.026 ? 5  1 ? ? ? 
1.750 1.960  ? 16.300 47057 ? ? ? 6774 99.500 ? ? ? ? 0.040 ? ? ? ? ? ? ? ? 6.900 0.040 ? ? 33.800 0.052 0.020 ? 6  1 ? ? ? 
1.960 2.260  ? 19.200 40107 ? ? ? 5957 99.100 ? ? ? ? 0.033 ? ? ? ? ? ? ? ? 6.700 0.033 ? ? 41.600 0.042 0.016 ? 7  1 ? ? ? 
2.260 2.770  ? 20.400 35727 ? ? ? 5100 99.800 ? ? ? ? 0.031 ? ? ? ? ? ? ? ? 7.000 0.031 ? ? 47.100 0.039 0.015 ? 8  1 ? ? ? 
2.770 3.920  ? 18.200 26732 ? ? ? 3959 99.500 ? ? ? ? 0.029 ? ? ? ? ? ? ? ? 6.800 0.029 ? ? 52.100 0.035 0.013 ? 9  1 ? ? ? 
3.920 69.334 ? 15.400 14879 ? ? ? 2236 99.600 ? ? ? ? 0.032 ? ? ? ? ? ? ? ? 6.700 0.032 ? ? 54.100 0.038 0.015 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            0.0800 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            -0.0200 
_refine.aniso_B[2][2]                            -0.5300 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            0.4000 
_refine.B_iso_max                                124.070 
_refine.B_iso_mean                               17.0310 
_refine.B_iso_min                                4.250 
_refine.correlation_coeff_Fo_to_Fc               0.9760 
_refine.correlation_coeff_Fo_to_Fc_free          0.9650 
_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                                 7NZU 
_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                            1.2400 
_refine.ls_d_res_low                             40.9000 
_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                     59198 
_refine.ls_number_reflns_R_free                  6668 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.1400 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1359 
_refine.ls_R_factor_R_free                       0.1660 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1326 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4HT0 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0450 
_refine.pdbx_overall_ESU_R_Free                  0.0450 
_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             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.2400 
_refine_hist.d_res_low                        40.9000 
_refine_hist.number_atoms_solvent             291 
_refine_hist.number_atoms_total               2400 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       257 
_refine_hist.pdbx_B_iso_mean_ligand           29.56 
_refine_hist.pdbx_B_iso_mean_solvent          29.74 
_refine_hist.pdbx_number_atoms_protein        2031 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         78 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.018  0.012  2321 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.339  1.675  3184 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.035  5.000  289  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 35.065 23.578 109  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.865 15.000 365  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 18.777 15.000 8    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.147  0.200  279  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.016  0.020  1837 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 10.530 3.000  2321 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 23.812 5.000  168  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 15.090 5.000  2366 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.2400 
_refine_ls_shell.d_res_low                        1.2720 
_refine_ls_shell.number_reflns_all                3657 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             364 
_refine_ls_shell.number_reflns_R_work             3293 
_refine_ls_shell.percent_reflns_obs               73.4300 
_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                  0.1830 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1620 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     7NZU 
_struct.title                        
;Crystal structure of chimeric carbonic anhydrase VA with 3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        7NZU 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
# 
_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              7NZU 
_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       260 
# 
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 7NZU THR A 62  ? UNP P00918 ASN 62  'engineered mutation' 62  1 
1 7NZU TYR A 64  ? UNP P00918 HIS 64  'engineered mutation' 64  2 
1 7NZU LEU A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  3 
1 7NZU GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  4 
1 7NZU LYS A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  5 
1 7NZU TYR A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 6 
1 7NZU THR A 203 ? UNP P00918 LEU 203 'engineered mutation' 203 7 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 870   ? 
1 MORE         10    ? 
1 'SSA (A^2)'  11030 ? 
# 
_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 
# 
_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  ? GLU A 14  ? GLY A 12  GLU A 14  5 ? 3 
HELX_P HELX_P2  AA2 HIS A 15  ? PHE A 20  ? HIS A 15  PHE A 20  1 ? 6 
HELX_P HELX_P3  AA3 PRO A 21  ? GLY A 25  ? PRO A 21  GLY A 25  5 ? 5 
HELX_P HELX_P4  AA4 LYS A 126 ? GLY A 128 ? LYS A 126 GLY A 128 5 ? 3 
HELX_P HELX_P5  AA5 ASP A 129 ? VAL A 134 ? ASP A 129 VAL A 134 1 ? 6 
HELX_P HELX_P6  AA6 LYS A 153 ? GLY A 155 ? LYS A 153 GLY A 155 5 ? 3 
HELX_P HELX_P7  AA7 LEU A 156 ? LEU A 163 ? LEU A 156 LEU A 163 1 ? 8 
HELX_P HELX_P8  AA8 ASP A 164 ? LYS A 167 ? ASP A 164 LYS A 167 5 ? 4 
HELX_P HELX_P9  AA9 ASP A 179 ? LEU A 184 ? ASP A 179 LEU A 184 5 ? 6 
HELX_P HELX_P10 AB1 SER A 218 ? ARG A 226 ? SER A 218 ARG A 226 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 ? ? ? ? ? ? ? 2.028 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 1.999 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C WWO . N10 A ? A ZN  301 A WWO 302 1_555 ? ? ? ? ? ? ? 1.858 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C WWO . N10 B ? A ZN  301 A WWO 302 1_555 ? ? ? ? ? ? ? 1.943 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 104.2 ? 
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_555 108.7 ? 
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_555 100.3 ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C WWO .   ? A WWO 302 ? 1_555 110.1 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C WWO .   ? A WWO 302 ? 1_555 110.8 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C WWO .   ? A WWO 302 ? 1_555 121.2 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C WWO .   ? A WWO 302 ? 1_555 116.2 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C WWO .   ? A WWO 302 ? 1_555 114.6 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C WWO .   ? A WWO 302 ? 1_555 111.5 ? 
10 N10 A C WWO .   ? A WWO 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C WWO .   ? A WWO 302 ? 1_555 9.7   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -1.24 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 10.40 
# 
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 256 ALA A 257 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 206 LEU A 211 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
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 172 ASP A 174 
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 140 VAL A 149 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 215 VAL A 217 
# 
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 257 
AA2 2 3  O LYS A 256 ? O LYS A 256 N THR A 192 ? N THR A 192 
AA2 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O LEU A 211 ? O LEU A 211 N GLY A 144 ? N GLY A 144 
AA2 5 6  O ILE A 145 ? O ILE A 145 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 LYS A 91  ? O LYS A 91  N PHE A 70  ? N PHE A 70  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 173 
AA3 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
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 145 
AA3 5 6  N PHE A 146 ? N PHE A 146 O ILE A 215 ? O ILE A 215 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OG 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    SER 
_pdbx_validate_symm_contact.auth_seq_id_1     73 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     416 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_565 
_pdbx_validate_symm_contact.dist              2.18 
# 
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  ? ? -143.53 13.06   
2 1 ARG A 27  ? B -142.01 50.66   
3 1 LYS A 76  ? B -107.48 -91.02  
4 1 LYS A 111 ? ? 76.35   -5.98   
5 1 PHE A 175 ? ? -152.77 65.59   
6 1 ASN A 243 ? ? -95.16  46.45   
7 1 LYS A 251 ? A 65.59   -123.99 
8 1 LYS A 251 ? B 58.27   -137.80 
# 
_pdbx_entry_details.entry_id                 7NZU 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 689 ? 5.98 . 
2 1 O ? A HOH 690 ? 6.29 . 
3 1 O ? A HOH 691 ? 6.43 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
LEU N    N  N N 217 
LEU CA   C  N S 218 
LEU C    C  N N 219 
LEU O    O  N N 220 
LEU CB   C  N N 221 
LEU CG   C  N N 222 
LEU CD1  C  N N 223 
LEU CD2  C  N N 224 
LEU OXT  O  N N 225 
LEU H    H  N N 226 
LEU H2   H  N N 227 
LEU HA   H  N N 228 
LEU HB2  H  N N 229 
LEU HB3  H  N N 230 
LEU HG   H  N N 231 
LEU HD11 H  N N 232 
LEU HD12 H  N N 233 
LEU HD13 H  N N 234 
LEU HD21 H  N N 235 
LEU HD22 H  N N 236 
LEU HD23 H  N N 237 
LEU HXT  H  N N 238 
LYS N    N  N N 239 
LYS CA   C  N S 240 
LYS C    C  N N 241 
LYS O    O  N N 242 
LYS CB   C  N N 243 
LYS CG   C  N N 244 
LYS CD   C  N N 245 
LYS CE   C  N N 246 
LYS NZ   N  N N 247 
LYS OXT  O  N N 248 
LYS H    H  N N 249 
LYS H2   H  N N 250 
LYS HA   H  N N 251 
LYS HB2  H  N N 252 
LYS HB3  H  N N 253 
LYS HG2  H  N N 254 
LYS HG3  H  N N 255 
LYS HD2  H  N N 256 
LYS HD3  H  N N 257 
LYS HE2  H  N N 258 
LYS HE3  H  N N 259 
LYS HZ1  H  N N 260 
LYS HZ2  H  N N 261 
LYS HZ3  H  N N 262 
LYS HXT  H  N N 263 
MES O1   O  N N 264 
MES C2   C  N N 265 
MES C3   C  N N 266 
MES N4   N  N N 267 
MES C5   C  N N 268 
MES C6   C  N N 269 
MES C7   C  N N 270 
MES C8   C  N N 271 
MES S    S  N N 272 
MES O1S  O  N N 273 
MES O2S  O  N N 274 
MES O3S  O  N N 275 
MES H21  H  N N 276 
MES H22  H  N N 277 
MES H31  H  N N 278 
MES H32  H  N N 279 
MES HN4  H  N N 280 
MES H51  H  N N 281 
MES H52  H  N N 282 
MES H61  H  N N 283 
MES H62  H  N N 284 
MES H71  H  N N 285 
MES H72  H  N N 286 
MES H81  H  N N 287 
MES H82  H  N N 288 
MET N    N  N N 289 
MET CA   C  N S 290 
MET C    C  N N 291 
MET O    O  N N 292 
MET CB   C  N N 293 
MET CG   C  N N 294 
MET SD   S  N N 295 
MET CE   C  N N 296 
MET OXT  O  N N 297 
MET H    H  N N 298 
MET H2   H  N N 299 
MET HA   H  N N 300 
MET HB2  H  N N 301 
MET HB3  H  N N 302 
MET HG2  H  N N 303 
MET HG3  H  N N 304 
MET HE1  H  N N 305 
MET HE2  H  N N 306 
MET HE3  H  N N 307 
MET HXT  H  N N 308 
PHE N    N  N N 309 
PHE CA   C  N S 310 
PHE C    C  N N 311 
PHE O    O  N N 312 
PHE CB   C  N N 313 
PHE CG   C  Y N 314 
PHE CD1  C  Y N 315 
PHE CD2  C  Y N 316 
PHE CE1  C  Y N 317 
PHE CE2  C  Y N 318 
PHE CZ   C  Y N 319 
PHE OXT  O  N N 320 
PHE H    H  N N 321 
PHE H2   H  N N 322 
PHE HA   H  N N 323 
PHE HB2  H  N N 324 
PHE HB3  H  N N 325 
PHE HD1  H  N N 326 
PHE HD2  H  N N 327 
PHE HE1  H  N N 328 
PHE HE2  H  N N 329 
PHE HZ   H  N N 330 
PHE HXT  H  N N 331 
PRO N    N  N N 332 
PRO CA   C  N S 333 
PRO C    C  N N 334 
PRO O    O  N N 335 
PRO CB   C  N N 336 
PRO CG   C  N N 337 
PRO CD   C  N N 338 
PRO OXT  O  N N 339 
PRO H    H  N N 340 
PRO HA   H  N N 341 
PRO HB2  H  N N 342 
PRO HB3  H  N N 343 
PRO HG2  H  N N 344 
PRO HG3  H  N N 345 
PRO HD2  H  N N 346 
PRO HD3  H  N N 347 
PRO HXT  H  N N 348 
SER N    N  N N 349 
SER CA   C  N S 350 
SER C    C  N N 351 
SER O    O  N N 352 
SER CB   C  N N 353 
SER OG   O  N N 354 
SER OXT  O  N N 355 
SER H    H  N N 356 
SER H2   H  N N 357 
SER HA   H  N N 358 
SER HB2  H  N N 359 
SER HB3  H  N N 360 
SER HG   H  N N 361 
SER HXT  H  N N 362 
THR N    N  N N 363 
THR CA   C  N S 364 
THR C    C  N N 365 
THR O    O  N N 366 
THR CB   C  N R 367 
THR OG1  O  N N 368 
THR CG2  C  N N 369 
THR OXT  O  N N 370 
THR H    H  N N 371 
THR H2   H  N N 372 
THR HA   H  N N 373 
THR HB   H  N N 374 
THR HG1  H  N N 375 
THR HG21 H  N N 376 
THR HG22 H  N N 377 
THR HG23 H  N N 378 
THR HXT  H  N N 379 
TRP N    N  N N 380 
TRP CA   C  N S 381 
TRP C    C  N N 382 
TRP O    O  N N 383 
TRP CB   C  N N 384 
TRP CG   C  Y N 385 
TRP CD1  C  Y N 386 
TRP CD2  C  Y N 387 
TRP NE1  N  Y N 388 
TRP CE2  C  Y N 389 
TRP CE3  C  Y N 390 
TRP CZ2  C  Y N 391 
TRP CZ3  C  Y N 392 
TRP CH2  C  Y N 393 
TRP OXT  O  N N 394 
TRP H    H  N N 395 
TRP H2   H  N N 396 
TRP HA   H  N N 397 
TRP HB2  H  N N 398 
TRP HB3  H  N N 399 
TRP HD1  H  N N 400 
TRP HE1  H  N N 401 
TRP HE3  H  N N 402 
TRP HZ2  H  N N 403 
TRP HZ3  H  N N 404 
TRP HH2  H  N N 405 
TRP HXT  H  N N 406 
TYR N    N  N N 407 
TYR CA   C  N S 408 
TYR C    C  N N 409 
TYR O    O  N N 410 
TYR CB   C  N N 411 
TYR CG   C  Y N 412 
TYR CD1  C  Y N 413 
TYR CD2  C  Y N 414 
TYR CE1  C  Y N 415 
TYR CE2  C  Y N 416 
TYR CZ   C  Y N 417 
TYR OH   O  N N 418 
TYR OXT  O  N N 419 
TYR H    H  N N 420 
TYR H2   H  N N 421 
TYR HA   H  N N 422 
TYR HB2  H  N N 423 
TYR HB3  H  N N 424 
TYR HD1  H  N N 425 
TYR HD2  H  N N 426 
TYR HE1  H  N N 427 
TYR HE2  H  N N 428 
TYR HH   H  N N 429 
TYR HXT  H  N N 430 
VAL N    N  N N 431 
VAL CA   C  N S 432 
VAL C    C  N N 433 
VAL O    O  N N 434 
VAL CB   C  N N 435 
VAL CG1  C  N N 436 
VAL CG2  C  N N 437 
VAL OXT  O  N N 438 
VAL H    H  N N 439 
VAL H2   H  N N 440 
VAL HA   H  N N 441 
VAL HB   H  N N 442 
VAL HG11 H  N N 443 
VAL HG12 H  N N 444 
VAL HG13 H  N N 445 
VAL HG21 H  N N 446 
VAL HG22 H  N N 447 
VAL HG23 H  N N 448 
VAL HXT  H  N N 449 
WWO F27  F  N N 450 
WWO C5   C  Y N 451 
WWO C4   C  Y N 452 
WWO S7   S  N N 453 
WWO O9   O  N N 454 
WWO N10  N  N N 455 
WWO O8   O  N N 456 
WWO C3   C  Y N 457 
WWO F12  F  N N 458 
WWO C2   C  Y N 459 
WWO F13  F  N N 460 
WWO C6   C  Y N 461 
WWO C1   C  Y N 462 
WWO S11  S  N N 463 
WWO O22  O  N N 464 
WWO O23  O  N N 465 
WWO C21  C  N N 466 
WWO C24  C  N N 467 
WWO O25  O  N N 468 
WWO N26  N  N N 469 
WWO C14  C  N N 470 
WWO C15  C  Y N 471 
WWO C20  C  Y N 472 
WWO C19  C  Y N 473 
WWO C18  C  Y N 474 
WWO C17  C  Y N 475 
WWO C16  C  Y N 476 
WWO H1   H  N N 477 
WWO H2   H  N N 478 
WWO H3   H  N N 479 
WWO H4   H  N N 480 
WWO H5   H  N N 481 
WWO H6   H  N N 482 
WWO H7   H  N N 483 
WWO H8   H  N N 484 
WWO H9   H  N N 485 
WWO H10  H  N N 486 
WWO H11  H  N N 487 
WWO H12  H  N N 488 
WWO H13  H  N N 489 
WWO H14  H  N N 490 
WWO H15  H  N N 491 
ZN  ZN   ZN N N 492 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
GLN N   CA   sing N N 115 
GLN N   H    sing N N 116 
GLN N   H2   sing N N 117 
GLN CA  C    sing N N 118 
GLN CA  CB   sing N N 119 
GLN CA  HA   sing N N 120 
GLN C   O    doub N N 121 
GLN C   OXT  sing N N 122 
GLN CB  CG   sing N N 123 
GLN CB  HB2  sing N N 124 
GLN CB  HB3  sing N N 125 
GLN CG  CD   sing N N 126 
GLN CG  HG2  sing N N 127 
GLN CG  HG3  sing N N 128 
GLN CD  OE1  doub N N 129 
GLN CD  NE2  sing N N 130 
GLN NE2 HE21 sing N N 131 
GLN NE2 HE22 sing N N 132 
GLN OXT HXT  sing N N 133 
GLU N   CA   sing N N 134 
GLU N   H    sing N N 135 
GLU N   H2   sing N N 136 
GLU CA  C    sing N N 137 
GLU CA  CB   sing N N 138 
GLU CA  HA   sing N N 139 
GLU C   O    doub N N 140 
GLU C   OXT  sing N N 141 
GLU CB  CG   sing N N 142 
GLU CB  HB2  sing N N 143 
GLU CB  HB3  sing N N 144 
GLU CG  CD   sing N N 145 
GLU CG  HG2  sing N N 146 
GLU CG  HG3  sing N N 147 
GLU CD  OE1  doub N N 148 
GLU CD  OE2  sing N N 149 
GLU OE2 HE2  sing N N 150 
GLU OXT HXT  sing N N 151 
GLY N   CA   sing N N 152 
GLY N   H    sing N N 153 
GLY N   H2   sing N N 154 
GLY CA  C    sing N N 155 
GLY CA  HA2  sing N N 156 
GLY CA  HA3  sing N N 157 
GLY C   O    doub N N 158 
GLY C   OXT  sing N N 159 
GLY OXT HXT  sing N N 160 
HIS N   CA   sing N N 161 
HIS N   H    sing N N 162 
HIS N   H2   sing N N 163 
HIS CA  C    sing N N 164 
HIS CA  CB   sing N N 165 
HIS CA  HA   sing N N 166 
HIS C   O    doub N N 167 
HIS C   OXT  sing N N 168 
HIS CB  CG   sing N N 169 
HIS CB  HB2  sing N N 170 
HIS CB  HB3  sing N N 171 
HIS CG  ND1  sing Y N 172 
HIS CG  CD2  doub Y N 173 
HIS ND1 CE1  doub Y N 174 
HIS ND1 HD1  sing N N 175 
HIS CD2 NE2  sing Y N 176 
HIS CD2 HD2  sing N N 177 
HIS CE1 NE2  sing Y N 178 
HIS CE1 HE1  sing N N 179 
HIS NE2 HE2  sing N N 180 
HIS OXT HXT  sing N N 181 
HOH O   H1   sing N N 182 
HOH O   H2   sing N N 183 
ILE N   CA   sing N N 184 
ILE N   H    sing N N 185 
ILE N   H2   sing N N 186 
ILE CA  C    sing N N 187 
ILE CA  CB   sing N N 188 
ILE CA  HA   sing N N 189 
ILE C   O    doub N N 190 
ILE C   OXT  sing N N 191 
ILE CB  CG1  sing N N 192 
ILE CB  CG2  sing N N 193 
ILE CB  HB   sing N N 194 
ILE CG1 CD1  sing N N 195 
ILE CG1 HG12 sing N N 196 
ILE CG1 HG13 sing N N 197 
ILE CG2 HG21 sing N N 198 
ILE CG2 HG22 sing N N 199 
ILE CG2 HG23 sing N N 200 
ILE CD1 HD11 sing N N 201 
ILE CD1 HD12 sing N N 202 
ILE CD1 HD13 sing N N 203 
ILE OXT HXT  sing N N 204 
LEU N   CA   sing N N 205 
LEU N   H    sing N N 206 
LEU N   H2   sing N N 207 
LEU CA  C    sing N N 208 
LEU CA  CB   sing N N 209 
LEU CA  HA   sing N N 210 
LEU C   O    doub N N 211 
LEU C   OXT  sing N N 212 
LEU CB  CG   sing N N 213 
LEU CB  HB2  sing N N 214 
LEU CB  HB3  sing N N 215 
LEU CG  CD1  sing N N 216 
LEU CG  CD2  sing N N 217 
LEU CG  HG   sing N N 218 
LEU CD1 HD11 sing N N 219 
LEU CD1 HD12 sing N N 220 
LEU CD1 HD13 sing N N 221 
LEU CD2 HD21 sing N N 222 
LEU CD2 HD22 sing N N 223 
LEU CD2 HD23 sing N N 224 
LEU OXT HXT  sing N N 225 
LYS N   CA   sing N N 226 
LYS N   H    sing N N 227 
LYS N   H2   sing N N 228 
LYS CA  C    sing N N 229 
LYS CA  CB   sing N N 230 
LYS CA  HA   sing N N 231 
LYS C   O    doub N N 232 
LYS C   OXT  sing N N 233 
LYS CB  CG   sing N N 234 
LYS CB  HB2  sing N N 235 
LYS CB  HB3  sing N N 236 
LYS CG  CD   sing N N 237 
LYS CG  HG2  sing N N 238 
LYS CG  HG3  sing N N 239 
LYS CD  CE   sing N N 240 
LYS CD  HD2  sing N N 241 
LYS CD  HD3  sing N N 242 
LYS CE  NZ   sing N N 243 
LYS CE  HE2  sing N N 244 
LYS CE  HE3  sing N N 245 
LYS NZ  HZ1  sing N N 246 
LYS NZ  HZ2  sing N N 247 
LYS NZ  HZ3  sing N N 248 
LYS OXT HXT  sing N N 249 
MES O1  C2   sing N N 250 
MES O1  C6   sing N N 251 
MES C2  C3   sing N N 252 
MES C2  H21  sing N N 253 
MES C2  H22  sing N N 254 
MES C3  N4   sing N N 255 
MES C3  H31  sing N N 256 
MES C3  H32  sing N N 257 
MES N4  C5   sing N N 258 
MES N4  C7   sing N N 259 
MES N4  HN4  sing N N 260 
MES C5  C6   sing N N 261 
MES C5  H51  sing N N 262 
MES C5  H52  sing N N 263 
MES C6  H61  sing N N 264 
MES C6  H62  sing N N 265 
MES C7  C8   sing N N 266 
MES C7  H71  sing N N 267 
MES C7  H72  sing N N 268 
MES C8  S    sing N N 269 
MES C8  H81  sing N N 270 
MES C8  H82  sing N N 271 
MES S   O1S  doub N N 272 
MES S   O2S  doub N N 273 
MES S   O3S  sing N N 274 
MET N   CA   sing N N 275 
MET N   H    sing N N 276 
MET N   H2   sing N N 277 
MET CA  C    sing N N 278 
MET CA  CB   sing N N 279 
MET CA  HA   sing N N 280 
MET C   O    doub N N 281 
MET C   OXT  sing N N 282 
MET CB  CG   sing N N 283 
MET CB  HB2  sing N N 284 
MET CB  HB3  sing N N 285 
MET CG  SD   sing N N 286 
MET CG  HG2  sing N N 287 
MET CG  HG3  sing N N 288 
MET SD  CE   sing N N 289 
MET CE  HE1  sing N N 290 
MET CE  HE2  sing N N 291 
MET CE  HE3  sing N N 292 
MET OXT HXT  sing N N 293 
PHE N   CA   sing N N 294 
PHE N   H    sing N N 295 
PHE N   H2   sing N N 296 
PHE CA  C    sing N N 297 
PHE CA  CB   sing N N 298 
PHE CA  HA   sing N N 299 
PHE C   O    doub N N 300 
PHE C   OXT  sing N N 301 
PHE CB  CG   sing N N 302 
PHE CB  HB2  sing N N 303 
PHE CB  HB3  sing N N 304 
PHE CG  CD1  doub Y N 305 
PHE CG  CD2  sing Y N 306 
PHE CD1 CE1  sing Y N 307 
PHE CD1 HD1  sing N N 308 
PHE CD2 CE2  doub Y N 309 
PHE CD2 HD2  sing N N 310 
PHE CE1 CZ   doub Y N 311 
PHE CE1 HE1  sing N N 312 
PHE CE2 CZ   sing Y N 313 
PHE CE2 HE2  sing N N 314 
PHE CZ  HZ   sing N N 315 
PHE OXT HXT  sing N N 316 
PRO N   CA   sing N N 317 
PRO N   CD   sing N N 318 
PRO N   H    sing N N 319 
PRO CA  C    sing N N 320 
PRO CA  CB   sing N N 321 
PRO CA  HA   sing N N 322 
PRO C   O    doub N N 323 
PRO C   OXT  sing N N 324 
PRO CB  CG   sing N N 325 
PRO CB  HB2  sing N N 326 
PRO CB  HB3  sing N N 327 
PRO CG  CD   sing N N 328 
PRO CG  HG2  sing N N 329 
PRO CG  HG3  sing N N 330 
PRO CD  HD2  sing N N 331 
PRO CD  HD3  sing N N 332 
PRO OXT HXT  sing N N 333 
SER N   CA   sing N N 334 
SER N   H    sing N N 335 
SER N   H2   sing N N 336 
SER CA  C    sing N N 337 
SER CA  CB   sing N N 338 
SER CA  HA   sing N N 339 
SER C   O    doub N N 340 
SER C   OXT  sing N N 341 
SER CB  OG   sing N N 342 
SER CB  HB2  sing N N 343 
SER CB  HB3  sing N N 344 
SER OG  HG   sing N N 345 
SER OXT HXT  sing N N 346 
THR N   CA   sing N N 347 
THR N   H    sing N N 348 
THR N   H2   sing N N 349 
THR CA  C    sing N N 350 
THR CA  CB   sing N N 351 
THR CA  HA   sing N N 352 
THR C   O    doub N N 353 
THR C   OXT  sing N N 354 
THR CB  OG1  sing N N 355 
THR CB  CG2  sing N N 356 
THR CB  HB   sing N N 357 
THR OG1 HG1  sing N N 358 
THR CG2 HG21 sing N N 359 
THR CG2 HG22 sing N N 360 
THR CG2 HG23 sing N N 361 
THR OXT HXT  sing N N 362 
TRP N   CA   sing N N 363 
TRP N   H    sing N N 364 
TRP N   H2   sing N N 365 
TRP CA  C    sing N N 366 
TRP CA  CB   sing N N 367 
TRP CA  HA   sing N N 368 
TRP C   O    doub N N 369 
TRP C   OXT  sing N N 370 
TRP CB  CG   sing N N 371 
TRP CB  HB2  sing N N 372 
TRP CB  HB3  sing N N 373 
TRP CG  CD1  doub Y N 374 
TRP CG  CD2  sing Y N 375 
TRP CD1 NE1  sing Y N 376 
TRP CD1 HD1  sing N N 377 
TRP CD2 CE2  doub Y N 378 
TRP CD2 CE3  sing Y N 379 
TRP NE1 CE2  sing Y N 380 
TRP NE1 HE1  sing N N 381 
TRP CE2 CZ2  sing Y N 382 
TRP CE3 CZ3  doub Y N 383 
TRP CE3 HE3  sing N N 384 
TRP CZ2 CH2  doub Y N 385 
TRP CZ2 HZ2  sing N N 386 
TRP CZ3 CH2  sing Y N 387 
TRP CZ3 HZ3  sing N N 388 
TRP CH2 HH2  sing N N 389 
TRP OXT HXT  sing N N 390 
TYR N   CA   sing N N 391 
TYR N   H    sing N N 392 
TYR N   H2   sing N N 393 
TYR CA  C    sing N N 394 
TYR CA  CB   sing N N 395 
TYR CA  HA   sing N N 396 
TYR C   O    doub N N 397 
TYR C   OXT  sing N N 398 
TYR CB  CG   sing N N 399 
TYR CB  HB2  sing N N 400 
TYR CB  HB3  sing N N 401 
TYR CG  CD1  doub Y N 402 
TYR CG  CD2  sing Y N 403 
TYR CD1 CE1  sing Y N 404 
TYR CD1 HD1  sing N N 405 
TYR CD2 CE2  doub Y N 406 
TYR CD2 HD2  sing N N 407 
TYR CE1 CZ   doub Y N 408 
TYR CE1 HE1  sing N N 409 
TYR CE2 CZ   sing Y N 410 
TYR CE2 HE2  sing N N 411 
TYR CZ  OH   sing N N 412 
TYR OH  HH   sing N N 413 
TYR OXT HXT  sing N N 414 
VAL N   CA   sing N N 415 
VAL N   H    sing N N 416 
VAL N   H2   sing N N 417 
VAL CA  C    sing N N 418 
VAL CA  CB   sing N N 419 
VAL CA  HA   sing N N 420 
VAL C   O    doub N N 421 
VAL C   OXT  sing N N 422 
VAL CB  CG1  sing N N 423 
VAL CB  CG2  sing N N 424 
VAL CB  HB   sing N N 425 
VAL CG1 HG11 sing N N 426 
VAL CG1 HG12 sing N N 427 
VAL CG1 HG13 sing N N 428 
VAL CG2 HG21 sing N N 429 
VAL CG2 HG22 sing N N 430 
VAL CG2 HG23 sing N N 431 
VAL OXT HXT  sing N N 432 
WWO O9  S7   doub N N 433 
WWO S7  N10  sing N N 434 
WWO S7  C4   sing N N 435 
WWO S7  O8   doub N N 436 
WWO C16 C17  doub Y N 437 
WWO C16 C15  sing Y N 438 
WWO F27 C5   sing N N 439 
WWO C17 C18  sing Y N 440 
WWO C14 C15  sing N N 441 
WWO C14 N26  sing N N 442 
WWO C4  C5   doub Y N 443 
WWO C4  C3   sing Y N 444 
WWO C5  C6   sing Y N 445 
WWO C15 C20  doub Y N 446 
WWO C3  F12  sing N N 447 
WWO C3  C2   doub Y N 448 
WWO C6  N26  sing N N 449 
WWO C6  C1   doub Y N 450 
WWO O23 S11  doub N N 451 
WWO C18 C19  doub Y N 452 
WWO C2  C1   sing Y N 453 
WWO C2  F13  sing N N 454 
WWO C1  S11  sing N N 455 
WWO O22 S11  doub N N 456 
WWO C20 C19  sing Y N 457 
WWO S11 C21  sing N N 458 
WWO C21 C24  sing N N 459 
WWO O25 C24  sing N N 460 
WWO N10 H1   sing N N 461 
WWO N10 H2   sing N N 462 
WWO C21 H3   sing N N 463 
WWO C21 H4   sing N N 464 
WWO C24 H5   sing N N 465 
WWO C24 H6   sing N N 466 
WWO O25 H7   sing N N 467 
WWO N26 H8   sing N N 468 
WWO C14 H9   sing N N 469 
WWO C14 H10  sing N N 470 
WWO C20 H11  sing N N 471 
WWO C19 H12  sing N N 472 
WWO C18 H13  sing N N 473 
WWO C17 H14  sing N N 474 
WWO C16 H15  sing N N 475 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WWO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WWO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4HT0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7NZU 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.023698 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006012 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024230 
_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]   0.014423 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 32.320  1.531   7.970   1.00 67.75  ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 31.190  2.111   8.768   1.00 38.54  ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.574  0.994   9.641   1.00 30.65  ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.869  -0.185  9.471   1.00 27.87  ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 30.157  2.768   7.842   1.00 36.84  ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 29.720  4.121   8.295   1.00 76.67  ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 30.360  4.800   9.314   1.00 84.32  ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 28.717  4.922   7.877   1.00 92.35  ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 29.768  5.962   9.504   1.00 119.96 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 28.756  6.061   8.634   1.00 113.82 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.712  1.335   10.585  1.00 25.90  ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 29.071  0.330   11.424  1.00 19.75  ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 28.078  -0.485  10.594  1.00 17.88  ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.615  -0.056  9.530   1.00 19.13  ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.301  1.042   12.548  1.00 17.56  ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 27.089  1.819   12.135  1.00 16.55  ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 27.057  3.134   11.795  1.00 23.38  ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.746  1.357   12.096  1.00 17.83  ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.778  3.534   11.533  1.00 23.02  ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.952  2.445   11.675  1.00 17.82  ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 25.170  0.103   12.302  1.00 16.58  ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.563  2.343   11.533  1.00 22.95  ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.783  0.005   12.167  1.00 19.00  ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 22.998  1.100   11.748  1.00 18.55  ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.753  -1.694  11.060  1.00 17.65  ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.736  -2.546  10.443  1.00 19.32  ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.410  -3.683  11.399  1.00 18.91  ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.373  -3.488  12.631  1.00 18.13  ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 26.007  -4.806  10.845  1.00 19.13  ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.562  -5.948  11.640  1.00 19.40  ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.519  -7.158  11.599  1.00 27.13  ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 26.228  -8.150  12.294  1.00 27.78  ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 24.063  -6.256  11.420  1.00 19.53  ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.169  -5.171  11.923  1.00 15.35  ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.733  -5.179  13.234  1.00 16.38  ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.709  -4.191  11.065  1.00 16.16  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 21.881  -4.200  13.701  1.00 14.34  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 21.857  -3.203  11.513  1.00 11.58  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.450  -3.218  12.832  1.00 14.29  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.613  -2.261  13.279  1.00 15.92  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.666  -7.103  10.857  1.00 27.97  ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 28.595  -8.236  10.634  1.00 27.93  ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.606  -8.456  11.751  1.00 28.12  ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.729  -7.710  12.755  1.00 27.17  ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 30.358  -9.539  11.586  1.00 38.12  ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 31.374  -9.891  12.572  1.00 37.49  ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 32.359  -8.731  12.677  1.00 35.51  ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 32.794  -8.407  13.814  1.00 24.45  ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 32.133  -11.148 12.156  1.00 33.55  ? 9   LYS A CB  1 
ATOM   50   N  N   . HIS A 1 10  ? 32.608  -8.055  11.479  1.00 40.53  ? 10  HIS A N   1 
ATOM   51   C  CA  . HIS A 1 10  ? 33.732  -7.069  11.645  1.00 44.61  ? 10  HIS A CA  1 
ATOM   52   C  C   . HIS A 1 10  ? 33.235  -5.674  12.012  1.00 33.08  ? 10  HIS A C   1 
ATOM   53   O  O   . HIS A 1 10  ? 34.083  -4.868  12.426  1.00 25.91  ? 10  HIS A O   1 
ATOM   54   C  CB  . HIS A 1 10  ? 34.681  -7.091  10.460  1.00 40.60  ? 10  HIS A CB  1 
ATOM   55   C  CG  . HIS A 1 10  ? 35.509  -8.341  10.488  1.00 35.61  ? 10  HIS A CG  1 
ATOM   56   N  ND1 . HIS A 1 10  ? 36.555  -8.553  11.445  1.00 27.20  ? 10  HIS A ND1 1 
ATOM   57   C  CD2 . HIS A 1 10  ? 35.389  -9.474  9.727   1.00 40.53  ? 10  HIS A CD2 1 
ATOM   58   C  CE1 . HIS A 1 10  ? 37.078  -9.746  11.223  1.00 30.31  ? 10  HIS A CE1 1 
ATOM   59   N  NE2 . HIS A 1 10  ? 36.343  -10.348 10.177  1.00 32.86  ? 10  HIS A NE2 1 
ATOM   60   N  N   . ASN A 1 11  ? 31.888  -5.395  11.987  1.00 22.78  ? 11  ASN A N   1 
ATOM   61   C  CA  . ASN A 1 11  ? 31.380  -4.025  12.239  1.00 20.54  ? 11  ASN A CA  1 
ATOM   62   C  C   . ASN A 1 11  ? 30.050  -3.994  13.025  1.00 19.81  ? 11  ASN A C   1 
ATOM   63   O  O   . ASN A 1 11  ? 29.432  -2.956  13.158  1.00 18.26  ? 11  ASN A O   1 
ATOM   64   C  CB  . ASN A 1 11  ? 31.223  -3.215  10.967  1.00 20.56  ? 11  ASN A CB  1 
ATOM   65   C  CG  . ASN A 1 11  ? 30.168  -3.771  10.042  1.00 20.95  ? 11  ASN A CG  1 
ATOM   66   O  OD1 . ASN A 1 11  ? 29.514  -4.767  10.373  1.00 24.18  ? 11  ASN A OD1 1 
ATOM   67   N  ND2 . ASN A 1 11  ? 30.003  -3.162  8.863   1.00 24.38  ? 11  ASN A ND2 1 
ATOM   68   N  N   . GLY A 1 12  ? 29.693  -5.151  13.595  1.00 18.57  ? 12  GLY A N   1 
ATOM   69   C  CA  . GLY A 1 12  ? 28.406  -5.328  14.270  1.00 16.78  ? 12  GLY A CA  1 
ATOM   70   C  C   . GLY A 1 12  ? 28.390  -4.696  15.659  1.00 15.52  ? 12  GLY A C   1 
ATOM   71   O  O   . GLY A 1 12  ? 29.270  -3.974  16.088  1.00 15.23  ? 12  GLY A O   1 
ATOM   72   N  N   . PRO A 1 13  ? 27.294  -5.009  16.362  1.00 14.35  ? 13  PRO A N   1 
ATOM   73   C  CA  . PRO A 1 13  ? 27.017  -4.438  17.671  1.00 13.65  ? 13  PRO A CA  1 
ATOM   74   C  C   . PRO A 1 13  ? 28.164  -4.422  18.639  1.00 13.77  ? 13  PRO A C   1 
ATOM   75   O  O   . PRO A 1 13  ? 28.270  -3.496  19.434  1.00 14.34  ? 13  PRO A O   1 
ATOM   76   C  CB  . PRO A 1 13  ? 25.830  -5.285  18.162  1.00 15.37  ? 13  PRO A CB  1 
ATOM   77   C  CG  . PRO A 1 13  ? 25.041  -5.506  16.932  1.00 14.39  ? 13  PRO A CG  1 
ATOM   78   C  CD  . PRO A 1 13  ? 26.120  -5.775  15.861  1.00 14.31  ? 13  PRO A CD  1 
ATOM   79   N  N   . GLU A 1 14  ? 28.994  -5.454  18.615  1.00 15.13  ? 14  GLU A N   1 
ATOM   80   C  CA  . GLU A 1 14  ? 30.094  -5.543  19.579  1.00 16.95  ? 14  GLU A CA  1 
ATOM   81   C  C   . GLU A 1 14  ? 31.206  -4.529  19.287  1.00 15.59  ? 14  GLU A C   1 
ATOM   82   O  O   . GLU A 1 14  ? 32.086  -4.360  20.118  1.00 15.81  ? 14  GLU A O   1 
ATOM   83   C  CB  . GLU A 1 14  ? 30.694  -6.945  19.428  1.00 23.05  ? 14  GLU A CB  1 
ATOM   84   C  CG  . GLU A 1 14  ? 31.238  -7.227  18.028  1.00 29.47  ? 14  GLU A CG  1 
ATOM   85   C  CD  . GLU A 1 14  ? 30.380  -8.047  17.069  1.00 31.79  ? 14  GLU A CD  1 
ATOM   86   O  OE1 . GLU A 1 14  ? 29.185  -7.723  16.922  1.00 23.38  ? 14  GLU A OE1 1 
ATOM   87   O  OE2 . GLU A 1 14  ? 30.912  -9.005  16.474  1.00 33.63  ? 14  GLU A OE2 1 
ATOM   88   N  N   . HIS A 1 15  ? 31.172  -3.925  18.088  1.00 13.57  ? 15  HIS A N   1 
ATOM   89   C  CA  . HIS A 1 15  ? 32.187  -2.952  17.721  1.00 13.78  ? 15  HIS A CA  1 
ATOM   90   C  C   . HIS A 1 15  ? 31.727  -1.520  17.939  1.00 12.00  ? 15  HIS A C   1 
ATOM   91   O  O   . HIS A 1 15  ? 32.529  -0.611  17.906  1.00 12.76  ? 15  HIS A O   1 
ATOM   92   C  CB  . HIS A 1 15  ? 32.534  -3.107  16.262  1.00 14.22  ? 15  HIS A CB  1 
ATOM   93   C  CG  . HIS A 1 15  ? 33.270  -4.360  15.998  1.00 16.39  ? 15  HIS A CG  1 
ATOM   94   N  ND1 . HIS A 1 15  ? 34.649  -4.404  16.071  1.00 17.08  ? 15  HIS A ND1 1 
ATOM   95   C  CD2 . HIS A 1 15  ? 32.840  -5.597  15.696  1.00 17.25  ? 15  HIS A CD2 1 
ATOM   96   C  CE1 . HIS A 1 15  ? 35.070  -5.626  15.806  1.00 21.71  ? 15  HIS A CE1 1 
ATOM   97   N  NE2 . HIS A 1 15  ? 33.991  -6.402  15.563  1.00 18.92  ? 15  HIS A NE2 1 
ATOM   98   N  N   . TRP A 1 16  ? 30.408  -1.284  18.118  1.00 11.85  ? 16  TRP A N   1 
ATOM   99   C  CA  . TRP A 1 16  ? 29.873  0.069   18.011  1.00 11.15  ? 16  TRP A CA  1 
ATOM   100  C  C   . TRP A 1 16  ? 30.455  1.001   19.067  1.00 10.65  ? 16  TRP A C   1 
ATOM   101  O  O   . TRP A 1 16  ? 30.574  2.177   18.834  1.00 11.39  ? 16  TRP A O   1 
ATOM   102  C  CB  . TRP A 1 16  ? 28.344  0.043   18.112  1.00 11.55  ? 16  TRP A CB  1 
ATOM   103  C  CG  . TRP A 1 16  ? 27.677  -0.662  16.975  1.00 11.80  ? 16  TRP A CG  1 
ATOM   104  C  CD1 . TRP A 1 16  ? 28.242  -1.086  15.788  1.00 13.23  ? 16  TRP A CD1 1 
ATOM   105  C  CD2 . TRP A 1 16  ? 26.313  -1.016  16.898  1.00 10.59  ? 16  TRP A CD2 1 
ATOM   106  N  NE1 . TRP A 1 16  ? 27.274  -1.654  14.965  1.00 13.52  ? 16  TRP A NE1 1 
ATOM   107  C  CE2 . TRP A 1 16  ? 26.091  -1.630  15.651  1.00 11.98  ? 16  TRP A CE2 1 
ATOM   108  C  CE3 . TRP A 1 16  ? 25.227  -0.865  17.804  1.00 9.87   ? 16  TRP A CE3 1 
ATOM   109  C  CZ2 . TRP A 1 16  ? 24.851  -2.074  15.239  1.00 12.89  ? 16  TRP A CZ2 1 
ATOM   110  C  CZ3 . TRP A 1 16  ? 24.004  -1.346  17.413  1.00 9.25   ? 16  TRP A CZ3 1 
ATOM   111  C  CH2 . TRP A 1 16  ? 23.816  -1.869  16.118  1.00 11.34  ? 16  TRP A CH2 1 
ATOM   112  N  N   . HIS A 1 17  ? 30.802  0.459   20.233  1.00 11.40  ? 17  HIS A N   1 
ATOM   113  C  CA  . HIS A 1 17  ? 31.307  1.268   21.324  1.00 11.85  ? 17  HIS A CA  1 
ATOM   114  C  C   . HIS A 1 17  ? 32.553  2.090   20.963  1.00 12.96  ? 17  HIS A C   1 
ATOM   115  O  O   . HIS A 1 17  ? 32.828  3.123   21.574  1.00 13.45  ? 17  HIS A O   1 
ATOM   116  C  CB  . HIS A 1 17  ? 31.571  0.443   22.567  1.00 11.85  ? 17  HIS A CB  1 
ATOM   117  C  CG  . HIS A 1 17  ? 32.770  -0.427  22.440  1.00 11.99  ? 17  HIS A CG  1 
ATOM   118  N  ND1 . HIS A 1 17  ? 34.035  -0.063  22.955  1.00 14.22  ? 17  HIS A ND1 1 
ATOM   119  C  CD2 . HIS A 1 17  ? 32.942  -1.578  21.774  1.00 13.78  ? 17  HIS A CD2 1 
ATOM   120  C  CE1 . HIS A 1 17  ? 34.898  -1.010  22.640  1.00 17.59  ? 17  HIS A CE1 1 
ATOM   121  N  NE2 . HIS A 1 17  ? 34.261  -1.962  21.956  1.00 15.84  ? 17  HIS A NE2 1 
ATOM   122  N  N   . LYS A 1 18  ? 33.311  1.604   19.965  1.00 13.70  ? 18  LYS A N   1 
ATOM   123  C  CA  . LYS A 1 18  ? 34.575  2.320   19.635  1.00 13.51  ? 18  LYS A CA  1 
ATOM   124  C  C   . LYS A 1 18  ? 34.255  3.675   19.025  1.00 15.82  ? 18  LYS A C   1 
ATOM   125  O  O   . LYS A 1 18  ? 34.933  4.695   19.277  1.00 22.55  ? 18  LYS A O   1 
ATOM   126  C  CB  . LYS A 1 18  ? 35.407  1.445   18.671  1.00 14.73  ? 18  LYS A CB  1 
ATOM   127  C  CG  . LYS A 1 18  ? 35.989  0.224   19.400  1.00 14.71  ? 18  LYS A CG  1 
ATOM   128  C  CD  . LYS A 1 18  ? 36.753  -0.693  18.427  1.00 15.64  ? 18  LYS A CD  1 
ATOM   129  C  CE  . LYS A 1 18  ? 35.789  -1.615  17.738  1.00 14.49  ? 18  LYS A CE  1 
ATOM   130  N  NZ  . LYS A 1 18  ? 36.468  -2.367  16.655  1.00 15.31  ? 18  LYS A NZ  1 
ATOM   131  N  N   A ASP A 1 19  ? 33.149  3.722   18.211  0.50 15.37  ? 19  ASP A N   1 
ATOM   132  N  N   B ASP A 1 19  ? 33.164  3.727   18.201  0.50 14.78  ? 19  ASP A N   1 
ATOM   133  C  CA  A ASP A 1 19  ? 32.768  4.989   17.607  0.50 14.28  ? 19  ASP A CA  1 
ATOM   134  C  CA  B ASP A 1 19  ? 32.821  5.011   17.617  0.50 15.31  ? 19  ASP A CA  1 
ATOM   135  C  C   A ASP A 1 19  ? 31.844  5.794   18.494  0.50 15.11  ? 19  ASP A C   1 
ATOM   136  C  C   B ASP A 1 19  ? 31.868  5.790   18.506  0.50 14.43  ? 19  ASP A C   1 
ATOM   137  O  O   A ASP A 1 19  ? 31.786  7.025   18.373  0.50 16.81  ? 19  ASP A O   1 
ATOM   138  O  O   B ASP A 1 19  ? 31.816  7.018   18.420  0.50 16.83  ? 19  ASP A O   1 
ATOM   139  C  CB  A ASP A 1 19  ? 32.234  4.838   16.189  0.50 21.08  ? 19  ASP A CB  1 
ATOM   140  C  CB  B ASP A 1 19  ? 32.323  4.851   16.188  0.50 21.51  ? 19  ASP A CB  1 
ATOM   141  C  CG  A ASP A 1 19  ? 33.399  4.539   15.271  0.50 26.60  ? 19  ASP A CG  1 
ATOM   142  C  CG  B ASP A 1 19  ? 33.419  5.109   15.172  0.50 32.49  ? 19  ASP A CG  1 
ATOM   143  O  OD1 A ASP A 1 19  ? 34.255  5.485   15.052  0.50 21.09  ? 19  ASP A OD1 1 
ATOM   144  O  OD1 B ASP A 1 19  ? 34.521  5.499   15.586  0.50 30.67  ? 19  ASP A OD1 1 
ATOM   145  O  OD2 A ASP A 1 19  ? 33.528  3.345   14.928  0.50 25.91  ? 19  ASP A OD2 1 
ATOM   146  O  OD2 B ASP A 1 19  ? 33.168  4.858   14.016  0.50 24.40  ? 19  ASP A OD2 1 
ATOM   147  N  N   . PHE A 1 20  ? 31.047  5.022   19.265  1.00 12.66  ? 20  PHE A N   1 
ATOM   148  C  CA  . PHE A 1 20  ? 29.907  5.546   20.021  1.00 12.59  ? 20  PHE A CA  1 
ATOM   149  C  C   . PHE A 1 20  ? 30.002  5.008   21.425  1.00 13.24  ? 20  PHE A C   1 
ATOM   150  O  O   . PHE A 1 20  ? 29.345  4.037   21.756  1.00 12.20  ? 20  PHE A O   1 
ATOM   151  C  CB  . PHE A 1 20  ? 28.588  5.105   19.352  1.00 14.63  ? 20  PHE A CB  1 
ATOM   152  C  CG  . PHE A 1 20  ? 28.579  5.500   17.890  1.00 16.13  ? 20  PHE A CG  1 
ATOM   153  C  CD1 . PHE A 1 20  ? 28.230  6.791   17.539  1.00 19.61  ? 20  PHE A CD1 1 
ATOM   154  C  CD2 . PHE A 1 20  ? 28.974  4.609   16.885  1.00 17.32  ? 20  PHE A CD2 1 
ATOM   155  C  CE1 . PHE A 1 20  ? 28.380  7.216   16.176  1.00 19.84  ? 20  PHE A CE1 1 
ATOM   156  C  CE2 . PHE A 1 20  ? 28.996  4.968   15.540  1.00 18.87  ? 20  PHE A CE2 1 
ATOM   157  C  CZ  . PHE A 1 20  ? 28.706  6.287   15.195  1.00 20.53  ? 20  PHE A CZ  1 
ATOM   158  N  N   . PRO A 1 21  ? 30.820  5.610   22.305  1.00 13.44  ? 21  PRO A N   1 
ATOM   159  C  CA  . PRO A 1 21  ? 31.080  5.053   23.630  1.00 14.74  ? 21  PRO A CA  1 
ATOM   160  C  C   . PRO A 1 21  ? 29.839  4.927   24.488  1.00 12.39  ? 21  PRO A C   1 
ATOM   161  O  O   . PRO A 1 21  ? 29.855  4.138   25.454  1.00 12.81  ? 21  PRO A O   1 
ATOM   162  C  CB  . PRO A 1 21  ? 32.093  5.985   24.308  1.00 18.68  ? 21  PRO A CB  1 
ATOM   163  C  CG  . PRO A 1 21  ? 32.142  7.193   23.380  1.00 24.77  ? 21  PRO A CG  1 
ATOM   164  C  CD  . PRO A 1 21  ? 31.760  6.729   21.967  1.00 16.65  ? 21  PRO A CD  1 
ATOM   165  N  N   . ILE A 1 22  ? 28.767  5.701   24.176  1.00 11.53  ? 22  ILE A N   1 
ATOM   166  C  CA  . ILE A 1 22  ? 27.506  5.526   24.929  1.00 11.09  ? 22  ILE A CA  1 
ATOM   167  C  C   . ILE A 1 22  ? 26.937  4.129   24.734  1.00 10.28  ? 22  ILE A C   1 
ATOM   168  O  O   . ILE A 1 22  ? 26.018  3.774   25.479  1.00 10.08  ? 22  ILE A O   1 
ATOM   169  C  CB  . ILE A 1 22  ? 26.490  6.614   24.517  1.00 11.45  ? 22  ILE A CB  1 
ATOM   170  C  CG1 . ILE A 1 22  ? 25.383  6.845   25.559  1.00 13.99  ? 22  ILE A CG1 1 
ATOM   171  C  CG2 . ILE A 1 22  ? 25.917  6.352   23.098  1.00 12.24  ? 22  ILE A CG2 1 
ATOM   172  C  CD1 . ILE A 1 22  ? 25.898  7.388   26.854  1.00 18.40  ? 22  ILE A CD1 1 
ATOM   173  N  N   . ALA A 1 23  ? 27.470  3.338   23.784  1.00 10.16  ? 23  ALA A N   1 
ATOM   174  C  CA  . ALA A 1 23  ? 27.058  1.946   23.670  1.00 10.42  ? 23  ALA A CA  1 
ATOM   175  C  C   . ALA A 1 23  ? 27.143  1.163   24.978  1.00 10.00  ? 23  ALA A C   1 
ATOM   176  O  O   . ALA A 1 23  ? 26.427  0.182   25.106  1.00 11.58  ? 23  ALA A O   1 
ATOM   177  C  CB  . ALA A 1 23  ? 27.853  1.239   22.627  1.00 10.49  ? 23  ALA A CB  1 
ATOM   178  N  N   . LYS A 1 24  ? 28.043  1.604   25.895  1.00 11.13  ? 24  LYS A N   1 
ATOM   179  C  CA  . LYS A 1 24  ? 28.255  0.997   27.196  1.00 11.79  ? 24  LYS A CA  1 
ATOM   180  C  C   . LYS A 1 24  ? 27.614  1.830   28.303  1.00 12.53  ? 24  LYS A C   1 
ATOM   181  O  O   . LYS A 1 24  ? 28.002  1.741   29.477  1.00 15.13  ? 24  LYS A O   1 
ATOM   182  C  CB  . LYS A 1 24  ? 29.747  0.795   27.425  1.00 14.20  ? 24  LYS A CB  1 
ATOM   183  C  CG  . LYS A 1 24  ? 30.342  -0.237  26.476  1.00 17.20  ? 24  LYS A CG  1 
ATOM   184  C  CD  . LYS A 1 24  ? 31.827  -0.470  26.805  1.00 19.46  ? 24  LYS A CD  1 
ATOM   185  C  CE  . LYS A 1 24  ? 32.485  -1.383  25.812  1.00 23.53  ? 24  LYS A CE  1 
ATOM   186  N  NZ  . LYS A 1 24  ? 32.073  -2.752  26.143  1.00 27.77  ? 24  LYS A NZ  1 
ATOM   187  N  N   . GLY A 1 25  ? 26.611  2.655   27.942  1.00 12.00  ? 25  GLY A N   1 
ATOM   188  C  CA  . GLY A 1 25  ? 25.949  3.594   28.863  1.00 13.85  ? 25  GLY A CA  1 
ATOM   189  C  C   . GLY A 1 25  ? 25.000  2.906   29.826  1.00 12.60  ? 25  GLY A C   1 
ATOM   190  O  O   . GLY A 1 25  ? 24.844  1.673   29.822  1.00 12.34  ? 25  GLY A O   1 
ATOM   191  N  N   . GLU A 1 26  ? 24.289  3.743   30.611  1.00 12.65  ? 26  GLU A N   1 
ATOM   192  C  CA  . GLU A 1 26  ? 23.397  3.212   31.641  1.00 13.80  ? 26  GLU A CA  1 
ATOM   193  C  C   . GLU A 1 26  ? 21.974  3.050   31.192  1.00 10.42  ? 26  GLU A C   1 
ATOM   194  O  O   . GLU A 1 26  ? 21.157  2.550   31.984  1.00 11.84  ? 26  GLU A O   1 
ATOM   195  C  CB  . GLU A 1 26  ? 23.409  4.197   32.824  1.00 19.23  ? 26  GLU A CB  1 
ATOM   196  C  CG  . GLU A 1 26  ? 24.773  4.384   33.459  1.00 23.54  ? 26  GLU A CG  1 
ATOM   197  C  CD  . GLU A 1 26  ? 25.343  3.050   33.903  1.00 30.60  ? 26  GLU A CD  1 
ATOM   198  O  OE1 . GLU A 1 26  ? 24.696  2.339   34.716  1.00 40.55  ? 26  GLU A OE1 1 
ATOM   199  O  OE2 . GLU A 1 26  ? 26.511  2.833   33.502  1.00 37.58  ? 26  GLU A OE2 1 
ATOM   200  N  N   A ARG A 1 27  ? 21.612  3.544   29.998  0.50 8.89   ? 27  ARG A N   1 
ATOM   201  N  N   B ARG A 1 27  ? 21.699  3.422   29.941  0.50 9.32   ? 27  ARG A N   1 
ATOM   202  C  CA  A ARG A 1 27  ? 20.219  3.369   29.548  0.50 8.34   ? 27  ARG A CA  1 
ATOM   203  C  CA  B ARG A 1 27  ? 20.287  3.434   29.479  0.50 7.96   ? 27  ARG A CA  1 
ATOM   204  C  C   A ARG A 1 27  ? 20.141  2.873   28.102  0.50 7.55   ? 27  ARG A C   1 
ATOM   205  C  C   B ARG A 1 27  ? 20.268  2.950   28.032  0.50 7.75   ? 27  ARG A C   1 
ATOM   206  O  O   A ARG A 1 27  ? 19.381  3.379   27.281  0.50 7.72   ? 27  ARG A O   1 
ATOM   207  O  O   B ARG A 1 27  ? 19.584  3.557   27.201  0.50 8.85   ? 27  ARG A O   1 
ATOM   208  C  CB  A ARG A 1 27  ? 19.309  4.578   29.814  0.50 10.51  ? 27  ARG A CB  1 
ATOM   209  C  CB  B ARG A 1 27  ? 19.695  4.846   29.582  0.50 9.75   ? 27  ARG A CB  1 
ATOM   210  C  CG  A ARG A 1 27  ? 19.740  5.894   29.158  0.50 12.56  ? 27  ARG A CG  1 
ATOM   211  C  CG  B ARG A 1 27  ? 20.019  5.623   30.855  0.50 9.46   ? 27  ARG A CG  1 
ATOM   212  C  CD  A ARG A 1 27  ? 18.949  7.199   29.370  0.50 15.07  ? 27  ARG A CD  1 
ATOM   213  C  CD  B ARG A 1 27  ? 19.390  7.004   30.760  0.50 10.55  ? 27  ARG A CD  1 
ATOM   214  N  NE  A ARG A 1 27  ? 17.734  7.208   28.573  0.50 14.94  ? 27  ARG A NE  1 
ATOM   215  N  NE  B ARG A 1 27  ? 19.659  7.829   31.917  0.50 10.79  ? 27  ARG A NE  1 
ATOM   216  C  CZ  A ARG A 1 27  ? 16.851  8.173   28.381  0.50 11.51  ? 27  ARG A CZ  1 
ATOM   217  C  CZ  B ARG A 1 27  ? 20.710  8.631   32.042  0.50 10.65  ? 27  ARG A CZ  1 
ATOM   218  N  NH1 A ARG A 1 27  ? 17.018  9.348   28.963  0.50 4.25   ? 27  ARG A NH1 1 
ATOM   219  N  NH1 B ARG A 1 27  ? 21.599  8.714   31.067  0.50 12.45  ? 27  ARG A NH1 1 
ATOM   220  N  NH2 A ARG A 1 27  ? 15.802  7.965   27.604  0.50 8.82   ? 27  ARG A NH2 1 
ATOM   221  N  NH2 B ARG A 1 27  ? 20.869  9.347   33.140  0.50 11.94  ? 27  ARG A NH2 1 
ATOM   222  N  N   . GLN A 1 28  ? 20.906  1.815   27.780  1.00 8.04   ? 28  GLN A N   1 
ATOM   223  C  CA  . GLN A 1 28  ? 20.944  1.317   26.415  1.00 7.45   ? 28  GLN A CA  1 
ATOM   224  C  C   . GLN A 1 28  ? 19.781  0.369   26.151  1.00 6.85   ? 28  GLN A C   1 
ATOM   225  O  O   . GLN A 1 28  ? 19.273  -0.348  26.999  1.00 8.09   ? 28  GLN A O   1 
ATOM   226  C  CB  . GLN A 1 28  ? 22.299  0.616   26.190  1.00 8.30   ? 28  GLN A CB  1 
ATOM   227  C  CG  . GLN A 1 28  ? 23.422  1.643   26.153  1.00 8.54   ? 28  GLN A CG  1 
ATOM   228  C  CD  . GLN A 1 28  ? 23.317  2.486   24.894  1.00 8.01   ? 28  GLN A CD  1 
ATOM   229  O  OE1 . GLN A 1 28  ? 23.513  1.963   23.785  1.00 8.39   ? 28  GLN A OE1 1 
ATOM   230  N  NE2 . GLN A 1 28  ? 22.982  3.767   24.988  1.00 8.69   ? 28  GLN A NE2 1 
ATOM   231  N  N   . SER A 1 29  ? 19.399  0.323   24.857  1.00 6.85   ? 29  SER A N   1 
ATOM   232  C  CA  . SER A 1 29  ? 18.325  -0.534  24.374  1.00 6.46   ? 29  SER A CA  1 
ATOM   233  C  C   . SER A 1 29  ? 18.848  -1.369  23.229  1.00 6.35   ? 29  SER A C   1 
ATOM   234  O  O   . SER A 1 29  ? 19.812  -1.035  22.546  1.00 7.21   ? 29  SER A O   1 
ATOM   235  C  CB  . SER A 1 29  ? 17.176  0.346   23.842  1.00 7.06   ? 29  SER A CB  1 
ATOM   236  O  OG  . SER A 1 29  ? 16.598  1.081   24.912  1.00 7.33   ? 29  SER A OG  1 
ATOM   237  N  N   . PRO A 1 30  ? 18.194  -2.494  22.937  1.00 6.31   ? 30  PRO A N   1 
ATOM   238  C  CA  . PRO A 1 30  ? 17.011  -3.039  23.633  1.00 6.49   ? 30  PRO A CA  1 
ATOM   239  C  C   . PRO A 1 30  ? 17.425  -3.740  24.920  1.00 6.34   ? 30  PRO A C   1 
ATOM   240  O  O   . PRO A 1 30  ? 18.609  -3.791  25.267  1.00 7.26   ? 30  PRO A O   1 
ATOM   241  C  CB  . PRO A 1 30  ? 16.503  -4.054  22.601  1.00 6.56   ? 30  PRO A CB  1 
ATOM   242  C  CG  . PRO A 1 30  ? 17.767  -4.619  21.998  1.00 6.48   ? 30  PRO A CG  1 
ATOM   243  C  CD  . PRO A 1 30  ? 18.651  -3.402  21.864  1.00 6.77   ? 30  PRO A CD  1 
ATOM   244  N  N   . VAL A 1 31  ? 16.427  -4.292  25.612  1.00 7.29   ? 31  VAL A N   1 
ATOM   245  C  CA  . VAL A 1 31  ? 16.632  -5.036  26.840  1.00 7.79   ? 31  VAL A CA  1 
ATOM   246  C  C   . VAL A 1 31  ? 15.741  -6.284  26.769  1.00 7.43   ? 31  VAL A C   1 
ATOM   247  O  O   . VAL A 1 31  ? 14.774  -6.325  26.008  1.00 7.99   ? 31  VAL A O   1 
ATOM   248  C  CB  . VAL A 1 31  ? 16.323  -4.216  28.112  1.00 8.23   ? 31  VAL A CB  1 
ATOM   249  C  CG1 . VAL A 1 31  ? 17.223  -2.977  28.233  1.00 9.22   ? 31  VAL A CG1 1 
ATOM   250  C  CG2 . VAL A 1 31  ? 14.837  -3.826  28.167  1.00 9.09   ? 31  VAL A CG2 1 
ATOM   251  N  N   . ASP A 1 32  ? 16.083  -7.267  27.599  1.00 7.79   ? 32  ASP A N   1 
ATOM   252  C  CA  . ASP A 1 32  ? 15.164  -8.322  27.911  1.00 8.73   ? 32  ASP A CA  1 
ATOM   253  C  C   . ASP A 1 32  ? 14.124  -7.794  28.885  1.00 7.87   ? 32  ASP A C   1 
ATOM   254  O  O   . ASP A 1 32  ? 14.433  -7.187  29.924  1.00 9.71   ? 32  ASP A O   1 
ATOM   255  C  CB  . ASP A 1 32  ? 15.915  -9.517  28.500  1.00 9.75   ? 32  ASP A CB  1 
ATOM   256  C  CG  . ASP A 1 32  ? 14.953  -10.689 28.789  1.00 9.73   ? 32  ASP A CG  1 
ATOM   257  O  OD1 . ASP A 1 32  ? 14.273  -11.125 27.852  1.00 10.39  ? 32  ASP A OD1 1 
ATOM   258  O  OD2 . ASP A 1 32  ? 14.920  -11.123 29.951  1.00 12.76  ? 32  ASP A OD2 1 
ATOM   259  N  N   . ILE A 1 33  ? 12.869  -8.083  28.558  1.00 8.18   ? 33  ILE A N   1 
ATOM   260  C  CA  . ILE A 1 33  ? 11.758  -7.712  29.456  1.00 9.34   ? 33  ILE A CA  1 
ATOM   261  C  C   . ILE A 1 33  ? 11.475  -8.954  30.292  1.00 9.95   ? 33  ILE A C   1 
ATOM   262  O  O   . ILE A 1 33  ? 10.897  -9.925  29.828  1.00 10.85  ? 33  ILE A O   1 
ATOM   263  C  CB  . ILE A 1 33  ? 10.551  -7.261  28.629  1.00 9.20   ? 33  ILE A CB  1 
ATOM   264  C  CG1 . ILE A 1 33  ? 10.920  -6.047  27.756  1.00 9.76   ? 33  ILE A CG1 1 
ATOM   265  C  CG2 . ILE A 1 33  ? 9.355   -6.995  29.560  1.00 10.68  ? 33  ILE A CG2 1 
ATOM   266  C  CD1 . ILE A 1 33  ? 9.836   -5.767  26.672  1.00 11.70  ? 33  ILE A CD1 1 
ATOM   267  N  N   . ASP A 1 34  ? 11.839  -8.852  31.569  1.00 10.76  ? 34  ASP A N   1 
ATOM   268  C  CA  . ASP A 1 34  ? 11.570  -9.927  32.563  1.00 11.85  ? 34  ASP A CA  1 
ATOM   269  C  C   . ASP A 1 34  ? 10.164  -9.598  33.071  1.00 11.90  ? 34  ASP A C   1 
ATOM   270  O  O   . ASP A 1 34  ? 9.959   -8.635  33.840  1.00 14.54  ? 34  ASP A O   1 
ATOM   271  C  CB  . ASP A 1 34  ? 12.647  -9.895  33.663  1.00 13.79  ? 34  ASP A CB  1 
ATOM   272  C  CG  . ASP A 1 34  ? 12.431  -10.966 34.732  1.00 16.42  ? 34  ASP A CG  1 
ATOM   273  O  OD1 . ASP A 1 34  ? 11.320  -11.331 34.987  1.00 16.73  ? 34  ASP A OD1 1 
ATOM   274  O  OD2 . ASP A 1 34  ? 13.390  -11.363 35.407  1.00 25.74  ? 34  ASP A OD2 1 
ATOM   275  N  N   . THR A 1 35  ? 9.195   -10.396 32.638  1.00 13.39  ? 35  THR A N   1 
ATOM   276  C  CA  . THR A 1 35  ? 7.834   -10.040 32.919  1.00 15.60  ? 35  THR A CA  1 
ATOM   277  C  C   . THR A 1 35  ? 7.482   -10.258 34.378  1.00 15.66  ? 35  THR A C   1 
ATOM   278  O  O   . THR A 1 35  ? 6.491   -9.703  34.853  1.00 16.64  ? 35  THR A O   1 
ATOM   279  C  CB  . THR A 1 35  ? 6.938   -10.913 32.057  1.00 15.39  ? 35  THR A CB  1 
ATOM   280  O  OG1 . THR A 1 35  ? 7.024   -12.261 32.512  1.00 15.55  ? 35  THR A OG1 1 
ATOM   281  C  CG2 . THR A 1 35  ? 7.124   -10.759 30.567  1.00 17.74  ? 35  THR A CG2 1 
ATOM   282  N  N   . HIS A 1 36  ? 8.347   -10.987 35.133  1.00 15.38  ? 36  HIS A N   1 
ATOM   283  C  CA  . HIS A 1 36  ? 8.174   -11.221 36.585  1.00 16.33  ? 36  HIS A CA  1 
ATOM   284  C  C   . HIS A 1 36  ? 8.835   -10.188 37.516  1.00 18.22  ? 36  HIS A C   1 
ATOM   285  O  O   . HIS A 1 36  ? 8.720   -10.239 38.764  1.00 18.38  ? 36  HIS A O   1 
ATOM   286  C  CB  . HIS A 1 36  ? 8.852   -12.531 36.935  1.00 16.12  ? 36  HIS A CB  1 
ATOM   287  C  CG  . HIS A 1 36  ? 8.407   -13.567 35.996  1.00 16.65  ? 36  HIS A CG  1 
ATOM   288  N  ND1 . HIS A 1 36  ? 7.095   -14.067 35.957  1.00 18.81  ? 36  HIS A ND1 1 
ATOM   289  C  CD2 . HIS A 1 36  ? 9.055   -14.175 34.964  1.00 17.27  ? 36  HIS A CD2 1 
ATOM   290  C  CE1 . HIS A 1 36  ? 6.982   -14.999 35.025  1.00 21.19  ? 36  HIS A CE1 1 
ATOM   291  N  NE2 . HIS A 1 36  ? 8.185   -15.068 34.409  1.00 21.09  ? 36  HIS A NE2 1 
ATOM   292  N  N   . THR A 1 37  ? 9.636   -9.312  36.954  1.00 15.92  ? 37  THR A N   1 
ATOM   293  C  CA  . THR A 1 37  ? 10.179  -8.207  37.735  1.00 16.31  ? 37  THR A CA  1 
ATOM   294  C  C   . THR A 1 37  ? 9.563   -6.904  37.259  1.00 15.99  ? 37  THR A C   1 
ATOM   295  O  O   . THR A 1 37  ? 9.701   -5.937  37.979  1.00 22.98  ? 37  THR A O   1 
ATOM   296  C  CB  . THR A 1 37  ? 11.709  -8.171  37.833  1.00 22.41  ? 37  THR A CB  1 
ATOM   297  O  OG1 . THR A 1 37  ? 12.209  -8.200  36.548  1.00 24.01  ? 37  THR A OG1 1 
ATOM   298  C  CG2 . THR A 1 37  ? 12.215  -9.477  38.352  1.00 22.54  ? 37  THR A CG2 1 
ATOM   299  N  N   . ALA A 1 38  ? 8.900   -6.862  36.082  1.00 15.21  ? 38  ALA A N   1 
ATOM   300  C  CA  . ALA A 1 38  ? 8.262   -5.613  35.665  1.00 14.88  ? 38  ALA A CA  1 
ATOM   301  C  C   . ALA A 1 38  ? 7.223   -5.262  36.738  1.00 15.74  ? 38  ALA A C   1 
ATOM   302  O  O   . ALA A 1 38  ? 6.645   -6.114  37.353  1.00 18.58  ? 38  ALA A O   1 
ATOM   303  C  CB  . ALA A 1 38  ? 7.699   -5.748  34.273  1.00 13.53  ? 38  ALA A CB  1 
ATOM   304  N  N   . LYS A 1 39  ? 7.005   -3.986  36.963  1.00 16.43  ? 39  LYS A N   1 
ATOM   305  C  CA  . LYS A 1 39  ? 6.069   -3.540  37.978  1.00 19.11  ? 39  LYS A CA  1 
ATOM   306  C  C   . LYS A 1 39  ? 4.822   -3.002  37.289  1.00 15.21  ? 39  LYS A C   1 
ATOM   307  O  O   . LYS A 1 39  ? 4.925   -2.022  36.555  1.00 13.44  ? 39  LYS A O   1 
ATOM   308  C  CB  . LYS A 1 39  ? 6.869   -2.460  38.723  1.00 24.88  ? 39  LYS A CB  1 
ATOM   309  C  CG  . LYS A 1 39  ? 6.084   -1.538  39.630  1.00 25.13  ? 39  LYS A CG  1 
ATOM   310  C  CD  . LYS A 1 39  ? 5.798   -2.098  41.029  1.00 24.60  ? 39  LYS A CD  1 
ATOM   311  C  CE  . LYS A 1 39  ? 5.054   -1.115  41.886  1.00 26.86  ? 39  LYS A CE  1 
ATOM   312  N  NZ  . LYS A 1 39  ? 4.716   -1.761  43.167  1.00 26.60  ? 39  LYS A NZ  1 
ATOM   313  N  N   . TYR A 1 40  ? 3.643   -3.563  37.620  1.00 17.01  ? 40  TYR A N   1 
ATOM   314  C  CA  . TYR A 1 40  ? 2.333   -3.001  37.284  1.00 15.88  ? 40  TYR A CA  1 
ATOM   315  C  C   . TYR A 1 40  ? 2.309   -1.605  37.869  1.00 13.50  ? 40  TYR A C   1 
ATOM   316  O  O   . TYR A 1 40  ? 2.464   -1.433  39.083  1.00 17.06  ? 40  TYR A O   1 
ATOM   317  C  CB  . TYR A 1 40  ? 1.114   -3.843  37.728  1.00 22.11  ? 40  TYR A CB  1 
ATOM   318  C  CG  . TYR A 1 40  ? -0.224  -3.117  37.668  1.00 26.54  ? 40  TYR A CG  1 
ATOM   319  C  CD1 . TYR A 1 40  ? -0.776  -2.645  36.470  1.00 26.71  ? 40  TYR A CD1 1 
ATOM   320  C  CD2 . TYR A 1 40  ? -1.028  -2.969  38.841  1.00 41.07  ? 40  TYR A CD2 1 
ATOM   321  C  CE1 . TYR A 1 40  ? -2.040  -2.002  36.441  1.00 47.55  ? 40  TYR A CE1 1 
ATOM   322  C  CE2 . TYR A 1 40  ? -2.263  -2.293  38.824  1.00 52.09  ? 40  TYR A CE2 1 
ATOM   323  C  CZ  . TYR A 1 40  ? -2.770  -1.800  37.622  1.00 78.70  ? 40  TYR A CZ  1 
ATOM   324  O  OH  . TYR A 1 40  ? -3.981  -1.138  37.435  1.00 107.74 ? 40  TYR A OH  1 
ATOM   325  N  N   . ASP A 1 41  ? 2.013   -0.607  37.043  1.00 14.30  ? 41  ASP A N   1 
ATOM   326  C  CA  . ASP A 1 41  ? 1.950   0.763   37.539  1.00 14.25  ? 41  ASP A CA  1 
ATOM   327  C  C   . ASP A 1 41  ? 0.535   1.268   37.298  1.00 18.22  ? 41  ASP A C   1 
ATOM   328  O  O   . ASP A 1 41  ? 0.230   1.696   36.193  1.00 19.49  ? 41  ASP A O   1 
ATOM   329  C  CB  . ASP A 1 41  ? 3.000   1.663   36.887  1.00 16.96  ? 41  ASP A CB  1 
ATOM   330  C  CG  . ASP A 1 41  ? 2.959   3.087   37.424  1.00 25.39  ? 41  ASP A CG  1 
ATOM   331  O  OD1 . ASP A 1 41  ? 2.018   3.386   38.200  1.00 27.38  ? 41  ASP A OD1 1 
ATOM   332  O  OD2 . ASP A 1 41  ? 3.875   3.872   37.101  1.00 28.61  ? 41  ASP A OD2 1 
ATOM   333  N  N   . PRO A 1 42  ? -0.353  1.220   38.319  1.00 20.85  ? 42  PRO A N   1 
ATOM   334  C  CA  . PRO A 1 42  ? -1.748  1.663   38.180  1.00 33.74  ? 42  PRO A CA  1 
ATOM   335  C  C   . PRO A 1 42  ? -1.857  3.168   37.897  1.00 38.28  ? 42  PRO A C   1 
ATOM   336  O  O   . PRO A 1 42  ? -2.930  3.629   37.471  1.00 34.81  ? 42  PRO A O   1 
ATOM   337  C  CB  . PRO A 1 42  ? -2.378  1.331   39.542  1.00 42.13  ? 42  PRO A CB  1 
ATOM   338  C  CG  . PRO A 1 42  ? -1.205  1.302   40.495  1.00 45.49  ? 42  PRO A CG  1 
ATOM   339  C  CD  . PRO A 1 42  ? -0.059  0.747   39.674  1.00 36.31  ? 42  PRO A CD  1 
ATOM   340  N  N   . SER A 1 43  ? -0.709  3.890   37.954  1.00 27.44  ? 43  SER A N   1 
ATOM   341  C  CA  . SER A 1 43  ? -0.782  5.331   37.723  1.00 31.89  ? 43  SER A CA  1 
ATOM   342  C  C   . SER A 1 43  ? -0.523  5.666   36.247  1.00 31.59  ? 43  SER A C   1 
ATOM   343  O  O   . SER A 1 43  ? -0.824  6.787   35.830  1.00 39.29  ? 43  SER A O   1 
ATOM   344  C  CB  . SER A 1 43  ? 0.170   6.064   38.605  1.00 39.27  ? 43  SER A CB  1 
ATOM   345  O  OG  . SER A 1 43  ? 1.455   6.101   38.027  1.00 38.68  ? 43  SER A OG  1 
ATOM   346  N  N   . LEU A 1 44  ? -0.029  4.701   35.449  1.00 32.95  ? 44  LEU A N   1 
ATOM   347  C  CA  . LEU A 1 44  ? 0.180   4.958   34.038  1.00 34.41  ? 44  LEU A CA  1 
ATOM   348  C  C   . LEU A 1 44  ? -1.154  5.142   33.355  1.00 42.10  ? 44  LEU A C   1 
ATOM   349  O  O   . LEU A 1 44  ? -2.144  4.469   33.615  1.00 37.00  ? 44  LEU A O   1 
ATOM   350  C  CB  . LEU A 1 44  ? 0.784   3.754   33.339  1.00 22.82  ? 44  LEU A CB  1 
ATOM   351  C  CG  . LEU A 1 44  ? 2.270   3.513   33.562  1.00 19.57  ? 44  LEU A CG  1 
ATOM   352  C  CD1 . LEU A 1 44  ? 2.651   2.096   33.152  1.00 20.80  ? 44  LEU A CD1 1 
ATOM   353  C  CD2 . LEU A 1 44  ? 3.085   4.523   32.791  1.00 17.99  ? 44  LEU A CD2 1 
ATOM   354  N  N   . LYS A 1 45  ? -1.016  5.892   32.281  1.00 42.78  ? 45  LYS A N   1 
ATOM   355  C  CA  . LYS A 1 45  ? -2.310  6.149   31.637  1.00 41.54  ? 45  LYS A CA  1 
ATOM   356  C  C   . LYS A 1 45  ? -2.467  5.112   30.542  1.00 37.47  ? 45  LYS A C   1 
ATOM   357  O  O   . LYS A 1 45  ? -1.572  4.257   30.323  1.00 41.00  ? 45  LYS A O   1 
ATOM   358  C  CB  . LYS A 1 45  ? -2.348  7.569   31.064  1.00 35.78  ? 45  LYS A CB  1 
ATOM   359  C  CG  . LYS A 1 45  ? -2.270  8.689   32.093  1.00 36.28  ? 45  LYS A CG  1 
ATOM   360  N  N   . PRO A 1 46  ? -3.596  5.152   29.823  1.00 38.94  ? 46  PRO A N   1 
ATOM   361  C  CA  . PRO A 1 46  ? -3.677  4.378   28.614  1.00 26.76  ? 46  PRO A CA  1 
ATOM   362  C  C   . PRO A 1 46  ? -2.862  5.159   27.560  1.00 23.78  ? 46  PRO A C   1 
ATOM   363  O  O   . PRO A 1 46  ? -2.845  6.418   27.683  1.00 31.37  ? 46  PRO A O   1 
ATOM   364  C  CB  . PRO A 1 46  ? -5.175  4.428   28.279  1.00 62.02  ? 46  PRO A CB  1 
ATOM   365  C  CG  . PRO A 1 46  ? -5.647  5.734   28.889  1.00 45.08  ? 46  PRO A CG  1 
ATOM   366  C  CD  . PRO A 1 46  ? -4.801  5.921   30.132  1.00 66.23  ? 46  PRO A CD  1 
ATOM   367  N  N   . LEU A 1 47  ? -2.431  4.371   26.624  1.00 27.93  ? 47  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 47  ? -1.763  4.963   25.529  1.00 27.98  ? 47  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 47  ? -2.920  5.654   24.815  1.00 20.46  ? 47  LEU A C   1 
ATOM   370  O  O   . LEU A 1 47  ? -3.945  5.073   24.630  1.00 23.65  ? 47  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 47  ? -1.425  3.694   24.646  1.00 52.06  ? 47  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 47  ? 0.079   3.878   24.051  1.00 50.35  ? 47  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 47  ? 0.708   5.029   24.855  1.00 54.65  ? 47  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 47  ? 1.049   2.516   24.069  1.00 58.49  ? 47  LEU A CD2 1 
ATOM   375  N  N   . SER A 1 48  ? -2.587  6.706   24.120  1.00 13.91  ? 48  SER A N   1 
ATOM   376  C  CA  . SER A 1 48  ? -3.447  7.256   23.073  1.00 13.80  ? 48  SER A CA  1 
ATOM   377  C  C   . SER A 1 48  ? -2.643  7.257   21.775  1.00 13.56  ? 48  SER A C   1 
ATOM   378  O  O   . SER A 1 48  ? -1.648  7.972   21.641  1.00 14.28  ? 48  SER A O   1 
ATOM   379  C  CB  . SER A 1 48  ? -3.810  8.700   23.488  1.00 15.16  ? 48  SER A CB  1 
ATOM   380  O  OG  . SER A 1 48  ? -4.427  9.401   22.449  1.00 18.44  ? 48  SER A OG  1 
ATOM   381  N  N   . VAL A 1 49  ? -3.076  6.419   20.865  1.00 13.39  ? 49  VAL A N   1 
ATOM   382  C  CA  . VAL A 1 49  ? -2.427  6.285   19.582  1.00 15.10  ? 49  VAL A CA  1 
ATOM   383  C  C   . VAL A 1 49  ? -3.394  6.851   18.543  1.00 15.50  ? 49  VAL A C   1 
ATOM   384  O  O   . VAL A 1 49  ? -4.436  6.281   18.339  1.00 19.62  ? 49  VAL A O   1 
ATOM   385  C  CB  . VAL A 1 49  ? -2.134  4.806   19.283  1.00 17.95  ? 49  VAL A CB  1 
ATOM   386  C  CG1 . VAL A 1 49  ? -1.484  4.657   17.916  1.00 23.99  ? 49  VAL A CG1 1 
ATOM   387  C  CG2 . VAL A 1 49  ? -1.311  4.106   20.374  1.00 19.84  ? 49  VAL A CG2 1 
ATOM   388  N  N   . SER A 1 50  ? -3.131  8.002   17.938  1.00 15.98  ? 50  SER A N   1 
ATOM   389  C  CA  . SER A 1 50  ? -4.071  8.706   17.070  1.00 15.88  ? 50  SER A CA  1 
ATOM   390  C  C   . SER A 1 50  ? -3.465  8.835   15.687  1.00 14.00  ? 50  SER A C   1 
ATOM   391  O  O   . SER A 1 50  ? -2.768  9.796   15.420  1.00 15.76  ? 50  SER A O   1 
ATOM   392  C  CB  . SER A 1 50  ? -4.480  10.073  17.618  1.00 21.34  ? 50  SER A CB  1 
ATOM   393  O  OG  . SER A 1 50  ? -5.138  9.919   18.836  1.00 24.23  ? 50  SER A OG  1 
ATOM   394  N  N   . TYR A 1 51  ? -3.742  7.833   14.838  1.00 14.16  ? 51  TYR A N   1 
ATOM   395  C  CA  . TYR A 1 51  ? -3.142  7.767   13.535  1.00 14.20  ? 51  TYR A CA  1 
ATOM   396  C  C   . TYR A 1 51  ? -4.117  8.044   12.407  1.00 15.45  ? 51  TYR A C   1 
ATOM   397  O  O   . TYR A 1 51  ? -3.737  7.850   11.258  1.00 17.40  ? 51  TYR A O   1 
ATOM   398  C  CB  . TYR A 1 51  ? -2.486  6.389   13.326  1.00 13.30  ? 51  TYR A CB  1 
ATOM   399  C  CG  . TYR A 1 51  ? -1.215  6.096   14.097  1.00 12.87  ? 51  TYR A CG  1 
ATOM   400  C  CD1 . TYR A 1 51  ? -0.534  7.057   14.827  1.00 14.31  ? 51  TYR A CD1 1 
ATOM   401  C  CD2 . TYR A 1 51  ? -0.768  4.785   14.207  1.00 12.08  ? 51  TYR A CD2 1 
ATOM   402  C  CE1 . TYR A 1 51  ? 0.668   6.755   15.463  1.00 11.68  ? 51  TYR A CE1 1 
ATOM   403  C  CE2 . TYR A 1 51  ? 0.414   4.465   14.849  1.00 11.05  ? 51  TYR A CE2 1 
ATOM   404  C  CZ  . TYR A 1 51  ? 1.145   5.455   15.492  1.00 10.60  ? 51  TYR A CZ  1 
ATOM   405  O  OH  . TYR A 1 51  ? 2.249   5.074   16.185  1.00 11.23  ? 51  TYR A OH  1 
ATOM   406  N  N   A ASP A 1 52  ? -5.350  8.487   12.751  0.50 17.73  ? 52  ASP A N   1 
ATOM   407  N  N   B ASP A 1 52  ? -5.369  8.449   12.724  0.50 17.44  ? 52  ASP A N   1 
ATOM   408  C  CA  A ASP A 1 52  ? -6.406  8.714   11.764  0.50 20.90  ? 52  ASP A CA  1 
ATOM   409  C  CA  B ASP A 1 52  ? -6.362  8.671   11.669  0.50 19.75  ? 52  ASP A CA  1 
ATOM   410  C  C   A ASP A 1 52  ? -5.993  9.698   10.663  0.50 20.48  ? 52  ASP A C   1 
ATOM   411  C  C   B ASP A 1 52  ? -5.857  9.617   10.579  0.50 21.18  ? 52  ASP A C   1 
ATOM   412  O  O   A ASP A 1 52  ? -6.411  9.574   9.504   0.50 22.77  ? 52  ASP A O   1 
ATOM   413  O  O   B ASP A 1 52  ? -6.096  9.403   9.375   0.50 25.43  ? 52  ASP A O   1 
ATOM   414  C  CB  A ASP A 1 52  ? -7.728  9.128   12.450  0.50 24.73  ? 52  ASP A CB  1 
ATOM   415  C  CB  B ASP A 1 52  ? -7.710  9.170   12.240  0.50 23.44  ? 52  ASP A CB  1 
ATOM   416  C  CG  A ASP A 1 52  ? -7.521  10.207  13.497  0.50 28.21  ? 52  ASP A CG  1 
ATOM   417  C  CG  B ASP A 1 52  ? -8.804  9.354   11.193  0.50 25.22  ? 52  ASP A CG  1 
ATOM   418  O  OD1 A ASP A 1 52  ? -6.769  9.935   14.526  0.50 26.28  ? 52  ASP A OD1 1 
ATOM   419  O  OD1 B ASP A 1 52  ? -9.132  8.368   10.493  0.50 29.92  ? 52  ASP A OD1 1 
ATOM   420  O  OD2 A ASP A 1 52  ? -8.072  11.314  13.291  0.50 32.57  ? 52  ASP A OD2 1 
ATOM   421  O  OD2 B ASP A 1 52  ? -9.295  10.487  11.065  0.50 38.15  ? 52  ASP A OD2 1 
ATOM   422  N  N   . GLN A 1 53  ? -5.130  10.661  10.986  1.00 19.91  ? 53  GLN A N   1 
ATOM   423  C  CA  . GLN A 1 53  ? -4.754  11.574  9.912   1.00 24.91  ? 53  GLN A CA  1 
ATOM   424  C  C   . GLN A 1 53  ? -3.333  11.335  9.353   1.00 21.04  ? 53  GLN A C   1 
ATOM   425  O  O   . GLN A 1 53  ? -2.700  12.210  8.748   1.00 22.64  ? 53  GLN A O   1 
ATOM   426  C  CB  . GLN A 1 53  ? -5.026  13.011  10.351  1.00 36.08  ? 53  GLN A CB  1 
ATOM   427  C  CG  . GLN A 1 53  ? -6.517  13.284  10.524  1.00 41.43  ? 53  GLN A CG  1 
ATOM   428  C  CD  . GLN A 1 53  ? -7.160  13.369  9.146   1.00 56.30  ? 53  GLN A CD  1 
ATOM   429  O  OE1 . GLN A 1 53  ? -6.742  14.187  8.228   1.00 56.58  ? 53  GLN A OE1 1 
ATOM   430  N  NE2 . GLN A 1 53  ? -8.141  12.487  8.948   1.00 40.07  ? 53  GLN A NE2 1 
ATOM   431  N  N   . ALA A 1 54  ? -2.727  10.191  9.655   1.00 19.44  ? 54  ALA A N   1 
ATOM   432  C  CA  . ALA A 1 54  ? -1.344  9.973   9.243   1.00 15.92  ? 54  ALA A CA  1 
ATOM   433  C  C   . ALA A 1 54  ? -1.182  10.073  7.727   1.00 16.61  ? 54  ALA A C   1 
ATOM   434  O  O   . ALA A 1 54  ? -2.056  9.601   6.976   1.00 21.86  ? 54  ALA A O   1 
ATOM   435  C  CB  . ALA A 1 54  ? -0.894  8.610   9.731   1.00 17.35  ? 54  ALA A CB  1 
ATOM   436  N  N   . THR A 1 55  ? -0.100  10.724  7.299   1.00 14.48  ? 55  THR A N   1 
ATOM   437  C  CA  . THR A 1 55  ? 0.199   10.921  5.886   1.00 16.50  ? 55  THR A CA  1 
ATOM   438  C  C   . THR A 1 55  ? 1.551   10.288  5.550   1.00 11.21  ? 55  THR A C   1 
ATOM   439  O  O   . THR A 1 55  ? 2.578   10.890  5.785   1.00 11.35  ? 55  THR A O   1 
ATOM   440  C  CB  . THR A 1 55  ? 0.289   12.429  5.528   1.00 24.44  ? 55  THR A CB  1 
ATOM   441  O  OG1 . THR A 1 55  ? -0.985  13.017  5.828   1.00 34.28  ? 55  THR A OG1 1 
ATOM   442  C  CG2 . THR A 1 55  ? 0.524   12.568  4.037   1.00 33.06  ? 55  THR A CG2 1 
ATOM   443  N  N   . SER A 1 56  ? 1.533   9.092   5.001   1.00 11.78  ? 56  SER A N   1 
ATOM   444  C  CA  . SER A 1 56  ? 2.796   8.465   4.619   1.00 10.68  ? 56  SER A CA  1 
ATOM   445  C  C   . SER A 1 56  ? 3.317   9.129   3.343   1.00 12.74  ? 56  SER A C   1 
ATOM   446  O  O   . SER A 1 56  ? 2.563   9.598   2.486   1.00 14.22  ? 56  SER A O   1 
ATOM   447  C  CB  . SER A 1 56  ? 2.584   6.969   4.462   1.00 11.74  ? 56  SER A CB  1 
ATOM   448  O  OG  . SER A 1 56  ? 1.739   6.668   3.353   1.00 12.10  ? 56  SER A OG  1 
ATOM   449  N  N   . LEU A 1 57  ? 4.637   9.128   3.183   1.00 12.18  ? 57  LEU A N   1 
ATOM   450  C  CA  . LEU A 1 57  ? 5.270   9.759   2.032   1.00 12.87  ? 57  LEU A CA  1 
ATOM   451  C  C   . LEU A 1 57  ? 6.015   8.755   1.159   1.00 11.71  ? 57  LEU A C   1 
ATOM   452  O  O   . LEU A 1 57  ? 5.896   8.752   -0.091  1.00 12.67  ? 57  LEU A O   1 
ATOM   453  C  CB  . LEU A 1 57  ? 6.168   10.888  2.500   1.00 17.28  ? 57  LEU A CB  1 
ATOM   454  C  CG  . LEU A 1 57  ? 5.388   12.102  3.066   1.00 21.18  ? 57  LEU A CG  1 
ATOM   455  C  CD1 . LEU A 1 57  ? 6.368   13.179  3.584   1.00 29.92  ? 57  LEU A CD1 1 
ATOM   456  C  CD2 . LEU A 1 57  ? 4.377   12.726  2.065   1.00 29.24  ? 57  LEU A CD2 1 
ATOM   457  N  N   . ARG A 1 58  ? 6.894   7.971   1.749   1.00 11.46  ? 58  ARG A N   1 
ATOM   458  C  CA  . ARG A 1 58  ? 7.953   7.334   1.031   1.00 11.65  ? 58  ARG A CA  1 
ATOM   459  C  C   . ARG A 1 58  ? 8.415   6.119   1.803   1.00 10.24  ? 58  ARG A C   1 
ATOM   460  O  O   . ARG A 1 58  ? 8.357   6.105   3.026   1.00 11.21  ? 58  ARG A O   1 
ATOM   461  C  CB  . ARG A 1 58  ? 9.134   8.327   0.899   1.00 17.93  ? 58  ARG A CB  1 
ATOM   462  C  CG  . ARG A 1 58  ? 10.165  7.950   -0.097  1.00 19.77  ? 58  ARG A CG  1 
ATOM   463  C  CD  . ARG A 1 58  ? 11.119  9.153   -0.184  1.00 22.44  ? 58  ARG A CD  1 
ATOM   464  N  NE  . ARG A 1 58  ? 11.949  9.255   0.999   1.00 17.40  ? 58  ARG A NE  1 
ATOM   465  C  CZ  . ARG A 1 58  ? 13.267  9.371   1.032   1.00 16.79  ? 58  ARG A CZ  1 
ATOM   466  N  NH1 . ARG A 1 58  ? 13.945  9.628   -0.061  1.00 17.23  ? 58  ARG A NH1 1 
ATOM   467  N  NH2 . ARG A 1 58  ? 13.910  9.338   2.173   1.00 14.35  ? 58  ARG A NH2 1 
ATOM   468  N  N   . ILE A 1 59  ? 8.987   5.148   1.100   1.00 9.75   ? 59  ILE A N   1 
ATOM   469  C  CA  . ILE A 1 59  ? 9.649   4.008   1.721   1.00 9.01   ? 59  ILE A CA  1 
ATOM   470  C  C   . ILE A 1 59  ? 11.099  4.007   1.216   1.00 9.41   ? 59  ILE A C   1 
ATOM   471  O  O   . ILE A 1 59  ? 11.378  4.290   0.038   1.00 11.25  ? 59  ILE A O   1 
ATOM   472  C  CB  . ILE A 1 59  ? 8.902   2.704   1.427   1.00 9.53   ? 59  ILE A CB  1 
ATOM   473  C  CG1 . ILE A 1 59  ? 9.422   1.560   2.306   1.00 10.22  ? 59  ILE A CG1 1 
ATOM   474  C  CG2 . ILE A 1 59  ? 8.870   2.351   -0.067  1.00 10.71  ? 59  ILE A CG2 1 
ATOM   475  C  CD1 . ILE A 1 59  ? 8.558   0.303   2.185   1.00 12.39  ? 59  ILE A CD1 1 
ATOM   476  N  N   . LEU A 1 60  ? 12.064  3.676   2.094   1.00 9.91   ? 60  LEU A N   1 
ATOM   477  C  CA  . LEU A 1 60  ? 13.480  3.861   1.798   1.00 9.44   ? 60  LEU A CA  1 
ATOM   478  C  C   . LEU A 1 60  ? 14.255  2.651   2.349   1.00 9.73   ? 60  LEU A C   1 
ATOM   479  O  O   . LEU A 1 60  ? 14.053  2.286   3.510   1.00 9.85   ? 60  LEU A O   1 
ATOM   480  C  CB  . LEU A 1 60  ? 14.019  5.149   2.498   1.00 11.33  ? 60  LEU A CB  1 
ATOM   481  C  CG  . LEU A 1 60  ? 15.509  5.362   2.408   1.00 13.62  ? 60  LEU A CG  1 
ATOM   482  C  CD1 . LEU A 1 60  ? 16.011  5.572   1.013   1.00 15.78  ? 60  LEU A CD1 1 
ATOM   483  C  CD2 . LEU A 1 60  ? 15.900  6.508   3.342   1.00 14.52  ? 60  LEU A CD2 1 
ATOM   484  N  N   . ASN A 1 61  ? 15.164  2.100   1.547   1.00 9.52   ? 61  ASN A N   1 
ATOM   485  C  CA  . ASN A 1 61  ? 16.149  1.151   2.042   1.00 9.45   ? 61  ASN A CA  1 
ATOM   486  C  C   . ASN A 1 61  ? 17.367  1.944   2.480   1.00 10.02  ? 61  ASN A C   1 
ATOM   487  O  O   . ASN A 1 61  ? 17.997  2.623   1.655   1.00 10.92  ? 61  ASN A O   1 
ATOM   488  C  CB  . ASN A 1 61  ? 16.521  0.189   0.888   1.00 10.52  ? 61  ASN A CB  1 
ATOM   489  C  CG  . ASN A 1 61  ? 17.566  -0.831  1.281   1.00 9.54   ? 61  ASN A CG  1 
ATOM   490  O  OD1 . ASN A 1 61  ? 18.428  -0.524  2.146   1.00 10.26  ? 61  ASN A OD1 1 
ATOM   491  N  ND2 . ASN A 1 61  ? 17.539  -2.009  0.665   1.00 11.03  ? 61  ASN A ND2 1 
ATOM   492  N  N   . THR A 1 62  ? 17.637  1.965   3.793   1.00 9.68   ? 62  THR A N   1 
ATOM   493  C  CA  . THR A 1 62  ? 18.692  2.815   4.293   1.00 10.42  ? 62  THR A CA  1 
ATOM   494  C  C   . THR A 1 62  ? 20.061  2.145   4.216   1.00 10.20  ? 62  THR A C   1 
ATOM   495  O  O   . THR A 1 62  ? 21.070  2.781   4.581   1.00 14.17  ? 62  THR A O   1 
ATOM   496  C  CB  . THR A 1 62  ? 18.452  3.131   5.777   1.00 10.86  ? 62  THR A CB  1 
ATOM   497  O  OG1 . THR A 1 62  ? 18.604  1.897   6.529   1.00 10.93  ? 62  THR A OG1 1 
ATOM   498  C  CG2 . THR A 1 62  ? 17.096  3.765   6.013   1.00 13.76  ? 62  THR A CG2 1 
ATOM   499  N  N   . GLY A 1 63  ? 20.140  0.871   3.825   1.00 10.18  ? 63  GLY A N   1 
ATOM   500  C  CA  . GLY A 1 63  ? 21.363  0.112   3.886   1.00 10.44  ? 63  GLY A CA  1 
ATOM   501  C  C   . GLY A 1 63  ? 21.431  -0.687  5.184   1.00 9.87   ? 63  GLY A C   1 
ATOM   502  O  O   . GLY A 1 63  ? 22.292  -1.569  5.299   1.00 11.33  ? 63  GLY A O   1 
ATOM   503  N  N   . TYR A 1 64  ? 20.527  -0.429  6.136   1.00 9.42   ? 64  TYR A N   1 
ATOM   504  C  CA  . TYR A 1 64  ? 20.534  -1.181  7.423   1.00 9.91   ? 64  TYR A CA  1 
ATOM   505  C  C   . TYR A 1 64  ? 19.165  -1.802  7.645   1.00 8.77   ? 64  TYR A C   1 
ATOM   506  O  O   . TYR A 1 64  ? 19.088  -2.818  8.343   1.00 15.14  ? 64  TYR A O   1 
ATOM   507  C  CB  . TYR A 1 64  ? 20.911  -0.247  8.575   1.00 12.03  ? 64  TYR A CB  1 
ATOM   508  C  CG  . TYR A 1 64  ? 22.289  0.368   8.465   1.00 16.81  ? 64  TYR A CG  1 
ATOM   509  C  CD1 . TYR A 1 64  ? 23.426  -0.339  8.825   1.00 20.92  ? 64  TYR A CD1 1 
ATOM   510  C  CD2 . TYR A 1 64  ? 22.468  1.661   7.998   1.00 20.65  ? 64  TYR A CD2 1 
ATOM   511  C  CE1 . TYR A 1 64  ? 24.694  0.217   8.727   1.00 25.01  ? 64  TYR A CE1 1 
ATOM   512  C  CE2 . TYR A 1 64  ? 23.728  2.232   7.894   1.00 29.75  ? 64  TYR A CE2 1 
ATOM   513  C  CZ  . TYR A 1 64  ? 24.852  1.510   8.259   1.00 35.24  ? 64  TYR A CZ  1 
ATOM   514  O  OH  . TYR A 1 64  ? 26.102  2.067   8.159   1.00 42.60  ? 64  TYR A OH  1 
ATOM   515  N  N   . LEU A 1 65  ? 18.094  -1.206  7.123   1.00 8.28   ? 65  LEU A N   1 
ATOM   516  C  CA  . LEU A 1 65  ? 16.726  -1.614  7.347   1.00 8.85   ? 65  LEU A CA  1 
ATOM   517  C  C   . LEU A 1 65  ? 15.943  -0.918  6.246   1.00 8.42   ? 65  LEU A C   1 
ATOM   518  O  O   . LEU A 1 65  ? 16.530  -0.288  5.362   1.00 8.59   ? 65  LEU A O   1 
ATOM   519  C  CB  . LEU A 1 65  ? 16.258  -1.343  8.781   1.00 10.72  ? 65  LEU A CB  1 
ATOM   520  C  CG  . LEU A 1 65  ? 16.504  0.057   9.330   1.00 12.38  ? 65  LEU A CG  1 
ATOM   521  C  CD1 . LEU A 1 65  ? 15.747  1.145   8.538   1.00 14.16  ? 65  LEU A CD1 1 
ATOM   522  C  CD2 . LEU A 1 65  ? 16.143  0.077   10.806  1.00 17.27  ? 65  LEU A CD2 1 
ATOM   523  N  N   . PHE A 1 66  ? 14.627  -1.048  6.256   1.00 8.32   ? 66  PHE A N   1 
ATOM   524  C  CA  . PHE A 1 66  ? 13.768  -0.158  5.473   1.00 8.91   ? 66  PHE A CA  1 
ATOM   525  C  C   . PHE A 1 66  ? 12.827  0.593   6.400   1.00 8.46   ? 66  PHE A C   1 
ATOM   526  O  O   . PHE A 1 66  ? 12.516  0.143   7.514   1.00 8.92   ? 66  PHE A O   1 
ATOM   527  C  CB  . PHE A 1 66  ? 13.006  -0.916  4.353   1.00 10.16  ? 66  PHE A CB  1 
ATOM   528  C  CG  . PHE A 1 66  ? 11.889  -1.751  4.891   1.00 9.24   ? 66  PHE A CG  1 
ATOM   529  C  CD1 . PHE A 1 66  ? 10.609  -1.187  4.998   1.00 10.83  ? 66  PHE A CD1 1 
ATOM   530  C  CD2 . PHE A 1 66  ? 12.049  -3.079  5.210   1.00 10.29  ? 66  PHE A CD2 1 
ATOM   531  C  CE1 . PHE A 1 66  ? 9.553   -1.967  5.463   1.00 10.59  ? 66  PHE A CE1 1 
ATOM   532  C  CE2 . PHE A 1 66  ? 10.971  -3.841  5.645   1.00 9.39   ? 66  PHE A CE2 1 
ATOM   533  C  CZ  . PHE A 1 66  ? 9.715   -3.285  5.773   1.00 10.72  ? 66  PHE A CZ  1 
ATOM   534  N  N   . GLN A 1 67  ? 12.430  1.779   5.950   1.00 9.78   ? 67  GLN A N   1 
ATOM   535  C  CA  . GLN A 1 67  ? 11.589  2.641   6.779   1.00 9.59   ? 67  GLN A CA  1 
ATOM   536  C  C   . GLN A 1 67  ? 10.552  3.285   5.883   1.00 8.45   ? 67  GLN A C   1 
ATOM   537  O  O   . GLN A 1 67  ? 10.806  3.602   4.709   1.00 10.52  ? 67  GLN A O   1 
ATOM   538  C  CB  . GLN A 1 67  ? 12.427  3.704   7.471   1.00 11.28  ? 67  GLN A CB  1 
ATOM   539  C  CG  . GLN A 1 67  ? 13.104  4.641   6.506   1.00 12.14  ? 67  GLN A CG  1 
ATOM   540  C  CD  . GLN A 1 67  ? 14.119  5.505   7.202   1.00 16.84  ? 67  GLN A CD  1 
ATOM   541  O  OE1 . GLN A 1 67  ? 14.800  5.051   8.142   1.00 18.57  ? 67  GLN A OE1 1 
ATOM   542  N  NE2 . GLN A 1 67  ? 14.234  6.737   6.756   1.00 22.25  ? 67  GLN A NE2 1 
ATOM   543  N  N   . VAL A 1 68  ? 9.399   3.540   6.469   1.00 8.61   ? 68  VAL A N   1 
ATOM   544  C  CA  . VAL A 1 68  ? 8.336   4.315   5.868   1.00 9.08   ? 68  VAL A CA  1 
ATOM   545  C  C   . VAL A 1 68  ? 8.277   5.659   6.602   1.00 8.90   ? 68  VAL A C   1 
ATOM   546  O  O   . VAL A 1 68  ? 8.153   5.679   7.840   1.00 9.48   ? 68  VAL A O   1 
ATOM   547  C  CB  . VAL A 1 68  ? 6.987   3.566   5.942   1.00 9.38   ? 68  VAL A CB  1 
ATOM   548  C  CG1 . VAL A 1 68  ? 5.820   4.478   5.535   1.00 11.70  ? 68  VAL A CG1 1 
ATOM   549  C  CG2 . VAL A 1 68  ? 7.066   2.302   5.114   1.00 10.43  ? 68  VAL A CG2 1 
ATOM   550  N  N   . GLU A 1 69  ? 8.348   6.741   5.836   1.00 10.45  ? 69  GLU A N   1 
ATOM   551  C  CA  . GLU A 1 69  ? 8.387   8.062   6.411   1.00 9.77   ? 69  GLU A CA  1 
ATOM   552  C  C   . GLU A 1 69  ? 7.047   8.763   6.253   1.00 10.71  ? 69  GLU A C   1 
ATOM   553  O  O   . GLU A 1 69  ? 6.345   8.535   5.245   1.00 12.72  ? 69  GLU A O   1 
ATOM   554  C  CB  . GLU A 1 69  ? 9.435   8.886   5.722   1.00 12.83  ? 69  GLU A CB  1 
ATOM   555  C  CG  . GLU A 1 69  ? 10.786  8.250   5.809   1.00 16.40  ? 69  GLU A CG  1 
ATOM   556  C  CD  . GLU A 1 69  ? 11.659  8.717   4.684   1.00 16.01  ? 69  GLU A CD  1 
ATOM   557  O  OE1 . GLU A 1 69  ? 11.193  9.473   3.767   1.00 20.25  ? 69  GLU A OE1 1 
ATOM   558  O  OE2 . GLU A 1 69  ? 12.838  8.327   4.708   1.00 15.96  ? 69  GLU A OE2 1 
ATOM   559  N  N   . PHE A 1 70  ? 6.718   9.638   7.215   1.00 9.81   ? 70  PHE A N   1 
ATOM   560  C  CA  . PHE A 1 70  ? 5.444   10.352  7.247   1.00 10.43  ? 70  PHE A CA  1 
ATOM   561  C  C   . PHE A 1 70  ? 5.713   11.849  7.171   1.00 11.19  ? 70  PHE A C   1 
ATOM   562  O  O   . PHE A 1 70  ? 6.763   12.335  7.607   1.00 12.91  ? 70  PHE A O   1 
ATOM   563  C  CB  . PHE A 1 70  ? 4.719   10.021  8.556   1.00 10.76  ? 70  PHE A CB  1 
ATOM   564  C  CG  . PHE A 1 70  ? 4.190   8.634   8.545   1.00 9.96   ? 70  PHE A CG  1 
ATOM   565  C  CD1 . PHE A 1 70  ? 5.019   7.530   8.789   1.00 11.35  ? 70  PHE A CD1 1 
ATOM   566  C  CD2 . PHE A 1 70  ? 2.853   8.388   8.209   1.00 10.31  ? 70  PHE A CD2 1 
ATOM   567  C  CE1 . PHE A 1 70  ? 4.536   6.236   8.706   1.00 11.74  ? 70  PHE A CE1 1 
ATOM   568  C  CE2 . PHE A 1 70  ? 2.401   7.075   8.113   1.00 11.58  ? 70  PHE A CE2 1 
ATOM   569  C  CZ  . PHE A 1 70  ? 3.241   6.008   8.365   1.00 11.45  ? 70  PHE A CZ  1 
ATOM   570  N  N   . ASP A 1 71  ? 4.693   12.587  6.746   1.00 13.57  ? 71  ASP A N   1 
ATOM   571  C  CA  . ASP A 1 71  ? 4.717   14.025  6.864   1.00 14.15  ? 71  ASP A CA  1 
ATOM   572  C  C   . ASP A 1 71  ? 4.459   14.376  8.323   1.00 14.73  ? 71  ASP A C   1 
ATOM   573  O  O   . ASP A 1 71  ? 3.337   14.205  8.835   1.00 21.97  ? 71  ASP A O   1 
ATOM   574  C  CB  . ASP A 1 71  ? 3.559   14.657  6.063   1.00 20.67  ? 71  ASP A CB  1 
ATOM   575  C  CG  . ASP A 1 71  ? 3.423   16.197  6.205   1.00 24.46  ? 71  ASP A CG  1 
ATOM   576  O  OD1 . ASP A 1 71  ? 4.337   16.878  6.688   1.00 22.16  ? 71  ASP A OD1 1 
ATOM   577  O  OD2 . ASP A 1 71  ? 2.361   16.680  5.849   1.00 24.27  ? 71  ASP A OD2 1 
ATOM   578  N  N   . ASP A 1 72  ? 5.464   14.891  8.981   1.00 14.24  ? 72  ASP A N   1 
ATOM   579  C  CA  . ASP A 1 72  ? 5.375   15.313  10.370  1.00 17.03  ? 72  ASP A CA  1 
ATOM   580  C  C   . ASP A 1 72  ? 5.490   16.841  10.466  1.00 23.04  ? 72  ASP A C   1 
ATOM   581  O  O   . ASP A 1 72  ? 5.986   17.374  11.456  1.00 22.40  ? 72  ASP A O   1 
ATOM   582  C  CB  . ASP A 1 72  ? 6.496   14.637  11.188  1.00 16.90  ? 72  ASP A CB  1 
ATOM   583  C  CG  . ASP A 1 72  ? 7.872   15.124  10.798  1.00 17.07  ? 72  ASP A CG  1 
ATOM   584  O  OD1 . ASP A 1 72  ? 8.001   15.661  9.643   1.00 18.67  ? 72  ASP A OD1 1 
ATOM   585  O  OD2 . ASP A 1 72  ? 8.794   14.940  11.580  1.00 22.77  ? 72  ASP A OD2 1 
ATOM   586  N  N   . SER A 1 73  ? 5.056   17.535  9.421   1.00 19.00  ? 73  SER A N   1 
ATOM   587  C  CA  . SER A 1 73  ? 5.161   19.007  9.481   1.00 18.68  ? 73  SER A CA  1 
ATOM   588  C  C   . SER A 1 73  ? 3.848   19.572  10.022  1.00 23.33  ? 73  SER A C   1 
ATOM   589  O  O   . SER A 1 73  ? 3.731   20.790  10.160  1.00 20.39  ? 73  SER A O   1 
ATOM   590  C  CB  . SER A 1 73  ? 5.483   19.493  8.113   1.00 23.99  ? 73  SER A CB  1 
ATOM   591  O  OG  . SER A 1 73  ? 4.287   19.473  7.334   1.00 21.38  ? 73  SER A OG  1 
ATOM   592  N  N   . GLN A 1 74  ? 2.866   18.741  10.394  1.00 22.63  ? 74  GLN A N   1 
ATOM   593  C  CA  . GLN A 1 74  ? 1.698   19.232  11.122  1.00 25.90  ? 74  GLN A CA  1 
ATOM   594  C  C   . GLN A 1 74  ? 1.269   18.179  12.128  1.00 21.85  ? 74  GLN A C   1 
ATOM   595  O  O   . GLN A 1 74  ? 1.804   17.101  12.076  1.00 18.31  ? 74  GLN A O   1 
ATOM   596  C  CB  . GLN A 1 74  ? 0.488   19.325  10.188  1.00 32.65  ? 74  GLN A CB  1 
ATOM   597  C  CG  . GLN A 1 74  ? 0.645   20.460  9.208   1.00 39.62  ? 74  GLN A CG  1 
ATOM   598  C  CD  . GLN A 1 74  ? -0.697  20.694  8.579   1.00 42.10  ? 74  GLN A CD  1 
ATOM   599  O  OE1 . GLN A 1 74  ? -1.565  21.335  9.173   1.00 45.97  ? 74  GLN A OE1 1 
ATOM   600  N  NE2 . GLN A 1 74  ? -0.878  20.122  7.401   1.00 39.03  ? 74  GLN A NE2 1 
ATOM   601  N  N   A ASP A 1 75  ? 0.337   18.386  13.086  0.50 30.73  ? 75  ASP A N   1 
ATOM   602  N  N   B ASP A 1 75  ? 0.317   18.636  12.956  0.50 23.01  ? 75  ASP A N   1 
ATOM   603  C  CA  A ASP A 1 75  ? 0.048   17.263  13.994  0.50 29.27  ? 75  ASP A CA  1 
ATOM   604  C  CA  B ASP A 1 75  ? -0.191  17.970  14.131  0.50 20.35  ? 75  ASP A CA  1 
ATOM   605  C  C   A ASP A 1 75  ? -0.988  16.319  13.353  0.50 32.15  ? 75  ASP A C   1 
ATOM   606  C  C   B ASP A 1 75  ? -1.164  16.908  13.642  0.50 22.67  ? 75  ASP A C   1 
ATOM   607  O  O   A ASP A 1 75  ? -2.190  16.483  13.517  0.50 40.42  ? 75  ASP A O   1 
ATOM   608  O  O   B ASP A 1 75  ? -2.362  17.149  13.618  0.50 25.26  ? 75  ASP A O   1 
ATOM   609  C  CB  A ASP A 1 75  ? -0.416  17.677  15.406  0.50 25.55  ? 75  ASP A CB  1 
ATOM   610  C  CB  B ASP A 1 75  ? -0.953  18.969  15.005  0.50 19.46  ? 75  ASP A CB  1 
ATOM   611  C  CG  A ASP A 1 75  ? 0.617   17.905  16.519  0.50 25.85  ? 75  ASP A CG  1 
ATOM   612  C  CG  B ASP A 1 75  ? -1.601  18.287  16.196  0.50 18.74  ? 75  ASP A CG  1 
ATOM   613  O  OD1 A ASP A 1 75  ? 1.322   16.914  16.969  0.50 24.33  ? 75  ASP A OD1 1 
ATOM   614  O  OD1 B ASP A 1 75  ? -1.222  17.145  16.454  0.50 20.01  ? 75  ASP A OD1 1 
ATOM   615  O  OD2 A ASP A 1 75  ? 0.619   19.041  17.022  0.50 36.30  ? 75  ASP A OD2 1 
ATOM   616  O  OD2 B ASP A 1 75  ? -2.496  18.921  16.828  0.50 27.00  ? 75  ASP A OD2 1 
ATOM   617  N  N   A LYS A 1 76  ? -0.528  15.278  12.652  0.50 25.07  ? 76  LYS A N   1 
ATOM   618  N  N   B LYS A 1 76  ? -0.636  15.792  13.144  0.50 19.11  ? 76  LYS A N   1 
ATOM   619  C  CA  A LYS A 1 76  ? -1.376  14.416  11.827  0.50 26.33  ? 76  LYS A CA  1 
ATOM   620  C  CA  B LYS A 1 76  ? -1.496  14.744  12.634  0.50 22.01  ? 76  LYS A CA  1 
ATOM   621  C  C   A LYS A 1 76  ? -1.573  13.029  12.451  0.50 21.28  ? 76  LYS A C   1 
ATOM   622  C  C   B LYS A 1 76  ? -1.530  13.531  13.565  0.50 26.71  ? 76  LYS A C   1 
ATOM   623  O  O   A LYS A 1 76  ? -2.578  12.357  12.221  0.50 28.18  ? 76  LYS A O   1 
ATOM   624  O  O   B LYS A 1 76  ? -2.361  13.411  14.474  0.50 27.34  ? 76  LYS A O   1 
ATOM   625  C  CB  A LYS A 1 76  ? -0.777  14.269  10.420  0.50 27.49  ? 76  LYS A CB  1 
ATOM   626  C  CB  B LYS A 1 76  ? -1.004  14.397  11.221  0.50 19.26  ? 76  LYS A CB  1 
ATOM   627  C  CG  A LYS A 1 76  ? -1.134  15.376  9.422   0.50 30.56  ? 76  LYS A CG  1 
ATOM   628  C  CG  B LYS A 1 76  ? -1.200  15.553  10.248  0.50 22.72  ? 76  LYS A CG  1 
ATOM   629  C  CD  A LYS A 1 76  ? -0.311  15.298  8.141   0.50 26.93  ? 76  LYS A CD  1 
ATOM   630  C  CD  B LYS A 1 76  ? -0.436  15.352  8.938   0.50 28.43  ? 76  LYS A CD  1 
ATOM   631  C  CE  A LYS A 1 76  ? -0.815  16.254  7.066   0.50 22.48  ? 76  LYS A CE  1 
ATOM   632  C  CE  B LYS A 1 76  ? -0.997  16.173  7.783   0.50 26.97  ? 76  LYS A CE  1 
ATOM   633  N  NZ  A LYS A 1 76  ? -0.356  15.817  5.721   0.50 25.31  ? 76  LYS A NZ  1 
ATOM   634  N  NZ  B LYS A 1 76  ? -0.219  15.957  6.529   0.50 36.28  ? 76  LYS A NZ  1 
ATOM   635  N  N   . ALA A 1 77  ? -0.611  12.627  13.269  1.00 22.30  ? 77  ALA A N   1 
ATOM   636  C  CA  . ALA A 1 77  ? -0.513  11.294  13.843  1.00 18.07  ? 77  ALA A CA  1 
ATOM   637  C  C   . ALA A 1 77  ? 0.341   11.406  15.097  1.00 16.07  ? 77  ALA A C   1 
ATOM   638  O  O   . ALA A 1 77  ? 1.558   11.697  15.020  1.00 22.90  ? 77  ALA A O   1 
ATOM   639  C  CB  . ALA A 1 77  ? 0.175   10.443  12.790  1.00 21.03  ? 77  ALA A CB  1 
ATOM   640  N  N   A VAL A 1 78  ? -0.248  11.148  16.242  0.50 14.18  ? 78  VAL A N   1 
ATOM   641  N  N   B VAL A 1 78  ? -0.305  11.270  16.265  0.50 14.18  ? 78  VAL A N   1 
ATOM   642  C  CA  A VAL A 1 78  ? 0.508   11.434  17.429  0.50 15.95  ? 78  VAL A CA  1 
ATOM   643  C  CA  B VAL A 1 78  ? 0.187   11.621  17.594  0.50 13.26  ? 78  VAL A CA  1 
ATOM   644  C  C   A VAL A 1 78  ? 0.218   10.341  18.431  0.50 15.90  ? 78  VAL A C   1 
ATOM   645  C  C   B VAL A 1 78  ? 0.131   10.407  18.519  0.50 14.11  ? 78  VAL A C   1 
ATOM   646  O  O   A VAL A 1 78  ? -0.858  9.702   18.435  0.50 17.81  ? 78  VAL A O   1 
ATOM   647  O  O   B VAL A 1 78  ? -0.905  9.701   18.583  0.50 14.88  ? 78  VAL A O   1 
ATOM   648  C  CB  A VAL A 1 78  ? 0.161   12.815  18.015  0.50 16.39  ? 78  VAL A CB  1 
ATOM   649  C  CB  B VAL A 1 78  ? -0.625  12.789  18.216  0.50 16.24  ? 78  VAL A CB  1 
ATOM   650  C  CG1 A VAL A 1 78  ? 0.406   13.946  17.012  0.50 19.49  ? 78  VAL A CG1 1 
ATOM   651  C  CG1 B VAL A 1 78  ? -0.357  12.998  19.719  0.50 17.21  ? 78  VAL A CG1 1 
ATOM   652  C  CG2 A VAL A 1 78  ? -1.301  12.768  18.408  0.50 17.93  ? 78  VAL A CG2 1 
ATOM   653  C  CG2 B VAL A 1 78  ? -0.446  14.105  17.464  0.50 19.15  ? 78  VAL A CG2 1 
ATOM   654  N  N   . LEU A 1 79  ? 1.204   10.223  19.308  1.00 11.59  ? 79  LEU A N   1 
ATOM   655  C  CA  . LEU A 1 79  ? 1.238   9.345   20.468  1.00 11.63  ? 79  LEU A CA  1 
ATOM   656  C  C   . LEU A 1 79  ? 1.261   10.200  21.698  1.00 12.44  ? 79  LEU A C   1 
ATOM   657  O  O   . LEU A 1 79  ? 2.104   11.088  21.786  1.00 13.07  ? 79  LEU A O   1 
ATOM   658  C  CB  . LEU A 1 79  ? 2.471   8.436   20.355  1.00 12.70  ? 79  LEU A CB  1 
ATOM   659  C  CG  . LEU A 1 79  ? 2.650   7.377   21.428  1.00 13.53  ? 79  LEU A CG  1 
ATOM   660  C  CD1 . LEU A 1 79  ? 1.539   6.349   21.371  1.00 15.94  ? 79  LEU A CD1 1 
ATOM   661  C  CD2 . LEU A 1 79  ? 3.985   6.694   21.242  1.00 14.23  ? 79  LEU A CD2 1 
ATOM   662  N  N   . LYS A 1 80  ? 0.397   9.866   22.663  1.00 13.23  ? 80  LYS A N   1 
ATOM   663  C  CA  . LYS A 1 80  ? 0.455   10.556  23.934  1.00 14.94  ? 80  LYS A CA  1 
ATOM   664  C  C   . LYS A 1 80  ? -0.070  9.620   25.009  1.00 12.99  ? 80  LYS A C   1 
ATOM   665  O  O   . LYS A 1 80  ? -0.469  8.499   24.697  1.00 13.87  ? 80  LYS A O   1 
ATOM   666  C  CB  . LYS A 1 80  ? -0.275  11.901  23.922  1.00 18.33  ? 80  LYS A CB  1 
ATOM   667  C  CG  . LYS A 1 80  ? -1.740  11.741  23.661  1.00 18.70  ? 80  LYS A CG  1 
ATOM   668  C  CD  . LYS A 1 80  ? -2.388  13.130  23.720  1.00 25.64  ? 80  LYS A CD  1 
ATOM   669  C  CE  . LYS A 1 80  ? -1.842  14.164  22.778  1.00 32.59  ? 80  LYS A CE  1 
ATOM   670  N  N   . GLY A 1 81  ? -0.127  10.115  26.242  1.00 15.55  ? 81  GLY A N   1 
ATOM   671  C  CA  . GLY A 1 81  ? -0.578  9.333   27.348  1.00 16.34  ? 81  GLY A CA  1 
ATOM   672  C  C   . GLY A 1 81  ? 0.417   8.271   27.735  1.00 15.51  ? 81  GLY A C   1 
ATOM   673  O  O   . GLY A 1 81  ? 1.626   8.387   27.504  1.00 15.43  ? 81  GLY A O   1 
ATOM   674  N  N   . GLY A 1 82  ? -0.030  7.277   28.472  1.00 18.14  ? 82  GLY A N   1 
ATOM   675  C  CA  . GLY A 1 82  ? 0.907   6.321   29.021  1.00 18.10  ? 82  GLY A CA  1 
ATOM   676  C  C   . GLY A 1 82  ? 1.886   6.976   29.962  1.00 17.69  ? 82  GLY A C   1 
ATOM   677  O  O   . GLY A 1 82  ? 1.551   7.782   30.831  1.00 19.31  ? 82  GLY A O   1 
ATOM   678  N  N   . PRO A 1 83  ? 3.186   6.690   29.723  1.00 16.07  ? 83  PRO A N   1 
ATOM   679  C  CA  . PRO A 1 83  ? 4.218   7.283   30.555  1.00 17.73  ? 83  PRO A CA  1 
ATOM   680  C  C   . PRO A 1 83  ? 4.596   8.680   30.101  1.00 14.00  ? 83  PRO A C   1 
ATOM   681  O  O   . PRO A 1 83  ? 5.413   9.299   30.774  1.00 18.33  ? 83  PRO A O   1 
ATOM   682  C  CB  . PRO A 1 83  ? 5.373   6.312   30.327  1.00 15.74  ? 83  PRO A CB  1 
ATOM   683  C  CG  . PRO A 1 83  ? 5.235   5.908   28.845  1.00 15.22  ? 83  PRO A CG  1 
ATOM   684  C  CD  . PRO A 1 83  ? 3.734   5.772   28.668  1.00 16.07  ? 83  PRO A CD  1 
ATOM   685  N  N   . LEU A 1 84  ? 4.034   9.109   28.961  1.00 13.90  ? 84  LEU A N   1 
ATOM   686  C  CA  . LEU A 1 84  ? 4.542   10.281  28.272  1.00 14.64  ? 84  LEU A CA  1 
ATOM   687  C  C   . LEU A 1 84  ? 3.937   11.572  28.840  1.00 14.01  ? 84  LEU A C   1 
ATOM   688  O  O   . LEU A 1 84  ? 2.751   11.624  29.133  1.00 16.31  ? 84  LEU A O   1 
ATOM   689  C  CB  . LEU A 1 84  ? 4.225   10.200  26.766  1.00 13.07  ? 84  LEU A CB  1 
ATOM   690  C  CG  . LEU A 1 84  ? 4.738   8.916   26.101  1.00 12.25  ? 84  LEU A CG  1 
ATOM   691  C  CD1 . LEU A 1 84  ? 4.213   8.891   24.670  1.00 13.84  ? 84  LEU A CD1 1 
ATOM   692  C  CD2 . LEU A 1 84  ? 6.281   8.910   26.138  1.00 12.63  ? 84  LEU A CD2 1 
ATOM   693  N  N   . ASP A 1 85  ? 4.793   12.598  28.923  1.00 16.44  ? 85  ASP A N   1 
ATOM   694  C  CA  . ASP A 1 85  ? 4.351   13.963  29.200  1.00 16.11  ? 85  ASP A CA  1 
ATOM   695  C  C   . ASP A 1 85  ? 4.264   14.618  27.826  1.00 16.28  ? 85  ASP A C   1 
ATOM   696  O  O   . ASP A 1 85  ? 5.225   14.578  27.041  1.00 18.72  ? 85  ASP A O   1 
ATOM   697  C  CB  . ASP A 1 85  ? 5.316   14.651  30.184  1.00 18.01  ? 85  ASP A CB  1 
ATOM   698  C  CG  . ASP A 1 85  ? 5.159   14.144  31.616  1.00 20.43  ? 85  ASP A CG  1 
ATOM   699  O  OD1 . ASP A 1 85  ? 3.987   13.967  32.114  1.00 31.12  ? 85  ASP A OD1 1 
ATOM   700  O  OD2 . ASP A 1 85  ? 6.188   13.910  32.284  1.00 23.18  ? 85  ASP A OD2 1 
ATOM   701  N  N   . GLY A 1 86  ? 3.170   15.323  27.528  1.00 20.50  ? 86  GLY A N   1 
ATOM   702  C  CA  . GLY A 1 86  ? 3.095   16.041  26.252  1.00 18.75  ? 86  GLY A CA  1 
ATOM   703  C  C   . GLY A 1 86  ? 2.725   15.144  25.055  1.00 18.47  ? 86  GLY A C   1 
ATOM   704  O  O   . GLY A 1 86  ? 2.090   14.119  25.200  1.00 23.79  ? 86  GLY A O   1 
ATOM   705  N  N   A THR A 1 87  ? 3.151   15.539  23.841  0.50 18.85  ? 87  THR A N   1 
ATOM   706  N  N   B THR A 1 87  ? 3.076   15.574  23.850  0.50 16.35  ? 87  THR A N   1 
ATOM   707  C  CA  A THR A 1 87  ? 2.642   15.043  22.565  0.50 21.30  ? 87  THR A CA  1 
ATOM   708  C  CA  B THR A 1 87  ? 2.628   14.882  22.666  0.50 14.39  ? 87  THR A CA  1 
ATOM   709  C  C   A THR A 1 87  ? 3.796   14.665  21.633  0.50 15.71  ? 87  THR A C   1 
ATOM   710  C  C   B THR A 1 87  ? 3.838   14.584  21.794  0.50 11.78  ? 87  THR A C   1 
ATOM   711  O  O   A THR A 1 87  ? 4.698   15.462  21.347  0.50 16.31  ? 87  THR A O   1 
ATOM   712  O  O   B THR A 1 87  ? 4.807   15.363  21.697  0.50 12.48  ? 87  THR A O   1 
ATOM   713  C  CB  A THR A 1 87  ? 1.727   16.071  21.872  0.50 28.76  ? 87  THR A CB  1 
ATOM   714  C  CB  B THR A 1 87  ? 1.624   15.705  21.855  0.50 14.73  ? 87  THR A CB  1 
ATOM   715  O  OG1 A THR A 1 87  ? 0.565   16.255  22.680  0.50 36.10  ? 87  THR A OG1 1 
ATOM   716  O  OG1 B THR A 1 87  ? 2.195   16.988  21.618  0.50 14.69  ? 87  THR A OG1 1 
ATOM   717  C  CG2 A THR A 1 87  ? 1.284   15.686  20.472  0.50 23.48  ? 87  THR A CG2 1 
ATOM   718  C  CG2 B THR A 1 87  ? 0.373   16.023  22.631  0.50 17.63  ? 87  THR A CG2 1 
ATOM   719  N  N   . TYR A 1 88  ? 3.778   13.417  21.145  1.00 11.22  ? 88  TYR A N   1 
ATOM   720  C  CA  . TYR A 1 88  ? 4.887   12.948  20.328  1.00 10.82  ? 88  TYR A CA  1 
ATOM   721  C  C   . TYR A 1 88  ? 4.319   12.670  18.943  1.00 10.73  ? 88  TYR A C   1 
ATOM   722  O  O   . TYR A 1 88  ? 3.314   11.989  18.807  1.00 15.02  ? 88  TYR A O   1 
ATOM   723  C  CB  . TYR A 1 88  ? 5.507   11.701  20.911  1.00 10.34  ? 88  TYR A CB  1 
ATOM   724  C  CG  . TYR A 1 88  ? 6.313   11.885  22.169  1.00 9.60   ? 88  TYR A CG  1 
ATOM   725  C  CD1 . TYR A 1 88  ? 5.712   12.262  23.374  1.00 11.18  ? 88  TYR A CD1 1 
ATOM   726  C  CD2 . TYR A 1 88  ? 7.696   11.714  22.129  1.00 9.81   ? 88  TYR A CD2 1 
ATOM   727  C  CE1 . TYR A 1 88  ? 6.498   12.411  24.522  1.00 12.18  ? 88  TYR A CE1 1 
ATOM   728  C  CE2 . TYR A 1 88  ? 8.467   11.845  23.252  1.00 9.62   ? 88  TYR A CE2 1 
ATOM   729  C  CZ  . TYR A 1 88  ? 7.870   12.163  24.461  1.00 9.99   ? 88  TYR A CZ  1 
ATOM   730  O  OH  . TYR A 1 88  ? 8.626   12.241  25.625  1.00 11.02  ? 88  TYR A OH  1 
ATOM   731  N  N   . ARG A 1 89  ? 4.947   13.172  17.907  1.00 10.00  ? 89  ARG A N   1 
ATOM   732  C  CA  . ARG A 1 89  ? 4.495   13.116  16.537  1.00 9.95   ? 89  ARG A CA  1 
ATOM   733  C  C   . ARG A 1 89  ? 5.140   11.971  15.738  1.00 9.20   ? 89  ARG A C   1 
ATOM   734  O  O   . ARG A 1 89  ? 6.375   11.813  15.775  1.00 8.85   ? 89  ARG A O   1 
ATOM   735  C  CB  . ARG A 1 89  ? 4.770   14.439  15.877  1.00 12.44  ? 89  ARG A CB  1 
ATOM   736  C  CG  . ARG A 1 89  ? 4.102   14.604  14.524  1.00 15.97  ? 89  ARG A CG  1 
ATOM   737  C  CD  . ARG A 1 89  ? 4.304   16.010  13.967  1.00 18.02  ? 89  ARG A CD  1 
ATOM   738  N  NE  . ARG A 1 89  ? 3.676   17.026  14.810  1.00 19.05  ? 89  ARG A NE  1 
ATOM   739  C  CZ  . ARG A 1 89  ? 3.804   18.349  14.555  1.00 17.67  ? 89  ARG A CZ  1 
ATOM   740  N  NH1 . ARG A 1 89  ? 4.590   18.789  13.587  1.00 20.62  ? 89  ARG A NH1 1 
ATOM   741  N  NH2 . ARG A 1 89  ? 3.243   19.255  15.360  1.00 19.44  ? 89  ARG A NH2 1 
ATOM   742  N  N   . LEU A 1 90  ? 4.315   11.162  15.041  1.00 10.01  ? 90  LEU A N   1 
ATOM   743  C  CA  . LEU A 1 90  ? 4.871   10.062  14.271  1.00 9.59   ? 90  LEU A CA  1 
ATOM   744  C  C   . LEU A 1 90  ? 5.709   10.597  13.110  1.00 9.93   ? 90  LEU A C   1 
ATOM   745  O  O   . LEU A 1 90  ? 5.257   11.469  12.337  1.00 11.45  ? 90  LEU A O   1 
ATOM   746  C  CB  . LEU A 1 90  ? 3.715   9.251   13.703  1.00 10.61  ? 90  LEU A CB  1 
ATOM   747  C  CG  . LEU A 1 90  ? 4.147   8.077   12.801  1.00 11.48  ? 90  LEU A CG  1 
ATOM   748  C  CD1 . LEU A 1 90  ? 4.905   6.969   13.552  1.00 11.73  ? 90  LEU A CD1 1 
ATOM   749  C  CD2 . LEU A 1 90  ? 2.913   7.484   12.121  1.00 14.33  ? 90  LEU A CD2 1 
ATOM   750  N  N   . LYS A 1 91  ? 6.951   10.115  12.972  1.00 9.24   ? 91  LYS A N   1 
ATOM   751  C  CA  . LYS A 1 91  ? 7.847   10.473  11.875  1.00 9.59   ? 91  LYS A CA  1 
ATOM   752  C  C   . LYS A 1 91  ? 8.079   9.339   10.906  1.00 8.23   ? 91  LYS A C   1 
ATOM   753  O  O   . LYS A 1 91  ? 8.142   9.546   9.701   1.00 8.91   ? 91  LYS A O   1 
ATOM   754  C  CB  . LYS A 1 91  ? 9.199   10.958  12.440  1.00 12.47  ? 91  LYS A CB  1 
ATOM   755  C  CG  . LYS A 1 91  ? 10.274  11.228  11.407  1.00 18.40  ? 91  LYS A CG  1 
ATOM   756  C  CD  . LYS A 1 91  ? 11.109  12.350  11.782  1.00 27.23  ? 91  LYS A CD  1 
ATOM   757  C  CE  . LYS A 1 91  ? 11.662  12.989  10.493  1.00 29.32  ? 91  LYS A CE  1 
ATOM   758  N  NZ  . LYS A 1 91  ? 10.797  14.094  9.970   1.00 28.74  ? 91  LYS A NZ  1 
ATOM   759  N  N   . GLN A 1 92  ? 8.201   8.109   11.420  1.00 8.55   ? 92  GLN A N   1 
ATOM   760  C  CA  . GLN A 1 92  ? 8.614   7.001   10.597  1.00 8.46   ? 92  GLN A CA  1 
ATOM   761  C  C   . GLN A 1 92  ? 8.316   5.706   11.311  1.00 7.53   ? 92  GLN A C   1 
ATOM   762  O  O   . GLN A 1 92  ? 8.220   5.695   12.527  1.00 8.68   ? 92  GLN A O   1 
ATOM   763  C  CB  . GLN A 1 92  ? 10.072  7.035   10.155  1.00 13.06  ? 92  GLN A CB  1 
ATOM   764  C  CG  . GLN A 1 92  ? 11.161  7.088   11.186  1.00 15.42  ? 92  GLN A CG  1 
ATOM   765  C  CD  . GLN A 1 92  ? 11.800  5.687   11.110  1.00 16.20  ? 92  GLN A CD  1 
ATOM   766  O  OE1 . GLN A 1 92  ? 11.275  4.761   11.539  1.00 10.86  ? 92  GLN A OE1 1 
ATOM   767  N  NE2 . GLN A 1 92  ? 12.984  5.411   10.542  1.00 20.94  ? 92  GLN A NE2 1 
ATOM   768  N  N   . PHE A 1 93  ? 8.173   4.623   10.539  1.00 7.93   ? 93  PHE A N   1 
ATOM   769  C  CA  . PHE A 1 93  ? 8.297   3.316   11.148  1.00 7.10   ? 93  PHE A CA  1 
ATOM   770  C  C   . PHE A 1 93  ? 9.297   2.482   10.369  1.00 6.62   ? 93  PHE A C   1 
ATOM   771  O  O   . PHE A 1 93  ? 9.561   2.721   9.189   1.00 7.64   ? 93  PHE A O   1 
ATOM   772  C  CB  . PHE A 1 93  ? 6.957   2.577   11.302  1.00 7.58   ? 93  PHE A CB  1 
ATOM   773  C  CG  . PHE A 1 93  ? 6.273   2.148   10.038  1.00 7.35   ? 93  PHE A CG  1 
ATOM   774  C  CD1 . PHE A 1 93  ? 6.683   1.023   9.342   1.00 8.69   ? 93  PHE A CD1 1 
ATOM   775  C  CD2 . PHE A 1 93  ? 5.116   2.811   9.621   1.00 8.39   ? 93  PHE A CD2 1 
ATOM   776  C  CE1 . PHE A 1 93  ? 6.003   0.630   8.182   1.00 9.39   ? 93  PHE A CE1 1 
ATOM   777  C  CE2 . PHE A 1 93  ? 4.419   2.412   8.488   1.00 9.76   ? 93  PHE A CE2 1 
ATOM   778  C  CZ  . PHE A 1 93  ? 4.885   1.324   7.760   1.00 9.12   ? 93  PHE A CZ  1 
ATOM   779  N  N   . HIS A 1 94  ? 9.815   1.451   11.025  1.00 6.56   ? 94  HIS A N   1 
ATOM   780  C  CA  . HIS A 1 94  ? 10.773  0.566   10.403  1.00 6.33   ? 94  HIS A CA  1 
ATOM   781  C  C   . HIS A 1 94  ? 10.701  -0.765  11.102  1.00 6.53   ? 94  HIS A C   1 
ATOM   782  O  O   . HIS A 1 94  ? 10.039  -0.919  12.133  1.00 6.98   ? 94  HIS A O   1 
ATOM   783  C  CB  . HIS A 1 94  ? 12.173  1.176   10.462  1.00 6.99   ? 94  HIS A CB  1 
ATOM   784  C  CG  . HIS A 1 94  ? 12.674  1.384   11.823  1.00 6.87   ? 94  HIS A CG  1 
ATOM   785  N  ND1 . HIS A 1 94  ? 12.478  2.549   12.550  1.00 6.79   ? 94  HIS A ND1 1 
ATOM   786  C  CD2 . HIS A 1 94  ? 13.339  0.549   12.673  1.00 7.00   ? 94  HIS A CD2 1 
ATOM   787  C  CE1 . HIS A 1 94  ? 13.044  2.393   13.752  1.00 6.84   ? 94  HIS A CE1 1 
ATOM   788  N  NE2 . HIS A 1 94  ? 13.534  1.160   13.862  1.00 6.47   ? 94  HIS A NE2 1 
ATOM   789  N  N   . PHE A 1 95  ? 11.458  -1.745  10.573  1.00 7.11   ? 95  PHE A N   1 
ATOM   790  C  CA  . PHE A 1 95  ? 11.525  -3.080  11.149  1.00 6.95   ? 95  PHE A CA  1 
ATOM   791  C  C   . PHE A 1 95  ? 12.960  -3.529  11.328  1.00 6.76   ? 95  PHE A C   1 
ATOM   792  O  O   . PHE A 1 95  ? 13.867  -3.059  10.639  1.00 7.85   ? 95  PHE A O   1 
ATOM   793  C  CB  . PHE A 1 95  ? 10.837  -4.117  10.251  1.00 8.08   ? 95  PHE A CB  1 
ATOM   794  C  CG  . PHE A 1 95  ? 9.358   -3.862  9.999   1.00 7.19   ? 95  PHE A CG  1 
ATOM   795  C  CD1 . PHE A 1 95  ? 9.000   -2.946  9.014   1.00 9.00   ? 95  PHE A CD1 1 
ATOM   796  C  CD2 . PHE A 1 95  ? 8.368   -4.561  10.688  1.00 8.14   ? 95  PHE A CD2 1 
ATOM   797  C  CE1 . PHE A 1 95  ? 7.656   -2.738  8.727   1.00 9.31   ? 95  PHE A CE1 1 
ATOM   798  C  CE2 . PHE A 1 95  ? 7.024   -4.357  10.390  1.00 8.98   ? 95  PHE A CE2 1 
ATOM   799  C  CZ  . PHE A 1 95  ? 6.693   -3.438  9.409   1.00 10.21  ? 95  PHE A CZ  1 
ATOM   800  N  N   . HIS A 1 96  ? 13.139  -4.464  12.282  1.00 6.98   ? 96  HIS A N   1 
ATOM   801  C  CA  . HIS A 1 96  ? 14.340  -5.266  12.429  1.00 6.74   ? 96  HIS A CA  1 
ATOM   802  C  C   . HIS A 1 96  ? 13.889  -6.706  12.320  1.00 7.14   ? 96  HIS A C   1 
ATOM   803  O  O   . HIS A 1 96  ? 12.806  -7.049  12.784  1.00 7.81   ? 96  HIS A O   1 
ATOM   804  C  CB  . HIS A 1 96  ? 14.972  -5.055  13.828  1.00 7.00   ? 96  HIS A CB  1 
ATOM   805  C  CG  . HIS A 1 96  ? 15.270  -3.620  14.114  1.00 6.78   ? 96  HIS A CG  1 
ATOM   806  N  ND1 . HIS A 1 96  ? 16.481  -3.007  13.968  1.00 7.71   ? 96  HIS A ND1 1 
ATOM   807  C  CD2 . HIS A 1 96  ? 14.446  -2.642  14.573  1.00 6.42   ? 96  HIS A CD2 1 
ATOM   808  C  CE1 . HIS A 1 96  ? 16.401  -1.726  14.323  1.00 7.11   ? 96  HIS A CE1 1 
ATOM   809  N  NE2 . HIS A 1 96  ? 15.134  -1.473  14.677  1.00 6.76   ? 96  HIS A NE2 1 
ATOM   810  N  N   . TRP A 1 97  ? 14.699  -7.566  11.694  1.00 6.93   ? 97  TRP A N   1 
ATOM   811  C  CA  . TRP A 1 97  ? 14.284  -8.970  11.500  1.00 7.11   ? 97  TRP A CA  1 
ATOM   812  C  C   . TRP A 1 97  ? 15.474  -9.882  11.383  1.00 6.86   ? 97  TRP A C   1 
ATOM   813  O  O   . TRP A 1 97  ? 16.641  -9.459  11.319  1.00 7.49   ? 97  TRP A O   1 
ATOM   814  C  CB  . TRP A 1 97  ? 13.367  -9.070  10.262  1.00 7.77   ? 97  TRP A CB  1 
ATOM   815  C  CG  . TRP A 1 97  ? 14.048  -8.706  8.988   1.00 6.78   ? 97  TRP A CG  1 
ATOM   816  C  CD1 . TRP A 1 97  ? 14.748  -9.534  8.172   1.00 7.98   ? 97  TRP A CD1 1 
ATOM   817  C  CD2 . TRP A 1 97  ? 14.124  -7.400  8.425   1.00 7.45   ? 97  TRP A CD2 1 
ATOM   818  N  NE1 . TRP A 1 97  ? 15.219  -8.856  7.078   1.00 8.64   ? 97  TRP A NE1 1 
ATOM   819  C  CE2 . TRP A 1 97  ? 14.854  -7.530  7.213   1.00 8.25   ? 97  TRP A CE2 1 
ATOM   820  C  CE3 . TRP A 1 97  ? 13.637  -6.114  8.759   1.00 7.65   ? 97  TRP A CE3 1 
ATOM   821  C  CZ2 . TRP A 1 97  ? 15.081  -6.442  6.366   1.00 8.91   ? 97  TRP A CZ2 1 
ATOM   822  C  CZ3 . TRP A 1 97  ? 13.896  -5.044  7.941   1.00 8.81   ? 97  TRP A CZ3 1 
ATOM   823  C  CH2 . TRP A 1 97  ? 14.617  -5.212  6.753   1.00 8.82   ? 97  TRP A CH2 1 
ATOM   824  N  N   . GLY A 1 98  ? 15.166  -11.181 11.401  1.00 7.18   ? 98  GLY A N   1 
ATOM   825  C  CA  . GLY A 1 98  ? 16.183  -12.213 11.462  1.00 8.06   ? 98  GLY A CA  1 
ATOM   826  C  C   . GLY A 1 98  ? 16.408  -12.913 10.131  1.00 8.43   ? 98  GLY A C   1 
ATOM   827  O  O   . GLY A 1 98  ? 15.660  -12.751 9.161   1.00 9.45   ? 98  GLY A O   1 
ATOM   828  N  N   . SER A 1 99  ? 17.402  -13.798 10.153  1.00 9.20   ? 99  SER A N   1 
ATOM   829  C  CA  . SER A 1 99  ? 17.628  -14.723 9.041   1.00 10.17  ? 99  SER A CA  1 
ATOM   830  C  C   . SER A 1 99  ? 16.716  -15.946 9.167   1.00 9.63   ? 99  SER A C   1 
ATOM   831  O  O   . SER A 1 99  ? 16.643  -16.719 8.214   1.00 14.01  ? 99  SER A O   1 
ATOM   832  C  CB  . SER A 1 99  ? 19.094  -15.109 8.971   1.00 11.57  ? 99  SER A CB  1 
ATOM   833  O  OG  . SER A 1 99  ? 19.541  -15.592 10.230  1.00 12.15  ? 99  SER A OG  1 
ATOM   834  N  N   . LEU A 1 100 ? 16.165  -16.217 10.360  1.00 9.83   ? 100 LEU A N   1 
ATOM   835  C  CA  . LEU A 1 100 ? 15.392  -17.407 10.670  1.00 11.25  ? 100 LEU A CA  1 
ATOM   836  C  C   . LEU A 1 100 ? 14.213  -16.925 11.504  1.00 10.28  ? 100 LEU A C   1 
ATOM   837  O  O   . LEU A 1 100 ? 14.325  -15.922 12.216  1.00 10.52  ? 100 LEU A O   1 
ATOM   838  C  CB  . LEU A 1 100 ? 16.201  -18.315 11.614  1.00 14.68  ? 100 LEU A CB  1 
ATOM   839  C  CG  . LEU A 1 100 ? 17.546  -18.747 11.036  1.00 16.91  ? 100 LEU A CG  1 
ATOM   840  C  CD1 . LEU A 1 100 ? 18.479  -19.384 12.082  1.00 21.27  ? 100 LEU A CD1 1 
ATOM   841  C  CD2 . LEU A 1 100 ? 17.258  -19.768 9.930   1.00 21.07  ? 100 LEU A CD2 1 
ATOM   842  N  N   . ASP A 1 101 ? 13.128  -17.666 11.533  1.00 11.27  ? 101 ASP A N   1 
ATOM   843  C  CA  . ASP A 1 101 ? 11.923  -17.216 12.216  1.00 11.66  ? 101 ASP A CA  1 
ATOM   844  C  C   . ASP A 1 101 ? 12.138  -17.117 13.733  1.00 12.08  ? 101 ASP A C   1 
ATOM   845  O  O   . ASP A 1 101 ? 11.448  -16.384 14.386  1.00 15.15  ? 101 ASP A O   1 
ATOM   846  C  CB  . ASP A 1 101 ? 10.752  -18.150 11.958  1.00 13.58  ? 101 ASP A CB  1 
ATOM   847  C  CG  . ASP A 1 101 ? 10.240  -18.187 10.529  1.00 14.28  ? 101 ASP A CG  1 
ATOM   848  O  OD1 . ASP A 1 101 ? 10.622  -17.325 9.690   1.00 13.96  ? 101 ASP A OD1 1 
ATOM   849  O  OD2 . ASP A 1 101 ? 9.410   -19.080 10.270  1.00 18.24  ? 101 ASP A OD2 1 
ATOM   850  N  N   . GLY A 1 102 ? 13.152  -17.845 14.280  1.00 12.75  ? 102 GLY A N   1 
ATOM   851  C  CA  . GLY A 1 102 ? 13.439  -17.894 15.715  1.00 14.83  ? 102 GLY A CA  1 
ATOM   852  C  C   . GLY A 1 102 ? 14.272  -16.721 16.227  1.00 12.90  ? 102 GLY A C   1 
ATOM   853  O  O   . GLY A 1 102 ? 14.620  -16.701 17.411  1.00 13.66  ? 102 GLY A O   1 
ATOM   854  N  N   . GLN A 1 103 ? 14.547  -15.720 15.386  1.00 11.27  ? 103 GLN A N   1 
ATOM   855  C  CA  . GLN A 1 103 ? 15.299  -14.551 15.882  1.00 10.02  ? 103 GLN A CA  1 
ATOM   856  C  C   . GLN A 1 103 ? 14.933  -13.374 15.014  1.00 8.73   ? 103 GLN A C   1 
ATOM   857  O  O   . GLN A 1 103 ? 14.402  -13.557 13.914  1.00 9.57   ? 103 GLN A O   1 
ATOM   858  C  CB  . GLN A 1 103 ? 16.797  -14.801 15.871  1.00 10.75  ? 103 GLN A CB  1 
ATOM   859  C  CG  . GLN A 1 103 ? 17.352  -14.989 14.446  1.00 10.96  ? 103 GLN A CG  1 
ATOM   860  C  CD  . GLN A 1 103 ? 18.706  -15.615 14.496  1.00 13.67  ? 103 GLN A CD  1 
ATOM   861  O  OE1 . GLN A 1 103 ? 18.783  -16.633 15.143  1.00 21.72  ? 103 GLN A OE1 1 
ATOM   862  N  NE2 . GLN A 1 103 ? 19.680  -15.084 13.778  1.00 13.35  ? 103 GLN A NE2 1 
ATOM   863  N  N   . GLY A 1 104 ? 15.275  -12.175 15.476  1.00 7.87   ? 104 GLY A N   1 
ATOM   864  C  CA  . GLY A 1 104 ? 15.002  -10.989 14.675  1.00 8.50   ? 104 GLY A CA  1 
ATOM   865  C  C   . GLY A 1 104 ? 14.544  -9.807  15.528  1.00 7.61   ? 104 GLY A C   1 
ATOM   866  O  O   . GLY A 1 104 ? 14.792  -8.660  15.153  1.00 8.22   ? 104 GLY A O   1 
ATOM   867  N  N   . SER A 1 105 ? 13.865  -10.056 16.651  1.00 7.33   ? 105 SER A N   1 
ATOM   868  C  CA  . SER A 1 105 ? 13.470  -8.959  17.506  1.00 6.79   ? 105 SER A CA  1 
ATOM   869  C  C   . SER A 1 105 ? 14.680  -8.394  18.258  1.00 6.36   ? 105 SER A C   1 
ATOM   870  O  O   . SER A 1 105 ? 15.683  -9.070  18.430  1.00 7.73   ? 105 SER A O   1 
ATOM   871  C  CB  . SER A 1 105 ? 12.346  -9.300  18.438  1.00 7.27   ? 105 SER A CB  1 
ATOM   872  O  OG  . SER A 1 105 ? 12.702  -10.300 19.396  1.00 7.35   ? 105 SER A OG  1 
ATOM   873  N  N   . GLU A 1 106 ? 14.535  -7.146  18.660  1.00 6.46   ? 106 GLU A N   1 
ATOM   874  C  CA  . GLU A 1 106 ? 15.556  -6.465  19.455  1.00 6.61   ? 106 GLU A CA  1 
ATOM   875  C  C   . GLU A 1 106 ? 15.235  -6.667  20.948  1.00 5.97   ? 106 GLU A C   1 
ATOM   876  O  O   . GLU A 1 106 ? 16.014  -7.243  21.689  1.00 7.00   ? 106 GLU A O   1 
ATOM   877  C  CB  . GLU A 1 106 ? 15.591  -4.980  19.089  1.00 7.07   ? 106 GLU A CB  1 
ATOM   878  C  CG  . GLU A 1 106 ? 15.941  -4.801  17.627  1.00 7.43   ? 106 GLU A CG  1 
ATOM   879  C  CD  . GLU A 1 106 ? 16.682  -3.526  17.385  1.00 6.58   ? 106 GLU A CD  1 
ATOM   880  O  OE1 . GLU A 1 106 ? 16.104  -2.457  17.561  1.00 7.16   ? 106 GLU A OE1 1 
ATOM   881  O  OE2 . GLU A 1 106 ? 17.857  -3.627  16.988  1.00 8.22   ? 106 GLU A OE2 1 
ATOM   882  N  N   . HIS A 1 107 ? 14.037  -6.223  21.374  1.00 6.25   ? 107 HIS A N   1 
ATOM   883  C  CA  . HIS A 1 107 ? 13.586  -6.626  22.704  1.00 6.47   ? 107 HIS A CA  1 
ATOM   884  C  C   . HIS A 1 107 ? 13.298  -8.128  22.715  1.00 6.39   ? 107 HIS A C   1 
ATOM   885  O  O   . HIS A 1 107 ? 12.963  -8.720  21.677  1.00 7.29   ? 107 HIS A O   1 
ATOM   886  C  CB  . HIS A 1 107 ? 12.345  -5.827  23.108  1.00 6.63   ? 107 HIS A CB  1 
ATOM   887  C  CG  . HIS A 1 107 ? 12.666  -4.387  23.271  1.00 6.02   ? 107 HIS A CG  1 
ATOM   888  N  ND1 . HIS A 1 107 ? 12.613  -3.483  22.238  1.00 6.43   ? 107 HIS A ND1 1 
ATOM   889  C  CD2 . HIS A 1 107 ? 13.134  -3.705  24.338  1.00 6.25   ? 107 HIS A CD2 1 
ATOM   890  C  CE1 . HIS A 1 107 ? 13.052  -2.302  22.686  1.00 6.62   ? 107 HIS A CE1 1 
ATOM   891  N  NE2 . HIS A 1 107 ? 13.371  -2.396  23.957  1.00 6.64   ? 107 HIS A NE2 1 
ATOM   892  N  N   . THR A 1 108 ? 13.412  -8.712  23.908  1.00 7.52   ? 108 THR A N   1 
ATOM   893  C  CA  . THR A 1 108 ? 13.013  -10.098 24.168  1.00 7.91   ? 108 THR A CA  1 
ATOM   894  C  C   . THR A 1 108 ? 12.071  -10.091 25.369  1.00 7.47   ? 108 THR A C   1 
ATOM   895  O  O   . THR A 1 108 ? 12.060  -9.137  26.139  1.00 8.12   ? 108 THR A O   1 
ATOM   896  C  CB  . THR A 1 108 ? 14.224  -11.016 24.332  1.00 8.10   ? 108 THR A CB  1 
ATOM   897  O  OG1 . THR A 1 108 ? 15.041  -10.531 25.393  1.00 8.72   ? 108 THR A OG1 1 
ATOM   898  C  CG2 . THR A 1 108 ? 15.048  -11.093 23.055  1.00 9.37   ? 108 THR A CG2 1 
ATOM   899  N  N   . VAL A 1 109 ? 11.301  -11.164 25.482  1.00 8.51   ? 109 VAL A N   1 
ATOM   900  C  CA  . VAL A 1 109 ? 10.330  -11.263 26.590  1.00 9.73   ? 109 VAL A CA  1 
ATOM   901  C  C   . VAL A 1 109 ? 10.662  -12.541 27.327  1.00 10.09  ? 109 VAL A C   1 
ATOM   902  O  O   . VAL A 1 109 ? 10.445  -13.623 26.781  1.00 10.68  ? 109 VAL A O   1 
ATOM   903  C  CB  . VAL A 1 109 ? 8.894   -11.220 26.046  1.00 9.75   ? 109 VAL A CB  1 
ATOM   904  C  CG1 . VAL A 1 109 ? 7.891   -11.373 27.165  1.00 12.06  ? 109 VAL A CG1 1 
ATOM   905  C  CG2 . VAL A 1 109 ? 8.622   -9.974  25.247  1.00 11.77  ? 109 VAL A CG2 1 
ATOM   906  N  N   . ASP A 1 110 ? 11.147  -12.443 28.570  1.00 9.99   ? 110 ASP A N   1 
ATOM   907  C  CA  . ASP A 1 110 ? 11.607  -13.634 29.292  1.00 11.77  ? 110 ASP A CA  1 
ATOM   908  C  C   . ASP A 1 110 ? 12.521  -14.443 28.365  1.00 10.85  ? 110 ASP A C   1 
ATOM   909  O  O   . ASP A 1 110 ? 12.428  -15.671 28.321  1.00 11.97  ? 110 ASP A O   1 
ATOM   910  C  CB  . ASP A 1 110 ? 10.430  -14.454 29.831  1.00 15.26  ? 110 ASP A CB  1 
ATOM   911  C  CG  . ASP A 1 110 ? 9.605   -13.604 30.807  1.00 14.46  ? 110 ASP A CG  1 
ATOM   912  O  OD1 . ASP A 1 110 ? 10.190  -12.799 31.529  1.00 16.32  ? 110 ASP A OD1 1 
ATOM   913  O  OD2 . ASP A 1 110 ? 8.353   -13.897 30.846  1.00 19.09  ? 110 ASP A OD2 1 
ATOM   914  N  N   . LYS A 1 111 ? 13.438  -13.749 27.640  1.00 9.98   ? 111 LYS A N   1 
ATOM   915  C  CA  . LYS A 1 111 ? 14.450  -14.279 26.770  1.00 10.38  ? 111 LYS A CA  1 
ATOM   916  C  C   . LYS A 1 111 ? 13.879  -14.747 25.430  1.00 10.56  ? 111 LYS A C   1 
ATOM   917  O  O   . LYS A 1 111 ? 14.641  -15.107 24.533  1.00 11.25  ? 111 LYS A O   1 
ATOM   918  C  CB  . LYS A 1 111 ? 15.379  -15.325 27.405  1.00 13.36  ? 111 LYS A CB  1 
ATOM   919  C  CG  . LYS A 1 111 ? 16.121  -14.772 28.626  1.00 16.19  ? 111 LYS A CG  1 
ATOM   920  C  CD  . LYS A 1 111 ? 17.105  -13.617 28.268  1.00 19.78  ? 111 LYS A CD  1 
ATOM   921  C  CE  . LYS A 1 111 ? 17.731  -12.951 29.471  1.00 25.72  ? 111 LYS A CE  1 
ATOM   922  N  NZ  . LYS A 1 111 ? 18.936  -13.719 29.802  1.00 32.62  ? 111 LYS A NZ  1 
ATOM   923  N  N   . LYS A 1 112 ? 12.569  -14.749 25.226  1.00 10.19  ? 112 LYS A N   1 
ATOM   924  C  CA  . LYS A 1 112 ? 12.010  -15.120 23.941  1.00 11.80  ? 112 LYS A CA  1 
ATOM   925  C  C   . LYS A 1 112 ? 12.335  -14.083 22.887  1.00 10.32  ? 112 LYS A C   1 
ATOM   926  O  O   . LYS A 1 112 ? 12.052  -12.897 23.078  1.00 9.47   ? 112 LYS A O   1 
ATOM   927  C  CB  . LYS A 1 112 ? 10.481  -15.249 24.065  1.00 12.51  ? 112 LYS A CB  1 
ATOM   928  C  CG  . LYS A 1 112 ? 9.782   -15.634 22.777  1.00 14.28  ? 112 LYS A CG  1 
ATOM   929  C  CD  . LYS A 1 112 ? 8.239   -15.626 22.907  1.00 16.64  ? 112 LYS A CD  1 
ATOM   930  C  CE  . LYS A 1 112 ? 7.642   -15.885 21.560  1.00 18.93  ? 112 LYS A CE  1 
ATOM   931  N  NZ  . LYS A 1 112 ? 7.863   -17.240 21.054  1.00 20.01  ? 112 LYS A NZ  1 
ATOM   932  N  N   A LYS A 1 113 ? 12.820  -14.565 21.751  0.50 9.70   ? 113 LYS A N   1 
ATOM   933  N  N   B LYS A 1 113 ? 12.825  -14.562 21.752  0.50 9.69   ? 113 LYS A N   1 
ATOM   934  C  CA  A LYS A 1 113 ? 13.027  -13.760 20.559  0.50 9.84   ? 113 LYS A CA  1 
ATOM   935  C  CA  B LYS A 1 113 ? 13.026  -13.748 20.565  0.50 9.82   ? 113 LYS A CA  1 
ATOM   936  C  C   A LYS A 1 113 ? 11.876  -13.966 19.582  0.50 9.35   ? 113 LYS A C   1 
ATOM   937  C  C   B LYS A 1 113 ? 11.875  -13.962 19.587  0.50 9.34   ? 113 LYS A C   1 
ATOM   938  O  O   A LYS A 1 113 ? 11.489  -15.089 19.294  0.50 12.61  ? 113 LYS A O   1 
ATOM   939  O  O   B LYS A 1 113 ? 11.495  -15.087 19.298  0.50 12.58  ? 113 LYS A O   1 
ATOM   940  C  CB  A LYS A 1 113 ? 14.347  -14.151 19.876  0.50 10.85  ? 113 LYS A CB  1 
ATOM   941  C  CB  B LYS A 1 113 ? 14.325  -14.136 19.842  0.50 10.88  ? 113 LYS A CB  1 
ATOM   942  C  CG  A LYS A 1 113 ? 15.572  -13.794 20.702  0.50 11.97  ? 113 LYS A CG  1 
ATOM   943  C  CG  B LYS A 1 113 ? 15.600  -13.844 20.619  0.50 11.45  ? 113 LYS A CG  1 
ATOM   944  C  CD  A LYS A 1 113 ? 16.876  -14.350 20.142  0.50 12.87  ? 113 LYS A CD  1 
ATOM   945  C  CD  B LYS A 1 113 ? 16.827  -14.446 19.909  0.50 12.47  ? 113 LYS A CD  1 
ATOM   946  C  CE  A LYS A 1 113 ? 18.082  -13.683 20.784  0.50 14.48  ? 113 LYS A CE  1 
ATOM   947  C  CE  B LYS A 1 113 ? 18.136  -13.979 20.545  0.50 14.76  ? 113 LYS A CE  1 
ATOM   948  N  NZ  A LYS A 1 113 ? 19.318  -14.492 20.652  0.50 16.50  ? 113 LYS A NZ  1 
ATOM   949  N  NZ  B LYS A 1 113 ? 18.443  -14.666 21.829  0.50 14.93  ? 113 LYS A NZ  1 
ATOM   950  N  N   . TYR A 1 114 ? 11.393  -12.864 19.012  1.00 8.38   ? 114 TYR A N   1 
ATOM   951  C  CA  . TYR A 1 114 ? 10.395  -12.913 17.942  1.00 7.91   ? 114 TYR A CA  1 
ATOM   952  C  C   . TYR A 1 114 ? 11.075  -12.847 16.582  1.00 7.84   ? 114 TYR A C   1 
ATOM   953  O  O   . TYR A 1 114 ? 12.274  -12.580 16.486  1.00 8.46   ? 114 TYR A O   1 
ATOM   954  C  CB  . TYR A 1 114 ? 9.344   -11.826 18.142  1.00 8.31   ? 114 TYR A CB  1 
ATOM   955  C  CG  . TYR A 1 114 ? 8.440   -12.069 19.313  1.00 8.34   ? 114 TYR A CG  1 
ATOM   956  C  CD1 . TYR A 1 114 ? 8.741   -11.664 20.616  1.00 10.09  ? 114 TYR A CD1 1 
ATOM   957  C  CD2 . TYR A 1 114 ? 7.253   -12.723 19.114  1.00 10.69  ? 114 TYR A CD2 1 
ATOM   958  C  CE1 . TYR A 1 114 ? 7.880   -11.840 21.686  1.00 12.53  ? 114 TYR A CE1 1 
ATOM   959  C  CE2 . TYR A 1 114 ? 6.361   -12.975 20.168  1.00 13.07  ? 114 TYR A CE2 1 
ATOM   960  C  CZ  . TYR A 1 114 ? 6.688   -12.504 21.432  1.00 13.45  ? 114 TYR A CZ  1 
ATOM   961  O  OH  . TYR A 1 114 ? 5.832   -12.632 22.511  1.00 18.52  ? 114 TYR A OH  1 
ATOM   962  N  N   . ALA A 1 115 ? 10.304  -13.072 15.521  1.00 8.23   ? 115 ALA A N   1 
ATOM   963  C  CA  . ALA A 1 115 ? 10.860  -13.108 14.174  1.00 9.00   ? 115 ALA A CA  1 
ATOM   964  C  C   . ALA A 1 115 ? 11.250  -11.707 13.702  1.00 8.60   ? 115 ALA A C   1 
ATOM   965  O  O   . ALA A 1 115 ? 12.093  -11.569 12.797  1.00 9.06   ? 115 ALA A O   1 
ATOM   966  C  CB  . ALA A 1 115 ? 9.836   -13.694 13.238  1.00 11.38  ? 115 ALA A CB  1 
ATOM   967  N  N   . ALA A 1 116 ? 10.616  -10.666 14.245  1.00 7.92   ? 116 ALA A N   1 
ATOM   968  C  CA  . ALA A 1 116 ? 10.896  -9.308  13.804  1.00 7.38   ? 116 ALA A CA  1 
ATOM   969  C  C   . ALA A 1 116 ? 10.323  -8.374  14.845  1.00 6.76   ? 116 ALA A C   1 
ATOM   970  O  O   . ALA A 1 116 ? 9.583   -8.800  15.745  1.00 7.52   ? 116 ALA A O   1 
ATOM   971  C  CB  . ALA A 1 116 ? 10.375  -9.061  12.390  1.00 8.66   ? 116 ALA A CB  1 
ATOM   972  N  N   . GLU A 1 117 ? 10.622  -7.088  14.678  1.00 6.95   ? 117 GLU A N   1 
ATOM   973  C  CA  . GLU A 1 117 ? 10.083  -6.070  15.575  1.00 6.79   ? 117 GLU A CA  1 
ATOM   974  C  C   . GLU A 1 117 ? 9.873   -4.805  14.756  1.00 6.88   ? 117 GLU A C   1 
ATOM   975  O  O   . GLU A 1 117 ? 10.773  -4.372  14.015  1.00 7.80   ? 117 GLU A O   1 
ATOM   976  C  CB  . GLU A 1 117 ? 11.066  -5.854  16.758  1.00 7.36   ? 117 GLU A CB  1 
ATOM   977  C  CG  . GLU A 1 117 ? 10.494  -4.969  17.873  1.00 8.35   ? 117 GLU A CG  1 
ATOM   978  C  CD  . GLU A 1 117 ? 11.413  -4.944  19.091  1.00 7.57   ? 117 GLU A CD  1 
ATOM   979  O  OE1 . GLU A 1 117 ? 12.098  -5.944  19.377  1.00 7.83   ? 117 GLU A OE1 1 
ATOM   980  O  OE2 . GLU A 1 117 ? 11.436  -3.882  19.783  1.00 8.11   ? 117 GLU A OE2 1 
ATOM   981  N  N   . LEU A 1 118 ? 8.668   -4.254  14.914  1.00 6.71   ? 118 LEU A N   1 
ATOM   982  C  CA  . LEU A 1 118 ? 8.263   -3.019  14.267  1.00 6.71   ? 118 LEU A CA  1 
ATOM   983  C  C   . LEU A 1 118 ? 8.481   -1.891  15.271  1.00 6.77   ? 118 LEU A C   1 
ATOM   984  O  O   . LEU A 1 118 ? 8.048   -2.000  16.433  1.00 6.66   ? 118 LEU A O   1 
ATOM   985  C  CB  . LEU A 1 118 ? 6.765   -3.156  13.912  1.00 7.43   ? 118 LEU A CB  1 
ATOM   986  C  CG  . LEU A 1 118 ? 5.978   -1.864  13.600  1.00 7.51   ? 118 LEU A CG  1 
ATOM   987  C  CD1 . LEU A 1 118 ? 6.520   -1.114  12.388  1.00 8.43   ? 118 LEU A CD1 1 
ATOM   988  C  CD2 . LEU A 1 118 ? 4.533   -2.270  13.374  1.00 9.58   ? 118 LEU A CD2 1 
ATOM   989  N  N   . HIS A 1 119 ? 9.106   -0.792  14.811  1.00 5.73   ? 119 HIS A N   1 
ATOM   990  C  CA  . HIS A 1 119 ? 9.281   0.401   15.619  1.00 6.68   ? 119 HIS A CA  1 
ATOM   991  C  C   . HIS A 1 119 ? 8.630   1.577   14.960  1.00 5.70   ? 119 HIS A C   1 
ATOM   992  O  O   . HIS A 1 119 ? 8.983   1.905   13.810  1.00 7.21   ? 119 HIS A O   1 
ATOM   993  C  CB  . HIS A 1 119 ? 10.816  0.664   15.738  1.00 7.03   ? 119 HIS A CB  1 
ATOM   994  C  CG  . HIS A 1 119 ? 11.490  -0.352  16.591  1.00 6.51   ? 119 HIS A CG  1 
ATOM   995  N  ND1 . HIS A 1 119 ? 12.875  -0.534  16.567  1.00 6.82   ? 119 HIS A ND1 1 
ATOM   996  C  CD2 . HIS A 1 119 ? 10.958  -1.177  17.538  1.00 6.44   ? 119 HIS A CD2 1 
ATOM   997  C  CE1 . HIS A 1 119 ? 13.143  -1.479  17.483  1.00 7.00   ? 119 HIS A CE1 1 
ATOM   998  N  NE2 . HIS A 1 119 ? 11.992  -1.883  18.084  1.00 7.06   ? 119 HIS A NE2 1 
ATOM   999  N  N   . LEU A 1 120 ? 7.690   2.214   15.671  1.00 6.46   ? 120 LEU A N   1 
ATOM   1000 C  CA  . LEU A 1 120 ? 7.026   3.428   15.207  1.00 6.50   ? 120 LEU A CA  1 
ATOM   1001 C  C   . LEU A 1 120 ? 7.653   4.566   16.030  1.00 6.47   ? 120 LEU A C   1 
ATOM   1002 O  O   . LEU A 1 120 ? 7.573   4.588   17.264  1.00 6.76   ? 120 LEU A O   1 
ATOM   1003 C  CB  . LEU A 1 120 ? 5.503   3.357   15.411  1.00 7.71   ? 120 LEU A CB  1 
ATOM   1004 C  CG  . LEU A 1 120 ? 4.862   2.298   14.540  1.00 7.97   ? 120 LEU A CG  1 
ATOM   1005 C  CD1 . LEU A 1 120 ? 4.145   1.264   15.408  1.00 12.23  ? 120 LEU A CD1 1 
ATOM   1006 C  CD2 . LEU A 1 120 ? 3.920   2.969   13.536  1.00 11.32  ? 120 LEU A CD2 1 
ATOM   1007 N  N   . VAL A 1 121 ? 8.360   5.451   15.321  1.00 7.22   ? 121 VAL A N   1 
ATOM   1008 C  CA  . VAL A 1 121 ? 9.208   6.460   15.980  1.00 7.17   ? 121 VAL A CA  1 
ATOM   1009 C  C   . VAL A 1 121 ? 8.486   7.793   15.985  1.00 7.38   ? 121 VAL A C   1 
ATOM   1010 O  O   . VAL A 1 121 ? 8.080   8.289   14.941  1.00 8.49   ? 121 VAL A O   1 
ATOM   1011 C  CB  . VAL A 1 121 ? 10.546  6.591   15.200  1.00 8.52   ? 121 VAL A CB  1 
ATOM   1012 C  CG1 . VAL A 1 121 ? 11.452  7.649   15.863  1.00 10.81  ? 121 VAL A CG1 1 
ATOM   1013 C  CG2 . VAL A 1 121 ? 11.231  5.218   15.087  1.00 9.77   ? 121 VAL A CG2 1 
ATOM   1014 N  N   . HIS A 1 122 ? 8.430   8.414   17.168  1.00 7.20   ? 122 HIS A N   1 
ATOM   1015 C  CA  . HIS A 1 122 ? 7.705   9.665   17.372  1.00 7.72   ? 122 HIS A CA  1 
ATOM   1016 C  C   . HIS A 1 122 ? 8.627   10.622  18.113  1.00 7.16   ? 122 HIS A C   1 
ATOM   1017 O  O   . HIS A 1 122 ? 9.378   10.220  18.982  1.00 9.10   ? 122 HIS A O   1 
ATOM   1018 C  CB  . HIS A 1 122 ? 6.451   9.425   18.262  1.00 8.60   ? 122 HIS A CB  1 
ATOM   1019 C  CG  . HIS A 1 122 ? 5.582   8.307   17.867  1.00 7.74   ? 122 HIS A CG  1 
ATOM   1020 N  ND1 . HIS A 1 122 ? 5.914   6.983   18.107  1.00 7.91   ? 122 HIS A ND1 1 
ATOM   1021 C  CD2 . HIS A 1 122 ? 4.365   8.273   17.258  1.00 8.49   ? 122 HIS A CD2 1 
ATOM   1022 C  CE1 . HIS A 1 122 ? 4.935   6.234   17.681  1.00 8.38   ? 122 HIS A CE1 1 
ATOM   1023 N  NE2 . HIS A 1 122 ? 3.940   6.967   17.138  1.00 8.77   ? 122 HIS A NE2 1 
ATOM   1024 N  N   . TRP A 1 123 ? 8.519   11.907  17.797  1.00 7.61   ? 123 TRP A N   1 
ATOM   1025 C  CA  . TRP A 1 123 ? 9.348   12.907  18.485  1.00 8.02   ? 123 TRP A CA  1 
ATOM   1026 C  C   . TRP A 1 123 ? 8.501   13.884  19.298  1.00 8.26   ? 123 TRP A C   1 
ATOM   1027 O  O   . TRP A 1 123 ? 7.362   14.225  18.919  1.00 9.43   ? 123 TRP A O   1 
ATOM   1028 C  CB  . TRP A 1 123 ? 10.288  13.640  17.497  1.00 9.14   ? 123 TRP A CB  1 
ATOM   1029 C  CG  . TRP A 1 123 ? 9.584   14.291  16.346  1.00 9.38   ? 123 TRP A CG  1 
ATOM   1030 C  CD1 . TRP A 1 123 ? 9.321   13.725  15.131  1.00 10.95  ? 123 TRP A CD1 1 
ATOM   1031 C  CD2 . TRP A 1 123 ? 9.146   15.659  16.228  1.00 11.44  ? 123 TRP A CD2 1 
ATOM   1032 N  NE1 . TRP A 1 123 ? 8.716   14.617  14.282  1.00 13.28  ? 123 TRP A NE1 1 
ATOM   1033 C  CE2 . TRP A 1 123 ? 8.571   15.810  14.937  1.00 11.82  ? 123 TRP A CE2 1 
ATOM   1034 C  CE3 . TRP A 1 123 ? 9.120   16.770  17.081  1.00 11.69  ? 123 TRP A CE3 1 
ATOM   1035 C  CZ2 . TRP A 1 123 ? 8.014   17.000  14.460  1.00 14.22  ? 123 TRP A CZ2 1 
ATOM   1036 C  CZ3 . TRP A 1 123 ? 8.562   17.948  16.623  1.00 14.07  ? 123 TRP A CZ3 1 
ATOM   1037 C  CH2 . TRP A 1 123 ? 7.991   18.049  15.356  1.00 14.89  ? 123 TRP A CH2 1 
ATOM   1038 N  N   . ASN A 1 124 ? 9.096   14.334  20.375  1.00 8.60   ? 124 ASN A N   1 
ATOM   1039 C  CA  . ASN A 1 124 ? 8.418   15.187  21.359  1.00 10.01  ? 124 ASN A CA  1 
ATOM   1040 C  C   . ASN A 1 124 ? 8.251   16.575  20.759  1.00 9.57   ? 124 ASN A C   1 
ATOM   1041 O  O   . ASN A 1 124 ? 9.239   17.253  20.462  1.00 10.03  ? 124 ASN A O   1 
ATOM   1042 C  CB  . ASN A 1 124 ? 9.269   15.228  22.597  1.00 11.15  ? 124 ASN A CB  1 
ATOM   1043 C  CG  . ASN A 1 124 ? 8.568   15.802  23.788  1.00 11.56  ? 124 ASN A CG  1 
ATOM   1044 O  OD1 . ASN A 1 124 ? 7.744   16.729  23.600  1.00 13.41  ? 124 ASN A OD1 1 
ATOM   1045 N  ND2 . ASN A 1 124 ? 8.975   15.372  24.975  1.00 13.15  ? 124 ASN A ND2 1 
ATOM   1046 N  N   . THR A 1 125 ? 6.985   17.012  20.589  1.00 11.37  ? 125 THR A N   1 
ATOM   1047 C  CA  . THR A 1 125 ? 6.764   18.288  19.875  1.00 12.88  ? 125 THR A CA  1 
ATOM   1048 C  C   . THR A 1 125 ? 7.299   19.477  20.678  1.00 11.96  ? 125 THR A C   1 
ATOM   1049 O  O   . THR A 1 125 ? 7.479   20.551  20.000  1.00 14.17  ? 125 THR A O   1 
ATOM   1050 C  CB  . THR A 1 125 ? 5.271   18.467  19.561  1.00 15.43  ? 125 THR A CB  1 
ATOM   1051 O  OG1 . THR A 1 125 ? 4.533   18.441  20.795  1.00 19.97  ? 125 THR A OG1 1 
ATOM   1052 C  CG2 . THR A 1 125 ? 4.827   17.359  18.614  1.00 17.44  ? 125 THR A CG2 1 
ATOM   1053 N  N   . LYS A 1 126 ? 7.615   19.360  21.952  1.00 12.65  ? 126 LYS A N   1 
ATOM   1054 C  CA  . LYS A 1 126 ? 8.212   20.483  22.695  1.00 14.10  ? 126 LYS A CA  1 
ATOM   1055 C  C   . LYS A 1 126 ? 9.561   20.880  22.088  1.00 12.81  ? 126 LYS A C   1 
ATOM   1056 O  O   . LYS A 1 126 ? 10.010  21.971  22.421  1.00 15.77  ? 126 LYS A O   1 
ATOM   1057 C  CB  . LYS A 1 126 ? 8.294   20.191  24.183  1.00 17.09  ? 126 LYS A CB  1 
ATOM   1058 C  CG  . LYS A 1 126 ? 9.466   19.334  24.649  1.00 18.53  ? 126 LYS A CG  1 
ATOM   1059 C  CD  . LYS A 1 126 ? 9.337   18.851  26.151  1.00 25.50  ? 126 LYS A CD  1 
ATOM   1060 C  CE  . LYS A 1 126 ? 9.729   19.984  27.035  1.00 30.01  ? 126 LYS A CE  1 
ATOM   1061 N  NZ  . LYS A 1 126 ? 9.571   19.618  28.473  1.00 26.51  ? 126 LYS A NZ  1 
ATOM   1062 N  N   . TYR A 1 127 ? 10.193  20.014  21.293  1.00 12.51  ? 127 TYR A N   1 
ATOM   1063 C  CA  . TYR A 1 127 ? 11.500  20.324  20.738  1.00 11.76  ? 127 TYR A CA  1 
ATOM   1064 C  C   . TYR A 1 127 ? 11.474  20.761  19.278  1.00 11.80  ? 127 TYR A C   1 
ATOM   1065 O  O   . TYR A 1 127 ? 12.548  20.979  18.653  1.00 12.50  ? 127 TYR A O   1 
ATOM   1066 C  CB  . TYR A 1 127 ? 12.482  19.158  20.927  1.00 11.49  ? 127 TYR A CB  1 
ATOM   1067 C  CG  . TYR A 1 127 ? 12.633  18.825  22.380  1.00 12.26  ? 127 TYR A CG  1 
ATOM   1068 C  CD1 . TYR A 1 127 ? 13.084  19.744  23.304  1.00 13.94  ? 127 TYR A CD1 1 
ATOM   1069 C  CD2 . TYR A 1 127 ? 12.330  17.548  22.861  1.00 11.89  ? 127 TYR A CD2 1 
ATOM   1070 C  CE1 . TYR A 1 127 ? 13.210  19.433  24.648  1.00 16.08  ? 127 TYR A CE1 1 
ATOM   1071 C  CE2 . TYR A 1 127 ? 12.428  17.200  24.205  1.00 13.08  ? 127 TYR A CE2 1 
ATOM   1072 C  CZ  . TYR A 1 127 ? 12.895  18.168  25.100  1.00 15.55  ? 127 TYR A CZ  1 
ATOM   1073 O  OH  . TYR A 1 127 ? 13.052  17.919  26.414  1.00 16.55  ? 127 TYR A OH  1 
ATOM   1074 N  N   . GLY A 1 128 ? 10.268  20.867  18.715  1.00 11.34  ? 128 GLY A N   1 
ATOM   1075 C  CA  . GLY A 1 128 ? 10.167  21.589  17.444  1.00 12.63  ? 128 GLY A CA  1 
ATOM   1076 C  C   . GLY A 1 128 ? 10.455  20.776  16.201  1.00 11.97  ? 128 GLY A C   1 
ATOM   1077 O  O   . GLY A 1 128 ? 9.766   20.954  15.212  1.00 13.29  ? 128 GLY A O   1 
ATOM   1078 N  N   . ASP A 1 129 ? 11.491  19.902  16.243  1.00 12.35  ? 129 ASP A N   1 
ATOM   1079 C  CA  . ASP A 1 129 ? 11.660  19.019  15.118  1.00 12.65  ? 129 ASP A CA  1 
ATOM   1080 C  C   . ASP A 1 129 ? 12.403  17.791  15.638  1.00 12.98  ? 129 ASP A C   1 
ATOM   1081 O  O   . ASP A 1 129 ? 12.907  17.738  16.768  1.00 13.44  ? 129 ASP A O   1 
ATOM   1082 C  CB  . ASP A 1 129 ? 12.276  19.632  13.878  1.00 16.19  ? 129 ASP A CB  1 
ATOM   1083 C  CG  . ASP A 1 129 ? 13.672  20.089  14.106  1.00 15.65  ? 129 ASP A CG  1 
ATOM   1084 O  OD1 . ASP A 1 129 ? 14.266  19.718  15.076  1.00 23.34  ? 129 ASP A OD1 1 
ATOM   1085 O  OD2 . ASP A 1 129 ? 14.158  20.829  13.252  1.00 22.82  ? 129 ASP A OD2 1 
ATOM   1086 N  N   . TYR A 1 130 ? 12.487  16.785  14.763  1.00 12.81  ? 130 TYR A N   1 
ATOM   1087 C  CA  . TYR A 1 130 ? 13.078  15.520  15.125  1.00 14.66  ? 130 TYR A CA  1 
ATOM   1088 C  C   . TYR A 1 130 ? 14.568  15.691  15.450  1.00 13.91  ? 130 TYR A C   1 
ATOM   1089 O  O   . TYR A 1 130 ? 15.110  15.117  16.386  1.00 15.41  ? 130 TYR A O   1 
ATOM   1090 C  CB  . TYR A 1 130 ? 12.820  14.512  13.989  1.00 17.73  ? 130 TYR A CB  1 
ATOM   1091 C  CG  . TYR A 1 130 ? 13.697  13.284  14.091  1.00 25.81  ? 130 TYR A CG  1 
ATOM   1092 C  CD1 . TYR A 1 130 ? 15.003  13.349  13.666  1.00 35.78  ? 130 TYR A CD1 1 
ATOM   1093 C  CD2 . TYR A 1 130 ? 13.309  12.141  14.777  1.00 23.68  ? 130 TYR A CD2 1 
ATOM   1094 C  CE1 . TYR A 1 130 ? 15.907  12.292  13.771  1.00 38.46  ? 130 TYR A CE1 1 
ATOM   1095 C  CE2 . TYR A 1 130 ? 14.197  11.054  14.874  1.00 25.49  ? 130 TYR A CE2 1 
ATOM   1096 C  CZ  . TYR A 1 130 ? 15.500  11.124  14.389  1.00 31.54  ? 130 TYR A CZ  1 
ATOM   1097 O  OH  . TYR A 1 130 ? 16.405  10.078  14.491  1.00 34.73  ? 130 TYR A OH  1 
ATOM   1098 N  N   . GLY A 1 131 ? 15.268  16.512  14.620  1.00 16.87  ? 131 GLY A N   1 
ATOM   1099 C  CA  . GLY A 1 131 ? 16.695  16.634  14.831  1.00 20.19  ? 131 GLY A CA  1 
ATOM   1100 C  C   . GLY A 1 131 ? 17.051  17.222  16.189  1.00 18.80  ? 131 GLY A C   1 
ATOM   1101 O  O   . GLY A 1 131 ? 18.149  16.898  16.728  1.00 22.43  ? 131 GLY A O   1 
ATOM   1102 N  N   A LYS A 1 132 ? 16.177  18.117  16.694  0.50 18.59  ? 132 LYS A N   1 
ATOM   1103 N  N   B LYS A 1 132 ? 16.157  18.063  16.758  0.50 18.27  ? 132 LYS A N   1 
ATOM   1104 C  CA  A LYS A 1 132 ? 16.462  18.657  18.027  0.50 17.77  ? 132 LYS A CA  1 
ATOM   1105 C  CA  B LYS A 1 132 ? 16.387  18.697  18.073  0.50 18.26  ? 132 LYS A CA  1 
ATOM   1106 C  C   A LYS A 1 132 ? 16.093  17.531  19.011  0.50 11.60  ? 132 LYS A C   1 
ATOM   1107 C  C   B LYS A 1 132 ? 15.906  17.769  19.193  0.50 16.35  ? 132 LYS A C   1 
ATOM   1108 O  O   A LYS A 1 132 ? 16.898  17.125  19.849  0.50 10.16  ? 132 LYS A O   1 
ATOM   1109 O  O   B LYS A 1 132 ? 16.415  17.751  20.323  0.50 12.00  ? 132 LYS A O   1 
ATOM   1110 C  CB  A LYS A 1 132 ? 15.691  20.019  18.232  0.50 24.77  ? 132 LYS A CB  1 
ATOM   1111 C  CB  B LYS A 1 132 ? 15.596  20.013  18.204  0.50 20.16  ? 132 LYS A CB  1 
ATOM   1112 C  CG  A LYS A 1 132 ? 16.190  21.092  17.219  0.50 33.49  ? 132 LYS A CG  1 
ATOM   1113 C  CG  B LYS A 1 132 ? 16.287  21.252  17.632  0.50 24.78  ? 132 LYS A CG  1 
ATOM   1114 C  CD  A LYS A 1 132 ? 17.684  20.973  16.818  0.50 25.77  ? 132 LYS A CD  1 
ATOM   1115 C  CD  B LYS A 1 132 ? 17.402  21.754  18.549  0.50 26.26  ? 132 LYS A CD  1 
ATOM   1116 C  CE  A LYS A 1 132 ? 17.945  21.607  15.409  0.50 42.51  ? 132 LYS A CE  1 
ATOM   1117 C  CE  B LYS A 1 132 ? 17.824  23.153  18.139  0.50 29.04  ? 132 LYS A CE  1 
ATOM   1118 N  NZ  A LYS A 1 132 ? 17.046  22.837  15.190  0.50 40.27  ? 132 LYS A NZ  1 
ATOM   1119 N  NZ  B LYS A 1 132 ? 18.281  23.103  16.715  0.50 29.54  ? 132 LYS A NZ  1 
ATOM   1120 N  N   . ALA A 1 133 ? 14.872  16.992  18.864  1.00 12.59  ? 133 ALA A N   1 
ATOM   1121 C  CA  . ALA A 1 133 ? 14.377  16.015  19.802  1.00 11.46  ? 133 ALA A CA  1 
ATOM   1122 C  C   . ALA A 1 133 ? 15.383  14.912  20.083  1.00 11.14  ? 133 ALA A C   1 
ATOM   1123 O  O   . ALA A 1 133 ? 15.474  14.515  21.264  1.00 12.55  ? 133 ALA A O   1 
ATOM   1124 C  CB  . ALA A 1 133 ? 13.056  15.453  19.301  1.00 10.71  ? 133 ALA A CB  1 
ATOM   1125 N  N   . VAL A 1 134 ? 16.098  14.455  19.068  1.00 14.16  ? 134 VAL A N   1 
ATOM   1126 C  CA  . VAL A 1 134 ? 16.958  13.295  19.211  1.00 17.99  ? 134 VAL A CA  1 
ATOM   1127 C  C   . VAL A 1 134 ? 18.112  13.632  20.161  1.00 20.53  ? 134 VAL A C   1 
ATOM   1128 O  O   . VAL A 1 134 ? 18.874  12.727  20.526  1.00 24.65  ? 134 VAL A O   1 
ATOM   1129 C  CB  . VAL A 1 134 ? 17.483  12.816  17.843  1.00 25.35  ? 134 VAL A CB  1 
ATOM   1130 C  CG1 . VAL A 1 134 ? 16.359  12.306  16.955  1.00 37.42  ? 134 VAL A CG1 1 
ATOM   1131 C  CG2 . VAL A 1 134 ? 18.278  13.901  17.133  1.00 29.84  ? 134 VAL A CG2 1 
ATOM   1132 N  N   . GLN A 1 135 ? 18.210  14.887  20.571  1.00 21.38  ? 135 GLN A N   1 
ATOM   1133 C  CA  . GLN A 1 135 ? 19.373  15.314  21.364  1.00 32.43  ? 135 GLN A CA  1 
ATOM   1134 C  C   . GLN A 1 135 ? 18.951  15.528  22.794  1.00 22.97  ? 135 GLN A C   1 
ATOM   1135 O  O   . GLN A 1 135 ? 19.727  15.937  23.685  1.00 30.57  ? 135 GLN A O   1 
ATOM   1136 C  CB  . GLN A 1 135 ? 19.915  16.674  20.707  1.00 37.44  ? 135 GLN A CB  1 
ATOM   1137 C  CG  . GLN A 1 135 ? 20.248  16.543  19.126  1.00 62.73  ? 135 GLN A CG  1 
ATOM   1138 C  CD  . GLN A 1 135 ? 20.773  17.833  18.545  1.00 110.84 ? 135 GLN A CD  1 
ATOM   1139 O  OE1 . GLN A 1 135 ? 20.354  18.271  17.476  1.00 89.70  ? 135 GLN A OE1 1 
ATOM   1140 N  NE2 . GLN A 1 135 ? 21.703  18.455  19.252  1.00 124.07 ? 135 GLN A NE2 1 
ATOM   1141 N  N   . GLN A 1 136 ? 17.708  15.097  23.038  1.00 15.20  ? 136 GLN A N   1 
ATOM   1142 C  CA  . GLN A 1 136 ? 17.156  15.354  24.370  1.00 12.99  ? 136 GLN A CA  1 
ATOM   1143 C  C   . GLN A 1 136 ? 16.829  14.045  25.090  1.00 12.00  ? 136 GLN A C   1 
ATOM   1144 O  O   . GLN A 1 136 ? 16.495  13.049  24.456  1.00 11.20  ? 136 GLN A O   1 
ATOM   1145 C  CB  . GLN A 1 136 ? 15.842  16.137  24.328  1.00 15.82  ? 136 GLN A CB  1 
ATOM   1146 C  CG  . GLN A 1 136 ? 15.956  17.351  23.402  1.00 18.07  ? 136 GLN A CG  1 
ATOM   1147 C  CD  . GLN A 1 136 ? 16.953  18.365  23.902  1.00 18.93  ? 136 GLN A CD  1 
ATOM   1148 O  OE1 . GLN A 1 136 ? 17.142  18.490  25.116  1.00 20.83  ? 136 GLN A OE1 1 
ATOM   1149 N  NE2 . GLN A 1 136 ? 17.512  19.141  22.989  1.00 28.71  ? 136 GLN A NE2 1 
ATOM   1150 N  N   A PRO A 1 137 ? 16.827  14.069  26.451  0.50 12.40  ? 137 PRO A N   1 
ATOM   1151 N  N   B PRO A 1 137 ? 16.982  13.975  26.441  0.50 14.47  ? 137 PRO A N   1 
ATOM   1152 C  CA  A PRO A 1 137 ? 16.704  12.833  27.220  0.50 13.44  ? 137 PRO A CA  1 
ATOM   1153 C  CA  B PRO A 1 137 ? 16.741  12.697  27.100  0.50 14.14  ? 137 PRO A CA  1 
ATOM   1154 C  C   A PRO A 1 137 ? 15.346  12.184  26.972  0.50 12.43  ? 137 PRO A C   1 
ATOM   1155 C  C   B PRO A 1 137 ? 15.326  12.145  26.973  0.50 12.49  ? 137 PRO A C   1 
ATOM   1156 O  O   A PRO A 1 137 ? 15.250  10.965  27.017  0.50 14.24  ? 137 PRO A O   1 
ATOM   1157 O  O   B PRO A 1 137 ? 15.157  10.960  27.258  0.50 14.42  ? 137 PRO A O   1 
ATOM   1158 C  CB  A PRO A 1 137 ? 16.909  13.244  28.691  0.50 17.69  ? 137 PRO A CB  1 
ATOM   1159 C  CB  B PRO A 1 137 ? 17.006  12.976  28.583  0.50 16.99  ? 137 PRO A CB  1 
ATOM   1160 C  CG  A PRO A 1 137 ? 16.749  14.738  28.677  0.50 15.92  ? 137 PRO A CG  1 
ATOM   1161 C  CG  B PRO A 1 137 ? 17.971  14.120  28.545  0.50 20.79  ? 137 PRO A CG  1 
ATOM   1162 C  CD  A PRO A 1 137 ? 17.131  15.235  27.292  0.50 16.60  ? 137 PRO A CD  1 
ATOM   1163 C  CD  B PRO A 1 137 ? 17.572  14.980  27.347  0.50 15.94  ? 137 PRO A CD  1 
ATOM   1164 N  N   . ASP A 1 138 ? 14.328  13.032  26.691  1.00 11.56  ? 138 ASP A N   1 
ATOM   1165 C  CA  . ASP A 1 138 ? 12.940  12.603  26.495  1.00 11.31  ? 138 ASP A CA  1 
ATOM   1166 C  C   . ASP A 1 138 ? 12.510  13.057  25.098  1.00 9.71   ? 138 ASP A C   1 
ATOM   1167 O  O   . ASP A 1 138 ? 11.366  13.444  24.866  1.00 11.70  ? 138 ASP A O   1 
ATOM   1168 C  CB  . ASP A 1 138 ? 12.021  13.247  27.547  1.00 14.43  ? 138 ASP A CB  1 
ATOM   1169 C  CG  . ASP A 1 138 ? 12.044  14.736  27.523  1.00 12.72  ? 138 ASP A CG  1 
ATOM   1170 O  OD1 . ASP A 1 138 ? 12.976  15.358  26.958  1.00 14.19  ? 138 ASP A OD1 1 
ATOM   1171 O  OD2 . ASP A 1 138 ? 11.149  15.341  28.150  1.00 15.35  ? 138 ASP A OD2 1 
ATOM   1172 N  N   . GLY A 1 139 ? 13.393  12.933  24.125  1.00 8.94   ? 139 GLY A N   1 
ATOM   1173 C  CA  . GLY A 1 139 ? 13.083  13.441  22.802  1.00 8.75   ? 139 GLY A CA  1 
ATOM   1174 C  C   . GLY A 1 139 ? 12.200  12.524  21.953  1.00 7.40   ? 139 GLY A C   1 
ATOM   1175 O  O   . GLY A 1 139 ? 11.459  13.035  21.104  1.00 8.01   ? 139 GLY A O   1 
ATOM   1176 N  N   . LEU A 1 140 ? 12.348  11.209  22.119  1.00 7.13   ? 140 LEU A N   1 
ATOM   1177 C  CA  . LEU A 1 140 ? 11.621  10.262  21.272  1.00 6.94   ? 140 LEU A CA  1 
ATOM   1178 C  C   . LEU A 1 140 ? 10.779  9.324   22.110  1.00 6.79   ? 140 LEU A C   1 
ATOM   1179 O  O   . LEU A 1 140 ? 11.121  9.021   23.245  1.00 7.00   ? 140 LEU A O   1 
ATOM   1180 C  CB  . LEU A 1 140 ? 12.586  9.411   20.444  1.00 8.14   ? 140 LEU A CB  1 
ATOM   1181 C  CG  . LEU A 1 140 ? 13.485  10.118  19.450  1.00 9.00   ? 140 LEU A CG  1 
ATOM   1182 C  CD1 . LEU A 1 140 ? 14.263  9.086   18.647  1.00 10.25  ? 140 LEU A CD1 1 
ATOM   1183 C  CD2 . LEU A 1 140 ? 12.775  11.087  18.538  1.00 10.60  ? 140 LEU A CD2 1 
ATOM   1184 N  N   . ALA A 1 141 ? 9.712   8.853   21.479  1.00 7.37   ? 141 ALA A N   1 
ATOM   1185 C  CA  . ALA A 1 141 ? 8.931   7.743   22.041  1.00 7.32   ? 141 ALA A CA  1 
ATOM   1186 C  C   . ALA A 1 141 ? 8.849   6.750   20.885  1.00 7.07   ? 141 ALA A C   1 
ATOM   1187 O  O   . ALA A 1 141 ? 8.388   7.078   19.784  1.00 7.89   ? 141 ALA A O   1 
ATOM   1188 C  CB  . ALA A 1 141 ? 7.558   8.192   22.514  1.00 9.04   ? 141 ALA A CB  1 
ATOM   1189 N  N   . VAL A 1 142 ? 9.289   5.522   21.190  1.00 6.99   ? 142 VAL A N   1 
ATOM   1190 C  CA  . VAL A 1 142 ? 9.242   4.493   20.146  1.00 7.19   ? 142 VAL A CA  1 
ATOM   1191 C  C   . VAL A 1 142 ? 8.268   3.411   20.611  1.00 6.62   ? 142 VAL A C   1 
ATOM   1192 O  O   . VAL A 1 142 ? 8.429   2.877   21.718  1.00 7.29   ? 142 VAL A O   1 
ATOM   1193 C  CB  . VAL A 1 142 ? 10.625  3.920   19.781  1.00 7.30   ? 142 VAL A CB  1 
ATOM   1194 C  CG1 . VAL A 1 142 ? 10.451  2.912   18.644  1.00 7.96   ? 142 VAL A CG1 1 
ATOM   1195 C  CG2 . VAL A 1 142 ? 11.570  5.030   19.336  1.00 8.61   ? 142 VAL A CG2 1 
ATOM   1196 N  N   . LEU A 1 143 ? 7.262   3.164   19.778  1.00 6.87   ? 143 LEU A N   1 
ATOM   1197 C  CA  . LEU A 1 143 ? 6.303   2.117   20.047  1.00 7.45   ? 143 LEU A CA  1 
ATOM   1198 C  C   . LEU A 1 143 ? 6.821   0.863   19.337  1.00 7.25   ? 143 LEU A C   1 
ATOM   1199 O  O   . LEU A 1 143 ? 6.972   0.858   18.099  1.00 8.04   ? 143 LEU A O   1 
ATOM   1200 C  CB  . LEU A 1 143 ? 4.955   2.565   19.468  1.00 9.52   ? 143 LEU A CB  1 
ATOM   1201 C  CG  . LEU A 1 143 ? 3.788   1.634   19.671  1.00 10.42  ? 143 LEU A CG  1 
ATOM   1202 C  CD1 . LEU A 1 143 ? 3.515   1.374   21.152  1.00 14.00  ? 143 LEU A CD1 1 
ATOM   1203 C  CD2 . LEU A 1 143 ? 2.540   2.206   18.994  1.00 11.84  ? 143 LEU A CD2 1 
ATOM   1204 N  N   . GLY A 1 144 ? 7.093   -0.189  20.108  1.00 7.02   ? 144 GLY A N   1 
ATOM   1205 C  CA  . GLY A 1 144 ? 7.643   -1.431  19.565  1.00 6.97   ? 144 GLY A CA  1 
ATOM   1206 C  C   . GLY A 1 144 ? 6.577   -2.516  19.585  1.00 6.54   ? 144 GLY A C   1 
ATOM   1207 O  O   . GLY A 1 144 ? 5.838   -2.671  20.556  1.00 7.76   ? 144 GLY A O   1 
ATOM   1208 N  N   . ILE A 1 145 ? 6.526   -3.252  18.475  1.00 6.50   ? 145 ILE A N   1 
ATOM   1209 C  CA  . ILE A 1 145 ? 5.507   -4.286  18.292  1.00 6.55   ? 145 ILE A CA  1 
ATOM   1210 C  C   . ILE A 1 145 ? 6.236   -5.522  17.778  1.00 6.79   ? 145 ILE A C   1 
ATOM   1211 O  O   . ILE A 1 145 ? 6.951   -5.469  16.776  1.00 6.99   ? 145 ILE A O   1 
ATOM   1212 C  CB  . ILE A 1 145 ? 4.410   -3.827  17.317  1.00 7.58   ? 145 ILE A CB  1 
ATOM   1213 C  CG1 . ILE A 1 145 ? 3.775   -2.544  17.847  1.00 9.67   ? 145 ILE A CG1 1 
ATOM   1214 C  CG2 . ILE A 1 145 ? 3.412   -4.945  17.070  1.00 9.99   ? 145 ILE A CG2 1 
ATOM   1215 C  CD1 . ILE A 1 145 ? 2.717   -1.934  16.932  1.00 9.47   ? 145 ILE A CD1 1 
ATOM   1216 N  N   . PHE A 1 146 ? 6.050   -6.648  18.435  1.00 6.63   ? 146 PHE A N   1 
ATOM   1217 C  CA  . PHE A 1 146 ? 6.679   -7.896  18.009  1.00 6.82   ? 146 PHE A CA  1 
ATOM   1218 C  C   . PHE A 1 146 ? 5.934   -8.514  16.835  1.00 6.89   ? 146 PHE A C   1 
ATOM   1219 O  O   . PHE A 1 146 ? 4.700   -8.417  16.786  1.00 7.78   ? 146 PHE A O   1 
ATOM   1220 C  CB  . PHE A 1 146 ? 6.702   -8.881  19.165  1.00 7.83   ? 146 PHE A CB  1 
ATOM   1221 C  CG  . PHE A 1 146 ? 7.524   -8.411  20.335  1.00 6.45   ? 146 PHE A CG  1 
ATOM   1222 C  CD1 . PHE A 1 146 ? 8.908   -8.236  20.169  1.00 7.51   ? 146 PHE A CD1 1 
ATOM   1223 C  CD2 . PHE A 1 146 ? 6.984   -8.188  21.573  1.00 7.74   ? 146 PHE A CD2 1 
ATOM   1224 C  CE1 . PHE A 1 146 ? 9.707   -7.851  21.221  1.00 8.10   ? 146 PHE A CE1 1 
ATOM   1225 C  CE2 . PHE A 1 146 ? 7.758   -7.792  22.646  1.00 8.04   ? 146 PHE A CE2 1 
ATOM   1226 C  CZ  . PHE A 1 146 ? 9.136   -7.646  22.480  1.00 7.85   ? 146 PHE A CZ  1 
ATOM   1227 N  N   . LEU A 1 147 ? 6.670   -9.194  15.963  1.00 7.28   ? 147 LEU A N   1 
ATOM   1228 C  CA  . LEU A 1 147 ? 6.082   -9.968  14.888  1.00 7.78   ? 147 LEU A CA  1 
ATOM   1229 C  C   . LEU A 1 147 ? 6.398   -11.433 15.093  1.00 7.73   ? 147 LEU A C   1 
ATOM   1230 O  O   . LEU A 1 147 ? 7.564   -11.815 15.268  1.00 9.06   ? 147 LEU A O   1 
ATOM   1231 C  CB  . LEU A 1 147 ? 6.669   -9.559  13.530  1.00 7.99   ? 147 LEU A CB  1 
ATOM   1232 C  CG  . LEU A 1 147 ? 6.073   -8.307  12.879  1.00 8.05   ? 147 LEU A CG  1 
ATOM   1233 C  CD1 . LEU A 1 147 ? 6.274   -7.030  13.726  1.00 10.60  ? 147 LEU A CD1 1 
ATOM   1234 C  CD2 . LEU A 1 147 ? 6.693   -8.081  11.497  1.00 9.34   ? 147 LEU A CD2 1 
ATOM   1235 N  N   . LYS A 1 148 ? 5.349   -12.265 15.104  1.00 8.40   ? 148 LYS A N   1 
ATOM   1236 C  CA  . LYS A 1 148 ? 5.508   -13.720 15.122  1.00 9.52   ? 148 LYS A CA  1 
ATOM   1237 C  C   . LYS A 1 148 ? 5.036   -14.245 13.784  1.00 9.82   ? 148 LYS A C   1 
ATOM   1238 O  O   . LYS A 1 148 ? 4.177   -13.658 13.134  1.00 11.84  ? 148 LYS A O   1 
ATOM   1239 C  CB  . LYS A 1 148 ? 4.764   -14.346 16.286  1.00 12.62  ? 148 LYS A CB  1 
ATOM   1240 C  CG  . LYS A 1 148 ? 3.280   -14.271 16.178  1.00 13.29  ? 148 LYS A CG  1 
ATOM   1241 C  CD  . LYS A 1 148 ? 2.642   -14.980 17.344  1.00 19.64  ? 148 LYS A CD  1 
ATOM   1242 C  CE  . LYS A 1 148 ? 1.131   -14.988 17.230  1.00 29.21  ? 148 LYS A CE  1 
ATOM   1243 N  NZ  . LYS A 1 148 ? 0.563   -15.747 18.365  1.00 39.17  ? 148 LYS A NZ  1 
ATOM   1244 N  N   . VAL A 1 149 ? 5.559   -15.393 13.359  1.00 10.10  ? 149 VAL A N   1 
ATOM   1245 C  CA  . VAL A 1 149 ? 5.162   -15.982 12.102  1.00 10.92  ? 149 VAL A CA  1 
ATOM   1246 C  C   . VAL A 1 149 ? 3.938   -16.878 12.354  1.00 10.36  ? 149 VAL A C   1 
ATOM   1247 O  O   . VAL A 1 149 ? 3.956   -17.797 13.157  1.00 11.89  ? 149 VAL A O   1 
ATOM   1248 C  CB  . VAL A 1 149 ? 6.345   -16.761 11.517  1.00 11.05  ? 149 VAL A CB  1 
ATOM   1249 C  CG1 . VAL A 1 149 ? 5.888   -17.569 10.292  1.00 13.65  ? 149 VAL A CG1 1 
ATOM   1250 C  CG2 . VAL A 1 149 ? 7.489   -15.834 11.096  1.00 13.12  ? 149 VAL A CG2 1 
ATOM   1251 N  N   . GLY A 1 150 ? 2.901   -16.626 11.579  1.00 10.63  ? 150 GLY A N   1 
ATOM   1252 C  CA  . GLY A 1 150 ? 1.704   -17.433 11.626  1.00 12.26  ? 150 GLY A CA  1 
ATOM   1253 C  C   . GLY A 1 150 ? 0.809   -16.977 10.475  1.00 11.43  ? 150 GLY A C   1 
ATOM   1254 O  O   . GLY A 1 150 ? 1.183   -17.086 9.300   1.00 12.88  ? 150 GLY A O   1 
ATOM   1255 N  N   A SER A 1 151 ? -0.426  -16.498 10.780  0.50 11.79  ? 151 SER A N   1 
ATOM   1256 N  N   B SER A 1 151 ? -0.402  -16.465 10.816  0.50 12.43  ? 151 SER A N   1 
ATOM   1257 C  CA  A SER A 1 151 ? -1.328  -15.970 9.747   0.50 11.61  ? 151 SER A CA  1 
ATOM   1258 C  CA  B SER A 1 151 ? -1.297  -15.871 9.818   0.50 12.56  ? 151 SER A CA  1 
ATOM   1259 C  C   A SER A 1 151 ? -0.780  -14.638 9.221   0.50 10.87  ? 151 SER A C   1 
ATOM   1260 C  C   B SER A 1 151 ? -0.623  -14.662 9.172   0.50 11.55  ? 151 SER A C   1 
ATOM   1261 O  O   A SER A 1 151 ? -0.128  -13.876 9.941   0.50 9.14   ? 151 SER A O   1 
ATOM   1262 O  O   B SER A 1 151 ? 0.256   -14.027 9.758   0.50 12.44  ? 151 SER A O   1 
ATOM   1263 C  CB  A SER A 1 151 ? -2.727  -15.805 10.269  0.50 14.77  ? 151 SER A CB  1 
ATOM   1264 C  CB  B SER A 1 151 ? -2.633  -15.506 10.398  0.50 16.44  ? 151 SER A CB  1 
ATOM   1265 O  OG  A SER A 1 151 ? -2.712  -14.711 11.168  0.50 16.33  ? 151 SER A OG  1 
ATOM   1266 O  OG  B SER A 1 151 ? -3.246  -16.681 10.861  0.50 17.60  ? 151 SER A OG  1 
ATOM   1267 N  N   . ALA A 1 152 ? -1.026  -14.342 7.946   1.00 11.20  ? 152 ALA A N   1 
ATOM   1268 C  CA  . ALA A 1 152 ? -0.611  -13.116 7.305   1.00 11.23  ? 152 ALA A CA  1 
ATOM   1269 C  C   . ALA A 1 152 ? -1.227  -11.909 8.016   1.00 10.26  ? 152 ALA A C   1 
ATOM   1270 O  O   . ALA A 1 152 ? -2.347  -11.963 8.531   1.00 12.97  ? 152 ALA A O   1 
ATOM   1271 C  CB  . ALA A 1 152 ? -1.069  -13.088 5.850   1.00 13.11  ? 152 ALA A CB  1 
ATOM   1272 N  N   . LYS A 1 153 ? -0.520  -10.773 7.930   1.00 11.03  ? 153 LYS A N   1 
ATOM   1273 C  CA  . LYS A 1 153 ? -1.073  -9.508  8.410   1.00 11.89  ? 153 LYS A CA  1 
ATOM   1274 C  C   . LYS A 1 153 ? -1.533  -8.704  7.196   1.00 11.78  ? 153 LYS A C   1 
ATOM   1275 O  O   . LYS A 1 153 ? -0.688  -8.238  6.398   1.00 10.83  ? 153 LYS A O   1 
ATOM   1276 C  CB  . LYS A 1 153 ? 0.008   -8.747  9.192   1.00 11.88  ? 153 LYS A CB  1 
ATOM   1277 C  CG  . LYS A 1 153 ? -0.531  -7.516  9.952   1.00 13.08  ? 153 LYS A CG  1 
ATOM   1278 C  CD  . LYS A 1 153 ? -1.417  -7.900  11.152  1.00 13.30  ? 153 LYS A CD  1 
ATOM   1279 C  CE  . LYS A 1 153 ? -1.596  -6.689  12.055  1.00 17.86  ? 153 LYS A CE  1 
ATOM   1280 N  NZ  . LYS A 1 153 ? -2.557  -7.009  13.131  1.00 22.06  ? 153 LYS A NZ  1 
ATOM   1281 N  N   . PRO A 1 154 ? -2.849  -8.575  6.938   1.00 11.59  ? 154 PRO A N   1 
ATOM   1282 C  CA  . PRO A 1 154 ? -3.259  -7.953  5.670   1.00 12.98  ? 154 PRO A CA  1 
ATOM   1283 C  C   . PRO A 1 154 ? -2.734  -6.529  5.566   1.00 11.88  ? 154 PRO A C   1 
ATOM   1284 O  O   . PRO A 1 154 ? -2.325  -6.125  4.473   1.00 13.86  ? 154 PRO A O   1 
ATOM   1285 C  CB  . PRO A 1 154 ? -4.816  -7.950  5.787   1.00 15.45  ? 154 PRO A CB  1 
ATOM   1286 C  CG  . PRO A 1 154 ? -5.082  -9.174  6.657   1.00 18.16  ? 154 PRO A CG  1 
ATOM   1287 C  CD  . PRO A 1 154 ? -3.988  -9.175  7.699   1.00 13.60  ? 154 PRO A CD  1 
ATOM   1288 N  N   . GLY A 1 155 ? -2.648  -5.792  6.693   1.00 11.97  ? 155 GLY A N   1 
ATOM   1289 C  CA  . GLY A 1 155 ? -2.224  -4.391  6.648   1.00 13.14  ? 155 GLY A CA  1 
ATOM   1290 C  C   . GLY A 1 155 ? -0.727  -4.214  6.398   1.00 11.61  ? 155 GLY A C   1 
ATOM   1291 O  O   . GLY A 1 155 ? -0.291  -3.113  6.211   1.00 15.53  ? 155 GLY A O   1 
ATOM   1292 N  N   . LEU A 1 156 ? 0.012   -5.326  6.396   1.00 10.55  ? 156 LEU A N   1 
ATOM   1293 C  CA  . LEU A 1 156 ? 1.422   -5.304  6.042   1.00 9.42   ? 156 LEU A CA  1 
ATOM   1294 C  C   . LEU A 1 156 ? 1.680   -5.550  4.561   1.00 9.42   ? 156 LEU A C   1 
ATOM   1295 O  O   . LEU A 1 156 ? 2.785   -5.263  4.034   1.00 10.12  ? 156 LEU A O   1 
ATOM   1296 C  CB  . LEU A 1 156 ? 2.186   -6.343  6.869   1.00 10.51  ? 156 LEU A CB  1 
ATOM   1297 C  CG  . LEU A 1 156 ? 3.706   -6.472  6.717   1.00 10.49  ? 156 LEU A CG  1 
ATOM   1298 C  CD1 . LEU A 1 156 ? 4.408   -5.179  7.110   1.00 12.04  ? 156 LEU A CD1 1 
ATOM   1299 C  CD2 . LEU A 1 156 ? 4.234   -7.657  7.561   1.00 11.45  ? 156 LEU A CD2 1 
ATOM   1300 N  N   . GLN A 1 157 ? 0.697   -6.110  3.863   1.00 11.06  ? 157 GLN A N   1 
ATOM   1301 C  CA  . GLN A 1 157 ? 1.016   -6.589  2.518   1.00 11.78  ? 157 GLN A CA  1 
ATOM   1302 C  C   . GLN A 1 157 ? 1.419   -5.452  1.582   1.00 11.63  ? 157 GLN A C   1 
ATOM   1303 O  O   . GLN A 1 157 ? 2.291   -5.694  0.737   1.00 11.78  ? 157 GLN A O   1 
ATOM   1304 C  CB  . GLN A 1 157 ? -0.116  -7.430  1.933   1.00 12.77  ? 157 GLN A CB  1 
ATOM   1305 C  CG  . GLN A 1 157 ? 0.280   -8.189  0.646   1.00 14.80  ? 157 GLN A CG  1 
ATOM   1306 C  CD  . GLN A 1 157 ? 1.423   -9.155  0.846   1.00 13.20  ? 157 GLN A CD  1 
ATOM   1307 O  OE1 . GLN A 1 157 ? 1.621   -9.731  1.941   1.00 13.49  ? 157 GLN A OE1 1 
ATOM   1308 N  NE2 . GLN A 1 157 ? 2.244   -9.384  -0.180  1.00 15.54  ? 157 GLN A NE2 1 
ATOM   1309 N  N   . LYS A 1 158 ? 0.849   -4.246  1.687   1.00 11.66  ? 158 LYS A N   1 
ATOM   1310 C  CA  . LYS A 1 158 ? 1.258   -3.187  0.787   1.00 12.39  ? 158 LYS A CA  1 
ATOM   1311 C  C   . LYS A 1 158 ? 2.747   -2.872  0.953   1.00 11.41  ? 158 LYS A C   1 
ATOM   1312 O  O   . LYS A 1 158 ? 3.420   -2.471  -0.008  1.00 12.19  ? 158 LYS A O   1 
ATOM   1313 C  CB  . LYS A 1 158 ? 0.368   -1.964  1.016   1.00 15.15  ? 158 LYS A CB  1 
ATOM   1314 N  N   . VAL A 1 159 ? 3.221   -2.972  2.204   1.00 10.91  ? 159 VAL A N   1 
ATOM   1315 C  CA  . VAL A 1 159 ? 4.660   -2.782  2.448   1.00 10.37  ? 159 VAL A CA  1 
ATOM   1316 C  C   . VAL A 1 159 ? 5.475   -3.872  1.776   1.00 10.63  ? 159 VAL A C   1 
ATOM   1317 O  O   . VAL A 1 159 ? 6.413   -3.623  1.029   1.00 11.31  ? 159 VAL A O   1 
ATOM   1318 C  CB  . VAL A 1 159 ? 4.939   -2.766  3.952   1.00 10.61  ? 159 VAL A CB  1 
ATOM   1319 C  CG1 . VAL A 1 159 ? 6.449   -2.748  4.215   1.00 12.26  ? 159 VAL A CG1 1 
ATOM   1320 C  CG2 . VAL A 1 159 ? 4.238   -1.620  4.632   1.00 12.87  ? 159 VAL A CG2 1 
ATOM   1321 N  N   . VAL A 1 160 ? 5.111   -5.145  2.012   1.00 10.04  ? 160 VAL A N   1 
ATOM   1322 C  CA  . VAL A 1 160 ? 5.831   -6.270  1.433   1.00 12.45  ? 160 VAL A CA  1 
ATOM   1323 C  C   . VAL A 1 160 ? 5.872   -6.145  -0.080  1.00 11.91  ? 160 VAL A C   1 
ATOM   1324 O  O   . VAL A 1 160 ? 6.909   -6.412  -0.689  1.00 12.65  ? 160 VAL A O   1 
ATOM   1325 C  CB  . VAL A 1 160 ? 5.101   -7.596  1.873   1.00 13.57  ? 160 VAL A CB  1 
ATOM   1326 C  CG1 . VAL A 1 160 ? 5.504   -8.766  1.043   1.00 15.09  ? 160 VAL A CG1 1 
ATOM   1327 C  CG2 . VAL A 1 160 ? 5.300   -7.827  3.361   1.00 14.84  ? 160 VAL A CG2 1 
ATOM   1328 N  N   . ASP A 1 161 ? 4.757   -5.744  -0.719  1.00 13.29  ? 161 ASP A N   1 
ATOM   1329 C  CA  . ASP A 1 161 ? 4.733   -5.771  -2.173  1.00 14.71  ? 161 ASP A CA  1 
ATOM   1330 C  C   . ASP A 1 161 ? 5.576   -4.683  -2.822  1.00 14.74  ? 161 ASP A C   1 
ATOM   1331 O  O   . ASP A 1 161 ? 5.876   -4.821  -4.003  1.00 20.99  ? 161 ASP A O   1 
ATOM   1332 C  CB  . ASP A 1 161 ? 3.292   -5.616  -2.600  1.00 18.59  ? 161 ASP A CB  1 
ATOM   1333 C  CG  . ASP A 1 161 ? 2.677   -7.000  -2.619  1.00 22.14  ? 161 ASP A CG  1 
ATOM   1334 O  OD1 . ASP A 1 161 ? 3.433   -8.016  -2.759  1.00 24.46  ? 161 ASP A OD1 1 
ATOM   1335 O  OD2 . ASP A 1 161 ? 1.520   -7.042  -2.440  1.00 23.61  ? 161 ASP A OD2 1 
ATOM   1336 N  N   . VAL A 1 162 ? 6.014   -3.635  -2.119  1.00 13.15  ? 162 VAL A N   1 
ATOM   1337 C  CA  . VAL A 1 162 ? 6.823   -2.600  -2.734  1.00 13.92  ? 162 VAL A CA  1 
ATOM   1338 C  C   . VAL A 1 162 ? 8.301   -2.890  -2.485  1.00 12.51  ? 162 VAL A C   1 
ATOM   1339 O  O   . VAL A 1 162 ? 9.155   -2.217  -3.044  1.00 13.19  ? 162 VAL A O   1 
ATOM   1340 C  CB  . VAL A 1 162 ? 6.448   -1.208  -2.173  1.00 15.71  ? 162 VAL A CB  1 
ATOM   1341 C  CG1 . VAL A 1 162 ? 6.952   -0.982  -0.783  1.00 16.03  ? 162 VAL A CG1 1 
ATOM   1342 C  CG2 . VAL A 1 162 ? 6.758   -0.006  -3.043  1.00 18.45  ? 162 VAL A CG2 1 
ATOM   1343 N  N   . LEU A 1 163 ? 8.637   -3.907  -1.654  1.00 11.97  ? 163 LEU A N   1 
ATOM   1344 C  CA  . LEU A 1 163 ? 10.045  -4.085  -1.326  1.00 10.75  ? 163 LEU A CA  1 
ATOM   1345 C  C   . LEU A 1 163 ? 10.939  -4.427  -2.516  1.00 13.09  ? 163 LEU A C   1 
ATOM   1346 O  O   . LEU A 1 163 ? 12.119  -4.017  -2.531  1.00 12.88  ? 163 LEU A O   1 
ATOM   1347 C  CB  . LEU A 1 163 ? 10.246  -5.126  -0.225  1.00 11.62  ? 163 LEU A CB  1 
ATOM   1348 C  CG  . LEU A 1 163 ? 9.564   -4.803  1.128   1.00 11.62  ? 163 LEU A CG  1 
ATOM   1349 C  CD1 . LEU A 1 163 ? 9.874   -5.940  2.094   1.00 13.94  ? 163 LEU A CD1 1 
ATOM   1350 C  CD2 . LEU A 1 163 ? 10.050  -3.496  1.685   1.00 12.25  ? 163 LEU A CD2 1 
ATOM   1351 N  N   . ASP A 1 164 ? 10.405  -5.102  -3.526  1.00 14.82  ? 164 ASP A N   1 
ATOM   1352 C  CA  . ASP A 1 164 ? 11.234  -5.382  -4.703  1.00 18.74  ? 164 ASP A CA  1 
ATOM   1353 C  C   . ASP A 1 164 ? 11.692  -4.085  -5.364  1.00 17.13  ? 164 ASP A C   1 
ATOM   1354 O  O   . ASP A 1 164 ? 12.639  -4.160  -6.140  1.00 21.60  ? 164 ASP A O   1 
ATOM   1355 C  CB  . ASP A 1 164 ? 10.478  -6.303  -5.684  1.00 23.46  ? 164 ASP A CB  1 
ATOM   1356 C  CG  . ASP A 1 164 ? 9.519   -5.499  -6.537  1.00 29.05  ? 164 ASP A CG  1 
ATOM   1357 O  OD1 . ASP A 1 164 ? 8.562   -4.974  -5.969  1.00 34.64  ? 164 ASP A OD1 1 
ATOM   1358 O  OD2 . ASP A 1 164 ? 9.743   -5.370  -7.809  1.00 38.44  ? 164 ASP A OD2 1 
ATOM   1359 N  N   . SER A 1 165 ? 10.989  -2.960  -5.203  1.00 14.56  ? 165 SER A N   1 
ATOM   1360 C  CA  . SER A 1 165 ? 11.399  -1.712  -5.847  1.00 16.11  ? 165 SER A CA  1 
ATOM   1361 C  C   . SER A 1 165 ? 12.430  -0.942  -5.031  1.00 13.41  ? 165 SER A C   1 
ATOM   1362 O  O   . SER A 1 165 ? 12.935  0.075   -5.504  1.00 15.27  ? 165 SER A O   1 
ATOM   1363 C  CB  . SER A 1 165 ? 10.194  -0.874  -6.117  1.00 18.60  ? 165 SER A CB  1 
ATOM   1364 O  OG  . SER A 1 165 ? 9.681   -0.325  -4.930  1.00 17.32  ? 165 SER A OG  1 
ATOM   1365 N  N   . ILE A 1 166 ? 12.756  -1.418  -3.808  1.00 12.35  ? 166 ILE A N   1 
ATOM   1366 C  CA  . ILE A 1 166 ? 13.768  -0.779  -2.981  1.00 12.06  ? 166 ILE A CA  1 
ATOM   1367 C  C   . ILE A 1 166 ? 14.792  -1.827  -2.513  1.00 10.28  ? 166 ILE A C   1 
ATOM   1368 O  O   . ILE A 1 166 ? 15.202  -1.859  -1.341  1.00 11.65  ? 166 ILE A O   1 
ATOM   1369 C  CB  . ILE A 1 166 ? 13.170  0.047   -1.830  1.00 11.59  ? 166 ILE A CB  1 
ATOM   1370 C  CG1 . ILE A 1 166 ? 12.305  -0.827  -0.899  1.00 11.15  ? 166 ILE A CG1 1 
ATOM   1371 C  CG2 . ILE A 1 166 ? 12.386  1.261   -2.348  1.00 13.71  ? 166 ILE A CG2 1 
ATOM   1372 C  CD1 . ILE A 1 166 ? 12.299  -0.294  0.572   1.00 12.75  ? 166 ILE A CD1 1 
ATOM   1373 N  N   . LYS A 1 167 ? 15.228  -2.675  -3.439  1.00 11.27  ? 167 LYS A N   1 
ATOM   1374 C  CA  . LYS A 1 167 ? 16.001  -3.838  -3.032  1.00 11.84  ? 167 LYS A CA  1 
ATOM   1375 C  C   . LYS A 1 167 ? 17.297  -3.445  -2.345  1.00 10.50  ? 167 LYS A C   1 
ATOM   1376 O  O   . LYS A 1 167 ? 17.748  -4.113  -1.426  1.00 11.30  ? 167 LYS A O   1 
ATOM   1377 C  CB  . LYS A 1 167 ? 16.260  -4.757  -4.231  1.00 12.62  ? 167 LYS A CB  1 
ATOM   1378 C  CG  . LYS A 1 167 ? 17.017  -6.033  -3.828  1.00 14.90  ? 167 LYS A CG  1 
ATOM   1379 C  CD  . LYS A 1 167 ? 17.262  -6.965  -5.047  1.00 21.32  ? 167 LYS A CD  1 
ATOM   1380 C  CE  . LYS A 1 167 ? 18.075  -8.199  -4.702  1.00 28.69  ? 167 LYS A CE  1 
ATOM   1381 N  NZ  . LYS A 1 167 ? 18.141  -9.118  -5.869  1.00 41.47  ? 167 LYS A NZ  1 
ATOM   1382 N  N   . THR A 1 168 ? 17.945  -2.380  -2.828  1.00 10.74  ? 168 THR A N   1 
ATOM   1383 C  CA  . THR A 1 168 ? 19.312  -2.065  -2.456  1.00 11.14  ? 168 THR A CA  1 
ATOM   1384 C  C   . THR A 1 168 ? 19.401  -0.694  -1.797  1.00 9.87   ? 168 THR A C   1 
ATOM   1385 O  O   . THR A 1 168 ? 18.482  0.155   -1.847  1.00 11.50  ? 168 THR A O   1 
ATOM   1386 C  CB  . THR A 1 168 ? 20.226  -2.091  -3.689  1.00 11.75  ? 168 THR A CB  1 
ATOM   1387 O  OG1 . THR A 1 168 ? 19.668  -1.296  -4.734  1.00 13.35  ? 168 THR A OG1 1 
ATOM   1388 C  CG2 . THR A 1 168 ? 20.440  -3.496  -4.215  1.00 13.22  ? 168 THR A CG2 1 
ATOM   1389 N  N   . LYS A 1 169 ? 20.478  -0.541  -1.020  1.00 11.68  ? 169 LYS A N   1 
ATOM   1390 C  CA  . LYS A 1 169 ? 20.752  0.632   -0.227  1.00 10.85  ? 169 LYS A CA  1 
ATOM   1391 C  C   . LYS A 1 169 ? 20.576  1.904   -1.021  1.00 11.30  ? 169 LYS A C   1 
ATOM   1392 O  O   . LYS A 1 169 ? 21.134  2.053   -2.107  1.00 14.53  ? 169 LYS A O   1 
ATOM   1393 C  CB  . LYS A 1 169 ? 22.202  0.592   0.263   1.00 11.73  ? 169 LYS A CB  1 
ATOM   1394 C  CG  . LYS A 1 169 ? 22.598  1.807   1.133   1.00 13.84  ? 169 LYS A CG  1 
ATOM   1395 C  CD  . LYS A 1 169 ? 23.948  1.592   1.761   1.00 17.48  ? 169 LYS A CD  1 
ATOM   1396 N  N   . GLY A 1 170 ? 19.795  2.829   -0.475  1.00 12.09  ? 170 GLY A N   1 
ATOM   1397 C  CA  . GLY A 1 170 ? 19.619  4.131   -1.093  1.00 13.42  ? 170 GLY A CA  1 
ATOM   1398 C  C   . GLY A 1 170 ? 18.449  4.224   -2.048  1.00 13.78  ? 170 GLY A C   1 
ATOM   1399 O  O   . GLY A 1 170 ? 18.166  5.329   -2.551  1.00 16.40  ? 170 GLY A O   1 
ATOM   1400 N  N   . LYS A 1 171 ? 17.794  3.113   -2.377  1.00 11.72  ? 171 LYS A N   1 
ATOM   1401 C  CA  . LYS A 1 171 ? 16.583  3.167   -3.171  1.00 12.55  ? 171 LYS A CA  1 
ATOM   1402 C  C   . LYS A 1 171 ? 15.373  3.591   -2.329  1.00 11.55  ? 171 LYS A C   1 
ATOM   1403 O  O   . LYS A 1 171 ? 15.195  3.107   -1.218  1.00 11.89  ? 171 LYS A O   1 
ATOM   1404 C  CB  . LYS A 1 171 ? 16.284  1.822   -3.845  1.00 13.68  ? 171 LYS A CB  1 
ATOM   1405 C  CG  . LYS A 1 171 ? 17.344  1.432   -4.902  1.00 16.47  ? 171 LYS A CG  1 
ATOM   1406 C  CD  . LYS A 1 171 ? 16.815  0.336   -5.801  1.00 22.49  ? 171 LYS A CD  1 
ATOM   1407 N  N   . SER A 1 172 ? 14.556  4.494   -2.871  1.00 13.26  ? 172 SER A N   1 
ATOM   1408 C  CA  . SER A 1 172 ? 13.310  4.923   -2.297  1.00 13.69  ? 172 SER A CA  1 
ATOM   1409 C  C   . SER A 1 172 ? 12.186  4.741   -3.318  1.00 12.08  ? 172 SER A C   1 
ATOM   1410 O  O   . SER A 1 172 ? 12.397  4.709   -4.525  1.00 14.94  ? 172 SER A O   1 
ATOM   1411 C  CB  . SER A 1 172 ? 13.416  6.340   -1.714  1.00 14.96  ? 172 SER A CB  1 
ATOM   1412 O  OG  . SER A 1 172 ? 13.560  7.270   -2.752  1.00 17.22  ? 172 SER A OG  1 
ATOM   1413 N  N   . ALA A 1 173 ? 10.949  4.744   -2.828  1.00 12.96  ? 173 ALA A N   1 
ATOM   1414 C  CA  . ALA A 1 173 ? 9.773   4.709   -3.683  1.00 13.48  ? 173 ALA A CA  1 
ATOM   1415 C  C   . ALA A 1 173 ? 8.664   5.490   -3.000  1.00 13.01  ? 173 ALA A C   1 
ATOM   1416 O  O   . ALA A 1 173 ? 8.568   5.557   -1.764  1.00 12.29  ? 173 ALA A O   1 
ATOM   1417 C  CB  . ALA A 1 173 ? 9.310   3.284   -3.911  1.00 16.76  ? 173 ALA A CB  1 
ATOM   1418 N  N   . ASP A 1 174 ? 7.786   6.111   -3.782  1.00 14.22  ? 174 ASP A N   1 
ATOM   1419 C  CA  . ASP A 1 174 ? 6.610   6.754   -3.215  1.00 14.33  ? 174 ASP A CA  1 
ATOM   1420 C  C   . ASP A 1 174 ? 5.861   5.707   -2.421  1.00 13.72  ? 174 ASP A C   1 
ATOM   1421 O  O   . ASP A 1 174 ? 5.701   4.538   -2.789  1.00 17.41  ? 174 ASP A O   1 
ATOM   1422 C  CB  . ASP A 1 174 ? 5.761   7.415   -4.326  1.00 20.31  ? 174 ASP A CB  1 
ATOM   1423 C  CG  . ASP A 1 174 ? 6.476   8.515   -5.119  1.00 34.76  ? 174 ASP A CG  1 
ATOM   1424 O  OD1 . ASP A 1 174 ? 7.103   9.469   -4.502  1.00 38.45  ? 174 ASP A OD1 1 
ATOM   1425 O  OD2 . ASP A 1 174 ? 6.393   8.443   -6.379  1.00 49.34  ? 174 ASP A OD2 1 
ATOM   1426 N  N   . PHE A 1 175 ? 5.282   6.166   -1.324  1.00 11.75  ? 175 PHE A N   1 
ATOM   1427 C  CA  . PHE A 1 175 ? 4.536   5.247   -0.490  1.00 11.22  ? 175 PHE A CA  1 
ATOM   1428 C  C   . PHE A 1 175 ? 3.473   6.034   0.242   1.00 10.66  ? 175 PHE A C   1 
ATOM   1429 O  O   . PHE A 1 175 ? 3.468   6.181   1.470   1.00 15.90  ? 175 PHE A O   1 
ATOM   1430 C  CB  . PHE A 1 175 ? 5.461   4.452   0.453   1.00 12.39  ? 175 PHE A CB  1 
ATOM   1431 C  CG  . PHE A 1 175 ? 4.823   3.168   0.938   1.00 12.50  ? 175 PHE A CG  1 
ATOM   1432 C  CD1 . PHE A 1 175 ? 4.616   2.090   0.087   1.00 13.57  ? 175 PHE A CD1 1 
ATOM   1433 C  CD2 . PHE A 1 175 ? 4.458   3.029   2.276   1.00 13.71  ? 175 PHE A CD2 1 
ATOM   1434 C  CE1 . PHE A 1 175 ? 4.028   0.914   0.531   1.00 14.10  ? 175 PHE A CE1 1 
ATOM   1435 C  CE2 . PHE A 1 175 ? 3.889   1.832   2.739   1.00 13.22  ? 175 PHE A CE2 1 
ATOM   1436 C  CZ  . PHE A 1 175 ? 3.658   0.795   1.850   1.00 13.33  ? 175 PHE A CZ  1 
ATOM   1437 N  N   . THR A 1 176 ? 2.534   6.563   -0.535  1.00 11.55  ? 176 THR A N   1 
ATOM   1438 C  CA  . THR A 1 176 ? 1.472   7.388   0.007   1.00 10.74  ? 176 THR A CA  1 
ATOM   1439 C  C   . THR A 1 176 ? 0.258   6.576   0.385   1.00 9.49   ? 176 THR A C   1 
ATOM   1440 O  O   . THR A 1 176 ? 0.087   5.447   -0.068  1.00 11.38  ? 176 THR A O   1 
ATOM   1441 C  CB  . THR A 1 176 ? 1.121   8.462   -1.026  1.00 12.47  ? 176 THR A CB  1 
ATOM   1442 O  OG1 . THR A 1 176 ? 0.800   7.861   -2.267  1.00 18.16  ? 176 THR A OG1 1 
ATOM   1443 C  CG2 . THR A 1 176 ? 2.212   9.515   -1.117  1.00 18.82  ? 176 THR A CG2 1 
ATOM   1444 N  N   . ASN A 1 177 ? -0.580  7.171   1.245   1.00 10.40  ? 177 ASN A N   1 
ATOM   1445 C  CA  . ASN A 1 177 ? -1.873  6.614   1.612   1.00 10.78  ? 177 ASN A CA  1 
ATOM   1446 C  C   . ASN A 1 177 ? -1.740  5.275   2.330   1.00 10.81  ? 177 ASN A C   1 
ATOM   1447 O  O   . ASN A 1 177 ? -2.646  4.476   2.264   1.00 16.81  ? 177 ASN A O   1 
ATOM   1448 C  CB  . ASN A 1 177 ? -2.786  6.499   0.403   1.00 11.94  ? 177 ASN A CB  1 
ATOM   1449 C  CG  . ASN A 1 177 ? -2.990  7.871   -0.199  1.00 12.35  ? 177 ASN A CG  1 
ATOM   1450 O  OD1 . ASN A 1 177 ? -3.622  8.770   0.397   1.00 15.21  ? 177 ASN A OD1 1 
ATOM   1451 N  ND2 . ASN A 1 177 ? -2.406  8.095   -1.371  1.00 12.65  ? 177 ASN A ND2 1 
ATOM   1452 N  N   . PHE A 1 178 ? -0.672  5.064   3.050   1.00 9.69   ? 178 PHE A N   1 
ATOM   1453 C  CA  . PHE A 1 178 ? -0.567  3.857   3.865   1.00 10.01  ? 178 PHE A CA  1 
ATOM   1454 C  C   . PHE A 1 178 ? -1.037  4.126   5.295   1.00 9.69   ? 178 PHE A C   1 
ATOM   1455 O  O   . PHE A 1 178 ? -0.626  5.112   5.860   1.00 11.73  ? 178 PHE A O   1 
ATOM   1456 C  CB  . PHE A 1 178 ? 0.897   3.379   3.908   1.00 10.89  ? 178 PHE A CB  1 
ATOM   1457 C  CG  . PHE A 1 178 ? 1.026   2.116   4.735   1.00 10.94  ? 178 PHE A CG  1 
ATOM   1458 C  CD1 . PHE A 1 178 ? 0.648   0.891   4.219   1.00 12.77  ? 178 PHE A CD1 1 
ATOM   1459 C  CD2 . PHE A 1 178 ? 1.458   2.180   6.074   1.00 11.05  ? 178 PHE A CD2 1 
ATOM   1460 C  CE1 . PHE A 1 178 ? 0.681   -0.259  4.978   1.00 12.92  ? 178 PHE A CE1 1 
ATOM   1461 C  CE2 . PHE A 1 178 ? 1.502   1.023   6.851   1.00 10.97  ? 178 PHE A CE2 1 
ATOM   1462 C  CZ  . PHE A 1 178 ? 1.151   -0.194  6.293   1.00 11.69  ? 178 PHE A CZ  1 
ATOM   1463 N  N   . ASP A 1 179 ? -1.907  3.303   5.838   1.00 10.01  ? 179 ASP A N   1 
ATOM   1464 C  CA  . ASP A 1 179 ? -2.470  3.517   7.150   1.00 11.40  ? 179 ASP A CA  1 
ATOM   1465 C  C   . ASP A 1 179 ? -1.787  2.625   8.173   1.00 10.22  ? 179 ASP A C   1 
ATOM   1466 O  O   . ASP A 1 179 ? -1.978  1.406   8.186   1.00 11.10  ? 179 ASP A O   1 
ATOM   1467 C  CB  . ASP A 1 179 ? -3.954  3.145   7.048   1.00 13.23  ? 179 ASP A CB  1 
ATOM   1468 C  CG  . ASP A 1 179 ? -4.703  3.495   8.312   1.00 14.49  ? 179 ASP A CG  1 
ATOM   1469 O  OD1 . ASP A 1 179 ? -4.085  3.720   9.395   1.00 13.00  ? 179 ASP A OD1 1 
ATOM   1470 O  OD2 . ASP A 1 179 ? -5.916  3.513   8.236   1.00 22.98  ? 179 ASP A OD2 1 
ATOM   1471 N  N   . PRO A 1 180 ? -0.963  3.185   9.093   1.00 9.89   ? 180 PRO A N   1 
ATOM   1472 C  CA  . PRO A 1 180 ? -0.205  2.339   10.027  1.00 9.93   ? 180 PRO A CA  1 
ATOM   1473 C  C   . PRO A 1 180 ? -1.103  1.708   11.078  1.00 9.51   ? 180 PRO A C   1 
ATOM   1474 O  O   . PRO A 1 180 ? -0.650  0.814   11.779  1.00 10.35  ? 180 PRO A O   1 
ATOM   1475 C  CB  . PRO A 1 180 ? 0.791   3.291   10.624  1.00 11.66  ? 180 PRO A CB  1 
ATOM   1476 C  CG  . PRO A 1 180 ? 0.140   4.669   10.486  1.00 11.26  ? 180 PRO A CG  1 
ATOM   1477 C  CD  . PRO A 1 180 ? -0.621  4.606   9.193   1.00 10.68  ? 180 PRO A CD  1 
ATOM   1478 N  N   . ARG A 1 181 ? -2.390  2.099   11.155  1.00 9.82   ? 181 ARG A N   1 
ATOM   1479 C  CA  . ARG A 1 181 ? -3.299  1.437   12.083  1.00 10.77  ? 181 ARG A CA  1 
ATOM   1480 C  C   . ARG A 1 181 ? -3.414  -0.040  11.740  1.00 10.69  ? 181 ARG A C   1 
ATOM   1481 O  O   . ARG A 1 181 ? -3.745  -0.846  12.616  1.00 11.59  ? 181 ARG A O   1 
ATOM   1482 C  CB  . ARG A 1 181 ? -4.680  2.105   12.102  1.00 12.30  ? 181 ARG A CB  1 
ATOM   1483 C  CG  . ARG A 1 181 ? -4.580  3.512   12.648  1.00 13.29  ? 181 ARG A CG  1 
ATOM   1484 C  CD  . ARG A 1 181 ? -5.907  4.223   12.605  1.00 14.65  ? 181 ARG A CD  1 
ATOM   1485 N  NE  . ARG A 1 181 ? -6.285  4.475   11.228  1.00 14.70  ? 181 ARG A NE  1 
ATOM   1486 C  CZ  . ARG A 1 181 ? -7.339  5.192   10.857  1.00 16.84  ? 181 ARG A CZ  1 
ATOM   1487 N  NH1 . ARG A 1 181 ? -8.127  5.732   11.770  1.00 21.83  ? 181 ARG A NH1 1 
ATOM   1488 N  NH2 . ARG A 1 181 ? -7.602  5.367   9.574   1.00 20.26  ? 181 ARG A NH2 1 
ATOM   1489 N  N   . GLY A 1 182 ? -3.192  -0.409  10.468  1.00 11.16  ? 182 GLY A N   1 
ATOM   1490 C  CA  . GLY A 1 182 ? -3.281  -1.813  10.073  1.00 11.28  ? 182 GLY A CA  1 
ATOM   1491 C  C   . GLY A 1 182 ? -2.119  -2.695  10.558  1.00 10.91  ? 182 GLY A C   1 
ATOM   1492 O  O   . GLY A 1 182 ? -2.136  -3.893  10.279  1.00 14.19  ? 182 GLY A O   1 
ATOM   1493 N  N   . LEU A 1 183 ? -1.171  -2.084  11.267  1.00 10.30  ? 183 LEU A N   1 
ATOM   1494 C  CA  . LEU A 1 183 ? -0.042  -2.825  11.801  1.00 10.51  ? 183 LEU A CA  1 
ATOM   1495 C  C   . LEU A 1 183 ? -0.160  -3.087  13.302  1.00 9.80   ? 183 LEU A C   1 
ATOM   1496 O  O   . LEU A 1 183 ? 0.745   -3.665  13.915  1.00 12.66  ? 183 LEU A O   1 
ATOM   1497 C  CB  . LEU A 1 183 ? 1.298   -2.114  11.510  1.00 10.74  ? 183 LEU A CB  1 
ATOM   1498 C  CG  . LEU A 1 183 ? 1.598   -1.963  10.013  1.00 12.03  ? 183 LEU A CG  1 
ATOM   1499 C  CD1 . LEU A 1 183 ? 2.850   -1.127  9.798   1.00 15.28  ? 183 LEU A CD1 1 
ATOM   1500 C  CD2 . LEU A 1 183 ? 1.699   -3.311  9.319   1.00 15.57  ? 183 LEU A CD2 1 
ATOM   1501 N  N   . LEU A 1 184 ? -1.213  -2.585  13.951  1.00 10.29  ? 184 LEU A N   1 
ATOM   1502 C  CA  . LEU A 1 184 ? -1.343  -2.664  15.401  1.00 11.34  ? 184 LEU A CA  1 
ATOM   1503 C  C   . LEU A 1 184 ? -2.066  -3.946  15.813  1.00 12.33  ? 184 LEU A C   1 
ATOM   1504 O  O   . LEU A 1 184 ? -3.045  -4.355  15.208  1.00 19.54  ? 184 LEU A O   1 
ATOM   1505 C  CB  . LEU A 1 184 ? -2.161  -1.451  15.890  1.00 12.31  ? 184 LEU A CB  1 
ATOM   1506 C  CG  . LEU A 1 184 ? -1.566  -0.101  15.493  1.00 12.68  ? 184 LEU A CG  1 
ATOM   1507 C  CD1 . LEU A 1 184 ? -2.416  1.051   16.030  1.00 15.20  ? 184 LEU A CD1 1 
ATOM   1508 C  CD2 . LEU A 1 184 ? -0.156  -0.006  15.995  1.00 16.71  ? 184 LEU A CD2 1 
ATOM   1509 N  N   . PRO A 1 185 ? -1.704  -4.535  16.966  1.00 10.05  ? 185 PRO A N   1 
ATOM   1510 C  CA  . PRO A 1 185 ? -2.489  -5.649  17.515  1.00 10.94  ? 185 PRO A CA  1 
ATOM   1511 C  C   . PRO A 1 185 ? -3.749  -5.092  18.148  1.00 11.38  ? 185 PRO A C   1 
ATOM   1512 O  O   . PRO A 1 185 ? -3.968  -3.892  18.234  1.00 12.79  ? 185 PRO A O   1 
ATOM   1513 C  CB  . PRO A 1 185 ? -1.514  -6.251  18.540  1.00 10.96  ? 185 PRO A CB  1 
ATOM   1514 C  CG  . PRO A 1 185 ? -0.789  -5.042  19.032  1.00 10.62  ? 185 PRO A CG  1 
ATOM   1515 C  CD  . PRO A 1 185 ? -0.589  -4.124  17.806  1.00 9.46   ? 185 PRO A CD  1 
ATOM   1516 N  N   A GLU A 1 186 ? -4.621  -5.997  18.646  0.50 11.81  ? 186 GLU A N   1 
ATOM   1517 N  N   B GLU A 1 186 ? -4.552  -6.044  18.645  0.50 12.90  ? 186 GLU A N   1 
ATOM   1518 C  CA  A GLU A 1 186 ? -5.887  -5.596  19.266  0.50 12.65  ? 186 GLU A CA  1 
ATOM   1519 C  CA  B GLU A 1 186 ? -5.854  -5.740  19.213  0.50 12.93  ? 186 GLU A CA  1 
ATOM   1520 C  C   A GLU A 1 186 ? -5.624  -4.817  20.546  0.50 11.68  ? 186 GLU A C   1 
ATOM   1521 C  C   B GLU A 1 186 ? -5.687  -4.958  20.519  0.50 11.89  ? 186 GLU A C   1 
ATOM   1522 O  O   A GLU A 1 186 ? -6.234  -3.747  20.794  0.50 12.07  ? 186 GLU A O   1 
ATOM   1523 O  O   B GLU A 1 186 ? -6.359  -3.944  20.725  0.50 17.34  ? 186 GLU A O   1 
ATOM   1524 C  CB  A GLU A 1 186 ? -6.705  -6.809  19.684  0.50 14.71  ? 186 GLU A CB  1 
ATOM   1525 C  CB  B GLU A 1 186 ? -6.627  -7.042  19.345  0.50 16.29  ? 186 GLU A CB  1 
ATOM   1526 C  CG  A GLU A 1 186 ? -7.409  -7.428  18.512  0.50 17.54  ? 186 GLU A CG  1 
ATOM   1527 C  CG  B GLU A 1 186 ? -7.816  -6.876  20.225  0.50 18.34  ? 186 GLU A CG  1 
ATOM   1528 C  CD  A GLU A 1 186 ? -8.157  -8.691  18.933  0.50 18.07  ? 186 GLU A CD  1 
ATOM   1529 C  CD  B GLU A 1 186 ? -8.391  -8.191  20.707  0.50 19.44  ? 186 GLU A CD  1 
ATOM   1530 O  OE1 A GLU A 1 186 ? -8.650  -9.403  18.069  0.50 24.33  ? 186 GLU A OE1 1 
ATOM   1531 O  OE1 B GLU A 1 186 ? -8.134  -9.250  20.052  0.50 26.70  ? 186 GLU A OE1 1 
ATOM   1532 O  OE2 A GLU A 1 186 ? -8.267  -8.922  20.159  0.50 21.16  ? 186 GLU A OE2 1 
ATOM   1533 O  OE2 B GLU A 1 186 ? -9.102  -8.146  21.732  0.50 26.22  ? 186 GLU A OE2 1 
ATOM   1534 N  N   . SER A 1 187 ? -4.742  -5.386  21.389  1.00 11.20  ? 187 SER A N   1 
ATOM   1535 C  CA  . SER A 1 187 ? -4.525  -4.809  22.707  1.00 11.62  ? 187 SER A CA  1 
ATOM   1536 C  C   . SER A 1 187 ? -3.400  -3.776  22.692  1.00 11.26  ? 187 SER A C   1 
ATOM   1537 O  O   . SER A 1 187 ? -2.362  -3.994  22.042  1.00 12.89  ? 187 SER A O   1 
ATOM   1538 C  CB  . SER A 1 187 ? -4.146  -5.909  23.685  1.00 12.69  ? 187 SER A CB  1 
ATOM   1539 O  OG  . SER A 1 187 ? -3.875  -5.327  24.976  1.00 13.88  ? 187 SER A OG  1 
ATOM   1540 N  N   . LEU A 1 188 ? -3.555  -2.712  23.481  1.00 11.70  ? 188 LEU A N   1 
ATOM   1541 C  CA  . LEU A 1 188 ? -2.526  -1.712  23.718  1.00 13.10  ? 188 LEU A CA  1 
ATOM   1542 C  C   . LEU A 1 188 ? -1.860  -1.915  25.093  1.00 11.79  ? 188 LEU A C   1 
ATOM   1543 O  O   . LEU A 1 188 ? -1.129  -1.023  25.535  1.00 14.08  ? 188 LEU A O   1 
ATOM   1544 C  CB  . LEU A 1 188 ? -3.042  -0.271  23.547  1.00 16.16  ? 188 LEU A CB  1 
ATOM   1545 C  CG  . LEU A 1 188 ? -3.455  0.128   22.136  1.00 17.03  ? 188 LEU A CG  1 
ATOM   1546 C  CD1 . LEU A 1 188 ? -3.961  1.584   22.114  1.00 20.27  ? 188 LEU A CD1 1 
ATOM   1547 C  CD2 . LEU A 1 188 ? -2.322  -0.090  21.131  1.00 16.18  ? 188 LEU A CD2 1 
ATOM   1548 N  N   . ASP A 1 189 ? -1.963  -3.088  25.696  1.00 11.85  ? 189 ASP A N   1 
ATOM   1549 C  CA  . ASP A 1 189 ? -1.216  -3.343  26.907  1.00 12.34  ? 189 ASP A CA  1 
ATOM   1550 C  C   . ASP A 1 189 ? 0.282   -3.249  26.605  1.00 9.86   ? 189 ASP A C   1 
ATOM   1551 O  O   . ASP A 1 189 ? 0.702   -3.751  25.542  1.00 9.40   ? 189 ASP A O   1 
ATOM   1552 C  CB  . ASP A 1 189 ? -1.588  -4.732  27.484  1.00 15.79  ? 189 ASP A CB  1 
ATOM   1553 C  CG  . ASP A 1 189 ? -2.993  -4.949  28.135  1.00 20.86  ? 189 ASP A CG  1 
ATOM   1554 O  OD1 . ASP A 1 189 ? -3.617  -3.942  28.478  1.00 23.35  ? 189 ASP A OD1 1 
ATOM   1555 O  OD2 . ASP A 1 189 ? -3.297  -6.116  28.371  1.00 25.97  ? 189 ASP A OD2 1 
ATOM   1556 N  N   . TYR A 1 190 ? 1.080   -2.693  27.513  1.00 9.34   ? 190 TYR A N   1 
ATOM   1557 C  CA  . TYR A 1 190 ? 2.478   -2.438  27.155  1.00 9.16   ? 190 TYR A CA  1 
ATOM   1558 C  C   . TYR A 1 190 ? 3.375   -2.488  28.381  1.00 8.20   ? 190 TYR A C   1 
ATOM   1559 O  O   . TYR A 1 190 ? 2.890   -2.384  29.516  1.00 9.34   ? 190 TYR A O   1 
ATOM   1560 C  CB  . TYR A 1 190 ? 2.605   -1.054  26.483  1.00 9.05   ? 190 TYR A CB  1 
ATOM   1561 C  CG  . TYR A 1 190 ? 2.232   0.105   27.340  1.00 9.11   ? 190 TYR A CG  1 
ATOM   1562 C  CD1 . TYR A 1 190 ? 3.156   0.711   28.184  1.00 10.21  ? 190 TYR A CD1 1 
ATOM   1563 C  CD2 . TYR A 1 190 ? 0.940   0.665   27.330  1.00 9.97   ? 190 TYR A CD2 1 
ATOM   1564 C  CE1 . TYR A 1 190 ? 2.785   1.779   29.005  1.00 10.20  ? 190 TYR A CE1 1 
ATOM   1565 C  CE2 . TYR A 1 190 ? 0.547   1.716   28.142  1.00 11.18  ? 190 TYR A CE2 1 
ATOM   1566 C  CZ  . TYR A 1 190 ? 1.473   2.263   29.002  1.00 11.12  ? 190 TYR A CZ  1 
ATOM   1567 O  OH  . TYR A 1 190 ? 1.171   3.284   29.838  1.00 13.02  ? 190 TYR A OH  1 
ATOM   1568 N  N   . TRP A 1 191 ? 4.646   -2.593  28.088  1.00 8.11   ? 191 TRP A N   1 
ATOM   1569 C  CA  . TRP A 1 191 ? 5.734   -2.338  29.026  1.00 8.16   ? 191 TRP A CA  1 
ATOM   1570 C  C   . TRP A 1 191 ? 6.419   -1.043  28.618  1.00 7.30   ? 191 TRP A C   1 
ATOM   1571 O  O   . TRP A 1 191 ? 6.473   -0.718  27.436  1.00 8.86   ? 191 TRP A O   1 
ATOM   1572 C  CB  . TRP A 1 191 ? 6.774   -3.475  28.992  1.00 9.20   ? 191 TRP A CB  1 
ATOM   1573 C  CG  . TRP A 1 191 ? 6.239   -4.796  29.431  1.00 8.92   ? 191 TRP A CG  1 
ATOM   1574 C  CD1 . TRP A 1 191 ? 6.044   -5.234  30.722  1.00 9.89   ? 191 TRP A CD1 1 
ATOM   1575 C  CD2 . TRP A 1 191 ? 5.952   -5.913  28.566  1.00 9.05   ? 191 TRP A CD2 1 
ATOM   1576 N  NE1 . TRP A 1 191 ? 5.591   -6.553  30.682  1.00 10.96  ? 191 TRP A NE1 1 
ATOM   1577 C  CE2 . TRP A 1 191 ? 5.508   -6.972  29.377  1.00 9.92   ? 191 TRP A CE2 1 
ATOM   1578 C  CE3 . TRP A 1 191 ? 6.030   -6.064  27.175  1.00 9.82   ? 191 TRP A CE3 1 
ATOM   1579 C  CZ2 . TRP A 1 191 ? 5.220   -8.230  28.827  1.00 10.67  ? 191 TRP A CZ2 1 
ATOM   1580 C  CZ3 . TRP A 1 191 ? 5.770   -7.310  26.650  1.00 10.65  ? 191 TRP A CZ3 1 
ATOM   1581 C  CH2 . TRP A 1 191 ? 5.375   -8.370  27.449  1.00 11.24  ? 191 TRP A CH2 1 
ATOM   1582 N  N   . THR A 1 192 ? 7.008   -0.333  29.568  1.00 7.81   ? 192 THR A N   1 
ATOM   1583 C  CA  . THR A 1 192 ? 7.711   0.895   29.220  1.00 8.29   ? 192 THR A CA  1 
ATOM   1584 C  C   . THR A 1 192 ? 8.958   1.012   30.087  1.00 7.39   ? 192 THR A C   1 
ATOM   1585 O  O   . THR A 1 192 ? 8.976   0.651   31.273  1.00 8.31   ? 192 THR A O   1 
ATOM   1586 C  CB  . THR A 1 192 ? 6.769   2.084   29.337  1.00 8.41   ? 192 THR A CB  1 
ATOM   1587 O  OG1 . THR A 1 192 ? 7.473   3.259   28.922  1.00 8.88   ? 192 THR A OG1 1 
ATOM   1588 C  CG2 . THR A 1 192 ? 6.244   2.339   30.753  1.00 9.67   ? 192 THR A CG2 1 
ATOM   1589 N  N   . TYR A 1 193 ? 9.996   1.606   29.509  1.00 7.47   ? 193 TYR A N   1 
ATOM   1590 C  CA  . TYR A 1 193 ? 11.214  1.868   30.260  1.00 8.51   ? 193 TYR A CA  1 
ATOM   1591 C  C   . TYR A 1 193 ? 11.995  2.924   29.499  1.00 7.81   ? 193 TYR A C   1 
ATOM   1592 O  O   . TYR A 1 193 ? 11.806  3.138   28.296  1.00 7.86   ? 193 TYR A O   1 
ATOM   1593 C  CB  . TYR A 1 193 ? 12.016  0.537   30.441  1.00 8.35   ? 193 TYR A CB  1 
ATOM   1594 C  CG  . TYR A 1 193 ? 12.717  0.104   29.181  1.00 7.32   ? 193 TYR A CG  1 
ATOM   1595 C  CD1 . TYR A 1 193 ? 12.054  -0.626  28.182  1.00 7.27   ? 193 TYR A CD1 1 
ATOM   1596 C  CD2 . TYR A 1 193 ? 14.051  0.414   28.991  1.00 7.79   ? 193 TYR A CD2 1 
ATOM   1597 C  CE1 . TYR A 1 193 ? 12.678  -0.936  26.986  1.00 6.80   ? 193 TYR A CE1 1 
ATOM   1598 C  CE2 . TYR A 1 193 ? 14.710  0.100   27.799  1.00 8.32   ? 193 TYR A CE2 1 
ATOM   1599 C  CZ  . TYR A 1 193 ? 14.012  -0.532  26.793  1.00 6.25   ? 193 TYR A CZ  1 
ATOM   1600 O  OH  . TYR A 1 193 ? 14.677  -0.822  25.613  1.00 7.15   ? 193 TYR A OH  1 
ATOM   1601 N  N   . PRO A 1 194 ? 12.969  3.571   30.171  1.00 8.08   ? 194 PRO A N   1 
ATOM   1602 C  CA  . PRO A 1 194 ? 13.813  4.583   29.530  1.00 8.44   ? 194 PRO A CA  1 
ATOM   1603 C  C   . PRO A 1 194 ? 15.008  3.948   28.873  1.00 7.39   ? 194 PRO A C   1 
ATOM   1604 O  O   . PRO A 1 194 ? 15.709  3.135   29.474  1.00 8.51   ? 194 PRO A O   1 
ATOM   1605 C  CB  . PRO A 1 194 ? 14.229  5.469   30.721  1.00 11.03  ? 194 PRO A CB  1 
ATOM   1606 C  CG  . PRO A 1 194 ? 14.308  4.538   31.895  1.00 12.02  ? 194 PRO A CG  1 
ATOM   1607 C  CD  . PRO A 1 194 ? 13.171  3.554   31.634  1.00 10.87  ? 194 PRO A CD  1 
ATOM   1608 N  N   . GLY A 1 195 ? 15.247  4.297   27.600  1.00 7.55   ? 195 GLY A N   1 
ATOM   1609 C  CA  . GLY A 1 195 ? 16.369  3.698   26.871  1.00 7.71   ? 195 GLY A CA  1 
ATOM   1610 C  C   . GLY A 1 195 ? 16.912  4.590   25.796  1.00 6.78   ? 195 GLY A C   1 
ATOM   1611 O  O   . GLY A 1 195 ? 17.023  5.813   25.941  1.00 7.61   ? 195 GLY A O   1 
ATOM   1612 N  N   . SER A 1 196 ? 17.318  3.904   24.711  1.00 7.64   ? 196 SER A N   1 
ATOM   1613 C  CA  . SER A 1 196 ? 18.193  4.508   23.723  1.00 6.96   ? 196 SER A CA  1 
ATOM   1614 C  C   . SER A 1 196 ? 17.726  4.129   22.327  1.00 6.78   ? 196 SER A C   1 
ATOM   1615 O  O   . SER A 1 196 ? 16.943  3.201   22.130  1.00 6.91   ? 196 SER A O   1 
ATOM   1616 C  CB  . SER A 1 196 ? 19.644  4.108   23.889  1.00 7.90   ? 196 SER A CB  1 
ATOM   1617 O  OG  . SER A 1 196 ? 19.865  2.764   23.454  1.00 7.40   ? 196 SER A OG  1 
ATOM   1618 N  N   . LEU A 1 197 ? 18.313  4.807   21.327  1.00 7.15   ? 197 LEU A N   1 
ATOM   1619 C  CA  . LEU A 1 197 ? 18.319  4.285   19.970  1.00 7.24   ? 197 LEU A CA  1 
ATOM   1620 C  C   . LEU A 1 197 ? 19.017  2.947   19.984  1.00 7.17   ? 197 LEU A C   1 
ATOM   1621 O  O   . LEU A 1 197 ? 20.005  2.726   20.717  1.00 7.50   ? 197 LEU A O   1 
ATOM   1622 C  CB  . LEU A 1 197 ? 19.094  5.266   19.070  1.00 8.34   ? 197 LEU A CB  1 
ATOM   1623 C  CG  . LEU A 1 197 ? 18.535  6.675   19.016  1.00 8.99   ? 197 LEU A CG  1 
ATOM   1624 C  CD1 . LEU A 1 197 ? 19.429  7.530   18.132  1.00 11.03  ? 197 LEU A CD1 1 
ATOM   1625 C  CD2 . LEU A 1 197 ? 17.104  6.716   18.512  1.00 11.01  ? 197 LEU A CD2 1 
ATOM   1626 N  N   . THR A 1 198 ? 18.590  2.018   19.101  1.00 7.14   ? 198 THR A N   1 
ATOM   1627 C  CA  . THR A 1 198 ? 19.216  0.710   19.041  1.00 7.40   ? 198 THR A CA  1 
ATOM   1628 C  C   . THR A 1 198 ? 20.255  0.603   17.930  1.00 7.09   ? 198 THR A C   1 
ATOM   1629 O  O   . THR A 1 198 ? 20.801  -0.472  17.710  1.00 8.39   ? 198 THR A O   1 
ATOM   1630 C  CB  . THR A 1 198 ? 18.206  -0.432  18.923  1.00 6.75   ? 198 THR A CB  1 
ATOM   1631 O  OG1 . THR A 1 198 ? 17.607  -0.295  17.602  1.00 6.71   ? 198 THR A OG1 1 
ATOM   1632 C  CG2 . THR A 1 198 ? 17.146  -0.373  20.018  1.00 7.78   ? 198 THR A CG2 1 
ATOM   1633 N  N   . THR A 1 199 ? 20.494  1.709   17.228  1.00 8.09   ? 199 THR A N   1 
ATOM   1634 C  CA  . THR A 1 199 ? 21.557  1.764   16.258  1.00 9.25   ? 199 THR A CA  1 
ATOM   1635 C  C   . THR A 1 199 ? 22.391  2.997   16.552  1.00 9.96   ? 199 THR A C   1 
ATOM   1636 O  O   . THR A 1 199 ? 21.914  3.919   17.230  1.00 9.14   ? 199 THR A O   1 
ATOM   1637 C  CB  . THR A 1 199 ? 21.053  1.983   14.813  1.00 11.70  ? 199 THR A CB  1 
ATOM   1638 O  OG1 . THR A 1 199 ? 20.291  3.183   14.720  1.00 19.97  ? 199 THR A OG1 1 
ATOM   1639 C  CG2 . THR A 1 199 ? 20.078  0.900   14.404  1.00 10.65  ? 199 THR A CG2 1 
ATOM   1640 N  N   . PRO A 1 200 ? 23.664  3.052   16.091  1.00 10.23  ? 200 PRO A N   1 
ATOM   1641 C  CA  . PRO A 1 200 ? 24.438  4.295   16.198  1.00 10.93  ? 200 PRO A CA  1 
ATOM   1642 C  C   . PRO A 1 200 ? 23.555  5.438   15.742  1.00 10.80  ? 200 PRO A C   1 
ATOM   1643 O  O   . PRO A 1 200 ? 22.821  5.318   14.739  1.00 12.05  ? 200 PRO A O   1 
ATOM   1644 C  CB  . PRO A 1 200 ? 25.536  3.985   15.213  1.00 12.29  ? 200 PRO A CB  1 
ATOM   1645 C  CG  . PRO A 1 200 ? 25.795  2.506   15.465  1.00 13.20  ? 200 PRO A CG  1 
ATOM   1646 C  CD  . PRO A 1 200 ? 24.398  1.930   15.457  1.00 11.71  ? 200 PRO A CD  1 
ATOM   1647 N  N   . PRO A 1 201 ? 23.570  6.594   16.426  1.00 10.76  ? 201 PRO A N   1 
ATOM   1648 C  CA  . PRO A 1 201 ? 24.532  6.958   17.480  1.00 10.25  ? 201 PRO A CA  1 
ATOM   1649 C  C   . PRO A 1 201 ? 24.207  6.467   18.893  1.00 9.47   ? 201 PRO A C   1 
ATOM   1650 O  O   . PRO A 1 201 ? 24.908  6.837   19.823  1.00 10.56  ? 201 PRO A O   1 
ATOM   1651 C  CB  . PRO A 1 201 ? 24.511  8.479   17.433  1.00 12.03  ? 201 PRO A CB  1 
ATOM   1652 C  CG  . PRO A 1 201 ? 23.094  8.832   16.985  1.00 15.11  ? 201 PRO A CG  1 
ATOM   1653 C  CD  . PRO A 1 201 ? 22.760  7.738   15.996  1.00 12.49  ? 201 PRO A CD  1 
ATOM   1654 N  N   . LEU A 1 202 ? 23.128  5.672   19.070  1.00 8.76   ? 202 LEU A N   1 
ATOM   1655 C  CA  . LEU A 1 202 ? 22.837  5.022   20.355  1.00 8.32   ? 202 LEU A CA  1 
ATOM   1656 C  C   . LEU A 1 202 ? 22.472  6.002   21.468  1.00 7.80   ? 202 LEU A C   1 
ATOM   1657 O  O   . LEU A 1 202 ? 22.512  5.676   22.660  1.00 8.91   ? 202 LEU A O   1 
ATOM   1658 C  CB  . LEU A 1 202 ? 23.988  4.109   20.781  1.00 8.74   ? 202 LEU A CB  1 
ATOM   1659 C  CG  . LEU A 1 202 ? 24.312  2.967   19.794  1.00 8.66   ? 202 LEU A CG  1 
ATOM   1660 C  CD1 . LEU A 1 202 ? 25.598  2.297   20.213  1.00 10.30  ? 202 LEU A CD1 1 
ATOM   1661 C  CD2 . LEU A 1 202 ? 23.207  1.942   19.719  1.00 8.95   ? 202 LEU A CD2 1 
ATOM   1662 N  N   . THR A 1 203 ? 21.995  7.196   21.068  1.00 9.69   ? 203 THR A N   1 
ATOM   1663 C  CA  . THR A 1 203 ? 21.658  8.272   21.989  1.00 10.48  ? 203 THR A CA  1 
ATOM   1664 C  C   . THR A 1 203 ? 20.603  7.796   22.974  1.00 8.95   ? 203 THR A C   1 
ATOM   1665 O  O   . THR A 1 203 ? 19.608  7.126   22.564  1.00 8.56   ? 203 THR A O   1 
ATOM   1666 C  CB  . THR A 1 203 ? 21.115  9.443   21.180  1.00 13.36  ? 203 THR A CB  1 
ATOM   1667 O  OG1 . THR A 1 203 ? 22.089  9.673   20.148  1.00 14.37  ? 203 THR A OG1 1 
ATOM   1668 C  CG2 . THR A 1 203 ? 21.014  10.686  22.028  1.00 14.83  ? 203 THR A CG2 1 
ATOM   1669 N  N   . GLU A 1 204 ? 20.714  8.189   24.258  1.00 10.15  ? 204 GLU A N   1 
ATOM   1670 C  CA  . GLU A 1 204 ? 19.782  7.771   25.308  1.00 10.26  ? 204 GLU A CA  1 
ATOM   1671 C  C   . GLU A 1 204 ? 18.649  8.801   25.362  1.00 9.50   ? 204 GLU A C   1 
ATOM   1672 O  O   . GLU A 1 204 ? 18.414  9.501   26.349  1.00 13.63  ? 204 GLU A O   1 
ATOM   1673 C  CB  . GLU A 1 204 ? 20.558  7.629   26.624  1.00 10.74  ? 204 GLU A CB  1 
ATOM   1674 C  CG  . GLU A 1 204 ? 21.539  6.490   26.502  1.00 10.64  ? 204 GLU A CG  1 
ATOM   1675 C  CD  . GLU A 1 204 ? 22.380  6.182   27.729  1.00 11.99  ? 204 GLU A CD  1 
ATOM   1676 O  OE1 . GLU A 1 204 ? 22.564  7.058   28.612  1.00 14.36  ? 204 GLU A OE1 1 
ATOM   1677 O  OE2 . GLU A 1 204 ? 22.842  5.041   27.814  1.00 10.16  ? 204 GLU A OE2 1 
ATOM   1678 N  N   . CYS A 1 205 ? 17.826  8.821   24.307  1.00 7.79   ? 205 CYS A N   1 
ATOM   1679 C  CA  . CYS A 1 205 ? 16.778  9.800   24.097  1.00 7.92   ? 205 CYS A CA  1 
ATOM   1680 C  C   . CYS A 1 205 ? 15.378  9.207   23.966  1.00 7.24   ? 205 CYS A C   1 
ATOM   1681 O  O   . CYS A 1 205 ? 14.468  9.917   23.566  1.00 9.56   ? 205 CYS A O   1 
ATOM   1682 C  CB  . CYS A 1 205 ? 17.071  10.654  22.860  1.00 9.30   ? 205 CYS A CB  1 
ATOM   1683 S  SG  . CYS A 1 205 ? 17.144  9.674   21.333  1.00 11.38  ? 205 CYS A SG  1 
ATOM   1684 N  N   . VAL A 1 206 ? 15.235  7.900   24.285  1.00 7.47   ? 206 VAL A N   1 
ATOM   1685 C  CA  . VAL A 1 206 ? 13.993  7.198   23.952  1.00 7.23   ? 206 VAL A CA  1 
ATOM   1686 C  C   . VAL A 1 206 ? 13.222  6.733   25.168  1.00 7.77   ? 206 VAL A C   1 
ATOM   1687 O  O   . VAL A 1 206 ? 13.773  6.072   26.032  1.00 8.96   ? 206 VAL A O   1 
ATOM   1688 C  CB  . VAL A 1 206 ? 14.265  5.963   23.077  1.00 8.32   ? 206 VAL A CB  1 
ATOM   1689 C  CG1 . VAL A 1 206 ? 12.949  5.264   22.718  1.00 8.39   ? 206 VAL A CG1 1 
ATOM   1690 C  CG2 . VAL A 1 206 ? 15.057  6.318   21.813  1.00 8.99   ? 206 VAL A CG2 1 
ATOM   1691 N  N   . THR A 1 207 ? 11.908  7.072   25.193  1.00 7.42   ? 207 THR A N   1 
ATOM   1692 C  CA  . THR A 1 207 ? 10.974  6.346   26.057  1.00 7.73   ? 207 THR A CA  1 
ATOM   1693 C  C   . THR A 1 207 ? 10.450  5.180   25.217  1.00 6.71   ? 207 THR A C   1 
ATOM   1694 O  O   . THR A 1 207 ? 9.779   5.406   24.196  1.00 7.70   ? 207 THR A O   1 
ATOM   1695 C  CB  . THR A 1 207 ? 9.811   7.229   26.528  1.00 8.12   ? 207 THR A CB  1 
ATOM   1696 O  OG1 . THR A 1 207 ? 10.359  8.321   27.270  1.00 9.28   ? 207 THR A OG1 1 
ATOM   1697 C  CG2 . THR A 1 207 ? 8.891   6.407   27.427  1.00 10.11  ? 207 THR A CG2 1 
ATOM   1698 N  N   . TRP A 1 208 ? 10.770  3.953   25.614  1.00 6.42   ? 208 TRP A N   1 
ATOM   1699 C  CA  . TRP A 1 208 ? 10.289  2.770   24.921  1.00 6.37   ? 208 TRP A CA  1 
ATOM   1700 C  C   . TRP A 1 208 ? 8.938   2.367   25.445  1.00 6.08   ? 208 TRP A C   1 
ATOM   1701 O  O   . TRP A 1 208 ? 8.721   2.317   26.665  1.00 7.19   ? 208 TRP A O   1 
ATOM   1702 C  CB  . TRP A 1 208 ? 11.285  1.628   25.124  1.00 6.92   ? 208 TRP A CB  1 
ATOM   1703 C  CG  . TRP A 1 208 ? 12.436  1.742   24.165  1.00 6.17   ? 208 TRP A CG  1 
ATOM   1704 C  CD1 . TRP A 1 208 ? 13.653  2.318   24.405  1.00 7.65   ? 208 TRP A CD1 1 
ATOM   1705 C  CD2 . TRP A 1 208 ? 12.393  1.382   22.776  1.00 6.32   ? 208 TRP A CD2 1 
ATOM   1706 N  NE1 . TRP A 1 208 ? 14.379  2.320   23.231  1.00 7.95   ? 208 TRP A NE1 1 
ATOM   1707 C  CE2 . TRP A 1 208 ? 13.646  1.741   22.229  1.00 7.03   ? 208 TRP A CE2 1 
ATOM   1708 C  CE3 . TRP A 1 208 ? 11.430  0.745   21.982  1.00 6.56   ? 208 TRP A CE3 1 
ATOM   1709 C  CZ2 . TRP A 1 208 ? 13.910  1.520   20.889  1.00 8.01   ? 208 TRP A CZ2 1 
ATOM   1710 C  CZ3 . TRP A 1 208 ? 11.712  0.503   20.661  1.00 7.57   ? 208 TRP A CZ3 1 
ATOM   1711 C  CH2 . TRP A 1 208 ? 12.945  0.899   20.105  1.00 8.50   ? 208 TRP A CH2 1 
ATOM   1712 N  N   . ILE A 1 209 ? 8.040   2.030   24.532  1.00 6.49   ? 209 ILE A N   1 
ATOM   1713 C  CA  . ILE A 1 209 ? 6.715   1.513   24.851  1.00 6.72   ? 209 ILE A CA  1 
ATOM   1714 C  C   . ILE A 1 209 ? 6.578   0.253   23.995  1.00 6.25   ? 209 ILE A C   1 
ATOM   1715 O  O   . ILE A 1 209 ? 6.498   0.382   22.774  1.00 7.55   ? 209 ILE A O   1 
ATOM   1716 C  CB  . ILE A 1 209 ? 5.619   2.546   24.559  1.00 7.74   ? 209 ILE A CB  1 
ATOM   1717 C  CG1 . ILE A 1 209 ? 5.831   3.816   25.389  1.00 8.80   ? 209 ILE A CG1 1 
ATOM   1718 C  CG2 . ILE A 1 209 ? 4.248   1.899   24.772  1.00 9.13   ? 209 ILE A CG2 1 
ATOM   1719 C  CD1 . ILE A 1 209 ? 5.041   4.998   24.920  1.00 13.13  ? 209 ILE A CD1 1 
ATOM   1720 N  N   . VAL A 1 210 ? 6.644   -0.901  24.629  1.00 6.26   ? 210 VAL A N   1 
ATOM   1721 C  CA  . VAL A 1 210 ? 6.663   -2.172  23.894  1.00 6.50   ? 210 VAL A CA  1 
ATOM   1722 C  C   . VAL A 1 210 ? 5.339   -2.878  24.146  1.00 6.53   ? 210 VAL A C   1 
ATOM   1723 O  O   . VAL A 1 210 ? 5.013   -3.180  25.297  1.00 7.53   ? 210 VAL A O   1 
ATOM   1724 C  CB  . VAL A 1 210 ? 7.850   -3.029  24.324  1.00 7.16   ? 210 VAL A CB  1 
ATOM   1725 C  CG1 . VAL A 1 210 ? 7.829   -4.377  23.605  1.00 8.71   ? 210 VAL A CG1 1 
ATOM   1726 C  CG2 . VAL A 1 210 ? 9.177   -2.312  24.039  1.00 8.70   ? 210 VAL A CG2 1 
ATOM   1727 N  N   . LEU A 1 211 ? 4.589   -3.153  23.090  1.00 7.43   ? 211 LEU A N   1 
ATOM   1728 C  CA  . LEU A 1 211 ? 3.283   -3.788  23.279  1.00 7.48   ? 211 LEU A CA  1 
ATOM   1729 C  C   . LEU A 1 211 ? 3.478   -5.263  23.614  1.00 8.22   ? 211 LEU A C   1 
ATOM   1730 O  O   . LEU A 1 211 ? 4.329   -5.978  23.070  1.00 8.09   ? 211 LEU A O   1 
ATOM   1731 C  CB  . LEU A 1 211 ? 2.464   -3.661  22.004  1.00 8.42   ? 211 LEU A CB  1 
ATOM   1732 C  CG  . LEU A 1 211 ? 2.064   -2.237  21.609  1.00 9.42   ? 211 LEU A CG  1 
ATOM   1733 C  CD1 . LEU A 1 211 ? 1.042   -2.241  20.460  1.00 11.69  ? 211 LEU A CD1 1 
ATOM   1734 C  CD2 . LEU A 1 211 ? 1.595   -1.413  22.773  1.00 10.40  ? 211 LEU A CD2 1 
ATOM   1735 N  N   . LYS A 1 212 ? 2.598   -5.754  24.497  1.00 8.72   ? 212 LYS A N   1 
ATOM   1736 C  CA  . LYS A 1 212 ? 2.681   -7.154  24.917  1.00 9.14   ? 212 LYS A CA  1 
ATOM   1737 C  C   . LYS A 1 212 ? 2.200   -8.101  23.831  1.00 8.54   ? 212 LYS A C   1 
ATOM   1738 O  O   . LYS A 1 212 ? 2.720   -9.206  23.662  1.00 10.99  ? 212 LYS A O   1 
ATOM   1739 C  CB  . LYS A 1 212 ? 1.870   -7.353  26.189  1.00 12.16  ? 212 LYS A CB  1 
ATOM   1740 C  CG  . LYS A 1 212 ? 1.745   -8.831  26.569  1.00 16.34  ? 212 LYS A CG  1 
ATOM   1741 C  CD  . LYS A 1 212 ? 0.997   -9.027  27.883  1.00 27.95  ? 212 LYS A CD  1 
ATOM   1742 C  CE  . LYS A 1 212 ? 0.799   -10.491 28.253  1.00 32.11  ? 212 LYS A CE  1 
ATOM   1743 N  NZ  . LYS A 1 212 ? -0.278  -10.689 29.250  1.00 43.26  ? 212 LYS A NZ  1 
ATOM   1744 N  N   . GLU A 1 213 ? 1.167   -7.691  23.084  1.00 8.39   ? 213 GLU A N   1 
ATOM   1745 C  CA  . GLU A 1 213 ? 0.592   -8.612  22.104  1.00 8.42   ? 213 GLU A CA  1 
ATOM   1746 C  C   . GLU A 1 213 ? 1.357   -8.499  20.786  1.00 8.68   ? 213 GLU A C   1 
ATOM   1747 O  O   . GLU A 1 213 ? 1.399   -7.422  20.199  1.00 8.47   ? 213 GLU A O   1 
ATOM   1748 C  CB  . GLU A 1 213 ? -0.895  -8.227  21.837  1.00 9.68   ? 213 GLU A CB  1 
ATOM   1749 C  CG  . GLU A 1 213 ? -1.584  -9.215  20.942  1.00 13.54  ? 213 GLU A CG  1 
ATOM   1750 C  CD  . GLU A 1 213 ? -3.055  -8.882  20.625  1.00 21.86  ? 213 GLU A CD  1 
ATOM   1751 O  OE1 . GLU A 1 213 ? -3.626  -8.016  21.318  1.00 14.07  ? 213 GLU A OE1 1 
ATOM   1752 O  OE2 . GLU A 1 213 ? -3.609  -9.493  19.690  1.00 41.10  ? 213 GLU A OE2 1 
ATOM   1753 N  N   A PRO A 1 214 ? 1.888   -9.614  20.258  0.50 8.23   ? 214 PRO A N   1 
ATOM   1754 N  N   B PRO A 1 214 ? 1.979   -9.588  20.321  0.50 8.63   ? 214 PRO A N   1 
ATOM   1755 C  CA  A PRO A 1 214 ? 2.543   -9.535  18.951  0.50 7.98   ? 214 PRO A CA  1 
ATOM   1756 C  CA  B PRO A 1 214 ? 2.584   -9.570  18.977  0.50 8.61   ? 214 PRO A CA  1 
ATOM   1757 C  C   A PRO A 1 214 ? 1.471   -9.424  17.880  0.50 8.39   ? 214 PRO A C   1 
ATOM   1758 C  C   B PRO A 1 214 ? 1.543   -9.572  17.858  0.50 9.47   ? 214 PRO A C   1 
ATOM   1759 O  O   A PRO A 1 214 ? 0.317   -9.741  18.123  0.50 9.56   ? 214 PRO A O   1 
ATOM   1760 O  O   B PRO A 1 214 ? 0.460   -10.112 18.037  0.50 10.31  ? 214 PRO A O   1 
ATOM   1761 C  CB  A PRO A 1 214 ? 3.268   -10.879 18.837  0.50 9.42   ? 214 PRO A CB  1 
ATOM   1762 C  CB  B PRO A 1 214 ? 3.359   -10.891 18.945  0.50 10.22  ? 214 PRO A CB  1 
ATOM   1763 C  CG  A PRO A 1 214 ? 2.437   -11.841 19.675  0.50 10.52  ? 214 PRO A CG  1 
ATOM   1764 C  CG  B PRO A 1 214 ? 3.431   -11.356 20.391  0.50 12.66  ? 214 PRO A CG  1 
ATOM   1765 C  CD  A PRO A 1 214 ? 1.898   -10.992 20.810  0.50 9.59   ? 214 PRO A CD  1 
ATOM   1766 C  CD  B PRO A 1 214 ? 2.198   -10.850 21.069  0.50 10.55  ? 214 PRO A CD  1 
ATOM   1767 N  N   . ILE A 1 215 ? 1.922   -9.017  16.702  1.00 8.54   ? 215 ILE A N   1 
ATOM   1768 C  CA  . ILE A 1 215 ? 1.128   -9.240  15.491  1.00 8.94   ? 215 ILE A CA  1 
ATOM   1769 C  C   . ILE A 1 215 ? 1.659   -10.501 14.813  1.00 8.82   ? 215 ILE A C   1 
ATOM   1770 O  O   . ILE A 1 215 ? 2.835   -10.858 14.947  1.00 10.73  ? 215 ILE A O   1 
ATOM   1771 C  CB  . ILE A 1 215 ? 1.118   -8.027  14.556  1.00 9.59   ? 215 ILE A CB  1 
ATOM   1772 C  CG1 . ILE A 1 215 ? 2.517   -7.644  14.086  1.00 9.27   ? 215 ILE A CG1 1 
ATOM   1773 C  CG2 . ILE A 1 215 ? 0.381   -6.856  15.249  1.00 11.12  ? 215 ILE A CG2 1 
ATOM   1774 C  CD1 . ILE A 1 215 ? 2.475   -6.663  12.895  1.00 11.22  ? 215 ILE A CD1 1 
ATOM   1775 N  N   A SER A 1 216 ? 0.752   -11.140 14.083  0.50 9.79   ? 216 SER A N   1 
ATOM   1776 N  N   B SER A 1 216 ? 0.772   -11.237 14.152  0.50 10.42  ? 216 SER A N   1 
ATOM   1777 C  CA  A SER A 1 216 ? 1.082   -12.303 13.272  0.50 8.54   ? 216 SER A CA  1 
ATOM   1778 C  CA  B SER A 1 216 ? 1.286   -12.344 13.350  0.50 10.21  ? 216 SER A CA  1 
ATOM   1779 C  C   A SER A 1 216 ? 1.319   -11.855 11.838  0.50 8.60   ? 216 SER A C   1 
ATOM   1780 C  C   B SER A 1 216 ? 1.351   -11.887 11.900  0.50 8.96   ? 216 SER A C   1 
ATOM   1781 O  O   A SER A 1 216 ? 0.512   -11.117 11.259  0.50 10.27  ? 216 SER A O   1 
ATOM   1782 O  O   B SER A 1 216 ? 0.479   -11.179 11.380  0.50 11.46  ? 216 SER A O   1 
ATOM   1783 C  CB  A SER A 1 216 ? -0.062  -13.279 13.332  0.50 9.36   ? 216 SER A CB  1 
ATOM   1784 C  CB  B SER A 1 216 ? 0.475   -13.621 13.486  0.50 13.80  ? 216 SER A CB  1 
ATOM   1785 O  OG  A SER A 1 216 ? -0.043  -13.970 14.531  0.50 12.93  ? 216 SER A OG  1 
ATOM   1786 O  OG  B SER A 1 216 ? -0.848  -13.330 13.154  0.50 17.07  ? 216 SER A OG  1 
ATOM   1787 N  N   . VAL A 1 217 ? 2.427   -12.333 11.270  1.00 9.54   ? 217 VAL A N   1 
ATOM   1788 C  CA  . VAL A 1 217 ? 2.690   -12.117 9.846   1.00 9.34   ? 217 VAL A CA  1 
ATOM   1789 C  C   . VAL A 1 217 ? 2.949   -13.476 9.238   1.00 9.57   ? 217 VAL A C   1 
ATOM   1790 O  O   . VAL A 1 217 ? 3.314   -14.430 9.932   1.00 10.09  ? 217 VAL A O   1 
ATOM   1791 C  CB  . VAL A 1 217 ? 3.903   -11.179 9.620   1.00 10.45  ? 217 VAL A CB  1 
ATOM   1792 C  CG1 . VAL A 1 217 ? 3.661   -9.864  10.313  1.00 11.88  ? 217 VAL A CG1 1 
ATOM   1793 C  CG2 . VAL A 1 217 ? 5.181   -11.826 10.119  1.00 12.38  ? 217 VAL A CG2 1 
ATOM   1794 N  N   . SER A 1 218 ? 2.803   -13.620 7.926   1.00 9.26   ? 218 SER A N   1 
ATOM   1795 C  CA  . SER A 1 218 ? 3.027   -14.960 7.356   1.00 9.69   ? 218 SER A CA  1 
ATOM   1796 C  C   . SER A 1 218 ? 4.508   -15.211 7.102   1.00 9.97   ? 218 SER A C   1 
ATOM   1797 O  O   . SER A 1 218 ? 5.318   -14.272 6.998   1.00 10.00  ? 218 SER A O   1 
ATOM   1798 C  CB  . SER A 1 218 ? 2.248   -15.161 6.098   1.00 10.40  ? 218 SER A CB  1 
ATOM   1799 O  OG  . SER A 1 218 ? 2.709   -14.245 5.121   1.00 10.89  ? 218 SER A OG  1 
ATOM   1800 N  N   A SER A 1 219 ? 4.827   -16.495 6.939   0.50 10.41  ? 219 SER A N   1 
ATOM   1801 N  N   B SER A 1 219 ? 4.857   -16.493 6.961   0.50 10.53  ? 219 SER A N   1 
ATOM   1802 C  CA  A SER A 1 219 ? 6.179   -16.862 6.609   0.50 11.18  ? 219 SER A CA  1 
ATOM   1803 C  CA  B SER A 1 219 ? 6.208   -16.852 6.602   0.50 11.58  ? 219 SER A CA  1 
ATOM   1804 C  C   A SER A 1 219 ? 6.589   -16.143 5.313   0.50 10.54  ? 219 SER A C   1 
ATOM   1805 C  C   B SER A 1 219 ? 6.602   -16.126 5.306   0.50 10.65  ? 219 SER A C   1 
ATOM   1806 O  O   A SER A 1 219 ? 7.730   -15.679 5.155   0.50 12.50  ? 219 SER A O   1 
ATOM   1807 O  O   B SER A 1 219 ? 7.751   -15.679 5.130   0.50 12.67  ? 219 SER A O   1 
ATOM   1808 C  CB  A SER A 1 219 ? 6.290   -18.362 6.572   0.50 14.18  ? 219 SER A CB  1 
ATOM   1809 C  CB  B SER A 1 219 ? 6.319   -18.347 6.509   0.50 15.72  ? 219 SER A CB  1 
ATOM   1810 O  OG  A SER A 1 219 ? 5.388   -18.914 5.630   0.50 14.12  ? 219 SER A OG  1 
ATOM   1811 O  OG  B SER A 1 219 ? 7.630   -18.734 6.126   0.50 20.46  ? 219 SER A OG  1 
ATOM   1812 N  N   . GLU A 1 220 ? 5.669   -16.039 4.357   1.00 11.32  ? 220 GLU A N   1 
ATOM   1813 C  CA  . GLU A 1 220 ? 5.955   -15.429 3.083   1.00 12.25  ? 220 GLU A CA  1 
ATOM   1814 C  C   . GLU A 1 220 ? 6.233   -13.924 3.195   1.00 11.94  ? 220 GLU A C   1 
ATOM   1815 O  O   . GLU A 1 220 ? 7.099   -13.351 2.496   1.00 13.52  ? 220 GLU A O   1 
ATOM   1816 C  CB  . GLU A 1 220 ? 4.836   -15.596 2.068   1.00 15.11  ? 220 GLU A CB  1 
ATOM   1817 C  CG  . GLU A 1 220 ? 4.629   -17.061 1.644   1.00 19.20  ? 220 GLU A CG  1 
ATOM   1818 C  CD  . GLU A 1 220 ? 3.724   -17.852 2.565   1.00 19.21  ? 220 GLU A CD  1 
ATOM   1819 O  OE1 . GLU A 1 220 ? 3.216   -17.358 3.579   1.00 18.85  ? 220 GLU A OE1 1 
ATOM   1820 O  OE2 . GLU A 1 220 ? 3.553   -19.089 2.263   1.00 30.59  ? 220 GLU A OE2 1 
ATOM   1821 N  N   . GLN A 1 221 ? 5.514   -13.263 4.122   1.00 10.77  ? 221 GLN A N   1 
ATOM   1822 C  CA  . GLN A 1 221 ? 5.746   -11.831 4.345   1.00 10.05  ? 221 GLN A CA  1 
ATOM   1823 C  C   . GLN A 1 221 ? 7.166   -11.600 4.850   1.00 10.15  ? 221 GLN A C   1 
ATOM   1824 O  O   . GLN A 1 221 ? 7.904   -10.748 4.346   1.00 10.32  ? 221 GLN A O   1 
ATOM   1825 C  CB  . GLN A 1 221 ? 4.710   -11.246 5.282   1.00 9.80   ? 221 GLN A CB  1 
ATOM   1826 C  CG  . GLN A 1 221 ? 3.344   -11.140 4.580   1.00 10.15  ? 221 GLN A CG  1 
ATOM   1827 C  CD  . GLN A 1 221 ? 2.230   -10.601 5.430   1.00 9.44   ? 221 GLN A CD  1 
ATOM   1828 O  OE1 . GLN A 1 221 ? 2.119   -10.980 6.606   1.00 9.90   ? 221 GLN A OE1 1 
ATOM   1829 N  NE2 . GLN A 1 221 ? 1.388   -9.750  4.868   1.00 10.61  ? 221 GLN A NE2 1 
ATOM   1830 N  N   . VAL A 1 222 ? 7.593   -12.363 5.881   1.00 10.18  ? 222 VAL A N   1 
ATOM   1831 C  CA  . VAL A 1 222 ? 8.937   -12.123 6.424   1.00 10.37  ? 222 VAL A CA  1 
ATOM   1832 C  C   . VAL A 1 222 ? 10.024  -12.603 5.468   1.00 11.22  ? 222 VAL A C   1 
ATOM   1833 O  O   . VAL A 1 222 ? 11.075  -12.006 5.373   1.00 11.34  ? 222 VAL A O   1 
ATOM   1834 C  CB  . VAL A 1 222 ? 9.091   -12.678 7.851   1.00 13.90  ? 222 VAL A CB  1 
ATOM   1835 C  CG1 . VAL A 1 222 ? 9.046   -14.176 7.908   1.00 15.77  ? 222 VAL A CG1 1 
ATOM   1836 C  CG2 . VAL A 1 222 ? 10.352  -12.144 8.539   1.00 16.70  ? 222 VAL A CG2 1 
ATOM   1837 N  N   A LEU A 1 223 ? 9.756   -13.641 4.669   0.50 11.21  ? 223 LEU A N   1 
ATOM   1838 N  N   B LEU A 1 223 ? 9.709   -13.646 4.704   0.50 11.16  ? 223 LEU A N   1 
ATOM   1839 C  CA  A LEU A 1 223 ? 10.761  -14.046 3.683   0.50 12.03  ? 223 LEU A CA  1 
ATOM   1840 C  CA  B LEU A 1 223 ? 10.640  -14.121 3.694   0.50 14.03  ? 223 LEU A CA  1 
ATOM   1841 C  C   A LEU A 1 223 ? 11.061  -12.915 2.723   0.50 12.25  ? 223 LEU A C   1 
ATOM   1842 C  C   B LEU A 1 223 ? 11.000  -12.994 2.734   0.50 11.36  ? 223 LEU A C   1 
ATOM   1843 O  O   A LEU A 1 223 ? 12.198  -12.774 2.241   0.50 13.55  ? 223 LEU A O   1 
ATOM   1844 O  O   B LEU A 1 223 ? 12.177  -12.847 2.353   0.50 12.99  ? 223 LEU A O   1 
ATOM   1845 C  CB  A LEU A 1 223 ? 10.217  -15.230 2.855   0.50 17.01  ? 223 LEU A CB  1 
ATOM   1846 C  CB  B LEU A 1 223 ? 9.994   -15.319 2.971   0.50 16.56  ? 223 LEU A CB  1 
ATOM   1847 C  CG  A LEU A 1 223 ? 10.181  -16.540 3.616   0.50 18.54  ? 223 LEU A CG  1 
ATOM   1848 C  CG  B LEU A 1 223 ? 10.722  -15.861 1.753   0.50 20.87  ? 223 LEU A CG  1 
ATOM   1849 C  CD1 A LEU A 1 223 ? 9.298   -17.542 2.885   0.50 21.09  ? 223 LEU A CD1 1 
ATOM   1850 C  CD1 B LEU A 1 223 ? 12.067  -16.437 2.146   0.50 29.65  ? 223 LEU A CD1 1 
ATOM   1851 C  CD2 A LEU A 1 223 ? 11.592  -17.041 3.678   0.50 19.66  ? 223 LEU A CD2 1 
ATOM   1852 C  CD2 B LEU A 1 223 ? 9.879   -16.958 1.107   0.50 27.04  ? 223 LEU A CD2 1 
ATOM   1853 N  N   . LYS A 1 224 ? 10.046  -12.132 2.412   1.00 11.00  ? 224 LYS A N   1 
ATOM   1854 C  CA  . LYS A 1 224 ? 10.277  -11.009 1.514   1.00 11.17  ? 224 LYS A CA  1 
ATOM   1855 C  C   . LYS A 1 224 ? 11.131  -9.917  2.151   1.00 10.29  ? 224 LYS A C   1 
ATOM   1856 O  O   . LYS A 1 224 ? 11.910  -9.256  1.447   1.00 10.95  ? 224 LYS A O   1 
ATOM   1857 C  CB  . LYS A 1 224 ? 8.958   -10.530 0.889   1.00 14.33  ? 224 LYS A CB  1 
ATOM   1858 C  CG  . LYS A 1 224 ? 8.361   -11.565 -0.099  1.00 18.24  ? 224 LYS A CG  1 
ATOM   1859 C  CD  . LYS A 1 224 ? 7.060   -11.233 -0.760  1.00 21.20  ? 224 LYS A CD  1 
ATOM   1860 C  CE  . LYS A 1 224 ? 6.643   -12.289 -1.784  1.00 25.96  ? 224 LYS A CE  1 
ATOM   1861 N  NZ  . LYS A 1 224 ? 5.339   -11.995 -2.441  1.00 24.32  ? 224 LYS A NZ  1 
ATOM   1862 N  N   . PHE A 1 225 ? 10.996  -9.683  3.472   1.00 9.68   ? 225 PHE A N   1 
ATOM   1863 C  CA  . PHE A 1 225 ? 11.942  -8.800  4.143   1.00 9.29   ? 225 PHE A CA  1 
ATOM   1864 C  C   . PHE A 1 225 ? 13.385  -9.259  3.909   1.00 9.29   ? 225 PHE A C   1 
ATOM   1865 O  O   . PHE A 1 225 ? 14.296  -8.445  3.667   1.00 9.85   ? 225 PHE A O   1 
ATOM   1866 C  CB  . PHE A 1 225 ? 11.742  -8.783  5.666   1.00 9.87   ? 225 PHE A CB  1 
ATOM   1867 C  CG  . PHE A 1 225 ? 10.525  -8.070  6.208   1.00 8.75   ? 225 PHE A CG  1 
ATOM   1868 C  CD1 . PHE A 1 225 ? 9.503   -7.667  5.363   1.00 11.24  ? 225 PHE A CD1 1 
ATOM   1869 C  CD2 . PHE A 1 225 ? 10.405  -7.801  7.562   1.00 11.13  ? 225 PHE A CD2 1 
ATOM   1870 C  CE1 . PHE A 1 225 ? 8.387   -7.013  5.860   1.00 12.08  ? 225 PHE A CE1 1 
ATOM   1871 C  CE2 . PHE A 1 225 ? 9.288   -7.147  8.058   1.00 12.10  ? 225 PHE A CE2 1 
ATOM   1872 C  CZ  . PHE A 1 225 ? 8.282   -6.754  7.207   1.00 11.24  ? 225 PHE A CZ  1 
ATOM   1873 N  N   . ARG A 1 226 ? 13.602  -10.583 3.941   1.00 9.12   ? 226 ARG A N   1 
ATOM   1874 C  CA  . ARG A 1 226 ? 14.941  -11.141 3.866   1.00 9.49   ? 226 ARG A CA  1 
ATOM   1875 C  C   . ARG A 1 226 ? 15.501  -11.132 2.453   1.00 9.31   ? 226 ARG A C   1 
ATOM   1876 O  O   . ARG A 1 226 ? 16.672  -11.518 2.280   1.00 11.66  ? 226 ARG A O   1 
ATOM   1877 C  CB  . ARG A 1 226 ? 14.883  -12.592 4.382   1.00 10.54  ? 226 ARG A CB  1 
ATOM   1878 C  CG  . ARG A 1 226 ? 14.415  -12.715 5.849   1.00 10.11  ? 226 ARG A CG  1 
ATOM   1879 C  CD  . ARG A 1 226 ? 14.523  -14.161 6.280   1.00 11.79  ? 226 ARG A CD  1 
ATOM   1880 N  NE  . ARG A 1 226 ? 13.927  -14.340 7.602   1.00 10.49  ? 226 ARG A NE  1 
ATOM   1881 C  CZ  . ARG A 1 226 ? 12.949  -15.191 7.868   1.00 11.02  ? 226 ARG A CZ  1 
ATOM   1882 N  NH1 . ARG A 1 226 ? 12.522  -16.033 6.943   1.00 14.29  ? 226 ARG A NH1 1 
ATOM   1883 N  NH2 . ARG A 1 226 ? 12.439  -15.247 9.084   1.00 12.83  ? 226 ARG A NH2 1 
ATOM   1884 N  N   . LYS A 1 227 ? 14.732  -10.708 1.442   1.00 9.90   ? 227 LYS A N   1 
ATOM   1885 C  CA  . LYS A 1 227 ? 15.235  -10.553 0.103   1.00 11.46  ? 227 LYS A CA  1 
ATOM   1886 C  C   . LYS A 1 227 ? 15.839  -9.172  -0.135  1.00 11.10  ? 227 LYS A C   1 
ATOM   1887 O  O   . LYS A 1 227 ? 16.446  -8.949  -1.173  1.00 12.94  ? 227 LYS A O   1 
ATOM   1888 C  CB  . LYS A 1 227 ? 14.115  -10.858 -0.881  1.00 12.99  ? 227 LYS A CB  1 
ATOM   1889 C  CG  . LYS A 1 227 ? 13.732  -12.326 -0.921  1.00 17.03  ? 227 LYS A CG  1 
ATOM   1890 C  CD  . LYS A 1 227 ? 12.717  -12.580 -2.027  1.00 23.79  ? 227 LYS A CD  1 
ATOM   1891 C  CE  . LYS A 1 227 ? 13.251  -12.876 -3.423  1.00 33.62  ? 227 LYS A CE  1 
ATOM   1892 N  NZ  . LYS A 1 227 ? 12.205  -12.858 -4.486  1.00 51.97  ? 227 LYS A NZ  1 
ATOM   1893 N  N   . LEU A 1 228 ? 15.624  -8.226  0.792   1.00 10.79  ? 228 LEU A N   1 
ATOM   1894 C  CA  . LEU A 1 228 ? 16.286  -6.942  0.707   1.00 10.10  ? 228 LEU A CA  1 
ATOM   1895 C  C   . LEU A 1 228 ? 17.787  -7.133  0.795   1.00 10.14  ? 228 LEU A C   1 
ATOM   1896 O  O   . LEU A 1 228 ? 18.305  -8.198  1.219   1.00 10.11  ? 228 LEU A O   1 
ATOM   1897 C  CB  . LEU A 1 228 ? 15.796  -5.977  1.786   1.00 10.33  ? 228 LEU A CB  1 
ATOM   1898 C  CG  . LEU A 1 228 ? 14.326  -5.557  1.655   1.00 10.45  ? 228 LEU A CG  1 
ATOM   1899 C  CD1 . LEU A 1 228 ? 13.883  -4.894  2.945   1.00 10.84  ? 228 LEU A CD1 1 
ATOM   1900 C  CD2 . LEU A 1 228 ? 14.193  -4.589  0.482   1.00 12.33  ? 228 LEU A CD2 1 
ATOM   1901 N  N   . ASN A 1 229 ? 18.526  -6.095  0.406   1.00 10.29  ? 229 ASN A N   1 
ATOM   1902 C  CA  . ASN A 1 229 ? 19.994  -6.159  0.422   1.00 9.94   ? 229 ASN A CA  1 
ATOM   1903 C  C   . ASN A 1 229 ? 20.532  -5.007  1.254   1.00 10.17  ? 229 ASN A C   1 
ATOM   1904 O  O   . ASN A 1 229 ? 20.066  -3.860  1.180   1.00 11.20  ? 229 ASN A O   1 
ATOM   1905 C  CB  . ASN A 1 229 ? 20.544  -5.970  -0.975  1.00 11.92  ? 229 ASN A CB  1 
ATOM   1906 C  CG  . ASN A 1 229 ? 20.412  -7.109  -1.946  1.00 14.31  ? 229 ASN A CG  1 
ATOM   1907 O  OD1 . ASN A 1 229 ? 20.913  -6.961  -3.099  1.00 17.42  ? 229 ASN A OD1 1 
ATOM   1908 N  ND2 . ASN A 1 229 ? 19.807  -8.233  -1.559  1.00 15.55  ? 229 ASN A ND2 1 
ATOM   1909 N  N   . PHE A 1 230 ? 21.636  -5.312  1.994   1.00 9.94   ? 230 PHE A N   1 
ATOM   1910 C  CA  . PHE A 1 230 ? 22.374  -4.267  2.682   1.00 9.98   ? 230 PHE A CA  1 
ATOM   1911 C  C   . PHE A 1 230 ? 23.161  -3.407  1.717   1.00 10.25  ? 230 PHE A C   1 
ATOM   1912 O  O   . PHE A 1 230 ? 23.382  -2.214  1.923   1.00 11.72  ? 230 PHE A O   1 
ATOM   1913 C  CB  . PHE A 1 230 ? 23.370  -4.849  3.685   1.00 10.67  ? 230 PHE A CB  1 
ATOM   1914 C  CG  . PHE A 1 230 ? 22.835  -5.444  4.966   1.00 10.59  ? 230 PHE A CG  1 
ATOM   1915 C  CD1 . PHE A 1 230 ? 22.136  -4.694  5.902   1.00 10.65  ? 230 PHE A CD1 1 
ATOM   1916 C  CD2 . PHE A 1 230 ? 23.169  -6.767  5.277   1.00 11.51  ? 230 PHE A CD2 1 
ATOM   1917 C  CE1 . PHE A 1 230 ? 21.728  -5.237  7.110   1.00 11.17  ? 230 PHE A CE1 1 
ATOM   1918 C  CE2 . PHE A 1 230 ? 22.784  -7.316  6.495   1.00 11.34  ? 230 PHE A CE2 1 
ATOM   1919 C  CZ  . PHE A 1 230 ? 22.086  -6.550  7.408   1.00 10.89  ? 230 PHE A CZ  1 
ATOM   1920 N  N   . ASN A 1 231 ? 23.669  -4.009  0.652   1.00 10.79  ? 231 ASN A N   1 
ATOM   1921 C  CA  . ASN A 1 231 ? 24.554  -3.348  -0.305  1.00 12.03  ? 231 ASN A CA  1 
ATOM   1922 C  C   . ASN A 1 231 ? 23.730  -2.468  -1.232  1.00 11.37  ? 231 ASN A C   1 
ATOM   1923 O  O   . ASN A 1 231 ? 22.520  -2.551  -1.415  1.00 12.57  ? 231 ASN A O   1 
ATOM   1924 C  CB  . ASN A 1 231 ? 25.259  -4.426  -1.147  1.00 13.64  ? 231 ASN A CB  1 
ATOM   1925 C  CG  . ASN A 1 231 ? 24.193  -5.319  -1.765  1.00 11.55  ? 231 ASN A CG  1 
ATOM   1926 O  OD1 . ASN A 1 231 ? 23.680  -6.245  -1.125  1.00 12.54  ? 231 ASN A OD1 1 
ATOM   1927 N  ND2 . ASN A 1 231 ? 23.915  -5.169  -3.060  1.00 14.40  ? 231 ASN A ND2 1 
ATOM   1928 N  N   . GLY A 1 232 ? 24.481  -1.547  -1.884  1.00 12.33  ? 232 GLY A N   1 
ATOM   1929 C  CA  . GLY A 1 232 ? 23.985  -0.757  -2.994  1.00 13.21  ? 232 GLY A CA  1 
ATOM   1930 C  C   . GLY A 1 232 ? 23.904  -1.547  -4.274  1.00 12.49  ? 232 GLY A C   1 
ATOM   1931 O  O   . GLY A 1 232 ? 24.564  -2.593  -4.419  1.00 13.47  ? 232 GLY A O   1 
ATOM   1932 N  N   . GLU A 1 233 ? 23.128  -1.036  -5.224  1.00 12.79  ? 233 GLU A N   1 
ATOM   1933 C  CA  . GLU A 1 233 ? 23.122  -1.615  -6.569  1.00 12.72  ? 233 GLU A CA  1 
ATOM   1934 C  C   . GLU A 1 233 ? 24.543  -1.662  -7.120  1.00 13.53  ? 233 GLU A C   1 
ATOM   1935 O  O   . GLU A 1 233 ? 25.300  -0.705  -6.996  1.00 13.86  ? 233 GLU A O   1 
ATOM   1936 C  CB  . GLU A 1 233 ? 22.183  -0.761  -7.449  1.00 13.85  ? 233 GLU A CB  1 
ATOM   1937 C  CG  . GLU A 1 233 ? 21.893  -1.329  -8.836  1.00 17.58  ? 233 GLU A CG  1 
ATOM   1938 C  CD  . GLU A 1 233 ? 21.007  -0.474  -9.706  1.00 24.90  ? 233 GLU A CD  1 
ATOM   1939 O  OE1 . GLU A 1 233 ? 20.744  0.700   -9.334  1.00 26.47  ? 233 GLU A OE1 1 
ATOM   1940 O  OE2 . GLU A 1 233 ? 20.759  -0.922  -10.832 1.00 29.29  ? 233 GLU A OE2 1 
ATOM   1941 N  N   . GLY A 1 234 ? 24.882  -2.757  -7.781  1.00 16.83  ? 234 GLY A N   1 
ATOM   1942 C  CA  . GLY A 1 234 ? 26.178  -2.797  -8.443  1.00 16.61  ? 234 GLY A CA  1 
ATOM   1943 C  C   . GLY A 1 234 ? 27.286  -3.192  -7.460  1.00 18.24  ? 234 GLY A C   1 
ATOM   1944 O  O   . GLY A 1 234 ? 28.460  -3.307  -7.865  1.00 22.82  ? 234 GLY A O   1 
ATOM   1945 N  N   . GLU A 1 235 ? 26.955  -3.528  -6.221  1.00 16.01  ? 235 GLU A N   1 
ATOM   1946 C  CA  . GLU A 1 235 ? 27.893  -4.040  -5.219  1.00 14.90  ? 235 GLU A CA  1 
ATOM   1947 C  C   . GLU A 1 235 ? 27.533  -5.501  -4.935  1.00 14.57  ? 235 GLU A C   1 
ATOM   1948 O  O   . GLU A 1 235 ? 26.400  -5.942  -5.211  1.00 16.45  ? 235 GLU A O   1 
ATOM   1949 C  CB  . GLU A 1 235 ? 27.781  -3.258  -3.892  1.00 14.45  ? 235 GLU A CB  1 
ATOM   1950 C  CG  . GLU A 1 235 ? 28.149  -1.809  -4.074  1.00 17.94  ? 235 GLU A CG  1 
ATOM   1951 C  CD  . GLU A 1 235 ? 27.918  -0.998  -2.796  1.00 25.21  ? 235 GLU A CD  1 
ATOM   1952 O  OE1 . GLU A 1 235 ? 28.422  0.115   -2.736  1.00 36.53  ? 235 GLU A OE1 1 
ATOM   1953 O  OE2 . GLU A 1 235 ? 27.295  -1.475  -1.795  1.00 22.32  ? 235 GLU A OE2 1 
ATOM   1954 N  N   . PRO A 1 236 ? 28.466  -6.308  -4.375  1.00 15.14  ? 236 PRO A N   1 
ATOM   1955 C  CA  . PRO A 1 236 ? 28.166  -7.709  -4.089  1.00 14.14  ? 236 PRO A CA  1 
ATOM   1956 C  C   . PRO A 1 236 ? 26.932  -7.807  -3.190  1.00 12.83  ? 236 PRO A C   1 
ATOM   1957 O  O   . PRO A 1 236 ? 26.756  -7.047  -2.241  1.00 14.18  ? 236 PRO A O   1 
ATOM   1958 C  CB  . PRO A 1 236 ? 29.451  -8.212  -3.437  1.00 16.37  ? 236 PRO A CB  1 
ATOM   1959 C  CG  . PRO A 1 236 ? 30.563  -7.313  -4.055  1.00 18.67  ? 236 PRO A CG  1 
ATOM   1960 C  CD  . PRO A 1 236 ? 29.875  -5.940  -4.087  1.00 18.74  ? 236 PRO A CD  1 
ATOM   1961 N  N   . GLU A 1 237 ? 26.112  -8.812  -3.472  1.00 12.89  ? 237 GLU A N   1 
ATOM   1962 C  CA  . GLU A 1 237 ? 24.844  -8.973  -2.777  1.00 12.71  ? 237 GLU A CA  1 
ATOM   1963 C  C   . GLU A 1 237 ? 25.079  -9.504  -1.359  1.00 11.93  ? 237 GLU A C   1 
ATOM   1964 O  O   . GLU A 1 237 ? 25.715  -10.566 -1.178  1.00 13.08  ? 237 GLU A O   1 
ATOM   1965 C  CB  . GLU A 1 237 ? 23.951  -9.978  -3.504  1.00 16.77  ? 237 GLU A CB  1 
ATOM   1966 C  CG  . GLU A 1 237 ? 22.583  -10.093 -2.852  1.00 21.43  ? 237 GLU A CG  1 
ATOM   1967 C  CD  . GLU A 1 237 ? 21.441  -10.655 -3.719  1.00 29.06  ? 237 GLU A CD  1 
ATOM   1968 O  OE1 . GLU A 1 237 ? 21.730  -11.147 -4.831  1.00 34.23  ? 237 GLU A OE1 1 
ATOM   1969 O  OE2 . GLU A 1 237 ? 20.219  -10.454 -3.349  1.00 25.05  ? 237 GLU A OE2 1 
ATOM   1970 N  N   . GLU A 1 238 ? 24.525  -8.785  -0.383  1.00 10.69  ? 238 GLU A N   1 
ATOM   1971 C  CA  . GLU A 1 238 ? 24.538  -9.195  0.988   1.00 11.90  ? 238 GLU A CA  1 
ATOM   1972 C  C   . GLU A 1 238 ? 23.105  -9.068  1.493   1.00 10.45  ? 238 GLU A C   1 
ATOM   1973 O  O   . GLU A 1 238 ? 22.567  -7.977  1.568   1.00 12.83  ? 238 GLU A O   1 
ATOM   1974 C  CB  . GLU A 1 238 ? 25.426  -8.290  1.826   1.00 16.59  ? 238 GLU A CB  1 
ATOM   1975 C  CG  . GLU A 1 238 ? 25.643  -8.922  3.210   1.00 22.60  ? 238 GLU A CG  1 
ATOM   1976 N  N   . LEU A 1 239 ? 22.473  -10.220 1.789   1.00 10.97  ? 239 LEU A N   1 
ATOM   1977 C  CA  . LEU A 1 239 ? 21.075  -10.144 2.174   1.00 10.69  ? 239 LEU A CA  1 
ATOM   1978 C  C   . LEU A 1 239 ? 20.899  -9.375  3.488   1.00 9.20   ? 239 LEU A C   1 
ATOM   1979 O  O   . LEU A 1 239 ? 21.668  -9.554  4.440   1.00 9.84   ? 239 LEU A O   1 
ATOM   1980 C  CB  . LEU A 1 239 ? 20.569  -11.586 2.376   1.00 12.33  ? 239 LEU A CB  1 
ATOM   1981 C  CG  . LEU A 1 239 ? 20.529  -12.463 1.134   1.00 14.46  ? 239 LEU A CG  1 
ATOM   1982 C  CD1 . LEU A 1 239 ? 19.979  -13.828 1.498   1.00 18.42  ? 239 LEU A CD1 1 
ATOM   1983 C  CD2 . LEU A 1 239 ? 19.695  -11.778 0.057   1.00 14.94  ? 239 LEU A CD2 1 
ATOM   1984 N  N   . MET A 1 240 ? 19.849  -8.552  3.520   1.00 9.20   ? 240 MET A N   1 
ATOM   1985 C  CA  . MET A 1 240 ? 19.567  -7.755  4.709   1.00 9.66   ? 240 MET A CA  1 
ATOM   1986 C  C   . MET A 1 240 ? 18.754  -8.633  5.682   1.00 9.46   ? 240 MET A C   1 
ATOM   1987 O  O   . MET A 1 240 ? 17.558  -8.833  5.536   1.00 9.35   ? 240 MET A O   1 
ATOM   1988 C  CB  . MET A 1 240 ? 18.720  -6.543  4.269   1.00 11.05  ? 240 MET A CB  1 
ATOM   1989 C  CG  . MET A 1 240 ? 18.443  -5.614  5.474   1.00 9.33   ? 240 MET A CG  1 
ATOM   1990 S  SD  . MET A 1 240 ? 17.486  -4.177  4.995   1.00 10.35  ? 240 MET A SD  1 
ATOM   1991 C  CE  . MET A 1 240 ? 18.752  -3.153  4.254   1.00 11.48  ? 240 MET A CE  1 
ATOM   1992 N  N   . VAL A 1 241 ? 19.514  -9.272  6.586   1.00 8.27   ? 241 VAL A N   1 
ATOM   1993 C  CA  . VAL A 1 241 ? 18.964  -10.121 7.636   1.00 8.49   ? 241 VAL A CA  1 
ATOM   1994 C  C   . VAL A 1 241 ? 19.756  -9.861  8.896   1.00 7.67   ? 241 VAL A C   1 
ATOM   1995 O  O   . VAL A 1 241 ? 20.919  -9.458  8.850   1.00 9.06   ? 241 VAL A O   1 
ATOM   1996 C  CB  . VAL A 1 241 ? 19.057  -11.655 7.268   1.00 8.56   ? 241 VAL A CB  1 
ATOM   1997 C  CG1 . VAL A 1 241 ? 18.149  -11.970 6.082   1.00 10.90  ? 241 VAL A CG1 1 
ATOM   1998 C  CG2 . VAL A 1 241 ? 20.515  -12.105 6.999   1.00 10.24  ? 241 VAL A CG2 1 
ATOM   1999 N  N   . ASP A 1 242 ? 19.131  -10.158 10.040  1.00 7.74   ? 242 ASP A N   1 
ATOM   2000 C  CA  . ASP A 1 242 ? 19.798  -10.045 11.336  1.00 8.46   ? 242 ASP A CA  1 
ATOM   2001 C  C   . ASP A 1 242 ? 20.287  -8.644  11.597  1.00 7.95   ? 242 ASP A C   1 
ATOM   2002 O  O   . ASP A 1 242 ? 21.401  -8.409  12.091  1.00 9.95   ? 242 ASP A O   1 
ATOM   2003 C  CB  . ASP A 1 242 ? 20.876  -11.110 11.558  1.00 9.57   ? 242 ASP A CB  1 
ATOM   2004 C  CG  . ASP A 1 242 ? 20.273  -12.508 11.631  1.00 9.73   ? 242 ASP A CG  1 
ATOM   2005 O  OD1 . ASP A 1 242 ? 19.200  -12.674 12.268  1.00 8.45   ? 242 ASP A OD1 1 
ATOM   2006 O  OD2 . ASP A 1 242 ? 20.856  -13.425 11.014  1.00 11.48  ? 242 ASP A OD2 1 
ATOM   2007 N  N   . ASN A 1 243 ? 19.423  -7.668  11.339  1.00 7.56   ? 243 ASN A N   1 
ATOM   2008 C  CA  . ASN A 1 243 ? 19.680  -6.251  11.600  1.00 7.35   ? 243 ASN A CA  1 
ATOM   2009 C  C   . ASN A 1 243 ? 19.115  -5.825  12.953  1.00 7.17   ? 243 ASN A C   1 
ATOM   2010 O  O   . ASN A 1 243 ? 18.440  -4.786  13.044  1.00 8.94   ? 243 ASN A O   1 
ATOM   2011 C  CB  . ASN A 1 243 ? 19.196  -5.402  10.427  1.00 7.61   ? 243 ASN A CB  1 
ATOM   2012 C  CG  . ASN A 1 243 ? 17.733  -5.591  10.121  1.00 7.65   ? 243 ASN A CG  1 
ATOM   2013 O  OD1 . ASN A 1 243 ? 17.044  -6.419  10.730  1.00 8.96   ? 243 ASN A OD1 1 
ATOM   2014 N  ND2 . ASN A 1 243 ? 17.227  -4.858  9.162   1.00 10.42  ? 243 ASN A ND2 1 
ATOM   2015 N  N   . TRP A 1 244 ? 19.374  -6.633  13.983  1.00 7.04   ? 244 TRP A N   1 
ATOM   2016 C  CA  . TRP A 1 244 ? 18.904  -6.377  15.335  1.00 7.02   ? 244 TRP A CA  1 
ATOM   2017 C  C   . TRP A 1 244 ? 20.139  -6.261  16.239  1.00 6.87   ? 244 TRP A C   1 
ATOM   2018 O  O   . TRP A 1 244 ? 21.095  -7.015  16.075  1.00 8.41   ? 244 TRP A O   1 
ATOM   2019 C  CB  . TRP A 1 244 ? 17.949  -7.483  15.797  1.00 7.44   ? 244 TRP A CB  1 
ATOM   2020 C  CG  . TRP A 1 244 ? 18.393  -8.892  15.593  1.00 6.95   ? 244 TRP A CG  1 
ATOM   2021 C  CD1 . TRP A 1 244 ? 18.310  -9.612  14.422  1.00 7.51   ? 244 TRP A CD1 1 
ATOM   2022 C  CD2 . TRP A 1 244 ? 18.998  -9.771  16.551  1.00 7.50   ? 244 TRP A CD2 1 
ATOM   2023 N  NE1 . TRP A 1 244 ? 18.789  -10.881 14.594  1.00 7.80   ? 244 TRP A NE1 1 
ATOM   2024 C  CE2 . TRP A 1 244 ? 19.263  -10.998 15.889  1.00 7.98   ? 244 TRP A CE2 1 
ATOM   2025 C  CE3 . TRP A 1 244 ? 19.326  -9.642  17.915  1.00 9.25   ? 244 TRP A CE3 1 
ATOM   2026 C  CZ2 . TRP A 1 244 ? 19.804  -12.110 16.576  1.00 9.31   ? 244 TRP A CZ2 1 
ATOM   2027 C  CZ3 . TRP A 1 244 ? 19.838  -10.753 18.570  1.00 10.67  ? 244 TRP A CZ3 1 
ATOM   2028 C  CH2 . TRP A 1 244 ? 20.098  -11.947 17.905  1.00 10.00  ? 244 TRP A CH2 1 
ATOM   2029 N  N   . ARG A 1 245 ? 19.995  -5.420  17.252  1.00 7.24   ? 245 ARG A N   1 
ATOM   2030 C  CA  . ARG A 1 245 ? 20.967  -5.336  18.314  1.00 7.30   ? 245 ARG A CA  1 
ATOM   2031 C  C   . ARG A 1 245 ? 20.527  -6.280  19.410  1.00 7.66   ? 245 ARG A C   1 
ATOM   2032 O  O   . ARG A 1 245 ? 19.337  -6.286  19.775  1.00 8.09   ? 245 ARG A O   1 
ATOM   2033 C  CB  . ARG A 1 245 ? 21.045  -3.901  18.830  1.00 7.75   ? 245 ARG A CB  1 
ATOM   2034 C  CG  . ARG A 1 245 ? 22.172  -3.701  19.835  1.00 7.17   ? 245 ARG A CG  1 
ATOM   2035 C  CD  . ARG A 1 245 ? 22.102  -2.352  20.495  1.00 7.63   ? 245 ARG A CD  1 
ATOM   2036 N  NE  . ARG A 1 245 ? 23.344  -2.068  21.231  1.00 7.95   ? 245 ARG A NE  1 
ATOM   2037 C  CZ  . ARG A 1 245 ? 23.539  -1.067  22.070  1.00 8.19   ? 245 ARG A CZ  1 
ATOM   2038 N  NH1 . ARG A 1 245 ? 22.547  -0.276  22.467  1.00 8.94   ? 245 ARG A NH1 1 
ATOM   2039 N  NH2 . ARG A 1 245 ? 24.778  -0.811  22.526  1.00 9.83   ? 245 ARG A NH2 1 
ATOM   2040 N  N   . PRO A 1 246 ? 21.413  -7.091  20.029  1.00 8.42   ? 246 PRO A N   1 
ATOM   2041 C  CA  . PRO A 1 246 ? 20.976  -7.934  21.132  1.00 9.74   ? 246 PRO A CA  1 
ATOM   2042 C  C   . PRO A 1 246 ? 20.636  -7.124  22.386  1.00 7.99   ? 246 PRO A C   1 
ATOM   2043 O  O   . PRO A 1 246 ? 21.008  -5.953  22.535  1.00 8.62   ? 246 PRO A O   1 
ATOM   2044 C  CB  . PRO A 1 246 ? 22.205  -8.787  21.479  1.00 11.83  ? 246 PRO A CB  1 
ATOM   2045 C  CG  . PRO A 1 246 ? 23.091  -8.605  20.309  1.00 18.27  ? 246 PRO A CG  1 
ATOM   2046 C  CD  . PRO A 1 246 ? 22.807  -7.294  19.629  1.00 11.08  ? 246 PRO A CD  1 
ATOM   2047 N  N   . ALA A 1 247 ? 19.978  -7.795  23.320  1.00 8.82   ? 247 ALA A N   1 
ATOM   2048 C  CA  . ALA A 1 247 ? 19.611  -7.168  24.574  1.00 8.95   ? 247 ALA A CA  1 
ATOM   2049 C  C   . ALA A 1 247 ? 20.843  -6.663  25.317  1.00 8.57   ? 247 ALA A C   1 
ATOM   2050 O  O   . ALA A 1 247 ? 21.889  -7.348  25.375  1.00 9.83   ? 247 ALA A O   1 
ATOM   2051 C  CB  . ALA A 1 247 ? 18.867  -8.192  25.436  1.00 11.03  ? 247 ALA A CB  1 
ATOM   2052 N  N   . GLN A 1 248 ? 20.727  -5.477  25.913  1.00 8.06   ? 248 GLN A N   1 
ATOM   2053 C  CA  . GLN A 1 248 ? 21.783  -4.780  26.660  1.00 8.85   ? 248 GLN A CA  1 
ATOM   2054 C  C   . GLN A 1 248 ? 21.463  -4.802  28.139  1.00 9.27   ? 248 GLN A C   1 
ATOM   2055 O  O   . GLN A 1 248 ? 20.316  -5.047  28.540  1.00 10.68  ? 248 GLN A O   1 
ATOM   2056 C  CB  . GLN A 1 248 ? 21.828  -3.333  26.198  1.00 8.78   ? 248 GLN A CB  1 
ATOM   2057 C  CG  . GLN A 1 248 ? 22.173  -3.274  24.694  1.00 9.82   ? 248 GLN A CG  1 
ATOM   2058 C  CD  . GLN A 1 248 ? 23.496  -3.938  24.344  1.00 10.30  ? 248 GLN A CD  1 
ATOM   2059 O  OE1 . GLN A 1 248 ? 24.506  -3.637  24.942  1.00 13.02  ? 248 GLN A OE1 1 
ATOM   2060 N  NE2 . GLN A 1 248 ? 23.455  -4.868  23.410  1.00 10.73  ? 248 GLN A NE2 1 
ATOM   2061 N  N   . PRO A 1 249 ? 22.459  -4.564  29.010  1.00 10.63  ? 249 PRO A N   1 
ATOM   2062 C  CA  . PRO A 1 249 ? 22.166  -4.685  30.452  1.00 12.58  ? 249 PRO A CA  1 
ATOM   2063 C  C   . PRO A 1 249 ? 21.152  -3.631  30.935  1.00 10.56  ? 249 PRO A C   1 
ATOM   2064 O  O   . PRO A 1 249 ? 21.218  -2.447  30.596  1.00 10.68  ? 249 PRO A O   1 
ATOM   2065 C  CB  . PRO A 1 249 ? 23.567  -4.324  31.022  1.00 18.43  ? 249 PRO A CB  1 
ATOM   2066 C  CG  . PRO A 1 249 ? 24.565  -4.634  29.970  1.00 17.39  ? 249 PRO A CG  1 
ATOM   2067 C  CD  . PRO A 1 249 ? 23.861  -4.328  28.664  1.00 13.72  ? 249 PRO A CD  1 
ATOM   2068 N  N   . LEU A 1 250 ? 20.223  -4.096  31.784  1.00 11.34  ? 250 LEU A N   1 
ATOM   2069 C  CA  . LEU A 1 250 ? 19.200  -3.222  32.304  1.00 10.47  ? 250 LEU A CA  1 
ATOM   2070 C  C   . LEU A 1 250 ? 19.769  -2.173  33.279  1.00 11.12  ? 250 LEU A C   1 
ATOM   2071 O  O   . LEU A 1 250 ? 19.235  -1.056  33.399  1.00 11.74  ? 250 LEU A O   1 
ATOM   2072 C  CB  . LEU A 1 250 ? 18.128  -4.083  32.961  1.00 13.45  ? 250 LEU A CB  1 
ATOM   2073 C  CG  . LEU A 1 250 ? 16.864  -3.352  33.380  1.00 12.42  ? 250 LEU A CG  1 
ATOM   2074 C  CD1 . LEU A 1 250 ? 16.119  -2.722  32.180  1.00 12.94  ? 250 LEU A CD1 1 
ATOM   2075 C  CD2 . LEU A 1 250 ? 15.943  -4.330  34.172  1.00 16.34  ? 250 LEU A CD2 1 
ATOM   2076 N  N   A LYS A 1 251 ? 20.848  -2.523  33.972  0.50 12.96  ? 251 LYS A N   1 
ATOM   2077 N  N   B LYS A 1 251 ? 20.844  -2.547  33.959  0.50 13.07  ? 251 LYS A N   1 
ATOM   2078 C  CA  A LYS A 1 251 ? 21.529  -1.606  34.881  0.50 15.34  ? 251 LYS A CA  1 
ATOM   2079 C  CA  B LYS A 1 251 ? 21.473  -1.631  34.891  0.50 16.50  ? 251 LYS A CA  1 
ATOM   2080 C  C   A LYS A 1 251 ? 20.614  -1.269  36.046  0.50 16.83  ? 251 LYS A C   1 
ATOM   2081 C  C   B LYS A 1 251 ? 20.416  -1.252  35.911  0.50 20.09  ? 251 LYS A C   1 
ATOM   2082 O  O   A LYS A 1 251 ? 20.089  -2.197  36.672  0.50 20.59  ? 251 LYS A O   1 
ATOM   2083 O  O   B LYS A 1 251 ? 19.602  -2.108  36.298  0.50 26.51  ? 251 LYS A O   1 
ATOM   2084 C  CB  A LYS A 1 251 ? 22.276  -0.489  34.152  0.50 18.00  ? 251 LYS A CB  1 
ATOM   2085 C  CB  B LYS A 1 251 ? 22.188  -0.519  34.125  0.50 17.53  ? 251 LYS A CB  1 
ATOM   2086 C  CG  A LYS A 1 251 ? 23.461  -1.071  33.354  0.50 20.55  ? 251 LYS A CG  1 
ATOM   2087 C  CG  B LYS A 1 251 ? 23.175  -1.091  33.108  0.50 21.08  ? 251 LYS A CG  1 
ATOM   2088 C  CD  A LYS A 1 251 ? 24.266  -0.126  32.530  0.50 21.01  ? 251 LYS A CD  1 
ATOM   2089 C  CD  B LYS A 1 251 ? 24.470  -0.350  33.005  0.50 24.96  ? 251 LYS A CD  1 
ATOM   2090 C  CE  A LYS A 1 251 ? 25.524  -0.845  32.025  0.50 24.74  ? 251 LYS A CE  1 
ATOM   2091 C  CE  B LYS A 1 251 ? 25.582  -1.179  32.388  0.50 21.84  ? 251 LYS A CE  1 
ATOM   2092 N  NZ  A LYS A 1 251 ? 26.482  0.059   31.339  0.50 26.05  ? 251 LYS A NZ  1 
ATOM   2093 N  NZ  B LYS A 1 251 ? 26.561  -1.648  33.407  0.50 22.19  ? 251 LYS A NZ  1 
ATOM   2094 N  N   . ASN A 1 252 ? 20.354  0.020   36.274  1.00 18.15  ? 252 ASN A N   1 
ATOM   2095 C  CA  . ASN A 1 252 ? 19.447  0.295   37.441  1.00 24.04  ? 252 ASN A CA  1 
ATOM   2096 C  C   . ASN A 1 252 ? 17.976  0.549   37.084  1.00 23.43  ? 252 ASN A C   1 
ATOM   2097 O  O   . ASN A 1 252 ? 17.141  0.821   37.994  1.00 29.18  ? 252 ASN A O   1 
ATOM   2098 C  CB  . ASN A 1 252 ? 20.089  1.218   38.485  1.00 33.43  ? 252 ASN A CB  1 
ATOM   2099 C  CG  . ASN A 1 252 ? 21.317  0.610   39.138  1.00 35.09  ? 252 ASN A CG  1 
ATOM   2100 O  OD1 . ASN A 1 252 ? 22.406  1.173   39.049  1.00 57.11  ? 252 ASN A OD1 1 
ATOM   2101 N  ND2 . ASN A 1 252 ? 21.164  -0.532  39.796  1.00 36.66  ? 252 ASN A ND2 1 
ATOM   2102 N  N   . ARG A 1 253 ? 17.604  0.203   35.869  1.00 13.08  ? 253 ARG A N   1 
ATOM   2103 C  CA  . ARG A 1 253 ? 16.321  0.675   35.414  1.00 11.01  ? 253 ARG A CA  1 
ATOM   2104 C  C   . ARG A 1 253 ? 15.237  -0.280  35.864  1.00 11.15  ? 253 ARG A C   1 
ATOM   2105 O  O   . ARG A 1 253 ? 15.467  -1.460  36.084  1.00 15.40  ? 253 ARG A O   1 
ATOM   2106 C  CB  . ARG A 1 253 ? 16.340  0.744   33.906  1.00 9.99   ? 253 ARG A CB  1 
ATOM   2107 C  CG  . ARG A 1 253 ? 17.235  1.857   33.383  1.00 10.68  ? 253 ARG A CG  1 
ATOM   2108 C  CD  . ARG A 1 253 ? 17.343  1.856   31.900  1.00 9.86   ? 253 ARG A CD  1 
ATOM   2109 N  NE  . ARG A 1 253 ? 18.147  0.721   31.424  1.00 9.37   ? 253 ARG A NE  1 
ATOM   2110 C  CZ  . ARG A 1 253 ? 18.360  0.439   30.139  1.00 7.73   ? 253 ARG A CZ  1 
ATOM   2111 N  NH1 . ARG A 1 253 ? 17.767  1.129   29.174  1.00 7.80   ? 253 ARG A NH1 1 
ATOM   2112 N  NH2 . ARG A 1 253 ? 19.206  -0.534  29.818  1.00 7.75   ? 253 ARG A NH2 1 
ATOM   2113 N  N   . GLN A 1 254 ? 14.014  0.223   35.903  1.00 12.04  ? 254 GLN A N   1 
ATOM   2114 C  CA  . GLN A 1 254 ? 12.795  -0.531  36.119  1.00 12.54  ? 254 GLN A CA  1 
ATOM   2115 C  C   . GLN A 1 254 ? 11.940  -0.498  34.865  1.00 12.24  ? 254 GLN A C   1 
ATOM   2116 O  O   . GLN A 1 254 ? 11.779  0.565   34.219  1.00 15.44  ? 254 GLN A O   1 
ATOM   2117 C  CB  . GLN A 1 254 ? 12.021  0.112   37.264  1.00 18.74  ? 254 GLN A CB  1 
ATOM   2118 C  CG  . GLN A 1 254 ? 10.838  -0.707  37.784  1.00 30.60  ? 254 GLN A CG  1 
ATOM   2119 C  CD  . GLN A 1 254 ? 10.676  -0.533  39.286  1.00 60.90  ? 254 GLN A CD  1 
ATOM   2120 O  OE1 . GLN A 1 254 ? 10.106  -1.388  39.965  1.00 52.74  ? 254 GLN A OE1 1 
ATOM   2121 N  NE2 . GLN A 1 254 ? 11.252  0.559   39.814  1.00 53.20  ? 254 GLN A NE2 1 
ATOM   2122 N  N   . ILE A 1 255 ? 11.410  -1.653  34.501  1.00 10.50  ? 255 ILE A N   1 
ATOM   2123 C  CA  . ILE A 1 255 ? 10.413  -1.738  33.458  1.00 10.35  ? 255 ILE A CA  1 
ATOM   2124 C  C   . ILE A 1 255 ? 9.034   -1.726  34.122  1.00 9.95   ? 255 ILE A C   1 
ATOM   2125 O  O   . ILE A 1 255 ? 8.822   -2.442  35.107  1.00 12.27  ? 255 ILE A O   1 
ATOM   2126 C  CB  . ILE A 1 255 ? 10.611  -3.000  32.624  1.00 9.95   ? 255 ILE A CB  1 
ATOM   2127 C  CG1 . ILE A 1 255 ? 12.059  -3.033  32.079  1.00 10.36  ? 255 ILE A CG1 1 
ATOM   2128 C  CG2 . ILE A 1 255 ? 9.542   -3.060  31.522  1.00 11.55  ? 255 ILE A CG2 1 
ATOM   2129 C  CD1 . ILE A 1 255 ? 12.302  -4.251  31.165  1.00 12.69  ? 255 ILE A CD1 1 
ATOM   2130 N  N   . LYS A 1 256 ? 8.129   -0.862  33.647  1.00 9.62   ? 256 LYS A N   1 
ATOM   2131 C  CA  . LYS A 1 256 ? 6.776   -0.781  34.195  1.00 9.95   ? 256 LYS A CA  1 
ATOM   2132 C  C   . LYS A 1 256 ? 5.826   -1.437  33.214  1.00 9.51   ? 256 LYS A C   1 
ATOM   2133 O  O   . LYS A 1 256 ? 6.028   -1.392  32.016  1.00 11.28  ? 256 LYS A O   1 
ATOM   2134 C  CB  . LYS A 1 256 ? 6.416   0.700   34.442  1.00 12.43  ? 256 LYS A CB  1 
ATOM   2135 C  CG  . LYS A 1 256 ? 7.322   1.391   35.474  1.00 18.82  ? 256 LYS A CG  1 
ATOM   2136 C  CD  . LYS A 1 256 ? 7.040   2.811   35.706  1.00 29.01  ? 256 LYS A CD  1 
ATOM   2137 N  N   . ALA A 1 257 ? 4.777   -2.058  33.737  1.00 10.10  ? 257 ALA A N   1 
ATOM   2138 C  CA  . ALA A 1 257 ? 3.719   -2.658  32.957  1.00 10.37  ? 257 ALA A CA  1 
ATOM   2139 C  C   . ALA A 1 257 ? 2.443   -1.855  33.116  1.00 9.12   ? 257 ALA A C   1 
ATOM   2140 O  O   . ALA A 1 257 ? 2.081   -1.428  34.233  1.00 11.93  ? 257 ALA A O   1 
ATOM   2141 C  CB  . ALA A 1 257 ? 3.475   -4.109  33.334  1.00 13.14  ? 257 ALA A CB  1 
ATOM   2142 N  N   . SER A 1 258 ? 1.682   -1.730  32.053  1.00 10.32  ? 258 SER A N   1 
ATOM   2143 C  CA  . SER A 1 258 ? 0.404   -1.055  32.071  1.00 12.41  ? 258 SER A CA  1 
ATOM   2144 C  C   . SER A 1 258 ? -0.716  -1.958  32.525  1.00 12.16  ? 258 SER A C   1 
ATOM   2145 O  O   . SER A 1 258 ? -1.827  -1.444  32.602  1.00 17.46  ? 258 SER A O   1 
ATOM   2146 C  CB  . SER A 1 258 ? 0.107   -0.519  30.716  1.00 13.01  ? 258 SER A CB  1 
ATOM   2147 O  OG  . SER A 1 258 ? -0.311  -1.540  29.828  1.00 11.75  ? 258 SER A OG  1 
ATOM   2148 N  N   . PHE A 1 259 ? -0.439  -3.236  32.779  1.00 14.08  ? 259 PHE A N   1 
ATOM   2149 C  CA  . PHE A 1 259 ? -1.459  -4.283  32.961  1.00 17.09  ? 259 PHE A CA  1 
ATOM   2150 C  C   . PHE A 1 259 ? -0.958  -5.234  34.065  1.00 22.75  ? 259 PHE A C   1 
ATOM   2151 O  O   . PHE A 1 259 ? 0.273   -5.320  34.315  1.00 20.89  ? 259 PHE A O   1 
ATOM   2152 C  CB  . PHE A 1 259 ? -1.680  -5.021  31.642  1.00 15.68  ? 259 PHE A CB  1 
ATOM   2153 C  CG  . PHE A 1 259 ? -0.407  -5.739  31.229  1.00 14.40  ? 259 PHE A CG  1 
ATOM   2154 C  CD1 . PHE A 1 259 ? 0.582   -5.110  30.510  1.00 12.30  ? 259 PHE A CD1 1 
ATOM   2155 C  CD2 . PHE A 1 259 ? -0.181  -7.059  31.637  1.00 19.42  ? 259 PHE A CD2 1 
ATOM   2156 C  CE1 . PHE A 1 259 ? 1.770   -5.738  30.190  1.00 14.74  ? 259 PHE A CE1 1 
ATOM   2157 C  CE2 . PHE A 1 259 ? 1.034   -7.669  31.381  1.00 21.44  ? 259 PHE A CE2 1 
ATOM   2158 C  CZ  . PHE A 1 259 ? 1.962   -7.028  30.610  1.00 17.81  ? 259 PHE A CZ  1 
ATOM   2159 N  N   . LYS A 1 260 ? -1.944  -6.120  34.341  1.00 40.21  ? 260 LYS A N   1 
ATOM   2160 C  CA  . LYS A 1 260 ? -2.069  -7.302  35.245  1.00 52.14  ? 260 LYS A CA  1 
ATOM   2161 C  C   . LYS A 1 260 ? -1.214  -7.073  36.498  1.00 63.89  ? 260 LYS A C   1 
ATOM   2162 O  O   . LYS A 1 260 ? -0.014  -7.345  36.456  1.00 84.74  ? 260 LYS A O   1 
ATOM   2163 C  CB  . LYS A 1 260 ? -1.644  -8.580  34.515  1.00 51.49  ? 260 LYS A CB  1 
ATOM   2164 C  CG  . LYS A 1 260 ? -2.228  -8.758  33.120  1.00 75.48  ? 260 LYS A CG  1 
ATOM   2165 O  OXT . LYS A 1 260 ? -1.783  -6.620  37.502  1.00 64.52  ? 260 LYS A OXT 1 
HETATM 2166 ZN ZN  . ZN  B 2 .   ? 14.346  0.229   15.449  1.00 6.97   ? 301 ZN  A ZN  1 
HETATM 2167 F  F27 A WWO C 3 .   ? 14.217  5.143   15.210  0.30 17.44  ? 302 WWO A F27 1 
HETATM 2168 F  F27 B WWO C 3 .   ? 15.005  5.536   16.096  0.70 17.57  ? 302 WWO A F27 1 
HETATM 2169 C  C5  A WWO C 3 .   ? 15.542  5.122   15.262  0.30 16.32  ? 302 WWO A C5  1 
HETATM 2170 C  C5  B WWO C 3 .   ? 15.792  4.847   15.225  0.70 17.22  ? 302 WWO A C5  1 
HETATM 2171 C  C4  A WWO C 3 .   ? 16.178  4.108   15.969  0.30 12.01  ? 302 WWO A C4  1 
HETATM 2172 C  C4  B WWO C 3 .   ? 15.911  3.512   15.391  0.70 13.38  ? 302 WWO A C4  1 
HETATM 2173 S  S7  A WWO C 3 .   ? 15.342  2.800   16.856  0.30 7.87   ? 302 WWO A S7  1 
HETATM 2174 S  S7  B WWO C 3 .   ? 15.283  2.770   16.850  0.70 8.28   ? 302 WWO A S7  1 
HETATM 2175 O  O9  A WWO C 3 .   ? 13.911  3.063   16.783  0.30 8.73   ? 302 WWO A O9  1 
HETATM 2176 O  O9  B WWO C 3 .   ? 13.890  3.019   16.816  0.70 9.30   ? 302 WWO A O9  1 
HETATM 2177 N  N10 A WWO C 3 .   ? 15.675  1.288   16.201  0.30 10.85  ? 302 WWO A N10 1 
HETATM 2178 N  N10 B WWO C 3 .   ? 15.582  1.279   16.519  0.70 10.51  ? 302 WWO A N10 1 
HETATM 2179 O  O8  A WWO C 3 .   ? 15.944  2.969   18.161  0.30 9.39   ? 302 WWO A O8  1 
HETATM 2180 O  O8  B WWO C 3 .   ? 16.029  3.184   18.023  0.70 10.01  ? 302 WWO A O8  1 
HETATM 2181 C  C3  A WWO C 3 .   ? 17.567  4.166   16.011  0.30 11.12  ? 302 WWO A C3  1 
HETATM 2182 C  C3  B WWO C 3 .   ? 16.619  2.740   14.331  0.70 11.83  ? 302 WWO A C3  1 
HETATM 2183 F  F12 A WWO C 3 .   ? 18.266  3.222   16.691  0.30 11.04  ? 302 WWO A F12 1 
HETATM 2184 F  F12 B WWO C 3 .   ? 16.952  1.407   14.579  0.70 16.09  ? 302 WWO A F12 1 
HETATM 2185 C  C2  A WWO C 3 .   ? 18.292  5.139   15.382  0.30 12.48  ? 302 WWO A C2  1 
HETATM 2186 C  C2  B WWO C 3 .   ? 17.220  3.301   13.328  0.70 16.35  ? 302 WWO A C2  1 
HETATM 2187 F  F13 A WWO C 3 .   ? 19.638  5.151   15.545  0.30 12.71  ? 302 WWO A F13 1 
HETATM 2188 F  F13 B WWO C 3 .   ? 17.895  2.596   12.395  0.70 15.38  ? 302 WWO A F13 1 
HETATM 2189 C  C6  A WWO C 3 .   ? 16.254  6.138   14.556  0.30 16.03  ? 302 WWO A C6  1 
HETATM 2190 C  C6  B WWO C 3 .   ? 16.266  5.462   14.018  0.70 19.55  ? 302 WWO A C6  1 
HETATM 2191 C  C1  A WWO C 3 .   ? 17.686  6.127   14.646  0.30 11.34  ? 302 WWO A C1  1 
HETATM 2192 C  C1  B WWO C 3 .   ? 17.008  4.696   13.024  0.70 20.21  ? 302 WWO A C1  1 
HETATM 2193 S  S11 A WWO C 3 .   ? 18.844  7.210   13.769  0.30 15.38  ? 302 WWO A S11 1 
HETATM 2194 S  S11 B WWO C 3 .   ? 17.839  5.328   11.606  0.70 18.18  ? 302 WWO A S11 1 
HETATM 2195 O  O22 A WWO C 3 .   ? 18.062  7.998   12.861  0.30 18.85  ? 302 WWO A O22 1 
HETATM 2196 O  O22 B WWO C 3 .   ? 17.554  6.731   11.518  0.70 25.46  ? 302 WWO A O22 1 
HETATM 2197 O  O23 A WWO C 3 .   ? 19.845  6.360   13.192  0.30 28.32  ? 302 WWO A O23 1 
HETATM 2198 O  O23 B WWO C 3 .   ? 17.493  4.500   10.487  0.70 38.72  ? 302 WWO A O23 1 
HETATM 2199 C  C21 A WWO C 3 .   ? 19.680  8.331   14.808  0.30 14.61  ? 302 WWO A C21 1 
HETATM 2200 C  C21 B WWO C 3 .   ? 19.534  5.150   11.892  0.70 16.71  ? 302 WWO A C21 1 
HETATM 2201 C  C24 A WWO C 3 .   ? 19.367  9.821   14.488  0.30 21.14  ? 302 WWO A C24 1 
HETATM 2202 C  C24 B WWO C 3 .   ? 20.230  6.120   12.827  0.70 20.33  ? 302 WWO A C24 1 
HETATM 2203 O  O25 A WWO C 3 .   ? 20.140  10.582  15.390  0.30 23.33  ? 302 WWO A O25 1 
HETATM 2204 O  O25 B WWO C 3 .   ? 19.885  5.848   14.156  0.70 20.53  ? 302 WWO A O25 1 
HETATM 2205 N  N26 A WWO C 3 .   ? 15.633  7.181   13.798  0.30 16.32  ? 302 WWO A N26 1 
HETATM 2206 N  N26 B WWO C 3 .   ? 15.962  6.832   13.895  0.70 20.03  ? 302 WWO A N26 1 
HETATM 2207 C  C14 A WWO C 3 .   ? 14.349  7.156   13.011  0.30 30.17  ? 302 WWO A C14 1 
HETATM 2208 C  C14 B WWO C 3 .   ? 14.858  6.748   12.877  0.70 41.27  ? 302 WWO A C14 1 
HETATM 2209 C  C15 A WWO C 3 .   ? 14.541  7.969   11.699  0.30 38.76  ? 302 WWO A C15 1 
HETATM 2210 C  C15 B WWO C 3 .   ? 14.561  7.817   11.962  0.70 40.69  ? 302 WWO A C15 1 
HETATM 2211 C  C20 A WWO C 3 .   ? 15.458  7.562   10.646  0.30 49.92  ? 302 WWO A C20 1 
HETATM 2212 C  C20 B WWO C 3 .   ? 15.014  7.821   10.629  0.70 45.87  ? 302 WWO A C20 1 
HETATM 2213 C  C19 A WWO C 3 .   ? 15.349  8.246   9.433   0.30 56.06  ? 302 WWO A C19 1 
HETATM 2214 C  C19 B WWO C 3 .   ? 14.652  8.892   9.802   0.70 54.14  ? 302 WWO A C19 1 
HETATM 2215 C  C18 A WWO C 3 .   ? 14.539  9.406   9.246   0.30 63.08  ? 302 WWO A C18 1 
HETATM 2216 C  C18 B WWO C 3 .   ? 13.829  9.924   10.328  0.70 63.68  ? 302 WWO A C18 1 
HETATM 2217 C  C17 A WWO C 3 .   ? 13.781  9.923   10.345  0.30 46.08  ? 302 WWO A C17 1 
HETATM 2218 C  C17 B WWO C 3 .   ? 13.409  9.947   11.676  0.70 63.04  ? 302 WWO A C17 1 
HETATM 2219 C  C16 A WWO C 3 .   ? 13.783  9.236   11.626  0.30 44.14  ? 302 WWO A C16 1 
HETATM 2220 C  C16 B WWO C 3 .   ? 13.756  8.848   12.521  0.70 49.77  ? 302 WWO A C16 1 
HETATM 2221 S  S   . DMS D 4 .   ? 22.398  -9.793  14.936  1.00 22.50  ? 303 DMS A S   1 
HETATM 2222 O  O   . DMS D 4 .   ? 23.021  -11.140 14.511  1.00 33.73  ? 303 DMS A O   1 
HETATM 2223 C  C1  . DMS D 4 .   ? 22.640  -9.681  16.633  1.00 18.68  ? 303 DMS A C1  1 
HETATM 2224 C  C2  . DMS D 4 .   ? 23.593  -8.605  14.519  1.00 29.14  ? 303 DMS A C2  1 
HETATM 2225 O  O1  . MES E 5 .   ? 13.541  -7.121  -2.487  1.00 28.45  ? 304 MES A O1  1 
HETATM 2226 C  C2  . MES E 5 .   ? 12.864  -7.762  -1.400  1.00 25.02  ? 304 MES A C2  1 
HETATM 2227 C  C3  . MES E 5 .   ? 11.487  -8.330  -1.634  1.00 22.99  ? 304 MES A C3  1 
HETATM 2228 N  N4  . MES E 5 .   ? 11.315  -8.717  -3.105  1.00 33.64  ? 304 MES A N4  1 
HETATM 2229 C  C5  . MES E 5 .   ? 12.598  -8.970  -3.858  1.00 35.06  ? 304 MES A C5  1 
HETATM 2230 C  C6  . MES E 5 .   ? 13.721  -7.989  -3.608  1.00 34.63  ? 304 MES A C6  1 
HETATM 2231 C  C7  . MES E 5 .   ? 10.398  -9.882  -3.343  1.00 36.25  ? 304 MES A C7  1 
HETATM 2232 C  C8  . MES E 5 .   ? 8.948   -9.562  -3.102  1.00 29.57  ? 304 MES A C8  1 
HETATM 2233 N  N1  . BCN F 6 .   ? 0.442   -12.884 23.424  1.00 37.22  ? 305 BCN A N1  1 
HETATM 2234 C  C1  . BCN F 6 .   ? 1.343   -12.323 24.464  1.00 34.75  ? 305 BCN A C1  1 
HETATM 2235 C  C2  . BCN F 6 .   ? 0.919   -13.072 25.737  1.00 44.71  ? 305 BCN A C2  1 
HETATM 2236 O  O21 . BCN F 6 .   ? -0.275  -12.908 26.166  1.00 70.52  ? 305 BCN A O21 1 
HETATM 2237 O  O22 . BCN F 6 .   ? 1.735   -13.827 26.240  1.00 57.82  ? 305 BCN A O22 1 
HETATM 2238 C  C3  . BCN F 6 .   ? -0.615  -11.971 22.951  1.00 26.66  ? 305 BCN A C3  1 
HETATM 2239 C  C4  . BCN F 6 .   ? -1.723  -11.599 23.939  1.00 41.16  ? 305 BCN A C4  1 
HETATM 2240 O  O4  . BCN F 6 .   ? -1.421  -10.461 24.791  1.00 29.13  ? 305 BCN A O4  1 
HETATM 2241 C  C5  . BCN F 6 .   ? 1.094   -13.792 22.460  1.00 26.39  ? 305 BCN A C5  1 
HETATM 2242 C  C6  . BCN F 6 .   ? 0.125   -14.697 21.660  1.00 51.11  ? 305 BCN A C6  1 
HETATM 2243 O  O6  . BCN F 6 .   ? 0.307   -14.538 20.239  1.00 51.30  ? 305 BCN A O6  1 
HETATM 2244 O  O   . HOH G 7 .   ? -7.171  8.068   15.627  1.00 46.04  ? 401 HOH A O   1 
HETATM 2245 O  O   . HOH G 7 .   ? 27.978  3.180   31.885  1.00 41.18  ? 402 HOH A O   1 
HETATM 2246 O  O   . HOH G 7 .   ? 18.922  10.409  29.480  1.00 19.47  ? 403 HOH A O   1 
HETATM 2247 O  O   . HOH G 7 .   ? -4.438  -8.741  17.740  1.00 24.63  ? 404 HOH A O   1 
HETATM 2248 O  O   . HOH G 7 .   ? 2.066   19.618  18.673  1.00 42.11  ? 405 HOH A O   1 
HETATM 2249 O  O   . HOH G 7 .   ? 21.811  -6.510  -5.137  1.00 39.80  ? 406 HOH A O   1 
HETATM 2250 O  O   . HOH G 7 .   ? 9.667   -19.150 5.174   1.00 31.47  ? 407 HOH A O   1 
HETATM 2251 O  O   . HOH G 7 .   ? -5.890  -5.845  26.048  1.00 37.72  ? 408 HOH A O   1 
HETATM 2252 O  O   . HOH G 7 .   ? 32.783  1.566   16.268  1.00 24.70  ? 409 HOH A O   1 
HETATM 2253 O  O   . HOH G 7 .   ? -7.891  12.282  6.605   1.00 38.56  ? 410 HOH A O   1 
HETATM 2254 O  O   . HOH G 7 .   ? -2.418  -12.236 10.882  1.00 37.56  ? 411 HOH A O   1 
HETATM 2255 O  O   . HOH G 7 .   ? 7.317   -2.970  -6.415  1.00 41.61  ? 412 HOH A O   1 
HETATM 2256 O  O   . HOH G 7 .   ? 22.990  2.968   36.340  1.00 38.72  ? 413 HOH A O   1 
HETATM 2257 O  O   . HOH G 7 .   ? -4.410  11.536  13.611  1.00 37.22  ? 414 HOH A O   1 
HETATM 2258 O  O   . HOH G 7 .   ? -3.290  15.886  16.879  1.00 46.75  ? 415 HOH A O   1 
HETATM 2259 O  O   . HOH G 7 .   ? 3.363   -20.182 6.208   1.00 18.49  ? 416 HOH A O   1 
HETATM 2260 O  O   . HOH G 7 .   ? 7.845   -20.539 11.483  1.00 39.24  ? 417 HOH A O   1 
HETATM 2261 O  O   . HOH G 7 .   ? -1.551  -13.040 16.303  1.00 40.77  ? 418 HOH A O   1 
HETATM 2262 O  O   . HOH G 7 .   ? -4.630  8.123   27.234  1.00 35.75  ? 419 HOH A O   1 
HETATM 2263 O  O   . HOH G 7 .   ? 25.711  -0.951  29.174  1.00 21.65  ? 420 HOH A O   1 
HETATM 2264 O  O   . HOH G 7 .   ? 20.721  2.568   34.457  1.00 29.59  ? 421 HOH A O   1 
HETATM 2265 O  O   . HOH G 7 .   ? 0.071   -5.052  -1.874  1.00 32.24  ? 422 HOH A O   1 
HETATM 2266 O  O   . HOH G 7 .   ? -0.607  21.170  17.635  1.00 47.45  ? 423 HOH A O   1 
HETATM 2267 O  O   . HOH G 7 .   ? -0.549  -12.321 18.764  1.00 32.71  ? 424 HOH A O   1 
HETATM 2268 O  O   . HOH G 7 .   ? 6.862   -6.829  -5.203  1.00 29.36  ? 425 HOH A O   1 
HETATM 2269 O  O   . HOH G 7 .   ? 35.822  2.272   15.109  1.00 43.45  ? 426 HOH A O   1 
HETATM 2270 O  O   . HOH G 7 .   ? 20.858  11.295  18.617  1.00 39.89  ? 427 HOH A O   1 
HETATM 2271 O  O   . HOH G 7 .   ? 4.653   -12.699 33.337  1.00 37.60  ? 428 HOH A O   1 
HETATM 2272 O  O   . HOH G 7 .   ? 20.192  0.629   -12.784 1.00 44.76  ? 429 HOH A O   1 
HETATM 2273 O  O   . HOH G 7 .   ? 0.809   10.387  30.251  1.00 25.81  ? 430 HOH A O   1 
HETATM 2274 O  O   . HOH G 7 .   ? 32.235  -2.132  8.105   1.00 42.63  ? 431 HOH A O   1 
HETATM 2275 O  O   . HOH G 7 .   ? -2.860  -1.659  29.431  1.00 24.51  ? 432 HOH A O   1 
HETATM 2276 O  O   . HOH G 7 .   ? -3.109  10.538  20.531  1.00 18.75  ? 433 HOH A O   1 
HETATM 2277 O  O   . HOH G 7 .   ? 19.809  -2.240  15.749  1.00 10.06  ? 434 HOH A O   1 
HETATM 2278 O  O   . HOH G 7 .   ? 13.410  9.062   27.578  1.00 23.63  ? 435 HOH A O   1 
HETATM 2279 O  O   . HOH G 7 .   ? -4.463  0.182   35.241  1.00 38.21  ? 436 HOH A O   1 
HETATM 2280 O  O   . HOH G 7 .   ? 17.507  -3.002  37.569  1.00 26.65  ? 437 HOH A O   1 
HETATM 2281 O  O   . HOH G 7 .   ? -6.722  8.223   22.063  1.00 28.91  ? 438 HOH A O   1 
HETATM 2282 O  O   . HOH G 7 .   ? 8.143   -20.503 8.480   1.00 31.00  ? 439 HOH A O   1 
HETATM 2283 O  O   . HOH G 7 .   ? 4.492   7.315   -7.776  1.00 30.03  ? 440 HOH A O   1 
HETATM 2284 O  O   . HOH G 7 .   ? 11.365  17.588  29.471  1.00 21.14  ? 441 HOH A O   1 
HETATM 2285 O  O   . HOH G 7 .   ? 27.247  -9.099  15.812  1.00 43.34  ? 442 HOH A O   1 
HETATM 2286 O  O   . HOH G 7 .   ? 19.395  -1.033  11.306  1.00 33.33  ? 443 HOH A O   1 
HETATM 2287 O  O   . HOH G 7 .   ? 14.755  -2.605  -6.354  1.00 22.61  ? 444 HOH A O   1 
HETATM 2288 O  O   . HOH G 7 .   ? 3.710   -4.881  39.901  1.00 69.49  ? 445 HOH A O   1 
HETATM 2289 O  O   . HOH G 7 .   ? 9.039   14.213  29.257  1.00 20.51  ? 446 HOH A O   1 
HETATM 2290 O  O   . HOH G 7 .   ? 24.451  6.524   30.375  1.00 17.30  ? 447 HOH A O   1 
HETATM 2291 O  O   . HOH G 7 .   ? 3.870   -14.388 22.265  1.00 27.42  ? 448 HOH A O   1 
HETATM 2292 O  O   . HOH G 7 .   ? 6.658   -14.633 28.952  1.00 34.40  ? 449 HOH A O   1 
HETATM 2293 O  O   . HOH G 7 .   ? 16.319  -10.297 32.041  1.00 19.37  ? 450 HOH A O   1 
HETATM 2294 O  O   . HOH G 7 .   ? 12.372  2.657   -6.206  1.00 27.05  ? 451 HOH A O   1 
HETATM 2295 O  O   . HOH G 7 .   ? 5.840   -8.644  37.446  1.00 16.93  ? 452 HOH A O   1 
HETATM 2296 O  O   . HOH G 7 .   ? 25.443  -1.831  26.651  1.00 18.14  ? 453 HOH A O   1 
HETATM 2297 O  O   . HOH G 7 .   ? 10.763  10.436  25.699  1.00 11.41  ? 454 HOH A O   1 
HETATM 2298 O  O   . HOH G 7 .   ? -1.558  -7.857  25.401  1.00 24.43  ? 455 HOH A O   1 
HETATM 2299 O  O   . HOH G 7 .   ? 26.582  8.797   20.554  1.00 17.54  ? 456 HOH A O   1 
HETATM 2300 O  O   . HOH G 7 .   ? 21.084  0.979   -4.622  1.00 13.94  ? 457 HOH A O   1 
HETATM 2301 O  O   . HOH G 7 .   ? 23.106  9.601   27.954  1.00 16.30  ? 458 HOH A O   1 
HETATM 2302 O  O   . HOH G 7 .   ? 19.033  2.841   9.044   1.00 19.94  ? 459 HOH A O   1 
HETATM 2303 O  O   . HOH G 7 .   ? -2.181  -9.495  17.171  1.00 27.54  ? 460 HOH A O   1 
HETATM 2304 O  O   . HOH G 7 .   ? -2.179  1.882   34.336  1.00 44.84  ? 461 HOH A O   1 
HETATM 2305 O  O   . HOH G 7 .   ? -5.109  4.696   21.206  1.00 19.96  ? 462 HOH A O   1 
HETATM 2306 O  O   . HOH G 7 .   ? 6.247   12.950  34.795  1.00 24.78  ? 463 HOH A O   1 
HETATM 2307 O  O   . HOH G 7 .   ? 2.636   -2.015  -2.542  1.00 29.67  ? 464 HOH A O   1 
HETATM 2308 O  O   . HOH G 7 .   ? 1.031   12.610  27.161  1.00 18.87  ? 465 HOH A O   1 
HETATM 2309 O  O   . HOH G 7 .   ? 7.164   -19.044 3.490   1.00 34.99  ? 466 HOH A O   1 
HETATM 2310 O  O   . HOH G 7 .   ? 8.723   14.739  31.879  1.00 21.33  ? 467 HOH A O   1 
HETATM 2311 O  O   . HOH G 7 .   ? 25.396  0.574   36.635  1.00 44.91  ? 468 HOH A O   1 
HETATM 2312 O  O   . HOH G 7 .   ? 36.607  -0.455  14.754  1.00 22.61  ? 469 HOH A O   1 
HETATM 2313 O  O   . HOH G 7 .   ? 12.230  7.718   29.123  1.00 20.73  ? 470 HOH A O   1 
HETATM 2314 O  O   . HOH G 7 .   ? 13.121  -13.538 11.243  1.00 10.03  ? 471 HOH A O   1 
HETATM 2315 O  O   . HOH G 7 .   ? 7.597   12.164  28.137  1.00 15.14  ? 472 HOH A O   1 
HETATM 2316 O  O   . HOH G 7 .   ? 14.209  -13.225 31.517  1.00 22.76  ? 473 HOH A O   1 
HETATM 2317 O  O   . HOH G 7 .   ? -1.004  5.872   -2.686  1.00 27.45  ? 474 HOH A O   1 
HETATM 2318 O  O   . HOH G 7 .   ? -0.104  9.787   1.995   1.00 15.16  ? 475 HOH A O   1 
HETATM 2319 O  O   . HOH G 7 .   ? 3.976   -20.987 4.163   1.00 29.87  ? 476 HOH A O   1 
HETATM 2320 O  O   . HOH G 7 .   ? 18.554  -7.036  29.125  1.00 11.44  ? 477 HOH A O   1 
HETATM 2321 O  O   . HOH G 7 .   ? 4.999   -10.489 24.414  1.00 15.34  ? 478 HOH A O   1 
HETATM 2322 O  O   . HOH G 7 .   ? 32.227  3.061   26.242  1.00 22.60  ? 479 HOH A O   1 
HETATM 2323 O  O   . HOH G 7 .   ? 5.637   2.778   -4.864  1.00 34.80  ? 480 HOH A O   1 
HETATM 2324 O  O   . HOH G 7 .   ? 34.568  1.933   24.731  1.00 19.34  ? 481 HOH A O   1 
HETATM 2325 O  O   . HOH G 7 .   ? 14.313  22.903  19.432  1.00 16.99  ? 482 HOH A O   1 
HETATM 2326 O  O   . HOH G 7 .   ? 23.037  -13.634 9.393   1.00 21.11  ? 483 HOH A O   1 
HETATM 2327 O  O   . HOH G 7 .   ? 16.522  -14.068 1.316   1.00 26.70  ? 484 HOH A O   1 
HETATM 2328 O  O   . HOH G 7 .   ? 17.539  -9.358  20.874  1.00 9.17   ? 485 HOH A O   1 
HETATM 2329 O  O   . HOH G 7 .   ? 16.807  -6.925  31.255  1.00 20.05  ? 486 HOH A O   1 
HETATM 2330 O  O   . HOH G 7 .   ? 4.079   -6.578  20.408  1.00 8.35   ? 487 HOH A O   1 
HETATM 2331 O  O   . HOH G 7 .   ? 23.539  -11.448 5.100   1.00 17.49  ? 488 HOH A O   1 
HETATM 2332 O  O   . HOH G 7 .   ? 3.136   -18.602 8.110   1.00 14.31  ? 489 HOH A O   1 
HETATM 2333 O  O   . HOH G 7 .   ? 29.735  -2.032  21.236  1.00 14.35  ? 490 HOH A O   1 
HETATM 2334 O  O   . HOH G 7 .   ? 16.518  -11.647 17.984  1.00 8.75   ? 491 HOH A O   1 
HETATM 2335 O  O   . HOH G 7 .   ? 28.595  -5.754  -0.664  1.00 21.53  ? 492 HOH A O   1 
HETATM 2336 O  O   . HOH G 7 .   ? 1.320   -2.436  41.370  1.00 32.39  ? 493 HOH A O   1 
HETATM 2337 O  O   . HOH G 7 .   ? 10.631  -16.401 17.037  1.00 15.70  ? 494 HOH A O   1 
HETATM 2338 O  O   . HOH G 7 .   ? -0.499  -5.372  23.666  1.00 11.99  ? 495 HOH A O   1 
HETATM 2339 O  O   . HOH G 7 .   ? 4.387   -13.996 -4.090  1.00 33.11  ? 496 HOH A O   1 
HETATM 2340 O  O   . HOH G 7 .   ? 1.732   -18.906 5.322   1.00 25.26  ? 497 HOH A O   1 
HETATM 2341 O  O   . HOH G 7 .   ? 23.665  6.564   12.421  1.00 32.99  ? 498 HOH A O   1 
HETATM 2342 O  O   . HOH G 7 .   ? 2.923   12.732  11.562  1.00 18.22  ? 499 HOH A O   1 
HETATM 2343 O  O   . HOH G 7 .   ? 9.123   11.275  3.433   1.00 22.60  ? 500 HOH A O   1 
HETATM 2344 O  O   . HOH G 7 .   ? 35.010  3.915   23.076  1.00 20.19  ? 501 HOH A O   1 
HETATM 2345 O  O   . HOH G 7 .   ? 11.199  8.243   -3.819  1.00 35.12  ? 502 HOH A O   1 
HETATM 2346 O  O   . HOH G 7 .   ? 13.967  -14.851 1.686   1.00 18.29  ? 503 HOH A O   1 
HETATM 2347 O  O   . HOH G 7 .   ? -5.125  5.407   15.803  1.00 22.46  ? 504 HOH A O   1 
HETATM 2348 O  O   . HOH G 7 .   ? -2.120  -1.118  7.054   1.00 19.86  ? 505 HOH A O   1 
HETATM 2349 O  O   . HOH G 7 .   ? 21.286  5.262   5.794   1.00 26.53  ? 506 HOH A O   1 
HETATM 2350 O  O   . HOH G 7 .   ? 24.501  10.504  21.230  1.00 26.25  ? 507 HOH A O   1 
HETATM 2351 O  O   . HOH G 7 .   ? 8.034   -7.005  -3.154  1.00 20.83  ? 508 HOH A O   1 
HETATM 2352 O  O   . HOH G 7 .   ? 5.678   21.329  13.343  1.00 16.35  ? 509 HOH A O   1 
HETATM 2353 O  O   . HOH G 7 .   ? 17.318  -10.950 -2.889  1.00 24.97  ? 510 HOH A O   1 
HETATM 2354 O  O   . HOH G 7 .   ? 7.538   1.114   -5.958  1.00 25.76  ? 511 HOH A O   1 
HETATM 2355 O  O   . HOH G 7 .   ? 1.680   11.993  9.129   1.00 14.26  ? 512 HOH A O   1 
HETATM 2356 O  O   . HOH G 7 .   ? -1.022  7.714   4.964   1.00 16.26  ? 513 HOH A O   1 
HETATM 2357 O  O   . HOH G 7 .   ? 13.965  -6.366  -7.197  1.00 30.99  ? 514 HOH A O   1 
HETATM 2358 O  O   . HOH G 7 .   ? 20.667  -18.685 15.002  1.00 30.20  ? 515 HOH A O   1 
HETATM 2359 O  O   . HOH G 7 .   ? 7.176   21.981  15.363  1.00 19.57  ? 516 HOH A O   1 
HETATM 2360 O  O   . HOH G 7 .   ? 9.866   -17.286 6.967   1.00 23.44  ? 517 HOH A O   1 
HETATM 2361 O  O   . HOH G 7 .   ? 17.253  -14.108 24.295  1.00 12.41  ? 518 HOH A O   1 
HETATM 2362 O  O   . HOH G 7 .   ? 25.082  -1.281  3.935   1.00 30.08  ? 519 HOH A O   1 
HETATM 2363 O  O   . HOH G 7 .   ? 14.953  3.690   11.531  1.00 51.94  ? 520 HOH A O   1 
HETATM 2364 O  O   . HOH G 7 .   ? -4.782  10.062  6.558   1.00 43.11  ? 521 HOH A O   1 
HETATM 2365 O  O   . HOH G 7 .   ? -4.603  -5.313  34.002  1.00 40.29  ? 522 HOH A O   1 
HETATM 2366 O  O   . HOH G 7 .   ? -1.675  -3.901  2.902   1.00 20.39  ? 523 HOH A O   1 
HETATM 2367 O  O   . HOH G 7 .   ? -3.860  -5.844  9.247   1.00 16.69  ? 524 HOH A O   1 
HETATM 2368 O  O   . HOH G 7 .   ? 5.147   17.732  23.929  1.00 20.05  ? 525 HOH A O   1 
HETATM 2369 O  O   . HOH G 7 .   ? 8.023   -15.042 26.762  1.00 17.59  ? 526 HOH A O   1 
HETATM 2370 O  O   . HOH G 7 .   ? 7.648   15.899  27.560  1.00 19.87  ? 527 HOH A O   1 
HETATM 2371 O  O   . HOH G 7 .   ? 24.670  1.959   -6.363  1.00 30.94  ? 528 HOH A O   1 
HETATM 2372 O  O   . HOH G 7 .   ? 14.316  -3.700  37.333  1.00 16.65  ? 529 HOH A O   1 
HETATM 2373 O  O   . HOH G 7 .   ? 17.672  -11.485 25.099  1.00 10.87  ? 530 HOH A O   1 
HETATM 2374 O  O   . HOH G 7 .   ? 22.347  -10.094 24.958  1.00 25.98  ? 531 HOH A O   1 
HETATM 2375 O  O   . HOH G 7 .   ? 26.015  -3.056  21.075  1.00 13.86  ? 532 HOH A O   1 
HETATM 2376 O  O   . HOH G 7 .   ? -5.137  -5.891  30.504  1.00 38.49  ? 533 HOH A O   1 
HETATM 2377 O  O   . HOH G 7 .   ? -4.545  -1.873  31.957  1.00 36.66  ? 534 HOH A O   1 
HETATM 2378 O  O   . HOH G 7 .   ? 1.562   19.372  6.175   1.00 28.54  ? 535 HOH A O   1 
HETATM 2379 O  O   . HOH G 7 .   ? 23.670  -9.421  9.520   1.00 19.85  ? 536 HOH A O   1 
HETATM 2380 O  O   . HOH G 7 .   ? 13.740  -6.916  32.660  1.00 16.48  ? 537 HOH A O   1 
HETATM 2381 O  O   . HOH G 7 .   ? 9.159   4.624   30.754  1.00 20.41  ? 538 HOH A O   1 
HETATM 2382 O  O   . HOH G 7 .   ? 22.871  -13.748 -4.779  1.00 29.33  ? 539 HOH A O   1 
HETATM 2383 O  O   . HOH G 7 .   ? 19.541  6.381   -4.809  1.00 24.98  ? 540 HOH A O   1 
HETATM 2384 O  O   . HOH G 7 .   ? -6.578  6.135   24.365  1.00 29.99  ? 541 HOH A O   1 
HETATM 2385 O  O   . HOH G 7 .   ? 20.785  -12.465 22.032  1.00 22.62  ? 542 HOH A O   1 
HETATM 2386 O  O   . HOH G 7 .   ? 7.259   11.327  31.583  1.00 28.69  ? 543 HOH A O   1 
HETATM 2387 O  O   . HOH G 7 .   ? -1.183  -16.440 13.640  1.00 21.41  ? 544 HOH A O   1 
HETATM 2388 O  O   . HOH G 7 .   ? 22.854  9.878   25.138  1.00 17.60  ? 545 HOH A O   1 
HETATM 2389 O  O   . HOH G 7 .   ? 24.721  -7.302  25.825  1.00 34.76  ? 546 HOH A O   1 
HETATM 2390 O  O   . HOH G 7 .   ? -3.686  6.479   8.710   1.00 34.46  ? 547 HOH A O   1 
HETATM 2391 O  O   . HOH G 7 .   ? 18.929  -2.623  -7.172  1.00 32.39  ? 548 HOH A O   1 
HETATM 2392 O  O   . HOH G 7 .   ? -5.776  -2.274  25.254  1.00 21.46  ? 549 HOH A O   1 
HETATM 2393 O  O   . HOH G 7 .   ? 13.258  -17.343 30.511  1.00 33.83  ? 550 HOH A O   1 
HETATM 2394 O  O   . HOH G 7 .   ? 7.773   -16.639 14.712  1.00 18.27  ? 551 HOH A O   1 
HETATM 2395 O  O   . HOH G 7 .   ? 7.204   16.706  6.496   1.00 35.71  ? 552 HOH A O   1 
HETATM 2396 O  O   . HOH G 7 .   ? 23.121  -5.033  -7.966  1.00 32.77  ? 553 HOH A O   1 
HETATM 2397 O  O   . HOH G 7 .   ? -2.847  0.963   26.729  1.00 24.78  ? 554 HOH A O   1 
HETATM 2398 O  O   . HOH G 7 .   ? 10.315  3.052   34.238  1.00 35.15  ? 555 HOH A O   1 
HETATM 2399 O  O   . HOH G 7 .   ? -3.062  1.212   4.205   1.00 22.11  ? 556 HOH A O   1 
HETATM 2400 O  O   . HOH G 7 .   ? 20.359  15.851  15.181  1.00 43.12  ? 557 HOH A O   1 
HETATM 2401 O  O   . HOH G 7 .   ? 6.028   21.921  17.900  1.00 20.42  ? 558 HOH A O   1 
HETATM 2402 O  O   . HOH G 7 .   ? 25.613  -5.022  7.983   1.00 32.32  ? 559 HOH A O   1 
HETATM 2403 O  O   . HOH G 7 .   ? 35.343  7.553   19.517  1.00 29.93  ? 560 HOH A O   1 
HETATM 2404 O  O   . HOH G 7 .   ? 2.359   21.953  14.776  1.00 23.58  ? 561 HOH A O   1 
HETATM 2405 O  O   . HOH G 7 .   ? 10.765  16.935  12.314  1.00 22.78  ? 562 HOH A O   1 
HETATM 2406 O  O   . HOH G 7 .   ? 15.138  1.796   39.853  1.00 47.09  ? 563 HOH A O   1 
HETATM 2407 O  O   . HOH G 7 .   ? 20.398  -6.893  32.541  1.00 23.55  ? 564 HOH A O   1 
HETATM 2408 O  O   . HOH G 7 .   ? -2.658  -16.237 6.471   1.00 41.65  ? 565 HOH A O   1 
HETATM 2409 O  O   . HOH G 7 .   ? -3.023  1.753   1.317   1.00 32.28  ? 566 HOH A O   1 
HETATM 2410 O  O   . HOH G 7 .   ? 22.404  0.101   29.589  1.00 12.93  ? 567 HOH A O   1 
HETATM 2411 O  O   . HOH G 7 .   ? 9.522   19.775  12.564  1.00 24.87  ? 568 HOH A O   1 
HETATM 2412 O  O   . HOH G 7 .   ? 23.877  3.028   -2.198  1.00 32.17  ? 569 HOH A O   1 
HETATM 2413 O  O   . HOH G 7 .   ? -9.660  -5.404  22.554  1.00 32.22  ? 570 HOH A O   1 
HETATM 2414 O  O   . HOH G 7 .   ? 8.410   9.557   29.055  1.00 19.04  ? 571 HOH A O   1 
HETATM 2415 O  O   . HOH G 7 .   ? 11.929  -4.122  35.970  1.00 17.39  ? 572 HOH A O   1 
HETATM 2416 O  O   . HOH G 7 .   ? 21.504  -17.651 10.903  1.00 30.38  ? 573 HOH A O   1 
HETATM 2417 O  O   . HOH G 7 .   ? 10.536  23.687  20.113  1.00 18.78  ? 574 HOH A O   1 
HETATM 2418 O  O   . HOH G 7 .   ? 11.555  -6.191  34.056  1.00 20.19  ? 575 HOH A O   1 
HETATM 2419 O  O   . HOH G 7 .   ? 4.790   -8.172  33.024  1.00 17.69  ? 576 HOH A O   1 
HETATM 2420 O  O   . HOH G 7 .   ? -1.892  -9.864  14.138  1.00 19.20  ? 577 HOH A O   1 
HETATM 2421 O  O   . HOH G 7 .   ? 5.433   10.996  -1.939  1.00 32.58  ? 578 HOH A O   1 
HETATM 2422 O  O   . HOH G 7 .   ? 5.899   -18.523 22.834  1.00 38.12  ? 579 HOH A O   1 
HETATM 2423 O  O   . HOH G 7 .   ? 18.988  -10.517 22.786  1.00 10.21  ? 580 HOH A O   1 
HETATM 2424 O  O   . HOH G 7 .   ? 15.555  5.567   -5.426  1.00 36.33  ? 581 HOH A O   1 
HETATM 2425 O  O   . HOH G 7 .   ? 12.664  -18.134 26.720  1.00 27.22  ? 582 HOH A O   1 
HETATM 2426 O  O   . HOH G 7 .   ? -4.904  -3.891  12.968  1.00 42.78  ? 583 HOH A O   1 
HETATM 2427 O  O   . HOH G 7 .   ? 8.135   5.564   -6.660  1.00 23.50  ? 584 HOH A O   1 
HETATM 2428 O  O   . HOH G 7 .   ? 19.977  -15.510 17.962  1.00 32.82  ? 585 HOH A O   1 
HETATM 2429 O  O   . HOH G 7 .   ? 19.757  23.499  19.241  1.00 51.18  ? 586 HOH A O   1 
HETATM 2430 O  O   . HOH G 7 .   ? 12.416  -13.554 33.370  1.00 37.24  ? 587 HOH A O   1 
HETATM 2431 O  O   . HOH G 7 .   ? 26.396  -5.783  25.709  1.00 40.42  ? 588 HOH A O   1 
HETATM 2432 O  O   . HOH G 7 .   ? 4.192   -12.164 26.349  1.00 21.44  ? 589 HOH A O   1 
HETATM 2433 O  O   . HOH G 7 .   ? 26.135  -5.626  22.371  1.00 25.76  ? 590 HOH A O   1 
HETATM 2434 O  O   . HOH G 7 .   ? 29.538  5.477   28.092  1.00 44.52  ? 591 HOH A O   1 
HETATM 2435 O  O   . HOH G 7 .   ? 34.229  -4.067  24.569  1.00 24.46  ? 592 HOH A O   1 
HETATM 2436 O  O   . HOH G 7 .   ? 16.044  -11.582 34.076  1.00 37.23  ? 593 HOH A O   1 
HETATM 2437 O  O   . HOH G 7 .   ? 8.372   -16.764 31.949  1.00 29.70  ? 594 HOH A O   1 
HETATM 2438 O  O   . HOH G 7 .   ? 10.538  -17.683 27.160  1.00 40.15  ? 595 HOH A O   1 
HETATM 2439 O  O   . HOH G 7 .   ? -6.038  -9.142  22.698  1.00 37.77  ? 596 HOH A O   1 
HETATM 2440 O  O   . HOH G 7 .   ? 28.746  7.988   22.231  1.00 16.22  ? 597 HOH A O   1 
HETATM 2441 O  O   . HOH G 7 .   ? 14.041  3.171   35.323  1.00 30.70  ? 598 HOH A O   1 
HETATM 2442 O  O   . HOH G 7 .   ? 6.915   8.200   33.141  1.00 33.68  ? 599 HOH A O   1 
HETATM 2443 O  O   . HOH G 7 .   ? 9.503   12.660  6.399   1.00 56.82  ? 600 HOH A O   1 
HETATM 2444 O  O   . HOH G 7 .   ? 22.467  -5.050  34.469  1.00 48.80  ? 601 HOH A O   1 
HETATM 2445 O  O   . HOH G 7 .   ? 15.190  10.002  5.617   1.00 23.84  ? 602 HOH A O   1 
HETATM 2446 O  O   . HOH G 7 .   ? 13.904  -16.752 4.345   1.00 27.76  ? 603 HOH A O   1 
HETATM 2447 O  O   . HOH G 7 .   ? -5.644  4.408   1.828   1.00 45.49  ? 604 HOH A O   1 
HETATM 2448 O  O   . HOH G 7 .   ? -2.502  1.496   32.159  1.00 28.37  ? 605 HOH A O   1 
HETATM 2449 O  O   . HOH G 7 .   ? 12.581  -13.934 36.870  1.00 40.46  ? 606 HOH A O   1 
HETATM 2450 O  O   . HOH G 7 .   ? 31.227  -0.661  14.161  1.00 30.65  ? 607 HOH A O   1 
HETATM 2451 O  O   . HOH G 7 .   ? 2.735   -7.157  34.742  1.00 28.06  ? 608 HOH A O   1 
HETATM 2452 O  O   . HOH G 7 .   ? 4.138   21.262  22.061  1.00 42.19  ? 609 HOH A O   1 
HETATM 2453 O  O   . HOH G 7 .   ? 18.047  8.123   -1.168  1.00 35.49  ? 610 HOH A O   1 
HETATM 2454 O  O   . HOH G 7 .   ? 36.201  -8.427  14.685  1.00 30.34  ? 611 HOH A O   1 
HETATM 2455 O  O   . HOH G 7 .   ? 6.028   -9.184  -4.073  1.00 41.80  ? 612 HOH A O   1 
HETATM 2456 O  O   . HOH G 7 .   ? 28.689  -6.973  -7.431  1.00 43.05  ? 613 HOH A O   1 
HETATM 2457 O  O   . HOH G 7 .   ? 23.700  7.531   33.098  1.00 34.35  ? 614 HOH A O   1 
HETATM 2458 O  O   . HOH G 7 .   ? 22.675  -16.122 13.534  1.00 49.06  ? 615 HOH A O   1 
HETATM 2459 O  O   . HOH G 7 .   ? 14.894  -18.221 23.859  1.00 29.33  ? 616 HOH A O   1 
HETATM 2460 O  O   . HOH G 7 .   ? 2.421   5.340   -3.523  1.00 35.29  ? 617 HOH A O   1 
HETATM 2461 O  O   . HOH G 7 .   ? 17.159  8.102   6.475   1.00 25.05  ? 618 HOH A O   1 
HETATM 2462 O  O   . HOH G 7 .   ? 29.742  -2.869  23.844  1.00 27.91  ? 619 HOH A O   1 
HETATM 2463 O  O   . HOH G 7 .   ? 21.256  21.480  17.324  1.00 39.85  ? 620 HOH A O   1 
HETATM 2464 O  O   . HOH G 7 .   ? 20.345  12.125  25.466  1.00 39.56  ? 621 HOH A O   1 
HETATM 2465 O  O   . HOH G 7 .   ? 23.773  -1.598  37.672  1.00 42.49  ? 622 HOH A O   1 
HETATM 2466 O  O   . HOH G 7 .   ? 25.591  -7.769  8.214   1.00 35.98  ? 623 HOH A O   1 
HETATM 2467 O  O   . HOH G 7 .   ? 28.302  5.514   32.321  1.00 36.10  ? 624 HOH A O   1 
HETATM 2468 O  O   . HOH G 7 .   ? 35.404  -2.348  10.498  1.00 39.85  ? 625 HOH A O   1 
HETATM 2469 O  O   . HOH G 7 .   ? 1.137   -9.925  34.440  1.00 38.51  ? 626 HOH A O   1 
HETATM 2470 O  O   . HOH G 7 .   ? 8.181   -15.410 16.976  1.00 17.29  ? 627 HOH A O   1 
HETATM 2471 O  O   . HOH G 7 .   ? 3.375   21.917  17.610  1.00 27.10  ? 628 HOH A O   1 
HETATM 2472 O  O   . HOH G 7 .   ? -2.561  -1.348  4.234   1.00 36.19  ? 629 HOH A O   1 
HETATM 2473 O  O   . HOH G 7 .   ? -2.595  10.177  3.576   1.00 29.14  ? 630 HOH A O   1 
HETATM 2474 O  O   . HOH G 7 .   ? 3.300   -7.852  37.448  1.00 44.20  ? 631 HOH A O   1 
HETATM 2475 O  O   . HOH G 7 .   ? -4.158  13.110  19.909  1.00 30.39  ? 632 HOH A O   1 
HETATM 2476 O  O   . HOH G 7 .   ? 21.501  2.636   -6.506  1.00 26.57  ? 633 HOH A O   1 
HETATM 2477 O  O   . HOH G 7 .   ? 8.665   7.987   31.132  1.00 30.45  ? 634 HOH A O   1 
HETATM 2478 O  O   . HOH G 7 .   ? -0.096  23.521  6.795   1.00 25.42  ? 635 HOH A O   1 
HETATM 2479 O  O   . HOH G 7 .   ? 13.045  23.744  21.689  1.00 16.27  ? 636 HOH A O   1 
HETATM 2480 O  O   . HOH G 7 .   ? 19.443  1.534   11.144  1.00 27.97  ? 637 HOH A O   1 
HETATM 2481 O  O   . HOH G 7 .   ? 10.797  6.713   30.544  1.00 29.26  ? 638 HOH A O   1 
HETATM 2482 O  O   . HOH G 7 .   ? 26.672  -11.569 2.237   1.00 29.74  ? 639 HOH A O   1 
HETATM 2483 O  O   . HOH G 7 .   ? 19.625  -11.355 27.039  1.00 25.19  ? 640 HOH A O   1 
HETATM 2484 O  O   . HOH G 7 .   ? 26.476  -9.266  19.006  1.00 40.86  ? 641 HOH A O   1 
HETATM 2485 O  O   . HOH G 7 .   ? 19.163  -15.754 25.392  1.00 31.39  ? 642 HOH A O   1 
HETATM 2486 O  O   . HOH G 7 .   ? 18.933  -10.354 31.601  1.00 35.71  ? 643 HOH A O   1 
HETATM 2487 O  O   . HOH G 7 .   ? 5.560   -14.598 25.781  1.00 37.94  ? 644 HOH A O   1 
HETATM 2488 O  O   . HOH G 7 .   ? 21.459  5.946   34.819  1.00 31.15  ? 645 HOH A O   1 
HETATM 2489 O  O   . HOH G 7 .   ? 24.011  -11.604 7.945   1.00 28.16  ? 646 HOH A O   1 
HETATM 2490 O  O   . HOH G 7 .   ? 20.739  5.061   8.432   1.00 30.61  ? 647 HOH A O   1 
HETATM 2491 O  O   . HOH G 7 .   ? -10.938 7.330   14.067  1.00 55.93  ? 648 HOH A O   1 
HETATM 2492 O  O   . HOH G 7 .   ? 1.051   -0.245  43.020  1.00 50.15  ? 649 HOH A O   1 
HETATM 2493 O  O   . HOH G 7 .   ? 4.076   -16.179 20.298  1.00 29.34  ? 650 HOH A O   1 
HETATM 2494 O  O   . HOH G 7 .   ? 17.390  -2.521  40.218  1.00 25.57  ? 651 HOH A O   1 
HETATM 2495 O  O   . HOH G 7 .   ? 36.419  0.326   26.227  1.00 30.23  ? 652 HOH A O   1 
HETATM 2496 O  O   . HOH G 7 .   ? 4.503   -12.387 28.944  1.00 38.56  ? 653 HOH A O   1 
HETATM 2497 O  O   . HOH G 7 .   ? 12.468  -16.103 32.554  1.00 42.71  ? 654 HOH A O   1 
HETATM 2498 O  O   . HOH G 7 .   ? 27.190  -5.490  2.263   1.00 43.97  ? 655 HOH A O   1 
HETATM 2499 O  O   . HOH G 7 .   ? 23.261  9.710   12.754  1.00 49.22  ? 656 HOH A O   1 
HETATM 2500 O  O   . HOH G 7 .   ? 6.431   24.422  18.750  1.00 19.84  ? 657 HOH A O   1 
HETATM 2501 O  O   . HOH G 7 .   ? 22.977  -12.425 20.245  1.00 33.28  ? 658 HOH A O   1 
HETATM 2502 O  O   . HOH G 7 .   ? 9.236   3.007   -7.493  1.00 37.70  ? 659 HOH A O   1 
HETATM 2503 O  O   . HOH G 7 .   ? 3.222   -10.408 31.605  1.00 43.52  ? 660 HOH A O   1 
HETATM 2504 O  O   . HOH G 7 .   ? 16.269  -6.250  -8.360  1.00 39.05  ? 661 HOH A O   1 
HETATM 2505 O  O   . HOH G 7 .   ? 15.903  -8.158  34.213  1.00 41.74  ? 662 HOH A O   1 
HETATM 2506 O  O   . HOH G 7 .   ? 12.504  -19.035 3.936   1.00 37.31  ? 663 HOH A O   1 
HETATM 2507 O  O   . HOH G 7 .   ? 10.527  -18.498 25.041  1.00 24.73  ? 664 HOH A O   1 
HETATM 2508 O  O   . HOH G 7 .   ? 9.468   12.750  0.900   1.00 29.84  ? 665 HOH A O   1 
HETATM 2509 O  O   . HOH G 7 .   ? 15.071  -19.036 26.377  1.00 39.73  ? 666 HOH A O   1 
HETATM 2510 O  O   . HOH G 7 .   ? 8.814   15.307  5.147   1.00 31.93  ? 667 HOH A O   1 
HETATM 2511 O  O   . HOH G 7 .   ? 17.704  -15.539 3.687   1.00 31.47  ? 668 HOH A O   1 
HETATM 2512 O  O   . HOH G 7 .   ? 19.890  -9.391  28.955  1.00 17.35  ? 669 HOH A O   1 
HETATM 2513 O  O   . HOH G 7 .   ? 11.905  4.936   34.613  1.00 28.06  ? 670 HOH A O   1 
HETATM 2514 O  O   . HOH G 7 .   ? -7.317  7.430   26.210  1.00 35.68  ? 671 HOH A O   1 
HETATM 2515 O  O   . HOH G 7 .   ? -3.310  15.592  20.673  1.00 40.08  ? 672 HOH A O   1 
HETATM 2516 O  O   . HOH G 7 .   ? 16.846  -13.327 -2.359  1.00 41.39  ? 673 HOH A O   1 
HETATM 2517 O  O   . HOH G 7 .   ? 20.595  -5.244  -7.306  1.00 42.89  ? 674 HOH A O   1 
HETATM 2518 O  O   . HOH G 7 .   ? 27.438  7.116   30.234  1.00 34.21  ? 675 HOH A O   1 
HETATM 2519 O  O   . HOH G 7 .   ? 4.914   19.578  25.927  1.00 39.63  ? 676 HOH A O   1 
HETATM 2520 O  O   . HOH G 7 .   ? 35.797  -5.037  7.995   1.00 34.90  ? 677 HOH A O   1 
HETATM 2521 O  O   . HOH G 7 .   ? 19.540  5.071   -7.127  1.00 29.00  ? 678 HOH A O   1 
HETATM 2522 O  O   . HOH G 7 .   ? 25.299  -10.001 23.213  1.00 43.87  ? 679 HOH A O   1 
HETATM 2523 O  O   . HOH G 7 .   ? 25.264  10.776  23.650  1.00 41.04  ? 680 HOH A O   1 
HETATM 2524 O  O   . HOH G 7 .   ? 20.133  -15.387 5.097   1.00 30.32  ? 681 HOH A O   1 
HETATM 2525 O  O   . HOH G 7 .   ? 6.711   5.255   33.370  1.00 38.69  ? 682 HOH A O   1 
HETATM 2526 O  O   . HOH G 7 .   ? 23.444  -17.727 16.122  1.00 42.80  ? 683 HOH A O   1 
HETATM 2527 O  O   . HOH G 7 .   ? 25.018  10.791  14.252  1.00 44.03  ? 684 HOH A O   1 
HETATM 2528 O  O   . HOH G 7 .   ? 8.098   -17.992 26.299  1.00 33.72  ? 685 HOH A O   1 
HETATM 2529 O  O   . HOH G 7 .   ? 17.737  -15.797 -0.123  1.00 42.38  ? 686 HOH A O   1 
HETATM 2530 O  O   . HOH G 7 .   ? 3.776   12.928  -1.951  1.00 28.35  ? 687 HOH A O   1 
HETATM 2531 O  O   . HOH G 7 .   ? 20.009  -15.441 -2.043  1.00 29.39  ? 688 HOH A O   1 
HETATM 2532 O  O   . HOH G 7 .   ? 25.224  -11.503 21.371  1.00 35.59  ? 689 HOH A O   1 
HETATM 2533 O  O   . HOH G 7 .   ? 2.805   15.303  -0.270  1.00 41.44  ? 690 HOH A O   1 
HETATM 2534 O  O   . HOH G 7 .   ? 9.005   15.349  2.355   1.00 38.63  ? 691 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   ? 0.6749 0.9804 0.9190 0.0522  0.4919  0.0861  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.2946 0.4719 0.6976 -0.0741 0.1425  0.1342  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.2507 0.3944 0.5193 0.0279  0.0710  -0.0265 4   HIS A C   
4    O  O   . HIS A 4   ? 0.2942 0.3856 0.3790 0.0036  0.1483  0.0504  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.4713 0.5856 0.3430 -0.0814 0.1405  0.2509  4   HIS A CB  
6    C  CG  . HIS A 4   ? 1.3750 0.6026 0.9356 -0.1273 0.2896  0.1506  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.8043 1.3364 1.0630 -0.0417 -0.1402 0.3508  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 1.2587 1.1654 1.0847 -0.1805 0.1159  0.6009  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 1.4394 1.4016 1.7170 -0.2893 0.0758  0.4773  4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 1.8903 0.7514 1.6831 -0.3898 0.3940  0.7105  4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.2144 0.3643 0.4053 0.0153  0.0475  0.0950  5   TRP A N   
12   C  CA  . TRP A 5   ? 0.1950 0.2685 0.2867 0.0043  0.0353  0.0019  5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1645 0.2940 0.2208 0.0034  0.0251  0.0211  5   TRP A C   
14   O  O   . TRP A 5   ? 0.1684 0.3208 0.2374 0.0107  0.0489  0.0208  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1351 0.2593 0.2727 -0.0060 0.0442  -0.0071 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1839 0.2566 0.1882 -0.0171 0.0537  0.0274  5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.2593 0.2960 0.3330 0.0118  0.0207  0.0941  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.2029 0.2992 0.1753 -0.0156 0.0268  0.0335  5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.2459 0.3624 0.2662 0.0208  0.0709  0.1395  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1835 0.3078 0.1857 0.0089  0.0445  0.0366  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1551 0.2892 0.1857 -0.0519 0.0355  -0.0116 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.2252 0.4473 0.1993 -0.0725 0.0207  -0.0394 5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1580 0.3552 0.2088 -0.0226 0.0300  -0.0575 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1605 0.3884 0.1559 -0.0288 0.0119  -0.0517 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1519 0.2676 0.2508 0.0359  0.0491  -0.0016 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.2378 0.2845 0.2116 -0.0245 0.0697  -0.0066 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.2173 0.2638 0.2374 0.0150  0.0825  0.0063  6   GLY A C   
28   O  O   . GLY A 6   ? 0.1483 0.2827 0.2579 0.0023  0.0551  0.0087  6   GLY A O   
29   N  N   . TYR A 7   ? 0.1882 0.2975 0.2409 -0.0241 0.0756  -0.0310 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.1620 0.2417 0.3331 0.0040  0.1188  -0.0271 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.2051 0.2979 0.5279 0.0677  0.0838  -0.0610 7   TYR A C   
32   O  O   . TYR A 7   ? 0.2150 0.3100 0.5307 -0.0196 0.0493  -0.0996 7   TYR A O   
33   C  CB  . TYR A 7   ? 0.1631 0.2247 0.3542 0.0258  0.0387  -0.0489 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1641 0.1839 0.2352 0.0095  0.0242  -0.0364 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.1191 0.2597 0.2433 -0.0273 0.0504  -0.0949 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.1731 0.1897 0.2511 0.0200  0.0608  -0.0166 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.1760 0.1943 0.1742 -0.0736 0.0236  -0.0262 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.1106 0.1652 0.1641 -0.0036 0.0222  -0.0039 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.1137 0.1965 0.2326 -0.0572 0.0412  -0.0465 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.1771 0.1958 0.2319 -0.0469 0.0326  -0.0397 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.3082 0.3190 0.4354 0.0272  0.1297  -0.0240 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.3445 0.3140 0.4026 0.0647  0.1467  -0.0521 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.4524 0.3280 0.2878 0.1156  0.2134  0.0192  8   GLY A C   
44   O  O   . GLY A 8   ? 0.3385 0.3312 0.3628 0.0189  0.0566  0.0216  8   GLY A O   
45   N  N   . LYS A 9   ? 0.5098 0.3785 0.5600 0.1726  -0.0491 -0.0741 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.4451 0.3821 0.5973 0.1031  -0.0826 -0.0823 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.4103 0.5302 0.4087 0.0388  -0.0617 0.0502  9   LYS A C   
48   O  O   . LYS A 9   ? 0.2313 0.3337 0.3639 -0.0227 0.1143  0.0304  9   LYS A O   
49   C  CB  . LYS A 9   ? 0.3689 0.4491 0.4568 0.1504  -0.0194 -0.0655 9   LYS A CB  
50   N  N   . HIS A 10  ? 0.5856 0.4065 0.5479 0.0545  0.0992  0.1869  10  HIS A N   
51   C  CA  . HIS A 10  ? 0.5030 0.4869 0.7048 0.1661  0.1103  -0.0943 10  HIS A CA  
52   C  C   . HIS A 10  ? 0.3647 0.4070 0.4853 0.1205  0.0073  0.1078  10  HIS A C   
53   O  O   . HIS A 10  ? 0.1950 0.4814 0.3079 0.1448  0.1065  0.1047  10  HIS A O   
54   C  CB  . HIS A 10  ? 0.4911 0.4106 0.6411 0.0447  0.1552  0.1980  10  HIS A CB  
55   C  CG  . HIS A 10  ? 0.3143 0.5508 0.4877 0.1074  0.0731  0.2690  10  HIS A CG  
56   N  ND1 . HIS A 10  ? 0.3021 0.3435 0.3877 0.0951  0.1289  0.0456  10  HIS A ND1 
57   C  CD2 . HIS A 10  ? 0.4491 0.5613 0.5296 -0.0082 0.1476  0.2661  10  HIS A CD2 
58   C  CE1 . HIS A 10  ? 0.4446 0.2266 0.4801 -0.0050 0.0886  0.0345  10  HIS A CE1 
59   N  NE2 . HIS A 10  ? 0.4990 0.3231 0.4264 0.0219  0.1766  -0.0258 10  HIS A NE2 
60   N  N   . ASN A 11  ? 0.2874 0.3521 0.2259 0.0946  0.1011  0.0289  11  ASN A N   
61   C  CA  . ASN A 11  ? 0.2550 0.2906 0.2348 0.0390  0.0553  0.0460  11  ASN A CA  
62   C  C   . ASN A 11  ? 0.2515 0.2623 0.2389 0.0445  0.0478  -0.0207 11  ASN A C   
63   O  O   . ASN A 11  ? 0.1997 0.2997 0.1942 0.0183  0.0827  0.0095  11  ASN A O   
64   C  CB  . ASN A 11  ? 0.2579 0.3110 0.2122 0.0102  0.1043  0.0414  11  ASN A CB  
65   C  CG  . ASN A 11  ? 0.2298 0.3599 0.2063 0.0204  0.1108  0.0434  11  ASN A CG  
66   O  OD1 . ASN A 11  ? 0.2551 0.3556 0.3082 0.0288  0.0740  0.0525  11  ASN A OD1 
67   N  ND2 . ASN A 11  ? 0.3347 0.3664 0.2251 0.0535  0.0438  0.0330  11  ASN A ND2 
68   N  N   . GLY A 12  ? 0.1573 0.3068 0.2415 0.0046  0.0917  0.0070  12  GLY A N   
69   C  CA  . GLY A 12  ? 0.1254 0.3327 0.1796 0.0018  0.0620  0.0145  12  GLY A CA  
70   C  C   . GLY A 12  ? 0.1541 0.2257 0.2097 -0.0125 0.0341  0.0193  12  GLY A C   
71   O  O   . GLY A 12  ? 0.1100 0.2644 0.2043 0.0043  0.0530  0.0279  12  GLY A O   
72   N  N   . PRO A 13  ? 0.1208 0.2323 0.1922 -0.0164 0.0353  -0.0245 13  PRO A N   
73   C  CA  . PRO A 13  ? 0.1082 0.2004 0.2100 -0.0287 0.0753  -0.0462 13  PRO A CA  
74   C  C   . PRO A 13  ? 0.1408 0.1868 0.1954 -0.0265 0.0590  -0.0106 13  PRO A C   
75   O  O   . PRO A 13  ? 0.1265 0.1810 0.2372 -0.0132 0.0781  -0.0367 13  PRO A O   
76   C  CB  . PRO A 13  ? 0.1422 0.2245 0.2169 -0.0699 0.0825  -0.0697 13  PRO A CB  
77   C  CG  . PRO A 13  ? 0.1487 0.2119 0.1861 -0.0498 0.0815  -0.0548 13  PRO A CG  
78   C  CD  . PRO A 13  ? 0.1318 0.2277 0.1839 -0.0300 0.0636  -0.0377 13  PRO A CD  
79   N  N   . GLU A 14  ? 0.1742 0.1784 0.2221 -0.0141 0.0673  0.0168  14  GLU A N   
80   C  CA  . GLU A 14  ? 0.2125 0.1857 0.2459 0.0019  0.0269  0.0325  14  GLU A CA  
81   C  C   . GLU A 14  ? 0.1458 0.2065 0.2399 0.0491  0.0292  0.0228  14  GLU A C   
82   O  O   . GLU A 14  ? 0.1605 0.2093 0.2310 0.0432  0.0217  0.0400  14  GLU A O   
83   C  CB  . GLU A 14  ? 0.3402 0.1874 0.3482 0.0165  0.0535  0.0521  14  GLU A CB  
84   C  CG  . GLU A 14  ? 0.3292 0.4390 0.3514 0.0431  -0.0313 -0.0334 14  GLU A CG  
85   C  CD  . GLU A 14  ? 0.1943 0.5283 0.4853 0.0946  -0.0312 -0.1167 14  GLU A CD  
86   O  OE1 . GLU A 14  ? 0.2539 0.2647 0.3697 0.0886  -0.0767 -0.1233 14  GLU A OE1 
87   O  OE2 . GLU A 14  ? 0.6157 0.2451 0.4170 0.0694  0.0120  -0.0697 14  GLU A OE2 
88   N  N   . HIS A 15  ? 0.1208 0.1861 0.2086 0.0065  0.0518  0.0021  15  HIS A N   
89   C  CA  . HIS A 15  ? 0.1261 0.1925 0.2047 -0.0032 0.0640  0.0118  15  HIS A CA  
90   C  C   . HIS A 15  ? 0.0715 0.1784 0.2062 0.0055  0.0308  0.0317  15  HIS A C   
91   O  O   . HIS A 15  ? 0.0730 0.1982 0.2137 0.0052  0.0326  0.0212  15  HIS A O   
92   C  CB  . HIS A 15  ? 0.1038 0.2190 0.2173 0.0554  0.0221  0.0156  15  HIS A CB  
93   C  CG  . HIS A 15  ? 0.1500 0.2402 0.2324 0.0785  0.0732  -0.0008 15  HIS A CG  
94   N  ND1 . HIS A 15  ? 0.1552 0.2838 0.2101 0.0800  0.0212  -0.0020 15  HIS A ND1 
95   C  CD2 . HIS A 15  ? 0.1511 0.2440 0.2605 0.0663  0.0499  -0.0258 15  HIS A CD2 
96   C  CE1 . HIS A 15  ? 0.3154 0.2540 0.2555 0.0812  0.0032  0.0022  15  HIS A CE1 
97   N  NE2 . HIS A 15  ? 0.2219 0.2820 0.2151 0.1346  0.0550  -0.0568 15  HIS A NE2 
98   N  N   . TRP A 16  ? 0.0759 0.1742 0.2001 0.0130  0.0300  0.0201  16  TRP A N   
99   C  CA  . TRP A 16  ? 0.0577 0.1735 0.1922 0.0103  0.0106  -0.0010 16  TRP A CA  
100  C  C   . TRP A 16  ? 0.0338 0.1698 0.2008 0.0044  0.0181  0.0118  16  TRP A C   
101  O  O   . TRP A 16  ? 0.0602 0.1659 0.2065 0.0004  -0.0044 0.0195  16  TRP A O   
102  C  CB  . TRP A 16  ? 0.0582 0.2313 0.1493 -0.0034 0.0144  0.0234  16  TRP A CB  
103  C  CG  . TRP A 16  ? 0.0753 0.2240 0.1490 -0.0162 0.0328  0.0323  16  TRP A CG  
104  C  CD1 . TRP A 16  ? 0.0593 0.2970 0.1461 -0.0048 0.0461  0.0265  16  TRP A CD1 
105  C  CD2 . TRP A 16  ? 0.0688 0.1763 0.1570 -0.0080 0.0262  -0.0039 16  TRP A CD2 
106  N  NE1 . TRP A 16  ? 0.0861 0.2705 0.1570 0.0215  0.0258  -0.0075 16  TRP A NE1 
107  C  CE2 . TRP A 16  ? 0.0891 0.2133 0.1527 0.0089  0.0263  0.0075  16  TRP A CE2 
108  C  CE3 . TRP A 16  ? 0.0521 0.1491 0.1738 -0.0210 0.0325  0.0059  16  TRP A CE3 
109  C  CZ2 . TRP A 16  ? 0.0821 0.2144 0.1932 -0.0025 0.0413  0.0100  16  TRP A CZ2 
110  C  CZ3 . TRP A 16  ? 0.0580 0.1329 0.1606 -0.0119 0.0236  -0.0117 16  TRP A CZ3 
111  C  CH2 . TRP A 16  ? 0.0723 0.1864 0.1720 -0.0208 0.0340  -0.0326 16  TRP A CH2 
112  N  N   . HIS A 17  ? 0.0575 0.1979 0.1774 0.0190  0.0151  0.0077  17  HIS A N   
113  C  CA  . HIS A 17  ? 0.0756 0.1810 0.1936 0.0026  -0.0020 0.0216  17  HIS A CA  
114  C  C   . HIS A 17  ? 0.0873 0.1881 0.2169 0.0054  -0.0011 0.0073  17  HIS A C   
115  O  O   . HIS A 17  ? 0.0713 0.2288 0.2108 -0.0108 0.0218  0.0157  17  HIS A O   
116  C  CB  . HIS A 17  ? 0.0681 0.2180 0.1638 0.0219  0.0259  0.0201  17  HIS A CB  
117  C  CG  . HIS A 17  ? 0.0701 0.1965 0.1889 0.0199  0.0228  0.0446  17  HIS A CG  
118  N  ND1 . HIS A 17  ? 0.0740 0.2590 0.2072 0.0000  0.0198  0.0409  17  HIS A ND1 
119  C  CD2 . HIS A 17  ? 0.1354 0.1897 0.1983 0.0446  0.0228  0.0406  17  HIS A CD2 
120  C  CE1 . HIS A 17  ? 0.1376 0.2981 0.2324 0.0513  0.0234  0.0398  17  HIS A CE1 
121  N  NE2 . HIS A 17  ? 0.1252 0.2694 0.2073 0.0383  0.0295  0.0765  17  HIS A NE2 
122  N  N   . LYS A 18  ? 0.0636 0.2195 0.2374 0.0144  0.0186  0.0320  18  LYS A N   
123  C  CA  . LYS A 18  ? 0.0498 0.2457 0.2177 -0.0357 0.0505  0.0328  18  LYS A CA  
124  C  C   . LYS A 18  ? 0.0949 0.2613 0.2446 -0.0255 0.0070  0.0571  18  LYS A C   
125  O  O   . LYS A 18  ? 0.2277 0.2328 0.3962 -0.0283 -0.0405 0.1153  18  LYS A O   
126  C  CB  . LYS A 18  ? 0.1060 0.2328 0.2208 0.0298  0.0219  0.0560  18  LYS A CB  
127  C  CG  . LYS A 18  ? 0.0920 0.2508 0.2161 0.0476  0.0154  0.0381  18  LYS A CG  
128  C  CD  . LYS A 18  ? 0.1005 0.2528 0.2409 0.0516  0.0241  0.0540  18  LYS A CD  
129  C  CE  . LYS A 18  ? 0.1074 0.2264 0.2169 0.0463  0.0339  0.0472  18  LYS A CE  
130  N  NZ  . LYS A 18  ? 0.1040 0.2694 0.2083 0.0748  0.0490  0.0778  18  LYS A NZ  
131  N  N   A ASP A 19  ? 0.1333 0.2421 0.2083 0.0002  0.0120  0.0411  19  ASP A N   
132  N  N   B ASP A 19  ? 0.1262 0.2241 0.2112 -0.0185 0.0129  0.0461  19  ASP A N   
133  C  CA  A ASP A 19  ? 0.0967 0.1990 0.2467 -0.0494 0.0249  0.0178  19  ASP A CA  
134  C  CA  B ASP A 19  ? 0.1227 0.2029 0.2558 -0.0161 0.0243  0.0094  19  ASP A CA  
135  C  C   A ASP A 19  ? 0.1243 0.2044 0.2451 0.0167  0.0315  0.0569  19  ASP A C   
136  C  C   B ASP A 19  ? 0.1094 0.1868 0.2518 0.0129  0.0251  0.0508  19  ASP A C   
137  O  O   A ASP A 19  ? 0.1612 0.1864 0.2910 -0.0111 0.0560  0.0368  19  ASP A O   
138  O  O   B ASP A 19  ? 0.1624 0.1720 0.3049 0.0013  0.0522  0.0403  19  ASP A O   
139  C  CB  A ASP A 19  ? 0.2489 0.3227 0.2293 -0.0209 -0.0137 0.0186  19  ASP A CB  
140  C  CB  B ASP A 19  ? 0.2417 0.3050 0.2705 -0.0003 -0.0440 -0.0053 19  ASP A CB  
141  C  CG  A ASP A 19  ? 0.2631 0.3650 0.3826 -0.0753 0.0192  -0.0779 19  ASP A CG  
142  C  CG  B ASP A 19  ? 0.2931 0.5794 0.3617 0.0029  0.0386  0.0395  19  ASP A CG  
143  O  OD1 A ASP A 19  ? 0.1965 0.2784 0.3265 0.0171  0.0255  0.0731  19  ASP A OD1 
144  O  OD1 B ASP A 19  ? 0.1421 0.6370 0.3861 -0.0331 0.2233  0.0325  19  ASP A OD1 
145  O  OD2 A ASP A 19  ? 0.3441 0.3693 0.2712 -0.0027 0.1026  -0.0069 19  ASP A OD2 
146  O  OD2 B ASP A 19  ? 0.1742 0.3855 0.3671 0.0210  -0.0267 0.0234  19  ASP A OD2 
147  N  N   . PHE A 20  ? 0.0880 0.1904 0.2026 -0.0115 0.0080  0.0303  20  PHE A N   
148  C  CA  . PHE A 20  ? 0.0496 0.2089 0.2196 0.0002  0.0175  0.0394  20  PHE A CA  
149  C  C   . PHE A 20  ? 0.0935 0.1889 0.2205 -0.0210 0.0037  0.0140  20  PHE A C   
150  O  O   . PHE A 20  ? 0.0838 0.1742 0.2054 -0.0158 0.0350  -0.0057 20  PHE A O   
151  C  CB  . PHE A 20  ? 0.0692 0.2548 0.2318 -0.0130 -0.0038 0.0521  20  PHE A CB  
152  C  CG  . PHE A 20  ? 0.1021 0.2633 0.2476 -0.0119 0.0046  0.0574  20  PHE A CG  
153  C  CD1 . PHE A 20  ? 0.1591 0.2734 0.3125 -0.0089 -0.0100 0.1122  20  PHE A CD1 
154  C  CD2 . PHE A 20  ? 0.1343 0.3186 0.2051 -0.0769 -0.0392 0.0320  20  PHE A CD2 
155  C  CE1 . PHE A 20  ? 0.1465 0.3093 0.2979 -0.0364 -0.0193 0.0834  20  PHE A CE1 
156  C  CE2 . PHE A 20  ? 0.1191 0.3829 0.2148 -0.0285 0.0163  0.0398  20  PHE A CE2 
157  C  CZ  . PHE A 20  ? 0.1616 0.3391 0.2794 -0.0590 0.0128  0.1015  20  PHE A CZ  
158  N  N   . PRO A 21  ? 0.0839 0.2040 0.2226 -0.0413 0.0094  0.0133  21  PRO A N   
159  C  CA  . PRO A 21  ? 0.1098 0.2587 0.1917 -0.0245 0.0207  -0.0013 21  PRO A CA  
160  C  C   . PRO A 21  ? 0.0768 0.1832 0.2105 -0.0152 0.0009  -0.0098 21  PRO A C   
161  O  O   . PRO A 21  ? 0.0847 0.2011 0.2008 -0.0152 -0.0128 0.0137  21  PRO A O   
162  C  CB  . PRO A 21  ? 0.1656 0.2978 0.2460 -0.0719 -0.0115 -0.0022 21  PRO A CB  
163  C  CG  . PRO A 21  ? 0.2929 0.2655 0.3828 -0.0599 -0.0769 0.0326  21  PRO A CG  
164  C  CD  . PRO A 21  ? 0.0712 0.2440 0.3175 -0.0684 0.0223  0.0728  21  PRO A CD  
165  N  N   . ILE A 22  ? 0.0486 0.1814 0.2079 -0.0104 0.0063  -0.0052 22  ILE A N   
166  C  CA  . ILE A 22  ? 0.0699 0.1430 0.2083 -0.0198 0.0228  -0.0042 22  ILE A CA  
167  C  C   . ILE A 22  ? 0.0644 0.1641 0.1620 -0.0161 0.0146  -0.0033 22  ILE A C   
168  O  O   . ILE A 22  ? 0.0692 0.1451 0.1685 -0.0159 0.0162  -0.0027 22  ILE A O   
169  C  CB  . ILE A 22  ? 0.0832 0.1667 0.1850 -0.0240 -0.0071 0.0035  22  ILE A CB  
170  C  CG1 . ILE A 22  ? 0.1062 0.2047 0.2204 -0.0160 0.0170  -0.0392 22  ILE A CG1 
171  C  CG2 . ILE A 22  ? 0.0859 0.1918 0.1871 0.0000  -0.0033 -0.0263 22  ILE A CG2 
172  C  CD1 . ILE A 22  ? 0.1594 0.2522 0.2875 -0.0023 -0.0378 -0.0951 22  ILE A CD1 
173  N  N   . ALA A 23  ? 0.0663 0.1687 0.1508 -0.0168 0.0095  -0.0098 23  ALA A N   
174  C  CA  . ALA A 23  ? 0.0926 0.1580 0.1451 -0.0212 0.0153  -0.0128 23  ALA A CA  
175  C  C   . ALA A 23  ? 0.0715 0.1674 0.1411 -0.0013 0.0182  -0.0136 23  ALA A C   
176  O  O   . ALA A 23  ? 0.1075 0.1562 0.1760 -0.0110 0.0230  -0.0032 23  ALA A O   
177  C  CB  . ALA A 23  ? 0.0794 0.1735 0.1455 -0.0077 0.0208  0.0012  23  ALA A CB  
178  N  N   . LYS A 24  ? 0.0724 0.1925 0.1580 0.0042  0.0010  -0.0074 24  LYS A N   
179  C  CA  . LYS A 24  ? 0.0882 0.2090 0.1508 0.0172  -0.0066 -0.0016 24  LYS A CA  
180  C  C   . LYS A 24  ? 0.0942 0.2106 0.1713 0.0063  0.0049  -0.0118 24  LYS A C   
181  O  O   . LYS A 24  ? 0.1234 0.2762 0.1753 -0.0006 -0.0002 -0.0078 24  LYS A O   
182  C  CB  . LYS A 24  ? 0.0920 0.2381 0.2093 0.0245  -0.0078 0.0044  24  LYS A CB  
183  C  CG  . LYS A 24  ? 0.1346 0.2975 0.2216 0.0705  0.0126  0.0143  24  LYS A CG  
184  C  CD  . LYS A 24  ? 0.1196 0.2934 0.3263 0.0526  0.0148  -0.0074 24  LYS A CD  
185  C  CE  . LYS A 24  ? 0.2160 0.3057 0.3723 0.0257  0.0520  -0.0078 24  LYS A CE  
186  N  NZ  . LYS A 24  ? 0.2416 0.2648 0.5489 0.0436  0.0885  0.0027  24  LYS A NZ  
187  N  N   . GLY A 25  ? 0.0859 0.1871 0.1825 0.0081  0.0174  -0.0199 25  GLY A N   
188  C  CA  . GLY A 25  ? 0.1110 0.2374 0.1778 -0.0088 0.0234  -0.0502 25  GLY A CA  
189  C  C   . GLY A 25  ? 0.0970 0.2122 0.1692 -0.0118 -0.0264 -0.0359 25  GLY A C   
190  O  O   . GLY A 25  ? 0.0918 0.2312 0.1458 -0.0095 -0.0031 -0.0245 25  GLY A O   
191  N  N   . GLU A 26  ? 0.0997 0.2298 0.1509 -0.0097 -0.0149 -0.0444 26  GLU A N   
192  C  CA  . GLU A 26  ? 0.1024 0.2842 0.1376 -0.0183 0.0059  -0.0652 26  GLU A CA  
193  C  C   . GLU A 26  ? 0.1080 0.1853 0.1024 0.0057  -0.0022 -0.0236 26  GLU A C   
194  O  O   . GLU A 26  ? 0.1401 0.2165 0.0932 -0.0124 0.0058  -0.0106 26  GLU A O   
195  C  CB  . GLU A 26  ? 0.1631 0.3827 0.1849 -0.0403 -0.0165 -0.1189 26  GLU A CB  
196  C  CG  . GLU A 26  ? 0.1056 0.5111 0.2777 -0.0723 -0.0452 -0.1338 26  GLU A CG  
197  C  CD  . GLU A 26  ? 0.4013 0.5695 0.1918 -0.0190 -0.0443 -0.0445 26  GLU A CD  
198  O  OE1 . GLU A 26  ? 0.4970 0.6256 0.4180 -0.1157 0.0117  0.0309  26  GLU A OE1 
199  O  OE2 . GLU A 26  ? 0.3254 0.7048 0.3977 0.1729  -0.1001 -0.0322 26  GLU A OE2 
200  N  N   A ARG A 27  ? 0.0945 0.1432 0.0999 -0.0260 -0.0018 -0.0205 27  ARG A N   
201  N  N   B ARG A 27  ? 0.0873 0.1706 0.0961 0.0239  0.0096  -0.0250 27  ARG A N   
202  C  CA  A ARG A 27  ? 0.0706 0.1408 0.1054 0.0046  0.0093  -0.0323 27  ARG A CA  
203  C  CA  B ARG A 27  ? 0.0742 0.1451 0.0829 0.0086  0.0217  -0.0201 27  ARG A CA  
204  C  C   A ARG A 27  ? 0.0566 0.1343 0.0959 -0.0019 0.0098  -0.0178 27  ARG A C   
205  C  C   B ARG A 27  ? 0.0888 0.1225 0.0829 0.0016  0.0040  -0.0122 27  ARG A C   
206  O  O   A ARG A 27  ? 0.0490 0.1483 0.0961 -0.0164 0.0086  -0.0092 27  ARG A O   
207  O  O   B ARG A 27  ? 0.1032 0.1282 0.1047 0.0156  -0.0125 -0.0188 27  ARG A O   
208  C  CB  A ARG A 27  ? 0.1605 0.1181 0.1206 0.0151  0.0040  -0.0377 27  ARG A CB  
209  C  CB  B ARG A 27  ? 0.1419 0.1322 0.0961 -0.0033 0.0053  -0.0155 27  ARG A CB  
210  C  CG  A ARG A 27  ? 0.1500 0.1552 0.1720 -0.0108 -0.0119 -0.0118 27  ARG A CG  
211  C  CG  B ARG A 27  ? 0.1544 0.1121 0.0929 0.0149  0.0295  -0.0280 27  ARG A CG  
212  C  CD  A ARG A 27  ? 0.2440 0.1702 0.1584 0.0214  -0.0009 -0.0055 27  ARG A CD  
213  C  CD  B ARG A 27  ? 0.1867 0.1101 0.1040 0.0160  0.0015  -0.0264 27  ARG A CD  
214  N  NE  A ARG A 27  ? 0.2442 0.1624 0.1609 0.0435  0.0410  0.0234  27  ARG A NE  
215  N  NE  B ARG A 27  ? 0.1735 0.1548 0.0812 0.0258  0.0394  -0.0335 27  ARG A NE  
216  C  CZ  A ARG A 27  ? 0.2154 0.0873 0.1347 0.0204  0.0137  -0.0251 27  ARG A CZ  
217  C  CZ  B ARG A 27  ? 0.1212 0.1767 0.1067 0.0333  0.0086  -0.0231 27  ARG A CZ  
218  N  NH1 A ARG A 27  ? 0.0334 0.0877 0.0401 0.0172  -0.0095 -0.0524 27  ARG A NH1 
219  N  NH1 B ARG A 27  ? 0.1318 0.1771 0.1641 -0.0046 0.0343  -0.0063 27  ARG A NH1 
220  N  NH2 A ARG A 27  ? 0.0811 0.0645 0.1893 0.0057  0.0816  -0.0675 27  ARG A NH2 
221  N  NH2 B ARG A 27  ? 0.1241 0.2088 0.1207 -0.0077 -0.0010 -0.0236 27  ARG A NH2 
222  N  N   . GLN A 28  ? 0.0644 0.1368 0.1040 -0.0025 0.0073  -0.0351 28  GLN A N   
223  C  CA  . GLN A 28  ? 0.0572 0.1245 0.1013 -0.0082 0.0151  -0.0291 28  GLN A CA  
224  C  C   . GLN A 28  ? 0.0650 0.1062 0.0891 -0.0078 0.0088  -0.0047 28  GLN A C   
225  O  O   . GLN A 28  ? 0.0873 0.1258 0.0943 -0.0134 0.0111  0.0006  28  GLN A O   
226  C  CB  . GLN A 28  ? 0.0541 0.1272 0.1340 -0.0073 0.0148  -0.0219 28  GLN A CB  
227  C  CG  . GLN A 28  ? 0.0699 0.1272 0.1272 -0.0118 0.0089  -0.0032 28  GLN A CG  
228  C  CD  . GLN A 28  ? 0.0696 0.1221 0.1128 -0.0092 -0.0035 -0.0201 28  GLN A CD  
229  O  OE1 . GLN A 28  ? 0.0697 0.1272 0.1216 -0.0117 0.0046  -0.0236 28  GLN A OE1 
230  N  NE2 . GLN A 28  ? 0.0654 0.1260 0.1386 -0.0088 0.0146  -0.0215 28  GLN A NE2 
231  N  N   . SER A 29  ? 0.0653 0.1022 0.0926 0.0027  0.0024  -0.0166 29  SER A N   
232  C  CA  . SER A 29  ? 0.0489 0.1013 0.0952 0.0036  0.0120  -0.0184 29  SER A CA  
233  C  C   . SER A 29  ? 0.0531 0.1003 0.0879 -0.0013 0.0130  -0.0031 29  SER A C   
234  O  O   . SER A 29  ? 0.0651 0.1040 0.1048 -0.0069 0.0275  -0.0025 29  SER A O   
235  C  CB  . SER A 29  ? 0.0732 0.0893 0.1057 0.0159  0.0186  -0.0138 29  SER A CB  
236  O  OG  . SER A 29  ? 0.0627 0.0924 0.1232 0.0070  0.0335  -0.0121 29  SER A OG  
237  N  N   . PRO A 30  ? 0.0744 0.0882 0.0769 -0.0040 0.0196  0.0024  30  PRO A N   
238  C  CA  . PRO A 30  ? 0.0741 0.0929 0.0794 -0.0223 0.0137  0.0076  30  PRO A CA  
239  C  C   . PRO A 30  ? 0.0688 0.0880 0.0839 0.0022  0.0174  -0.0040 30  PRO A C   
240  O  O   . PRO A 30  ? 0.0751 0.1109 0.0897 0.0069  0.0085  0.0016  30  PRO A O   
241  C  CB  . PRO A 30  ? 0.0597 0.0999 0.0897 0.0038  0.0154  -0.0089 30  PRO A CB  
242  C  CG  . PRO A 30  ? 0.0635 0.0778 0.1049 0.0071  0.0151  0.0019  30  PRO A CG  
243  C  CD  . PRO A 30  ? 0.0844 0.0877 0.0850 -0.0027 0.0194  -0.0127 30  PRO A CD  
244  N  N   . VAL A 31  ? 0.0909 0.0926 0.0935 0.0059  0.0317  0.0137  31  VAL A N   
245  C  CA  . VAL A 31  ? 0.1084 0.1153 0.0721 -0.0104 0.0172  0.0117  31  VAL A CA  
246  C  C   . VAL A 31  ? 0.0897 0.1033 0.0891 0.0053  0.0296  0.0212  31  VAL A C   
247  O  O   . VAL A 31  ? 0.0891 0.1005 0.1137 0.0109  0.0103  0.0175  31  VAL A O   
248  C  CB  . VAL A 31  ? 0.0841 0.1085 0.1199 0.0018  0.0199  -0.0099 31  VAL A CB  
249  C  CG1 . VAL A 31  ? 0.1038 0.1336 0.1127 -0.0249 0.0262  0.0067  31  VAL A CG1 
250  C  CG2 . VAL A 31  ? 0.0977 0.1300 0.1176 0.0332  0.0210  -0.0069 31  VAL A CG2 
251  N  N   . ASP A 32  ? 0.1012 0.1006 0.0938 0.0051  0.0232  0.0253  32  ASP A N   
252  C  CA  . ASP A 32  ? 0.1045 0.1137 0.1135 0.0049  0.0466  0.0376  32  ASP A CA  
253  C  C   . ASP A 32  ? 0.0952 0.1116 0.0923 -0.0027 0.0201  0.0210  32  ASP A C   
254  O  O   . ASP A 32  ? 0.1065 0.1461 0.1164 -0.0024 0.0084  -0.0069 32  ASP A O   
255  C  CB  . ASP A 32  ? 0.1311 0.1092 0.1300 0.0103  0.0188  0.0318  32  ASP A CB  
256  C  CG  . ASP A 32  ? 0.1292 0.1253 0.1151 0.0002  0.0258  0.0418  32  ASP A CG  
257  O  OD1 . ASP A 32  ? 0.1491 0.1157 0.1297 0.0002  0.0015  0.0323  32  ASP A OD1 
258  O  OD2 . ASP A 32  ? 0.2240 0.1365 0.1243 -0.0321 0.0168  0.0460  32  ASP A OD2 
259  N  N   . ILE A 33  ? 0.0856 0.1196 0.1056 -0.0034 0.0366  0.0203  33  ILE A N   
260  C  CA  . ILE A 33  ? 0.1060 0.1261 0.1227 0.0276  0.0422  0.0291  33  ILE A CA  
261  C  C   . ILE A 33  ? 0.1311 0.1028 0.1440 0.0321  0.0414  0.0240  33  ILE A C   
262  O  O   . ILE A 33  ? 0.1516 0.1204 0.1404 0.0035  0.0540  0.0232  33  ILE A O   
263  C  CB  . ILE A 33  ? 0.1040 0.1224 0.1232 0.0237  0.0329  0.0248  33  ILE A CB  
264  C  CG1 . ILE A 33  ? 0.1325 0.1017 0.1365 0.0156  0.0034  0.0266  33  ILE A CG1 
265  C  CG2 . ILE A 33  ? 0.1014 0.1397 0.1645 0.0182  0.0509  0.0139  33  ILE A CG2 
266  C  CD1 . ILE A 33  ? 0.1261 0.1753 0.1429 0.0179  -0.0042 0.0266  33  ILE A CD1 
267  N  N   . ASP A 34  ? 0.1343 0.1601 0.1143 0.0130  0.0408  0.0453  34  ASP A N   
268  C  CA  . ASP A 34  ? 0.1303 0.1648 0.1552 0.0058  0.0553  0.0622  34  ASP A CA  
269  C  C   . ASP A 34  ? 0.1656 0.1386 0.1476 0.0233  0.0576  0.0872  34  ASP A C   
270  O  O   . ASP A 34  ? 0.1993 0.1939 0.1591 0.0550  0.0659  0.0418  34  ASP A O   
271  C  CB  . ASP A 34  ? 0.1530 0.2094 0.1613 0.0314  0.0455  0.0604  34  ASP A CB  
272  C  CG  . ASP A 34  ? 0.2094 0.2417 0.1728 0.0139  0.0277  0.0688  34  ASP A CG  
273  O  OD1 . ASP A 34  ? 0.2043 0.2515 0.1796 0.0439  0.0675  0.0847  34  ASP A OD1 
274  O  OD2 . ASP A 34  ? 0.3230 0.3854 0.2697 0.0455  -0.0250 0.1562  34  ASP A OD2 
275  N  N   . THR A 35  ? 0.1451 0.1753 0.1882 0.0220  0.0576  0.0835  35  THR A N   
276  C  CA  . THR A 35  ? 0.1236 0.2534 0.2155 0.0236  0.0674  0.0575  35  THR A CA  
277  C  C   . THR A 35  ? 0.1825 0.2080 0.2043 0.0633  0.0696  0.0328  35  THR A C   
278  O  O   . THR A 35  ? 0.2032 0.2137 0.2154 0.0628  0.0691  0.0100  35  THR A O   
279  C  CB  . THR A 35  ? 0.1760 0.2081 0.2004 0.0373  0.0635  0.0719  35  THR A CB  
280  O  OG1 . THR A 35  ? 0.1620 0.2022 0.2266 0.0058  0.0441  0.0674  35  THR A OG1 
281  C  CG2 . THR A 35  ? 0.1907 0.2960 0.1874 0.0243  0.0421  0.0690  35  THR A CG2 
282  N  N   . HIS A 36  ? 0.2108 0.1814 0.1918 0.0665  0.1032  0.0741  36  HIS A N   
283  C  CA  . HIS A 36  ? 0.2889 0.1552 0.1760 0.0262  0.1039  0.0666  36  HIS A CA  
284  C  C   . HIS A 36  ? 0.3157 0.1921 0.1843 0.0156  0.1305  0.0239  36  HIS A C   
285  O  O   . HIS A 36  ? 0.2302 0.2708 0.1972 0.0325  0.0763  0.0309  36  HIS A O   
286  C  CB  . HIS A 36  ? 0.3096 0.1638 0.1390 0.0432  0.0795  0.0422  36  HIS A CB  
287  C  CG  . HIS A 36  ? 0.3025 0.2068 0.1234 0.0078  0.0216  0.0288  36  HIS A CG  
288  N  ND1 . HIS A 36  ? 0.3603 0.2083 0.1461 0.0008  0.0255  0.0163  36  HIS A ND1 
289  C  CD2 . HIS A 36  ? 0.3147 0.1810 0.1602 0.0463  0.0297  0.0433  36  HIS A CD2 
290  C  CE1 . HIS A 36  ? 0.4171 0.2320 0.1558 0.0643  0.0002  -0.0106 36  HIS A CE1 
291  N  NE2 . HIS A 36  ? 0.3996 0.1666 0.2349 0.0806  -0.0535 -0.0376 36  HIS A NE2 
292  N  N   . THR A 37  ? 0.2475 0.1825 0.1746 0.0435  0.0842  0.0593  37  THR A N   
293  C  CA  . THR A 37  ? 0.2597 0.1760 0.1839 0.0496  0.0757  0.0447  37  THR A CA  
294  C  C   . THR A 37  ? 0.2834 0.1760 0.1483 0.0688  0.0550  0.0190  37  THR A C   
295  O  O   . THR A 37  ? 0.4408 0.2069 0.2252 0.0375  0.0212  0.0031  37  THR A O   
296  C  CB  . THR A 37  ? 0.2482 0.3466 0.2565 0.1274  0.0895  0.0505  37  THR A CB  
297  O  OG1 . THR A 37  ? 0.3380 0.3395 0.2345 0.1010  0.0335  0.0825  37  THR A OG1 
298  C  CG2 . THR A 37  ? 0.2514 0.2410 0.3639 0.0961  0.0743  0.0089  37  THR A CG2 
299  N  N   . ALA A 38  ? 0.2087 0.1932 0.1760 0.0507  0.0770  0.0401  38  ALA A N   
300  C  CA  . ALA A 38  ? 0.2442 0.1641 0.1569 0.0529  0.0625  0.0194  38  ALA A CA  
301  C  C   . ALA A 38  ? 0.2523 0.2079 0.1379 0.0405  0.0791  0.0458  38  ALA A C   
302  O  O   . ALA A 38  ? 0.2317 0.2155 0.2587 0.0449  0.0856  0.0571  38  ALA A O   
303  C  CB  . ALA A 38  ? 0.1577 0.1634 0.1929 0.0109  0.0546  0.0165  38  ALA A CB  
304  N  N   . LYS A 39  ? 0.2493 0.2274 0.1476 0.0952  0.0255  0.0290  39  LYS A N   
305  C  CA  . LYS A 39  ? 0.3015 0.2651 0.1595 0.1486  0.0263  0.0113  39  LYS A CA  
306  C  C   . LYS A 39  ? 0.2482 0.2019 0.1279 0.0587  0.0423  0.0089  39  LYS A C   
307  O  O   . LYS A 39  ? 0.1534 0.2405 0.1168 0.0419  0.0201  0.0345  39  LYS A O   
308  C  CB  . LYS A 39  ? 0.3349 0.3890 0.2216 0.1675  -0.0819 -0.0660 39  LYS A CB  
309  C  CG  . LYS A 39  ? 0.3000 0.4613 0.1935 0.0973  0.0223  -0.0285 39  LYS A CG  
310  C  CD  . LYS A 39  ? 0.3248 0.3574 0.2522 0.1736  0.0142  0.0475  39  LYS A CD  
311  C  CE  . LYS A 39  ? 0.4108 0.3632 0.2464 0.1339  0.0269  0.0350  39  LYS A CE  
312  N  NZ  . LYS A 39  ? 0.2515 0.4030 0.3561 0.1203  0.0932  0.1221  39  LYS A NZ  
313  N  N   . TYR A 40  ? 0.2636 0.2708 0.1119 0.0297  0.0274  0.0374  40  TYR A N   
314  C  CA  . TYR A 40  ? 0.2399 0.2569 0.1063 -0.0095 0.0719  0.0165  40  TYR A CA  
315  C  C   . TYR A 40  ? 0.1433 0.2431 0.1265 -0.0047 0.0275  -0.0021 40  TYR A C   
316  O  O   . TYR A 40  ? 0.2126 0.3286 0.1067 0.0560  0.0373  0.0054  40  TYR A O   
317  C  CB  . TYR A 40  ? 0.3453 0.3179 0.1767 -0.1171 0.0389  0.0134  40  TYR A CB  
318  C  CG  . TYR A 40  ? 0.3148 0.4165 0.2770 -0.1185 -0.0093 0.0785  40  TYR A CG  
319  C  CD1 . TYR A 40  ? 0.4482 0.3963 0.1703 -0.1500 0.0074  -0.0052 40  TYR A CD1 
320  C  CD2 . TYR A 40  ? 0.3786 0.7957 0.3862 0.3009  0.2976  -0.0375 40  TYR A CD2 
321  C  CE1 . TYR A 40  ? 0.4192 0.5834 0.8039 -0.1288 -0.4295 -0.0377 40  TYR A CE1 
322  C  CE2 . TYR A 40  ? 0.4501 0.5100 1.0189 0.2030  0.2509  -0.1161 40  TYR A CE2 
323  C  CZ  . TYR A 40  ? 1.0795 1.3236 0.5870 -0.1218 0.6749  -0.1918 40  TYR A CZ  
324  O  OH  . TYR A 40  ? 0.1724 1.5782 2.3431 0.1544  0.3958  0.4531  40  TYR A OH  
325  N  N   . ASP A 41  ? 0.1692 0.2152 0.1588 0.0443  0.0469  -0.0093 41  ASP A N   
326  C  CA  . ASP A 41  ? 0.1649 0.2162 0.1602 0.0168  0.0136  -0.0017 41  ASP A CA  
327  C  C   . ASP A 41  ? 0.2320 0.3079 0.1523 0.1132  0.0057  -0.0390 41  ASP A C   
328  O  O   . ASP A 41  ? 0.1825 0.3862 0.1717 0.0724  0.0160  -0.0121 41  ASP A O   
329  C  CB  . ASP A 41  ? 0.1900 0.2177 0.2367 -0.0210 -0.0033 -0.0111 41  ASP A CB  
330  C  CG  . ASP A 41  ? 0.4106 0.2187 0.3352 -0.0227 0.0116  -0.0438 41  ASP A CG  
331  O  OD1 . ASP A 41  ? 0.4311 0.3150 0.2943 0.0680  -0.0919 -0.1207 41  ASP A OD1 
332  O  OD2 . ASP A 41  ? 0.3876 0.2666 0.4328 -0.0844 -0.1388 0.0279  41  ASP A OD2 
333  N  N   . PRO A 42  ? 0.2037 0.3931 0.1954 0.0844  0.0559  -0.0428 42  PRO A N   
334  C  CA  . PRO A 42  ? 0.3269 0.4005 0.5543 0.1854  -0.1693 -0.1123 42  PRO A CA  
335  C  C   . PRO A 42  ? 0.5177 0.5263 0.4106 0.0288  -0.1249 0.1009  42  PRO A C   
336  O  O   . PRO A 42  ? 0.2608 0.7067 0.3552 0.1878  0.0368  0.0475  42  PRO A O   
337  C  CB  . PRO A 42  ? 0.5307 0.4668 0.6031 -0.0480 -0.0072 0.1957  42  PRO A CB  
338  C  CG  . PRO A 42  ? 0.5137 0.5403 0.6743 0.0161  -0.0889 0.2094  42  PRO A CG  
339  C  CD  . PRO A 42  ? 0.6380 0.3089 0.4327 0.0166  -0.0534 0.3121  42  PRO A CD  
340  N  N   . SER A 43  ? 0.3746 0.4121 0.2558 0.1654  -0.0298 0.0122  43  SER A N   
341  C  CA  . SER A 43  ? 0.6102 0.3383 0.2633 0.1735  0.0089  -0.1174 43  SER A CA  
342  C  C   . SER A 43  ? 0.4537 0.4087 0.3378 0.2197  0.0605  0.0055  43  SER A C   
343  O  O   . SER A 43  ? 0.5748 0.4127 0.5053 0.1311  -0.1961 0.0469  43  SER A O   
344  C  CB  . SER A 43  ? 0.6001 0.5030 0.3890 0.1412  -0.0797 -0.0652 43  SER A CB  
345  O  OG  . SER A 43  ? 0.6750 0.4462 0.3484 0.0587  -0.0547 -0.1701 43  SER A OG  
346  N  N   . LEU A 44  ? 0.4015 0.5594 0.2911 0.2302  0.0008  -0.0575 44  LEU A N   
347  C  CA  . LEU A 44  ? 0.4273 0.5457 0.3345 0.0757  0.0336  0.0239  44  LEU A CA  
348  C  C   . LEU A 44  ? 0.4699 0.5820 0.5477 0.0256  -0.1208 0.0914  44  LEU A C   
349  O  O   . LEU A 44  ? 0.4137 0.7537 0.2384 -0.1128 0.1625  0.1688  44  LEU A O   
350  C  CB  . LEU A 44  ? 0.2083 0.4934 0.1652 -0.0540 0.0227  0.0126  44  LEU A CB  
351  C  CG  . LEU A 44  ? 0.2310 0.2508 0.2618 -0.0316 -0.0012 0.0244  44  LEU A CG  
352  C  CD1 . LEU A 44  ? 0.3103 0.2859 0.1940 -0.0665 0.0474  -0.0095 44  LEU A CD1 
353  C  CD2 . LEU A 44  ? 0.2252 0.2551 0.2029 -0.0013 0.0335  0.0079  44  LEU A CD2 
354  N  N   . LYS A 45  ? 0.1702 0.9442 0.5109 0.0075  0.0991  0.1254  45  LYS A N   
355  C  CA  . LYS A 45  ? 0.4206 0.5495 0.6081 -0.0504 -0.0812 0.0266  45  LYS A CA  
356  C  C   . LYS A 45  ? 0.3340 0.7210 0.3686 0.0480  -0.0027 0.0458  45  LYS A C   
357  O  O   . LYS A 45  ? 0.4242 0.6144 0.5191 -0.1248 -0.1849 -0.0737 45  LYS A O   
358  C  CB  . LYS A 45  ? 0.3276 0.5410 0.4909 0.1504  0.0104  -0.1356 45  LYS A CB  
359  C  CG  . LYS A 45  ? 0.3631 0.7427 0.2727 0.0833  -0.0439 -0.1327 45  LYS A CG  
360  N  N   . PRO A 46  ? 0.5156 0.5026 0.4611 -0.1656 -0.1514 0.0385  46  PRO A N   
361  C  CA  . PRO A 46  ? 0.3039 0.2911 0.4216 -0.0283 0.0111  0.0986  46  PRO A CA  
362  C  C   . PRO A 46  ? 0.2484 0.4371 0.2180 0.0686  -0.0131 0.0583  46  PRO A C   
363  O  O   . PRO A 46  ? 0.2898 0.5398 0.3625 0.0151  0.0156  0.1441  46  PRO A O   
364  C  CB  . PRO A 46  ? 0.4796 0.8953 0.9815 -0.2138 -0.2584 0.0897  46  PRO A CB  
365  C  CG  . PRO A 46  ? 0.0723 0.9694 0.6710 0.1177  0.0335  -0.0142 46  PRO A CG  
366  C  CD  . PRO A 46  ? 1.1260 0.8654 0.5251 0.2945  0.3983  0.1529  46  PRO A CD  
367  N  N   . LEU A 47  ? 0.2203 0.4798 0.3610 -0.0138 -0.0364 0.1472  47  LEU A N   
368  C  CA  . LEU A 47  ? 0.1710 0.4932 0.3986 0.0264  0.0260  0.1377  47  LEU A CA  
369  C  C   . LEU A 47  ? 0.2180 0.1505 0.4086 -0.0153 0.0255  0.0867  47  LEU A C   
370  O  O   . LEU A 47  ? 0.2094 0.2830 0.4062 -0.0466 -0.0391 0.1764  47  LEU A O   
371  C  CB  . LEU A 47  ? 0.7684 0.5815 0.6281 0.3972  0.0537  -0.1359 47  LEU A CB  
372  C  CG  . LEU A 47  ? 0.4826 0.7957 0.6348 -0.0469 -0.0300 -0.1269 47  LEU A CG  
373  C  CD1 . LEU A 47  ? 1.0855 0.5475 0.4433 -0.0228 0.3601  -0.1412 47  LEU A CD1 
374  C  CD2 . LEU A 47  ? 0.2619 0.8930 1.0675 -0.2928 0.0623  0.3955  47  LEU A CD2 
375  N  N   . SER A 48  ? 0.0665 0.2094 0.2526 -0.0039 0.0183  0.0714  48  SER A N   
376  C  CA  . SER A 48  ? 0.1023 0.2187 0.2032 -0.0079 0.0286  0.0423  48  SER A CA  
377  C  C   . SER A 48  ? 0.0942 0.1842 0.2370 -0.0230 0.0381  0.0305  48  SER A C   
378  O  O   . SER A 48  ? 0.0954 0.2029 0.2440 -0.0354 0.0601  0.0197  48  SER A O   
379  C  CB  . SER A 48  ? 0.1318 0.2119 0.2320 0.0223  0.0129  0.0496  48  SER A CB  
380  O  OG  . SER A 48  ? 0.1728 0.2629 0.2648 0.0326  0.0238  0.0520  48  SER A OG  
381  N  N   . VAL A 49  ? 0.1203 0.1904 0.1979 -0.0226 0.0508  0.0193  49  VAL A N   
382  C  CA  . VAL A 49  ? 0.1634 0.1986 0.2116 -0.0594 0.0649  -0.0164 49  VAL A CA  
383  C  C   . VAL A 49  ? 0.1609 0.2331 0.1950 -0.0740 0.0504  -0.0124 49  VAL A C   
384  O  O   . VAL A 49  ? 0.1868 0.3151 0.2435 -0.1113 0.0421  -0.0136 49  VAL A O   
385  C  CB  . VAL A 49  ? 0.1889 0.2202 0.2727 -0.0490 0.0974  -0.0234 49  VAL A CB  
386  C  CG1 . VAL A 49  ? 0.3101 0.2928 0.3085 -0.1057 0.1912  -0.0420 49  VAL A CG1 
387  C  CG2 . VAL A 49  ? 0.1612 0.2026 0.3898 -0.0236 0.0732  0.0091  49  VAL A CG2 
388  N  N   . SER A 50  ? 0.1437 0.2061 0.2572 -0.0486 0.0419  0.0010  50  SER A N   
389  C  CA  . SER A 50  ? 0.1347 0.2148 0.2540 -0.0432 0.0368  -0.0136 50  SER A CA  
390  C  C   . SER A 50  ? 0.0915 0.2040 0.2362 -0.0089 0.0168  -0.0159 50  SER A C   
391  O  O   . SER A 50  ? 0.1465 0.2033 0.2489 -0.0217 0.0370  0.0039  50  SER A O   
392  C  CB  . SER A 50  ? 0.2176 0.2795 0.3139 -0.0436 0.1123  -0.1055 50  SER A CB  
393  O  OG  . SER A 50  ? 0.2323 0.3639 0.3244 0.0029  0.0655  -0.0447 50  SER A OG  
394  N  N   . TYR A 51  ? 0.0967 0.1943 0.2470 -0.0027 0.0220  -0.0215 51  TYR A N   
395  C  CA  . TYR A 51  ? 0.1094 0.2065 0.2234 0.0154  0.0292  -0.0155 51  TYR A CA  
396  C  C   . TYR A 51  ? 0.1315 0.1983 0.2573 -0.0075 0.0262  0.0412  51  TYR A C   
397  O  O   . TYR A 51  ? 0.1111 0.2673 0.2828 0.0109  -0.0059 0.0383  51  TYR A O   
398  C  CB  . TYR A 51  ? 0.1038 0.1874 0.2140 0.0038  -0.0087 -0.0195 51  TYR A CB  
399  C  CG  . TYR A 51  ? 0.1099 0.1879 0.1911 -0.0136 0.0055  -0.0116 51  TYR A CG  
400  C  CD1 . TYR A 51  ? 0.1137 0.1925 0.2374 -0.0201 -0.0159 -0.0058 51  TYR A CD1 
401  C  CD2 . TYR A 51  ? 0.0891 0.1742 0.1954 -0.0021 0.0231  -0.0083 51  TYR A CD2 
402  C  CE1 . TYR A 51  ? 0.0783 0.1422 0.2231 -0.0212 0.0126  0.0185  51  TYR A CE1 
403  C  CE2 . TYR A 51  ? 0.0979 0.1372 0.1845 -0.0356 0.0181  0.0042  51  TYR A CE2 
404  C  CZ  . TYR A 51  ? 0.0925 0.1340 0.1760 -0.0258 0.0136  -0.0018 51  TYR A CZ  
405  O  OH  . TYR A 51  ? 0.0908 0.1375 0.1983 -0.0178 -0.0010 -0.0086 51  TYR A OH  
406  N  N   A ASP A 52  ? 0.0917 0.2705 0.3116 -0.0031 -0.0086 0.0384  52  ASP A N   
407  N  N   B ASP A 52  ? 0.0756 0.2819 0.3050 -0.0229 -0.0111 0.0483  52  ASP A N   
408  C  CA  A ASP A 52  ? 0.1850 0.2861 0.3229 0.0276  -0.0323 0.0802  52  ASP A CA  
409  C  CA  B ASP A 52  ? 0.1065 0.3076 0.3362 -0.0165 -0.0248 0.0778  52  ASP A CA  
410  C  C   A ASP A 52  ? 0.2673 0.2413 0.2694 0.0252  -0.0027 0.0133  52  ASP A C   
411  C  C   B ASP A 52  ? 0.1717 0.3251 0.3080 -0.0013 -0.0099 0.0570  52  ASP A C   
412  O  O   A ASP A 52  ? 0.2960 0.3017 0.2676 0.1347  0.0001  0.0049  52  ASP A O   
413  O  O   B ASP A 52  ? 0.2126 0.4444 0.3093 0.0280  -0.0269 0.0807  52  ASP A O   
414  C  CB  A ASP A 52  ? 0.0599 0.4374 0.4424 0.0611  -0.0520 0.0295  52  ASP A CB  
415  C  CB  B ASP A 52  ? 0.1254 0.3847 0.3804 0.0713  -0.0290 0.1130  52  ASP A CB  
416  C  CG  A ASP A 52  ? 0.2570 0.3847 0.4300 0.0635  0.0107  0.0548  52  ASP A CG  
417  C  CG  B ASP A 52  ? 0.3251 0.3499 0.2834 0.0150  -0.0714 0.0708  52  ASP A CG  
418  O  OD1 A ASP A 52  ? 0.1577 0.4270 0.4139 0.0421  0.0837  0.1314  52  ASP A OD1 
419  O  OD1 B ASP A 52  ? 0.2187 0.4568 0.4615 0.1513  0.0096  -0.0783 52  ASP A OD1 
420  O  OD2 A ASP A 52  ? 0.2784 0.4523 0.5068 0.0610  -0.0744 0.1104  52  ASP A OD2 
421  O  OD2 B ASP A 52  ? 0.5578 0.4117 0.4802 0.1749  0.0019  0.0264  52  ASP A OD2 
422  N  N   . GLN A 53  ? 0.1382 0.2342 0.3840 0.0451  0.0469  0.0726  53  GLN A N   
423  C  CA  . GLN A 53  ? 0.1846 0.3022 0.4595 -0.0193 0.0871  0.1056  53  GLN A CA  
424  C  C   . GLN A 53  ? 0.2198 0.2058 0.3736 0.0372  0.0850  0.0597  53  GLN A C   
425  O  O   . GLN A 53  ? 0.2197 0.2151 0.4255 0.0163  0.0547  0.0705  53  GLN A O   
426  C  CB  . GLN A 53  ? 0.4792 0.3610 0.5305 0.0350  0.0842  0.0273  53  GLN A CB  
427  C  CG  . GLN A 53  ? 0.4518 0.4180 0.7044 -0.0368 0.1159  0.0908  53  GLN A CG  
428  C  CD  . GLN A 53  ? 0.7259 0.6282 0.7852 -0.1436 0.0443  0.1215  53  GLN A CD  
429  O  OE1 . GLN A 53  ? 0.5631 0.6840 0.9025 -0.0835 0.0043  0.0866  53  GLN A OE1 
430  N  NE2 . GLN A 53  ? 0.6633 0.4390 0.4201 0.0233  -0.0210 0.1694  53  GLN A NE2 
431  N  N   . ALA A 54  ? 0.1361 0.1734 0.4288 0.0047  0.0566  0.0305  54  ALA A N   
432  C  CA  . ALA A 54  ? 0.1289 0.1703 0.3057 0.0164  0.0190  -0.0025 54  ALA A CA  
433  C  C   . ALA A 54  ? 0.1448 0.1624 0.3240 -0.0176 0.0122  -0.0223 54  ALA A C   
434  O  O   . ALA A 54  ? 0.1443 0.3037 0.3826 -0.0331 0.0000  -0.1185 54  ALA A O   
435  C  CB  . ALA A 54  ? 0.1576 0.1738 0.3277 -0.0074 0.0263  0.0139  54  ALA A CB  
436  N  N   . THR A 55  ? 0.1127 0.1508 0.2867 0.0155  0.0108  0.0313  55  THR A N   
437  C  CA  . THR A 55  ? 0.1195 0.2263 0.2810 0.0241  -0.0392 0.0650  55  THR A CA  
438  C  C   . THR A 55  ? 0.1307 0.1376 0.1573 -0.0225 -0.0206 0.0277  55  THR A C   
439  O  O   . THR A 55  ? 0.1121 0.1190 0.2001 0.0071  -0.0318 0.0223  55  THR A O   
440  C  CB  . THR A 55  ? 0.3093 0.2428 0.3765 0.0294  -0.0471 0.0318  55  THR A CB  
441  O  OG1 . THR A 55  ? 0.3446 0.3153 0.6427 -0.0013 -0.0709 -0.0466 55  THR A OG1 
442  C  CG2 . THR A 55  ? 0.4108 0.4340 0.4112 0.0352  0.0479  0.1376  55  THR A CG2 
443  N  N   . SER A 56  ? 0.1322 0.1275 0.1875 0.0059  -0.0372 0.0226  56  SER A N   
444  C  CA  . SER A 56  ? 0.1289 0.1195 0.1573 -0.0010 -0.0220 0.0076  56  SER A CA  
445  C  C   . SER A 56  ? 0.1857 0.1383 0.1598 -0.0125 -0.0618 0.0241  56  SER A C   
446  O  O   . SER A 56  ? 0.2029 0.1487 0.1886 0.0093  -0.0678 0.0475  56  SER A O   
447  C  CB  . SER A 56  ? 0.1889 0.1333 0.1238 0.0114  -0.0542 0.0108  56  SER A CB  
448  O  OG  . SER A 56  ? 0.1638 0.1426 0.1530 -0.0307 -0.0560 0.0364  56  SER A OG  
449  N  N   . LEU A 57  ? 0.1789 0.1179 0.1656 -0.0009 -0.0216 0.0392  57  LEU A N   
450  C  CA  . LEU A 57  ? 0.1899 0.1242 0.1749 0.0037  0.0055  0.0383  57  LEU A CA  
451  C  C   . LEU A 57  ? 0.1433 0.1383 0.1631 0.0118  -0.0173 0.0483  57  LEU A C   
452  O  O   . LEU A 57  ? 0.1773 0.1465 0.1573 0.0131  -0.0330 0.0401  57  LEU A O   
453  C  CB  . LEU A 57  ? 0.3195 0.1329 0.2043 -0.0760 0.0342  0.0293  57  LEU A CB  
454  C  CG  . LEU A 57  ? 0.4242 0.1795 0.2008 -0.0274 0.0215  0.0044  57  LEU A CG  
455  C  CD1 . LEU A 57  ? 0.5739 0.2861 0.2770 -0.1852 0.0298  -0.0118 57  LEU A CD1 
456  C  CD2 . LEU A 57  ? 0.5368 0.1907 0.3834 0.0810  -0.0436 0.0535  57  LEU A CD2 
457  N  N   . ARG A 58  ? 0.1469 0.1307 0.1577 0.0243  -0.0399 0.0030  58  ARG A N   
458  C  CA  . ARG A 58  ? 0.1314 0.1333 0.1778 0.0266  -0.0074 0.0586  58  ARG A CA  
459  C  C   . ARG A 58  ? 0.1182 0.1340 0.1365 -0.0154 0.0010  0.0519  58  ARG A C   
460  O  O   . ARG A 58  ? 0.1573 0.1448 0.1238 0.0089  -0.0149 0.0285  58  ARG A O   
461  C  CB  . ARG A 58  ? 0.2313 0.1429 0.3072 -0.0011 0.0495  0.1007  58  ARG A CB  
462  C  CG  . ARG A 58  ? 0.1993 0.2594 0.2924 -0.0096 0.0350  0.0939  58  ARG A CG  
463  C  CD  . ARG A 58  ? 0.2220 0.3356 0.2952 -0.0576 -0.0008 0.0558  58  ARG A CD  
464  N  NE  . ARG A 58  ? 0.1810 0.2377 0.2425 -0.0533 0.0271  0.0497  58  ARG A NE  
465  C  CZ  . ARG A 58  ? 0.1662 0.2536 0.2180 -0.0708 0.0350  0.0314  58  ARG A CZ  
466  N  NH1 . ARG A 58  ? 0.2402 0.2178 0.1965 -0.0585 0.0469  -0.0124 58  ARG A NH1 
467  N  NH2 . ARG A 58  ? 0.1505 0.1749 0.2198 -0.0206 0.0699  0.0179  58  ARG A NH2 
468  N  N   . ILE A 59  ? 0.1062 0.1401 0.1239 -0.0024 0.0062  0.0309  59  ILE A N   
469  C  CA  . ILE A 59  ? 0.1042 0.1223 0.1155 0.0015  0.0046  0.0239  59  ILE A CA  
470  C  C   . ILE A 59  ? 0.1185 0.1412 0.0978 0.0114  0.0120  0.0453  59  ILE A C   
471  O  O   . ILE A 59  ? 0.1329 0.1918 0.1024 0.0216  0.0214  0.0529  59  ILE A O   
472  C  CB  . ILE A 59  ? 0.1162 0.1418 0.1040 -0.0085 -0.0111 0.0314  59  ILE A CB  
473  C  CG1 . ILE A 59  ? 0.1322 0.1408 0.1150 0.0059  0.0048  0.0401  59  ILE A CG1 
474  C  CG2 . ILE A 59  ? 0.1552 0.1523 0.0990 0.0096  0.0034  0.0273  59  ILE A CG2 
475  C  CD1 . ILE A 59  ? 0.1835 0.1448 0.1425 -0.0114 -0.0064 0.0480  59  ILE A CD1 
476  N  N   . LEU A 60  ? 0.0911 0.1555 0.1297 0.0060  0.0054  0.0285  60  LEU A N   
477  C  CA  . LEU A 60  ? 0.0979 0.1358 0.1248 0.0074  0.0150  0.0401  60  LEU A CA  
478  C  C   . LEU A 60  ? 0.1057 0.1462 0.1176 -0.0020 0.0223  0.0495  60  LEU A C   
479  O  O   . LEU A 60  ? 0.1055 0.1595 0.1093 -0.0118 0.0251  0.0414  60  LEU A O   
480  C  CB  . LEU A 60  ? 0.1102 0.1317 0.1886 -0.0052 0.0027  0.0414  60  LEU A CB  
481  C  CG  . LEU A 60  ? 0.1296 0.2008 0.1870 -0.0292 -0.0092 0.0535  60  LEU A CG  
482  C  CD1 . LEU A 60  ? 0.1390 0.2223 0.2380 -0.0175 0.0672  0.0787  60  LEU A CD1 
483  C  CD2 . LEU A 60  ? 0.1318 0.1828 0.2367 -0.0584 -0.0245 0.0413  60  LEU A CD2 
484  N  N   . ASN A 61  ? 0.0956 0.1357 0.1304 -0.0013 0.0152  0.0291  61  ASN A N   
485  C  CA  . ASN A 61  ? 0.0811 0.1379 0.1401 0.0105  0.0239  0.0209  61  ASN A CA  
486  C  C   . ASN A 61  ? 0.1190 0.1177 0.1440 -0.0147 0.0171  0.0409  61  ASN A C   
487  O  O   . ASN A 61  ? 0.1249 0.1390 0.1509 -0.0099 0.0277  0.0521  61  ASN A O   
488  C  CB  . ASN A 61  ? 0.1177 0.1659 0.1161 0.0018  0.0223  0.0337  61  ASN A CB  
489  C  CG  . ASN A 61  ? 0.1014 0.1505 0.1103 -0.0173 0.0307  0.0343  61  ASN A CG  
490  O  OD1 . ASN A 61  ? 0.1180 0.1501 0.1216 -0.0044 0.0204  0.0205  61  ASN A OD1 
491  N  ND2 . ASN A 61  ? 0.1559 0.1576 0.1057 -0.0193 0.0445  0.0096  61  ASN A ND2 
492  N  N   . THR A 62  ? 0.0954 0.1289 0.1433 -0.0071 0.0096  0.0240  62  THR A N   
493  C  CA  . THR A 62  ? 0.1133 0.1333 0.1491 -0.0062 0.0254  0.0265  62  THR A CA  
494  C  C   . THR A 62  ? 0.0967 0.1412 0.1498 -0.0214 0.0370  0.0190  62  THR A C   
495  O  O   . THR A 62  ? 0.1342 0.1781 0.2259 -0.0439 0.0076  0.0234  62  THR A O   
496  C  CB  . THR A 62  ? 0.1247 0.1426 0.1451 0.0029  0.0160  0.0089  62  THR A CB  
497  O  OG1 . THR A 62  ? 0.1285 0.1297 0.1569 -0.0008 0.0073  0.0128  62  THR A OG1 
498  C  CG2 . THR A 62  ? 0.1462 0.1577 0.2187 0.0392  -0.0158 -0.0339 62  THR A CG2 
499  N  N   . GLY A 63  ? 0.1164 0.1322 0.1379 0.0026  0.0223  0.0310  63  GLY A N   
500  C  CA  . GLY A 63  ? 0.1141 0.1613 0.1209 0.0070  0.0261  0.0346  63  GLY A CA  
501  C  C   . GLY A 63  ? 0.1383 0.1213 0.1153 -0.0032 0.0419  0.0041  63  GLY A C   
502  O  O   . GLY A 63  ? 0.1238 0.1638 0.1426 0.0073  0.0372  0.0233  63  GLY A O   
503  N  N   . TYR A 64  ? 0.1189 0.1411 0.0978 -0.0122 0.0375  0.0079  64  TYR A N   
504  C  CA  . TYR A 64  ? 0.0945 0.1659 0.1160 -0.0168 0.0126  0.0278  64  TYR A CA  
505  C  C   . TYR A 64  ? 0.0918 0.1670 0.0742 0.0004  0.0240  0.0125  64  TYR A C   
506  O  O   . TYR A 64  ? 0.1155 0.2433 0.2165 0.0102  0.0253  0.1274  64  TYR A O   
507  C  CB  . TYR A 64  ? 0.1304 0.2055 0.1209 -0.0122 -0.0024 0.0027  64  TYR A CB  
508  C  CG  . TYR A 64  ? 0.1936 0.2648 0.1803 -0.0388 -0.0116 0.0381  64  TYR A CG  
509  C  CD1 . TYR A 64  ? 0.1515 0.4284 0.2148 0.0027  -0.0042 -0.0042 64  TYR A CD1 
510  C  CD2 . TYR A 64  ? 0.2920 0.2615 0.2310 -0.1186 -0.0253 0.0173  64  TYR A CD2 
511  C  CE1 . TYR A 64  ? 0.1204 0.5131 0.3168 0.0074  -0.0130 -0.0019 64  TYR A CE1 
512  C  CE2 . TYR A 64  ? 0.2874 0.4500 0.3928 -0.1846 0.1086  0.0159  64  TYR A CE2 
513  C  CZ  . TYR A 64  ? 0.4769 0.4207 0.4410 -0.0856 0.0272  -0.0719 64  TYR A CZ  
514  O  OH  . TYR A 64  ? 0.4874 0.6815 0.4498 -0.1090 0.0266  -0.0774 64  TYR A OH  
515  N  N   . LEU A 65  ? 0.0911 0.1227 0.1005 0.0042  0.0216  0.0130  65  LEU A N   
516  C  CA  . LEU A 65  ? 0.0968 0.1394 0.0997 -0.0039 0.0410  0.0132  65  LEU A CA  
517  C  C   . LEU A 65  ? 0.1024 0.1157 0.1015 -0.0110 0.0339  0.0142  65  LEU A C   
518  O  O   . LEU A 65  ? 0.0902 0.1230 0.1128 -0.0121 0.0280  0.0217  65  LEU A O   
519  C  CB  . LEU A 65  ? 0.1408 0.1638 0.1028 0.0001  0.0410  -0.0074 65  LEU A CB  
520  C  CG  . LEU A 65  ? 0.1375 0.2083 0.1243 0.0018  0.0148  -0.0420 65  LEU A CG  
521  C  CD1 . LEU A 65  ? 0.1788 0.1342 0.2249 0.0046  0.0129  -0.0626 65  LEU A CD1 
522  C  CD2 . LEU A 65  ? 0.1547 0.3722 0.1293 0.0096  0.0386  -0.0604 65  LEU A CD2 
523  N  N   . PHE A 66  ? 0.0925 0.1146 0.1090 0.0046  0.0179  0.0133  66  PHE A N   
524  C  CA  . PHE A 66  ? 0.1032 0.1350 0.1004 0.0037  0.0179  0.0121  66  PHE A CA  
525  C  C   . PHE A 66  ? 0.0969 0.1190 0.1054 -0.0092 0.0111  0.0047  66  PHE A C   
526  O  O   . PHE A 66  ? 0.0890 0.1443 0.1057 -0.0031 0.0135  0.0201  66  PHE A O   
527  C  CB  . PHE A 66  ? 0.1118 0.1631 0.1111 -0.0277 0.0026  0.0238  66  PHE A CB  
528  C  CG  . PHE A 66  ? 0.1286 0.1372 0.0850 -0.0240 0.0003  0.0156  66  PHE A CG  
529  C  CD1 . PHE A 66  ? 0.1037 0.1824 0.1254 -0.0125 -0.0048 0.0065  66  PHE A CD1 
530  C  CD2 . PHE A 66  ? 0.1318 0.1336 0.1254 -0.0194 -0.0128 0.0036  66  PHE A CD2 
531  C  CE1 . PHE A 66  ? 0.1297 0.1552 0.1173 -0.0065 0.0062  0.0184  66  PHE A CE1 
532  C  CE2 . PHE A 66  ? 0.1254 0.1254 0.1058 -0.0218 -0.0259 0.0087  66  PHE A CE2 
533  C  CZ  . PHE A 66  ? 0.1371 0.1559 0.1141 -0.0023 -0.0276 0.0152  66  PHE A CZ  
534  N  N   . GLN A 67  ? 0.1081 0.1511 0.1125 0.0145  0.0199  0.0377  67  GLN A N   
535  C  CA  . GLN A 67  ? 0.0929 0.1358 0.1354 0.0307  0.0072  0.0230  67  GLN A CA  
536  C  C   . GLN A 67  ? 0.0873 0.1292 0.1046 -0.0033 0.0106  0.0306  67  GLN A C   
537  O  O   . GLN A 67  ? 0.1076 0.1842 0.1080 0.0012  0.0236  0.0483  67  GLN A O   
538  C  CB  . GLN A 67  ? 0.1272 0.1533 0.1480 -0.0093 -0.0060 0.0372  67  GLN A CB  
539  C  CG  . GLN A 67  ? 0.1368 0.1631 0.1613 -0.0348 0.0030  0.0292  67  GLN A CG  
540  C  CD  . GLN A 67  ? 0.2026 0.2137 0.2233 -0.0958 -0.0075 0.0401  67  GLN A CD  
541  O  OE1 . GLN A 67  ? 0.1720 0.3067 0.2266 -0.0624 -0.0179 0.0215  67  GLN A OE1 
542  N  NE2 . GLN A 67  ? 0.3018 0.2159 0.3276 -0.1047 -0.0946 0.0725  67  GLN A NE2 
543  N  N   . VAL A 68  ? 0.0820 0.1150 0.1300 0.0188  0.0030  0.0248  68  VAL A N   
544  C  CA  . VAL A 68  ? 0.1148 0.1199 0.1102 0.0222  -0.0100 0.0229  68  VAL A CA  
545  C  C   . VAL A 68  ? 0.1085 0.1198 0.1098 0.0151  -0.0097 0.0138  68  VAL A C   
546  O  O   . VAL A 68  ? 0.1411 0.1132 0.1058 0.0198  0.0029  0.0272  68  VAL A O   
547  C  CB  . VAL A 68  ? 0.1133 0.1168 0.1262 0.0080  -0.0110 0.0055  68  VAL A CB  
548  C  CG1 . VAL A 68  ? 0.1080 0.1735 0.1630 0.0270  -0.0408 -0.0078 68  VAL A CG1 
549  C  CG2 . VAL A 68  ? 0.1342 0.1264 0.1354 -0.0009 0.0128  -0.0013 68  VAL A CG2 
550  N  N   . GLU A 69  ? 0.1462 0.1164 0.1342 0.0265  -0.0121 0.0294  69  GLU A N   
551  C  CA  . GLU A 69  ? 0.1170 0.1091 0.1451 -0.0006 0.0102  0.0351  69  GLU A CA  
552  C  C   . GLU A 69  ? 0.1728 0.1083 0.1260 0.0378  -0.0119 0.0469  69  GLU A C   
553  O  O   . GLU A 69  ? 0.1954 0.1400 0.1479 0.0377  -0.0460 0.0244  69  GLU A O   
554  C  CB  . GLU A 69  ? 0.1602 0.1634 0.1638 0.0001  0.0534  0.0542  69  GLU A CB  
555  C  CG  . GLU A 69  ? 0.1272 0.2069 0.2889 -0.0234 0.0880  0.0609  69  GLU A CG  
556  C  CD  . GLU A 69  ? 0.1717 0.1674 0.2692 -0.0099 0.0862  0.0589  69  GLU A CD  
557  O  OE1 . GLU A 69  ? 0.2328 0.2469 0.2896 -0.0029 0.0822  0.0872  69  GLU A OE1 
558  O  OE2 . GLU A 69  ? 0.1433 0.2405 0.2226 -0.0182 0.0658  0.0262  69  GLU A OE2 
559  N  N   . PHE A 70  ? 0.1259 0.1164 0.1303 0.0049  0.0050  0.0239  70  PHE A N   
560  C  CA  . PHE A 70  ? 0.1108 0.1172 0.1681 0.0021  -0.0120 0.0257  70  PHE A CA  
561  C  C   . PHE A 70  ? 0.1318 0.1231 0.1703 0.0072  -0.0359 0.0109  70  PHE A C   
562  O  O   . PHE A 70  ? 0.1268 0.1318 0.2318 0.0054  -0.0285 0.0367  70  PHE A O   
563  C  CB  . PHE A 70  ? 0.1408 0.1098 0.1583 0.0019  -0.0057 0.0304  70  PHE A CB  
564  C  CG  . PHE A 70  ? 0.1247 0.1093 0.1444 0.0088  -0.0049 0.0205  70  PHE A CG  
565  C  CD1 . PHE A 70  ? 0.1508 0.1051 0.1753 0.0201  0.0097  0.0468  70  PHE A CD1 
566  C  CD2 . PHE A 70  ? 0.1196 0.1322 0.1397 -0.0016 0.0063  0.0296  70  PHE A CD2 
567  C  CE1 . PHE A 70  ? 0.1304 0.1347 0.1810 0.0044  0.0372  0.0568  70  PHE A CE1 
568  C  CE2 . PHE A 70  ? 0.1580 0.1200 0.1616 -0.0012 0.0003  0.0403  70  PHE A CE2 
569  C  CZ  . PHE A 70  ? 0.1519 0.1266 0.1566 0.0083  0.0376  0.0226  70  PHE A CZ  
570  N  N   . ASP A 71  ? 0.1551 0.1064 0.2540 0.0115  -0.0643 0.0339  71  ASP A N   
571  C  CA  . ASP A 71  ? 0.1738 0.0916 0.2724 -0.0015 -0.0578 0.0413  71  ASP A CA  
572  C  C   . ASP A 71  ? 0.1415 0.0987 0.3195 0.0076  -0.0011 0.0194  71  ASP A C   
573  O  O   . ASP A 71  ? 0.1670 0.1903 0.4776 -0.0337 0.0513  -0.0026 71  ASP A O   
574  C  CB  . ASP A 71  ? 0.2126 0.2141 0.3585 0.0110  -0.0853 0.0853  71  ASP A CB  
575  C  CG  . ASP A 71  ? 0.2536 0.2338 0.4421 0.0649  -0.1439 0.0197  71  ASP A CG  
576  O  OD1 . ASP A 71  ? 0.3003 0.1731 0.3686 0.0294  -0.0770 0.0529  71  ASP A OD1 
577  O  OD2 . ASP A 71  ? 0.2362 0.2051 0.4810 -0.0029 -0.1179 0.0746  71  ASP A OD2 
578  N  N   . ASP A 72  ? 0.1663 0.1252 0.2493 -0.0030 0.0041  0.0438  72  ASP A N   
579  C  CA  . ASP A 72  ? 0.2108 0.1813 0.2547 -0.0117 0.0156  0.0153  72  ASP A CA  
580  C  C   . ASP A 72  ? 0.3407 0.2080 0.3265 -0.0386 -0.0031 0.0134  72  ASP A C   
581  O  O   . ASP A 72  ? 0.3707 0.1541 0.3262 -0.0685 -0.0082 0.0215  72  ASP A O   
582  C  CB  . ASP A 72  ? 0.2284 0.1565 0.2572 -0.0062 0.0100  0.0285  72  ASP A CB  
583  C  CG  . ASP A 72  ? 0.2499 0.2544 0.1443 0.0033  0.0326  0.0241  72  ASP A CG  
584  O  OD1 . ASP A 72  ? 0.2378 0.3114 0.1602 -0.0446 -0.0148 0.0529  72  ASP A OD1 
585  O  OD2 . ASP A 72  ? 0.3053 0.3592 0.2004 -0.0587 -0.0205 0.0985  72  ASP A OD2 
586  N  N   . SER A 73  ? 0.2467 0.1209 0.3541 -0.0173 0.0436  0.0326  73  SER A N   
587  C  CA  . SER A 73  ? 0.2539 0.1239 0.3319 -0.0420 0.0258  0.0196  73  SER A CA  
588  C  C   . SER A 73  ? 0.3057 0.1501 0.4304 -0.0220 0.1004  0.0034  73  SER A C   
589  O  O   . SER A 73  ? 0.3283 0.1562 0.2904 -0.0104 0.0238  0.0152  73  SER A O   
590  C  CB  . SER A 73  ? 0.3118 0.2587 0.3412 -0.0062 0.0282  0.0626  73  SER A CB  
591  O  OG  . SER A 73  ? 0.3079 0.1695 0.3349 0.0472  0.0406  0.0446  73  SER A OG  
592  N  N   . GLN A 74  ? 0.3610 0.0944 0.4046 -0.0225 0.1211  0.0212  74  GLN A N   
593  C  CA  . GLN A 74  ? 0.3482 0.2093 0.4264 0.0097  0.1073  0.0469  74  GLN A CA  
594  C  C   . GLN A 74  ? 0.2910 0.2040 0.3352 -0.0592 0.0150  -0.0146 74  GLN A C   
595  O  O   . GLN A 74  ? 0.2504 0.1713 0.2737 -0.0342 -0.0269 0.0111  74  GLN A O   
596  C  CB  . GLN A 74  ? 0.3358 0.2737 0.6311 -0.0431 0.0226  0.0625  74  GLN A CB  
597  C  CG  . GLN A 74  ? 0.4600 0.3513 0.6939 -0.0927 -0.0570 0.0983  74  GLN A CG  
598  C  CD  . GLN A 74  ? 0.4888 0.4381 0.6728 -0.1183 -0.1401 0.0279  74  GLN A CD  
599  O  OE1 . GLN A 74  ? 0.5547 0.5589 0.6330 -0.0760 -0.2121 -0.0110 74  GLN A OE1 
600  N  NE2 . GLN A 74  ? 0.6065 0.3828 0.4934 -0.0283 -0.1258 0.1418  74  GLN A NE2 
601  N  N   A ASP A 75  ? 0.3740 0.4060 0.3876 -0.0190 0.0621  -0.1012 75  ASP A N   
602  N  N   B ASP A 75  ? 0.3240 0.2655 0.2848 -0.0494 0.0229  -0.0248 75  ASP A N   
603  C  CA  A ASP A 75  ? 0.3592 0.4261 0.3269 -0.0061 0.0044  -0.0889 75  ASP A CA  
604  C  CA  B ASP A 75  ? 0.2691 0.1544 0.3495 -0.0741 0.0493  -0.0210 75  ASP A CA  
605  C  C   A ASP A 75  ? 0.3933 0.4194 0.4087 0.0875  -0.1179 -0.1518 75  ASP A C   
606  C  C   B ASP A 75  ? 0.2044 0.2229 0.4338 -0.0268 -0.0105 -0.0882 75  ASP A C   
607  O  O   A ASP A 75  ? 0.4579 0.7395 0.3385 0.0604  0.0776  -0.2236 75  ASP A O   
608  O  O   B ASP A 75  ? 0.2205 0.2019 0.5370 0.0275  -0.0168 0.0297  75  ASP A O   
609  C  CB  A ASP A 75  ? 0.2586 0.3819 0.3301 -0.0078 -0.0102 -0.0803 75  ASP A CB  
610  C  CB  B ASP A 75  ? 0.2870 0.2015 0.2508 -0.0216 0.0385  0.0232  75  ASP A CB  
611  C  CG  A ASP A 75  ? 0.1965 0.3323 0.4532 -0.0783 -0.0290 0.0184  75  ASP A CG  
612  C  CG  B ASP A 75  ? 0.2039 0.2486 0.2597 0.0337  0.0504  0.0407  75  ASP A CG  
613  O  OD1 A ASP A 75  ? 0.1961 0.4257 0.3025 -0.0325 0.0062  0.1102  75  ASP A OD1 
614  O  OD1 B ASP A 75  ? 0.1724 0.2518 0.3360 -0.0016 0.0024  0.1042  75  ASP A OD1 
615  O  OD2 A ASP A 75  ? 0.3499 0.4963 0.5330 0.0350  0.1106  -0.1161 75  ASP A OD2 
616  O  OD2 B ASP A 75  ? 0.3534 0.3949 0.2777 0.1085  0.0354  -0.1024 75  ASP A OD2 
617  N  N   A LYS A 76  ? 0.2838 0.3862 0.2825 0.0903  -0.0558 -0.0562 76  LYS A N   
618  N  N   B LYS A 76  ? 0.3082 0.1372 0.2806 -0.0587 0.0598  0.0272  76  LYS A N   
619  C  CA  A LYS A 76  ? 0.3632 0.2922 0.3449 0.0030  -0.0535 0.0400  76  LYS A CA  
620  C  CA  B LYS A 76  ? 0.2979 0.2270 0.3111 -0.0651 -0.0147 0.0050  76  LYS A CA  
621  C  C   A LYS A 76  ? 0.2449 0.2882 0.2755 -0.0013 -0.0528 0.0261  76  LYS A C   
622  C  C   B LYS A 76  ? 0.4443 0.2606 0.3100 0.0291  -0.0601 0.0326  76  LYS A C   
623  O  O   A LYS A 76  ? 0.1990 0.4167 0.4551 -0.0372 -0.0230 0.1250  76  LYS A O   
624  O  O   B LYS A 76  ? 0.3550 0.2878 0.3958 0.0671  -0.0700 0.0145  76  LYS A O   
625  C  CB  A LYS A 76  ? 0.3258 0.3093 0.4094 0.0304  0.0464  0.0729  76  LYS A CB  
626  C  CB  B LYS A 76  ? 0.3033 0.1530 0.2753 -0.0665 -0.0638 0.0082  76  LYS A CB  
627  C  CG  A LYS A 76  ? 0.4709 0.3309 0.3592 0.0305  0.1037  0.0705  76  LYS A CG  
628  C  CG  B LYS A 76  ? 0.4036 0.3042 0.1555 -0.0545 -0.1303 0.0387  76  LYS A CG  
629  C  CD  A LYS A 76  ? 0.2548 0.2946 0.4737 0.0597  0.1282  0.0741  76  LYS A CD  
630  C  CD  B LYS A 76  ? 0.5122 0.3653 0.2026 -0.0553 -0.0372 0.0710  76  LYS A CD  
631  C  CE  A LYS A 76  ? 0.1735 0.2845 0.3960 0.0926  0.1406  0.0136  76  LYS A CE  
632  C  CE  B LYS A 76  ? 0.3553 0.4008 0.2684 0.0121  -0.1702 -0.0146 76  LYS A CE  
633  N  NZ  A LYS A 76  ? 0.3128 0.3510 0.2977 0.0660  0.0844  0.0602  76  LYS A NZ  
634  N  NZ  B LYS A 76  ? 0.4417 0.5392 0.3974 0.1205  -0.0268 0.0271  76  LYS A NZ  
635  N  N   . ALA A 77  ? 0.2115 0.3083 0.3276 -0.0279 -0.0783 0.0498  77  ALA A N   
636  C  CA  . ALA A 77  ? 0.1634 0.3259 0.1971 -0.0376 0.0263  0.0671  77  ALA A CA  
637  C  C   . ALA A 77  ? 0.0952 0.2489 0.2663 -0.0205 -0.0127 0.0277  77  ALA A C   
638  O  O   . ALA A 77  ? 0.0650 0.4539 0.3510 -0.0395 -0.0259 -0.0242 77  ALA A O   
639  C  CB  . ALA A 77  ? 0.2240 0.3398 0.2354 0.0350  0.0245  0.0664  77  ALA A CB  
640  N  N   A VAL A 78  ? 0.1279 0.1771 0.2337 0.0247  0.0035  -0.0107 78  VAL A N   
641  N  N   B VAL A 78  ? 0.1588 0.1390 0.2409 -0.0381 -0.0241 0.0597  78  VAL A N   
642  C  CA  A VAL A 78  ? 0.1533 0.2130 0.2397 0.0387  -0.0145 0.0227  78  VAL A CA  
643  C  CA  B VAL A 78  ? 0.0988 0.1573 0.2476 0.0032  0.0047  0.0517  78  VAL A CA  
644  C  C   A VAL A 78  ? 0.1315 0.1936 0.2789 -0.0337 0.0006  0.0125  78  VAL A C   
645  C  C   B VAL A 78  ? 0.1186 0.1390 0.2784 -0.0590 0.0114  0.0504  78  VAL A C   
646  O  O   A VAL A 78  ? 0.1645 0.1843 0.3279 -0.0627 -0.0373 0.0525  78  VAL A O   
647  O  O   B VAL A 78  ? 0.1014 0.1587 0.3051 -0.0563 0.0184  0.0544  78  VAL A O   
648  C  CB  A VAL A 78  ? 0.1864 0.2083 0.2280 0.0153  0.0223  0.0072  78  VAL A CB  
649  C  CB  B VAL A 78  ? 0.2051 0.1541 0.2576 0.0103  0.0153  0.0103  78  VAL A CB  
650  C  CG1 A VAL A 78  ? 0.1918 0.1774 0.3711 0.0431  -0.0261 0.0666  78  VAL A CG1 
651  C  CG1 B VAL A 78  ? 0.1802 0.1993 0.2744 -0.0078 0.0353  -0.0214 78  VAL A CG1 
652  C  CG2 A VAL A 78  ? 0.1821 0.2856 0.2133 0.0736  0.0331  0.0094  78  VAL A CG2 
653  C  CG2 B VAL A 78  ? 0.2496 0.1490 0.3291 -0.0217 -0.0132 0.0141  78  VAL A CG2 
654  N  N   . LEU A 79  ? 0.1225 0.1318 0.1861 0.0121  0.0348  0.0241  79  LEU A N   
655  C  CA  . LEU A 79  ? 0.1179 0.1487 0.1752 0.0042  0.0351  0.0182  79  LEU A CA  
656  C  C   . LEU A 79  ? 0.1480 0.1215 0.2032 -0.0239 0.0653  0.0142  79  LEU A C   
657  O  O   . LEU A 79  ? 0.1505 0.1414 0.2046 -0.0201 0.0661  -0.0041 79  LEU A O   
658  C  CB  . LEU A 79  ? 0.0841 0.1570 0.2414 -0.0121 0.0311  0.0422  79  LEU A CB  
659  C  CG  . LEU A 79  ? 0.1164 0.1652 0.2320 0.0157  0.0340  0.0340  79  LEU A CG  
660  C  CD1 . LEU A 79  ? 0.1494 0.1401 0.3161 0.0082  0.0729  0.0496  79  LEU A CD1 
661  C  CD2 . LEU A 79  ? 0.1383 0.1850 0.2172 0.0552  0.0344  0.0204  79  LEU A CD2 
662  N  N   . LYS A 80  ? 0.1444 0.1601 0.1979 -0.0116 0.0668  0.0265  80  LYS A N   
663  C  CA  . LYS A 80  ? 0.2040 0.1562 0.2072 0.0150  0.0837  0.0071  80  LYS A CA  
664  C  C   . LYS A 80  ? 0.0994 0.1807 0.2134 -0.0035 0.0491  0.0104  80  LYS A C   
665  O  O   . LYS A 80  ? 0.1032 0.1828 0.2410 -0.0317 0.0420  0.0285  80  LYS A O   
666  C  CB  . LYS A 80  ? 0.2421 0.2029 0.2514 0.0447  0.0474  0.0421  80  LYS A CB  
667  C  CG  . LYS A 80  ? 0.2385 0.2089 0.2631 0.0048  0.0517  0.0218  80  LYS A CG  
668  C  CD  . LYS A 80  ? 0.1950 0.3240 0.4552 0.1120  0.0345  0.0131  80  LYS A CD  
669  C  CE  . LYS A 80  ? 0.2331 0.4230 0.5818 0.0337  -0.0336 0.0917  80  LYS A CE  
670  N  N   . GLY A 81  ? 0.1828 0.1577 0.2500 0.0287  0.1053  0.0093  81  GLY A N   
671  C  CA  . GLY A 81  ? 0.1376 0.1990 0.2842 0.0276  0.0890  0.0615  81  GLY A CA  
672  C  C   . GLY A 81  ? 0.1576 0.1746 0.2572 0.0357  0.1178  0.0417  81  GLY A C   
673  O  O   . GLY A 81  ? 0.1547 0.1710 0.2605 0.0009  0.0961  -0.0091 81  GLY A O   
674  N  N   . GLY A 82  ? 0.1272 0.2284 0.3337 0.0325  0.1128  0.0978  82  GLY A N   
675  C  CA  . GLY A 82  ? 0.1458 0.2098 0.3319 0.0120  0.0626  0.0842  82  GLY A CA  
676  C  C   . GLY A 82  ? 0.1911 0.2158 0.2652 0.0403  0.1029  0.0167  82  GLY A C   
677  O  O   . GLY A 82  ? 0.2338 0.2308 0.2690 0.0793  0.0738  0.0074  82  GLY A O   
678  N  N   . PRO A 83  ? 0.1576 0.1569 0.2961 0.0410  0.0873  0.0139  83  PRO A N   
679  C  CA  . PRO A 83  ? 0.1925 0.1695 0.3116 0.0211  0.1078  0.0052  83  PRO A CA  
680  C  C   . PRO A 83  ? 0.1534 0.1552 0.2231 0.0344  0.0485  -0.0118 83  PRO A C   
681  O  O   . PRO A 83  ? 0.2196 0.2471 0.2295 -0.0074 0.0247  0.0103  83  PRO A O   
682  C  CB  . PRO A 83  ? 0.1756 0.1882 0.2344 0.0446  0.0651  -0.0027 83  PRO A CB  
683  C  CG  . PRO A 83  ? 0.1458 0.1648 0.2676 0.0290  0.0377  -0.0050 83  PRO A CG  
684  C  CD  . PRO A 83  ? 0.1547 0.1745 0.2812 0.0201  0.0775  0.0159  83  PRO A CD  
685  N  N   . LEU A 84  ? 0.1720 0.1516 0.2044 0.0323  0.0743  0.0227  84  LEU A N   
686  C  CA  . LEU A 84  ? 0.1839 0.1483 0.2238 0.0215  0.0901  -0.0008 84  LEU A CA  
687  C  C   . LEU A 84  ? 0.1487 0.1792 0.2044 0.0274  0.0577  -0.0212 84  LEU A C   
688  O  O   . LEU A 84  ? 0.1856 0.1911 0.2428 0.0551  0.1018  -0.0153 84  LEU A O   
689  C  CB  . LEU A 84  ? 0.1487 0.1134 0.2345 0.0177  0.0758  -0.0085 84  LEU A CB  
690  C  CG  . LEU A 84  ? 0.1300 0.1275 0.2080 0.0225  0.0475  -0.0159 84  LEU A CG  
691  C  CD1 . LEU A 84  ? 0.1544 0.1534 0.2180 0.0262  0.0514  0.0095  84  LEU A CD1 
692  C  CD2 . LEU A 84  ? 0.1245 0.1329 0.2223 0.0178  0.0666  -0.0290 84  LEU A CD2 
693  N  N   . ASP A 85  ? 0.1940 0.1624 0.2684 0.0076  0.0995  -0.0337 85  ASP A N   
694  C  CA  . ASP A 85  ? 0.2674 0.1828 0.1619 0.0199  0.0507  -0.0494 85  ASP A CA  
695  C  C   . ASP A 85  ? 0.2514 0.1760 0.1910 0.0301  0.0734  -0.0089 85  ASP A C   
696  O  O   . ASP A 85  ? 0.2361 0.2453 0.2295 0.0219  0.0598  -0.0389 85  ASP A O   
697  C  CB  . ASP A 85  ? 0.2356 0.2324 0.2162 -0.0506 0.0455  -0.0282 85  ASP A CB  
698  C  CG  . ASP A 85  ? 0.2720 0.2374 0.2667 -0.0120 0.0111  0.0256  85  ASP A CG  
699  O  OD1 . ASP A 85  ? 0.3427 0.5894 0.2504 -0.0509 0.0804  0.1061  85  ASP A OD1 
700  O  OD2 . ASP A 85  ? 0.2907 0.3212 0.2690 -0.0582 -0.0116 0.0156  85  ASP A OD2 
701  N  N   . GLY A 86  ? 0.2755 0.2367 0.2666 0.0441  0.0955  0.0414  86  GLY A N   
702  C  CA  . GLY A 86  ? 0.2777 0.2263 0.2083 0.0379  0.0305  0.0073  86  GLY A CA  
703  C  C   . GLY A 86  ? 0.2771 0.1824 0.2424 0.0274  0.0611  0.0012  86  GLY A C   
704  O  O   . GLY A 86  ? 0.2953 0.2916 0.3169 -0.0760 -0.0037 0.0774  86  GLY A O   
705  N  N   A THR A 87  ? 0.2902 0.1692 0.2569 0.0312  0.0883  -0.0061 87  THR A N   
706  N  N   B THR A 87  ? 0.2295 0.1533 0.2384 0.0251  0.0674  -0.0033 87  THR A N   
707  C  CA  A THR A 87  ? 0.2878 0.2281 0.2934 -0.0004 0.0788  -0.0326 87  THR A CA  
708  C  CA  B THR A 87  ? 0.1695 0.1753 0.2015 0.0314  0.0841  0.0098  87  THR A CA  
709  C  C   A THR A 87  ? 0.2019 0.0918 0.3028 -0.0285 0.0558  0.0164  87  THR A C   
710  C  C   B THR A 87  ? 0.1433 0.1097 0.1943 0.0134  0.0679  0.0158  87  THR A C   
711  O  O   A THR A 87  ? 0.1670 0.0961 0.3564 -0.0060 0.1037  -0.0025 87  THR A O   
712  O  O   B THR A 87  ? 0.1451 0.1282 0.2008 0.0052  0.0773  0.0005  87  THR A O   
713  C  CB  A THR A 87  ? 0.3582 0.3729 0.3617 0.0348  0.0348  0.0131  87  THR A CB  
714  C  CB  B THR A 87  ? 0.1681 0.1814 0.2101 0.0290  0.0574  -0.0184 87  THR A CB  
715  O  OG1 A THR A 87  ? 0.1058 0.5523 0.7133 0.1751  -0.0518 -0.1301 87  THR A OG1 
716  O  OG1 B THR A 87  ? 0.1433 0.1900 0.2249 0.0326  0.0389  0.0130  87  THR A OG1 
717  C  CG2 A THR A 87  ? 0.1493 0.3809 0.3621 0.0696  0.1171  -0.0493 87  THR A CG2 
718  C  CG2 B THR A 87  ? 0.1232 0.1684 0.3783 0.1005  0.0297  -0.1015 87  THR A CG2 
719  N  N   . TYR A 88  ? 0.1073 0.1057 0.2134 0.0160  0.0493  0.0033  88  TYR A N   
720  C  CA  . TYR A 88  ? 0.1187 0.1085 0.1838 0.0239  0.0432  -0.0061 88  TYR A CA  
721  C  C   . TYR A 88  ? 0.1042 0.1128 0.1904 0.0006  0.0229  0.0186  88  TYR A C   
722  O  O   . TYR A 88  ? 0.1383 0.2019 0.2306 -0.0625 0.0040  0.0501  88  TYR A O   
723  C  CB  . TYR A 88  ? 0.1259 0.0988 0.1681 0.0106  0.0511  -0.0051 88  TYR A CB  
724  C  CG  . TYR A 88  ? 0.1304 0.0900 0.1440 -0.0023 0.0495  -0.0027 88  TYR A CG  
725  C  CD1 . TYR A 88  ? 0.1236 0.1208 0.1803 0.0064  0.0684  -0.0100 88  TYR A CD1 
726  C  CD2 . TYR A 88  ? 0.1307 0.0812 0.1609 0.0021  0.0455  0.0051  88  TYR A CD2 
727  C  CE1 . TYR A 88  ? 0.1361 0.1433 0.1831 -0.0177 0.0570  0.0010  88  TYR A CE1 
728  C  CE2 . TYR A 88  ? 0.1289 0.0900 0.1465 0.0085  0.0434  0.0010  88  TYR A CE2 
729  C  CZ  . TYR A 88  ? 0.1322 0.0952 0.1518 -0.0127 0.0471  -0.0092 88  TYR A CZ  
730  O  OH  . TYR A 88  ? 0.1480 0.1307 0.1397 -0.0006 0.0540  -0.0190 88  TYR A OH  
731  N  N   . ARG A 89  ? 0.1071 0.0916 0.1810 0.0140  0.0326  -0.0024 89  ARG A N   
732  C  CA  . ARG A 89  ? 0.1168 0.1107 0.1505 0.0132  0.0292  0.0210  89  ARG A CA  
733  C  C   . ARG A 89  ? 0.1022 0.0963 0.1509 -0.0004 0.0129  0.0227  89  ARG A C   
734  O  O   . ARG A 89  ? 0.0970 0.1023 0.1368 0.0092  0.0165  0.0129  89  ARG A O   
735  C  CB  . ARG A 89  ? 0.1835 0.0932 0.1957 -0.0143 -0.0144 0.0271  89  ARG A CB  
736  C  CG  . ARG A 89  ? 0.2946 0.1371 0.1749 0.0008  -0.0097 0.0413  89  ARG A CG  
737  C  CD  . ARG A 89  ? 0.3134 0.1379 0.2331 0.0151  -0.0147 0.0582  89  ARG A CD  
738  N  NE  . ARG A 89  ? 0.3273 0.1548 0.2415 0.0171  -0.0053 0.0536  89  ARG A NE  
739  C  CZ  . ARG A 89  ? 0.3115 0.1606 0.1993 0.0143  -0.0089 0.0576  89  ARG A CZ  
740  N  NH1 . ARG A 89  ? 0.3096 0.1706 0.3031 0.0085  0.0387  0.0899  89  ARG A NH1 
741  N  NH2 . ARG A 89  ? 0.2874 0.2073 0.2441 0.0039  -0.0279 0.0057  89  ARG A NH2 
742  N  N   . LEU A 90  ? 0.1208 0.1005 0.1591 0.0054  0.0070  0.0100  90  LEU A N   
743  C  CA  . LEU A 90  ? 0.1318 0.1055 0.1268 -0.0162 0.0010  0.0064  90  LEU A CA  
744  C  C   . LEU A 90  ? 0.1315 0.0979 0.1479 -0.0003 -0.0079 0.0321  90  LEU A C   
745  O  O   . LEU A 90  ? 0.1293 0.1321 0.1735 0.0117  -0.0084 0.0445  90  LEU A O   
746  C  CB  . LEU A 90  ? 0.1383 0.1102 0.1544 -0.0088 -0.0392 0.0037  90  LEU A CB  
747  C  CG  . LEU A 90  ? 0.1609 0.1128 0.1620 -0.0355 -0.0130 0.0114  90  LEU A CG  
748  C  CD1 . LEU A 90  ? 0.1835 0.1030 0.1591 -0.0343 0.0075  0.0302  90  LEU A CD1 
749  C  CD2 . LEU A 90  ? 0.1932 0.1756 0.1756 -0.0859 -0.0271 0.0142  90  LEU A CD2 
750  N  N   . LYS A 91  ? 0.1178 0.1029 0.1304 0.0038  0.0127  0.0205  91  LYS A N   
751  C  CA  . LYS A 91  ? 0.1430 0.0888 0.1325 0.0086  0.0131  0.0061  91  LYS A CA  
752  C  C   . LYS A 91  ? 0.1155 0.0805 0.1164 0.0114  -0.0049 0.0189  91  LYS A C   
753  O  O   . LYS A 91  ? 0.1225 0.1097 0.1062 -0.0092 -0.0021 0.0188  91  LYS A O   
754  C  CB  . LYS A 91  ? 0.1773 0.1573 0.1390 -0.0630 0.0299  -0.0466 91  LYS A CB  
755  C  CG  . LYS A 91  ? 0.2100 0.2927 0.1965 -0.0859 0.0593  -0.0519 91  LYS A CG  
756  C  CD  . LYS A 91  ? 0.3915 0.3915 0.2514 -0.2007 0.0257  -0.0496 91  LYS A CD  
757  C  CE  . LYS A 91  ? 0.4670 0.3328 0.3141 -0.2024 0.0960  0.0133  91  LYS A CE  
758  N  NZ  . LYS A 91  ? 0.3441 0.3732 0.3746 -0.1542 0.1340  -0.0995 91  LYS A NZ  
759  N  N   . GLN A 92  ? 0.1307 0.0744 0.1195 0.0114  0.0117  0.0177  92  GLN A N   
760  C  CA  . GLN A 92  ? 0.1189 0.0908 0.1117 0.0013  0.0293  0.0278  92  GLN A CA  
761  C  C   . GLN A 92  ? 0.0959 0.0830 0.1071 0.0078  0.0156  0.0234  92  GLN A C   
762  O  O   . GLN A 92  ? 0.1325 0.0981 0.0988 0.0055  0.0161  0.0155  92  GLN A O   
763  C  CB  . GLN A 92  ? 0.1347 0.1570 0.2044 -0.0178 0.0270  0.0851  92  GLN A CB  
764  C  CG  . GLN A 92  ? 0.1947 0.1731 0.2179 -0.0002 -0.0179 0.0452  92  GLN A CG  
765  C  CD  . GLN A 92  ? 0.1207 0.1925 0.3024 0.0099  0.0023  0.1324  92  GLN A CD  
766  O  OE1 . GLN A 92  ? 0.1577 0.1024 0.1526 0.0071  -0.0292 0.0256  92  GLN A OE1 
767  N  NE2 . GLN A 92  ? 0.1353 0.3646 0.2958 0.0228  0.0073  0.0760  92  GLN A NE2 
768  N  N   . PHE A 93  ? 0.1002 0.0749 0.1261 0.0002  -0.0074 0.0193  93  PHE A N   
769  C  CA  . PHE A 93  ? 0.0826 0.0719 0.1153 0.0042  0.0093  0.0130  93  PHE A CA  
770  C  C   . PHE A 93  ? 0.0747 0.0963 0.0803 -0.0042 -0.0013 0.0172  93  PHE A C   
771  O  O   . PHE A 93  ? 0.1008 0.1058 0.0836 0.0164  0.0026  0.0149  93  PHE A O   
772  C  CB  . PHE A 93  ? 0.0906 0.1017 0.0956 -0.0089 0.0131  0.0091  93  PHE A CB  
773  C  CG  . PHE A 93  ? 0.0732 0.0963 0.1094 0.0000  0.0015  0.0113  93  PHE A CG  
774  C  CD1 . PHE A 93  ? 0.1190 0.1048 0.1065 -0.0009 0.0067  -0.0010 93  PHE A CD1 
775  C  CD2 . PHE A 93  ? 0.0844 0.1358 0.0987 0.0116  -0.0029 0.0223  93  PHE A CD2 
776  C  CE1 . PHE A 93  ? 0.1185 0.1137 0.1243 0.0040  -0.0168 0.0086  93  PHE A CE1 
777  C  CE2 . PHE A 93  ? 0.1264 0.1120 0.1324 -0.0153 -0.0226 -0.0008 93  PHE A CE2 
778  C  CZ  . PHE A 93  ? 0.0970 0.1136 0.1358 -0.0006 0.0015  0.0176  93  PHE A CZ  
779  N  N   . HIS A 94  ? 0.0644 0.0839 0.1008 0.0060  0.0030  0.0100  94  HIS A N   
780  C  CA  . HIS A 94  ? 0.0706 0.0785 0.0911 0.0036  0.0025  0.0118  94  HIS A CA  
781  C  C   . HIS A 94  ? 0.0880 0.0856 0.0744 -0.0006 0.0000  0.0133  94  HIS A C   
782  O  O   . HIS A 94  ? 0.1022 0.0917 0.0712 -0.0093 0.0086  0.0177  94  HIS A O   
783  C  CB  . HIS A 94  ? 0.0803 0.1100 0.0753 -0.0140 0.0088  0.0195  94  HIS A CB  
784  C  CG  . HIS A 94  ? 0.0979 0.0970 0.0662 -0.0190 0.0073  0.0150  94  HIS A CG  
785  N  ND1 . HIS A 94  ? 0.0760 0.0888 0.0929 -0.0172 0.0013  0.0065  94  HIS A ND1 
786  C  CD2 . HIS A 94  ? 0.0832 0.1031 0.0794 -0.0071 0.0062  0.0070  94  HIS A CD2 
787  C  CE1 . HIS A 94  ? 0.0774 0.0856 0.0967 -0.0134 -0.0002 0.0168  94  HIS A CE1 
788  N  NE2 . HIS A 94  ? 0.0785 0.0902 0.0769 -0.0079 -0.0143 0.0135  94  HIS A NE2 
789  N  N   . PHE A 95  ? 0.0952 0.0814 0.0933 0.0018  -0.0100 -0.0053 95  PHE A N   
790  C  CA  . PHE A 95  ? 0.0793 0.0879 0.0970 -0.0003 0.0019  0.0044  95  PHE A CA  
791  C  C   . PHE A 95  ? 0.0819 0.0947 0.0803 -0.0053 0.0110  -0.0064 95  PHE A C   
792  O  O   . PHE A 95  ? 0.0954 0.0935 0.1092 -0.0051 0.0212  0.0013  95  PHE A O   
793  C  CB  . PHE A 95  ? 0.0864 0.0976 0.1230 0.0072  -0.0059 -0.0205 95  PHE A CB  
794  C  CG  . PHE A 95  ? 0.0838 0.0870 0.1024 0.0040  -0.0015 -0.0172 95  PHE A CG  
795  C  CD1 . PHE A 95  ? 0.1215 0.1103 0.1102 0.0141  -0.0211 -0.0149 95  PHE A CD1 
796  C  CD2 . PHE A 95  ? 0.0863 0.1023 0.1207 -0.0185 -0.0035 -0.0145 95  PHE A CD2 
797  C  CE1 . PHE A 95  ? 0.1231 0.1186 0.1121 0.0089  -0.0298 -0.0094 95  PHE A CE1 
798  C  CE2 . PHE A 95  ? 0.1002 0.1128 0.1282 -0.0050 -0.0232 -0.0339 95  PHE A CE2 
799  C  CZ  . PHE A 95  ? 0.1231 0.1177 0.1469 0.0078  -0.0109 -0.0324 95  PHE A CZ  
800  N  N   . HIS A 96  ? 0.0828 0.0891 0.0933 0.0092  0.0069  0.0063  96  HIS A N   
801  C  CA  . HIS A 96  ? 0.0690 0.0880 0.0988 0.0078  -0.0006 -0.0188 96  HIS A CA  
802  C  C   . HIS A 96  ? 0.0714 0.0917 0.1083 -0.0042 0.0164  -0.0080 96  HIS A C   
803  O  O   . HIS A 96  ? 0.0758 0.1058 0.1150 -0.0071 0.0218  -0.0098 96  HIS A O   
804  C  CB  . HIS A 96  ? 0.0945 0.0823 0.0891 0.0039  -0.0019 -0.0140 96  HIS A CB  
805  C  CG  . HIS A 96  ? 0.0830 0.0778 0.0965 0.0073  -0.0018 -0.0066 96  HIS A CG  
806  N  ND1 . HIS A 96  ? 0.0805 0.0905 0.1216 -0.0036 -0.0051 -0.0177 96  HIS A ND1 
807  C  CD2 . HIS A 96  ? 0.0956 0.0708 0.0775 0.0097  0.0041  -0.0002 96  HIS A CD2 
808  C  CE1 . HIS A 96  ? 0.0747 0.0914 0.1040 0.0085  0.0055  -0.0044 96  HIS A CE1 
809  N  NE2 . HIS A 96  ? 0.0759 0.0733 0.1076 0.0089  -0.0010 0.0005  96  HIS A NE2 
810  N  N   . TRP A 97  ? 0.0870 0.0820 0.0944 0.0039  0.0097  -0.0074 97  TRP A N   
811  C  CA  . TRP A 97  ? 0.0848 0.0899 0.0954 0.0127  0.0093  -0.0062 97  TRP A CA  
812  C  C   . TRP A 97  ? 0.0807 0.0945 0.0854 0.0106  0.0183  -0.0111 97  TRP A C   
813  O  O   . TRP A 97  ? 0.0938 0.0974 0.0932 -0.0031 0.0329  -0.0009 97  TRP A O   
814  C  CB  . TRP A 97  ? 0.1160 0.1067 0.0724 -0.0174 0.0170  -0.0103 97  TRP A CB  
815  C  CG  . TRP A 97  ? 0.0880 0.0891 0.0803 0.0010  0.0119  -0.0130 97  TRP A CG  
816  C  CD1 . TRP A 97  ? 0.1164 0.1117 0.0750 0.0076  0.0216  -0.0106 97  TRP A CD1 
817  C  CD2 . TRP A 97  ? 0.0974 0.1044 0.0812 0.0044  0.0114  -0.0050 97  TRP A CD2 
818  N  NE1 . TRP A 97  ? 0.1440 0.1023 0.0818 0.0013  0.0166  0.0019  97  TRP A NE1 
819  C  CE2 . TRP A 97  ? 0.1109 0.1084 0.0941 -0.0074 0.0301  -0.0055 97  TRP A CE2 
820  C  CE3 . TRP A 97  ? 0.1066 0.1074 0.0765 0.0079  0.0151  0.0002  97  TRP A CE3 
821  C  CZ2 . TRP A 97  ? 0.1329 0.1112 0.0944 -0.0114 0.0035  0.0052  97  TRP A CZ2 
822  C  CZ3 . TRP A 97  ? 0.1133 0.1421 0.0794 0.0017  0.0022  0.0214  97  TRP A CZ3 
823  C  CH2 . TRP A 97  ? 0.1354 0.1218 0.0778 0.0011  0.0133  0.0105  97  TRP A CH2 
824  N  N   . GLY A 98  ? 0.1023 0.0864 0.0839 0.0008  0.0249  -0.0075 98  GLY A N   
825  C  CA  . GLY A 98  ? 0.1275 0.0841 0.0945 0.0143  0.0240  -0.0147 98  GLY A CA  
826  C  C   . GLY A 98  ? 0.1461 0.0884 0.0857 -0.0038 0.0161  -0.0054 98  GLY A C   
827  O  O   . GLY A 98  ? 0.1580 0.1084 0.0926 0.0000  0.0117  -0.0087 98  GLY A O   
828  N  N   . SER A 99  ? 0.1505 0.0902 0.1085 0.0117  0.0320  -0.0067 99  SER A N   
829  C  CA  . SER A 99  ? 0.1602 0.1171 0.1092 0.0086  0.0498  -0.0129 99  SER A CA  
830  C  C   . SER A 99  ? 0.1570 0.1111 0.0977 0.0082  0.0160  -0.0124 99  SER A C   
831  O  O   . SER A 99  ? 0.2566 0.1401 0.1357 0.0088  0.0204  -0.0281 99  SER A O   
832  C  CB  . SER A 99  ? 0.1638 0.1242 0.1516 0.0330  0.0441  0.0049  99  SER A CB  
833  O  OG  . SER A 99  ? 0.1509 0.1180 0.1929 0.0390  0.0335  0.0111  99  SER A OG  
834  N  N   . LEU A 100 ? 0.1422 0.1058 0.1254 -0.0022 0.0317  -0.0023 100 LEU A N   
835  C  CA  . LEU A 100 ? 0.1527 0.0821 0.1925 0.0128  0.0486  -0.0116 100 LEU A CA  
836  C  C   . LEU A 100 ? 0.1559 0.0895 0.1451 0.0165  0.0386  -0.0103 100 LEU A C   
837  O  O   . LEU A 100 ? 0.1806 0.0920 0.1271 0.0009  0.0301  -0.0070 100 LEU A O   
838  C  CB  . LEU A 100 ? 0.2344 0.1116 0.2119 0.0130  0.0308  0.0186  100 LEU A CB  
839  C  CG  . LEU A 100 ? 0.2724 0.1595 0.2105 0.0530  0.0436  -0.0183 100 LEU A CG  
840  C  CD1 . LEU A 100 ? 0.2389 0.2449 0.3243 0.1251  0.0513  0.0192  100 LEU A CD1 
841  C  CD2 . LEU A 100 ? 0.3412 0.2144 0.2450 0.0978  0.0982  -0.1102 100 LEU A CD2 
842  N  N   . ASP A 101 ? 0.1498 0.0990 0.1792 0.0029  0.0269  -0.0036 101 ASP A N   
843  C  CA  . ASP A 101 ? 0.1638 0.1216 0.1577 -0.0064 0.0390  -0.0103 101 ASP A CA  
844  C  C   . ASP A 101 ? 0.1817 0.1112 0.1656 -0.0161 0.0294  -0.0171 101 ASP A C   
845  O  O   . ASP A 101 ? 0.2979 0.1148 0.1630 0.0156  0.0935  0.0039  101 ASP A O   
846  C  CB  . ASP A 101 ? 0.1789 0.1234 0.2136 -0.0231 0.0211  -0.0113 101 ASP A CB  
847  C  CG  . ASP A 101 ? 0.1670 0.1358 0.2397 -0.0270 0.0425  -0.0212 101 ASP A CG  
848  O  OD1 . ASP A 101 ? 0.2132 0.1473 0.1698 -0.0479 0.0231  -0.0242 101 ASP A OD1 
849  O  OD2 . ASP A 101 ? 0.2416 0.1782 0.2734 -0.0822 0.0239  -0.0274 101 ASP A OD2 
850  N  N   . GLY A 102 ? 0.2101 0.1135 0.1609 -0.0340 0.0190  -0.0118 102 GLY A N   
851  C  CA  . GLY A 102 ? 0.3019 0.1080 0.1537 -0.0472 0.0103  0.0105  102 GLY A CA  
852  C  C   . GLY A 102 ? 0.2209 0.1304 0.1386 -0.0419 0.0331  0.0193  102 GLY A C   
853  O  O   . GLY A 102 ? 0.2415 0.1329 0.1444 -0.0325 0.0332  0.0219  102 GLY A O   
854  N  N   . GLN A 103 ? 0.1993 0.1064 0.1224 -0.0269 0.0542  -0.0022 103 GLN A N   
855  C  CA  . GLN A 103 ? 0.1649 0.1049 0.1107 0.0020  0.0251  0.0017  103 GLN A CA  
856  C  C   . GLN A 103 ? 0.1209 0.0911 0.1196 -0.0088 0.0340  -0.0083 103 GLN A C   
857  O  O   . GLN A 103 ? 0.1432 0.0968 0.1236 -0.0082 0.0219  -0.0119 103 GLN A O   
858  C  CB  . GLN A 103 ? 0.1867 0.1014 0.1203 0.0329  0.0442  0.0154  103 GLN A CB  
859  C  CG  . GLN A 103 ? 0.1720 0.1263 0.1182 0.0289  0.0551  0.0188  103 GLN A CG  
860  C  CD  . GLN A 103 ? 0.2194 0.1483 0.1516 0.0810  0.0746  0.0530  103 GLN A CD  
861  O  OE1 . GLN A 103 ? 0.3211 0.2169 0.2870 0.1254  0.1619  0.1447  103 GLN A OE1 
862  N  NE2 . GLN A 103 ? 0.1979 0.1544 0.1548 0.0528  0.0792  0.0241  103 GLN A NE2 
863  N  N   . GLY A 104 ? 0.1069 0.0888 0.1032 0.0041  0.0402  -0.0093 104 GLY A N   
864  C  CA  . GLY A 104 ? 0.1177 0.0958 0.1093 0.0042  0.0147  -0.0036 104 GLY A CA  
865  C  C   . GLY A 104 ? 0.0923 0.0951 0.1017 0.0011  0.0131  0.0006  104 GLY A C   
866  O  O   . GLY A 104 ? 0.0890 0.1023 0.1212 -0.0011 0.0105  0.0010  104 GLY A O   
867  N  N   . SER A 105 ? 0.0981 0.0936 0.0864 -0.0011 0.0201  -0.0131 105 SER A N   
868  C  CA  . SER A 105 ? 0.0791 0.0845 0.0943 -0.0100 0.0203  -0.0115 105 SER A CA  
869  C  C   . SER A 105 ? 0.0873 0.0694 0.0848 -0.0009 0.0062  0.0055  105 SER A C   
870  O  O   . SER A 105 ? 0.1031 0.0767 0.1137 0.0148  0.0058  -0.0085 105 SER A O   
871  C  CB  . SER A 105 ? 0.0810 0.0990 0.0961 -0.0041 0.0207  0.0147  105 SER A CB  
872  O  OG  . SER A 105 ? 0.0997 0.0712 0.1083 -0.0124 0.0219  0.0001  105 SER A OG  
873  N  N   . GLU A 106 ? 0.0920 0.0687 0.0846 -0.0048 0.0204  -0.0036 106 GLU A N   
874  C  CA  . GLU A 106 ? 0.0839 0.0762 0.0908 -0.0238 0.0201  0.0018  106 GLU A CA  
875  C  C   . GLU A 106 ? 0.0713 0.0674 0.0879 0.0006  0.0064  -0.0015 106 GLU A C   
876  O  O   . GLU A 106 ? 0.0729 0.0907 0.1024 0.0095  0.0038  0.0005  106 GLU A O   
877  C  CB  . GLU A 106 ? 0.1152 0.0830 0.0705 -0.0061 0.0137  -0.0009 106 GLU A CB  
878  C  CG  . GLU A 106 ? 0.1208 0.0750 0.0864 -0.0085 0.0220  0.0043  106 GLU A CG  
879  C  CD  . GLU A 106 ? 0.0742 0.0879 0.0880 0.0032  0.0146  0.0107  106 GLU A CD  
880  O  OE1 . GLU A 106 ? 0.0780 0.0859 0.1078 -0.0042 0.0048  -0.0049 106 GLU A OE1 
881  O  OE2 . GLU A 106 ? 0.0794 0.1103 0.1223 0.0054  0.0243  0.0055  106 GLU A OE2 
882  N  N   . HIS A 107 ? 0.0747 0.0811 0.0818 -0.0041 0.0132  0.0079  107 HIS A N   
883  C  CA  . HIS A 107 ? 0.0841 0.0830 0.0785 0.0066  0.0193  0.0113  107 HIS A CA  
884  C  C   . HIS A 107 ? 0.0632 0.0814 0.0979 0.0042  0.0066  0.0094  107 HIS A C   
885  O  O   . HIS A 107 ? 0.0818 0.0920 0.1032 -0.0096 -0.0040 0.0038  107 HIS A O   
886  C  CB  . HIS A 107 ? 0.0732 0.0789 0.0996 0.0065  0.0115  0.0060  107 HIS A CB  
887  C  CG  . HIS A 107 ? 0.0566 0.0762 0.0959 0.0051  0.0170  0.0032  107 HIS A CG  
888  N  ND1 . HIS A 107 ? 0.0800 0.0778 0.0863 0.0086  0.0172  0.0017  107 HIS A ND1 
889  C  CD2 . HIS A 107 ? 0.0452 0.0899 0.1022 0.0024  0.0111  -0.0063 107 HIS A CD2 
890  C  CE1 . HIS A 107 ? 0.0988 0.0732 0.0796 0.0165  0.0117  -0.0116 107 HIS A CE1 
891  N  NE2 . HIS A 107 ? 0.0802 0.0853 0.0868 -0.0020 0.0183  -0.0130 107 HIS A NE2 
892  N  N   . THR A 108 ? 0.1074 0.0864 0.0918 -0.0064 0.0194  0.0201  108 THR A N   
893  C  CA  . THR A 108 ? 0.1097 0.0759 0.1150 0.0067  0.0273  0.0220  108 THR A CA  
894  C  C   . THR A 108 ? 0.0787 0.0947 0.1102 0.0022  0.0006  0.0072  108 THR A C   
895  O  O   . THR A 108 ? 0.1054 0.0972 0.1057 0.0079  0.0176  0.0137  108 THR A O   
896  C  CB  . THR A 108 ? 0.1146 0.0952 0.0976 0.0172  0.0033  0.0094  108 THR A CB  
897  O  OG1 . THR A 108 ? 0.1161 0.1029 0.1121 0.0134  0.0041  0.0027  108 THR A OG1 
898  C  CG2 . THR A 108 ? 0.1282 0.1189 0.1091 0.0131  0.0154  0.0091  108 THR A CG2 
899  N  N   . VAL A 109 ? 0.1060 0.0884 0.1286 -0.0041 0.0212  0.0395  109 VAL A N   
900  C  CA  . VAL A 109 ? 0.1100 0.1191 0.1404 -0.0061 0.0249  0.0447  109 VAL A CA  
901  C  C   . VAL A 109 ? 0.1376 0.0961 0.1494 -0.0233 0.0351  0.0397  109 VAL A C   
902  O  O   . VAL A 109 ? 0.1351 0.1101 0.1605 -0.0231 0.0272  0.0248  109 VAL A O   
903  C  CB  . VAL A 109 ? 0.1015 0.1186 0.1501 0.0027  0.0305  0.0205  109 VAL A CB  
904  C  CG1 . VAL A 109 ? 0.1040 0.1792 0.1746 0.0161  0.0351  0.0337  109 VAL A CG1 
905  C  CG2 . VAL A 109 ? 0.1368 0.1346 0.1756 0.0163  0.0057  0.0480  109 VAL A CG2 
906  N  N   . ASP A 110 ? 0.1401 0.1137 0.1258 0.0035  0.0328  0.0375  110 ASP A N   
907  C  CA  . ASP A 110 ? 0.1738 0.1099 0.1634 0.0178  0.0552  0.0563  110 ASP A CA  
908  C  C   . ASP A 110 ? 0.1961 0.1040 0.1120 0.0088  0.0291  0.0414  110 ASP A C   
909  O  O   . ASP A 110 ? 0.1825 0.1137 0.1584 0.0059  0.0267  0.0506  110 ASP A O   
910  C  CB  . ASP A 110 ? 0.2434 0.1461 0.1903 -0.0068 0.0842  0.0641  110 ASP A CB  
911  C  CG  . ASP A 110 ? 0.2221 0.1623 0.1652 0.0147  0.0576  0.0656  110 ASP A CG  
912  O  OD1 . ASP A 110 ? 0.2349 0.1821 0.2029 0.0323  0.1043  0.0666  110 ASP A OD1 
913  O  OD2 . ASP A 110 ? 0.2274 0.2709 0.2270 0.0314  0.0930  0.0741  110 ASP A OD2 
914  N  N   . LYS A 111 ? 0.1351 0.1067 0.1375 0.0201  0.0239  0.0416  111 LYS A N   
915  C  CA  . LYS A 111 ? 0.1559 0.1190 0.1195 0.0372  0.0113  0.0194  111 LYS A CA  
916  C  C   . LYS A 111 ? 0.1634 0.1013 0.1364 0.0152  0.0125  0.0163  111 LYS A C   
917  O  O   . LYS A 111 ? 0.1627 0.1197 0.1451 0.0089  0.0183  -0.0072 111 LYS A O   
918  C  CB  . LYS A 111 ? 0.1863 0.1749 0.1462 0.0710  -0.0096 0.0299  111 LYS A CB  
919  C  CG  . LYS A 111 ? 0.2302 0.1983 0.1864 0.0688  -0.0451 0.0318  111 LYS A CG  
920  C  CD  . LYS A 111 ? 0.2094 0.3434 0.1986 0.0006  -0.0048 -0.0391 111 LYS A CD  
921  C  CE  . LYS A 111 ? 0.3344 0.4518 0.1907 0.0203  -0.0675 -0.0128 111 LYS A CE  
922  N  NZ  . LYS A 111 ? 0.3895 0.4304 0.4194 0.0657  -0.2203 -0.0190 111 LYS A NZ  
923  N  N   . LYS A 112 ? 0.1343 0.1128 0.1400 -0.0016 0.0085  0.0303  112 LYS A N   
924  C  CA  . LYS A 112 ? 0.1483 0.1325 0.1674 -0.0100 0.0089  0.0265  112 LYS A CA  
925  C  C   . LYS A 112 ? 0.1529 0.0945 0.1447 -0.0050 0.0080  -0.0018 112 LYS A C   
926  O  O   . LYS A 112 ? 0.1440 0.0916 0.1240 -0.0022 0.0226  -0.0003 112 LYS A O   
927  C  CB  . LYS A 112 ? 0.1451 0.1440 0.1863 -0.0384 0.0060  0.0173  112 LYS A CB  
928  C  CG  . LYS A 112 ? 0.1584 0.1785 0.2055 -0.0272 -0.0071 0.0035  112 LYS A CG  
929  C  CD  . LYS A 112 ? 0.1649 0.2345 0.2328 -0.0236 -0.0160 0.0457  112 LYS A CD  
930  C  CE  . LYS A 112 ? 0.1936 0.2478 0.2777 -0.0244 -0.0440 0.0136  112 LYS A CE  
931  N  NZ  . LYS A 112 ? 0.2594 0.2169 0.2837 -0.0552 -0.0675 0.0328  112 LYS A NZ  
932  N  N   A LYS A 113 ? 0.1415 0.0956 0.1311 0.0086  0.0022  0.0127  113 LYS A N   
933  N  N   B LYS A 113 ? 0.1415 0.0941 0.1324 0.0089  0.0030  0.0120  113 LYS A N   
934  C  CA  A LYS A 113 ? 0.1368 0.1169 0.1200 0.0046  0.0022  0.0081  113 LYS A CA  
935  C  CA  B LYS A 113 ? 0.1371 0.1186 0.1176 0.0046  0.0036  0.0058  113 LYS A CA  
936  C  C   A LYS A 113 ? 0.1468 0.0823 0.1262 -0.0089 0.0023  0.0018  113 LYS A C   
937  C  C   B LYS A 113 ? 0.1469 0.0823 0.1254 -0.0084 0.0027  0.0009  113 LYS A C   
938  O  O   A LYS A 113 ? 0.1993 0.0838 0.1960 -0.0285 -0.0063 0.0082  113 LYS A O   
939  O  O   B LYS A 113 ? 0.1993 0.0850 0.1936 -0.0273 -0.0085 0.0055  113 LYS A O   
940  C  CB  A LYS A 113 ? 0.1458 0.1419 0.1243 0.0184  0.0083  0.0029  113 LYS A CB  
941  C  CB  B LYS A 113 ? 0.1583 0.1365 0.1186 0.0116  0.0172  -0.0158 113 LYS A CB  
942  C  CG  A LYS A 113 ? 0.1426 0.1692 0.1429 0.0226  0.0047  -0.0068 113 LYS A CG  
943  C  CG  B LYS A 113 ? 0.1339 0.1544 0.1465 0.0212  0.0258  -0.0168 113 LYS A CG  
944  C  CD  A LYS A 113 ? 0.1400 0.2148 0.1342 0.0373  0.0088  0.0183  113 LYS A CD  
945  C  CD  B LYS A 113 ? 0.1570 0.1048 0.2119 0.0362  0.0273  -0.0596 113 LYS A CD  
946  C  CE  A LYS A 113 ? 0.1198 0.2227 0.2076 0.0168  -0.0004 0.0350  113 LYS A CE  
947  C  CE  B LYS A 113 ? 0.1857 0.1936 0.1814 -0.0172 -0.0038 -0.0036 113 LYS A CE  
948  N  NZ  A LYS A 113 ? 0.2216 0.2069 0.1983 0.0963  -0.0187 0.0294  113 LYS A NZ  
949  N  NZ  B LYS A 113 ? 0.1976 0.2301 0.1394 0.0531  0.0089  -0.0399 113 LYS A NZ  
950  N  N   . TYR A 114 ? 0.1037 0.0952 0.1195 0.0091  0.0181  0.0008  114 TYR A N   
951  C  CA  . TYR A 114 ? 0.1112 0.0760 0.1130 -0.0008 0.0147  -0.0035 114 TYR A CA  
952  C  C   . TYR A 114 ? 0.0938 0.0820 0.1218 -0.0078 0.0186  -0.0034 114 TYR A C   
953  O  O   . TYR A 114 ? 0.0882 0.0935 0.1394 -0.0073 0.0099  -0.0145 114 TYR A O   
954  C  CB  . TYR A 114 ? 0.1042 0.0859 0.1253 0.0089  0.0314  0.0053  114 TYR A CB  
955  C  CG  . TYR A 114 ? 0.1063 0.0916 0.1190 0.0084  0.0215  0.0103  114 TYR A CG  
956  C  CD1 . TYR A 114 ? 0.1512 0.1155 0.1164 0.0392  0.0147  0.0072  114 TYR A CD1 
957  C  CD2 . TYR A 114 ? 0.1012 0.1044 0.2004 0.0006  0.0319  0.0286  114 TYR A CD2 
958  C  CE1 . TYR A 114 ? 0.2053 0.1419 0.1289 0.0390  0.0375  0.0114  114 TYR A CE1 
959  C  CE2 . TYR A 114 ? 0.1587 0.1444 0.1936 -0.0048 0.0700  0.0316  114 TYR A CE2 
960  C  CZ  . TYR A 114 ? 0.1986 0.1544 0.1577 0.0097  0.0729  0.0469  114 TYR A CZ  
961  O  OH  . TYR A 114 ? 0.2558 0.2619 0.1857 0.0425  0.1089  0.0595  114 TYR A OH  
962  N  N   . ALA A 115 ? 0.0993 0.0923 0.1209 0.0039  0.0071  -0.0111 115 ALA A N   
963  C  CA  . ALA A 115 ? 0.1293 0.0830 0.1293 -0.0137 0.0104  -0.0263 115 ALA A CA  
964  C  C   . ALA A 115 ? 0.0949 0.0900 0.1419 -0.0012 0.0100  -0.0130 115 ALA A C   
965  O  O   . ALA A 115 ? 0.1182 0.0952 0.1307 -0.0119 0.0218  -0.0217 115 ALA A O   
966  C  CB  . ALA A 115 ? 0.1529 0.1300 0.1494 -0.0334 -0.0153 -0.0210 115 ALA A CB  
967  N  N   . ALA A 116 ? 0.1093 0.0697 0.1218 -0.0063 0.0053  -0.0166 116 ALA A N   
968  C  CA  . ALA A 116 ? 0.1090 0.0672 0.1040 0.0044  0.0175  -0.0176 116 ALA A CA  
969  C  C   . ALA A 116 ? 0.0827 0.0794 0.0945 0.0022  0.0093  -0.0137 116 ALA A C   
970  O  O   . ALA A 116 ? 0.0809 0.0870 0.1178 -0.0062 0.0186  -0.0084 116 ALA A O   
971  C  CB  . ALA A 116 ? 0.1036 0.1188 0.1067 -0.0099 0.0081  0.0021  116 ALA A CB  
972  N  N   . GLU A 117 ? 0.0925 0.0740 0.0977 0.0133  0.0081  -0.0016 117 GLU A N   
973  C  CA  . GLU A 117 ? 0.1014 0.0724 0.0841 0.0124  0.0006  -0.0046 117 GLU A CA  
974  C  C   . GLU A 117 ? 0.0845 0.0850 0.0917 -0.0042 0.0139  0.0027  117 GLU A C   
975  O  O   . GLU A 117 ? 0.0768 0.1119 0.1076 0.0057  0.0179  0.0100  117 GLU A O   
976  C  CB  . GLU A 117 ? 0.0821 0.1112 0.0861 -0.0001 0.0054  0.0000  117 GLU A CB  
977  C  CG  . GLU A 117 ? 0.1239 0.1111 0.0821 0.0109  -0.0111 -0.0087 117 GLU A CG  
978  C  CD  . GLU A 117 ? 0.0796 0.1091 0.0988 0.0058  0.0055  -0.0108 117 GLU A CD  
979  O  OE1 . GLU A 117 ? 0.0853 0.1108 0.1014 0.0055  0.0041  -0.0055 117 GLU A OE1 
980  O  OE2 . GLU A 117 ? 0.1098 0.1029 0.0954 0.0044  -0.0020 0.0000  117 GLU A OE2 
981  N  N   . LEU A 118 ? 0.0805 0.0818 0.0924 0.0037  -0.0042 -0.0044 118 LEU A N   
982  C  CA  . LEU A 118 ? 0.0759 0.0784 0.1006 -0.0027 -0.0058 0.0030  118 LEU A CA  
983  C  C   . LEU A 118 ? 0.0944 0.0765 0.0863 0.0129  0.0050  0.0141  118 LEU A C   
984  O  O   . LEU A 118 ? 0.0872 0.0802 0.0855 -0.0017 0.0057  0.0040  118 LEU A O   
985  C  CB  . LEU A 118 ? 0.0706 0.0943 0.1172 0.0000  -0.0033 0.0105  118 LEU A CB  
986  C  CG  . LEU A 118 ? 0.0837 0.0981 0.1033 0.0072  -0.0106 0.0133  118 LEU A CG  
987  C  CD1 . LEU A 118 ? 0.1031 0.1030 0.1141 -0.0004 -0.0054 0.0139  118 LEU A CD1 
988  C  CD2 . LEU A 118 ? 0.0882 0.1541 0.1216 0.0000  -0.0341 -0.0080 118 LEU A CD2 
989  N  N   . HIS A 119 ? 0.0794 0.0615 0.0768 0.0099  -0.0035 0.0084  119 HIS A N   
990  C  CA  . HIS A 119 ? 0.0803 0.0694 0.1040 -0.0006 0.0010  0.0021  119 HIS A CA  
991  C  C   . HIS A 119 ? 0.0785 0.0606 0.0774 -0.0048 0.0085  -0.0061 119 HIS A C   
992  O  O   . HIS A 119 ? 0.0879 0.0999 0.0861 0.0060  0.0153  0.0041  119 HIS A O   
993  C  CB  . HIS A 119 ? 0.0836 0.0866 0.0967 -0.0005 0.0000  0.0073  119 HIS A CB  
994  C  CG  . HIS A 119 ? 0.0663 0.0895 0.0916 -0.0031 -0.0037 -0.0002 119 HIS A CG  
995  N  ND1 . HIS A 119 ? 0.0715 0.1011 0.0864 0.0033  0.0104  -0.0069 119 HIS A ND1 
996  C  CD2 . HIS A 119 ? 0.0769 0.0895 0.0783 0.0048  -0.0033 0.0005  119 HIS A CD2 
997  C  CE1 . HIS A 119 ? 0.0925 0.0942 0.0793 -0.0104 -0.0019 -0.0017 119 HIS A CE1 
998  N  NE2 . HIS A 119 ? 0.0634 0.0936 0.1111 0.0015  -0.0115 0.0042  119 HIS A NE2 
999  N  N   . LEU A 120 ? 0.0726 0.0729 0.0997 0.0060  -0.0010 -0.0010 120 LEU A N   
1000 C  CA  . LEU A 120 ? 0.0721 0.0775 0.0974 0.0094  0.0006  -0.0035 120 LEU A CA  
1001 C  C   . LEU A 120 ? 0.0793 0.0724 0.0943 0.0121  -0.0024 0.0058  120 LEU A C   
1002 O  O   . LEU A 120 ? 0.0671 0.0945 0.0951 0.0042  0.0000  0.0019  120 LEU A O   
1003 C  CB  . LEU A 120 ? 0.0672 0.0938 0.1317 -0.0013 -0.0022 -0.0024 120 LEU A CB  
1004 C  CG  . LEU A 120 ? 0.0749 0.1164 0.1112 -0.0188 -0.0057 0.0037  120 LEU A CG  
1005 C  CD1 . LEU A 120 ? 0.1677 0.1401 0.1566 -0.0707 -0.0093 0.0107  120 LEU A CD1 
1006 C  CD2 . LEU A 120 ? 0.1045 0.1703 0.1552 0.0178  -0.0197 0.0022  120 LEU A CD2 
1007 N  N   . VAL A 121 ? 0.0936 0.0751 0.1055 -0.0098 0.0037  0.0009  121 VAL A N   
1008 C  CA  . VAL A 121 ? 0.0880 0.0665 0.1178 -0.0108 0.0148  0.0059  121 VAL A CA  
1009 C  C   . VAL A 121 ? 0.1039 0.0715 0.1049 -0.0012 0.0136  0.0197  121 VAL A C   
1010 O  O   . VAL A 121 ? 0.1289 0.0882 0.1053 0.0036  0.0021  0.0131  121 VAL A O   
1011 C  CB  . VAL A 121 ? 0.0935 0.0864 0.1437 -0.0065 0.0233  -0.0076 121 VAL A CB  
1012 C  CG1 . VAL A 121 ? 0.1060 0.1161 0.1886 -0.0268 0.0015  -0.0153 121 VAL A CG1 
1013 C  CG2 . VAL A 121 ? 0.1003 0.1088 0.1620 0.0226  0.0000  -0.0100 121 VAL A CG2 
1014 N  N   . HIS A 122 ? 0.0653 0.0900 0.1181 -0.0084 0.0122  -0.0015 122 HIS A N   
1015 C  CA  . HIS A 122 ? 0.0817 0.0744 0.1372 -0.0068 0.0100  -0.0006 122 HIS A CA  
1016 C  C   . HIS A 122 ? 0.0880 0.0776 0.1064 -0.0012 0.0164  0.0033  122 HIS A C   
1017 O  O   . HIS A 122 ? 0.1297 0.0818 0.1342 -0.0138 -0.0142 0.0164  122 HIS A O   
1018 C  CB  . HIS A 122 ? 0.0794 0.0938 0.1534 -0.0060 0.0142  -0.0057 122 HIS A CB  
1019 C  CG  . HIS A 122 ? 0.0803 0.0841 0.1293 -0.0029 0.0190  -0.0021 122 HIS A CG  
1020 N  ND1 . HIS A 122 ? 0.0820 0.0847 0.1336 0.0000  0.0166  0.0046  122 HIS A ND1 
1021 C  CD2 . HIS A 122 ? 0.0796 0.1125 0.1304 -0.0081 0.0182  -0.0029 122 HIS A CD2 
1022 C  CE1 . HIS A 122 ? 0.0641 0.1185 0.1358 -0.0012 0.0157  -0.0106 122 HIS A CE1 
1023 N  NE2 . HIS A 122 ? 0.0798 0.1185 0.1351 -0.0163 0.0059  0.0067  122 HIS A NE2 
1024 N  N   . TRP A 123 ? 0.1027 0.0665 0.1197 0.0023  0.0269  -0.0038 123 TRP A N   
1025 C  CA  . TRP A 123 ? 0.1154 0.0771 0.1121 -0.0143 0.0355  -0.0094 123 TRP A CA  
1026 C  C   . TRP A 123 ? 0.1023 0.0751 0.1365 -0.0010 0.0190  0.0054  123 TRP A C   
1027 O  O   . TRP A 123 ? 0.1078 0.0805 0.1698 0.0050  0.0208  0.0071  123 TRP A O   
1028 C  CB  . TRP A 123 ? 0.1274 0.1164 0.1033 -0.0326 0.0231  0.0027  123 TRP A CB  
1029 C  CG  . TRP A 123 ? 0.1182 0.1030 0.1350 -0.0271 0.0364  0.0077  123 TRP A CG  
1030 C  CD1 . TRP A 123 ? 0.1784 0.1036 0.1340 -0.0295 -0.0011 0.0174  123 TRP A CD1 
1031 C  CD2 . TRP A 123 ? 0.1936 0.0974 0.1437 -0.0216 0.0036  0.0258  123 TRP A CD2 
1032 N  NE1 . TRP A 123 ? 0.2558 0.0918 0.1566 -0.0319 -0.0067 0.0178  123 TRP A NE1 
1033 C  CE2 . TRP A 123 ? 0.1928 0.0871 0.1692 -0.0275 -0.0107 0.0243  123 TRP A CE2 
1034 C  CE3 . TRP A 123 ? 0.1904 0.0789 0.1745 -0.0306 0.0378  0.0100  123 TRP A CE3 
1035 C  CZ2 . TRP A 123 ? 0.2381 0.1164 0.1857 -0.0114 -0.0055 0.0463  123 TRP A CZ2 
1036 C  CZ3 . TRP A 123 ? 0.2195 0.0890 0.2262 -0.0443 -0.0091 0.0110  123 TRP A CZ3 
1037 C  CH2 . TRP A 123 ? 0.2341 0.1051 0.2264 -0.0328 0.0124  0.0165  123 TRP A CH2 
1038 N  N   . ASN A 124 ? 0.1231 0.0812 0.1222 -0.0158 0.0286  -0.0154 124 ASN A N   
1039 C  CA  . ASN A 124 ? 0.1394 0.0863 0.1547 -0.0005 0.0443  -0.0125 124 ASN A CA  
1040 C  C   . ASN A 124 ? 0.1297 0.0820 0.1519 0.0058  0.0305  -0.0198 124 ASN A C   
1041 O  O   . ASN A 124 ? 0.1376 0.0926 0.1508 0.0000  0.0374  -0.0130 124 ASN A O   
1042 C  CB  . ASN A 124 ? 0.1893 0.1094 0.1245 -0.0190 0.0537  -0.0117 124 ASN A CB  
1043 C  CG  . ASN A 124 ? 0.1853 0.1060 0.1476 -0.0054 0.0612  -0.0047 124 ASN A CG  
1044 O  OD1 . ASN A 124 ? 0.2108 0.1173 0.1810 0.0192  0.0761  -0.0125 124 ASN A OD1 
1045 N  ND2 . ASN A 124 ? 0.2244 0.1270 0.1480 -0.0049 0.0739  -0.0044 124 ASN A ND2 
1046 N  N   . THR A 125 ? 0.1458 0.0744 0.2117 0.0109  0.0418  -0.0033 125 THR A N   
1047 C  CA  . THR A 125 ? 0.1444 0.0933 0.2515 0.0259  0.0228  -0.0043 125 THR A CA  
1048 C  C   . THR A 125 ? 0.1565 0.0905 0.2073 0.0204  0.0523  -0.0105 125 THR A C   
1049 O  O   . THR A 125 ? 0.1893 0.1017 0.2471 0.0209  0.0396  0.0223  125 THR A O   
1050 C  CB  . THR A 125 ? 0.1465 0.1354 0.3043 0.0165  0.0164  0.0145  125 THR A CB  
1051 O  OG1 . THR A 125 ? 0.1878 0.1670 0.4039 0.0482  0.0828  0.0044  125 THR A OG1 
1052 C  CG2 . THR A 125 ? 0.1828 0.1372 0.3427 0.0024  -0.0348 0.0146  125 THR A CG2 
1053 N  N   . LYS A 126 ? 0.2124 0.1054 0.1627 0.0041  0.0776  -0.0104 126 LYS A N   
1054 C  CA  . LYS A 126 ? 0.2523 0.0954 0.1879 0.0027  0.0771  -0.0190 126 LYS A CA  
1055 C  C   . LYS A 126 ? 0.2349 0.0866 0.1652 -0.0256 0.0425  -0.0132 126 LYS A C   
1056 O  O   . LYS A 126 ? 0.3010 0.0988 0.1993 -0.0255 0.0358  -0.0294 126 LYS A O   
1057 C  CB  . LYS A 126 ? 0.2868 0.1814 0.1810 -0.0316 0.0748  -0.0287 126 LYS A CB  
1058 C  CG  . LYS A 126 ? 0.3295 0.1688 0.2057 -0.0189 0.0603  -0.0421 126 LYS A CG  
1059 C  CD  . LYS A 126 ? 0.4496 0.3086 0.2107 -0.0064 0.0559  -0.0097 126 LYS A CD  
1060 C  CE  . LYS A 126 ? 0.6045 0.3233 0.2124 0.0163  -0.0384 0.0365  126 LYS A CE  
1061 N  NZ  . LYS A 126 ? 0.4848 0.3164 0.2062 0.0391  -0.0388 0.0447  126 LYS A NZ  
1062 N  N   . TYR A 127 ? 0.2072 0.1146 0.1534 -0.0195 0.0385  -0.0214 127 TYR A N   
1063 C  CA  . TYR A 127 ? 0.1817 0.1017 0.1631 -0.0105 0.0194  -0.0001 127 TYR A CA  
1064 C  C   . TYR A 127 ? 0.1634 0.1154 0.1694 0.0053  0.0304  0.0034  127 TYR A C   
1065 O  O   . TYR A 127 ? 0.1735 0.1190 0.1821 -0.0119 0.0168  -0.0012 127 TYR A O   
1066 C  CB  . TYR A 127 ? 0.1965 0.0936 0.1465 -0.0040 0.0086  -0.0226 127 TYR A CB  
1067 C  CG  . TYR A 127 ? 0.2137 0.1011 0.1511 -0.0105 0.0177  -0.0233 127 TYR A CG  
1068 C  CD1 . TYR A 127 ? 0.2539 0.1002 0.1756 -0.0057 0.0042  -0.0366 127 TYR A CD1 
1069 C  CD2 . TYR A 127 ? 0.2057 0.0923 0.1537 0.0041  0.0142  -0.0192 127 TYR A CD2 
1070 C  CE1 . TYR A 127 ? 0.2972 0.1293 0.1843 0.0055  0.0201  -0.0083 127 TYR A CE1 
1071 C  CE2 . TYR A 127 ? 0.2111 0.1433 0.1426 0.0093  0.0038  -0.0261 127 TYR A CE2 
1072 C  CZ  . TYR A 127 ? 0.3244 0.1144 0.1519 0.0043  -0.0121 -0.0201 127 TYR A CZ  
1073 O  OH  . TYR A 127 ? 0.3158 0.1623 0.1508 0.0148  0.0027  -0.0399 127 TYR A OH  
1074 N  N   . GLY A 128 ? 0.1746 0.1015 0.1547 0.0111  0.0178  0.0064  128 GLY A N   
1075 C  CA  . GLY A 128 ? 0.2071 0.0978 0.1749 -0.0027 0.0482  0.0214  128 GLY A CA  
1076 C  C   . GLY A 128 ? 0.1662 0.1168 0.1717 -0.0033 0.0108  0.0199  128 GLY A C   
1077 O  O   . GLY A 128 ? 0.2057 0.1232 0.1759 0.0183  0.0039  0.0127  128 GLY A O   
1078 N  N   . ASP A 129 ? 0.1979 0.1124 0.1587 0.0240  0.0419  0.0006  129 ASP A N   
1079 C  CA  . ASP A 129 ? 0.2180 0.1251 0.1372 0.0469  0.0291  0.0115  129 ASP A CA  
1080 C  C   . ASP A 129 ? 0.2302 0.1071 0.1559 0.0285  -0.0004 0.0011  129 ASP A C   
1081 O  O   . ASP A 129 ? 0.2161 0.1361 0.1584 0.0295  0.0130  0.0196  129 ASP A O   
1082 C  CB  . ASP A 129 ? 0.2446 0.1870 0.1835 0.0234  0.0376  0.0634  129 ASP A CB  
1083 C  CG  . ASP A 129 ? 0.2363 0.0970 0.2612 0.0514  0.0726  0.0637  129 ASP A CG  
1084 O  OD1 . ASP A 129 ? 0.2728 0.2301 0.3840 -0.0392 -0.0345 0.1248  129 ASP A OD1 
1085 O  OD2 . ASP A 129 ? 0.2673 0.1893 0.4103 0.0256  0.1694  0.1028  129 ASP A OD2 
1086 N  N   . TYR A 130 ? 0.2428 0.1154 0.1282 0.0200  0.0422  0.0063  130 TYR A N   
1087 C  CA  . TYR A 130 ? 0.2514 0.1286 0.1771 0.0325  0.0678  0.0353  130 TYR A CA  
1088 C  C   . TYR A 130 ? 0.2385 0.1472 0.1426 0.0407  0.0882  0.0435  130 TYR A C   
1089 O  O   . TYR A 130 ? 0.2179 0.1918 0.1756 0.0476  0.0851  0.0750  130 TYR A O   
1090 C  CB  . TYR A 130 ? 0.3132 0.1145 0.2460 -0.0060 0.1103  -0.0257 130 TYR A CB  
1091 C  CG  . TYR A 130 ? 0.5077 0.1252 0.3477 0.0351  0.1421  0.0907  130 TYR A CG  
1092 C  CD1 . TYR A 130 ? 0.6055 0.1972 0.5569 0.1687  0.3673  -0.0697 130 TYR A CD1 
1093 C  CD2 . TYR A 130 ? 0.5586 0.1117 0.2295 -0.0385 0.1295  0.0025  130 TYR A CD2 
1094 C  CE1 . TYR A 130 ? 0.5335 0.2935 0.6344 0.0990  0.2339  0.0574  130 TYR A CE1 
1095 C  CE2 . TYR A 130 ? 0.4681 0.2752 0.2252 0.0333  0.1112  -0.0181 130 TYR A CE2 
1096 C  CZ  . TYR A 130 ? 0.4408 0.3010 0.4564 0.0812  0.0938  0.0174  130 TYR A CZ  
1097 O  OH  . TYR A 130 ? 0.3362 0.2469 0.7364 0.0450  0.0523  -0.1314 130 TYR A OH  
1098 N  N   . GLY A 131 ? 0.2681 0.2001 0.1724 0.0212  0.0971  0.0688  131 GLY A N   
1099 C  CA  . GLY A 131 ? 0.2344 0.2576 0.2751 0.0348  0.0795  0.0778  131 GLY A CA  
1100 C  C   . GLY A 131 ? 0.2299 0.2309 0.2537 -0.0332 0.0576  0.1423  131 GLY A C   
1101 O  O   . GLY A 131 ? 0.1720 0.3154 0.3647 0.0302  0.1010  0.1496  131 GLY A O   
1102 N  N   A LYS A 132 ? 0.1986 0.2154 0.2924 -0.0467 0.0421  0.0730  132 LYS A N   
1103 N  N   B LYS A 132 ? 0.1340 0.2349 0.3251 -0.0493 0.0552  0.0995  132 LYS A N   
1104 C  CA  A LYS A 132 ? 0.2180 0.1947 0.2623 -0.0732 0.0482  0.1379  132 LYS A CA  
1105 C  CA  B LYS A 132 ? 0.1753 0.1771 0.3413 -0.0372 0.0253  0.1090  132 LYS A CA  
1106 C  C   A LYS A 132 ? 0.1304 0.1404 0.1698 -0.0208 0.0217  0.0591  132 LYS A C   
1107 C  C   B LYS A 132 ? 0.1097 0.2572 0.2543 -0.0509 -0.0118 0.0686  132 LYS A C   
1108 O  O   A LYS A 132 ? 0.1229 0.1133 0.1498 -0.0115 0.0119  0.0031  132 LYS A O   
1109 O  O   B LYS A 132 ? 0.1231 0.0744 0.2584 -0.0204 -0.0143 0.0279  132 LYS A O   
1110 C  CB  A LYS A 132 ? 0.2532 0.1935 0.4943 -0.0061 0.0053  0.1385  132 LYS A CB  
1111 C  CB  B LYS A 132 ? 0.2223 0.1422 0.4013 -0.0354 -0.1121 0.0396  132 LYS A CB  
1112 C  CG  A LYS A 132 ? 0.4947 0.3157 0.4620 -0.0195 0.0153  0.1874  132 LYS A CG  
1113 C  CG  B LYS A 132 ? 0.3453 0.1843 0.4117 0.0300  0.0017  0.1530  132 LYS A CG  
1114 C  CD  A LYS A 132 ? 0.5262 0.1573 0.2957 -0.0710 -0.0205 0.0576  132 LYS A CD  
1115 C  CD  B LYS A 132 ? 0.4030 0.2270 0.3675 0.0499  -0.0002 0.0653  132 LYS A CD  
1116 C  CE  A LYS A 132 ? 0.9282 0.1382 0.5488 -0.1988 0.0100  0.2174  132 LYS A CE  
1117 C  CE  B LYS A 132 ? 0.4101 0.2407 0.4523 -0.1025 -0.0722 0.0294  132 LYS A CE  
1118 N  NZ  A LYS A 132 ? 0.4755 0.4094 0.6450 0.0826  -0.0196 0.0961  132 LYS A NZ  
1119 N  NZ  B LYS A 132 ? 0.2283 0.3859 0.5083 -0.1269 -0.0231 -0.0188 132 LYS A NZ  
1120 N  N   . ALA A 133 ? 0.1591 0.1383 0.1807 -0.0350 0.0183  0.0354  133 ALA A N   
1121 C  CA  . ALA A 133 ? 0.1238 0.1415 0.1703 -0.0304 0.0251  0.0323  133 ALA A CA  
1122 C  C   . ALA A 133 ? 0.1455 0.1223 0.1552 -0.0392 0.0332  0.0285  133 ALA A C   
1123 O  O   . ALA A 133 ? 0.1173 0.2051 0.1541 -0.0206 0.0258  0.0308  133 ALA A O   
1124 C  CB  . ALA A 133 ? 0.1365 0.1458 0.1243 -0.0473 0.0155  -0.0089 133 ALA A CB  
1125 N  N   . VAL A 134 ? 0.1439 0.1641 0.2298 0.0194  0.0930  0.0769  134 VAL A N   
1126 C  CA  . VAL A 134 ? 0.2374 0.2037 0.2425 0.0790  0.1310  0.0798  134 VAL A CA  
1127 C  C   . VAL A 134 ? 0.2108 0.3025 0.2666 0.0518  0.0979  0.1741  134 VAL A C   
1128 O  O   . VAL A 134 ? 0.1717 0.3743 0.3904 0.1194  0.1276  0.1683  134 VAL A O   
1129 C  CB  . VAL A 134 ? 0.3856 0.2018 0.3759 0.1775  0.1077  -0.0047 134 VAL A CB  
1130 C  CG1 . VAL A 134 ? 0.4758 0.4063 0.5398 0.0692  0.0480  -0.0053 134 VAL A CG1 
1131 C  CG2 . VAL A 134 ? 0.4034 0.2136 0.5166 0.0447  0.0330  0.0952  134 VAL A CG2 
1132 N  N   . GLN A 135 ? 0.1681 0.3369 0.3074 -0.0131 0.0261  0.1061  135 GLN A N   
1133 C  CA  . GLN A 135 ? 0.3426 0.5343 0.3552 0.0886  -0.1177 -0.0288 135 GLN A CA  
1134 C  C   . GLN A 135 ? 0.1537 0.3951 0.3236 -0.0310 -0.0816 0.0816  135 GLN A C   
1135 O  O   . GLN A 135 ? 0.3143 0.4986 0.3486 -0.1444 -0.0930 0.1582  135 GLN A O   
1136 C  CB  . GLN A 135 ? 0.5533 0.4913 0.3777 0.0276  0.2002  0.1298  135 GLN A CB  
1137 C  CG  . GLN A 135 ? 0.5826 1.1883 0.6124 0.3543  0.3823  -0.0255 135 GLN A CG  
1138 C  CD  . GLN A 135 ? 1.5570 0.9966 1.6580 -0.1688 0.5054  0.7183  135 GLN A CD  
1139 O  OE1 . GLN A 135 ? 0.4769 1.2179 1.7133 0.1073  0.3250  -0.0075 135 GLN A OE1 
1140 N  NE2 . GLN A 135 ? 1.5544 1.3881 1.7717 0.2398  0.9230  0.9805  135 GLN A NE2 
1141 N  N   . GLN A 136 ? 0.1566 0.1918 0.2288 -0.0107 -0.0346 0.0653  136 GLN A N   
1142 C  CA  . GLN A 136 ? 0.1702 0.1067 0.2166 -0.0186 -0.0671 -0.0145 136 GLN A CA  
1143 C  C   . GLN A 136 ? 0.1781 0.1236 0.1541 0.0149  -0.0370 -0.0241 136 GLN A C   
1144 O  O   . GLN A 136 ? 0.1731 0.1372 0.1150 -0.0135 0.0094  -0.0176 136 GLN A O   
1145 C  CB  . GLN A 136 ? 0.2162 0.1249 0.2597 0.0135  -0.0634 0.0107  136 GLN A CB  
1146 C  CG  . GLN A 136 ? 0.2902 0.1738 0.2226 -0.0122 -0.0223 0.0241  136 GLN A CG  
1147 C  CD  . GLN A 136 ? 0.2813 0.2148 0.2231 -0.0519 -0.0153 0.0522  136 GLN A CD  
1148 O  OE1 . GLN A 136 ? 0.3535 0.2148 0.2231 -0.0512 -0.0582 -0.0111 136 GLN A OE1 
1149 N  NE2 . GLN A 136 ? 0.3468 0.3370 0.4069 -0.0571 0.0547  0.1482  136 GLN A NE2 
1150 N  N   A PRO A 137 ? 0.1505 0.1677 0.1530 0.0593  -0.0560 -0.0357 137 PRO A N   
1151 N  N   B PRO A 137 ? 0.2460 0.1609 0.1426 0.0127  -0.0270 -0.0478 137 PRO A N   
1152 C  CA  A PRO A 137 ? 0.1764 0.1914 0.1426 0.0418  0.0018  -0.0118 137 PRO A CA  
1153 C  CA  B PRO A 137 ? 0.2266 0.1928 0.1176 0.0403  -0.0062 0.0048  137 PRO A CA  
1154 C  C   A PRO A 137 ? 0.2011 0.1853 0.0856 0.0232  0.0392  -0.0067 137 PRO A C   
1155 C  C   B PRO A 137 ? 0.2301 0.1814 0.0629 0.0395  0.0513  -0.0060 137 PRO A C   
1156 O  O   A PRO A 137 ? 0.1932 0.1831 0.1645 0.0168  0.1029  0.0260  137 PRO A O   
1157 O  O   B PRO A 137 ? 0.2565 0.1620 0.1293 0.0491  0.0094  -0.0154 137 PRO A O   
1158 C  CB  A PRO A 137 ? 0.2728 0.2371 0.1620 0.0279  -0.0559 -0.0266 137 PRO A CB  
1159 C  CB  B PRO A 137 ? 0.2875 0.2313 0.1266 0.0814  -0.0357 -0.0046 137 PRO A CB  
1160 C  CG  A PRO A 137 ? 0.1972 0.2460 0.1613 0.0427  -0.0401 -0.1157 137 PRO A CG  
1161 C  CG  B PRO A 137 ? 0.3043 0.3373 0.1483 0.0066  0.0178  -0.0255 137 PRO A CG  
1162 C  CD  A PRO A 137 ? 0.2185 0.2105 0.2015 0.0226  -0.0728 -0.0670 137 PRO A CD  
1163 C  CD  B PRO A 137 ? 0.2058 0.1746 0.2251 0.0399  -0.0600 -0.0856 137 PRO A CD  
1164 N  N   . ASP A 138 ? 0.1713 0.1706 0.0974 0.0060  0.0157  -0.0094 138 ASP A N   
1165 C  CA  . ASP A 138 ? 0.1796 0.1530 0.0970 -0.0061 0.0315  -0.0096 138 ASP A CA  
1166 C  C   . ASP A 138 ? 0.1443 0.1170 0.1075 -0.0021 0.0247  -0.0103 138 ASP A C   
1167 O  O   . ASP A 138 ? 0.1541 0.1745 0.1157 0.0108  0.0280  0.0025  138 ASP A O   
1168 C  CB  . ASP A 138 ? 0.2308 0.1900 0.1275 0.0475  0.0500  -0.0100 138 ASP A CB  
1169 C  CG  . ASP A 138 ? 0.1879 0.2040 0.0911 0.0328  0.0485  -0.0115 138 ASP A CG  
1170 O  OD1 . ASP A 138 ? 0.2244 0.1544 0.1602 0.0125  0.0220  -0.0255 138 ASP A OD1 
1171 O  OD2 . ASP A 138 ? 0.2512 0.1893 0.1426 0.0692  0.0427  -0.0357 138 ASP A OD2 
1172 N  N   . GLY A 139 ? 0.1455 0.1017 0.0924 -0.0178 0.0251  0.0006  139 GLY A N   
1173 C  CA  . GLY A 139 ? 0.1455 0.0997 0.0870 -0.0132 -0.0006 0.0001  139 GLY A CA  
1174 C  C   . GLY A 139 ? 0.0970 0.1003 0.0837 -0.0079 0.0343  0.0048  139 GLY A C   
1175 O  O   . GLY A 139 ? 0.1094 0.0875 0.1074 -0.0047 -0.0002 -0.0020 139 GLY A O   
1176 N  N   . LEU A 140 ? 0.0787 0.0911 0.1008 -0.0041 0.0255  -0.0093 140 LEU A N   
1177 C  CA  . LEU A 140 ? 0.0782 0.0969 0.0884 -0.0084 0.0249  -0.0095 140 LEU A CA  
1178 C  C   . LEU A 140 ? 0.0803 0.0873 0.0900 -0.0036 0.0238  -0.0136 140 LEU A C   
1179 O  O   . LEU A 140 ? 0.0757 0.0979 0.0925 -0.0018 0.0159  -0.0019 140 LEU A O   
1180 C  CB  . LEU A 140 ? 0.0932 0.1051 0.1107 -0.0022 0.0359  -0.0149 140 LEU A CB  
1181 C  CG  . LEU A 140 ? 0.0979 0.1179 0.1260 0.0155  0.0491  -0.0011 140 LEU A CG  
1182 C  CD1 . LEU A 140 ? 0.1238 0.1627 0.1028 0.0255  0.0609  -0.0088 140 LEU A CD1 
1183 C  CD2 . LEU A 140 ? 0.1368 0.1522 0.1137 0.0168  0.0361  0.0064  140 LEU A CD2 
1184 N  N   . ALA A 141 ? 0.0778 0.0862 0.1160 -0.0069 0.0144  -0.0001 141 ALA A N   
1185 C  CA  . ALA A 141 ? 0.0812 0.0697 0.1270 -0.0122 0.0251  -0.0136 141 ALA A CA  
1186 C  C   . ALA A 141 ? 0.0751 0.0803 0.1132 0.0000  0.0130  -0.0015 141 ALA A C   
1187 O  O   . ALA A 141 ? 0.1005 0.0782 0.1209 -0.0036 -0.0042 0.0061  141 ALA A O   
1188 C  CB  . ALA A 141 ? 0.0895 0.1040 0.1497 -0.0049 0.0482  -0.0024 141 ALA A CB  
1189 N  N   . VAL A 142 ? 0.0832 0.0803 0.1017 0.0011  0.0170  0.0000  142 VAL A N   
1190 C  CA  . VAL A 142 ? 0.0780 0.0759 0.1191 0.0026  0.0291  -0.0137 142 VAL A CA  
1191 C  C   . VAL A 142 ? 0.0782 0.0807 0.0925 0.0027  0.0100  0.0053  142 VAL A C   
1192 O  O   . VAL A 142 ? 0.0981 0.0873 0.0911 0.0005  -0.0050 0.0031  142 VAL A O   
1193 C  CB  . VAL A 142 ? 0.0794 0.0866 0.1112 0.0127  0.0135  -0.0055 142 VAL A CB  
1194 C  CG1 . VAL A 142 ? 0.0807 0.1243 0.0972 0.0237  0.0304  -0.0210 142 VAL A CG1 
1195 C  CG2 . VAL A 142 ? 0.0845 0.1342 0.1084 -0.0152 0.0050  0.0217  142 VAL A CG2 
1196 N  N   . LEU A 143 ? 0.0810 0.0748 0.1053 -0.0041 -0.0002 -0.0094 143 LEU A N   
1197 C  CA  . LEU A 143 ? 0.0692 0.0838 0.1300 -0.0055 -0.0013 0.0002  143 LEU A CA  
1198 C  C   . LEU A 143 ? 0.0848 0.0908 0.0996 -0.0214 0.0124  0.0091  143 LEU A C   
1199 O  O   . LEU A 143 ? 0.1120 0.0909 0.1023 -0.0163 0.0150  0.0048  143 LEU A O   
1200 C  CB  . LEU A 143 ? 0.0829 0.1267 0.1519 -0.0042 -0.0054 0.0085  143 LEU A CB  
1201 C  CG  . LEU A 143 ? 0.0836 0.1304 0.1820 -0.0080 0.0004  0.0217  143 LEU A CG  
1202 C  CD1 . LEU A 143 ? 0.1329 0.2101 0.1889 -0.0560 -0.0089 0.0487  143 LEU A CD1 
1203 C  CD2 . LEU A 143 ? 0.0819 0.1857 0.1821 0.0137  -0.0160 0.0018  143 LEU A CD2 
1204 N  N   . GLY A 144 ? 0.0889 0.0812 0.0965 -0.0100 0.0118  0.0008  144 GLY A N   
1205 C  CA  . GLY A 144 ? 0.0820 0.0791 0.1038 -0.0070 0.0052  -0.0092 144 GLY A CA  
1206 C  C   . GLY A 144 ? 0.0927 0.0828 0.0729 -0.0044 0.0103  0.0098  144 GLY A C   
1207 O  O   . GLY A 144 ? 0.1032 0.0970 0.0945 -0.0076 0.0201  0.0098  144 GLY A O   
1208 N  N   . ILE A 145 ? 0.0915 0.0677 0.0875 0.0032  0.0024  -0.0013 145 ILE A N   
1209 C  CA  . ILE A 145 ? 0.0787 0.0744 0.0954 0.0013  -0.0005 -0.0013 145 ILE A CA  
1210 C  C   . ILE A 145 ? 0.0696 0.0917 0.0965 -0.0054 0.0111  -0.0095 145 ILE A C   
1211 O  O   . ILE A 145 ? 0.0873 0.0863 0.0917 -0.0047 0.0131  -0.0051 145 ILE A O   
1212 C  CB  . ILE A 145 ? 0.0821 0.0933 0.1126 0.0037  -0.0071 -0.0041 145 ILE A CB  
1213 C  CG1 . ILE A 145 ? 0.1297 0.1190 0.1189 0.0413  -0.0088 -0.0013 145 ILE A CG1 
1214 C  CG2 . ILE A 145 ? 0.0905 0.1322 0.1566 -0.0122 -0.0189 0.0001  145 ILE A CG2 
1215 C  CD1 . ILE A 145 ? 0.1168 0.0986 0.1444 0.0156  -0.0309 0.0035  145 ILE A CD1 
1216 N  N   . PHE A 146 ? 0.0807 0.0762 0.0950 0.0013  0.0009  -0.0043 146 PHE A N   
1217 C  CA  . PHE A 146 ? 0.1048 0.0812 0.0731 0.0099  -0.0055 -0.0008 146 PHE A CA  
1218 C  C   . PHE A 146 ? 0.0756 0.0961 0.0900 -0.0046 -0.0013 -0.0020 146 PHE A C   
1219 O  O   . PHE A 146 ? 0.0726 0.1121 0.1106 -0.0074 -0.0021 -0.0111 146 PHE A O   
1220 C  CB  . PHE A 146 ? 0.0936 0.1039 0.0997 -0.0219 -0.0089 0.0121  146 PHE A CB  
1221 C  CG  . PHE A 146 ? 0.0803 0.0748 0.0900 -0.0033 0.0016  0.0047  146 PHE A CG  
1222 C  CD1 . PHE A 146 ? 0.0783 0.0857 0.1213 -0.0044 -0.0034 0.0034  146 PHE A CD1 
1223 C  CD2 . PHE A 146 ? 0.0979 0.0911 0.1049 -0.0050 0.0171  0.0119  146 PHE A CD2 
1224 C  CE1 . PHE A 146 ? 0.0898 0.1080 0.1098 0.0027  -0.0040 0.0022  146 PHE A CE1 
1225 C  CE2 . PHE A 146 ? 0.0996 0.0942 0.1118 0.0024  0.0008  0.0066  146 PHE A CE2 
1226 C  CZ  . PHE A 146 ? 0.1017 0.0891 0.1072 -0.0019 0.0003  0.0115  146 PHE A CZ  
1227 N  N   . LEU A 147 ? 0.0970 0.0776 0.1017 -0.0113 0.0121  -0.0068 147 LEU A N   
1228 C  CA  . LEU A 147 ? 0.1172 0.0805 0.0977 -0.0163 -0.0017 -0.0036 147 LEU A CA  
1229 C  C   . LEU A 147 ? 0.1172 0.0884 0.0881 -0.0132 -0.0011 -0.0095 147 LEU A C   
1230 O  O   . LEU A 147 ? 0.1148 0.1021 0.1274 -0.0104 0.0047  -0.0006 147 LEU A O   
1231 C  CB  . LEU A 147 ? 0.1160 0.0886 0.0990 0.0003  0.0168  -0.0062 147 LEU A CB  
1232 C  CG  . LEU A 147 ? 0.1187 0.0891 0.0979 -0.0285 0.0039  0.0044  147 LEU A CG  
1233 C  CD1 . LEU A 147 ? 0.1795 0.0856 0.1376 -0.0200 -0.0071 -0.0065 147 LEU A CD1 
1234 C  CD2 . LEU A 147 ? 0.1157 0.1340 0.1049 -0.0182 0.0121  0.0031  147 LEU A CD2 
1235 N  N   . LYS A 148 ? 0.1218 0.0938 0.1033 -0.0207 0.0066  -0.0168 148 LYS A N   
1236 C  CA  . LYS A 148 ? 0.1602 0.0835 0.1178 -0.0283 -0.0111 0.0079  148 LYS A CA  
1237 C  C   . LYS A 148 ? 0.1487 0.0871 0.1371 -0.0190 -0.0322 0.0025  148 LYS A C   
1238 O  O   . LYS A 148 ? 0.1925 0.1155 0.1419 0.0189  -0.0398 -0.0042 148 LYS A O   
1239 C  CB  . LYS A 148 ? 0.1684 0.1799 0.1311 -0.0575 -0.0267 0.0372  148 LYS A CB  
1240 C  CG  . LYS A 148 ? 0.1764 0.2075 0.1209 -0.0316 -0.0042 0.0204  148 LYS A CG  
1241 C  CD  . LYS A 148 ? 0.2825 0.2878 0.1760 -0.0575 0.0379  0.0429  148 LYS A CD  
1242 C  CE  . LYS A 148 ? 0.2821 0.4839 0.3438 -0.0122 0.0507  0.0851  148 LYS A CE  
1243 N  NZ  . LYS A 148 ? 0.4690 0.5224 0.4968 -0.1403 0.1321  0.1736  148 LYS A NZ  
1244 N  N   . VAL A 149 ? 0.1598 0.0897 0.1340 -0.0111 -0.0156 0.0003  149 VAL A N   
1245 C  CA  . VAL A 149 ? 0.1620 0.1053 0.1476 -0.0170 -0.0065 -0.0238 149 VAL A CA  
1246 C  C   . VAL A 149 ? 0.1602 0.0801 0.1533 -0.0067 -0.0199 0.0067  149 VAL A C   
1247 O  O   . VAL A 149 ? 0.1789 0.1136 0.1590 -0.0083 -0.0244 0.0200  149 VAL A O   
1248 C  CB  . VAL A 149 ? 0.1534 0.1364 0.1300 -0.0250 0.0022  -0.0027 149 VAL A CB  
1249 C  CG1 . VAL A 149 ? 0.1972 0.1615 0.1595 -0.0162 -0.0308 -0.0221 149 VAL A CG1 
1250 C  CG2 . VAL A 149 ? 0.2043 0.1376 0.1565 -0.0516 -0.0078 0.0197  149 VAL A CG2 
1251 N  N   . GLY A 150 ? 0.1451 0.1132 0.1455 -0.0258 -0.0197 0.0182  150 GLY A N   
1252 C  CA  . GLY A 150 ? 0.1681 0.1252 0.1724 -0.0430 -0.0423 0.0204  150 GLY A CA  
1253 C  C   . GLY A 150 ? 0.1613 0.1286 0.1440 -0.0477 -0.0160 0.0242  150 GLY A C   
1254 O  O   . GLY A 150 ? 0.2001 0.1256 0.1637 -0.0486 -0.0242 0.0042  150 GLY A O   
1255 N  N   A SER A 151 ? 0.1462 0.1269 0.1746 -0.0372 -0.0312 0.0067  151 SER A N   
1256 N  N   B SER A 151 ? 0.1548 0.1322 0.1850 -0.0341 -0.0211 -0.0001 151 SER A N   
1257 C  CA  A SER A 151 ? 0.1254 0.1437 0.1717 -0.0264 -0.0149 0.0269  151 SER A CA  
1258 C  CA  B SER A 151 ? 0.1584 0.1379 0.1807 -0.0259 -0.0124 0.0182  151 SER A CA  
1259 C  C   A SER A 151 ? 0.1494 0.1267 0.1371 -0.0275 -0.0047 -0.0065 151 SER A C   
1260 C  C   B SER A 151 ? 0.1766 0.1216 0.1404 -0.0193 -0.0157 0.0025  151 SER A C   
1261 O  O   A SER A 151 ? 0.1057 0.1251 0.1164 -0.0104 0.0163  -0.0179 151 SER A O   
1262 O  O   B SER A 151 ? 0.1929 0.1275 0.1522 -0.0262 -0.0319 -0.0002 151 SER A O   
1263 C  CB  A SER A 151 ? 0.1190 0.1778 0.2644 -0.0582 -0.0097 0.0150  151 SER A CB  
1264 C  CB  B SER A 151 ? 0.1663 0.1688 0.2893 -0.0160 0.0074  0.0637  151 SER A CB  
1265 O  OG  A SER A 151 ? 0.1154 0.2575 0.2474 -0.0571 0.0074  -0.0260 151 SER A OG  
1266 O  OG  B SER A 151 ? 0.1580 0.1900 0.3208 -0.0223 0.0167  0.0770  151 SER A OG  
1267 N  N   . ALA A 152 ? 0.1569 0.1239 0.1448 -0.0164 -0.0320 0.0017  152 ALA A N   
1268 C  CA  . ALA A 152 ? 0.1430 0.1394 0.1440 -0.0201 -0.0190 0.0032  152 ALA A CA  
1269 C  C   . ALA A 152 ? 0.1145 0.1278 0.1473 -0.0209 -0.0298 0.0008  152 ALA A C   
1270 O  O   . ALA A 152 ? 0.1448 0.1570 0.1911 -0.0417 0.0006  0.0062  152 ALA A O   
1271 C  CB  . ALA A 152 ? 0.2180 0.1411 0.1389 -0.0019 -0.0372 -0.0222 152 ALA A CB  
1272 N  N   . LYS A 153 ? 0.1358 0.1130 0.1699 -0.0188 -0.0314 0.0268  153 LYS A N   
1273 C  CA  . LYS A 153 ? 0.1728 0.1353 0.1433 -0.0290 -0.0244 0.0197  153 LYS A CA  
1274 C  C   . LYS A 153 ? 0.1419 0.1383 0.1673 -0.0173 -0.0135 0.0195  153 LYS A C   
1275 O  O   . LYS A 153 ? 0.1257 0.1376 0.1483 -0.0210 -0.0198 0.0234  153 LYS A O   
1276 C  CB  . LYS A 153 ? 0.1415 0.1340 0.1759 -0.0234 -0.0386 0.0195  153 LYS A CB  
1277 C  CG  . LYS A 153 ? 0.1669 0.1300 0.2000 -0.0418 -0.0137 0.0196  153 LYS A CG  
1278 C  CD  . LYS A 153 ? 0.1746 0.1649 0.1659 -0.0232 0.0020  0.0032  153 LYS A CD  
1279 C  CE  . LYS A 153 ? 0.3362 0.1667 0.1756 -0.0385 -0.0131 0.0144  153 LYS A CE  
1280 N  NZ  . LYS A 153 ? 0.3674 0.2398 0.2309 -0.0340 0.0214  0.0533  153 LYS A NZ  
1281 N  N   . PRO A 154 ? 0.1272 0.1608 0.1523 -0.0429 -0.0170 0.0093  154 PRO A N   
1282 C  CA  . PRO A 154 ? 0.1303 0.1767 0.1861 -0.0462 -0.0394 0.0411  154 PRO A CA  
1283 C  C   . PRO A 154 ? 0.1090 0.1609 0.1813 -0.0018 -0.0124 0.0487  154 PRO A C   
1284 O  O   . PRO A 154 ? 0.1300 0.2187 0.1778 -0.0136 -0.0127 0.0692  154 PRO A O   
1285 C  CB  . PRO A 154 ? 0.1152 0.2178 0.2540 -0.0315 -0.0300 0.0186  154 PRO A CB  
1286 C  CG  . PRO A 154 ? 0.1577 0.2467 0.2856 -0.0388 -0.0486 0.0688  154 PRO A CG  
1287 C  CD  . PRO A 154 ? 0.1289 0.1752 0.2125 -0.0434 -0.0076 0.0614  154 PRO A CD  
1288 N  N   . GLY A 155 ? 0.1014 0.1358 0.2173 -0.0011 -0.0030 0.0096  155 GLY A N   
1289 C  CA  . GLY A 155 ? 0.1161 0.1422 0.2410 0.0013  0.0100  0.0212  155 GLY A CA  
1290 C  C   . GLY A 155 ? 0.1258 0.1194 0.1961 -0.0110 -0.0017 0.0381  155 GLY A C   
1291 O  O   . GLY A 155 ? 0.1695 0.1111 0.3094 -0.0017 0.0146  0.0428  155 GLY A O   
1292 N  N   . LEU A 156 ? 0.1006 0.1297 0.1705 -0.0044 -0.0145 0.0125  156 LEU A N   
1293 C  CA  . LEU A 156 ? 0.1054 0.1168 0.1357 -0.0244 -0.0054 0.0198  156 LEU A CA  
1294 C  C   . LEU A 156 ? 0.1116 0.1062 0.1400 -0.0146 -0.0076 0.0013  156 LEU A C   
1295 O  O   . LEU A 156 ? 0.1078 0.1440 0.1324 -0.0220 -0.0098 0.0114  156 LEU A O   
1296 C  CB  . LEU A 156 ? 0.1125 0.1239 0.1631 -0.0257 -0.0259 0.0291  156 LEU A CB  
1297 C  CG  . LEU A 156 ? 0.1146 0.1170 0.1670 -0.0243 -0.0048 0.0142  156 LEU A CG  
1298 C  CD1 . LEU A 156 ? 0.1458 0.1508 0.1606 -0.0400 -0.0119 0.0015  156 LEU A CD1 
1299 C  CD2 . LEU A 156 ? 0.1176 0.1282 0.1893 0.0026  -0.0147 0.0098  156 LEU A CD2 
1300 N  N   . GLN A 157 ? 0.1394 0.1272 0.1537 -0.0284 -0.0267 0.0034  157 GLN A N   
1301 C  CA  . GLN A 157 ? 0.1509 0.1476 0.1487 -0.0560 -0.0134 -0.0044 157 GLN A CA  
1302 C  C   . GLN A 157 ? 0.1426 0.1371 0.1620 -0.0216 -0.0422 0.0133  157 GLN A C   
1303 O  O   . GLN A 157 ? 0.1537 0.1451 0.1487 -0.0225 -0.0370 0.0094  157 GLN A O   
1304 C  CB  . GLN A 157 ? 0.1365 0.1771 0.1713 -0.0618 -0.0423 0.0201  157 GLN A CB  
1305 C  CG  . GLN A 157 ? 0.2186 0.1637 0.1800 -0.0373 -0.0677 0.0036  157 GLN A CG  
1306 C  CD  . GLN A 157 ? 0.1828 0.1469 0.1717 -0.0586 -0.0149 0.0150  157 GLN A CD  
1307 O  OE1 . GLN A 157 ? 0.2169 0.1375 0.1580 -0.0245 -0.0192 0.0168  157 GLN A OE1 
1308 N  NE2 . GLN A 157 ? 0.2302 0.2032 0.1570 -0.0573 -0.0232 -0.0289 157 GLN A NE2 
1309 N  N   . LYS A 158 ? 0.1249 0.1522 0.1659 -0.0188 -0.0479 0.0324  158 LYS A N   
1310 C  CA  . LYS A 158 ? 0.1458 0.1519 0.1727 -0.0184 -0.0524 0.0366  158 LYS A CA  
1311 C  C   . LYS A 158 ? 0.1415 0.1329 0.1590 -0.0070 -0.0261 0.0281  158 LYS A C   
1312 O  O   . LYS A 158 ? 0.1723 0.1473 0.1437 -0.0312 -0.0118 0.0053  158 LYS A O   
1313 C  CB  . LYS A 158 ? 0.1710 0.1491 0.2555 -0.0146 -0.0643 0.0435  158 LYS A CB  
1314 N  N   . VAL A 159 ? 0.1297 0.1390 0.1458 -0.0141 -0.0239 0.0166  159 VAL A N   
1315 C  CA  . VAL A 159 ? 0.1216 0.1364 0.1358 -0.0111 -0.0078 0.0073  159 VAL A CA  
1316 C  C   . VAL A 159 ? 0.1261 0.1448 0.1329 -0.0085 0.0010  0.0172  159 VAL A C   
1317 O  O   . VAL A 159 ? 0.1310 0.1458 0.1530 -0.0135 0.0113  0.0085  159 VAL A O   
1318 C  CB  . VAL A 159 ? 0.1286 0.1317 0.1426 -0.0151 -0.0207 0.0050  159 VAL A CB  
1319 C  CG1 . VAL A 159 ? 0.1088 0.1663 0.1907 -0.0465 -0.0139 0.0155  159 VAL A CG1 
1320 C  CG2 . VAL A 159 ? 0.2044 0.1476 0.1368 0.0140  -0.0243 -0.0118 159 VAL A CG2 
1321 N  N   . VAL A 160 ? 0.1267 0.1176 0.1372 0.0051  -0.0105 0.0150  160 VAL A N   
1322 C  CA  . VAL A 160 ? 0.1875 0.1422 0.1433 0.0032  0.0068  -0.0024 160 VAL A CA  
1323 C  C   . VAL A 160 ? 0.1476 0.1624 0.1425 -0.0173 0.0132  -0.0146 160 VAL A C   
1324 O  O   . VAL A 160 ? 0.1770 0.1613 0.1425 -0.0220 0.0245  -0.0001 160 VAL A O   
1325 C  CB  . VAL A 160 ? 0.2309 0.1346 0.1501 -0.0015 0.0164  0.0135  160 VAL A CB  
1326 C  CG1 . VAL A 160 ? 0.2022 0.1789 0.1922 -0.0227 -0.0163 -0.0066 160 VAL A CG1 
1327 C  CG2 . VAL A 160 ? 0.2679 0.1480 0.1480 0.0223  0.0509  0.0130  160 VAL A CG2 
1328 N  N   . ASP A 161 ? 0.1947 0.1753 0.1347 -0.0369 -0.0425 -0.0203 161 ASP A N   
1329 C  CA  . ASP A 161 ? 0.2277 0.1950 0.1358 -0.0660 -0.0322 -0.0175 161 ASP A CA  
1330 C  C   . ASP A 161 ? 0.1864 0.2299 0.1436 -0.0401 -0.0168 0.0082  161 ASP A C   
1331 O  O   . ASP A 161 ? 0.3352 0.3262 0.1361 -0.0717 0.0212  -0.0129 161 ASP A O   
1332 C  CB  . ASP A 161 ? 0.2474 0.2899 0.1692 -0.0801 -0.0682 -0.0020 161 ASP A CB  
1333 C  CG  . ASP A 161 ? 0.3158 0.3014 0.2241 -0.0946 -0.0091 -0.0694 161 ASP A CG  
1334 O  OD1 . ASP A 161 ? 0.3629 0.3147 0.2516 -0.1267 -0.0214 0.0050  161 ASP A OD1 
1335 O  OD2 . ASP A 161 ? 0.2694 0.3441 0.2834 -0.0444 -0.0117 -0.0100 161 ASP A OD2 
1336 N  N   . VAL A 162 ? 0.1695 0.1957 0.1343 -0.0313 -0.0341 0.0288  162 VAL A N   
1337 C  CA  . VAL A 162 ? 0.1555 0.2068 0.1666 -0.0179 -0.0003 0.0588  162 VAL A CA  
1338 C  C   . VAL A 162 ? 0.1591 0.1889 0.1271 -0.0314 0.0077  0.0248  162 VAL A C   
1339 O  O   . VAL A 162 ? 0.1608 0.2112 0.1289 -0.0229 0.0179  0.0255  162 VAL A O   
1340 C  CB  . VAL A 162 ? 0.1626 0.1843 0.2500 -0.0078 -0.0427 0.0598  162 VAL A CB  
1341 C  CG1 . VAL A 162 ? 0.2435 0.1433 0.2221 -0.0179 0.0124  0.0170  162 VAL A CG1 
1342 C  CG2 . VAL A 162 ? 0.2435 0.2019 0.2554 0.0021  0.0306  0.0545  162 VAL A CG2 
1343 N  N   . LEU A 163 ? 0.1566 0.1803 0.1177 -0.0001 -0.0199 0.0103  163 LEU A N   
1344 C  CA  . LEU A 163 ? 0.1333 0.1591 0.1160 -0.0143 0.0198  0.0155  163 LEU A CA  
1345 C  C   . LEU A 163 ? 0.1868 0.1781 0.1322 -0.0182 0.0428  0.0010  163 LEU A C   
1346 O  O   . LEU A 163 ? 0.1645 0.1953 0.1296 -0.0081 0.0253  0.0336  163 LEU A O   
1347 C  CB  . LEU A 163 ? 0.1580 0.1534 0.1300 0.0144  0.0168  0.0091  163 LEU A CB  
1348 C  CG  . LEU A 163 ? 0.1820 0.1386 0.1208 -0.0039 0.0296  0.0223  163 LEU A CG  
1349 C  CD1 . LEU A 163 ? 0.1990 0.1810 0.1494 0.0370  0.0104  0.0482  163 LEU A CD1 
1350 C  CD2 . LEU A 163 ? 0.1512 0.1764 0.1379 -0.0073 0.0009  0.0084  163 LEU A CD2 
1351 N  N   . ASP A 164 ? 0.2478 0.1900 0.1252 -0.0141 0.0134  -0.0128 164 ASP A N   
1352 C  CA  . ASP A 164 ? 0.3434 0.2471 0.1213 -0.0520 0.0569  -0.0228 164 ASP A CA  
1353 C  C   . ASP A 164 ? 0.2827 0.2658 0.1022 -0.0121 0.0457  0.0000  164 ASP A C   
1354 O  O   . ASP A 164 ? 0.2927 0.3226 0.2053 0.0074  0.1190  -0.0030 164 ASP A O   
1355 C  CB  . ASP A 164 ? 0.4098 0.3010 0.1803 -0.0781 0.0121  -0.0405 164 ASP A CB  
1356 C  CG  . ASP A 164 ? 0.4192 0.4717 0.2129 -0.1495 -0.0208 -0.0205 164 ASP A CG  
1357 O  OD1 . ASP A 164 ? 0.4762 0.5265 0.3133 -0.1854 0.0018  -0.0491 164 ASP A OD1 
1358 O  OD2 . ASP A 164 ? 0.6533 0.6057 0.2015 -0.1643 0.0578  -0.0389 164 ASP A OD2 
1359 N  N   . SER A 165 ? 0.2001 0.2530 0.0999 -0.0313 -0.0132 0.0183  165 SER A N   
1360 C  CA  . SER A 165 ? 0.2464 0.2392 0.1264 -0.0016 -0.0290 0.0410  165 SER A CA  
1361 C  C   . SER A 165 ? 0.1601 0.2231 0.1262 0.0178  0.0270  0.0358  165 SER A C   
1362 O  O   . SER A 165 ? 0.1904 0.2415 0.1483 -0.0166 0.0210  0.0589  165 SER A O   
1363 C  CB  . SER A 165 ? 0.2763 0.2618 0.1685 0.0070  0.0328  0.0748  165 SER A CB  
1364 O  OG  . SER A 165 ? 0.2342 0.2180 0.2055 -0.0039 -0.0314 0.0433  165 SER A OG  
1365 N  N   . ILE A 166 ? 0.1583 0.2173 0.0934 0.0064  0.0032  0.0104  166 ILE A N   
1366 C  CA  . ILE A 166 ? 0.1523 0.1588 0.1472 0.0078  0.0255  0.0031  166 ILE A CA  
1367 C  C   . ILE A 166 ? 0.1300 0.1584 0.1021 -0.0105 0.0254  0.0185  166 ILE A C   
1368 O  O   . ILE A 166 ? 0.1476 0.1897 0.1051 0.0074  0.0100  0.0218  166 ILE A O   
1369 C  CB  . ILE A 166 ? 0.1706 0.1473 0.1221 -0.0023 0.0353  0.0077  166 ILE A CB  
1370 C  CG1 . ILE A 166 ? 0.1552 0.1516 0.1164 -0.0134 0.0219  0.0109  166 ILE A CG1 
1371 C  CG2 . ILE A 166 ? 0.1523 0.1738 0.1947 0.0069  0.0035  0.0369  166 ILE A CG2 
1372 C  CD1 . ILE A 166 ? 0.1814 0.1717 0.1311 -0.0160 0.0285  -0.0081 166 ILE A CD1 
1373 N  N   . LYS A 167 ? 0.1372 0.1814 0.1094 0.0133  0.0299  0.0146  167 LYS A N   
1374 C  CA  . LYS A 167 ? 0.1242 0.1882 0.1372 0.0093  0.0231  -0.0011 167 LYS A CA  
1375 C  C   . LYS A 167 ? 0.1400 0.1462 0.1128 0.0052  0.0373  0.0132  167 LYS A C   
1376 O  O   . LYS A 167 ? 0.1498 0.1519 0.1274 -0.0041 0.0129  0.0311  167 LYS A O   
1377 C  CB  . LYS A 167 ? 0.1440 0.2015 0.1339 0.0167  0.0239  -0.0009 167 LYS A CB  
1378 C  CG  . LYS A 167 ? 0.2101 0.2029 0.1530 0.0381  0.0092  -0.0137 167 LYS A CG  
1379 C  CD  . LYS A 167 ? 0.2619 0.2864 0.2619 0.0319  -0.0365 -0.1210 167 LYS A CD  
1380 C  CE  . LYS A 167 ? 0.4120 0.2893 0.3886 0.0287  -0.0677 -0.0951 167 LYS A CE  
1381 N  NZ  . LYS A 167 ? 0.4086 0.6646 0.5022 -0.0119 0.0103  -0.2798 167 LYS A NZ  
1382 N  N   . THR A 168 ? 0.1347 0.1652 0.1081 -0.0032 0.0326  0.0217  168 THR A N   
1383 C  CA  . THR A 168 ? 0.1336 0.1541 0.1354 -0.0134 0.0524  0.0275  168 THR A CA  
1384 C  C   . THR A 168 ? 0.1516 0.1289 0.0942 0.0142  0.0517  0.0277  168 THR A C   
1385 O  O   . THR A 168 ? 0.1491 0.1465 0.1415 0.0093  0.0420  0.0353  168 THR A O   
1386 C  CB  . THR A 168 ? 0.1839 0.1630 0.0996 0.0002  0.0487  0.0245  168 THR A CB  
1387 O  OG1 . THR A 168 ? 0.1458 0.2251 0.1361 0.0201  0.0434  0.0436  168 THR A OG1 
1388 C  CG2 . THR A 168 ? 0.1856 0.1821 0.1343 -0.0023 0.0680  -0.0297 168 THR A CG2 
1389 N  N   . LYS A 169 ? 0.1595 0.1705 0.1136 -0.0053 0.0502  0.0186  169 LYS A N   
1390 C  CA  . LYS A 169 ? 0.1216 0.1285 0.1620 0.0016  0.0471  0.0248  169 LYS A CA  
1391 C  C   . LYS A 169 ? 0.1336 0.1436 0.1519 -0.0113 0.0369  0.0429  169 LYS A C   
1392 O  O   . LYS A 169 ? 0.1670 0.2258 0.1591 -0.0308 0.0457  0.0555  169 LYS A O   
1393 C  CB  . LYS A 169 ? 0.1307 0.1771 0.1376 0.0171  0.0368  0.0289  169 LYS A CB  
1394 C  CG  . LYS A 169 ? 0.1645 0.1867 0.1746 -0.0176 0.0320  0.0212  169 LYS A CG  
1395 C  CD  . LYS A 169 ? 0.1649 0.2640 0.2352 -0.0049 0.0754  0.0342  169 LYS A CD  
1396 N  N   . GLY A 170 ? 0.1504 0.1304 0.1785 -0.0026 0.0297  0.0414  170 GLY A N   
1397 C  CA  . GLY A 170 ? 0.1347 0.1537 0.2215 -0.0087 0.0207  0.0697  170 GLY A CA  
1398 C  C   . GLY A 170 ? 0.1422 0.1552 0.2259 0.0086  0.0234  0.0488  170 GLY A C   
1399 O  O   . GLY A 170 ? 0.2099 0.1613 0.2518 -0.0017 0.0156  0.0754  170 GLY A O   
1400 N  N   . LYS A 171 ? 0.1376 0.1656 0.1419 -0.0103 0.0396  0.0508  171 LYS A N   
1401 C  CA  . LYS A 171 ? 0.1401 0.2150 0.1216 -0.0251 0.0359  0.0703  171 LYS A CA  
1402 C  C   . LYS A 171 ? 0.1544 0.1662 0.1182 0.0060  0.0304  0.0567  171 LYS A C   
1403 O  O   . LYS A 171 ? 0.1332 0.2037 0.1146 0.0219  0.0364  0.0608  171 LYS A O   
1404 C  CB  . LYS A 171 ? 0.1512 0.2216 0.1469 -0.0116 0.0408  0.0508  171 LYS A CB  
1405 C  CG  . LYS A 171 ? 0.1343 0.2495 0.2420 0.0194  0.0240  -0.0176 171 LYS A CG  
1406 C  CD  . LYS A 171 ? 0.2807 0.2920 0.2820 0.0418  0.0359  -0.0424 171 LYS A CD  
1407 N  N   . SER A 172 ? 0.1792 0.1932 0.1315 0.0208  0.0286  0.0666  172 SER A N   
1408 C  CA  . SER A 172 ? 0.1634 0.2132 0.1433 0.0160  0.0209  0.0622  172 SER A CA  
1409 C  C   . SER A 172 ? 0.1598 0.1857 0.1134 0.0350  0.0194  0.0548  172 SER A C   
1410 O  O   . SER A 172 ? 0.2011 0.2557 0.1109 0.0436  0.0168  0.0488  172 SER A O   
1411 C  CB  . SER A 172 ? 0.1917 0.2252 0.1512 -0.0113 -0.0133 0.0558  172 SER A CB  
1412 O  OG  . SER A 172 ? 0.2638 0.2100 0.1803 -0.0086 -0.0098 0.0592  172 SER A OG  
1413 N  N   . ALA A 173 ? 0.1408 0.1983 0.1534 0.0239  0.0070  0.0610  173 ALA A N   
1414 C  CA  . ALA A 173 ? 0.1468 0.2349 0.1304 0.0245  0.0067  0.0449  173 ALA A CA  
1415 C  C   . ALA A 173 ? 0.1570 0.2055 0.1318 0.0321  0.0055  0.0477  173 ALA A C   
1416 O  O   . ALA A 173 ? 0.1663 0.1824 0.1181 0.0017  -0.0102 0.0256  173 ALA A O   
1417 C  CB  . ALA A 173 ? 0.2230 0.2392 0.1746 0.0078  0.0314  0.0108  173 ALA A CB  
1418 N  N   . ASP A 174 ? 0.1590 0.2464 0.1347 0.0417  -0.0242 0.0200  174 ASP A N   
1419 C  CA  . ASP A 174 ? 0.1523 0.2601 0.1318 0.0407  -0.0157 0.0326  174 ASP A CA  
1420 C  C   . ASP A 174 ? 0.1394 0.2019 0.1800 0.0480  -0.0206 0.0206  174 ASP A C   
1421 O  O   . ASP A 174 ? 0.1706 0.2534 0.2374 0.0329  -0.0098 -0.0666 174 ASP A O   
1422 C  CB  . ASP A 174 ? 0.2039 0.3697 0.1979 0.1064  -0.0343 0.0599  174 ASP A CB  
1423 C  CG  . ASP A 174 ? 0.5582 0.4324 0.3299 -0.0468 -0.1122 0.1252  174 ASP A CG  
1424 O  OD1 . ASP A 174 ? 0.5587 0.4970 0.4051 -0.1803 -0.1086 0.1539  174 ASP A OD1 
1425 O  OD2 . ASP A 174 ? 0.5404 0.9886 0.3456 -0.1606 -0.0972 0.0027  174 ASP A OD2 
1426 N  N   . PHE A 175 ? 0.1300 0.1530 0.1634 0.0200  0.0011  0.0133  175 PHE A N   
1427 C  CA  . PHE A 175 ? 0.1058 0.1462 0.1742 0.0186  -0.0075 0.0141  175 PHE A CA  
1428 C  C   . PHE A 175 ? 0.1227 0.1028 0.1796 0.0036  -0.0105 0.0293  175 PHE A C   
1429 O  O   . PHE A 175 ? 0.1921 0.2150 0.1968 0.0628  -0.0763 -0.0504 175 PHE A O   
1430 C  CB  . PHE A 175 ? 0.1412 0.1322 0.1972 0.0026  -0.0188 0.0463  175 PHE A CB  
1431 C  CG  . PHE A 175 ? 0.1229 0.1261 0.2258 0.0010  -0.0063 0.0225  175 PHE A CG  
1432 C  CD1 . PHE A 175 ? 0.1800 0.1440 0.1914 -0.0008 0.0136  0.0207  175 PHE A CD1 
1433 C  CD2 . PHE A 175 ? 0.1382 0.1595 0.2233 0.0083  -0.0173 0.0239  175 PHE A CD2 
1434 C  CE1 . PHE A 175 ? 0.2094 0.1230 0.2032 -0.0107 0.0257  0.0054  175 PHE A CE1 
1435 C  CE2 . PHE A 175 ? 0.1297 0.1713 0.2011 0.0083  -0.0232 0.0411  175 PHE A CE2 
1436 C  CZ  . PHE A 175 ? 0.1376 0.1746 0.1940 0.0135  -0.0122 0.0228  175 PHE A CZ  
1437 N  N   . THR A 176 ? 0.1419 0.1702 0.1267 0.0350  0.0082  0.0491  176 THR A N   
1438 C  CA  . THR A 176 ? 0.1065 0.1710 0.1304 0.0244  0.0017  0.0554  176 THR A CA  
1439 C  C   . THR A 176 ? 0.1234 0.1318 0.1053 0.0116  -0.0114 0.0348  176 THR A C   
1440 O  O   . THR A 176 ? 0.1555 0.1570 0.1196 0.0151  -0.0212 0.0114  176 THR A O   
1441 C  CB  . THR A 176 ? 0.1125 0.2043 0.1570 0.0351  0.0135  0.0831  176 THR A CB  
1442 O  OG1 . THR A 176 ? 0.3186 0.2460 0.1251 0.1017  0.0103  0.0641  176 THR A OG1 
1443 C  CG2 . THR A 176 ? 0.1720 0.2308 0.3123 -0.0020 0.0122  0.1511  176 THR A CG2 
1444 N  N   . ASN A 177 ? 0.1274 0.1745 0.0933 0.0061  0.0027  0.0174  177 ASN A N   
1445 C  CA  . ASN A 177 ? 0.1100 0.1770 0.1225 0.0015  -0.0233 0.0420  177 ASN A CA  
1446 C  C   . ASN A 177 ? 0.1300 0.1588 0.1216 0.0022  -0.0174 0.0230  177 ASN A C   
1447 O  O   . ASN A 177 ? 0.1576 0.2047 0.2763 -0.0381 -0.0719 0.0998  177 ASN A O   
1448 C  CB  . ASN A 177 ? 0.1231 0.1731 0.1573 0.0095  -0.0546 0.0475  177 ASN A CB  
1449 C  CG  . ASN A 177 ? 0.1523 0.1720 0.1447 0.0212  -0.0240 0.0412  177 ASN A CG  
1450 O  OD1 . ASN A 177 ? 0.1860 0.1863 0.2055 0.0248  0.0054  0.0200  177 ASN A OD1 
1451 N  ND2 . ASN A 177 ? 0.1810 0.1756 0.1239 0.0012  -0.0313 0.0347  177 ASN A ND2 
1452 N  N   . PHE A 178 ? 0.1286 0.1408 0.0985 -0.0111 -0.0184 0.0401  178 PHE A N   
1453 C  CA  . PHE A 178 ? 0.1282 0.1426 0.1093 -0.0072 -0.0029 0.0482  178 PHE A CA  
1454 C  C   . PHE A 178 ? 0.1372 0.1225 0.1083 -0.0177 -0.0091 0.0345  178 PHE A C   
1455 O  O   . PHE A 178 ? 0.1781 0.1476 0.1199 -0.0428 -0.0094 0.0257  178 PHE A O   
1456 C  CB  . PHE A 178 ? 0.1372 0.1527 0.1236 0.0005  -0.0109 0.0396  178 PHE A CB  
1457 C  CG  . PHE A 178 ? 0.1368 0.1390 0.1397 -0.0238 -0.0127 0.0399  178 PHE A CG  
1458 C  CD1 . PHE A 178 ? 0.1522 0.1389 0.1940 -0.0344 -0.0182 0.0458  178 PHE A CD1 
1459 C  CD2 . PHE A 178 ? 0.1137 0.1720 0.1339 -0.0023 -0.0037 0.0443  178 PHE A CD2 
1460 C  CE1 . PHE A 178 ? 0.1634 0.1412 0.1863 -0.0083 -0.0204 0.0321  178 PHE A CE1 
1461 C  CE2 . PHE A 178 ? 0.1081 0.1677 0.1408 -0.0131 -0.0031 0.0487  178 PHE A CE2 
1462 C  CZ  . PHE A 178 ? 0.1143 0.1667 0.1630 -0.0053 0.0033  0.0163  178 PHE A CZ  
1463 N  N   . ASP A 179 ? 0.1243 0.1397 0.1161 -0.0233 -0.0144 0.0325  179 ASP A N   
1464 C  CA  . ASP A 179 ? 0.1307 0.1867 0.1155 -0.0079 -0.0087 0.0254  179 ASP A CA  
1465 C  C   . ASP A 179 ? 0.1347 0.1401 0.1135 -0.0177 0.0053  0.0325  179 ASP A C   
1466 O  O   . ASP A 179 ? 0.1279 0.1469 0.1468 -0.0190 0.0036  0.0175  179 ASP A O   
1467 C  CB  . ASP A 179 ? 0.1254 0.2270 0.1501 -0.0066 -0.0203 0.0630  179 ASP A CB  
1468 C  CG  . ASP A 179 ? 0.1329 0.2460 0.1717 -0.0041 -0.0036 0.0429  179 ASP A CG  
1469 O  OD1 . ASP A 179 ? 0.1282 0.1846 0.1810 0.0222  0.0066  0.0488  179 ASP A OD1 
1470 O  OD2 . ASP A 179 ? 0.1448 0.4570 0.2713 0.0118  -0.0035 -0.0413 179 ASP A OD2 
1471 N  N   . PRO A 180 ? 0.1151 0.1315 0.1292 -0.0077 -0.0043 0.0175  180 PRO A N   
1472 C  CA  . PRO A 180 ? 0.1101 0.1534 0.1136 -0.0182 -0.0063 0.0316  180 PRO A CA  
1473 C  C   . PRO A 180 ? 0.0986 0.1333 0.1296 -0.0051 0.0027  0.0212  180 PRO A C   
1474 O  O   . PRO A 180 ? 0.1325 0.1389 0.1218 -0.0098 -0.0116 0.0332  180 PRO A O   
1475 C  CB  . PRO A 180 ? 0.0897 0.1764 0.1767 -0.0309 -0.0035 0.0237  180 PRO A CB  
1476 C  CG  . PRO A 180 ? 0.1343 0.1627 0.1304 -0.0156 -0.0050 0.0182  180 PRO A CG  
1477 C  CD  . PRO A 180 ? 0.1594 0.1304 0.1159 -0.0084 -0.0021 0.0107  180 PRO A CD  
1478 N  N   . ARG A 181 ? 0.0968 0.1509 0.1256 -0.0103 0.0087  0.0229  181 ARG A N   
1479 C  CA  . ARG A 181 ? 0.1040 0.1591 0.1458 -0.0168 0.0135  0.0421  181 ARG A CA  
1480 C  C   . ARG A 181 ? 0.0968 0.1620 0.1472 -0.0100 -0.0139 0.0328  181 ARG A C   
1481 O  O   . ARG A 181 ? 0.1074 0.1706 0.1624 0.0116  -0.0026 0.0452  181 ARG A O   
1482 C  CB  . ARG A 181 ? 0.1325 0.1526 0.1821 0.0073  -0.0074 0.0352  181 ARG A CB  
1483 C  CG  . ARG A 181 ? 0.1537 0.1570 0.1942 -0.0234 -0.0137 0.0241  181 ARG A CG  
1484 C  CD  . ARG A 181 ? 0.1595 0.1950 0.2019 0.0003  0.0275  0.0279  181 ARG A CD  
1485 N  NE  . ARG A 181 ? 0.1534 0.1929 0.2119 0.0113  0.0334  0.0590  181 ARG A NE  
1486 C  CZ  . ARG A 181 ? 0.1792 0.2244 0.2360 0.0321  0.0080  0.0375  181 ARG A CZ  
1487 N  NH1 . ARG A 181 ? 0.2108 0.2712 0.3474 0.0562  0.0392  0.0039  181 ARG A NH1 
1488 N  NH2 . ARG A 181 ? 0.2014 0.3114 0.2568 0.0312  0.0111  0.0782  181 ARG A NH2 
1489 N  N   . GLY A 182 ? 0.1236 0.1443 0.1559 0.0098  -0.0294 0.0152  182 GLY A N   
1490 C  CA  . GLY A 182 ? 0.1419 0.1347 0.1516 -0.0179 -0.0274 0.0277  182 GLY A CA  
1491 C  C   . GLY A 182 ? 0.1304 0.1336 0.1501 -0.0095 -0.0144 0.0177  182 GLY A C   
1492 O  O   . GLY A 182 ? 0.1850 0.1336 0.2205 -0.0077 -0.0766 0.0029  182 GLY A O   
1493 N  N   . LEU A 183 ? 0.1164 0.1361 0.1386 -0.0024 -0.0265 0.0120  183 LEU A N   
1494 C  CA  . LEU A 183 ? 0.1168 0.1490 0.1336 0.0027  -0.0138 0.0168  183 LEU A CA  
1495 C  C   . LEU A 183 ? 0.1324 0.1116 0.1282 -0.0119 -0.0163 0.0074  183 LEU A C   
1496 O  O   . LEU A 183 ? 0.1649 0.1619 0.1540 0.0114  -0.0268 0.0456  183 LEU A O   
1497 C  CB  . LEU A 183 ? 0.1047 0.1688 0.1346 0.0004  -0.0132 0.0296  183 LEU A CB  
1498 C  CG  . LEU A 183 ? 0.1400 0.1914 0.1257 0.0192  0.0021  0.0184  183 LEU A CG  
1499 C  CD1 . LEU A 183 ? 0.1663 0.2407 0.1734 -0.0010 -0.0020 0.0715  183 LEU A CD1 
1500 C  CD2 . LEU A 183 ? 0.2288 0.2076 0.1551 0.0496  0.0070  -0.0140 183 LEU A CD2 
1501 N  N   . LEU A 184 ? 0.1270 0.1328 0.1311 -0.0025 0.0060  0.0223  184 LEU A N   
1502 C  CA  . LEU A 184 ? 0.1448 0.1462 0.1397 -0.0411 -0.0177 0.0496  184 LEU A CA  
1503 C  C   . LEU A 184 ? 0.1322 0.1785 0.1577 -0.0663 -0.0341 0.0641  184 LEU A C   
1504 O  O   . LEU A 184 ? 0.2203 0.2586 0.2636 -0.1240 -0.1393 0.1283  184 LEU A O   
1505 C  CB  . LEU A 184 ? 0.1182 0.1637 0.1856 -0.0253 0.0029  0.0367  184 LEU A CB  
1506 C  CG  . LEU A 184 ? 0.0960 0.1742 0.2115 -0.0064 0.0135  0.0447  184 LEU A CG  
1507 C  CD1 . LEU A 184 ? 0.1476 0.2231 0.2065 0.0151  0.0301  0.0152  184 LEU A CD1 
1508 C  CD2 . LEU A 184 ? 0.1155 0.2001 0.3191 -0.0076 -0.0282 -0.0208 184 LEU A CD2 
1509 N  N   . PRO A 185 ? 0.1170 0.1335 0.1314 -0.0229 -0.0104 0.0288  185 PRO A N   
1510 C  CA  . PRO A 185 ? 0.1037 0.1447 0.1674 -0.0146 -0.0054 0.0553  185 PRO A CA  
1511 C  C   . PRO A 185 ? 0.0841 0.1652 0.1828 -0.0203 -0.0401 0.0589  185 PRO A C   
1512 O  O   . PRO A 185 ? 0.0803 0.1584 0.2471 -0.0166 -0.0217 0.0499  185 PRO A O   
1513 C  CB  . PRO A 185 ? 0.1089 0.1688 0.1386 -0.0051 -0.0114 0.0261  185 PRO A CB  
1514 C  CG  . PRO A 185 ? 0.1060 0.1505 0.1469 0.0037  -0.0055 0.0292  185 PRO A CG  
1515 C  CD  . PRO A 185 ? 0.0750 0.1692 0.1153 0.0069  0.0040  0.0122  185 PRO A CD  
1516 N  N   A GLU A 186 ? 0.1033 0.1597 0.1856 -0.0276 -0.0170 0.0579  186 GLU A N   
1517 N  N   B GLU A 186 ? 0.0750 0.2008 0.2142 -0.0572 -0.0308 0.0516  186 GLU A N   
1518 C  CA  A GLU A 186 ? 0.0893 0.2008 0.1904 -0.0299 -0.0154 0.0548  186 GLU A CA  
1519 C  CA  B GLU A 186 ? 0.1006 0.1954 0.1950 -0.0201 -0.0296 0.0709  186 GLU A CA  
1520 C  C   A GLU A 186 ? 0.1083 0.1397 0.1954 -0.0054 -0.0017 0.0441  186 GLU A C   
1521 C  C   B GLU A 186 ? 0.1048 0.1509 0.1960 -0.0205 -0.0108 0.0594  186 GLU A C   
1522 O  O   A GLU A 186 ? 0.0371 0.1871 0.2342 0.0273  0.0021  0.0267  186 GLU A O   
1523 O  O   B GLU A 186 ? 0.1583 0.2293 0.2712 0.0727  -0.0114 0.0369  186 GLU A O   
1524 C  CB  A GLU A 186 ? 0.1279 0.1760 0.2548 -0.0537 -0.0247 0.0113  186 GLU A CB  
1525 C  CB  B GLU A 186 ? 0.1602 0.1997 0.2590 -0.0414 -0.0194 0.0438  186 GLU A CB  
1526 C  CG  A GLU A 186 ? 0.1997 0.1523 0.3143 -0.0686 -0.0824 0.0168  186 GLU A CG  
1527 C  CG  B GLU A 186 ? 0.1547 0.2165 0.3258 0.0185  -0.0134 0.0604  186 GLU A CG  
1528 C  CD  A GLU A 186 ? 0.2331 0.1089 0.3444 -0.0055 -0.0621 0.0736  186 GLU A CD  
1529 C  CD  B GLU A 186 ? 0.1432 0.2266 0.3689 0.0363  0.0501  0.0770  186 GLU A CD  
1530 O  OE1 A GLU A 186 ? 0.2680 0.2366 0.4200 -0.0829 -0.0476 0.0273  186 GLU A OE1 
1531 O  OE1 B GLU A 186 ? 0.2349 0.3028 0.4767 0.0324  0.0982  0.0144  186 GLU A OE1 
1532 O  OE2 A GLU A 186 ? 0.2240 0.2421 0.3377 -0.0844 -0.0842 0.0416  186 GLU A OE2 
1533 O  OE2 B GLU A 186 ? 0.2787 0.3154 0.4022 0.0335  0.1314  0.1678  186 GLU A OE2 
1534 N  N   . SER A 187 ? 0.0638 0.1832 0.1782 -0.0174 -0.0064 0.0375  187 SER A N   
1535 C  CA  . SER A 187 ? 0.0726 0.1943 0.1745 -0.0107 0.0109  0.0457  187 SER A CA  
1536 C  C   . SER A 187 ? 0.0724 0.1910 0.1644 -0.0179 0.0121  0.0225  187 SER A C   
1537 O  O   . SER A 187 ? 0.0938 0.2241 0.1716 -0.0240 0.0232  -0.0117 187 SER A O   
1538 C  CB  . SER A 187 ? 0.1241 0.2051 0.1529 0.0058  0.0111  0.0391  187 SER A CB  
1539 O  OG  . SER A 187 ? 0.1248 0.2308 0.1717 -0.0155 0.0125  0.0249  187 SER A OG  
1540 N  N   . LEU A 188 ? 0.0706 0.1717 0.2019 -0.0036 -0.0061 0.0098  188 LEU A N   
1541 C  CA  . LEU A 188 ? 0.0941 0.1893 0.2143 -0.0231 -0.0302 0.0077  188 LEU A CA  
1542 C  C   . LEU A 188 ? 0.0780 0.1911 0.1785 -0.0152 0.0111  0.0031  188 LEU A C   
1543 O  O   . LEU A 188 ? 0.1248 0.2169 0.1932 -0.0328 -0.0005 -0.0299 188 LEU A O   
1544 C  CB  . LEU A 188 ? 0.1379 0.1800 0.2960 -0.0138 -0.0326 0.0054  188 LEU A CB  
1545 C  CG  . LEU A 188 ? 0.1318 0.2195 0.2957 0.0237  0.0247  0.0387  188 LEU A CG  
1546 C  CD1 . LEU A 188 ? 0.1566 0.1950 0.4185 0.0230  -0.0080 0.1035  188 LEU A CD1 
1547 C  CD2 . LEU A 188 ? 0.1408 0.2665 0.2073 -0.0031 0.0089  0.0482  188 LEU A CD2 
1548 N  N   . ASP A 189 ? 0.0647 0.2072 0.1782 0.0079  0.0330  0.0192  189 ASP A N   
1549 C  CA  . ASP A 189 ? 0.0697 0.2319 0.1670 -0.0036 0.0316  -0.0186 189 ASP A CA  
1550 C  C   . ASP A 189 ? 0.0715 0.1670 0.1361 -0.0075 0.0222  -0.0216 189 ASP A C   
1551 O  O   . ASP A 189 ? 0.0681 0.1608 0.1282 -0.0036 0.0165  -0.0003 189 ASP A O   
1552 C  CB  . ASP A 189 ? 0.1738 0.2737 0.1523 -0.0444 -0.0212 0.0142  189 ASP A CB  
1553 C  CG  . ASP A 189 ? 0.2081 0.3559 0.2284 -0.0356 -0.0108 -0.0053 189 ASP A CG  
1554 O  OD1 . ASP A 189 ? 0.1893 0.4295 0.2683 -0.0373 0.0804  -0.0740 189 ASP A OD1 
1555 O  OD2 . ASP A 189 ? 0.2057 0.5315 0.2495 -0.1641 0.0425  0.0877  189 ASP A OD2 
1556 N  N   . TYR A 190 ? 0.0697 0.1562 0.1286 -0.0102 0.0268  0.0030  190 TYR A N   
1557 C  CA  . TYR A 190 ? 0.0696 0.1483 0.1300 -0.0197 0.0161  0.0167  190 TYR A CA  
1558 C  C   . TYR A 190 ? 0.0787 0.1315 0.1011 -0.0051 0.0333  -0.0122 190 TYR A C   
1559 O  O   . TYR A 190 ? 0.0911 0.1666 0.0969 -0.0024 0.0460  0.0047  190 TYR A O   
1560 C  CB  . TYR A 190 ? 0.0791 0.1328 0.1318 -0.0044 0.0294  -0.0003 190 TYR A CB  
1561 C  CG  . TYR A 190 ? 0.0886 0.1379 0.1198 -0.0038 0.0206  0.0091  190 TYR A CG  
1562 C  CD1 . TYR A 190 ? 0.1150 0.1462 0.1266 -0.0346 0.0206  0.0000  190 TYR A CD1 
1563 C  CD2 . TYR A 190 ? 0.1027 0.1372 0.1390 0.0238  0.0375  0.0146  190 TYR A CD2 
1564 C  CE1 . TYR A 190 ? 0.1133 0.1208 0.1533 -0.0110 0.0201  0.0152  190 TYR A CE1 
1565 C  CE2 . TYR A 190 ? 0.1169 0.1404 0.1673 0.0095  0.0175  -0.0050 190 TYR A CE2 
1566 C  CZ  . TYR A 190 ? 0.1254 0.1519 0.1451 -0.0050 0.0259  0.0152  190 TYR A CZ  
1567 O  OH  . TYR A 190 ? 0.1667 0.1573 0.1705 -0.0012 0.0208  -0.0109 190 TYR A OH  
1568 N  N   . TRP A 191 ? 0.0680 0.1231 0.1171 -0.0100 0.0147  -0.0197 191 TRP A N   
1569 C  CA  . TRP A 191 ? 0.0715 0.1275 0.1107 -0.0158 0.0149  -0.0048 191 TRP A CA  
1570 C  C   . TRP A 191 ? 0.0803 0.1272 0.0697 0.0004  0.0234  -0.0088 191 TRP A C   
1571 O  O   . TRP A 191 ? 0.1196 0.1509 0.0662 -0.0133 0.0196  -0.0119 191 TRP A O   
1572 C  CB  . TRP A 191 ? 0.0965 0.1272 0.1259 0.0019  0.0267  -0.0086 191 TRP A CB  
1573 C  CG  . TRP A 191 ? 0.0884 0.1258 0.1248 0.0079  0.0259  -0.0006 191 TRP A CG  
1574 C  CD1 . TRP A 191 ? 0.1173 0.1304 0.1279 0.0107  0.0267  0.0046  191 TRP A CD1 
1575 C  CD2 . TRP A 191 ? 0.0907 0.1223 0.1307 0.0117  0.0141  0.0092  191 TRP A CD2 
1576 N  NE1 . TRP A 191 ? 0.1408 0.1425 0.1329 -0.0078 0.0189  0.0038  191 TRP A NE1 
1577 C  CE2 . TRP A 191 ? 0.1137 0.1164 0.1468 0.0100  0.0036  0.0120  191 TRP A CE2 
1578 C  CE3 . TRP A 191 ? 0.0811 0.1518 0.1401 0.0035  0.0024  0.0020  191 TRP A CE3 
1579 C  CZ2 . TRP A 191 ? 0.1164 0.1264 0.1624 0.0105  0.0062  0.0078  191 TRP A CZ2 
1580 C  CZ3 . TRP A 191 ? 0.0723 0.1584 0.1741 -0.0009 0.0184  -0.0091 191 TRP A CZ3 
1581 C  CH2 . TRP A 191 ? 0.0920 0.1551 0.1800 0.0069  0.0158  -0.0029 191 TRP A CH2 
1582 N  N   . THR A 192 ? 0.0829 0.1157 0.0979 -0.0034 0.0072  -0.0100 192 THR A N   
1583 C  CA  . THR A 192 ? 0.0837 0.1188 0.1125 -0.0109 0.0032  -0.0088 192 THR A CA  
1584 C  C   . THR A 192 ? 0.0759 0.1268 0.0780 0.0089  0.0242  -0.0110 192 THR A C   
1585 O  O   . THR A 192 ? 0.0956 0.1408 0.0791 0.0048  0.0108  -0.0044 192 THR A O   
1586 C  CB  . THR A 192 ? 0.0997 0.1241 0.0958 0.0131  0.0244  -0.0020 192 THR A CB  
1587 O  OG1 . THR A 192 ? 0.0873 0.1311 0.1190 0.0134  0.0216  -0.0044 192 THR A OG1 
1588 C  CG2 . THR A 192 ? 0.1190 0.1498 0.0985 0.0298  0.0308  -0.0097 192 THR A CG2 
1589 N  N   . TYR A 193 ? 0.0671 0.1216 0.0950 0.0089  0.0177  -0.0126 193 TYR A N   
1590 C  CA  . TYR A 193 ? 0.0774 0.1340 0.1120 0.0248  0.0082  -0.0157 193 TYR A CA  
1591 C  C   . TYR A 193 ? 0.1011 0.1094 0.0863 0.0122  0.0164  -0.0384 193 TYR A C   
1592 O  O   . TYR A 193 ? 0.0977 0.1173 0.0837 0.0110  0.0096  -0.0257 193 TYR A O   
1593 C  CB  . TYR A 193 ? 0.1160 0.1220 0.0792 0.0332  0.0087  -0.0097 193 TYR A CB  
1594 C  CG  . TYR A 193 ? 0.0848 0.1124 0.0807 0.0067  0.0078  0.0037  193 TYR A CG  
1595 C  CD1 . TYR A 193 ? 0.0977 0.0988 0.0798 0.0144  0.0137  -0.0111 193 TYR A CD1 
1596 C  CD2 . TYR A 193 ? 0.0814 0.1169 0.0976 0.0159  0.0203  0.0066  193 TYR A CD2 
1597 C  CE1 . TYR A 193 ? 0.0677 0.0956 0.0950 0.0125  0.0286  0.0053  193 TYR A CE1 
1598 C  CE2 . TYR A 193 ? 0.0943 0.1289 0.0927 0.0054  0.0051  -0.0136 193 TYR A CE2 
1599 C  CZ  . TYR A 193 ? 0.0672 0.0882 0.0820 0.0115  0.0134  -0.0089 193 TYR A CZ  
1600 O  OH  . TYR A 193 ? 0.0854 0.0900 0.0963 -0.0037 0.0241  -0.0077 193 TYR A OH  
1601 N  N   . PRO A 194 ? 0.0891 0.1232 0.0945 0.0127  0.0102  -0.0340 194 PRO A N   
1602 C  CA  . PRO A 194 ? 0.0979 0.1124 0.1102 0.0104  0.0158  -0.0416 194 PRO A CA  
1603 C  C   . PRO A 194 ? 0.0740 0.1058 0.1006 0.0134  -0.0062 -0.0309 194 PRO A C   
1604 O  O   . PRO A 194 ? 0.0942 0.1329 0.0961 0.0250  0.0064  -0.0214 194 PRO A O   
1605 C  CB  . PRO A 194 ? 0.1248 0.1597 0.1343 0.0102  0.0148  -0.0781 194 PRO A CB  
1606 C  CG  . PRO A 194 ? 0.1143 0.1971 0.1454 -0.0200 0.0133  -0.0475 194 PRO A CG  
1607 C  CD  . PRO A 194 ? 0.1128 0.2116 0.0886 -0.0134 0.0063  -0.0498 194 PRO A CD  
1608 N  N   . GLY A 195 ? 0.0741 0.1170 0.0959 -0.0048 0.0179  -0.0294 195 GLY A N   
1609 C  CA  . GLY A 195 ? 0.0697 0.1073 0.1160 0.0092  0.0216  0.0037  195 GLY A CA  
1610 C  C   . GLY A 195 ? 0.0584 0.0853 0.1139 0.0026  -0.0071 0.0036  195 GLY A C   
1611 O  O   . GLY A 195 ? 0.0863 0.0864 0.1163 -0.0105 0.0137  -0.0089 195 GLY A O   
1612 N  N   . SER A 196 ? 0.0638 0.1040 0.1223 -0.0058 0.0179  -0.0127 196 SER A N   
1613 C  CA  . SER A 196 ? 0.0653 0.0967 0.1023 -0.0048 0.0175  -0.0082 196 SER A CA  
1614 C  C   . SER A 196 ? 0.0600 0.0889 0.1085 -0.0103 0.0081  -0.0010 196 SER A C   
1615 O  O   . SER A 196 ? 0.0566 0.0999 0.1058 -0.0062 0.0034  -0.0066 196 SER A O   
1616 C  CB  . SER A 196 ? 0.0671 0.1062 0.1267 0.0041  0.0166  -0.0255 196 SER A CB  
1617 O  OG  . SER A 196 ? 0.0507 0.0926 0.1376 0.0055  0.0036  -0.0077 196 SER A OG  
1618 N  N   . LEU A 197 ? 0.0643 0.1058 0.1015 -0.0004 0.0068  -0.0027 197 LEU A N   
1619 C  CA  . LEU A 197 ? 0.0826 0.0916 0.1006 -0.0039 0.0073  -0.0006 197 LEU A CA  
1620 C  C   . LEU A 197 ? 0.0602 0.0895 0.1225 -0.0178 0.0015  0.0080  197 LEU A C   
1621 O  O   . LEU A 197 ? 0.0656 0.1084 0.1107 -0.0043 0.0012  -0.0135 197 LEU A O   
1622 C  CB  . LEU A 197 ? 0.0838 0.1073 0.1259 -0.0050 0.0273  0.0027  197 LEU A CB  
1623 C  CG  . LEU A 197 ? 0.1014 0.0994 0.1408 -0.0182 0.0210  0.0059  197 LEU A CG  
1624 C  CD1 . LEU A 197 ? 0.1032 0.1311 0.1846 -0.0125 0.0214  0.0304  197 LEU A CD1 
1625 C  CD2 . LEU A 197 ? 0.0832 0.1286 0.2064 0.0013  0.0374  0.0462  197 LEU A CD2 
1626 N  N   . THR A 198 ? 0.0647 0.0818 0.1248 -0.0118 0.0000  -0.0025 198 THR A N   
1627 C  CA  . THR A 198 ? 0.0685 0.0899 0.1229 0.0002  0.0240  -0.0137 198 THR A CA  
1628 C  C   . THR A 198 ? 0.0645 0.0979 0.1067 -0.0050 0.0141  -0.0158 198 THR A C   
1629 O  O   . THR A 198 ? 0.0653 0.1120 0.1415 0.0017  0.0216  -0.0283 198 THR A O   
1630 C  CB  . THR A 198 ? 0.0787 0.0970 0.0805 -0.0130 0.0168  0.0032  198 THR A CB  
1631 O  OG1 . THR A 198 ? 0.0632 0.0943 0.0972 0.0029  0.0073  0.0071  198 THR A OG1 
1632 C  CG2 . THR A 198 ? 0.0836 0.1143 0.0978 -0.0084 0.0339  -0.0067 198 THR A CG2 
1633 N  N   . THR A 199 ? 0.0619 0.1347 0.1108 -0.0094 0.0239  0.0082  199 THR A N   
1634 C  CA  . THR A 199 ? 0.0899 0.1465 0.1148 -0.0258 0.0361  -0.0062 199 THR A CA  
1635 C  C   . THR A 199 ? 0.0902 0.1666 0.1216 -0.0414 0.0271  -0.0037 199 THR A C   
1636 O  O   . THR A 199 ? 0.0765 0.1473 0.1233 -0.0277 0.0201  0.0125  199 THR A O   
1637 C  CB  . THR A 199 ? 0.1169 0.2112 0.1164 -0.0364 0.0179  -0.0329 199 THR A CB  
1638 O  OG1 . THR A 199 ? 0.4137 0.1522 0.1929 -0.0449 -0.1268 0.0317  199 THR A OG1 
1639 C  CG2 . THR A 199 ? 0.1458 0.1386 0.1199 -0.0114 -0.0098 -0.0163 199 THR A CG2 
1640 N  N   . PRO A 200 ? 0.0841 0.1619 0.1426 -0.0329 0.0316  0.0105  200 PRO A N   
1641 C  CA  . PRO A 200 ? 0.0747 0.1785 0.1620 -0.0397 0.0358  0.0302  200 PRO A CA  
1642 C  C   . PRO A 200 ? 0.0800 0.1868 0.1437 -0.0424 0.0161  0.0209  200 PRO A C   
1643 O  O   . PRO A 200 ? 0.0935 0.2313 0.1329 -0.0346 0.0138  0.0296  200 PRO A O   
1644 C  CB  . PRO A 200 ? 0.0708 0.2313 0.1645 -0.0212 0.0304  0.0345  200 PRO A CB  
1645 C  CG  . PRO A 200 ? 0.0970 0.2169 0.1875 -0.0356 0.0372  -0.0100 200 PRO A CG  
1646 C  CD  . PRO A 200 ? 0.0765 0.2068 0.1615 -0.0144 0.0381  -0.0100 200 PRO A CD  
1647 N  N   . PRO A 201 ? 0.0880 0.1799 0.1408 -0.0346 0.0006  0.0359  201 PRO A N   
1648 C  CA  . PRO A 201 ? 0.0850 0.1552 0.1491 -0.0295 0.0077  0.0251  201 PRO A CA  
1649 C  C   . PRO A 201 ? 0.0776 0.1390 0.1429 -0.0236 -0.0032 0.0251  201 PRO A C   
1650 O  O   . PRO A 201 ? 0.0884 0.1548 0.1580 -0.0414 0.0023  -0.0001 201 PRO A O   
1651 C  CB  . PRO A 201 ? 0.1300 0.1429 0.1839 -0.0436 0.0253  0.0482  201 PRO A CB  
1652 C  CG  . PRO A 201 ? 0.1580 0.1742 0.2417 -0.0355 -0.0325 0.0296  201 PRO A CG  
1653 C  CD  . PRO A 201 ? 0.1015 0.1724 0.2007 -0.0229 0.0148  0.0352  201 PRO A CD  
1654 N  N   . LEU A 202 ? 0.0672 0.1181 0.1473 -0.0105 0.0223  0.0179  202 LEU A N   
1655 C  CA  . LEU A 202 ? 0.0641 0.1173 0.1346 -0.0061 0.0176  0.0078  202 LEU A CA  
1656 C  C   . LEU A 202 ? 0.0446 0.1030 0.1487 -0.0258 0.0176  -0.0023 202 LEU A C   
1657 O  O   . LEU A 202 ? 0.0713 0.1270 0.1401 -0.0088 0.0085  -0.0044 202 LEU A O   
1658 C  CB  . LEU A 202 ? 0.0629 0.1340 0.1350 0.0055  0.0075  -0.0057 202 LEU A CB  
1659 C  CG  . LEU A 202 ? 0.0563 0.1322 0.1404 0.0009  0.0153  -0.0088 202 LEU A CG  
1660 C  CD1 . LEU A 202 ? 0.0460 0.1685 0.1767 -0.0052 0.0089  -0.0158 202 LEU A CD1 
1661 C  CD2 . LEU A 202 ? 0.0695 0.1358 0.1347 -0.0096 0.0096  0.0047  202 LEU A CD2 
1662 N  N   . THR A 203 ? 0.0864 0.1067 0.1749 -0.0111 0.0245  0.0074  203 THR A N   
1663 C  CA  . THR A 203 ? 0.0802 0.1171 0.2008 -0.0137 0.0335  0.0000  203 THR A CA  
1664 C  C   . THR A 203 ? 0.0612 0.1166 0.1620 -0.0084 0.0188  -0.0041 203 THR A C   
1665 O  O   . THR A 203 ? 0.0672 0.1120 0.1458 -0.0115 0.0085  -0.0116 203 THR A O   
1666 C  CB  . THR A 203 ? 0.1659 0.1060 0.2356 -0.0215 0.0759  0.0324  203 THR A CB  
1667 O  OG1 . THR A 203 ? 0.1472 0.1394 0.2595 -0.0201 0.0736  0.0379  203 THR A OG1 
1668 C  CG2 . THR A 203 ? 0.1519 0.1195 0.2918 0.0063  0.0465  -0.0096 203 THR A CG2 
1669 N  N   . GLU A 204 ? 0.1021 0.1130 0.1703 -0.0125 -0.0100 -0.0352 204 GLU A N   
1670 C  CA  . GLU A 204 ? 0.0760 0.1297 0.1839 0.0002  -0.0074 -0.0229 204 GLU A CA  
1671 C  C   . GLU A 204 ? 0.0839 0.1058 0.1713 -0.0143 -0.0218 -0.0486 204 GLU A C   
1672 O  O   . GLU A 204 ? 0.1663 0.1649 0.1864 0.0379  -0.0588 -0.0898 204 GLU A O   
1673 C  CB  . GLU A 204 ? 0.1120 0.1155 0.1806 0.0137  -0.0295 -0.0314 204 GLU A CB  
1674 C  CG  . GLU A 204 ? 0.0996 0.1358 0.1687 0.0222  -0.0168 -0.0240 204 GLU A CG  
1675 C  CD  . GLU A 204 ? 0.1005 0.1746 0.1803 0.0188  -0.0303 -0.0409 204 GLU A CD  
1676 O  OE1 . GLU A 204 ? 0.1282 0.1857 0.2317 0.0151  -0.0715 -0.0533 204 GLU A OE1 
1677 O  OE2 . GLU A 204 ? 0.0846 0.1516 0.1498 -0.0052 -0.0085 -0.0226 204 GLU A OE2 
1678 N  N   . CYS A 205 ? 0.0751 0.0907 0.1300 -0.0154 -0.0003 -0.0319 205 CYS A N   
1679 C  CA  . CYS A 205 ? 0.0647 0.1209 0.1153 0.0024  0.0212  -0.0027 205 CYS A CA  
1680 C  C   . CYS A 205 ? 0.0756 0.0911 0.1084 0.0111  0.0109  -0.0221 205 CYS A C   
1681 O  O   . CYS A 205 ? 0.0920 0.0938 0.1771 0.0001  -0.0150 0.0032  205 CYS A O   
1682 C  CB  . CYS A 205 ? 0.0988 0.1340 0.1204 -0.0118 0.0159  0.0037  205 CYS A CB  
1683 S  SG  . CYS A 205 ? 0.1325 0.1627 0.1368 0.0230  0.0058  -0.0312 205 CYS A SG  
1684 N  N   . VAL A 206 ? 0.0634 0.0999 0.1204 -0.0065 0.0006  -0.0134 206 VAL A N   
1685 C  CA  . VAL A 206 ? 0.0678 0.0917 0.1152 -0.0063 -0.0089 -0.0126 206 VAL A CA  
1686 C  C   . VAL A 206 ? 0.0768 0.0753 0.1430 -0.0042 -0.0003 0.0069  206 VAL A C   
1687 O  O   . VAL A 206 ? 0.0875 0.1094 0.1433 0.0055  -0.0136 0.0113  206 VAL A O   
1688 C  CB  . VAL A 206 ? 0.0753 0.1055 0.1351 -0.0140 0.0125  -0.0316 206 VAL A CB  
1689 C  CG1 . VAL A 206 ? 0.0821 0.1073 0.1293 0.0037  -0.0276 -0.0272 206 VAL A CG1 
1690 C  CG2 . VAL A 206 ? 0.0870 0.1171 0.1372 0.0131  0.0109  -0.0172 206 VAL A CG2 
1691 N  N   . THR A 207 ? 0.0724 0.0853 0.1242 -0.0027 0.0033  -0.0071 207 THR A N   
1692 C  CA  . THR A 207 ? 0.0893 0.0900 0.1141 -0.0072 0.0166  -0.0237 207 THR A CA  
1693 C  C   . THR A 207 ? 0.0785 0.0841 0.0920 -0.0086 0.0175  -0.0087 207 THR A C   
1694 O  O   . THR A 207 ? 0.0902 0.0997 0.1023 0.0019  0.0044  -0.0073 207 THR A O   
1695 C  CB  . THR A 207 ? 0.0927 0.0817 0.1340 0.0017  0.0127  -0.0121 207 THR A CB  
1696 O  OG1 . THR A 207 ? 0.1187 0.0934 0.1404 -0.0058 0.0273  -0.0290 207 THR A OG1 
1697 C  CG2 . THR A 207 ? 0.0941 0.1195 0.1705 -0.0141 0.0332  0.0013  207 THR A CG2 
1698 N  N   . TRP A 208 ? 0.0638 0.0789 0.1012 -0.0012 0.0220  -0.0160 208 TRP A N   
1699 C  CA  . TRP A 208 ? 0.0697 0.0791 0.0934 0.0027  0.0145  -0.0139 208 TRP A CA  
1700 C  C   . TRP A 208 ? 0.0712 0.0859 0.0740 0.0107  0.0163  0.0037  208 TRP A C   
1701 O  O   . TRP A 208 ? 0.0841 0.1103 0.0785 0.0034  0.0194  0.0006  208 TRP A O   
1702 C  CB  . TRP A 208 ? 0.0714 0.1098 0.0818 0.0209  0.0133  0.0099  208 TRP A CB  
1703 C  CG  . TRP A 208 ? 0.0621 0.0751 0.0969 0.0038  0.0062  0.0010  208 TRP A CG  
1704 C  CD1 . TRP A 208 ? 0.0687 0.0807 0.1412 0.0065  0.0164  -0.0120 208 TRP A CD1 
1705 C  CD2 . TRP A 208 ? 0.0550 0.0776 0.1075 0.0121  0.0131  0.0057  208 TRP A CD2 
1706 N  NE1 . TRP A 208 ? 0.0651 0.1004 0.1364 0.0059  0.0153  -0.0005 208 TRP A NE1 
1707 C  CE2 . TRP A 208 ? 0.0674 0.0814 0.1181 0.0049  0.0297  0.0033  208 TRP A CE2 
1708 C  CE3 . TRP A 208 ? 0.0848 0.0742 0.0900 0.0227  0.0012  -0.0069 208 TRP A CE3 
1709 C  CZ2 . TRP A 208 ? 0.0952 0.0850 0.1239 0.0147  0.0328  0.0069  208 TRP A CZ2 
1710 C  CZ3 . TRP A 208 ? 0.1102 0.0881 0.0893 0.0228  0.0266  0.0134  208 TRP A CZ3 
1711 C  CH2 . TRP A 208 ? 0.1199 0.0830 0.1200 0.0156  0.0223  -0.0013 208 TRP A CH2 
1712 N  N   . ILE A 209 ? 0.0656 0.0856 0.0952 0.0001  0.0137  0.0020  209 ILE A N   
1713 C  CA  . ILE A 209 ? 0.0636 0.0914 0.1005 0.0011  0.0179  0.0021  209 ILE A CA  
1714 C  C   . ILE A 209 ? 0.0626 0.0902 0.0846 0.0096  0.0005  0.0086  209 ILE A C   
1715 O  O   . ILE A 209 ? 0.1094 0.0997 0.0775 -0.0008 0.0092  0.0066  209 ILE A O   
1716 C  CB  . ILE A 209 ? 0.0701 0.1036 0.1204 0.0142  0.0135  -0.0096 209 ILE A CB  
1717 C  CG1 . ILE A 209 ? 0.0741 0.0949 0.1652 0.0189  0.0215  -0.0296 209 ILE A CG1 
1718 C  CG2 . ILE A 209 ? 0.0650 0.1412 0.1408 0.0137  0.0234  0.0022  209 ILE A CG2 
1719 C  CD1 . ILE A 209 ? 0.1186 0.1262 0.2540 0.0469  -0.0111 -0.0033 209 ILE A CD1 
1720 N  N   . VAL A 210 ? 0.0688 0.0785 0.0906 0.0178  0.0140  0.0025  210 VAL A N   
1721 C  CA  . VAL A 210 ? 0.0636 0.0875 0.0954 0.0060  0.0088  -0.0026 210 VAL A CA  
1722 C  C   . VAL A 210 ? 0.0602 0.0988 0.0891 0.0083  0.0207  -0.0070 210 VAL A C   
1723 O  O   . VAL A 210 ? 0.0880 0.1089 0.0891 -0.0119 0.0264  -0.0035 210 VAL A O   
1724 C  CB  . VAL A 210 ? 0.0538 0.0972 0.1209 0.0054  0.0124  0.0020  210 VAL A CB  
1725 C  CG1 . VAL A 210 ? 0.0990 0.0846 0.1473 0.0071  0.0070  -0.0070 210 VAL A CG1 
1726 C  CG2 . VAL A 210 ? 0.0660 0.1142 0.1504 -0.0146 0.0044  0.0061  210 VAL A CG2 
1727 N  N   . LEU A 211 ? 0.0644 0.1103 0.1076 -0.0116 0.0010  0.0005  211 LEU A N   
1728 C  CA  . LEU A 211 ? 0.0608 0.1115 0.1120 -0.0108 0.0066  0.0010  211 LEU A CA  
1729 C  C   . LEU A 211 ? 0.0927 0.1101 0.1093 -0.0164 0.0145  0.0027  211 LEU A C   
1730 O  O   . LEU A 211 ? 0.0873 0.1143 0.1058 -0.0206 0.0102  0.0022  211 LEU A O   
1731 C  CB  . LEU A 211 ? 0.0909 0.1300 0.0988 -0.0013 0.0092  0.0122  211 LEU A CB  
1732 C  CG  . LEU A 211 ? 0.0979 0.1437 0.1164 -0.0094 0.0122  0.0154  211 LEU A CG  
1733 C  CD1 . LEU A 211 ? 0.1083 0.1921 0.1437 -0.0079 -0.0103 0.0077  211 LEU A CD1 
1734 C  CD2 . LEU A 211 ? 0.1164 0.1516 0.1272 0.0119  0.0373  0.0198  211 LEU A CD2 
1735 N  N   . LYS A 212 ? 0.0794 0.1361 0.1157 -0.0272 0.0072  0.0194  212 LYS A N   
1736 C  CA  . LYS A 212 ? 0.1304 0.1325 0.0844 -0.0085 0.0089  0.0091  212 LYS A CA  
1737 C  C   . LYS A 212 ? 0.0891 0.1336 0.1015 -0.0088 0.0192  0.0122  212 LYS A C   
1738 O  O   . LYS A 212 ? 0.1065 0.1314 0.1796 -0.0111 -0.0140 0.0263  212 LYS A O   
1739 C  CB  . LYS A 212 ? 0.1778 0.1760 0.1082 -0.0515 0.0314  -0.0092 212 LYS A CB  
1740 C  CG  . LYS A 212 ? 0.2195 0.2055 0.1960 -0.0526 -0.0042 0.0329  212 LYS A CG  
1741 C  CD  . LYS A 212 ? 0.5308 0.3345 0.1965 -0.0708 0.0704  0.0939  212 LYS A CD  
1742 C  CE  . LYS A 212 ? 0.6519 0.3093 0.2588 0.0479  0.1932  0.0912  212 LYS A CE  
1743 N  NZ  . LYS A 212 ? 0.6721 0.5131 0.4586 0.0131  0.2782  0.0845  212 LYS A NZ  
1744 N  N   . GLU A 213 ? 0.0800 0.1354 0.1031 -0.0245 0.0016  0.0173  213 GLU A N   
1745 C  CA  . GLU A 213 ? 0.0864 0.1115 0.1222 -0.0087 0.0003  0.0141  213 GLU A CA  
1746 C  C   . GLU A 213 ? 0.0961 0.1053 0.1282 -0.0203 0.0076  0.0229  213 GLU A C   
1747 O  O   . GLU A 213 ? 0.0879 0.1103 0.1234 -0.0107 0.0114  0.0264  213 GLU A O   
1748 C  CB  . GLU A 213 ? 0.0785 0.1461 0.1433 -0.0231 0.0145  0.0140  213 GLU A CB  
1749 C  CG  . GLU A 213 ? 0.1300 0.1936 0.1907 -0.0298 -0.0040 -0.0132 213 GLU A CG  
1750 C  CD  . GLU A 213 ? 0.1501 0.2241 0.4560 0.0307  0.1020  0.0672  213 GLU A CD  
1751 O  OE1 . GLU A 213 ? 0.0972 0.1868 0.2503 -0.0234 -0.0206 0.0195  213 GLU A OE1 
1752 O  OE2 . GLU A 213 ? 0.1886 0.8489 0.5242 -0.1556 -0.1872 -0.1119 213 GLU A OE2 
1753 N  N   A PRO A 214 ? 0.0941 0.1110 0.1075 -0.0161 0.0053  0.0145  214 PRO A N   
1754 N  N   B PRO A 214 ? 0.1146 0.1071 0.1060 -0.0139 -0.0022 0.0073  214 PRO A N   
1755 C  CA  A PRO A 214 ? 0.0880 0.1076 0.1074 -0.0152 0.0084  -0.0008 214 PRO A CA  
1756 C  CA  B PRO A 214 ? 0.0850 0.1260 0.1159 -0.0034 0.0077  0.0006  214 PRO A CA  
1757 C  C   A PRO A 214 ? 0.0920 0.0974 0.1293 -0.0245 -0.0024 0.0109  214 PRO A C   
1758 C  C   B PRO A 214 ? 0.1094 0.1342 0.1161 -0.0347 -0.0027 0.0020  214 PRO A C   
1759 O  O   A PRO A 214 ? 0.0934 0.1103 0.1595 -0.0435 -0.0091 0.0177  214 PRO A O   
1760 O  O   B PRO A 214 ? 0.0993 0.1753 0.1172 -0.0369 0.0033  0.0080  214 PRO A O   
1761 C  CB  A PRO A 214 ? 0.1205 0.0990 0.1383 -0.0161 0.0142  -0.0052 214 PRO A CB  
1762 C  CB  B PRO A 214 ? 0.1176 0.1262 0.1444 0.0069  0.0134  0.0129  214 PRO A CB  
1763 C  CG  A PRO A 214 ? 0.1450 0.1075 0.1473 -0.0193 0.0126  0.0119  214 PRO A CG  
1764 C  CG  B PRO A 214 ? 0.1494 0.1839 0.1476 0.0171  0.0165  0.0241  214 PRO A CG  
1765 C  CD  A PRO A 214 ? 0.1376 0.0935 0.1333 -0.0312 -0.0138 -0.0015 214 PRO A CD  
1766 C  CD  B PRO A 214 ? 0.1137 0.0936 0.1932 -0.0089 0.0148  0.0230  214 PRO A CD  
1767 N  N   . ILE A 215 ? 0.1014 0.1102 0.1128 -0.0129 -0.0013 0.0016  215 ILE A N   
1768 C  CA  . ILE A 215 ? 0.1204 0.1182 0.1008 -0.0156 0.0057  -0.0074 215 ILE A CA  
1769 C  C   . ILE A 215 ? 0.1180 0.1137 0.1036 -0.0245 0.0046  0.0000  215 ILE A C   
1770 O  O   . ILE A 215 ? 0.1253 0.1240 0.1584 -0.0086 0.0022  -0.0223 215 ILE A O   
1771 C  CB  . ILE A 215 ? 0.0974 0.1171 0.1497 0.0021  0.0083  0.0046  215 ILE A CB  
1772 C  CG1 . ILE A 215 ? 0.1011 0.1253 0.1259 -0.0015 0.0050  0.0080  215 ILE A CG1 
1773 C  CG2 . ILE A 215 ? 0.1448 0.1368 0.1408 0.0283  0.0033  -0.0099 215 ILE A CG2 
1774 C  CD1 . ILE A 215 ? 0.1534 0.1329 0.1397 0.0075  -0.0126 0.0242  215 ILE A CD1 
1775 N  N   A SER A 216 ? 0.1397 0.1053 0.1269 -0.0225 -0.0155 -0.0062 216 SER A N   
1776 N  N   B SER A 216 ? 0.1407 0.1282 0.1271 -0.0240 -0.0190 -0.0121 216 SER A N   
1777 C  CA  A SER A 216 ? 0.1083 0.1172 0.0988 -0.0251 -0.0234 -0.0037 216 SER A CA  
1778 C  CA  B SER A 216 ? 0.1347 0.1324 0.1208 -0.0378 0.0148  -0.0036 216 SER A CA  
1779 C  C   A SER A 216 ? 0.1094 0.1002 0.1169 -0.0317 -0.0186 0.0189  216 SER A C   
1780 C  C   B SER A 216 ? 0.1098 0.0996 0.1311 -0.0386 -0.0144 0.0127  216 SER A C   
1781 O  O   A SER A 216 ? 0.1150 0.1426 0.1328 -0.0157 -0.0186 0.0309  216 SER A O   
1782 O  O   B SER A 216 ? 0.1386 0.1480 0.1486 -0.0033 -0.0211 0.0109  216 SER A O   
1783 C  CB  A SER A 216 ? 0.1076 0.0986 0.1493 -0.0183 -0.0353 0.0147  216 SER A CB  
1784 C  CB  B SER A 216 ? 0.1756 0.1667 0.1821 -0.0611 0.0155  0.0888  216 SER A CB  
1785 O  OG  A SER A 216 ? 0.1791 0.1638 0.1480 -0.0655 -0.0278 0.0278  216 SER A OG  
1786 O  OG  B SER A 216 ? 0.1828 0.1993 0.2661 -0.0678 -0.0150 0.0343  216 SER A OG  
1787 N  N   . VAL A 217 ? 0.1179 0.1115 0.1329 -0.0299 -0.0114 0.0069  217 VAL A N   
1788 C  CA  . VAL A 217 ? 0.1371 0.0999 0.1177 -0.0295 -0.0135 0.0005  217 VAL A CA  
1789 C  C   . VAL A 217 ? 0.1419 0.1017 0.1200 -0.0199 -0.0076 0.0086  217 VAL A C   
1790 O  O   . VAL A 217 ? 0.1354 0.1033 0.1444 -0.0315 -0.0273 0.0089  217 VAL A O   
1791 C  CB  . VAL A 217 ? 0.1415 0.0943 0.1613 -0.0192 -0.0194 0.0095  217 VAL A CB  
1792 C  CG1 . VAL A 217 ? 0.1764 0.0917 0.1832 -0.0366 -0.0506 -0.0122 217 VAL A CG1 
1793 C  CG2 . VAL A 217 ? 0.1376 0.1162 0.2165 -0.0186 -0.0358 -0.0223 217 VAL A CG2 
1794 N  N   . SER A 218 ? 0.1297 0.0997 0.1225 -0.0237 -0.0041 -0.0146 218 SER A N   
1795 C  CA  . SER A 218 ? 0.1537 0.0898 0.1245 -0.0054 -0.0196 -0.0027 218 SER A CA  
1796 C  C   . SER A 218 ? 0.1583 0.0909 0.1293 -0.0151 -0.0127 0.0039  218 SER A C   
1797 O  O   . SER A 218 ? 0.1591 0.0963 0.1242 -0.0161 -0.0156 0.0128  218 SER A O   
1798 C  CB  . SER A 218 ? 0.1663 0.1091 0.1197 -0.0303 -0.0190 -0.0024 218 SER A CB  
1799 O  OG  . SER A 218 ? 0.1490 0.1368 0.1279 -0.0306 -0.0275 0.0064  218 SER A OG  
1800 N  N   A SER A 219 ? 0.1455 0.0949 0.1552 -0.0060 -0.0106 0.0055  219 SER A N   
1801 N  N   B SER A 219 ? 0.1562 0.0938 0.1500 -0.0104 -0.0078 0.0035  219 SER A N   
1802 C  CA  A SER A 219 ? 0.1365 0.1071 0.1810 -0.0206 0.0005  0.0151  219 SER A CA  
1803 C  CA  B SER A 219 ? 0.1494 0.1089 0.1814 -0.0265 0.0073  0.0175  219 SER A CA  
1804 C  C   A SER A 219 ? 0.1422 0.0938 0.1641 -0.0138 0.0086  -0.0043 219 SER A C   
1805 C  C   B SER A 219 ? 0.1497 0.0961 0.1587 -0.0154 0.0095  -0.0030 219 SER A C   
1806 O  O   A SER A 219 ? 0.1318 0.1172 0.2258 -0.0198 -0.0070 0.0022  219 SER A O   
1807 O  O   B SER A 219 ? 0.1394 0.1168 0.2252 -0.0215 -0.0017 0.0041  219 SER A O   
1808 C  CB  A SER A 219 ? 0.1907 0.1146 0.2331 0.0120  0.0053  -0.0251 219 SER A CB  
1809 C  CB  B SER A 219 ? 0.2414 0.1155 0.2403 -0.0088 0.0079  -0.0100 219 SER A CB  
1810 O  OG  A SER A 219 ? 0.2306 0.0821 0.2234 0.0223  -0.0157 -0.0272 219 SER A OG  
1811 O  OG  B SER A 219 ? 0.3104 0.1767 0.2900 0.0441  0.0615  -0.0138 219 SER A OG  
1812 N  N   . GLU A 220 ? 0.1785 0.1067 0.1448 -0.0015 -0.0070 -0.0168 220 GLU A N   
1813 C  CA  . GLU A 220 ? 0.1810 0.1146 0.1698 -0.0232 -0.0151 0.0060  220 GLU A CA  
1814 C  C   . GLU A 220 ? 0.1753 0.1046 0.1735 0.0055  -0.0020 0.0037  220 GLU A C   
1815 O  O   . GLU A 220 ? 0.2058 0.1473 0.1602 -0.0032 0.0337  -0.0066 220 GLU A O   
1816 C  CB  . GLU A 220 ? 0.2392 0.1580 0.1767 -0.0115 -0.0544 -0.0086 220 GLU A CB  
1817 C  CG  . GLU A 220 ? 0.2782 0.2014 0.2500 -0.0339 -0.0295 -0.0673 220 GLU A CG  
1818 C  CD  . GLU A 220 ? 0.3179 0.1500 0.2620 -0.0491 -0.0501 -0.0586 220 GLU A CD  
1819 O  OE1 . GLU A 220 ? 0.2453 0.2081 0.2627 -0.0501 -0.0375 -0.0458 220 GLU A OE1 
1820 O  OE2 . GLU A 220 ? 0.5660 0.1285 0.4679 -0.1052 -0.0036 -0.1073 220 GLU A OE2 
1821 N  N   . GLN A 221 ? 0.1530 0.1066 0.1494 -0.0040 0.0006  -0.0057 221 GLN A N   
1822 C  CA  . GLN A 221 ? 0.1379 0.1008 0.1429 -0.0251 -0.0010 0.0080  221 GLN A CA  
1823 C  C   . GLN A 221 ? 0.1340 0.1164 0.1353 -0.0188 0.0033  0.0175  221 GLN A C   
1824 O  O   . GLN A 221 ? 0.1487 0.1225 0.1207 -0.0188 0.0071  0.0185  221 GLN A O   
1825 C  CB  . GLN A 221 ? 0.1120 0.1336 0.1267 -0.0062 -0.0088 0.0212  221 GLN A CB  
1826 C  CG  . GLN A 221 ? 0.1160 0.1372 0.1322 -0.0147 -0.0085 0.0139  221 GLN A CG  
1827 C  CD  . GLN A 221 ? 0.1189 0.1044 0.1353 -0.0278 -0.0092 0.0001  221 GLN A CD  
1828 O  OE1 . GLN A 221 ? 0.1300 0.1171 0.1289 -0.0160 -0.0182 0.0119  221 GLN A OE1 
1829 N  NE2 . GLN A 221 ? 0.1389 0.1116 0.1526 -0.0114 -0.0161 0.0158  221 GLN A NE2 
1830 N  N   . VAL A 222 ? 0.1430 0.1206 0.1232 -0.0225 0.0006  0.0188  222 VAL A N   
1831 C  CA  . VAL A 222 ? 0.1389 0.1329 0.1223 -0.0172 -0.0032 0.0234  222 VAL A CA  
1832 C  C   . VAL A 222 ? 0.1318 0.1282 0.1663 -0.0263 0.0008  0.0206  222 VAL A C   
1833 O  O   . VAL A 222 ? 0.1307 0.1364 0.1638 -0.0388 -0.0076 0.0301  222 VAL A O   
1834 C  CB  . VAL A 222 ? 0.1759 0.1965 0.1558 -0.0381 -0.0323 0.0576  222 VAL A CB  
1835 C  CG1 . VAL A 222 ? 0.2119 0.1886 0.1983 -0.0513 -0.0059 0.0664  222 VAL A CG1 
1836 C  CG2 . VAL A 222 ? 0.1936 0.2597 0.1810 -0.0606 -0.0428 0.0403  222 VAL A CG2 
1837 N  N   A LEU A 223 ? 0.1234 0.1335 0.1688 0.0053  0.0139  -0.0027 223 LEU A N   
1838 N  N   B LEU A 223 ? 0.1258 0.1340 0.1641 -0.0031 0.0067  0.0036  223 LEU A N   
1839 C  CA  A LEU A 223 ? 0.0952 0.1293 0.2324 -0.0003 0.0293  -0.0121 223 LEU A CA  
1840 C  CA  B LEU A 223 ? 0.1842 0.1469 0.2018 0.0129  0.0414  0.0027  223 LEU A CA  
1841 C  C   A LEU A 223 ? 0.1487 0.1419 0.1746 0.0055  -0.0030 -0.0148 223 LEU A C   
1842 C  C   B LEU A 223 ? 0.1243 0.1329 0.1742 -0.0193 -0.0140 -0.0151 223 LEU A C   
1843 O  O   A LEU A 223 ? 0.1401 0.1615 0.2129 0.0058  0.0094  -0.0185 223 LEU A O   
1844 O  O   B LEU A 223 ? 0.1340 0.1544 0.2051 -0.0256 0.0103  0.0063  223 LEU A O   
1845 C  CB  A LEU A 223 ? 0.1879 0.1537 0.3046 0.0160  0.0838  -0.1036 223 LEU A CB  
1846 C  CB  B LEU A 223 ? 0.1932 0.1354 0.3004 -0.0558 0.0845  0.0221  223 LEU A CB  
1847 C  CG  A LEU A 223 ? 0.2244 0.2177 0.2622 -0.0284 0.1098  -0.0880 223 LEU A CG  
1848 C  CG  B LEU A 223 ? 0.1886 0.2101 0.3940 -0.0337 0.0951  -0.0656 223 LEU A CG  
1849 C  CD1 A LEU A 223 ? 0.1333 0.3179 0.3500 -0.0358 0.0763  -0.1169 223 LEU A CD1 
1850 C  CD1 B LEU A 223 ? 0.2752 0.3578 0.4934 0.0319  0.0368  0.0178  223 LEU A CD1 
1851 C  CD2 A LEU A 223 ? 0.2505 0.2547 0.2417 -0.0372 -0.0500 -0.0161 223 LEU A CD2 
1852 C  CD2 B LEU A 223 ? 0.3556 0.3186 0.3532 -0.0541 -0.0304 -0.0904 223 LEU A CD2 
1853 N  N   . LYS A 224 ? 0.1333 0.1519 0.1328 -0.0113 0.0006  -0.0024 224 LYS A N   
1854 C  CA  . LYS A 224 ? 0.1534 0.1555 0.1153 -0.0124 0.0068  -0.0011 224 LYS A CA  
1855 C  C   . LYS A 224 ? 0.1548 0.1249 0.1112 -0.0080 0.0321  0.0110  224 LYS A C   
1856 O  O   . LYS A 224 ? 0.1448 0.1570 0.1144 -0.0158 0.0089  0.0313  224 LYS A O   
1857 C  CB  . LYS A 224 ? 0.1486 0.2252 0.1705 -0.0071 0.0054  0.0306  224 LYS A CB  
1858 C  CG  . LYS A 224 ? 0.2119 0.2891 0.1918 -0.0753 -0.0071 0.0247  224 LYS A CG  
1859 C  CD  . LYS A 224 ? 0.2098 0.3500 0.2458 -0.0531 -0.0323 -0.0484 224 LYS A CD  
1860 C  CE  . LYS A 224 ? 0.3917 0.3783 0.2162 -0.1059 -0.0832 -0.0176 224 LYS A CE  
1861 N  NZ  . LYS A 224 ? 0.3273 0.3775 0.2191 -0.0989 0.0306  -0.0540 224 LYS A NZ  
1862 N  N   . PHE A 225 ? 0.1340 0.1358 0.0979 -0.0066 0.0008  0.0057  225 PHE A N   
1863 C  CA  . PHE A 225 ? 0.1300 0.1267 0.0961 -0.0083 0.0177  0.0004  225 PHE A CA  
1864 C  C   . PHE A 225 ? 0.1225 0.1300 0.1002 -0.0102 0.0281  0.0065  225 PHE A C   
1865 O  O   . PHE A 225 ? 0.1491 0.1243 0.1005 -0.0113 0.0337  0.0011  225 PHE A O   
1866 C  CB  . PHE A 225 ? 0.1426 0.1400 0.0925 0.0136  0.0302  0.0167  225 PHE A CB  
1867 C  CG  . PHE A 225 ? 0.1060 0.1003 0.1260 -0.0237 0.0240  0.0006  225 PHE A CG  
1868 C  CD1 . PHE A 225 ? 0.1426 0.1408 0.1433 0.0234  0.0190  0.0095  225 PHE A CD1 
1869 C  CD2 . PHE A 225 ? 0.1234 0.1519 0.1476 -0.0122 0.0175  -0.0272 225 PHE A CD2 
1870 C  CE1 . PHE A 225 ? 0.1641 0.1412 0.1534 0.0188  0.0439  0.0005  225 PHE A CE1 
1871 C  CE2 . PHE A 225 ? 0.0938 0.1925 0.1731 -0.0015 0.0118  -0.0366 225 PHE A CE2 
1872 C  CZ  . PHE A 225 ? 0.1242 0.1436 0.1591 -0.0117 0.0227  -0.0197 225 PHE A CZ  
1873 N  N   . ARG A 226 ? 0.1163 0.1265 0.1039 0.0080  0.0174  0.0073  226 ARG A N   
1874 C  CA  . ARG A 226 ? 0.1296 0.1379 0.0927 0.0107  0.0142  0.0113  226 ARG A CA  
1875 C  C   . ARG A 226 ? 0.1170 0.1343 0.1024 -0.0059 0.0217  -0.0037 226 ARG A C   
1876 O  O   . ARG A 226 ? 0.1447 0.1652 0.1332 0.0265  0.0261  -0.0032 226 ARG A O   
1877 C  CB  . ARG A 226 ? 0.1501 0.1444 0.1058 -0.0046 0.0299  0.0207  226 ARG A CB  
1878 C  CG  . ARG A 226 ? 0.1673 0.1236 0.0929 -0.0152 0.0126  0.0226  226 ARG A CG  
1879 C  CD  . ARG A 226 ? 0.2277 0.1209 0.0993 -0.0030 0.0218  0.0103  226 ARG A CD  
1880 N  NE  . ARG A 226 ? 0.1771 0.1180 0.1032 -0.0276 0.0085  0.0044  226 ARG A NE  
1881 C  CZ  . ARG A 226 ? 0.1624 0.1017 0.1544 -0.0254 0.0041  -0.0129 226 ARG A CZ  
1882 N  NH1 . ARG A 226 ? 0.1782 0.1667 0.1979 -0.0400 0.0001  -0.0545 226 ARG A NH1 
1883 N  NH2 . ARG A 226 ? 0.2134 0.1150 0.1591 -0.0296 0.0322  0.0000  226 ARG A NH2 
1884 N  N   . LYS A 227 ? 0.1422 0.1548 0.0789 -0.0121 0.0135  -0.0121 227 LYS A N   
1885 C  CA  . LYS A 227 ? 0.1882 0.1638 0.0832 -0.0214 0.0210  0.0080  227 LYS A CA  
1886 C  C   . LYS A 227 ? 0.1843 0.1562 0.0810 -0.0208 0.0345  0.0109  227 LYS A C   
1887 O  O   . LYS A 227 ? 0.1993 0.1871 0.1049 -0.0314 0.0585  0.0044  227 LYS A O   
1888 C  CB  . LYS A 227 ? 0.1849 0.2026 0.1062 -0.0269 0.0275  -0.0230 227 LYS A CB  
1889 C  CG  . LYS A 227 ? 0.2540 0.2306 0.1623 -0.0715 0.0205  -0.0230 227 LYS A CG  
1890 C  CD  . LYS A 227 ? 0.3021 0.3503 0.2515 -0.1377 -0.0478 -0.0458 227 LYS A CD  
1891 C  CE  . LYS A 227 ? 0.4782 0.5869 0.2123 -0.0627 -0.0710 -0.0160 227 LYS A CE  
1892 N  NZ  . LYS A 227 ? 0.7741 0.8296 0.3711 -0.2755 -0.2926 -0.0411 227 LYS A NZ  
1893 N  N   . LEU A 228 ? 0.1627 0.1401 0.1072 -0.0122 0.0129  0.0067  228 LEU A N   
1894 C  CA  . LEU A 228 ? 0.1365 0.1361 0.1109 -0.0013 0.0301  -0.0075 228 LEU A CA  
1895 C  C   . LEU A 228 ? 0.1437 0.1562 0.0853 0.0054  0.0330  0.0072  228 LEU A C   
1896 O  O   . LEU A 228 ? 0.1432 0.1469 0.0941 0.0076  0.0150  0.0013  228 LEU A O   
1897 C  CB  . LEU A 228 ? 0.1494 0.1552 0.0877 0.0192  0.0379  -0.0006 228 LEU A CB  
1898 C  CG  . LEU A 228 ? 0.1383 0.1608 0.0978 0.0201  0.0254  0.0125  228 LEU A CG  
1899 C  CD1 . LEU A 228 ? 0.1401 0.1746 0.0970 0.0092  0.0283  -0.0012 228 LEU A CD1 
1900 C  CD2 . LEU A 228 ? 0.1698 0.1807 0.1177 0.0106  0.0322  0.0361  228 LEU A CD2 
1901 N  N   . ASN A 229 ? 0.1329 0.1562 0.1017 0.0002  0.0469  0.0066  229 ASN A N   
1902 C  CA  . ASN A 229 ? 0.1368 0.1534 0.0875 0.0049  0.0410  -0.0010 229 ASN A CA  
1903 C  C   . ASN A 229 ? 0.1365 0.1394 0.1103 -0.0013 0.0337  0.0217  229 ASN A C   
1904 O  O   . ASN A 229 ? 0.1430 0.1544 0.1279 0.0096  0.0412  0.0165  229 ASN A O   
1905 C  CB  . ASN A 229 ? 0.1713 0.1921 0.0893 0.0044  0.0475  0.0027  229 ASN A CB  
1906 C  CG  . ASN A 229 ? 0.2169 0.2205 0.1062 0.0232  0.0315  -0.0080 229 ASN A CG  
1907 O  OD1 . ASN A 229 ? 0.2550 0.2974 0.1094 0.0512  0.0526  -0.0328 229 ASN A OD1 
1908 N  ND2 . ASN A 229 ? 0.2082 0.2155 0.1670 0.0023  0.0436  -0.0414 229 ASN A ND2 
1909 N  N   . PHE A 230 ? 0.1134 0.1648 0.0995 -0.0054 0.0433  0.0091  230 PHE A N   
1910 C  CA  . PHE A 230 ? 0.1372 0.1429 0.0990 -0.0120 0.0333  0.0154  230 PHE A CA  
1911 C  C   . PHE A 230 ? 0.1365 0.1515 0.1014 -0.0023 0.0392  0.0146  230 PHE A C   
1912 O  O   . PHE A 230 ? 0.1717 0.1505 0.1230 -0.0216 0.0325  0.0215  230 PHE A O   
1913 C  CB  . PHE A 230 ? 0.1430 0.1692 0.0929 -0.0136 0.0375  0.0082  230 PHE A CB  
1914 C  CG  . PHE A 230 ? 0.1498 0.1504 0.1021 -0.0206 0.0528  0.0069  230 PHE A CG  
1915 C  CD1 . PHE A 230 ? 0.1487 0.1656 0.0900 0.0039  0.0380  0.0006  230 PHE A CD1 
1916 C  CD2 . PHE A 230 ? 0.1692 0.1404 0.1275 0.0051  0.0335  -0.0023 230 PHE A CD2 
1917 C  CE1 . PHE A 230 ? 0.1958 0.1440 0.0846 -0.0081 0.0318  0.0048  230 PHE A CE1 
1918 C  CE2 . PHE A 230 ? 0.1716 0.1498 0.1093 -0.0168 0.0065  -0.0044 230 PHE A CE2 
1919 C  CZ  . PHE A 230 ? 0.1509 0.1329 0.1300 -0.0170 0.0157  0.0027  230 PHE A CZ  
1920 N  N   . ASN A 231 ? 0.1328 0.1735 0.1036 -0.0010 0.0518  0.0064  231 ASN A N   
1921 C  CA  . ASN A 231 ? 0.1541 0.1720 0.1307 -0.0048 0.0550  0.0219  231 ASN A CA  
1922 C  C   . ASN A 231 ? 0.1390 0.1871 0.1058 0.0146  0.0619  0.0105  231 ASN A C   
1923 O  O   . ASN A 231 ? 0.1512 0.1917 0.1347 0.0401  0.0600  0.0052  231 ASN A O   
1924 C  CB  . ASN A 231 ? 0.1436 0.1832 0.1914 -0.0044 0.0885  0.0096  231 ASN A CB  
1925 C  CG  . ASN A 231 ? 0.1358 0.1379 0.1649 0.0333  0.0541  0.0343  231 ASN A CG  
1926 O  OD1 . ASN A 231 ? 0.1746 0.1451 0.1566 0.0116  0.0613  0.0132  231 ASN A OD1 
1927 N  ND2 . ASN A 231 ? 0.2026 0.1810 0.1631 0.0293  0.0436  0.0053  231 ASN A ND2 
1928 N  N   . GLY A 232 ? 0.1652 0.1566 0.1465 -0.0008 0.0383  0.0282  232 GLY A N   
1929 C  CA  . GLY A 232 ? 0.2097 0.1613 0.1310 0.0424  0.0571  0.0208  232 GLY A CA  
1930 C  C   . GLY A 232 ? 0.1845 0.1580 0.1321 0.0039  0.0559  0.0337  232 GLY A C   
1931 O  O   . GLY A 232 ? 0.1943 0.1893 0.1279 0.0369  0.0780  0.0384  232 GLY A O   
1932 N  N   . GLU A 233 ? 0.1886 0.1846 0.1124 -0.0082 0.0660  0.0436  233 GLU A N   
1933 C  CA  . GLU A 233 ? 0.1537 0.1861 0.1433 0.0119  0.0536  0.0222  233 GLU A CA  
1934 C  C   . GLU A 233 ? 0.1552 0.1954 0.1631 0.0179  0.0519  0.0183  233 GLU A C   
1935 O  O   . GLU A 233 ? 0.1641 0.2055 0.1570 0.0153  0.0528  0.0315  233 GLU A O   
1936 C  CB  . GLU A 233 ? 0.1850 0.1882 0.1529 0.0168  0.0435  0.0292  233 GLU A CB  
1937 C  CG  . GLU A 233 ? 0.2460 0.2547 0.1670 -0.0348 0.0461  0.0223  233 GLU A CG  
1938 C  CD  . GLU A 233 ? 0.2489 0.4121 0.2849 0.0373  -0.0315 -0.0156 233 GLU A CD  
1939 O  OE1 . GLU A 233 ? 0.3578 0.3547 0.2931 0.0605  0.0780  0.1049  233 GLU A OE1 
1940 O  OE2 . GLU A 233 ? 0.3793 0.4623 0.2713 -0.1104 -0.0625 0.0364  233 GLU A OE2 
1941 N  N   . GLY A 234 ? 0.2425 0.2381 0.1588 0.0626  0.0928  0.0194  234 GLY A N   
1942 C  CA  . GLY A 234 ? 0.2065 0.2631 0.1613 0.0134  0.0523  0.0147  234 GLY A CA  
1943 C  C   . GLY A 234 ? 0.2522 0.2820 0.1587 0.0829  0.0401  0.0321  234 GLY A C   
1944 O  O   . GLY A 234 ? 0.2906 0.3778 0.1986 0.1011  0.1530  0.0074  234 GLY A O   
1945 N  N   . GLU A 235 ? 0.2082 0.2338 0.1663 0.0672  0.0478  0.0552  235 GLU A N   
1946 C  CA  . GLU A 235 ? 0.1910 0.1983 0.1767 0.0662  0.0469  0.0328  235 GLU A CA  
1947 C  C   . GLU A 235 ? 0.1857 0.2198 0.1479 0.0457  0.0639  0.0075  235 GLU A C   
1948 O  O   . GLU A 235 ? 0.2008 0.2554 0.1687 0.0256  0.0419  0.0228  235 GLU A O   
1949 C  CB  . GLU A 235 ? 0.1597 0.2341 0.1552 0.0015  0.0647  0.0222  235 GLU A CB  
1950 C  CG  . GLU A 235 ? 0.2144 0.2244 0.2428 -0.0320 0.0578  0.0197  235 GLU A CG  
1951 C  CD  . GLU A 235 ? 0.3582 0.2766 0.3231 -0.0581 0.1060  -0.0422 235 GLU A CD  
1952 O  OE1 . GLU A 235 ? 0.5558 0.3050 0.5271 -0.1221 0.2943  -0.0416 235 GLU A OE1 
1953 O  OE2 . GLU A 235 ? 0.1764 0.2734 0.3984 -0.0039 0.0290  0.0664  235 GLU A OE2 
1954 N  N   . PRO A 236 ? 0.1602 0.2158 0.1990 0.0348  0.0851  0.0326  236 PRO A N   
1955 C  CA  . PRO A 236 ? 0.1544 0.2046 0.1781 0.0284  0.0754  0.0438  236 PRO A CA  
1956 C  C   . PRO A 236 ? 0.1468 0.2231 0.1173 0.0307  0.0584  0.0095  236 PRO A C   
1957 O  O   . PRO A 236 ? 0.1943 0.2047 0.1397 0.0153  0.0545  0.0072  236 PRO A O   
1958 C  CB  . PRO A 236 ? 0.1121 0.2827 0.2270 0.0363  0.0835  0.0155  236 PRO A CB  
1959 C  CG  . PRO A 236 ? 0.1939 0.2428 0.2726 0.0388  0.1260  0.0533  236 PRO A CG  
1960 C  CD  . PRO A 236 ? 0.1746 0.2565 0.2809 0.0498  0.0304  0.0791  236 PRO A CD  
1961 N  N   . GLU A 237 ? 0.1432 0.2004 0.1461 0.0386  0.0583  -0.0103 237 GLU A N   
1962 C  CA  . GLU A 237 ? 0.1583 0.1843 0.1401 -0.0095 0.0642  -0.0120 237 GLU A CA  
1963 C  C   . GLU A 237 ? 0.1289 0.1645 0.1597 0.0063  0.0616  -0.0111 237 GLU A C   
1964 O  O   . GLU A 237 ? 0.1523 0.1828 0.1616 0.0220  0.0583  -0.0069 237 GLU A O   
1965 C  CB  . GLU A 237 ? 0.1947 0.2263 0.2160 -0.0231 0.0234  -0.0616 237 GLU A CB  
1966 C  CG  . GLU A 237 ? 0.2019 0.3046 0.3079 -0.0370 0.0332  -0.0761 237 GLU A CG  
1967 C  CD  . GLU A 237 ? 0.3215 0.4393 0.3434 0.0081  -0.0267 -0.2004 237 GLU A CD  
1968 O  OE1 . GLU A 237 ? 0.4855 0.4482 0.3668 0.0119  -0.0167 -0.2198 237 GLU A OE1 
1969 O  OE2 . GLU A 237 ? 0.3984 0.2791 0.2741 -0.0424 0.0961  -0.1001 237 GLU A OE2 
1970 N  N   . GLU A 238 ? 0.1173 0.1753 0.1133 -0.0027 0.0502  -0.0055 238 GLU A N   
1971 C  CA  . GLU A 238 ? 0.1325 0.1967 0.1225 0.0061  0.0387  0.0142  238 GLU A CA  
1972 C  C   . GLU A 238 ? 0.1207 0.1570 0.1194 0.0195  0.0446  0.0029  238 GLU A C   
1973 O  O   . GLU A 238 ? 0.1760 0.1523 0.1591 0.0019  0.0641  0.0092  238 GLU A O   
1974 C  CB  . GLU A 238 ? 0.1472 0.3021 0.1810 -0.0489 0.0431  -0.0223 238 GLU A CB  
1975 C  CG  . GLU A 238 ? 0.2249 0.3958 0.2380 -0.0013 -0.0352 -0.0199 238 GLU A CG  
1976 N  N   . LEU A 239 ? 0.1393 0.1577 0.1198 0.0097  0.0450  -0.0128 239 LEU A N   
1977 C  CA  . LEU A 239 ? 0.1329 0.1547 0.1186 -0.0183 0.0592  -0.0179 239 LEU A CA  
1978 C  C   . LEU A 239 ? 0.1285 0.1253 0.0956 0.0016  0.0399  0.0074  239 LEU A C   
1979 O  O   . LEU A 239 ? 0.1318 0.1329 0.1088 0.0171  0.0406  -0.0022 239 LEU A O   
1980 C  CB  . LEU A 239 ? 0.1390 0.1419 0.1875 -0.0060 0.0524  -0.0295 239 LEU A CB  
1981 C  CG  . LEU A 239 ? 0.1723 0.1774 0.1997 0.0015  0.0283  -0.0622 239 LEU A CG  
1982 C  CD1 . LEU A 239 ? 0.2270 0.1437 0.3288 -0.0023 0.0040  -0.0731 239 LEU A CD1 
1983 C  CD2 . LEU A 239 ? 0.1845 0.1800 0.2033 0.0088  0.0598  -0.0474 239 LEU A CD2 
1984 N  N   . MET A 240 ? 0.1436 0.1209 0.0848 0.0252  0.0436  0.0030  240 MET A N   
1985 C  CA  . MET A 240 ? 0.1476 0.1394 0.0796 0.0299  0.0649  0.0055  240 MET A CA  
1986 C  C   . MET A 240 ? 0.1225 0.1411 0.0959 0.0097  0.0374  0.0016  240 MET A C   
1987 O  O   . MET A 240 ? 0.1207 0.1315 0.1031 0.0016  0.0287  0.0055  240 MET A O   
1988 C  CB  . MET A 240 ? 0.1939 0.1386 0.0873 0.0489  0.0657  0.0091  240 MET A CB  
1989 C  CG  . MET A 240 ? 0.1376 0.1243 0.0925 0.0053  0.0381  -0.0086 240 MET A CG  
1990 S  SD  . MET A 240 ? 0.1577 0.1230 0.1124 0.0047  0.0432  0.0050  240 MET A SD  
1991 C  CE  . MET A 240 ? 0.1504 0.1429 0.1430 0.0066  0.0705  0.0195  240 MET A CE  
1992 N  N   . VAL A 241 ? 0.1252 0.1084 0.0805 0.0022  0.0295  0.0065  241 VAL A N   
1993 C  CA  . VAL A 241 ? 0.1182 0.1190 0.0850 -0.0048 0.0237  0.0103  241 VAL A CA  
1994 C  C   . VAL A 241 ? 0.1107 0.0972 0.0832 0.0076  0.0354  0.0069  241 VAL A C   
1995 O  O   . VAL A 241 ? 0.1128 0.1333 0.0979 0.0000  0.0301  -0.0013 241 VAL A O   
1996 C  CB  . VAL A 241 ? 0.1121 0.1187 0.0944 -0.0098 0.0348  -0.0004 241 VAL A CB  
1997 C  CG1 . VAL A 241 ? 0.1523 0.1472 0.1146 -0.0329 0.0152  0.0013  241 VAL A CG1 
1998 C  CG2 . VAL A 241 ? 0.1260 0.1354 0.1274 0.0124  0.0439  -0.0038 241 VAL A CG2 
1999 N  N   . ASP A 242 ? 0.1177 0.0987 0.0776 0.0017  0.0347  0.0113  242 ASP A N   
2000 C  CA  . ASP A 242 ? 0.1161 0.1047 0.1006 0.0201  0.0125  0.0067  242 ASP A CA  
2001 C  C   . ASP A 242 ? 0.0961 0.1124 0.0935 0.0061  0.0250  0.0018  242 ASP A C   
2002 O  O   . ASP A 242 ? 0.1099 0.1200 0.1479 0.0081  0.0021  0.0032  242 ASP A O   
2003 C  CB  . ASP A 242 ? 0.1342 0.1014 0.1278 0.0221  0.0273  -0.0029 242 ASP A CB  
2004 C  CG  . ASP A 242 ? 0.1458 0.1047 0.1190 0.0058  0.0557  -0.0035 242 ASP A CG  
2005 O  OD1 . ASP A 242 ? 0.1215 0.0996 0.0999 0.0113  0.0320  0.0030  242 ASP A OD1 
2006 O  OD2 . ASP A 242 ? 0.1597 0.1152 0.1613 0.0216  0.0540  -0.0134 242 ASP A OD2 
2007 N  N   . ASN A 243 ? 0.0977 0.1029 0.0866 0.0009  0.0337  0.0005  243 ASN A N   
2008 C  CA  . ASN A 243 ? 0.1033 0.0952 0.0807 0.0043  0.0189  -0.0029 243 ASN A CA  
2009 C  C   . ASN A 243 ? 0.0680 0.1120 0.0926 -0.0020 0.0148  -0.0037 243 ASN A C   
2010 O  O   . ASN A 243 ? 0.1166 0.1250 0.0979 0.0232  0.0330  0.0030  243 ASN A O   
2011 C  CB  . ASN A 243 ? 0.0924 0.1172 0.0796 -0.0005 0.0221  0.0070  243 ASN A CB  
2012 C  CG  . ASN A 243 ? 0.0933 0.1179 0.0793 0.0021  0.0301  0.0111  243 ASN A CG  
2013 O  OD1 . ASN A 243 ? 0.0902 0.1198 0.1304 -0.0062 0.0159  0.0291  243 ASN A OD1 
2014 N  ND2 . ASN A 243 ? 0.1108 0.1624 0.1225 -0.0017 0.0185  0.0528  243 ASN A ND2 
2015 N  N   . TRP A 244 ? 0.0936 0.1058 0.0680 -0.0058 0.0145  -0.0055 244 TRP A N   
2016 C  CA  . TRP A 244 ? 0.0800 0.1098 0.0769 0.0015  0.0111  -0.0134 244 TRP A CA  
2017 C  C   . TRP A 244 ? 0.0654 0.1110 0.0844 -0.0027 0.0223  -0.0027 244 TRP A C   
2018 O  O   . TRP A 244 ? 0.0923 0.1304 0.0967 0.0179  0.0122  -0.0188 244 TRP A O   
2019 C  CB  . TRP A 244 ? 0.0981 0.0927 0.0917 -0.0016 0.0203  -0.0106 244 TRP A CB  
2020 C  CG  . TRP A 244 ? 0.0873 0.1005 0.0762 0.0117  0.0295  -0.0002 244 TRP A CG  
2021 C  CD1 . TRP A 244 ? 0.0864 0.1071 0.0917 0.0135  0.0210  -0.0005 244 TRP A CD1 
2022 C  CD2 . TRP A 244 ? 0.0954 0.0961 0.0933 -0.0016 0.0153  0.0016  244 TRP A CD2 
2023 N  NE1 . TRP A 244 ? 0.0927 0.1046 0.0990 0.0115  0.0293  0.0170  244 TRP A NE1 
2024 C  CE2 . TRP A 244 ? 0.0889 0.1017 0.1126 0.0105  0.0201  0.0022  244 TRP A CE2 
2025 C  CE3 . TRP A 244 ? 0.1094 0.1433 0.0986 0.0176  0.0081  0.0146  244 TRP A CE3 
2026 C  CZ2 . TRP A 244 ? 0.1282 0.1148 0.1107 0.0113  0.0151  0.0064  244 TRP A CZ2 
2027 C  CZ3 . TRP A 244 ? 0.1529 0.1332 0.1195 0.0366  0.0136  0.0135  244 TRP A CZ3 
2028 C  CH2 . TRP A 244 ? 0.1419 0.1252 0.1128 0.0135  0.0071  0.0076  244 TRP A CH2 
2029 N  N   . ARG A 245 ? 0.0920 0.1008 0.0819 -0.0098 0.0093  -0.0081 245 ARG A N   
2030 C  CA  . ARG A 245 ? 0.0807 0.1065 0.0902 -0.0128 0.0100  -0.0089 245 ARG A CA  
2031 C  C   . ARG A 245 ? 0.0688 0.1187 0.1033 -0.0078 0.0085  -0.0105 245 ARG A C   
2032 O  O   . ARG A 245 ? 0.0839 0.1230 0.1005 -0.0066 0.0218  -0.0032 245 ARG A O   
2033 C  CB  . ARG A 245 ? 0.0864 0.1152 0.0926 -0.0072 0.0033  -0.0251 245 ARG A CB  
2034 C  CG  . ARG A 245 ? 0.0661 0.1137 0.0926 -0.0033 0.0121  -0.0190 245 ARG A CG  
2035 C  CD  . ARG A 245 ? 0.0642 0.1208 0.1049 -0.0318 0.0121  -0.0271 245 ARG A CD  
2036 N  NE  . ARG A 245 ? 0.0672 0.1249 0.1097 -0.0222 0.0082  -0.0134 245 ARG A NE  
2037 C  CZ  . ARG A 245 ? 0.0636 0.1236 0.1236 -0.0283 0.0132  -0.0210 245 ARG A CZ  
2038 N  NH1 . ARG A 245 ? 0.0882 0.1386 0.1127 -0.0095 0.0354  -0.0115 245 ARG A NH1 
2039 N  NH2 . ARG A 245 ? 0.0785 0.1562 0.1386 -0.0396 -0.0089 -0.0165 245 ARG A NH2 
2040 N  N   . PRO A 246 ? 0.1093 0.1112 0.0995 0.0114  0.0254  0.0024  246 PRO A N   
2041 C  CA  . PRO A 246 ? 0.1340 0.1249 0.1111 0.0215  0.0297  0.0048  246 PRO A CA  
2042 C  C   . PRO A 246 ? 0.0990 0.1062 0.0981 0.0174  0.0210  0.0114  246 PRO A C   
2043 O  O   . PRO A 246 ? 0.0952 0.1199 0.1125 0.0076  0.0118  0.0003  246 PRO A O   
2044 C  CB  . PRO A 246 ? 0.1490 0.1717 0.1286 0.0703  0.0230  -0.0013 246 PRO A CB  
2045 C  CG  . PRO A 246 ? 0.1397 0.2634 0.2910 0.0963  0.0841  0.1326  246 PRO A CG  
2046 C  CD  . PRO A 246 ? 0.0951 0.1541 0.1717 0.0228  0.0207  0.0297  246 PRO A CD  
2047 N  N   . ALA A 247 ? 0.1164 0.1243 0.0942 0.0127  0.0155  0.0168  247 ALA A N   
2048 C  CA  . ALA A 247 ? 0.1206 0.1321 0.0873 0.0177  0.0122  0.0130  247 ALA A CA  
2049 C  C   . ALA A 247 ? 0.1074 0.1197 0.0986 0.0303  0.0167  0.0126  247 ALA A C   
2050 O  O   . ALA A 247 ? 0.1160 0.1448 0.1126 0.0413  0.0003  -0.0010 247 ALA A O   
2051 C  CB  . ALA A 247 ? 0.1631 0.1425 0.1133 -0.0253 0.0139  0.0218  247 ALA A CB  
2052 N  N   . GLN A 248 ? 0.0927 0.1198 0.0936 0.0059  0.0079  0.0115  248 GLN A N   
2053 C  CA  . GLN A 248 ? 0.0862 0.1389 0.1111 0.0042  0.0061  0.0026  248 GLN A CA  
2054 C  C   . GLN A 248 ? 0.1135 0.1289 0.1099 0.0113  0.0017  0.0046  248 GLN A C   
2055 O  O   . GLN A 248 ? 0.1376 0.1569 0.1111 0.0082  0.0223  0.0170  248 GLN A O   
2056 C  CB  . GLN A 248 ? 0.0938 0.1318 0.1076 0.0100  0.0176  0.0013  248 GLN A CB  
2057 C  CG  . GLN A 248 ? 0.1257 0.1415 0.1057 0.0055  0.0225  0.0089  248 GLN A CG  
2058 C  CD  . GLN A 248 ? 0.0854 0.1845 0.1213 -0.0184 0.0057  0.0015  248 GLN A CD  
2059 O  OE1 . GLN A 248 ? 0.0864 0.2500 0.1580 -0.0317 0.0079  -0.0226 248 GLN A OE1 
2060 N  NE2 . GLN A 248 ? 0.1318 0.1800 0.0956 0.0124  0.0116  -0.0085 248 GLN A NE2 
2061 N  N   . PRO A 249 ? 0.1214 0.1634 0.1190 0.0365  0.0053  -0.0212 249 PRO A N   
2062 C  CA  . PRO A 249 ? 0.1627 0.2144 0.1008 0.0925  -0.0021 -0.0206 249 PRO A CA  
2063 C  C   . PRO A 249 ? 0.1620 0.1580 0.0812 0.0588  0.0095  0.0093  249 PRO A C   
2064 O  O   . PRO A 249 ? 0.1094 0.1676 0.1286 0.0369  0.0034  0.0075  249 PRO A O   
2065 C  CB  . PRO A 249 ? 0.1649 0.3420 0.1935 0.1538  -0.0551 -0.0520 249 PRO A CB  
2066 C  CG  . PRO A 249 ? 0.1746 0.3291 0.1569 0.0311  -0.0369 -0.0284 249 PRO A CG  
2067 C  CD  . PRO A 249 ? 0.0888 0.2625 0.1699 0.0281  -0.0277 -0.0304 249 PRO A CD  
2068 N  N   . LEU A 250 ? 0.1609 0.1904 0.0793 0.0430  0.0148  0.0043  250 LEU A N   
2069 C  CA  . LEU A 250 ? 0.1279 0.1685 0.1014 0.0204  0.0194  -0.0073 250 LEU A CA  
2070 C  C   . LEU A 250 ? 0.1573 0.1648 0.1002 0.0129  -0.0122 0.0071  250 LEU A C   
2071 O  O   . LEU A 250 ? 0.1473 0.1741 0.1245 0.0228  -0.0050 -0.0011 250 LEU A O   
2072 C  CB  . LEU A 250 ? 0.1993 0.1900 0.1216 0.0079  0.0402  0.0244  250 LEU A CB  
2073 C  CG  . LEU A 250 ? 0.1746 0.1803 0.1168 -0.0238 0.0401  0.0055  250 LEU A CG  
2074 C  CD1 . LEU A 250 ? 0.1845 0.1838 0.1234 -0.0208 0.0434  0.0022  250 LEU A CD1 
2075 C  CD2 . LEU A 250 ? 0.2385 0.2294 0.1530 -0.0858 0.0436  0.0110  250 LEU A CD2 
2076 N  N   A LYS A 251 ? 0.1613 0.2152 0.1160 0.0505  -0.0113 -0.0020 251 LYS A N   
2077 N  N   B LYS A 251 ? 0.1720 0.2155 0.1090 0.0528  -0.0150 -0.0038 251 LYS A N   
2078 C  CA  A LYS A 251 ? 0.2112 0.2606 0.1108 0.0406  0.0009  -0.0391 251 LYS A CA  
2079 C  CA  B LYS A 251 ? 0.2416 0.2685 0.1168 0.0548  -0.0116 -0.0527 251 LYS A CA  
2080 C  C   A LYS A 251 ? 0.0995 0.3669 0.1728 0.0259  -0.0192 -0.0897 251 LYS A C   
2081 C  C   B LYS A 251 ? 0.2269 0.3524 0.1839 0.0310  0.0078  -0.0961 251 LYS A C   
2082 O  O   A LYS A 251 ? 0.1807 0.3864 0.2151 -0.0096 0.0193  -0.0663 251 LYS A O   
2083 O  O   B LYS A 251 ? 0.3086 0.4424 0.2561 -0.0672 0.0519  -0.1007 251 LYS A O   
2084 C  CB  A LYS A 251 ? 0.2083 0.2917 0.1839 -0.0098 0.0186  -0.0381 251 LYS A CB  
2085 C  CB  B LYS A 251 ? 0.1907 0.2532 0.2221 0.0143  -0.0256 -0.0757 251 LYS A CB  
2086 C  CG  A LYS A 251 ? 0.2069 0.4077 0.1663 -0.0744 0.0147  -0.1055 251 LYS A CG  
2087 C  CG  B LYS A 251 ? 0.2353 0.3881 0.1777 0.0584  -0.0127 -0.0234 251 LYS A CG  
2088 C  CD  A LYS A 251 ? 0.1882 0.4249 0.1850 -0.0450 -0.0195 -0.0432 251 LYS A CD  
2089 C  CD  B LYS A 251 ? 0.2270 0.4134 0.3079 0.0659  0.0834  -0.1086 251 LYS A CD  
2090 C  CE  A LYS A 251 ? 0.2082 0.2713 0.4604 -0.0242 -0.0265 -0.0767 251 LYS A CE  
2091 C  CE  B LYS A 251 ? 0.2295 0.3459 0.2544 0.1228  0.0046  -0.0673 251 LYS A CE  
2092 N  NZ  A LYS A 251 ? 0.2640 0.3958 0.3299 -0.0552 0.0116  -0.0598 251 LYS A NZ  
2093 N  NZ  B LYS A 251 ? 0.2282 0.4371 0.1778 0.0779  0.0453  0.0400  251 LYS A NZ  
2094 N  N   . ASN A 252 ? 0.1433 0.3585 0.1875 0.0522  -0.0364 -0.1086 252 ASN A N   
2095 C  CA  . ASN A 252 ? 0.2004 0.4947 0.2183 0.0895  0.0130  -0.1002 252 ASN A CA  
2096 C  C   . ASN A 252 ? 0.2245 0.4903 0.1752 0.0264  -0.0400 -0.0851 252 ASN A C   
2097 O  O   . ASN A 252 ? 0.2848 0.5386 0.2852 0.1656  -0.0068 -0.0277 252 ASN A O   
2098 C  CB  . ASN A 252 ? 0.2979 0.5983 0.3740 0.0642  -0.1039 -0.1601 252 ASN A CB  
2099 C  CG  . ASN A 252 ? 0.3220 0.6628 0.3486 0.1214  0.0442  0.0309  252 ASN A CG  
2100 O  OD1 . ASN A 252 ? 0.4027 0.9944 0.7728 0.0177  -0.2107 0.2527  252 ASN A OD1 
2101 N  ND2 . ASN A 252 ? 0.3410 0.6969 0.3552 0.0937  -0.0216 0.0473  252 ASN A ND2 
2102 N  N   . ARG A 253 ? 0.1389 0.2504 0.1076 0.0162  0.0095  0.0025  253 ARG A N   
2103 C  CA  . ARG A 253 ? 0.1275 0.1879 0.1030 0.0100  0.0249  -0.0103 253 ARG A CA  
2104 C  C   . ARG A 253 ? 0.1487 0.1673 0.1075 0.0035  0.0250  -0.0201 253 ARG A C   
2105 O  O   . ARG A 253 ? 0.1975 0.1879 0.1997 0.0221  0.0666  0.0058  253 ARG A O   
2106 C  CB  . ARG A 253 ? 0.1200 0.1612 0.0983 -0.0053 0.0062  -0.0040 253 ARG A CB  
2107 C  CG  . ARG A 253 ? 0.1749 0.1472 0.0837 -0.0135 0.0186  -0.0100 253 ARG A CG  
2108 C  CD  . ARG A 253 ? 0.1512 0.1324 0.0909 0.0241  0.0233  -0.0010 253 ARG A CD  
2109 N  NE  . ARG A 253 ? 0.1195 0.1415 0.0950 0.0104  0.0168  -0.0120 253 ARG A NE  
2110 C  CZ  . ARG A 253 ? 0.0917 0.1181 0.0839 0.0081  0.0016  -0.0053 253 ARG A CZ  
2111 N  NH1 . ARG A 253 ? 0.0703 0.1307 0.0952 -0.0029 -0.0071 0.0071  253 ARG A NH1 
2112 N  NH2 . ARG A 253 ? 0.0897 0.0996 0.1049 -0.0015 0.0023  -0.0064 253 ARG A NH2 
2113 N  N   . GLN A 254 ? 0.1346 0.1893 0.1336 -0.0008 0.0290  -0.0294 254 GLN A N   
2114 C  CA  . GLN A 254 ? 0.1329 0.2345 0.1090 -0.0147 0.0146  -0.0118 254 GLN A CA  
2115 C  C   . GLN A 254 ? 0.1685 0.1975 0.0988 0.0060  0.0125  -0.0074 254 GLN A C   
2116 O  O   . GLN A 254 ? 0.2331 0.1803 0.1731 -0.0229 -0.0354 -0.0047 254 GLN A O   
2117 C  CB  . GLN A 254 ? 0.1569 0.3936 0.1615 -0.0190 0.0652  -0.0718 254 GLN A CB  
2118 C  CG  . GLN A 254 ? 0.1943 0.5752 0.3929 -0.0973 0.0268  -0.0379 254 GLN A CG  
2119 C  CD  . GLN A 254 ? 0.9362 1.0267 0.3510 -0.0556 0.0745  0.1337  254 GLN A CD  
2120 O  OE1 . GLN A 254 ? 0.8049 1.0470 0.1519 -0.0690 0.0536  -0.1278 254 GLN A OE1 
2121 N  NE2 . GLN A 254 ? 0.8323 0.7354 0.4536 -0.1166 -0.1145 -0.3208 254 GLN A NE2 
2122 N  N   . ILE A 255 ? 0.1130 0.1723 0.1134 0.0105  0.0077  -0.0010 255 ILE A N   
2123 C  CA  . ILE A 255 ? 0.1260 0.1669 0.1003 0.0347  0.0083  0.0089  255 ILE A CA  
2124 C  C   . ILE A 255 ? 0.1146 0.1498 0.1136 0.0054  0.0111  0.0262  255 ILE A C   
2125 O  O   . ILE A 255 ? 0.1404 0.1867 0.1389 0.0282  0.0384  0.0480  255 ILE A O   
2126 C  CB  . ILE A 255 ? 0.1084 0.1490 0.1205 0.0116  0.0069  0.0063  255 ILE A CB  
2127 C  CG1 . ILE A 255 ? 0.1094 0.1541 0.1300 0.0230  0.0070  -0.0122 255 ILE A CG1 
2128 C  CG2 . ILE A 255 ? 0.1225 0.1825 0.1336 0.0161  0.0015  0.0124  255 ILE A CG2 
2129 C  CD1 . ILE A 255 ? 0.1390 0.1695 0.1735 0.0115  0.0326  -0.0178 255 ILE A CD1 
2130 N  N   . LYS A 256 ? 0.1139 0.1597 0.0917 0.0173  0.0106  0.0107  256 LYS A N   
2131 C  CA  . LYS A 256 ? 0.1088 0.1537 0.1155 0.0096  0.0137  -0.0036 256 LYS A CA  
2132 C  C   . LYS A 256 ? 0.1220 0.1652 0.0741 -0.0063 0.0271  0.0098  256 LYS A C   
2133 O  O   . LYS A 256 ? 0.1443 0.2062 0.0782 -0.0301 0.0334  0.0048  256 LYS A O   
2134 C  CB  . LYS A 256 ? 0.1458 0.1674 0.1588 0.0119  0.0131  -0.0201 256 LYS A CB  
2135 C  CG  . LYS A 256 ? 0.2223 0.2331 0.2594 -0.0624 0.0005  -0.0545 256 LYS A CG  
2136 C  CD  . LYS A 256 ? 0.3835 0.3330 0.3856 0.0245  0.0323  -0.1683 256 LYS A CD  
2137 N  N   . ALA A 257 ? 0.1208 0.1634 0.0995 0.0021  0.0375  0.0198  257 ALA A N   
2138 C  CA  . ALA A 257 ? 0.1033 0.1900 0.1005 0.0138  0.0277  -0.0023 257 ALA A CA  
2139 C  C   . ALA A 257 ? 0.0976 0.1691 0.0796 -0.0089 0.0422  0.0163  257 ALA A C   
2140 O  O   . ALA A 257 ? 0.1213 0.2256 0.1065 -0.0042 0.0512  -0.0074 257 ALA A O   
2141 C  CB  . ALA A 257 ? 0.1421 0.1936 0.1634 0.0096  0.0304  0.0304  257 ALA A CB  
2142 N  N   . SER A 258 ? 0.1053 0.1746 0.1121 -0.0006 0.0234  0.0107  258 SER A N   
2143 C  CA  . SER A 258 ? 0.1102 0.2216 0.1394 0.0256  0.0346  0.0111  258 SER A CA  
2144 C  C   . SER A 258 ? 0.1247 0.2076 0.1297 0.0150  0.0516  -0.0291 258 SER A C   
2145 O  O   . SER A 258 ? 0.1182 0.3486 0.1965 0.0386  0.0710  -0.0230 258 SER A O   
2146 C  CB  . SER A 258 ? 0.1649 0.1738 0.1555 0.0002  -0.0111 -0.0005 258 SER A CB  
2147 O  OG  . SER A 258 ? 0.1132 0.1990 0.1340 -0.0078 0.0362  0.0000  258 SER A OG  
2148 N  N   . PHE A 259 ? 0.1204 0.2417 0.1728 -0.0271 0.0436  -0.0111 259 PHE A N   
2149 C  CA  . PHE A 259 ? 0.1742 0.2533 0.2216 -0.0702 0.0236  -0.0234 259 PHE A CA  
2150 C  C   . PHE A 259 ? 0.2940 0.3194 0.2511 0.0092  -0.0186 -0.0652 259 PHE A C   
2151 O  O   . PHE A 259 ? 0.3110 0.2752 0.2076 -0.1046 -0.0065 0.0766  259 PHE A O   
2152 C  CB  . PHE A 259 ? 0.1838 0.1886 0.2234 -0.0092 0.0279  -0.0016 259 PHE A CB  
2153 C  CG  . PHE A 259 ? 0.1358 0.1936 0.2176 -0.0335 0.0033  0.0155  259 PHE A CG  
2154 C  CD1 . PHE A 259 ? 0.1293 0.1784 0.1594 -0.0342 0.0013  -0.0172 259 PHE A CD1 
2155 C  CD2 . PHE A 259 ? 0.1867 0.2216 0.3295 -0.0254 0.0047  0.0526  259 PHE A CD2 
2156 C  CE1 . PHE A 259 ? 0.1911 0.2004 0.1685 0.0017  -0.0096 -0.0114 259 PHE A CE1 
2157 C  CE2 . PHE A 259 ? 0.2043 0.2414 0.3690 -0.0189 0.0006  0.0473  259 PHE A CE2 
2158 C  CZ  . PHE A 259 ? 0.2047 0.1680 0.3039 -0.0155 0.0016  -0.0237 259 PHE A CZ  
2159 N  N   . LYS A 260 ? 0.4740 0.5346 0.5192 -0.4888 -0.0722 -0.0175 260 LYS A N   
2160 C  CA  . LYS A 260 ? 1.1279 0.4251 0.4279 -0.0092 0.0714  0.2074  260 LYS A CA  
2161 C  C   . LYS A 260 ? 1.1571 0.8678 0.4028 -0.0919 0.2810  0.0658  260 LYS A C   
2162 O  O   . LYS A 260 ? 0.8914 1.0411 1.2873 0.3917  -0.2227 -0.1270 260 LYS A O   
2163 C  CB  . LYS A 260 ? 0.6391 0.6571 0.6600 0.1948  0.0913  0.2298  260 LYS A CB  
2164 C  CG  . LYS A 260 ? 1.1809 0.6872 0.9999 0.0818  0.0084  0.1742  260 LYS A CG  
2165 O  OXT . LYS A 260 ? 0.9126 0.5827 0.9562 -0.2306 0.0970  -0.0628 260 LYS A OXT 
2166 ZN ZN  . ZN  B .   ? 0.0757 0.0900 0.0993 0.0016  -0.0013 -0.0022 301 ZN  A ZN  
2167 F  F27 A WWO C .   ? 0.1566 0.2107 0.2953 0.0465  0.0205  0.0916  302 WWO A F27 
2168 F  F27 B WWO C .   ? 0.2037 0.1234 0.3405 0.0127  -0.0954 0.0378  302 WWO A F27 
2169 C  C5  A WWO C .   ? 0.1691 0.2233 0.2275 -0.0352 0.0323  0.0245  302 WWO A C5  
2170 C  C5  B WWO C .   ? 0.1821 0.2094 0.2626 -0.0233 -0.0273 0.0881  302 WWO A C5  
2171 C  C4  A WWO C .   ? 0.0907 0.2446 0.1209 -0.0154 0.0938  0.0096  302 WWO A C4  
2172 C  C4  B WWO C .   ? 0.1093 0.2112 0.1875 -0.0197 0.0060  0.0135  302 WWO A C4  
2173 S  S7  A WWO C .   ? 0.0774 0.0924 0.1293 0.0011  -0.0069 -0.0044 302 WWO A S7  
2174 S  S7  B WWO C .   ? 0.0778 0.1044 0.1322 -0.0025 -0.0060 -0.0031 302 WWO A S7  
2175 O  O9  A WWO C .   ? 0.0798 0.1196 0.1322 0.0201  0.0096  -0.0057 302 WWO A O9  
2176 O  O9  B WWO C .   ? 0.0830 0.1365 0.1335 0.0200  -0.0089 -0.0024 302 WWO A O9  
2177 N  N10 A WWO C .   ? 0.1208 0.0798 0.2115 0.0095  -0.0094 -0.0022 302 WWO A N10 
2178 N  N10 B WWO C .   ? 0.1014 0.1040 0.1940 -0.0030 -0.0680 -0.0434 302 WWO A N10 
2179 O  O8  A WWO C .   ? 0.0891 0.1216 0.1458 0.0201  -0.0132 -0.0396 302 WWO A O8  
2180 O  O8  B WWO C .   ? 0.1200 0.0997 0.1602 0.0125  -0.0366 -0.0168 302 WWO A O8  
2181 C  C3  A WWO C .   ? 0.0970 0.1843 0.1411 -0.0510 0.0862  0.0402  302 WWO A C3  
2182 C  C3  B WWO C .   ? 0.0369 0.1932 0.2191 -0.0201 0.0178  0.0566  302 WWO A C3  
2183 F  F12 A WWO C .   ? 0.1024 0.1372 0.1796 -0.0135 0.0585  -0.0126 302 WWO A F12 
2184 F  F12 B WWO C .   ? 0.1300 0.2561 0.2252 -0.0237 0.0420  -0.0590 302 WWO A F12 
2185 C  C2  A WWO C .   ? 0.0988 0.2252 0.1498 -0.0609 0.0837  0.0551  302 WWO A C2  
2186 C  C2  B WWO C .   ? 0.1339 0.3154 0.1717 0.0386  0.0553  0.0199  302 WWO A C2  
2187 F  F13 A WWO C .   ? 0.0914 0.2377 0.1537 -0.0430 0.0660  0.0300  302 WWO A F13 
2188 F  F13 B WWO C .   ? 0.1849 0.2007 0.1986 -0.0297 0.0842  0.0078  302 WWO A F13 
2189 C  C6  A WWO C .   ? 0.1594 0.2776 0.1720 -0.0166 0.0473  0.0651  302 WWO A C6  
2190 C  C6  B WWO C .   ? 0.1591 0.2755 0.3083 -0.0677 0.0285  0.1002  302 WWO A C6  
2191 C  C1  A WWO C .   ? 0.1573 0.1868 0.0864 -0.0353 0.0608  -0.0226 302 WWO A C1  
2192 C  C1  B WWO C .   ? 0.2008 0.2670 0.3000 -0.0174 0.0021  0.0917  302 WWO A C1  
2193 S  S11 A WWO C .   ? 0.1447 0.2655 0.1742 -0.0504 0.0159  0.0758  302 WWO A S11 
2194 S  S11 B WWO C .   ? 0.2026 0.2468 0.2413 -0.0138 0.0206  0.0537  302 WWO A S11 
2195 O  O22 A WWO C .   ? 0.2509 0.2735 0.1917 -0.1202 -0.0256 0.1605  302 WWO A O22 
2196 O  O22 B WWO C .   ? 0.3574 0.2284 0.3814 -0.0171 -0.0163 0.0840  302 WWO A O22 
2197 O  O23 A WWO C .   ? 0.3811 0.3864 0.3086 0.1163  0.0184  0.0615  302 WWO A O23 
2198 O  O23 B WWO C .   ? 0.8455 0.3991 0.2266 -0.1116 -0.1406 -0.2002 302 WWO A O23 
2199 C  C21 A WWO C .   ? 0.1577 0.1904 0.2069 -0.0367 -0.0193 0.0912  302 WWO A C21 
2200 C  C21 B WWO C .   ? 0.1857 0.2288 0.2202 -0.0381 -0.0257 0.1025  302 WWO A C21 
2201 C  C24 A WWO C .   ? 0.2587 0.2169 0.3277 0.0072  -0.0758 0.1134  302 WWO A C24 
2202 C  C24 B WWO C .   ? 0.2266 0.1993 0.3464 -0.0510 -0.0133 0.0222  302 WWO A C24 
2203 O  O25 A WWO C .   ? 0.3796 0.1649 0.3420 0.0253  -0.0418 0.0271  302 WWO A O25 
2204 O  O25 B WWO C .   ? 0.2896 0.2039 0.2864 0.0249  0.0250  0.0210  302 WWO A O25 
2205 N  N26 A WWO C .   ? 0.2176 0.3328 0.0697 -0.0089 0.0476  0.0766  302 WWO A N26 
2206 N  N26 B WWO C .   ? 0.2667 0.2964 0.1979 0.0433  -0.0107 0.0054  302 WWO A N26 
2207 C  C14 A WWO C .   ? 0.2280 0.3510 0.5674 0.0529  -0.0337 -0.0586 302 WWO A C14 
2208 C  C14 B WWO C .   ? 0.5651 0.5014 0.5015 0.0387  -0.2906 -0.2030 302 WWO A C14 
2209 C  C15 A WWO C .   ? 0.5764 0.2640 0.6322 0.0801  0.0351  0.0509  302 WWO A C15 
2210 C  C15 B WWO C .   ? 0.7623 0.1996 0.5840 -0.0236 -0.2394 -0.2719 302 WWO A C15 
2211 C  C20 A WWO C .   ? 0.5904 0.6225 0.6837 0.1363  0.0782  -0.1191 302 WWO A C20 
2212 C  C20 B WWO C .   ? 0.7094 0.4972 0.5362 0.0305  -0.2523 -0.1124 302 WWO A C20 
2213 C  C19 A WWO C .   ? 0.7562 0.6054 0.7686 0.1170  0.1318  -0.0168 302 WWO A C19 
2214 C  C19 B WWO C .   ? 0.9879 0.4041 0.6650 0.2398  -0.0707 -0.1155 302 WWO A C19 
2215 C  C18 A WWO C .   ? 0.7355 0.8429 0.8184 0.1005  0.1793  -0.0947 302 WWO A C18 
2216 C  C18 B WWO C .   ? 0.6808 0.9606 0.7781 0.2011  0.1373  0.0793  302 WWO A C18 
2217 C  C17 A WWO C .   ? 0.6555 0.3517 0.7437 0.1997  0.1423  -0.0663 302 WWO A C17 
2218 C  C17 B WWO C .   ? 0.9076 0.7031 0.7847 0.2859  -0.0427 0.1385  302 WWO A C17 
2219 C  C16 A WWO C .   ? 0.5093 0.3345 0.8333 0.0858  0.1149  -0.1203 302 WWO A C16 
2220 C  C16 B WWO C .   ? 0.6251 0.3689 0.8971 -0.0290 -0.3072 -0.1344 302 WWO A C16 
2221 S  S   . DMS D .   ? 0.2478 0.3143 0.2927 -0.0142 -0.0047 -0.0316 303 DMS A S   
2222 O  O   . DMS D .   ? 0.4177 0.4165 0.4473 0.1043  0.0425  -0.1509 303 DMS A O   
2223 C  C1  . DMS D .   ? 0.1875 0.3079 0.2142 0.0256  0.0185  -0.0581 303 DMS A C1  
2224 C  C2  . DMS D .   ? 0.2374 0.3445 0.5253 -0.0782 0.0116  -0.0500 303 DMS A C2  
2225 O  O1  . MES E .   ? 0.3574 0.4634 0.2601 0.0555  0.0354  0.0726  304 MES A O1  
2226 C  C2  . MES E .   ? 0.4230 0.2723 0.2554 -0.0257 -0.0454 -0.0236 304 MES A C2  
2227 C  C3  . MES E .   ? 0.2824 0.1789 0.4124 0.0679  0.0795  0.0226  304 MES A C3  
2228 N  N4  . MES E .   ? 0.4433 0.3753 0.4595 -0.0957 0.0013  0.0626  304 MES A N4  
2229 C  C5  . MES E .   ? 0.5947 0.2438 0.4936 0.0323  0.0231  -0.1644 304 MES A C5  
2230 C  C6  . MES E .   ? 0.4550 0.3516 0.5090 -0.0345 0.0708  0.0231  304 MES A C6  
2231 C  C7  . MES E .   ? 0.3225 0.3841 0.6707 -0.1116 -0.0469 0.2329  304 MES A C7  
2232 C  C8  . MES E .   ? 0.4819 0.2633 0.3782 0.0729  0.1754  0.0208  304 MES A C8  
2233 N  N1  . BCN F .   ? 0.5023 0.6069 0.3050 -0.0047 0.0932  0.1297  305 BCN A N1  
2234 C  C1  . BCN F .   ? 0.2302 0.6230 0.4670 -0.1289 0.0193  0.2041  305 BCN A C1  
2235 C  C2  . BCN F .   ? 0.3071 0.9529 0.4386 0.0153  0.0968  0.2832  305 BCN A C2  
2236 O  O21 . BCN F .   ? 0.3560 1.3306 0.9929 -0.0547 0.2247  0.1808  305 BCN A O21 
2237 O  O22 . BCN F .   ? 0.5653 0.8312 0.8003 0.0194  -0.1096 0.3467  305 BCN A O22 
2238 C  C3  . BCN F .   ? 0.2723 0.3398 0.4007 -0.1327 0.0660  0.0463  305 BCN A C3  
2239 C  C4  . BCN F .   ? 0.4365 0.4453 0.6821 0.0418  0.1101  -0.1644 305 BCN A C4  
2240 O  O4  . BCN F .   ? 0.4232 0.3312 0.3524 -0.0330 0.0716  0.0010  305 BCN A O4  
2241 C  C5  . BCN F .   ? 0.3288 0.3495 0.3243 -0.0995 0.1179  0.1170  305 BCN A C5  
2242 C  C6  . BCN F .   ? 0.7664 0.7623 0.4133 -0.1754 -0.1597 -0.0538 305 BCN A C6  
2243 O  O6  . BCN F .   ? 0.9251 0.5419 0.4819 -0.1813 0.0779  0.0316  305 BCN A O6  
2244 O  O   . HOH G .   ? 0.5416 0.3366 0.8712 0.0337  -0.3068 0.0895  401 HOH A O   
2245 O  O   . HOH G .   ? 0.5122 0.6334 0.4189 0.0140  0.0849  0.0221  402 HOH A O   
2246 O  O   . HOH G .   ? 0.2338 0.2683 0.2374 0.0247  -0.0178 -0.0480 403 HOH A O   
2247 O  O   . HOH G .   ? 0.2810 0.2126 0.4422 -0.0269 -0.0305 -0.0480 404 HOH A O   
2248 O  O   . HOH G .   ? 0.3797 0.5088 0.7116 0.0695  0.0128  -0.1222 405 HOH A O   
2249 O  O   . HOH G .   ? 0.6650 0.3956 0.4515 0.0662  0.1723  0.0718  406 HOH A O   
2250 O  O   . HOH G .   ? 0.3247 0.4792 0.3919 0.0253  -0.0124 -0.1106 407 HOH A O   
2251 O  O   . HOH G .   ? 0.4094 0.5721 0.4514 -0.1324 0.1217  -0.1434 408 HOH A O   
2252 O  O   . HOH G .   ? 0.2640 0.2852 0.3892 0.0562  0.0505  0.0719  409 HOH A O   
2253 O  O   . HOH G .   ? 0.5561 0.5138 0.3951 0.1142  0.1812  0.0323  410 HOH A O   
2254 O  O   . HOH G .   ? 0.5582 0.6820 0.1868 -0.0452 0.1177  0.2703  411 HOH A O   
2255 O  O   . HOH G .   ? 0.4340 0.6541 0.4929 -0.0842 0.0900  0.1456  412 HOH A O   
2256 O  O   . HOH G .   ? 0.4909 0.6997 0.2805 -0.1287 -0.0155 -0.0436 413 HOH A O   
2257 O  O   . HOH G .   ? 0.5141 0.3517 0.5485 0.0979  -0.1892 -0.0195 414 HOH A O   
2258 O  O   . HOH G .   ? 0.3908 0.6652 0.7202 0.0189  0.0398  0.0860  415 HOH A O   
2259 O  O   . HOH G .   ? 0.3093 0.1504 0.2428 -0.0206 -0.0193 -0.0044 416 HOH A O   
2260 O  O   . HOH G .   ? 0.4975 0.3326 0.6610 0.0283  0.1932  0.0783  417 HOH A O   
2261 O  O   . HOH G .   ? 0.5272 0.5529 0.4688 -0.0218 0.3033  -0.0508 418 HOH A O   
2262 O  O   . HOH G .   ? 0.2892 0.4572 0.6120 0.0009  -0.0214 0.0463  419 HOH A O   
2263 O  O   . HOH G .   ? 0.3334 0.2512 0.2381 -0.0244 0.0363  -0.0509 420 HOH A O   
2264 O  O   . HOH G .   ? 0.3628 0.5060 0.2554 -0.0862 0.0385  -0.1253 421 HOH A O   
2265 O  O   . HOH G .   ? 0.4604 0.3431 0.4214 -0.0303 -0.1485 -0.0837 422 HOH A O   
2266 O  O   . HOH G .   ? 0.3657 0.9629 0.4742 0.0146  0.0022  0.0344  423 HOH A O   
2267 O  O   . HOH G .   ? 0.4135 0.2996 0.5296 -0.1140 -0.0374 0.0734  424 HOH A O   
2268 O  O   . HOH G .   ? 0.4220 0.4860 0.2075 -0.2335 0.0926  -0.0666 425 HOH A O   
2269 O  O   . HOH G .   ? 0.6039 0.5098 0.5371 -0.1132 0.0906  -0.0602 426 HOH A O   
2270 O  O   . HOH G .   ? 0.2986 0.5594 0.6578 0.1689  0.1552  0.0304  427 HOH A O   
2271 O  O   . HOH G .   ? 0.3129 0.5043 0.6115 -0.0016 0.1046  0.1018  428 HOH A O   
2272 O  O   . HOH G .   ? 0.4988 0.5851 0.6169 -0.0826 -0.0587 0.2676  429 HOH A O   
2273 O  O   . HOH G .   ? 0.3312 0.2789 0.3707 0.0212  0.1800  -0.0126 430 HOH A O   
2274 O  O   . HOH G .   ? 0.3890 0.4710 0.7598 0.0108  -0.0347 0.0567  431 HOH A O   
2275 O  O   . HOH G .   ? 0.1648 0.4397 0.3268 0.0324  0.0153  -0.1273 432 HOH A O   
2276 O  O   . HOH G .   ? 0.1846 0.2537 0.2741 0.0122  0.0337  0.0183  433 HOH A O   
2277 O  O   . HOH G .   ? 0.1212 0.1358 0.1250 -0.0240 0.0397  -0.0083 434 HOH A O   
2278 O  O   . HOH G .   ? 0.2658 0.2850 0.3470 0.0084  0.0013  -0.1126 435 HOH A O   
2279 O  O   . HOH G .   ? 0.2293 0.7573 0.4652 0.1069  -0.0100 -0.0494 436 HOH A O   
2280 O  O   . HOH G .   ? 0.4014 0.4130 0.1982 0.0421  0.0372  0.0829  437 HOH A O   
2281 O  O   . HOH G .   ? 0.2363 0.3549 0.5072 0.0055  0.0298  0.0583  438 HOH A O   
2282 O  O   . HOH G .   ? 0.4155 0.3560 0.4064 -0.1283 -0.1812 0.0961  439 HOH A O   
2283 O  O   . HOH G .   ? 0.2867 0.2940 0.5604 0.1021  -0.1300 -0.0111 440 HOH A O   
2284 O  O   . HOH G .   ? 0.4019 0.2344 0.1670 -0.0155 0.0422  -0.0348 441 HOH A O   
2285 O  O   . HOH G .   ? 0.3525 0.3718 0.9223 -0.0113 -0.2020 -0.0472 442 HOH A O   
2286 O  O   . HOH G .   ? 0.6544 0.2288 0.3832 0.0490  -0.1622 -0.0273 443 HOH A O   
2287 O  O   . HOH G .   ? 0.3238 0.3747 0.1606 0.0142  0.0021  0.0268  444 HOH A O   
2288 O  O   . HOH G .   ? 1.0745 0.6194 0.9464 0.6013  0.4690  0.2380  445 HOH A O   
2289 O  O   . HOH G .   ? 0.2975 0.2828 0.1990 -0.0363 0.0801  -0.0924 446 HOH A O   
2290 O  O   . HOH G .   ? 0.1703 0.2173 0.2697 0.0031  -0.1003 -0.0760 447 HOH A O   
2291 O  O   . HOH G .   ? 0.4041 0.2345 0.4029 -0.0284 0.1885  0.0758  448 HOH A O   
2292 O  O   . HOH G .   ? 0.4419 0.4984 0.3665 -0.0858 0.0196  -0.0239 449 HOH A O   
2293 O  O   . HOH G .   ? 0.2939 0.2379 0.2040 0.0029  -0.0111 0.0067  450 HOH A O   
2294 O  O   . HOH G .   ? 0.5503 0.2928 0.1846 0.0987  0.0942  0.0330  451 HOH A O   
2295 O  O   . HOH G .   ? 0.2213 0.2058 0.2162 0.0018  0.0223  0.0269  452 HOH A O   
2296 O  O   . HOH G .   ? 0.2830 0.2155 0.1904 -0.0685 -0.0210 -0.0016 453 HOH A O   
2297 O  O   . HOH G .   ? 0.1871 0.1081 0.1382 -0.0342 0.0535  -0.0164 454 HOH A O   
2298 O  O   . HOH G .   ? 0.1796 0.4304 0.3183 0.0117  0.0006  0.0560  455 HOH A O   
2299 O  O   . HOH G .   ? 0.1386 0.1796 0.3480 -0.0551 -0.0561 0.0251  456 HOH A O   
2300 O  O   . HOH G .   ? 0.1677 0.1845 0.1774 0.0249  0.0648  0.0535  457 HOH A O   
2301 O  O   . HOH G .   ? 0.1857 0.2173 0.2162 -0.0572 -0.0042 -0.0716 458 HOH A O   
2302 O  O   . HOH G .   ? 0.2687 0.2672 0.2216 -0.0520 0.0358  -0.0900 459 HOH A O   
2303 O  O   . HOH G .   ? 0.2518 0.5256 0.2690 -0.0835 -0.0482 0.0873  460 HOH A O   
2304 O  O   . HOH G .   ? 0.3024 0.8482 0.5532 -0.0602 -0.0239 0.0708  461 HOH A O   
2305 O  O   . HOH G .   ? 0.1645 0.2518 0.3420 -0.0844 0.0148  0.0691  462 HOH A O   
2306 O  O   . HOH G .   ? 0.4073 0.2467 0.2874 0.0543  0.0400  -0.0108 463 HOH A O   
2307 O  O   . HOH G .   ? 0.4080 0.4848 0.2342 0.0100  -0.0949 0.0800  464 HOH A O   
2308 O  O   . HOH G .   ? 0.2381 0.1497 0.3290 0.0113  0.1069  -0.0154 465 HOH A O   
2309 O  O   . HOH G .   ? 0.4701 0.5647 0.2945 0.0800  0.0643  0.0242  466 HOH A O   
2310 O  O   . HOH G .   ? 0.2627 0.3499 0.1979 -0.0709 0.0618  -0.0867 467 HOH A O   
2311 O  O   . HOH G .   ? 0.5873 0.5655 0.5535 -0.0418 -0.2122 0.0082  468 HOH A O   
2312 O  O   . HOH G .   ? 0.2773 0.3491 0.2324 0.0992  0.1092  0.1321  469 HOH A O   
2313 O  O   . HOH G .   ? 0.2470 0.2526 0.2881 0.0231  -0.0712 -0.0167 470 HOH A O   
2314 O  O   . HOH G .   ? 0.1519 0.1143 0.1148 -0.0081 0.0278  -0.0086 471 HOH A O   
2315 O  O   . HOH G .   ? 0.1746 0.2288 0.1717 -0.0013 0.0851  -0.0356 472 HOH A O   
2316 O  O   . HOH G .   ? 0.4192 0.2173 0.2282 -0.0386 0.0740  0.0688  473 HOH A O   
2317 O  O   . HOH G .   ? 0.3028 0.5441 0.1960 0.1884  -0.0226 -0.0715 474 HOH A O   
2318 O  O   . HOH G .   ? 0.1889 0.1602 0.2269 0.0255  -0.0833 0.0100  475 HOH A O   
2319 O  O   . HOH G .   ? 0.5291 0.2942 0.3118 -0.1123 -0.0630 0.1078  476 HOH A O   
2320 O  O   . HOH G .   ? 0.1221 0.1591 0.1534 0.0092  -0.0149 0.0219  477 HOH A O   
2321 O  O   . HOH G .   ? 0.1500 0.2367 0.1961 0.0585  -0.0077 -0.0012 478 HOH A O   
2322 O  O   . HOH G .   ? 0.1354 0.3876 0.3355 0.0227  0.0080  0.0989  479 HOH A O   
2323 O  O   . HOH G .   ? 0.3561 0.4472 0.5191 0.1050  -0.1315 -0.1870 480 HOH A O   
2324 O  O   . HOH G .   ? 0.1266 0.3373 0.2710 -0.0385 0.0043  0.0227  481 HOH A O   
2325 O  O   . HOH G .   ? 0.2532 0.2141 0.1781 -0.0309 -0.0080 0.0136  482 HOH A O   
2326 O  O   . HOH G .   ? 0.2037 0.3277 0.2705 0.0392  0.0838  0.0243  483 HOH A O   
2327 O  O   . HOH G .   ? 0.1882 0.2328 0.5933 -0.0066 0.0758  -0.0775 484 HOH A O   
2328 O  O   . HOH G .   ? 0.1110 0.1304 0.1067 0.0185  0.0113  0.0013  485 HOH A O   
2329 O  O   . HOH G .   ? 0.1656 0.3744 0.2216 -0.0053 0.0165  -0.0836 486 HOH A O   
2330 O  O   . HOH G .   ? 0.0864 0.1185 0.1124 -0.0160 0.0242  0.0010  487 HOH A O   
2331 O  O   . HOH G .   ? 0.1961 0.2449 0.2234 0.0609  0.0245  0.0220  488 HOH A O   
2332 O  O   . HOH G .   ? 0.1965 0.1465 0.2007 -0.0603 0.0149  -0.0021 489 HOH A O   
2333 O  O   . HOH G .   ? 0.1187 0.2173 0.2094 -0.0186 0.0358  0.0158  490 HOH A O   
2334 O  O   . HOH G .   ? 0.1247 0.0972 0.1103 0.0133  0.0091  -0.0111 491 HOH A O   
2335 O  O   . HOH G .   ? 0.1954 0.3172 0.3055 -0.0036 0.0252  -0.0747 492 HOH A O   
2336 O  O   . HOH G .   ? 0.3683 0.5941 0.2681 -0.0051 0.0423  0.0792  493 HOH A O   
2337 O  O   . HOH G .   ? 0.2608 0.1401 0.1954 -0.0363 0.0362  -0.0033 494 HOH A O   
2338 O  O   . HOH G .   ? 0.0838 0.1688 0.2029 0.0167  0.0114  -0.0468 495 HOH A O   
2339 O  O   . HOH G .   ? 0.3157 0.5391 0.4030 -0.0819 0.0761  -0.0934 496 HOH A O   
2340 O  O   . HOH G .   ? 0.2773 0.1896 0.4929 -0.0622 0.0564  -0.0501 497 HOH A O   
2341 O  O   . HOH G .   ? 0.5138 0.4435 0.2961 -0.0434 0.0575  0.1010  498 HOH A O   
2342 O  O   . HOH G .   ? 0.2126 0.2216 0.2579 0.0168  -0.0551 -0.0148 499 HOH A O   
2343 O  O   . HOH G .   ? 0.2558 0.2719 0.3310 -0.0429 0.0337  0.0718  500 HOH A O   
2344 O  O   . HOH G .   ? 0.1419 0.3308 0.2945 0.0160  0.0236  0.0465  501 HOH A O   
2345 O  O   . HOH G .   ? 0.4717 0.4139 0.4489 0.0623  -0.0794 0.1032  502 HOH A O   
2346 O  O   . HOH G .   ? 0.1852 0.2137 0.2958 0.0150  0.0088  -0.0300 503 HOH A O   
2347 O  O   . HOH G .   ? 0.2363 0.3661 0.2511 -0.1234 0.0476  -0.0375 504 HOH A O   
2348 O  O   . HOH G .   ? 0.2249 0.1814 0.3481 -0.0281 0.0912  -0.0458 505 HOH A O   
2349 O  O   . HOH G .   ? 0.3977 0.2910 0.3194 -0.1094 0.0288  -0.0255 506 HOH A O   
2350 O  O   . HOH G .   ? 0.2471 0.2885 0.4616 -0.0726 0.1211  -0.0469 507 HOH A O   
2351 O  O   . HOH G .   ? 0.2964 0.2741 0.2209 -0.0471 0.0452  -0.0551 508 HOH A O   
2352 O  O   . HOH G .   ? 0.2223 0.1451 0.2539 0.0159  0.0313  0.0517  509 HOH A O   
2353 O  O   . HOH G .   ? 0.3721 0.3668 0.2098 0.0234  0.0792  -0.0605 510 HOH A O   
2354 O  O   . HOH G .   ? 0.2922 0.3013 0.3850 -0.0178 -0.0162 -0.0334 511 HOH A O   
2355 O  O   . HOH G .   ? 0.1498 0.1472 0.2446 -0.0100 -0.0133 0.0229  512 HOH A O   
2356 O  O   . HOH G .   ? 0.1932 0.1724 0.2522 -0.0232 -0.0753 0.0363  513 HOH A O   
2357 O  O   . HOH G .   ? 0.4196 0.3658 0.3919 -0.0403 0.0078  0.0121  514 HOH A O   
2358 O  O   . HOH G .   ? 0.3914 0.2742 0.4816 0.1791  -0.0010 0.0113  515 HOH A O   
2359 O  O   . HOH G .   ? 0.2888 0.1911 0.2636 0.0785  -0.0304 -0.0140 516 HOH A O   
2360 O  O   . HOH G .   ? 0.2680 0.3741 0.2485 -0.0908 0.0443  -0.0749 517 HOH A O   
2361 O  O   . HOH G .   ? 0.1849 0.1365 0.1498 0.0170  0.0179  0.0035  518 HOH A O   
2362 O  O   . HOH G .   ? 0.3176 0.2946 0.5307 -0.0234 -0.1696 -0.0387 519 HOH A O   
2363 O  O   . HOH G .   ? 0.7401 0.3908 0.8425 0.0104  0.5143  0.0908  520 HOH A O   
2364 O  O   . HOH G .   ? 0.5057 0.4733 0.6590 0.0164  -0.1191 0.0502  521 HOH A O   
2365 O  O   . HOH G .   ? 0.3351 0.6866 0.5091 -0.0633 0.0575  0.0284  522 HOH A O   
2366 O  O   . HOH G .   ? 0.1922 0.2477 0.3348 0.0167  0.0414  0.1386  523 HOH A O   
2367 O  O   . HOH G .   ? 0.1922 0.2313 0.2107 -0.0428 -0.0245 0.0211  524 HOH A O   
2368 O  O   . HOH G .   ? 0.2669 0.1832 0.3116 -0.0155 0.0785  -0.0726 525 HOH A O   
2369 O  O   . HOH G .   ? 0.1716 0.1742 0.3226 -0.0425 0.0631  -0.0366 526 HOH A O   
2370 O  O   . HOH G .   ? 0.3446 0.2241 0.1864 -0.0608 0.1234  -0.0536 527 HOH A O   
2371 O  O   . HOH G .   ? 0.4013 0.3309 0.4431 0.0523  0.0817  -0.0880 528 HOH A O   
2372 O  O   . HOH G .   ? 0.2406 0.2489 0.1432 0.0381  0.0096  0.0024  529 HOH A O   
2373 O  O   . HOH G .   ? 0.1212 0.1509 0.1411 0.0199  0.0071  0.0120  530 HOH A O   
2374 O  O   . HOH G .   ? 0.4057 0.2662 0.3154 0.1459  -0.1005 -0.0741 531 HOH A O   
2375 O  O   . HOH G .   ? 0.0823 0.2602 0.1842 0.0247  0.0130  -0.0425 532 HOH A O   
2376 O  O   . HOH G .   ? 0.3274 0.6960 0.4390 -0.0086 0.0543  -0.0652 533 HOH A O   
2377 O  O   . HOH G .   ? 0.3262 0.6300 0.4367 -0.0277 -0.0009 -0.0866 534 HOH A O   
2378 O  O   . HOH G .   ? 0.2745 0.3467 0.4632 -0.0064 -0.0321 0.0757  535 HOH A O   
2379 O  O   . HOH G .   ? 0.1878 0.2692 0.2971 0.0052  0.0261  0.0330  536 HOH A O   
2380 O  O   . HOH G .   ? 0.2208 0.2148 0.1904 0.0055  0.0424  0.0259  537 HOH A O   
2381 O  O   . HOH G .   ? 0.3014 0.2516 0.2223 -0.0352 -0.0201 -0.0557 538 HOH A O   
2382 O  O   . HOH G .   ? 0.2134 0.4925 0.4084 0.0263  -0.0158 -0.1157 539 HOH A O   
2383 O  O   . HOH G .   ? 0.3921 0.3068 0.2500 -0.0502 0.0521  0.0814  540 HOH A O   
2384 O  O   . HOH G .   ? 0.3213 0.4275 0.3907 -0.0270 -0.0031 0.0174  541 HOH A O   
2385 O  O   . HOH G .   ? 0.2468 0.2561 0.3565 0.1122  -0.0406 -0.0741 542 HOH A O   
2386 O  O   . HOH G .   ? 0.4627 0.2799 0.3474 0.0605  -0.0205 -0.1072 543 HOH A O   
2387 O  O   . HOH G .   ? 0.3499 0.2205 0.2428 -0.0055 0.0307  -0.0321 544 HOH A O   
2388 O  O   . HOH G .   ? 0.1465 0.2090 0.3133 -0.0797 -0.0471 -0.0540 545 HOH A O   
2389 O  O   . HOH G .   ? 0.1541 0.4706 0.6960 0.0185  -0.1208 0.0311  546 HOH A O   
2390 O  O   . HOH G .   ? 0.4611 0.2749 0.5733 -0.0179 -0.0563 -0.1305 547 HOH A O   
2391 O  O   . HOH G .   ? 0.5283 0.4376 0.2647 -0.1835 -0.0679 0.0494  548 HOH A O   
2392 O  O   . HOH G .   ? 0.1688 0.3427 0.3039 0.0697  0.0696  0.0569  549 HOH A O   
2393 O  O   . HOH G .   ? 0.6745 0.3502 0.2605 0.1120  0.0256  0.0937  550 HOH A O   
2394 O  O   . HOH G .   ? 0.2331 0.2055 0.2557 0.0511  -0.0253 0.0396  551 HOH A O   
2395 O  O   . HOH G .   ? 0.3504 0.3190 0.6874 -0.0283 0.1527  0.0146  552 HOH A O   
2396 O  O   . HOH G .   ? 0.4817 0.2547 0.5088 -0.0727 -0.1045 -0.0234 553 HOH A O   
2397 O  O   . HOH G .   ? 0.1875 0.3956 0.3582 0.0384  -0.0282 -0.1340 554 HOH A O   
2398 O  O   . HOH G .   ? 0.3992 0.2666 0.6699 -0.0170 0.2533  0.0648  555 HOH A O   
2399 O  O   . HOH G .   ? 0.2867 0.2605 0.2928 -0.0760 -0.0666 -0.0130 556 HOH A O   
2400 O  O   . HOH G .   ? 0.5026 0.4106 0.7250 0.0543  0.1295  0.2435  557 HOH A O   
2401 O  O   . HOH G .   ? 0.2241 0.3028 0.2489 -0.0521 0.0134  -0.0164 558 HOH A O   
2402 O  O   . HOH G .   ? 0.5001 0.4304 0.2977 -0.0723 0.1105  -0.0857 559 HOH A O   
2403 O  O   . HOH G .   ? 0.2702 0.3094 0.5577 -0.0344 0.1213  0.0320  560 HOH A O   
2404 O  O   . HOH G .   ? 0.3621 0.2065 0.3274 -0.0019 0.1034  0.0736  561 HOH A O   
2405 O  O   . HOH G .   ? 0.4214 0.2269 0.2173 -0.0237 -0.0287 0.0292  562 HOH A O   
2406 O  O   . HOH G .   ? 0.8980 0.4162 0.4749 0.0292  -0.0594 0.0684  563 HOH A O   
2407 O  O   . HOH G .   ? 0.4124 0.2043 0.2780 0.0691  0.0482  0.0556  564 HOH A O   
2408 O  O   . HOH G .   ? 0.8288 0.2062 0.5475 -0.2566 0.0193  -0.0149 565 HOH A O   
2409 O  O   . HOH G .   ? 0.5048 0.3467 0.3750 0.0083  -0.0363 0.0020  566 HOH A O   
2410 O  O   . HOH G .   ? 0.1097 0.2377 0.1437 0.0047  -0.0039 0.0221  567 HOH A O   
2411 O  O   . HOH G .   ? 0.3538 0.2749 0.3162 -0.0985 0.0271  0.0077  568 HOH A O   
2412 O  O   . HOH G .   ? 0.2778 0.5077 0.4370 -0.0723 0.0848  0.0807  569 HOH A O   
2413 O  O   . HOH G .   ? 0.3920 0.5779 0.2543 0.0439  0.0018  0.1347  570 HOH A O   
2414 O  O   . HOH G .   ? 0.2496 0.2140 0.2597 0.0302  0.0232  0.0053  571 HOH A O   
2415 O  O   . HOH G .   ? 0.2284 0.2201 0.2124 0.0281  -0.0055 0.0787  572 HOH A O   
2416 O  O   . HOH G .   ? 0.3758 0.2658 0.5127 0.1293  -0.1650 -0.0964 573 HOH A O   
2417 O  O   . HOH G .   ? 0.2900 0.1500 0.2734 -0.0281 -0.0051 -0.0179 574 HOH A O   
2418 O  O   . HOH G .   ? 0.2954 0.2136 0.2583 0.0214  0.0941  0.0368  575 HOH A O   
2419 O  O   . HOH G .   ? 0.1946 0.2284 0.2489 0.0310  0.0641  0.0949  576 HOH A O   
2420 O  O   . HOH G .   ? 0.1645 0.3100 0.2550 0.0431  -0.0261 0.0069  577 HOH A O   
2421 O  O   . HOH G .   ? 0.2586 0.4501 0.5291 -0.0467 -0.0042 0.2258  578 HOH A O   
2422 O  O   . HOH G .   ? 0.4252 0.3186 0.7044 0.1427  0.2009  0.2285  579 HOH A O   
2423 O  O   . HOH G .   ? 0.1297 0.1168 0.1412 0.0099  0.0131  -0.0019 580 HOH A O   
2424 O  O   . HOH G .   ? 0.4084 0.5784 0.3933 0.0376  0.0405  0.1110  581 HOH A O   
2425 O  O   . HOH G .   ? 0.3926 0.2381 0.4034 0.0262  -0.0462 -0.0319 582 HOH A O   
2426 O  O   . HOH G .   ? 0.6181 0.5534 0.4539 0.2870  0.0905  0.2612  583 HOH A O   
2427 O  O   . HOH G .   ? 0.3151 0.4178 0.1598 0.0837  -0.0030 0.0377  584 HOH A O   
2428 O  O   . HOH G .   ? 0.6412 0.2733 0.3327 0.1425  0.0033  0.0029  585 HOH A O   
2429 O  O   . HOH G .   ? 1.2167 0.2727 0.4551 0.0732  -0.0025 0.0629  586 HOH A O   
2430 O  O   . HOH G .   ? 0.3777 0.6231 0.4142 0.0829  0.0566  0.1779  587 HOH A O   
2431 O  O   . HOH G .   ? 0.5431 0.3459 0.6469 -0.0862 -0.0201 -0.1123 588 HOH A O   
2432 O  O   . HOH G .   ? 0.2058 0.2676 0.3413 -0.0075 0.0179  0.0536  589 HOH A O   
2433 O  O   . HOH G .   ? 0.2719 0.4201 0.2868 0.0904  0.0707  0.0154  590 HOH A O   
2434 O  O   . HOH G .   ? 0.5917 0.7106 0.3893 0.0517  0.0004  -0.0535 591 HOH A O   
2435 O  O   . HOH G .   ? 0.2654 0.3092 0.3549 0.0622  0.0616  0.0888  592 HOH A O   
2436 O  O   . HOH G .   ? 0.5527 0.5258 0.3362 0.0309  -0.1053 0.1084  593 HOH A O   
2437 O  O   . HOH G .   ? 0.3165 0.2796 0.5322 -0.0954 -0.0731 0.1388  594 HOH A O   
2438 O  O   . HOH G .   ? 0.4367 0.3536 0.7350 -0.0724 -0.0341 0.0255  595 HOH A O   
2439 O  O   . HOH G .   ? 0.6518 0.3183 0.4647 -0.1062 0.1733  0.0267  596 HOH A O   
2440 O  O   . HOH G .   ? 0.0996 0.2237 0.2929 -0.0389 0.0036  0.0086  597 HOH A O   
2441 O  O   . HOH G .   ? 0.3649 0.3107 0.4907 0.1252  0.2071  0.1426  598 HOH A O   
2442 O  O   . HOH G .   ? 0.3556 0.6153 0.3086 0.0151  0.0414  -0.1002 599 HOH A O   
2443 O  O   . HOH G .   ? 0.4853 0.7139 0.9598 -0.0293 -0.0195 0.3340  600 HOH A O   
2444 O  O   . HOH G .   ? 0.6937 0.6424 0.5182 0.1016  0.0880  -0.1524 601 HOH A O   
2445 O  O   . HOH G .   ? 0.3265 0.2801 0.2992 -0.0290 0.1329  0.0983  602 HOH A O   
2446 O  O   . HOH G .   ? 0.3948 0.3459 0.3140 -0.0126 0.0151  -0.0854 603 HOH A O   
2447 O  O   . HOH G .   ? 0.3604 0.6024 0.7657 -0.0649 0.3619  -0.0627 604 HOH A O   
2448 O  O   . HOH G .   ? 0.3559 0.3039 0.4182 0.0402  0.1961  -0.0011 605 HOH A O   
2449 O  O   . HOH G .   ? 0.4266 0.2770 0.8336 0.2232  0.0616  0.1342  606 HOH A O   
2450 O  O   . HOH G .   ? 0.2537 0.5150 0.3957 -0.0058 0.0423  0.0929  607 HOH A O   
2451 O  O   . HOH G .   ? 0.4361 0.2613 0.3686 0.0592  0.1777  0.0700  608 HOH A O   
2452 O  O   . HOH G .   ? 0.3341 0.6481 0.6208 0.1007  0.2244  0.0251  609 HOH A O   
2453 O  O   . HOH G .   ? 0.3646 0.3165 0.6675 0.1458  0.0166  -0.0262 610 HOH A O   
2454 O  O   . HOH G .   ? 0.3420 0.3024 0.5084 0.0872  -0.0295 -0.0630 611 HOH A O   
2455 O  O   . HOH G .   ? 0.4379 0.6154 0.5349 -0.2273 -0.0445 -0.1101 612 HOH A O   
2456 O  O   . HOH G .   ? 0.5809 0.7877 0.2672 0.1474  0.1313  0.0172  613 HOH A O   
2457 O  O   . HOH G .   ? 0.4963 0.4656 0.3431 0.0551  -0.0233 -0.1591 614 HOH A O   
2458 O  O   . HOH G .   ? 0.2223 1.0096 0.6322 -0.1456 0.1603  0.1717  615 HOH A O   
2459 O  O   . HOH G .   ? 0.5987 0.2608 0.2548 0.0929  -0.0243 -0.0254 616 HOH A O   
2460 O  O   . HOH G .   ? 0.5733 0.4939 0.2735 0.0919  -0.0712 0.0100  617 HOH A O   
2461 O  O   . HOH G .   ? 0.2855 0.3543 0.3118 -0.0628 -0.0484 0.0521  618 HOH A O   
2462 O  O   . HOH G .   ? 0.3635 0.4063 0.2907 -0.0006 -0.0510 -0.0833 619 HOH A O   
2463 O  O   . HOH G .   ? 0.4771 0.3864 0.6505 0.1251  -0.0544 0.0768  620 HOH A O   
2464 O  O   . HOH G .   ? 0.2928 0.6905 0.5198 -0.1433 0.0923  -0.2462 621 HOH A O   
2465 O  O   . HOH G .   ? 0.5747 0.7981 0.2415 -0.0714 -0.2035 0.0601  622 HOH A O   
2466 O  O   . HOH G .   ? 0.3028 0.6287 0.4352 -0.0932 -0.0132 0.0355  623 HOH A O   
2467 O  O   . HOH G .   ? 0.3202 0.6657 0.3856 -0.0403 0.0027  0.0068  624 HOH A O   
2468 O  O   . HOH G .   ? 0.1785 0.7887 0.5468 -0.0737 -0.0298 0.1498  625 HOH A O   
2469 O  O   . HOH G .   ? 0.7251 0.3256 0.4124 -0.1430 0.0190  0.1129  626 HOH A O   
2470 O  O   . HOH G .   ? 0.2112 0.1670 0.2787 -0.0013 -0.0229 -0.0134 627 HOH A O   
2471 O  O   . HOH G .   ? 0.2478 0.3568 0.4249 0.0139  0.0069  -0.0719 628 HOH A O   
2472 O  O   . HOH G .   ? 0.3998 0.3389 0.6362 0.0168  -0.0995 0.1080  629 HOH A O   
2473 O  O   . HOH G .   ? 0.3355 0.5021 0.2694 0.1703  -0.0504 -0.1116 630 HOH A O   
2474 O  O   . HOH G .   ? 0.6989 0.3426 0.6378 -0.0522 0.2163  -0.0198 631 HOH A O   
2475 O  O   . HOH G .   ? 0.3586 0.3510 0.4451 0.0620  -0.0407 0.0279  632 HOH A O   
2476 O  O   . HOH G .   ? 0.4819 0.2423 0.2852 0.0353  0.1398  0.0637  633 HOH A O   
2477 O  O   . HOH G .   ? 0.2415 0.6320 0.2834 -0.0608 -0.0194 0.0073  634 HOH A O   
2478 O  O   . HOH G .   ? 0.3498 0.3256 0.2906 0.0469  -0.0199 -0.0368 635 HOH A O   
2479 O  O   . HOH G .   ? 0.3256 0.0976 0.1947 0.0261  0.0103  0.0064  636 HOH A O   
2480 O  O   . HOH G .   ? 0.4697 0.2896 0.3036 0.0583  -0.0883 -0.0252 637 HOH A O   
2481 O  O   . HOH G .   ? 0.3463 0.3847 0.3807 -0.0243 -0.0960 -0.1603 638 HOH A O   
2482 O  O   . HOH G .   ? 0.3998 0.4445 0.2856 0.1093  0.0240  0.0442  639 HOH A O   
2483 O  O   . HOH G .   ? 0.3545 0.2421 0.3604 0.0815  -0.1835 -0.0370 640 HOH A O   
2484 O  O   . HOH G .   ? 0.3965 0.6086 0.5472 -0.0403 0.2025  -0.1525 641 HOH A O   
2485 O  O   . HOH G .   ? 0.3531 0.3726 0.4670 0.1126  -0.0832 0.0081  642 HOH A O   
2486 O  O   . HOH G .   ? 0.2428 0.7137 0.4001 0.0272  -0.0223 -0.1309 643 HOH A O   
2487 O  O   . HOH G .   ? 0.3270 0.4275 0.6870 0.0216  -0.0561 0.0103  644 HOH A O   
2488 O  O   . HOH G .   ? 0.3240 0.3369 0.5227 -0.0205 0.0754  -0.1237 645 HOH A O   
2489 O  O   . HOH G .   ? 0.2777 0.4645 0.3276 -0.0939 0.0190  0.0582  646 HOH A O   
2490 O  O   . HOH G .   ? 0.5326 0.2861 0.3444 -0.1350 0.0702  0.0035  647 HOH A O   
2491 O  O   . HOH G .   ? 0.5026 0.6195 1.0029 0.0719  0.0260  0.2357  648 HOH A O   
2492 O  O   . HOH G .   ? 0.7511 0.5787 0.5758 0.1196  -0.0381 -0.0161 649 HOH A O   
2493 O  O   . HOH G .   ? 0.3184 0.4151 0.3811 -0.0943 0.1107  -0.0051 650 HOH A O   
2494 O  O   . HOH G .   ? 0.4187 0.3093 0.2435 0.0245  0.0248  0.0403  651 HOH A O   
2495 O  O   . HOH G .   ? 0.3661 0.4553 0.3272 0.1018  -0.0868 -0.0067 652 HOH A O   
2496 O  O   . HOH G .   ? 0.3456 0.6960 0.4235 -0.1229 0.1083  0.1670  653 HOH A O   
2497 O  O   . HOH G .   ? 0.5951 0.4733 0.5543 0.1713  -0.1773 -0.0613 654 HOH A O   
2498 O  O   . HOH G .   ? 0.3704 0.7059 0.5944 -0.1476 -0.0064 -0.1632 655 HOH A O   
2499 O  O   . HOH G .   ? 0.6806 0.8208 0.3689 -0.0556 -0.0355 0.2460  656 HOH A O   
2500 O  O   . HOH G .   ? 0.2861 0.2748 0.1929 -0.0192 0.0464  0.0396  657 HOH A O   
2501 O  O   . HOH G .   ? 0.3054 0.5195 0.4397 0.0847  -0.0012 0.1086  658 HOH A O   
2502 O  O   . HOH G .   ? 0.6120 0.4830 0.3376 0.0389  -0.0552 0.0424  659 HOH A O   
2503 O  O   . HOH G .   ? 0.2222 0.5147 0.9168 0.0936  0.0763  0.0261  660 HOH A O   
2504 O  O   . HOH G .   ? 0.4867 0.6469 0.3500 0.2000  -0.0120 -0.0012 661 HOH A O   
2505 O  O   . HOH G .   ? 0.4809 0.4135 0.6917 -0.1535 -0.2930 0.0823  662 HOH A O   
2506 O  O   . HOH G .   ? 0.5729 0.3948 0.4498 -0.1259 -0.1117 -0.0195 663 HOH A O   
2507 O  O   . HOH G .   ? 0.4834 0.2090 0.2471 -0.0088 -0.0408 -0.0237 664 HOH A O   
2508 O  O   . HOH G .   ? 0.3635 0.3122 0.4579 -0.0788 -0.0316 0.0512  665 HOH A O   
2509 O  O   . HOH G .   ? 0.4963 0.3532 0.6600 -0.0280 -0.0252 -0.0802 666 HOH A O   
2510 O  O   . HOH G .   ? 0.3984 0.2584 0.5565 -0.0646 0.1603  -0.1078 667 HOH A O   
2511 O  O   . HOH G .   ? 0.5018 0.3055 0.3884 0.1248  0.1103  -0.0278 668 HOH A O   
2512 O  O   . HOH G .   ? 0.2231 0.2101 0.2259 0.0700  -0.0326 -0.0001 669 HOH A O   
2513 O  O   . HOH G .   ? 0.3768 0.3777 0.3115 0.0683  0.0774  -0.1282 670 HOH A O   
2514 O  O   . HOH G .   ? 0.4199 0.4324 0.5031 -0.0694 -0.2033 -0.0519 671 HOH A O   
2515 O  O   . HOH G .   ? 0.4789 0.4462 0.5978 0.0770  0.1047  0.0671  672 HOH A O   
2516 O  O   . HOH G .   ? 0.5123 0.4503 0.6099 -0.1879 0.1412  -0.2376 673 HOH A O   
2517 O  O   . HOH G .   ? 0.6366 0.5858 0.4071 -0.0707 0.1350  -0.1899 674 HOH A O   
2518 O  O   . HOH G .   ? 0.3455 0.4983 0.4561 -0.0093 -0.0439 -0.0779 675 HOH A O   
2519 O  O   . HOH G .   ? 0.5315 0.4745 0.4997 0.0032  0.0354  -0.1523 676 HOH A O   
2520 O  O   . HOH G .   ? 0.3694 0.4273 0.5295 0.1118  0.0807  0.0851  677 HOH A O   
2521 O  O   . HOH G .   ? 0.4819 0.2874 0.3323 -0.0116 0.0699  0.0526  678 HOH A O   
2522 O  O   . HOH G .   ? 0.4552 0.6912 0.5206 0.1680  -0.0111 0.0450  679 HOH A O   
2523 O  O   . HOH G .   ? 0.4929 0.6731 0.3934 -0.1486 0.0060  0.0040  680 HOH A O   
2524 O  O   . HOH G .   ? 0.4001 0.3037 0.4482 -0.0310 0.0549  0.0969  681 HOH A O   
2525 O  O   . HOH G .   ? 0.5774 0.5205 0.3723 0.1374  -0.0222 -0.1252 682 HOH A O   
2526 O  O   . HOH G .   ? 0.6890 0.5838 0.3534 -0.0537 -0.0190 0.0366  683 HOH A O   
2527 O  O   . HOH G .   ? 0.4929 0.7001 0.4798 -0.1532 0.1065  0.2565  684 HOH A O   
2528 O  O   . HOH G .   ? 0.3986 0.2435 0.6389 -0.0611 0.2208  -0.0082 685 HOH A O   
2529 O  O   . HOH G .   ? 0.3191 0.5292 0.7621 -0.0747 0.0684  -0.2840 686 HOH A O   
2530 O  O   . HOH G .   ? 0.3457 0.3608 0.3708 0.0544  -0.1009 0.0620  687 HOH A O   
2531 O  O   . HOH G .   ? 0.4523 0.2910 0.3732 -0.0173 0.1348  -0.0647 688 HOH A O   
2532 O  O   . HOH G .   ? 0.2866 0.4558 0.6100 0.1242  -0.0182 -0.0132 689 HOH A O   
2533 O  O   . HOH G .   ? 0.7007 0.4080 0.4656 -0.0508 -0.2533 0.0456  690 HOH A O   
2534 O  O   . HOH G .   ? 0.3133 0.3299 0.8247 -0.0108 0.0534  0.1350  691 HOH A O   
# 
